data_5E2Z
# 
_entry.id   5E2Z 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5E2Z         
WWPDB D_1000214267 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'This entry contains the same protein with 5E2Y, but complexed with LSTa.' 5W2Y unspecified 
PDB .                                                                          5E2Y unspecified 
PDB .                                                                          5E30 unspecified 
PDB .                                                                          5E32 unspecified 
PDB .                                                                          5E34 unspecified 
PDB .                                                                          5E35 unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5E2Z 
_pdbx_database_status.recvd_initial_deposition_date   2015-10-01 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Zhu, X.'      1 
'Wilson, I.A.' 2 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Cell Rep' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2211-1247 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            13 
_citation.language                  ? 
_citation.page_first                1683 
_citation.page_last                 1691 
_citation.title                     
'Structural Basis for a Switch in Receptor Binding Specificity of Two H5N1 Hemagglutinin Mutants.' 
_citation.year                      2015 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.celrep.2015.10.027 
_citation.pdbx_database_id_PubMed   26586437 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Zhu, X.'          1 
primary 'Viswanathan, K.'  2 
primary 'Raman, R.'        3 
primary 'Yu, W.'           4 
primary 'Sasisekharan, R.' 5 
primary 'Wilson, I.A.'     6 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   115.49 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5E2Z 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     73.063 
_cell.length_a_esd                 ? 
_cell.length_b                     234.150 
_cell.length_b_esd                 ? 
_cell.length_c                     72.947 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         5E2Z 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Hemagglutinin          37701.578 3   ? Q226L 'UNP residues 17-345'  ? 
2 polymer     man Hemagglutinin          20822.039 3   ? ?     'UNP residues 347-520' ? 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   10  ? ?     ?                      ? 
4 non-polymer man BETA-L-FUCOSE          164.156   3   ? ?     ?                      ? 
5 non-polymer man 'O-SIALIC ACID'        309.270   3   ? ?     ?                      ? 
6 non-polymer man BETA-D-GALACTOSE       180.156   3   ? ?     ?                      ? 
7 non-polymer man ALPHA-L-FUCOSE         164.156   1   ? ?     ?                      ? 
8 water       nat water                  18.015    167 ? ?     ?                      ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'HEMAGGLUTININ HA1 CHAIN' 
2 'HEMAGGLUTININ HA2 CHAIN' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;ADPGDQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCNLDGVKPLILRDCSVAGWLLGNPMCDEFLNVPEW
SYIVEKINPANDLCYPGNFNDYEELKHLLSRINHFEKIQITPKNSWSDHEASGVSSACPYQGRSSFFRNVVWLTKKDNAY
PTIKRSYNNTNQEDLLVLWGIHHPNDATEQTRLYQNPTTYISVGTSTLNQKLVPKIATRSKVKGLSGRMEFFWTILKSND
AINFESNGNFIAPENAYKIVKKGDSTIMKSELEYGDCNTKCQTPIGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGL
RNSPQGERRRKKR
;
;ADPGDQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCNLDGVKPLILRDCSVAGWLLGNPMCDEFLNVPEW
SYIVEKINPANDLCYPGNFNDYEELKHLLSRINHFEKIQITPKNSWSDHEASGVSSACPYQGRSSFFRNVVWLTKKDNAY
PTIKRSYNNTNQEDLLVLWGIHHPNDATEQTRLYQNPTTYISVGTSTLNQKLVPKIATRSKVKGLSGRMEFFWTILKSND
AINFESNGNFIAPENAYKIVKKGDSTIMKSELEYGDCNTKCQTPIGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGL
RNSPQGERRRKKR
;
C,A,E ? 
2 'polypeptide(L)' no no 
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL
NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHRCDNECMESVRNGTYDYP
QYSEEARLKREEISGRLVPR
;
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL
NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHRCDNECMESVRNGTYDYP
QYSEEARLKREEISGRLVPR
;
D,B,F ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   ASP n 
1 3   PRO n 
1 4   GLY n 
1 5   ASP n 
1 6   GLN n 
1 7   ILE n 
1 8   CYS n 
1 9   ILE n 
1 10  GLY n 
1 11  TYR n 
1 12  HIS n 
1 13  ALA n 
1 14  ASN n 
1 15  ASN n 
1 16  SER n 
1 17  THR n 
1 18  GLU n 
1 19  GLN n 
1 20  VAL n 
1 21  ASP n 
1 22  THR n 
1 23  ILE n 
1 24  MET n 
1 25  GLU n 
1 26  LYS n 
1 27  ASN n 
1 28  VAL n 
1 29  THR n 
1 30  VAL n 
1 31  THR n 
1 32  HIS n 
1 33  ALA n 
1 34  GLN n 
1 35  ASP n 
1 36  ILE n 
1 37  LEU n 
1 38  GLU n 
1 39  LYS n 
1 40  THR n 
1 41  HIS n 
1 42  ASN n 
1 43  GLY n 
1 44  LYS n 
1 45  LEU n 
1 46  CYS n 
1 47  ASN n 
1 48  LEU n 
1 49  ASP n 
1 50  GLY n 
1 51  VAL n 
1 52  LYS n 
1 53  PRO n 
1 54  LEU n 
1 55  ILE n 
1 56  LEU n 
1 57  ARG n 
1 58  ASP n 
1 59  CYS n 
1 60  SER n 
1 61  VAL n 
1 62  ALA n 
1 63  GLY n 
1 64  TRP n 
1 65  LEU n 
1 66  LEU n 
1 67  GLY n 
1 68  ASN n 
1 69  PRO n 
1 70  MET n 
1 71  CYS n 
1 72  ASP n 
1 73  GLU n 
1 74  PHE n 
1 75  LEU n 
1 76  ASN n 
1 77  VAL n 
1 78  PRO n 
1 79  GLU n 
1 80  TRP n 
1 81  SER n 
1 82  TYR n 
1 83  ILE n 
1 84  VAL n 
1 85  GLU n 
1 86  LYS n 
1 87  ILE n 
1 88  ASN n 
1 89  PRO n 
1 90  ALA n 
1 91  ASN n 
1 92  ASP n 
1 93  LEU n 
1 94  CYS n 
1 95  TYR n 
1 96  PRO n 
1 97  GLY n 
1 98  ASN n 
1 99  PHE n 
1 100 ASN n 
1 101 ASP n 
1 102 TYR n 
1 103 GLU n 
1 104 GLU n 
1 105 LEU n 
1 106 LYS n 
1 107 HIS n 
1 108 LEU n 
1 109 LEU n 
1 110 SER n 
1 111 ARG n 
1 112 ILE n 
1 113 ASN n 
1 114 HIS n 
1 115 PHE n 
1 116 GLU n 
1 117 LYS n 
1 118 ILE n 
1 119 GLN n 
1 120 ILE n 
1 121 THR n 
1 122 PRO n 
1 123 LYS n 
1 124 ASN n 
1 125 SER n 
1 126 TRP n 
1 127 SER n 
1 128 ASP n 
1 129 HIS n 
1 130 GLU n 
1 131 ALA n 
1 132 SER n 
1 133 GLY n 
1 134 VAL n 
1 135 SER n 
1 136 SER n 
1 137 ALA n 
1 138 CYS n 
1 139 PRO n 
1 140 TYR n 
1 141 GLN n 
1 142 GLY n 
1 143 ARG n 
1 144 SER n 
1 145 SER n 
1 146 PHE n 
1 147 PHE n 
1 148 ARG n 
1 149 ASN n 
1 150 VAL n 
1 151 VAL n 
1 152 TRP n 
1 153 LEU n 
1 154 THR n 
1 155 LYS n 
1 156 LYS n 
1 157 ASP n 
1 158 ASN n 
1 159 ALA n 
1 160 TYR n 
1 161 PRO n 
1 162 THR n 
1 163 ILE n 
1 164 LYS n 
1 165 ARG n 
1 166 SER n 
1 167 TYR n 
1 168 ASN n 
1 169 ASN n 
1 170 THR n 
1 171 ASN n 
1 172 GLN n 
1 173 GLU n 
1 174 ASP n 
1 175 LEU n 
1 176 LEU n 
1 177 VAL n 
1 178 LEU n 
1 179 TRP n 
1 180 GLY n 
1 181 ILE n 
1 182 HIS n 
1 183 HIS n 
1 184 PRO n 
1 185 ASN n 
1 186 ASP n 
1 187 ALA n 
1 188 THR n 
1 189 GLU n 
1 190 GLN n 
1 191 THR n 
1 192 ARG n 
1 193 LEU n 
1 194 TYR n 
1 195 GLN n 
1 196 ASN n 
1 197 PRO n 
1 198 THR n 
1 199 THR n 
1 200 TYR n 
1 201 ILE n 
1 202 SER n 
1 203 VAL n 
1 204 GLY n 
1 205 THR n 
1 206 SER n 
1 207 THR n 
1 208 LEU n 
1 209 ASN n 
1 210 GLN n 
1 211 LYS n 
1 212 LEU n 
1 213 VAL n 
1 214 PRO n 
1 215 LYS n 
1 216 ILE n 
1 217 ALA n 
1 218 THR n 
1 219 ARG n 
1 220 SER n 
1 221 LYS n 
1 222 VAL n 
1 223 LYS n 
1 224 GLY n 
1 225 LEU n 
1 226 SER n 
1 227 GLY n 
1 228 ARG n 
1 229 MET n 
1 230 GLU n 
1 231 PHE n 
1 232 PHE n 
1 233 TRP n 
1 234 THR n 
1 235 ILE n 
1 236 LEU n 
1 237 LYS n 
1 238 SER n 
1 239 ASN n 
1 240 ASP n 
1 241 ALA n 
1 242 ILE n 
1 243 ASN n 
1 244 PHE n 
1 245 GLU n 
1 246 SER n 
1 247 ASN n 
1 248 GLY n 
1 249 ASN n 
1 250 PHE n 
1 251 ILE n 
1 252 ALA n 
1 253 PRO n 
1 254 GLU n 
1 255 ASN n 
1 256 ALA n 
1 257 TYR n 
1 258 LYS n 
1 259 ILE n 
1 260 VAL n 
1 261 LYS n 
1 262 LYS n 
1 263 GLY n 
1 264 ASP n 
1 265 SER n 
1 266 THR n 
1 267 ILE n 
1 268 MET n 
1 269 LYS n 
1 270 SER n 
1 271 GLU n 
1 272 LEU n 
1 273 GLU n 
1 274 TYR n 
1 275 GLY n 
1 276 ASP n 
1 277 CYS n 
1 278 ASN n 
1 279 THR n 
1 280 LYS n 
1 281 CYS n 
1 282 GLN n 
1 283 THR n 
1 284 PRO n 
1 285 ILE n 
1 286 GLY n 
1 287 ALA n 
1 288 ILE n 
1 289 ASN n 
1 290 SER n 
1 291 SER n 
1 292 MET n 
1 293 PRO n 
1 294 PHE n 
1 295 HIS n 
1 296 ASN n 
1 297 ILE n 
1 298 HIS n 
1 299 PRO n 
1 300 LEU n 
1 301 THR n 
1 302 ILE n 
1 303 GLY n 
1 304 GLU n 
1 305 CYS n 
1 306 PRO n 
1 307 LYS n 
1 308 TYR n 
1 309 VAL n 
1 310 LYS n 
1 311 SER n 
1 312 ASN n 
1 313 ARG n 
1 314 LEU n 
1 315 VAL n 
1 316 LEU n 
1 317 ALA n 
1 318 THR n 
1 319 GLY n 
1 320 LEU n 
1 321 ARG n 
1 322 ASN n 
1 323 SER n 
1 324 PRO n 
1 325 GLN n 
1 326 GLY n 
1 327 GLU n 
1 328 ARG n 
1 329 ARG n 
1 330 ARG n 
1 331 LYS n 
1 332 LYS n 
1 333 ARG n 
2 1   GLY n 
2 2   LEU n 
2 3   PHE n 
2 4   GLY n 
2 5   ALA n 
2 6   ILE n 
2 7   ALA n 
2 8   GLY n 
2 9   PHE n 
2 10  ILE n 
2 11  GLU n 
2 12  GLY n 
2 13  GLY n 
2 14  TRP n 
2 15  GLN n 
2 16  GLY n 
2 17  MET n 
2 18  VAL n 
2 19  ASP n 
2 20  GLY n 
2 21  TRP n 
2 22  TYR n 
2 23  GLY n 
2 24  TYR n 
2 25  HIS n 
2 26  HIS n 
2 27  SER n 
2 28  ASN n 
2 29  GLU n 
2 30  GLN n 
2 31  GLY n 
2 32  SER n 
2 33  GLY n 
2 34  TYR n 
2 35  ALA n 
2 36  ALA n 
2 37  ASP n 
2 38  LYS n 
2 39  GLU n 
2 40  SER n 
2 41  THR n 
2 42  GLN n 
2 43  LYS n 
2 44  ALA n 
2 45  ILE n 
2 46  ASP n 
2 47  GLY n 
2 48  VAL n 
2 49  THR n 
2 50  ASN n 
2 51  LYS n 
2 52  VAL n 
2 53  ASN n 
2 54  SER n 
2 55  ILE n 
2 56  ILE n 
2 57  ASP n 
2 58  LYS n 
2 59  MET n 
2 60  ASN n 
2 61  THR n 
2 62  GLN n 
2 63  PHE n 
2 64  GLU n 
2 65  ALA n 
2 66  VAL n 
2 67  GLY n 
2 68  ARG n 
2 69  GLU n 
2 70  PHE n 
2 71  ASN n 
2 72  ASN n 
2 73  LEU n 
2 74  GLU n 
2 75  ARG n 
2 76  ARG n 
2 77  ILE n 
2 78  GLU n 
2 79  ASN n 
2 80  LEU n 
2 81  ASN n 
2 82  LYS n 
2 83  LYS n 
2 84  MET n 
2 85  GLU n 
2 86  ASP n 
2 87  GLY n 
2 88  PHE n 
2 89  LEU n 
2 90  ASP n 
2 91  VAL n 
2 92  TRP n 
2 93  THR n 
2 94  TYR n 
2 95  ASN n 
2 96  ALA n 
2 97  GLU n 
2 98  LEU n 
2 99  LEU n 
2 100 VAL n 
2 101 LEU n 
2 102 MET n 
2 103 GLU n 
2 104 ASN n 
2 105 GLU n 
2 106 ARG n 
2 107 THR n 
2 108 LEU n 
2 109 ASP n 
2 110 PHE n 
2 111 HIS n 
2 112 ASP n 
2 113 SER n 
2 114 ASN n 
2 115 VAL n 
2 116 LYS n 
2 117 ASN n 
2 118 LEU n 
2 119 TYR n 
2 120 ASP n 
2 121 LYS n 
2 122 VAL n 
2 123 ARG n 
2 124 LEU n 
2 125 GLN n 
2 126 LEU n 
2 127 ARG n 
2 128 ASP n 
2 129 ASN n 
2 130 ALA n 
2 131 LYS n 
2 132 GLU n 
2 133 LEU n 
2 134 GLY n 
2 135 ASN n 
2 136 GLY n 
2 137 CYS n 
2 138 PHE n 
2 139 GLU n 
2 140 PHE n 
2 141 TYR n 
2 142 HIS n 
2 143 ARG n 
2 144 CYS n 
2 145 ASP n 
2 146 ASN n 
2 147 GLU n 
2 148 CYS n 
2 149 MET n 
2 150 GLU n 
2 151 SER n 
2 152 VAL n 
2 153 ARG n 
2 154 ASN n 
2 155 GLY n 
2 156 THR n 
2 157 TYR n 
2 158 ASP n 
2 159 TYR n 
2 160 PRO n 
2 161 GLN n 
2 162 TYR n 
2 163 SER n 
2 164 GLU n 
2 165 GLU n 
2 166 ALA n 
2 167 ARG n 
2 168 LEU n 
2 169 LYS n 
2 170 ARG n 
2 171 GLU n 
2 172 GLU n 
2 173 ILE n 
2 174 SER n 
2 175 GLY n 
2 176 ARG n 
2 177 LEU n 
2 178 VAL n 
2 179 PRO n 
2 180 ARG n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 333 ? ? HA ? 'A/duck/Egypt/10185SS/2010(H5N1)' ? ? ? ? 
'Influenza A virus (A/duck/Egypt/10185SS/2010(H5N1))' 1092915 ? ? ? ? ? ? ? ? 'TRICHOPLUSIA NI' 7111 ? ? ? ? ? ? Hi5 ? ? ? ? ? ? ? 
BACULOVIRUS ? ?           ? PFASTBAC-HT ? ? 
2 1 sample 'Biological sequence' 1 180 ? ? HA ? 'A/duck/Egypt/10185SS/2010(H5N1)' ? ? ? ? 'Influenza A virus' 1092915 ? ? ? ? ? ? 
? ? 'TRICHOPLUSIA NI' 7111 ? ? ? ? ? ? Hi5 ? ? ? ? ? ? ? ?           ? PFASTBAC-HT ? BACULOVIRUS ? ? 
# 
loop_
_struct_ref.db_code 
_struct_ref.db_name 
_struct_ref.details 
_struct_ref.entity_id 
_struct_ref.id 
_struct_ref.seq_align 
_struct_ref.seq_dif 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_align_end 
G8IPF0_9INFA UNP ? 1 1 ? ? G8IPF0 ? 
;DQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCNLDGVKPLILRDCSVAGWLLGNPMCDEFLNVPEWSYIV
EKINPANDLCYPGNFNDYEELKHLLSRINHFEKIQITPKNSWSDHEASGVSSACPYQGRSSFFRNVVWLTKKDNAYPTIK
RSYNNTNQEDLLVLWGIHHPNDATEQTRLYQNPTTYISVGTSTLNQKLVPKIATRSKVKGQSGRMEFFWTILKSNDAINF
ESNGNFIAPENAYKIVKKGDSTIMKSELEYGDCNTKCQTPIGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNSP
QGERRRKKR
;
17  ? 
G8IPF0_9INFA UNP ? 2 2 ? ? G8IPF0 ? 
;LFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENLN
KKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHRCDNECMESVRNGTYDYPQ
YSEEARLKREEISG
;
347 ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 5E2Z C 5 ? 333 ? G8IPF0 17  ? 345 ? 11 333 
2 2 5E2Z D 2 ? 175 ? G8IPF0 347 ? 520 ? 2  175 
3 1 5E2Z A 5 ? 333 ? G8IPF0 17  ? 345 ? 11 333 
4 2 5E2Z B 2 ? 175 ? G8IPF0 347 ? 520 ? 2  175 
5 1 5E2Z E 5 ? 333 ? G8IPF0 17  ? 345 ? 11 333 
6 2 5E2Z F 2 ? 175 ? G8IPF0 347 ? 520 ? 2  175 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 5E2Z ALA C 1   ? UNP G8IPF0 ?   ?   'expression tag'      7   1  
1 5E2Z ASP C 2   ? UNP G8IPF0 ?   ?   'expression tag'      8   2  
1 5E2Z PRO C 3   ? UNP G8IPF0 ?   ?   'expression tag'      9   3  
1 5E2Z GLY C 4   ? UNP G8IPF0 ?   ?   'expression tag'      10  4  
1 5E2Z LEU C 225 ? UNP G8IPF0 GLN 237 'engineered mutation' 226 5  
2 5E2Z GLY D 1   ? UNP G8IPF0 ?   ?   'expression tag'      1   6  
2 5E2Z ARG D 176 ? UNP G8IPF0 ?   ?   'expression tag'      176 7  
2 5E2Z LEU D 177 ? UNP G8IPF0 ?   ?   'expression tag'      177 8  
2 5E2Z VAL D 178 ? UNP G8IPF0 ?   ?   'expression tag'      178 9  
2 5E2Z PRO D 179 ? UNP G8IPF0 ?   ?   'expression tag'      179 10 
2 5E2Z ARG D 180 ? UNP G8IPF0 ?   ?   'expression tag'      180 11 
3 5E2Z ALA A 1   ? UNP G8IPF0 ?   ?   'expression tag'      7   12 
3 5E2Z ASP A 2   ? UNP G8IPF0 ?   ?   'expression tag'      8   13 
3 5E2Z PRO A 3   ? UNP G8IPF0 ?   ?   'expression tag'      9   14 
3 5E2Z GLY A 4   ? UNP G8IPF0 ?   ?   'expression tag'      10  15 
3 5E2Z LEU A 225 ? UNP G8IPF0 GLN 237 'engineered mutation' 226 16 
4 5E2Z GLY B 1   ? UNP G8IPF0 ?   ?   'expression tag'      1   17 
4 5E2Z ARG B 176 ? UNP G8IPF0 ?   ?   'expression tag'      176 18 
4 5E2Z LEU B 177 ? UNP G8IPF0 ?   ?   'expression tag'      177 19 
4 5E2Z VAL B 178 ? UNP G8IPF0 ?   ?   'expression tag'      178 20 
4 5E2Z PRO B 179 ? UNP G8IPF0 ?   ?   'expression tag'      179 21 
4 5E2Z ARG B 180 ? UNP G8IPF0 ?   ?   'expression tag'      180 22 
5 5E2Z ALA E 1   ? UNP G8IPF0 ?   ?   'expression tag'      7   23 
5 5E2Z ASP E 2   ? UNP G8IPF0 ?   ?   'expression tag'      8   24 
5 5E2Z PRO E 3   ? UNP G8IPF0 ?   ?   'expression tag'      9   25 
5 5E2Z GLY E 4   ? UNP G8IPF0 ?   ?   'expression tag'      10  26 
5 5E2Z LEU E 225 ? UNP G8IPF0 GLN 237 'engineered mutation' 226 27 
6 5E2Z GLY F 1   ? UNP G8IPF0 ?   ?   'expression tag'      1   28 
6 5E2Z ARG F 176 ? UNP G8IPF0 ?   ?   'expression tag'      176 29 
6 5E2Z LEU F 177 ? UNP G8IPF0 ?   ?   'expression tag'      177 30 
6 5E2Z VAL F 178 ? UNP G8IPF0 ?   ?   'expression tag'      178 31 
6 5E2Z PRO F 179 ? UNP G8IPF0 ?   ?   'expression tag'      179 32 
6 5E2Z ARG F 180 ? UNP G8IPF0 ?   ?   'expression tag'      180 33 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ?                        'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ?                        'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ?                        'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ?                        'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE               ?                        'C3 H7 N O2 S'   121.158 
FUC saccharide          . ALPHA-L-FUCOSE         ?                        'C6 H12 O5'      164.156 
FUL L-saccharide        . BETA-L-FUCOSE          6-DEOXY-BETA-L-GALACTOSE 'C6 H12 O5'      164.156 
GAL D-saccharide        . BETA-D-GALACTOSE       ?                        'C6 H12 O6'      180.156 
GLN 'L-peptide linking' y GLUTAMINE              ?                        'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ?                        'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                ?                        'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE              ?                        'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                  ?                        'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE             ?                        'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                ?                        'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                 ?                        'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE             ?                        'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ?                        'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE          ?                        'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                ?                        'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                 ?                        'C3 H7 N O3'     105.093 
SIA non-polymer         . 'O-SIALIC ACID'        ?                        'C11 H19 N O9'   309.270 
THR 'L-peptide linking' y THREONINE              ?                        'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN             ?                        'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE               ?                        'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                 ?                        'C5 H11 N O2'    117.146 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   5E2Z 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            3.3 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         61.66 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            295 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.085 M Tris, pH 8.5, 10% (v/v) glycerol, 0.17% (w/v) sodium acetate, 21% (w/v) PEG4000.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 300 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-06-15 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.03314 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 23-ID-B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.03314 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-B 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5E2Z 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.60 
_reflns.d_resolution_low                 50.0 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       57187 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             89.4 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.3 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.11 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            17.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  2.60 
_reflns_shell.d_res_low                   2.64 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         1.6 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           ? 
_reflns_shell.percent_possible_all        87.6 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                0.88 
_reflns_shell.meanI_over_sigI_gt          ? 
_reflns_shell.meanI_over_uI_all           ? 
_reflns_shell.meanI_over_uI_gt            ? 
_reflns_shell.number_measured_gt          ? 
_reflns_shell.number_unique_gt            ? 
_reflns_shell.percent_possible_gt         ? 
_reflns_shell.Rmerge_F_gt                 ? 
_reflns_shell.Rmerge_I_gt                 ? 
_reflns_shell.pdbx_redundancy             3.0 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 5E2Z 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.624 
_refine.ls_d_res_low                             50.0 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     57132 
_refine.ls_number_reflns_R_free                  2919 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    86.78 
_refine.ls_percent_reflns_R_free                 5.11 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2046 
_refine.ls_R_factor_R_free                       0.2485 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2023 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.38 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      5E2Y 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 28.08 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.38 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        11928 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         274 
_refine_hist.number_atoms_solvent             167 
_refine_hist.number_atoms_total               12369 
_refine_hist.d_res_high                       2.624 
_refine_hist.d_res_low                        50.0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  ? 12501 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.297  ? 16928 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.257 ? 4678  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.060  ? 1850  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 2191  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 2.624  2.6670  . . 66  1359 46.00  . . . 0.4641 . 0.3280 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.6670 2.7130  . . 143 2446 82.00  . . . 0.3321 . 0.2945 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.7130 2.7623  . . 132 2567 87.00  . . . 0.3672 . 0.2917 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.7623 2.8154  . . 138 2577 86.00  . . . 0.3163 . 0.2757 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.8154 2.8729  . . 137 2553 86.00  . . . 0.3152 . 0.2700 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.8729 2.9353  . . 142 2540 86.00  . . . 0.3126 . 0.2556 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.9353 3.0036  . . 123 2557 85.00  . . . 0.2929 . 0.2561 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.0036 3.0787  . . 143 2538 86.00  . . . 0.3250 . 0.2583 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.0787 3.1619  . . 141 2544 85.00  . . . 0.2844 . 0.2482 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.1619 3.2550  . . 136 2476 85.00  . . . 0.2887 . 0.2458 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.2550 3.3600  . . 131 2541 85.00  . . . 0.2869 . 0.2336 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.3600 3.4801  . . 136 2491 83.00  . . . 0.3107 . 0.2336 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.4801 3.6193  . . 153 2470 84.00  . . . 0.2762 . 0.2225 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.6193 3.7840  . . 146 2522 85.00  . . . 0.2761 . 0.2041 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.7840 3.9834  . . 147 2595 88.00  . . . 0.2471 . 0.1950 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.9834 4.2329  . . 144 2749 92.00  . . . 0.2262 . 0.1807 . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.2329 4.5595  . . 139 2899 95.00  . . . 0.2244 . 0.1642 . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.5595 5.0179  . . 146 2836 97.00  . . . 0.1920 . 0.1575 . . . . . . . . . . 
'X-RAY DIFFRACTION' 5.0179 5.7430  . . 162 2983 100.00 . . . 0.2038 . 0.1689 . . . . . . . . . . 
'X-RAY DIFFRACTION' 5.7430 7.2317  . . 135 3007 100.00 . . . 0.2272 . 0.1920 . . . . . . . . . . 
'X-RAY DIFFRACTION' 7.2317 48.4291 . . 179 2963 99.00  . . . 0.1965 . 0.1730 . . . . . . . . . . 
# 
_struct.entry_id                     5E2Z 
_struct.title                        
'Crystal structure of H5 hemagglutinin Q226L mutant from the influenza virus A/duck/Egypt/10185SS/2010 (H5N1) with LSTa' 
_struct.pdbx_descriptor              Hemagglutinin 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5E2Z 
_struct_keywords.text            
'H5N1 influenza virus, hemagglutinin, receptor binding specificity, transmission, glycan complex, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 2 ? 
C  N N 1 ? 
D  N N 2 ? 
E  N N 1 ? 
F  N N 2 ? 
G  N N 3 ? 
H  N N 3 ? 
I  N N 4 ? 
J  N N 3 ? 
K  N N 5 ? 
L  N N 6 ? 
M  N N 3 ? 
N  N N 3 ? 
O  N N 7 ? 
P  N N 4 ? 
Q  N N 3 ? 
R  N N 5 ? 
S  N N 6 ? 
T  N N 3 ? 
U  N N 3 ? 
V  N N 3 ? 
W  N N 4 ? 
X  N N 3 ? 
Y  N N 5 ? 
Z  N N 6 ? 
AA N N 8 ? 
BA N N 8 ? 
CA N N 8 ? 
DA N N 8 ? 
EA N N 8 ? 
FA N N 8 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 60  ? GLY A 67  ? SER C 65  GLY C 72  1 ? 8  
HELX_P HELX_P2  AA2 ASN A 68  ? LEU A 75  ? ASN C 73  LEU C 80  5 ? 8  
HELX_P HELX_P3  AA3 ASP A 101 ? SER A 110 ? ASP C 104 SER C 113 1 ? 10 
HELX_P HELX_P4  AA4 PRO A 122 ? TRP A 126 ? PRO C 125 TRP C 127 5 ? 5  
HELX_P HELX_P5  AA5 ASP A 186 ? GLN A 195 ? ASP C 187 GLN C 196 1 ? 10 
HELX_P HELX_P6  AA6 ASP B 37  ? LYS B 58  ? ASP D 37  LYS D 58  1 ? 22 
HELX_P HELX_P7  AA7 GLU B 74  ? ARG B 127 ? GLU D 74  ARG D 127 1 ? 54 
HELX_P HELX_P8  AA8 CYS B 148 ? ASN B 154 ? CYS D 148 ASN D 154 1 ? 7  
HELX_P HELX_P9  AA9 ASP B 158 ? GLN B 161 ? ASP D 158 GLN D 161 5 ? 4  
HELX_P HELX_P10 AB1 TYR B 162 ? SER B 174 ? TYR D 162 SER D 174 1 ? 13 
HELX_P HELX_P11 AB2 SER C 60  ? GLY C 67  ? SER A 65  GLY A 72  1 ? 8  
HELX_P HELX_P12 AB3 ASN C 68  ? LEU C 75  ? ASN A 73  LEU A 80  5 ? 8  
HELX_P HELX_P13 AB4 ASP C 101 ? LEU C 109 ? ASP A 104 LEU A 112 1 ? 9  
HELX_P HELX_P14 AB5 PRO C 122 ? TRP C 126 ? PRO A 125 TRP A 127 5 ? 5  
HELX_P HELX_P15 AB6 ASP C 186 ? GLN C 195 ? ASP A 187 GLN A 196 1 ? 10 
HELX_P HELX_P16 AB7 ASP D 37  ? LYS D 58  ? ASP B 37  LYS B 58  1 ? 22 
HELX_P HELX_P17 AB8 GLU D 74  ? ARG D 127 ? GLU B 74  ARG B 127 1 ? 54 
HELX_P HELX_P18 AB9 CYS D 148 ? ASN D 154 ? CYS B 148 ASN B 154 1 ? 7  
HELX_P HELX_P19 AC1 TYR D 162 ? SER D 174 ? TYR B 162 SER B 174 1 ? 13 
HELX_P HELX_P20 AC2 SER E 60  ? GLY E 67  ? SER E 65  GLY E 72  1 ? 8  
HELX_P HELX_P21 AC3 ASN E 68  ? LEU E 75  ? ASN E 73  LEU E 80  5 ? 8  
HELX_P HELX_P22 AC4 ASP E 101 ? LEU E 109 ? ASP E 104 LEU E 112 1 ? 9  
HELX_P HELX_P23 AC5 PRO E 122 ? TRP E 126 ? PRO E 125 TRP E 127 5 ? 5  
HELX_P HELX_P24 AC6 ASP E 186 ? GLN E 195 ? ASP E 187 GLN E 196 1 ? 10 
HELX_P HELX_P25 AC7 ASP F 37  ? LYS F 58  ? ASP F 37  LYS F 58  1 ? 22 
HELX_P HELX_P26 AC8 GLU F 74  ? ARG F 127 ? GLU F 74  ARG F 127 1 ? 54 
HELX_P HELX_P27 AC9 CYS F 148 ? ASN F 154 ? CYS F 148 ASN F 154 1 ? 7  
HELX_P HELX_P28 AD1 TYR F 159 ? SER F 174 ? TYR F 159 SER F 174 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ?    ? A CYS 8   SG  ? ? ? 1_555 B CYS 137 SG ? ? C CYS 14   D CYS 137  1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf2  disulf ?    ? A CYS 46  SG  ? ? ? 1_555 A CYS 277 SG ? ? C CYS 52   C CYS 277  1_555 ? ? ? ? ? ? ? 2.069 ? 
disulf3  disulf ?    ? A CYS 59  SG  ? ? ? 1_555 A CYS 71  SG ? ? C CYS 64   C CYS 76   1_555 ? ? ? ? ? ? ? 2.078 ? 
disulf4  disulf ?    ? A CYS 94  SG  ? ? ? 1_555 A CYS 138 SG ? ? C CYS 97   C CYS 139  1_555 ? ? ? ? ? ? ? 2.076 ? 
disulf5  disulf ?    ? A CYS 281 SG  ? ? ? 1_555 A CYS 305 SG ? ? C CYS 281  C CYS 305  1_555 ? ? ? ? ? ? ? 2.053 ? 
disulf6  disulf ?    ? B CYS 144 SG  ? ? ? 1_555 B CYS 148 SG ? ? D CYS 144  D CYS 148  1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf7  disulf ?    ? C CYS 8   SG  ? ? ? 1_555 D CYS 137 SG ? ? A CYS 14   B CYS 137  1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf8  disulf ?    ? C CYS 46  SG  ? ? ? 1_555 C CYS 277 SG ? ? A CYS 52   A CYS 277  1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf9  disulf ?    ? C CYS 59  SG  ? ? ? 1_555 C CYS 71  SG ? ? A CYS 64   A CYS 76   1_555 ? ? ? ? ? ? ? 2.059 ? 
disulf10 disulf ?    ? C CYS 94  SG  ? ? ? 1_555 C CYS 138 SG ? ? A CYS 97   A CYS 139  1_555 ? ? ? ? ? ? ? 2.101 ? 
disulf11 disulf ?    ? C CYS 281 SG  ? ? ? 1_555 C CYS 305 SG ? ? A CYS 281  A CYS 305  1_555 ? ? ? ? ? ? ? 2.057 ? 
disulf12 disulf ?    ? D CYS 144 SG  ? ? ? 1_555 D CYS 148 SG ? ? B CYS 144  B CYS 148  1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf13 disulf ?    ? E CYS 8   SG  ? ? ? 1_555 F CYS 137 SG ? ? E CYS 14   F CYS 137  1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf14 disulf ?    ? E CYS 46  SG  ? ? ? 1_555 E CYS 277 SG ? ? E CYS 52   E CYS 277  1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf15 disulf ?    ? E CYS 59  SG  ? ? ? 1_555 E CYS 71  SG ? ? E CYS 64   E CYS 76   1_555 ? ? ? ? ? ? ? 2.052 ? 
disulf16 disulf ?    ? E CYS 94  SG  ? ? ? 1_555 E CYS 138 SG ? ? E CYS 97   E CYS 139  1_555 ? ? ? ? ? ? ? 2.087 ? 
disulf17 disulf ?    ? E CYS 281 SG  ? ? ? 1_555 E CYS 305 SG ? ? E CYS 281  E CYS 305  1_555 ? ? ? ? ? ? ? 2.045 ? 
disulf18 disulf ?    ? F CYS 144 SG  ? ? ? 1_555 F CYS 148 SG ? ? F CYS 144  F CYS 148  1_555 ? ? ? ? ? ? ? 2.045 ? 
covale1  covale one  ? A ASN 27  ND2 ? ? ? 1_555 G NAG .   C1 ? ? C ASN 33   C NAG 1001 1_555 ? ? ? ? ? ? ? 1.454 ? 
covale2  covale one  ? A ASN 168 ND2 ? ? ? 1_555 H NAG .   C1 ? ? C ASN 169  C NAG 1002 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale3  covale one  ? C ASN 27  ND2 ? ? ? 1_555 M NAG .   C1 ? ? A ASN 33   A NAG 1001 1_555 ? ? ? ? ? ? ? 1.452 ? 
covale4  covale one  ? C ASN 168 ND2 ? ? ? 1_555 N NAG .   C1 ? ? A ASN 169  A NAG 1002 1_555 ? ? ? ? ? ? ? 1.455 ? 
covale5  covale one  ? E ASN 27  ND2 ? ? ? 1_555 U NAG .   C1 ? ? E ASN 33   E NAG 1001 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale6  covale one  ? E ASN 168 ND2 ? ? ? 1_555 V NAG .   C1 ? ? E ASN 169  E NAG 1002 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale7  covale one  ? H NAG .   O3  ? ? ? 1_555 I FUL .   C1 ? ? C NAG 1002 C FUL 1003 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale8  covale both ? H NAG .   O4  ? ? ? 1_555 J NAG .   C1 ? ? C NAG 1002 C NAG 1004 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale9  covale one  ? K SIA .   C2  ? ? ? 1_555 L GAL .   O3 ? ? C SIA 1005 C GAL 1006 1_555 ? ? ? ? ? ? ? 1.465 ? 
covale10 covale one  ? N NAG .   O3  ? ? ? 1_555 P FUL .   C1 ? ? A NAG 1002 A FUL 1004 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale11 covale both ? N NAG .   O4  ? ? ? 1_555 Q NAG .   C1 ? ? A NAG 1002 A NAG 1005 1_555 ? ? ? ? ? ? ? 1.454 ? 
covale12 covale one  ? N NAG .   O6  ? ? ? 1_555 O FUC .   C1 ? ? A NAG 1002 A FUC 1003 1_555 ? ? ? ? ? ? ? 1.456 ? 
covale13 covale one  ? R SIA .   C2  ? ? ? 1_555 S GAL .   O3 ? ? A SIA 1006 A GAL 1007 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale14 covale one  ? S GAL .   C1  ? ? ? 1_555 T NAG .   O3 ? ? A GAL 1007 A NAG 1008 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale15 covale one  ? V NAG .   O3  ? ? ? 1_555 W FUL .   C1 ? ? E NAG 1002 E FUL 1003 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale16 covale both ? V NAG .   O4  ? ? ? 1_555 X NAG .   C1 ? ? E NAG 1002 E NAG 1004 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale17 covale one  ? Y SIA .   C2  ? ? ? 1_555 Z GAL .   O3 ? ? E SIA 1005 E GAL 1006 1_555 ? ? ? ? ? ? ? 1.474 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 5 ? 
AA8 ? 6 ? 
AA9 ? 2 ? 
AB1 ? 4 ? 
AB2 ? 3 ? 
AB3 ? 5 ? 
AB4 ? 2 ? 
AB5 ? 2 ? 
AB6 ? 3 ? 
AB7 ? 2 ? 
AB8 ? 3 ? 
AB9 ? 5 ? 
AC1 ? 5 ? 
AC2 ? 2 ? 
AC3 ? 4 ? 
AC4 ? 3 ? 
AC5 ? 5 ? 
AC6 ? 2 ? 
AC7 ? 2 ? 
AC8 ? 3 ? 
AC9 ? 2 ? 
AD1 ? 3 ? 
AD2 ? 5 ? 
AD3 ? 5 ? 
AD4 ? 2 ? 
AD5 ? 2 ? 
AD6 ? 4 ? 
AD7 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA5 1 2 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB7 1 2 ? parallel      
AB8 1 2 ? parallel      
AB8 2 3 ? parallel      
AB9 1 2 ? parallel      
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AB9 4 5 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC1 4 5 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC5 2 3 ? anti-parallel 
AC5 3 4 ? anti-parallel 
AC5 4 5 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC7 1 2 ? anti-parallel 
AC8 1 2 ? parallel      
AC8 2 3 ? parallel      
AC9 1 2 ? parallel      
AD1 1 2 ? parallel      
AD1 2 3 ? parallel      
AD2 1 2 ? parallel      
AD2 2 3 ? anti-parallel 
AD2 3 4 ? anti-parallel 
AD2 4 5 ? anti-parallel 
AD3 1 2 ? parallel      
AD3 2 3 ? anti-parallel 
AD3 3 4 ? anti-parallel 
AD3 4 5 ? anti-parallel 
AD4 1 2 ? anti-parallel 
AD5 1 2 ? anti-parallel 
AD6 1 2 ? anti-parallel 
AD6 2 3 ? anti-parallel 
AD6 3 4 ? anti-parallel 
AD7 1 2 ? anti-parallel 
AD7 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR B 34  ? ALA B 36  ? TYR D 34  ALA D 36  
AA1 2 TYR B 22  ? SER B 27  ? TYR D 22  SER D 27  
AA1 3 GLN A 6   ? TYR A 11  ? GLN C 12  TYR C 17  
AA1 4 CYS B 137 ? PHE B 140 ? CYS D 137 PHE D 140 
AA1 5 ALA B 130 ? GLU B 132 ? ALA D 130 GLU D 132 
AA2 1 GLN A 19  ? VAL A 20  ? GLN C 25  VAL C 26  
AA2 2 VAL A 28  ? THR A 29  ? VAL C 34  THR C 35  
AA3 1 ALA A 33  ? ASP A 35  ? ALA C 39  ASP C 41  
AA3 2 VAL A 315 ? ALA A 317 ? VAL C 315 ALA C 317 
AA4 1 LEU A 37  ? GLU A 38  ? LEU C 43  GLU C 44  
AA4 2 PHE A 294 ? HIS A 295 ? PHE C 294 HIS C 295 
AA4 3 LYS A 307 ? TYR A 308 ? LYS C 307 TYR C 308 
AA5 1 LEU A 45  ? LEU A 48  ? LEU C 51  LEU C 54  
AA5 2 TYR A 274 ? THR A 279 ? TYR C 274 THR C 279 
AA6 1 LEU A 54  ? ILE A 55  ? LEU C 59  ILE C 60  
AA6 2 ILE A 83  ? GLU A 85  ? ILE C 87  GLU C 89  
AA6 3 ILE A 267 ? LYS A 269 ? ILE C 267 LYS C 269 
AA7 1 GLY A 97  ? PHE A 99  ? GLY C 100 PHE C 102 
AA7 2 ARG A 228 ? LEU A 236 ? ARG C 229 LEU C 237 
AA7 3 LEU A 175 ? HIS A 183 ? LEU C 176 HIS C 184 
AA7 4 ASN A 255 ? LYS A 262 ? ASN C 256 LYS C 262 
AA7 5 ILE A 112 ? GLN A 119 ? ILE C 115 GLN C 122 
AA8 1 GLY A 97  ? PHE A 99  ? GLY C 100 PHE C 102 
AA8 2 ARG A 228 ? LEU A 236 ? ARG C 229 LEU C 237 
AA8 3 LEU A 175 ? HIS A 183 ? LEU C 176 HIS C 184 
AA8 4 PHE A 250 ? PRO A 253 ? PHE C 251 PRO C 254 
AA8 5 VAL A 150 ? THR A 154 ? VAL C 151 THR C 155 
AA8 6 GLU A 130 ? ALA A 131 ? GLU C 131 ALA C 132 
AA9 1 SER A 135 ? PRO A 139 ? SER C 136 PRO C 140 
AA9 2 SER A 144 ? SER A 145 ? SER C 145 SER C 146 
AB1 1 ILE A 163 ? ASN A 168 ? ILE C 164 ASN C 169 
AB1 2 ALA A 241 ? SER A 246 ? ALA C 242 SER C 247 
AB1 3 ILE A 201 ? GLY A 204 ? ILE C 202 GLY C 205 
AB1 4 ASN A 209 ? LEU A 212 ? ASN C 210 LEU C 213 
AB2 1 GLY A 286 ? ALA A 287 ? GLY C 286 ALA C 287 
AB2 2 CYS A 281 ? THR A 283 ? CYS C 281 THR C 283 
AB2 3 ILE A 302 ? GLY A 303 ? ILE C 302 GLY C 303 
AB3 1 TYR D 34  ? ALA D 36  ? TYR B 34  ALA B 36  
AB3 2 TYR D 22  ? SER D 27  ? TYR B 22  SER B 27  
AB3 3 GLN C 6   ? TYR C 11  ? GLN A 12  TYR A 17  
AB3 4 CYS D 137 ? PHE D 140 ? CYS B 137 PHE B 140 
AB3 5 ALA D 130 ? GLU D 132 ? ALA B 130 GLU B 132 
AB4 1 GLN C 19  ? VAL C 20  ? GLN A 25  VAL A 26  
AB4 2 VAL C 28  ? THR C 29  ? VAL A 34  THR A 35  
AB5 1 ALA C 33  ? ASP C 35  ? ALA A 39  ASP A 41  
AB5 2 VAL C 315 ? ALA C 317 ? VAL A 315 ALA A 317 
AB6 1 LEU C 37  ? GLU C 38  ? LEU A 43  GLU A 44  
AB6 2 PHE C 294 ? HIS C 295 ? PHE A 294 HIS A 295 
AB6 3 LYS C 307 ? TYR C 308 ? LYS A 307 TYR A 308 
AB7 1 LEU C 45  ? LEU C 48  ? LEU A 51  LEU A 54  
AB7 2 TYR C 274 ? THR C 279 ? TYR A 274 THR A 279 
AB8 1 LEU C 54  ? ILE C 55  ? LEU A 59  ILE A 60  
AB8 2 ILE C 83  ? GLU C 85  ? ILE A 87  GLU A 89  
AB8 3 ILE C 267 ? LYS C 269 ? ILE A 267 LYS A 269 
AB9 1 GLY C 97  ? PHE C 99  ? GLY A 100 PHE A 102 
AB9 2 ARG C 228 ? LEU C 236 ? ARG A 229 LEU A 237 
AB9 3 LEU C 175 ? HIS C 183 ? LEU A 176 HIS A 184 
AB9 4 ASN C 255 ? LYS C 262 ? ASN A 256 LYS A 262 
AB9 5 ILE C 112 ? GLN C 119 ? ILE A 115 GLN A 122 
AC1 1 GLY C 97  ? PHE C 99  ? GLY A 100 PHE A 102 
AC1 2 ARG C 228 ? LEU C 236 ? ARG A 229 LEU A 237 
AC1 3 LEU C 175 ? HIS C 183 ? LEU A 176 HIS A 184 
AC1 4 PHE C 250 ? PRO C 253 ? PHE A 251 PRO A 254 
AC1 5 VAL C 150 ? TRP C 152 ? VAL A 151 TRP A 153 
AC2 1 SER C 135 ? PRO C 139 ? SER A 136 PRO A 140 
AC2 2 SER C 144 ? SER C 145 ? SER A 145 SER A 146 
AC3 1 ILE C 163 ? ASN C 168 ? ILE A 164 ASN A 169 
AC3 2 ALA C 241 ? SER C 246 ? ALA A 242 SER A 247 
AC3 3 ILE C 201 ? GLY C 204 ? ILE A 202 GLY A 205 
AC3 4 ASN C 209 ? LEU C 212 ? ASN A 210 LEU A 213 
AC4 1 GLY C 286 ? ALA C 287 ? GLY A 286 ALA A 287 
AC4 2 CYS C 281 ? THR C 283 ? CYS A 281 THR A 283 
AC4 3 ILE C 302 ? GLY C 303 ? ILE A 302 GLY A 303 
AC5 1 TYR F 34  ? ALA F 36  ? TYR F 34  ALA F 36  
AC5 2 TYR F 22  ? SER F 27  ? TYR F 22  SER F 27  
AC5 3 GLN E 6   ? TYR E 11  ? GLN E 12  TYR E 17  
AC5 4 CYS F 137 ? PHE F 140 ? CYS F 137 PHE F 140 
AC5 5 ALA F 130 ? GLU F 132 ? ALA F 130 GLU F 132 
AC6 1 GLN E 19  ? VAL E 20  ? GLN E 25  VAL E 26  
AC6 2 VAL E 28  ? THR E 29  ? VAL E 34  THR E 35  
AC7 1 ALA E 33  ? ASP E 35  ? ALA E 39  ASP E 41  
AC7 2 VAL E 315 ? ALA E 317 ? VAL E 315 ALA E 317 
AC8 1 LEU E 37  ? GLU E 38  ? LEU E 43  GLU E 44  
AC8 2 PHE E 294 ? HIS E 295 ? PHE E 294 HIS E 295 
AC8 3 LYS E 307 ? TYR E 308 ? LYS E 307 TYR E 308 
AC9 1 LEU E 45  ? LEU E 48  ? LEU E 51  LEU E 54  
AC9 2 TYR E 274 ? THR E 279 ? TYR E 274 THR E 279 
AD1 1 LEU E 54  ? ILE E 55  ? LEU E 59  ILE E 60  
AD1 2 ILE E 83  ? GLU E 85  ? ILE E 87  GLU E 89  
AD1 3 ILE E 267 ? LYS E 269 ? ILE E 267 LYS E 269 
AD2 1 GLY E 97  ? PHE E 99  ? GLY E 100 PHE E 102 
AD2 2 ARG E 228 ? LEU E 236 ? ARG E 229 LEU E 237 
AD2 3 ASP E 174 ? HIS E 183 ? ASP E 175 HIS E 184 
AD2 4 ASN E 255 ? LYS E 262 ? ASN E 256 LYS E 262 
AD2 5 ILE E 112 ? GLN E 119 ? ILE E 115 GLN E 122 
AD3 1 GLY E 97  ? PHE E 99  ? GLY E 100 PHE E 102 
AD3 2 ARG E 228 ? LEU E 236 ? ARG E 229 LEU E 237 
AD3 3 ASP E 174 ? HIS E 183 ? ASP E 175 HIS E 184 
AD3 4 PHE E 250 ? PRO E 253 ? PHE E 251 PRO E 254 
AD3 5 VAL E 150 ? TRP E 152 ? VAL E 151 TRP E 153 
AD4 1 HIS E 129 ? GLU E 130 ? HIS E 130 GLU E 131 
AD4 2 THR E 154 ? LYS E 155 ? THR E 155 LYS E 156 
AD5 1 SER E 135 ? PRO E 139 ? SER E 136 PRO E 140 
AD5 2 SER E 144 ? SER E 145 ? SER E 145 SER E 146 
AD6 1 ILE E 163 ? ASN E 168 ? ILE E 164 ASN E 169 
AD6 2 ALA E 241 ? SER E 246 ? ALA E 242 SER E 247 
AD6 3 ILE E 201 ? GLY E 204 ? ILE E 202 GLY E 205 
AD6 4 ASN E 209 ? LEU E 212 ? ASN E 210 LEU E 213 
AD7 1 GLY E 286 ? ALA E 287 ? GLY E 286 ALA E 287 
AD7 2 CYS E 281 ? THR E 283 ? CYS E 281 THR E 283 
AD7 3 ILE E 302 ? GLY E 303 ? ILE E 302 GLY E 303 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_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 
AA1 1 2 O ALA B 35  ? O ALA D 35  N TYR B 24  ? N TYR D 24  
AA1 2 3 O HIS B 25  ? O HIS D 25  N CYS A 8   ? N CYS C 14  
AA1 3 4 N ILE A 7   ? N ILE C 13  O PHE B 138 ? O PHE D 138 
AA1 4 5 O GLU B 139 ? O GLU D 139 N LYS B 131 ? N LYS D 131 
AA2 1 2 N VAL A 20  ? N VAL C 26  O VAL A 28  ? O VAL C 34  
AA3 1 2 N GLN A 34  ? N GLN C 40  O LEU A 316 ? O LEU C 316 
AA4 1 2 N GLU A 38  ? N GLU C 44  O PHE A 294 ? O PHE C 294 
AA4 2 3 N HIS A 295 ? N HIS C 295 O LYS A 307 ? O LYS C 307 
AA5 1 2 N ASN A 47  ? N ASN C 53  O THR A 279 ? O THR C 279 
AA6 1 2 N LEU A 54  ? N LEU C 59  O VAL A 84  ? O VAL C 88  
AA6 2 3 N ILE A 83  ? N ILE C 87  O MET A 268 ? O MET C 268 
AA7 1 2 N ASN A 98  ? N ASN C 101 O PHE A 231 ? O PHE C 232 
AA7 2 3 O PHE A 232 ? O PHE C 233 N TRP A 179 ? N TRP C 180 
AA7 3 4 N LEU A 176 ? N LEU C 177 O TYR A 257 ? O TYR C 258 
AA7 4 5 O LYS A 261 ? O LYS C 261 N ASN A 113 ? N ASN C 116 
AA8 1 2 N ASN A 98  ? N ASN C 101 O PHE A 231 ? O PHE C 232 
AA8 2 3 O PHE A 232 ? O PHE C 233 N TRP A 179 ? N TRP C 180 
AA8 3 4 N GLY A 180 ? N GLY C 181 O ILE A 251 ? O ILE C 252 
AA8 4 5 O ALA A 252 ? O ALA C 253 N VAL A 151 ? N VAL C 152 
AA8 5 6 O THR A 154 ? O THR C 155 N GLU A 130 ? N GLU C 131 
AA9 1 2 N SER A 135 ? N SER C 136 O SER A 145 ? O SER C 146 
AB1 1 2 N ARG A 165 ? N ARG C 166 O PHE A 244 ? O PHE C 245 
AB1 2 3 O GLU A 245 ? O GLU C 246 N SER A 202 ? N SER C 203 
AB1 3 4 N ILE A 201 ? N ILE C 202 O LEU A 212 ? O LEU C 213 
AB2 1 2 O GLY A 286 ? O GLY C 286 N THR A 283 ? N THR C 283 
AB2 2 3 N GLN A 282 ? N GLN C 282 O ILE A 302 ? O ILE C 302 
AB3 1 2 O ALA D 35  ? O ALA B 35  N TYR D 24  ? N TYR B 24  
AB3 2 3 O GLY D 23  ? O GLY B 23  N GLY C 10  ? N GLY A 16  
AB3 3 4 N ILE C 7   ? N ILE A 13  O PHE D 138 ? O PHE B 138 
AB3 4 5 O GLU D 139 ? O GLU B 139 N LYS D 131 ? N LYS B 131 
AB4 1 2 N VAL C 20  ? N VAL A 26  O VAL C 28  ? O VAL A 34  
AB5 1 2 N GLN C 34  ? N GLN A 40  O LEU C 316 ? O LEU A 316 
AB6 1 2 N GLU C 38  ? N GLU A 44  O PHE C 294 ? O PHE A 294 
AB6 2 3 N HIS C 295 ? N HIS A 295 O LYS C 307 ? O LYS A 307 
AB7 1 2 N ASN C 47  ? N ASN A 53  O THR C 279 ? O THR A 279 
AB8 1 2 N LEU C 54  ? N LEU A 59  O VAL C 84  ? O VAL A 88  
AB8 2 3 N ILE C 83  ? N ILE A 87  O MET C 268 ? O MET A 268 
AB9 1 2 N ASN C 98  ? N ASN A 101 O PHE C 231 ? O PHE A 232 
AB9 2 3 O PHE C 232 ? O PHE A 233 N TRP C 179 ? N TRP A 180 
AB9 3 4 N LEU C 176 ? N LEU A 177 O TYR C 257 ? O TYR A 258 
AB9 4 5 O ALA C 256 ? O ALA A 257 N ILE C 118 ? N ILE A 121 
AC1 1 2 N ASN C 98  ? N ASN A 101 O PHE C 231 ? O PHE A 232 
AC1 2 3 O PHE C 232 ? O PHE A 233 N TRP C 179 ? N TRP A 180 
AC1 3 4 N GLY C 180 ? N GLY A 181 O ILE C 251 ? O ILE A 252 
AC1 4 5 O ALA C 252 ? O ALA A 253 N VAL C 151 ? N VAL A 152 
AC2 1 2 N SER C 135 ? N SER A 136 O SER C 145 ? O SER A 146 
AC3 1 2 N ILE C 163 ? N ILE A 164 O SER C 246 ? O SER A 247 
AC3 2 3 O GLU C 245 ? O GLU A 246 N SER C 202 ? N SER A 203 
AC3 3 4 N VAL C 203 ? N VAL A 204 O GLN C 210 ? O GLN A 211 
AC4 1 2 O GLY C 286 ? O GLY A 286 N THR C 283 ? N THR A 283 
AC4 2 3 N GLN C 282 ? N GLN A 282 O ILE C 302 ? O ILE A 302 
AC5 1 2 O ALA F 35  ? O ALA F 35  N TYR F 24  ? N TYR F 24  
AC5 2 3 O GLY F 23  ? O GLY F 23  N GLY E 10  ? N GLY E 16  
AC5 3 4 N ILE E 7   ? N ILE E 13  O PHE F 138 ? O PHE F 138 
AC5 4 5 O GLU F 139 ? O GLU F 139 N LYS F 131 ? N LYS F 131 
AC6 1 2 N VAL E 20  ? N VAL E 26  O VAL E 28  ? O VAL E 34  
AC7 1 2 N GLN E 34  ? N GLN E 40  O LEU E 316 ? O LEU E 316 
AC8 1 2 N GLU E 38  ? N GLU E 44  O PHE E 294 ? O PHE E 294 
AC8 2 3 N HIS E 295 ? N HIS E 295 O LYS E 307 ? O LYS E 307 
AC9 1 2 N ASN E 47  ? N ASN E 53  O CYS E 277 ? O CYS E 277 
AD1 1 2 N LEU E 54  ? N LEU E 59  O VAL E 84  ? O VAL E 88  
AD1 2 3 N ILE E 83  ? N ILE E 87  O MET E 268 ? O MET E 268 
AD2 1 2 N ASN E 98  ? N ASN E 101 O PHE E 231 ? O PHE E 232 
AD2 2 3 O PHE E 232 ? O PHE E 233 N TRP E 179 ? N TRP E 180 
AD2 3 4 N LEU E 176 ? N LEU E 177 O TYR E 257 ? O TYR E 258 
AD2 4 5 O ALA E 256 ? O ALA E 257 N ILE E 118 ? N ILE E 121 
AD3 1 2 N ASN E 98  ? N ASN E 101 O PHE E 231 ? O PHE E 232 
AD3 2 3 O PHE E 232 ? O PHE E 233 N TRP E 179 ? N TRP E 180 
AD3 3 4 N GLY E 180 ? N GLY E 181 O ILE E 251 ? O ILE E 252 
AD3 4 5 O ALA E 252 ? O ALA E 253 N VAL E 151 ? N VAL E 152 
AD4 1 2 N GLU E 130 ? N GLU E 131 O THR E 154 ? O THR E 155 
AD5 1 2 N SER E 135 ? N SER E 136 O SER E 145 ? O SER E 146 
AD6 1 2 N ILE E 163 ? N ILE E 164 O SER E 246 ? O SER E 247 
AD6 2 3 O GLU E 245 ? O GLU E 246 N SER E 202 ? N SER E 203 
AD6 3 4 N ILE E 201 ? N ILE E 202 O LEU E 212 ? O LEU E 213 
AD7 1 2 O GLY E 286 ? O GLY E 286 N THR E 283 ? N THR E 283 
AD7 2 3 N GLN E 282 ? N GLN E 282 O ILE E 302 ? O ILE E 302 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_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 
_struct_site.details 
AC1 Software A NAG 1001 ? 1  'binding site for Mono-Saccharide NAG A 1001 bound to ASN A 33'                              
AC2 Software A ASN 169  ? 5  'binding site for Poly-Saccharide residues NAG A 1002 through NAG A 1005 bound to ASN A 169' 
AC3 Software C NAG 1001 ? 2  'binding site for Mono-Saccharide NAG C 1001 bound to ASN C 33'                              
AC4 Software C ASN 169  ? 2  'binding site for Poly-Saccharide residues NAG C 1002 through NAG C 1004 bound to ASN C 169' 
AC5 Software E NAG 1001 ? 2  'binding site for Mono-Saccharide NAG E 1001 bound to ASN E 33'                              
AC6 Software E ASN 169  ? 4  'binding site for Poly-Saccharide residues NAG E 1002 through NAG E 1004 bound to ASN E 169' 
AC7 Software A SIA 1006 ? 15 'binding site for Poly-Saccharide residues SIA A 1006 through NAG A 1008'                    
AC8 Software C SIA 1005 ? 27 'binding site for Poly-Saccharide residues SIA C 1005 through GAL C 1006'                    
AC9 Software E SIA 1005 ? 7  'binding site for Poly-Saccharide residues SIA E 1005 through GAL E 1006'                    
# 
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 1  ASN C  27  ? ASN A 33   . ? 1_555 ? 
2  AC2 5  ASN C  168 ? ASN A 169  . ? 1_555 ? 
3  AC2 5  ASN C  239 ? ASN A 240  . ? 1_555 ? 
4  AC2 5  HOH CA .   ? HOH A 1145 . ? 1_555 ? 
5  AC2 5  GLY A  43  ? GLY C 49   . ? 1_454 ? 
6  AC2 5  SER E  220 ? SER E 221  . ? 1_555 ? 
7  AC3 2  GLN A  19  ? GLN C 25   . ? 1_555 ? 
8  AC3 2  ASN A  27  ? ASN C 33   . ? 1_555 ? 
9  AC4 2  ASN A  168 ? ASN C 169  . ? 1_555 ? 
10 AC4 2  ASN A  239 ? ASN C 240  . ? 1_555 ? 
11 AC5 2  GLN E  19  ? GLN E 25   . ? 1_555 ? 
12 AC5 2  ASN E  27  ? ASN E 33   . ? 1_555 ? 
13 AC6 4  ASN E  168 ? ASN E 169  . ? 1_555 ? 
14 AC6 4  ASN E  239 ? ASN E 240  . ? 1_555 ? 
15 AC6 4  ASP E  240 ? ASP E 241  . ? 1_555 ? 
16 AC6 4  HOH EA .   ? HOH E 1113 . ? 1_555 ? 
17 AC7 15 TYR C  95  ? TYR A 98   . ? 1_555 ? 
18 AC7 15 GLY C  133 ? GLY A 134  . ? 1_555 ? 
19 AC7 15 VAL C  134 ? VAL A 135  . ? 1_555 ? 
20 AC7 15 SER C  135 ? SER A 136  . ? 1_555 ? 
21 AC7 15 SER C  136 ? SER A 137  . ? 1_555 ? 
22 AC7 15 TRP C  152 ? TRP A 153  . ? 1_555 ? 
23 AC7 15 HIS C  182 ? HIS A 183  . ? 1_555 ? 
24 AC7 15 GLU C  189 ? GLU A 190  . ? 1_555 ? 
25 AC7 15 ARG C  192 ? ARG A 193  . ? 1_555 ? 
26 AC7 15 LEU C  193 ? LEU A 194  . ? 1_555 ? 
27 AC7 15 LYS C  221 ? LYS A 222  . ? 1_555 ? 
28 AC7 15 LEU C  225 ? LEU A 226  . ? 1_555 ? 
29 AC7 15 HOH CA .   ? HOH A 1110 . ? 1_555 ? 
30 AC7 15 HOH CA .   ? HOH A 1114 . ? 1_555 ? 
31 AC7 15 HOH CA .   ? HOH A 1133 . ? 1_555 ? 
32 AC8 27 TYR C  95  ? TYR A 98   . ? 1_555 ? 
33 AC8 27 GLY C  133 ? GLY A 134  . ? 1_555 ? 
34 AC8 27 VAL C  134 ? VAL A 135  . ? 1_555 ? 
35 AC8 27 SER C  135 ? SER A 136  . ? 1_555 ? 
36 AC8 27 SER C  136 ? SER A 137  . ? 1_555 ? 
37 AC8 27 TRP C  152 ? TRP A 153  . ? 1_555 ? 
38 AC8 27 HIS C  182 ? HIS A 183  . ? 1_555 ? 
39 AC8 27 GLU C  189 ? GLU A 190  . ? 1_555 ? 
40 AC8 27 ARG C  192 ? ARG A 193  . ? 1_555 ? 
41 AC8 27 LEU C  193 ? LEU A 194  . ? 1_555 ? 
42 AC8 27 LYS C  221 ? LYS A 222  . ? 1_555 ? 
43 AC8 27 LEU C  225 ? LEU A 226  . ? 1_555 ? 
44 AC8 27 NAG N  .   ? NAG A 1002 . ? 1_555 ? 
45 AC8 27 FUC O  .   ? FUC A 1003 . ? 1_555 ? 
46 AC8 27 FUL P  .   ? FUL A 1004 . ? 1_555 ? 
47 AC8 27 HOH CA .   ? HOH A 1110 . ? 1_555 ? 
48 AC8 27 HOH CA .   ? HOH A 1114 . ? 1_555 ? 
49 AC8 27 HOH CA .   ? HOH A 1133 . ? 1_555 ? 
50 AC8 27 TYR A  95  ? TYR C 98   . ? 1_555 ? 
51 AC8 27 VAL A  134 ? VAL C 135  . ? 1_555 ? 
52 AC8 27 SER A  135 ? SER C 136  . ? 1_555 ? 
53 AC8 27 SER A  136 ? SER C 137  . ? 1_555 ? 
54 AC8 27 HIS A  182 ? HIS C 183  . ? 1_555 ? 
55 AC8 27 GLU A  189 ? GLU C 190  . ? 1_555 ? 
56 AC8 27 ARG A  192 ? ARG C 193  . ? 1_555 ? 
57 AC8 27 LEU A  193 ? LEU C 194  . ? 1_555 ? 
58 AC8 27 GLY A  224 ? GLY C 225  . ? 1_555 ? 
59 AC9 7  TYR E  95  ? TYR E 98   . ? 1_555 ? 
60 AC9 7  VAL E  134 ? VAL E 135  . ? 1_555 ? 
61 AC9 7  SER E  135 ? SER E 136  . ? 1_555 ? 
62 AC9 7  SER E  136 ? SER E 137  . ? 1_555 ? 
63 AC9 7  HIS E  182 ? HIS E 183  . ? 1_555 ? 
64 AC9 7  GLU E  189 ? GLU E 190  . ? 1_555 ? 
65 AC9 7  ARG E  192 ? ARG E 193  . ? 1_555 ? 
# 
_atom_sites.entry_id                    5E2Z 
_atom_sites.fract_transf_matrix[1][1]   0.013687 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006524 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.004271 
_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]   0.015186 
_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   . ASP A  1 2   ? 51.907  -75.078 56.520  1.00 122.12 ? 8    ASP C N   1 
ATOM   2     C CA  . ASP A  1 2   ? 52.119  -73.783 57.158  1.00 127.22 ? 8    ASP C CA  1 
ATOM   3     C C   . ASP A  1 2   ? 52.180  -72.682 56.096  1.00 130.97 ? 8    ASP C C   1 
ATOM   4     O O   . ASP A  1 2   ? 52.367  -72.983 54.909  1.00 125.57 ? 8    ASP C O   1 
ATOM   5     C CB  . ASP A  1 2   ? 53.413  -73.809 57.986  1.00 127.97 ? 8    ASP C CB  1 
ATOM   6     C CG  . ASP A  1 2   ? 53.541  -72.622 58.928  1.00 124.50 ? 8    ASP C CG  1 
ATOM   7     O OD1 . ASP A  1 2   ? 52.598  -72.380 59.713  1.00 117.49 ? 8    ASP C OD1 1 
ATOM   8     O OD2 . ASP A  1 2   ? 54.587  -71.933 58.878  1.00 124.10 ? 8    ASP C OD2 1 
ATOM   9     N N   . PRO A  1 3   ? 51.968  -71.412 56.504  1.00 131.35 ? 9    PRO C N   1 
ATOM   10    C CA  . PRO A  1 3   ? 52.350  -70.295 55.630  1.00 128.76 ? 9    PRO C CA  1 
ATOM   11    C C   . PRO A  1 3   ? 53.804  -70.343 55.138  1.00 130.33 ? 9    PRO C C   1 
ATOM   12    O O   . PRO A  1 3   ? 54.739  -70.385 55.944  1.00 129.63 ? 9    PRO C O   1 
ATOM   13    C CB  . PRO A  1 3   ? 52.134  -69.067 56.526  1.00 122.05 ? 9    PRO C CB  1 
ATOM   14    C CG  . PRO A  1 3   ? 51.122  -69.503 57.565  1.00 122.41 ? 9    PRO C CG  1 
ATOM   15    C CD  . PRO A  1 3   ? 50.953  -71.001 57.491  1.00 122.43 ? 9    PRO C CD  1 
ATOM   16    N N   . GLY A  1 4   ? 53.972  -70.313 53.816  1.00 129.72 ? 10   GLY C N   1 
ATOM   17    C CA  . GLY A  1 4   ? 55.275  -70.236 53.181  1.00 124.98 ? 10   GLY C CA  1 
ATOM   18    C C   . GLY A  1 4   ? 55.567  -68.801 52.796  1.00 128.46 ? 10   GLY C C   1 
ATOM   19    O O   . GLY A  1 4   ? 55.167  -67.862 53.483  1.00 129.74 ? 10   GLY C O   1 
ATOM   20    N N   . ASP A  1 5   ? 56.260  -68.626 51.680  1.00 129.66 ? 11   ASP C N   1 
ATOM   21    C CA  . ASP A  1 5   ? 56.546  -67.289 51.183  1.00 130.56 ? 11   ASP C CA  1 
ATOM   22    C C   . ASP A  1 5   ? 55.372  -66.832 50.308  1.00 126.83 ? 11   ASP C C   1 
ATOM   23    O O   . ASP A  1 5   ? 54.678  -67.666 49.719  1.00 122.80 ? 11   ASP C O   1 
ATOM   24    C CB  . ASP A  1 5   ? 57.863  -67.261 50.399  1.00 130.61 ? 11   ASP C CB  1 
ATOM   25    C CG  . ASP A  1 5   ? 59.045  -67.721 51.221  1.00 127.65 ? 11   ASP C CG  1 
ATOM   26    O OD1 . ASP A  1 5   ? 58.887  -67.875 52.451  1.00 125.01 ? 11   ASP C OD1 1 
ATOM   27    O OD2 . ASP A  1 5   ? 60.132  -67.907 50.634  1.00 126.15 ? 11   ASP C OD2 1 
ATOM   28    N N   . GLN A  1 6   ? 55.126  -65.523 50.250  1.00 127.09 ? 12   GLN C N   1 
ATOM   29    C CA  . GLN A  1 6   ? 54.024  -64.991 49.441  1.00 123.61 ? 12   GLN C CA  1 
ATOM   30    C C   . GLN A  1 6   ? 54.460  -63.917 48.435  1.00 120.03 ? 12   GLN C C   1 
ATOM   31    O O   . GLN A  1 6   ? 55.575  -63.388 48.507  1.00 120.89 ? 12   GLN C O   1 
ATOM   32    C CB  . GLN A  1 6   ? 52.920  -64.409 50.338  1.00 122.05 ? 12   GLN C CB  1 
ATOM   33    C CG  . GLN A  1 6   ? 52.108  -65.439 51.116  1.00 122.32 ? 12   GLN C CG  1 
ATOM   34    C CD  . GLN A  1 6   ? 50.743  -64.909 51.521  1.00 118.50 ? 12   GLN C CD  1 
ATOM   35    O OE1 . GLN A  1 6   ? 50.464  -63.717 51.386  1.00 115.39 ? 12   GLN C OE1 1 
ATOM   36    N NE2 . GLN A  1 6   ? 49.886  -65.792 52.020  1.00 116.14 ? 12   GLN C NE2 1 
ATOM   37    N N   . ILE A  1 7   ? 53.564  -63.620 47.491  1.00 119.55 ? 13   ILE C N   1 
ATOM   38    C CA  . ILE A  1 7   ? 53.688  -62.471 46.584  1.00 115.31 ? 13   ILE C CA  1 
ATOM   39    C C   . ILE A  1 7   ? 52.300  -62.012 46.091  1.00 109.97 ? 13   ILE C C   1 
ATOM   40    O O   . ILE A  1 7   ? 51.434  -62.834 45.770  1.00 107.14 ? 13   ILE C O   1 
ATOM   41    C CB  . ILE A  1 7   ? 54.611  -62.779 45.368  1.00 104.95 ? 13   ILE C CB  1 
ATOM   42    C CG1 . ILE A  1 7   ? 55.027  -61.474 44.682  1.00 99.29  ? 13   ILE C CG1 1 
ATOM   43    C CG2 . ILE A  1 7   ? 53.950  -63.763 44.394  1.00 100.96 ? 13   ILE C CG2 1 
ATOM   44    C CD1 . ILE A  1 7   ? 56.070  -61.636 43.607  1.00 93.37  ? 13   ILE C CD1 1 
ATOM   45    N N   . CYS A  1 8   ? 52.075  -60.698 46.077  1.00 106.20 ? 14   CYS C N   1 
ATOM   46    C CA  . CYS A  1 8   ? 50.770  -60.153 45.688  1.00 103.61 ? 14   CYS C CA  1 
ATOM   47    C C   . CYS A  1 8   ? 50.862  -59.019 44.645  1.00 102.84 ? 14   CYS C C   1 
ATOM   48    O O   . CYS A  1 8   ? 51.874  -58.309 44.566  1.00 99.59  ? 14   CYS C O   1 
ATOM   49    C CB  . CYS A  1 8   ? 50.012  -59.669 46.930  1.00 102.70 ? 14   CYS C CB  1 
ATOM   50    S SG  . CYS A  1 8   ? 49.601  -60.979 48.125  1.00 108.61 ? 14   CYS C SG  1 
ATOM   51    N N   . ILE A  1 9   ? 49.803  -58.880 43.839  1.00 101.27 ? 15   ILE C N   1 
ATOM   52    C CA  . ILE A  1 9   ? 49.698  -57.843 42.805  1.00 95.92  ? 15   ILE C CA  1 
ATOM   53    C C   . ILE A  1 9   ? 48.659  -56.797 43.203  1.00 91.41  ? 15   ILE C C   1 
ATOM   54    O O   . ILE A  1 9   ? 47.562  -57.149 43.626  1.00 90.62  ? 15   ILE C O   1 
ATOM   55    C CB  . ILE A  1 9   ? 49.314  -58.445 41.443  1.00 88.97  ? 15   ILE C CB  1 
ATOM   56    C CG1 . ILE A  1 9   ? 50.325  -59.503 41.030  1.00 89.93  ? 15   ILE C CG1 1 
ATOM   57    C CG2 . ILE A  1 9   ? 49.197  -57.371 40.370  1.00 87.59  ? 15   ILE C CG2 1 
ATOM   58    C CD1 . ILE A  1 9   ? 49.679  -60.813 40.735  1.00 91.18  ? 15   ILE C CD1 1 
ATOM   59    N N   . GLY A  1 10  ? 48.990  -55.518 43.046  1.00 91.27  ? 16   GLY C N   1 
ATOM   60    C CA  . GLY A  1 10  ? 48.074  -54.455 43.425  1.00 91.39  ? 16   GLY C CA  1 
ATOM   61    C C   . GLY A  1 10  ? 48.369  -53.118 42.773  1.00 88.86  ? 16   GLY C C   1 
ATOM   62    O O   . GLY A  1 10  ? 49.270  -53.000 41.936  1.00 86.72  ? 16   GLY C O   1 
ATOM   63    N N   . TYR A  1 11  ? 47.596  -52.105 43.146  1.00 86.18  ? 17   TYR C N   1 
ATOM   64    C CA  . TYR A  1 11  ? 47.708  -50.810 42.495  1.00 87.16  ? 17   TYR C CA  1 
ATOM   65    C C   . TYR A  1 11  ? 47.815  -49.653 43.482  1.00 87.79  ? 17   TYR C C   1 
ATOM   66    O O   . TYR A  1 11  ? 47.583  -49.811 44.687  1.00 86.13  ? 17   TYR C O   1 
ATOM   67    C CB  . TYR A  1 11  ? 46.513  -50.594 41.555  1.00 83.17  ? 17   TYR C CB  1 
ATOM   68    C CG  . TYR A  1 11  ? 45.163  -50.913 42.162  1.00 71.75  ? 17   TYR C CG  1 
ATOM   69    C CD1 . TYR A  1 11  ? 44.450  -49.954 42.861  1.00 74.46  ? 17   TYR C CD1 1 
ATOM   70    C CD2 . TYR A  1 11  ? 44.599  -52.169 42.018  1.00 77.64  ? 17   TYR C CD2 1 
ATOM   71    C CE1 . TYR A  1 11  ? 43.214  -50.239 43.410  1.00 78.20  ? 17   TYR C CE1 1 
ATOM   72    C CE2 . TYR A  1 11  ? 43.364  -52.471 42.570  1.00 79.74  ? 17   TYR C CE2 1 
ATOM   73    C CZ  . TYR A  1 11  ? 42.675  -51.501 43.264  1.00 77.57  ? 17   TYR C CZ  1 
ATOM   74    O OH  . TYR A  1 11  ? 41.447  -51.795 43.812  1.00 75.08  ? 17   TYR C OH  1 
ATOM   75    N N   . HIS A  1 12  ? 48.154  -48.484 42.944  1.00 87.75  ? 18   HIS C N   1 
ATOM   76    C CA  . HIS A  1 12  ? 48.357  -47.280 43.739  1.00 85.28  ? 18   HIS C CA  1 
ATOM   77    C C   . HIS A  1 12  ? 47.056  -46.732 44.298  1.00 84.43  ? 18   HIS C C   1 
ATOM   78    O O   . HIS A  1 12  ? 46.011  -46.785 43.653  1.00 85.70  ? 18   HIS C O   1 
ATOM   79    C CB  . HIS A  1 12  ? 49.051  -46.207 42.892  1.00 86.90  ? 18   HIS C CB  1 
ATOM   80    C CG  . HIS A  1 12  ? 49.334  -44.933 43.629  1.00 93.14  ? 18   HIS C CG  1 
ATOM   81    N ND1 . HIS A  1 12  ? 49.971  -44.895 44.853  1.00 96.12  ? 18   HIS C ND1 1 
ATOM   82    C CD2 . HIS A  1 12  ? 49.068  -43.643 43.306  1.00 87.27  ? 18   HIS C CD2 1 
ATOM   83    C CE1 . HIS A  1 12  ? 50.077  -43.639 45.256  1.00 86.67  ? 18   HIS C CE1 1 
ATOM   84    N NE2 . HIS A  1 12  ? 49.535  -42.861 44.337  1.00 85.71  ? 18   HIS C NE2 1 
ATOM   85    N N   . ALA A  1 13  ? 47.130  -46.212 45.514  1.00 83.38  ? 19   ALA C N   1 
ATOM   86    C CA  . ALA A  1 13  ? 46.044  -45.429 46.075  1.00 81.28  ? 19   ALA C CA  1 
ATOM   87    C C   . ALA A  1 13  ? 46.711  -44.270 46.794  1.00 84.23  ? 19   ALA C C   1 
ATOM   88    O O   . ALA A  1 13  ? 47.904  -44.326 47.096  1.00 84.70  ? 19   ALA C O   1 
ATOM   89    C CB  . ALA A  1 13  ? 45.168  -46.254 47.016  1.00 73.66  ? 19   ALA C CB  1 
ATOM   90    N N   . ASN A  1 14  ? 45.953  -43.208 47.030  1.00 83.92  ? 20   ASN C N   1 
ATOM   91    C CA  . ASN A  1 14  ? 46.467  -42.023 47.708  1.00 81.52  ? 20   ASN C CA  1 
ATOM   92    C C   . ASN A  1 14  ? 45.334  -41.318 48.442  1.00 84.70  ? 20   ASN C C   1 
ATOM   93    O O   . ASN A  1 14  ? 44.284  -41.918 48.689  1.00 86.54  ? 20   ASN C O   1 
ATOM   94    C CB  . ASN A  1 14  ? 47.214  -41.087 46.728  1.00 80.74  ? 20   ASN C CB  1 
ATOM   95    C CG  . ASN A  1 14  ? 46.402  -40.725 45.477  1.00 82.15  ? 20   ASN C CG  1 
ATOM   96    O OD1 . ASN A  1 14  ? 45.195  -40.510 45.536  1.00 81.66  ? 20   ASN C OD1 1 
ATOM   97    N ND2 . ASN A  1 14  ? 47.085  -40.656 44.331  1.00 78.00  ? 20   ASN C ND2 1 
ATOM   98    N N   . ASN A  1 15  ? 45.555  -40.063 48.816  1.00 86.10  ? 21   ASN C N   1 
ATOM   99    C CA  . ASN A  1 15  ? 44.557  -39.288 49.555  1.00 90.17  ? 21   ASN C CA  1 
ATOM   100   C C   . ASN A  1 15  ? 43.830  -38.249 48.677  1.00 89.10  ? 21   ASN C C   1 
ATOM   101   O O   . ASN A  1 15  ? 43.344  -37.222 49.170  1.00 84.28  ? 21   ASN C O   1 
ATOM   102   C CB  . ASN A  1 15  ? 45.224  -38.605 50.759  1.00 93.90  ? 21   ASN C CB  1 
ATOM   103   C CG  . ASN A  1 15  ? 46.543  -37.914 50.384  1.00 97.20  ? 21   ASN C CG  1 
ATOM   104   O OD1 . ASN A  1 15  ? 47.188  -38.276 49.389  1.00 89.34  ? 21   ASN C OD1 1 
ATOM   105   N ND2 . ASN A  1 15  ? 46.946  -36.913 51.181  1.00 98.86  ? 21   ASN C ND2 1 
ATOM   106   N N   . SER A  1 16  ? 43.742  -38.536 47.379  1.00 86.55  ? 22   SER C N   1 
ATOM   107   C CA  . SER A  1 16  ? 43.085  -37.634 46.440  1.00 82.85  ? 22   SER C CA  1 
ATOM   108   C C   . SER A  1 16  ? 41.593  -37.646 46.732  1.00 82.85  ? 22   SER C C   1 
ATOM   109   O O   . SER A  1 16  ? 41.070  -38.618 47.282  1.00 82.92  ? 22   SER C O   1 
ATOM   110   C CB  . SER A  1 16  ? 43.358  -38.063 44.989  1.00 78.02  ? 22   SER C CB  1 
ATOM   111   O OG  . SER A  1 16  ? 42.857  -37.133 44.048  1.00 76.71  ? 22   SER C OG  1 
ATOM   112   N N   . THR A  1 17  ? 40.910  -36.564 46.370  1.00 82.32  ? 23   THR C N   1 
ATOM   113   C CA  . THR A  1 17  ? 39.473  -36.470 46.593  1.00 75.52  ? 23   THR C CA  1 
ATOM   114   C C   . THR A  1 17  ? 38.789  -35.928 45.329  1.00 66.94  ? 23   THR C C   1 
ATOM   115   O O   . THR A  1 17  ? 37.573  -35.717 45.305  1.00 66.96  ? 23   THR C O   1 
ATOM   116   C CB  . THR A  1 17  ? 39.172  -35.594 47.853  1.00 72.84  ? 23   THR C CB  1 
ATOM   117   O OG1 . THR A  1 17  ? 37.761  -35.545 48.099  1.00 73.28  ? 23   THR C OG1 1 
ATOM   118   C CG2 . THR A  1 17  ? 39.755  -34.176 47.712  1.00 68.06  ? 23   THR C CG2 1 
ATOM   119   N N   . GLU A  1 18  ? 39.588  -35.758 44.272  1.00 68.46  ? 24   GLU C N   1 
ATOM   120   C CA  . GLU A  1 18  ? 39.119  -35.255 42.976  1.00 64.94  ? 24   GLU C CA  1 
ATOM   121   C C   . GLU A  1 18  ? 38.150  -36.176 42.246  1.00 62.64  ? 24   GLU C C   1 
ATOM   122   O O   . GLU A  1 18  ? 38.325  -37.394 42.241  1.00 65.20  ? 24   GLU C O   1 
ATOM   123   C CB  . GLU A  1 18  ? 40.305  -34.969 42.074  1.00 63.25  ? 24   GLU C CB  1 
ATOM   124   C CG  . GLU A  1 18  ? 41.130  -33.817 42.567  1.00 74.83  ? 24   GLU C CG  1 
ATOM   125   C CD  . GLU A  1 18  ? 42.193  -33.430 41.585  1.00 79.94  ? 24   GLU C CD  1 
ATOM   126   O OE1 . GLU A  1 18  ? 42.517  -34.266 40.713  1.00 81.88  ? 24   GLU C OE1 1 
ATOM   127   O OE2 . GLU A  1 18  ? 42.683  -32.284 41.674  1.00 82.00  ? 24   GLU C OE2 1 
ATOM   128   N N   . GLN A  1 19  ? 37.170  -35.578 41.570  1.00 62.05  ? 25   GLN C N   1 
ATOM   129   C CA  . GLN A  1 19  ? 36.108  -36.331 40.904  1.00 61.62  ? 25   GLN C CA  1 
ATOM   130   C C   . GLN A  1 19  ? 36.031  -36.071 39.392  1.00 60.86  ? 25   GLN C C   1 
ATOM   131   O O   . GLN A  1 19  ? 36.293  -34.960 38.930  1.00 66.77  ? 25   GLN C O   1 
ATOM   132   C CB  . GLN A  1 19  ? 34.759  -35.989 41.539  1.00 63.74  ? 25   GLN C CB  1 
ATOM   133   C CG  . GLN A  1 19  ? 34.666  -36.233 43.044  1.00 66.45  ? 25   GLN C CG  1 
ATOM   134   C CD  . GLN A  1 19  ? 33.359  -35.713 43.651  1.00 73.03  ? 25   GLN C CD  1 
ATOM   135   O OE1 . GLN A  1 19  ? 32.667  -34.880 43.060  1.00 75.11  ? 25   GLN C OE1 1 
ATOM   136   N NE2 . GLN A  1 19  ? 33.003  -36.232 44.816  1.00 70.28  ? 25   GLN C NE2 1 
ATOM   137   N N   . VAL A  1 20  ? 35.694  -37.113 38.630  1.00 55.20  ? 26   VAL C N   1 
ATOM   138   C CA  . VAL A  1 20  ? 35.464  -36.991 37.192  1.00 54.05  ? 26   VAL C CA  1 
ATOM   139   C C   . VAL A  1 20  ? 34.082  -37.572 36.894  1.00 54.53  ? 26   VAL C C   1 
ATOM   140   O O   . VAL A  1 20  ? 33.527  -38.288 37.719  1.00 57.08  ? 26   VAL C O   1 
ATOM   141   C CB  . VAL A  1 20  ? 36.531  -37.718 36.331  1.00 54.32  ? 26   VAL C CB  1 
ATOM   142   C CG1 . VAL A  1 20  ? 37.927  -37.298 36.722  1.00 54.10  ? 26   VAL C CG1 1 
ATOM   143   C CG2 . VAL A  1 20  ? 36.370  -39.222 36.419  1.00 54.51  ? 26   VAL C CG2 1 
ATOM   144   N N   . ASP A  1 21  ? 33.517  -37.251 35.734  1.00 54.48  ? 27   ASP C N   1 
ATOM   145   C CA  . ASP A  1 21  ? 32.224  -37.820 35.340  1.00 52.33  ? 27   ASP C CA  1 
ATOM   146   C C   . ASP A  1 21  ? 32.405  -38.766 34.164  1.00 47.25  ? 27   ASP C C   1 
ATOM   147   O O   . ASP A  1 21  ? 33.403  -38.691 33.451  1.00 48.51  ? 27   ASP C O   1 
ATOM   148   C CB  . ASP A  1 21  ? 31.210  -36.731 34.961  1.00 57.99  ? 27   ASP C CB  1 
ATOM   149   C CG  . ASP A  1 21  ? 30.637  -35.997 36.171  1.00 61.70  ? 27   ASP C CG  1 
ATOM   150   O OD1 . ASP A  1 21  ? 31.228  -36.080 37.271  1.00 63.04  ? 27   ASP C OD1 1 
ATOM   151   O OD2 . ASP A  1 21  ? 29.578  -35.345 36.015  1.00 62.67  ? 27   ASP C OD2 1 
ATOM   152   N N   . THR A  1 22  ? 31.464  -39.694 34.009  1.00 53.97  ? 28   THR C N   1 
ATOM   153   C CA  . THR A  1 22  ? 31.407  -40.610 32.857  1.00 54.63  ? 28   THR C CA  1 
ATOM   154   C C   . THR A  1 22  ? 29.922  -40.650 32.489  1.00 54.85  ? 28   THR C C   1 
ATOM   155   O O   . THR A  1 22  ? 29.094  -40.055 33.192  1.00 55.55  ? 28   THR C O   1 
ATOM   156   C CB  . THR A  1 22  ? 31.924  -42.052 33.158  1.00 55.40  ? 28   THR C CB  1 
ATOM   157   O OG1 . THR A  1 22  ? 30.976  -42.773 33.949  1.00 52.80  ? 28   THR C OG1 1 
ATOM   158   C CG2 . THR A  1 22  ? 33.304  -42.031 33.831  1.00 51.44  ? 28   THR C CG2 1 
ATOM   159   N N   . ILE A  1 23  ? 29.552  -41.331 31.414  1.00 52.75  ? 29   ILE C N   1 
ATOM   160   C CA  . ILE A  1 23  ? 28.140  -41.310 31.055  1.00 54.81  ? 29   ILE C CA  1 
ATOM   161   C C   . ILE A  1 23  ? 27.250  -42.231 31.922  1.00 58.83  ? 29   ILE C C   1 
ATOM   162   O O   . ILE A  1 23  ? 26.043  -42.017 32.025  1.00 60.84  ? 29   ILE C O   1 
ATOM   163   C CB  . ILE A  1 23  ? 27.946  -41.677 29.592  1.00 57.07  ? 29   ILE C CB  1 
ATOM   164   C CG1 . ILE A  1 23  ? 27.992  -43.174 29.426  1.00 57.53  ? 29   ILE C CG1 1 
ATOM   165   C CG2 . ILE A  1 23  ? 28.999  -41.006 28.710  1.00 58.01  ? 29   ILE C CG2 1 
ATOM   166   C CD1 . ILE A  1 23  ? 27.000  -43.624 28.437  1.00 64.95  ? 29   ILE C CD1 1 
ATOM   167   N N   . MET A  1 24  ? 27.834  -43.219 32.594  1.00 60.88  ? 30   MET C N   1 
ATOM   168   C CA  . MET A  1 24  ? 27.025  -44.150 33.385  1.00 59.74  ? 30   MET C CA  1 
ATOM   169   C C   . MET A  1 24  ? 27.047  -43.791 34.861  1.00 59.51  ? 30   MET C C   1 
ATOM   170   O O   . MET A  1 24  ? 26.196  -44.238 35.630  1.00 59.83  ? 30   MET C O   1 
ATOM   171   C CB  . MET A  1 24  ? 27.506  -45.597 33.199  1.00 58.42  ? 30   MET C CB  1 
ATOM   172   C CG  . MET A  1 24  ? 26.625  -46.432 32.269  1.00 62.68  ? 30   MET C CG  1 
ATOM   173   S SD  . MET A  1 24  ? 26.927  -48.210 32.372  1.00 57.87  ? 30   MET C SD  1 
ATOM   174   C CE  . MET A  1 24  ? 28.707  -48.226 32.129  1.00 51.10  ? 30   MET C CE  1 
ATOM   175   N N   . GLU A  1 25  ? 27.982  -42.926 35.238  1.00 58.62  ? 31   GLU C N   1 
ATOM   176   C CA  . GLU A  1 25  ? 28.238  -42.653 36.640  1.00 62.99  ? 31   GLU C CA  1 
ATOM   177   C C   . GLU A  1 25  ? 28.829  -41.243 36.829  1.00 62.38  ? 31   GLU C C   1 
ATOM   178   O O   . GLU A  1 25  ? 29.729  -40.823 36.098  1.00 55.95  ? 31   GLU C O   1 
ATOM   179   C CB  . GLU A  1 25  ? 29.175  -43.748 37.202  1.00 67.48  ? 31   GLU C CB  1 
ATOM   180   C CG  . GLU A  1 25  ? 29.388  -43.734 38.728  1.00 70.46  ? 31   GLU C CG  1 
ATOM   181   C CD  . GLU A  1 25  ? 30.351  -44.822 39.236  1.00 68.33  ? 31   GLU C CD  1 
ATOM   182   O OE1 . GLU A  1 25  ? 30.816  -45.672 38.432  1.00 67.96  ? 31   GLU C OE1 1 
ATOM   183   O OE2 . GLU A  1 25  ? 30.627  -44.820 40.456  1.00 64.39  ? 31   GLU C OE2 1 
ATOM   184   N N   . LYS A  1 26  ? 28.289  -40.518 37.807  1.00 69.56  ? 32   LYS C N   1 
ATOM   185   C CA  . LYS A  1 26  ? 28.683  -39.138 38.089  1.00 66.04  ? 32   LYS C CA  1 
ATOM   186   C C   . LYS A  1 26  ? 29.565  -39.092 39.350  1.00 65.24  ? 32   LYS C C   1 
ATOM   187   O O   . LYS A  1 26  ? 29.471  -39.971 40.201  1.00 69.48  ? 32   LYS C O   1 
ATOM   188   C CB  . LYS A  1 26  ? 27.433  -38.274 38.293  1.00 66.79  ? 32   LYS C CB  1 
ATOM   189   C CG  . LYS A  1 26  ? 26.521  -38.174 37.065  1.00 68.30  ? 32   LYS C CG  1 
ATOM   190   C CD  . LYS A  1 26  ? 27.147  -37.353 35.952  1.00 73.69  ? 32   LYS C CD  1 
ATOM   191   C CE  . LYS A  1 26  ? 26.213  -37.197 34.737  1.00 77.29  ? 32   LYS C CE  1 
ATOM   192   N NZ  . LYS A  1 26  ? 26.313  -38.324 33.738  1.00 67.64  ? 32   LYS C NZ  1 
ATOM   193   N N   . ASN A  1 27  ? 30.393  -38.058 39.474  1.00 66.44  ? 33   ASN C N   1 
ATOM   194   C CA  . ASN A  1 27  ? 31.240  -37.803 40.657  1.00 69.26  ? 33   ASN C CA  1 
ATOM   195   C C   . ASN A  1 27  ? 32.128  -38.972 41.161  1.00 67.04  ? 33   ASN C C   1 
ATOM   196   O O   . ASN A  1 27  ? 32.116  -39.311 42.351  1.00 65.34  ? 33   ASN C O   1 
ATOM   197   C CB  . ASN A  1 27  ? 30.340  -37.329 41.821  1.00 72.56  ? 33   ASN C CB  1 
ATOM   198   C CG  . ASN A  1 27  ? 29.767  -35.924 41.594  1.00 76.25  ? 33   ASN C CG  1 
ATOM   199   O OD1 . ASN A  1 27  ? 30.250  -35.180 40.739  1.00 73.64  ? 33   ASN C OD1 1 
ATOM   200   N ND2 . ASN A  1 27  ? 28.737  -35.558 42.375  1.00 82.17  ? 33   ASN C ND2 1 
ATOM   201   N N   . VAL A  1 28  ? 32.958  -39.515 40.270  1.00 66.00  ? 34   VAL C N   1 
ATOM   202   C CA  . VAL A  1 28  ? 33.875  -40.619 40.590  1.00 59.97  ? 34   VAL C CA  1 
ATOM   203   C C   . VAL A  1 28  ? 35.235  -40.129 41.120  1.00 64.72  ? 34   VAL C C   1 
ATOM   204   O O   . VAL A  1 28  ? 35.931  -39.355 40.449  1.00 64.75  ? 34   VAL C O   1 
ATOM   205   C CB  . VAL A  1 28  ? 34.131  -41.523 39.339  1.00 53.59  ? 34   VAL C CB  1 
ATOM   206   C CG1 . VAL A  1 28  ? 35.362  -42.393 39.537  1.00 55.22  ? 34   VAL C CG1 1 
ATOM   207   C CG2 . VAL A  1 28  ? 32.920  -42.389 39.024  1.00 54.99  ? 34   VAL C CG2 1 
ATOM   208   N N   . THR A  1 29  ? 35.608  -40.563 42.325  1.00 60.64  ? 35   THR C N   1 
ATOM   209   C CA  . THR A  1 29  ? 36.873  -40.130 42.915  1.00 58.86  ? 35   THR C CA  1 
ATOM   210   C C   . THR A  1 29  ? 38.057  -40.891 42.319  1.00 60.92  ? 35   THR C C   1 
ATOM   211   O O   . THR A  1 29  ? 38.001  -42.111 42.165  1.00 63.34  ? 35   THR C O   1 
ATOM   212   C CB  . THR A  1 29  ? 36.852  -40.297 44.424  1.00 60.48  ? 35   THR C CB  1 
ATOM   213   O OG1 . THR A  1 29  ? 35.611  -39.783 44.927  1.00 61.17  ? 35   THR C OG1 1 
ATOM   214   C CG2 . THR A  1 29  ? 38.011  -39.545 45.051  1.00 60.34  ? 35   THR C CG2 1 
ATOM   215   N N   . VAL A  1 30  ? 39.135  -40.167 42.022  1.00 60.41  ? 36   VAL C N   1 
ATOM   216   C CA  . VAL A  1 30  ? 40.251  -40.682 41.216  1.00 62.78  ? 36   VAL C CA  1 
ATOM   217   C C   . VAL A  1 30  ? 41.590  -40.293 41.864  1.00 70.13  ? 36   VAL C C   1 
ATOM   218   O O   . VAL A  1 30  ? 41.634  -39.357 42.667  1.00 73.09  ? 36   VAL C O   1 
ATOM   219   C CB  . VAL A  1 30  ? 40.141  -40.147 39.743  1.00 65.33  ? 36   VAL C CB  1 
ATOM   220   C CG1 . VAL A  1 30  ? 41.417  -40.322 38.958  1.00 63.06  ? 36   VAL C CG1 1 
ATOM   221   C CG2 . VAL A  1 30  ? 38.973  -40.816 39.018  1.00 60.57  ? 36   VAL C CG2 1 
ATOM   222   N N   . THR A  1 31  ? 42.660  -41.038 41.570  1.00 68.97  ? 37   THR C N   1 
ATOM   223   C CA  . THR A  1 31  ? 43.971  -40.776 42.175  1.00 72.36  ? 37   THR C CA  1 
ATOM   224   C C   . THR A  1 31  ? 44.660  -39.570 41.563  1.00 68.40  ? 37   THR C C   1 
ATOM   225   O O   . THR A  1 31  ? 45.265  -38.764 42.263  1.00 71.62  ? 37   THR C O   1 
ATOM   226   C CB  . THR A  1 31  ? 44.915  -42.001 42.064  1.00 71.46  ? 37   THR C CB  1 
ATOM   227   O OG1 . THR A  1 31  ? 45.306  -42.179 40.700  1.00 73.01  ? 37   THR C OG1 1 
ATOM   228   C CG2 . THR A  1 31  ? 44.213  -43.263 42.517  1.00 73.56  ? 37   THR C CG2 1 
ATOM   229   N N   . HIS A  1 32  ? 44.554  -39.448 40.249  1.00 71.47  ? 38   HIS C N   1 
ATOM   230   C CA  . HIS A  1 32  ? 45.163  -38.340 39.531  1.00 70.93  ? 38   HIS C CA  1 
ATOM   231   C C   . HIS A  1 32  ? 44.196  -37.816 38.463  1.00 72.53  ? 38   HIS C C   1 
ATOM   232   O O   . HIS A  1 32  ? 43.609  -38.599 37.708  1.00 67.54  ? 38   HIS C O   1 
ATOM   233   C CB  . HIS A  1 32  ? 46.490  -38.760 38.879  1.00 70.54  ? 38   HIS C CB  1 
ATOM   234   C CG  . HIS A  1 32  ? 47.520  -39.283 39.836  1.00 77.86  ? 38   HIS C CG  1 
ATOM   235   N ND1 . HIS A  1 32  ? 47.487  -40.565 40.344  1.00 76.87  ? 38   HIS C ND1 1 
ATOM   236   C CD2 . HIS A  1 32  ? 48.621  -38.697 40.365  1.00 76.53  ? 38   HIS C CD2 1 
ATOM   237   C CE1 . HIS A  1 32  ? 48.522  -40.745 41.145  1.00 77.03  ? 38   HIS C CE1 1 
ATOM   238   N NE2 . HIS A  1 32  ? 49.224  -39.627 41.176  1.00 78.62  ? 38   HIS C NE2 1 
ATOM   239   N N   . ALA A  1 33  ? 44.056  -36.494 38.377  1.00 74.74  ? 39   ALA C N   1 
ATOM   240   C CA  . ALA A  1 33  ? 43.188  -35.885 37.371  1.00 67.66  ? 39   ALA C CA  1 
ATOM   241   C C   . ALA A  1 33  ? 43.812  -34.626 36.802  1.00 67.32  ? 39   ALA C C   1 
ATOM   242   O O   . ALA A  1 33  ? 44.690  -34.027 37.422  1.00 70.78  ? 39   ALA C O   1 
ATOM   243   C CB  . ALA A  1 33  ? 41.829  -35.562 37.970  1.00 55.77  ? 39   ALA C CB  1 
ATOM   244   N N   . GLN A  1 34  ? 43.344  -34.217 35.626  1.00 66.02  ? 40   GLN C N   1 
ATOM   245   C CA  . GLN A  1 34  ? 43.807  -32.978 35.016  1.00 64.23  ? 40   GLN C CA  1 
ATOM   246   C C   . GLN A  1 34  ? 42.619  -32.114 34.594  1.00 59.32  ? 40   GLN C C   1 
ATOM   247   O O   . GLN A  1 34  ? 41.816  -32.529 33.750  1.00 58.26  ? 40   GLN C O   1 
ATOM   248   C CB  . GLN A  1 34  ? 44.713  -33.260 33.806  1.00 55.63  ? 40   GLN C CB  1 
ATOM   249   C CG  . GLN A  1 34  ? 45.212  -31.992 33.108  1.00 53.57  ? 40   GLN C CG  1 
ATOM   250   C CD  . GLN A  1 34  ? 46.211  -32.260 31.978  1.00 58.36  ? 40   GLN C CD  1 
ATOM   251   O OE1 . GLN A  1 34  ? 46.758  -33.361 31.845  1.00 65.90  ? 40   GLN C OE1 1 
ATOM   252   N NE2 . GLN A  1 34  ? 46.463  -31.240 31.167  1.00 51.14  ? 40   GLN C NE2 1 
ATOM   253   N N   . ASP A  1 35  ? 42.516  -30.925 35.191  1.00 59.35  ? 41   ASP C N   1 
ATOM   254   C CA  . ASP A  1 35  ? 41.540  -29.905 34.783  1.00 59.89  ? 41   ASP C CA  1 
ATOM   255   C C   . ASP A  1 35  ? 42.004  -29.350 33.447  1.00 57.90  ? 41   ASP C C   1 
ATOM   256   O O   . ASP A  1 35  ? 43.193  -29.048 33.295  1.00 59.27  ? 41   ASP C O   1 
ATOM   257   C CB  . ASP A  1 35  ? 41.452  -28.771 35.821  1.00 60.00  ? 41   ASP C CB  1 
ATOM   258   C CG  . ASP A  1 35  ? 40.316  -27.768 35.540  1.00 59.90  ? 41   ASP C CG  1 
ATOM   259   O OD1 . ASP A  1 35  ? 39.654  -27.840 34.476  1.00 54.98  ? 41   ASP C OD1 1 
ATOM   260   O OD2 . ASP A  1 35  ? 40.110  -26.877 36.395  1.00 59.07  ? 41   ASP C OD2 1 
ATOM   261   N N   . ILE A  1 36  ? 41.083  -29.156 32.502  1.00 53.76  ? 42   ILE C N   1 
ATOM   262   C CA  . ILE A  1 36  ? 41.491  -28.626 31.194  1.00 58.29  ? 42   ILE C CA  1 
ATOM   263   C C   . ILE A  1 36  ? 40.716  -27.361 30.800  1.00 51.33  ? 42   ILE C C   1 
ATOM   264   O O   . ILE A  1 36  ? 40.743  -26.949 29.642  1.00 48.02  ? 42   ILE C O   1 
ATOM   265   C CB  . ILE A  1 36  ? 41.323  -29.687 30.065  1.00 50.82  ? 42   ILE C CB  1 
ATOM   266   C CG1 . ILE A  1 36  ? 39.859  -30.103 29.898  1.00 49.46  ? 42   ILE C CG1 1 
ATOM   267   C CG2 . ILE A  1 36  ? 42.238  -30.885 30.313  1.00 46.72  ? 42   ILE C CG2 1 
ATOM   268   C CD1 . ILE A  1 36  ? 39.614  -31.112 28.758  1.00 39.79  ? 42   ILE C CD1 1 
ATOM   269   N N   . LEU A  1 37  ? 40.072  -26.734 31.783  1.00 47.28  ? 43   LEU C N   1 
ATOM   270   C CA  . LEU A  1 37  ? 39.231  -25.568 31.551  1.00 43.93  ? 43   LEU C CA  1 
ATOM   271   C C   . LEU A  1 37  ? 39.656  -24.328 32.364  1.00 48.85  ? 43   LEU C C   1 
ATOM   272   O O   . LEU A  1 37  ? 39.611  -24.322 33.609  1.00 47.92  ? 43   LEU C O   1 
ATOM   273   C CB  . LEU A  1 37  ? 37.782  -25.918 31.869  1.00 44.08  ? 43   LEU C CB  1 
ATOM   274   C CG  . LEU A  1 37  ? 36.759  -24.806 31.699  1.00 46.27  ? 43   LEU C CG  1 
ATOM   275   C CD1 . LEU A  1 37  ? 36.593  -24.526 30.204  1.00 46.04  ? 43   LEU C CD1 1 
ATOM   276   C CD2 . LEU A  1 37  ? 35.435  -25.171 32.351  1.00 43.26  ? 43   LEU C CD2 1 
ATOM   277   N N   . GLU A  1 38  ? 40.083  -23.285 31.651  1.00 45.81  ? 44   GLU C N   1 
ATOM   278   C CA  . GLU A  1 38  ? 40.429  -22.022 32.287  1.00 41.35  ? 44   GLU C CA  1 
ATOM   279   C C   . GLU A  1 38  ? 39.155  -21.259 32.621  1.00 41.32  ? 44   GLU C C   1 
ATOM   280   O O   . GLU A  1 38  ? 38.297  -21.073 31.765  1.00 39.39  ? 44   GLU C O   1 
ATOM   281   C CB  . GLU A  1 38  ? 41.344  -21.186 31.390  1.00 40.88  ? 44   GLU C CB  1 
ATOM   282   C CG  . GLU A  1 38  ? 41.633  -19.818 31.978  1.00 41.87  ? 44   GLU C CG  1 
ATOM   283   C CD  . GLU A  1 38  ? 42.319  -19.932 33.328  1.00 48.13  ? 44   GLU C CD  1 
ATOM   284   O OE1 . GLU A  1 38  ? 41.760  -19.407 34.333  1.00 39.34  ? 44   GLU C OE1 1 
ATOM   285   O OE2 . GLU A  1 38  ? 43.404  -20.573 33.371  1.00 52.24  ? 44   GLU C OE2 1 
ATOM   286   N N   . LYS A  1 39  ? 39.013  -20.844 33.874  1.00 41.71  ? 45   LYS C N   1 
ATOM   287   C CA  . LYS A  1 39  ? 37.776  -20.220 34.311  1.00 35.80  ? 45   LYS C CA  1 
ATOM   288   C C   . LYS A  1 39  ? 38.056  -18.859 34.914  1.00 35.47  ? 45   LYS C C   1 
ATOM   289   O O   . LYS A  1 39  ? 37.148  -18.244 35.479  1.00 32.11  ? 45   LYS C O   1 
ATOM   290   C CB  . LYS A  1 39  ? 37.048  -21.105 35.325  1.00 31.95  ? 45   LYS C CB  1 
ATOM   291   C CG  . LYS A  1 39  ? 36.555  -22.419 34.747  1.00 46.31  ? 45   LYS C CG  1 
ATOM   292   C CD  . LYS A  1 39  ? 36.058  -23.415 35.818  1.00 45.39  ? 45   LYS C CD  1 
ATOM   293   C CE  . LYS A  1 39  ? 37.259  -24.031 36.551  1.00 46.17  ? 45   LYS C CE  1 
ATOM   294   N NZ  . LYS A  1 39  ? 38.340  -24.517 35.603  1.00 43.77  ? 45   LYS C NZ  1 
ATOM   295   N N   . THR A  1 40  ? 39.293  -18.375 34.799  1.00 31.59  ? 46   THR C N   1 
ATOM   296   C CA  . THR A  1 40  ? 39.610  -17.083 35.416  1.00 37.06  ? 46   THR C CA  1 
ATOM   297   C C   . THR A  1 40  ? 40.249  -16.123 34.397  1.00 31.19  ? 46   THR C C   1 
ATOM   298   O O   . THR A  1 40  ? 40.955  -16.529 33.469  1.00 35.43  ? 46   THR C O   1 
ATOM   299   C CB  . THR A  1 40  ? 40.542  -17.217 36.708  1.00 39.25  ? 46   THR C CB  1 
ATOM   300   O OG1 . THR A  1 40  ? 41.907  -17.465 36.356  1.00 36.91  ? 46   THR C OG1 1 
ATOM   301   C CG2 . THR A  1 40  ? 40.044  -18.312 37.652  1.00 30.35  ? 46   THR C CG2 1 
ATOM   302   N N   . HIS A  1 41  ? 39.949  -14.845 34.573  1.00 33.90  ? 47   HIS C N   1 
ATOM   303   C CA  . HIS A  1 41  ? 40.481  -13.765 33.759  1.00 37.16  ? 47   HIS C CA  1 
ATOM   304   C C   . HIS A  1 41  ? 40.900  -12.640 34.709  1.00 34.39  ? 47   HIS C C   1 
ATOM   305   O O   . HIS A  1 41  ? 40.476  -12.639 35.843  1.00 40.29  ? 47   HIS C O   1 
ATOM   306   C CB  . HIS A  1 41  ? 39.418  -13.285 32.777  1.00 33.80  ? 47   HIS C CB  1 
ATOM   307   C CG  . HIS A  1 41  ? 38.192  -12.740 33.445  1.00 34.03  ? 47   HIS C CG  1 
ATOM   308   N ND1 . HIS A  1 41  ? 38.057  -11.404 33.779  1.00 38.97  ? 47   HIS C ND1 1 
ATOM   309   C CD2 . HIS A  1 41  ? 37.040  -13.341 33.828  1.00 31.84  ? 47   HIS C CD2 1 
ATOM   310   C CE1 . HIS A  1 41  ? 36.878  -11.207 34.347  1.00 37.25  ? 47   HIS C CE1 1 
ATOM   311   N NE2 . HIS A  1 41  ? 36.245  -12.368 34.395  1.00 36.53  ? 47   HIS C NE2 1 
ATOM   312   N N   . ASN A  1 42  ? 41.677  -11.664 34.259  1.00 34.05  ? 48   ASN C N   1 
ATOM   313   C CA  . ASN A  1 42  ? 42.180  -10.638 35.181  1.00 35.50  ? 48   ASN C CA  1 
ATOM   314   C C   . ASN A  1 42  ? 41.289  -9.394  35.303  1.00 36.94  ? 48   ASN C C   1 
ATOM   315   O O   . ASN A  1 42  ? 41.659  -8.428  35.961  1.00 35.34  ? 48   ASN C O   1 
ATOM   316   C CB  . ASN A  1 42  ? 43.612  -10.222 34.794  1.00 34.31  ? 48   ASN C CB  1 
ATOM   317   C CG  . ASN A  1 42  ? 43.680  -9.281  33.553  1.00 38.39  ? 48   ASN C CG  1 
ATOM   318   O OD1 . ASN A  1 42  ? 42.660  -8.884  32.963  1.00 38.16  ? 48   ASN C OD1 1 
ATOM   319   N ND2 . ASN A  1 42  ? 44.910  -8.897  33.186  1.00 33.46  ? 48   ASN C ND2 1 
ATOM   320   N N   . GLY A  1 43  ? 40.164  -9.392  34.593  1.00 38.15  ? 49   GLY C N   1 
ATOM   321   C CA  . GLY A  1 43  ? 39.190  -8.309  34.669  1.00 36.57  ? 49   GLY C CA  1 
ATOM   322   C C   . GLY A  1 43  ? 39.641  -6.989  34.063  1.00 38.42  ? 49   GLY C C   1 
ATOM   323   O O   . GLY A  1 43  ? 39.031  -5.951  34.344  1.00 43.07  ? 49   GLY C O   1 
ATOM   324   N N   . LYS A  1 44  ? 40.656  -7.026  33.192  1.00 36.19  ? 50   LYS C N   1 
ATOM   325   C CA  . LYS A  1 44  ? 41.249  -5.807  32.603  1.00 39.85  ? 50   LYS C CA  1 
ATOM   326   C C   . LYS A  1 44  ? 41.317  -5.758  31.066  1.00 36.39  ? 50   LYS C C   1 
ATOM   327   O O   . LYS A  1 44  ? 41.230  -6.795  30.395  1.00 34.77  ? 50   LYS C O   1 
ATOM   328   C CB  . LYS A  1 44  ? 42.701  -5.633  33.088  1.00 36.61  ? 50   LYS C CB  1 
ATOM   329   C CG  . LYS A  1 44  ? 42.960  -5.545  34.584  1.00 38.33  ? 50   LYS C CG  1 
ATOM   330   C CD  . LYS A  1 44  ? 44.483  -5.390  34.842  1.00 36.03  ? 50   LYS C CD  1 
ATOM   331   C CE  . LYS A  1 44  ? 44.785  -4.878  36.264  1.00 44.97  ? 50   LYS C CE  1 
ATOM   332   N NZ  . LYS A  1 44  ? 45.836  -3.781  36.336  1.00 35.78  ? 50   LYS C NZ  1 
ATOM   333   N N   . LEU A  1 45  ? 41.529  -4.554  30.526  1.00 34.42  ? 51   LEU C N   1 
ATOM   334   C CA  . LEU A  1 45  ? 41.827  -4.387  29.091  1.00 32.37  ? 51   LEU C CA  1 
ATOM   335   C C   . LEU A  1 45  ? 43.329  -4.140  28.869  1.00 32.57  ? 51   LEU C C   1 
ATOM   336   O O   . LEU A  1 45  ? 43.837  -3.101  29.304  1.00 35.23  ? 51   LEU C O   1 
ATOM   337   C CB  . LEU A  1 45  ? 41.016  -3.220  28.510  1.00 28.20  ? 51   LEU C CB  1 
ATOM   338   C CG  . LEU A  1 45  ? 39.494  -3.398  28.475  1.00 31.51  ? 51   LEU C CG  1 
ATOM   339   C CD1 . LEU A  1 45  ? 38.794  -2.168  27.958  1.00 32.63  ? 51   LEU C CD1 1 
ATOM   340   C CD2 . LEU A  1 45  ? 39.071  -4.634  27.687  1.00 27.65  ? 51   LEU C CD2 1 
ATOM   341   N N   . CYS A  1 46  ? 44.018  -5.042  28.157  1.00 27.37  ? 52   CYS C N   1 
ATOM   342   C CA  . CYS A  1 46  ? 45.478  -4.948  28.006  1.00 29.83  ? 52   CYS C CA  1 
ATOM   343   C C   . CYS A  1 46  ? 46.025  -4.795  26.598  1.00 30.97  ? 52   CYS C C   1 
ATOM   344   O O   . CYS A  1 46  ? 45.286  -4.818  25.596  1.00 33.90  ? 52   CYS C O   1 
ATOM   345   C CB  . CYS A  1 46  ? 46.170  -6.170  28.597  1.00 33.72  ? 52   CYS C CB  1 
ATOM   346   S SG  . CYS A  1 46  ? 45.598  -6.669  30.203  1.00 35.95  ? 52   CYS C SG  1 
ATOM   347   N N   . ASN A  1 47  ? 47.344  -4.616  26.547  1.00 29.16  ? 53   ASN C N   1 
ATOM   348   C CA  . ASN A  1 47  ? 48.069  -4.673  25.294  1.00 29.96  ? 53   ASN C CA  1 
ATOM   349   C C   . ASN A  1 47  ? 48.024  -6.083  24.773  1.00 34.09  ? 53   ASN C C   1 
ATOM   350   O O   . ASN A  1 47  ? 48.104  -7.062  25.551  1.00 32.17  ? 53   ASN C O   1 
ATOM   351   C CB  . ASN A  1 47  ? 49.526  -4.262  25.477  1.00 30.85  ? 53   ASN C CB  1 
ATOM   352   C CG  . ASN A  1 47  ? 49.699  -2.783  25.783  1.00 37.23  ? 53   ASN C CG  1 
ATOM   353   O OD1 . ASN A  1 47  ? 48.748  -2.061  26.134  1.00 36.68  ? 53   ASN C OD1 1 
ATOM   354   N ND2 . ASN A  1 47  ? 50.938  -2.324  25.665  1.00 39.47  ? 53   ASN C ND2 1 
ATOM   355   N N   . LEU A  1 48  ? 47.965  -6.175  23.451  1.00 28.45  ? 54   LEU C N   1 
ATOM   356   C CA  . LEU A  1 48  ? 48.040  -7.443  22.763  1.00 31.20  ? 54   LEU C CA  1 
ATOM   357   C C   . LEU A  1 48  ? 49.425  -7.508  22.143  1.00 33.59  ? 54   LEU C C   1 
ATOM   358   O O   . LEU A  1 48  ? 49.798  -6.654  21.331  1.00 32.42  ? 54   LEU C O   1 
ATOM   359   C CB  . LEU A  1 48  ? 46.931  -7.547  21.738  1.00 32.83  ? 54   LEU C CB  1 
ATOM   360   C CG  . LEU A  1 48  ? 46.590  -8.920  21.205  1.00 32.21  ? 54   LEU C CG  1 
ATOM   361   C CD1 . LEU A  1 48  ? 45.970  -9.782  22.291  1.00 22.41  ? 54   LEU C CD1 1 
ATOM   362   C CD2 . LEU A  1 48  ? 45.592  -8.672  20.083  1.00 29.39  ? 54   LEU C CD2 1 
ATOM   363   N N   . ASP A  1 49  ? 50.203  -8.485  22.601  1.00 38.55  ? 55   ASP C N   1 
ATOM   364   C CA  . ASP A  1 49  ? 51.660  -8.495  22.431  1.00 36.84  ? 55   ASP C CA  1 
ATOM   365   C C   . ASP A  1 49  ? 52.234  -7.184  22.923  1.00 40.60  ? 55   ASP C C   1 
ATOM   366   O O   . ASP A  1 49  ? 52.040  -6.802  24.049  1.00 43.44  ? 55   ASP C O   1 
ATOM   367   C CB  . ASP A  1 49  ? 52.056  -8.736  21.004  1.00 38.60  ? 55   ASP C CB  1 
ATOM   368   C CG  . ASP A  1 49  ? 52.234  -10.196 20.726  1.00 54.44  ? 55   ASP C CG  1 
ATOM   369   O OD1 . ASP A  1 49  ? 52.589  -10.911 21.690  1.00 61.56  ? 55   ASP C OD1 1 
ATOM   370   O OD2 . ASP A  1 49  ? 52.027  -10.625 19.566  1.00 64.16  ? 55   ASP C OD2 1 
ATOM   371   N N   . GLY A  1 50  A 52.934  -6.446  22.103  1.00 41.49  ? 55   GLY C N   1 
ATOM   372   C CA  . GLY A  1 50  A 53.407  -5.186  22.655  1.00 32.91  ? 55   GLY C CA  1 
ATOM   373   C C   . GLY A  1 50  A 52.412  -4.060  22.487  1.00 33.59  ? 55   GLY C C   1 
ATOM   374   O O   . GLY A  1 50  A 52.621  -2.991  23.035  1.00 43.88  ? 55   GLY C O   1 
ATOM   375   N N   . VAL A  1 51  ? 51.339  -4.280  21.725  1.00 29.82  ? 56   VAL C N   1 
ATOM   376   C CA  . VAL A  1 51  ? 50.587  -3.165  21.134  1.00 26.83  ? 56   VAL C CA  1 
ATOM   377   C C   . VAL A  1 51  ? 49.339  -2.725  21.874  1.00 25.71  ? 56   VAL C C   1 
ATOM   378   O O   . VAL A  1 51  ? 48.450  -3.516  22.156  1.00 29.39  ? 56   VAL C O   1 
ATOM   379   C CB  . VAL A  1 51  ? 50.180  -3.510  19.680  1.00 32.94  ? 56   VAL C CB  1 
ATOM   380   C CG1 . VAL A  1 51  ? 49.505  -2.313  19.012  1.00 25.02  ? 56   VAL C CG1 1 
ATOM   381   C CG2 . VAL A  1 51  ? 51.388  -3.994  18.899  1.00 21.39  ? 56   VAL C CG2 1 
ATOM   382   N N   . LYS A  1 52  ? 49.247  -1.433  22.140  1.00 28.35  ? 57   LYS C N   1 
ATOM   383   C CA  . LYS A  1 52  ? 48.133  -0.897  22.915  1.00 26.89  ? 57   LYS C CA  1 
ATOM   384   C C   . LYS A  1 52  ? 46.834  -0.783  22.106  1.00 33.45  ? 57   LYS C C   1 
ATOM   385   O O   . LYS A  1 52  ? 46.852  -0.461  20.914  1.00 34.98  ? 57   LYS C O   1 
ATOM   386   C CB  . LYS A  1 52  ? 48.528  0.471   23.487  1.00 22.12  ? 57   LYS C CB  1 
ATOM   387   C CG  . LYS A  1 52  ? 47.468  1.099   24.392  1.00 35.29  ? 57   LYS C CG  1 
ATOM   388   C CD  . LYS A  1 52  ? 47.992  2.336   25.109  1.00 39.11  ? 57   LYS C CD  1 
ATOM   389   C CE  . LYS A  1 52  ? 46.927  2.956   25.997  1.00 35.36  ? 57   LYS C CE  1 
ATOM   390   N NZ  . LYS A  1 52  ? 47.506  4.039   26.858  1.00 39.93  ? 57   LYS C NZ  1 
ATOM   391   N N   . PRO A  1 53  ? 45.690  -1.077  22.743  1.00 35.57  ? 58   PRO C N   1 
ATOM   392   C CA  . PRO A  1 53  ? 44.414  -0.875  22.039  1.00 32.83  ? 58   PRO C CA  1 
ATOM   393   C C   . PRO A  1 53  ? 44.036  0.611   21.930  1.00 33.37  ? 58   PRO C C   1 
ATOM   394   O O   . PRO A  1 53  ? 44.590  1.426   22.662  1.00 29.19  ? 58   PRO C O   1 
ATOM   395   C CB  . PRO A  1 53  ? 43.403  -1.607  22.925  1.00 28.01  ? 58   PRO C CB  1 
ATOM   396   C CG  . PRO A  1 53  ? 44.014  -1.521  24.296  1.00 28.97  ? 58   PRO C CG  1 
ATOM   397   C CD  . PRO A  1 53  ? 45.494  -1.685  24.074  1.00 30.72  ? 58   PRO C CD  1 
ATOM   398   N N   . LEU A  1 54  ? 43.158  0.943   20.979  1.00 34.92  ? 59   LEU C N   1 
ATOM   399   C CA  . LEU A  1 54  ? 42.500  2.242   20.920  1.00 32.38  ? 59   LEU C CA  1 
ATOM   400   C C   . LEU A  1 54  ? 41.283  2.192   21.854  1.00 34.76  ? 59   LEU C C   1 
ATOM   401   O O   . LEU A  1 54  ? 40.292  1.526   21.562  1.00 35.99  ? 59   LEU C O   1 
ATOM   402   C CB  . LEU A  1 54  ? 42.085  2.591   19.488  1.00 27.26  ? 59   LEU C CB  1 
ATOM   403   C CG  . LEU A  1 54  ? 41.232  3.841   19.208  1.00 34.07  ? 59   LEU C CG  1 
ATOM   404   C CD1 . LEU A  1 54  ? 41.901  5.167   19.678  1.00 26.69  ? 59   LEU C CD1 1 
ATOM   405   C CD2 . LEU A  1 54  ? 40.867  3.941   17.689  1.00 27.28  ? 59   LEU C CD2 1 
ATOM   406   N N   . ILE A  1 55  ? 41.376  2.861   23.000  1.00 35.57  ? 60   ILE C N   1 
ATOM   407   C CA  . ILE A  1 55  ? 40.285  2.892   23.979  1.00 32.51  ? 60   ILE C CA  1 
ATOM   408   C C   . ILE A  1 55  ? 39.584  4.239   23.852  1.00 31.85  ? 60   ILE C C   1 
ATOM   409   O O   . ILE A  1 55  ? 40.153  5.257   24.206  1.00 37.59  ? 60   ILE C O   1 
ATOM   410   C CB  . ILE A  1 55  ? 40.830  2.626   25.415  1.00 34.95  ? 60   ILE C CB  1 
ATOM   411   C CG1 . ILE A  1 55  ? 41.483  1.243   25.423  1.00 36.36  ? 60   ILE C CG1 1 
ATOM   412   C CG2 . ILE A  1 55  ? 39.736  2.654   26.450  1.00 30.86  ? 60   ILE C CG2 1 
ATOM   413   C CD1 . ILE A  1 55  ? 41.993  0.780   26.715  1.00 32.07  ? 60   ILE C CD1 1 
ATOM   414   N N   . LEU A  1 56  ? 38.421  4.254   23.197  1.00 34.05  ? 61   LEU C N   1 
ATOM   415   C CA  . LEU A  1 56  ? 37.543  5.433   23.128  1.00 34.34  ? 61   LEU C CA  1 
ATOM   416   C C   . LEU A  1 56  ? 36.946  5.580   24.509  1.00 39.86  ? 61   LEU C C   1 
ATOM   417   O O   . LEU A  1 56  ? 36.984  4.621   25.279  1.00 54.93  ? 61   LEU C O   1 
ATOM   418   C CB  . LEU A  1 56  ? 36.466  5.273   22.036  1.00 34.89  ? 61   LEU C CB  1 
ATOM   419   C CG  . LEU A  1 56  ? 36.991  4.807   20.666  1.00 35.30  ? 61   LEU C CG  1 
ATOM   420   C CD1 . LEU A  1 56  ? 35.895  4.373   19.704  1.00 26.68  ? 61   LEU C CD1 1 
ATOM   421   C CD2 . LEU A  1 56  ? 37.838  5.904   20.033  1.00 31.38  ? 61   LEU C CD2 1 
ATOM   422   N N   . ARG A  1 57  ? 36.472  6.737   24.925  1.00 38.55  ? 62   ARG C N   1 
ATOM   423   C CA  . ARG A  1 57  ? 35.911  6.687   26.281  1.00 42.87  ? 62   ARG C CA  1 
ATOM   424   C C   . ARG A  1 57  ? 34.431  6.618   26.217  1.00 39.30  ? 62   ARG C C   1 
ATOM   425   O O   . ARG A  1 57  ? 33.832  5.546   26.248  1.00 36.89  ? 62   ARG C O   1 
ATOM   426   C CB  . ARG A  1 57  ? 36.296  7.885   27.150  1.00 50.89  ? 62   ARG C CB  1 
ATOM   427   C CG  . ARG A  1 57  ? 37.680  7.823   27.716  1.00 50.14  ? 62   ARG C CG  1 
ATOM   428   C CD  . ARG A  1 57  ? 37.970  8.959   28.705  1.00 47.72  ? 62   ARG C CD  1 
ATOM   429   N NE  . ARG A  1 57  ? 39.355  9.326   28.463  1.00 50.08  ? 62   ARG C NE  1 
ATOM   430   C CZ  . ARG A  1 57  ? 40.403  8.686   28.955  1.00 41.71  ? 62   ARG C CZ  1 
ATOM   431   N NH1 . ARG A  1 57  ? 40.236  7.677   29.797  1.00 51.44  ? 62   ARG C NH1 1 
ATOM   432   N NH2 . ARG A  1 57  ? 41.620  9.078   28.612  1.00 39.54  ? 62   ARG C NH2 1 
ATOM   433   N N   . ASP A  1 58  ? 33.863  7.813   26.181  1.00 38.89  ? 63   ASP C N   1 
ATOM   434   C CA  . ASP A  1 58  ? 32.445  8.013   26.024  1.00 42.96  ? 63   ASP C CA  1 
ATOM   435   C C   . ASP A  1 58  ? 32.201  8.476   24.594  1.00 41.20  ? 63   ASP C C   1 
ATOM   436   O O   . ASP A  1 58  ? 31.187  9.124   24.311  1.00 38.01  ? 63   ASP C O   1 
ATOM   437   C CB  . ASP A  1 58  ? 31.927  9.044   27.023  1.00 44.42  ? 63   ASP C CB  1 
ATOM   438   C CG  . ASP A  1 58  ? 32.194  8.643   28.445  1.00 48.32  ? 63   ASP C CG  1 
ATOM   439   O OD1 . ASP A  1 58  ? 31.581  7.636   28.885  1.00 47.36  ? 63   ASP C OD1 1 
ATOM   440   O OD2 . ASP A  1 58  ? 32.994  9.346   29.115  1.00 47.95  ? 63   ASP C OD2 1 
ATOM   441   N N   . CYS A  1 59  ? 33.163  8.174   23.712  1.00 39.39  ? 64   CYS C N   1 
ATOM   442   C CA  . CYS A  1 59  ? 33.052  8.546   22.304  1.00 38.51  ? 64   CYS C CA  1 
ATOM   443   C C   . CYS A  1 59  ? 32.687  7.321   21.440  1.00 35.02  ? 64   CYS C C   1 
ATOM   444   O O   . CYS A  1 59  ? 33.196  6.194   21.639  1.00 31.56  ? 64   CYS C O   1 
ATOM   445   C CB  . CYS A  1 59  ? 34.364  9.193   21.816  1.00 37.33  ? 64   CYS C CB  1 
ATOM   446   S SG  . CYS A  1 59  ? 34.596  10.977  22.295  1.00 46.98  ? 64   CYS C SG  1 
ATOM   447   N N   . SER A  1 60  ? 31.842  7.554   20.442  1.00 32.41  ? 65   SER C N   1 
ATOM   448   C CA  . SER A  1 60  ? 31.488  6.489   19.505  1.00 29.07  ? 65   SER C CA  1 
ATOM   449   C C   . SER A  1 60  ? 32.433  6.535   18.314  1.00 28.87  ? 65   SER C C   1 
ATOM   450   O O   . SER A  1 60  ? 33.196  7.519   18.147  1.00 26.15  ? 65   SER C O   1 
ATOM   451   C CB  . SER A  1 60  ? 30.041  6.642   19.040  1.00 24.78  ? 65   SER C CB  1 
ATOM   452   O OG  . SER A  1 60  ? 29.890  7.789   18.203  1.00 24.65  ? 65   SER C OG  1 
ATOM   453   N N   . VAL A  1 61  ? 32.358  5.512   17.458  1.00 26.86  ? 66   VAL C N   1 
ATOM   454   C CA  . VAL A  1 61  ? 33.206  5.498   16.270  1.00 24.95  ? 66   VAL C CA  1 
ATOM   455   C C   . VAL A  1 61  ? 32.885  6.746   15.447  1.00 22.53  ? 66   VAL C C   1 
ATOM   456   O O   . VAL A  1 61  ? 33.792  7.466   15.014  1.00 23.68  ? 66   VAL C O   1 
ATOM   457   C CB  . VAL A  1 61  ? 33.027  4.199   15.436  1.00 22.17  ? 66   VAL C CB  1 
ATOM   458   C CG1 . VAL A  1 61  ? 33.620  4.359   14.069  1.00 23.86  ? 66   VAL C CG1 1 
ATOM   459   C CG2 . VAL A  1 61  ? 33.689  3.049   16.138  1.00 21.38  ? 66   VAL C CG2 1 
ATOM   460   N N   . ALA A  1 62  ? 31.601  7.052   15.322  1.00 23.46  ? 67   ALA C N   1 
ATOM   461   C CA  . ALA A  1 62  ? 31.190  8.230   14.551  1.00 26.45  ? 67   ALA C CA  1 
ATOM   462   C C   . ALA A  1 62  ? 31.735  9.483   15.158  1.00 28.91  ? 67   ALA C C   1 
ATOM   463   O O   . ALA A  1 62  ? 32.196  10.367  14.424  1.00 31.84  ? 67   ALA C O   1 
ATOM   464   C CB  . ALA A  1 62  ? 29.670  8.328   14.439  1.00 25.10  ? 67   ALA C CB  1 
ATOM   465   N N   . GLY A  1 63  ? 31.691  9.564   16.494  1.00 28.22  ? 68   GLY C N   1 
ATOM   466   C CA  . GLY A  1 63  ? 32.173  10.747  17.178  1.00 26.19  ? 68   GLY C CA  1 
ATOM   467   C C   . GLY A  1 63  ? 33.641  10.986  16.873  1.00 26.65  ? 68   GLY C C   1 
ATOM   468   O O   . GLY A  1 63  ? 34.038  12.103  16.543  1.00 26.61  ? 68   GLY C O   1 
ATOM   469   N N   . TRP A  1 64  ? 34.444  9.934   16.979  1.00 23.95  ? 69   TRP C N   1 
ATOM   470   C CA  . TRP A  1 64  ? 35.874  10.037  16.706  1.00 26.53  ? 69   TRP C CA  1 
ATOM   471   C C   . TRP A  1 64  ? 36.189  10.497  15.278  1.00 29.06  ? 69   TRP C C   1 
ATOM   472   O O   . TRP A  1 64  ? 36.841  11.519  15.090  1.00 27.76  ? 69   TRP C O   1 
ATOM   473   C CB  . TRP A  1 64  ? 36.544  8.680   17.006  1.00 27.64  ? 69   TRP C CB  1 
ATOM   474   C CG  . TRP A  1 64  ? 37.911  8.438   16.389  1.00 25.67  ? 69   TRP C CG  1 
ATOM   475   C CD1 . TRP A  1 64  ? 38.932  9.323   16.246  1.00 24.44  ? 69   TRP C CD1 1 
ATOM   476   C CD2 . TRP A  1 64  ? 38.360  7.208   15.799  1.00 24.21  ? 69   TRP C CD2 1 
ATOM   477   N NE1 . TRP A  1 64  ? 40.003  8.716   15.612  1.00 25.02  ? 69   TRP C NE1 1 
ATOM   478   C CE2 . TRP A  1 64  ? 39.667  7.418   15.330  1.00 22.50  ? 69   TRP C CE2 1 
ATOM   479   C CE3 . TRP A  1 64  ? 37.780  5.949   15.628  1.00 21.64  ? 69   TRP C CE3 1 
ATOM   480   C CZ2 . TRP A  1 64  ? 40.403  6.410   14.711  1.00 25.91  ? 69   TRP C CZ2 1 
ATOM   481   C CZ3 . TRP A  1 64  ? 38.523  4.942   15.003  1.00 20.56  ? 69   TRP C CZ3 1 
ATOM   482   C CH2 . TRP A  1 64  ? 39.807  5.179   14.555  1.00 21.59  ? 69   TRP C CH2 1 
ATOM   483   N N   . LEU A  1 65  ? 35.682  9.778   14.271  1.00 32.79  ? 70   LEU C N   1 
ATOM   484   C CA  . LEU A  1 65  ? 36.122  10.000  12.882  1.00 26.28  ? 70   LEU C CA  1 
ATOM   485   C C   . LEU A  1 65  ? 35.706  11.376  12.378  1.00 26.12  ? 70   LEU C C   1 
ATOM   486   O O   . LEU A  1 65  ? 36.509  12.060  11.767  1.00 28.50  ? 70   LEU C O   1 
ATOM   487   C CB  . LEU A  1 65  ? 35.555  8.900   11.999  1.00 21.03  ? 70   LEU C CB  1 
ATOM   488   C CG  . LEU A  1 65  ? 36.164  7.519   12.276  1.00 24.77  ? 70   LEU C CG  1 
ATOM   489   C CD1 . LEU A  1 65  ? 35.486  6.444   11.449  1.00 21.36  ? 70   LEU C CD1 1 
ATOM   490   C CD2 . LEU A  1 65  ? 37.680  7.513   12.020  1.00 18.63  ? 70   LEU C CD2 1 
ATOM   491   N N   . LEU A  1 66  ? 34.497  11.814  12.732  1.00 26.32  ? 71   LEU C N   1 
ATOM   492   C CA  . LEU A  1 66  ? 33.980  13.123  12.330  1.00 27.85  ? 71   LEU C CA  1 
ATOM   493   C C   . LEU A  1 66  ? 34.609  14.242  13.160  1.00 29.67  ? 71   LEU C C   1 
ATOM   494   O O   . LEU A  1 66  ? 34.711  15.395  12.727  1.00 26.29  ? 71   LEU C O   1 
ATOM   495   C CB  . LEU A  1 66  ? 32.447  13.176  12.503  1.00 25.61  ? 71   LEU C CB  1 
ATOM   496   C CG  . LEU A  1 66  ? 31.633  12.477  11.406  1.00 30.61  ? 71   LEU C CG  1 
ATOM   497   C CD1 . LEU A  1 66  ? 30.141  12.422  11.700  1.00 28.17  ? 71   LEU C CD1 1 
ATOM   498   C CD2 . LEU A  1 66  ? 31.900  13.087  10.037  1.00 26.94  ? 71   LEU C CD2 1 
ATOM   499   N N   . GLY A  1 67  ? 34.995  13.891  14.384  1.00 31.15  ? 72   GLY C N   1 
ATOM   500   C CA  . GLY A  1 67  ? 35.622  14.842  15.274  1.00 30.64  ? 72   GLY C CA  1 
ATOM   501   C C   . GLY A  1 67  ? 34.619  15.643  16.088  1.00 34.46  ? 72   GLY C C   1 
ATOM   502   O O   . GLY A  1 67  ? 34.637  16.888  16.039  1.00 33.21  ? 72   GLY C O   1 
ATOM   503   N N   . ASN A  1 68  ? 33.721  14.942  16.788  1.00 31.61  ? 73   ASN C N   1 
ATOM   504   C CA  . ASN A  1 68  ? 32.930  15.554  17.843  1.00 36.43  ? 73   ASN C CA  1 
ATOM   505   C C   . ASN A  1 68  ? 33.917  16.308  18.774  1.00 40.75  ? 73   ASN C C   1 
ATOM   506   O O   . ASN A  1 68  ? 34.954  15.748  19.152  1.00 37.93  ? 73   ASN C O   1 
ATOM   507   C CB  . ASN A  1 68  ? 32.128  14.471  18.575  1.00 40.11  ? 73   ASN C CB  1 
ATOM   508   C CG  . ASN A  1 68  ? 31.230  15.025  19.695  1.00 41.85  ? 73   ASN C CG  1 
ATOM   509   O OD1 . ASN A  1 68  ? 31.633  15.914  20.445  1.00 39.79  ? 73   ASN C OD1 1 
ATOM   510   N ND2 . ASN A  1 68  ? 30.042  14.444  19.850  1.00 37.27  ? 73   ASN C ND2 1 
ATOM   511   N N   . PRO A  1 69  ? 33.628  17.597  19.088  1.00 41.86  ? 74   PRO C N   1 
ATOM   512   C CA  . PRO A  1 69  ? 34.547  18.461  19.864  1.00 45.91  ? 74   PRO C CA  1 
ATOM   513   C C   . PRO A  1 69  ? 34.894  17.919  21.262  1.00 44.06  ? 74   PRO C C   1 
ATOM   514   O O   . PRO A  1 69  ? 35.903  18.309  21.855  1.00 44.78  ? 74   PRO C O   1 
ATOM   515   C CB  . PRO A  1 69  ? 33.775  19.775  19.997  1.00 47.11  ? 74   PRO C CB  1 
ATOM   516   C CG  . PRO A  1 69  ? 32.742  19.740  18.916  1.00 45.53  ? 74   PRO C CG  1 
ATOM   517   C CD  . PRO A  1 69  ? 32.377  18.303  18.741  1.00 38.34  ? 74   PRO C CD  1 
ATOM   518   N N   . MET A  1 70  ? 34.058  17.016  21.764  1.00 41.11  ? 75   MET C N   1 
ATOM   519   C CA  . MET A  1 70  ? 34.257  16.417  23.073  1.00 45.67  ? 75   MET C CA  1 
ATOM   520   C C   . MET A  1 70  ? 35.150  15.186  22.932  1.00 41.68  ? 75   MET C C   1 
ATOM   521   O O   . MET A  1 70  ? 35.369  14.474  23.910  1.00 42.99  ? 75   MET C O   1 
ATOM   522   C CB  . MET A  1 70  ? 32.904  16.009  23.698  1.00 39.74  ? 75   MET C CB  1 
ATOM   523   C CG  . MET A  1 70  ? 31.951  17.143  24.078  1.00 45.89  ? 75   MET C CG  1 
ATOM   524   S SD  . MET A  1 70  ? 32.180  17.910  25.705  1.00 62.41  ? 75   MET C SD  1 
ATOM   525   C CE  . MET A  1 70  ? 33.692  18.871  25.516  1.00 55.24  ? 75   MET C CE  1 
ATOM   526   N N   . CYS A  1 71  ? 35.677  14.945  21.732  1.00 35.92  ? 76   CYS C N   1 
ATOM   527   C CA  . CYS A  1 71  ? 36.477  13.740  21.498  1.00 35.82  ? 76   CYS C CA  1 
ATOM   528   C C   . CYS A  1 71  ? 37.909  14.040  21.055  1.00 39.00  ? 76   CYS C C   1 
ATOM   529   O O   . CYS A  1 71  ? 38.539  13.194  20.413  1.00 40.23  ? 76   CYS C O   1 
ATOM   530   C CB  . CYS A  1 71  ? 35.816  12.858  20.439  1.00 33.52  ? 76   CYS C CB  1 
ATOM   531   S SG  . CYS A  1 71  ? 34.129  12.352  20.809  1.00 41.18  ? 76   CYS C SG  1 
ATOM   532   N N   . ASP A  1 72  ? 38.434  15.202  21.449  1.00 38.42  ? 77   ASP C N   1 
ATOM   533   C CA  . ASP A  1 72  ? 39.732  15.695  20.981  1.00 40.33  ? 77   ASP C CA  1 
ATOM   534   C C   . ASP A  1 72  ? 40.941  14.840  21.380  1.00 39.54  ? 77   ASP C C   1 
ATOM   535   O O   . ASP A  1 72  ? 42.042  15.045  20.859  1.00 38.66  ? 77   ASP C O   1 
ATOM   536   C CB  . ASP A  1 72  ? 39.963  17.131  21.491  1.00 41.10  ? 77   ASP C CB  1 
ATOM   537   C CG  . ASP A  1 72  ? 39.212  18.191  20.676  1.00 48.34  ? 77   ASP C CG  1 
ATOM   538   O OD1 . ASP A  1 72  ? 38.789  17.907  19.531  1.00 48.76  ? 77   ASP C OD1 1 
ATOM   539   O OD2 . ASP A  1 72  ? 39.072  19.325  21.181  1.00 52.87  ? 77   ASP C OD2 1 
ATOM   540   N N   . GLU A  1 73  ? 40.742  13.900  22.301  1.00 34.93  ? 78   GLU C N   1 
ATOM   541   C CA  . GLU A  1 73  ? 41.795  12.965  22.696  1.00 35.97  ? 78   GLU C CA  1 
ATOM   542   C C   . GLU A  1 73  ? 42.281  12.100  21.530  1.00 39.39  ? 78   GLU C C   1 
ATOM   543   O O   . GLU A  1 73  ? 43.438  11.636  21.504  1.00 37.32  ? 78   GLU C O   1 
ATOM   544   C CB  . GLU A  1 73  ? 41.316  12.061  23.839  1.00 36.72  ? 78   GLU C CB  1 
ATOM   545   C CG  . GLU A  1 73  ? 42.374  11.035  24.261  1.00 36.96  ? 78   GLU C CG  1 
ATOM   546   C CD  . GLU A  1 73  ? 41.914  10.125  25.381  1.00 40.73  ? 78   GLU C CD  1 
ATOM   547   O OE1 . GLU A  1 73  ? 40.815  10.368  25.946  1.00 38.87  ? 78   GLU C OE1 1 
ATOM   548   O OE2 . GLU A  1 73  ? 42.642  9.147   25.667  1.00 38.73  ? 78   GLU C OE2 1 
ATOM   549   N N   . PHE A  1 74  ? 41.391  11.869  20.569  1.00 39.08  ? 79   PHE C N   1 
ATOM   550   C CA  . PHE A  1 74  ? 41.680  10.929  19.500  1.00 36.84  ? 79   PHE C CA  1 
ATOM   551   C C   . PHE A  1 74  ? 41.942  11.627  18.155  1.00 36.45  ? 79   PHE C C   1 
ATOM   552   O O   . PHE A  1 74  ? 41.814  10.996  17.092  1.00 40.45  ? 79   PHE C O   1 
ATOM   553   C CB  . PHE A  1 74  ? 40.513  9.954   19.381  1.00 32.75  ? 79   PHE C CB  1 
ATOM   554   C CG  . PHE A  1 74  ? 40.034  9.431   20.694  1.00 36.14  ? 79   PHE C CG  1 
ATOM   555   C CD1 . PHE A  1 74  ? 40.756  8.453   21.378  1.00 36.97  ? 79   PHE C CD1 1 
ATOM   556   C CD2 . PHE A  1 74  ? 38.878  9.953   21.276  1.00 41.28  ? 79   PHE C CD2 1 
ATOM   557   C CE1 . PHE A  1 74  ? 40.317  7.967   22.589  1.00 30.96  ? 79   PHE C CE1 1 
ATOM   558   C CE2 . PHE A  1 74  ? 38.431  9.485   22.508  1.00 33.46  ? 79   PHE C CE2 1 
ATOM   559   C CZ  . PHE A  1 74  ? 39.156  8.484   23.156  1.00 37.08  ? 79   PHE C CZ  1 
ATOM   560   N N   . LEU A  1 75  ? 42.354  12.896  18.198  1.00 31.88  ? 80   LEU C N   1 
ATOM   561   C CA  . LEU A  1 75  ? 42.581  13.666  16.970  1.00 38.31  ? 80   LEU C CA  1 
ATOM   562   C C   . LEU A  1 75  ? 43.698  13.064  16.094  1.00 42.27  ? 80   LEU C C   1 
ATOM   563   O O   . LEU A  1 75  ? 43.665  13.209  14.866  1.00 42.50  ? 80   LEU C O   1 
ATOM   564   C CB  . LEU A  1 75  ? 42.887  15.126  17.306  1.00 39.57  ? 80   LEU C CB  1 
ATOM   565   C CG  . LEU A  1 75  ? 41.686  16.036  17.634  1.00 44.30  ? 80   LEU C CG  1 
ATOM   566   C CD1 . LEU A  1 75  ? 42.168  17.403  18.054  1.00 40.76  ? 80   LEU C CD1 1 
ATOM   567   C CD2 . LEU A  1 75  ? 40.711  16.190  16.471  1.00 44.98  ? 80   LEU C CD2 1 
ATOM   568   N N   . ASN A  1 76  ? 44.656  12.381  16.725  1.00 35.17  ? 81   ASN C N   1 
ATOM   569   C CA  . ASN A  1 76  ? 45.749  11.708  16.032  1.00 36.29  ? 81   ASN C CA  1 
ATOM   570   C C   . ASN A  1 76  ? 46.217  10.455  16.792  1.00 44.47  ? 81   ASN C C   1 
ATOM   571   O O   . ASN A  1 76  ? 47.102  10.531  17.656  1.00 55.60  ? 81   ASN C O   1 
ATOM   572   C CB  . ASN A  1 76  ? 46.926  12.663  15.846  1.00 39.35  ? 81   ASN C CB  1 
ATOM   573   C CG  . ASN A  1 76  ? 46.691  13.684  14.751  1.00 50.65  ? 81   ASN C CG  1 
ATOM   574   O OD1 . ASN A  1 76  ? 46.815  13.378  13.559  1.00 51.96  ? 81   ASN C OD1 1 
ATOM   575   N ND2 . ASN A  1 76  ? 46.353  14.909  15.145  1.00 51.81  ? 81   ASN C ND2 1 
ATOM   576   N N   . VAL A  1 77  ? 45.643  9.298   16.492  1.00 35.12  ? 82   VAL C N   1 
ATOM   577   C CA  . VAL A  1 77  ? 45.972  8.137   17.293  1.00 34.38  ? 82   VAL C CA  1 
ATOM   578   C C   . VAL A  1 77  ? 47.089  7.303   16.680  1.00 32.62  ? 82   VAL C C   1 
ATOM   579   O O   . VAL A  1 77  ? 47.255  7.228   15.465  1.00 40.30  ? 82   VAL C O   1 
ATOM   580   C CB  . VAL A  1 77  ? 44.717  7.244   17.529  1.00 38.31  ? 82   VAL C CB  1 
ATOM   581   C CG1 . VAL A  1 77  ? 43.567  8.116   18.054  1.00 32.36  ? 82   VAL C CG1 1 
ATOM   582   C CG2 . VAL A  1 77  ? 44.280  6.533   16.250  1.00 37.33  ? 82   VAL C CG2 1 
ATOM   583   N N   . PRO A  1 78  ? 47.875  6.659   17.528  1.00 34.44  ? 83   PRO C N   1 
ATOM   584   C CA  . PRO A  1 78  ? 48.874  5.750   16.981  1.00 34.07  ? 83   PRO C CA  1 
ATOM   585   C C   . PRO A  1 78  ? 48.278  4.397   16.612  1.00 34.96  ? 83   PRO C C   1 
ATOM   586   O O   . PRO A  1 78  ? 47.118  4.122   16.936  1.00 36.21  ? 83   PRO C O   1 
ATOM   587   C CB  . PRO A  1 78  ? 49.864  5.603   18.137  1.00 31.50  ? 83   PRO C CB  1 
ATOM   588   C CG  . PRO A  1 78  ? 49.044  5.812   19.334  1.00 27.46  ? 83   PRO C CG  1 
ATOM   589   C CD  . PRO A  1 78  ? 48.033  6.846   18.976  1.00 28.18  ? 83   PRO C CD  1 
ATOM   590   N N   . GLU A  1 79  A 49.090  3.575   15.956  1.00 31.88  ? 83   GLU C N   1 
ATOM   591   C CA  . GLU A  1 79  A 48.749  2.209   15.608  1.00 33.89  ? 83   GLU C CA  1 
ATOM   592   C C   . GLU A  1 79  A 48.176  1.500   16.814  1.00 28.98  ? 83   GLU C C   1 
ATOM   593   O O   . GLU A  1 79  A 48.646  1.702   17.926  1.00 42.10  ? 83   GLU C O   1 
ATOM   594   C CB  . GLU A  1 79  A 49.996  1.480   15.082  1.00 34.34  ? 83   GLU C CB  1 
ATOM   595   C CG  . GLU A  1 79  A 49.837  -0.004  14.787  1.00 35.00  ? 83   GLU C CG  1 
ATOM   596   C CD  . GLU A  1 79  A 51.082  -0.587  14.151  1.00 41.79  ? 83   GLU C CD  1 
ATOM   597   O OE1 . GLU A  1 79  A 51.985  0.206   13.843  1.00 48.69  ? 83   GLU C OE1 1 
ATOM   598   O OE2 . GLU A  1 79  A 51.151  -1.814  13.918  1.00 48.65  ? 83   GLU C OE2 1 
ATOM   599   N N   . TRP A  1 80  ? 47.121  0.728   16.591  1.00 28.05  ? 84   TRP C N   1 
ATOM   600   C CA  . TRP A  1 80  ? 46.420  0.008   17.644  1.00 29.99  ? 84   TRP C CA  1 
ATOM   601   C C   . TRP A  1 80  ? 46.381  -1.458  17.296  1.00 29.16  ? 84   TRP C C   1 
ATOM   602   O O   . TRP A  1 80  ? 46.745  -1.874  16.196  1.00 29.59  ? 84   TRP C O   1 
ATOM   603   C CB  . TRP A  1 80  ? 44.992  0.528   17.877  1.00 27.71  ? 84   TRP C CB  1 
ATOM   604   C CG  . TRP A  1 80  ? 44.090  0.358   16.687  1.00 34.26  ? 84   TRP C CG  1 
ATOM   605   C CD1 . TRP A  1 80  ? 43.395  -0.774  16.315  1.00 32.09  ? 84   TRP C CD1 1 
ATOM   606   C CD2 . TRP A  1 80  ? 43.792  1.354   15.696  1.00 30.11  ? 84   TRP C CD2 1 
ATOM   607   N NE1 . TRP A  1 80  ? 42.686  -0.534  15.148  1.00 30.38  ? 84   TRP C NE1 1 
ATOM   608   C CE2 . TRP A  1 80  ? 42.911  0.762   14.752  1.00 31.35  ? 84   TRP C CE2 1 
ATOM   609   C CE3 . TRP A  1 80  ? 44.178  2.681   15.520  1.00 26.58  ? 84   TRP C CE3 1 
ATOM   610   C CZ2 . TRP A  1 80  ? 42.416  1.465   13.653  1.00 29.73  ? 84   TRP C CZ2 1 
ATOM   611   C CZ3 . TRP A  1 80  ? 43.686  3.381   14.412  1.00 32.68  ? 84   TRP C CZ3 1 
ATOM   612   C CH2 . TRP A  1 80  ? 42.816  2.775   13.500  1.00 30.70  ? 84   TRP C CH2 1 
ATOM   613   N N   . SER A  1 81  ? 45.966  -2.243  18.272  1.00 29.24  ? 85   SER C N   1 
ATOM   614   C CA  . SER A  1 81  ? 45.883  -3.678  18.129  1.00 28.85  ? 85   SER C CA  1 
ATOM   615   C C   . SER A  1 81  ? 44.440  -4.165  17.976  1.00 28.74  ? 85   SER C C   1 
ATOM   616   O O   . SER A  1 81  ? 44.187  -5.133  17.270  1.00 31.10  ? 85   SER C O   1 
ATOM   617   C CB  . SER A  1 81  ? 46.551  -4.317  19.343  1.00 24.34  ? 85   SER C CB  1 
ATOM   618   O OG  . SER A  1 81  ? 45.995  -3.727  20.503  1.00 27.36  ? 85   SER C OG  1 
ATOM   619   N N   . TYR A  1 82  ? 43.524  -3.494  18.677  1.00 27.83  ? 86   TYR C N   1 
ATOM   620   C CA  . TYR A  1 82  ? 42.079  -3.696  18.597  1.00 27.07  ? 86   TYR C CA  1 
ATOM   621   C C   . TYR A  1 82  ? 41.385  -2.419  19.146  1.00 30.53  ? 86   TYR C C   1 
ATOM   622   O O   . TYR A  1 82  ? 42.061  -1.529  19.649  1.00 29.77  ? 86   TYR C O   1 
ATOM   623   C CB  . TYR A  1 82  ? 41.624  -4.956  19.366  1.00 22.91  ? 86   TYR C CB  1 
ATOM   624   C CG  . TYR A  1 82  ? 41.874  -4.969  20.880  1.00 31.67  ? 86   TYR C CG  1 
ATOM   625   C CD1 . TYR A  1 82  ? 43.068  -5.455  21.414  1.00 26.12  ? 86   TYR C CD1 1 
ATOM   626   C CD2 . TYR A  1 82  ? 40.916  -4.457  21.772  1.00 28.30  ? 86   TYR C CD2 1 
ATOM   627   C CE1 . TYR A  1 82  ? 43.283  -5.458  22.767  1.00 27.12  ? 86   TYR C CE1 1 
ATOM   628   C CE2 . TYR A  1 82  ? 41.129  -4.451  23.126  1.00 25.64  ? 86   TYR C CE2 1 
ATOM   629   C CZ  . TYR A  1 82  ? 42.315  -4.953  23.627  1.00 31.01  ? 86   TYR C CZ  1 
ATOM   630   O OH  . TYR A  1 82  ? 42.547  -4.939  24.994  1.00 28.44  ? 86   TYR C OH  1 
ATOM   631   N N   . ILE A  1 83  ? 40.059  -2.319  19.046  1.00 32.00  ? 87   ILE C N   1 
ATOM   632   C CA  . ILE A  1 83  ? 39.337  -1.103  19.453  1.00 29.78  ? 87   ILE C CA  1 
ATOM   633   C C   . ILE A  1 83  ? 38.273  -1.387  20.535  1.00 31.15  ? 87   ILE C C   1 
ATOM   634   O O   . ILE A  1 83  ? 37.632  -2.427  20.484  1.00 32.31  ? 87   ILE C O   1 
ATOM   635   C CB  . ILE A  1 83  ? 38.653  -0.436  18.223  1.00 30.86  ? 87   ILE C CB  1 
ATOM   636   C CG1 . ILE A  1 83  ? 39.671  -0.141  17.110  1.00 28.65  ? 87   ILE C CG1 1 
ATOM   637   C CG2 . ILE A  1 83  ? 37.876  0.814   18.653  1.00 24.31  ? 87   ILE C CG2 1 
ATOM   638   C CD1 . ILE A  1 83  ? 39.058  0.489   15.834  1.00 24.22  ? 87   ILE C CD1 1 
ATOM   639   N N   . VAL A  1 84  ? 38.106  -0.512  21.532  1.00 30.76  ? 88   VAL C N   1 
ATOM   640   C CA  . VAL A  1 84  ? 37.085  -0.722  22.576  1.00 29.15  ? 88   VAL C CA  1 
ATOM   641   C C   . VAL A  1 84  ? 36.064  0.423   22.568  1.00 29.11  ? 88   VAL C C   1 
ATOM   642   O O   . VAL A  1 84  ? 36.444  1.583   22.477  1.00 31.58  ? 88   VAL C O   1 
ATOM   643   C CB  . VAL A  1 84  ? 37.732  -0.872  23.993  1.00 35.30  ? 88   VAL C CB  1 
ATOM   644   C CG1 . VAL A  1 84  ? 36.684  -0.976  25.091  1.00 29.89  ? 88   VAL C CG1 1 
ATOM   645   C CG2 . VAL A  1 84  ? 38.659  -2.079  24.055  1.00 30.07  ? 88   VAL C CG2 1 
ATOM   646   N N   . GLU A  1 85  ? 34.774  0.086   22.598  1.00 28.70  ? 89   GLU C N   1 
ATOM   647   C CA  . GLU A  1 85  ? 33.686  1.068   22.503  1.00 29.29  ? 89   GLU C CA  1 
ATOM   648   C C   . GLU A  1 85  ? 32.612  0.708   23.535  1.00 30.45  ? 89   GLU C C   1 
ATOM   649   O O   . GLU A  1 85  ? 32.353  -0.467  23.752  1.00 37.32  ? 89   GLU C O   1 
ATOM   650   C CB  . GLU A  1 85  ? 33.088  1.096   21.077  1.00 23.80  ? 89   GLU C CB  1 
ATOM   651   C CG  . GLU A  1 85  ? 32.071  2.225   20.818  1.00 26.49  ? 89   GLU C CG  1 
ATOM   652   C CD  . GLU A  1 85  ? 31.298  2.122   19.476  1.00 35.85  ? 89   GLU C CD  1 
ATOM   653   O OE1 . GLU A  1 85  ? 30.712  1.051   19.217  1.00 37.97  ? 89   GLU C OE1 1 
ATOM   654   O OE2 . GLU A  1 85  ? 31.272  3.113   18.683  1.00 31.33  ? 89   GLU C OE2 1 
ATOM   655   N N   . LYS A  1 86  ? 31.979  1.690   24.166  1.00 30.74  ? 90   LYS C N   1 
ATOM   656   C CA  . LYS A  1 86  ? 30.929  1.404   25.158  1.00 38.69  ? 90   LYS C CA  1 
ATOM   657   C C   . LYS A  1 86  ? 29.632  1.026   24.466  1.00 38.62  ? 90   LYS C C   1 
ATOM   658   O O   . LYS A  1 86  ? 29.506  1.208   23.269  1.00 38.67  ? 90   LYS C O   1 
ATOM   659   C CB  . LYS A  1 86  ? 30.699  2.596   26.110  1.00 34.38  ? 90   LYS C CB  1 
ATOM   660   C CG  . LYS A  1 86  ? 31.682  2.667   27.267  1.00 36.65  ? 90   LYS C CG  1 
ATOM   661   C CD  . LYS A  1 86  ? 31.490  3.940   28.103  1.00 43.31  ? 90   LYS C CD  1 
ATOM   662   C CE  . LYS A  1 86  ? 32.311  3.926   29.397  1.00 46.08  ? 90   LYS C CE  1 
ATOM   663   N NZ  . LYS A  1 86  ? 33.802  3.812   29.242  1.00 42.91  ? 90   LYS C NZ  1 
ATOM   664   N N   . ILE A  1 87  ? 28.675  0.503   25.230  1.00 45.48  ? 91   ILE C N   1 
ATOM   665   C CA  . ILE A  1 87  ? 27.411  0.031   24.675  1.00 46.41  ? 91   ILE C CA  1 
ATOM   666   C C   . ILE A  1 87  ? 26.625  1.180   24.070  1.00 49.03  ? 91   ILE C C   1 
ATOM   667   O O   . ILE A  1 87  ? 26.130  1.074   22.943  1.00 52.54  ? 91   ILE C O   1 
ATOM   668   C CB  . ILE A  1 87  ? 26.516  -0.630  25.746  1.00 44.23  ? 91   ILE C CB  1 
ATOM   669   C CG1 . ILE A  1 87  ? 27.248  -1.765  26.458  1.00 47.39  ? 91   ILE C CG1 1 
ATOM   670   C CG2 . ILE A  1 87  ? 25.209  -1.090  25.120  1.00 44.91  ? 91   ILE C CG2 1 
ATOM   671   C CD1 . ILE A  1 87  ? 27.612  -2.940  25.565  1.00 51.26  ? 91   ILE C CD1 1 
ATOM   672   N N   . ASN A  1 88  ? 26.532  2.273   24.828  1.00 46.75  ? 92   ASN C N   1 
ATOM   673   C CA  . ASN A  1 88  ? 25.798  3.475   24.431  1.00 46.50  ? 92   ASN C CA  1 
ATOM   674   C C   . ASN A  1 88  ? 26.618  4.733   24.626  1.00 44.93  ? 92   ASN C C   1 
ATOM   675   O O   . ASN A  1 88  ? 26.334  5.500   25.542  1.00 46.91  ? 92   ASN C O   1 
ATOM   676   C CB  . ASN A  1 88  ? 24.505  3.617   25.235  1.00 52.82  ? 92   ASN C CB  1 
ATOM   677   C CG  . ASN A  1 88  ? 23.446  2.637   24.808  1.00 60.60  ? 92   ASN C CG  1 
ATOM   678   O OD1 . ASN A  1 88  ? 23.333  2.313   23.626  1.00 67.02  ? 92   ASN C OD1 1 
ATOM   679   N ND2 . ASN A  1 88  ? 22.655  2.156   25.763  1.00 60.89  ? 92   ASN C ND2 1 
ATOM   680   N N   . PRO A  1 89  ? 27.626  4.958   23.765  1.00 43.24  ? 93   PRO C N   1 
ATOM   681   C CA  . PRO A  1 89  ? 28.534  6.090   23.972  1.00 39.95  ? 93   PRO C CA  1 
ATOM   682   C C   . PRO A  1 89  ? 27.762  7.384   24.047  1.00 42.40  ? 93   PRO C C   1 
ATOM   683   O O   . PRO A  1 89  ? 26.711  7.510   23.406  1.00 41.87  ? 93   PRO C O   1 
ATOM   684   C CB  . PRO A  1 89  ? 29.443  6.041   22.737  1.00 37.19  ? 93   PRO C CB  1 
ATOM   685   C CG  . PRO A  1 89  ? 29.384  4.623   22.300  1.00 31.59  ? 93   PRO C CG  1 
ATOM   686   C CD  . PRO A  1 89  ? 27.982  4.191   22.562  1.00 35.19  ? 93   PRO C CD  1 
ATOM   687   N N   . ALA A  1 90  ? 28.276  8.328   24.826  1.00 41.55  ? 94   ALA C N   1 
ATOM   688   C CA  . ALA A  1 90  ? 27.556  9.564   25.076  1.00 41.34  ? 94   ALA C CA  1 
ATOM   689   C C   . ALA A  1 90  ? 27.866  10.596  24.014  1.00 38.32  ? 94   ALA C C   1 
ATOM   690   O O   . ALA A  1 90  ? 27.013  11.393  23.645  1.00 41.97  ? 94   ALA C O   1 
ATOM   691   C CB  . ALA A  1 90  ? 27.900  10.104  26.450  1.00 33.50  ? 94   ALA C CB  1 
ATOM   692   N N   . ASN A  1 91  ? 29.103  10.580  23.539  1.00 39.99  ? 95   ASN C N   1 
ATOM   693   C CA  . ASN A  1 91  ? 29.566  11.513  22.524  1.00 39.61  ? 95   ASN C CA  1 
ATOM   694   C C   . ASN A  1 91  ? 29.567  10.839  21.146  1.00 37.56  ? 95   ASN C C   1 
ATOM   695   O O   . ASN A  1 91  ? 30.539  10.163  20.777  1.00 33.23  ? 95   ASN C O   1 
ATOM   696   C CB  . ASN A  1 91  ? 30.960  12.036  22.895  1.00 39.25  ? 95   ASN C CB  1 
ATOM   697   C CG  . ASN A  1 91  ? 30.958  12.818  24.211  1.00 43.51  ? 95   ASN C CG  1 
ATOM   698   O OD1 . ASN A  1 91  ? 30.053  13.617  24.452  1.00 47.11  ? 95   ASN C OD1 1 
ATOM   699   N ND2 . ASN A  1 91  ? 31.967  12.597  25.054  1.00 36.86  ? 95   ASN C ND2 1 
ATOM   700   N N   . ASP A  1 92  ? 28.451  11.034  20.427  1.00 30.82  ? 96   ASP C N   1 
ATOM   701   C CA  . ASP A  1 92  ? 28.143  10.403  19.135  1.00 32.08  ? 96   ASP C CA  1 
ATOM   702   C C   . ASP A  1 92  ? 27.932  11.527  18.076  1.00 34.07  ? 96   ASP C C   1 
ATOM   703   O O   . ASP A  1 92  ? 28.827  12.380  17.868  1.00 31.67  ? 96   ASP C O   1 
ATOM   704   C CB  . ASP A  1 92  ? 26.900  9.476   19.294  1.00 28.74  ? 96   ASP C CB  1 
ATOM   705   C CG  . ASP A  1 92  ? 26.591  8.592   18.036  1.00 37.71  ? 96   ASP C CG  1 
ATOM   706   O OD1 . ASP A  1 92  ? 27.510  7.957   17.459  1.00 35.69  ? 96   ASP C OD1 1 
ATOM   707   O OD2 . ASP A  1 92  ? 25.397  8.512   17.640  1.00 32.74  ? 96   ASP C OD2 1 
ATOM   708   N N   . LEU A  1 93  A 26.770  11.550  17.419  1.00 30.20  ? 96   LEU C N   1 
ATOM   709   C CA  . LEU A  1 93  A 26.437  12.697  16.560  1.00 39.58  ? 96   LEU C CA  1 
ATOM   710   C C   . LEU A  1 93  A 25.857  13.828  17.440  1.00 41.76  ? 96   LEU C C   1 
ATOM   711   O O   . LEU A  1 93  A 24.695  13.766  17.864  1.00 41.64  ? 96   LEU C O   1 
ATOM   712   C CB  . LEU A  1 93  A 25.450  12.301  15.435  1.00 31.63  ? 96   LEU C CB  1 
ATOM   713   C CG  . LEU A  1 93  A 25.810  11.173  14.439  1.00 31.85  ? 96   LEU C CG  1 
ATOM   714   C CD1 . LEU A  1 93  A 24.613  10.801  13.559  1.00 32.28  ? 96   LEU C CD1 1 
ATOM   715   C CD2 . LEU A  1 93  A 27.028  11.487  13.552  1.00 26.40  ? 96   LEU C CD2 1 
ATOM   716   N N   . CYS A  1 94  ? 26.651  14.868  17.684  1.00 40.84  ? 97   CYS C N   1 
ATOM   717   C CA  . CYS A  1 94  ? 26.245  15.931  18.610  1.00 46.05  ? 97   CYS C CA  1 
ATOM   718   C C   . CYS A  1 94  ? 25.082  16.761  18.024  1.00 45.52  ? 97   CYS C C   1 
ATOM   719   O O   . CYS A  1 94  ? 24.148  17.100  18.758  1.00 42.47  ? 97   CYS C O   1 
ATOM   720   C CB  . CYS A  1 94  ? 27.465  16.808  19.002  1.00 42.53  ? 97   CYS C CB  1 
ATOM   721   S SG  . CYS A  1 94  ? 28.585  17.395  17.635  1.00 44.20  ? 97   CYS C SG  1 
ATOM   722   N N   . TYR A  1 95  ? 25.137  17.064  16.718  1.00 43.81  ? 98   TYR C N   1 
ATOM   723   C CA  . TYR A  1 95  ? 23.980  17.581  15.962  1.00 41.76  ? 98   TYR C CA  1 
ATOM   724   C C   . TYR A  1 95  ? 23.134  16.388  15.465  1.00 37.01  ? 98   TYR C C   1 
ATOM   725   O O   . TYR A  1 95  ? 23.679  15.460  14.886  1.00 40.29  ? 98   TYR C O   1 
ATOM   726   C CB  . TYR A  1 95  ? 24.439  18.442  14.780  1.00 38.71  ? 98   TYR C CB  1 
ATOM   727   C CG  . TYR A  1 95  ? 23.390  19.405  14.245  1.00 39.59  ? 98   TYR C CG  1 
ATOM   728   C CD1 . TYR A  1 95  ? 22.240  18.932  13.610  1.00 41.27  ? 98   TYR C CD1 1 
ATOM   729   C CD2 . TYR A  1 95  ? 23.566  20.790  14.340  1.00 37.79  ? 98   TYR C CD2 1 
ATOM   730   C CE1 . TYR A  1 95  ? 21.281  19.794  13.108  1.00 40.90  ? 98   TYR C CE1 1 
ATOM   731   C CE2 . TYR A  1 95  ? 22.610  21.670  13.836  1.00 44.36  ? 98   TYR C CE2 1 
ATOM   732   C CZ  . TYR A  1 95  ? 21.465  21.158  13.224  1.00 46.08  ? 98   TYR C CZ  1 
ATOM   733   O OH  . TYR A  1 95  ? 20.500  21.993  12.708  1.00 44.93  ? 98   TYR C OH  1 
ATOM   734   N N   . PRO A  1 96  ? 21.815  16.388  15.728  1.00 39.41  ? 99   PRO C N   1 
ATOM   735   C CA  . PRO A  1 96  ? 20.953  15.229  15.404  1.00 38.19  ? 99   PRO C CA  1 
ATOM   736   C C   . PRO A  1 96  ? 20.894  14.911  13.895  1.00 40.67  ? 99   PRO C C   1 
ATOM   737   O O   . PRO A  1 96  ? 21.070  15.808  13.048  1.00 36.56  ? 99   PRO C O   1 
ATOM   738   C CB  . PRO A  1 96  ? 19.566  15.644  15.930  1.00 36.94  ? 99   PRO C CB  1 
ATOM   739   C CG  . PRO A  1 96  ? 19.621  17.139  16.018  1.00 42.34  ? 99   PRO C CG  1 
ATOM   740   C CD  . PRO A  1 96  ? 21.051  17.489  16.347  1.00 41.50  ? 99   PRO C CD  1 
ATOM   741   N N   . GLY A  1 97  ? 20.720  13.625  13.582  1.00 37.34  ? 100  GLY C N   1 
ATOM   742   C CA  . GLY A  1 97  ? 20.654  13.142  12.214  1.00 36.60  ? 100  GLY C CA  1 
ATOM   743   C C   . GLY A  1 97  ? 21.024  11.673  12.103  1.00 36.76  ? 100  GLY C C   1 
ATOM   744   O O   . GLY A  1 97  ? 20.787  10.909  13.029  1.00 37.91  ? 100  GLY C O   1 
ATOM   745   N N   . ASN A  1 98  ? 21.627  11.276  10.987  1.00 35.03  ? 101  ASN C N   1 
ATOM   746   C CA  . ASN A  1 98  ? 21.988  9.870   10.770  1.00 35.74  ? 101  ASN C CA  1 
ATOM   747   C C   . ASN A  1 98  ? 23.268  9.729   9.945   1.00 42.09  ? 101  ASN C C   1 
ATOM   748   O O   . ASN A  1 98  ? 23.703  10.682  9.249   1.00 37.38  ? 101  ASN C O   1 
ATOM   749   C CB  . ASN A  1 98  ? 20.855  9.094   10.080  1.00 32.88  ? 101  ASN C CB  1 
ATOM   750   C CG  . ASN A  1 98  ? 20.581  9.599   8.661   1.00 45.73  ? 101  ASN C CG  1 
ATOM   751   O OD1 . ASN A  1 98  ? 20.068  10.718  8.455   1.00 46.09  ? 101  ASN C OD1 1 
ATOM   752   N ND2 . ASN A  1 98  ? 20.992  8.813   7.674   1.00 43.19  ? 101  ASN C ND2 1 
ATOM   753   N N   . PHE A  1 99  ? 23.854  8.531   10.027  1.00 36.27  ? 102  PHE C N   1 
ATOM   754   C CA  . PHE A  1 99  ? 25.135  8.225   9.400   1.00 32.64  ? 102  PHE C CA  1 
ATOM   755   C C   . PHE A  1 99  ? 24.931  7.122   8.379   1.00 30.23  ? 102  PHE C C   1 
ATOM   756   O O   . PHE A  1 99  ? 24.904  5.943   8.738   1.00 30.07  ? 102  PHE C O   1 
ATOM   757   C CB  . PHE A  1 99  ? 26.133  7.763   10.472  1.00 32.65  ? 102  PHE C CB  1 
ATOM   758   C CG  . PHE A  1 99  ? 27.569  7.927   10.093  1.00 29.98  ? 102  PHE C CG  1 
ATOM   759   C CD1 . PHE A  1 99  ? 28.126  7.192   9.072   1.00 37.05  ? 102  PHE C CD1 1 
ATOM   760   C CD2 . PHE A  1 99  ? 28.379  8.800   10.801  1.00 29.68  ? 102  PHE C CD2 1 
ATOM   761   C CE1 . PHE A  1 99  ? 29.484  7.371   8.730   1.00 43.00  ? 102  PHE C CE1 1 
ATOM   762   C CE2 . PHE A  1 99  ? 29.716  8.974   10.478  1.00 30.34  ? 102  PHE C CE2 1 
ATOM   763   C CZ  . PHE A  1 99  ? 30.273  8.259   9.444   1.00 28.65  ? 102  PHE C CZ  1 
ATOM   764   N N   . ASN A  1 100 ? 24.894  7.477   7.107   1.00 30.37  ? 103  ASN C N   1 
ATOM   765   C CA  . ASN A  1 100 ? 24.580  6.510   6.065   1.00 25.20  ? 103  ASN C CA  1 
ATOM   766   C C   . ASN A  1 100 ? 25.555  5.320   5.983   1.00 25.72  ? 103  ASN C C   1 
ATOM   767   O O   . ASN A  1 100 ? 26.778  5.481   6.026   1.00 30.01  ? 103  ASN C O   1 
ATOM   768   C CB  . ASN A  1 100 ? 24.522  7.252   4.736   1.00 28.66  ? 103  ASN C CB  1 
ATOM   769   C CG  . ASN A  1 100 ? 23.527  6.646   3.786   1.00 31.47  ? 103  ASN C CG  1 
ATOM   770   O OD1 . ASN A  1 100 ? 22.326  6.837   3.922   1.00 35.89  ? 103  ASN C OD1 1 
ATOM   771   N ND2 . ASN A  1 100 ? 24.024  5.899   2.812   1.00 31.20  ? 103  ASN C ND2 1 
ATOM   772   N N   . ASP A  1 101 ? 25.006  4.116   5.898   1.00 25.79  ? 104  ASP C N   1 
ATOM   773   C CA  . ASP A  1 101 ? 25.825  2.891   5.840   1.00 28.29  ? 104  ASP C CA  1 
ATOM   774   C C   . ASP A  1 101 ? 26.836  2.755   7.007   1.00 28.70  ? 104  ASP C C   1 
ATOM   775   O O   . ASP A  1 101 ? 27.983  2.304   6.801   1.00 27.11  ? 104  ASP C O   1 
ATOM   776   C CB  . ASP A  1 101 ? 26.581  2.820   4.502   1.00 25.27  ? 104  ASP C CB  1 
ATOM   777   C CG  . ASP A  1 101 ? 25.691  2.346   3.337   1.00 31.50  ? 104  ASP C CG  1 
ATOM   778   O OD1 . ASP A  1 101 ? 24.842  1.455   3.555   1.00 37.60  ? 104  ASP C OD1 1 
ATOM   779   O OD2 . ASP A  1 101 ? 25.836  2.875   2.207   1.00 27.16  ? 104  ASP C OD2 1 
ATOM   780   N N   . TYR A  1 102 ? 26.418  3.155   8.209   1.00 23.29  ? 105  TYR C N   1 
ATOM   781   C CA  . TYR A  1 102 ? 27.265  3.124   9.403   1.00 24.91  ? 105  TYR C CA  1 
ATOM   782   C C   . TYR A  1 102 ? 27.800  1.728   9.754   1.00 26.48  ? 105  TYR C C   1 
ATOM   783   O O   . TYR A  1 102 ? 28.951  1.563   10.176  1.00 24.07  ? 105  TYR C O   1 
ATOM   784   C CB  . TYR A  1 102 ? 26.493  3.675   10.610  1.00 25.56  ? 105  TYR C CB  1 
ATOM   785   C CG  . TYR A  1 102 ? 27.341  3.943   11.836  1.00 26.73  ? 105  TYR C CG  1 
ATOM   786   C CD1 . TYR A  1 102 ? 28.545  4.635   11.731  1.00 28.53  ? 105  TYR C CD1 1 
ATOM   787   C CD2 . TYR A  1 102 ? 26.909  3.560   13.109  1.00 32.97  ? 105  TYR C CD2 1 
ATOM   788   C CE1 . TYR A  1 102 ? 29.325  4.905   12.849  1.00 27.82  ? 105  TYR C CE1 1 
ATOM   789   C CE2 . TYR A  1 102 ? 27.667  3.836   14.247  1.00 28.37  ? 105  TYR C CE2 1 
ATOM   790   C CZ  . TYR A  1 102 ? 28.884  4.509   14.117  1.00 32.88  ? 105  TYR C CZ  1 
ATOM   791   O OH  . TYR A  1 102 ? 29.660  4.790   15.249  1.00 29.04  ? 105  TYR C OH  1 
ATOM   792   N N   . GLU A  1 103 ? 26.954  0.715   9.626   1.00 25.85  ? 106  GLU C N   1 
ATOM   793   C CA  . GLU A  1 103 ? 27.368  -0.611  10.045  1.00 23.02  ? 106  GLU C CA  1 
ATOM   794   C C   . GLU A  1 103 ? 28.437  -1.157  9.068   1.00 24.65  ? 106  GLU C C   1 
ATOM   795   O O   . GLU A  1 103 ? 29.387  -1.798  9.516   1.00 23.15  ? 106  GLU C O   1 
ATOM   796   C CB  . GLU A  1 103 ? 26.138  -1.537  10.146  1.00 23.54  ? 106  GLU C CB  1 
ATOM   797   C CG  . GLU A  1 103 ? 25.228  -1.301  11.382  1.00 25.62  ? 106  GLU C CG  1 
ATOM   798   C CD  . GLU A  1 103 ? 24.361  -0.008  11.334  1.00 27.12  ? 106  GLU C CD  1 
ATOM   799   O OE1 . GLU A  1 103 ? 23.994  0.475   10.239  1.00 25.86  ? 106  GLU C OE1 1 
ATOM   800   O OE2 . GLU A  1 103 ? 24.033  0.529   12.421  1.00 26.81  ? 106  GLU C OE2 1 
ATOM   801   N N   . GLU A  1 104 ? 28.342  -0.847  7.764   1.00 22.08  ? 107  GLU C N   1 
ATOM   802   C CA  . GLU A  1 104 ? 29.388  -1.263  6.811   1.00 22.36  ? 107  GLU C CA  1 
ATOM   803   C C   . GLU A  1 104 ? 30.760  -0.514  7.057   1.00 23.49  ? 107  GLU C C   1 
ATOM   804   O O   . GLU A  1 104 ? 31.848  -1.111  6.979   1.00 19.89  ? 107  GLU C O   1 
ATOM   805   C CB  . GLU A  1 104 ? 28.888  -1.052  5.367   1.00 23.04  ? 107  GLU C CB  1 
ATOM   806   C CG  . GLU A  1 104 ? 27.850  -2.096  4.844   1.00 21.18  ? 107  GLU C CG  1 
ATOM   807   C CD  . GLU A  1 104 ? 28.410  -3.514  4.572   1.00 25.53  ? 107  GLU C CD  1 
ATOM   808   O OE1 . GLU A  1 104 ? 29.425  -3.631  3.847   1.00 25.87  ? 107  GLU C OE1 1 
ATOM   809   O OE2 . GLU A  1 104 ? 27.841  -4.516  5.097   1.00 24.40  ? 107  GLU C OE2 1 
ATOM   810   N N   . LEU A  1 105 ? 30.714  0.765   7.435   1.00 25.16  ? 108  LEU C N   1 
ATOM   811   C CA  . LEU A  1 105 ? 31.953  1.464   7.803   1.00 22.61  ? 108  LEU C CA  1 
ATOM   812   C C   . LEU A  1 105 ? 32.602  0.791   9.022   1.00 27.40  ? 108  LEU C C   1 
ATOM   813   O O   . LEU A  1 105 ? 33.838  0.663   9.120   1.00 26.44  ? 108  LEU C O   1 
ATOM   814   C CB  . LEU A  1 105 ? 31.677  2.919   8.146   1.00 20.91  ? 108  LEU C CB  1 
ATOM   815   C CG  . LEU A  1 105 ? 32.854  3.749   8.684   1.00 26.05  ? 108  LEU C CG  1 
ATOM   816   C CD1 . LEU A  1 105 ? 33.911  3.931   7.590   1.00 24.70  ? 108  LEU C CD1 1 
ATOM   817   C CD2 . LEU A  1 105 ? 32.404  5.120   9.236   1.00 22.88  ? 108  LEU C CD2 1 
ATOM   818   N N   . LYS A  1 106 ? 31.770  0.367   9.968   1.00 25.76  ? 109  LYS C N   1 
ATOM   819   C CA  . LYS A  1 106 ? 32.309  -0.246  11.172  1.00 26.08  ? 109  LYS C CA  1 
ATOM   820   C C   . LYS A  1 106 ? 33.027  -1.564  10.881  1.00 26.02  ? 109  LYS C C   1 
ATOM   821   O O   . LYS A  1 106 ? 34.071  -1.862  11.450  1.00 27.61  ? 109  LYS C O   1 
ATOM   822   C CB  . LYS A  1 106 ? 31.194  -0.471  12.183  1.00 24.91  ? 109  LYS C CB  1 
ATOM   823   C CG  . LYS A  1 106 ? 30.883  0.738   13.044  1.00 25.14  ? 109  LYS C CG  1 
ATOM   824   C CD  . LYS A  1 106 ? 29.619  0.460   13.848  1.00 28.47  ? 109  LYS C CD  1 
ATOM   825   C CE  . LYS A  1 106 ? 29.618  1.219   15.158  1.00 28.97  ? 109  LYS C CE  1 
ATOM   826   N NZ  . LYS A  1 106 ? 30.497  0.588   16.168  1.00 34.44  ? 109  LYS C NZ  1 
ATOM   827   N N   . HIS A  1 107 ? 32.489  -2.322  9.936   1.00 28.77  ? 110  HIS C N   1 
ATOM   828   C CA  . HIS A  1 107 ? 33.047  -3.607  9.570   1.00 23.15  ? 110  HIS C CA  1 
ATOM   829   C C   . HIS A  1 107 ? 34.382  -3.371  8.880   1.00 26.32  ? 110  HIS C C   1 
ATOM   830   O O   . HIS A  1 107 ? 35.357  -4.096  9.115   1.00 26.42  ? 110  HIS C O   1 
ATOM   831   C CB  . HIS A  1 107 ? 32.067  -4.364  8.655   1.00 23.39  ? 110  HIS C CB  1 
ATOM   832   C CG  . HIS A  1 107 ? 32.576  -5.687  8.182   1.00 29.33  ? 110  HIS C CG  1 
ATOM   833   N ND1 . HIS A  1 107 ? 32.335  -6.861  8.869   1.00 28.84  ? 110  HIS C ND1 1 
ATOM   834   C CD2 . HIS A  1 107 ? 33.321  -6.027  7.098   1.00 28.17  ? 110  HIS C CD2 1 
ATOM   835   C CE1 . HIS A  1 107 ? 32.899  -7.866  8.220   1.00 29.64  ? 110  HIS C CE1 1 
ATOM   836   N NE2 . HIS A  1 107 ? 33.513  -7.387  7.150   1.00 29.93  ? 110  HIS C NE2 1 
ATOM   837   N N   . LEU A  1 108 ? 34.428  -2.350  8.024   1.00 28.01  ? 111  LEU C N   1 
ATOM   838   C CA  . LEU A  1 108 ? 35.693  -1.997  7.367   1.00 28.85  ? 111  LEU C CA  1 
ATOM   839   C C   . LEU A  1 108 ? 36.759  -1.629  8.381   1.00 26.66  ? 111  LEU C C   1 
ATOM   840   O O   . LEU A  1 108 ? 37.904  -2.061  8.269   1.00 22.95  ? 111  LEU C O   1 
ATOM   841   C CB  . LEU A  1 108 ? 35.493  -0.845  6.393   1.00 21.76  ? 111  LEU C CB  1 
ATOM   842   C CG  . LEU A  1 108 ? 36.652  -0.474  5.487   1.00 24.89  ? 111  LEU C CG  1 
ATOM   843   C CD1 . LEU A  1 108 ? 37.132  -1.634  4.616   1.00 30.17  ? 111  LEU C CD1 1 
ATOM   844   C CD2 . LEU A  1 108 ? 36.238  0.755   4.651   1.00 28.85  ? 111  LEU C CD2 1 
ATOM   845   N N   . LEU A  1 109 ? 36.338  -0.909  9.417   1.00 28.40  ? 112  LEU C N   1 
ATOM   846   C CA  . LEU A  1 109 ? 37.259  -0.406  10.430  1.00 30.85  ? 112  LEU C CA  1 
ATOM   847   C C   . LEU A  1 109 ? 37.923  -1.512  11.225  1.00 28.16  ? 112  LEU C C   1 
ATOM   848   O O   . LEU A  1 109 ? 39.045  -1.361  11.688  1.00 26.70  ? 112  LEU C O   1 
ATOM   849   C CB  . LEU A  1 109 ? 36.506  0.515   11.384  1.00 31.72  ? 112  LEU C CB  1 
ATOM   850   C CG  . LEU A  1 109 ? 37.287  1.457   12.298  1.00 34.12  ? 112  LEU C CG  1 
ATOM   851   C CD1 . LEU A  1 109 ? 38.396  2.226   11.567  1.00 31.00  ? 112  LEU C CD1 1 
ATOM   852   C CD2 . LEU A  1 109 ? 36.290  2.430   12.925  1.00 30.81  ? 112  LEU C CD2 1 
ATOM   853   N N   . SER A  1 110 ? 37.278  -2.662  11.285  1.00 25.93  ? 113  SER C N   1 
ATOM   854   C CA  . SER A  1 110 ? 37.810  -3.757  12.057  1.00 29.16  ? 113  SER C CA  1 
ATOM   855   C C   . SER A  1 110 ? 38.782  -4.631  11.229  1.00 36.98  ? 113  SER C C   1 
ATOM   856   O O   . SER A  1 110 ? 39.213  -5.700  11.683  1.00 38.11  ? 113  SER C O   1 
ATOM   857   C CB  . SER A  1 110 ? 36.654  -4.582  12.592  1.00 32.03  ? 113  SER C CB  1 
ATOM   858   O OG  . SER A  1 110 ? 36.162  -5.391  11.548  1.00 40.61  ? 113  SER C OG  1 
ATOM   859   N N   . ARG A  1 111 ? 39.183  -4.118  10.059  1.00 36.15  ? 114  ARG C N   1 
ATOM   860   C CA  . ARG A  1 111 ? 40.209  -4.728  9.201   1.00 33.94  ? 114  ARG C CA  1 
ATOM   861   C C   . ARG A  1 111 ? 41.425  -3.796  9.070   1.00 37.30  ? 114  ARG C C   1 
ATOM   862   O O   . ARG A  1 111 ? 42.323  -4.026  8.265   1.00 40.37  ? 114  ARG C O   1 
ATOM   863   C CB  . ARG A  1 111 ? 39.664  -4.984  7.786   1.00 38.02  ? 114  ARG C CB  1 
ATOM   864   C CG  . ARG A  1 111 ? 38.393  -5.830  7.608   1.00 37.90  ? 114  ARG C CG  1 
ATOM   865   C CD  . ARG A  1 111 ? 38.650  -7.285  7.878   1.00 41.25  ? 114  ARG C CD  1 
ATOM   866   N NE  . ARG A  1 111 ? 37.462  -8.131  7.723   1.00 55.29  ? 114  ARG C NE  1 
ATOM   867   C CZ  . ARG A  1 111 ? 37.116  -8.761  6.587   1.00 63.84  ? 114  ARG C CZ  1 
ATOM   868   N NH1 . ARG A  1 111 ? 37.854  -8.634  5.473   1.00 55.15  ? 114  ARG C NH1 1 
ATOM   869   N NH2 . ARG A  1 111 ? 36.020  -9.527  6.557   1.00 52.78  ? 114  ARG C NH2 1 
ATOM   870   N N   . ILE A  1 112 ? 41.461  -2.768  9.903   1.00 32.94  ? 115  ILE C N   1 
ATOM   871   C CA  . ILE A  1 112 ? 42.462  -1.712  9.845   1.00 34.59  ? 115  ILE C CA  1 
ATOM   872   C C   . ILE A  1 112 ? 43.197  -1.551  11.197  1.00 38.38  ? 115  ILE C C   1 
ATOM   873   O O   . ILE A  1 112 ? 42.554  -1.585  12.252  1.00 36.24  ? 115  ILE C O   1 
ATOM   874   C CB  . ILE A  1 112 ? 41.793  -0.386  9.461   1.00 29.48  ? 115  ILE C CB  1 
ATOM   875   C CG1 . ILE A  1 112 ? 41.354  -0.433  7.998   1.00 30.88  ? 115  ILE C CG1 1 
ATOM   876   C CG2 . ILE A  1 112 ? 42.715  0.765   9.697   1.00 30.70  ? 115  ILE C CG2 1 
ATOM   877   C CD1 . ILE A  1 112 ? 40.568  0.786   7.567   1.00 23.39  ? 115  ILE C CD1 1 
ATOM   878   N N   . ASN A  1 113 ? 44.525  -1.369  11.159  1.00 38.47  ? 116  ASN C N   1 
ATOM   879   C CA  . ASN A  1 113 ? 45.325  -1.155  12.366  1.00 33.15  ? 116  ASN C CA  1 
ATOM   880   C C   . ASN A  1 113 ? 45.880  0.256   12.437  1.00 34.69  ? 116  ASN C C   1 
ATOM   881   O O   . ASN A  1 113 ? 46.243  0.717   13.522  1.00 31.20  ? 116  ASN C O   1 
ATOM   882   C CB  . ASN A  1 113 ? 46.501  -2.139  12.458  1.00 37.08  ? 116  ASN C CB  1 
ATOM   883   C CG  . ASN A  1 113 ? 46.061  -3.558  12.659  1.00 35.10  ? 116  ASN C CG  1 
ATOM   884   O OD1 . ASN A  1 113 ? 46.334  -4.426  11.836  1.00 40.31  ? 116  ASN C OD1 1 
ATOM   885   N ND2 . ASN A  1 113 ? 45.370  -3.806  13.747  1.00 34.96  ? 116  ASN C ND2 1 
ATOM   886   N N   . HIS A  1 114 ? 45.940  0.971   11.314  1.00 31.85  ? 117  HIS C N   1 
ATOM   887   C CA  . HIS A  1 114 ? 46.538  2.297   11.421  1.00 38.35  ? 117  HIS C CA  1 
ATOM   888   C C   . HIS A  1 114 ? 46.109  3.352   10.370  1.00 38.94  ? 117  HIS C C   1 
ATOM   889   O O   . HIS A  1 114 ? 46.231  3.155   9.156   1.00 39.45  ? 117  HIS C O   1 
ATOM   890   C CB  . HIS A  1 114 ? 48.079  2.107   11.443  1.00 40.01  ? 117  HIS C CB  1 
ATOM   891   C CG  . HIS A  1 114 ? 48.843  3.322   11.876  1.00 38.23  ? 117  HIS C CG  1 
ATOM   892   N ND1 . HIS A  1 114 ? 50.149  3.561   11.480  1.00 37.00  ? 117  HIS C ND1 1 
ATOM   893   C CD2 . HIS A  1 114 ? 48.459  4.412   12.583  1.00 32.32  ? 117  HIS C CD2 1 
ATOM   894   C CE1 . HIS A  1 114 ? 50.549  4.720   11.970  1.00 31.48  ? 117  HIS C CE1 1 
ATOM   895   N NE2 . HIS A  1 114 ? 49.541  5.263   12.632  1.00 34.92  ? 117  HIS C NE2 1 
ATOM   896   N N   . PHE A  1 115 ? 45.646  4.496   10.887  1.00 35.76  ? 118  PHE C N   1 
ATOM   897   C CA  . PHE A  1 115 ? 45.283  5.664   10.088  1.00 33.59  ? 118  PHE C CA  1 
ATOM   898   C C   . PHE A  1 115 ? 46.387  6.713   10.201  1.00 40.21  ? 118  PHE C C   1 
ATOM   899   O O   . PHE A  1 115 ? 47.151  6.713   11.175  1.00 49.42  ? 118  PHE C O   1 
ATOM   900   C CB  . PHE A  1 115 ? 43.972  6.307   10.575  1.00 33.84  ? 118  PHE C CB  1 
ATOM   901   C CG  . PHE A  1 115 ? 42.699  5.621   10.101  1.00 35.86  ? 118  PHE C CG  1 
ATOM   902   C CD1 . PHE A  1 115 ? 42.579  5.141   8.812   1.00 31.67  ? 118  PHE C CD1 1 
ATOM   903   C CD2 . PHE A  1 115 ? 41.581  5.552   10.940  1.00 30.25  ? 118  PHE C CD2 1 
ATOM   904   C CE1 . PHE A  1 115 ? 41.402  4.538   8.384   1.00 29.52  ? 118  PHE C CE1 1 
ATOM   905   C CE2 . PHE A  1 115 ? 40.401  4.956   10.513  1.00 26.25  ? 118  PHE C CE2 1 
ATOM   906   C CZ  . PHE A  1 115 ? 40.315  4.456   9.229   1.00 27.39  ? 118  PHE C CZ  1 
ATOM   907   N N   . GLU A  1 116 ? 46.520  7.578   9.207   1.00 36.03  ? 119  GLU C N   1 
ATOM   908   C CA  . GLU A  1 116 ? 47.313  8.787   9.396   1.00 37.81  ? 119  GLU C CA  1 
ATOM   909   C C   . GLU A  1 116 ? 46.591  9.985   8.814   1.00 39.69  ? 119  GLU C C   1 
ATOM   910   O O   . GLU A  1 116 ? 46.540  10.153  7.579   1.00 37.55  ? 119  GLU C O   1 
ATOM   911   C CB  . GLU A  1 116 ? 48.693  8.650   8.780   1.00 43.82  ? 119  GLU C CB  1 
ATOM   912   C CG  . GLU A  1 116 ? 49.542  9.871   9.007   1.00 49.11  ? 119  GLU C CG  1 
ATOM   913   C CD  . GLU A  1 116 ? 50.913  9.656   8.465   1.00 66.43  ? 119  GLU C CD  1 
ATOM   914   O OE1 . GLU A  1 116 ? 51.513  8.648   8.915   1.00 73.23  ? 119  GLU C OE1 1 
ATOM   915   O OE2 . GLU A  1 116 ? 51.357  10.449  7.583   1.00 64.17  ? 119  GLU C OE2 1 
ATOM   916   N N   . LYS A  1 117 ? 46.074  10.834  9.700   1.00 31.66  ? 120  LYS C N   1 
ATOM   917   C CA  . LYS A  1 117 ? 45.203  11.916  9.279   1.00 34.78  ? 120  LYS C CA  1 
ATOM   918   C C   . LYS A  1 117 ? 45.970  13.031  8.530   1.00 42.03  ? 120  LYS C C   1 
ATOM   919   O O   . LYS A  1 117 ? 47.104  13.378  8.880   1.00 41.63  ? 120  LYS C O   1 
ATOM   920   C CB  . LYS A  1 117 ? 44.474  12.500  10.481  1.00 38.53  ? 120  LYS C CB  1 
ATOM   921   C CG  . LYS A  1 117 ? 43.122  13.135  10.140  1.00 37.78  ? 120  LYS C CG  1 
ATOM   922   C CD  . LYS A  1 117 ? 42.288  13.363  11.377  1.00 29.13  ? 120  LYS C CD  1 
ATOM   923   C CE  . LYS A  1 117 ? 42.612  14.717  11.976  1.00 36.11  ? 120  LYS C CE  1 
ATOM   924   N NZ  . LYS A  1 117 ? 41.959  14.960  13.303  1.00 45.05  ? 120  LYS C NZ  1 
ATOM   925   N N   . ILE A  1 118 ? 45.371  13.522  7.447   1.00 40.54  ? 121  ILE C N   1 
ATOM   926   C CA  . ILE A  1 118 ? 45.874  14.685  6.710   1.00 40.89  ? 121  ILE C CA  1 
ATOM   927   C C   . ILE A  1 118 ? 44.798  15.701  6.361   1.00 43.74  ? 121  ILE C C   1 
ATOM   928   O O   . ILE A  1 118 ? 43.604  15.399  6.331   1.00 46.99  ? 121  ILE C O   1 
ATOM   929   C CB  . ILE A  1 118 ? 46.562  14.274  5.403   1.00 38.57  ? 121  ILE C CB  1 
ATOM   930   C CG1 . ILE A  1 118 ? 45.556  13.568  4.498   1.00 34.03  ? 121  ILE C CG1 1 
ATOM   931   C CG2 . ILE A  1 118 ? 47.698  13.321  5.667   1.00 44.09  ? 121  ILE C CG2 1 
ATOM   932   C CD1 . ILE A  1 118 ? 46.107  13.264  3.145   1.00 36.21  ? 121  ILE C CD1 1 
ATOM   933   N N   . GLN A  1 119 ? 45.235  16.922  6.103   1.00 49.05  ? 122  GLN C N   1 
ATOM   934   C CA  . GLN A  1 119 ? 44.329  17.972  5.688   1.00 42.93  ? 122  GLN C CA  1 
ATOM   935   C C   . GLN A  1 119 ? 44.273  17.999  4.168   1.00 44.52  ? 122  GLN C C   1 
ATOM   936   O O   . GLN A  1 119 ? 45.314  18.043  3.513   1.00 36.79  ? 122  GLN C O   1 
ATOM   937   C CB  . GLN A  1 119 ? 44.791  19.289  6.252   1.00 39.04  ? 122  GLN C CB  1 
ATOM   938   C CG  . GLN A  1 119 ? 43.929  20.448  5.896   1.00 54.06  ? 122  GLN C CG  1 
ATOM   939   C CD  . GLN A  1 119 ? 44.431  21.699  6.559   1.00 57.82  ? 122  GLN C CD  1 
ATOM   940   O OE1 . GLN A  1 119 ? 45.187  22.464  5.964   1.00 56.77  ? 122  GLN C OE1 1 
ATOM   941   N NE2 . GLN A  1 119 ? 44.023  21.910  7.812   1.00 56.56  ? 122  GLN C NE2 1 
ATOM   942   N N   . ILE A  1 120 ? 43.061  17.973  3.613   1.00 46.81  ? 123  ILE C N   1 
ATOM   943   C CA  . ILE A  1 120 ? 42.898  17.920  2.163   1.00 49.04  ? 123  ILE C CA  1 
ATOM   944   C C   . ILE A  1 120 ? 42.372  19.246  1.604   1.00 54.65  ? 123  ILE C C   1 
ATOM   945   O O   . ILE A  1 120 ? 42.688  19.606  0.468   1.00 59.69  ? 123  ILE C O   1 
ATOM   946   C CB  . ILE A  1 120 ? 41.967  16.759  1.729   1.00 46.00  ? 123  ILE C CB  1 
ATOM   947   C CG1 . ILE A  1 120 ? 40.598  16.857  2.383   1.00 43.05  ? 123  ILE C CG1 1 
ATOM   948   C CG2 . ILE A  1 120 ? 42.617  15.400  2.021   1.00 42.28  ? 123  ILE C CG2 1 
ATOM   949   C CD1 . ILE A  1 120 ? 39.663  15.802  1.882   1.00 39.53  ? 123  ILE C CD1 1 
ATOM   950   N N   . THR A  1 121 ? 41.551  19.954  2.374   1.00 49.05  ? 124  THR C N   1 
ATOM   951   C CA  . THR A  1 121 ? 41.149  21.302  1.981   1.00 57.65  ? 124  THR C CA  1 
ATOM   952   C C   . THR A  1 121 ? 41.215  22.196  3.224   1.00 64.54  ? 124  THR C C   1 
ATOM   953   O O   . THR A  1 121 ? 40.361  22.100  4.112   1.00 65.02  ? 124  THR C O   1 
ATOM   954   C CB  . THR A  1 121 ? 39.716  21.321  1.316   1.00 60.82  ? 124  THR C CB  1 
ATOM   955   O OG1 . THR A  1 121 ? 38.943  22.437  1.780   1.00 59.55  ? 124  THR C OG1 1 
ATOM   956   C CG2 . THR A  1 121 ? 38.950  20.038  1.591   1.00 55.10  ? 124  THR C CG2 1 
ATOM   957   N N   . PRO A  1 122 ? 42.213  23.102  3.267   1.00 65.96  ? 125  PRO C N   1 
ATOM   958   C CA  . PRO A  1 122 ? 42.418  24.021  4.404   1.00 66.69  ? 125  PRO C CA  1 
ATOM   959   C C   . PRO A  1 122 ? 41.214  24.955  4.676   1.00 68.03  ? 125  PRO C C   1 
ATOM   960   O O   . PRO A  1 122 ? 40.573  25.407  3.730   1.00 69.18  ? 125  PRO C O   1 
ATOM   961   C CB  . PRO A  1 122 ? 43.665  24.834  3.984   1.00 65.71  ? 125  PRO C CB  1 
ATOM   962   C CG  . PRO A  1 122 ? 43.790  24.649  2.490   1.00 67.22  ? 125  PRO C CG  1 
ATOM   963   C CD  . PRO A  1 122 ? 43.234  23.271  2.211   1.00 64.50  ? 125  PRO C CD  1 
ATOM   964   N N   . LYS A  1 123 A 40.907  25.213  5.951   1.00 70.90  ? 125  LYS C N   1 
ATOM   965   C CA  . LYS A  1 123 A 39.778  26.070  6.353   1.00 69.58  ? 125  LYS C CA  1 
ATOM   966   C C   . LYS A  1 123 A 39.922  27.514  5.827   1.00 72.39  ? 125  LYS C C   1 
ATOM   967   O O   . LYS A  1 123 A 38.951  28.274  5.777   1.00 71.18  ? 125  LYS C O   1 
ATOM   968   C CB  . LYS A  1 123 A 39.630  26.096  7.883   1.00 67.80  ? 125  LYS C CB  1 
ATOM   969   C CG  . LYS A  1 123 A 38.285  26.677  8.387   1.00 69.15  ? 125  LYS C CG  1 
ATOM   970   C CD  . LYS A  1 123 A 38.144  26.620  9.917   1.00 66.91  ? 125  LYS C CD  1 
ATOM   971   C CE  . LYS A  1 123 A 38.078  25.192  10.448  1.00 67.49  ? 125  LYS C CE  1 
ATOM   972   N NZ  . LYS A  1 123 A 37.923  25.163  11.932  1.00 67.57  ? 125  LYS C NZ  1 
ATOM   973   N N   . ASN A  1 124 B 41.138  27.892  5.447   1.00 75.13  ? 125  ASN C N   1 
ATOM   974   C CA  . ASN A  1 124 B 41.391  29.232  4.934   1.00 73.23  ? 125  ASN C CA  1 
ATOM   975   C C   . ASN A  1 124 B 41.366  29.294  3.401   1.00 68.62  ? 125  ASN C C   1 
ATOM   976   O O   . ASN A  1 124 B 41.995  30.163  2.811   1.00 72.76  ? 125  ASN C O   1 
ATOM   977   C CB  . ASN A  1 124 B 42.741  29.738  5.466   1.00 74.47  ? 125  ASN C CB  1 
ATOM   978   C CG  . ASN A  1 124 B 43.941  29.042  4.811   1.00 78.26  ? 125  ASN C CG  1 
ATOM   979   O OD1 . ASN A  1 124 B 43.832  27.933  4.275   1.00 75.55  ? 125  ASN C OD1 1 
ATOM   980   N ND2 . ASN A  1 124 B 45.101  29.689  4.883   1.00 80.19  ? 125  ASN C ND2 1 
ATOM   981   N N   . SER A  1 125 ? 40.652  28.364  2.765   1.00 66.98  ? 126  SER C N   1 
ATOM   982   C CA  . SER A  1 125 ? 40.510  28.347  1.300   1.00 64.32  ? 126  SER C CA  1 
ATOM   983   C C   . SER A  1 125 ? 39.094  28.736  0.887   1.00 58.64  ? 126  SER C C   1 
ATOM   984   O O   . SER A  1 125 ? 38.800  28.829  -0.298  1.00 60.30  ? 126  SER C O   1 
ATOM   985   C CB  . SER A  1 125 ? 40.868  26.979  0.691   1.00 64.82  ? 126  SER C CB  1 
ATOM   986   O OG  . SER A  1 125 ? 39.870  25.995  0.921   1.00 64.40  ? 126  SER C OG  1 
ATOM   987   N N   . TRP A  1 126 ? 38.205  28.908  1.860   1.00 59.40  ? 127  TRP C N   1 
ATOM   988   C CA  . TRP A  1 126 ? 36.822  29.274  1.559   1.00 57.98  ? 127  TRP C CA  1 
ATOM   989   C C   . TRP A  1 126 ? 36.640  30.774  1.528   1.00 59.87  ? 127  TRP C C   1 
ATOM   990   O O   . TRP A  1 126 ? 36.361  31.392  2.553   1.00 64.42  ? 127  TRP C O   1 
ATOM   991   C CB  . TRP A  1 126 ? 35.871  28.639  2.580   1.00 52.69  ? 127  TRP C CB  1 
ATOM   992   C CG  . TRP A  1 126 ? 36.032  27.161  2.618   1.00 57.61  ? 127  TRP C CG  1 
ATOM   993   C CD1 . TRP A  1 126 ? 36.692  26.421  3.561   1.00 60.86  ? 127  TRP C CD1 1 
ATOM   994   C CD2 . TRP A  1 126 ? 35.561  26.233  1.635   1.00 58.57  ? 127  TRP C CD2 1 
ATOM   995   N NE1 . TRP A  1 126 ? 36.646  25.082  3.231   1.00 60.45  ? 127  TRP C NE1 1 
ATOM   996   C CE2 . TRP A  1 126 ? 35.958  24.942  2.052   1.00 58.74  ? 127  TRP C CE2 1 
ATOM   997   C CE3 . TRP A  1 126 ? 34.839  26.367  0.442   1.00 50.07  ? 127  TRP C CE3 1 
ATOM   998   C CZ2 . TRP A  1 126 ? 35.650  23.796  1.320   1.00 53.80  ? 127  TRP C CZ2 1 
ATOM   999   C CZ3 . TRP A  1 126 ? 34.534  25.229  -0.278  1.00 54.94  ? 127  TRP C CZ3 1 
ATOM   1000  C CH2 . TRP A  1 126 ? 34.937  23.959  0.162   1.00 53.25  ? 127  TRP C CH2 1 
ATOM   1001  N N   . SER A  1 127 ? 36.732  31.340  0.327   1.00 61.64  ? 128  SER C N   1 
ATOM   1002  C CA  . SER A  1 127 ? 36.809  32.787  0.170   1.00 57.65  ? 128  SER C CA  1 
ATOM   1003  C C   . SER A  1 127 ? 35.523  33.477  -0.283  1.00 55.27  ? 128  SER C C   1 
ATOM   1004  O O   . SER A  1 127 ? 35.466  34.701  -0.299  1.00 60.56  ? 128  SER C O   1 
ATOM   1005  C CB  . SER A  1 127 ? 37.944  33.128  -0.795  1.00 53.89  ? 128  SER C CB  1 
ATOM   1006  O OG  . SER A  1 127 ? 37.838  32.393  -1.995  1.00 65.91  ? 128  SER C OG  1 
ATOM   1007  N N   . ASP A  1 128 ? 34.498  32.714  -0.655  1.00 59.46  ? 129  ASP C N   1 
ATOM   1008  C CA  . ASP A  1 128 ? 33.209  33.310  -1.032  1.00 53.63  ? 129  ASP C CA  1 
ATOM   1009  C C   . ASP A  1 128 ? 32.060  32.774  -0.203  1.00 50.94  ? 129  ASP C C   1 
ATOM   1010  O O   . ASP A  1 128 ? 30.910  33.052  -0.499  1.00 52.78  ? 129  ASP C O   1 
ATOM   1011  C CB  . ASP A  1 128 ? 32.900  33.073  -2.513  1.00 57.10  ? 129  ASP C CB  1 
ATOM   1012  C CG  . ASP A  1 128 ? 33.864  33.783  -3.439  1.00 51.92  ? 129  ASP C CG  1 
ATOM   1013  O OD1 . ASP A  1 128 ? 34.318  34.887  -3.091  1.00 50.08  ? 129  ASP C OD1 1 
ATOM   1014  O OD2 . ASP A  1 128 ? 34.179  33.217  -4.508  1.00 55.48  ? 129  ASP C OD2 1 
ATOM   1015  N N   . HIS A  1 129 ? 32.376  32.009  0.836   1.00 57.69  ? 130  HIS C N   1 
ATOM   1016  C CA  . HIS A  1 129 ? 31.364  31.458  1.736   1.00 54.30  ? 130  HIS C CA  1 
ATOM   1017  C C   . HIS A  1 129 ? 31.829  31.611  3.164   1.00 56.25  ? 130  HIS C C   1 
ATOM   1018  O O   . HIS A  1 129 ? 33.025  31.814  3.414   1.00 57.15  ? 130  HIS C O   1 
ATOM   1019  C CB  . HIS A  1 129 ? 31.094  29.981  1.455   1.00 53.06  ? 130  HIS C CB  1 
ATOM   1020  C CG  . HIS A  1 129 ? 30.745  29.683  0.032   1.00 51.55  ? 130  HIS C CG  1 
ATOM   1021  N ND1 . HIS A  1 129 ? 31.689  29.644  -0.973  1.00 45.23  ? 130  HIS C ND1 1 
ATOM   1022  C CD2 . HIS A  1 129 ? 29.557  29.384  -0.549  1.00 48.01  ? 130  HIS C CD2 1 
ATOM   1023  C CE1 . HIS A  1 129 ? 31.095  29.340  -2.112  1.00 46.32  ? 130  HIS C CE1 1 
ATOM   1024  N NE2 . HIS A  1 129 ? 29.802  29.182  -1.884  1.00 46.38  ? 130  HIS C NE2 1 
ATOM   1025  N N   . GLU A  1 130 ? 30.890  31.499  4.100   1.00 58.14  ? 131  GLU C N   1 
ATOM   1026  C CA  . GLU A  1 130 ? 31.239  31.542  5.514   1.00 57.00  ? 131  GLU C CA  1 
ATOM   1027  C C   . GLU A  1 130 ? 31.529  30.137  6.051   1.00 57.55  ? 131  GLU C C   1 
ATOM   1028  O O   . GLU A  1 130 ? 30.630  29.283  6.128   1.00 53.27  ? 131  GLU C O   1 
ATOM   1029  C CB  . GLU A  1 130 ? 30.107  32.177  6.311   1.00 50.69  ? 131  GLU C CB  1 
ATOM   1030  C CG  . GLU A  1 130 ? 29.875  33.615  5.964   1.00 62.01  ? 131  GLU C CG  1 
ATOM   1031  C CD  . GLU A  1 130 ? 30.920  34.513  6.571   1.00 73.28  ? 131  GLU C CD  1 
ATOM   1032  O OE1 . GLU A  1 130 ? 31.509  34.082  7.594   1.00 73.91  ? 131  GLU C OE1 1 
ATOM   1033  O OE2 . GLU A  1 130 ? 31.134  35.636  6.037   1.00 70.46  ? 131  GLU C OE2 1 
ATOM   1034  N N   . ALA A  1 131 ? 32.774  29.929  6.469   1.00 48.55  ? 132  ALA C N   1 
ATOM   1035  C CA  . ALA A  1 131 ? 33.222  28.629  6.937   1.00 47.19  ? 132  ALA C CA  1 
ATOM   1036  C C   . ALA A  1 131 ? 33.486  28.670  8.427   1.00 49.14  ? 132  ALA C C   1 
ATOM   1037  O O   . ALA A  1 131 ? 34.624  28.474  8.868   1.00 52.14  ? 132  ALA C O   1 
ATOM   1038  C CB  . ALA A  1 131 ? 34.477  28.181  6.192   1.00 49.34  ? 132  ALA C CB  1 
ATOM   1039  N N   . SER A  1 132 ? 32.436  28.968  9.188   1.00 50.07  ? 133  SER C N   1 
ATOM   1040  C CA  . SER A  1 132 ? 32.536  29.082  10.643  1.00 49.41  ? 133  SER C CA  1 
ATOM   1041  C C   . SER A  1 132 ? 31.212  28.679  11.311  1.00 50.00  ? 133  SER C C   1 
ATOM   1042  O O   . SER A  1 132 ? 30.862  29.180  12.379  1.00 46.01  ? 133  SER C O   1 
ATOM   1043  C CB  . SER A  1 132 ? 32.950  30.509  11.039  1.00 48.23  ? 133  SER C CB  1 
ATOM   1044  O OG  . SER A  1 132 ? 32.113  31.491  10.435  1.00 55.21  ? 133  SER C OG  1 
ATOM   1045  N N   . GLY A  1 133 ? 30.463  27.797  10.651  1.00 53.79  ? 134  GLY C N   1 
ATOM   1046  C CA  . GLY A  1 133 ? 29.191  27.326  11.170  1.00 43.37  ? 134  GLY C CA  1 
ATOM   1047  C C   . GLY A  1 133 ? 29.321  26.599  12.497  1.00 48.19  ? 134  GLY C C   1 
ATOM   1048  O O   . GLY A  1 133 ? 30.303  25.887  12.767  1.00 43.95  ? 134  GLY C O   1 
ATOM   1049  N N   . VAL A  1 134 ? 28.320  26.776  13.347  1.00 49.73  ? 135  VAL C N   1 
ATOM   1050  C CA  . VAL A  1 134 ? 28.452  26.343  14.719  1.00 44.73  ? 135  VAL C CA  1 
ATOM   1051  C C   . VAL A  1 134 ? 27.073  26.067  15.321  1.00 48.10  ? 135  VAL C C   1 
ATOM   1052  O O   . VAL A  1 134 ? 26.067  26.591  14.850  1.00 50.18  ? 135  VAL C O   1 
ATOM   1053  C CB  . VAL A  1 134 ? 29.266  27.400  15.512  1.00 48.93  ? 135  VAL C CB  1 
ATOM   1054  C CG1 . VAL A  1 134 ? 28.550  27.856  16.747  1.00 50.94  ? 135  VAL C CG1 1 
ATOM   1055  C CG2 . VAL A  1 134 ? 30.677  26.878  15.817  1.00 44.92  ? 135  VAL C CG2 1 
ATOM   1056  N N   . SER A  1 135 ? 27.024  25.203  16.332  1.00 47.90  ? 136  SER C N   1 
ATOM   1057  C CA  . SER A  1 135 ? 25.758  24.861  16.950  1.00 49.78  ? 136  SER C CA  1 
ATOM   1058  C C   . SER A  1 135 ? 25.917  24.610  18.448  1.00 54.30  ? 136  SER C C   1 
ATOM   1059  O O   . SER A  1 135 ? 26.959  24.128  18.921  1.00 50.19  ? 136  SER C O   1 
ATOM   1060  C CB  . SER A  1 135 ? 25.142  23.631  16.284  1.00 47.04  ? 136  SER C CB  1 
ATOM   1061  O OG  . SER A  1 135 ? 24.031  23.145  17.034  1.00 50.05  ? 136  SER C OG  1 
ATOM   1062  N N   . SER A  1 136 ? 24.861  24.945  19.184  1.00 47.45  ? 137  SER C N   1 
ATOM   1063  C CA  . SER A  1 136 ? 24.843  24.777  20.616  1.00 48.82  ? 137  SER C CA  1 
ATOM   1064  C C   . SER A  1 136 ? 24.670  23.301  20.983  1.00 53.54  ? 137  SER C C   1 
ATOM   1065  O O   . SER A  1 136 ? 24.875  22.915  22.135  1.00 57.83  ? 137  SER C O   1 
ATOM   1066  C CB  . SER A  1 136 ? 23.727  25.630  21.231  1.00 51.90  ? 137  SER C CB  1 
ATOM   1067  O OG  . SER A  1 136 ? 22.443  25.154  20.849  1.00 58.21  ? 137  SER C OG  1 
ATOM   1068  N N   . ALA A  1 137 ? 24.282  22.477  20.010  1.00 52.80  ? 138  ALA C N   1 
ATOM   1069  C CA  . ALA A  1 137 ? 24.149  21.041  20.246  1.00 46.36  ? 138  ALA C CA  1 
ATOM   1070  C C   . ALA A  1 137 ? 25.523  20.396  20.199  1.00 45.49  ? 138  ALA C C   1 
ATOM   1071  O O   . ALA A  1 137 ? 25.667  19.207  20.482  1.00 47.70  ? 138  ALA C O   1 
ATOM   1072  C CB  . ALA A  1 137 ? 23.209  20.404  19.251  1.00 43.17  ? 138  ALA C CB  1 
ATOM   1073  N N   . CYS A  1 138 ? 26.514  21.179  19.781  1.00 43.65  ? 139  CYS C N   1 
ATOM   1074  C CA  . CYS A  1 138 ? 27.909  20.737  19.753  1.00 50.58  ? 139  CYS C CA  1 
ATOM   1075  C C   . CYS A  1 138 ? 28.834  21.649  20.557  1.00 51.07  ? 139  CYS C C   1 
ATOM   1076  O O   . CYS A  1 138 ? 29.639  22.384  19.977  1.00 52.17  ? 139  CYS C O   1 
ATOM   1077  C CB  . CYS A  1 138 ? 28.429  20.654  18.307  1.00 43.55  ? 139  CYS C CB  1 
ATOM   1078  S SG  . CYS A  1 138 ? 27.756  19.276  17.342  1.00 63.28  ? 139  CYS C SG  1 
ATOM   1079  N N   . PRO A  1 139 ? 28.752  21.590  21.893  1.00 49.40  ? 140  PRO C N   1 
ATOM   1080  C CA  . PRO A  1 139 ? 29.597  22.453  22.735  1.00 52.35  ? 140  PRO C CA  1 
ATOM   1081  C C   . PRO A  1 139 ? 31.033  21.951  22.890  1.00 53.69  ? 140  PRO C C   1 
ATOM   1082  O O   . PRO A  1 139 ? 31.287  20.748  22.774  1.00 56.96  ? 140  PRO C O   1 
ATOM   1083  C CB  . PRO A  1 139 ? 28.881  22.423  24.087  1.00 51.75  ? 140  PRO C CB  1 
ATOM   1084  C CG  . PRO A  1 139 ? 28.236  21.075  24.125  1.00 45.31  ? 140  PRO C CG  1 
ATOM   1085  C CD  . PRO A  1 139 ? 27.803  20.796  22.697  1.00 50.68  ? 140  PRO C CD  1 
ATOM   1086  N N   . TYR A  1 140 ? 31.955  22.870  23.153  1.00 53.37  ? 141  TYR C N   1 
ATOM   1087  C CA  . TYR A  1 140 ? 33.346  22.517  23.450  1.00 56.76  ? 141  TYR C CA  1 
ATOM   1088  C C   . TYR A  1 140 ? 33.716  22.932  24.893  1.00 61.62  ? 141  TYR C C   1 
ATOM   1089  O O   . TYR A  1 140 ? 33.764  22.087  25.798  1.00 66.37  ? 141  TYR C O   1 
ATOM   1090  C CB  . TYR A  1 140 ? 34.294  23.125  22.418  1.00 53.62  ? 141  TYR C CB  1 
ATOM   1091  C CG  . TYR A  1 140 ? 35.757  22.920  22.736  1.00 52.00  ? 141  TYR C CG  1 
ATOM   1092  C CD1 . TYR A  1 140 ? 36.233  21.706  23.213  1.00 50.62  ? 141  TYR C CD1 1 
ATOM   1093  C CD2 . TYR A  1 140 ? 36.671  23.949  22.538  1.00 56.62  ? 141  TYR C CD2 1 
ATOM   1094  C CE1 . TYR A  1 140 ? 37.582  21.538  23.499  1.00 53.66  ? 141  TYR C CE1 1 
ATOM   1095  C CE2 . TYR A  1 140 ? 38.013  23.792  22.819  1.00 47.25  ? 141  TYR C CE2 1 
ATOM   1096  C CZ  . TYR A  1 140 ? 38.462  22.595  23.294  1.00 50.68  ? 141  TYR C CZ  1 
ATOM   1097  O OH  . TYR A  1 140 ? 39.799  22.455  23.553  1.00 54.39  ? 141  TYR C OH  1 
ATOM   1098  N N   . GLN A  1 141 ? 34.010  24.206  25.117  1.00 58.49  ? 142  GLN C N   1 
ATOM   1099  C CA  . GLN A  1 141 ? 34.329  24.656  26.477  1.00 63.06  ? 142  GLN C CA  1 
ATOM   1100  C C   . GLN A  1 141 ? 33.263  25.619  26.980  1.00 65.86  ? 142  GLN C C   1 
ATOM   1101  O O   . GLN A  1 141 ? 33.543  26.781  27.272  1.00 67.82  ? 142  GLN C O   1 
ATOM   1102  C CB  . GLN A  1 141 ? 35.714  25.310  26.507  1.00 61.19  ? 142  GLN C CB  1 
ATOM   1103  C CG  . GLN A  1 141 ? 36.867  24.307  26.514  1.00 58.81  ? 142  GLN C CG  1 
ATOM   1104  C CD  . GLN A  1 141 ? 38.228  24.961  26.276  1.00 59.85  ? 142  GLN C CD  1 
ATOM   1105  O OE1 . GLN A  1 141 ? 38.321  26.124  25.855  1.00 57.89  ? 142  GLN C OE1 1 
ATOM   1106  N NE2 . GLN A  1 141 ? 39.290  24.205  26.524  1.00 59.50  ? 142  GLN C NE2 1 
ATOM   1107  N N   . GLY A  1 142 ? 32.025  25.140  27.023  1.00 61.92  ? 143  GLY C N   1 
ATOM   1108  C CA  . GLY A  1 142 ? 30.920  25.938  27.506  1.00 60.00  ? 143  GLY C CA  1 
ATOM   1109  C C   . GLY A  1 142 ? 30.354  26.801  26.396  1.00 69.11  ? 143  GLY C C   1 
ATOM   1110  O O   . GLY A  1 142 ? 29.349  27.480  26.583  1.00 79.96  ? 143  GLY C O   1 
ATOM   1111  N N   . ARG A  1 143 ? 30.992  26.767  25.230  1.00 65.75  ? 144  ARG C N   1 
ATOM   1112  C CA  . ARG A  1 143 ? 30.539  27.558  24.089  1.00 66.16  ? 144  ARG C CA  1 
ATOM   1113  C C   . ARG A  1 143 ? 30.289  26.691  22.840  1.00 63.92  ? 144  ARG C C   1 
ATOM   1114  O O   . ARG A  1 143 ? 30.816  25.576  22.741  1.00 61.59  ? 144  ARG C O   1 
ATOM   1115  C CB  . ARG A  1 143 ? 31.577  28.648  23.815  1.00 71.50  ? 144  ARG C CB  1 
ATOM   1116  C CG  . ARG A  1 143 ? 32.887  28.115  23.262  1.00 75.78  ? 144  ARG C CG  1 
ATOM   1117  C CD  . ARG A  1 143 ? 33.936  29.218  23.188  1.00 89.56  ? 144  ARG C CD  1 
ATOM   1118  N NE  . ARG A  1 143 ? 35.159  28.810  22.485  1.00 103.16 ? 144  ARG C NE  1 
ATOM   1119  C CZ  . ARG A  1 143 ? 36.201  28.216  23.069  1.00 90.69  ? 144  ARG C CZ  1 
ATOM   1120  N NH1 . ARG A  1 143 ? 36.157  27.910  24.363  1.00 81.32  ? 144  ARG C NH1 1 
ATOM   1121  N NH2 . ARG A  1 143 ? 37.277  27.895  22.355  1.00 79.71  ? 144  ARG C NH2 1 
ATOM   1122  N N   . SER A  1 144 ? 29.548  27.233  21.867  1.00 64.63  ? 145  SER C N   1 
ATOM   1123  C CA  . SER A  1 144 ? 29.144  26.477  20.671  1.00 53.76  ? 145  SER C CA  1 
ATOM   1124  C C   . SER A  1 144 ? 30.239  26.232  19.651  1.00 54.24  ? 145  SER C C   1 
ATOM   1125  O O   . SER A  1 144 ? 30.978  27.144  19.246  1.00 50.15  ? 145  SER C O   1 
ATOM   1126  C CB  . SER A  1 144 ? 27.985  27.176  19.965  1.00 48.95  ? 145  SER C CB  1 
ATOM   1127  O OG  . SER A  1 144 ? 26.837  27.195  20.780  1.00 53.39  ? 145  SER C OG  1 
ATOM   1128  N N   . SER A  1 145 ? 30.264  24.991  19.175  1.00 48.50  ? 146  SER C N   1 
ATOM   1129  C CA  . SER A  1 145 ? 31.326  24.527  18.312  1.00 44.95  ? 146  SER C CA  1 
ATOM   1130  C C   . SER A  1 145 ? 30.708  23.650  17.197  1.00 45.75  ? 146  SER C C   1 
ATOM   1131  O O   . SER A  1 145 ? 29.494  23.712  16.956  1.00 42.83  ? 146  SER C O   1 
ATOM   1132  C CB  . SER A  1 145 ? 32.358  23.770  19.173  1.00 44.65  ? 146  SER C CB  1 
ATOM   1133  O OG  . SER A  1 145 ? 33.562  23.495  18.482  1.00 51.97  ? 146  SER C OG  1 
ATOM   1134  N N   . PHE A  1 146 ? 31.519  22.812  16.554  1.00 39.52  ? 147  PHE C N   1 
ATOM   1135  C CA  . PHE A  1 146 ? 31.041  21.925  15.499  1.00 40.41  ? 147  PHE C CA  1 
ATOM   1136  C C   . PHE A  1 146 ? 32.109  20.851  15.314  1.00 41.38  ? 147  PHE C C   1 
ATOM   1137  O O   . PHE A  1 146 ? 33.229  20.986  15.830  1.00 44.02  ? 147  PHE C O   1 
ATOM   1138  C CB  . PHE A  1 146 ? 30.795  22.690  14.179  1.00 45.30  ? 147  PHE C CB  1 
ATOM   1139  C CG  . PHE A  1 146 ? 29.881  21.967  13.188  1.00 42.51  ? 147  PHE C CG  1 
ATOM   1140  C CD1 . PHE A  1 146 ? 28.517  21.835  13.437  1.00 39.97  ? 147  PHE C CD1 1 
ATOM   1141  C CD2 . PHE A  1 146 ? 30.392  21.430  12.007  1.00 38.48  ? 147  PHE C CD2 1 
ATOM   1142  C CE1 . PHE A  1 146 ? 27.681  21.176  12.532  1.00 36.88  ? 147  PHE C CE1 1 
ATOM   1143  C CE2 . PHE A  1 146 ? 29.566  20.761  11.105  1.00 35.20  ? 147  PHE C CE2 1 
ATOM   1144  C CZ  . PHE A  1 146 ? 28.212  20.628  11.371  1.00 34.24  ? 147  PHE C CZ  1 
ATOM   1145  N N   . PHE A  1 147 ? 31.772  19.815  14.552  1.00 37.73  ? 148  PHE C N   1 
ATOM   1146  C CA  . PHE A  1 147 ? 32.719  18.755  14.175  1.00 40.03  ? 148  PHE C CA  1 
ATOM   1147  C C   . PHE A  1 147 ? 34.023  19.307  13.602  1.00 38.61  ? 148  PHE C C   1 
ATOM   1148  O O   . PHE A  1 147 ? 33.992  20.221  12.791  1.00 40.45  ? 148  PHE C O   1 
ATOM   1149  C CB  . PHE A  1 147 ? 32.094  17.829  13.122  1.00 33.55  ? 148  PHE C CB  1 
ATOM   1150  C CG  . PHE A  1 147 ? 30.808  17.185  13.552  1.00 30.20  ? 148  PHE C CG  1 
ATOM   1151  C CD1 . PHE A  1 147 ? 30.817  16.076  14.405  1.00 29.76  ? 148  PHE C CD1 1 
ATOM   1152  C CD2 . PHE A  1 147 ? 29.590  17.665  13.076  1.00 28.33  ? 148  PHE C CD2 1 
ATOM   1153  C CE1 . PHE A  1 147 ? 29.621  15.464  14.791  1.00 28.98  ? 148  PHE C CE1 1 
ATOM   1154  C CE2 . PHE A  1 147 ? 28.393  17.069  13.438  1.00 27.87  ? 148  PHE C CE2 1 
ATOM   1155  C CZ  . PHE A  1 147 ? 28.404  15.967  14.303  1.00 34.92  ? 148  PHE C CZ  1 
ATOM   1156  N N   . ARG A  1 148 ? 35.160  18.722  13.977  1.00 40.71  ? 149  ARG C N   1 
ATOM   1157  C CA  . ARG A  1 148 ? 36.464  19.294  13.604  1.00 39.32  ? 149  ARG C CA  1 
ATOM   1158  C C   . ARG A  1 148 ? 37.016  18.848  12.256  1.00 38.66  ? 149  ARG C C   1 
ATOM   1159  O O   . ARG A  1 148 ? 37.970  19.434  11.751  1.00 44.15  ? 149  ARG C O   1 
ATOM   1160  C CB  . ARG A  1 148 ? 37.495  19.011  14.701  1.00 38.76  ? 149  ARG C CB  1 
ATOM   1161  C CG  . ARG A  1 148 ? 37.007  19.426  16.085  1.00 40.97  ? 149  ARG C CG  1 
ATOM   1162  C CD  . ARG A  1 148 ? 38.131  19.991  16.914  1.00 47.00  ? 149  ARG C CD  1 
ATOM   1163  N NE  . ARG A  1 148 ? 37.699  20.323  18.267  1.00 53.54  ? 149  ARG C NE  1 
ATOM   1164  C CZ  . ARG A  1 148 ? 37.189  21.497  18.633  1.00 53.86  ? 149  ARG C CZ  1 
ATOM   1165  N NH1 . ARG A  1 148 ? 37.020  22.462  17.740  1.00 52.09  ? 149  ARG C NH1 1 
ATOM   1166  N NH2 . ARG A  1 148 ? 36.831  21.702  19.896  1.00 52.68  ? 149  ARG C NH2 1 
ATOM   1167  N N   . ASN A  1 149 ? 36.449  17.790  11.697  1.00 35.76  ? 150  ASN C N   1 
ATOM   1168  C CA  . ASN A  1 149 ? 36.935  17.238  10.449  1.00 35.28  ? 150  ASN C CA  1 
ATOM   1169  C C   . ASN A  1 149 ? 36.069  17.594  9.202   1.00 40.53  ? 150  ASN C C   1 
ATOM   1170  O O   . ASN A  1 149 ? 36.385  17.208  8.065   1.00 38.00  ? 150  ASN C O   1 
ATOM   1171  C CB  . ASN A  1 149 ? 37.056  15.741  10.636  1.00 33.80  ? 150  ASN C CB  1 
ATOM   1172  C CG  . ASN A  1 149 ? 38.134  15.395  11.616  1.00 35.92  ? 150  ASN C CG  1 
ATOM   1173  O OD1 . ASN A  1 149 ? 39.221  15.984  11.579  1.00 39.13  ? 150  ASN C OD1 1 
ATOM   1174  N ND2 . ASN A  1 149 ? 37.837  14.477  12.537  1.00 30.78  ? 150  ASN C ND2 1 
ATOM   1175  N N   . VAL A  1 150 ? 34.963  18.300  9.434   1.00 42.31  ? 151  VAL C N   1 
ATOM   1176  C CA  . VAL A  1 150 ? 34.111  18.813  8.356   1.00 38.98  ? 151  VAL C CA  1 
ATOM   1177  C C   . VAL A  1 150 ? 33.715  20.270  8.660   1.00 42.70  ? 151  VAL C C   1 
ATOM   1178  O O   . VAL A  1 150 ? 33.728  20.682  9.819   1.00 36.58  ? 151  VAL C O   1 
ATOM   1179  C CB  . VAL A  1 150 ? 32.837  17.958  8.181   1.00 39.36  ? 151  VAL C CB  1 
ATOM   1180  C CG1 . VAL A  1 150 ? 33.216  16.538  7.746   1.00 31.76  ? 151  VAL C CG1 1 
ATOM   1181  C CG2 . VAL A  1 150 ? 32.020  17.920  9.486   1.00 30.33  ? 151  VAL C CG2 1 
ATOM   1182  N N   . VAL A  1 151 ? 33.327  21.037  7.638   1.00 40.93  ? 152  VAL C N   1 
ATOM   1183  C CA  . VAL A  1 151 ? 33.026  22.462  7.823   1.00 38.88  ? 152  VAL C CA  1 
ATOM   1184  C C   . VAL A  1 151 ? 31.599  22.844  7.377   1.00 41.71  ? 152  VAL C C   1 
ATOM   1185  O O   . VAL A  1 151 ? 31.163  22.474  6.282   1.00 48.82  ? 152  VAL C O   1 
ATOM   1186  C CB  . VAL A  1 151 ? 34.074  23.326  7.056   1.00 47.54  ? 152  VAL C CB  1 
ATOM   1187  C CG1 . VAL A  1 151 ? 33.788  24.824  7.199   1.00 43.49  ? 152  VAL C CG1 1 
ATOM   1188  C CG2 . VAL A  1 151 ? 35.486  22.998  7.547   1.00 44.16  ? 152  VAL C CG2 1 
ATOM   1189  N N   . TRP A  1 152 ? 30.880  23.586  8.222   1.00 40.40  ? 153  TRP C N   1 
ATOM   1190  C CA  . TRP A  1 152 ? 29.528  24.081  7.897   1.00 42.92  ? 153  TRP C CA  1 
ATOM   1191  C C   . TRP A  1 152 ? 29.577  25.416  7.128   1.00 46.80  ? 153  TRP C C   1 
ATOM   1192  O O   . TRP A  1 152 ? 29.776  26.472  7.730   1.00 49.73  ? 153  TRP C O   1 
ATOM   1193  C CB  . TRP A  1 152 ? 28.703  24.247  9.176   1.00 38.72  ? 153  TRP C CB  1 
ATOM   1194  C CG  . TRP A  1 152 ? 27.229  24.408  8.976   1.00 38.62  ? 153  TRP C CG  1 
ATOM   1195  C CD1 . TRP A  1 152 ? 26.577  24.579  7.799   1.00 41.90  ? 153  TRP C CD1 1 
ATOM   1196  C CD2 . TRP A  1 152 ? 26.221  24.432  9.997   1.00 43.17  ? 153  TRP C CD2 1 
ATOM   1197  N NE1 . TRP A  1 152 ? 25.215  24.692  8.011   1.00 36.86  ? 153  TRP C NE1 1 
ATOM   1198  C CE2 . TRP A  1 152 ? 24.974  24.599  9.354   1.00 41.32  ? 153  TRP C CE2 1 
ATOM   1199  C CE3 . TRP A  1 152 ? 26.248  24.314  11.394  1.00 44.39  ? 153  TRP C CE3 1 
ATOM   1200  C CZ2 . TRP A  1 152 ? 23.771  24.657  10.056  1.00 44.07  ? 153  TRP C CZ2 1 
ATOM   1201  C CZ3 . TRP A  1 152 ? 25.039  24.364  12.094  1.00 40.49  ? 153  TRP C CZ3 1 
ATOM   1202  C CH2 . TRP A  1 152 ? 23.826  24.535  11.422  1.00 46.67  ? 153  TRP C CH2 1 
ATOM   1203  N N   . LEU A  1 153 ? 29.395  25.359  5.807   1.00 45.69  ? 154  LEU C N   1 
ATOM   1204  C CA  . LEU A  1 153 ? 29.418  26.552  4.955   1.00 45.44  ? 154  LEU C CA  1 
ATOM   1205  C C   . LEU A  1 153 ? 28.033  27.208  4.860   1.00 47.18  ? 154  LEU C C   1 
ATOM   1206  O O   . LEU A  1 153 ? 27.025  26.537  4.651   1.00 45.82  ? 154  LEU C O   1 
ATOM   1207  C CB  . LEU A  1 153 ? 29.940  26.194  3.552   1.00 42.52  ? 154  LEU C CB  1 
ATOM   1208  C CG  . LEU A  1 153 ? 31.312  25.502  3.488   1.00 42.64  ? 154  LEU C CG  1 
ATOM   1209  C CD1 . LEU A  1 153 ? 31.591  24.868  2.122   1.00 41.80  ? 154  LEU C CD1 1 
ATOM   1210  C CD2 . LEU A  1 153 ? 32.431  26.478  3.826   1.00 42.19  ? 154  LEU C CD2 1 
ATOM   1211  N N   . THR A  1 154 ? 28.005  28.532  4.997   1.00 50.95  ? 155  THR C N   1 
ATOM   1212  C CA  . THR A  1 154 ? 26.767  29.310  4.917   1.00 50.19  ? 155  THR C CA  1 
ATOM   1213  C C   . THR A  1 154 ? 26.949  30.502  3.973   1.00 49.79  ? 155  THR C C   1 
ATOM   1214  O O   . THR A  1 154 ? 28.076  30.773  3.527   1.00 47.02  ? 155  THR C O   1 
ATOM   1215  C CB  . THR A  1 154 ? 26.334  29.808  6.310   1.00 45.27  ? 155  THR C CB  1 
ATOM   1216  O OG1 . THR A  1 154 ? 27.466  30.395  6.958   1.00 50.06  ? 155  THR C OG1 1 
ATOM   1217  C CG2 . THR A  1 154 ? 25.885  28.656  7.167   1.00 48.84  ? 155  THR C CG2 1 
ATOM   1218  N N   . LYS A  1 155 ? 25.866  31.233  3.701   1.00 44.20  ? 156  LYS C N   1 
ATOM   1219  C CA  . LYS A  1 155 ? 25.944  32.344  2.749   1.00 50.74  ? 156  LYS C CA  1 
ATOM   1220  C C   . LYS A  1 155 ? 26.842  33.464  3.258   1.00 52.65  ? 156  LYS C C   1 
ATOM   1221  O O   . LYS A  1 155 ? 26.984  33.658  4.465   1.00 56.15  ? 156  LYS C O   1 
ATOM   1222  C CB  . LYS A  1 155 ? 24.554  32.894  2.430   1.00 51.98  ? 156  LYS C CB  1 
ATOM   1223  C CG  . LYS A  1 155 ? 23.925  33.730  3.522   1.00 49.59  ? 156  LYS C CG  1 
ATOM   1224  C CD  . LYS A  1 155 ? 22.516  34.142  3.123   1.00 54.62  ? 156  LYS C CD  1 
ATOM   1225  C CE  . LYS A  1 155 ? 21.863  35.050  4.152   1.00 52.08  ? 156  LYS C CE  1 
ATOM   1226  N NZ  . LYS A  1 155 ? 20.463  35.399  3.796   1.00 50.92  ? 156  LYS C NZ  1 
ATOM   1227  N N   . LYS A  1 156 ? 27.506  34.134  2.322   1.00 53.03  ? 157  LYS C N   1 
ATOM   1228  C CA  . LYS A  1 156 ? 28.370  35.276  2.612   1.00 58.80  ? 157  LYS C CA  1 
ATOM   1229  C C   . LYS A  1 156 ? 27.876  36.472  1.813   1.00 64.53  ? 157  LYS C C   1 
ATOM   1230  O O   . LYS A  1 156 ? 27.653  36.365  0.598   1.00 61.52  ? 157  LYS C O   1 
ATOM   1231  C CB  . LYS A  1 156 ? 29.832  34.980  2.279   1.00 61.44  ? 157  LYS C CB  1 
ATOM   1232  C CG  . LYS A  1 156 ? 30.772  36.161  2.477   1.00 58.34  ? 157  LYS C CG  1 
ATOM   1233  C CD  . LYS A  1 156 ? 32.214  35.730  2.263   1.00 59.59  ? 157  LYS C CD  1 
ATOM   1234  C CE  . LYS A  1 156 ? 33.172  36.901  2.375   1.00 61.73  ? 157  LYS C CE  1 
ATOM   1235  N NZ  . LYS A  1 156 ? 34.581  36.463  2.149   1.00 66.35  ? 157  LYS C NZ  1 
ATOM   1236  N N   . ASP A  1 157 ? 27.778  37.614  2.494   1.00 70.26  ? 158  ASP C N   1 
ATOM   1237  C CA  . ASP A  1 157 ? 26.990  38.757  2.040   1.00 70.76  ? 158  ASP C CA  1 
ATOM   1238  C C   . ASP A  1 157 ? 25.546  38.278  2.004   1.00 72.24  ? 158  ASP C C   1 
ATOM   1239  O O   . ASP A  1 157 ? 24.970  37.979  3.060   1.00 70.86  ? 158  ASP C O   1 
ATOM   1240  C CB  . ASP A  1 157 ? 27.470  39.275  0.679   1.00 61.42  ? 158  ASP C CB  1 
ATOM   1241  C CG  . ASP A  1 157 ? 28.939  39.689  0.710   1.00 71.81  ? 158  ASP C CG  1 
ATOM   1242  O OD1 . ASP A  1 157 ? 29.391  40.231  1.754   1.00 68.67  ? 158  ASP C OD1 1 
ATOM   1243  O OD2 . ASP A  1 157 ? 29.647  39.446  -0.297  1.00 69.79  ? 158  ASP C OD2 1 
ATOM   1244  N N   . ASN A  1 158 ? 24.953  38.210  0.818   1.00 69.13  ? 159  ASN C N   1 
ATOM   1245  C CA  . ASN A  1 158 ? 23.649  37.574  0.698   1.00 65.55  ? 159  ASN C CA  1 
ATOM   1246  C C   . ASN A  1 158 ? 23.639  36.621  -0.463  1.00 65.13  ? 159  ASN C C   1 
ATOM   1247  O O   . ASN A  1 158 ? 22.647  36.533  -1.184  1.00 69.76  ? 159  ASN C O   1 
ATOM   1248  C CB  . ASN A  1 158 ? 22.539  38.606  0.522   1.00 69.49  ? 159  ASN C CB  1 
ATOM   1249  C CG  . ASN A  1 158 ? 21.869  38.954  1.823   1.00 67.18  ? 159  ASN C CG  1 
ATOM   1250  O OD1 . ASN A  1 158 ? 20.962  38.255  2.284   1.00 69.90  ? 159  ASN C OD1 1 
ATOM   1251  N ND2 . ASN A  1 158 ? 22.317  40.036  2.433   1.00 70.33  ? 159  ASN C ND2 1 
ATOM   1252  N N   . ALA A  1 159 ? 24.727  35.877  -0.627  1.00 63.71  ? 160  ALA C N   1 
ATOM   1253  C CA  . ALA A  1 159 ? 24.840  34.986  -1.773  1.00 61.31  ? 160  ALA C CA  1 
ATOM   1254  C C   . ALA A  1 159 ? 25.546  33.674  -1.428  1.00 62.08  ? 160  ALA C C   1 
ATOM   1255  O O   . ALA A  1 159 ? 26.447  33.639  -0.578  1.00 57.16  ? 160  ALA C O   1 
ATOM   1256  C CB  . ALA A  1 159 ? 25.577  35.690  -2.903  1.00 51.51  ? 160  ALA C CB  1 
ATOM   1257  N N   . TYR A  1 160 ? 25.179  32.623  -2.163  1.00 55.78  ? 161  TYR C N   1 
ATOM   1258  C CA  . TYR A  1 160 ? 25.832  31.327  -2.070  1.00 47.51  ? 161  TYR C CA  1 
ATOM   1259  C C   . TYR A  1 160 ? 26.125  30.914  -3.500  1.00 49.94  ? 161  TYR C C   1 
ATOM   1260  O O   . TYR A  1 160 ? 25.309  30.247  -4.166  1.00 44.38  ? 161  TYR C O   1 
ATOM   1261  C CB  . TYR A  1 160 ? 24.957  30.282  -1.358  1.00 46.58  ? 161  TYR C CB  1 
ATOM   1262  C CG  . TYR A  1 160 ? 25.683  29.009  -0.898  1.00 46.92  ? 161  TYR C CG  1 
ATOM   1263  C CD1 . TYR A  1 160 ? 26.250  28.118  -1.821  1.00 45.29  ? 161  TYR C CD1 1 
ATOM   1264  C CD2 . TYR A  1 160 ? 25.739  28.669  0.453   1.00 48.38  ? 161  TYR C CD2 1 
ATOM   1265  C CE1 . TYR A  1 160 ? 26.890  26.955  -1.406  1.00 45.04  ? 161  TYR C CE1 1 
ATOM   1266  C CE2 . TYR A  1 160 ? 26.361  27.502  0.882   1.00 44.97  ? 161  TYR C CE2 1 
ATOM   1267  C CZ  . TYR A  1 160 ? 26.938  26.648  -0.053  1.00 48.04  ? 161  TYR C CZ  1 
ATOM   1268  O OH  . TYR A  1 160 ? 27.563  25.490  0.364   1.00 43.04  ? 161  TYR C OH  1 
ATOM   1269  N N   . PRO A  1 161 ? 27.300  31.331  -3.985  1.00 48.85  ? 162  PRO C N   1 
ATOM   1270  C CA  . PRO A  1 161 ? 27.741  30.955  -5.323  1.00 41.64  ? 162  PRO C CA  1 
ATOM   1271  C C   . PRO A  1 161 ? 27.823  29.438  -5.397  1.00 44.48  ? 162  PRO C C   1 
ATOM   1272  O O   . PRO A  1 161 ? 27.961  28.820  -4.342  1.00 45.56  ? 162  PRO C O   1 
ATOM   1273  C CB  . PRO A  1 161 ? 29.138  31.585  -5.428  1.00 40.06  ? 162  PRO C CB  1 
ATOM   1274  C CG  . PRO A  1 161 ? 29.209  32.592  -4.335  1.00 41.75  ? 162  PRO C CG  1 
ATOM   1275  C CD  . PRO A  1 161 ? 28.315  32.110  -3.250  1.00 46.73  ? 162  PRO C CD  1 
ATOM   1276  N N   . THR A  1 162 ? 27.759  28.857  -6.594  1.00 45.32  ? 163  THR C N   1 
ATOM   1277  C CA  . THR A  1 162 ? 27.874  27.409  -6.758  1.00 42.15  ? 163  THR C CA  1 
ATOM   1278  C C   . THR A  1 162 ? 29.333  27.016  -6.510  1.00 43.27  ? 163  THR C C   1 
ATOM   1279  O O   . THR A  1 162 ? 30.248  27.642  -7.041  1.00 40.87  ? 163  THR C O   1 
ATOM   1280  C CB  . THR A  1 162 ? 27.403  26.926  -8.163  1.00 41.32  ? 163  THR C CB  1 
ATOM   1281  O OG1 . THR A  1 162 ? 25.982  27.083  -8.283  1.00 47.80  ? 163  THR C OG1 1 
ATOM   1282  C CG2 . THR A  1 162 ? 27.731  25.462  -8.377  1.00 44.40  ? 163  THR C CG2 1 
ATOM   1283  N N   . ILE A  1 163 ? 29.527  25.999  -5.667  1.00 43.52  ? 164  ILE C N   1 
ATOM   1284  C CA  . ILE A  1 163 ? 30.843  25.479  -5.286  1.00 40.00  ? 164  ILE C CA  1 
ATOM   1285  C C   . ILE A  1 163 ? 31.267  24.375  -6.260  1.00 41.94  ? 164  ILE C C   1 
ATOM   1286  O O   . ILE A  1 163 ? 30.479  23.485  -6.558  1.00 42.05  ? 164  ILE C O   1 
ATOM   1287  C CB  . ILE A  1 163 ? 30.813  24.919  -3.806  1.00 41.43  ? 164  ILE C CB  1 
ATOM   1288  C CG1 . ILE A  1 163 ? 30.448  26.041  -2.824  1.00 44.55  ? 164  ILE C CG1 1 
ATOM   1289  C CG2 . ILE A  1 163 ? 32.133  24.272  -3.422  1.00 38.96  ? 164  ILE C CG2 1 
ATOM   1290  C CD1 . ILE A  1 163 ? 30.322  25.652  -1.345  1.00 42.31  ? 164  ILE C CD1 1 
ATOM   1291  N N   . LYS A  1 164 ? 32.473  24.475  -6.817  1.00 42.02  ? 165  LYS C N   1 
ATOM   1292  C CA  . LYS A  1 164 ? 33.059  23.376  -7.588  1.00 38.36  ? 165  LYS C CA  1 
ATOM   1293  C C   . LYS A  1 164 ? 34.469  23.078  -7.113  1.00 43.28  ? 165  LYS C C   1 
ATOM   1294  O O   . LYS A  1 164 ? 35.395  23.795  -7.437  1.00 50.50  ? 165  LYS C O   1 
ATOM   1295  C CB  . LYS A  1 164 ? 33.094  23.666  -9.086  1.00 39.94  ? 165  LYS C CB  1 
ATOM   1296  C CG  . LYS A  1 164 ? 31.739  23.602  -9.776  1.00 58.72  ? 165  LYS C CG  1 
ATOM   1297  C CD  . LYS A  1 164 ? 31.838  23.885  -11.287 1.00 62.68  ? 165  LYS C CD  1 
ATOM   1298  C CE  . LYS A  1 164 ? 30.453  23.852  -11.956 1.00 71.23  ? 165  LYS C CE  1 
ATOM   1299  N NZ  . LYS A  1 164 ? 30.505  24.235  -13.400 1.00 77.73  ? 165  LYS C NZ  1 
ATOM   1300  N N   . ARG A  1 165 ? 34.646  22.007  -6.358  1.00 44.02  ? 166  ARG C N   1 
ATOM   1301  C CA  . ARG A  1 165 ? 35.950  21.738  -5.782  1.00 45.58  ? 166  ARG C CA  1 
ATOM   1302  C C   . ARG A  1 165 ? 36.307  20.290  -6.047  1.00 42.51  ? 166  ARG C C   1 
ATOM   1303  O O   . ARG A  1 165 ? 35.421  19.431  -6.068  1.00 44.30  ? 166  ARG C O   1 
ATOM   1304  C CB  . ARG A  1 165 ? 35.952  22.024  -4.275  1.00 50.46  ? 166  ARG C CB  1 
ATOM   1305  C CG  . ARG A  1 165 ? 37.345  22.072  -3.687  1.00 54.27  ? 166  ARG C CG  1 
ATOM   1306  C CD  . ARG A  1 165 ? 37.342  22.527  -2.248  1.00 61.54  ? 166  ARG C CD  1 
ATOM   1307  N NE  . ARG A  1 165 ? 37.140  23.969  -2.100  1.00 68.46  ? 166  ARG C NE  1 
ATOM   1308  C CZ  . ARG A  1 165 ? 38.115  24.859  -1.938  1.00 65.90  ? 166  ARG C CZ  1 
ATOM   1309  N NH1 . ARG A  1 165 ? 39.384  24.468  -1.939  1.00 64.97  ? 166  ARG C NH1 1 
ATOM   1310  N NH2 . ARG A  1 165 ? 37.816  26.145  -1.795  1.00 62.08  ? 166  ARG C NH2 1 
ATOM   1311  N N   . SER A  1 166 ? 37.597  20.010  -6.214  1.00 46.59  ? 167  SER C N   1 
ATOM   1312  C CA  . SER A  1 166 ? 38.056  18.644  -6.481  1.00 40.90  ? 167  SER C CA  1 
ATOM   1313  C C   . SER A  1 166 ? 39.365  18.345  -5.727  1.00 39.63  ? 167  SER C C   1 
ATOM   1314  O O   . SER A  1 166 ? 40.149  19.252  -5.481  1.00 41.01  ? 167  SER C O   1 
ATOM   1315  C CB  . SER A  1 166 ? 38.239  18.434  -7.976  1.00 33.77  ? 167  SER C CB  1 
ATOM   1316  O OG  . SER A  1 166 ? 39.592  18.178  -8.266  1.00 40.06  ? 167  SER C OG  1 
ATOM   1317  N N   . TYR A  1 167 ? 39.620  17.073  -5.409  1.00 40.41  ? 168  TYR C N   1 
ATOM   1318  C CA  . TYR A  1 167 ? 40.859  16.672  -4.717  1.00 39.09  ? 168  TYR C CA  1 
ATOM   1319  C C   . TYR A  1 167 ? 41.431  15.404  -5.302  1.00 39.01  ? 168  TYR C C   1 
ATOM   1320  O O   . TYR A  1 167 ? 40.723  14.403  -5.385  1.00 43.95  ? 168  TYR C O   1 
ATOM   1321  C CB  . TYR A  1 167 ? 40.639  16.435  -3.209  1.00 34.88  ? 168  TYR C CB  1 
ATOM   1322  C CG  . TYR A  1 167 ? 41.877  15.800  -2.550  1.00 44.89  ? 168  TYR C CG  1 
ATOM   1323  C CD1 . TYR A  1 167 ? 42.946  16.574  -2.102  1.00 38.96  ? 168  TYR C CD1 1 
ATOM   1324  C CD2 . TYR A  1 167 ? 41.987  14.402  -2.419  1.00 45.60  ? 168  TYR C CD2 1 
ATOM   1325  C CE1 . TYR A  1 167 ? 44.075  15.985  -1.528  1.00 41.01  ? 168  TYR C CE1 1 
ATOM   1326  C CE2 . TYR A  1 167 ? 43.113  13.809  -1.858  1.00 44.00  ? 168  TYR C CE2 1 
ATOM   1327  C CZ  . TYR A  1 167 ? 44.153  14.601  -1.406  1.00 44.09  ? 168  TYR C CZ  1 
ATOM   1328  O OH  . TYR A  1 167 ? 45.263  13.996  -0.837  1.00 42.10  ? 168  TYR C OH  1 
ATOM   1329  N N   . ASN A  1 168 ? 42.728  15.424  -5.626  1.00 39.72  ? 169  ASN C N   1 
ATOM   1330  C CA  . ASN A  1 168 ? 43.423  14.251  -6.183  1.00 41.91  ? 169  ASN C CA  1 
ATOM   1331  C C   . ASN A  1 168 ? 44.357  13.560  -5.162  1.00 46.12  ? 169  ASN C C   1 
ATOM   1332  O O   . ASN A  1 168 ? 45.285  14.167  -4.625  1.00 47.69  ? 169  ASN C O   1 
ATOM   1333  C CB  . ASN A  1 168 ? 44.188  14.688  -7.442  1.00 39.82  ? 169  ASN C CB  1 
ATOM   1334  C CG  . ASN A  1 168 ? 44.863  13.536  -8.185  1.00 48.35  ? 169  ASN C CG  1 
ATOM   1335  O OD1 . ASN A  1 168 ? 45.669  12.802  -7.617  1.00 48.80  ? 169  ASN C OD1 1 
ATOM   1336  N ND2 . ASN A  1 168 ? 44.550  13.395  -9.481  1.00 52.38  ? 169  ASN C ND2 1 
ATOM   1337  N N   . ASN A  1 169 ? 44.096  12.277  -4.917  1.00 44.22  ? 170  ASN C N   1 
ATOM   1338  C CA  . ASN A  1 169 ? 44.863  11.484  -3.966  1.00 40.73  ? 170  ASN C CA  1 
ATOM   1339  C C   . ASN A  1 169 ? 46.221  11.063  -4.485  1.00 45.14  ? 170  ASN C C   1 
ATOM   1340  O O   . ASN A  1 169 ? 46.423  9.926   -4.931  1.00 41.84  ? 170  ASN C O   1 
ATOM   1341  C CB  . ASN A  1 169 ? 44.070  10.242  -3.582  1.00 38.40  ? 170  ASN C CB  1 
ATOM   1342  C CG  . ASN A  1 169 ? 44.762  9.411   -2.531  1.00 42.03  ? 170  ASN C CG  1 
ATOM   1343  O OD1 . ASN A  1 169 ? 45.709  9.864   -1.889  1.00 42.88  ? 170  ASN C OD1 1 
ATOM   1344  N ND2 . ASN A  1 169 ? 44.304  8.167   -2.361  1.00 42.45  ? 170  ASN C ND2 1 
ATOM   1345  N N   . THR A  1 170 ? 47.171  11.974  -4.334  1.00 49.12  ? 171  THR C N   1 
ATOM   1346  C CA  . THR A  1 170 ? 48.543  11.760  -4.782  1.00 50.17  ? 171  THR C CA  1 
ATOM   1347  C C   . THR A  1 170 ? 49.349  10.946  -3.770  1.00 49.14  ? 171  THR C C   1 
ATOM   1348  O O   . THR A  1 170 ? 50.562  10.809  -3.907  1.00 51.47  ? 171  THR C O   1 
ATOM   1349  C CB  . THR A  1 170 ? 49.259  13.105  -5.025  1.00 48.22  ? 171  THR C CB  1 
ATOM   1350  O OG1 . THR A  1 170 ? 49.200  13.893  -3.821  1.00 45.92  ? 171  THR C OG1 1 
ATOM   1351  C CG2 . THR A  1 170 ? 48.563  13.871  -6.115  1.00 49.89  ? 171  THR C CG2 1 
ATOM   1352  N N   . ASN A  1 171 ? 48.679  10.435  -2.741  1.00 46.52  ? 172  ASN C N   1 
ATOM   1353  C CA  . ASN A  1 171 ? 49.339  9.575   -1.776  1.00 46.14  ? 172  ASN C CA  1 
ATOM   1354  C C   . ASN A  1 171 ? 49.349  8.164   -2.307  1.00 47.84  ? 172  ASN C C   1 
ATOM   1355  O O   . ASN A  1 171 ? 48.535  7.807   -3.163  1.00 49.89  ? 172  ASN C O   1 
ATOM   1356  C CB  . ASN A  1 171 ? 48.644  9.618   -0.411  1.00 45.83  ? 172  ASN C CB  1 
ATOM   1357  C CG  . ASN A  1 171 ? 48.524  11.022  0.140   1.00 47.97  ? 172  ASN C CG  1 
ATOM   1358  O OD1 . ASN A  1 171 ? 49.478  11.561  0.709   1.00 49.49  ? 172  ASN C OD1 1 
ATOM   1359  N ND2 . ASN A  1 171 ? 47.338  11.616  0.002   1.00 49.71  ? 172  ASN C ND2 1 
ATOM   1360  N N   . GLN A  1 172 ? 50.236  7.340   -1.780  1.00 44.19  ? 173  GLN C N   1 
ATOM   1361  C CA  . GLN A  1 172 ? 50.294  5.964   -2.244  1.00 44.42  ? 173  GLN C CA  1 
ATOM   1362  C C   . GLN A  1 172 ? 49.172  5.114   -1.610  1.00 48.78  ? 173  GLN C C   1 
ATOM   1363  O O   . GLN A  1 172 ? 48.740  4.115   -2.200  1.00 46.54  ? 173  GLN C O   1 
ATOM   1364  C CB  . GLN A  1 172 ? 51.685  5.387   -1.979  1.00 42.22  ? 173  GLN C CB  1 
ATOM   1365  C CG  . GLN A  1 172 ? 51.947  4.028   -2.607  1.00 46.78  ? 173  GLN C CG  1 
ATOM   1366  C CD  . GLN A  1 172 ? 51.987  4.086   -4.113  1.00 50.86  ? 173  GLN C CD  1 
ATOM   1367  O OE1 . GLN A  1 172 ? 52.384  5.102   -4.695  1.00 53.29  ? 173  GLN C OE1 1 
ATOM   1368  N NE2 . GLN A  1 172 ? 51.581  2.993   -4.760  1.00 47.36  ? 173  GLN C NE2 1 
ATOM   1369  N N   . GLU A  1 173 ? 48.716  5.482   -0.406  1.00 47.04  ? 174  GLU C N   1 
ATOM   1370  C CA  . GLU A  1 173 ? 47.669  4.692   0.264   1.00 46.32  ? 174  GLU C CA  1 
ATOM   1371  C C   . GLU A  1 173 ? 46.243  5.252   0.038   1.00 44.04  ? 174  GLU C C   1 
ATOM   1372  O O   . GLU A  1 173 ? 46.080  6.417   -0.347  1.00 40.30  ? 174  GLU C O   1 
ATOM   1373  C CB  . GLU A  1 173 ? 47.972  4.554   1.769   1.00 40.83  ? 174  GLU C CB  1 
ATOM   1374  C CG  . GLU A  1 173 ? 48.358  5.821   2.499   1.00 43.23  ? 174  GLU C CG  1 
ATOM   1375  C CD  . GLU A  1 173 ? 49.840  6.151   2.431   1.00 49.65  ? 174  GLU C CD  1 
ATOM   1376  O OE1 . GLU A  1 173 ? 50.629  5.394   3.031   1.00 50.59  ? 174  GLU C OE1 1 
ATOM   1377  O OE2 . GLU A  1 173 ? 50.200  7.196   1.825   1.00 51.42  ? 174  GLU C OE2 1 
ATOM   1378  N N   . ASP A  1 174 ? 45.222  4.428   0.317   1.00 40.84  ? 175  ASP C N   1 
ATOM   1379  C CA  . ASP A  1 174 ? 43.820  4.818   0.096   1.00 36.60  ? 175  ASP C CA  1 
ATOM   1380  C C   . ASP A  1 174 ? 43.348  5.814   1.162   1.00 38.56  ? 175  ASP C C   1 
ATOM   1381  O O   . ASP A  1 174 ? 43.852  5.824   2.308   1.00 35.24  ? 175  ASP C O   1 
ATOM   1382  C CB  . ASP A  1 174 ? 42.877  3.601   0.149   1.00 36.99  ? 175  ASP C CB  1 
ATOM   1383  C CG  . ASP A  1 174 ? 43.105  2.590   -0.974  1.00 42.13  ? 175  ASP C CG  1 
ATOM   1384  O OD1 . ASP A  1 174 ? 43.647  2.940   -2.057  1.00 43.07  ? 175  ASP C OD1 1 
ATOM   1385  O OD2 . ASP A  1 174 ? 42.699  1.426   -0.746  1.00 41.40  ? 175  ASP C OD2 1 
ATOM   1386  N N   . LEU A  1 175 ? 42.348  6.615   0.803   1.00 34.42  ? 176  LEU C N   1 
ATOM   1387  C CA  . LEU A  1 175 ? 41.835  7.662   1.690   1.00 31.80  ? 176  LEU C CA  1 
ATOM   1388  C C   . LEU A  1 175 ? 40.381  7.460   2.097   1.00 30.95  ? 176  LEU C C   1 
ATOM   1389  O O   . LEU A  1 175 ? 39.532  7.223   1.242   1.00 30.78  ? 176  LEU C O   1 
ATOM   1390  C CB  . LEU A  1 175 ? 41.945  9.017   1.011   1.00 35.55  ? 176  LEU C CB  1 
ATOM   1391  C CG  . LEU A  1 175 ? 43.072  9.962   1.371   1.00 40.13  ? 176  LEU C CG  1 
ATOM   1392  C CD1 . LEU A  1 175 ? 42.778  11.250  0.618   1.00 42.22  ? 176  LEU C CD1 1 
ATOM   1393  C CD2 . LEU A  1 175 ? 43.153  10.204  2.869   1.00 31.97  ? 176  LEU C CD2 1 
ATOM   1394  N N   . LEU A  1 176 ? 40.083  7.597   3.387   1.00 31.50  ? 177  LEU C N   1 
ATOM   1395  C CA  . LEU A  1 176 ? 38.687  7.664   3.845   1.00 27.92  ? 177  LEU C CA  1 
ATOM   1396  C C   . LEU A  1 176 ? 38.192  9.127   3.899   1.00 28.86  ? 177  LEU C C   1 
ATOM   1397  O O   . LEU A  1 176 ? 38.707  9.944   4.687   1.00 24.34  ? 177  LEU C O   1 
ATOM   1398  C CB  . LEU A  1 176 ? 38.527  7.007   5.211   1.00 22.27  ? 177  LEU C CB  1 
ATOM   1399  C CG  . LEU A  1 176 ? 37.150  7.141   5.873   1.00 22.47  ? 177  LEU C CG  1 
ATOM   1400  C CD1 . LEU A  1 176 ? 36.136  6.443   4.986   1.00 26.84  ? 177  LEU C CD1 1 
ATOM   1401  C CD2 . LEU A  1 176 ? 37.129  6.508   7.248   1.00 19.11  ? 177  LEU C CD2 1 
ATOM   1402  N N   . VAL A  1 177 ? 37.212  9.453   3.046   1.00 26.16  ? 178  VAL C N   1 
ATOM   1403  C CA  . VAL A  1 177 ? 36.687  10.824  2.944   1.00 27.46  ? 178  VAL C CA  1 
ATOM   1404  C C   . VAL A  1 177 ? 35.239  10.886  3.498   1.00 28.26  ? 178  VAL C C   1 
ATOM   1405  O O   . VAL A  1 177 ? 34.474  9.923   3.330   1.00 30.17  ? 178  VAL C O   1 
ATOM   1406  C CB  . VAL A  1 177 ? 36.761  11.315  1.477   1.00 26.62  ? 178  VAL C CB  1 
ATOM   1407  C CG1 . VAL A  1 177 ? 36.520  12.800  1.392   1.00 24.77  ? 178  VAL C CG1 1 
ATOM   1408  C CG2 . VAL A  1 177 ? 38.143  10.998  0.909   1.00 25.62  ? 178  VAL C CG2 1 
ATOM   1409  N N   . LEU A  1 178 ? 34.915  11.947  4.251   1.00 26.90  ? 179  LEU C N   1 
ATOM   1410  C CA  . LEU A  1 178 ? 33.602  12.109  4.906   1.00 24.76  ? 179  LEU C CA  1 
ATOM   1411  C C   . LEU A  1 178 ? 32.929  13.447  4.564   1.00 28.48  ? 179  LEU C C   1 
ATOM   1412  O O   . LEU A  1 178 ? 33.617  14.464  4.434   1.00 30.17  ? 179  LEU C O   1 
ATOM   1413  C CB  . LEU A  1 178 ? 33.746  11.991  6.430   1.00 22.63  ? 179  LEU C CB  1 
ATOM   1414  C CG  . LEU A  1 178 ? 34.557  10.811  6.988   1.00 26.01  ? 179  LEU C CG  1 
ATOM   1415  C CD1 . LEU A  1 178 ? 34.982  11.033  8.455   1.00 23.82  ? 179  LEU C CD1 1 
ATOM   1416  C CD2 . LEU A  1 178 ? 33.786  9.501   6.864   1.00 26.24  ? 179  LEU C CD2 1 
ATOM   1417  N N   . TRP A  1 179 ? 31.601  13.459  4.429   1.00 25.11  ? 180  TRP C N   1 
ATOM   1418  C CA  . TRP A  1 179 ? 30.860  14.710  4.197   1.00 24.83  ? 180  TRP C CA  1 
ATOM   1419  C C   . TRP A  1 179 ? 29.389  14.566  4.585   1.00 31.26  ? 180  TRP C C   1 
ATOM   1420  O O   . TRP A  1 179 ? 28.917  13.438  4.893   1.00 28.44  ? 180  TRP C O   1 
ATOM   1421  C CB  . TRP A  1 179 ? 30.954  15.146  2.735   1.00 26.69  ? 180  TRP C CB  1 
ATOM   1422  C CG  . TRP A  1 179 ? 30.218  14.253  1.775   1.00 27.08  ? 180  TRP C CG  1 
ATOM   1423  C CD1 . TRP A  1 179 ? 28.940  14.419  1.305   1.00 24.16  ? 180  TRP C CD1 1 
ATOM   1424  C CD2 . TRP A  1 179 ? 30.718  13.049  1.170   1.00 25.65  ? 180  TRP C CD2 1 
ATOM   1425  N NE1 . TRP A  1 179 ? 28.621  13.388  0.437   1.00 24.76  ? 180  TRP C NE1 1 
ATOM   1426  C CE2 . TRP A  1 179 ? 29.697  12.542  0.334   1.00 24.08  ? 180  TRP C CE2 1 
ATOM   1427  C CE3 . TRP A  1 179 ? 31.929  12.354  1.251   1.00 24.44  ? 180  TRP C CE3 1 
ATOM   1428  C CZ2 . TRP A  1 179 ? 29.858  11.366  -0.416  1.00 27.11  ? 180  TRP C CZ2 1 
ATOM   1429  C CZ3 . TRP A  1 179 ? 32.088  11.171  0.486   1.00 24.57  ? 180  TRP C CZ3 1 
ATOM   1430  C CH2 . TRP A  1 179 ? 31.061  10.697  -0.325  1.00 22.78  ? 180  TRP C CH2 1 
ATOM   1431  N N   . GLY A  1 180 ? 28.653  15.680  4.523   1.00 26.03  ? 181  GLY C N   1 
ATOM   1432  C CA  . GLY A  1 180 ? 27.274  15.671  4.979   1.00 27.82  ? 181  GLY C CA  1 
ATOM   1433  C C   . GLY A  1 180 ? 26.363  16.643  4.252   1.00 30.78  ? 181  GLY C C   1 
ATOM   1434  O O   . GLY A  1 180 ? 26.819  17.422  3.414   1.00 33.17  ? 181  GLY C O   1 
ATOM   1435  N N   . ILE A  1 181 ? 25.070  16.588  4.576   1.00 31.14  ? 182  ILE C N   1 
ATOM   1436  C CA  . ILE A  1 181 ? 24.055  17.502  4.027   1.00 36.80  ? 182  ILE C CA  1 
ATOM   1437  C C   . ILE A  1 181 ? 23.105  17.950  5.149   1.00 37.51  ? 182  ILE C C   1 
ATOM   1438  O O   . ILE A  1 181 ? 22.680  17.132  5.974   1.00 34.82  ? 182  ILE C O   1 
ATOM   1439  C CB  . ILE A  1 181 ? 23.215  16.828  2.882   1.00 37.68  ? 182  ILE C CB  1 
ATOM   1440  C CG1 . ILE A  1 181 ? 22.156  17.790  2.331   1.00 38.70  ? 182  ILE C CG1 1 
ATOM   1441  C CG2 . ILE A  1 181 ? 22.517  15.569  3.386   1.00 27.62  ? 182  ILE C CG2 1 
ATOM   1442  C CD1 . ILE A  1 181 ? 21.274  17.179  1.241   1.00 34.55  ? 182  ILE C CD1 1 
ATOM   1443  N N   . HIS A  1 182 ? 22.731  19.229  5.150   1.00 35.45  ? 183  HIS C N   1 
ATOM   1444  C CA  . HIS A  1 182 ? 21.824  19.747  6.169   1.00 35.75  ? 183  HIS C CA  1 
ATOM   1445  C C   . HIS A  1 182 ? 20.364  19.850  5.718   1.00 36.91  ? 183  HIS C C   1 
ATOM   1446  O O   . HIS A  1 182 ? 20.082  20.527  4.729   1.00 42.43  ? 183  HIS C O   1 
ATOM   1447  C CB  . HIS A  1 182 ? 22.294  21.129  6.623   1.00 38.93  ? 183  HIS C CB  1 
ATOM   1448  C CG  . HIS A  1 182 ? 21.395  21.755  7.644   1.00 45.64  ? 183  HIS C CG  1 
ATOM   1449  N ND1 . HIS A  1 182 ? 20.860  23.017  7.492   1.00 45.36  ? 183  HIS C ND1 1 
ATOM   1450  C CD2 . HIS A  1 182 ? 20.903  21.274  8.815   1.00 44.81  ? 183  HIS C CD2 1 
ATOM   1451  C CE1 . HIS A  1 182 ? 20.095  23.293  8.535   1.00 48.85  ? 183  HIS C CE1 1 
ATOM   1452  N NE2 . HIS A  1 182 ? 20.105  22.253  9.352   1.00 46.33  ? 183  HIS C NE2 1 
ATOM   1453  N N   . HIS A  1 183 ? 19.446  19.233  6.473   1.00 36.69  ? 184  HIS C N   1 
ATOM   1454  C CA  . HIS A  1 183 ? 17.998  19.319  6.207   1.00 41.69  ? 184  HIS C CA  1 
ATOM   1455  C C   . HIS A  1 183 ? 17.322  20.316  7.135   1.00 45.56  ? 184  HIS C C   1 
ATOM   1456  O O   . HIS A  1 183 ? 17.114  19.996  8.294   1.00 47.56  ? 184  HIS C O   1 
ATOM   1457  C CB  . HIS A  1 183 ? 17.292  17.976  6.405   1.00 38.28  ? 184  HIS C CB  1 
ATOM   1458  C CG  . HIS A  1 183 ? 17.872  16.856  5.610   1.00 40.88  ? 184  HIS C CG  1 
ATOM   1459  N ND1 . HIS A  1 183 ? 17.694  16.741  4.248   1.00 44.04  ? 184  HIS C ND1 1 
ATOM   1460  C CD2 . HIS A  1 183 ? 18.602  15.779  5.988   1.00 42.08  ? 184  HIS C CD2 1 
ATOM   1461  C CE1 . HIS A  1 183 ? 18.315  15.656  3.815   1.00 40.70  ? 184  HIS C CE1 1 
ATOM   1462  N NE2 . HIS A  1 183 ? 18.871  15.052  4.851   1.00 43.27  ? 184  HIS C NE2 1 
ATOM   1463  N N   . PRO A  1 184 ? 16.959  21.513  6.630   1.00 51.41  ? 185  PRO C N   1 
ATOM   1464  C CA  . PRO A  1 184 ? 16.299  22.531  7.469   1.00 48.41  ? 185  PRO C CA  1 
ATOM   1465  C C   . PRO A  1 184 ? 14.823  22.226  7.848   1.00 49.59  ? 185  PRO C C   1 
ATOM   1466  O O   . PRO A  1 184 ? 14.216  21.248  7.378   1.00 46.07  ? 185  PRO C O   1 
ATOM   1467  C CB  . PRO A  1 184 ? 16.395  23.806  6.610   1.00 49.05  ? 185  PRO C CB  1 
ATOM   1468  C CG  . PRO A  1 184 ? 16.530  23.335  5.212   1.00 49.85  ? 185  PRO C CG  1 
ATOM   1469  C CD  . PRO A  1 184 ? 17.230  21.996  5.258   1.00 48.60  ? 185  PRO C CD  1 
ATOM   1470  N N   . ASN A  1 185 ? 14.245  23.113  8.662   1.00 55.06  ? 186  ASN C N   1 
ATOM   1471  C CA  . ASN A  1 185 ? 12.911  22.911  9.235   1.00 53.22  ? 186  ASN C CA  1 
ATOM   1472  C C   . ASN A  1 185 ? 11.773  23.577  8.438   1.00 51.55  ? 186  ASN C C   1 
ATOM   1473  O O   . ASN A  1 185 ? 10.647  23.060  8.388   1.00 48.26  ? 186  ASN C O   1 
ATOM   1474  C CB  . ASN A  1 185 ? 12.908  23.430  10.681  1.00 55.20  ? 186  ASN C CB  1 
ATOM   1475  C CG  . ASN A  1 185 ? 11.529  23.324  11.356  1.00 63.28  ? 186  ASN C CG  1 
ATOM   1476  O OD1 . ASN A  1 185 ? 11.135  22.255  11.838  1.00 63.04  ? 186  ASN C OD1 1 
ATOM   1477  N ND2 . ASN A  1 185 ? 10.804  24.445  11.405  1.00 54.75  ? 186  ASN C ND2 1 
ATOM   1478  N N   . ASP A  1 186 ? 12.081  24.695  7.783   1.00 53.18  ? 187  ASP C N   1 
ATOM   1479  C CA  . ASP A  1 186 ? 11.093  25.423  6.977   1.00 53.46  ? 187  ASP C CA  1 
ATOM   1480  C C   . ASP A  1 186 ? 11.750  26.312  5.901   1.00 54.83  ? 187  ASP C C   1 
ATOM   1481  O O   . ASP A  1 186 ? 12.981  26.524  5.892   1.00 46.72  ? 187  ASP C O   1 
ATOM   1482  C CB  . ASP A  1 186 ? 10.183  26.293  7.868   1.00 48.74  ? 187  ASP C CB  1 
ATOM   1483  C CG  . ASP A  1 186 ? 10.967  27.303  8.710   1.00 56.66  ? 187  ASP C CG  1 
ATOM   1484  O OD1 . ASP A  1 186 ? 11.637  28.189  8.128   1.00 51.12  ? 187  ASP C OD1 1 
ATOM   1485  O OD2 . ASP A  1 186 ? 10.893  27.225  9.958   1.00 65.60  ? 187  ASP C OD2 1 
ATOM   1486  N N   . ALA A  1 187 ? 10.913  26.840  5.006   1.00 52.40  ? 188  ALA C N   1 
ATOM   1487  C CA  . ALA A  1 187 ? 11.387  27.607  3.867   1.00 46.94  ? 188  ALA C CA  1 
ATOM   1488  C C   . ALA A  1 187 ? 12.159  28.863  4.284   1.00 50.08  ? 188  ALA C C   1 
ATOM   1489  O O   . ALA A  1 187 ? 13.107  29.270  3.609   1.00 53.20  ? 188  ALA C O   1 
ATOM   1490  C CB  . ALA A  1 187 ? 10.211  27.982  2.992   1.00 42.09  ? 188  ALA C CB  1 
ATOM   1491  N N   . THR A  1 188 ? 11.801  29.421  5.438   1.00 49.01  ? 189  THR C N   1 
ATOM   1492  C CA  . THR A  1 188 ? 12.389  30.663  5.937   1.00 50.37  ? 189  THR C CA  1 
ATOM   1493  C C   . THR A  1 188 ? 13.825  30.487  6.409   1.00 53.53  ? 189  THR C C   1 
ATOM   1494  O O   . THR A  1 188 ? 14.712  31.284  6.072   1.00 55.27  ? 189  THR C O   1 
ATOM   1495  C CB  . THR A  1 188 ? 11.569  31.232  7.128   1.00 57.00  ? 189  THR C CB  1 
ATOM   1496  O OG1 . THR A  1 188 ? 10.216  31.481  6.713   1.00 54.94  ? 189  THR C OG1 1 
ATOM   1497  C CG2 . THR A  1 188 ? 12.199  32.523  7.648   1.00 52.93  ? 189  THR C CG2 1 
ATOM   1498  N N   . GLU A  1 189 ? 14.032  29.439  7.203   1.00 52.56  ? 190  GLU C N   1 
ATOM   1499  C CA  . GLU A  1 189 ? 15.350  29.041  7.678   1.00 49.77  ? 190  GLU C CA  1 
ATOM   1500  C C   . GLU A  1 189 ? 16.275  28.697  6.506   1.00 49.78  ? 190  GLU C C   1 
ATOM   1501  O O   . GLU A  1 189 ? 17.486  28.967  6.555   1.00 48.53  ? 190  GLU C O   1 
ATOM   1502  C CB  . GLU A  1 189 ? 15.224  27.840  8.615   1.00 53.08  ? 190  GLU C CB  1 
ATOM   1503  C CG  . GLU A  1 189 ? 16.546  27.273  9.120   1.00 57.50  ? 190  GLU C CG  1 
ATOM   1504  C CD  . GLU A  1 189 ? 16.343  26.005  9.941   1.00 65.14  ? 190  GLU C CD  1 
ATOM   1505  O OE1 . GLU A  1 189 ? 15.265  25.845  10.559  1.00 70.27  ? 190  GLU C OE1 1 
ATOM   1506  O OE2 . GLU A  1 189 ? 17.248  25.146  9.933   1.00 66.07  ? 190  GLU C OE2 1 
ATOM   1507  N N   . GLN A  1 190 ? 15.698  28.091  5.463   1.00 47.72  ? 191  GLN C N   1 
ATOM   1508  C CA  . GLN A  1 190 ? 16.463  27.737  4.265   1.00 51.48  ? 191  GLN C CA  1 
ATOM   1509  C C   . GLN A  1 190 ? 17.118  28.928  3.555   1.00 50.03  ? 191  GLN C C   1 
ATOM   1510  O O   . GLN A  1 190 ? 18.303  28.874  3.197   1.00 47.90  ? 191  GLN C O   1 
ATOM   1511  C CB  . GLN A  1 190 ? 15.554  26.986  3.272   1.00 50.27  ? 191  GLN C CB  1 
ATOM   1512  C CG  . GLN A  1 190 ? 16.140  26.850  1.865   1.00 49.00  ? 191  GLN C CG  1 
ATOM   1513  C CD  . GLN A  1 190 ? 17.279  25.842  1.806   1.00 47.84  ? 191  GLN C CD  1 
ATOM   1514  O OE1 . GLN A  1 190 ? 17.447  25.017  2.718   1.00 44.46  ? 191  GLN C OE1 1 
ATOM   1515  N NE2 . GLN A  1 190 ? 18.077  25.911  0.736   1.00 39.87  ? 191  GLN C NE2 1 
ATOM   1516  N N   . THR A  1 191 ? 16.382  30.032  3.447   1.00 55.60  ? 192  THR C N   1 
ATOM   1517  C CA  . THR A  1 191 ? 16.874  31.198  2.713   1.00 55.06  ? 192  THR C CA  1 
ATOM   1518  C C   . THR A  1 191 ? 17.810  31.998  3.610   1.00 48.91  ? 192  THR C C   1 
ATOM   1519  O O   . THR A  1 191 ? 18.697  32.684  3.121   1.00 48.86  ? 192  THR C O   1 
ATOM   1520  C CB  . THR A  1 191 ? 15.712  32.094  2.157   1.00 56.08  ? 192  THR C CB  1 
ATOM   1521  O OG1 . THR A  1 191 ? 14.724  32.310  3.164   1.00 56.59  ? 192  THR C OG1 1 
ATOM   1522  C CG2 . THR A  1 191 ? 15.034  31.412  0.963   1.00 55.73  ? 192  THR C CG2 1 
ATOM   1523  N N   . ARG A  1 192 ? 17.636  31.900  4.925   1.00 47.69  ? 193  ARG C N   1 
ATOM   1524  C CA  . ARG A  1 192 ? 18.530  32.636  5.803   1.00 49.98  ? 193  ARG C CA  1 
ATOM   1525  C C   . ARG A  1 192 ? 19.945  32.035  5.796   1.00 54.92  ? 193  ARG C C   1 
ATOM   1526  O O   . ARG A  1 192 ? 20.935  32.763  5.869   1.00 55.21  ? 193  ARG C O   1 
ATOM   1527  C CB  . ARG A  1 192 ? 17.954  32.683  7.230   1.00 53.59  ? 193  ARG C CB  1 
ATOM   1528  C CG  . ARG A  1 192 ? 18.832  33.414  8.261   1.00 53.93  ? 193  ARG C CG  1 
ATOM   1529  C CD  . ARG A  1 192 ? 18.184  33.457  9.651   1.00 62.86  ? 193  ARG C CD  1 
ATOM   1530  N NE  . ARG A  1 192 ? 18.126  32.155  10.300  1.00 65.81  ? 193  ARG C NE  1 
ATOM   1531  C CZ  . ARG A  1 192 ? 19.136  31.624  10.984  1.00 68.91  ? 193  ARG C CZ  1 
ATOM   1532  N NH1 . ARG A  1 192 ? 20.285  32.286  11.102  1.00 58.95  ? 193  ARG C NH1 1 
ATOM   1533  N NH2 . ARG A  1 192 ? 19.000  30.425  11.543  1.00 70.76  ? 193  ARG C NH2 1 
ATOM   1534  N N   . LEU A  1 193 ? 20.050  30.725  5.586   1.00 56.70  ? 194  LEU C N   1 
ATOM   1535  C CA  . LEU A  1 193 ? 21.340  30.040  5.703   1.00 49.68  ? 194  LEU C CA  1 
ATOM   1536  C C   . LEU A  1 193 ? 22.121  29.981  4.393   1.00 48.87  ? 194  LEU C C   1 
ATOM   1537  O O   . LEU A  1 193 ? 23.355  30.176  4.387   1.00 43.14  ? 194  LEU C O   1 
ATOM   1538  C CB  . LEU A  1 193 ? 21.114  28.621  6.243   1.00 49.51  ? 194  LEU C CB  1 
ATOM   1539  C CG  . LEU A  1 193 ? 20.749  28.540  7.735   1.00 54.40  ? 194  LEU C CG  1 
ATOM   1540  C CD1 . LEU A  1 193 ? 20.500  27.119  8.214   1.00 47.44  ? 194  LEU C CD1 1 
ATOM   1541  C CD2 . LEU A  1 193 ? 21.837  29.193  8.574   1.00 55.49  ? 194  LEU C CD2 1 
ATOM   1542  N N   . TYR A  1 194 ? 21.393  29.717  3.298   1.00 49.68  ? 195  TYR C N   1 
ATOM   1543  C CA  . TYR A  1 194 ? 21.999  29.411  1.996   1.00 46.34  ? 195  TYR C CA  1 
ATOM   1544  C C   . TYR A  1 194 ? 21.475  30.271  0.822   1.00 53.26  ? 195  TYR C C   1 
ATOM   1545  O O   . TYR A  1 194 ? 21.949  30.140  -0.326  1.00 50.88  ? 195  TYR C O   1 
ATOM   1546  C CB  . TYR A  1 194 ? 21.786  27.923  1.688   1.00 41.67  ? 195  TYR C CB  1 
ATOM   1547  C CG  . TYR A  1 194 ? 22.043  27.011  2.875   1.00 42.60  ? 195  TYR C CG  1 
ATOM   1548  C CD1 . TYR A  1 194 ? 23.343  26.808  3.356   1.00 40.82  ? 195  TYR C CD1 1 
ATOM   1549  C CD2 . TYR A  1 194 ? 20.999  26.332  3.499   1.00 40.72  ? 195  TYR C CD2 1 
ATOM   1550  C CE1 . TYR A  1 194 ? 23.588  25.976  4.428   1.00 34.90  ? 195  TYR C CE1 1 
ATOM   1551  C CE2 . TYR A  1 194 ? 21.232  25.496  4.566   1.00 36.38  ? 195  TYR C CE2 1 
ATOM   1552  C CZ  . TYR A  1 194 ? 22.531  25.318  5.031   1.00 39.69  ? 195  TYR C CZ  1 
ATOM   1553  O OH  . TYR A  1 194 ? 22.775  24.483  6.115   1.00 41.47  ? 195  TYR C OH  1 
ATOM   1554  N N   . GLN A  1 195 ? 20.509  31.145  1.128   1.00 56.92  ? 196  GLN C N   1 
ATOM   1555  C CA  . GLN A  1 195 ? 19.901  32.119  0.192   1.00 53.59  ? 196  GLN C CA  1 
ATOM   1556  C C   . GLN A  1 195 ? 18.963  31.495  -0.861  1.00 50.55  ? 196  GLN C C   1 
ATOM   1557  O O   . GLN A  1 195 ? 17.798  31.874  -0.952  1.00 50.43  ? 196  GLN C O   1 
ATOM   1558  C CB  . GLN A  1 195 ? 20.988  32.942  -0.509  1.00 53.09  ? 196  GLN C CB  1 
ATOM   1559  C CG  . GLN A  1 195 ? 20.436  34.100  -1.314  1.00 60.23  ? 196  GLN C CG  1 
ATOM   1560  C CD  . GLN A  1 195 ? 19.833  35.191  -0.443  1.00 61.84  ? 196  GLN C CD  1 
ATOM   1561  O OE1 . GLN A  1 195 ? 20.379  35.555  0.606   1.00 58.37  ? 196  GLN C OE1 1 
ATOM   1562  N NE2 . GLN A  1 195 ? 18.680  35.696  -0.860  1.00 59.38  ? 196  GLN C NE2 1 
ATOM   1563  N N   . ASN A  1 196 ? 19.463  30.528  -1.625  1.00 50.88  ? 197  ASN C N   1 
ATOM   1564  C CA  . ASN A  1 196 ? 18.675  29.810  -2.634  1.00 48.19  ? 197  ASN C CA  1 
ATOM   1565  C C   . ASN A  1 196 ? 17.679  28.806  -2.045  1.00 47.48  ? 197  ASN C C   1 
ATOM   1566  O O   . ASN A  1 196 ? 18.018  28.040  -1.141  1.00 49.33  ? 197  ASN C O   1 
ATOM   1567  C CB  . ASN A  1 196 ? 19.612  29.067  -3.575  1.00 45.96  ? 197  ASN C CB  1 
ATOM   1568  C CG  . ASN A  1 196 ? 20.817  29.882  -3.923  1.00 49.68  ? 197  ASN C CG  1 
ATOM   1569  O OD1 . ASN A  1 196 ? 21.955  29.455  -3.684  1.00 47.92  ? 197  ASN C OD1 1 
ATOM   1570  N ND2 . ASN A  1 196 ? 20.587  31.093  -4.442  1.00 48.93  ? 197  ASN C ND2 1 
ATOM   1571  N N   . PRO A  1 197 ? 16.449  28.792  -2.571  1.00 48.46  ? 198  PRO C N   1 
ATOM   1572  C CA  . PRO A  1 197 ? 15.366  27.929  -2.072  1.00 45.05  ? 198  PRO C CA  1 
ATOM   1573  C C   . PRO A  1 197 ? 15.448  26.457  -2.529  1.00 44.09  ? 198  PRO C C   1 
ATOM   1574  O O   . PRO A  1 197 ? 14.963  25.574  -1.835  1.00 48.80  ? 198  PRO C O   1 
ATOM   1575  C CB  . PRO A  1 197 ? 14.111  28.606  -2.640  1.00 44.35  ? 198  PRO C CB  1 
ATOM   1576  C CG  . PRO A  1 197 ? 14.581  29.229  -3.924  1.00 43.43  ? 198  PRO C CG  1 
ATOM   1577  C CD  . PRO A  1 197 ? 15.999  29.682  -3.659  1.00 44.89  ? 198  PRO C CD  1 
ATOM   1578  N N   . THR A  1 198 ? 16.030  26.209  -3.696  1.00 46.33  ? 199  THR C N   1 
ATOM   1579  C CA  . THR A  1 198 ? 16.111  24.864  -4.268  1.00 48.24  ? 199  THR C CA  1 
ATOM   1580  C C   . THR A  1 198 ? 17.558  24.424  -4.570  1.00 46.62  ? 199  THR C C   1 
ATOM   1581  O O   . THR A  1 198 ? 18.203  24.915  -5.513  1.00 40.34  ? 199  THR C O   1 
ATOM   1582  C CB  . THR A  1 198 ? 15.256  24.773  -5.532  1.00 45.95  ? 199  THR C CB  1 
ATOM   1583  O OG1 . THR A  1 198 ? 13.894  25.012  -5.162  1.00 48.46  ? 199  THR C OG1 1 
ATOM   1584  C CG2 . THR A  1 198 ? 15.344  23.393  -6.125  1.00 42.52  ? 199  THR C CG2 1 
ATOM   1585  N N   . THR A  1 199 ? 18.050  23.497  -3.750  1.00 42.51  ? 200  THR C N   1 
ATOM   1586  C CA  . THR A  1 199 ? 19.469  23.158  -3.734  1.00 39.66  ? 200  THR C CA  1 
ATOM   1587  C C   . THR A  1 199 ? 19.754  21.658  -3.930  1.00 41.36  ? 200  THR C C   1 
ATOM   1588  O O   . THR A  1 199 ? 18.837  20.812  -3.927  1.00 38.62  ? 200  THR C O   1 
ATOM   1589  C CB  . THR A  1 199 ? 20.119  23.623  -2.405  1.00 42.32  ? 200  THR C CB  1 
ATOM   1590  O OG1 . THR A  1 199 ? 19.454  22.999  -1.299  1.00 39.46  ? 200  THR C OG1 1 
ATOM   1591  C CG2 . THR A  1 199 ? 20.010  25.130  -2.262  1.00 38.36  ? 200  THR C CG2 1 
ATOM   1592  N N   . TYR A  1 200 ? 21.043  21.358  -4.098  1.00 40.36  ? 201  TYR C N   1 
ATOM   1593  C CA  . TYR A  1 200 ? 21.540  20.018  -4.357  1.00 36.54  ? 201  TYR C CA  1 
ATOM   1594  C C   . TYR A  1 200 ? 23.021  19.871  -3.956  1.00 38.28  ? 201  TYR C C   1 
ATOM   1595  O O   . TYR A  1 200 ? 23.768  20.866  -3.832  1.00 35.81  ? 201  TYR C O   1 
ATOM   1596  C CB  . TYR A  1 200 ? 21.383  19.674  -5.853  1.00 35.08  ? 201  TYR C CB  1 
ATOM   1597  C CG  . TYR A  1 200 ? 22.344  20.466  -6.718  1.00 35.74  ? 201  TYR C CG  1 
ATOM   1598  C CD1 . TYR A  1 200 ? 22.018  21.741  -7.161  1.00 39.77  ? 201  TYR C CD1 1 
ATOM   1599  C CD2 . TYR A  1 200 ? 23.597  19.958  -7.059  1.00 36.95  ? 201  TYR C CD2 1 
ATOM   1600  C CE1 . TYR A  1 200 ? 22.905  22.486  -7.937  1.00 39.11  ? 201  TYR C CE1 1 
ATOM   1601  C CE2 . TYR A  1 200 ? 24.498  20.694  -7.830  1.00 34.96  ? 201  TYR C CE2 1 
ATOM   1602  C CZ  . TYR A  1 200 ? 24.144  21.958  -8.263  1.00 39.17  ? 201  TYR C CZ  1 
ATOM   1603  O OH  . TYR A  1 200 ? 25.028  22.692  -9.021  1.00 43.34  ? 201  TYR C OH  1 
ATOM   1604  N N   . ILE A  1 201 ? 23.449  18.617  -3.812  1.00 36.79  ? 202  ILE C N   1 
ATOM   1605  C CA  . ILE A  1 201 ? 24.872  18.279  -3.694  1.00 34.66  ? 202  ILE C CA  1 
ATOM   1606  C C   . ILE A  1 201 ? 25.200  17.101  -4.627  1.00 36.87  ? 202  ILE C C   1 
ATOM   1607  O O   . ILE A  1 201 ? 24.505  16.068  -4.641  1.00 33.41  ? 202  ILE C O   1 
ATOM   1608  C CB  . ILE A  1 201 ? 25.277  17.911  -2.279  1.00 30.72  ? 202  ILE C CB  1 
ATOM   1609  C CG1 . ILE A  1 201 ? 25.008  19.068  -1.343  1.00 31.36  ? 202  ILE C CG1 1 
ATOM   1610  C CG2 . ILE A  1 201 ? 26.747  17.553  -2.225  1.00 30.46  ? 202  ILE C CG2 1 
ATOM   1611  C CD1 . ILE A  1 201 ? 25.259  18.692  0.104   1.00 37.63  ? 202  ILE C CD1 1 
ATOM   1612  N N   . SER A  1 202 ? 26.225  17.290  -5.445  1.00 32.77  ? 203  SER C N   1 
ATOM   1613  C CA  . SER A  1 202 ? 26.697  16.243  -6.330  1.00 35.47  ? 203  SER C CA  1 
ATOM   1614  C C   . SER A  1 202 ? 28.085  15.760  -5.915  1.00 33.74  ? 203  SER C C   1 
ATOM   1615  O O   . SER A  1 202 ? 28.989  16.589  -5.654  1.00 31.20  ? 203  SER C O   1 
ATOM   1616  C CB  . SER A  1 202 ? 26.747  16.765  -7.772  1.00 38.20  ? 203  SER C CB  1 
ATOM   1617  O OG  . SER A  1 202 ? 25.457  16.747  -8.328  1.00 45.88  ? 203  SER C OG  1 
ATOM   1618  N N   . VAL A  1 203 ? 28.286  14.444  -5.901  1.00 27.56  ? 204  VAL C N   1 
ATOM   1619  C CA  . VAL A  1 203 ? 29.616  13.923  -5.608  1.00 29.70  ? 204  VAL C CA  1 
ATOM   1620  C C   . VAL A  1 203 ? 30.009  12.828  -6.578  1.00 28.06  ? 204  VAL C C   1 
ATOM   1621  O O   . VAL A  1 203 ? 29.262  11.878  -6.761  1.00 31.60  ? 204  VAL C O   1 
ATOM   1622  C CB  . VAL A  1 203 ? 29.743  13.372  -4.174  1.00 27.57  ? 204  VAL C CB  1 
ATOM   1623  C CG1 . VAL A  1 203 ? 31.207  12.999  -3.897  1.00 23.27  ? 204  VAL C CG1 1 
ATOM   1624  C CG2 . VAL A  1 203 ? 29.243  14.394  -3.151  1.00 25.15  ? 204  VAL C CG2 1 
ATOM   1625  N N   . GLY A  1 204 ? 31.187  12.962  -7.181  1.00 25.62  ? 205  GLY C N   1 
ATOM   1626  C CA  . GLY A  1 204 ? 31.667  12.004  -8.149  1.00 28.80  ? 205  GLY C CA  1 
ATOM   1627  C C   . GLY A  1 204 ? 33.097  11.491  -7.989  1.00 32.98  ? 205  GLY C C   1 
ATOM   1628  O O   . GLY A  1 204 ? 34.005  12.205  -7.553  1.00 34.12  ? 205  GLY C O   1 
ATOM   1629  N N   . THR A  1 205 ? 33.282  10.242  -8.412  1.00 30.18  ? 206  THR C N   1 
ATOM   1630  C CA  . THR A  1 205 ? 34.510  9.486   -8.259  1.00 30.93  ? 206  THR C CA  1 
ATOM   1631  C C   . THR A  1 205 ? 34.562  8.548   -9.468  1.00 34.39  ? 206  THR C C   1 
ATOM   1632  O O   . THR A  1 205 ? 33.654  8.590   -10.294 1.00 33.52  ? 206  THR C O   1 
ATOM   1633  C CB  . THR A  1 205 ? 34.477  8.753   -6.885  1.00 31.90  ? 206  THR C CB  1 
ATOM   1634  O OG1 . THR A  1 205 ? 35.154  9.555   -5.908  1.00 35.51  ? 206  THR C OG1 1 
ATOM   1635  C CG2 . THR A  1 205 ? 35.046  7.343   -6.904  1.00 28.04  ? 206  THR C CG2 1 
ATOM   1636  N N   . SER A  1 206 ? 35.597  7.721   -9.598  1.00 36.14  ? 207  SER C N   1 
ATOM   1637  C CA  . SER A  1 206 ? 35.601  6.685   -10.619 1.00 33.46  ? 207  SER C CA  1 
ATOM   1638  C C   . SER A  1 206 ? 34.458  5.683   -10.454 1.00 30.63  ? 207  SER C C   1 
ATOM   1639  O O   . SER A  1 206 ? 34.017  5.084   -11.443 1.00 29.90  ? 207  SER C O   1 
ATOM   1640  C CB  . SER A  1 206 ? 36.936  5.938   -10.592 1.00 34.61  ? 207  SER C CB  1 
ATOM   1641  O OG  . SER A  1 206 ? 37.961  6.816   -11.036 1.00 46.90  ? 207  SER C OG  1 
ATOM   1642  N N   . THR A  1 207 ? 33.978  5.491   -9.224  1.00 29.36  ? 208  THR C N   1 
ATOM   1643  C CA  . THR A  1 207 ? 32.854  4.580   -9.024  1.00 25.11  ? 208  THR C CA  1 
ATOM   1644  C C   . THR A  1 207 ? 31.624  5.221   -8.360  1.00 26.55  ? 208  THR C C   1 
ATOM   1645  O O   . THR A  1 207 ? 30.536  4.692   -8.519  1.00 29.84  ? 208  THR C O   1 
ATOM   1646  C CB  . THR A  1 207 ? 33.282  3.306   -8.220  1.00 30.47  ? 208  THR C CB  1 
ATOM   1647  O OG1 . THR A  1 207 ? 33.776  3.675   -6.924  1.00 35.74  ? 208  THR C OG1 1 
ATOM   1648  C CG2 . THR A  1 207 ? 34.385  2.567   -8.943  1.00 27.93  ? 208  THR C CG2 1 
ATOM   1649  N N   . LEU A  1 208 ? 31.751  6.384   -7.702  1.00 29.25  ? 209  LEU C N   1 
ATOM   1650  C CA  . LEU A  1 208 ? 30.623  6.993   -6.959  1.00 26.26  ? 209  LEU C CA  1 
ATOM   1651  C C   . LEU A  1 208 ? 29.900  8.022   -7.843  1.00 30.00  ? 209  LEU C C   1 
ATOM   1652  O O   . LEU A  1 208 ? 30.555  8.828   -8.503  1.00 31.88  ? 209  LEU C O   1 
ATOM   1653  C CB  . LEU A  1 208 ? 31.135  7.689   -5.683  1.00 25.65  ? 209  LEU C CB  1 
ATOM   1654  C CG  . LEU A  1 208 ? 30.207  8.454   -4.710  1.00 29.59  ? 209  LEU C CG  1 
ATOM   1655  C CD1 . LEU A  1 208 ? 29.314  7.537   -3.853  1.00 20.61  ? 209  LEU C CD1 1 
ATOM   1656  C CD2 . LEU A  1 208 ? 30.943  9.438   -3.816  1.00 29.03  ? 209  LEU C CD2 1 
ATOM   1657  N N   . ASN A  1 209 ? 28.565  7.998   -7.871  1.00 29.16  ? 210  ASN C N   1 
ATOM   1658  C CA  . ASN A  1 209 ? 27.760  8.964   -8.667  1.00 27.02  ? 210  ASN C CA  1 
ATOM   1659  C C   . ASN A  1 209 ? 26.488  9.381   -7.889  1.00 27.65  ? 210  ASN C C   1 
ATOM   1660  O O   . ASN A  1 209 ? 25.390  8.844   -8.096  1.00 29.62  ? 210  ASN C O   1 
ATOM   1661  C CB  . ASN A  1 209 ? 27.406  8.351   -10.040 1.00 24.05  ? 210  ASN C CB  1 
ATOM   1662  C CG  . ASN A  1 209 ? 26.660  9.308   -10.961 1.00 25.42  ? 210  ASN C CG  1 
ATOM   1663  O OD1 . ASN A  1 209 ? 26.675  10.520  -10.774 1.00 29.75  ? 210  ASN C OD1 1 
ATOM   1664  N ND2 . ASN A  1 209 ? 26.010  8.756   -11.975 1.00 26.58  ? 210  ASN C ND2 1 
ATOM   1665  N N   . GLN A  1 210 ? 26.649  10.349  -6.996  1.00 25.55  ? 211  GLN C N   1 
ATOM   1666  C CA  . GLN A  1 210 ? 25.644  10.665  -5.990  1.00 27.81  ? 211  GLN C CA  1 
ATOM   1667  C C   . GLN A  1 210 ? 24.975  12.043  -6.229  1.00 28.36  ? 211  GLN C C   1 
ATOM   1668  O O   . GLN A  1 210 ? 25.645  12.993  -6.645  1.00 30.89  ? 211  GLN C O   1 
ATOM   1669  C CB  . GLN A  1 210 ? 26.332  10.616  -4.615  1.00 21.77  ? 211  GLN C CB  1 
ATOM   1670  C CG  . GLN A  1 210 ? 25.533  11.120  -3.451  1.00 24.30  ? 211  GLN C CG  1 
ATOM   1671  C CD  . GLN A  1 210 ? 26.351  11.133  -2.153  1.00 33.81  ? 211  GLN C CD  1 
ATOM   1672  O OE1 . GLN A  1 210 ? 26.650  12.210  -1.613  1.00 31.17  ? 211  GLN C OE1 1 
ATOM   1673  N NE2 . GLN A  1 210 ? 26.739  9.941   -1.661  1.00 27.61  ? 211  GLN C NE2 1 
ATOM   1674  N N   . LYS A  1 211 ? 23.675  12.150  -5.926  1.00 27.22  ? 212  LYS C N   1 
ATOM   1675  C CA  . LYS A  1 211 ? 22.931  13.429  -5.956  1.00 30.03  ? 212  LYS C CA  1 
ATOM   1676  C C   . LYS A  1 211 ? 21.977  13.575  -4.768  1.00 32.52  ? 212  LYS C C   1 
ATOM   1677  O O   . LYS A  1 211 ? 21.075  12.753  -4.559  1.00 32.54  ? 212  LYS C O   1 
ATOM   1678  C CB  . LYS A  1 211 ? 22.126  13.593  -7.235  1.00 31.21  ? 212  LYS C CB  1 
ATOM   1679  C CG  . LYS A  1 211 ? 21.347  14.903  -7.249  1.00 35.81  ? 212  LYS C CG  1 
ATOM   1680  C CD  . LYS A  1 211 ? 21.411  15.547  -8.626  1.00 40.99  ? 212  LYS C CD  1 
ATOM   1681  C CE  . LYS A  1 211 ? 20.744  16.900  -8.678  1.00 36.11  ? 212  LYS C CE  1 
ATOM   1682  N NZ  . LYS A  1 211 ? 20.839  17.439  -10.072 1.00 42.16  ? 212  LYS C NZ  1 
ATOM   1683  N N   . LEU A  1 212 ? 22.215  14.607  -3.969  1.00 36.32  ? 213  LEU C N   1 
ATOM   1684  C CA  . LEU A  1 212 ? 21.424  14.849  -2.766  1.00 35.26  ? 213  LEU C CA  1 
ATOM   1685  C C   . LEU A  1 212 ? 20.594  16.157  -2.870  1.00 39.69  ? 213  LEU C C   1 
ATOM   1686  O O   . LEU A  1 212 ? 21.050  17.166  -3.429  1.00 34.27  ? 213  LEU C O   1 
ATOM   1687  C CB  . LEU A  1 212 ? 22.371  14.869  -1.547  1.00 36.50  ? 213  LEU C CB  1 
ATOM   1688  C CG  . LEU A  1 212 ? 23.339  13.678  -1.384  1.00 34.85  ? 213  LEU C CG  1 
ATOM   1689  C CD1 . LEU A  1 212 ? 24.397  13.921  -0.303  1.00 30.41  ? 213  LEU C CD1 1 
ATOM   1690  C CD2 . LEU A  1 212 ? 22.585  12.390  -1.068  1.00 31.33  ? 213  LEU C CD2 1 
ATOM   1691  N N   . VAL A  1 213 ? 19.371  16.110  -2.333  1.00 41.26  ? 214  VAL C N   1 
ATOM   1692  C CA  . VAL A  1 213 ? 18.462  17.254  -2.286  1.00 36.00  ? 214  VAL C CA  1 
ATOM   1693  C C   . VAL A  1 213 ? 17.852  17.299  -0.894  1.00 35.27  ? 214  VAL C C   1 
ATOM   1694  O O   . VAL A  1 213 ? 17.435  16.268  -0.384  1.00 37.91  ? 214  VAL C O   1 
ATOM   1695  C CB  . VAL A  1 213 ? 17.337  17.160  -3.337  1.00 37.65  ? 214  VAL C CB  1 
ATOM   1696  C CG1 . VAL A  1 213 ? 16.347  18.343  -3.200  1.00 34.85  ? 214  VAL C CG1 1 
ATOM   1697  C CG2 . VAL A  1 213 ? 17.915  17.096  -4.728  1.00 30.79  ? 214  VAL C CG2 1 
ATOM   1698  N N   . PRO A  1 214 ? 17.823  18.487  -0.265  1.00 38.63  ? 215  PRO C N   1 
ATOM   1699  C CA  . PRO A  1 214 ? 17.317  18.637  1.102   1.00 35.13  ? 215  PRO C CA  1 
ATOM   1700  C C   . PRO A  1 214 ? 15.846  18.336  1.241   1.00 35.93  ? 215  PRO C C   1 
ATOM   1701  O O   . PRO A  1 214 ? 15.076  18.551  0.317   1.00 45.20  ? 215  PRO C O   1 
ATOM   1702  C CB  . PRO A  1 214 ? 17.583  20.113  1.424   1.00 36.71  ? 215  PRO C CB  1 
ATOM   1703  C CG  . PRO A  1 214 ? 18.603  20.556  0.469   1.00 38.19  ? 215  PRO C CG  1 
ATOM   1704  C CD  . PRO A  1 214 ? 18.396  19.747  -0.775  1.00 40.66  ? 215  PRO C CD  1 
ATOM   1705  N N   . LYS A  1 215 ? 15.472  17.853  2.412   1.00 36.73  ? 216  LYS C N   1 
ATOM   1706  C CA  . LYS A  1 215 ? 14.077  17.611  2.756   1.00 44.31  ? 216  LYS C CA  1 
ATOM   1707  C C   . LYS A  1 215 ? 13.645  18.687  3.770   1.00 44.45  ? 216  LYS C C   1 
ATOM   1708  O O   . LYS A  1 215 ? 14.119  18.728  4.910   1.00 43.39  ? 216  LYS C O   1 
ATOM   1709  C CB  . LYS A  1 215 ? 13.864  16.196  3.311   1.00 37.02  ? 216  LYS C CB  1 
ATOM   1710  C CG  . LYS A  1 215 ? 14.064  15.126  2.282   1.00 36.89  ? 216  LYS C CG  1 
ATOM   1711  C CD  . LYS A  1 215 ? 13.743  13.745  2.794   1.00 40.09  ? 216  LYS C CD  1 
ATOM   1712  C CE  . LYS A  1 215 ? 14.985  12.877  2.867   1.00 42.93  ? 216  LYS C CE  1 
ATOM   1713  N NZ  . LYS A  1 215 ? 14.753  11.663  3.719   1.00 47.83  ? 216  LYS C NZ  1 
ATOM   1714  N N   . ILE A  1 216 ? 12.867  19.647  3.289   1.00 44.02  ? 217  ILE C N   1 
ATOM   1715  C CA  . ILE A  1 216 ? 12.422  20.734  4.136   1.00 44.14  ? 217  ILE C CA  1 
ATOM   1716  C C   . ILE A  1 216 ? 11.026  20.439  4.684   1.00 45.24  ? 217  ILE C C   1 
ATOM   1717  O O   . ILE A  1 216 ? 10.075  20.276  3.918   1.00 47.70  ? 217  ILE C O   1 
ATOM   1718  C CB  . ILE A  1 216 ? 12.465  22.056  3.374   1.00 42.58  ? 217  ILE C CB  1 
ATOM   1719  C CG1 . ILE A  1 216 ? 13.903  22.290  2.887   1.00 38.44  ? 217  ILE C CG1 1 
ATOM   1720  C CG2 . ILE A  1 216 ? 12.011  23.191  4.268   1.00 46.95  ? 217  ILE C CG2 1 
ATOM   1721  C CD1 . ILE A  1 216 ? 14.136  23.542  2.088   1.00 37.30  ? 217  ILE C CD1 1 
ATOM   1722  N N   . ALA A  1 217 ? 10.923  20.286  6.004   1.00 46.36  ? 218  ALA C N   1 
ATOM   1723  C CA  . ALA A  1 217 ? 9.660   19.880  6.637   1.00 50.32  ? 218  ALA C CA  1 
ATOM   1724  C C   . ALA A  1 217 ? 9.736   19.999  8.163   1.00 56.04  ? 218  ALA C C   1 
ATOM   1725  O O   . ALA A  1 217 ? 10.804  20.284  8.710   1.00 59.63  ? 218  ALA C O   1 
ATOM   1726  C CB  . ALA A  1 217 ? 9.297   18.462  6.237   1.00 45.72  ? 218  ALA C CB  1 
ATOM   1727  N N   . THR A  1 218 ? 8.620   19.764  8.855   1.00 57.90  ? 219  THR C N   1 
ATOM   1728  C CA  . THR A  1 218 ? 8.600   19.926  10.318  1.00 61.11  ? 219  THR C CA  1 
ATOM   1729  C C   . THR A  1 218 ? 8.582   18.579  11.036  1.00 61.68  ? 219  THR C C   1 
ATOM   1730  O O   . THR A  1 218 ? 7.765   17.695  10.725  1.00 56.04  ? 219  THR C O   1 
ATOM   1731  C CB  . THR A  1 218 ? 7.410   20.777  10.833  1.00 63.54  ? 219  THR C CB  1 
ATOM   1732  O OG1 . THR A  1 218 ? 7.526   22.121  10.348  1.00 60.59  ? 219  THR C OG1 1 
ATOM   1733  C CG2 . THR A  1 218 ? 7.426   20.825  12.363  1.00 59.71  ? 219  THR C CG2 1 
ATOM   1734  N N   . ARG A  1 219 ? 9.515   18.433  11.979  1.00 62.32  ? 220  ARG C N   1 
ATOM   1735  C CA  . ARG A  1 219 ? 9.705   17.197  12.734  1.00 57.37  ? 220  ARG C CA  1 
ATOM   1736  C C   . ARG A  1 219 ? 9.850   17.474  14.226  1.00 57.95  ? 220  ARG C C   1 
ATOM   1737  O O   . ARG A  1 219 ? 10.111  18.615  14.658  1.00 57.16  ? 220  ARG C O   1 
ATOM   1738  C CB  . ARG A  1 219 ? 10.951  16.440  12.248  1.00 57.22  ? 220  ARG C CB  1 
ATOM   1739  C CG  . ARG A  1 219 ? 11.130  16.437  10.746  1.00 62.11  ? 220  ARG C CG  1 
ATOM   1740  C CD  . ARG A  1 219 ? 12.549  16.117  10.347  1.00 50.90  ? 220  ARG C CD  1 
ATOM   1741  N NE  . ARG A  1 219 ? 12.770  16.452  8.947   1.00 48.80  ? 220  ARG C NE  1 
ATOM   1742  C CZ  . ARG A  1 219 ? 13.495  17.493  8.555   1.00 46.24  ? 220  ARG C CZ  1 
ATOM   1743  N NH1 . ARG A  1 219 ? 14.068  18.284  9.463   1.00 41.27  ? 220  ARG C NH1 1 
ATOM   1744  N NH2 . ARG A  1 219 ? 13.662  17.727  7.264   1.00 44.68  ? 220  ARG C NH2 1 
ATOM   1745  N N   . SER A  1 220 ? 9.733   16.400  14.998  1.00 54.32  ? 221  SER C N   1 
ATOM   1746  C CA  . SER A  1 220 ? 9.881   16.461  16.441  1.00 56.44  ? 221  SER C CA  1 
ATOM   1747  C C   . SER A  1 220 ? 11.232  17.083  16.821  1.00 56.53  ? 221  SER C C   1 
ATOM   1748  O O   . SER A  1 220 ? 12.176  17.057  16.034  1.00 55.39  ? 221  SER C O   1 
ATOM   1749  C CB  . SER A  1 220 ? 9.731   15.049  17.016  1.00 55.94  ? 221  SER C CB  1 
ATOM   1750  O OG  . SER A  1 220 ? 8.561   14.414  16.492  1.00 54.68  ? 221  SER C OG  1 
ATOM   1751  N N   . LYS A  1 221 ? 11.314  17.634  18.030  1.00 57.78  ? 222  LYS C N   1 
ATOM   1752  C CA  . LYS A  1 221 ? 12.525  18.302  18.505  1.00 52.86  ? 222  LYS C CA  1 
ATOM   1753  C C   . LYS A  1 221 ? 13.463  17.264  19.104  1.00 51.98  ? 222  LYS C C   1 
ATOM   1754  O O   . LYS A  1 221 ? 13.019  16.342  19.786  1.00 55.27  ? 222  LYS C O   1 
ATOM   1755  C CB  . LYS A  1 221 ? 12.185  19.375  19.549  1.00 59.66  ? 222  LYS C CB  1 
ATOM   1756  C CG  . LYS A  1 221 ? 11.240  20.482  19.047  1.00 68.37  ? 222  LYS C CG  1 
ATOM   1757  C CD  . LYS A  1 221 ? 11.404  21.807  19.804  1.00 64.37  ? 222  LYS C CD  1 
ATOM   1758  C CE  . LYS A  1 221 ? 12.583  22.628  19.291  1.00 62.11  ? 222  LYS C CE  1 
ATOM   1759  N NZ  . LYS A  1 221 ? 12.286  23.388  18.028  1.00 64.84  ? 222  LYS C NZ  1 
ATOM   1760  N N   . VAL A  1 222 ? 14.737  17.323  18.739  1.00 47.22  ? 223  VAL C N   1 
ATOM   1761  C CA  . VAL A  1 222 ? 15.727  16.469  19.361  1.00 43.89  ? 223  VAL C CA  1 
ATOM   1762  C C   . VAL A  1 222 ? 16.867  17.375  19.827  1.00 48.25  ? 223  VAL C C   1 
ATOM   1763  O O   . VAL A  1 222 ? 17.469  18.061  19.008  1.00 48.69  ? 223  VAL C O   1 
ATOM   1764  C CB  . VAL A  1 222 ? 16.214  15.369  18.404  1.00 48.01  ? 223  VAL C CB  1 
ATOM   1765  C CG1 . VAL A  1 222 ? 17.198  14.455  19.119  1.00 44.38  ? 223  VAL C CG1 1 
ATOM   1766  C CG2 . VAL A  1 222 ? 15.023  14.551  17.864  1.00 44.21  ? 223  VAL C CG2 1 
ATOM   1767  N N   . LYS A  1 223 ? 17.137  17.392  21.137  1.00 50.47  ? 224  LYS C N   1 
ATOM   1768  C CA  . LYS A  1 223 ? 18.056  18.360  21.767  1.00 46.51  ? 224  LYS C CA  1 
ATOM   1769  C C   . LYS A  1 223 ? 17.733  19.787  21.360  1.00 49.31  ? 224  LYS C C   1 
ATOM   1770  O O   . LYS A  1 223 ? 18.645  20.598  21.131  1.00 48.64  ? 224  LYS C O   1 
ATOM   1771  C CB  . LYS A  1 223 ? 19.534  18.067  21.462  1.00 45.54  ? 224  LYS C CB  1 
ATOM   1772  C CG  . LYS A  1 223 ? 20.056  16.786  22.108  1.00 48.31  ? 224  LYS C CG  1 
ATOM   1773  C CD  . LYS A  1 223 ? 21.482  16.433  21.654  1.00 46.91  ? 224  LYS C CD  1 
ATOM   1774  C CE  . LYS A  1 223 ? 22.460  17.577  21.901  1.00 49.19  ? 224  LYS C CE  1 
ATOM   1775  N NZ  . LYS A  1 223 ? 23.872  17.193  21.564  1.00 50.61  ? 224  LYS C NZ  1 
ATOM   1776  N N   . GLY A  1 224 ? 16.437  20.081  21.250  1.00 47.39  ? 225  GLY C N   1 
ATOM   1777  C CA  . GLY A  1 224 ? 16.006  21.429  20.943  1.00 53.02  ? 225  GLY C CA  1 
ATOM   1778  C C   . GLY A  1 224 ? 16.019  21.789  19.471  1.00 58.21  ? 225  GLY C C   1 
ATOM   1779  O O   . GLY A  1 224 ? 15.753  22.942  19.125  1.00 57.89  ? 225  GLY C O   1 
ATOM   1780  N N   . LEU A  1 225 ? 16.377  20.834  18.612  1.00 55.50  ? 226  LEU C N   1 
ATOM   1781  C CA  . LEU A  1 225 ? 16.481  21.114  17.186  1.00 51.35  ? 226  LEU C CA  1 
ATOM   1782  C C   . LEU A  1 225 ? 15.489  20.344  16.333  1.00 45.48  ? 226  LEU C C   1 
ATOM   1783  O O   . LEU A  1 225 ? 15.199  19.190  16.593  1.00 49.84  ? 226  LEU C O   1 
ATOM   1784  C CB  . LEU A  1 225 ? 17.897  20.811  16.721  1.00 50.52  ? 226  LEU C CB  1 
ATOM   1785  C CG  . LEU A  1 225 ? 18.980  21.647  17.397  1.00 54.28  ? 226  LEU C CG  1 
ATOM   1786  C CD1 . LEU A  1 225 ? 20.316  21.442  16.696  1.00 53.97  ? 226  LEU C CD1 1 
ATOM   1787  C CD2 . LEU A  1 225 ? 18.593  23.109  17.368  1.00 53.52  ? 226  LEU C CD2 1 
ATOM   1788  N N   . SER A  1 226 ? 15.037  20.962  15.255  1.00 46.88  ? 227  SER C N   1 
ATOM   1789  C CA  . SER A  1 226 ? 14.110  20.288  14.360  1.00 49.22  ? 227  SER C CA  1 
ATOM   1790  C C   . SER A  1 226 ? 14.796  20.027  13.018  1.00 47.75  ? 227  SER C C   1 
ATOM   1791  O O   . SER A  1 226 ? 14.250  19.348  12.147  1.00 52.20  ? 227  SER C O   1 
ATOM   1792  C CB  . SER A  1 226 ? 12.844  21.133  14.179  1.00 52.36  ? 227  SER C CB  1 
ATOM   1793  O OG  . SER A  1 226 ? 11.735  20.358  13.754  1.00 58.14  ? 227  SER C OG  1 
ATOM   1794  N N   . GLY A  1 227 ? 16.026  20.522  12.894  1.00 46.66  ? 228  GLY C N   1 
ATOM   1795  C CA  . GLY A  1 227 ? 16.873  20.265  11.740  1.00 45.09  ? 228  GLY C CA  1 
ATOM   1796  C C   . GLY A  1 227 ? 17.591  18.929  11.870  1.00 41.39  ? 228  GLY C C   1 
ATOM   1797  O O   . GLY A  1 227 ? 17.611  18.332  12.944  1.00 45.83  ? 228  GLY C O   1 
ATOM   1798  N N   . ARG A  1 228 ? 18.155  18.432  10.778  1.00 37.78  ? 229  ARG C N   1 
ATOM   1799  C CA  . ARG A  1 228 ? 18.856  17.153  10.805  1.00 35.14  ? 229  ARG C CA  1 
ATOM   1800  C C   . ARG A  1 228 ? 20.140  17.244  9.998   1.00 37.40  ? 229  ARG C C   1 
ATOM   1801  O O   . ARG A  1 228 ? 20.257  18.078  9.092   1.00 35.91  ? 229  ARG C O   1 
ATOM   1802  C CB  . ARG A  1 228 ? 17.977  16.029  10.257  1.00 33.91  ? 229  ARG C CB  1 
ATOM   1803  C CG  . ARG A  1 228 ? 16.692  15.757  11.020  1.00 38.26  ? 229  ARG C CG  1 
ATOM   1804  C CD  . ARG A  1 228 ? 16.935  15.190  12.427  1.00 46.24  ? 229  ARG C CD  1 
ATOM   1805  N NE  . ARG A  1 228 ? 15.674  14.777  13.048  1.00 48.78  ? 229  ARG C NE  1 
ATOM   1806  C CZ  . ARG A  1 228 ? 14.988  15.508  13.921  1.00 46.15  ? 229  ARG C CZ  1 
ATOM   1807  N NH1 . ARG A  1 228 ? 15.469  16.681  14.330  1.00 45.10  ? 229  ARG C NH1 1 
ATOM   1808  N NH2 . ARG A  1 228 ? 13.842  15.047  14.412  1.00 43.09  ? 229  ARG C NH2 1 
ATOM   1809  N N   . MET A  1 229 ? 21.120  16.416  10.346  1.00 34.14  ? 230  MET C N   1 
ATOM   1810  C CA  . MET A  1 229 ? 22.315  16.304  9.516   1.00 33.55  ? 230  MET C CA  1 
ATOM   1811  C C   . MET A  1 229 ? 22.538  14.855  9.108   1.00 32.32  ? 230  MET C C   1 
ATOM   1812  O O   . MET A  1 229 ? 22.455  13.941  9.929   1.00 31.86  ? 230  MET C O   1 
ATOM   1813  C CB  . MET A  1 229 ? 23.540  16.872  10.222  1.00 34.71  ? 230  MET C CB  1 
ATOM   1814  C CG  . MET A  1 229 ? 23.429  18.357  10.448  1.00 38.62  ? 230  MET C CG  1 
ATOM   1815  S SD  . MET A  1 229 ? 25.012  19.186  10.193  1.00 48.06  ? 230  MET C SD  1 
ATOM   1816  C CE  . MET A  1 229 ? 24.457  20.897  10.120  1.00 37.47  ? 230  MET C CE  1 
ATOM   1817  N N   . GLU A  1 230 ? 22.788  14.650  7.818   1.00 30.97  ? 231  GLU C N   1 
ATOM   1818  C CA  . GLU A  1 230 ? 22.942  13.307  7.294   1.00 32.59  ? 231  GLU C CA  1 
ATOM   1819  C C   . GLU A  1 230 ? 24.323  13.123  6.693   1.00 31.13  ? 231  GLU C C   1 
ATOM   1820  O O   . GLU A  1 230 ? 24.702  13.897  5.802   1.00 26.19  ? 231  GLU C O   1 
ATOM   1821  C CB  . GLU A  1 230 ? 21.860  13.025  6.260   1.00 32.97  ? 231  GLU C CB  1 
ATOM   1822  C CG  . GLU A  1 230 ? 21.654  11.556  5.964   1.00 39.52  ? 231  GLU C CG  1 
ATOM   1823  C CD  . GLU A  1 230 ? 20.550  11.313  4.951   1.00 39.14  ? 231  GLU C CD  1 
ATOM   1824  O OE1 . GLU A  1 230 ? 19.972  12.316  4.472   1.00 39.98  ? 231  GLU C OE1 1 
ATOM   1825  O OE2 . GLU A  1 230 ? 20.261  10.125  4.661   1.00 35.12  ? 231  GLU C OE2 1 
ATOM   1826  N N   . PHE A  1 231 ? 25.071  12.115  7.173   1.00 30.62  ? 232  PHE C N   1 
ATOM   1827  C CA  . PHE A  1 231 ? 26.466  11.951  6.743   1.00 28.86  ? 232  PHE C CA  1 
ATOM   1828  C C   . PHE A  1 231 ? 26.758  10.762  5.829   1.00 29.13  ? 232  PHE C C   1 
ATOM   1829  O O   . PHE A  1 231 ? 26.006  9.774   5.789   1.00 29.22  ? 232  PHE C O   1 
ATOM   1830  C CB  . PHE A  1 231 ? 27.374  11.921  7.974   1.00 27.96  ? 232  PHE C CB  1 
ATOM   1831  C CG  . PHE A  1 231 ? 27.481  13.277  8.660   1.00 30.86  ? 232  PHE C CG  1 
ATOM   1832  C CD1 . PHE A  1 231 ? 28.338  14.257  8.167   1.00 31.80  ? 232  PHE C CD1 1 
ATOM   1833  C CD2 . PHE A  1 231 ? 26.680  13.593  9.735   1.00 27.23  ? 232  PHE C CD2 1 
ATOM   1834  C CE1 . PHE A  1 231 ? 28.424  15.515  8.778   1.00 30.82  ? 232  PHE C CE1 1 
ATOM   1835  C CE2 . PHE A  1 231 ? 26.755  14.836  10.328  1.00 30.16  ? 232  PHE C CE2 1 
ATOM   1836  C CZ  . PHE A  1 231 ? 27.633  15.792  9.854   1.00 27.67  ? 232  PHE C CZ  1 
ATOM   1837  N N   . PHE A  1 232 ? 27.822  10.918  5.035   1.00 25.48  ? 233  PHE C N   1 
ATOM   1838  C CA  . PHE A  1 232 ? 28.204  9.943   4.022   1.00 22.12  ? 233  PHE C CA  1 
ATOM   1839  C C   . PHE A  1 232 ? 29.708  9.722   4.032   1.00 24.66  ? 233  PHE C C   1 
ATOM   1840  O O   . PHE A  1 232 ? 30.447  10.585  4.501   1.00 30.86  ? 233  PHE C O   1 
ATOM   1841  C CB  . PHE A  1 232 ? 27.746  10.421  2.619   1.00 24.73  ? 233  PHE C CB  1 
ATOM   1842  C CG  . PHE A  1 232 ? 26.254  10.504  2.482   1.00 23.87  ? 233  PHE C CG  1 
ATOM   1843  C CD1 . PHE A  1 232 ? 25.571  11.655  2.874   1.00 24.13  ? 233  PHE C CD1 1 
ATOM   1844  C CD2 . PHE A  1 232 ? 25.523  9.394   2.044   1.00 22.77  ? 233  PHE C CD2 1 
ATOM   1845  C CE1 . PHE A  1 232 ? 24.184  11.720  2.798   1.00 27.23  ? 233  PHE C CE1 1 
ATOM   1846  C CE2 . PHE A  1 232 ? 24.150  9.441   1.954   1.00 23.00  ? 233  PHE C CE2 1 
ATOM   1847  C CZ  . PHE A  1 232 ? 23.472  10.606  2.327   1.00 31.79  ? 233  PHE C CZ  1 
ATOM   1848  N N   . TRP A  1 233 ? 30.166  8.621   3.432   1.00 28.27  ? 234  TRP C N   1 
ATOM   1849  C CA  . TRP A  1 233 ? 31.593  8.269   3.340   1.00 24.97  ? 234  TRP C CA  1 
ATOM   1850  C C   . TRP A  1 233 ? 31.877  7.480   2.071   1.00 25.86  ? 234  TRP C C   1 
ATOM   1851  O O   . TRP A  1 233 ? 30.986  6.810   1.550   1.00 26.09  ? 234  TRP C O   1 
ATOM   1852  C CB  . TRP A  1 233 ? 32.019  7.445   4.563   1.00 19.43  ? 234  TRP C CB  1 
ATOM   1853  C CG  . TRP A  1 233 ? 31.240  6.153   4.702   1.00 20.73  ? 234  TRP C CG  1 
ATOM   1854  C CD1 . TRP A  1 233 ? 29.975  6.016   5.234   1.00 20.53  ? 234  TRP C CD1 1 
ATOM   1855  C CD2 . TRP A  1 233 ? 31.692  4.820   4.400   1.00 18.39  ? 234  TRP C CD2 1 
ATOM   1856  N NE1 . TRP A  1 233 ? 29.599  4.692   5.217   1.00 19.25  ? 234  TRP C NE1 1 
ATOM   1857  C CE2 . TRP A  1 233 ? 30.638  3.935   4.727   1.00 16.68  ? 234  TRP C CE2 1 
ATOM   1858  C CE3 . TRP A  1 233 ? 32.866  4.296   3.849   1.00 22.21  ? 234  TRP C CE3 1 
ATOM   1859  C CZ2 . TRP A  1 233 ? 30.724  2.550   4.512   1.00 20.19  ? 234  TRP C CZ2 1 
ATOM   1860  C CZ3 . TRP A  1 233 ? 32.955  2.917   3.636   1.00 21.86  ? 234  TRP C CZ3 1 
ATOM   1861  C CH2 . TRP A  1 233 ? 31.887  2.060   3.966   1.00 20.26  ? 234  TRP C CH2 1 
ATOM   1862  N N   . THR A  1 234 ? 33.135  7.512   1.633   1.00 23.29  ? 235  THR C N   1 
ATOM   1863  C CA  . THR A  1 234 ? 33.612  6.732   0.506   1.00 23.66  ? 235  THR C CA  1 
ATOM   1864  C C   . THR A  1 234 ? 35.107  6.458   0.731   1.00 29.83  ? 235  THR C C   1 
ATOM   1865  O O   . THR A  1 234 ? 35.774  7.111   1.546   1.00 28.55  ? 235  THR C O   1 
ATOM   1866  C CB  . THR A  1 234 ? 33.392  7.459   -0.879  1.00 25.99  ? 235  THR C CB  1 
ATOM   1867  O OG1 . THR A  1 234 ? 33.259  6.498   -1.929  1.00 21.27  ? 235  THR C OG1 1 
ATOM   1868  C CG2 . THR A  1 234 ? 34.537  8.421   -1.215  1.00 22.00  ? 235  THR C CG2 1 
ATOM   1869  N N   . ILE A  1 235 ? 35.613  5.448   0.037   1.00 34.65  ? 236  ILE C N   1 
ATOM   1870  C CA  . ILE A  1 235 ? 37.036  5.153   0.001   1.00 30.69  ? 236  ILE C CA  1 
ATOM   1871  C C   . ILE A  1 235 ? 37.555  5.604   -1.355  1.00 31.27  ? 236  ILE C C   1 
ATOM   1872  O O   . ILE A  1 235 ? 37.180  5.018   -2.381  1.00 30.02  ? 236  ILE C O   1 
ATOM   1873  C CB  . ILE A  1 235 ? 37.298  3.648   0.191   1.00 27.62  ? 236  ILE C CB  1 
ATOM   1874  C CG1 . ILE A  1 235 ? 36.893  3.214   1.598   1.00 29.14  ? 236  ILE C CG1 1 
ATOM   1875  C CG2 . ILE A  1 235 ? 38.760  3.314   -0.068  1.00 26.88  ? 236  ILE C CG2 1 
ATOM   1876  C CD1 . ILE A  1 235 ? 37.854  3.708   2.655   1.00 28.70  ? 236  ILE C CD1 1 
ATOM   1877  N N   . LEU A  1 236 ? 38.419  6.624   -1.350  1.00 30.66  ? 237  LEU C N   1 
ATOM   1878  C CA  . LEU A  1 236 ? 39.038  7.154   -2.560  1.00 27.46  ? 237  LEU C CA  1 
ATOM   1879  C C   . LEU A  1 236 ? 40.395  6.491   -2.837  1.00 31.35  ? 237  LEU C C   1 
ATOM   1880  O O   . LEU A  1 236 ? 41.403  6.837   -2.214  1.00 34.68  ? 237  LEU C O   1 
ATOM   1881  C CB  . LEU A  1 236 ? 39.218  8.674   -2.421  1.00 28.61  ? 237  LEU C CB  1 
ATOM   1882  C CG  . LEU A  1 236 ? 39.706  9.526   -3.610  1.00 33.40  ? 237  LEU C CG  1 
ATOM   1883  C CD1 . LEU A  1 236 ? 38.722  9.521   -4.780  1.00 27.85  ? 237  LEU C CD1 1 
ATOM   1884  C CD2 . LEU A  1 236 ? 40.003  10.957  -3.178  1.00 29.18  ? 237  LEU C CD2 1 
ATOM   1885  N N   . LYS A  1 237 ? 40.436  5.615   -3.833  1.00 31.72  ? 238  LYS C N   1 
ATOM   1886  C CA  . LYS A  1 237 ? 41.671  4.908   -4.199  1.00 36.70  ? 238  LYS C CA  1 
ATOM   1887  C C   . LYS A  1 237 ? 42.807  5.812   -4.678  1.00 35.74  ? 238  LYS C C   1 
ATOM   1888  O O   . LYS A  1 237 ? 42.580  6.867   -5.246  1.00 38.84  ? 238  LYS C O   1 
ATOM   1889  C CB  . LYS A  1 237 ? 41.371  3.863   -5.274  1.00 34.68  ? 238  LYS C CB  1 
ATOM   1890  C CG  . LYS A  1 237 ? 40.444  2.742   -4.797  1.00 33.87  ? 238  LYS C CG  1 
ATOM   1891  C CD  . LYS A  1 237 ? 40.325  1.695   -5.887  1.00 43.31  ? 238  LYS C CD  1 
ATOM   1892  C CE  . LYS A  1 237 ? 40.116  0.275   -5.357  1.00 42.22  ? 238  LYS C CE  1 
ATOM   1893  N NZ  . LYS A  1 237 ? 39.621  -0.583  -6.485  1.00 39.17  ? 238  LYS C NZ  1 
ATOM   1894  N N   . SER A  1 238 ? 44.034  5.360   -4.467  1.00 40.11  ? 239  SER C N   1 
ATOM   1895  C CA  . SER A  1 238 ? 45.219  6.098   -4.882  1.00 39.23  ? 239  SER C CA  1 
ATOM   1896  C C   . SER A  1 238 ? 45.216  6.461   -6.359  1.00 45.75  ? 239  SER C C   1 
ATOM   1897  O O   . SER A  1 238 ? 45.009  5.602   -7.233  1.00 46.20  ? 239  SER C O   1 
ATOM   1898  C CB  . SER A  1 238 ? 46.468  5.284   -4.575  1.00 41.00  ? 239  SER C CB  1 
ATOM   1899  O OG  . SER A  1 238 ? 47.613  6.032   -4.903  1.00 48.02  ? 239  SER C OG  1 
ATOM   1900  N N   . ASN A  1 239 ? 45.484  7.744   -6.602  1.00 44.57  ? 240  ASN C N   1 
ATOM   1901  C CA  . ASN A  1 239 ? 45.518  8.365   -7.923  1.00 43.75  ? 240  ASN C CA  1 
ATOM   1902  C C   . ASN A  1 239 ? 44.124  8.632   -8.535  1.00 45.64  ? 240  ASN C C   1 
ATOM   1903  O O   . ASN A  1 239 ? 44.037  9.053   -9.680  1.00 43.93  ? 240  ASN C O   1 
ATOM   1904  C CB  . ASN A  1 239 ? 46.367  7.531   -8.892  1.00 45.73  ? 240  ASN C CB  1 
ATOM   1905  C CG  . ASN A  1 239 ? 47.050  8.379   -9.955  1.00 59.04  ? 240  ASN C CG  1 
ATOM   1906  O OD1 . ASN A  1 239 ? 47.517  9.490   -9.679  1.00 58.58  ? 240  ASN C OD1 1 
ATOM   1907  N ND2 . ASN A  1 239 ? 47.104  7.859   -11.184 1.00 59.64  ? 240  ASN C ND2 1 
ATOM   1908  N N   . ASP A  1 240 ? 43.053  8.488   -7.751  1.00 41.92  ? 241  ASP C N   1 
ATOM   1909  C CA  . ASP A  1 240 ? 41.705  8.852   -8.208  1.00 37.62  ? 241  ASP C CA  1 
ATOM   1910  C C   . ASP A  1 240 ? 41.412  10.250  -7.659  1.00 41.25  ? 241  ASP C C   1 
ATOM   1911  O O   . ASP A  1 240 ? 42.193  10.792  -6.868  1.00 38.16  ? 241  ASP C O   1 
ATOM   1912  C CB  . ASP A  1 240 ? 40.635  7.819   -7.740  1.00 36.20  ? 241  ASP C CB  1 
ATOM   1913  C CG  . ASP A  1 240 ? 39.237  7.982   -8.446  1.00 35.11  ? 241  ASP C CG  1 
ATOM   1914  O OD1 . ASP A  1 240 ? 39.131  8.620   -9.514  1.00 37.02  ? 241  ASP C OD1 1 
ATOM   1915  O OD2 . ASP A  1 240 ? 38.221  7.466   -7.918  1.00 31.59  ? 241  ASP C OD2 1 
ATOM   1916  N N   . ALA A  1 241 ? 40.303  10.837  -8.102  1.00 38.43  ? 242  ALA C N   1 
ATOM   1917  C CA  . ALA A  1 241 ? 39.919  12.178  -7.698  1.00 37.43  ? 242  ALA C CA  1 
ATOM   1918  C C   . ALA A  1 241 ? 38.439  12.193  -7.304  1.00 35.62  ? 242  ALA C C   1 
ATOM   1919  O O   . ALA A  1 241 ? 37.639  11.361  -7.779  1.00 33.26  ? 242  ALA C O   1 
ATOM   1920  C CB  . ALA A  1 241 ? 40.204  13.178  -8.815  1.00 35.11  ? 242  ALA C CB  1 
ATOM   1921  N N   . ILE A  1 242 ? 38.091  13.099  -6.395  1.00 31.57  ? 243  ILE C N   1 
ATOM   1922  C CA  . ILE A  1 242 ? 36.714  13.229  -5.948  1.00 34.30  ? 243  ILE C CA  1 
ATOM   1923  C C   . ILE A  1 242 ? 36.249  14.643  -6.307  1.00 31.89  ? 243  ILE C C   1 
ATOM   1924  O O   . ILE A  1 242 ? 37.026  15.598  -6.198  1.00 30.17  ? 243  ILE C O   1 
ATOM   1925  C CB  . ILE A  1 242 ? 36.573  12.896  -4.405  1.00 33.31  ? 243  ILE C CB  1 
ATOM   1926  C CG1 . ILE A  1 242 ? 35.104  12.640  -4.000  1.00 31.48  ? 243  ILE C CG1 1 
ATOM   1927  C CG2 . ILE A  1 242 ? 37.281  13.938  -3.532  1.00 24.98  ? 243  ILE C CG2 1 
ATOM   1928  C CD1 . ILE A  1 242 ? 34.915  12.094  -2.538  1.00 22.11  ? 243  ILE C CD1 1 
ATOM   1929  N N   . ASN A  1 243 ? 35.000  14.755  -6.769  1.00 27.37  ? 244  ASN C N   1 
ATOM   1930  C CA  . ASN A  1 243 ? 34.442  16.020  -7.220  1.00 30.68  ? 244  ASN C CA  1 
ATOM   1931  C C   . ASN A  1 243 ? 33.166  16.447  -6.507  1.00 35.15  ? 244  ASN C C   1 
ATOM   1932  O O   . ASN A  1 243 ? 32.156  15.726  -6.500  1.00 33.06  ? 244  ASN C O   1 
ATOM   1933  C CB  . ASN A  1 243 ? 34.175  15.948  -8.712  1.00 28.94  ? 244  ASN C CB  1 
ATOM   1934  C CG  . ASN A  1 243 ? 35.440  15.824  -9.495  1.00 39.47  ? 244  ASN C CG  1 
ATOM   1935  O OD1 . ASN A  1 243 ? 36.036  16.835  -9.869  1.00 42.90  ? 244  ASN C OD1 1 
ATOM   1936  N ND2 . ASN A  1 243 ? 35.910  14.584  -9.698  1.00 43.70  ? 244  ASN C ND2 1 
ATOM   1937  N N   . PHE A  1 244 ? 33.216  17.648  -5.941  1.00 33.97  ? 245  PHE C N   1 
ATOM   1938  C CA  . PHE A  1 244 ? 32.086  18.215  -5.243  1.00 35.13  ? 245  PHE C CA  1 
ATOM   1939  C C   . PHE A  1 244 ? 31.492  19.407  -5.988  1.00 37.53  ? 245  PHE C C   1 
ATOM   1940  O O   . PHE A  1 244 ? 32.226  20.282  -6.453  1.00 37.34  ? 245  PHE C O   1 
ATOM   1941  C CB  . PHE A  1 244 ? 32.508  18.646  -3.830  1.00 32.02  ? 245  PHE C CB  1 
ATOM   1942  C CG  . PHE A  1 244 ? 32.921  17.509  -2.943  1.00 33.09  ? 245  PHE C CG  1 
ATOM   1943  C CD1 . PHE A  1 244 ? 31.955  16.754  -2.275  1.00 30.90  ? 245  PHE C CD1 1 
ATOM   1944  C CD2 . PHE A  1 244 ? 34.277  17.205  -2.747  1.00 32.18  ? 245  PHE C CD2 1 
ATOM   1945  C CE1 . PHE A  1 244 ? 32.337  15.700  -1.433  1.00 31.23  ? 245  PHE C CE1 1 
ATOM   1946  C CE2 . PHE A  1 244 ? 34.665  16.157  -1.918  1.00 28.17  ? 245  PHE C CE2 1 
ATOM   1947  C CZ  . PHE A  1 244 ? 33.700  15.404  -1.256  1.00 27.58  ? 245  PHE C CZ  1 
ATOM   1948  N N   . GLU A  1 245 ? 30.163  19.453  -6.075  1.00 39.38  ? 246  GLU C N   1 
ATOM   1949  C CA  . GLU A  1 245 ? 29.484  20.641  -6.579  1.00 40.45  ? 246  GLU C CA  1 
ATOM   1950  C C   . GLU A  1 245 ? 28.198  20.898  -5.763  1.00 35.47  ? 246  GLU C C   1 
ATOM   1951  O O   . GLU A  1 245 ? 27.400  19.982  -5.548  1.00 36.98  ? 246  GLU C O   1 
ATOM   1952  C CB  . GLU A  1 245 ? 29.186  20.480  -8.072  1.00 41.92  ? 246  GLU C CB  1 
ATOM   1953  C CG  . GLU A  1 245 ? 28.642  21.723  -8.803  1.00 49.67  ? 246  GLU C CG  1 
ATOM   1954  C CD  . GLU A  1 245 ? 28.411  21.451  -10.297 1.00 59.89  ? 246  GLU C CD  1 
ATOM   1955  O OE1 . GLU A  1 245 ? 29.182  20.643  -10.876 1.00 67.19  ? 246  GLU C OE1 1 
ATOM   1956  O OE2 . GLU A  1 245 ? 27.475  22.047  -10.887 1.00 56.73  ? 246  GLU C OE2 1 
ATOM   1957  N N   . SER A  1 246 ? 28.003  22.130  -5.302  1.00 30.07  ? 247  SER C N   1 
ATOM   1958  C CA  . SER A  1 246 ? 26.863  22.428  -4.460  1.00 34.09  ? 247  SER C CA  1 
ATOM   1959  C C   . SER A  1 246 ? 26.478  23.910  -4.468  1.00 34.96  ? 247  SER C C   1 
ATOM   1960  O O   . SER A  1 246 ? 27.328  24.793  -4.444  1.00 37.51  ? 247  SER C O   1 
ATOM   1961  C CB  . SER A  1 246 ? 27.169  21.996  -3.023  1.00 33.48  ? 247  SER C CB  1 
ATOM   1962  O OG  . SER A  1 246 ? 26.038  22.116  -2.183  1.00 33.52  ? 247  SER C OG  1 
ATOM   1963  N N   . ASN A  1 247 ? 25.182  24.175  -4.432  1.00 35.04  ? 248  ASN C N   1 
ATOM   1964  C CA  . ASN A  1 247 ? 24.705  25.536  -4.229  1.00 40.71  ? 248  ASN C CA  1 
ATOM   1965  C C   . ASN A  1 247 ? 23.930  25.683  -2.913  1.00 45.95  ? 248  ASN C C   1 
ATOM   1966  O O   . ASN A  1 247 ? 23.025  26.523  -2.830  1.00 44.87  ? 248  ASN C O   1 
ATOM   1967  C CB  . ASN A  1 247 ? 23.794  25.976  -5.372  1.00 36.22  ? 248  ASN C CB  1 
ATOM   1968  C CG  . ASN A  1 247 ? 22.486  25.207  -5.388  1.00 40.50  ? 248  ASN C CG  1 
ATOM   1969  O OD1 . ASN A  1 247 ? 22.426  24.035  -4.981  1.00 44.51  ? 248  ASN C OD1 1 
ATOM   1970  N ND2 . ASN A  1 247 ? 21.422  25.870  -5.811  1.00 37.25  ? 248  ASN C ND2 1 
ATOM   1971  N N   . GLY A  1 248 ? 24.248  24.852  -1.908  1.00 44.27  ? 249  GLY C N   1 
ATOM   1972  C CA  . GLY A  1 248 ? 23.700  25.027  -0.561  1.00 40.47  ? 249  GLY C CA  1 
ATOM   1973  C C   . GLY A  1 248 ? 23.512  23.750  0.239   1.00 39.97  ? 249  GLY C C   1 
ATOM   1974  O O   . GLY A  1 248 ? 23.373  22.675  -0.360  1.00 38.24  ? 249  GLY C O   1 
ATOM   1975  N N   . ASN A  1 249 ? 23.485  23.875  1.573   1.00 34.91  ? 250  ASN C N   1 
ATOM   1976  C CA  . ASN A  1 249 ? 23.227  22.762  2.519   1.00 37.18  ? 250  ASN C CA  1 
ATOM   1977  C C   . ASN A  1 249 ? 24.361  21.742  2.599   1.00 33.50  ? 250  ASN C C   1 
ATOM   1978  O O   . ASN A  1 249 ? 24.163  20.607  3.047   1.00 32.45  ? 250  ASN C O   1 
ATOM   1979  C CB  . ASN A  1 249 ? 21.936  22.018  2.138   1.00 40.92  ? 250  ASN C CB  1 
ATOM   1980  C CG  . ASN A  1 249 ? 20.747  22.944  1.983   1.00 39.78  ? 250  ASN C CG  1 
ATOM   1981  O OD1 . ASN A  1 249 ? 20.629  23.662  0.979   1.00 36.09  ? 250  ASN C OD1 1 
ATOM   1982  N ND2 . ASN A  1 249 ? 19.823  22.880  2.936   1.00 40.90  ? 250  ASN C ND2 1 
ATOM   1983  N N   . PHE A  1 250 ? 25.536  22.167  2.156   1.00 33.05  ? 251  PHE C N   1 
ATOM   1984  C CA  . PHE A  1 250 ? 26.709  21.321  1.991   1.00 30.93  ? 251  PHE C CA  1 
ATOM   1985  C C   . PHE A  1 250 ? 27.588  21.380  3.240   1.00 31.08  ? 251  PHE C C   1 
ATOM   1986  O O   . PHE A  1 250 ? 28.061  22.468  3.632   1.00 32.96  ? 251  PHE C O   1 
ATOM   1987  C CB  . PHE A  1 250 ? 27.500  21.785  0.735   1.00 31.76  ? 251  PHE C CB  1 
ATOM   1988  C CG  . PHE A  1 250 ? 28.734  20.964  0.411   1.00 26.53  ? 251  PHE C CG  1 
ATOM   1989  C CD1 . PHE A  1 250 ? 28.781  19.605  0.634   1.00 27.85  ? 251  PHE C CD1 1 
ATOM   1990  C CD2 . PHE A  1 250 ? 29.867  21.582  -0.068  1.00 28.54  ? 251  PHE C CD2 1 
ATOM   1991  C CE1 . PHE A  1 250 ? 29.930  18.871  0.353   1.00 25.66  ? 251  PHE C CE1 1 
ATOM   1992  C CE2 . PHE A  1 250 ? 31.014  20.852  -0.348  1.00 28.76  ? 251  PHE C CE2 1 
ATOM   1993  C CZ  . PHE A  1 250 ? 31.042  19.494  -0.126  1.00 22.28  ? 251  PHE C CZ  1 
ATOM   1994  N N   . ILE A  1 251 ? 27.814  20.223  3.863   1.00 28.00  ? 252  ILE C N   1 
ATOM   1995  C CA  . ILE A  1 251 ? 28.810  20.137  4.934   1.00 32.81  ? 252  ILE C CA  1 
ATOM   1996  C C   . ILE A  1 251 ? 30.124  19.523  4.379   1.00 36.04  ? 252  ILE C C   1 
ATOM   1997  O O   . ILE A  1 251 ? 30.226  18.300  4.207   1.00 35.04  ? 252  ILE C O   1 
ATOM   1998  C CB  . ILE A  1 251 ? 28.304  19.313  6.133   1.00 34.24  ? 252  ILE C CB  1 
ATOM   1999  C CG1 . ILE A  1 251 ? 27.162  20.031  6.849   1.00 39.31  ? 252  ILE C CG1 1 
ATOM   2000  C CG2 . ILE A  1 251 ? 29.400  19.183  7.154   1.00 38.43  ? 252  ILE C CG2 1 
ATOM   2001  C CD1 . ILE A  1 251 ? 25.784  19.638  6.390   1.00 38.13  ? 252  ILE C CD1 1 
ATOM   2002  N N   . ALA A  1 252 ? 31.113  20.380  4.101   1.00 33.04  ? 253  ALA C N   1 
ATOM   2003  C CA  . ALA A  1 252 ? 32.292  20.025  3.312   1.00 30.86  ? 253  ALA C CA  1 
ATOM   2004  C C   . ALA A  1 252 ? 33.420  19.363  4.124   1.00 35.93  ? 253  ALA C C   1 
ATOM   2005  O O   . ALA A  1 252 ? 33.505  19.566  5.330   1.00 39.92  ? 253  ALA C O   1 
ATOM   2006  C CB  . ALA A  1 252 ? 32.810  21.259  2.630   1.00 30.81  ? 253  ALA C CB  1 
ATOM   2007  N N   . PRO A  1 253 ? 34.277  18.556  3.461   1.00 36.20  ? 254  PRO C N   1 
ATOM   2008  C CA  . PRO A  1 253 ? 35.469  17.923  4.053   1.00 33.59  ? 254  PRO C CA  1 
ATOM   2009  C C   . PRO A  1 253 ? 36.536  18.890  4.502   1.00 37.33  ? 254  PRO C C   1 
ATOM   2010  O O   . PRO A  1 253 ? 36.754  19.844  3.782   1.00 45.44  ? 254  PRO C O   1 
ATOM   2011  C CB  . PRO A  1 253 ? 36.039  17.082  2.908   1.00 30.36  ? 254  PRO C CB  1 
ATOM   2012  C CG  . PRO A  1 253 ? 34.911  16.865  1.974   1.00 31.35  ? 254  PRO C CG  1 
ATOM   2013  C CD  . PRO A  1 253 ? 34.008  18.046  2.099   1.00 32.41  ? 254  PRO C CD  1 
ATOM   2014  N N   . GLU A  1 254 ? 37.161  18.677  5.661   1.00 41.46  ? 255  GLU C N   1 
ATOM   2015  C CA  . GLU A  1 254 ? 38.436  19.341  5.936   1.00 43.22  ? 255  GLU C CA  1 
ATOM   2016  C C   . GLU A  1 254 ? 39.605  18.349  6.104   1.00 41.16  ? 255  GLU C C   1 
ATOM   2017  O O   . GLU A  1 254 ? 40.666  18.549  5.513   1.00 43.66  ? 255  GLU C O   1 
ATOM   2018  C CB  . GLU A  1 254 ? 38.379  20.236  7.163   1.00 47.35  ? 255  GLU C CB  1 
ATOM   2019  C CG  . GLU A  1 254 ? 39.729  20.939  7.348   1.00 49.69  ? 255  GLU C CG  1 
ATOM   2020  C CD  . GLU A  1 254 ? 39.699  22.011  8.391   1.00 56.26  ? 255  GLU C CD  1 
ATOM   2021  O OE1 . GLU A  1 254 ? 38.814  22.887  8.289   1.00 57.88  ? 255  GLU C OE1 1 
ATOM   2022  O OE2 . GLU A  1 254 ? 40.581  21.984  9.289   1.00 60.33  ? 255  GLU C OE2 1 
ATOM   2023  N N   . ASN A  1 255 ? 39.418  17.298  6.910   1.00 41.72  ? 256  ASN C N   1 
ATOM   2024  C CA  . ASN A  1 255 ? 40.460  16.268  7.137   1.00 41.61  ? 256  ASN C CA  1 
ATOM   2025  C C   . ASN A  1 255 ? 40.035  14.881  6.643   1.00 34.90  ? 256  ASN C C   1 
ATOM   2026  O O   . ASN A  1 255 ? 38.846  14.598  6.588   1.00 33.53  ? 256  ASN C O   1 
ATOM   2027  C CB  . ASN A  1 255 ? 40.805  16.174  8.632   1.00 40.16  ? 256  ASN C CB  1 
ATOM   2028  C CG  . ASN A  1 255 ? 41.335  17.491  9.210   1.00 42.55  ? 256  ASN C CG  1 
ATOM   2029  O OD1 . ASN A  1 255 ? 42.137  18.181  8.582   1.00 43.86  ? 256  ASN C OD1 1 
ATOM   2030  N ND2 . ASN A  1 255 ? 40.841  17.862  10.397  1.00 38.23  ? 256  ASN C ND2 1 
ATOM   2031  N N   . ALA A  1 256 ? 40.989  14.037  6.248   1.00 27.87  ? 257  ALA C N   1 
ATOM   2032  C CA  . ALA A  1 256 ? 40.669  12.662  5.862   1.00 28.22  ? 257  ALA C CA  1 
ATOM   2033  C C   . ALA A  1 256 ? 41.732  11.643  6.364   1.00 32.19  ? 257  ALA C C   1 
ATOM   2034  O O   . ALA A  1 256 ? 42.787  12.058  6.853   1.00 35.33  ? 257  ALA C O   1 
ATOM   2035  C CB  . ALA A  1 256 ? 40.503  12.582  4.368   1.00 31.08  ? 257  ALA C CB  1 
ATOM   2036  N N   . TYR A  1 257 ? 41.509  10.331  6.199   1.00 26.22  ? 258  TYR C N   1 
ATOM   2037  C CA  . TYR A  1 257 ? 42.435  9.345   6.788   1.00 29.42  ? 258  TYR C CA  1 
ATOM   2038  C C   . TYR A  1 257 ? 43.205  8.430   5.786   1.00 33.60  ? 258  TYR C C   1 
ATOM   2039  O O   . TYR A  1 257 ? 42.609  7.766   4.931   1.00 35.54  ? 258  TYR C O   1 
ATOM   2040  C CB  . TYR A  1 257 ? 41.666  8.455   7.773   1.00 26.72  ? 258  TYR C CB  1 
ATOM   2041  C CG  . TYR A  1 257 ? 40.993  9.211   8.886   1.00 30.67  ? 258  TYR C CG  1 
ATOM   2042  C CD1 . TYR A  1 257 ? 39.749  9.796   8.683   1.00 29.88  ? 258  TYR C CD1 1 
ATOM   2043  C CD2 . TYR A  1 257 ? 41.586  9.337   10.143  1.00 29.23  ? 258  TYR C CD2 1 
ATOM   2044  C CE1 . TYR A  1 257 ? 39.113  10.494  9.691   1.00 29.31  ? 258  TYR C CE1 1 
ATOM   2045  C CE2 . TYR A  1 257 ? 40.951  10.027  11.167  1.00 26.40  ? 258  TYR C CE2 1 
ATOM   2046  C CZ  . TYR A  1 257 ? 39.704  10.605  10.935  1.00 29.88  ? 258  TYR C CZ  1 
ATOM   2047  O OH  . TYR A  1 257 ? 39.028  11.313  11.925  1.00 30.86  ? 258  TYR C OH  1 
ATOM   2048  N N   . LYS A  1 258 ? 44.532  8.380   5.902   1.00 31.33  ? 259  LYS C N   1 
ATOM   2049  C CA  . LYS A  1 258 ? 45.300  7.468   5.053   1.00 30.85  ? 259  LYS C CA  1 
ATOM   2050  C C   . LYS A  1 258 ? 45.368  6.096   5.701   1.00 34.25  ? 259  LYS C C   1 
ATOM   2051  O O   . LYS A  1 258 ? 45.728  5.956   6.879   1.00 34.57  ? 259  LYS C O   1 
ATOM   2052  C CB  . LYS A  1 258 ? 46.712  8.021   4.785   1.00 36.88  ? 259  LYS C CB  1 
ATOM   2053  C CG  . LYS A  1 258 ? 46.710  9.323   3.973   1.00 40.01  ? 259  LYS C CG  1 
ATOM   2054  C CD  . LYS A  1 258 ? 48.078  9.750   3.429   1.00 44.36  ? 259  LYS C CD  1 
ATOM   2055  C CE  . LYS A  1 258 ? 49.058  10.091  4.546   1.00 48.83  ? 259  LYS C CE  1 
ATOM   2056  N NZ  . LYS A  1 258 ? 50.337  10.669  4.026   1.00 51.41  ? 259  LYS C NZ  1 
ATOM   2057  N N   . ILE A  1 259 ? 44.983  5.083   4.935   1.00 33.77  ? 260  ILE C N   1 
ATOM   2058  C CA  . ILE A  1 259 ? 45.006  3.721   5.428   1.00 28.46  ? 260  ILE C CA  1 
ATOM   2059  C C   . ILE A  1 259 ? 46.405  3.173   5.266   1.00 33.93  ? 260  ILE C C   1 
ATOM   2060  O O   . ILE A  1 259 ? 46.833  2.883   4.150   1.00 35.22  ? 260  ILE C O   1 
ATOM   2061  C CB  . ILE A  1 259 ? 43.956  2.844   4.728   1.00 27.86  ? 260  ILE C CB  1 
ATOM   2062  C CG1 . ILE A  1 259 ? 42.556  3.346   5.112   1.00 31.35  ? 260  ILE C CG1 1 
ATOM   2063  C CG2 . ILE A  1 259 ? 44.063  1.396   5.185   1.00 25.25  ? 260  ILE C CG2 1 
ATOM   2064  C CD1 . ILE A  1 259 ? 41.436  3.026   4.133   1.00 29.75  ? 260  ILE C CD1 1 
ATOM   2065  N N   . VAL A  1 260 A 47.103  3.051   6.404   1.00 34.61  ? 260  VAL C N   1 
ATOM   2066  C CA  . VAL A  1 260 A 48.534  2.783   6.449   1.00 34.53  ? 260  VAL C CA  1 
ATOM   2067  C C   . VAL A  1 260 A 48.827  1.311   6.668   1.00 41.22  ? 260  VAL C C   1 
ATOM   2068  O O   . VAL A  1 260 A 49.754  0.752   6.072   1.00 44.51  ? 260  VAL C O   1 
ATOM   2069  C CB  . VAL A  1 260 A 49.229  3.565   7.610   1.00 42.02  ? 260  VAL C CB  1 
ATOM   2070  C CG1 . VAL A  1 260 A 50.646  3.023   7.844   1.00 37.21  ? 260  VAL C CG1 1 
ATOM   2071  C CG2 . VAL A  1 260 A 49.258  5.085   7.352   1.00 36.74  ? 260  VAL C CG2 1 
ATOM   2072  N N   . LYS A  1 261 ? 48.012  0.665   7.494   1.00 40.36  ? 261  LYS C N   1 
ATOM   2073  C CA  . LYS A  1 261 ? 48.203  -0.755  7.775   1.00 38.33  ? 261  LYS C CA  1 
ATOM   2074  C C   . LYS A  1 261 ? 46.909  -1.543  7.946   1.00 38.96  ? 261  LYS C C   1 
ATOM   2075  O O   . LYS A  1 261 ? 46.029  -1.140  8.716   1.00 40.83  ? 261  LYS C O   1 
ATOM   2076  C CB  . LYS A  1 261 ? 49.040  -0.935  9.042   1.00 41.04  ? 261  LYS C CB  1 
ATOM   2077  C CG  . LYS A  1 261 ? 49.268  -2.412  9.376   1.00 44.09  ? 261  LYS C CG  1 
ATOM   2078  C CD  . LYS A  1 261 ? 50.319  -2.633  10.443  1.00 45.22  ? 261  LYS C CD  1 
ATOM   2079  C CE  . LYS A  1 261 ? 50.350  -4.111  10.842  1.00 47.92  ? 261  LYS C CE  1 
ATOM   2080  N NZ  . LYS A  1 261 ? 51.137  -4.327  12.078  1.00 48.16  ? 261  LYS C NZ  1 
ATOM   2081  N N   . LYS A  1 262 ? 46.785  -2.674  7.264   1.00 39.44  ? 262  LYS C N   1 
ATOM   2082  C CA  . LYS A  1 262 ? 45.640  -3.550  7.519   1.00 38.64  ? 262  LYS C CA  1 
ATOM   2083  C C   . LYS A  1 262 ? 46.051  -4.814  8.292   1.00 39.05  ? 262  LYS C C   1 
ATOM   2084  O O   . LYS A  1 262 ? 47.208  -5.227  8.249   1.00 43.75  ? 262  LYS C O   1 
ATOM   2085  C CB  . LYS A  1 262 ? 44.920  -3.938  6.215   1.00 30.29  ? 262  LYS C CB  1 
ATOM   2086  C CG  . LYS A  1 262 ? 44.030  -2.832  5.659   1.00 32.73  ? 262  LYS C CG  1 
ATOM   2087  C CD  . LYS A  1 262 ? 43.121  -3.314  4.518   1.00 42.47  ? 262  LYS C CD  1 
ATOM   2088  C CE  . LYS A  1 262 ? 42.146  -2.198  4.096   1.00 42.18  ? 262  LYS C CE  1 
ATOM   2089  N NZ  . LYS A  1 262 ? 41.216  -2.580  2.987   1.00 46.28  ? 262  LYS C NZ  1 
ATOM   2090  N N   . GLY A  1 263 ? 45.097  -5.412  9.004   1.00 37.49  ? 263  GLY C N   1 
ATOM   2091  C CA  . GLY A  1 263 ? 45.336  -6.643  9.743   1.00 37.36  ? 263  GLY C CA  1 
ATOM   2092  C C   . GLY A  1 263 ? 44.133  -7.151  10.531  1.00 43.52  ? 263  GLY C C   1 
ATOM   2093  O O   . GLY A  1 263 ? 43.001  -6.709  10.316  1.00 48.20  ? 263  GLY C O   1 
ATOM   2094  N N   . ASP A  1 264 ? 44.370  -8.057  11.474  1.00 51.81  ? 264  ASP C N   1 
ATOM   2095  C CA  . ASP A  1 264 ? 43.279  -8.581  12.301  1.00 52.91  ? 264  ASP C CA  1 
ATOM   2096  C C   . ASP A  1 264 ? 43.072  -7.653  13.464  1.00 45.28  ? 264  ASP C C   1 
ATOM   2097  O O   . ASP A  1 264 ? 44.016  -7.255  14.165  1.00 44.14  ? 264  ASP C O   1 
ATOM   2098  C CB  . ASP A  1 264 ? 43.560  -9.998  12.798  1.00 60.80  ? 264  ASP C CB  1 
ATOM   2099  C CG  . ASP A  1 264 ? 43.223  -11.036 11.765  1.00 65.81  ? 264  ASP C CG  1 
ATOM   2100  O OD1 . ASP A  1 264 ? 42.513  -10.671 10.797  1.00 63.82  ? 264  ASP C OD1 1 
ATOM   2101  O OD2 . ASP A  1 264 ? 43.677  -12.195 11.913  1.00 75.38  ? 264  ASP C OD2 1 
ATOM   2102  N N   . SER A  1 265 ? 41.822  -7.257  13.612  1.00 42.66  ? 265  SER C N   1 
ATOM   2103  C CA  . SER A  1 265 ? 41.445  -6.331  14.647  1.00 37.36  ? 265  SER C CA  1 
ATOM   2104  C C   . SER A  1 265 ? 39.987  -6.628  14.875  1.00 37.50  ? 265  SER C C   1 
ATOM   2105  O O   . SER A  1 265 ? 39.442  -7.549  14.275  1.00 35.64  ? 265  SER C O   1 
ATOM   2106  C CB  . SER A  1 265 ? 41.703  -4.895  14.217  1.00 35.14  ? 265  SER C CB  1 
ATOM   2107  O OG  . SER A  1 265 ? 41.371  -3.983  15.240  1.00 36.62  ? 265  SER C OG  1 
ATOM   2108  N N   . THR A  1 266 ? 39.373  -5.915  15.798  1.00 34.68  ? 266  THR C N   1 
ATOM   2109  C CA  . THR A  1 266 ? 37.968  -6.089  16.070  1.00 29.09  ? 266  THR C CA  1 
ATOM   2110  C C   . THR A  1 266 ? 37.473  -4.859  16.804  1.00 32.25  ? 266  THR C C   1 
ATOM   2111  O O   . THR A  1 266 ? 38.287  -4.054  17.298  1.00 30.74  ? 266  THR C O   1 
ATOM   2112  C CB  . THR A  1 266 ? 37.743  -7.386  16.888  1.00 27.69  ? 266  THR C CB  1 
ATOM   2113  O OG1 . THR A  1 266 ? 36.350  -7.552  17.141  1.00 27.96  ? 266  THR C OG1 1 
ATOM   2114  C CG2 . THR A  1 266 ? 38.433  -7.300  18.230  1.00 28.06  ? 266  THR C CG2 1 
ATOM   2115  N N   . ILE A  1 267 ? 36.154  -4.706  16.904  1.00 33.87  ? 267  ILE C N   1 
ATOM   2116  C CA  . ILE A  1 267 ? 35.610  -3.660  17.772  1.00 32.71  ? 267  ILE C CA  1 
ATOM   2117  C C   . ILE A  1 267 ? 34.893  -4.321  18.973  1.00 32.05  ? 267  ILE C C   1 
ATOM   2118  O O   . ILE A  1 267 ? 33.879  -4.990  18.807  1.00 40.11  ? 267  ILE C O   1 
ATOM   2119  C CB  . ILE A  1 267 ? 34.665  -2.708  17.001  1.00 26.32  ? 267  ILE C CB  1 
ATOM   2120  C CG1 . ILE A  1 267 ? 35.412  -2.047  15.842  1.00 26.12  ? 267  ILE C CG1 1 
ATOM   2121  C CG2 . ILE A  1 267 ? 34.101  -1.593  17.914  1.00 25.18  ? 267  ILE C CG2 1 
ATOM   2122  C CD1 . ILE A  1 267 ? 34.560  -1.041  15.052  1.00 23.40  ? 267  ILE C CD1 1 
ATOM   2123  N N   . MET A  1 268 ? 35.435  -4.134  20.171  1.00 28.86  ? 268  MET C N   1 
ATOM   2124  C CA  . MET A  1 268 ? 34.891  -4.737  21.388  1.00 31.29  ? 268  MET C CA  1 
ATOM   2125  C C   . MET A  1 268 ? 33.897  -3.827  22.090  1.00 33.01  ? 268  MET C C   1 
ATOM   2126  O O   . MET A  1 268 ? 34.100  -2.611  22.174  1.00 34.63  ? 268  MET C O   1 
ATOM   2127  C CB  . MET A  1 268 ? 36.013  -5.120  22.379  1.00 28.74  ? 268  MET C CB  1 
ATOM   2128  C CG  . MET A  1 268 ? 36.404  -6.599  22.297  1.00 47.84  ? 268  MET C CG  1 
ATOM   2129  S SD  . MET A  1 268 ? 37.865  -7.162  23.234  1.00 46.57  ? 268  MET C SD  1 
ATOM   2130  C CE  . MET A  1 268 ? 37.689  -6.175  24.683  1.00 27.21  ? 268  MET C CE  1 
ATOM   2131  N N   . LYS A  1 269 ? 32.826  -4.437  22.592  1.00 31.61  ? 269  LYS C N   1 
ATOM   2132  C CA  . LYS A  1 269 ? 31.823  -3.750  23.389  1.00 33.21  ? 269  LYS C CA  1 
ATOM   2133  C C   . LYS A  1 269 ? 32.119  -3.991  24.874  1.00 35.11  ? 269  LYS C C   1 
ATOM   2134  O O   . LYS A  1 269 ? 31.979  -5.115  25.347  1.00 35.77  ? 269  LYS C O   1 
ATOM   2135  C CB  . LYS A  1 269 ? 30.438  -4.275  23.025  1.00 32.57  ? 269  LYS C CB  1 
ATOM   2136  C CG  . LYS A  1 269 ? 30.077  -4.045  21.602  1.00 31.36  ? 269  LYS C CG  1 
ATOM   2137  C CD  . LYS A  1 269 ? 29.978  -2.555  21.409  1.00 40.53  ? 269  LYS C CD  1 
ATOM   2138  C CE  . LYS A  1 269 ? 29.525  -2.124  20.027  1.00 33.71  ? 269  LYS C CE  1 
ATOM   2139  N NZ  . LYS A  1 269 ? 29.060  -0.702  20.273  1.00 44.08  ? 269  LYS C NZ  1 
ATOM   2140  N N   . SER A  1 270 ? 32.526  -2.959  25.605  1.00 31.59  ? 270  SER C N   1 
ATOM   2141  C CA  . SER A  1 270 ? 32.954  -3.154  26.984  1.00 34.61  ? 270  SER C CA  1 
ATOM   2142  C C   . SER A  1 270 ? 32.892  -1.865  27.789  1.00 37.33  ? 270  SER C C   1 
ATOM   2143  O O   . SER A  1 270 ? 33.080  -0.779  27.245  1.00 37.24  ? 270  SER C O   1 
ATOM   2144  C CB  . SER A  1 270 ? 34.378  -3.717  27.006  1.00 39.08  ? 270  SER C CB  1 
ATOM   2145  O OG  . SER A  1 270 ? 34.870  -3.809  28.328  1.00 42.19  ? 270  SER C OG  1 
ATOM   2146  N N   . GLU A  1 271 ? 32.698  -1.991  29.098  1.00 42.90  ? 271  GLU C N   1 
ATOM   2147  C CA  . GLU A  1 271 ? 32.603  -0.817  29.965  1.00 40.82  ? 271  GLU C CA  1 
ATOM   2148  C C   . GLU A  1 271 ? 33.929  -0.515  30.660  1.00 43.73  ? 271  GLU C C   1 
ATOM   2149  O O   . GLU A  1 271 ? 34.106  0.566   31.207  1.00 48.52  ? 271  GLU C O   1 
ATOM   2150  C CB  . GLU A  1 271 ? 31.486  -1.017  30.989  1.00 38.39  ? 271  GLU C CB  1 
ATOM   2151  C CG  . GLU A  1 271 ? 30.082  -1.203  30.362  1.00 38.96  ? 271  GLU C CG  1 
ATOM   2152  C CD  . GLU A  1 271 ? 29.619  0.038   29.600  1.00 50.42  ? 271  GLU C CD  1 
ATOM   2153  O OE1 . GLU A  1 271 ? 29.682  1.141   30.206  1.00 49.46  ? 271  GLU C OE1 1 
ATOM   2154  O OE2 . GLU A  1 271 ? 29.220  -0.083  28.409  1.00 45.42  ? 271  GLU C OE2 1 
ATOM   2155  N N   . LEU A  1 272 ? 34.891  -1.426  30.524  1.00 45.92  ? 272  LEU C N   1 
ATOM   2156  C CA  . LEU A  1 272 ? 36.197  -1.311  31.168  1.00 40.08  ? 272  LEU C CA  1 
ATOM   2157  C C   . LEU A  1 272 ? 37.060  -0.200  30.556  1.00 48.21  ? 272  LEU C C   1 
ATOM   2158  O O   . LEU A  1 272 ? 36.662  0.457   29.579  1.00 46.12  ? 272  LEU C O   1 
ATOM   2159  C CB  . LEU A  1 272 ? 36.959  -2.630  31.062  1.00 39.61  ? 272  LEU C CB  1 
ATOM   2160  C CG  . LEU A  1 272 ? 36.236  -3.892  31.512  1.00 45.67  ? 272  LEU C CG  1 
ATOM   2161  C CD1 . LEU A  1 272 ? 37.121  -5.120  31.280  1.00 36.50  ? 272  LEU C CD1 1 
ATOM   2162  C CD2 . LEU A  1 272 ? 35.870  -3.741  32.982  1.00 39.05  ? 272  LEU C CD2 1 
ATOM   2163  N N   . GLU A  1 273 ? 38.211  0.037   31.193  1.00 44.79  ? 273  GLU C N   1 
ATOM   2164  C CA  . GLU A  1 273 ? 39.227  0.984   30.735  1.00 39.39  ? 273  GLU C CA  1 
ATOM   2165  C C   . GLU A  1 273 ? 40.602  0.318   30.766  1.00 42.61  ? 273  GLU C C   1 
ATOM   2166  O O   . GLU A  1 273 ? 40.726  -0.837  31.223  1.00 36.50  ? 273  GLU C O   1 
ATOM   2167  C CB  . GLU A  1 273 ? 39.221  2.248   31.596  1.00 49.22  ? 273  GLU C CB  1 
ATOM   2168  C CG  . GLU A  1 273 ? 37.919  3.011   31.467  1.00 55.04  ? 273  GLU C CG  1 
ATOM   2169  C CD  . GLU A  1 273 ? 37.762  3.621   30.070  1.00 64.41  ? 273  GLU C CD  1 
ATOM   2170  O OE1 . GLU A  1 273 ? 38.807  3.904   29.421  1.00 62.11  ? 273  GLU C OE1 1 
ATOM   2171  O OE2 . GLU A  1 273 ? 36.595  3.764   29.608  1.00 59.52  ? 273  GLU C OE2 1 
ATOM   2172  N N   . TYR A  1 274 ? 41.620  1.031   30.265  1.00 40.17  ? 274  TYR C N   1 
ATOM   2173  C CA  . TYR A  1 274 ? 42.989  0.499   30.201  1.00 36.09  ? 274  TYR C CA  1 
ATOM   2174  C C   . TYR A  1 274 ? 43.468  0.002   31.558  1.00 39.53  ? 274  TYR C C   1 
ATOM   2175  O O   . TYR A  1 274 ? 43.072  0.552   32.579  1.00 41.94  ? 274  TYR C O   1 
ATOM   2176  C CB  . TYR A  1 274 ? 43.934  1.553   29.666  1.00 35.50  ? 274  TYR C CB  1 
ATOM   2177  C CG  . TYR A  1 274 ? 45.288  1.018   29.273  1.00 38.20  ? 274  TYR C CG  1 
ATOM   2178  C CD1 . TYR A  1 274 ? 45.418  -0.157  28.531  1.00 35.75  ? 274  TYR C CD1 1 
ATOM   2179  C CD2 . TYR A  1 274 ? 46.439  1.719   29.603  1.00 35.27  ? 274  TYR C CD2 1 
ATOM   2180  C CE1 . TYR A  1 274 ? 46.676  -0.634  28.169  1.00 37.08  ? 274  TYR C CE1 1 
ATOM   2181  C CE2 . TYR A  1 274 ? 47.684  1.255   29.251  1.00 37.00  ? 274  TYR C CE2 1 
ATOM   2182  C CZ  . TYR A  1 274 ? 47.804  0.087   28.534  1.00 37.22  ? 274  TYR C CZ  1 
ATOM   2183  O OH  . TYR A  1 274 ? 49.067  -0.337  28.193  1.00 36.31  ? 274  TYR C OH  1 
ATOM   2184  N N   . GLY A  1 275 ? 44.331  -1.017  31.563  1.00 39.75  ? 275  GLY C N   1 
ATOM   2185  C CA  . GLY A  1 275 ? 44.754  -1.673  32.800  1.00 37.13  ? 275  GLY C CA  1 
ATOM   2186  C C   . GLY A  1 275 ? 46.264  -1.752  32.972  1.00 36.34  ? 275  GLY C C   1 
ATOM   2187  O O   . GLY A  1 275 ? 46.766  -2.451  33.837  1.00 33.46  ? 275  GLY C O   1 
ATOM   2188  N N   . ASP A  1 276 ? 46.979  -1.054  32.091  1.00 44.68  ? 276  ASP C N   1 
ATOM   2189  C CA  . ASP A  1 276 ? 48.448  -0.936  32.086  1.00 43.13  ? 276  ASP C CA  1 
ATOM   2190  C C   . ASP A  1 276 ? 49.158  -2.300  32.192  1.00 45.99  ? 276  ASP C C   1 
ATOM   2191  O O   . ASP A  1 276 ? 50.145  -2.451  32.924  1.00 45.31  ? 276  ASP C O   1 
ATOM   2192  C CB  . ASP A  1 276 ? 48.887  -0.006  33.228  1.00 36.03  ? 276  ASP C CB  1 
ATOM   2193  C CG  . ASP A  1 276 ? 48.348  1.414   33.055  1.00 40.56  ? 276  ASP C CG  1 
ATOM   2194  O OD1 . ASP A  1 276 ? 48.950  2.240   32.314  1.00 39.36  ? 276  ASP C OD1 1 
ATOM   2195  O OD2 . ASP A  1 276 ? 47.291  1.685   33.669  1.00 38.88  ? 276  ASP C OD2 1 
ATOM   2196  N N   . CYS A  1 277 ? 48.625  -3.292  31.481  1.00 42.31  ? 277  CYS C N   1 
ATOM   2197  C CA  . CYS A  1 277 ? 49.158  -4.652  31.511  1.00 38.89  ? 277  CYS C CA  1 
ATOM   2198  C C   . CYS A  1 277 ? 49.420  -5.189  30.080  1.00 38.83  ? 277  CYS C C   1 
ATOM   2199  O O   . CYS A  1 277 ? 49.155  -4.509  29.077  1.00 35.88  ? 277  CYS C O   1 
ATOM   2200  C CB  . CYS A  1 277 ? 48.179  -5.555  32.282  1.00 34.02  ? 277  CYS C CB  1 
ATOM   2201  S SG  . CYS A  1 277 ? 46.424  -5.443  31.651  1.00 50.92  ? 277  CYS C SG  1 
ATOM   2202  N N   . ASN A  1 278 ? 49.864  -6.436  29.982  1.00 37.78  ? 278  ASN C N   1 
ATOM   2203  C CA  . ASN A  1 278 ? 50.101  -7.018  28.684  1.00 29.05  ? 278  ASN C CA  1 
ATOM   2204  C C   . ASN A  1 278 ? 49.637  -8.466  28.623  1.00 31.80  ? 278  ASN C C   1 
ATOM   2205  O O   . ASN A  1 278 ? 49.762  -9.173  29.603  1.00 40.07  ? 278  ASN C O   1 
ATOM   2206  C CB  . ASN A  1 278 ? 51.570  -6.961  28.317  1.00 31.28  ? 278  ASN C CB  1 
ATOM   2207  C CG  . ASN A  1 278 ? 51.773  -7.270  26.855  1.00 36.64  ? 278  ASN C CG  1 
ATOM   2208  O OD1 . ASN A  1 278 ? 50.839  -7.102  26.073  1.00 35.25  ? 278  ASN C OD1 1 
ATOM   2209  N ND2 . ASN A  1 278 ? 52.934  -7.767  26.481  1.00 32.24  ? 278  ASN C ND2 1 
ATOM   2210  N N   . THR A  1 279 ? 49.099  -8.889  27.469  1.00 34.81  ? 279  THR C N   1 
ATOM   2211  C CA  . THR A  1 279 ? 48.533  -10.235 27.248  1.00 30.19  ? 279  THR C CA  1 
ATOM   2212  C C   . THR A  1 279 ? 48.568  -10.713 25.776  1.00 34.64  ? 279  THR C C   1 
ATOM   2213  O O   . THR A  1 279 ? 48.821  -9.938  24.849  1.00 32.13  ? 279  THR C O   1 
ATOM   2214  C CB  . THR A  1 279 ? 47.052  -10.298 27.732  1.00 30.63  ? 279  THR C CB  1 
ATOM   2215  O OG1 . THR A  1 279 ? 46.554  -11.642 27.623  1.00 32.12  ? 279  THR C OG1 1 
ATOM   2216  C CG2 . THR A  1 279 ? 46.171  -9.391  26.892  1.00 30.99  ? 279  THR C CG2 1 
ATOM   2217  N N   . LYS A  1 280 ? 48.216  -11.982 25.578  1.00 38.91  ? 280  LYS C N   1 
ATOM   2218  C CA  . LYS A  1 280 ? 48.135  -12.603 24.255  1.00 32.94  ? 280  LYS C CA  1 
ATOM   2219  C C   . LYS A  1 280 ? 46.714  -13.085 23.963  1.00 33.08  ? 280  LYS C C   1 
ATOM   2220  O O   . LYS A  1 280 ? 46.435  -13.660 22.901  1.00 37.73  ? 280  LYS C O   1 
ATOM   2221  C CB  . LYS A  1 280 ? 49.124  -13.776 24.171  1.00 36.18  ? 280  LYS C CB  1 
ATOM   2222  C CG  . LYS A  1 280 ? 50.573  -13.315 24.031  1.00 49.92  ? 280  LYS C CG  1 
ATOM   2223  C CD  . LYS A  1 280 ? 51.558  -14.431 23.692  1.00 57.67  ? 280  LYS C CD  1 
ATOM   2224  C CE  . LYS A  1 280 ? 52.982  -13.857 23.567  1.00 59.41  ? 280  LYS C CE  1 
ATOM   2225  N NZ  . LYS A  1 280 ? 54.068  -14.891 23.612  1.00 59.81  ? 280  LYS C NZ  1 
ATOM   2226  N N   . CYS A  1 281 ? 45.815  -12.817 24.903  1.00 32.94  ? 281  CYS C N   1 
ATOM   2227  C CA  . CYS A  1 281 ? 44.406  -13.171 24.754  1.00 36.70  ? 281  CYS C CA  1 
ATOM   2228  C C   . CYS A  1 281 ? 43.513  -12.192 25.509  1.00 32.14  ? 281  CYS C C   1 
ATOM   2229  O O   . CYS A  1 281 ? 43.615  -12.080 26.739  1.00 38.39  ? 281  CYS C O   1 
ATOM   2230  C CB  . CYS A  1 281 ? 44.160  -14.603 25.260  1.00 36.49  ? 281  CYS C CB  1 
ATOM   2231  S SG  . CYS A  1 281 ? 42.455  -15.185 25.005  1.00 43.57  ? 281  CYS C SG  1 
ATOM   2232  N N   . GLN A  1 282 ? 42.640  -11.499 24.787  1.00 29.56  ? 282  GLN C N   1 
ATOM   2233  C CA  . GLN A  1 282 ? 41.773  -10.459 25.360  1.00 28.36  ? 282  GLN C CA  1 
ATOM   2234  C C   . GLN A  1 282 ? 40.289  -10.778 25.073  1.00 34.42  ? 282  GLN C C   1 
ATOM   2235  O O   . GLN A  1 282 ? 39.944  -11.210 23.948  1.00 37.53  ? 282  GLN C O   1 
ATOM   2236  C CB  . GLN A  1 282 ? 42.143  -9.078  24.797  1.00 25.40  ? 282  GLN C CB  1 
ATOM   2237  C CG  . GLN A  1 282 ? 41.367  -7.922  25.425  1.00 30.73  ? 282  GLN C CG  1 
ATOM   2238  C CD  . GLN A  1 282 ? 41.736  -7.707  26.905  1.00 32.83  ? 282  GLN C CD  1 
ATOM   2239  O OE1 . GLN A  1 282 ? 42.854  -7.286  27.239  1.00 25.46  ? 282  GLN C OE1 1 
ATOM   2240  N NE2 . GLN A  1 282 ? 40.819  -8.080  27.793  1.00 31.28  ? 282  GLN C NE2 1 
ATOM   2241  N N   . THR A  1 283 ? 39.439  -10.594 26.095  1.00 28.68  ? 283  THR C N   1 
ATOM   2242  C CA  . THR A  1 283 ? 37.968  -10.729 26.022  1.00 30.38  ? 283  THR C CA  1 
ATOM   2243  C C   . THR A  1 283 ? 37.374  -9.415  26.553  1.00 32.44  ? 283  THR C C   1 
ATOM   2244  O O   . THR A  1 283 ? 38.098  -8.655  27.203  1.00 30.67  ? 283  THR C O   1 
ATOM   2245  C CB  . THR A  1 283 ? 37.416  -11.949 26.849  1.00 30.59  ? 283  THR C CB  1 
ATOM   2246  O OG1 . THR A  1 283 ? 37.212  -11.553 28.212  1.00 34.52  ? 283  THR C OG1 1 
ATOM   2247  C CG2 . THR A  1 283 ? 38.347  -13.132 26.801  1.00 30.01  ? 283  THR C CG2 1 
ATOM   2248  N N   . PRO A  1 284 ? 36.071  -9.140  26.275  1.00 35.78  ? 284  PRO C N   1 
ATOM   2249  C CA  . PRO A  1 284 ? 35.435  -7.865  26.682  1.00 35.90  ? 284  PRO C CA  1 
ATOM   2250  C C   . PRO A  1 284 ? 35.359  -7.621  28.198  1.00 40.29  ? 284  PRO C C   1 
ATOM   2251  O O   . PRO A  1 284 ? 35.077  -6.482  28.609  1.00 38.50  ? 284  PRO C O   1 
ATOM   2252  C CB  . PRO A  1 284 ? 34.015  -7.966  26.093  1.00 35.31  ? 284  PRO C CB  1 
ATOM   2253  C CG  . PRO A  1 284 ? 34.129  -8.949  24.974  1.00 34.75  ? 284  PRO C CG  1 
ATOM   2254  C CD  . PRO A  1 284 ? 35.163  -9.951  25.436  1.00 31.68  ? 284  PRO C CD  1 
ATOM   2255  N N   . ILE A  1 285 ? 35.561  -8.671  29.002  1.00 35.50  ? 285  ILE C N   1 
ATOM   2256  C CA  . ILE A  1 285 ? 35.465  -8.536  30.447  1.00 36.32  ? 285  ILE C CA  1 
ATOM   2257  C C   . ILE A  1 285 ? 36.793  -8.848  31.169  1.00 41.44  ? 285  ILE C C   1 
ATOM   2258  O O   . ILE A  1 285 ? 36.843  -8.890  32.417  1.00 42.98  ? 285  ILE C O   1 
ATOM   2259  C CB  . ILE A  1 285 ? 34.385  -9.463  31.010  1.00 38.33  ? 285  ILE C CB  1 
ATOM   2260  C CG1 . ILE A  1 285 ? 34.869  -10.921 30.981  1.00 38.03  ? 285  ILE C CG1 1 
ATOM   2261  C CG2 . ILE A  1 285 ? 33.093  -9.265  30.249  1.00 35.61  ? 285  ILE C CG2 1 
ATOM   2262  C CD1 . ILE A  1 285 ? 33.865  -11.926 31.512  1.00 33.79  ? 285  ILE C CD1 1 
ATOM   2263  N N   . GLY A  1 286 ? 37.855  -9.117  30.407  1.00 34.90  ? 286  GLY C N   1 
ATOM   2264  C CA  . GLY A  1 286 ? 39.144  -9.394  31.019  1.00 33.83  ? 286  GLY C CA  1 
ATOM   2265  C C   . GLY A  1 286 ? 40.084  -10.256 30.199  1.00 33.00  ? 286  GLY C C   1 
ATOM   2266  O O   . GLY A  1 286 ? 39.640  -10.996 29.316  1.00 29.92  ? 286  GLY C O   1 
ATOM   2267  N N   . ALA A  1 287 ? 41.376  -10.205 30.524  1.00 30.32  ? 287  ALA C N   1 
ATOM   2268  C CA  . ALA A  1 287 ? 42.362  -10.946 29.751  1.00 30.76  ? 287  ALA C CA  1 
ATOM   2269  C C   . ALA A  1 287 ? 42.706  -12.304 30.384  1.00 33.86  ? 287  ALA C C   1 
ATOM   2270  O O   . ALA A  1 287 ? 42.434  -12.562 31.558  1.00 31.10  ? 287  ALA C O   1 
ATOM   2271  C CB  . ALA A  1 287 ? 43.620  -10.108 29.558  1.00 33.57  ? 287  ALA C CB  1 
ATOM   2272  N N   . ILE A  1 288 ? 43.319  -13.154 29.565  1.00 36.62  ? 288  ILE C N   1 
ATOM   2273  C CA  . ILE A  1 288 ? 43.627  -14.554 29.862  1.00 33.45  ? 288  ILE C CA  1 
ATOM   2274  C C   . ILE A  1 288 ? 45.119  -14.876 29.651  1.00 38.55  ? 288  ILE C C   1 
ATOM   2275  O O   . ILE A  1 288 ? 45.686  -14.543 28.615  1.00 44.34  ? 288  ILE C O   1 
ATOM   2276  C CB  . ILE A  1 288 ? 42.760  -15.503 28.959  1.00 38.87  ? 288  ILE C CB  1 
ATOM   2277  C CG1 . ILE A  1 288 ? 41.285  -15.475 29.382  1.00 33.25  ? 288  ILE C CG1 1 
ATOM   2278  C CG2 . ILE A  1 288 ? 43.291  -16.953 28.969  1.00 38.17  ? 288  ILE C CG2 1 
ATOM   2279  C CD1 . ILE A  1 288 ? 40.380  -16.206 28.441  1.00 32.77  ? 288  ILE C CD1 1 
ATOM   2280  N N   . ASN A  1 289 ? 45.758  -15.458 30.659  1.00 40.88  ? 289  ASN C N   1 
ATOM   2281  C CA  . ASN A  1 289 ? 47.113  -16.004 30.555  1.00 44.25  ? 289  ASN C CA  1 
ATOM   2282  C C   . ASN A  1 289 ? 47.042  -17.449 31.018  1.00 49.89  ? 289  ASN C C   1 
ATOM   2283  O O   . ASN A  1 289 ? 47.058  -17.733 32.215  1.00 55.63  ? 289  ASN C O   1 
ATOM   2284  C CB  . ASN A  1 289 ? 48.125  -15.178 31.381  1.00 44.48  ? 289  ASN C CB  1 
ATOM   2285  C CG  . ASN A  1 289 ? 49.584  -15.645 31.200  1.00 52.58  ? 289  ASN C CG  1 
ATOM   2286  O OD1 . ASN A  1 289 ? 49.912  -16.359 30.252  1.00 58.03  ? 289  ASN C OD1 1 
ATOM   2287  N ND2 . ASN A  1 289 ? 50.466  -15.215 32.112  1.00 49.94  ? 289  ASN C ND2 1 
ATOM   2288  N N   . SER A  1 290 ? 46.927  -18.367 30.075  1.00 49.89  ? 290  SER C N   1 
ATOM   2289  C CA  . SER A  1 290 ? 46.642  -19.740 30.434  1.00 49.17  ? 290  SER C CA  1 
ATOM   2290  C C   . SER A  1 290 ? 47.256  -20.657 29.417  1.00 50.39  ? 290  SER C C   1 
ATOM   2291  O O   . SER A  1 290 ? 47.663  -20.218 28.346  1.00 55.41  ? 290  SER C O   1 
ATOM   2292  C CB  . SER A  1 290 ? 45.129  -19.982 30.529  1.00 54.28  ? 290  SER C CB  1 
ATOM   2293  O OG  . SER A  1 290 ? 44.823  -21.307 30.944  1.00 52.90  ? 290  SER C OG  1 
ATOM   2294  N N   . SER A  1 291 ? 47.296  -21.939 29.758  1.00 56.45  ? 291  SER C N   1 
ATOM   2295  C CA  . SER A  1 291 ? 47.825  -22.978 28.883  1.00 59.99  ? 291  SER C CA  1 
ATOM   2296  C C   . SER A  1 291 ? 46.749  -24.042 28.674  1.00 56.78  ? 291  SER C C   1 
ATOM   2297  O O   . SER A  1 291 ? 46.972  -25.039 27.974  1.00 55.70  ? 291  SER C O   1 
ATOM   2298  C CB  . SER A  1 291 ? 49.095  -23.596 29.478  1.00 63.00  ? 291  SER C CB  1 
ATOM   2299  O OG  . SER A  1 291 ? 48.848  -24.055 30.801  1.00 66.26  ? 291  SER C OG  1 
ATOM   2300  N N   . MET A  1 292 ? 45.593  -23.836 29.305  1.00 47.46  ? 292  MET C N   1 
ATOM   2301  C CA  . MET A  1 292 ? 44.470  -24.746 29.125  1.00 47.19  ? 292  MET C CA  1 
ATOM   2302  C C   . MET A  1 292 ? 43.940  -24.801 27.685  1.00 48.42  ? 292  MET C C   1 
ATOM   2303  O O   . MET A  1 292 ? 43.982  -23.814 26.939  1.00 48.37  ? 292  MET C O   1 
ATOM   2304  C CB  . MET A  1 292 ? 43.339  -24.375 30.069  1.00 48.54  ? 292  MET C CB  1 
ATOM   2305  C CG  . MET A  1 292 ? 43.781  -24.137 31.490  1.00 50.11  ? 292  MET C CG  1 
ATOM   2306  S SD  . MET A  1 292 ? 43.848  -25.697 32.361  1.00 59.08  ? 292  MET C SD  1 
ATOM   2307  C CE  . MET A  1 292 ? 43.417  -25.155 34.018  1.00 56.15  ? 292  MET C CE  1 
ATOM   2308  N N   . PRO A  1 293 ? 43.431  -25.969 27.281  1.00 47.22  ? 293  PRO C N   1 
ATOM   2309  C CA  . PRO A  1 293 ? 42.941  -26.003 25.902  1.00 47.07  ? 293  PRO C CA  1 
ATOM   2310  C C   . PRO A  1 293 ? 41.564  -25.372 25.716  1.00 42.78  ? 293  PRO C C   1 
ATOM   2311  O O   . PRO A  1 293 ? 41.213  -25.052 24.589  1.00 45.96  ? 293  PRO C O   1 
ATOM   2312  C CB  . PRO A  1 293 ? 42.884  -27.504 25.604  1.00 49.18  ? 293  PRO C CB  1 
ATOM   2313  C CG  . PRO A  1 293 ? 42.643  -28.135 26.934  1.00 46.75  ? 293  PRO C CG  1 
ATOM   2314  C CD  . PRO A  1 293 ? 43.406  -27.298 27.920  1.00 44.80  ? 293  PRO C CD  1 
ATOM   2315  N N   . PHE A  1 294 ? 40.835  -25.147 26.806  1.00 46.77  ? 294  PHE C N   1 
ATOM   2316  C CA  . PHE A  1 294 ? 39.477  -24.599 26.762  1.00 42.35  ? 294  PHE C CA  1 
ATOM   2317  C C   . PHE A  1 294 ? 39.314  -23.456 27.707  1.00 39.49  ? 294  PHE C C   1 
ATOM   2318  O O   . PHE A  1 294 ? 40.006  -23.399 28.712  1.00 43.26  ? 294  PHE C O   1 
ATOM   2319  C CB  . PHE A  1 294 ? 38.448  -25.671 27.149  1.00 41.90  ? 294  PHE C CB  1 
ATOM   2320  C CG  . PHE A  1 294 ? 38.300  -26.761 26.146  1.00 40.67  ? 294  PHE C CG  1 
ATOM   2321  C CD1 . PHE A  1 294 ? 37.601  -26.540 24.969  1.00 43.50  ? 294  PHE C CD1 1 
ATOM   2322  C CD2 . PHE A  1 294 ? 38.884  -27.996 26.353  1.00 46.46  ? 294  PHE C CD2 1 
ATOM   2323  C CE1 . PHE A  1 294 ? 37.461  -27.545 24.015  1.00 50.13  ? 294  PHE C CE1 1 
ATOM   2324  C CE2 . PHE A  1 294 ? 38.750  -29.007 25.409  1.00 50.27  ? 294  PHE C CE2 1 
ATOM   2325  C CZ  . PHE A  1 294 ? 38.036  -28.777 24.230  1.00 46.97  ? 294  PHE C CZ  1 
ATOM   2326  N N   . HIS A  1 295 ? 38.344  -22.591 27.445  1.00 37.18  ? 295  HIS C N   1 
ATOM   2327  C CA  . HIS A  1 295 ? 37.999  -21.576 28.420  1.00 40.68  ? 295  HIS C CA  1 
ATOM   2328  C C   . HIS A  1 295 ? 36.506  -21.330 28.346  1.00 42.70  ? 295  HIS C C   1 
ATOM   2329  O O   . HIS A  1 295 ? 35.874  -21.696 27.359  1.00 42.66  ? 295  HIS C O   1 
ATOM   2330  C CB  . HIS A  1 295 ? 38.774  -20.273 28.178  1.00 40.13  ? 295  HIS C CB  1 
ATOM   2331  C CG  . HIS A  1 295 ? 38.197  -19.409 27.100  1.00 41.88  ? 295  HIS C CG  1 
ATOM   2332  N ND1 . HIS A  1 295 ? 37.145  -18.544 27.322  1.00 45.74  ? 295  HIS C ND1 1 
ATOM   2333  C CD2 . HIS A  1 295 ? 38.543  -19.247 25.801  1.00 44.18  ? 295  HIS C CD2 1 
ATOM   2334  C CE1 . HIS A  1 295 ? 36.857  -17.900 26.203  1.00 40.44  ? 295  HIS C CE1 1 
ATOM   2335  N NE2 . HIS A  1 295 ? 37.691  -18.308 25.264  1.00 40.16  ? 295  HIS C NE2 1 
ATOM   2336  N N   . ASN A  1 296 ? 35.943  -20.656 29.349  1.00 42.17  ? 296  ASN C N   1 
ATOM   2337  C CA  . ASN A  1 296 ? 34.504  -20.436 29.354  1.00 38.02  ? 296  ASN C CA  1 
ATOM   2338  C C   . ASN A  1 296 ? 34.123  -19.014 29.772  1.00 38.01  ? 296  ASN C C   1 
ATOM   2339  O O   . ASN A  1 296 ? 32.992  -18.775 30.194  1.00 36.82  ? 296  ASN C O   1 
ATOM   2340  C CB  . ASN A  1 296 ? 33.818  -21.465 30.270  1.00 42.06  ? 296  ASN C CB  1 
ATOM   2341  C CG  . ASN A  1 296 ? 33.939  -21.131 31.779  1.00 45.08  ? 296  ASN C CG  1 
ATOM   2342  O OD1 . ASN A  1 296 ? 34.843  -20.392 32.242  1.00 38.88  ? 296  ASN C OD1 1 
ATOM   2343  N ND2 . ASN A  1 296 ? 32.999  -21.675 32.547  1.00 40.47  ? 296  ASN C ND2 1 
ATOM   2344  N N   . ILE A  1 297 ? 35.023  -18.058 29.546  1.00 37.14  ? 297  ILE C N   1 
ATOM   2345  C CA  . ILE A  1 297 ? 34.810  -16.685 30.013  1.00 35.47  ? 297  ILE C CA  1 
ATOM   2346  C C   . ILE A  1 297 ? 33.862  -15.827 29.153  1.00 41.25  ? 297  ILE C C   1 
ATOM   2347  O O   . ILE A  1 297 ? 33.020  -15.110 29.703  1.00 43.31  ? 297  ILE C O   1 
ATOM   2348  C CB  . ILE A  1 297 ? 36.157  -15.962 30.163  1.00 36.02  ? 297  ILE C CB  1 
ATOM   2349  C CG1 . ILE A  1 297 ? 36.798  -16.362 31.499  1.00 39.59  ? 297  ILE C CG1 1 
ATOM   2350  C CG2 . ILE A  1 297 ? 35.949  -14.471 30.268  1.00 34.14  ? 297  ILE C CG2 1 
ATOM   2351  C CD1 . ILE A  1 297 ? 37.730  -17.509 31.457  1.00 36.99  ? 297  ILE C CD1 1 
ATOM   2352  N N   . HIS A  1 298 ? 34.041  -15.841 27.829  1.00 39.99  ? 298  HIS C N   1 
ATOM   2353  C CA  . HIS A  1 298 ? 33.239  -15.035 26.888  1.00 33.04  ? 298  HIS C CA  1 
ATOM   2354  C C   . HIS A  1 298 ? 33.534  -15.535 25.496  1.00 34.32  ? 298  HIS C C   1 
ATOM   2355  O O   . HIS A  1 298 ? 34.685  -15.886 25.220  1.00 35.18  ? 298  HIS C O   1 
ATOM   2356  C CB  . HIS A  1 298 ? 33.585  -13.539 26.977  1.00 36.46  ? 298  HIS C CB  1 
ATOM   2357  C CG  . HIS A  1 298 ? 32.533  -12.614 26.421  1.00 34.58  ? 298  HIS C CG  1 
ATOM   2358  N ND1 . HIS A  1 298 ? 32.224  -12.548 25.073  1.00 35.95  ? 298  HIS C ND1 1 
ATOM   2359  C CD2 . HIS A  1 298 ? 31.793  -11.649 27.022  1.00 30.48  ? 298  HIS C CD2 1 
ATOM   2360  C CE1 . HIS A  1 298 ? 31.293  -11.629 24.882  1.00 35.71  ? 298  HIS C CE1 1 
ATOM   2361  N NE2 . HIS A  1 298 ? 31.017  -11.066 26.049  1.00 37.27  ? 298  HIS C NE2 1 
ATOM   2362  N N   . PRO A  1 299 ? 32.518  -15.572 24.611  1.00 36.96  ? 299  PRO C N   1 
ATOM   2363  C CA  . PRO A  1 299 ? 32.702  -16.015 23.212  1.00 35.87  ? 299  PRO C CA  1 
ATOM   2364  C C   . PRO A  1 299 ? 33.350  -14.978 22.278  1.00 35.75  ? 299  PRO C C   1 
ATOM   2365  O O   . PRO A  1 299 ? 33.830  -15.390 21.222  1.00 36.21  ? 299  PRO C O   1 
ATOM   2366  C CB  . PRO A  1 299 ? 31.273  -16.322 22.736  1.00 34.58  ? 299  PRO C CB  1 
ATOM   2367  C CG  . PRO A  1 299 ? 30.396  -15.510 23.640  1.00 37.11  ? 299  PRO C CG  1 
ATOM   2368  C CD  . PRO A  1 299 ? 31.094  -15.517 24.984  1.00 33.18  ? 299  PRO C CD  1 
ATOM   2369  N N   . LEU A  1 300 ? 33.356  -13.685 22.612  1.00 30.86  ? 300  LEU C N   1 
ATOM   2370  C CA  . LEU A  1 300 ? 33.973  -12.736 21.687  1.00 33.70  ? 300  LEU C CA  1 
ATOM   2371  C C   . LEU A  1 300 ? 35.420  -12.375 22.091  1.00 36.09  ? 300  LEU C C   1 
ATOM   2372  O O   . LEU A  1 300 ? 35.631  -11.400 22.801  1.00 36.15  ? 300  LEU C O   1 
ATOM   2373  C CB  . LEU A  1 300 ? 33.104  -11.468 21.574  1.00 27.59  ? 300  LEU C CB  1 
ATOM   2374  C CG  . LEU A  1 300 ? 31.667  -11.680 21.051  1.00 32.02  ? 300  LEU C CG  1 
ATOM   2375  C CD1 . LEU A  1 300 ? 30.877  -10.389 20.904  1.00 28.01  ? 300  LEU C CD1 1 
ATOM   2376  C CD2 . LEU A  1 300 ? 31.597  -12.489 19.753  1.00 39.15  ? 300  LEU C CD2 1 
ATOM   2377  N N   . THR A  1 301 ? 36.415  -13.097 21.553  1.00 37.01  ? 301  THR C N   1 
ATOM   2378  C CA  . THR A  1 301 ? 37.828  -12.898 21.950  1.00 40.41  ? 301  THR C CA  1 
ATOM   2379  C C   . THR A  1 301 ? 38.752  -12.458 20.788  1.00 37.16  ? 301  THR C C   1 
ATOM   2380  O O   . THR A  1 301 ? 38.330  -12.455 19.650  1.00 37.35  ? 301  THR C O   1 
ATOM   2381  C CB  . THR A  1 301 ? 38.403  -14.185 22.596  1.00 40.66  ? 301  THR C CB  1 
ATOM   2382  O OG1 . THR A  1 301 ? 38.704  -15.164 21.586  1.00 40.38  ? 301  THR C OG1 1 
ATOM   2383  C CG2 . THR A  1 301 ? 37.422  -14.745 23.616  1.00 29.93  ? 301  THR C CG2 1 
ATOM   2384  N N   . ILE A  1 302 ? 39.972  -12.008 21.094  1.00 36.84  ? 302  ILE C N   1 
ATOM   2385  C CA  . ILE A  1 302 ? 40.985  -11.721 20.066  1.00 34.17  ? 302  ILE C CA  1 
ATOM   2386  C C   . ILE A  1 302 ? 42.374  -12.084 20.591  1.00 35.56  ? 302  ILE C C   1 
ATOM   2387  O O   . ILE A  1 302 ? 42.637  -12.005 21.789  1.00 36.77  ? 302  ILE C O   1 
ATOM   2388  C CB  . ILE A  1 302 ? 40.936  -10.224 19.567  1.00 30.46  ? 302  ILE C CB  1 
ATOM   2389  C CG1 . ILE A  1 302 ? 41.857  -10.018 18.359  1.00 29.52  ? 302  ILE C CG1 1 
ATOM   2390  C CG2 . ILE A  1 302 ? 41.308  -9.230  20.660  1.00 32.14  ? 302  ILE C CG2 1 
ATOM   2391  C CD1 . ILE A  1 302 ? 41.836  -8.592  17.778  1.00 25.95  ? 302  ILE C CD1 1 
ATOM   2392  N N   . GLY A  1 303 ? 43.228  -12.562 19.698  1.00 36.58  ? 303  GLY C N   1 
ATOM   2393  C CA  . GLY A  1 303 ? 44.568  -12.988 20.047  1.00 35.53  ? 303  GLY C CA  1 
ATOM   2394  C C   . GLY A  1 303 ? 44.684  -14.495 20.003  1.00 38.24  ? 303  GLY C C   1 
ATOM   2395  O O   . GLY A  1 303 ? 43.806  -15.176 19.495  1.00 45.31  ? 303  GLY C O   1 
ATOM   2396  N N   . GLU A  1 304 ? 45.730  -15.023 20.618  1.00 44.64  ? 304  GLU C N   1 
ATOM   2397  C CA  . GLU A  1 304 ? 45.989  -16.454 20.619  1.00 42.57  ? 304  GLU C CA  1 
ATOM   2398  C C   . GLU A  1 304 ? 45.353  -17.103 21.835  1.00 43.63  ? 304  GLU C C   1 
ATOM   2399  O O   . GLU A  1 304 ? 45.964  -17.144 22.894  1.00 42.11  ? 304  GLU C O   1 
ATOM   2400  C CB  . GLU A  1 304 ? 47.488  -16.689 20.617  1.00 45.95  ? 304  GLU C CB  1 
ATOM   2401  C CG  . GLU A  1 304 ? 47.900  -18.122 20.405  1.00 65.44  ? 304  GLU C CG  1 
ATOM   2402  C CD  . GLU A  1 304 ? 49.409  -18.268 20.392  1.00 69.16  ? 304  GLU C CD  1 
ATOM   2403  O OE1 . GLU A  1 304 ? 50.063  -17.512 19.639  1.00 75.55  ? 304  GLU C OE1 1 
ATOM   2404  O OE2 . GLU A  1 304 ? 49.937  -19.119 21.145  1.00 67.30  ? 304  GLU C OE2 1 
ATOM   2405  N N   . CYS A  1 305 ? 44.141  -17.631 21.671  1.00 46.70  ? 305  CYS C N   1 
ATOM   2406  C CA  . CYS A  1 305 ? 43.301  -18.044 22.806  1.00 42.79  ? 305  CYS C CA  1 
ATOM   2407  C C   . CYS A  1 305 ? 42.922  -19.521 22.832  1.00 46.80  ? 305  CYS C C   1 
ATOM   2408  O O   . CYS A  1 305 ? 42.999  -20.227 21.812  1.00 49.73  ? 305  CYS C O   1 
ATOM   2409  C CB  . CYS A  1 305 ? 42.005  -17.233 22.821  1.00 46.05  ? 305  CYS C CB  1 
ATOM   2410  S SG  . CYS A  1 305 ? 42.216  -15.457 22.984  1.00 57.66  ? 305  CYS C SG  1 
ATOM   2411  N N   . PRO A  1 306 ? 42.525  -20.003 24.021  1.00 49.50  ? 306  PRO C N   1 
ATOM   2412  C CA  . PRO A  1 306 ? 41.874  -21.310 24.180  1.00 42.38  ? 306  PRO C CA  1 
ATOM   2413  C C   . PRO A  1 306 ? 40.506  -21.343 23.469  1.00 43.49  ? 306  PRO C C   1 
ATOM   2414  O O   . PRO A  1 306 ? 40.022  -20.267 23.077  1.00 45.31  ? 306  PRO C O   1 
ATOM   2415  C CB  . PRO A  1 306 ? 41.698  -21.419 25.696  1.00 42.38  ? 306  PRO C CB  1 
ATOM   2416  C CG  . PRO A  1 306 ? 42.714  -20.500 26.270  1.00 36.41  ? 306  PRO C CG  1 
ATOM   2417  C CD  . PRO A  1 306 ? 42.803  -19.363 25.323  1.00 42.51  ? 306  PRO C CD  1 
ATOM   2418  N N   . LYS A  1 307 ? 39.870  -22.513 23.359  1.00 38.90  ? 307  LYS C N   1 
ATOM   2419  C CA  . LYS A  1 307 ? 38.556  -22.613 22.701  1.00 46.42  ? 307  LYS C CA  1 
ATOM   2420  C C   . LYS A  1 307 ? 37.400  -22.439 23.645  1.00 40.27  ? 307  LYS C C   1 
ATOM   2421  O O   . LYS A  1 307 ? 37.436  -22.945 24.752  1.00 46.12  ? 307  LYS C O   1 
ATOM   2422  C CB  . LYS A  1 307 ? 38.411  -23.953 21.959  1.00 49.15  ? 307  LYS C CB  1 
ATOM   2423  C CG  . LYS A  1 307 ? 39.355  -24.046 20.777  1.00 61.08  ? 307  LYS C CG  1 
ATOM   2424  C CD  . LYS A  1 307 ? 39.141  -22.811 19.863  1.00 65.68  ? 307  LYS C CD  1 
ATOM   2425  C CE  . LYS A  1 307 ? 40.241  -22.652 18.817  1.00 73.35  ? 307  LYS C CE  1 
ATOM   2426  N NZ  . LYS A  1 307 ? 41.569  -22.366 19.464  1.00 63.50  ? 307  LYS C NZ  1 
ATOM   2427  N N   . TYR A  1 308 ? 36.357  -21.753 23.190  1.00 38.60  ? 308  TYR C N   1 
ATOM   2428  C CA  . TYR A  1 308 ? 35.221  -21.434 24.054  1.00 40.66  ? 308  TYR C CA  1 
ATOM   2429  C C   . TYR A  1 308 ? 34.155  -22.556 24.070  1.00 39.65  ? 308  TYR C C   1 
ATOM   2430  O O   . TYR A  1 308 ? 33.844  -23.177 23.054  1.00 40.58  ? 308  TYR C O   1 
ATOM   2431  C CB  . TYR A  1 308 ? 34.584  -20.083 23.651  1.00 34.39  ? 308  TYR C CB  1 
ATOM   2432  C CG  . TYR A  1 308 ? 33.353  -19.737 24.468  1.00 38.71  ? 308  TYR C CG  1 
ATOM   2433  C CD1 . TYR A  1 308 ? 33.467  -19.237 25.776  1.00 39.36  ? 308  TYR C CD1 1 
ATOM   2434  C CD2 . TYR A  1 308 ? 32.076  -19.951 23.961  1.00 39.22  ? 308  TYR C CD2 1 
ATOM   2435  C CE1 . TYR A  1 308 ? 32.336  -18.955 26.545  1.00 34.79  ? 308  TYR C CE1 1 
ATOM   2436  C CE2 . TYR A  1 308 ? 30.941  -19.666 24.720  1.00 36.67  ? 308  TYR C CE2 1 
ATOM   2437  C CZ  . TYR A  1 308 ? 31.079  -19.176 26.006  1.00 35.77  ? 308  TYR C CZ  1 
ATOM   2438  O OH  . TYR A  1 308 ? 29.944  -18.890 26.732  1.00 37.66  ? 308  TYR C OH  1 
ATOM   2439  N N   . VAL A  1 309 ? 33.656  -22.841 25.268  1.00 36.97  ? 309  VAL C N   1 
ATOM   2440  C CA  . VAL A  1 309 ? 32.563  -23.782 25.493  1.00 33.58  ? 309  VAL C CA  1 
ATOM   2441  C C   . VAL A  1 309 ? 31.701  -23.178 26.598  1.00 36.25  ? 309  VAL C C   1 
ATOM   2442  O O   . VAL A  1 309 ? 32.182  -22.308 27.334  1.00 36.77  ? 309  VAL C O   1 
ATOM   2443  C CB  . VAL A  1 309 ? 33.070  -25.187 25.901  1.00 34.82  ? 309  VAL C CB  1 
ATOM   2444  C CG1 . VAL A  1 309 ? 33.790  -25.858 24.758  1.00 29.11  ? 309  VAL C CG1 1 
ATOM   2445  C CG2 . VAL A  1 309 ? 33.978  -25.104 27.142  1.00 33.09  ? 309  VAL C CG2 1 
ATOM   2446  N N   . LYS A  1 310 ? 30.442  -23.612 26.696  1.00 35.58  ? 310  LYS C N   1 
ATOM   2447  C CA  . LYS A  1 310 ? 29.519  -23.144 27.739  1.00 36.32  ? 310  LYS C CA  1 
ATOM   2448  C C   . LYS A  1 310 ? 29.495  -24.043 28.988  1.00 41.22  ? 310  LYS C C   1 
ATOM   2449  O O   . LYS A  1 310 ? 28.490  -24.084 29.691  1.00 48.42  ? 310  LYS C O   1 
ATOM   2450  C CB  . LYS A  1 310 ? 28.093  -23.077 27.205  1.00 37.29  ? 310  LYS C CB  1 
ATOM   2451  C CG  . LYS A  1 310 ? 27.786  -22.000 26.181  1.00 44.87  ? 310  LYS C CG  1 
ATOM   2452  C CD  . LYS A  1 310 ? 26.273  -21.912 25.974  1.00 47.02  ? 310  LYS C CD  1 
ATOM   2453  C CE  . LYS A  1 310 ? 25.912  -21.448 24.573  1.00 47.30  ? 310  LYS C CE  1 
ATOM   2454  N NZ  . LYS A  1 310 ? 24.474  -21.719 24.266  1.00 49.96  ? 310  LYS C NZ  1 
ATOM   2455  N N   . SER A  1 311 ? 30.574  -24.767 29.260  1.00 41.87  ? 311  SER C N   1 
ATOM   2456  C CA  . SER A  1 311 ? 30.596  -25.732 30.357  1.00 39.30  ? 311  SER C CA  1 
ATOM   2457  C C   . SER A  1 311 ? 30.969  -25.083 31.684  1.00 45.08  ? 311  SER C C   1 
ATOM   2458  O O   . SER A  1 311 ? 31.722  -24.115 31.729  1.00 47.43  ? 311  SER C O   1 
ATOM   2459  C CB  . SER A  1 311 ? 31.587  -26.860 30.054  1.00 37.22  ? 311  SER C CB  1 
ATOM   2460  O OG  . SER A  1 311 ? 31.327  -27.430 28.787  1.00 44.52  ? 311  SER C OG  1 
ATOM   2461  N N   . ASN A  1 312 ? 30.427  -25.623 32.764  1.00 47.26  ? 312  ASN C N   1 
ATOM   2462  C CA  . ASN A  1 312 ? 30.807  -25.201 34.099  1.00 51.87  ? 312  ASN C CA  1 
ATOM   2463  C C   . ASN A  1 312 ? 32.001  -25.964 34.640  1.00 50.37  ? 312  ASN C C   1 
ATOM   2464  O O   . ASN A  1 312 ? 32.683  -25.484 35.547  1.00 54.58  ? 312  ASN C O   1 
ATOM   2465  C CB  . ASN A  1 312 ? 29.624  -25.335 35.035  1.00 56.22  ? 312  ASN C CB  1 
ATOM   2466  C CG  . ASN A  1 312 ? 28.475  -24.450 34.605  1.00 72.95  ? 312  ASN C CG  1 
ATOM   2467  O OD1 . ASN A  1 312 ? 28.686  -23.419 33.941  1.00 59.80  ? 312  ASN C OD1 1 
ATOM   2468  N ND2 . ASN A  1 312 ? 27.251  -24.833 34.980  1.00 77.65  ? 312  ASN C ND2 1 
ATOM   2469  N N   . ARG A  1 313 ? 32.214  -27.169 34.107  1.00 47.86  ? 313  ARG C N   1 
ATOM   2470  C CA  . ARG A  1 313 ? 33.293  -28.056 34.532  1.00 45.57  ? 313  ARG C CA  1 
ATOM   2471  C C   . ARG A  1 313 ? 33.783  -28.905 33.382  1.00 44.71  ? 313  ARG C C   1 
ATOM   2472  O O   . ARG A  1 313 ? 32.984  -29.395 32.583  1.00 43.01  ? 313  ARG C O   1 
ATOM   2473  C CB  . ARG A  1 313 ? 32.830  -29.007 35.650  1.00 52.79  ? 313  ARG C CB  1 
ATOM   2474  C CG  . ARG A  1 313 ? 32.931  -28.481 37.079  1.00 62.78  ? 313  ARG C CG  1 
ATOM   2475  C CD  . ARG A  1 313 ? 32.592  -29.593 38.084  1.00 77.15  ? 313  ARG C CD  1 
ATOM   2476  N NE  . ARG A  1 313 ? 33.645  -30.619 38.203  1.00 87.74  ? 313  ARG C NE  1 
ATOM   2477  C CZ  . ARG A  1 313 ? 34.599  -30.652 39.145  1.00 82.77  ? 313  ARG C CZ  1 
ATOM   2478  N NH1 . ARG A  1 313 ? 34.632  -29.742 40.119  1.00 73.80  ? 313  ARG C NH1 1 
ATOM   2479  N NH2 . ARG A  1 313 ? 35.501  -31.636 39.143  1.00 72.41  ? 313  ARG C NH2 1 
ATOM   2480  N N   . LEU A  1 314 ? 35.094  -29.090 33.296  1.00 44.15  ? 314  LEU C N   1 
ATOM   2481  C CA  . LEU A  1 314 ? 35.651  -30.043 32.349  1.00 43.63  ? 314  LEU C CA  1 
ATOM   2482  C C   . LEU A  1 314 ? 36.947  -30.584 32.929  1.00 49.55  ? 314  LEU C C   1 
ATOM   2483  O O   . LEU A  1 314 ? 38.012  -29.991 32.762  1.00 52.30  ? 314  LEU C O   1 
ATOM   2484  C CB  . LEU A  1 314 ? 35.880  -29.399 30.980  1.00 51.33  ? 314  LEU C CB  1 
ATOM   2485  C CG  . LEU A  1 314 ? 35.487  -30.207 29.732  1.00 53.24  ? 314  LEU C CG  1 
ATOM   2486  C CD1 . LEU A  1 314 ? 33.998  -30.535 29.781  1.00 49.47  ? 314  LEU C CD1 1 
ATOM   2487  C CD2 . LEU A  1 314 ? 35.837  -29.462 28.417  1.00 43.33  ? 314  LEU C CD2 1 
ATOM   2488  N N   . VAL A  1 315 ? 36.863  -31.725 33.601  1.00 54.60  ? 315  VAL C N   1 
ATOM   2489  C CA  . VAL A  1 315 ? 38.042  -32.313 34.219  1.00 53.70  ? 315  VAL C CA  1 
ATOM   2490  C C   . VAL A  1 315 ? 38.208  -33.753 33.731  1.00 49.05  ? 315  VAL C C   1 
ATOM   2491  O O   . VAL A  1 315 ? 37.253  -34.531 33.658  1.00 48.45  ? 315  VAL C O   1 
ATOM   2492  C CB  . VAL A  1 315 ? 37.965  -32.226 35.766  1.00 56.38  ? 315  VAL C CB  1 
ATOM   2493  C CG1 . VAL A  1 315 ? 36.586  -32.642 36.265  1.00 61.16  ? 315  VAL C CG1 1 
ATOM   2494  C CG2 . VAL A  1 315 ? 39.076  -33.036 36.419  1.00 52.04  ? 315  VAL C CG2 1 
ATOM   2495  N N   . LEU A  1 316 ? 39.443  -34.068 33.365  1.00 52.31  ? 316  LEU C N   1 
ATOM   2496  C CA  . LEU A  1 316 ? 39.819  -35.331 32.742  1.00 51.14  ? 316  LEU C CA  1 
ATOM   2497  C C   . LEU A  1 316 ? 40.453  -36.307 33.749  1.00 57.39  ? 316  LEU C C   1 
ATOM   2498  O O   . LEU A  1 316 ? 41.301  -35.914 34.554  1.00 56.62  ? 316  LEU C O   1 
ATOM   2499  C CB  . LEU A  1 316 ? 40.802  -35.038 31.607  1.00 50.03  ? 316  LEU C CB  1 
ATOM   2500  C CG  . LEU A  1 316 ? 40.786  -35.749 30.260  1.00 49.16  ? 316  LEU C CG  1 
ATOM   2501  C CD1 . LEU A  1 316 ? 39.433  -35.630 29.613  1.00 53.20  ? 316  LEU C CD1 1 
ATOM   2502  C CD2 . LEU A  1 316 ? 41.839  -35.141 29.360  1.00 44.87  ? 316  LEU C CD2 1 
ATOM   2503  N N   . ALA A  1 317 ? 40.025  -37.569 33.729  1.00 61.98  ? 317  ALA C N   1 
ATOM   2504  C CA  . ALA A  1 317 ? 40.663  -38.602 34.554  1.00 59.49  ? 317  ALA C CA  1 
ATOM   2505  C C   . ALA A  1 317 ? 41.997  -38.974 33.936  1.00 59.67  ? 317  ALA C C   1 
ATOM   2506  O O   . ALA A  1 317 ? 42.049  -39.301 32.749  1.00 65.95  ? 317  ALA C O   1 
ATOM   2507  C CB  . ALA A  1 317 ? 39.783  -39.826 34.686  1.00 57.89  ? 317  ALA C CB  1 
ATOM   2508  N N   . THR A  1 318 ? 43.073  -38.903 34.717  1.00 60.01  ? 318  THR C N   1 
ATOM   2509  C CA  . THR A  1 318 ? 44.395  -39.284 34.220  1.00 62.56  ? 318  THR C CA  1 
ATOM   2510  C C   . THR A  1 318 ? 44.937  -40.507 34.976  1.00 68.57  ? 318  THR C C   1 
ATOM   2511  O O   . THR A  1 318 ? 45.618  -41.357 34.394  1.00 71.93  ? 318  THR C O   1 
ATOM   2512  C CB  . THR A  1 318 ? 45.396  -38.083 34.284  1.00 64.71  ? 318  THR C CB  1 
ATOM   2513  O OG1 . THR A  1 318 ? 46.529  -38.339 33.445  1.00 70.66  ? 318  THR C OG1 1 
ATOM   2514  C CG2 . THR A  1 318 ? 45.867  -37.794 35.678  1.00 58.51  ? 318  THR C CG2 1 
ATOM   2515  N N   . GLY A  1 319 ? 44.607  -40.597 36.264  1.00 71.91  ? 319  GLY C N   1 
ATOM   2516  C CA  . GLY A  1 319 ? 45.012  -41.710 37.107  1.00 68.04  ? 319  GLY C CA  1 
ATOM   2517  C C   . GLY A  1 319 ? 43.937  -42.783 37.165  1.00 65.26  ? 319  GLY C C   1 
ATOM   2518  O O   . GLY A  1 319 ? 43.157  -42.945 36.224  1.00 62.86  ? 319  GLY C O   1 
ATOM   2519  N N   . LEU A  1 320 ? 43.874  -43.519 38.270  1.00 66.74  ? 320  LEU C N   1 
ATOM   2520  C CA  . LEU A  1 320 ? 42.865  -44.571 38.380  1.00 69.19  ? 320  LEU C CA  1 
ATOM   2521  C C   . LEU A  1 320 ? 41.867  -44.333 39.517  1.00 58.41  ? 320  LEU C C   1 
ATOM   2522  O O   . LEU A  1 320 ? 41.978  -43.372 40.271  1.00 62.69  ? 320  LEU C O   1 
ATOM   2523  C CB  . LEU A  1 320 ? 43.551  -45.938 38.533  1.00 67.80  ? 320  LEU C CB  1 
ATOM   2524  C CG  . LEU A  1 320 ? 44.647  -46.065 39.589  1.00 70.61  ? 320  LEU C CG  1 
ATOM   2525  C CD1 . LEU A  1 320 ? 44.074  -46.653 40.873  1.00 74.99  ? 320  LEU C CD1 1 
ATOM   2526  C CD2 . LEU A  1 320 ? 45.808  -46.893 39.073  1.00 68.21  ? 320  LEU C CD2 1 
ATOM   2527  N N   . ARG A  1 321 ? 40.875  -45.206 39.607  1.00 56.31  ? 321  ARG C N   1 
ATOM   2528  C CA  . ARG A  1 321 ? 39.817  -45.061 40.590  1.00 62.62  ? 321  ARG C CA  1 
ATOM   2529  C C   . ARG A  1 321 ? 40.379  -45.169 42.002  1.00 68.81  ? 321  ARG C C   1 
ATOM   2530  O O   . ARG A  1 321 ? 41.178  -46.066 42.290  1.00 71.57  ? 321  ARG C O   1 
ATOM   2531  C CB  . ARG A  1 321 ? 38.746  -46.127 40.379  1.00 53.21  ? 321  ARG C CB  1 
ATOM   2532  C CG  . ARG A  1 321 ? 37.517  -45.891 41.214  1.00 58.81  ? 321  ARG C CG  1 
ATOM   2533  C CD  . ARG A  1 321 ? 36.540  -47.021 41.049  1.00 62.87  ? 321  ARG C CD  1 
ATOM   2534  N NE  . ARG A  1 321 ? 36.104  -47.212 39.670  1.00 62.03  ? 321  ARG C NE  1 
ATOM   2535  C CZ  . ARG A  1 321 ? 34.881  -46.919 39.236  1.00 62.07  ? 321  ARG C CZ  1 
ATOM   2536  N NH1 . ARG A  1 321 ? 33.976  -46.421 40.082  1.00 51.79  ? 321  ARG C NH1 1 
ATOM   2537  N NH2 . ARG A  1 321 ? 34.563  -47.135 37.962  1.00 59.38  ? 321  ARG C NH2 1 
ATOM   2538  N N   . ASN A  1 322 ? 39.990  -44.251 42.879  1.00 63.89  ? 322  ASN C N   1 
ATOM   2539  C CA  . ASN A  1 322 ? 40.565  -44.248 44.218  1.00 75.99  ? 322  ASN C CA  1 
ATOM   2540  C C   . ASN A  1 322 ? 39.684  -44.910 45.281  1.00 81.98  ? 322  ASN C C   1 
ATOM   2541  O O   . ASN A  1 322 ? 38.478  -44.650 45.381  1.00 76.68  ? 322  ASN C O   1 
ATOM   2542  C CB  . ASN A  1 322 ? 40.930  -42.834 44.660  1.00 76.43  ? 322  ASN C CB  1 
ATOM   2543  C CG  . ASN A  1 322 ? 42.113  -42.821 45.618  1.00 78.35  ? 322  ASN C CG  1 
ATOM   2544  O OD1 . ASN A  1 322 ? 42.353  -43.784 46.349  1.00 78.13  ? 322  ASN C OD1 1 
ATOM   2545  N ND2 . ASN A  1 322 ? 42.877  -41.744 45.589  1.00 81.68  ? 322  ASN C ND2 1 
ATOM   2546  N N   . SER A  1 323 ? 40.329  -45.770 46.067  1.00 89.17  ? 323  SER C N   1 
ATOM   2547  C CA  . SER A  1 323 ? 39.685  -46.548 47.120  1.00 95.58  ? 323  SER C CA  1 
ATOM   2548  C C   . SER A  1 323 ? 39.232  -45.632 48.254  1.00 97.25  ? 323  SER C C   1 
ATOM   2549  O O   . SER A  1 323 ? 39.992  -44.764 48.697  1.00 95.64  ? 323  SER C O   1 
ATOM   2550  C CB  . SER A  1 323 ? 40.649  -47.617 47.649  1.00 90.17  ? 323  SER C CB  1 
ATOM   2551  O OG  . SER A  1 323 ? 41.354  -48.234 46.582  1.00 85.79  ? 323  SER C OG  1 
ATOM   2552  N N   . PRO A  1 324 ? 37.981  -45.811 48.712  1.00 102.40 ? 324  PRO C N   1 
ATOM   2553  C CA  . PRO A  1 324 ? 37.393  -44.975 49.770  1.00 105.53 ? 324  PRO C CA  1 
ATOM   2554  C C   . PRO A  1 324 ? 38.205  -44.964 51.073  1.00 107.33 ? 324  PRO C C   1 
ATOM   2555  O O   . PRO A  1 324 ? 38.307  -45.978 51.769  1.00 109.51 ? 324  PRO C O   1 
ATOM   2556  C CB  . PRO A  1 324 ? 36.011  -45.612 49.989  1.00 104.16 ? 324  PRO C CB  1 
ATOM   2557  C CG  . PRO A  1 324 ? 36.140  -47.011 49.468  1.00 98.31  ? 324  PRO C CG  1 
ATOM   2558  C CD  . PRO A  1 324 ? 37.075  -46.899 48.302  1.00 96.29  ? 324  PRO C CD  1 
ATOM   2559  N N   . GLY B  2 1   ? 31.715  -53.029 36.960  1.00 78.46  ? 1    GLY D N   1 
ATOM   2560  C CA  . GLY B  2 1   ? 32.536  -52.538 35.862  1.00 86.17  ? 1    GLY D CA  1 
ATOM   2561  C C   . GLY B  2 1   ? 32.871  -53.567 34.787  1.00 84.82  ? 1    GLY D C   1 
ATOM   2562  O O   . GLY B  2 1   ? 32.385  -54.706 34.832  1.00 83.54  ? 1    GLY D O   1 
ATOM   2563  N N   . LEU B  2 2   ? 33.711  -53.178 33.825  1.00 76.45  ? 2    LEU D N   1 
ATOM   2564  C CA  . LEU B  2 2   ? 34.014  -54.041 32.674  1.00 76.87  ? 2    LEU D CA  1 
ATOM   2565  C C   . LEU B  2 2   ? 35.124  -55.040 32.912  1.00 73.34  ? 2    LEU D C   1 
ATOM   2566  O O   . LEU B  2 2   ? 35.652  -55.617 31.973  1.00 73.95  ? 2    LEU D O   1 
ATOM   2567  C CB  . LEU B  2 2   ? 34.406  -53.219 31.444  1.00 69.12  ? 2    LEU D CB  1 
ATOM   2568  C CG  . LEU B  2 2   ? 33.345  -52.383 30.740  1.00 68.99  ? 2    LEU D CG  1 
ATOM   2569  C CD1 . LEU B  2 2   ? 33.907  -51.846 29.408  1.00 43.45  ? 2    LEU D CD1 1 
ATOM   2570  C CD2 . LEU B  2 2   ? 32.023  -53.159 30.581  1.00 58.34  ? 2    LEU D CD2 1 
ATOM   2571  N N   . PHE B  2 3   ? 35.494  -55.251 34.157  1.00 77.93  ? 3    PHE D N   1 
ATOM   2572  C CA  . PHE B  2 3   ? 36.820  -55.771 34.363  1.00 76.53  ? 3    PHE D CA  1 
ATOM   2573  C C   . PHE B  2 3   ? 37.105  -56.861 35.406  1.00 75.67  ? 3    PHE D C   1 
ATOM   2574  O O   . PHE B  2 3   ? 37.888  -57.783 35.164  1.00 73.72  ? 3    PHE D O   1 
ATOM   2575  C CB  . PHE B  2 3   ? 37.611  -54.538 34.726  1.00 79.94  ? 3    PHE D CB  1 
ATOM   2576  C CG  . PHE B  2 3   ? 36.830  -53.544 35.616  1.00 81.12  ? 3    PHE D CG  1 
ATOM   2577  C CD1 . PHE B  2 3   ? 36.378  -53.903 36.894  1.00 79.07  ? 3    PHE D CD1 1 
ATOM   2578  C CD2 . PHE B  2 3   ? 36.581  -52.246 35.184  1.00 80.27  ? 3    PHE D CD2 1 
ATOM   2579  C CE1 . PHE B  2 3   ? 35.673  -53.008 37.704  1.00 77.62  ? 3    PHE D CE1 1 
ATOM   2580  C CE2 . PHE B  2 3   ? 35.884  -51.335 36.000  1.00 78.27  ? 3    PHE D CE2 1 
ATOM   2581  C CZ  . PHE B  2 3   ? 35.435  -51.721 37.259  1.00 75.40  ? 3    PHE D CZ  1 
ATOM   2582  N N   . GLY B  2 4   ? 36.484  -56.717 36.570  1.00 69.63  ? 4    GLY D N   1 
ATOM   2583  C CA  . GLY B  2 4   ? 36.552  -57.669 37.655  1.00 74.81  ? 4    GLY D CA  1 
ATOM   2584  C C   . GLY B  2 4   ? 37.774  -57.509 38.548  1.00 73.83  ? 4    GLY D C   1 
ATOM   2585  O O   . GLY B  2 4   ? 37.806  -58.088 39.628  1.00 74.75  ? 4    GLY D O   1 
ATOM   2586  N N   . ALA B  2 5   ? 38.751  -56.700 38.131  1.00 70.60  ? 5    ALA D N   1 
ATOM   2587  C CA  . ALA B  2 5   ? 40.007  -56.563 38.883  1.00 72.85  ? 5    ALA D CA  1 
ATOM   2588  C C   . ALA B  2 5   ? 39.966  -55.447 39.943  1.00 79.66  ? 5    ALA D C   1 
ATOM   2589  O O   . ALA B  2 5   ? 39.845  -55.736 41.133  1.00 81.42  ? 5    ALA D O   1 
ATOM   2590  C CB  . ALA B  2 5   ? 41.187  -56.354 37.921  1.00 68.82  ? 5    ALA D CB  1 
ATOM   2591  N N   . ILE B  2 6   ? 40.085  -54.186 39.520  1.00 80.76  ? 6    ILE D N   1 
ATOM   2592  C CA  . ILE B  2 6   ? 40.002  -53.038 40.440  1.00 77.33  ? 6    ILE D CA  1 
ATOM   2593  C C   . ILE B  2 6   ? 38.606  -53.005 41.081  1.00 74.75  ? 6    ILE D C   1 
ATOM   2594  O O   . ILE B  2 6   ? 37.603  -53.132 40.378  1.00 76.26  ? 6    ILE D O   1 
ATOM   2595  C CB  . ILE B  2 6   ? 40.298  -51.680 39.718  1.00 76.65  ? 6    ILE D CB  1 
ATOM   2596  C CG1 . ILE B  2 6   ? 41.747  -51.627 39.217  1.00 76.67  ? 6    ILE D CG1 1 
ATOM   2597  C CG2 . ILE B  2 6   ? 39.980  -50.490 40.625  1.00 72.23  ? 6    ILE D CG2 1 
ATOM   2598  C CD1 . ILE B  2 6   ? 42.115  -50.354 38.471  1.00 70.50  ? 6    ILE D CD1 1 
ATOM   2599  N N   . ALA B  2 7   ? 38.545  -52.868 42.406  1.00 78.94  ? 7    ALA D N   1 
ATOM   2600  C CA  . ALA B  2 7   ? 37.281  -52.949 43.141  1.00 76.68  ? 7    ALA D CA  1 
ATOM   2601  C C   . ALA B  2 7   ? 36.551  -54.254 42.799  1.00 79.27  ? 7    ALA D C   1 
ATOM   2602  O O   . ALA B  2 7   ? 35.320  -54.307 42.779  1.00 79.15  ? 7    ALA D O   1 
ATOM   2603  C CB  . ALA B  2 7   ? 36.403  -51.743 42.842  1.00 72.09  ? 7    ALA D CB  1 
ATOM   2604  N N   . GLY B  2 8   ? 37.334  -55.296 42.523  1.00 78.38  ? 8    GLY D N   1 
ATOM   2605  C CA  . GLY B  2 8   ? 36.824  -56.594 42.117  1.00 79.07  ? 8    GLY D CA  1 
ATOM   2606  C C   . GLY B  2 8   ? 37.407  -57.705 42.973  1.00 83.08  ? 8    GLY D C   1 
ATOM   2607  O O   . GLY B  2 8   ? 37.162  -57.738 44.178  1.00 84.66  ? 8    GLY D O   1 
ATOM   2608  N N   . PHE B  2 9   ? 38.161  -58.625 42.367  1.00 83.71  ? 9    PHE D N   1 
ATOM   2609  C CA  . PHE B  2 9   ? 38.763  -59.691 43.158  1.00 83.16  ? 9    PHE D CA  1 
ATOM   2610  C C   . PHE B  2 9   ? 39.892  -59.070 43.968  1.00 80.49  ? 9    PHE D C   1 
ATOM   2611  O O   . PHE B  2 9   ? 40.241  -59.571 45.035  1.00 86.63  ? 9    PHE D O   1 
ATOM   2612  C CB  . PHE B  2 9   ? 39.246  -60.886 42.296  1.00 82.44  ? 9    PHE D CB  1 
ATOM   2613  C CG  . PHE B  2 9   ? 40.480  -60.627 41.460  1.00 80.58  ? 9    PHE D CG  1 
ATOM   2614  C CD1 . PHE B  2 9   ? 41.750  -60.781 41.991  1.00 85.73  ? 9    PHE D CD1 1 
ATOM   2615  C CD2 . PHE B  2 9   ? 40.367  -60.327 40.120  1.00 78.09  ? 9    PHE D CD2 1 
ATOM   2616  C CE1 . PHE B  2 9   ? 42.883  -60.575 41.213  1.00 82.78  ? 9    PHE D CE1 1 
ATOM   2617  C CE2 . PHE B  2 9   ? 41.495  -60.124 39.340  1.00 80.63  ? 9    PHE D CE2 1 
ATOM   2618  C CZ  . PHE B  2 9   ? 42.754  -60.246 39.889  1.00 79.46  ? 9    PHE D CZ  1 
ATOM   2619  N N   . ILE B  2 10  ? 40.437  -57.959 43.480  1.00 78.73  ? 10   ILE D N   1 
ATOM   2620  C CA  . ILE B  2 10  ? 41.261  -57.109 44.332  1.00 81.48  ? 10   ILE D CA  1 
ATOM   2621  C C   . ILE B  2 10  ? 40.429  -55.909 44.773  1.00 83.25  ? 10   ILE D C   1 
ATOM   2622  O O   . ILE B  2 10  ? 39.984  -55.107 43.953  1.00 85.53  ? 10   ILE D O   1 
ATOM   2623  C CB  . ILE B  2 10  ? 42.542  -56.614 43.623  1.00 74.38  ? 10   ILE D CB  1 
ATOM   2624  C CG1 . ILE B  2 10  ? 43.324  -57.792 43.062  1.00 75.18  ? 10   ILE D CG1 1 
ATOM   2625  C CG2 . ILE B  2 10  ? 43.409  -55.826 44.583  1.00 72.57  ? 10   ILE D CG2 1 
ATOM   2626  C CD1 . ILE B  2 10  ? 44.641  -57.420 42.459  1.00 77.29  ? 10   ILE D CD1 1 
ATOM   2627  N N   . GLU B  2 11  ? 40.220  -55.786 46.076  1.00 84.11  ? 11   GLU D N   1 
ATOM   2628  C CA  . GLU B  2 11  ? 39.461  -54.674 46.623  1.00 82.18  ? 11   GLU D CA  1 
ATOM   2629  C C   . GLU B  2 11  ? 40.478  -53.701 47.192  1.00 85.54  ? 11   GLU D C   1 
ATOM   2630  O O   . GLU B  2 11  ? 41.373  -54.109 47.935  1.00 92.78  ? 11   GLU D O   1 
ATOM   2631  C CB  . GLU B  2 11  ? 38.495  -55.145 47.698  1.00 87.27  ? 11   GLU D CB  1 
ATOM   2632  C CG  . GLU B  2 11  ? 37.661  -54.049 48.318  1.00 92.45  ? 11   GLU D CG  1 
ATOM   2633  C CD  . GLU B  2 11  ? 36.967  -54.522 49.584  1.00 98.12  ? 11   GLU D CD  1 
ATOM   2634  O OE1 . GLU B  2 11  ? 37.223  -55.678 50.001  1.00 95.80  ? 11   GLU D OE1 1 
ATOM   2635  O OE2 . GLU B  2 11  ? 36.181  -53.739 50.164  1.00 97.24  ? 11   GLU D OE2 1 
ATOM   2636  N N   . GLY B  2 12  ? 40.348  -52.424 46.854  1.00 81.65  ? 12   GLY D N   1 
ATOM   2637  C CA  . GLY B  2 12  ? 41.234  -51.406 47.391  1.00 82.54  ? 12   GLY D CA  1 
ATOM   2638  C C   . GLY B  2 12  ? 42.689  -51.450 46.918  1.00 84.65  ? 12   GLY D C   1 
ATOM   2639  O O   . GLY B  2 12  ? 43.228  -52.492 46.508  1.00 71.34  ? 12   GLY D O   1 
ATOM   2640  N N   . GLY B  2 13  ? 43.332  -50.288 47.011  1.00 88.28  ? 13   GLY D N   1 
ATOM   2641  C CA  . GLY B  2 13  ? 44.710  -50.114 46.600  1.00 84.84  ? 13   GLY D CA  1 
ATOM   2642  C C   . GLY B  2 13  ? 45.656  -49.975 47.771  1.00 86.88  ? 13   GLY D C   1 
ATOM   2643  O O   . GLY B  2 13  ? 45.241  -49.932 48.936  1.00 76.46  ? 13   GLY D O   1 
ATOM   2644  N N   . TRP B  2 14  ? 46.943  -49.925 47.452  1.00 87.75  ? 14   TRP D N   1 
ATOM   2645  C CA  . TRP B  2 14  ? 47.974  -49.842 48.473  1.00 91.49  ? 14   TRP D CA  1 
ATOM   2646  C C   . TRP B  2 14  ? 48.512  -48.425 48.613  1.00 90.10  ? 14   TRP D C   1 
ATOM   2647  O O   . TRP B  2 14  ? 49.275  -47.954 47.757  1.00 89.08  ? 14   TRP D O   1 
ATOM   2648  C CB  . TRP B  2 14  ? 49.146  -50.764 48.146  1.00 94.72  ? 14   TRP D CB  1 
ATOM   2649  C CG  . TRP B  2 14  ? 48.834  -52.213 47.966  1.00 95.09  ? 14   TRP D CG  1 
ATOM   2650  C CD1 . TRP B  2 14  ? 47.847  -52.945 48.574  1.00 96.62  ? 14   TRP D CD1 1 
ATOM   2651  C CD2 . TRP B  2 14  ? 49.549  -53.119 47.128  1.00 92.52  ? 14   TRP D CD2 1 
ATOM   2652  N NE1 . TRP B  2 14  ? 47.905  -54.254 48.149  1.00 91.66  ? 14   TRP D NE1 1 
ATOM   2653  C CE2 . TRP B  2 14  ? 48.942  -54.381 47.260  1.00 92.14  ? 14   TRP D CE2 1 
ATOM   2654  C CE3 . TRP B  2 14  ? 50.644  -52.980 46.271  1.00 92.77  ? 14   TRP D CE3 1 
ATOM   2655  C CZ2 . TRP B  2 14  ? 49.397  -55.496 46.564  1.00 94.60  ? 14   TRP D CZ2 1 
ATOM   2656  C CZ3 . TRP B  2 14  ? 51.091  -54.085 45.583  1.00 96.06  ? 14   TRP D CZ3 1 
ATOM   2657  C CH2 . TRP B  2 14  ? 50.473  -55.328 45.735  1.00 95.41  ? 14   TRP D CH2 1 
ATOM   2658  N N   . GLN B  2 15  ? 48.141  -47.758 49.702  1.00 86.09  ? 15   GLN D N   1 
ATOM   2659  C CA  . GLN B  2 15  ? 48.659  -46.426 49.974  1.00 88.87  ? 15   GLN D CA  1 
ATOM   2660  C C   . GLN B  2 15  ? 50.171  -46.469 50.188  1.00 91.27  ? 15   GLN D C   1 
ATOM   2661  O O   . GLN B  2 15  ? 50.869  -45.470 49.995  1.00 90.15  ? 15   GLN D O   1 
ATOM   2662  C CB  . GLN B  2 15  ? 47.962  -45.816 51.189  1.00 88.60  ? 15   GLN D CB  1 
ATOM   2663  C CG  . GLN B  2 15  ? 46.494  -45.510 50.980  1.00 87.73  ? 15   GLN D CG  1 
ATOM   2664  C CD  . GLN B  2 15  ? 45.807  -45.145 52.274  1.00 98.72  ? 15   GLN D CD  1 
ATOM   2665  O OE1 . GLN B  2 15  ? 46.222  -45.587 53.351  1.00 100.09 ? 15   GLN D OE1 1 
ATOM   2666  N NE2 . GLN B  2 15  ? 44.764  -44.323 52.186  1.00 96.48  ? 15   GLN D NE2 1 
ATOM   2667  N N   . GLY B  2 16  ? 50.682  -47.644 50.540  1.00 93.65  ? 16   GLY D N   1 
ATOM   2668  C CA  . GLY B  2 16  ? 52.090  -47.777 50.846  1.00 92.53  ? 16   GLY D CA  1 
ATOM   2669  C C   . GLY B  2 16  ? 52.931  -47.965 49.605  1.00 95.62  ? 16   GLY D C   1 
ATOM   2670  O O   . GLY B  2 16  ? 54.153  -47.838 49.662  1.00 97.71  ? 16   GLY D O   1 
ATOM   2671  N N   . MET B  2 17  ? 52.289  -48.235 48.473  1.00 98.24  ? 17   MET D N   1 
ATOM   2672  C CA  . MET B  2 17  ? 53.031  -48.350 47.223  1.00 98.53  ? 17   MET D CA  1 
ATOM   2673  C C   . MET B  2 17  ? 52.967  -47.017 46.500  1.00 99.50  ? 17   MET D C   1 
ATOM   2674  O O   . MET B  2 17  ? 51.939  -46.678 45.917  1.00 102.23 ? 17   MET D O   1 
ATOM   2675  C CB  . MET B  2 17  ? 52.492  -49.464 46.328  1.00 95.63  ? 17   MET D CB  1 
ATOM   2676  C CG  . MET B  2 17  ? 53.267  -49.550 45.030  1.00 94.02  ? 17   MET D CG  1 
ATOM   2677  S SD  . MET B  2 17  ? 52.771  -50.836 43.879  1.00 101.68 ? 17   MET D SD  1 
ATOM   2678  C CE  . MET B  2 17  ? 53.586  -50.212 42.424  1.00 91.15  ? 17   MET D CE  1 
ATOM   2679  N N   . VAL B  2 18  ? 54.066  -46.267 46.536  1.00 100.03 ? 18   VAL D N   1 
ATOM   2680  C CA  . VAL B  2 18  ? 54.073  -44.889 46.050  1.00 102.11 ? 18   VAL D CA  1 
ATOM   2681  C C   . VAL B  2 18  ? 55.162  -44.679 45.008  1.00 96.18  ? 18   VAL D C   1 
ATOM   2682  O O   . VAL B  2 18  ? 55.761  -43.611 44.921  1.00 99.82  ? 18   VAL D O   1 
ATOM   2683  C CB  . VAL B  2 18  ? 54.271  -43.876 47.202  1.00 99.73  ? 18   VAL D CB  1 
ATOM   2684  C CG1 . VAL B  2 18  ? 53.591  -42.541 46.867  1.00 98.42  ? 18   VAL D CG1 1 
ATOM   2685  C CG2 . VAL B  2 18  ? 53.726  -44.438 48.501  1.00 93.07  ? 18   VAL D CG2 1 
ATOM   2686  N N   . ASP B  2 19  ? 55.421  -45.706 44.214  1.00 96.33  ? 19   ASP D N   1 
ATOM   2687  C CA  . ASP B  2 19  ? 56.449  -45.589 43.200  1.00 106.19 ? 19   ASP D CA  1 
ATOM   2688  C C   . ASP B  2 19  ? 55.840  -45.763 41.811  1.00 105.09 ? 19   ASP D C   1 
ATOM   2689  O O   . ASP B  2 19  ? 56.441  -45.405 40.793  1.00 109.20 ? 19   ASP D O   1 
ATOM   2690  C CB  . ASP B  2 19  ? 57.543  -46.632 43.445  1.00 105.90 ? 19   ASP D CB  1 
ATOM   2691  C CG  . ASP B  2 19  ? 58.816  -46.348 42.660  1.00 114.00 ? 19   ASP D CG  1 
ATOM   2692  O OD1 . ASP B  2 19  ? 58.831  -45.420 41.813  1.00 113.16 ? 19   ASP D OD1 1 
ATOM   2693  O OD2 . ASP B  2 19  ? 59.815  -47.061 42.901  1.00 116.99 ? 19   ASP D OD2 1 
ATOM   2694  N N   . GLY B  2 20  ? 54.621  -46.277 41.765  1.00 98.08  ? 20   GLY D N   1 
ATOM   2695  C CA  . GLY B  2 20  ? 53.988  -46.472 40.482  1.00 94.82  ? 20   GLY D CA  1 
ATOM   2696  C C   . GLY B  2 20  ? 52.504  -46.690 40.571  1.00 92.04  ? 20   GLY D C   1 
ATOM   2697  O O   . GLY B  2 20  ? 51.883  -46.461 41.613  1.00 91.08  ? 20   GLY D O   1 
ATOM   2698  N N   . TRP B  2 21  ? 51.946  -47.157 39.462  1.00 90.97  ? 21   TRP D N   1 
ATOM   2699  C CA  . TRP B  2 21  ? 50.521  -47.403 39.348  1.00 87.40  ? 21   TRP D CA  1 
ATOM   2700  C C   . TRP B  2 21  ? 50.268  -48.883 39.593  1.00 87.84  ? 21   TRP D C   1 
ATOM   2701  O O   . TRP B  2 21  ? 49.299  -49.261 40.253  1.00 88.34  ? 21   TRP D O   1 
ATOM   2702  C CB  . TRP B  2 21  ? 50.009  -46.968 37.966  1.00 87.26  ? 21   TRP D CB  1 
ATOM   2703  C CG  . TRP B  2 21  ? 49.553  -45.500 37.873  1.00 86.98  ? 21   TRP D CG  1 
ATOM   2704  C CD1 . TRP B  2 21  ? 49.077  -44.709 38.893  1.00 85.75  ? 21   TRP D CD1 1 
ATOM   2705  C CD2 . TRP B  2 21  ? 49.548  -44.670 36.696  1.00 80.93  ? 21   TRP D CD2 1 
ATOM   2706  N NE1 . TRP B  2 21  ? 48.776  -43.449 38.419  1.00 78.66  ? 21   TRP D NE1 1 
ATOM   2707  C CE2 . TRP B  2 21  ? 49.055  -43.401 37.077  1.00 79.64  ? 21   TRP D CE2 1 
ATOM   2708  C CE3 . TRP B  2 21  ? 49.914  -44.878 35.359  1.00 82.94  ? 21   TRP D CE3 1 
ATOM   2709  C CZ2 . TRP B  2 21  ? 48.915  -42.350 36.167  1.00 77.75  ? 21   TRP D CZ2 1 
ATOM   2710  C CZ3 . TRP B  2 21  ? 49.774  -43.827 34.457  1.00 81.98  ? 21   TRP D CZ3 1 
ATOM   2711  C CH2 . TRP B  2 21  ? 49.277  -42.583 34.865  1.00 77.40  ? 21   TRP D CH2 1 
ATOM   2712  N N   . TYR B  2 22  ? 51.156  -49.716 39.059  1.00 87.04  ? 22   TYR D N   1 
ATOM   2713  C CA  . TYR B  2 22  ? 51.062  -51.161 39.234  1.00 91.93  ? 22   TYR D CA  1 
ATOM   2714  C C   . TYR B  2 22  ? 52.373  -51.756 39.782  1.00 97.80  ? 22   TYR D C   1 
ATOM   2715  O O   . TYR B  2 22  ? 53.457  -51.240 39.503  1.00 101.94 ? 22   TYR D O   1 
ATOM   2716  C CB  . TYR B  2 22  ? 50.694  -51.834 37.904  1.00 90.11  ? 22   TYR D CB  1 
ATOM   2717  C CG  . TYR B  2 22  ? 49.786  -51.027 36.985  1.00 90.40  ? 22   TYR D CG  1 
ATOM   2718  C CD1 . TYR B  2 22  ? 48.433  -50.855 37.274  1.00 87.93  ? 22   TYR D CD1 1 
ATOM   2719  C CD2 . TYR B  2 22  ? 50.280  -50.452 35.816  1.00 93.08  ? 22   TYR D CD2 1 
ATOM   2720  C CE1 . TYR B  2 22  ? 47.598  -50.123 36.423  1.00 82.98  ? 22   TYR D CE1 1 
ATOM   2721  C CE2 . TYR B  2 22  ? 49.456  -49.721 34.964  1.00 87.53  ? 22   TYR D CE2 1 
ATOM   2722  C CZ  . TYR B  2 22  ? 48.118  -49.561 35.271  1.00 82.78  ? 22   TYR D CZ  1 
ATOM   2723  O OH  . TYR B  2 22  ? 47.305  -48.836 34.424  1.00 75.98  ? 22   TYR D OH  1 
ATOM   2724  N N   . GLY B  2 23  ? 52.277  -52.831 40.566  1.00 96.42  ? 23   GLY D N   1 
ATOM   2725  C CA  . GLY B  2 23  ? 53.461  -53.489 41.102  1.00 100.08 ? 23   GLY D CA  1 
ATOM   2726  C C   . GLY B  2 23  ? 53.210  -54.679 42.024  1.00 103.87 ? 23   GLY D C   1 
ATOM   2727  O O   . GLY B  2 23  ? 52.155  -55.322 41.945  1.00 99.79  ? 23   GLY D O   1 
ATOM   2728  N N   . TYR B  2 24  ? 54.179  -54.955 42.907  1.00 107.31 ? 24   TYR D N   1 
ATOM   2729  C CA  . TYR B  2 24  ? 54.186  -56.161 43.754  1.00 104.19 ? 24   TYR D CA  1 
ATOM   2730  C C   . TYR B  2 24  ? 54.413  -55.902 45.257  1.00 103.27 ? 24   TYR D C   1 
ATOM   2731  O O   . TYR B  2 24  ? 55.231  -55.060 45.625  1.00 102.81 ? 24   TYR D O   1 
ATOM   2732  C CB  . TYR B  2 24  ? 55.271  -57.131 43.274  1.00 99.94  ? 24   TYR D CB  1 
ATOM   2733  C CG  . TYR B  2 24  ? 55.379  -57.310 41.773  1.00 101.93 ? 24   TYR D CG  1 
ATOM   2734  C CD1 . TYR B  2 24  ? 56.131  -56.437 40.988  1.00 102.16 ? 24   TYR D CD1 1 
ATOM   2735  C CD2 . TYR B  2 24  ? 54.749  -58.374 41.143  1.00 100.92 ? 24   TYR D CD2 1 
ATOM   2736  C CE1 . TYR B  2 24  ? 56.235  -56.619 39.611  1.00 99.66  ? 24   TYR D CE1 1 
ATOM   2737  C CE2 . TYR B  2 24  ? 54.848  -58.561 39.774  1.00 95.83  ? 24   TYR D CE2 1 
ATOM   2738  C CZ  . TYR B  2 24  ? 55.590  -57.688 39.016  1.00 94.36  ? 24   TYR D CZ  1 
ATOM   2739  O OH  . TYR B  2 24  ? 55.673  -57.896 37.661  1.00 97.58  ? 24   TYR D OH  1 
ATOM   2740  N N   . HIS B  2 25  ? 53.689  -56.637 46.108  1.00 103.77 ? 25   HIS D N   1 
ATOM   2741  C CA  . HIS B  2 25  ? 53.970  -56.741 47.556  1.00 108.05 ? 25   HIS D CA  1 
ATOM   2742  C C   . HIS B  2 25  ? 54.355  -58.180 47.942  1.00 112.82 ? 25   HIS D C   1 
ATOM   2743  O O   . HIS B  2 25  ? 53.505  -59.072 47.925  1.00 113.09 ? 25   HIS D O   1 
ATOM   2744  C CB  . HIS B  2 25  ? 52.751  -56.286 48.382  1.00 105.41 ? 25   HIS D CB  1 
ATOM   2745  C CG  . HIS B  2 25  ? 52.948  -56.348 49.874  1.00 107.79 ? 25   HIS D CG  1 
ATOM   2746  N ND1 . HIS B  2 25  ? 51.893  -56.313 50.764  1.00 102.92 ? 25   HIS D ND1 1 
ATOM   2747  C CD2 . HIS B  2 25  ? 54.070  -56.440 50.628  1.00 104.95 ? 25   HIS D CD2 1 
ATOM   2748  C CE1 . HIS B  2 25  ? 52.356  -56.382 51.999  1.00 93.85  ? 25   HIS D CE1 1 
ATOM   2749  N NE2 . HIS B  2 25  ? 53.673  -56.461 51.945  1.00 101.13 ? 25   HIS D NE2 1 
ATOM   2750  N N   . HIS B  2 26  ? 55.611  -58.409 48.325  1.00 114.98 ? 26   HIS D N   1 
ATOM   2751  C CA  . HIS B  2 26  ? 56.066  -59.771 48.625  1.00 115.77 ? 26   HIS D CA  1 
ATOM   2752  C C   . HIS B  2 26  ? 56.234  -59.903 50.131  1.00 120.27 ? 26   HIS D C   1 
ATOM   2753  O O   . HIS B  2 26  ? 56.546  -58.922 50.806  1.00 121.92 ? 26   HIS D O   1 
ATOM   2754  C CB  . HIS B  2 26  ? 57.398  -60.109 47.943  1.00 113.42 ? 26   HIS D CB  1 
ATOM   2755  C CG  . HIS B  2 26  ? 58.579  -59.430 48.567  1.00 118.55 ? 26   HIS D CG  1 
ATOM   2756  N ND1 . HIS B  2 26  ? 58.854  -58.090 48.397  1.00 121.07 ? 26   HIS D ND1 1 
ATOM   2757  C CD2 . HIS B  2 26  ? 59.542  -59.909 49.391  1.00 120.79 ? 26   HIS D CD2 1 
ATOM   2758  C CE1 . HIS B  2 26  ? 59.941  -57.775 49.080  1.00 118.88 ? 26   HIS D CE1 1 
ATOM   2759  N NE2 . HIS B  2 26  ? 60.378  -58.861 49.692  1.00 121.43 ? 26   HIS D NE2 1 
ATOM   2760  N N   . SER B  2 27  ? 56.025  -61.103 50.663  1.00 123.59 ? 27   SER D N   1 
ATOM   2761  C CA  . SER B  2 27  ? 56.146  -61.311 52.102  1.00 126.34 ? 27   SER D CA  1 
ATOM   2762  C C   . SER B  2 27  ? 56.825  -62.653 52.391  1.00 130.16 ? 27   SER D C   1 
ATOM   2763  O O   . SER B  2 27  ? 56.151  -63.681 52.522  1.00 128.30 ? 27   SER D O   1 
ATOM   2764  C CB  . SER B  2 27  ? 54.770  -61.239 52.778  1.00 123.31 ? 27   SER D CB  1 
ATOM   2765  O OG  . SER B  2 27  ? 54.871  -61.387 54.185  1.00 123.86 ? 27   SER D OG  1 
ATOM   2766  N N   . ASN B  2 28  ? 58.160  -62.636 52.479  1.00 131.03 ? 28   ASN D N   1 
ATOM   2767  C CA  . ASN B  2 28  ? 58.932  -63.835 52.831  1.00 132.10 ? 28   ASN D CA  1 
ATOM   2768  C C   . ASN B  2 28  ? 59.813  -63.633 54.085  1.00 130.42 ? 28   ASN D C   1 
ATOM   2769  O O   . ASN B  2 28  ? 59.565  -62.725 54.886  1.00 127.29 ? 28   ASN D O   1 
ATOM   2770  C CB  . ASN B  2 28  ? 59.773  -64.319 51.616  1.00 129.14 ? 28   ASN D CB  1 
ATOM   2771  C CG  . ASN B  2 28  ? 60.919  -63.370 51.232  1.00 124.24 ? 28   ASN D CG  1 
ATOM   2772  O OD1 . ASN B  2 28  ? 60.943  -62.205 51.621  1.00 126.75 ? 28   ASN D OD1 1 
ATOM   2773  N ND2 . ASN B  2 28  ? 61.863  -63.878 50.441  1.00 118.37 ? 28   ASN D ND2 1 
ATOM   2774  N N   . GLU B  2 29  ? 60.814  -64.498 54.264  1.00 133.60 ? 29   GLU D N   1 
ATOM   2775  C CA  . GLU B  2 29  ? 61.684  -64.458 55.447  1.00 131.43 ? 29   GLU D CA  1 
ATOM   2776  C C   . GLU B  2 29  ? 62.477  -63.155 55.545  1.00 128.67 ? 29   GLU D C   1 
ATOM   2777  O O   . GLU B  2 29  ? 62.609  -62.579 56.629  1.00 124.80 ? 29   GLU D O   1 
ATOM   2778  C CB  . GLU B  2 29  ? 62.648  -65.661 55.463  1.00 130.89 ? 29   GLU D CB  1 
ATOM   2779  C CG  . GLU B  2 29  ? 61.997  -67.050 55.590  1.00 128.56 ? 29   GLU D CG  1 
ATOM   2780  C CD  . GLU B  2 29  ? 61.369  -67.573 54.307  1.00 128.15 ? 29   GLU D CD  1 
ATOM   2781  O OE1 . GLU B  2 29  ? 61.516  -66.926 53.247  1.00 125.54 ? 29   GLU D OE1 1 
ATOM   2782  O OE2 . GLU B  2 29  ? 60.728  -68.645 54.368  1.00 128.81 ? 29   GLU D OE2 1 
ATOM   2783  N N   . GLN B  2 30  ? 62.997  -62.690 54.413  1.00 130.08 ? 30   GLN D N   1 
ATOM   2784  C CA  . GLN B  2 30  ? 63.626  -61.378 54.356  1.00 130.32 ? 30   GLN D CA  1 
ATOM   2785  C C   . GLN B  2 30  ? 62.542  -60.295 54.377  1.00 131.47 ? 30   GLN D C   1 
ATOM   2786  O O   . GLN B  2 30  ? 62.395  -59.527 53.417  1.00 128.43 ? 30   GLN D O   1 
ATOM   2787  C CB  . GLN B  2 30  ? 64.497  -61.229 53.096  1.00 125.63 ? 30   GLN D CB  1 
ATOM   2788  C CG  . GLN B  2 30  ? 65.712  -62.155 53.012  1.00 120.76 ? 30   GLN D CG  1 
ATOM   2789  C CD  . GLN B  2 30  ? 65.392  -63.504 52.385  1.00 125.29 ? 30   GLN D CD  1 
ATOM   2790  O OE1 . GLN B  2 30  ? 64.327  -64.070 52.614  1.00 127.94 ? 30   GLN D OE1 1 
ATOM   2791  N NE2 . GLN B  2 30  ? 66.317  -64.017 51.579  1.00 123.05 ? 30   GLN D NE2 1 
ATOM   2792  N N   . GLY B  2 31  ? 61.800  -60.235 55.484  1.00 128.72 ? 31   GLY D N   1 
ATOM   2793  C CA  . GLY B  2 31  ? 60.779  -59.223 55.704  1.00 132.45 ? 31   GLY D CA  1 
ATOM   2794  C C   . GLY B  2 31  ? 59.739  -59.045 54.609  1.00 133.22 ? 31   GLY D C   1 
ATOM   2795  O O   . GLY B  2 31  ? 59.491  -59.955 53.811  1.00 129.68 ? 31   GLY D O   1 
ATOM   2796  N N   . SER B  2 32  ? 59.122  -57.863 54.587  1.00 130.92 ? 32   SER D N   1 
ATOM   2797  C CA  . SER B  2 32  ? 58.094  -57.529 53.604  1.00 123.80 ? 32   SER D CA  1 
ATOM   2798  C C   . SER B  2 32  ? 58.663  -56.572 52.554  1.00 120.65 ? 32   SER D C   1 
ATOM   2799  O O   . SER B  2 32  ? 59.878  -56.397 52.464  1.00 121.06 ? 32   SER D O   1 
ATOM   2800  C CB  . SER B  2 32  ? 56.872  -56.905 54.290  1.00 118.01 ? 32   SER D CB  1 
ATOM   2801  O OG  . SER B  2 32  ? 56.281  -57.797 55.220  1.00 110.46 ? 32   SER D OG  1 
ATOM   2802  N N   . GLY B  2 33  ? 57.789  -55.961 51.758  1.00 117.27 ? 33   GLY D N   1 
ATOM   2803  C CA  . GLY B  2 33  ? 58.223  -54.957 50.801  1.00 116.01 ? 33   GLY D CA  1 
ATOM   2804  C C   . GLY B  2 33  ? 57.352  -54.756 49.571  1.00 114.60 ? 33   GLY D C   1 
ATOM   2805  O O   . GLY B  2 33  ? 56.536  -55.612 49.219  1.00 110.49 ? 33   GLY D O   1 
ATOM   2806  N N   . TYR B  2 34  ? 57.556  -53.613 48.912  1.00 113.34 ? 34   TYR D N   1 
ATOM   2807  C CA  . TYR B  2 34  ? 56.855  -53.249 47.679  1.00 105.85 ? 34   TYR D CA  1 
ATOM   2808  C C   . TYR B  2 34  ? 57.802  -53.090 46.486  1.00 102.77 ? 34   TYR D C   1 
ATOM   2809  O O   . TYR B  2 34  ? 58.988  -52.804 46.655  1.00 103.61 ? 34   TYR D O   1 
ATOM   2810  C CB  . TYR B  2 34  ? 56.069  -51.949 47.872  1.00 97.55  ? 34   TYR D CB  1 
ATOM   2811  C CG  . TYR B  2 34  ? 54.905  -52.038 48.835  1.00 97.73  ? 34   TYR D CG  1 
ATOM   2812  C CD1 . TYR B  2 34  ? 53.753  -52.741 48.501  1.00 99.79  ? 34   TYR D CD1 1 
ATOM   2813  C CD2 . TYR B  2 34  ? 54.940  -51.384 50.056  1.00 94.24  ? 34   TYR D CD2 1 
ATOM   2814  C CE1 . TYR B  2 34  ? 52.678  -52.812 49.373  1.00 97.17  ? 34   TYR D CE1 1 
ATOM   2815  C CE2 . TYR B  2 34  ? 53.870  -51.447 50.934  1.00 93.59  ? 34   TYR D CE2 1 
ATOM   2816  C CZ  . TYR B  2 34  ? 52.742  -52.161 50.588  1.00 95.95  ? 34   TYR D CZ  1 
ATOM   2817  O OH  . TYR B  2 34  ? 51.673  -52.227 51.455  1.00 93.55  ? 34   TYR D OH  1 
ATOM   2818  N N   . ALA B  2 35  ? 57.272  -53.264 45.280  1.00 99.35  ? 35   ALA D N   1 
ATOM   2819  C CA  . ALA B  2 35  ? 58.067  -53.102 44.066  1.00 103.95 ? 35   ALA D CA  1 
ATOM   2820  C C   . ALA B  2 35  ? 57.155  -52.718 42.906  1.00 107.44 ? 35   ALA D C   1 
ATOM   2821  O O   . ALA B  2 35  ? 56.143  -53.375 42.670  1.00 108.88 ? 35   ALA D O   1 
ATOM   2822  C CB  . ALA B  2 35  ? 58.830  -54.380 43.747  1.00 105.37 ? 35   ALA D CB  1 
ATOM   2823  N N   . ALA B  2 36  ? 57.523  -51.676 42.165  1.00 104.98 ? 36   ALA D N   1 
ATOM   2824  C CA  . ALA B  2 36  ? 56.678  -51.213 41.073  1.00 103.13 ? 36   ALA D CA  1 
ATOM   2825  C C   . ALA B  2 36  ? 57.119  -51.822 39.751  1.00 101.96 ? 36   ALA D C   1 
ATOM   2826  O O   . ALA B  2 36  ? 58.296  -51.745 39.400  1.00 101.68 ? 36   ALA D O   1 
ATOM   2827  C CB  . ALA B  2 36  ? 56.716  -49.696 40.995  1.00 100.39 ? 36   ALA D CB  1 
ATOM   2828  N N   . ASP B  2 37  ? 56.166  -52.378 38.997  1.00 104.37 ? 37   ASP D N   1 
ATOM   2829  C CA  . ASP B  2 37  ? 56.463  -52.875 37.654  1.00 103.19 ? 37   ASP D CA  1 
ATOM   2830  C C   . ASP B  2 37  ? 56.491  -51.681 36.728  1.00 105.58 ? 37   ASP D C   1 
ATOM   2831  O O   . ASP B  2 37  ? 55.448  -51.169 36.317  1.00 104.01 ? 37   ASP D O   1 
ATOM   2832  C CB  . ASP B  2 37  ? 55.432  -53.904 37.171  1.00 95.97  ? 37   ASP D CB  1 
ATOM   2833  C CG  . ASP B  2 37  ? 55.854  -54.590 35.868  1.00 105.97 ? 37   ASP D CG  1 
ATOM   2834  O OD1 . ASP B  2 37  ? 57.072  -54.770 35.646  1.00 109.31 ? 37   ASP D OD1 1 
ATOM   2835  O OD2 . ASP B  2 37  ? 54.970  -54.944 35.057  1.00 108.80 ? 37   ASP D OD2 1 
ATOM   2836  N N   . LYS B  2 38  ? 57.702  -51.243 36.410  1.00 106.35 ? 38   LYS D N   1 
ATOM   2837  C CA  . LYS B  2 38  ? 57.902  -50.028 35.643  1.00 105.78 ? 38   LYS D CA  1 
ATOM   2838  C C   . LYS B  2 38  ? 57.377  -50.175 34.212  1.00 104.00 ? 38   LYS D C   1 
ATOM   2839  O O   . LYS B  2 38  ? 56.723  -49.266 33.699  1.00 102.51 ? 38   LYS D O   1 
ATOM   2840  C CB  . LYS B  2 38  ? 59.380  -49.633 35.665  1.00 110.01 ? 38   LYS D CB  1 
ATOM   2841  C CG  . LYS B  2 38  ? 59.963  -49.575 37.085  1.00 106.65 ? 38   LYS D CG  1 
ATOM   2842  C CD  . LYS B  2 38  ? 59.206  -48.586 37.963  1.00 104.51 ? 38   LYS D CD  1 
ATOM   2843  C CE  . LYS B  2 38  ? 59.513  -47.145 37.604  1.00 105.83 ? 38   LYS D CE  1 
ATOM   2844  N NZ  . LYS B  2 38  ? 58.770  -46.216 38.502  1.00 106.71 ? 38   LYS D NZ  1 
ATOM   2845  N N   . GLU B  2 39  ? 57.666  -51.315 33.582  1.00 105.52 ? 39   GLU D N   1 
ATOM   2846  C CA  . GLU B  2 39  ? 57.314  -51.556 32.180  1.00 102.84 ? 39   GLU D CA  1 
ATOM   2847  C C   . GLU B  2 39  ? 55.821  -51.380 31.932  1.00 104.00 ? 39   GLU D C   1 
ATOM   2848  O O   . GLU B  2 39  ? 55.416  -50.748 30.954  1.00 100.73 ? 39   GLU D O   1 
ATOM   2849  C CB  . GLU B  2 39  ? 57.734  -52.958 31.741  1.00 100.58 ? 39   GLU D CB  1 
ATOM   2850  C CG  . GLU B  2 39  ? 59.229  -53.184 31.737  1.00 110.32 ? 39   GLU D CG  1 
ATOM   2851  C CD  . GLU B  2 39  ? 59.774  -53.551 33.107  1.00 115.17 ? 39   GLU D CD  1 
ATOM   2852  O OE1 . GLU B  2 39  ? 58.976  -53.639 34.067  1.00 110.42 ? 39   GLU D OE1 1 
ATOM   2853  O OE2 . GLU B  2 39  ? 61.002  -53.757 33.220  1.00 116.56 ? 39   GLU D OE2 1 
ATOM   2854  N N   . SER B  2 40  ? 55.004  -51.960 32.807  1.00 105.11 ? 40   SER D N   1 
ATOM   2855  C CA  . SER B  2 40  ? 53.561  -51.864 32.645  1.00 101.43 ? 40   SER D CA  1 
ATOM   2856  C C   . SER B  2 40  ? 53.094  -50.465 33.060  1.00 99.05  ? 40   SER D C   1 
ATOM   2857  O O   . SER B  2 40  ? 52.081  -49.977 32.551  1.00 96.79  ? 40   SER D O   1 
ATOM   2858  C CB  . SER B  2 40  ? 52.840  -52.956 33.449  1.00 96.87  ? 40   SER D CB  1 
ATOM   2859  O OG  . SER B  2 40  ? 52.998  -52.771 34.845  1.00 98.16  ? 40   SER D OG  1 
ATOM   2860  N N   . THR B  2 41  ? 53.845  -49.826 33.964  1.00 96.22  ? 41   THR D N   1 
ATOM   2861  C CA  . THR B  2 41  ? 53.566  -48.451 34.393  1.00 97.07  ? 41   THR D CA  1 
ATOM   2862  C C   . THR B  2 41  ? 54.018  -47.467 33.311  1.00 96.82  ? 41   THR D C   1 
ATOM   2863  O O   . THR B  2 41  ? 53.389  -46.431 33.091  1.00 96.36  ? 41   THR D O   1 
ATOM   2864  C CB  . THR B  2 41  ? 54.266  -48.094 35.740  1.00 97.67  ? 41   THR D CB  1 
ATOM   2865  O OG1 . THR B  2 41  ? 53.561  -48.693 36.837  1.00 90.92  ? 41   THR D OG1 1 
ATOM   2866  C CG2 . THR B  2 41  ? 54.317  -46.580 35.952  1.00 90.73  ? 41   THR D CG2 1 
ATOM   2867  N N   . GLN B  2 42  ? 55.103  -47.807 32.624  1.00 98.79  ? 42   GLN D N   1 
ATOM   2868  C CA  . GLN B  2 42  ? 55.634  -46.946 31.572  1.00 99.25  ? 42   GLN D CA  1 
ATOM   2869  C C   . GLN B  2 42  ? 54.724  -46.909 30.353  1.00 98.87  ? 42   GLN D C   1 
ATOM   2870  O O   . GLN B  2 42  ? 54.522  -45.853 29.750  1.00 102.31 ? 42   GLN D O   1 
ATOM   2871  C CB  . GLN B  2 42  ? 57.034  -47.391 31.150  1.00 102.98 ? 42   GLN D CB  1 
ATOM   2872  C CG  . GLN B  2 42  ? 57.694  -46.454 30.138  1.00 105.14 ? 42   GLN D CG  1 
ATOM   2873  C CD  . GLN B  2 42  ? 57.759  -45.010 30.630  1.00 107.75 ? 42   GLN D CD  1 
ATOM   2874  O OE1 . GLN B  2 42  ? 57.971  -44.752 31.820  1.00 107.22 ? 42   GLN D OE1 1 
ATOM   2875  N NE2 . GLN B  2 42  ? 57.578  -44.064 29.711  1.00 104.20 ? 42   GLN D NE2 1 
ATOM   2876  N N   . LYS B  2 43  ? 54.199  -48.064 29.966  1.00 97.87  ? 43   LYS D N   1 
ATOM   2877  C CA  . LYS B  2 43  ? 53.271  -48.102 28.849  1.00 97.60  ? 43   LYS D CA  1 
ATOM   2878  C C   . LYS B  2 43  ? 51.976  -47.375 29.233  1.00 94.18  ? 43   LYS D C   1 
ATOM   2879  O O   . LYS B  2 43  ? 51.281  -46.830 28.378  1.00 89.67  ? 43   LYS D O   1 
ATOM   2880  C CB  . LYS B  2 43  ? 52.975  -49.552 28.441  1.00 95.73  ? 43   LYS D CB  1 
ATOM   2881  C CG  . LYS B  2 43  ? 54.199  -50.346 27.995  1.00 98.82  ? 43   LYS D CG  1 
ATOM   2882  C CD  . LYS B  2 43  ? 54.919  -49.700 26.817  1.00 103.74 ? 43   LYS D CD  1 
ATOM   2883  C CE  . LYS B  2 43  ? 54.130  -49.866 25.528  1.00 104.40 ? 43   LYS D CE  1 
ATOM   2884  N NZ  . LYS B  2 43  ? 54.870  -49.336 24.352  1.00 104.14 ? 43   LYS D NZ  1 
ATOM   2885  N N   . ALA B  2 44  ? 51.692  -47.320 30.533  1.00 93.42  ? 44   ALA D N   1 
ATOM   2886  C CA  . ALA B  2 44  ? 50.484  -46.670 31.025  1.00 88.54  ? 44   ALA D CA  1 
ATOM   2887  C C   . ALA B  2 44  ? 50.626  -45.159 31.152  1.00 88.94  ? 44   ALA D C   1 
ATOM   2888  O O   . ALA B  2 44  ? 49.683  -44.439 30.836  1.00 90.06  ? 44   ALA D O   1 
ATOM   2889  C CB  . ALA B  2 44  ? 50.067  -47.267 32.359  1.00 89.15  ? 44   ALA D CB  1 
ATOM   2890  N N   . ILE B  2 45  ? 51.774  -44.672 31.626  1.00 91.14  ? 45   ILE D N   1 
ATOM   2891  C CA  . ILE B  2 45  ? 51.982  -43.221 31.698  1.00 92.65  ? 45   ILE D CA  1 
ATOM   2892  C C   . ILE B  2 45  ? 52.134  -42.647 30.279  1.00 92.06  ? 45   ILE D C   1 
ATOM   2893  O O   . ILE B  2 45  ? 51.641  -41.555 29.995  1.00 92.94  ? 45   ILE D O   1 
ATOM   2894  C CB  . ILE B  2 45  ? 53.208  -42.829 32.585  1.00 89.04  ? 45   ILE D CB  1 
ATOM   2895  C CG1 . ILE B  2 45  ? 53.429  -41.313 32.584  1.00 84.18  ? 45   ILE D CG1 1 
ATOM   2896  C CG2 . ILE B  2 45  ? 54.472  -43.499 32.102  1.00 95.30  ? 45   ILE D CG2 1 
ATOM   2897  C CD1 . ILE B  2 45  ? 52.245  -40.499 33.071  1.00 81.86  ? 45   ILE D CD1 1 
ATOM   2898  N N   . ASP B  2 46  ? 52.799  -43.380 29.389  1.00 89.58  ? 46   ASP D N   1 
ATOM   2899  C CA  . ASP B  2 46  ? 52.898  -42.966 27.987  1.00 92.32  ? 46   ASP D CA  1 
ATOM   2900  C C   . ASP B  2 46  ? 51.562  -43.082 27.242  1.00 91.83  ? 46   ASP D C   1 
ATOM   2901  O O   . ASP B  2 46  ? 51.252  -42.258 26.381  1.00 90.93  ? 46   ASP D O   1 
ATOM   2902  C CB  . ASP B  2 46  ? 53.977  -43.776 27.247  1.00 95.48  ? 46   ASP D CB  1 
ATOM   2903  C CG  . ASP B  2 46  ? 55.395  -43.334 27.595  1.00 100.34 ? 46   ASP D CG  1 
ATOM   2904  O OD1 . ASP B  2 46  ? 55.561  -42.222 28.151  1.00 100.53 ? 46   ASP D OD1 1 
ATOM   2905  O OD2 . ASP B  2 46  ? 56.343  -44.100 27.305  1.00 95.77  ? 46   ASP D OD2 1 
ATOM   2906  N N   . GLY B  2 47  ? 50.770  -44.094 27.583  1.00 90.31  ? 47   GLY D N   1 
ATOM   2907  C CA  . GLY B  2 47  ? 49.523  -44.345 26.883  1.00 83.70  ? 47   GLY D CA  1 
ATOM   2908  C C   . GLY B  2 47  ? 48.481  -43.272 27.122  1.00 88.91  ? 47   GLY D C   1 
ATOM   2909  O O   . GLY B  2 47  ? 47.784  -42.853 26.189  1.00 88.40  ? 47   GLY D O   1 
ATOM   2910  N N   . VAL B  2 48  ? 48.380  -42.825 28.374  1.00 88.60  ? 48   VAL D N   1 
ATOM   2911  C CA  . VAL B  2 48  ? 47.382  -41.838 28.772  1.00 83.52  ? 48   VAL D CA  1 
ATOM   2912  C C   . VAL B  2 48  ? 47.780  -40.428 28.315  1.00 88.01  ? 48   VAL D C   1 
ATOM   2913  O O   . VAL B  2 48  ? 46.918  -39.624 27.965  1.00 90.16  ? 48   VAL D O   1 
ATOM   2914  C CB  . VAL B  2 48  ? 47.154  -41.856 30.314  1.00 82.88  ? 48   VAL D CB  1 
ATOM   2915  C CG1 . VAL B  2 48  ? 48.321  -41.232 31.059  1.00 86.04  ? 48   VAL D CG1 1 
ATOM   2916  C CG2 . VAL B  2 48  ? 45.870  -41.142 30.683  1.00 81.40  ? 48   VAL D CG2 1 
ATOM   2917  N N   . THR B  2 49  ? 49.081  -40.137 28.292  1.00 89.90  ? 49   THR D N   1 
ATOM   2918  C CA  . THR B  2 49  ? 49.576  -38.818 27.888  1.00 84.45  ? 49   THR D CA  1 
ATOM   2919  C C   . THR B  2 49  ? 49.448  -38.621 26.375  1.00 82.08  ? 49   THR D C   1 
ATOM   2920  O O   . THR B  2 49  ? 49.368  -37.489 25.903  1.00 81.28  ? 49   THR D O   1 
ATOM   2921  C CB  . THR B  2 49  ? 51.028  -38.574 28.351  1.00 83.44  ? 49   THR D CB  1 
ATOM   2922  O OG1 . THR B  2 49  ? 51.871  -39.627 27.881  1.00 90.11  ? 49   THR D OG1 1 
ATOM   2923  C CG2 . THR B  2 49  ? 51.096  -38.497 29.891  1.00 80.88  ? 49   THR D CG2 1 
ATOM   2924  N N   . ASN B  2 50  ? 49.474  -39.717 25.618  1.00 87.18  ? 50   ASN D N   1 
ATOM   2925  C CA  . ASN B  2 50  ? 49.190  -39.659 24.180  1.00 86.19  ? 50   ASN D CA  1 
ATOM   2926  C C   . ASN B  2 50  ? 47.746  -39.231 23.972  1.00 85.35  ? 50   ASN D C   1 
ATOM   2927  O O   . ASN B  2 50  ? 47.429  -38.447 23.076  1.00 81.44  ? 50   ASN D O   1 
ATOM   2928  C CB  . ASN B  2 50  ? 49.388  -41.022 23.494  1.00 82.88  ? 50   ASN D CB  1 
ATOM   2929  C CG  . ASN B  2 50  ? 50.841  -41.378 23.275  1.00 86.38  ? 50   ASN D CG  1 
ATOM   2930  O OD1 . ASN B  2 50  ? 51.703  -40.506 23.191  1.00 95.68  ? 50   ASN D OD1 1 
ATOM   2931  N ND2 . ASN B  2 50  ? 51.114  -42.672 23.132  1.00 82.53  ? 50   ASN D ND2 1 
ATOM   2932  N N   . LYS B  2 51  ? 46.876  -39.778 24.817  1.00 86.46  ? 51   LYS D N   1 
ATOM   2933  C CA  . LYS B  2 51  ? 45.447  -39.516 24.760  1.00 82.66  ? 51   LYS D CA  1 
ATOM   2934  C C   . LYS B  2 51  ? 45.112  -38.034 24.946  1.00 81.09  ? 51   LYS D C   1 
ATOM   2935  O O   . LYS B  2 51  ? 44.369  -37.466 24.148  1.00 83.39  ? 51   LYS D O   1 
ATOM   2936  C CB  . LYS B  2 51  ? 44.721  -40.360 25.812  1.00 83.06  ? 51   LYS D CB  1 
ATOM   2937  C CG  . LYS B  2 51  ? 43.233  -40.088 25.921  1.00 80.70  ? 51   LYS D CG  1 
ATOM   2938  C CD  . LYS B  2 51  ? 42.589  -40.916 27.024  1.00 73.83  ? 51   LYS D CD  1 
ATOM   2939  C CE  . LYS B  2 51  ? 42.479  -42.384 26.635  1.00 72.95  ? 51   LYS D CE  1 
ATOM   2940  N NZ  . LYS B  2 51  ? 41.515  -43.135 27.509  1.00 72.03  ? 51   LYS D NZ  1 
ATOM   2941  N N   . VAL B  2 52  ? 45.659  -37.407 25.985  1.00 78.04  ? 52   VAL D N   1 
ATOM   2942  C CA  . VAL B  2 52  ? 45.300  -36.021 26.301  1.00 81.58  ? 52   VAL D CA  1 
ATOM   2943  C C   . VAL B  2 52  ? 45.807  -35.005 25.259  1.00 79.39  ? 52   VAL D C   1 
ATOM   2944  O O   . VAL B  2 52  ? 45.170  -33.974 25.017  1.00 78.00  ? 52   VAL D O   1 
ATOM   2945  C CB  . VAL B  2 52  ? 45.810  -35.599 27.728  1.00 79.04  ? 52   VAL D CB  1 
ATOM   2946  C CG1 . VAL B  2 52  ? 45.268  -36.542 28.788  1.00 74.28  ? 52   VAL D CG1 1 
ATOM   2947  C CG2 . VAL B  2 52  ? 47.327  -35.550 27.800  1.00 83.81  ? 52   VAL D CG2 1 
ATOM   2948  N N   . ASN B  2 53  ? 46.928  -35.308 24.618  1.00 77.38  ? 53   ASN D N   1 
ATOM   2949  C CA  . ASN B  2 53  ? 47.468  -34.420 23.597  1.00 80.03  ? 53   ASN D CA  1 
ATOM   2950  C C   . ASN B  2 53  ? 46.675  -34.504 22.287  1.00 82.08  ? 53   ASN D C   1 
ATOM   2951  O O   . ASN B  2 53  ? 46.457  -33.493 21.620  1.00 81.78  ? 53   ASN D O   1 
ATOM   2952  C CB  . ASN B  2 53  ? 48.948  -34.737 23.362  1.00 80.05  ? 53   ASN D CB  1 
ATOM   2953  C CG  . ASN B  2 53  ? 49.806  -34.459 24.595  1.00 82.35  ? 53   ASN D CG  1 
ATOM   2954  O OD1 . ASN B  2 53  ? 49.383  -33.754 25.513  1.00 81.77  ? 53   ASN D OD1 1 
ATOM   2955  N ND2 . ASN B  2 53  ? 51.014  -35.016 24.618  1.00 79.13  ? 53   ASN D ND2 1 
ATOM   2956  N N   . SER B  2 54  ? 46.229  -35.709 21.939  1.00 83.65  ? 54   SER D N   1 
ATOM   2957  C CA  . SER B  2 54  ? 45.434  -35.922 20.735  1.00 82.51  ? 54   SER D CA  1 
ATOM   2958  C C   . SER B  2 54  ? 44.097  -35.182 20.791  1.00 82.97  ? 54   SER D C   1 
ATOM   2959  O O   . SER B  2 54  ? 43.637  -34.642 19.780  1.00 87.79  ? 54   SER D O   1 
ATOM   2960  C CB  . SER B  2 54  ? 45.174  -37.425 20.524  1.00 84.87  ? 54   SER D CB  1 
ATOM   2961  O OG  . SER B  2 54  ? 46.343  -38.122 20.123  1.00 88.69  ? 54   SER D OG  1 
ATOM   2962  N N   . ILE B  2 55  ? 43.494  -35.137 21.978  1.00 79.43  ? 55   ILE D N   1 
ATOM   2963  C CA  . ILE B  2 55  ? 42.187  -34.501 22.167  1.00 84.08  ? 55   ILE D CA  1 
ATOM   2964  C C   . ILE B  2 55  ? 42.308  -32.973 22.124  1.00 86.40  ? 55   ILE D C   1 
ATOM   2965  O O   . ILE B  2 55  ? 41.396  -32.268 21.676  1.00 87.23  ? 55   ILE D O   1 
ATOM   2966  C CB  . ILE B  2 55  ? 41.524  -34.936 23.503  1.00 82.31  ? 55   ILE D CB  1 
ATOM   2967  C CG1 . ILE B  2 55  ? 41.114  -36.404 23.453  1.00 77.00  ? 55   ILE D CG1 1 
ATOM   2968  C CG2 . ILE B  2 55  ? 40.285  -34.112 23.798  1.00 77.51  ? 55   ILE D CG2 1 
ATOM   2969  C CD1 . ILE B  2 55  ? 40.638  -36.930 24.774  1.00 68.72  ? 55   ILE D CD1 1 
ATOM   2970  N N   . ILE B  2 56  ? 43.455  -32.471 22.567  1.00 82.95  ? 56   ILE D N   1 
ATOM   2971  C CA  . ILE B  2 56  ? 43.708  -31.040 22.578  1.00 80.90  ? 56   ILE D CA  1 
ATOM   2972  C C   . ILE B  2 56  ? 43.959  -30.562 21.147  1.00 85.85  ? 56   ILE D C   1 
ATOM   2973  O O   . ILE B  2 56  ? 43.457  -29.507 20.740  1.00 86.28  ? 56   ILE D O   1 
ATOM   2974  C CB  . ILE B  2 56  ? 44.899  -30.690 23.496  1.00 74.28  ? 56   ILE D CB  1 
ATOM   2975  C CG1 . ILE B  2 56  ? 44.500  -30.891 24.958  1.00 66.69  ? 56   ILE D CG1 1 
ATOM   2976  C CG2 . ILE B  2 56  ? 45.352  -29.258 23.281  1.00 71.09  ? 56   ILE D CG2 1 
ATOM   2977  C CD1 . ILE B  2 56  ? 45.634  -30.718 25.920  1.00 67.48  ? 56   ILE D CD1 1 
ATOM   2978  N N   . ASP B  2 57  ? 44.728  -31.350 20.392  1.00 86.93  ? 57   ASP D N   1 
ATOM   2979  C CA  . ASP B  2 57  ? 45.092  -31.010 19.014  1.00 89.37  ? 57   ASP D CA  1 
ATOM   2980  C C   . ASP B  2 57  ? 43.922  -31.154 18.019  1.00 87.59  ? 57   ASP D C   1 
ATOM   2981  O O   . ASP B  2 57  ? 43.949  -30.555 16.942  1.00 87.03  ? 57   ASP D O   1 
ATOM   2982  C CB  . ASP B  2 57  ? 46.279  -31.875 18.545  1.00 87.38  ? 57   ASP D CB  1 
ATOM   2983  C CG  . ASP B  2 57  ? 47.581  -31.576 19.307  1.00 91.37  ? 57   ASP D CG  1 
ATOM   2984  O OD1 . ASP B  2 57  ? 47.835  -30.400 19.663  1.00 90.87  ? 57   ASP D OD1 1 
ATOM   2985  O OD2 . ASP B  2 57  ? 48.364  -32.529 19.534  1.00 89.64  ? 57   ASP D OD2 1 
ATOM   2986  N N   . LYS B  2 58  ? 42.903  -31.936 18.381  1.00 86.55  ? 58   LYS D N   1 
ATOM   2987  C CA  . LYS B  2 58  ? 41.708  -32.104 17.538  1.00 84.86  ? 58   LYS D CA  1 
ATOM   2988  C C   . LYS B  2 58  ? 40.754  -30.923 17.665  1.00 86.46  ? 58   LYS D C   1 
ATOM   2989  O O   . LYS B  2 58  ? 39.802  -30.785 16.889  1.00 83.26  ? 58   LYS D O   1 
ATOM   2990  C CB  . LYS B  2 58  ? 40.955  -33.385 17.910  1.00 81.65  ? 58   LYS D CB  1 
ATOM   2991  C CG  . LYS B  2 58  ? 41.428  -34.632 17.207  1.00 83.00  ? 58   LYS D CG  1 
ATOM   2992  C CD  . LYS B  2 58  ? 41.498  -34.412 15.712  1.00 78.05  ? 58   LYS D CD  1 
ATOM   2993  C CE  . LYS B  2 58  ? 41.981  -35.662 15.005  1.00 72.39  ? 58   LYS D CE  1 
ATOM   2994  N NZ  . LYS B  2 58  ? 42.582  -35.335 13.684  1.00 72.91  ? 58   LYS D NZ  1 
ATOM   2995  N N   . MET B  2 59  ? 41.038  -30.062 18.639  1.00 88.21  ? 59   MET D N   1 
ATOM   2996  C CA  . MET B  2 59  ? 40.149  -28.963 19.003  1.00 87.56  ? 59   MET D CA  1 
ATOM   2997  C C   . MET B  2 59  ? 40.732  -27.574 18.702  1.00 86.29  ? 59   MET D C   1 
ATOM   2998  O O   . MET B  2 59  ? 40.096  -26.553 18.974  1.00 78.37  ? 59   MET D O   1 
ATOM   2999  C CB  . MET B  2 59  ? 39.802  -29.068 20.497  1.00 83.15  ? 59   MET D CB  1 
ATOM   3000  C CG  . MET B  2 59  ? 39.059  -30.345 20.913  1.00 74.47  ? 59   MET D CG  1 
ATOM   3001  S SD  . MET B  2 59  ? 37.303  -30.302 20.468  1.00 77.12  ? 59   MET D SD  1 
ATOM   3002  C CE  . MET B  2 59  ? 36.696  -31.864 21.109  1.00 54.18  ? 59   MET D CE  1 
ATOM   3003  N N   . ASN B  2 60  ? 41.936  -27.537 18.139  1.00 89.85  ? 60   ASN D N   1 
ATOM   3004  C CA  . ASN B  2 60  ? 42.595  -26.264 17.868  1.00 88.38  ? 60   ASN D CA  1 
ATOM   3005  C C   . ASN B  2 60  ? 41.882  -25.498 16.758  1.00 86.50  ? 60   ASN D C   1 
ATOM   3006  O O   . ASN B  2 60  ? 41.883  -24.263 16.754  1.00 83.05  ? 60   ASN D O   1 
ATOM   3007  C CB  . ASN B  2 60  ? 44.060  -26.493 17.495  1.00 88.25  ? 60   ASN D CB  1 
ATOM   3008  C CG  . ASN B  2 60  ? 44.208  -27.216 16.171  1.00 89.10  ? 60   ASN D CG  1 
ATOM   3009  O OD1 . ASN B  2 60  ? 43.341  -28.004 15.787  1.00 86.86  ? 60   ASN D OD1 1 
ATOM   3010  N ND2 . ASN B  2 60  ? 45.293  -26.940 15.456  1.00 94.19  ? 60   ASN D ND2 1 
ATOM   3011  N N   . THR B  2 61  ? 41.265  -26.242 15.831  1.00 89.21  ? 61   THR D N   1 
ATOM   3012  C CA  . THR B  2 61  ? 40.412  -25.654 14.791  1.00 88.95  ? 61   THR D CA  1 
ATOM   3013  C C   . THR B  2 61  ? 38.946  -25.846 15.142  1.00 85.52  ? 61   THR D C   1 
ATOM   3014  O O   . THR B  2 61  ? 38.366  -26.899 14.871  1.00 85.64  ? 61   THR D O   1 
ATOM   3015  C CB  . THR B  2 61  ? 40.640  -26.281 13.399  1.00 88.49  ? 61   THR D CB  1 
ATOM   3016  O OG1 . THR B  2 61  ? 42.043  -26.389 13.121  1.00 101.30 ? 61   THR D OG1 1 
ATOM   3017  C CG2 . THR B  2 61  ? 39.959  -25.430 12.325  1.00 82.11  ? 61   THR D CG2 1 
ATOM   3018  N N   . GLN B  2 62  ? 38.348  -24.806 15.706  1.00 79.96  ? 62   GLN D N   1 
ATOM   3019  C CA  . GLN B  2 62  ? 37.001  -24.873 16.247  1.00 75.05  ? 62   GLN D CA  1 
ATOM   3020  C C   . GLN B  2 62  ? 36.402  -23.490 16.066  1.00 74.64  ? 62   GLN D C   1 
ATOM   3021  O O   . GLN B  2 62  ? 37.143  -22.506 16.049  1.00 84.04  ? 62   GLN D O   1 
ATOM   3022  C CB  . GLN B  2 62  ? 37.040  -25.325 17.713  1.00 70.76  ? 62   GLN D CB  1 
ATOM   3023  C CG  . GLN B  2 62  ? 35.900  -24.848 18.597  1.00 65.64  ? 62   GLN D CG  1 
ATOM   3024  C CD  . GLN B  2 62  ? 35.996  -25.432 19.991  1.00 64.11  ? 62   GLN D CD  1 
ATOM   3025  O OE1 . GLN B  2 62  ? 36.703  -26.412 20.203  1.00 65.30  ? 62   GLN D OE1 1 
ATOM   3026  N NE2 . GLN B  2 62  ? 35.288  -24.837 20.951  1.00 60.76  ? 62   GLN D NE2 1 
ATOM   3027  N N   . PHE B  2 63  ? 35.078  -23.410 15.943  1.00 67.87  ? 63   PHE D N   1 
ATOM   3028  C CA  . PHE B  2 63  ? 34.401  -22.163 15.573  1.00 66.36  ? 63   PHE D CA  1 
ATOM   3029  C C   . PHE B  2 63  ? 34.716  -20.960 16.465  1.00 68.55  ? 63   PHE D C   1 
ATOM   3030  O O   . PHE B  2 63  ? 34.673  -21.055 17.690  1.00 76.38  ? 63   PHE D O   1 
ATOM   3031  C CB  . PHE B  2 63  ? 32.887  -22.380 15.572  1.00 58.06  ? 63   PHE D CB  1 
ATOM   3032  C CG  . PHE B  2 63  ? 32.105  -21.180 15.128  1.00 61.11  ? 63   PHE D CG  1 
ATOM   3033  C CD1 . PHE B  2 63  ? 31.878  -20.948 13.763  1.00 54.26  ? 63   PHE D CD1 1 
ATOM   3034  C CD2 . PHE B  2 63  ? 31.617  -20.261 16.067  1.00 58.11  ? 63   PHE D CD2 1 
ATOM   3035  C CE1 . PHE B  2 63  ? 31.156  -19.831 13.334  1.00 52.08  ? 63   PHE D CE1 1 
ATOM   3036  C CE2 . PHE B  2 63  ? 30.900  -19.129 15.655  1.00 56.69  ? 63   PHE D CE2 1 
ATOM   3037  C CZ  . PHE B  2 63  ? 30.667  -18.911 14.283  1.00 53.75  ? 63   PHE D CZ  1 
ATOM   3038  N N   . GLU B  2 64  ? 35.003  -19.819 15.839  1.00 67.76  ? 64   GLU D N   1 
ATOM   3039  C CA  . GLU B  2 64  ? 35.192  -18.579 16.581  1.00 65.60  ? 64   GLU D CA  1 
ATOM   3040  C C   . GLU B  2 64  ? 34.186  -17.527 16.101  1.00 64.50  ? 64   GLU D C   1 
ATOM   3041  O O   . GLU B  2 64  ? 34.045  -17.275 14.909  1.00 63.90  ? 64   GLU D O   1 
ATOM   3042  C CB  . GLU B  2 64  ? 36.637  -18.058 16.463  1.00 72.57  ? 64   GLU D CB  1 
ATOM   3043  C CG  . GLU B  2 64  ? 37.723  -19.012 17.002  1.00 81.03  ? 64   GLU D CG  1 
ATOM   3044  C CD  . GLU B  2 64  ? 39.107  -18.355 17.116  1.00 91.66  ? 64   GLU D CD  1 
ATOM   3045  O OE1 . GLU B  2 64  ? 39.298  -17.261 16.542  1.00 103.42 ? 64   GLU D OE1 1 
ATOM   3046  O OE2 . GLU B  2 64  ? 39.996  -18.920 17.803  1.00 92.08  ? 64   GLU D OE2 1 
ATOM   3047  N N   . ALA B  2 65  ? 33.458  -16.951 17.051  1.00 61.84  ? 65   ALA D N   1 
ATOM   3048  C CA  . ALA B  2 65  ? 32.428  -15.970 16.756  1.00 54.50  ? 65   ALA D CA  1 
ATOM   3049  C C   . ALA B  2 65  ? 32.995  -14.549 16.677  1.00 55.39  ? 65   ALA D C   1 
ATOM   3050  O O   . ALA B  2 65  ? 33.847  -14.178 17.482  1.00 54.99  ? 65   ALA D O   1 
ATOM   3051  C CB  . ALA B  2 65  ? 31.326  -16.061 17.821  1.00 51.42  ? 65   ALA D CB  1 
ATOM   3052  N N   . VAL B  2 66  ? 32.500  -13.745 15.735  1.00 55.72  ? 66   VAL D N   1 
ATOM   3053  C CA  . VAL B  2 66  ? 32.872  -12.329 15.663  1.00 52.36  ? 66   VAL D CA  1 
ATOM   3054  C C   . VAL B  2 66  ? 31.601  -11.474 15.707  1.00 54.66  ? 66   VAL D C   1 
ATOM   3055  O O   . VAL B  2 66  ? 30.535  -11.872 15.219  1.00 55.00  ? 66   VAL D O   1 
ATOM   3056  C CB  . VAL B  2 66  ? 33.722  -11.981 14.393  1.00 51.28  ? 66   VAL D CB  1 
ATOM   3057  C CG1 . VAL B  2 66  ? 32.980  -12.334 13.119  1.00 53.25  ? 66   VAL D CG1 1 
ATOM   3058  C CG2 . VAL B  2 66  ? 34.165  -10.485 14.384  1.00 47.93  ? 66   VAL D CG2 1 
ATOM   3059  N N   . GLY B  2 67  ? 31.707  -10.314 16.342  1.00 58.32  ? 67   GLY D N   1 
ATOM   3060  C CA  . GLY B  2 67  ? 30.597  -9.381  16.413  1.00 58.78  ? 67   GLY D CA  1 
ATOM   3061  C C   . GLY B  2 67  ? 30.349  -8.711  15.061  1.00 59.69  ? 67   GLY D C   1 
ATOM   3062  O O   . GLY B  2 67  ? 31.293  -8.373  14.312  1.00 54.98  ? 67   GLY D O   1 
ATOM   3063  N N   . ARG B  2 68  ? 29.064  -8.616  14.716  1.00 53.67  ? 68   ARG D N   1 
ATOM   3064  C CA  . ARG B  2 68  ? 28.591  -7.869  13.556  1.00 41.15  ? 68   ARG D CA  1 
ATOM   3065  C C   . ARG B  2 68  ? 27.399  -7.058  14.029  1.00 38.93  ? 68   ARG D C   1 
ATOM   3066  O O   . ARG B  2 68  ? 26.627  -7.533  14.863  1.00 46.13  ? 68   ARG D O   1 
ATOM   3067  C CB  . ARG B  2 68  ? 28.196  -8.800  12.429  1.00 42.50  ? 68   ARG D CB  1 
ATOM   3068  C CG  . ARG B  2 68  ? 29.283  -9.724  12.009  1.00 39.23  ? 68   ARG D CG  1 
ATOM   3069  C CD  . ARG B  2 68  ? 28.761  -10.640 10.957  1.00 37.06  ? 68   ARG D CD  1 
ATOM   3070  N NE  . ARG B  2 68  ? 29.771  -11.613 10.611  1.00 35.49  ? 68   ARG D NE  1 
ATOM   3071  C CZ  . ARG B  2 68  ? 29.936  -12.754 11.268  1.00 38.81  ? 68   ARG D CZ  1 
ATOM   3072  N NH1 . ARG B  2 68  ? 29.169  -13.045 12.320  1.00 39.03  ? 68   ARG D NH1 1 
ATOM   3073  N NH2 . ARG B  2 68  ? 30.890  -13.590 10.895  1.00 42.35  ? 68   ARG D NH2 1 
ATOM   3074  N N   . GLU B  2 69  ? 27.217  -5.859  13.493  1.00 35.12  ? 69   GLU D N   1 
ATOM   3075  C CA  . GLU B  2 69  ? 26.152  -4.983  13.975  1.00 30.79  ? 69   GLU D CA  1 
ATOM   3076  C C   . GLU B  2 69  ? 25.103  -4.744  12.895  1.00 29.44  ? 69   GLU D C   1 
ATOM   3077  O O   . GLU B  2 69  ? 25.441  -4.774  11.717  1.00 31.44  ? 69   GLU D O   1 
ATOM   3078  C CB  . GLU B  2 69  ? 26.756  -3.660  14.434  1.00 30.76  ? 69   GLU D CB  1 
ATOM   3079  C CG  . GLU B  2 69  ? 28.132  -3.855  15.073  1.00 41.08  ? 69   GLU D CG  1 
ATOM   3080  C CD  . GLU B  2 69  ? 28.458  -2.850  16.179  1.00 45.50  ? 69   GLU D CD  1 
ATOM   3081  O OE1 . GLU B  2 69  ? 27.630  -2.702  17.125  1.00 37.12  ? 69   GLU D OE1 1 
ATOM   3082  O OE2 . GLU B  2 69  ? 29.552  -2.233  16.085  1.00 39.32  ? 69   GLU D OE2 1 
ATOM   3083  N N   . PHE B  2 70  ? 23.855  -4.459  13.291  1.00 31.84  ? 70   PHE D N   1 
ATOM   3084  C CA  . PHE B  2 70  ? 22.734  -4.301  12.348  1.00 29.90  ? 70   PHE D CA  1 
ATOM   3085  C C   . PHE B  2 70  ? 21.830  -3.121  12.721  1.00 27.46  ? 70   PHE D C   1 
ATOM   3086  O O   . PHE B  2 70  ? 21.703  -2.814  13.889  1.00 32.12  ? 70   PHE D O   1 
ATOM   3087  C CB  . PHE B  2 70  ? 21.920  -5.608  12.290  1.00 26.58  ? 70   PHE D CB  1 
ATOM   3088  C CG  . PHE B  2 70  ? 22.726  -6.797  11.835  1.00 28.10  ? 70   PHE D CG  1 
ATOM   3089  C CD1 . PHE B  2 70  ? 22.854  -7.080  10.480  1.00 24.26  ? 70   PHE D CD1 1 
ATOM   3090  C CD2 . PHE B  2 70  ? 23.374  -7.613  12.756  1.00 29.88  ? 70   PHE D CD2 1 
ATOM   3091  C CE1 . PHE B  2 70  ? 23.600  -8.145  10.038  1.00 20.17  ? 70   PHE D CE1 1 
ATOM   3092  C CE2 . PHE B  2 70  ? 24.122  -8.713  12.327  1.00 28.46  ? 70   PHE D CE2 1 
ATOM   3093  C CZ  . PHE B  2 70  ? 24.240  -8.968  10.958  1.00 28.71  ? 70   PHE D CZ  1 
ATOM   3094  N N   . ASN B  2 71  ? 21.195  -2.448  11.758  1.00 28.99  ? 71   ASN D N   1 
ATOM   3095  C CA  . ASN B  2 71  ? 20.306  -1.342  12.141  1.00 26.32  ? 71   ASN D CA  1 
ATOM   3096  C C   . ASN B  2 71  ? 18.895  -1.841  12.449  1.00 26.08  ? 71   ASN D C   1 
ATOM   3097  O O   . ASN B  2 71  ? 18.653  -3.041  12.473  1.00 30.67  ? 71   ASN D O   1 
ATOM   3098  C CB  . ASN B  2 71  ? 20.305  -0.210  11.070  1.00 24.96  ? 71   ASN D CB  1 
ATOM   3099  C CG  . ASN B  2 71  ? 19.679  -0.607  9.755   1.00 30.12  ? 71   ASN D CG  1 
ATOM   3100  O OD1 . ASN B  2 71  ? 18.555  -1.114  9.698   1.00 28.59  ? 71   ASN D OD1 1 
ATOM   3101  N ND2 . ASN B  2 71  ? 20.409  -0.358  8.667   1.00 35.23  ? 71   ASN D ND2 1 
ATOM   3102  N N   . ASN B  2 72  ? 17.975  -0.923  12.698  1.00 27.89  ? 72   ASN D N   1 
ATOM   3103  C CA  . ASN B  2 72  ? 16.645  -1.247  13.213  1.00 29.22  ? 72   ASN D CA  1 
ATOM   3104  C C   . ASN B  2 72  ? 15.688  -1.894  12.215  1.00 31.37  ? 72   ASN D C   1 
ATOM   3105  O O   . ASN B  2 72  ? 14.660  -2.441  12.615  1.00 35.91  ? 72   ASN D O   1 
ATOM   3106  C CB  . ASN B  2 72  ? 15.999  0.038   13.750  1.00 36.01  ? 72   ASN D CB  1 
ATOM   3107  C CG  . ASN B  2 72  ? 14.798  -0.232  14.662  1.00 48.63  ? 72   ASN D CG  1 
ATOM   3108  O OD1 . ASN B  2 72  ? 14.802  -1.176  15.479  1.00 46.31  ? 72   ASN D OD1 1 
ATOM   3109  N ND2 . ASN B  2 72  ? 13.758  0.606   14.527  1.00 49.93  ? 72   ASN D ND2 1 
ATOM   3110  N N   . LEU B  2 73  ? 16.011  -1.824  10.924  1.00 31.86  ? 73   LEU D N   1 
ATOM   3111  C CA  . LEU B  2 73  ? 15.211  -2.476  9.873   1.00 30.67  ? 73   LEU D CA  1 
ATOM   3112  C C   . LEU B  2 73  ? 16.018  -3.611  9.239   1.00 30.83  ? 73   LEU D C   1 
ATOM   3113  O O   . LEU B  2 73  ? 15.879  -3.906  8.049   1.00 32.79  ? 73   LEU D O   1 
ATOM   3114  C CB  . LEU B  2 73  ? 14.761  -1.461  8.800   1.00 26.24  ? 73   LEU D CB  1 
ATOM   3115  C CG  . LEU B  2 73  ? 13.585  -0.550  9.207   1.00 30.26  ? 73   LEU D CG  1 
ATOM   3116  C CD1 . LEU B  2 73  ? 13.400  0.680   8.285   1.00 17.24  ? 73   LEU D CD1 1 
ATOM   3117  C CD2 . LEU B  2 73  ? 12.264  -1.330  9.352   1.00 24.65  ? 73   LEU D CD2 1 
ATOM   3118  N N   . GLU B  2 74  ? 16.911  -4.198  10.032  1.00 31.04  ? 74   GLU D N   1 
ATOM   3119  C CA  . GLU B  2 74  ? 17.631  -5.418  9.668   1.00 30.22  ? 74   GLU D CA  1 
ATOM   3120  C C   . GLU B  2 74  ? 17.381  -6.499  10.732  1.00 27.62  ? 74   GLU D C   1 
ATOM   3121  O O   . GLU B  2 74  ? 18.264  -7.294  11.044  1.00 29.66  ? 74   GLU D O   1 
ATOM   3122  C CB  . GLU B  2 74  ? 19.136  -5.119  9.515   1.00 29.12  ? 74   GLU D CB  1 
ATOM   3123  C CG  . GLU B  2 74  ? 19.521  -4.365  8.221   1.00 28.02  ? 74   GLU D CG  1 
ATOM   3124  C CD  . GLU B  2 74  ? 20.958  -3.784  8.237   1.00 30.51  ? 74   GLU D CD  1 
ATOM   3125  O OE1 . GLU B  2 74  ? 21.429  -3.332  9.309   1.00 27.51  ? 74   GLU D OE1 1 
ATOM   3126  O OE2 . GLU B  2 74  ? 21.625  -3.786  7.176   1.00 30.15  ? 74   GLU D OE2 1 
ATOM   3127  N N   . ARG B  2 75  ? 16.170  -6.556  11.271  1.00 26.21  ? 75   ARG D N   1 
ATOM   3128  C CA  . ARG B  2 75  ? 15.902  -7.480  12.372  1.00 29.15  ? 75   ARG D CA  1 
ATOM   3129  C C   . ARG B  2 75  ? 16.023  -8.943  11.963  1.00 28.50  ? 75   ARG D C   1 
ATOM   3130  O O   . ARG B  2 75  ? 16.612  -9.750  12.694  1.00 29.74  ? 75   ARG D O   1 
ATOM   3131  C CB  . ARG B  2 75  ? 14.508  -7.217  12.938  1.00 31.89  ? 75   ARG D CB  1 
ATOM   3132  C CG  . ARG B  2 75  ? 14.391  -5.859  13.613  1.00 29.20  ? 75   ARG D CG  1 
ATOM   3133  C CD  . ARG B  2 75  ? 15.419  -5.761  14.709  1.00 31.12  ? 75   ARG D CD  1 
ATOM   3134  N NE  . ARG B  2 75  ? 15.303  -4.513  15.449  1.00 42.09  ? 75   ARG D NE  1 
ATOM   3135  C CZ  . ARG B  2 75  ? 16.278  -4.012  16.208  1.00 46.60  ? 75   ARG D CZ  1 
ATOM   3136  N NH1 . ARG B  2 75  ? 17.416  -4.693  16.338  1.00 52.83  ? 75   ARG D NH1 1 
ATOM   3137  N NH2 . ARG B  2 75  ? 16.119  -2.848  16.845  1.00 39.19  ? 75   ARG D NH2 1 
ATOM   3138  N N   . ARG B  2 76  ? 15.565  -9.265  10.757  1.00 26.79  ? 76   ARG D N   1 
ATOM   3139  C CA  . ARG B  2 76  ? 15.619  -10.644 10.266  1.00 27.37  ? 76   ARG D CA  1 
ATOM   3140  C C   . ARG B  2 76  ? 17.041  -11.222 10.143  1.00 28.72  ? 76   ARG D C   1 
ATOM   3141  O O   . ARG B  2 76  ? 17.299  -12.314 10.655  1.00 28.81  ? 76   ARG D O   1 
ATOM   3142  C CB  . ARG B  2 76  ? 14.908  -10.743 8.903   1.00 28.14  ? 76   ARG D CB  1 
ATOM   3143  C CG  . ARG B  2 76  ? 13.382  -10.656 8.984   1.00 27.10  ? 76   ARG D CG  1 
ATOM   3144  C CD  . ARG B  2 76  ? 12.770  -10.586 7.628   1.00 20.34  ? 76   ARG D CD  1 
ATOM   3145  N NE  . ARG B  2 76  ? 13.263  -9.380  7.011   1.00 25.18  ? 76   ARG D NE  1 
ATOM   3146  C CZ  . ARG B  2 76  ? 13.358  -9.200  5.707   1.00 26.06  ? 76   ARG D CZ  1 
ATOM   3147  N NH1 . ARG B  2 76  ? 12.984  -10.164 4.868   1.00 27.79  ? 76   ARG D NH1 1 
ATOM   3148  N NH2 . ARG B  2 76  ? 13.855  -8.062  5.252   1.00 23.12  ? 76   ARG D NH2 1 
ATOM   3149  N N   . ILE B  2 77  ? 17.976  -10.489 9.523   1.00 28.06  ? 77   ILE D N   1 
ATOM   3150  C CA  . ILE B  2 77  ? 19.327  -11.035 9.357   1.00 28.43  ? 77   ILE D CA  1 
ATOM   3151  C C   . ILE B  2 77  ? 20.106  -10.922 10.661  1.00 27.69  ? 77   ILE D C   1 
ATOM   3152  O O   . ILE B  2 77  ? 20.969  -11.752 10.932  1.00 29.41  ? 77   ILE D O   1 
ATOM   3153  C CB  . ILE B  2 77  ? 20.139  -10.342 8.216   1.00 24.49  ? 77   ILE D CB  1 
ATOM   3154  C CG1 . ILE B  2 77  ? 20.217  -8.841  8.457   1.00 31.19  ? 77   ILE D CG1 1 
ATOM   3155  C CG2 . ILE B  2 77  ? 19.535  -10.629 6.849   1.00 20.12  ? 77   ILE D CG2 1 
ATOM   3156  C CD1 . ILE B  2 77  ? 21.018  -8.085  7.421   1.00 28.57  ? 77   ILE D CD1 1 
ATOM   3157  N N   . GLU B  2 78  ? 19.741  -9.970  11.514  1.00 29.18  ? 78   GLU D N   1 
ATOM   3158  C CA  . GLU B  2 78  ? 20.322  -9.915  12.849  1.00 27.47  ? 78   GLU D CA  1 
ATOM   3159  C C   . GLU B  2 78  ? 19.994  -11.183 13.620  1.00 28.81  ? 78   GLU D C   1 
ATOM   3160  O O   . GLU B  2 78  ? 20.842  -11.732 14.320  1.00 30.73  ? 78   GLU D O   1 
ATOM   3161  C CB  . GLU B  2 78  ? 19.816  -8.698  13.604  1.00 28.87  ? 78   GLU D CB  1 
ATOM   3162  C CG  . GLU B  2 78  ? 20.297  -8.641  15.043  1.00 29.43  ? 78   GLU D CG  1 
ATOM   3163  C CD  . GLU B  2 78  ? 19.862  -7.372  15.730  1.00 43.59  ? 78   GLU D CD  1 
ATOM   3164  O OE1 . GLU B  2 78  ? 18.641  -7.059  15.717  1.00 42.34  ? 78   GLU D OE1 1 
ATOM   3165  O OE2 . GLU B  2 78  ? 20.761  -6.660  16.236  1.00 46.75  ? 78   GLU D OE2 1 
ATOM   3166  N N   . ASN B  2 79  ? 18.760  -11.650 13.454  1.00 31.31  ? 79   ASN D N   1 
ATOM   3167  C CA  . ASN B  2 79  ? 18.244  -12.877 14.058  1.00 26.68  ? 79   ASN D CA  1 
ATOM   3168  C C   . ASN B  2 79  ? 18.905  -14.107 13.392  1.00 36.27  ? 79   ASN D C   1 
ATOM   3169  O O   . ASN B  2 79  ? 19.181  -15.116 14.068  1.00 35.89  ? 79   ASN D O   1 
ATOM   3170  C CB  . ASN B  2 79  ? 16.704  -12.896 13.923  1.00 30.54  ? 79   ASN D CB  1 
ATOM   3171  C CG  . ASN B  2 79  ? 16.031  -14.018 14.724  1.00 34.33  ? 79   ASN D CG  1 
ATOM   3172  O OD1 . ASN B  2 79  ? 15.438  -14.930 14.152  1.00 32.82  ? 79   ASN D OD1 1 
ATOM   3173  N ND2 . ASN B  2 79  ? 16.084  -13.924 16.038  1.00 34.14  ? 79   ASN D ND2 1 
ATOM   3174  N N   . LEU B  2 80  ? 19.150  -14.032 12.070  1.00 34.80  ? 80   LEU D N   1 
ATOM   3175  C CA  . LEU B  2 80  ? 19.930  -15.068 11.371  1.00 31.01  ? 80   LEU D CA  1 
ATOM   3176  C C   . LEU B  2 80  ? 21.305  -15.204 12.001  1.00 31.51  ? 80   LEU D C   1 
ATOM   3177  O O   . LEU B  2 80  ? 21.701  -16.296 12.432  1.00 38.22  ? 80   LEU D O   1 
ATOM   3178  C CB  . LEU B  2 80  ? 20.102  -14.717 9.899   1.00 30.22  ? 80   LEU D CB  1 
ATOM   3179  C CG  . LEU B  2 80  ? 20.521  -15.651 8.758   1.00 27.86  ? 80   LEU D CG  1 
ATOM   3180  C CD1 . LEU B  2 80  ? 21.069  -16.932 9.229   1.00 28.40  ? 80   LEU D CD1 1 
ATOM   3181  C CD2 . LEU B  2 80  ? 19.412  -15.876 7.756   1.00 25.99  ? 80   LEU D CD2 1 
ATOM   3182  N N   . ASN B  2 81  ? 21.991  -14.074 12.124  1.00 26.44  ? 81   ASN D N   1 
ATOM   3183  C CA  . ASN B  2 81  ? 23.352  -14.057 12.629  1.00 31.04  ? 81   ASN D CA  1 
ATOM   3184  C C   . ASN B  2 81  ? 23.454  -14.617 14.060  1.00 34.10  ? 81   ASN D C   1 
ATOM   3185  O O   . ASN B  2 81  ? 24.366  -15.385 14.375  1.00 37.27  ? 81   ASN D O   1 
ATOM   3186  C CB  . ASN B  2 81  ? 23.917  -12.627 12.578  1.00 30.43  ? 81   ASN D CB  1 
ATOM   3187  C CG  . ASN B  2 81  ? 25.419  -12.569 12.914  1.00 35.65  ? 81   ASN D CG  1 
ATOM   3188  O OD1 . ASN B  2 81  ? 26.266  -12.909 12.058  1.00 33.00  ? 81   ASN D OD1 1 
ATOM   3189  N ND2 . ASN B  2 81  ? 25.757  -12.133 14.144  1.00 26.41  ? 81   ASN D ND2 1 
ATOM   3190  N N   . LYS B  2 82  ? 22.501  -14.259 14.909  1.00 29.54  ? 82   LYS D N   1 
ATOM   3191  C CA  . LYS B  2 82  ? 22.532  -14.687 16.289  1.00 32.83  ? 82   LYS D CA  1 
ATOM   3192  C C   . LYS B  2 82  ? 22.293  -16.182 16.419  1.00 35.47  ? 82   LYS D C   1 
ATOM   3193  O O   . LYS B  2 82  ? 22.988  -16.865 17.174  1.00 33.66  ? 82   LYS D O   1 
ATOM   3194  C CB  . LYS B  2 82  ? 21.507  -13.907 17.114  1.00 32.88  ? 82   LYS D CB  1 
ATOM   3195  C CG  . LYS B  2 82  ? 21.432  -14.386 18.554  1.00 40.16  ? 82   LYS D CG  1 
ATOM   3196  C CD  . LYS B  2 82  ? 20.393  -13.620 19.391  1.00 52.42  ? 82   LYS D CD  1 
ATOM   3197  C CE  . LYS B  2 82  ? 20.284  -14.213 20.811  1.00 51.94  ? 82   LYS D CE  1 
ATOM   3198  N NZ  . LYS B  2 82  ? 21.610  -14.227 21.514  1.00 47.13  ? 82   LYS D NZ  1 
ATOM   3199  N N   . LYS B  2 83  ? 21.334  -16.688 15.651  1.00 33.38  ? 83   LYS D N   1 
ATOM   3200  C CA  . LYS B  2 83  ? 20.999  -18.097 15.701  1.00 36.88  ? 83   LYS D CA  1 
ATOM   3201  C C   . LYS B  2 83  ? 22.107  -18.967 15.120  1.00 38.16  ? 83   LYS D C   1 
ATOM   3202  O O   . LYS B  2 83  ? 22.305  -20.095 15.584  1.00 40.17  ? 83   LYS D O   1 
ATOM   3203  C CB  . LYS B  2 83  ? 19.685  -18.371 14.957  1.00 38.77  ? 83   LYS D CB  1 
ATOM   3204  C CG  . LYS B  2 83  ? 18.459  -17.899 15.718  1.00 42.85  ? 83   LYS D CG  1 
ATOM   3205  C CD  . LYS B  2 83  ? 18.192  -18.760 16.951  1.00 42.12  ? 83   LYS D CD  1 
ATOM   3206  C CE  . LYS B  2 83  ? 16.799  -18.528 17.508  1.00 53.59  ? 83   LYS D CE  1 
ATOM   3207  N NZ  . LYS B  2 83  ? 16.201  -19.778 18.091  1.00 65.24  ? 83   LYS D NZ  1 
ATOM   3208  N N   . MET B  2 84  ? 22.825  -18.462 14.115  1.00 34.09  ? 84   MET D N   1 
ATOM   3209  C CA  . MET B  2 84  ? 23.928  -19.238 13.556  1.00 39.07  ? 84   MET D CA  1 
ATOM   3210  C C   . MET B  2 84  ? 25.118  -19.327 14.538  1.00 37.15  ? 84   MET D C   1 
ATOM   3211  O O   . MET B  2 84  ? 25.730  -20.387 14.721  1.00 34.80  ? 84   MET D O   1 
ATOM   3212  C CB  . MET B  2 84  ? 24.388  -18.643 12.234  1.00 33.51  ? 84   MET D CB  1 
ATOM   3213  C CG  . MET B  2 84  ? 25.477  -19.443 11.539  1.00 27.71  ? 84   MET D CG  1 
ATOM   3214  S SD  . MET B  2 84  ? 26.727  -18.374 10.773  1.00 39.19  ? 84   MET D SD  1 
ATOM   3215  C CE  . MET B  2 84  ? 27.852  -17.949 12.080  1.00 33.71  ? 84   MET D CE  1 
ATOM   3216  N N   . GLU B  2 85  ? 25.446  -18.220 15.183  1.00 36.52  ? 85   GLU D N   1 
ATOM   3217  C CA  . GLU B  2 85  ? 26.561  -18.251 16.122  1.00 41.40  ? 85   GLU D CA  1 
ATOM   3218  C C   . GLU B  2 85  ? 26.240  -19.065 17.377  1.00 44.75  ? 85   GLU D C   1 
ATOM   3219  O O   . GLU B  2 85  ? 27.077  -19.847 17.833  1.00 44.00  ? 85   GLU D O   1 
ATOM   3220  C CB  . GLU B  2 85  ? 26.980  -16.844 16.511  1.00 43.06  ? 85   GLU D CB  1 
ATOM   3221  C CG  . GLU B  2 85  ? 27.681  -16.071 15.415  1.00 40.01  ? 85   GLU D CG  1 
ATOM   3222  C CD  . GLU B  2 85  ? 28.564  -14.991 16.007  1.00 50.82  ? 85   GLU D CD  1 
ATOM   3223  O OE1 . GLU B  2 85  ? 28.165  -14.390 17.046  1.00 44.90  ? 85   GLU D OE1 1 
ATOM   3224  O OE2 . GLU B  2 85  ? 29.668  -14.783 15.450  1.00 54.32  ? 85   GLU D OE2 1 
ATOM   3225  N N   . ASP B  2 86  ? 25.037  -18.892 17.923  1.00 41.22  ? 86   ASP D N   1 
ATOM   3226  C CA  . ASP B  2 86  ? 24.590  -19.728 19.033  1.00 41.57  ? 86   ASP D CA  1 
ATOM   3227  C C   . ASP B  2 86  ? 24.610  -21.205 18.657  1.00 42.87  ? 86   ASP D C   1 
ATOM   3228  O O   . ASP B  2 86  ? 24.900  -22.073 19.487  1.00 42.49  ? 86   ASP D O   1 
ATOM   3229  C CB  . ASP B  2 86  ? 23.168  -19.363 19.460  1.00 42.98  ? 86   ASP D CB  1 
ATOM   3230  C CG  . ASP B  2 86  ? 23.102  -18.095 20.265  1.00 47.79  ? 86   ASP D CG  1 
ATOM   3231  O OD1 . ASP B  2 86  ? 24.154  -17.407 20.375  1.00 46.32  ? 86   ASP D OD1 1 
ATOM   3232  O OD2 . ASP B  2 86  ? 21.985  -17.792 20.766  1.00 47.83  ? 86   ASP D OD2 1 
ATOM   3233  N N   . GLY B  2 87  ? 24.282  -21.478 17.403  1.00 37.15  ? 87   GLY D N   1 
ATOM   3234  C CA  . GLY B  2 87  ? 24.183  -22.841 16.936  1.00 40.93  ? 87   GLY D CA  1 
ATOM   3235  C C   . GLY B  2 87  ? 25.504  -23.565 16.993  1.00 40.92  ? 87   GLY D C   1 
ATOM   3236  O O   . GLY B  2 87  ? 25.576  -24.718 17.429  1.00 40.04  ? 87   GLY D O   1 
ATOM   3237  N N   . PHE B  2 88  ? 26.557  -22.884 16.570  1.00 40.70  ? 88   PHE D N   1 
ATOM   3238  C CA  . PHE B  2 88  ? 27.859  -23.511 16.549  1.00 40.05  ? 88   PHE D CA  1 
ATOM   3239  C C   . PHE B  2 88  ? 28.411  -23.672 17.971  1.00 43.45  ? 88   PHE D C   1 
ATOM   3240  O O   . PHE B  2 88  ? 29.088  -24.658 18.257  1.00 47.33  ? 88   PHE D O   1 
ATOM   3241  C CB  . PHE B  2 88  ? 28.816  -22.703 15.663  1.00 43.22  ? 88   PHE D CB  1 
ATOM   3242  C CG  . PHE B  2 88  ? 28.617  -22.934 14.170  1.00 42.50  ? 88   PHE D CG  1 
ATOM   3243  C CD1 . PHE B  2 88  ? 28.928  -24.156 13.591  1.00 39.82  ? 88   PHE D CD1 1 
ATOM   3244  C CD2 . PHE B  2 88  ? 28.121  -21.925 13.355  1.00 41.99  ? 88   PHE D CD2 1 
ATOM   3245  C CE1 . PHE B  2 88  ? 28.740  -24.381 12.233  1.00 38.48  ? 88   PHE D CE1 1 
ATOM   3246  C CE2 . PHE B  2 88  ? 27.935  -22.139 11.994  1.00 41.09  ? 88   PHE D CE2 1 
ATOM   3247  C CZ  . PHE B  2 88  ? 28.246  -23.376 11.436  1.00 44.07  ? 88   PHE D CZ  1 
ATOM   3248  N N   . LEU B  2 89  ? 28.074  -22.757 18.881  1.00 41.43  ? 89   LEU D N   1 
ATOM   3249  C CA  . LEU B  2 89  ? 28.603  -22.837 20.246  1.00 42.65  ? 89   LEU D CA  1 
ATOM   3250  C C   . LEU B  2 89  ? 27.969  -24.021 20.990  1.00 43.44  ? 89   LEU D C   1 
ATOM   3251  O O   . LEU B  2 89  ? 28.605  -24.661 21.823  1.00 37.32  ? 89   LEU D O   1 
ATOM   3252  C CB  . LEU B  2 89  ? 28.370  -21.526 21.010  1.00 39.96  ? 89   LEU D CB  1 
ATOM   3253  C CG  . LEU B  2 89  ? 29.137  -20.313 20.446  1.00 44.38  ? 89   LEU D CG  1 
ATOM   3254  C CD1 . LEU B  2 89  ? 28.829  -19.022 21.194  1.00 42.88  ? 89   LEU D CD1 1 
ATOM   3255  C CD2 . LEU B  2 89  ? 30.632  -20.536 20.405  1.00 46.31  ? 89   LEU D CD2 1 
ATOM   3256  N N   . ASP B  2 90  ? 26.717  -24.319 20.662  1.00 46.15  ? 90   ASP D N   1 
ATOM   3257  C CA  . ASP B  2 90  ? 26.044  -25.478 21.216  1.00 40.23  ? 90   ASP D CA  1 
ATOM   3258  C C   . ASP B  2 90  ? 26.630  -26.770 20.606  1.00 42.16  ? 90   ASP D C   1 
ATOM   3259  O O   . ASP B  2 90  ? 26.918  -27.727 21.330  1.00 45.31  ? 90   ASP D O   1 
ATOM   3260  C CB  . ASP B  2 90  ? 24.541  -25.382 20.945  1.00 36.89  ? 90   ASP D CB  1 
ATOM   3261  C CG  . ASP B  2 90  ? 23.867  -24.259 21.736  1.00 48.97  ? 90   ASP D CG  1 
ATOM   3262  O OD1 . ASP B  2 90  ? 24.438  -23.813 22.765  1.00 50.77  ? 90   ASP D OD1 1 
ATOM   3263  O OD2 . ASP B  2 90  ? 22.780  -23.798 21.296  1.00 48.57  ? 90   ASP D OD2 1 
ATOM   3264  N N   . VAL B  2 91  ? 26.921  -26.759 19.311  1.00 35.32  ? 91   VAL D N   1 
ATOM   3265  C CA  . VAL B  2 91  ? 27.464  -27.956 18.658  1.00 43.99  ? 91   VAL D CA  1 
ATOM   3266  C C   . VAL B  2 91  ? 28.833  -28.361 19.257  1.00 48.15  ? 91   VAL D C   1 
ATOM   3267  O O   . VAL B  2 91  ? 29.055  -29.538 19.575  1.00 44.07  ? 91   VAL D O   1 
ATOM   3268  C CB  . VAL B  2 91  ? 27.611  -27.755 17.111  1.00 37.79  ? 91   VAL D CB  1 
ATOM   3269  C CG1 . VAL B  2 91  ? 28.461  -28.837 16.498  1.00 35.46  ? 91   VAL D CG1 1 
ATOM   3270  C CG2 . VAL B  2 91  ? 26.255  -27.708 16.444  1.00 36.29  ? 91   VAL D CG2 1 
ATOM   3271  N N   . TRP B  2 92  ? 29.727  -27.383 19.425  1.00 47.71  ? 92   TRP D N   1 
ATOM   3272  C CA  . TRP B  2 92  ? 31.072  -27.623 19.944  1.00 45.33  ? 92   TRP D CA  1 
ATOM   3273  C C   . TRP B  2 92  ? 31.139  -27.836 21.457  1.00 43.72  ? 92   TRP D C   1 
ATOM   3274  O O   . TRP B  2 92  ? 32.081  -28.452 21.947  1.00 40.97  ? 92   TRP D O   1 
ATOM   3275  C CB  . TRP B  2 92  ? 31.987  -26.456 19.559  1.00 45.32  ? 92   TRP D CB  1 
ATOM   3276  C CG  . TRP B  2 92  ? 32.453  -26.554 18.163  1.00 52.68  ? 92   TRP D CG  1 
ATOM   3277  C CD1 . TRP B  2 92  ? 32.036  -25.808 17.089  1.00 51.33  ? 92   TRP D CD1 1 
ATOM   3278  C CD2 . TRP B  2 92  ? 33.434  -27.469 17.665  1.00 57.87  ? 92   TRP D CD2 1 
ATOM   3279  N NE1 . TRP B  2 92  ? 32.705  -26.211 15.950  1.00 57.37  ? 92   TRP D NE1 1 
ATOM   3280  C CE2 . TRP B  2 92  ? 33.569  -27.227 16.279  1.00 59.96  ? 92   TRP D CE2 1 
ATOM   3281  C CE3 . TRP B  2 92  ? 34.210  -28.478 18.255  1.00 54.02  ? 92   TRP D CE3 1 
ATOM   3282  C CZ2 . TRP B  2 92  ? 34.452  -27.956 15.479  1.00 58.47  ? 92   TRP D CZ2 1 
ATOM   3283  C CZ3 . TRP B  2 92  ? 35.089  -29.196 17.462  1.00 51.28  ? 92   TRP D CZ3 1 
ATOM   3284  C CH2 . TRP B  2 92  ? 35.200  -28.934 16.090  1.00 59.78  ? 92   TRP D CH2 1 
ATOM   3285  N N   . THR B  2 93  ? 30.137  -27.339 22.182  1.00 44.39  ? 93   THR D N   1 
ATOM   3286  C CA  . THR B  2 93  ? 30.028  -27.562 23.618  1.00 38.24  ? 93   THR D CA  1 
ATOM   3287  C C   . THR B  2 93  ? 29.587  -29.000 23.863  1.00 43.43  ? 93   THR D C   1 
ATOM   3288  O O   . THR B  2 93  ? 30.138  -29.699 24.724  1.00 40.73  ? 93   THR D O   1 
ATOM   3289  C CB  . THR B  2 93  ? 29.042  -26.596 24.259  1.00 38.98  ? 93   THR D CB  1 
ATOM   3290  O OG1 . THR B  2 93  ? 29.649  -25.304 24.354  1.00 34.67  ? 93   THR D OG1 1 
ATOM   3291  C CG2 . THR B  2 93  ? 28.660  -27.056 25.665  1.00 42.99  ? 93   THR D CG2 1 
ATOM   3292  N N   . TYR B  2 94  ? 28.629  -29.452 23.058  1.00 43.96  ? 94   TYR D N   1 
ATOM   3293  C CA  . TYR B  2 94  ? 28.217  -30.851 23.082  1.00 46.07  ? 94   TYR D CA  1 
ATOM   3294  C C   . TYR B  2 94  ? 29.415  -31.740 22.710  1.00 44.26  ? 94   TYR D C   1 
ATOM   3295  O O   . TYR B  2 94  ? 29.659  -32.759 23.351  1.00 44.02  ? 94   TYR D O   1 
ATOM   3296  C CB  . TYR B  2 94  ? 27.021  -31.082 22.133  1.00 42.83  ? 94   TYR D CB  1 
ATOM   3297  C CG  . TYR B  2 94  ? 26.681  -32.535 21.804  1.00 46.54  ? 94   TYR D CG  1 
ATOM   3298  C CD1 . TYR B  2 94  ? 27.342  -33.208 20.784  1.00 45.92  ? 94   TYR D CD1 1 
ATOM   3299  C CD2 . TYR B  2 94  ? 25.680  -33.219 22.490  1.00 50.49  ? 94   TYR D CD2 1 
ATOM   3300  C CE1 . TYR B  2 94  ? 27.033  -34.521 20.463  1.00 47.88  ? 94   TYR D CE1 1 
ATOM   3301  C CE2 . TYR B  2 94  ? 25.365  -34.540 22.178  1.00 51.74  ? 94   TYR D CE2 1 
ATOM   3302  C CZ  . TYR B  2 94  ? 26.043  -35.188 21.156  1.00 49.88  ? 94   TYR D CZ  1 
ATOM   3303  O OH  . TYR B  2 94  ? 25.754  -36.509 20.824  1.00 49.30  ? 94   TYR D OH  1 
ATOM   3304  N N   . ASN B  2 95  ? 30.167  -31.351 21.689  1.00 41.83  ? 95   ASN D N   1 
ATOM   3305  C CA  . ASN B  2 95  ? 31.282  -32.174 21.238  1.00 44.24  ? 95   ASN D CA  1 
ATOM   3306  C C   . ASN B  2 95  ? 32.374  -32.336 22.317  1.00 47.49  ? 95   ASN D C   1 
ATOM   3307  O O   . ASN B  2 95  ? 33.021  -33.381 22.393  1.00 52.11  ? 95   ASN D O   1 
ATOM   3308  C CB  . ASN B  2 95  ? 31.879  -31.613 19.939  1.00 40.69  ? 95   ASN D CB  1 
ATOM   3309  C CG  . ASN B  2 95  ? 31.129  -32.092 18.682  1.00 45.37  ? 95   ASN D CG  1 
ATOM   3310  O OD1 . ASN B  2 95  ? 30.075  -32.733 18.760  1.00 44.62  ? 95   ASN D OD1 1 
ATOM   3311  N ND2 . ASN B  2 95  ? 31.677  -31.772 17.518  1.00 51.34  ? 95   ASN D ND2 1 
ATOM   3312  N N   . ALA B  2 96  ? 32.590  -31.319 23.143  1.00 41.86  ? 96   ALA D N   1 
ATOM   3313  C CA  . ALA B  2 96  ? 33.645  -31.407 24.150  1.00 44.13  ? 96   ALA D CA  1 
ATOM   3314  C C   . ALA B  2 96  ? 33.184  -32.148 25.411  1.00 45.20  ? 96   ALA D C   1 
ATOM   3315  O O   . ALA B  2 96  ? 33.942  -32.889 26.023  1.00 45.42  ? 96   ALA D O   1 
ATOM   3316  C CB  . ALA B  2 96  ? 34.144  -30.014 24.524  1.00 44.57  ? 96   ALA D CB  1 
ATOM   3317  N N   . GLU B  2 97  ? 31.947  -31.925 25.820  1.00 41.63  ? 97   GLU D N   1 
ATOM   3318  C CA  . GLU B  2 97  ? 31.478  -32.541 27.045  1.00 45.71  ? 97   GLU D CA  1 
ATOM   3319  C C   . GLU B  2 97  ? 31.367  -34.045 26.864  1.00 49.94  ? 97   GLU D C   1 
ATOM   3320  O O   . GLU B  2 97  ? 31.815  -34.828 27.711  1.00 50.49  ? 97   GLU D O   1 
ATOM   3321  C CB  . GLU B  2 97  ? 30.131  -31.945 27.460  1.00 42.33  ? 97   GLU D CB  1 
ATOM   3322  C CG  . GLU B  2 97  ? 30.245  -30.503 27.922  1.00 42.95  ? 97   GLU D CG  1 
ATOM   3323  C CD  . GLU B  2 97  ? 28.917  -29.917 28.343  1.00 39.88  ? 97   GLU D CD  1 
ATOM   3324  O OE1 . GLU B  2 97  ? 27.878  -30.561 28.103  1.00 43.75  ? 97   GLU D OE1 1 
ATOM   3325  O OE2 . GLU B  2 97  ? 28.911  -28.806 28.902  1.00 37.90  ? 97   GLU D OE2 1 
ATOM   3326  N N   . LEU B  2 98  ? 30.776  -34.437 25.745  1.00 46.90  ? 98   LEU D N   1 
ATOM   3327  C CA  . LEU B  2 98  ? 30.524  -35.834 25.470  1.00 43.14  ? 98   LEU D CA  1 
ATOM   3328  C C   . LEU B  2 98  ? 31.843  -36.556 25.240  1.00 50.04  ? 98   LEU D C   1 
ATOM   3329  O O   . LEU B  2 98  ? 31.966  -37.759 25.504  1.00 51.87  ? 98   LEU D O   1 
ATOM   3330  C CB  . LEU B  2 98  ? 29.588  -35.989 24.279  1.00 40.84  ? 98   LEU D CB  1 
ATOM   3331  C CG  . LEU B  2 98  ? 29.121  -37.416 23.996  1.00 47.26  ? 98   LEU D CG  1 
ATOM   3332  C CD1 . LEU B  2 98  ? 28.016  -37.836 24.985  1.00 41.84  ? 98   LEU D CD1 1 
ATOM   3333  C CD2 . LEU B  2 98  ? 28.638  -37.542 22.546  1.00 38.71  ? 98   LEU D CD2 1 
ATOM   3334  N N   . LEU B  2 99  ? 32.839  -35.835 24.746  1.00 47.34  ? 99   LEU D N   1 
ATOM   3335  C CA  . LEU B  2 99  ? 34.114  -36.486 24.510  1.00 48.89  ? 99   LEU D CA  1 
ATOM   3336  C C   . LEU B  2 99  ? 34.838  -36.782 25.833  1.00 49.97  ? 99   LEU D C   1 
ATOM   3337  O O   . LEU B  2 99  ? 35.432  -37.843 25.973  1.00 49.08  ? 99   LEU D O   1 
ATOM   3338  C CB  . LEU B  2 99  ? 34.996  -35.636 23.607  1.00 48.24  ? 99   LEU D CB  1 
ATOM   3339  C CG  . LEU B  2 99  ? 36.429  -36.136 23.413  1.00 57.07  ? 99   LEU D CG  1 
ATOM   3340  C CD1 . LEU B  2 99  ? 36.481  -37.481 22.685  1.00 57.36  ? 99   LEU D CD1 1 
ATOM   3341  C CD2 . LEU B  2 99  ? 37.222  -35.098 22.660  1.00 56.03  ? 99   LEU D CD2 1 
ATOM   3342  N N   . VAL B  2 100 ? 34.733  -35.881 26.811  1.00 45.40  ? 100  VAL D N   1 
ATOM   3343  C CA  . VAL B  2 100 ? 35.371  -36.073 28.122  1.00 48.70  ? 100  VAL D CA  1 
ATOM   3344  C C   . VAL B  2 100 ? 34.708  -37.217 28.918  1.00 50.78  ? 100  VAL D C   1 
ATOM   3345  O O   . VAL B  2 100 ? 35.389  -37.980 29.604  1.00 48.52  ? 100  VAL D O   1 
ATOM   3346  C CB  . VAL B  2 100 ? 35.344  -34.761 28.952  1.00 48.76  ? 100  VAL D CB  1 
ATOM   3347  C CG1 . VAL B  2 100 ? 35.760  -35.008 30.390  1.00 46.19  ? 100  VAL D CG1 1 
ATOM   3348  C CG2 . VAL B  2 100 ? 36.270  -33.737 28.333  1.00 46.49  ? 100  VAL D CG2 1 
ATOM   3349  N N   . LEU B  2 101 ? 33.382  -37.315 28.828  1.00 52.21  ? 101  LEU D N   1 
ATOM   3350  C CA  . LEU B  2 101 ? 32.628  -38.414 29.416  1.00 45.37  ? 101  LEU D CA  1 
ATOM   3351  C C   . LEU B  2 101 ? 33.007  -39.759 28.813  1.00 50.39  ? 101  LEU D C   1 
ATOM   3352  O O   . LEU B  2 101 ? 33.111  -40.757 29.521  1.00 57.73  ? 101  LEU D O   1 
ATOM   3353  C CB  . LEU B  2 101 ? 31.133  -38.222 29.210  1.00 44.98  ? 101  LEU D CB  1 
ATOM   3354  C CG  . LEU B  2 101 ? 30.436  -37.116 29.963  1.00 46.50  ? 101  LEU D CG  1 
ATOM   3355  C CD1 . LEU B  2 101 ? 28.929  -37.287 29.852  1.00 43.15  ? 101  LEU D CD1 1 
ATOM   3356  C CD2 . LEU B  2 101 ? 30.886  -37.139 31.392  1.00 44.77  ? 101  LEU D CD2 1 
ATOM   3357  N N   . MET B  2 102 ? 33.178  -39.796 27.499  1.00 49.46  ? 102  MET D N   1 
ATOM   3358  C CA  . MET B  2 102 ? 33.482  -41.048 26.835  1.00 51.72  ? 102  MET D CA  1 
ATOM   3359  C C   . MET B  2 102 ? 34.891  -41.540 27.156  1.00 55.66  ? 102  MET D C   1 
ATOM   3360  O O   . MET B  2 102 ? 35.095  -42.731 27.389  1.00 56.93  ? 102  MET D O   1 
ATOM   3361  C CB  . MET B  2 102 ? 33.310  -40.915 25.325  1.00 53.20  ? 102  MET D CB  1 
ATOM   3362  C CG  . MET B  2 102 ? 31.862  -40.896 24.859  1.00 54.89  ? 102  MET D CG  1 
ATOM   3363  S SD  . MET B  2 102 ? 31.717  -40.987 23.047  1.00 62.59  ? 102  MET D SD  1 
ATOM   3364  C CE  . MET B  2 102 ? 30.101  -41.757 22.920  1.00 49.82  ? 102  MET D CE  1 
ATOM   3365  N N   . GLU B  2 103 ? 35.864  -40.636 27.159  1.00 50.78  ? 103  GLU D N   1 
ATOM   3366  C CA  . GLU B  2 103 ? 37.248  -41.048 27.361  1.00 53.28  ? 103  GLU D CA  1 
ATOM   3367  C C   . GLU B  2 103 ? 37.610  -41.209 28.847  1.00 61.94  ? 103  GLU D C   1 
ATOM   3368  O O   . GLU B  2 103 ? 38.619  -41.839 29.178  1.00 64.20  ? 103  GLU D O   1 
ATOM   3369  C CB  . GLU B  2 103 ? 38.198  -40.057 26.693  1.00 56.88  ? 103  GLU D CB  1 
ATOM   3370  C CG  . GLU B  2 103 ? 38.134  -40.081 25.162  1.00 66.36  ? 103  GLU D CG  1 
ATOM   3371  C CD  . GLU B  2 103 ? 38.406  -41.466 24.562  1.00 68.44  ? 103  GLU D CD  1 
ATOM   3372  O OE1 . GLU B  2 103 ? 39.322  -42.160 25.064  1.00 72.94  ? 103  GLU D OE1 1 
ATOM   3373  O OE2 . GLU B  2 103 ? 37.692  -41.860 23.602  1.00 61.65  ? 103  GLU D OE2 1 
ATOM   3374  N N   . ASN B  2 104 ? 36.808  -40.624 29.734  1.00 54.89  ? 104  ASN D N   1 
ATOM   3375  C CA  . ASN B  2 104 ? 36.924  -40.902 31.156  1.00 55.12  ? 104  ASN D CA  1 
ATOM   3376  C C   . ASN B  2 104 ? 36.554  -42.388 31.386  1.00 58.39  ? 104  ASN D C   1 
ATOM   3377  O O   . ASN B  2 104 ? 37.258  -43.120 32.090  1.00 56.81  ? 104  ASN D O   1 
ATOM   3378  C CB  . ASN B  2 104 ? 36.049  -39.941 31.991  1.00 55.68  ? 104  ASN D CB  1 
ATOM   3379  C CG  . ASN B  2 104 ? 36.734  -38.578 32.256  1.00 55.75  ? 104  ASN D CG  1 
ATOM   3380  O OD1 . ASN B  2 104 ? 37.844  -38.334 31.788  1.00 53.31  ? 104  ASN D OD1 1 
ATOM   3381  N ND2 . ASN B  2 104 ? 36.069  -37.702 33.017  1.00 49.86  ? 104  ASN D ND2 1 
ATOM   3382  N N   . GLU B  2 105 ? 35.454  -42.823 30.770  1.00 56.73  ? 105  GLU D N   1 
ATOM   3383  C CA  . GLU B  2 105 ? 34.973  -44.207 30.865  1.00 58.72  ? 105  GLU D CA  1 
ATOM   3384  C C   . GLU B  2 105 ? 36.045  -45.210 30.412  1.00 57.20  ? 105  GLU D C   1 
ATOM   3385  O O   . GLU B  2 105 ? 36.180  -46.274 30.994  1.00 64.47  ? 105  GLU D O   1 
ATOM   3386  C CB  . GLU B  2 105 ? 33.701  -44.387 30.008  1.00 59.64  ? 105  GLU D CB  1 
ATOM   3387  C CG  . GLU B  2 105 ? 32.879  -45.679 30.225  1.00 58.80  ? 105  GLU D CG  1 
ATOM   3388  C CD  . GLU B  2 105 ? 31.993  -45.642 31.478  1.00 68.42  ? 105  GLU D CD  1 
ATOM   3389  O OE1 . GLU B  2 105 ? 31.149  -44.718 31.619  1.00 63.04  ? 105  GLU D OE1 1 
ATOM   3390  O OE2 . GLU B  2 105 ? 32.146  -46.551 32.327  1.00 72.82  ? 105  GLU D OE2 1 
ATOM   3391  N N   . ARG B  2 106 ? 36.807  -44.872 29.379  1.00 57.63  ? 106  ARG D N   1 
ATOM   3392  C CA  . ARG B  2 106 ? 37.852  -45.769 28.878  1.00 64.26  ? 106  ARG D CA  1 
ATOM   3393  C C   . ARG B  2 106 ? 39.153  -45.738 29.658  1.00 63.91  ? 106  ARG D C   1 
ATOM   3394  O O   . ARG B  2 106 ? 39.866  -46.741 29.739  1.00 63.47  ? 106  ARG D O   1 
ATOM   3395  C CB  . ARG B  2 106 ? 38.170  -45.467 27.413  1.00 65.51  ? 106  ARG D CB  1 
ATOM   3396  C CG  . ARG B  2 106 ? 37.165  -46.041 26.482  1.00 65.28  ? 106  ARG D CG  1 
ATOM   3397  C CD  . ARG B  2 106 ? 37.523  -45.809 25.034  1.00 80.42  ? 106  ARG D CD  1 
ATOM   3398  N NE  . ARG B  2 106 ? 36.467  -46.344 24.189  1.00 97.72  ? 106  ARG D NE  1 
ATOM   3399  C CZ  . ARG B  2 106 ? 35.246  -45.812 24.087  1.00 94.92  ? 106  ARG D CZ  1 
ATOM   3400  N NH1 . ARG B  2 106 ? 34.923  -44.713 24.779  1.00 79.96  ? 106  ARG D NH1 1 
ATOM   3401  N NH2 . ARG B  2 106 ? 34.338  -46.383 23.292  1.00 87.74  ? 106  ARG D NH2 1 
ATOM   3402  N N   . THR B  2 107 ? 39.457  -44.585 30.230  1.00 65.35  ? 107  THR D N   1 
ATOM   3403  C CA  . THR B  2 107 ? 40.677  -44.413 30.998  1.00 63.51  ? 107  THR D CA  1 
ATOM   3404  C C   . THR B  2 107 ? 40.666  -45.249 32.278  1.00 64.52  ? 107  THR D C   1 
ATOM   3405  O O   . THR B  2 107 ? 41.656  -45.903 32.610  1.00 63.57  ? 107  THR D O   1 
ATOM   3406  C CB  . THR B  2 107 ? 40.875  -42.925 31.332  1.00 62.89  ? 107  THR D CB  1 
ATOM   3407  O OG1 . THR B  2 107 ? 41.336  -42.254 30.153  1.00 68.15  ? 107  THR D OG1 1 
ATOM   3408  C CG2 . THR B  2 107 ? 41.883  -42.734 32.448  1.00 58.79  ? 107  THR D CG2 1 
ATOM   3409  N N   . LEU B  2 108 ? 39.537  -45.258 32.976  1.00 59.49  ? 108  LEU D N   1 
ATOM   3410  C CA  . LEU B  2 108 ? 39.422  -46.040 34.187  1.00 56.71  ? 108  LEU D CA  1 
ATOM   3411  C C   . LEU B  2 108 ? 39.428  -47.547 33.883  1.00 60.06  ? 108  LEU D C   1 
ATOM   3412  O O   . LEU B  2 108 ? 40.037  -48.336 34.611  1.00 62.61  ? 108  LEU D O   1 
ATOM   3413  C CB  . LEU B  2 108 ? 38.166  -45.626 34.953  1.00 51.30  ? 108  LEU D CB  1 
ATOM   3414  C CG  . LEU B  2 108 ? 38.278  -44.183 35.469  1.00 59.30  ? 108  LEU D CG  1 
ATOM   3415  C CD1 . LEU B  2 108 ? 37.053  -43.735 36.278  1.00 57.38  ? 108  LEU D CD1 1 
ATOM   3416  C CD2 . LEU B  2 108 ? 39.567  -43.951 36.253  1.00 54.75  ? 108  LEU D CD2 1 
ATOM   3417  N N   . ASP B  2 109 ? 38.780  -47.941 32.792  1.00 59.84  ? 109  ASP D N   1 
ATOM   3418  C CA  . ASP B  2 109 ? 38.762  -49.346 32.403  1.00 58.08  ? 109  ASP D CA  1 
ATOM   3419  C C   . ASP B  2 109 ? 40.104  -49.753 31.807  1.00 58.93  ? 109  ASP D C   1 
ATOM   3420  O O   . ASP B  2 109 ? 40.408  -50.934 31.714  1.00 65.09  ? 109  ASP D O   1 
ATOM   3421  C CB  . ASP B  2 109 ? 37.633  -49.634 31.397  1.00 55.63  ? 109  ASP D CB  1 
ATOM   3422  C CG  . ASP B  2 109 ? 36.244  -49.581 32.032  1.00 61.86  ? 109  ASP D CG  1 
ATOM   3423  O OD1 . ASP B  2 109 ? 36.141  -49.687 33.275  1.00 60.20  ? 109  ASP D OD1 1 
ATOM   3424  O OD2 . ASP B  2 109 ? 35.251  -49.453 31.282  1.00 63.33  ? 109  ASP D OD2 1 
ATOM   3425  N N   . PHE B  2 110 ? 40.905  -48.772 31.402  1.00 61.95  ? 110  PHE D N   1 
ATOM   3426  C CA  . PHE B  2 110 ? 42.238  -49.037 30.846  1.00 66.23  ? 110  PHE D CA  1 
ATOM   3427  C C   . PHE B  2 110 ? 43.270  -49.440 31.895  1.00 67.10  ? 110  PHE D C   1 
ATOM   3428  O O   . PHE B  2 110 ? 44.086  -50.337 31.663  1.00 67.46  ? 110  PHE D O   1 
ATOM   3429  C CB  . PHE B  2 110 ? 42.783  -47.811 30.102  1.00 62.28  ? 110  PHE D CB  1 
ATOM   3430  C CG  . PHE B  2 110 ? 44.207  -47.976 29.631  1.00 60.44  ? 110  PHE D CG  1 
ATOM   3431  C CD1 . PHE B  2 110 ? 44.529  -48.912 28.644  1.00 61.58  ? 110  PHE D CD1 1 
ATOM   3432  C CD2 . PHE B  2 110 ? 45.227  -47.205 30.180  1.00 60.62  ? 110  PHE D CD2 1 
ATOM   3433  C CE1 . PHE B  2 110 ? 45.843  -49.071 28.204  1.00 57.44  ? 110  PHE D CE1 1 
ATOM   3434  C CE2 . PHE B  2 110 ? 46.546  -47.349 29.744  1.00 67.58  ? 110  PHE D CE2 1 
ATOM   3435  C CZ  . PHE B  2 110 ? 46.853  -48.286 28.751  1.00 61.24  ? 110  PHE D CZ  1 
ATOM   3436  N N   . HIS B  2 111 ? 43.242  -48.759 33.038  1.00 67.01  ? 111  HIS D N   1 
ATOM   3437  C CA  . HIS B  2 111 ? 44.123  -49.099 34.134  1.00 68.49  ? 111  HIS D CA  1 
ATOM   3438  C C   . HIS B  2 111 ? 43.731  -50.484 34.558  1.00 74.13  ? 111  HIS D C   1 
ATOM   3439  O O   . HIS B  2 111 ? 44.580  -51.342 34.833  1.00 76.43  ? 111  HIS D O   1 
ATOM   3440  C CB  . HIS B  2 111 ? 43.987  -48.119 35.302  1.00 66.75  ? 111  HIS D CB  1 
ATOM   3441  C CG  . HIS B  2 111 ? 44.590  -46.772 35.046  1.00 70.52  ? 111  HIS D CG  1 
ATOM   3442  N ND1 . HIS B  2 111 ? 45.843  -46.608 34.492  1.00 70.24  ? 111  HIS D ND1 1 
ATOM   3443  C CD2 . HIS B  2 111 ? 44.102  -45.524 35.252  1.00 66.55  ? 111  HIS D CD2 1 
ATOM   3444  C CE1 . HIS B  2 111 ? 46.105  -45.317 34.382  1.00 69.58  ? 111  HIS D CE1 1 
ATOM   3445  N NE2 . HIS B  2 111 ? 45.063  -44.638 34.831  1.00 69.00  ? 111  HIS D NE2 1 
ATOM   3446  N N   . ASP B  2 112 ? 42.424  -50.706 34.566  1.00 69.49  ? 112  ASP D N   1 
ATOM   3447  C CA  . ASP B  2 112 ? 41.903  -51.970 35.014  1.00 69.67  ? 112  ASP D CA  1 
ATOM   3448  C C   . ASP B  2 112 ? 42.340  -53.134 34.125  1.00 66.76  ? 112  ASP D C   1 
ATOM   3449  O O   . ASP B  2 112 ? 42.669  -54.205 34.617  1.00 65.02  ? 112  ASP D O   1 
ATOM   3450  C CB  . ASP B  2 112 ? 40.402  -51.907 35.106  1.00 66.79  ? 112  ASP D CB  1 
ATOM   3451  C CG  . ASP B  2 112 ? 39.884  -52.948 36.018  1.00 73.20  ? 112  ASP D CG  1 
ATOM   3452  O OD1 . ASP B  2 112 ? 40.271  -54.116 35.851  1.00 73.66  ? 112  ASP D OD1 1 
ATOM   3453  O OD2 . ASP B  2 112 ? 39.138  -52.603 36.945  1.00 78.21  ? 112  ASP D OD2 1 
ATOM   3454  N N   . SER B  2 113 ? 42.361  -52.911 32.820  1.00 68.61  ? 113  SER D N   1 
ATOM   3455  C CA  . SER B  2 113 ? 42.836  -53.927 31.894  1.00 69.95  ? 113  SER D CA  1 
ATOM   3456  C C   . SER B  2 113 ? 44.296  -54.263 32.173  1.00 68.87  ? 113  SER D C   1 
ATOM   3457  O O   . SER B  2 113 ? 44.712  -55.405 32.004  1.00 71.52  ? 113  SER D O   1 
ATOM   3458  C CB  . SER B  2 113 ? 42.672  -53.449 30.444  1.00 69.05  ? 113  SER D CB  1 
ATOM   3459  O OG  . SER B  2 113 ? 43.393  -54.253 29.519  1.00 66.52  ? 113  SER D OG  1 
ATOM   3460  N N   . ASN B  2 114 ? 45.065  -53.271 32.614  1.00 67.37  ? 114  ASN D N   1 
ATOM   3461  C CA  . ASN B  2 114 ? 46.496  -53.459 32.842  1.00 72.83  ? 114  ASN D CA  1 
ATOM   3462  C C   . ASN B  2 114 ? 46.792  -54.219 34.149  1.00 74.69  ? 114  ASN D C   1 
ATOM   3463  O O   . ASN B  2 114 ? 47.820  -54.891 34.255  1.00 71.02  ? 114  ASN D O   1 
ATOM   3464  C CB  . ASN B  2 114 ? 47.232  -52.105 32.842  1.00 75.78  ? 114  ASN D CB  1 
ATOM   3465  C CG  . ASN B  2 114 ? 47.439  -51.532 31.430  1.00 74.00  ? 114  ASN D CG  1 
ATOM   3466  O OD1 . ASN B  2 114 ? 47.295  -52.234 30.421  1.00 74.85  ? 114  ASN D OD1 1 
ATOM   3467  N ND2 . ASN B  2 114 ? 47.800  -50.250 31.365  1.00 70.84  ? 114  ASN D ND2 1 
ATOM   3468  N N   . VAL B  2 115 ? 45.889  -54.101 35.129  1.00 73.74  ? 115  VAL D N   1 
ATOM   3469  C CA  . VAL B  2 115 ? 45.997  -54.811 36.408  1.00 71.35  ? 115  VAL D CA  1 
ATOM   3470  C C   . VAL B  2 115 ? 45.746  -56.317 36.213  1.00 73.54  ? 115  VAL D C   1 
ATOM   3471  O O   . VAL B  2 115 ? 46.534  -57.152 36.657  1.00 75.03  ? 115  VAL D O   1 
ATOM   3472  C CB  . VAL B  2 115 ? 44.993  -54.240 37.451  1.00 69.96  ? 115  VAL D CB  1 
ATOM   3473  C CG1 . VAL B  2 115 ? 44.718  -55.251 38.562  1.00 68.07  ? 115  VAL D CG1 1 
ATOM   3474  C CG2 . VAL B  2 115 ? 45.490  -52.914 38.028  1.00 67.42  ? 115  VAL D CG2 1 
ATOM   3475  N N   . LYS B  2 116 ? 44.658  -56.647 35.523  1.00 70.22  ? 116  LYS D N   1 
ATOM   3476  C CA  . LYS B  2 116 ? 44.306  -58.030 35.208  1.00 72.29  ? 116  LYS D CA  1 
ATOM   3477  C C   . LYS B  2 116 ? 45.349  -58.727 34.328  1.00 79.14  ? 116  LYS D C   1 
ATOM   3478  O O   . LYS B  2 116 ? 45.604  -59.921 34.477  1.00 81.95  ? 116  LYS D O   1 
ATOM   3479  C CB  . LYS B  2 116 ? 42.948  -58.078 34.507  1.00 70.13  ? 116  LYS D CB  1 
ATOM   3480  C CG  . LYS B  2 116 ? 42.532  -59.461 34.043  1.00 71.42  ? 116  LYS D CG  1 
ATOM   3481  C CD  . LYS B  2 116 ? 41.197  -59.411 33.334  1.00 76.45  ? 116  LYS D CD  1 
ATOM   3482  C CE  . LYS B  2 116 ? 40.702  -60.789 32.932  1.00 77.74  ? 116  LYS D CE  1 
ATOM   3483  N NZ  . LYS B  2 116 ? 39.410  -60.674 32.194  1.00 73.36  ? 116  LYS D NZ  1 
ATOM   3484  N N   . ASN B  2 117 ? 45.913  -57.996 33.374  1.00 77.35  ? 117  ASN D N   1 
ATOM   3485  C CA  . ASN B  2 117 ? 46.905  -58.584 32.489  1.00 79.40  ? 117  ASN D CA  1 
ATOM   3486  C C   . ASN B  2 117 ? 48.216  -58.890 33.219  1.00 83.62  ? 117  ASN D C   1 
ATOM   3487  O O   . ASN B  2 117 ? 48.877  -59.883 32.915  1.00 89.12  ? 117  ASN D O   1 
ATOM   3488  C CB  . ASN B  2 117 ? 47.164  -57.657 31.299  1.00 78.92  ? 117  ASN D CB  1 
ATOM   3489  C CG  . ASN B  2 117 ? 45.993  -57.609 30.318  1.00 79.29  ? 117  ASN D CG  1 
ATOM   3490  O OD1 . ASN B  2 117 ? 44.928  -58.194 30.557  1.00 72.93  ? 117  ASN D OD1 1 
ATOM   3491  N ND2 . ASN B  2 117 ? 46.190  -56.904 29.205  1.00 81.97  ? 117  ASN D ND2 1 
ATOM   3492  N N   . LEU B  2 118 ? 48.565  -58.051 34.196  1.00 81.47  ? 118  LEU D N   1 
ATOM   3493  C CA  . LEU B  2 118 ? 49.763  -58.243 35.026  1.00 83.34  ? 118  LEU D CA  1 
ATOM   3494  C C   . LEU B  2 118 ? 49.579  -59.393 36.013  1.00 87.65  ? 118  LEU D C   1 
ATOM   3495  O O   . LEU B  2 118 ? 50.514  -60.151 36.280  1.00 89.07  ? 118  LEU D O   1 
ATOM   3496  C CB  . LEU B  2 118 ? 50.116  -56.962 35.786  1.00 79.46  ? 118  LEU D CB  1 
ATOM   3497  C CG  . LEU B  2 118 ? 51.420  -57.009 36.582  1.00 82.13  ? 118  LEU D CG  1 
ATOM   3498  C CD1 . LEU B  2 118 ? 52.596  -57.081 35.635  1.00 86.29  ? 118  LEU D CD1 1 
ATOM   3499  C CD2 . LEU B  2 118 ? 51.557  -55.816 37.514  1.00 81.06  ? 118  LEU D CD2 1 
ATOM   3500  N N   . TYR B  2 119 ? 48.380  -59.486 36.584  1.00 84.89  ? 119  TYR D N   1 
ATOM   3501  C CA  . TYR B  2 119 ? 48.021  -60.601 37.452  1.00 85.94  ? 119  TYR D CA  1 
ATOM   3502  C C   . TYR B  2 119 ? 48.090  -61.901 36.651  1.00 87.30  ? 119  TYR D C   1 
ATOM   3503  O O   . TYR B  2 119 ? 48.676  -62.880 37.095  1.00 90.50  ? 119  TYR D O   1 
ATOM   3504  C CB  . TYR B  2 119 ? 46.612  -60.410 38.041  1.00 85.43  ? 119  TYR D CB  1 
ATOM   3505  C CG  . TYR B  2 119 ? 46.123  -61.559 38.907  1.00 87.34  ? 119  TYR D CG  1 
ATOM   3506  C CD1 . TYR B  2 119 ? 45.444  -62.643 38.348  1.00 86.63  ? 119  TYR D CD1 1 
ATOM   3507  C CD2 . TYR B  2 119 ? 46.323  -61.551 40.286  1.00 86.03  ? 119  TYR D CD2 1 
ATOM   3508  C CE1 . TYR B  2 119 ? 45.000  -63.696 39.134  1.00 86.67  ? 119  TYR D CE1 1 
ATOM   3509  C CE2 . TYR B  2 119 ? 45.881  -62.594 41.079  1.00 89.59  ? 119  TYR D CE2 1 
ATOM   3510  C CZ  . TYR B  2 119 ? 45.219  -63.663 40.499  1.00 89.08  ? 119  TYR D CZ  1 
ATOM   3511  O OH  . TYR B  2 119 ? 44.777  -64.698 41.291  1.00 89.08  ? 119  TYR D OH  1 
ATOM   3512  N N   . ASP B  2 120 ? 47.500  -61.891 35.459  1.00 89.48  ? 120  ASP D N   1 
ATOM   3513  C CA  . ASP B  2 120 ? 47.479  -63.061 34.584  1.00 89.31  ? 120  ASP D CA  1 
ATOM   3514  C C   . ASP B  2 120 ? 48.872  -63.369 34.035  1.00 91.63  ? 120  ASP D C   1 
ATOM   3515  O O   . ASP B  2 120 ? 49.134  -64.469 33.547  1.00 91.67  ? 120  ASP D O   1 
ATOM   3516  C CB  . ASP B  2 120 ? 46.496  -62.843 33.427  1.00 87.24  ? 120  ASP D CB  1 
ATOM   3517  C CG  . ASP B  2 120 ? 45.048  -62.971 33.858  1.00 88.18  ? 120  ASP D CG  1 
ATOM   3518  O OD1 . ASP B  2 120 ? 44.799  -63.354 35.025  1.00 88.19  ? 120  ASP D OD1 1 
ATOM   3519  O OD2 . ASP B  2 120 ? 44.160  -62.683 33.025  1.00 83.91  ? 120  ASP D OD2 1 
ATOM   3520  N N   . LYS B  2 121 ? 49.755  -62.377 34.106  1.00 90.70  ? 121  LYS D N   1 
ATOM   3521  C CA  . LYS B  2 121 ? 51.123  -62.505 33.606  1.00 95.31  ? 121  LYS D CA  1 
ATOM   3522  C C   . LYS B  2 121 ? 51.972  -63.445 34.469  1.00 95.23  ? 121  LYS D C   1 
ATOM   3523  O O   . LYS B  2 121 ? 52.776  -64.229 33.951  1.00 93.32  ? 121  LYS D O   1 
ATOM   3524  C CB  . LYS B  2 121 ? 51.769  -61.111 33.542  1.00 91.29  ? 121  LYS D CB  1 
ATOM   3525  C CG  . LYS B  2 121 ? 53.251  -61.059 33.177  1.00 91.68  ? 121  LYS D CG  1 
ATOM   3526  C CD  . LYS B  2 121 ? 53.857  -59.716 33.609  1.00 89.45  ? 121  LYS D CD  1 
ATOM   3527  C CE  . LYS B  2 121 ? 55.349  -59.621 33.317  1.00 90.63  ? 121  LYS D CE  1 
ATOM   3528  N NZ  . LYS B  2 121 ? 55.615  -59.488 31.851  1.00 90.41  ? 121  LYS D NZ  1 
ATOM   3529  N N   . VAL B  2 122 ? 51.769  -63.362 35.784  1.00 94.33  ? 122  VAL D N   1 
ATOM   3530  C CA  . VAL B  2 122 ? 52.516  -64.160 36.761  1.00 97.28  ? 122  VAL D CA  1 
ATOM   3531  C C   . VAL B  2 122 ? 51.812  -65.491 37.073  1.00 98.85  ? 122  VAL D C   1 
ATOM   3532  O O   . VAL B  2 122 ? 52.469  -66.483 37.383  1.00 100.17 ? 122  VAL D O   1 
ATOM   3533  C CB  . VAL B  2 122 ? 52.759  -63.370 38.070  1.00 90.41  ? 122  VAL D CB  1 
ATOM   3534  C CG1 . VAL B  2 122 ? 53.886  -62.349 37.889  1.00 85.28  ? 122  VAL D CG1 1 
ATOM   3535  C CG2 . VAL B  2 122 ? 51.506  -62.673 38.491  1.00 91.13  ? 122  VAL D CG2 1 
ATOM   3536  N N   . ARG B  2 123 ? 50.481  -65.492 37.028  1.00 95.12  ? 123  ARG D N   1 
ATOM   3537  C CA  . ARG B  2 123 ? 49.696  -66.709 37.212  1.00 92.63  ? 123  ARG D CA  1 
ATOM   3538  C C   . ARG B  2 123 ? 50.028  -67.711 36.108  1.00 97.96  ? 123  ARG D C   1 
ATOM   3539  O O   . ARG B  2 123 ? 49.936  -68.921 36.304  1.00 100.16 ? 123  ARG D O   1 
ATOM   3540  C CB  . ARG B  2 123 ? 48.207  -66.388 37.226  1.00 91.89  ? 123  ARG D CB  1 
ATOM   3541  C CG  . ARG B  2 123 ? 47.306  -67.593 37.330  1.00 94.03  ? 123  ARG D CG  1 
ATOM   3542  C CD  . ARG B  2 123 ? 45.866  -67.194 37.096  1.00 93.93  ? 123  ARG D CD  1 
ATOM   3543  N NE  . ARG B  2 123 ? 45.706  -66.608 35.772  1.00 96.66  ? 123  ARG D NE  1 
ATOM   3544  C CZ  . ARG B  2 123 ? 45.538  -67.307 34.655  1.00 98.90  ? 123  ARG D CZ  1 
ATOM   3545  N NH1 . ARG B  2 123 ? 45.531  -68.632 34.695  1.00 98.55  ? 123  ARG D NH1 1 
ATOM   3546  N NH2 . ARG B  2 123 ? 45.399  -66.677 33.494  1.00 95.02  ? 123  ARG D NH2 1 
ATOM   3547  N N   . LEU B  2 124 ? 50.382  -67.186 34.937  1.00 97.10  ? 124  LEU D N   1 
ATOM   3548  C CA  . LEU B  2 124 ? 50.813  -67.997 33.800  1.00 95.23  ? 124  LEU D CA  1 
ATOM   3549  C C   . LEU B  2 124 ? 52.275  -68.432 33.941  1.00 100.45 ? 124  LEU D C   1 
ATOM   3550  O O   . LEU B  2 124 ? 52.739  -69.331 33.236  1.00 99.16  ? 124  LEU D O   1 
ATOM   3551  C CB  . LEU B  2 124 ? 50.635  -67.229 32.486  1.00 96.20  ? 124  LEU D CB  1 
ATOM   3552  C CG  . LEU B  2 124 ? 49.257  -67.213 31.824  1.00 100.40 ? 124  LEU D CG  1 
ATOM   3553  C CD1 . LEU B  2 124 ? 49.178  -66.146 30.737  1.00 96.56  ? 124  LEU D CD1 1 
ATOM   3554  C CD2 . LEU B  2 124 ? 48.968  -68.587 31.233  1.00 97.92  ? 124  LEU D CD2 1 
ATOM   3555  N N   . GLN B  2 125 ? 53.001  -67.775 34.841  1.00 103.17 ? 125  GLN D N   1 
ATOM   3556  C CA  . GLN B  2 125 ? 54.430  -68.027 35.016  1.00 105.06 ? 125  GLN D CA  1 
ATOM   3557  C C   . GLN B  2 125 ? 54.726  -69.074 36.092  1.00 110.45 ? 125  GLN D C   1 
ATOM   3558  O O   . GLN B  2 125 ? 55.576  -69.956 35.920  1.00 111.72 ? 125  GLN D O   1 
ATOM   3559  C CB  . GLN B  2 125 ? 55.144  -66.723 35.384  1.00 105.14 ? 125  GLN D CB  1 
ATOM   3560  C CG  . GLN B  2 125 ? 56.479  -66.507 34.700  1.00 109.79 ? 125  GLN D CG  1 
ATOM   3561  C CD  . GLN B  2 125 ? 57.058  -65.139 34.995  1.00 115.81 ? 125  GLN D CD  1 
ATOM   3562  O OE1 . GLN B  2 125 ? 56.441  -64.315 35.676  1.00 109.19 ? 125  GLN D OE1 1 
ATOM   3563  N NE2 . GLN B  2 125 ? 58.258  -64.895 34.496  1.00 123.38 ? 125  GLN D NE2 1 
ATOM   3564  N N   . LEU B  2 126 ? 53.999  -68.978 37.198  1.00 108.93 ? 126  LEU D N   1 
ATOM   3565  C CA  . LEU B  2 126 ? 54.247  -69.819 38.357  1.00 104.55 ? 126  LEU D CA  1 
ATOM   3566  C C   . LEU B  2 126 ? 53.583  -71.171 38.161  1.00 108.82 ? 126  LEU D C   1 
ATOM   3567  O O   . LEU B  2 126 ? 54.204  -72.211 38.376  1.00 115.81 ? 126  LEU D O   1 
ATOM   3568  C CB  . LEU B  2 126 ? 53.747  -69.128 39.624  1.00 98.87  ? 126  LEU D CB  1 
ATOM   3569  C CG  . LEU B  2 126 ? 54.377  -67.749 39.856  1.00 94.98  ? 126  LEU D CG  1 
ATOM   3570  C CD1 . LEU B  2 126 ? 54.020  -67.216 41.230  1.00 95.27  ? 126  LEU D CD1 1 
ATOM   3571  C CD2 . LEU B  2 126 ? 55.887  -67.792 39.674  1.00 98.07  ? 126  LEU D CD2 1 
ATOM   3572  N N   . ARG B  2 127 ? 52.334  -71.142 37.705  1.00 109.81 ? 127  ARG D N   1 
ATOM   3573  C CA  . ARG B  2 127 ? 51.523  -72.343 37.533  1.00 108.04 ? 127  ARG D CA  1 
ATOM   3574  C C   . ARG B  2 127 ? 51.352  -73.134 38.838  1.00 107.05 ? 127  ARG D C   1 
ATOM   3575  O O   . ARG B  2 127 ? 50.944  -72.565 39.852  1.00 103.92 ? 127  ARG D O   1 
ATOM   3576  C CB  . ARG B  2 127 ? 52.159  -73.195 36.434  1.00 106.06 ? 127  ARG D CB  1 
ATOM   3577  C CG  . ARG B  2 127 ? 52.561  -72.338 35.238  1.00 101.63 ? 127  ARG D CG  1 
ATOM   3578  C CD  . ARG B  2 127 ? 53.771  -72.868 34.493  1.00 108.00 ? 127  ARG D CD  1 
ATOM   3579  N NE  . ARG B  2 127 ? 53.579  -74.203 33.939  1.00 112.91 ? 127  ARG D NE  1 
ATOM   3580  C CZ  . ARG B  2 127 ? 54.408  -74.772 33.067  1.00 109.95 ? 127  ARG D CZ  1 
ATOM   3581  N NH1 . ARG B  2 127 ? 55.479  -74.120 32.637  1.00 109.79 ? 127  ARG D NH1 1 
ATOM   3582  N NH2 . ARG B  2 127 ? 54.164  -75.991 32.619  1.00 106.56 ? 127  ARG D NH2 1 
ATOM   3583  N N   . ASP B  2 128 ? 51.658  -74.429 38.831  1.00 114.02 ? 128  ASP D N   1 
ATOM   3584  C CA  . ASP B  2 128 ? 51.374  -75.266 40.003  1.00 115.93 ? 128  ASP D CA  1 
ATOM   3585  C C   . ASP B  2 128 ? 52.439  -75.192 41.099  1.00 116.95 ? 128  ASP D C   1 
ATOM   3586  O O   . ASP B  2 128 ? 52.450  -76.020 42.011  1.00 118.49 ? 128  ASP D O   1 
ATOM   3587  C CB  . ASP B  2 128 ? 51.183  -76.738 39.585  1.00 114.94 ? 128  ASP D CB  1 
ATOM   3588  C CG  . ASP B  2 128 ? 52.339  -77.283 38.753  1.00 111.95 ? 128  ASP D CG  1 
ATOM   3589  O OD1 . ASP B  2 128 ? 53.457  -76.728 38.824  1.00 112.58 ? 128  ASP D OD1 1 
ATOM   3590  O OD2 . ASP B  2 128 ? 52.124  -78.277 38.027  1.00 111.17 ? 128  ASP D OD2 1 
ATOM   3591  N N   . ASN B  2 129 ? 53.307  -74.186 41.032  1.00 115.76 ? 129  ASN D N   1 
ATOM   3592  C CA  . ASN B  2 129 ? 54.282  -73.946 42.096  1.00 117.45 ? 129  ASN D CA  1 
ATOM   3593  C C   . ASN B  2 129 ? 53.754  -72.969 43.155  1.00 121.07 ? 129  ASN D C   1 
ATOM   3594  O O   . ASN B  2 129 ? 54.485  -72.604 44.078  1.00 117.33 ? 129  ASN D O   1 
ATOM   3595  C CB  . ASN B  2 129 ? 55.604  -73.428 41.514  1.00 117.17 ? 129  ASN D CB  1 
ATOM   3596  C CG  . ASN B  2 129 ? 56.353  -74.486 40.714  1.00 120.59 ? 129  ASN D CG  1 
ATOM   3597  O OD1 . ASN B  2 129 ? 55.815  -75.555 40.418  1.00 120.07 ? 129  ASN D OD1 1 
ATOM   3598  N ND2 . ASN B  2 129 ? 57.599  -74.187 40.352  1.00 120.69 ? 129  ASN D ND2 1 
ATOM   3599  N N   . ALA B  2 130 ? 52.488  -72.562 43.014  1.00 120.23 ? 130  ALA D N   1 
ATOM   3600  C CA  . ALA B  2 130 ? 51.830  -71.635 43.944  1.00 114.60 ? 130  ALA D CA  1 
ATOM   3601  C C   . ALA B  2 130 ? 50.321  -71.873 44.053  1.00 115.04 ? 130  ALA D C   1 
ATOM   3602  O O   . ALA B  2 130 ? 49.752  -72.633 43.269  1.00 116.15 ? 130  ALA D O   1 
ATOM   3603  C CB  . ALA B  2 130 ? 52.082  -70.200 43.504  1.00 111.17 ? 130  ALA D CB  1 
ATOM   3604  N N   . LYS B  2 131 ? 49.677  -71.219 45.023  1.00 114.08 ? 131  LYS D N   1 
ATOM   3605  C CA  . LYS B  2 131 ? 48.217  -71.301 45.166  1.00 112.27 ? 131  LYS D CA  1 
ATOM   3606  C C   . LYS B  2 131 ? 47.577  -69.933 44.943  1.00 108.82 ? 131  LYS D C   1 
ATOM   3607  O O   . LYS B  2 131 ? 48.036  -68.928 45.485  1.00 110.67 ? 131  LYS D O   1 
ATOM   3608  C CB  . LYS B  2 131 ? 47.794  -71.799 46.557  1.00 108.58 ? 131  LYS D CB  1 
ATOM   3609  C CG  . LYS B  2 131 ? 48.205  -73.201 46.958  1.00 109.12 ? 131  LYS D CG  1 
ATOM   3610  C CD  . LYS B  2 131 ? 47.471  -73.601 48.244  1.00 108.36 ? 131  LYS D CD  1 
ATOM   3611  C CE  . LYS B  2 131 ? 47.753  -72.603 49.373  1.00 107.21 ? 131  LYS D CE  1 
ATOM   3612  N NZ  . LYS B  2 131 ? 47.064  -72.920 50.660  1.00 95.67  ? 131  LYS D NZ  1 
ATOM   3613  N N   . GLU B  2 132 ? 46.489  -69.905 44.182  1.00 107.47 ? 132  GLU D N   1 
ATOM   3614  C CA  . GLU B  2 132 ? 45.735  -68.675 43.993  1.00 101.57 ? 132  GLU D CA  1 
ATOM   3615  C C   . GLU B  2 132 ? 44.795  -68.489 45.176  1.00 102.93 ? 132  GLU D C   1 
ATOM   3616  O O   . GLU B  2 132 ? 43.842  -69.260 45.332  1.00 99.02  ? 132  GLU D O   1 
ATOM   3617  C CB  . GLU B  2 132 ? 44.948  -68.710 42.678  1.00 100.05 ? 132  GLU D CB  1 
ATOM   3618  C CG  . GLU B  2 132 ? 45.788  -69.080 41.464  1.00 101.40 ? 132  GLU D CG  1 
ATOM   3619  C CD  . GLU B  2 132 ? 45.082  -68.815 40.145  1.00 103.18 ? 132  GLU D CD  1 
ATOM   3620  O OE1 . GLU B  2 132 ? 44.229  -67.901 40.096  1.00 102.40 ? 132  GLU D OE1 1 
ATOM   3621  O OE2 . GLU B  2 132 ? 45.379  -69.526 39.158  1.00 104.94 ? 132  GLU D OE2 1 
ATOM   3622  N N   . LEU B  2 133 ? 45.052  -67.480 46.008  1.00 101.07 ? 133  LEU D N   1 
ATOM   3623  C CA  . LEU B  2 133 ? 44.188  -67.246 47.165  1.00 98.66  ? 133  LEU D CA  1 
ATOM   3624  C C   . LEU B  2 133 ? 42.850  -66.627 46.745  1.00 98.31  ? 133  LEU D C   1 
ATOM   3625  O O   . LEU B  2 133 ? 41.840  -66.823 47.417  1.00 93.96  ? 133  LEU D O   1 
ATOM   3626  C CB  . LEU B  2 133 ? 44.890  -66.372 48.222  1.00 100.44 ? 133  LEU D CB  1 
ATOM   3627  C CG  . LEU B  2 133 ? 45.963  -66.993 49.143  1.00 98.34  ? 133  LEU D CG  1 
ATOM   3628  C CD1 . LEU B  2 133 ? 47.229  -67.433 48.409  1.00 101.75 ? 133  LEU D CD1 1 
ATOM   3629  C CD2 . LEU B  2 133 ? 46.316  -66.061 50.307  1.00 93.74  ? 133  LEU D CD2 1 
ATOM   3630  N N   . GLY B  2 134 ? 42.846  -65.882 45.640  1.00 102.47 ? 134  GLY D N   1 
ATOM   3631  C CA  . GLY B  2 134 ? 41.612  -65.355 45.073  1.00 98.10  ? 134  GLY D CA  1 
ATOM   3632  C C   . GLY B  2 134 ? 41.319  -63.898 45.398  1.00 97.07  ? 134  GLY D C   1 
ATOM   3633  O O   . GLY B  2 134 ? 40.189  -63.432 45.207  1.00 91.97  ? 134  GLY D O   1 
ATOM   3634  N N   . ASN B  2 135 ? 42.329  -63.186 45.897  1.00 96.62  ? 135  ASN D N   1 
ATOM   3635  C CA  . ASN B  2 135 ? 42.197  -61.773 46.259  1.00 94.61  ? 135  ASN D CA  1 
ATOM   3636  C C   . ASN B  2 135 ? 43.415  -60.962 45.808  1.00 91.76  ? 135  ASN D C   1 
ATOM   3637  O O   . ASN B  2 135 ? 43.656  -59.846 46.283  1.00 88.56  ? 135  ASN D O   1 
ATOM   3638  C CB  . ASN B  2 135 ? 41.964  -61.622 47.766  1.00 90.53  ? 135  ASN D CB  1 
ATOM   3639  C CG  . ASN B  2 135 ? 43.126  -62.135 48.593  1.00 94.62  ? 135  ASN D CG  1 
ATOM   3640  O OD1 . ASN B  2 135 ? 43.941  -62.931 48.118  1.00 94.02  ? 135  ASN D OD1 1 
ATOM   3641  N ND2 . ASN B  2 135 ? 43.194  -61.702 49.850  1.00 91.86  ? 135  ASN D ND2 1 
ATOM   3642  N N   . GLY B  2 136 ? 44.175  -61.543 44.883  1.00 89.98  ? 136  GLY D N   1 
ATOM   3643  C CA  . GLY B  2 136 ? 45.356  -60.908 44.328  1.00 93.67  ? 136  GLY D CA  1 
ATOM   3644  C C   . GLY B  2 136 ? 46.674  -61.441 44.860  1.00 101.65 ? 136  GLY D C   1 
ATOM   3645  O O   . GLY B  2 136 ? 47.740  -61.055 44.372  1.00 96.20  ? 136  GLY D O   1 
ATOM   3646  N N   . CYS B  2 137 ? 46.606  -62.342 45.841  1.00 106.66 ? 137  CYS D N   1 
ATOM   3647  C CA  . CYS B  2 137 ? 47.808  -62.893 46.466  1.00 102.69 ? 137  CYS D CA  1 
ATOM   3648  C C   . CYS B  2 137 ? 48.133  -64.326 46.004  1.00 103.94 ? 137  CYS D C   1 
ATOM   3649  O O   . CYS B  2 137 ? 47.233  -65.151 45.800  1.00 98.93  ? 137  CYS D O   1 
ATOM   3650  C CB  . CYS B  2 137 ? 47.662  -62.868 47.992  1.00 102.92 ? 137  CYS D CB  1 
ATOM   3651  S SG  . CYS B  2 137 ? 47.685  -61.220 48.768  1.00 107.05 ? 137  CYS D SG  1 
ATOM   3652  N N   . PHE B  2 138 ? 49.428  -64.607 45.841  1.00 108.26 ? 138  PHE D N   1 
ATOM   3653  C CA  . PHE B  2 138 ? 49.922  -65.957 45.537  1.00 112.84 ? 138  PHE D CA  1 
ATOM   3654  C C   . PHE B  2 138 ? 50.860  -66.518 46.636  1.00 119.78 ? 138  PHE D C   1 
ATOM   3655  O O   . PHE B  2 138 ? 51.958  -65.982 46.838  1.00 120.04 ? 138  PHE D O   1 
ATOM   3656  C CB  . PHE B  2 138 ? 50.691  -65.981 44.202  1.00 106.34 ? 138  PHE D CB  1 
ATOM   3657  C CG  . PHE B  2 138 ? 49.837  -65.776 42.972  1.00 107.04 ? 138  PHE D CG  1 
ATOM   3658  C CD1 . PHE B  2 138 ? 49.000  -66.786 42.520  1.00 107.30 ? 138  PHE D CD1 1 
ATOM   3659  C CD2 . PHE B  2 138 ? 49.946  -64.621 42.207  1.00 103.47 ? 138  PHE D CD2 1 
ATOM   3660  C CE1 . PHE B  2 138 ? 48.231  -66.622 41.361  1.00 102.70 ? 138  PHE D CE1 1 
ATOM   3661  C CE2 . PHE B  2 138 ? 49.184  -64.453 41.048  1.00 95.50  ? 138  PHE D CE2 1 
ATOM   3662  C CZ  . PHE B  2 138 ? 48.328  -65.457 40.626  1.00 95.61  ? 138  PHE D CZ  1 
ATOM   3663  N N   . GLU B  2 139 ? 50.464  -67.602 47.316  1.00 120.35 ? 139  GLU D N   1 
ATOM   3664  C CA  . GLU B  2 139 ? 51.369  -68.268 48.264  1.00 118.99 ? 139  GLU D CA  1 
ATOM   3665  C C   . GLU B  2 139 ? 52.012  -69.503 47.630  1.00 116.18 ? 139  GLU D C   1 
ATOM   3666  O O   . GLU B  2 139 ? 51.387  -70.565 47.572  1.00 108.70 ? 139  GLU D O   1 
ATOM   3667  C CB  . GLU B  2 139 ? 50.619  -68.682 49.531  1.00 119.66 ? 139  GLU D CB  1 
ATOM   3668  C CG  . GLU B  2 139 ? 51.526  -69.243 50.610  1.00 124.00 ? 139  GLU D CG  1 
ATOM   3669  C CD  . GLU B  2 139 ? 50.783  -69.617 51.876  1.00 123.97 ? 139  GLU D CD  1 
ATOM   3670  O OE1 . GLU B  2 139 ? 49.707  -70.254 51.792  1.00 119.66 ? 139  GLU D OE1 1 
ATOM   3671  O OE2 . GLU B  2 139 ? 51.279  -69.262 52.962  1.00 127.88 ? 139  GLU D OE2 1 
ATOM   3672  N N   . PHE B  2 140 ? 53.264  -69.367 47.187  1.00 119.40 ? 140  PHE D N   1 
ATOM   3673  C CA  . PHE B  2 140 ? 53.932  -70.454 46.460  1.00 121.87 ? 140  PHE D CA  1 
ATOM   3674  C C   . PHE B  2 140 ? 54.499  -71.544 47.371  1.00 125.18 ? 140  PHE D C   1 
ATOM   3675  O O   . PHE B  2 140 ? 54.548  -71.400 48.599  1.00 121.84 ? 140  PHE D O   1 
ATOM   3676  C CB  . PHE B  2 140 ? 54.990  -69.963 45.428  1.00 119.54 ? 140  PHE D CB  1 
ATOM   3677  C CG  . PHE B  2 140 ? 56.049  -69.021 45.933  1.00 121.43 ? 140  PHE D CG  1 
ATOM   3678  C CD1 . PHE B  2 140 ? 55.810  -68.089 46.924  1.00 122.76 ? 140  PHE D CD1 1 
ATOM   3679  C CD2 . PHE B  2 140 ? 57.295  -69.032 45.323  1.00 123.11 ? 140  PHE D CD2 1 
ATOM   3680  C CE1 . PHE B  2 140 ? 56.797  -67.223 47.323  1.00 125.06 ? 140  PHE D CE1 1 
ATOM   3681  C CE2 . PHE B  2 140 ? 58.284  -68.174 45.722  1.00 125.93 ? 140  PHE D CE2 1 
ATOM   3682  C CZ  . PHE B  2 140 ? 58.033  -67.267 46.730  1.00 125.64 ? 140  PHE D CZ  1 
ATOM   3683  N N   . TYR B  2 141 ? 54.902  -72.641 46.727  1.00 126.33 ? 141  TYR D N   1 
ATOM   3684  C CA  . TYR B  2 141 ? 55.247  -73.900 47.383  1.00 122.32 ? 141  TYR D CA  1 
ATOM   3685  C C   . TYR B  2 141 ? 56.737  -74.111 47.707  1.00 123.62 ? 141  TYR D C   1 
ATOM   3686  O O   . TYR B  2 141 ? 57.138  -75.224 48.063  1.00 124.95 ? 141  TYR D O   1 
ATOM   3687  C CB  . TYR B  2 141 ? 54.786  -75.052 46.480  1.00 119.57 ? 141  TYR D CB  1 
ATOM   3688  C CG  . TYR B  2 141 ? 53.291  -75.301 46.431  1.00 114.40 ? 141  TYR D CG  1 
ATOM   3689  C CD1 . TYR B  2 141 ? 52.501  -75.224 47.574  1.00 112.27 ? 141  TYR D CD1 1 
ATOM   3690  C CD2 . TYR B  2 141 ? 52.671  -75.622 45.227  1.00 109.83 ? 141  TYR D CD2 1 
ATOM   3691  C CE1 . TYR B  2 141 ? 51.137  -75.458 47.514  1.00 107.31 ? 141  TYR D CE1 1 
ATOM   3692  C CE2 . TYR B  2 141 ? 51.316  -75.856 45.159  1.00 106.04 ? 141  TYR D CE2 1 
ATOM   3693  C CZ  . TYR B  2 141 ? 50.555  -75.775 46.302  1.00 106.56 ? 141  TYR D CZ  1 
ATOM   3694  O OH  . TYR B  2 141 ? 49.206  -76.015 46.234  1.00 103.43 ? 141  TYR D OH  1 
ATOM   3695  N N   . HIS B  2 142 ? 57.556  -73.065 47.597  1.00 123.40 ? 142  HIS D N   1 
ATOM   3696  C CA  . HIS B  2 142 ? 58.964  -73.184 47.986  1.00 124.48 ? 142  HIS D CA  1 
ATOM   3697  C C   . HIS B  2 142 ? 59.475  -71.891 48.618  1.00 125.02 ? 142  HIS D C   1 
ATOM   3698  O O   . HIS B  2 142 ? 58.695  -71.015 48.992  1.00 125.97 ? 142  HIS D O   1 
ATOM   3699  C CB  . HIS B  2 142 ? 59.855  -73.558 46.793  1.00 125.10 ? 142  HIS D CB  1 
ATOM   3700  C CG  . HIS B  2 142 ? 59.884  -72.536 45.697  1.00 129.39 ? 142  HIS D CG  1 
ATOM   3701  N ND1 . HIS B  2 142 ? 60.661  -71.398 45.761  1.00 130.40 ? 142  HIS D ND1 1 
ATOM   3702  C CD2 . HIS B  2 142 ? 59.253  -72.493 44.498  1.00 128.97 ? 142  HIS D CD2 1 
ATOM   3703  C CE1 . HIS B  2 142 ? 60.498  -70.692 44.656  1.00 130.40 ? 142  HIS D CE1 1 
ATOM   3704  N NE2 . HIS B  2 142 ? 59.648  -71.335 43.873  1.00 128.72 ? 142  HIS D NE2 1 
ATOM   3705  N N   . ARG B  2 143 ? 60.789  -71.785 48.759  1.00 123.73 ? 143  ARG D N   1 
ATOM   3706  C CA  . ARG B  2 143 ? 61.368  -70.593 49.353  1.00 128.21 ? 143  ARG D CA  1 
ATOM   3707  C C   . ARG B  2 143 ? 61.990  -69.698 48.297  1.00 128.12 ? 143  ARG D C   1 
ATOM   3708  O O   . ARG B  2 143 ? 62.584  -70.173 47.324  1.00 123.18 ? 143  ARG D O   1 
ATOM   3709  C CB  . ARG B  2 143 ? 62.409  -70.972 50.409  1.00 125.53 ? 143  ARG D CB  1 
ATOM   3710  C CG  . ARG B  2 143 ? 61.816  -71.473 51.712  1.00 120.69 ? 143  ARG D CG  1 
ATOM   3711  C CD  . ARG B  2 143 ? 62.919  -71.805 52.690  1.00 117.84 ? 143  ARG D CD  1 
ATOM   3712  N NE  . ARG B  2 143 ? 63.754  -72.885 52.174  1.00 118.61 ? 143  ARG D NE  1 
ATOM   3713  C CZ  . ARG B  2 143 ? 64.841  -73.348 52.782  1.00 117.22 ? 143  ARG D CZ  1 
ATOM   3714  N NH1 . ARG B  2 143 ? 65.235  -72.822 53.932  1.00 116.09 ? 143  ARG D NH1 1 
ATOM   3715  N NH2 . ARG B  2 143 ? 65.539  -74.336 52.238  1.00 117.55 ? 143  ARG D NH2 1 
ATOM   3716  N N   . CYS B  2 144 ? 61.803  -68.396 48.473  1.00 129.87 ? 144  CYS D N   1 
ATOM   3717  C CA  . CYS B  2 144 ? 62.358  -67.438 47.537  1.00 132.28 ? 144  CYS D CA  1 
ATOM   3718  C C   . CYS B  2 144 ? 63.119  -66.317 48.246  1.00 132.12 ? 144  CYS D C   1 
ATOM   3719  O O   . CYS B  2 144 ? 62.566  -65.592 49.083  1.00 127.27 ? 144  CYS D O   1 
ATOM   3720  C CB  . CYS B  2 144 ? 61.267  -66.862 46.650  1.00 131.66 ? 144  CYS D CB  1 
ATOM   3721  S SG  . CYS B  2 144 ? 61.892  -66.121 45.135  1.00 133.86 ? 144  CYS D SG  1 
ATOM   3722  N N   . ASP B  2 145 ? 64.396  -66.197 47.894  1.00 134.59 ? 145  ASP D N   1 
ATOM   3723  C CA  . ASP B  2 145 ? 65.285  -65.177 48.434  1.00 134.89 ? 145  ASP D CA  1 
ATOM   3724  C C   . ASP B  2 145 ? 64.955  -63.800 47.855  1.00 133.90 ? 145  ASP D C   1 
ATOM   3725  O O   . ASP B  2 145 ? 63.832  -63.553 47.407  1.00 130.91 ? 145  ASP D O   1 
ATOM   3726  C CB  . ASP B  2 145 ? 66.754  -65.546 48.144  1.00 135.87 ? 145  ASP D CB  1 
ATOM   3727  C CG  . ASP B  2 145 ? 67.005  -65.909 46.669  1.00 134.20 ? 145  ASP D CG  1 
ATOM   3728  O OD1 . ASP B  2 145 ? 66.088  -66.440 46.003  1.00 130.70 ? 145  ASP D OD1 1 
ATOM   3729  O OD2 . ASP B  2 145 ? 68.131  -65.670 46.177  1.00 130.91 ? 145  ASP D OD2 1 
ATOM   3730  N N   . ASN B  2 146 ? 65.930  -62.897 47.890  1.00 133.52 ? 146  ASN D N   1 
ATOM   3731  C CA  . ASN B  2 146 ? 65.785  -61.597 47.248  1.00 132.23 ? 146  ASN D CA  1 
ATOM   3732  C C   . ASN B  2 146 ? 66.495  -61.534 45.888  1.00 133.60 ? 146  ASN D C   1 
ATOM   3733  O O   . ASN B  2 146 ? 67.157  -60.544 45.558  1.00 133.45 ? 146  ASN D O   1 
ATOM   3734  C CB  . ASN B  2 146 ? 66.291  -60.497 48.188  1.00 130.30 ? 146  ASN D CB  1 
ATOM   3735  C CG  . ASN B  2 146 ? 65.465  -60.398 49.472  1.00 126.24 ? 146  ASN D CG  1 
ATOM   3736  O OD1 . ASN B  2 146 ? 64.710  -61.314 49.815  1.00 125.04 ? 146  ASN D OD1 1 
ATOM   3737  N ND2 . ASN B  2 146 ? 65.603  -59.285 50.181  1.00 118.71 ? 146  ASN D ND2 1 
ATOM   3738  N N   . GLU B  2 147 ? 66.342  -62.606 45.111  1.00 134.08 ? 147  GLU D N   1 
ATOM   3739  C CA  . GLU B  2 147 ? 66.847  -62.687 43.739  1.00 134.45 ? 147  GLU D CA  1 
ATOM   3740  C C   . GLU B  2 147 ? 65.953  -63.643 42.931  1.00 133.39 ? 147  GLU D C   1 
ATOM   3741  O O   . GLU B  2 147 ? 66.056  -63.723 41.703  1.00 128.40 ? 147  GLU D O   1 
ATOM   3742  C CB  . GLU B  2 147 ? 68.318  -63.137 43.712  1.00 136.85 ? 147  GLU D CB  1 
ATOM   3743  C CG  . GLU B  2 147 ? 69.049  -62.872 42.383  1.00 138.12 ? 147  GLU D CG  1 
ATOM   3744  C CD  . GLU B  2 147 ? 70.531  -63.242 42.426  1.00 137.29 ? 147  GLU D CD  1 
ATOM   3745  O OE1 . GLU B  2 147 ? 71.014  -63.640 43.508  1.00 131.92 ? 147  GLU D OE1 1 
ATOM   3746  O OE2 . GLU B  2 147 ? 71.212  -63.130 41.379  1.00 134.85 ? 147  GLU D OE2 1 
ATOM   3747  N N   . CYS B  2 148 ? 65.092  -64.376 43.643  1.00 134.32 ? 148  CYS D N   1 
ATOM   3748  C CA  . CYS B  2 148 ? 64.027  -65.185 43.037  1.00 133.48 ? 148  CYS D CA  1 
ATOM   3749  C C   . CYS B  2 148 ? 62.818  -64.309 42.675  1.00 132.73 ? 148  CYS D C   1 
ATOM   3750  O O   . CYS B  2 148 ? 62.329  -64.339 41.537  1.00 128.05 ? 148  CYS D O   1 
ATOM   3751  C CB  . CYS B  2 148 ? 63.606  -66.315 43.990  1.00 132.61 ? 148  CYS D CB  1 
ATOM   3752  S SG  . CYS B  2 148 ? 62.152  -67.293 43.493  1.00 128.93 ? 148  CYS D SG  1 
ATOM   3753  N N   . MET B  2 149 ? 62.332  -63.554 43.666  1.00 134.41 ? 149  MET D N   1 
ATOM   3754  C CA  . MET B  2 149 ? 61.277  -62.554 43.472  1.00 129.40 ? 149  MET D CA  1 
ATOM   3755  C C   . MET B  2 149 ? 61.636  -61.669 42.286  1.00 126.95 ? 149  MET D C   1 
ATOM   3756  O O   . MET B  2 149 ? 60.785  -61.277 41.493  1.00 125.20 ? 149  MET D O   1 
ATOM   3757  C CB  . MET B  2 149 ? 61.076  -61.708 44.736  1.00 119.44 ? 149  MET D CB  1 
ATOM   3758  C CG  . MET B  2 149 ? 60.677  -62.487 45.991  1.00 120.56 ? 149  MET D CG  1 
ATOM   3759  S SD  . MET B  2 149 ? 59.060  -63.298 45.873  1.00 121.52 ? 149  MET D SD  1 
ATOM   3760  C CE  . MET B  2 149 ? 58.637  -63.579 47.590  1.00 111.64 ? 149  MET D CE  1 
ATOM   3761  N N   . GLU B  2 150 ? 62.922  -61.368 42.179  1.00 127.70 ? 150  GLU D N   1 
ATOM   3762  C CA  . GLU B  2 150 ? 63.441  -60.571 41.090  1.00 129.05 ? 150  GLU D CA  1 
ATOM   3763  C C   . GLU B  2 150 ? 63.284  -61.282 39.728  1.00 130.54 ? 150  GLU D C   1 
ATOM   3764  O O   . GLU B  2 150 ? 63.033  -60.631 38.711  1.00 130.43 ? 150  GLU D O   1 
ATOM   3765  C CB  . GLU B  2 150 ? 64.912  -60.239 41.370  1.00 130.58 ? 150  GLU D CB  1 
ATOM   3766  C CG  . GLU B  2 150 ? 65.564  -59.334 40.348  1.00 129.14 ? 150  GLU D CG  1 
ATOM   3767  C CD  . GLU B  2 150 ? 64.898  -57.977 40.247  1.00 131.58 ? 150  GLU D CD  1 
ATOM   3768  O OE1 . GLU B  2 150 ? 64.154  -57.591 41.182  1.00 131.60 ? 150  GLU D OE1 1 
ATOM   3769  O OE2 . GLU B  2 150 ? 65.113  -57.305 39.214  1.00 134.48 ? 150  GLU D OE2 1 
ATOM   3770  N N   . SER B  2 151 ? 63.424  -62.608 39.705  1.00 130.43 ? 151  SER D N   1 
ATOM   3771  C CA  . SER B  2 151 ? 63.363  -63.355 38.445  1.00 126.49 ? 151  SER D CA  1 
ATOM   3772  C C   . SER B  2 151 ? 61.961  -63.396 37.842  1.00 126.10 ? 151  SER D C   1 
ATOM   3773  O O   . SER B  2 151 ? 61.815  -63.581 36.639  1.00 127.52 ? 151  SER D O   1 
ATOM   3774  C CB  . SER B  2 151 ? 63.873  -64.789 38.629  1.00 124.05 ? 151  SER D CB  1 
ATOM   3775  O OG  . SER B  2 151 ? 62.860  -65.636 39.135  1.00 121.00 ? 151  SER D OG  1 
ATOM   3776  N N   . VAL B  2 152 ? 60.933  -63.240 38.672  1.00 127.05 ? 152  VAL D N   1 
ATOM   3777  C CA  . VAL B  2 152 ? 59.561  -63.253 38.160  1.00 126.99 ? 152  VAL D CA  1 
ATOM   3778  C C   . VAL B  2 152 ? 59.188  -61.867 37.629  1.00 128.80 ? 152  VAL D C   1 
ATOM   3779  O O   . VAL B  2 152 ? 58.441  -61.744 36.653  1.00 126.44 ? 152  VAL D O   1 
ATOM   3780  C CB  . VAL B  2 152 ? 58.526  -63.701 39.232  1.00 125.82 ? 152  VAL D CB  1 
ATOM   3781  C CG1 . VAL B  2 152 ? 58.943  -65.029 39.840  1.00 125.33 ? 152  VAL D CG1 1 
ATOM   3782  C CG2 . VAL B  2 152 ? 58.367  -62.668 40.332  1.00 121.92 ? 152  VAL D CG2 1 
ATOM   3783  N N   . ARG B  2 153 ? 59.722  -60.833 38.279  1.00 128.01 ? 153  ARG D N   1 
ATOM   3784  C CA  . ARG B  2 153 ? 59.446  -59.442 37.940  1.00 122.44 ? 153  ARG D CA  1 
ATOM   3785  C C   . ARG B  2 153 ? 60.127  -59.031 36.636  1.00 128.66 ? 153  ARG D C   1 
ATOM   3786  O O   . ARG B  2 153 ? 59.672  -58.100 35.962  1.00 132.18 ? 153  ARG D O   1 
ATOM   3787  C CB  . ARG B  2 153 ? 59.883  -58.532 39.089  1.00 113.74 ? 153  ARG D CB  1 
ATOM   3788  C CG  . ARG B  2 153 ? 58.965  -58.631 40.285  1.00 109.74 ? 153  ARG D CG  1 
ATOM   3789  C CD  . ARG B  2 153 ? 59.375  -57.722 41.424  1.00 108.82 ? 153  ARG D CD  1 
ATOM   3790  N NE  . ARG B  2 153 ? 60.548  -58.230 42.130  1.00 116.95 ? 153  ARG D NE  1 
ATOM   3791  C CZ  . ARG B  2 153 ? 60.713  -58.163 43.448  1.00 117.00 ? 153  ARG D CZ  1 
ATOM   3792  N NH1 . ARG B  2 153 ? 59.764  -57.634 44.211  1.00 115.37 ? 153  ARG D NH1 1 
ATOM   3793  N NH2 . ARG B  2 153 ? 61.814  -58.651 44.006  1.00 115.00 ? 153  ARG D NH2 1 
ATOM   3794  N N   . ASN B  2 154 ? 61.203  -59.734 36.276  1.00 127.37 ? 154  ASN D N   1 
ATOM   3795  C CA  . ASN B  2 154 ? 61.859  -59.502 34.991  1.00 128.63 ? 154  ASN D CA  1 
ATOM   3796  C C   . ASN B  2 154 ? 61.530  -60.624 34.017  1.00 128.12 ? 154  ASN D C   1 
ATOM   3797  O O   . ASN B  2 154 ? 62.082  -60.690 32.918  1.00 126.70 ? 154  ASN D O   1 
ATOM   3798  C CB  . ASN B  2 154 ? 63.387  -59.354 35.149  1.00 130.27 ? 154  ASN D CB  1 
ATOM   3799  C CG  . ASN B  2 154 ? 64.036  -60.512 35.907  1.00 131.18 ? 154  ASN D CG  1 
ATOM   3800  O OD1 . ASN B  2 154 ? 63.997  -61.663 35.473  1.00 132.52 ? 154  ASN D OD1 1 
ATOM   3801  N ND2 . ASN B  2 154 ? 64.684  -60.193 37.022  1.00 127.82 ? 154  ASN D ND2 1 
ATOM   3802  N N   . GLY B  2 155 ? 60.603  -61.487 34.428  1.00 129.24 ? 155  GLY D N   1 
ATOM   3803  C CA  . GLY B  2 155 ? 60.075  -62.541 33.577  1.00 131.36 ? 155  GLY D CA  1 
ATOM   3804  C C   . GLY B  2 155 ? 61.069  -63.573 33.067  1.00 135.78 ? 155  GLY D C   1 
ATOM   3805  O O   . GLY B  2 155 ? 61.076  -63.884 31.871  1.00 135.70 ? 155  GLY D O   1 
ATOM   3806  N N   . THR B  2 156 ? 61.882  -64.129 33.967  1.00 135.84 ? 156  THR D N   1 
ATOM   3807  C CA  . THR B  2 156 ? 62.880  -65.133 33.586  1.00 134.48 ? 156  THR D CA  1 
ATOM   3808  C C   . THR B  2 156 ? 62.722  -66.442 34.366  1.00 132.78 ? 156  THR D C   1 
ATOM   3809  O O   . THR B  2 156 ? 63.338  -67.454 34.019  1.00 133.64 ? 156  THR D O   1 
ATOM   3810  C CB  . THR B  2 156 ? 64.322  -64.607 33.813  1.00 131.07 ? 156  THR D CB  1 
ATOM   3811  O OG1 . THR B  2 156 ? 64.416  -64.001 35.109  1.00 128.01 ? 156  THR D OG1 1 
ATOM   3812  C CG2 . THR B  2 156 ? 64.715  -63.595 32.736  1.00 129.83 ? 156  THR D CG2 1 
ATOM   3813  N N   . TYR B  2 157 ? 61.890  -66.399 35.406  1.00 130.88 ? 157  TYR D N   1 
ATOM   3814  C CA  . TYR B  2 157 ? 61.609  -67.527 36.299  1.00 128.80 ? 157  TYR D CA  1 
ATOM   3815  C C   . TYR B  2 157 ? 61.531  -68.882 35.582  1.00 131.68 ? 157  TYR D C   1 
ATOM   3816  O O   . TYR B  2 157 ? 60.585  -69.150 34.834  1.00 128.85 ? 157  TYR D O   1 
ATOM   3817  C CB  . TYR B  2 157 ? 60.301  -67.245 37.056  1.00 125.48 ? 157  TYR D CB  1 
ATOM   3818  C CG  . TYR B  2 157 ? 59.837  -68.315 38.028  1.00 123.99 ? 157  TYR D CG  1 
ATOM   3819  C CD1 . TYR B  2 157 ? 58.999  -69.348 37.616  1.00 122.23 ? 157  TYR D CD1 1 
ATOM   3820  C CD2 . TYR B  2 157 ? 60.208  -68.268 39.370  1.00 122.98 ? 157  TYR D CD2 1 
ATOM   3821  C CE1 . TYR B  2 157 ? 58.566  -70.317 38.509  1.00 122.34 ? 157  TYR D CE1 1 
ATOM   3822  C CE2 . TYR B  2 157 ? 59.776  -69.228 40.269  1.00 121.36 ? 157  TYR D CE2 1 
ATOM   3823  C CZ  . TYR B  2 157 ? 58.957  -70.250 39.832  1.00 120.51 ? 157  TYR D CZ  1 
ATOM   3824  O OH  . TYR B  2 157 ? 58.529  -71.207 40.720  1.00 120.78 ? 157  TYR D OH  1 
ATOM   3825  N N   . ASP B  2 158 ? 62.544  -69.720 35.810  1.00 132.96 ? 158  ASP D N   1 
ATOM   3826  C CA  . ASP B  2 158 ? 62.609  -71.064 35.231  1.00 133.31 ? 158  ASP D CA  1 
ATOM   3827  C C   . ASP B  2 158 ? 61.753  -72.005 36.078  1.00 133.08 ? 158  ASP D C   1 
ATOM   3828  O O   . ASP B  2 158 ? 62.102  -72.306 37.225  1.00 132.44 ? 158  ASP D O   1 
ATOM   3829  C CB  . ASP B  2 158 ? 64.053  -71.576 35.147  1.00 131.11 ? 158  ASP D CB  1 
ATOM   3830  C CG  . ASP B  2 158 ? 64.211  -72.737 34.165  1.00 131.43 ? 158  ASP D CG  1 
ATOM   3831  O OD1 . ASP B  2 158 ? 63.202  -73.390 33.829  1.00 128.66 ? 158  ASP D OD1 1 
ATOM   3832  O OD2 . ASP B  2 158 ? 65.352  -73.002 33.733  1.00 134.06 ? 158  ASP D OD2 1 
ATOM   3833  N N   . TYR B  2 159 ? 60.643  -72.471 35.509  1.00 129.90 ? 159  TYR D N   1 
ATOM   3834  C CA  . TYR B  2 159 ? 59.644  -73.235 36.257  1.00 128.78 ? 159  TYR D CA  1 
ATOM   3835  C C   . TYR B  2 159 ? 60.168  -74.557 36.854  1.00 129.72 ? 159  TYR D C   1 
ATOM   3836  O O   . TYR B  2 159 ? 60.003  -74.771 38.063  1.00 127.09 ? 159  TYR D O   1 
ATOM   3837  C CB  . TYR B  2 159 ? 58.416  -73.478 35.361  1.00 122.91 ? 159  TYR D CB  1 
ATOM   3838  C CG  . TYR B  2 159 ? 57.487  -74.582 35.822  1.00 120.42 ? 159  TYR D CG  1 
ATOM   3839  C CD1 . TYR B  2 159 ? 56.668  -74.420 36.930  1.00 116.89 ? 159  TYR D CD1 1 
ATOM   3840  C CD2 . TYR B  2 159 ? 57.405  -75.777 35.112  1.00 116.27 ? 159  TYR D CD2 1 
ATOM   3841  C CE1 . TYR B  2 159 ? 55.820  -75.431 37.334  1.00 114.76 ? 159  TYR D CE1 1 
ATOM   3842  C CE2 . TYR B  2 159 ? 56.560  -76.785 35.502  1.00 109.78 ? 159  TYR D CE2 1 
ATOM   3843  C CZ  . TYR B  2 159 ? 55.771  -76.610 36.611  1.00 114.71 ? 159  TYR D CZ  1 
ATOM   3844  O OH  . TYR B  2 159 ? 54.929  -77.624 36.996  1.00 119.60 ? 159  TYR D OH  1 
ATOM   3845  N N   . PRO B  2 160 ? 60.782  -75.446 36.037  1.00 131.86 ? 160  PRO D N   1 
ATOM   3846  C CA  . PRO B  2 160 ? 61.220  -76.723 36.627  1.00 132.24 ? 160  PRO D CA  1 
ATOM   3847  C C   . PRO B  2 160 ? 62.313  -76.600 37.707  1.00 131.59 ? 160  PRO D C   1 
ATOM   3848  O O   . PRO B  2 160 ? 62.460  -77.522 38.511  1.00 131.05 ? 160  PRO D O   1 
ATOM   3849  C CB  . PRO B  2 160 ? 61.758  -77.502 35.415  1.00 127.61 ? 160  PRO D CB  1 
ATOM   3850  C CG  . PRO B  2 160 ? 61.106  -76.877 34.236  1.00 124.38 ? 160  PRO D CG  1 
ATOM   3851  C CD  . PRO B  2 160 ? 61.029  -75.425 34.582  1.00 127.88 ? 160  PRO D CD  1 
ATOM   3852  N N   . GLN B  2 161 ? 63.042  -75.483 37.732  1.00 130.47 ? 161  GLN D N   1 
ATOM   3853  C CA  . GLN B  2 161 ? 64.166  -75.280 38.655  1.00 127.81 ? 161  GLN D CA  1 
ATOM   3854  C C   . GLN B  2 161 ? 63.708  -75.154 40.120  1.00 127.24 ? 161  GLN D C   1 
ATOM   3855  O O   . GLN B  2 161 ? 64.524  -75.132 41.045  1.00 125.91 ? 161  GLN D O   1 
ATOM   3856  C CB  . GLN B  2 161 ? 64.975  -74.049 38.214  1.00 130.70 ? 161  GLN D CB  1 
ATOM   3857  C CG  . GLN B  2 161 ? 66.302  -73.825 38.944  1.00 132.22 ? 161  GLN D CG  1 
ATOM   3858  C CD  . GLN B  2 161 ? 67.058  -72.604 38.434  1.00 133.99 ? 161  GLN D CD  1 
ATOM   3859  O OE1 . GLN B  2 161 ? 66.770  -72.087 37.354  1.00 134.73 ? 161  GLN D OE1 1 
ATOM   3860  N NE2 . GLN B  2 161 ? 68.033  -72.140 39.214  1.00 129.85 ? 161  GLN D NE2 1 
ATOM   3861  N N   . TYR B  2 162 ? 62.394  -75.087 40.318  1.00 129.07 ? 162  TYR D N   1 
ATOM   3862  C CA  . TYR B  2 162 ? 61.788  -75.001 41.649  1.00 132.03 ? 162  TYR D CA  1 
ATOM   3863  C C   . TYR B  2 162 ? 60.624  -75.989 41.793  1.00 129.35 ? 162  TYR D C   1 
ATOM   3864  O O   . TYR B  2 162 ? 59.958  -76.037 42.834  1.00 124.11 ? 162  TYR D O   1 
ATOM   3865  C CB  . TYR B  2 162 ? 61.320  -73.567 41.937  1.00 131.91 ? 162  TYR D CB  1 
ATOM   3866  C CG  . TYR B  2 162 ? 62.442  -72.548 42.013  1.00 131.22 ? 162  TYR D CG  1 
ATOM   3867  C CD1 . TYR B  2 162 ? 63.113  -72.324 43.214  1.00 128.17 ? 162  TYR D CD1 1 
ATOM   3868  C CD2 . TYR B  2 162 ? 62.850  -71.835 40.890  1.00 129.01 ? 162  TYR D CD2 1 
ATOM   3869  C CE1 . TYR B  2 162 ? 64.136  -71.407 43.302  1.00 125.54 ? 162  TYR D CE1 1 
ATOM   3870  C CE2 . TYR B  2 162 ? 63.882  -70.914 40.969  1.00 127.63 ? 162  TYR D CE2 1 
ATOM   3871  C CZ  . TYR B  2 162 ? 64.520  -70.708 42.180  1.00 125.68 ? 162  TYR D CZ  1 
ATOM   3872  O OH  . TYR B  2 162 ? 65.545  -69.799 42.275  1.00 125.09 ? 162  TYR D OH  1 
ATOM   3873  N N   . SER B  2 163 ? 60.400  -76.773 40.737  1.00 129.94 ? 163  SER D N   1 
ATOM   3874  C CA  . SER B  2 163 ? 59.295  -77.731 40.665  1.00 129.09 ? 163  SER D CA  1 
ATOM   3875  C C   . SER B  2 163 ? 59.400  -78.829 41.720  1.00 128.09 ? 163  SER D C   1 
ATOM   3876  O O   . SER B  2 163 ? 58.384  -79.333 42.194  1.00 123.66 ? 163  SER D O   1 
ATOM   3877  C CB  . SER B  2 163 ? 59.221  -78.378 39.274  1.00 127.04 ? 163  SER D CB  1 
ATOM   3878  O OG  . SER B  2 163 ? 60.474  -78.904 38.869  1.00 126.00 ? 163  SER D OG  1 
ATOM   3879  N N   . GLU B  2 164 ? 60.634  -79.200 42.065  1.00 131.09 ? 164  GLU D N   1 
ATOM   3880  C CA  . GLU B  2 164 ? 60.892  -80.335 42.948  1.00 127.48 ? 164  GLU D CA  1 
ATOM   3881  C C   . GLU B  2 164 ? 60.573  -80.036 44.415  1.00 125.22 ? 164  GLU D C   1 
ATOM   3882  O O   . GLU B  2 164 ? 59.795  -80.763 45.021  1.00 124.18 ? 164  GLU D O   1 
ATOM   3883  C CB  . GLU B  2 164 ? 62.353  -80.805 42.814  1.00 127.94 ? 164  GLU D CB  1 
ATOM   3884  C CG  . GLU B  2 164 ? 63.435  -79.784 43.201  1.00 131.22 ? 164  GLU D CG  1 
ATOM   3885  C CD  . GLU B  2 164 ? 63.498  -78.580 42.281  1.00 128.82 ? 164  GLU D CD  1 
ATOM   3886  O OE1 . GLU B  2 164 ? 63.105  -78.714 41.103  1.00 128.85 ? 164  GLU D OE1 1 
ATOM   3887  O OE2 . GLU B  2 164 ? 63.921  -77.498 42.747  1.00 128.49 ? 164  GLU D OE2 1 
ATOM   3888  N N   . GLU B  2 165 ? 61.165  -78.984 44.983  1.00 125.83 ? 165  GLU D N   1 
ATOM   3889  C CA  . GLU B  2 165 ? 60.886  -78.588 46.366  1.00 127.00 ? 165  GLU D CA  1 
ATOM   3890  C C   . GLU B  2 165 ? 59.389  -78.352 46.541  1.00 128.94 ? 165  GLU D C   1 
ATOM   3891  O O   . GLU B  2 165 ? 58.810  -78.621 47.602  1.00 125.36 ? 165  GLU D O   1 
ATOM   3892  C CB  . GLU B  2 165 ? 61.675  -77.346 46.768  1.00 123.69 ? 165  GLU D CB  1 
ATOM   3893  C CG  . GLU B  2 165 ? 61.346  -76.876 48.176  1.00 120.12 ? 165  GLU D CG  1 
ATOM   3894  C CD  . GLU B  2 165 ? 62.142  -75.662 48.584  1.00 119.53 ? 165  GLU D CD  1 
ATOM   3895  O OE1 . GLU B  2 165 ? 62.993  -75.220 47.786  1.00 120.93 ? 165  GLU D OE1 1 
ATOM   3896  O OE2 . GLU B  2 165 ? 61.920  -75.150 49.703  1.00 118.28 ? 165  GLU D OE2 1 
ATOM   3897  N N   . ALA B  2 166 ? 58.794  -77.783 45.495  1.00 132.06 ? 166  ALA D N   1 
ATOM   3898  C CA  . ALA B  2 166 ? 57.353  -77.571 45.416  1.00 131.29 ? 166  ALA D CA  1 
ATOM   3899  C C   . ALA B  2 166 ? 56.618  -78.919 45.365  1.00 129.29 ? 166  ALA D C   1 
ATOM   3900  O O   . ALA B  2 166 ? 55.646  -79.129 46.098  1.00 125.68 ? 166  ALA D O   1 
ATOM   3901  C CB  . ALA B  2 166 ? 57.009  -76.719 44.197  1.00 128.59 ? 166  ALA D CB  1 
ATOM   3902  N N   . ARG B  2 167 ? 57.094  -79.817 44.497  1.00 128.30 ? 167  ARG D N   1 
ATOM   3903  C CA  . ARG B  2 167 ? 56.507  -81.147 44.311  1.00 125.54 ? 167  ARG D CA  1 
ATOM   3904  C C   . ARG B  2 167 ? 56.449  -81.874 45.645  1.00 125.88 ? 167  ARG D C   1 
ATOM   3905  O O   . ARG B  2 167 ? 55.455  -82.528 45.965  1.00 123.45 ? 167  ARG D O   1 
ATOM   3906  C CB  . ARG B  2 167 ? 57.339  -81.966 43.325  1.00 126.22 ? 167  ARG D CB  1 
ATOM   3907  C CG  . ARG B  2 167 ? 56.814  -83.354 42.976  1.00 127.80 ? 167  ARG D CG  1 
ATOM   3908  C CD  . ARG B  2 167 ? 57.801  -83.991 42.006  1.00 130.89 ? 167  ARG D CD  1 
ATOM   3909  N NE  . ARG B  2 167 ? 59.075  -84.212 42.695  1.00 134.91 ? 167  ARG D NE  1 
ATOM   3910  C CZ  . ARG B  2 167 ? 60.276  -84.152 42.123  1.00 134.42 ? 167  ARG D CZ  1 
ATOM   3911  N NH1 . ARG B  2 167 ? 60.391  -83.850 40.836  1.00 133.94 ? 167  ARG D NH1 1 
ATOM   3912  N NH2 . ARG B  2 167 ? 61.369  -84.366 42.850  1.00 129.95 ? 167  ARG D NH2 1 
ATOM   3913  N N   . LEU B  2 168 ? 57.529  -81.743 46.418  1.00 126.30 ? 168  LEU D N   1 
ATOM   3914  C CA  . LEU B  2 168 ? 57.592  -82.305 47.762  1.00 127.81 ? 168  LEU D CA  1 
ATOM   3915  C C   . LEU B  2 168 ? 56.521  -81.693 48.659  1.00 129.85 ? 168  LEU D C   1 
ATOM   3916  O O   . LEU B  2 168 ? 55.775  -82.420 49.313  1.00 128.65 ? 168  LEU D O   1 
ATOM   3917  C CB  . LEU B  2 168 ? 58.978  -82.077 48.399  1.00 127.70 ? 168  LEU D CB  1 
ATOM   3918  C CG  . LEU B  2 168 ? 60.207  -82.973 48.177  1.00 126.40 ? 168  LEU D CG  1 
ATOM   3919  C CD1 . LEU B  2 168 ? 60.584  -83.132 46.713  1.00 125.33 ? 168  LEU D CD1 1 
ATOM   3920  C CD2 . LEU B  2 168 ? 61.401  -82.432 48.976  1.00 119.72 ? 168  LEU D CD2 1 
ATOM   3921  N N   . LYS B  2 169 ? 56.428  -80.361 48.652  1.00 129.03 ? 169  LYS D N   1 
ATOM   3922  C CA  . LYS B  2 169 ? 55.538  -79.640 49.566  1.00 125.84 ? 169  LYS D CA  1 
ATOM   3923  C C   . LYS B  2 169 ? 54.044  -79.884 49.325  1.00 125.94 ? 169  LYS D C   1 
ATOM   3924  O O   . LYS B  2 169 ? 53.274  -79.981 50.283  1.00 125.07 ? 169  LYS D O   1 
ATOM   3925  C CB  . LYS B  2 169 ? 55.828  -78.137 49.518  1.00 119.63 ? 169  LYS D CB  1 
ATOM   3926  C CG  . LYS B  2 169 ? 54.900  -77.322 50.416  1.00 119.18 ? 169  LYS D CG  1 
ATOM   3927  C CD  . LYS B  2 169 ? 55.022  -77.717 51.887  1.00 117.19 ? 169  LYS D CD  1 
ATOM   3928  C CE  . LYS B  2 169 ? 54.262  -76.755 52.793  1.00 114.15 ? 169  LYS D CE  1 
ATOM   3929  N NZ  . LYS B  2 169 ? 54.280  -77.178 54.220  1.00 113.66 ? 169  LYS D NZ  1 
ATOM   3930  N N   . ARG B  2 170 ? 53.624  -79.976 48.066  1.00 122.93 ? 170  ARG D N   1 
ATOM   3931  C CA  . ARG B  2 170 ? 52.206  -80.187 47.783  1.00 121.60 ? 170  ARG D CA  1 
ATOM   3932  C C   . ARG B  2 170 ? 51.798  -81.632 48.080  1.00 125.72 ? 170  ARG D C   1 
ATOM   3933  O O   . ARG B  2 170 ? 50.624  -81.919 48.332  1.00 124.64 ? 170  ARG D O   1 
ATOM   3934  C CB  . ARG B  2 170 ? 51.857  -79.775 46.345  1.00 120.07 ? 170  ARG D CB  1 
ATOM   3935  C CG  . ARG B  2 170 ? 52.815  -80.178 45.236  1.00 119.59 ? 170  ARG D CG  1 
ATOM   3936  C CD  . ARG B  2 170 ? 52.532  -79.277 44.034  1.00 110.83 ? 170  ARG D CD  1 
ATOM   3937  N NE  . ARG B  2 170 ? 53.369  -79.533 42.868  1.00 109.47 ? 170  ARG D NE  1 
ATOM   3938  C CZ  . ARG B  2 170 ? 52.952  -80.181 41.784  1.00 112.99 ? 170  ARG D CZ  1 
ATOM   3939  N NH1 . ARG B  2 170 ? 51.706  -80.633 41.717  1.00 111.13 ? 170  ARG D NH1 1 
ATOM   3940  N NH2 . ARG B  2 170 ? 53.774  -80.366 40.759  1.00 113.54 ? 170  ARG D NH2 1 
ATOM   3941  N N   . GLU B  2 171 ? 52.766  -82.543 48.041  1.00 128.41 ? 171  GLU D N   1 
ATOM   3942  C CA  . GLU B  2 171 ? 52.524  -83.906 48.501  1.00 127.76 ? 171  GLU D CA  1 
ATOM   3943  C C   . GLU B  2 171 ? 52.403  -83.947 50.036  1.00 131.39 ? 171  GLU D C   1 
ATOM   3944  O O   . GLU B  2 171 ? 51.647  -84.749 50.578  1.00 134.29 ? 171  GLU D O   1 
ATOM   3945  C CB  . GLU B  2 171 ? 53.634  -84.850 48.028  1.00 125.13 ? 171  GLU D CB  1 
ATOM   3946  C CG  . GLU B  2 171 ? 53.697  -85.038 46.515  1.00 129.16 ? 171  GLU D CG  1 
ATOM   3947  C CD  . GLU B  2 171 ? 52.370  -85.459 45.906  1.00 127.85 ? 171  GLU D CD  1 
ATOM   3948  O OE1 . GLU B  2 171 ? 51.622  -86.223 46.556  1.00 127.10 ? 171  GLU D OE1 1 
ATOM   3949  O OE2 . GLU B  2 171 ? 52.081  -85.022 44.770  1.00 122.41 ? 171  GLU D OE2 1 
ATOM   3950  N N   . GLU B  2 172 ? 53.153  -83.083 50.725  1.00 131.18 ? 172  GLU D N   1 
ATOM   3951  C CA  . GLU B  2 172 ? 53.100  -82.956 52.192  1.00 126.64 ? 172  GLU D CA  1 
ATOM   3952  C C   . GLU B  2 172 ? 51.737  -82.444 52.677  1.00 126.00 ? 172  GLU D C   1 
ATOM   3953  O O   . GLU B  2 172 ? 51.290  -82.788 53.775  1.00 122.04 ? 172  GLU D O   1 
ATOM   3954  C CB  . GLU B  2 172 ? 54.227  -82.041 52.680  1.00 127.92 ? 172  GLU D CB  1 
ATOM   3955  C CG  . GLU B  2 172 ? 55.615  -82.546 52.286  1.00 130.21 ? 172  GLU D CG  1 
ATOM   3956  C CD  . GLU B  2 172 ? 56.722  -81.546 52.569  1.00 130.76 ? 172  GLU D CD  1 
ATOM   3957  O OE1 . GLU B  2 172 ? 56.421  -80.468 53.127  1.00 133.42 ? 172  GLU D OE1 1 
ATOM   3958  O OE2 . GLU B  2 172 ? 57.884  -81.820 52.189  1.00 127.04 ? 172  GLU D OE2 1 
ATOM   3959  N N   . ILE B  2 173 ? 51.101  -81.603 51.860  1.00 128.96 ? 173  ILE D N   1 
ATOM   3960  C CA  . ILE B  2 173 ? 49.737  -81.127 52.112  1.00 129.38 ? 173  ILE D CA  1 
ATOM   3961  C C   . ILE B  2 173 ? 48.787  -82.264 51.726  1.00 129.17 ? 173  ILE D C   1 
ATOM   3962  O O   . ILE B  2 173 ? 47.710  -82.433 52.315  1.00 127.62 ? 173  ILE D O   1 
ATOM   3963  C CB  . ILE B  2 173 ? 49.405  -79.814 51.340  1.00 123.63 ? 173  ILE D CB  1 
ATOM   3964  C CG1 . ILE B  2 173 ? 50.087  -78.618 52.009  1.00 119.19 ? 173  ILE D CG1 1 
ATOM   3965  C CG2 . ILE B  2 173 ? 47.915  -79.523 51.370  1.00 118.96 ? 173  ILE D CG2 1 
ATOM   3966  C CD1 . ILE B  2 173 ? 51.150  -77.950 51.180  1.00 115.71 ? 173  ILE D CD1 1 
ATOM   3967  N N   . SER B  2 174 ? 49.222  -83.079 50.767  1.00 128.23 ? 174  SER D N   1 
ATOM   3968  C CA  . SER B  2 174 ? 48.436  -84.219 50.312  1.00 129.60 ? 174  SER D CA  1 
ATOM   3969  C C   . SER B  2 174 ? 48.740  -85.411 51.226  1.00 131.69 ? 174  SER D C   1 
ATOM   3970  O O   . SER B  2 174 ? 48.712  -86.569 50.800  1.00 130.04 ? 174  SER D O   1 
ATOM   3971  C CB  . SER B  2 174 ? 48.760  -84.554 48.850  1.00 122.49 ? 174  SER D CB  1 
ATOM   3972  O OG  . SER B  2 174 ? 47.854  -85.505 48.316  1.00 120.95 ? 174  SER D OG  1 
ATOM   3973  N N   . GLY B  2 175 ? 49.023  -85.100 52.493  1.00 128.05 ? 175  GLY D N   1 
ATOM   3974  C CA  . GLY B  2 175 ? 49.310  -86.090 53.514  1.00 123.03 ? 175  GLY D CA  1 
ATOM   3975  C C   . GLY B  2 175 ? 48.522  -85.815 54.783  1.00 124.87 ? 175  GLY D C   1 
ATOM   3976  O O   . GLY B  2 175 ? 47.779  -84.835 54.872  1.00 123.16 ? 175  GLY D O   1 
ATOM   3977  N N   . ASP C  1 2   ? 58.110  -88.870 26.811  1.00 125.20 ? 8    ASP A N   1 
ATOM   3978  C CA  . ASP C  1 2   ? 58.305  -87.897 25.735  1.00 128.16 ? 8    ASP A CA  1 
ATOM   3979  C C   . ASP C  1 2   ? 57.249  -86.794 25.766  1.00 126.61 ? 8    ASP A C   1 
ATOM   3980  O O   . ASP C  1 2   ? 56.203  -86.948 26.406  1.00 124.46 ? 8    ASP A O   1 
ATOM   3981  C CB  . ASP C  1 2   ? 58.264  -88.576 24.356  1.00 122.32 ? 8    ASP A CB  1 
ATOM   3982  C CG  . ASP C  1 2   ? 59.075  -89.849 24.302  1.00 123.57 ? 8    ASP A CG  1 
ATOM   3983  O OD1 . ASP C  1 2   ? 58.843  -90.733 25.159  1.00 125.19 ? 8    ASP A OD1 1 
ATOM   3984  O OD2 . ASP C  1 2   ? 59.939  -89.956 23.401  1.00 117.12 ? 8    ASP A OD2 1 
ATOM   3985  N N   . PRO C  1 3   ? 57.534  -85.668 25.084  1.00 126.68 ? 9    PRO A N   1 
ATOM   3986  C CA  . PRO C  1 3   ? 56.507  -84.683 24.734  1.00 117.28 ? 9    PRO A CA  1 
ATOM   3987  C C   . PRO C  1 3   ? 55.316  -85.371 24.077  1.00 115.04 ? 9    PRO A C   1 
ATOM   3988  O O   . PRO C  1 3   ? 55.516  -86.202 23.187  1.00 111.83 ? 9    PRO A O   1 
ATOM   3989  C CB  . PRO C  1 3   ? 57.218  -83.760 23.739  1.00 111.80 ? 9    PRO A CB  1 
ATOM   3990  C CG  . PRO C  1 3   ? 58.685  -83.927 24.007  1.00 116.53 ? 9    PRO A CG  1 
ATOM   3991  C CD  . PRO C  1 3   ? 58.890  -85.110 24.927  1.00 123.83 ? 9    PRO A CD  1 
ATOM   3992  N N   . GLY C  1 4   ? 54.100  -85.054 24.507  1.00 109.48 ? 10   GLY A N   1 
ATOM   3993  C CA  . GLY C  1 4   ? 52.949  -85.628 23.850  1.00 103.75 ? 10   GLY A CA  1 
ATOM   3994  C C   . GLY C  1 4   ? 52.519  -84.694 22.739  1.00 105.03 ? 10   GLY A C   1 
ATOM   3995  O O   . GLY C  1 4   ? 53.337  -83.963 22.178  1.00 100.24 ? 10   GLY A O   1 
ATOM   3996  N N   . ASP C  1 5   ? 51.226  -84.675 22.459  1.00 107.09 ? 11   ASP A N   1 
ATOM   3997  C CA  . ASP C  1 5   ? 50.694  -83.851 21.383  1.00 105.74 ? 11   ASP A CA  1 
ATOM   3998  C C   . ASP C  1 5   ? 50.390  -82.427 21.829  1.00 105.74 ? 11   ASP A C   1 
ATOM   3999  O O   . ASP C  1 5   ? 50.180  -82.158 23.019  1.00 103.41 ? 11   ASP A O   1 
ATOM   4000  C CB  . ASP C  1 5   ? 49.444  -84.501 20.782  1.00 104.14 ? 11   ASP A CB  1 
ATOM   4001  C CG  . ASP C  1 5   ? 49.730  -85.871 20.214  1.00 100.90 ? 11   ASP A CG  1 
ATOM   4002  O OD1 . ASP C  1 5   ? 50.844  -86.391 20.447  1.00 96.32  ? 11   ASP A OD1 1 
ATOM   4003  O OD2 . ASP C  1 5   ? 48.849  -86.414 19.527  1.00 96.51  ? 11   ASP A OD2 1 
ATOM   4004  N N   . GLN C  1 6   ? 50.431  -81.509 20.867  1.00 103.81 ? 12   GLN A N   1 
ATOM   4005  C CA  . GLN C  1 6   ? 50.159  -80.111 21.144  1.00 101.55 ? 12   GLN A CA  1 
ATOM   4006  C C   . GLN C  1 6   ? 49.029  -79.575 20.271  1.00 99.31  ? 12   GLN A C   1 
ATOM   4007  O O   . GLN C  1 6   ? 48.565  -80.229 19.327  1.00 93.46  ? 12   GLN A O   1 
ATOM   4008  C CB  . GLN C  1 6   ? 51.414  -79.256 20.948  1.00 97.93  ? 12   GLN A CB  1 
ATOM   4009  C CG  . GLN C  1 6   ? 52.483  -79.466 22.008  1.00 99.14  ? 12   GLN A CG  1 
ATOM   4010  C CD  . GLN C  1 6   ? 53.430  -78.281 22.117  1.00 104.53 ? 12   GLN A CD  1 
ATOM   4011  O OE1 . GLN C  1 6   ? 53.412  -77.380 21.277  1.00 105.06 ? 12   GLN A OE1 1 
ATOM   4012  N NE2 . GLN C  1 6   ? 54.263  -78.276 23.155  1.00 104.44 ? 12   GLN A NE2 1 
ATOM   4013  N N   . ILE C  1 7   ? 48.552  -78.399 20.666  1.00 101.06 ? 13   ILE A N   1 
ATOM   4014  C CA  . ILE C  1 7   ? 47.645  -77.575 19.880  1.00 99.53  ? 13   ILE A CA  1 
ATOM   4015  C C   . ILE C  1 7   ? 47.890  -76.146 20.373  1.00 95.30  ? 13   ILE A C   1 
ATOM   4016  O O   . ILE C  1 7   ? 48.046  -75.915 21.576  1.00 94.32  ? 13   ILE A O   1 
ATOM   4017  C CB  . ILE C  1 7   ? 46.157  -78.020 20.018  1.00 89.79  ? 13   ILE A CB  1 
ATOM   4018  C CG1 . ILE C  1 7   ? 45.310  -77.419 18.895  1.00 86.05  ? 13   ILE A CG1 1 
ATOM   4019  C CG2 . ILE C  1 7   ? 45.593  -77.698 21.399  1.00 90.68  ? 13   ILE A CG2 1 
ATOM   4020  C CD1 . ILE C  1 7   ? 43.890  -77.943 18.847  1.00 84.69  ? 13   ILE A CD1 1 
ATOM   4021  N N   . CYS C  1 8   ? 47.978  -75.195 19.449  1.00 95.94  ? 14   CYS A N   1 
ATOM   4022  C CA  . CYS C  1 8   ? 48.324  -73.818 19.815  1.00 100.85 ? 14   CYS A CA  1 
ATOM   4023  C C   . CYS C  1 8   ? 47.328  -72.808 19.247  1.00 98.42  ? 14   CYS A C   1 
ATOM   4024  O O   . CYS C  1 8   ? 46.665  -73.085 18.252  1.00 98.37  ? 14   CYS A O   1 
ATOM   4025  C CB  . CYS C  1 8   ? 49.745  -73.484 19.350  1.00 102.07 ? 14   CYS A CB  1 
ATOM   4026  S SG  . CYS C  1 8   ? 51.037  -74.491 20.147  1.00 107.37 ? 14   CYS A SG  1 
ATOM   4027  N N   . ILE C  1 9   ? 47.195  -71.659 19.910  1.00 93.46  ? 15   ILE A N   1 
ATOM   4028  C CA  . ILE C  1 9   ? 46.271  -70.619 19.460  1.00 95.85  ? 15   ILE A CA  1 
ATOM   4029  C C   . ILE C  1 9   ? 47.039  -69.437 18.892  1.00 94.53  ? 15   ILE A C   1 
ATOM   4030  O O   . ILE C  1 9   ? 48.014  -68.990 19.490  1.00 92.42  ? 15   ILE A O   1 
ATOM   4031  C CB  . ILE C  1 9   ? 45.348  -70.116 20.609  1.00 93.82  ? 15   ILE A CB  1 
ATOM   4032  C CG1 . ILE C  1 9   ? 44.528  -71.268 21.212  1.00 89.16  ? 15   ILE A CG1 1 
ATOM   4033  C CG2 . ILE C  1 9   ? 44.430  -68.995 20.121  1.00 85.88  ? 15   ILE A CG2 1 
ATOM   4034  C CD1 . ILE C  1 9   ? 43.472  -71.850 20.286  1.00 84.13  ? 15   ILE A CD1 1 
ATOM   4035  N N   . GLY C  1 10  ? 46.602  -68.954 17.730  1.00 98.12  ? 16   GLY A N   1 
ATOM   4036  C CA  . GLY C  1 10  ? 47.225  -67.810 17.085  1.00 98.32  ? 16   GLY A CA  1 
ATOM   4037  C C   . GLY C  1 10  ? 46.386  -67.115 16.018  1.00 99.52  ? 16   GLY A C   1 
ATOM   4038  O O   . GLY C  1 10  ? 45.274  -67.545 15.682  1.00 97.42  ? 16   GLY A O   1 
ATOM   4039  N N   . TYR C  1 11  ? 46.966  -66.065 15.441  1.00 99.09  ? 17   TYR A N   1 
ATOM   4040  C CA  . TYR C  1 11  ? 46.272  -65.181 14.507  1.00 98.41  ? 17   TYR A CA  1 
ATOM   4041  C C   . TYR C  1 11  ? 47.085  -64.937 13.228  1.00 97.00  ? 17   TYR A C   1 
ATOM   4042  O O   . TYR C  1 11  ? 48.250  -65.327 13.132  1.00 97.22  ? 17   TYR A O   1 
ATOM   4043  C CB  . TYR C  1 11  ? 45.956  -63.844 15.191  1.00 90.83  ? 17   TYR A CB  1 
ATOM   4044  C CG  . TYR C  1 11  ? 47.136  -63.238 15.927  1.00 86.76  ? 17   TYR A CG  1 
ATOM   4045  C CD1 . TYR C  1 11  ? 48.023  -62.388 15.282  1.00 86.54  ? 17   TYR A CD1 1 
ATOM   4046  C CD2 . TYR C  1 11  ? 47.365  -63.523 17.269  1.00 89.56  ? 17   TYR A CD2 1 
ATOM   4047  C CE1 . TYR C  1 11  ? 49.098  -61.830 15.953  1.00 87.64  ? 17   TYR A CE1 1 
ATOM   4048  C CE2 . TYR C  1 11  ? 48.444  -62.975 17.948  1.00 85.71  ? 17   TYR A CE2 1 
ATOM   4049  C CZ  . TYR C  1 11  ? 49.305  -62.132 17.285  1.00 87.18  ? 17   TYR A CZ  1 
ATOM   4050  O OH  . TYR C  1 11  ? 50.373  -61.586 17.962  1.00 89.75  ? 17   TYR A OH  1 
ATOM   4051  N N   . HIS C  1 12  ? 46.463  -64.276 12.258  1.00 94.73  ? 18   HIS A N   1 
ATOM   4052  C CA  . HIS C  1 12  ? 47.068  -64.014 10.953  1.00 95.86  ? 18   HIS A CA  1 
ATOM   4053  C C   . HIS C  1 12  ? 48.210  -62.971 11.090  1.00 91.91  ? 18   HIS A C   1 
ATOM   4054  O O   . HIS C  1 12  ? 48.129  -62.059 11.914  1.00 90.21  ? 18   HIS A O   1 
ATOM   4055  C CB  . HIS C  1 12  ? 45.952  -63.549 9.996   1.00 95.47  ? 18   HIS A CB  1 
ATOM   4056  C CG  . HIS C  1 12  ? 46.353  -63.413 8.554   1.00 101.54 ? 18   HIS A CG  1 
ATOM   4057  N ND1 . HIS C  1 12  ? 47.622  -63.063 8.143   1.00 97.40  ? 18   HIS A ND1 1 
ATOM   4058  C CD2 . HIS C  1 12  ? 45.622  -63.565 7.421   1.00 102.73 ? 18   HIS A CD2 1 
ATOM   4059  C CE1 . HIS C  1 12  ? 47.659  -63.015 6.822   1.00 99.44  ? 18   HIS A CE1 1 
ATOM   4060  N NE2 . HIS C  1 12  ? 46.458  -63.315 6.360   1.00 102.33 ? 18   HIS A NE2 1 
ATOM   4061  N N   . ALA C  1 13  ? 49.284  -63.136 10.315  1.00 89.81  ? 19   ALA A N   1 
ATOM   4062  C CA  . ALA C  1 13  ? 50.334  -62.117 10.185  1.00 94.55  ? 19   ALA A CA  1 
ATOM   4063  C C   . ALA C  1 13  ? 50.773  -62.043 8.719   1.00 97.59  ? 19   ALA A C   1 
ATOM   4064  O O   . ALA C  1 13  ? 50.522  -62.972 7.946   1.00 96.74  ? 19   ALA A O   1 
ATOM   4065  C CB  . ALA C  1 13  ? 51.526  -62.410 11.100  1.00 82.03  ? 19   ALA A CB  1 
ATOM   4066  N N   . ASN C  1 14  ? 51.428  -60.944 8.344   1.00 95.94  ? 20   ASN A N   1 
ATOM   4067  C CA  . ASN C  1 14  ? 51.845  -60.724 6.959   1.00 94.28  ? 20   ASN A CA  1 
ATOM   4068  C C   . ASN C  1 14  ? 53.115  -59.906 6.802   1.00 93.49  ? 20   ASN A C   1 
ATOM   4069  O O   . ASN C  1 14  ? 53.825  -59.626 7.773   1.00 88.98  ? 20   ASN A O   1 
ATOM   4070  C CB  . ASN C  1 14  ? 50.736  -59.997 6.185   1.00 97.37  ? 20   ASN A CB  1 
ATOM   4071  C CG  . ASN C  1 14  ? 49.850  -60.936 5.403   1.00 99.26  ? 20   ASN A CG  1 
ATOM   4072  O OD1 . ASN C  1 14  ? 50.121  -62.130 5.316   1.00 102.22 ? 20   ASN A OD1 1 
ATOM   4073  N ND2 . ASN C  1 14  ? 48.789  -60.396 4.812   1.00 95.99  ? 20   ASN A ND2 1 
ATOM   4074  N N   . ASN C  1 15  ? 53.368  -59.506 5.558   1.00 93.63  ? 21   ASN A N   1 
ATOM   4075  C CA  . ASN C  1 15  ? 54.524  -58.691 5.209   1.00 94.92  ? 21   ASN A CA  1 
ATOM   4076  C C   . ASN C  1 15  ? 54.078  -57.266 4.895   1.00 96.57  ? 21   ASN A C   1 
ATOM   4077  O O   . ASN C  1 15  ? 54.754  -56.538 4.168   1.00 97.89  ? 21   ASN A O   1 
ATOM   4078  C CB  . ASN C  1 15  ? 55.268  -59.287 4.008   1.00 97.35  ? 21   ASN A CB  1 
ATOM   4079  C CG  . ASN C  1 15  ? 56.152  -60.476 4.379   1.00 94.93  ? 21   ASN A CG  1 
ATOM   4080  O OD1 . ASN C  1 15  ? 57.240  -60.307 4.931   1.00 97.48  ? 21   ASN A OD1 1 
ATOM   4081  N ND2 . ASN C  1 15  ? 55.694  -61.682 4.052   1.00 86.69  ? 21   ASN A ND2 1 
ATOM   4082  N N   . SER C  1 16  ? 52.924  -56.890 5.448   1.00 101.00 ? 22   SER A N   1 
ATOM   4083  C CA  . SER C  1 16  ? 52.319  -55.575 5.233   1.00 97.75  ? 22   SER A CA  1 
ATOM   4084  C C   . SER C  1 16  ? 53.067  -54.474 5.993   1.00 89.16  ? 22   SER A C   1 
ATOM   4085  O O   . SER C  1 16  ? 53.812  -54.758 6.929   1.00 90.01  ? 22   SER A O   1 
ATOM   4086  C CB  . SER C  1 16  ? 50.835  -55.606 5.641   1.00 93.46  ? 22   SER A CB  1 
ATOM   4087  O OG  . SER C  1 16  ? 50.164  -54.409 5.285   1.00 89.23  ? 22   SER A OG  1 
ATOM   4088  N N   . THR C  1 17  ? 52.908  -53.228 5.555   1.00 89.54  ? 23   THR A N   1 
ATOM   4089  C CA  . THR C  1 17  ? 53.527  -52.094 6.242   1.00 90.69  ? 23   THR A CA  1 
ATOM   4090  C C   . THR C  1 17  ? 52.571  -50.913 6.418   1.00 89.18  ? 23   THR A C   1 
ATOM   4091  O O   . THR C  1 17  ? 52.972  -49.847 6.893   1.00 87.25  ? 23   THR A O   1 
ATOM   4092  C CB  . THR C  1 17  ? 54.780  -51.599 5.499   1.00 95.58  ? 23   THR A CB  1 
ATOM   4093  O OG1 . THR C  1 17  ? 54.567  -51.674 4.080   1.00 89.38  ? 23   THR A OG1 1 
ATOM   4094  C CG2 . THR C  1 17  ? 55.985  -52.439 5.886   1.00 93.80  ? 23   THR A CG2 1 
ATOM   4095  N N   . GLU C  1 18  ? 51.310  -51.106 6.045   1.00 87.23  ? 24   GLU A N   1 
ATOM   4096  C CA  . GLU C  1 18  ? 50.317  -50.046 6.159   1.00 87.74  ? 24   GLU A CA  1 
ATOM   4097  C C   . GLU C  1 18  ? 50.057  -49.670 7.616   1.00 83.74  ? 24   GLU A C   1 
ATOM   4098  O O   . GLU C  1 18  ? 50.017  -50.534 8.489   1.00 84.52  ? 24   GLU A O   1 
ATOM   4099  C CB  . GLU C  1 18  ? 49.021  -50.475 5.480   1.00 93.43  ? 24   GLU A CB  1 
ATOM   4100  C CG  . GLU C  1 18  ? 49.141  -50.623 3.973   1.00 95.43  ? 24   GLU A CG  1 
ATOM   4101  C CD  . GLU C  1 18  ? 47.806  -50.929 3.331   1.00 100.15 ? 24   GLU A CD  1 
ATOM   4102  O OE1 . GLU C  1 18  ? 46.882  -51.363 4.062   1.00 95.89  ? 24   GLU A OE1 1 
ATOM   4103  O OE2 . GLU C  1 18  ? 47.684  -50.745 2.099   1.00 99.51  ? 24   GLU A OE2 1 
ATOM   4104  N N   . GLN C  1 19  ? 49.874  -48.377 7.871   1.00 85.65  ? 25   GLN A N   1 
ATOM   4105  C CA  . GLN C  1 19  ? 49.706  -47.894 9.237   1.00 82.07  ? 25   GLN A CA  1 
ATOM   4106  C C   . GLN C  1 19  ? 48.422  -47.087 9.418   1.00 82.96  ? 25   GLN A C   1 
ATOM   4107  O O   . GLN C  1 19  ? 48.023  -46.324 8.535   1.00 84.30  ? 25   GLN A O   1 
ATOM   4108  C CB  . GLN C  1 19  ? 50.905  -47.042 9.646   1.00 78.43  ? 25   GLN A CB  1 
ATOM   4109  C CG  . GLN C  1 19  ? 52.234  -47.739 9.491   1.00 80.25  ? 25   GLN A CG  1 
ATOM   4110  C CD  . GLN C  1 19  ? 53.402  -46.817 9.776   1.00 88.67  ? 25   GLN A CD  1 
ATOM   4111  O OE1 . GLN C  1 19  ? 53.252  -45.595 9.812   1.00 93.25  ? 25   GLN A OE1 1 
ATOM   4112  N NE2 . GLN C  1 19  ? 54.581  -47.398 9.955   1.00 87.28  ? 25   GLN A NE2 1 
ATOM   4113  N N   . VAL C  1 20  ? 47.806  -47.237 10.588  1.00 78.96  ? 26   VAL A N   1 
ATOM   4114  C CA  . VAL C  1 20  ? 46.601  -46.499 10.938  1.00 71.00  ? 26   VAL A CA  1 
ATOM   4115  C C   . VAL C  1 20  ? 46.865  -45.788 12.248  1.00 73.87  ? 26   VAL A C   1 
ATOM   4116  O O   . VAL C  1 20  ? 47.863  -46.056 12.915  1.00 73.59  ? 26   VAL A O   1 
ATOM   4117  C CB  . VAL C  1 20  ? 45.350  -47.405 11.068  1.00 64.64  ? 26   VAL A CB  1 
ATOM   4118  C CG1 . VAL C  1 20  ? 45.192  -48.287 9.845   1.00 71.62  ? 26   VAL A CG1 1 
ATOM   4119  C CG2 . VAL C  1 20  ? 45.425  -48.248 12.306  1.00 73.24  ? 26   VAL A CG2 1 
ATOM   4120  N N   . ASP C  1 21  ? 46.018  -44.818 12.570  1.00 75.30  ? 27   ASP A N   1 
ATOM   4121  C CA  . ASP C  1 21  ? 46.132  -44.114 13.834  1.00 71.79  ? 27   ASP A CA  1 
ATOM   4122  C C   . ASP C  1 21  ? 44.940  -44.393 14.736  1.00 68.95  ? 27   ASP A C   1 
ATOM   4123  O O   . ASP C  1 21  ? 43.872  -44.804 14.272  1.00 63.86  ? 27   ASP A O   1 
ATOM   4124  C CB  . ASP C  1 21  ? 46.280  -42.612 13.604  1.00 75.98  ? 27   ASP A CB  1 
ATOM   4125  C CG  . ASP C  1 21  ? 47.672  -42.227 13.167  1.00 78.18  ? 27   ASP A CG  1 
ATOM   4126  O OD1 . ASP C  1 21  ? 48.439  -43.121 12.756  1.00 83.06  ? 27   ASP A OD1 1 
ATOM   4127  O OD2 . ASP C  1 21  ? 48.000  -41.027 13.244  1.00 82.07  ? 27   ASP A OD2 1 
ATOM   4128  N N   . THR C  1 22  ? 45.182  -44.233 16.034  1.00 68.93  ? 28   THR A N   1 
ATOM   4129  C CA  . THR C  1 22  ? 44.177  -44.315 17.095  1.00 69.13  ? 28   THR A CA  1 
ATOM   4130  C C   . THR C  1 22  ? 44.462  -43.188 18.096  1.00 73.93  ? 28   THR A C   1 
ATOM   4131  O O   . THR C  1 22  ? 45.445  -42.451 17.963  1.00 76.56  ? 28   THR A O   1 
ATOM   4132  C CB  . THR C  1 22  ? 44.161  -45.679 17.811  1.00 67.61  ? 28   THR A CB  1 
ATOM   4133  O OG1 . THR C  1 22  ? 45.445  -45.911 18.394  1.00 76.22  ? 28   THR A OG1 1 
ATOM   4134  C CG2 . THR C  1 22  ? 43.870  -46.809 16.841  1.00 65.98  ? 28   THR A CG2 1 
ATOM   4135  N N   . ILE C  1 23  ? 43.604  -43.031 19.091  1.00 72.14  ? 29   ILE A N   1 
ATOM   4136  C CA  . ILE C  1 23  ? 43.792  -41.935 20.028  1.00 72.24  ? 29   ILE A CA  1 
ATOM   4137  C C   . ILE C  1 23  ? 44.887  -42.172 21.071  1.00 76.07  ? 29   ILE A C   1 
ATOM   4138  O O   . ILE C  1 23  ? 45.361  -41.215 21.685  1.00 82.83  ? 29   ILE A O   1 
ATOM   4139  C CB  . ILE C  1 23  ? 42.504  -41.623 20.764  1.00 73.48  ? 29   ILE A CB  1 
ATOM   4140  C CG1 . ILE C  1 23  ? 42.333  -42.582 21.934  1.00 75.89  ? 29   ILE A CG1 1 
ATOM   4141  C CG2 . ILE C  1 23  ? 41.331  -41.681 19.793  1.00 74.55  ? 29   ILE A CG2 1 
ATOM   4142  C CD1 . ILE C  1 23  ? 41.788  -41.919 23.161  1.00 78.28  ? 29   ILE A CD1 1 
ATOM   4143  N N   . MET C  1 24  ? 45.284  -43.426 21.292  1.00 77.30  ? 30   MET A N   1 
ATOM   4144  C CA  . MET C  1 24  ? 46.309  -43.708 22.303  1.00 79.17  ? 30   MET A CA  1 
ATOM   4145  C C   . MET C  1 24  ? 47.701  -43.961 21.707  1.00 78.37  ? 30   MET A C   1 
ATOM   4146  O O   . MET C  1 24  ? 48.704  -43.893 22.421  1.00 81.14  ? 30   MET A O   1 
ATOM   4147  C CB  . MET C  1 24  ? 45.892  -44.905 23.165  1.00 73.71  ? 30   MET A CB  1 
ATOM   4148  C CG  . MET C  1 24  ? 45.384  -44.527 24.544  1.00 76.55  ? 30   MET A CG  1 
ATOM   4149  S SD  . MET C  1 24  ? 45.297  -45.943 25.665  1.00 76.74  ? 30   MET A SD  1 
ATOM   4150  C CE  . MET C  1 24  ? 43.800  -45.584 26.572  1.00 65.10  ? 30   MET A CE  1 
ATOM   4151  N N   . GLU C  1 25  ? 47.766  -44.227 20.405  1.00 75.37  ? 31   GLU A N   1 
ATOM   4152  C CA  . GLU C  1 25  ? 49.028  -44.614 19.779  1.00 83.03  ? 31   GLU A CA  1 
ATOM   4153  C C   . GLU C  1 25  ? 49.035  -44.326 18.274  1.00 80.66  ? 31   GLU A C   1 
ATOM   4154  O O   . GLU C  1 25  ? 48.094  -44.674 17.557  1.00 74.28  ? 31   GLU A O   1 
ATOM   4155  C CB  . GLU C  1 25  ? 49.320  -46.095 20.034  1.00 89.68  ? 31   GLU A CB  1 
ATOM   4156  C CG  . GLU C  1 25  ? 50.714  -46.538 19.588  1.00 93.56  ? 31   GLU A CG  1 
ATOM   4157  C CD  . GLU C  1 25  ? 50.956  -48.024 19.793  1.00 94.50  ? 31   GLU A CD  1 
ATOM   4158  O OE1 . GLU C  1 25  ? 50.064  -48.704 20.358  1.00 92.62  ? 31   GLU A OE1 1 
ATOM   4159  O OE2 . GLU C  1 25  ? 52.039  -48.510 19.387  1.00 92.66  ? 31   GLU A OE2 1 
ATOM   4160  N N   . LYS C  1 26  ? 50.129  -43.734 17.801  1.00 84.16  ? 32   LYS A N   1 
ATOM   4161  C CA  . LYS C  1 26  ? 50.231  -43.299 16.414  1.00 86.92  ? 32   LYS A CA  1 
ATOM   4162  C C   . LYS C  1 26  ? 51.093  -44.256 15.576  1.00 85.58  ? 32   LYS A C   1 
ATOM   4163  O O   . LYS C  1 26  ? 51.921  -44.994 16.120  1.00 85.17  ? 32   LYS A O   1 
ATOM   4164  C CB  . LYS C  1 26  ? 50.806  -41.881 16.371  1.00 83.62  ? 32   LYS A CB  1 
ATOM   4165  C CG  . LYS C  1 26  ? 49.915  -40.823 17.020  1.00 82.12  ? 32   LYS A CG  1 
ATOM   4166  C CD  . LYS C  1 26  ? 48.660  -40.542 16.221  1.00 81.80  ? 32   LYS A CD  1 
ATOM   4167  C CE  . LYS C  1 26  ? 47.839  -39.425 16.860  1.00 85.61  ? 32   LYS A CE  1 
ATOM   4168  N NZ  . LYS C  1 26  ? 46.720  -38.960 15.979  1.00 83.84  ? 32   LYS A NZ  1 
ATOM   4169  N N   . ASN C  1 27  ? 50.878  -44.235 14.258  1.00 86.39  ? 33   ASN A N   1 
ATOM   4170  C CA  . ASN C  1 27  ? 51.631  -45.047 13.288  1.00 90.25  ? 33   ASN A CA  1 
ATOM   4171  C C   . ASN C  1 27  ? 51.703  -46.512 13.714  1.00 87.87  ? 33   ASN A C   1 
ATOM   4172  O O   . ASN C  1 27  ? 52.784  -47.077 13.862  1.00 90.91  ? 33   ASN A O   1 
ATOM   4173  C CB  . ASN C  1 27  ? 53.057  -44.499 13.053  1.00 92.61  ? 33   ASN A CB  1 
ATOM   4174  C CG  . ASN C  1 27  ? 53.087  -43.236 12.176  1.00 99.73  ? 33   ASN A CG  1 
ATOM   4175  O OD1 . ASN C  1 27  ? 52.123  -42.928 11.467  1.00 97.86  ? 33   ASN A OD1 1 
ATOM   4176  N ND2 . ASN C  1 27  ? 54.218  -42.515 12.215  1.00 105.44 ? 33   ASN A ND2 1 
ATOM   4177  N N   . VAL C  1 28  ? 50.546  -47.122 13.926  1.00 83.96  ? 34   VAL A N   1 
ATOM   4178  C CA  . VAL C  1 28  ? 50.511  -48.533 14.255  1.00 78.90  ? 34   VAL A CA  1 
ATOM   4179  C C   . VAL C  1 28  ? 50.412  -49.307 12.957  1.00 80.23  ? 34   VAL A C   1 
ATOM   4180  O O   . VAL C  1 28  ? 49.442  -49.157 12.220  1.00 80.60  ? 34   VAL A O   1 
ATOM   4181  C CB  . VAL C  1 28  ? 49.327  -48.870 15.183  1.00 79.54  ? 34   VAL A CB  1 
ATOM   4182  C CG1 . VAL C  1 28  ? 49.018  -50.361 15.174  1.00 76.89  ? 34   VAL A CG1 1 
ATOM   4183  C CG2 . VAL C  1 28  ? 49.613  -48.376 16.590  1.00 83.15  ? 34   VAL A CG2 1 
ATOM   4184  N N   . THR C  1 29  ? 51.412  -50.139 12.678  1.00 82.86  ? 35   THR A N   1 
ATOM   4185  C CA  . THR C  1 29  ? 51.431  -50.888 11.427  1.00 84.07  ? 35   THR A CA  1 
ATOM   4186  C C   . THR C  1 29  ? 50.474  -52.074 11.549  1.00 79.79  ? 35   THR A C   1 
ATOM   4187  O O   . THR C  1 29  ? 50.415  -52.720 12.588  1.00 81.75  ? 35   THR A O   1 
ATOM   4188  C CB  . THR C  1 29  ? 52.850  -51.344 11.060  1.00 80.70  ? 35   THR A CB  1 
ATOM   4189  O OG1 . THR C  1 29  ? 52.869  -52.767 10.925  1.00 90.59  ? 35   THR A OG1 1 
ATOM   4190  C CG2 . THR C  1 29  ? 53.855  -50.889 12.125  1.00 69.16  ? 35   THR A CG2 1 
ATOM   4191  N N   . VAL C  1 30  ? 49.714  -52.337 10.489  1.00 81.37  ? 36   VAL A N   1 
ATOM   4192  C CA  . VAL C  1 30  ? 48.570  -53.250 10.546  1.00 82.65  ? 36   VAL A CA  1 
ATOM   4193  C C   . VAL C  1 30  ? 48.565  -54.185 9.314   1.00 88.98  ? 36   VAL A C   1 
ATOM   4194  O O   . VAL C  1 30  ? 49.143  -53.848 8.282   1.00 93.36  ? 36   VAL A O   1 
ATOM   4195  C CB  . VAL C  1 30  ? 47.244  -52.417 10.651  1.00 81.24  ? 36   VAL A CB  1 
ATOM   4196  C CG1 . VAL C  1 30  ? 46.010  -53.263 10.441  1.00 83.11  ? 36   VAL A CG1 1 
ATOM   4197  C CG2 . VAL C  1 30  ? 47.154  -51.729 12.004  1.00 79.98  ? 36   VAL A CG2 1 
ATOM   4198  N N   . THR C  1 31  ? 47.927  -55.353 9.425   1.00 87.62  ? 37   THR A N   1 
ATOM   4199  C CA  . THR C  1 31  ? 47.908  -56.353 8.351   1.00 87.94  ? 37   THR A CA  1 
ATOM   4200  C C   . THR C  1 31  ? 46.989  -55.980 7.185   1.00 86.98  ? 37   THR A C   1 
ATOM   4201  O O   . THR C  1 31  ? 47.318  -56.225 6.017   1.00 84.50  ? 37   THR A O   1 
ATOM   4202  C CB  . THR C  1 31  ? 47.473  -57.745 8.888   1.00 90.49  ? 37   THR A CB  1 
ATOM   4203  O OG1 . THR C  1 31  ? 46.057  -57.765 9.114   1.00 84.76  ? 37   THR A OG1 1 
ATOM   4204  C CG2 . THR C  1 31  ? 48.204  -58.085 10.185  1.00 86.63  ? 37   THR A CG2 1 
ATOM   4205  N N   . HIS C  1 32  ? 45.832  -55.407 7.519   1.00 88.41  ? 38   HIS A N   1 
ATOM   4206  C CA  . HIS C  1 32  ? 44.829  -54.988 6.533   1.00 88.36  ? 38   HIS A CA  1 
ATOM   4207  C C   . HIS C  1 32  ? 44.252  -53.613 6.876   1.00 82.12  ? 38   HIS A C   1 
ATOM   4208  O O   . HIS C  1 32  ? 43.855  -53.371 8.012   1.00 80.87  ? 38   HIS A O   1 
ATOM   4209  C CB  . HIS C  1 32  ? 43.660  -55.981 6.466   1.00 87.74  ? 38   HIS A CB  1 
ATOM   4210  C CG  . HIS C  1 32  ? 44.053  -57.388 6.137   1.00 91.20  ? 38   HIS A CG  1 
ATOM   4211  N ND1 . HIS C  1 32  ? 44.629  -58.236 7.061   1.00 93.94  ? 38   HIS A ND1 1 
ATOM   4212  C CD2 . HIS C  1 32  ? 43.903  -58.113 5.003   1.00 88.96  ? 38   HIS A CD2 1 
ATOM   4213  C CE1 . HIS C  1 32  ? 44.840  -59.414 6.501   1.00 93.94  ? 38   HIS A CE1 1 
ATOM   4214  N NE2 . HIS C  1 32  ? 44.409  -59.365 5.253   1.00 93.39  ? 38   HIS A NE2 1 
ATOM   4215  N N   . ALA C  1 33  ? 44.177  -52.730 5.886   1.00 81.02  ? 39   ALA A N   1 
ATOM   4216  C CA  . ALA C  1 33  ? 43.570  -51.412 6.069   1.00 77.38  ? 39   ALA A CA  1 
ATOM   4217  C C   . ALA C  1 33  ? 42.799  -51.006 4.809   1.00 79.64  ? 39   ALA A C   1 
ATOM   4218  O O   . ALA C  1 33  ? 43.015  -51.567 3.728   1.00 77.42  ? 39   ALA A O   1 
ATOM   4219  C CB  . ALA C  1 33  ? 44.625  -50.367 6.421   1.00 66.76  ? 39   ALA A CB  1 
ATOM   4220  N N   . GLN C  1 34  ? 41.894  -50.041 4.955   1.00 75.54  ? 40   GLN A N   1 
ATOM   4221  C CA  . GLN C  1 34  ? 41.119  -49.532 3.829   1.00 75.90  ? 40   GLN A CA  1 
ATOM   4222  C C   . GLN C  1 34  ? 41.150  -48.005 3.758   1.00 74.21  ? 40   GLN A C   1 
ATOM   4223  O O   . GLN C  1 34  ? 40.717  -47.324 4.689   1.00 74.19  ? 40   GLN A O   1 
ATOM   4224  C CB  . GLN C  1 34  ? 39.679  -50.025 3.918   1.00 70.97  ? 40   GLN A CB  1 
ATOM   4225  C CG  . GLN C  1 34  ? 38.795  -49.478 2.833   1.00 74.19  ? 40   GLN A CG  1 
ATOM   4226  C CD  . GLN C  1 34  ? 37.403  -50.063 2.881   1.00 83.14  ? 40   GLN A CD  1 
ATOM   4227  O OE1 . GLN C  1 34  ? 37.167  -51.082 3.539   1.00 85.35  ? 40   GLN A OE1 1 
ATOM   4228  N NE2 . GLN C  1 34  ? 36.463  -49.416 2.193   1.00 81.77  ? 40   GLN A NE2 1 
ATOM   4229  N N   . ASP C  1 35  ? 41.686  -47.472 2.663   1.00 73.12  ? 41   ASP A N   1 
ATOM   4230  C CA  . ASP C  1 35  ? 41.672  -46.032 2.427   1.00 68.20  ? 41   ASP A CA  1 
ATOM   4231  C C   . ASP C  1 35  ? 40.266  -45.593 2.021   1.00 68.03  ? 41   ASP A C   1 
ATOM   4232  O O   . ASP C  1 35  ? 39.576  -46.307 1.293   1.00 67.09  ? 41   ASP A O   1 
ATOM   4233  C CB  . ASP C  1 35  ? 42.684  -45.643 1.348   1.00 62.11  ? 41   ASP A CB  1 
ATOM   4234  C CG  . ASP C  1 35  ? 42.933  -44.142 1.287   1.00 69.19  ? 41   ASP A CG  1 
ATOM   4235  O OD1 . ASP C  1 35  ? 42.230  -43.384 1.989   1.00 72.05  ? 41   ASP A OD1 1 
ATOM   4236  O OD2 . ASP C  1 35  ? 43.841  -43.712 0.544   1.00 71.72  ? 41   ASP A OD2 1 
ATOM   4237  N N   . ILE C  1 36  ? 39.827  -44.445 2.536   1.00 68.23  ? 42   ILE A N   1 
ATOM   4238  C CA  . ILE C  1 36  ? 38.524  -43.883 2.173   1.00 68.46  ? 42   ILE A CA  1 
ATOM   4239  C C   . ILE C  1 36  ? 38.572  -42.398 1.744   1.00 65.13  ? 42   ILE A C   1 
ATOM   4240  O O   . ILE C  1 36  ? 37.523  -41.769 1.603   1.00 62.16  ? 42   ILE A O   1 
ATOM   4241  C CB  . ILE C  1 36  ? 37.516  -44.026 3.342   1.00 66.50  ? 42   ILE A CB  1 
ATOM   4242  C CG1 . ILE C  1 36  ? 38.092  -43.411 4.618   1.00 60.88  ? 42   ILE A CG1 1 
ATOM   4243  C CG2 . ILE C  1 36  ? 37.191  -45.485 3.590   1.00 67.45  ? 42   ILE A CG2 1 
ATOM   4244  C CD1 . ILE C  1 36  ? 37.166  -43.475 5.787   1.00 56.85  ? 42   ILE A CD1 1 
ATOM   4245  N N   . LEU C  1 37  ? 39.769  -41.867 1.479   1.00 61.54  ? 43   LEU A N   1 
ATOM   4246  C CA  . LEU C  1 37  ? 39.940  -40.453 1.118   1.00 63.84  ? 43   LEU A CA  1 
ATOM   4247  C C   . LEU C  1 37  ? 40.619  -40.229 -0.247  1.00 61.57  ? 43   LEU A C   1 
ATOM   4248  O O   . LEU C  1 37  ? 41.832  -40.415 -0.376  1.00 59.34  ? 43   LEU A O   1 
ATOM   4249  C CB  . LEU C  1 37  ? 40.763  -39.730 2.203   1.00 61.39  ? 43   LEU A CB  1 
ATOM   4250  C CG  . LEU C  1 37  ? 41.077  -38.259 1.895   1.00 59.44  ? 43   LEU A CG  1 
ATOM   4251  C CD1 . LEU C  1 37  ? 39.807  -37.419 1.970   1.00 55.96  ? 43   LEU A CD1 1 
ATOM   4252  C CD2 . LEU C  1 37  ? 42.175  -37.696 2.797   1.00 57.75  ? 43   LEU A CD2 1 
ATOM   4253  N N   . GLU C  1 38  ? 39.857  -39.725 -1.221  1.00 62.99  ? 44   GLU A N   1 
ATOM   4254  C CA  . GLU C  1 38  ? 40.392  -39.411 -2.557  1.00 59.30  ? 44   GLU A CA  1 
ATOM   4255  C C   . GLU C  1 38  ? 41.232  -38.128 -2.569  1.00 52.13  ? 44   GLU A C   1 
ATOM   4256  O O   . GLU C  1 38  ? 40.764  -37.069 -2.150  1.00 50.04  ? 44   GLU A O   1 
ATOM   4257  C CB  . GLU C  1 38  ? 39.248  -39.274 -3.560  1.00 56.29  ? 44   GLU A CB  1 
ATOM   4258  C CG  . GLU C  1 38  ? 39.700  -38.827 -4.931  1.00 57.55  ? 44   GLU A CG  1 
ATOM   4259  C CD  . GLU C  1 38  ? 40.646  -39.814 -5.588  1.00 59.08  ? 44   GLU A CD  1 
ATOM   4260  O OE1 . GLU C  1 38  ? 41.769  -39.411 -5.967  1.00 57.57  ? 44   GLU A OE1 1 
ATOM   4261  O OE2 . GLU C  1 38  ? 40.251  -40.987 -5.742  1.00 58.56  ? 44   GLU A OE2 1 
ATOM   4262  N N   . LYS C  1 39  ? 42.460  -38.224 -3.082  1.00 52.40  ? 45   LYS A N   1 
ATOM   4263  C CA  . LYS C  1 39  ? 43.420  -37.114 -3.015  1.00 54.29  ? 45   LYS A CA  1 
ATOM   4264  C C   . LYS C  1 39  ? 43.929  -36.669 -4.395  1.00 56.16  ? 45   LYS A C   1 
ATOM   4265  O O   . LYS C  1 39  ? 44.857  -35.852 -4.474  1.00 51.33  ? 45   LYS A O   1 
ATOM   4266  C CB  . LYS C  1 39  ? 44.633  -37.497 -2.143  1.00 46.92  ? 45   LYS A CB  1 
ATOM   4267  C CG  . LYS C  1 39  ? 44.323  -37.723 -0.673  1.00 58.40  ? 45   LYS A CG  1 
ATOM   4268  C CD  . LYS C  1 39  ? 45.511  -38.320 0.103   1.00 62.20  ? 45   LYS A CD  1 
ATOM   4269  C CE  . LYS C  1 39  ? 45.721  -39.814 -0.195  1.00 54.97  ? 45   LYS A CE  1 
ATOM   4270  N NZ  . LYS C  1 39  ? 44.466  -40.622 -0.085  1.00 52.30  ? 45   LYS A NZ  1 
ATOM   4271  N N   . THR C  1 40  ? 43.338  -37.203 -5.466  1.00 47.96  ? 46   THR A N   1 
ATOM   4272  C CA  . THR C  1 40  ? 43.787  -36.869 -6.813  1.00 54.50  ? 46   THR A CA  1 
ATOM   4273  C C   . THR C  1 40  ? 42.661  -36.431 -7.757  1.00 56.02  ? 46   THR A C   1 
ATOM   4274  O O   . THR C  1 40  ? 41.545  -36.977 -7.746  1.00 52.34  ? 46   THR A O   1 
ATOM   4275  C CB  . THR C  1 40  ? 44.541  -38.059 -7.479  1.00 55.09  ? 46   THR A CB  1 
ATOM   4276  O OG1 . THR C  1 40  ? 43.622  -39.106 -7.813  1.00 51.02  ? 46   THR A OG1 1 
ATOM   4277  C CG2 . THR C  1 40  ? 45.600  -38.609 -6.551  1.00 53.99  ? 46   THR A CG2 1 
ATOM   4278  N N   . HIS C  1 41  ? 42.996  -35.468 -8.610  1.00 58.84  ? 47   HIS A N   1 
ATOM   4279  C CA  . HIS C  1 41  ? 42.091  -34.972 -9.650  1.00 59.02  ? 47   HIS A CA  1 
ATOM   4280  C C   . HIS C  1 41  ? 42.857  -34.852 -10.964 1.00 54.42  ? 47   HIS A C   1 
ATOM   4281  O O   . HIS C  1 41  ? 44.095  -34.845 -10.973 1.00 51.45  ? 47   HIS A O   1 
ATOM   4282  C CB  . HIS C  1 41  ? 41.496  -33.622 -9.255  1.00 49.19  ? 47   HIS A CB  1 
ATOM   4283  C CG  . HIS C  1 41  ? 42.528  -32.562 -9.033  1.00 46.81  ? 47   HIS A CG  1 
ATOM   4284  N ND1 . HIS C  1 41  ? 43.133  -32.363 -7.809  1.00 47.61  ? 47   HIS A ND1 1 
ATOM   4285  C CD2 . HIS C  1 41  ? 43.074  -31.652 -9.877  1.00 44.62  ? 47   HIS A CD2 1 
ATOM   4286  C CE1 . HIS C  1 41  ? 43.999  -31.367 -7.903  1.00 46.83  ? 47   HIS A CE1 1 
ATOM   4287  N NE2 . HIS C  1 41  ? 43.983  -30.919 -9.148  1.00 49.11  ? 47   HIS A NE2 1 
ATOM   4288  N N   . ASN C  1 42  ? 42.129  -34.705 -12.067 1.00 53.31  ? 48   ASN A N   1 
ATOM   4289  C CA  . ASN C  1 42  ? 42.771  -34.716 -13.377 1.00 48.50  ? 48   ASN A CA  1 
ATOM   4290  C C   . ASN C  1 42  ? 43.209  -33.344 -13.883 1.00 50.62  ? 48   ASN A C   1 
ATOM   4291  O O   . ASN C  1 42  ? 43.819  -33.241 -14.951 1.00 53.97  ? 48   ASN A O   1 
ATOM   4292  C CB  . ASN C  1 42  ? 41.851  -35.410 -14.397 1.00 43.88  ? 48   ASN A CB  1 
ATOM   4293  C CG  . ASN C  1 42  ? 40.663  -34.562 -14.831 1.00 48.88  ? 48   ASN A CG  1 
ATOM   4294  O OD1 . ASN C  1 42  ? 40.499  -33.404 -14.432 1.00 51.64  ? 48   ASN A OD1 1 
ATOM   4295  N ND2 . ASN C  1 42  ? 39.806  -35.157 -15.659 1.00 51.43  ? 48   ASN A ND2 1 
ATOM   4296  N N   . GLY C  1 43  ? 42.909  -32.302 -13.111 1.00 45.09  ? 49   GLY A N   1 
ATOM   4297  C CA  . GLY C  1 43  ? 43.353  -30.955 -13.427 1.00 45.20  ? 49   GLY A CA  1 
ATOM   4298  C C   . GLY C  1 43  ? 42.757  -30.240 -14.638 1.00 47.98  ? 49   GLY A C   1 
ATOM   4299  O O   . GLY C  1 43  ? 43.363  -29.275 -15.110 1.00 46.31  ? 49   GLY A O   1 
ATOM   4300  N N   . LYS C  1 44  ? 41.609  -30.703 -15.152 1.00 45.96  ? 50   LYS A N   1 
ATOM   4301  C CA  . LYS C  1 44  ? 40.949  -30.050 -16.297 1.00 50.62  ? 50   LYS A CA  1 
ATOM   4302  C C   . LYS C  1 44  ? 39.411  -29.824 -16.137 1.00 57.63  ? 50   LYS A C   1 
ATOM   4303  O O   . LYS C  1 44  ? 38.771  -30.395 -15.232 1.00 52.45  ? 50   LYS A O   1 
ATOM   4304  C CB  . LYS C  1 44  ? 41.241  -30.830 -17.585 1.00 50.32  ? 50   LYS A CB  1 
ATOM   4305  C CG  . LYS C  1 44  ? 41.113  -32.334 -17.496 1.00 54.77  ? 50   LYS A CG  1 
ATOM   4306  C CD  . LYS C  1 44  ? 41.648  -32.984 -18.772 1.00 56.75  ? 50   LYS A CD  1 
ATOM   4307  C CE  . LYS C  1 44  ? 43.094  -32.546 -19.021 1.00 61.39  ? 50   LYS A CE  1 
ATOM   4308  N NZ  . LYS C  1 44  ? 43.635  -32.924 -20.367 1.00 61.94  ? 50   LYS A NZ  1 
ATOM   4309  N N   . LEU C  1 45  ? 38.829  -29.010 -17.035 1.00 54.48  ? 51   LEU A N   1 
ATOM   4310  C CA  . LEU C  1 45  ? 37.367  -28.793 -17.085 1.00 51.59  ? 51   LEU A CA  1 
ATOM   4311  C C   . LEU C  1 45  ? 36.677  -29.664 -18.124 1.00 49.84  ? 51   LEU A C   1 
ATOM   4312  O O   . LEU C  1 45  ? 37.004  -29.604 -19.307 1.00 57.73  ? 51   LEU A O   1 
ATOM   4313  C CB  . LEU C  1 45  ? 37.009  -27.323 -17.366 1.00 49.69  ? 51   LEU A CB  1 
ATOM   4314  C CG  . LEU C  1 45  ? 37.199  -26.179 -16.360 1.00 52.96  ? 51   LEU A CG  1 
ATOM   4315  C CD1 . LEU C  1 45  ? 38.084  -26.558 -15.182 1.00 50.44  ? 51   LEU A CD1 1 
ATOM   4316  C CD2 . LEU C  1 45  ? 37.697  -24.896 -17.043 1.00 51.73  ? 51   LEU A CD2 1 
ATOM   4317  N N   . CYS C  1 46  ? 35.697  -30.446 -17.678 1.00 46.11  ? 52   CYS A N   1 
ATOM   4318  C CA  . CYS C  1 46  ? 35.062  -31.466 -18.516 1.00 51.99  ? 52   CYS A CA  1 
ATOM   4319  C C   . CYS C  1 46  ? 33.576  -31.248 -18.735 1.00 46.88  ? 52   CYS A C   1 
ATOM   4320  O O   . CYS C  1 46  ? 32.984  -30.348 -18.156 1.00 47.74  ? 52   CYS A O   1 
ATOM   4321  C CB  . CYS C  1 46  ? 35.264  -32.858 -17.883 1.00 53.66  ? 52   CYS A CB  1 
ATOM   4322  S SG  . CYS C  1 46  ? 36.956  -33.154 -17.274 1.00 52.71  ? 52   CYS A SG  1 
ATOM   4323  N N   . ASN C  1 47  ? 32.977  -32.070 -19.589 1.00 47.65  ? 53   ASN A N   1 
ATOM   4324  C CA  . ASN C  1 47  ? 31.526  -32.115 -19.692 1.00 45.41  ? 53   ASN A CA  1 
ATOM   4325  C C   . ASN C  1 47  ? 30.960  -32.711 -18.415 1.00 51.01  ? 53   ASN A C   1 
ATOM   4326  O O   . ASN C  1 47  ? 31.643  -33.476 -17.732 1.00 53.74  ? 53   ASN A O   1 
ATOM   4327  C CB  . ASN C  1 47  ? 31.067  -32.945 -20.891 1.00 55.10  ? 53   ASN A CB  1 
ATOM   4328  C CG  . ASN C  1 47  ? 31.356  -32.281 -22.227 1.00 57.09  ? 53   ASN A CG  1 
ATOM   4329  O OD1 . ASN C  1 47  ? 32.151  -31.341 -22.317 1.00 57.16  ? 53   ASN A OD1 1 
ATOM   4330  N ND2 . ASN C  1 47  ? 30.697  -32.770 -23.280 1.00 50.70  ? 53   ASN A ND2 1 
ATOM   4331  N N   . LEU C  1 48  ? 29.732  -32.342 -18.070 1.00 48.48  ? 54   LEU A N   1 
ATOM   4332  C CA  . LEU C  1 48  ? 29.046  -32.980 -16.954 1.00 49.92  ? 54   LEU A CA  1 
ATOM   4333  C C   . LEU C  1 48  ? 27.980  -33.892 -17.534 1.00 53.64  ? 54   LEU A C   1 
ATOM   4334  O O   . LEU C  1 48  ? 27.021  -33.403 -18.131 1.00 52.44  ? 54   LEU A O   1 
ATOM   4335  C CB  . LEU C  1 48  ? 28.425  -31.946 -16.003 1.00 50.55  ? 54   LEU A CB  1 
ATOM   4336  C CG  . LEU C  1 48  ? 27.984  -32.411 -14.604 1.00 51.27  ? 54   LEU A CG  1 
ATOM   4337  C CD1 . LEU C  1 48  ? 29.178  -32.758 -13.695 1.00 46.97  ? 54   LEU A CD1 1 
ATOM   4338  C CD2 . LEU C  1 48  ? 27.068  -31.382 -13.943 1.00 48.69  ? 54   LEU A CD2 1 
ATOM   4339  N N   . ASP C  1 49  ? 28.130  -35.204 -17.325 1.00 56.03  ? 55   ASP A N   1 
ATOM   4340  C CA  . ASP C  1 49  ? 27.397  -36.219 -18.100 1.00 59.65  ? 55   ASP A CA  1 
ATOM   4341  C C   . ASP C  1 49  ? 27.648  -35.992 -19.581 1.00 57.62  ? 55   ASP A C   1 
ATOM   4342  O O   . ASP C  1 49  ? 28.794  -35.996 -20.038 1.00 54.30  ? 55   ASP A O   1 
ATOM   4343  C CB  . ASP C  1 49  ? 25.880  -36.194 -17.822 1.00 66.54  ? 55   ASP A CB  1 
ATOM   4344  C CG  . ASP C  1 49  ? 25.461  -37.168 -16.721 1.00 75.14  ? 55   ASP A CG  1 
ATOM   4345  O OD1 . ASP C  1 49  ? 26.130  -38.219 -16.590 1.00 83.53  ? 55   ASP A OD1 1 
ATOM   4346  O OD2 . ASP C  1 49  ? 24.474  -36.878 -15.990 1.00 67.89  ? 55   ASP A OD2 1 
ATOM   4347  N N   . GLY C  1 50  A 26.581  -35.780 -20.339 1.00 53.58  ? 55   GLY A N   1 
ATOM   4348  C CA  . GLY C  1 50  A 26.771  -35.530 -21.756 1.00 61.47  ? 55   GLY A CA  1 
ATOM   4349  C C   . GLY C  1 50  A 26.997  -34.062 -22.082 1.00 57.68  ? 55   GLY A C   1 
ATOM   4350  O O   . GLY C  1 50  A 27.458  -33.725 -23.171 1.00 57.01  ? 55   GLY A O   1 
ATOM   4351  N N   . VAL C  1 51  ? 26.733  -33.197 -21.106 1.00 55.69  ? 56   VAL A N   1 
ATOM   4352  C CA  . VAL C  1 51  ? 26.545  -31.778 -21.367 1.00 53.96  ? 56   VAL A CA  1 
ATOM   4353  C C   . VAL C  1 51  ? 27.771  -30.923 -21.111 1.00 52.50  ? 56   VAL A C   1 
ATOM   4354  O O   . VAL C  1 51  ? 28.304  -30.893 -19.994 1.00 49.36  ? 56   VAL A O   1 
ATOM   4355  C CB  . VAL C  1 51  ? 25.391  -31.222 -20.510 1.00 54.36  ? 56   VAL A CB  1 
ATOM   4356  C CG1 . VAL C  1 51  ? 25.125  -29.756 -20.841 1.00 48.94  ? 56   VAL A CG1 1 
ATOM   4357  C CG2 . VAL C  1 51  ? 24.147  -32.084 -20.688 1.00 49.66  ? 56   VAL A CG2 1 
ATOM   4358  N N   . LYS C  1 52  ? 28.145  -30.168 -22.146 1.00 51.07  ? 57   LYS A N   1 
ATOM   4359  C CA  . LYS C  1 52  ? 29.296  -29.278 -22.100 1.00 49.49  ? 57   LYS A CA  1 
ATOM   4360  C C   . LYS C  1 52  ? 28.940  -27.994 -21.301 1.00 46.70  ? 57   LYS A C   1 
ATOM   4361  O O   . LYS C  1 52  ? 27.817  -27.485 -21.392 1.00 44.42  ? 57   LYS A O   1 
ATOM   4362  C CB  . LYS C  1 52  ? 29.758  -28.927 -23.530 1.00 44.15  ? 57   LYS A CB  1 
ATOM   4363  C CG  . LYS C  1 52  ? 31.010  -28.049 -23.554 1.00 47.69  ? 57   LYS A CG  1 
ATOM   4364  C CD  . LYS C  1 52  ? 31.562  -27.779 -24.937 1.00 47.90  ? 57   LYS A CD  1 
ATOM   4365  C CE  . LYS C  1 52  ? 32.740  -26.798 -24.834 1.00 48.06  ? 57   LYS A CE  1 
ATOM   4366  N NZ  . LYS C  1 52  ? 33.434  -26.504 -26.129 1.00 61.86  ? 57   LYS A NZ  1 
ATOM   4367  N N   . PRO C  1 53  ? 29.878  -27.502 -20.476 1.00 39.15  ? 58   PRO A N   1 
ATOM   4368  C CA  . PRO C  1 53  ? 29.673  -26.241 -19.749 1.00 41.74  ? 58   PRO A CA  1 
ATOM   4369  C C   . PRO C  1 53  ? 29.846  -25.028 -20.667 1.00 42.46  ? 58   PRO A C   1 
ATOM   4370  O O   . PRO C  1 53  ? 30.536  -25.135 -21.692 1.00 39.78  ? 58   PRO A O   1 
ATOM   4371  C CB  . PRO C  1 53  ? 30.784  -26.250 -18.705 1.00 39.35  ? 58   PRO A CB  1 
ATOM   4372  C CG  . PRO C  1 53  ? 31.882  -27.043 -19.380 1.00 47.06  ? 58   PRO A CG  1 
ATOM   4373  C CD  . PRO C  1 53  ? 31.168  -28.130 -20.138 1.00 41.32  ? 58   PRO A CD  1 
ATOM   4374  N N   . LEU C  1 54  ? 29.253  -23.898 -20.282 1.00 40.77  ? 59   LEU A N   1 
ATOM   4375  C CA  . LEU C  1 54  ? 29.479  -22.596 -20.932 1.00 33.62  ? 59   LEU A CA  1 
ATOM   4376  C C   . LEU C  1 54  ? 30.743  -21.963 -20.383 1.00 33.92  ? 59   LEU A C   1 
ATOM   4377  O O   . LEU C  1 54  ? 30.781  -21.506 -19.248 1.00 40.35  ? 59   LEU A O   1 
ATOM   4378  C CB  . LEU C  1 54  ? 28.291  -21.652 -20.711 1.00 31.73  ? 59   LEU A CB  1 
ATOM   4379  C CG  . LEU C  1 54  ? 28.381  -20.183 -21.144 1.00 34.49  ? 59   LEU A CG  1 
ATOM   4380  C CD1 . LEU C  1 54  ? 28.581  -20.040 -22.644 1.00 37.69  ? 59   LEU A CD1 1 
ATOM   4381  C CD2 . LEU C  1 54  ? 27.162  -19.397 -20.703 1.00 33.90  ? 59   LEU A CD2 1 
ATOM   4382  N N   . ILE C  1 55  ? 31.793  -21.941 -21.176 1.00 32.21  ? 60   ILE A N   1 
ATOM   4383  C CA  . ILE C  1 55  ? 33.029  -21.358 -20.705 1.00 37.56  ? 60   ILE A CA  1 
ATOM   4384  C C   . ILE C  1 55  ? 33.182  -19.952 -21.312 1.00 41.16  ? 60   ILE A C   1 
ATOM   4385  O O   . ILE C  1 55  ? 33.557  -19.805 -22.477 1.00 41.14  ? 60   ILE A O   1 
ATOM   4386  C CB  . ILE C  1 55  ? 34.227  -22.285 -21.080 1.00 43.08  ? 60   ILE A CB  1 
ATOM   4387  C CG1 . ILE C  1 55  ? 33.922  -23.725 -20.631 1.00 40.70  ? 60   ILE A CG1 1 
ATOM   4388  C CG2 . ILE C  1 55  ? 35.577  -21.728 -20.566 1.00 36.52  ? 60   ILE A CG2 1 
ATOM   4389  C CD1 . ILE C  1 55  ? 35.023  -24.703 -20.841 1.00 43.82  ? 60   ILE A CD1 1 
ATOM   4390  N N   . LEU C  1 56  ? 32.851  -18.907 -20.553 1.00 43.09  ? 61   LEU A N   1 
ATOM   4391  C CA  . LEU C  1 56  ? 33.175  -17.568 -21.038 1.00 42.00  ? 61   LEU A CA  1 
ATOM   4392  C C   . LEU C  1 56  ? 34.678  -17.557 -20.940 1.00 44.42  ? 61   LEU A C   1 
ATOM   4393  O O   . LEU C  1 56  ? 35.246  -18.318 -20.163 1.00 51.82  ? 61   LEU A O   1 
ATOM   4394  C CB  . LEU C  1 56  ? 32.534  -16.433 -20.227 1.00 42.25  ? 61   LEU A CB  1 
ATOM   4395  C CG  . LEU C  1 56  ? 31.050  -16.364 -19.836 1.00 36.83  ? 61   LEU A CG  1 
ATOM   4396  C CD1 . LEU C  1 56  ? 30.131  -16.440 -21.054 1.00 36.98  ? 61   LEU A CD1 1 
ATOM   4397  C CD2 . LEU C  1 56  ? 30.686  -17.430 -18.854 1.00 39.03  ? 61   LEU A CD2 1 
ATOM   4398  N N   . ARG C  1 57  ? 35.344  -16.751 -21.734 1.00 41.19  ? 62   ARG A N   1 
ATOM   4399  C CA  . ARG C  1 57  ? 36.793  -16.772 -21.663 1.00 47.75  ? 62   ARG A CA  1 
ATOM   4400  C C   . ARG C  1 57  ? 37.214  -15.598 -20.835 1.00 50.25  ? 62   ARG A C   1 
ATOM   4401  O O   . ARG C  1 57  ? 37.482  -15.719 -19.644 1.00 48.77  ? 62   ARG A O   1 
ATOM   4402  C CB  . ARG C  1 57  ? 37.436  -16.670 -23.034 1.00 48.08  ? 62   ARG A CB  1 
ATOM   4403  C CG  . ARG C  1 57  ? 37.390  -17.873 -23.877 1.00 48.77  ? 62   ARG A CG  1 
ATOM   4404  C CD  . ARG C  1 57  ? 38.189  -17.575 -25.144 1.00 54.56  ? 62   ARG A CD  1 
ATOM   4405  N NE  . ARG C  1 57  ? 37.627  -18.264 -26.292 1.00 54.00  ? 62   ARG A NE  1 
ATOM   4406  C CZ  . ARG C  1 57  ? 37.882  -19.538 -26.540 1.00 54.96  ? 62   ARG A CZ  1 
ATOM   4407  N NH1 . ARG C  1 57  ? 38.666  -20.197 -25.700 1.00 53.14  ? 62   ARG A NH1 1 
ATOM   4408  N NH2 . ARG C  1 57  ? 37.345  -20.155 -27.587 1.00 56.28  ? 62   ARG A NH2 1 
ATOM   4409  N N   . ASP C  1 58  ? 37.312  -14.466 -21.529 1.00 46.81  ? 63   ASP A N   1 
ATOM   4410  C CA  . ASP C  1 58  ? 37.629  -13.192 -20.935 1.00 51.43  ? 63   ASP A CA  1 
ATOM   4411  C C   . ASP C  1 58  ? 36.360  -12.351 -20.833 1.00 43.83  ? 63   ASP A C   1 
ATOM   4412  O O   . ASP C  1 58  ? 36.430  -11.124 -20.678 1.00 40.77  ? 63   ASP A O   1 
ATOM   4413  C CB  . ASP C  1 58  ? 38.705  -12.475 -21.762 1.00 50.52  ? 63   ASP A CB  1 
ATOM   4414  C CG  . ASP C  1 58  ? 39.987  -13.266 -21.842 1.00 56.59  ? 63   ASP A CG  1 
ATOM   4415  O OD1 . ASP C  1 58  ? 40.676  -13.363 -20.795 1.00 60.63  ? 63   ASP A OD1 1 
ATOM   4416  O OD2 . ASP C  1 58  ? 40.282  -13.813 -22.932 1.00 61.56  ? 63   ASP A OD2 1 
ATOM   4417  N N   . CYS C  1 59  ? 35.213  -13.026 -20.895 1.00 37.60  ? 64   CYS A N   1 
ATOM   4418  C CA  . CYS C  1 59  ? 33.918  -12.369 -20.728 1.00 40.21  ? 64   CYS A CA  1 
ATOM   4419  C C   . CYS C  1 59  ? 33.287  -12.650 -19.351 1.00 35.05  ? 64   CYS A C   1 
ATOM   4420  O O   . CYS C  1 59  ? 33.484  -13.727 -18.780 1.00 31.08  ? 64   CYS A O   1 
ATOM   4421  C CB  . CYS C  1 59  ? 32.943  -12.793 -21.841 1.00 30.48  ? 64   CYS A CB  1 
ATOM   4422  S SG  . CYS C  1 59  ? 33.158  -11.881 -23.368 1.00 56.67  ? 64   CYS A SG  1 
ATOM   4423  N N   . SER C  1 60  ? 32.558  -11.659 -18.824 1.00 34.75  ? 65   SER A N   1 
ATOM   4424  C CA  . SER C  1 60  ? 31.713  -11.815 -17.614 1.00 32.93  ? 65   SER A CA  1 
ATOM   4425  C C   . SER C  1 60  ? 30.236  -12.091 -17.968 1.00 30.80  ? 65   SER A C   1 
ATOM   4426  O O   . SER C  1 60  ? 29.835  -12.027 -19.146 1.00 28.58  ? 65   SER A O   1 
ATOM   4427  C CB  . SER C  1 60  ? 31.793  -10.562 -16.744 1.00 30.39  ? 65   SER A CB  1 
ATOM   4428  O OG  . SER C  1 60  ? 31.145  -9.471  -17.385 1.00 30.71  ? 65   SER A OG  1 
ATOM   4429  N N   . VAL C  1 61  ? 29.415  -12.385 -16.963 1.00 33.02  ? 66   VAL A N   1 
ATOM   4430  C CA  . VAL C  1 61  ? 27.989  -12.588 -17.235 1.00 31.05  ? 66   VAL A CA  1 
ATOM   4431  C C   . VAL C  1 61  ? 27.414  -11.265 -17.802 1.00 25.41  ? 66   VAL A C   1 
ATOM   4432  O O   . VAL C  1 61  ? 26.779  -11.268 -18.867 1.00 29.07  ? 66   VAL A O   1 
ATOM   4433  C CB  . VAL C  1 61  ? 27.228  -13.100 -15.955 1.00 29.42  ? 66   VAL A CB  1 
ATOM   4434  C CG1 . VAL C  1 61  ? 25.684  -13.047 -16.118 1.00 20.63  ? 66   VAL A CG1 1 
ATOM   4435  C CG2 . VAL C  1 61  ? 27.633  -14.513 -15.669 1.00 24.27  ? 66   VAL A CG2 1 
ATOM   4436  N N   . ALA C  1 62  ? 27.763  -10.134 -17.194 1.00 24.88  ? 67   ALA A N   1 
ATOM   4437  C CA  . ALA C  1 62  ? 27.305  -8.832  -17.677 1.00 26.93  ? 67   ALA A CA  1 
ATOM   4438  C C   . ALA C  1 62  ? 27.718  -8.574  -19.142 1.00 29.59  ? 67   ALA A C   1 
ATOM   4439  O O   . ALA C  1 62  ? 26.902  -8.136  -19.954 1.00 28.66  ? 67   ALA A O   1 
ATOM   4440  C CB  . ALA C  1 62  ? 27.865  -7.717  -16.793 1.00 21.89  ? 67   ALA A CB  1 
ATOM   4441  N N   . GLY C  1 63  ? 28.973  -8.878  -19.477 1.00 30.19  ? 68   GLY A N   1 
ATOM   4442  C CA  . GLY C  1 63  ? 29.482  -8.715  -20.833 1.00 27.83  ? 68   GLY A CA  1 
ATOM   4443  C C   . GLY C  1 63  ? 28.704  -9.577  -21.809 1.00 29.59  ? 68   GLY A C   1 
ATOM   4444  O O   . GLY C  1 63  ? 28.341  -9.147  -22.920 1.00 27.51  ? 68   GLY A O   1 
ATOM   4445  N N   . TRP C  1 64  ? 28.475  -10.821 -21.395 1.00 29.97  ? 69   TRP A N   1 
ATOM   4446  C CA  . TRP C  1 64  ? 27.718  -11.779 -22.192 1.00 28.50  ? 69   TRP A CA  1 
ATOM   4447  C C   . TRP C  1 64  ? 26.290  -11.311 -22.500 1.00 30.44  ? 69   TRP A C   1 
ATOM   4448  O O   . TRP C  1 64  ? 25.900  -11.197 -23.654 1.00 27.12  ? 69   TRP A O   1 
ATOM   4449  C CB  . TRP C  1 64  ? 27.677  -13.127 -21.457 1.00 28.91  ? 69   TRP A CB  1 
ATOM   4450  C CG  . TRP C  1 64  ? 26.651  -14.100 -21.971 1.00 29.60  ? 69   TRP A CG  1 
ATOM   4451  C CD1 . TRP C  1 64  ? 26.275  -14.292 -23.277 1.00 27.43  ? 69   TRP A CD1 1 
ATOM   4452  C CD2 . TRP C  1 64  ? 25.907  -15.052 -21.196 1.00 28.64  ? 69   TRP A CD2 1 
ATOM   4453  N NE1 . TRP C  1 64  ? 25.318  -15.276 -23.343 1.00 28.17  ? 69   TRP A NE1 1 
ATOM   4454  C CE2 . TRP C  1 64  ? 25.080  -15.761 -22.086 1.00 25.36  ? 69   TRP A CE2 1 
ATOM   4455  C CE3 . TRP C  1 64  ? 25.845  -15.357 -19.829 1.00 26.41  ? 69   TRP A CE3 1 
ATOM   4456  C CZ2 . TRP C  1 64  ? 24.206  -16.754 -21.658 1.00 27.82  ? 69   TRP A CZ2 1 
ATOM   4457  C CZ3 . TRP C  1 64  ? 24.974  -16.330 -19.410 1.00 22.86  ? 69   TRP A CZ3 1 
ATOM   4458  C CH2 . TRP C  1 64  ? 24.171  -17.026 -20.320 1.00 28.01  ? 69   TRP A CH2 1 
ATOM   4459  N N   . LEU C  1 65  ? 25.517  -11.043 -21.449 1.00 33.68  ? 70   LEU A N   1 
ATOM   4460  C CA  . LEU C  1 65  ? 24.081  -10.808 -21.591 1.00 31.33  ? 70   LEU A CA  1 
ATOM   4461  C C   . LEU C  1 65  ? 23.737  -9.471  -22.274 1.00 27.18  ? 70   LEU A C   1 
ATOM   4462  O O   . LEU C  1 65  ? 22.747  -9.396  -23.016 1.00 25.11  ? 70   LEU A O   1 
ATOM   4463  C CB  . LEU C  1 65  ? 23.405  -10.927 -20.202 1.00 27.86  ? 70   LEU A CB  1 
ATOM   4464  C CG  . LEU C  1 65  ? 23.365  -12.356 -19.605 1.00 26.49  ? 70   LEU A CG  1 
ATOM   4465  C CD1 . LEU C  1 65  ? 22.685  -12.390 -18.250 1.00 22.16  ? 70   LEU A CD1 1 
ATOM   4466  C CD2 . LEU C  1 65  ? 22.720  -13.371 -20.547 1.00 24.15  ? 70   LEU A CD2 1 
ATOM   4467  N N   . LEU C  1 66  ? 24.517  -8.426  -21.998 1.00 23.06  ? 71   LEU A N   1 
ATOM   4468  C CA  . LEU C  1 66  ? 24.269  -7.107  -22.610 1.00 29.02  ? 71   LEU A CA  1 
ATOM   4469  C C   . LEU C  1 66  ? 24.791  -7.068  -24.048 1.00 28.65  ? 71   LEU A C   1 
ATOM   4470  O O   . LEU C  1 66  ? 24.317  -6.274  -24.867 1.00 24.91  ? 71   LEU A O   1 
ATOM   4471  C CB  . LEU C  1 66  ? 24.914  -5.981  -21.795 1.00 24.33  ? 71   LEU A CB  1 
ATOM   4472  C CG  . LEU C  1 66  ? 24.147  -5.576  -20.534 1.00 27.40  ? 71   LEU A CG  1 
ATOM   4473  C CD1 . LEU C  1 66  ? 24.980  -4.671  -19.639 1.00 27.01  ? 71   LEU A CD1 1 
ATOM   4474  C CD2 . LEU C  1 66  ? 22.873  -4.847  -20.920 1.00 25.96  ? 71   LEU A CD2 1 
ATOM   4475  N N   . GLY C  1 67  ? 25.782  -7.916  -24.333 1.00 26.99  ? 72   GLY A N   1 
ATOM   4476  C CA  . GLY C  1 67  ? 26.368  -8.002  -25.656 1.00 23.01  ? 72   GLY A CA  1 
ATOM   4477  C C   . GLY C  1 67  ? 27.531  -7.033  -25.865 1.00 28.70  ? 72   GLY A C   1 
ATOM   4478  O O   . GLY C  1 67  ? 27.501  -6.218  -26.801 1.00 25.65  ? 72   GLY A O   1 
ATOM   4479  N N   . ASN C  1 68  ? 28.527  -7.095  -24.972 1.00 26.34  ? 73   ASN A N   1 
ATOM   4480  C CA  . ASN C  1 68  ? 29.831  -6.453  -25.165 1.00 26.16  ? 73   ASN A CA  1 
ATOM   4481  C C   . ASN C  1 68  ? 30.337  -6.836  -26.555 1.00 31.08  ? 73   ASN A C   1 
ATOM   4482  O O   . ASN C  1 68  ? 30.305  -8.026  -26.921 1.00 29.74  ? 73   ASN A O   1 
ATOM   4483  C CB  . ASN C  1 68  ? 30.805  -6.918  -24.061 1.00 28.11  ? 73   ASN A CB  1 
ATOM   4484  C CG  . ASN C  1 68  ? 32.164  -6.184  -24.066 1.00 30.39  ? 73   ASN A CG  1 
ATOM   4485  O OD1 . ASN C  1 68  ? 32.773  -5.931  -25.112 1.00 31.55  ? 73   ASN A OD1 1 
ATOM   4486  N ND2 . ASN C  1 68  ? 32.651  -5.872  -22.867 1.00 31.01  ? 73   ASN A ND2 1 
ATOM   4487  N N   . PRO C  1 69  ? 30.773  -5.840  -27.350 1.00 26.92  ? 74   PRO A N   1 
ATOM   4488  C CA  . PRO C  1 69  ? 31.162  -6.115  -28.750 1.00 30.78  ? 74   PRO A CA  1 
ATOM   4489  C C   . PRO C  1 69  ? 32.277  -7.168  -28.866 1.00 31.01  ? 74   PRO A C   1 
ATOM   4490  O O   . PRO C  1 69  ? 32.385  -7.817  -29.902 1.00 27.63  ? 74   PRO A O   1 
ATOM   4491  C CB  . PRO C  1 69  ? 31.678  -4.751  -29.254 1.00 24.64  ? 74   PRO A CB  1 
ATOM   4492  C CG  . PRO C  1 69  ? 31.089  -3.754  -28.353 1.00 30.40  ? 74   PRO A CG  1 
ATOM   4493  C CD  . PRO C  1 69  ? 30.947  -4.423  -27.004 1.00 25.89  ? 74   PRO A CD  1 
ATOM   4494  N N   . MET C  1 70  ? 33.056  -7.346  -27.796 1.00 29.87  ? 75   MET A N   1 
ATOM   4495  C CA  . MET C  1 70  ? 34.165  -8.305  -27.757 1.00 34.57  ? 75   MET A CA  1 
ATOM   4496  C C   . MET C  1 70  ? 33.712  -9.676  -27.302 1.00 32.48  ? 75   MET A C   1 
ATOM   4497  O O   . MET C  1 70  ? 34.535  -10.507 -26.949 1.00 37.25  ? 75   MET A O   1 
ATOM   4498  C CB  . MET C  1 70  ? 35.303  -7.811  -26.837 1.00 37.49  ? 75   MET A CB  1 
ATOM   4499  C CG  . MET C  1 70  ? 36.108  -6.605  -27.375 1.00 39.55  ? 75   MET A CG  1 
ATOM   4500  S SD  . MET C  1 70  ? 37.358  -7.193  -28.538 1.00 54.82  ? 75   MET A SD  1 
ATOM   4501  C CE  . MET C  1 70  ? 38.016  -5.648  -29.198 1.00 47.32  ? 75   MET A CE  1 
ATOM   4502  N N   . CYS C  1 71  ? 32.407  -9.886  -27.230 1.00 30.39  ? 76   CYS A N   1 
ATOM   4503  C CA  . CYS C  1 71  ? 31.888  -11.153 -26.753 1.00 34.06  ? 76   CYS A CA  1 
ATOM   4504  C C   . CYS C  1 71  ? 30.961  -11.807 -27.759 1.00 33.84  ? 76   CYS A C   1 
ATOM   4505  O O   . CYS C  1 71  ? 30.055  -12.572 -27.371 1.00 35.52  ? 76   CYS A O   1 
ATOM   4506  C CB  . CYS C  1 71  ? 31.162  -10.948 -25.417 1.00 27.66  ? 76   CYS A CB  1 
ATOM   4507  S SG  . CYS C  1 71  ? 32.246  -10.220 -24.173 1.00 40.75  ? 76   CYS A SG  1 
ATOM   4508  N N   . ASP C  1 72  ? 31.164  -11.531 -29.042 1.00 32.79  ? 77   ASP A N   1 
ATOM   4509  C CA  . ASP C  1 72  ? 30.188  -12.006 -30.033 1.00 33.66  ? 77   ASP A CA  1 
ATOM   4510  C C   . ASP C  1 72  ? 30.165  -13.533 -30.089 1.00 30.11  ? 77   ASP A C   1 
ATOM   4511  O O   . ASP C  1 72  ? 29.227  -14.126 -30.610 1.00 28.02  ? 77   ASP A O   1 
ATOM   4512  C CB  . ASP C  1 72  ? 30.486  -11.462 -31.437 1.00 35.75  ? 77   ASP A CB  1 
ATOM   4513  C CG  . ASP C  1 72  ? 30.139  -9.979  -31.594 1.00 36.59  ? 77   ASP A CG  1 
ATOM   4514  O OD1 . ASP C  1 72  ? 29.431  -9.427  -30.720 1.00 31.05  ? 77   ASP A OD1 1 
ATOM   4515  O OD2 . ASP C  1 72  ? 30.535  -9.394  -32.637 1.00 37.85  ? 77   ASP A OD2 1 
ATOM   4516  N N   . GLU C  1 73  ? 31.173  -14.168 -29.490 1.00 35.19  ? 78   GLU A N   1 
ATOM   4517  C CA  . GLU C  1 73  ? 31.231  -15.628 -29.393 1.00 30.62  ? 78   GLU A CA  1 
ATOM   4518  C C   . GLU C  1 73  ? 29.993  -16.144 -28.667 1.00 31.46  ? 78   GLU A C   1 
ATOM   4519  O O   . GLU C  1 73  ? 29.523  -17.245 -28.955 1.00 33.45  ? 78   GLU A O   1 
ATOM   4520  C CB  . GLU C  1 73  ? 32.516  -16.068 -28.666 1.00 32.95  ? 78   GLU A CB  1 
ATOM   4521  C CG  . GLU C  1 73  ? 32.718  -17.596 -28.502 1.00 40.11  ? 78   GLU A CG  1 
ATOM   4522  C CD  . GLU C  1 73  ? 34.036  -17.947 -27.755 1.00 49.07  ? 78   GLU A CD  1 
ATOM   4523  O OE1 . GLU C  1 73  ? 34.825  -17.016 -27.468 1.00 54.25  ? 78   GLU A OE1 1 
ATOM   4524  O OE2 . GLU C  1 73  ? 34.290  -19.144 -27.461 1.00 47.09  ? 78   GLU A OE2 1 
ATOM   4525  N N   . PHE C  1 74  ? 29.426  -15.343 -27.761 1.00 30.06  ? 79   PHE A N   1 
ATOM   4526  C CA  . PHE C  1 74  ? 28.305  -15.837 -26.975 1.00 29.00  ? 79   PHE A CA  1 
ATOM   4527  C C   . PHE C  1 74  ? 26.944  -15.242 -27.371 1.00 25.75  ? 79   PHE A C   1 
ATOM   4528  O O   . PHE C  1 74  ? 26.045  -15.178 -26.566 1.00 33.29  ? 79   PHE A O   1 
ATOM   4529  C CB  . PHE C  1 74  ? 28.598  -15.626 -25.493 1.00 32.09  ? 79   PHE A CB  1 
ATOM   4530  C CG  . PHE C  1 74  ? 29.984  -16.067 -25.097 1.00 35.06  ? 79   PHE A CG  1 
ATOM   4531  C CD1 . PHE C  1 74  ? 30.303  -17.426 -25.033 1.00 35.99  ? 79   PHE A CD1 1 
ATOM   4532  C CD2 . PHE C  1 74  ? 30.965  -15.128 -24.787 1.00 31.91  ? 79   PHE A CD2 1 
ATOM   4533  C CE1 . PHE C  1 74  ? 31.588  -17.845 -24.687 1.00 35.98  ? 79   PHE A CE1 1 
ATOM   4534  C CE2 . PHE C  1 74  ? 32.238  -15.530 -24.427 1.00 36.77  ? 79   PHE A CE2 1 
ATOM   4535  C CZ  . PHE C  1 74  ? 32.555  -16.896 -24.384 1.00 39.19  ? 79   PHE A CZ  1 
ATOM   4536  N N   . LEU C  1 75  ? 26.787  -14.822 -28.618 1.00 28.66  ? 80   LEU A N   1 
ATOM   4537  C CA  . LEU C  1 75  ? 25.525  -14.248 -29.081 1.00 31.42  ? 80   LEU A CA  1 
ATOM   4538  C C   . LEU C  1 75  ? 24.332  -15.209 -29.087 1.00 33.00  ? 80   LEU A C   1 
ATOM   4539  O O   . LEU C  1 75  ? 23.181  -14.776 -28.994 1.00 34.17  ? 80   LEU A O   1 
ATOM   4540  C CB  . LEU C  1 75  ? 25.679  -13.672 -30.489 1.00 31.83  ? 80   LEU A CB  1 
ATOM   4541  C CG  . LEU C  1 75  ? 26.309  -12.287 -30.627 1.00 35.61  ? 80   LEU A CG  1 
ATOM   4542  C CD1 . LEU C  1 75  ? 26.396  -11.959 -32.109 1.00 26.25  ? 80   LEU A CD1 1 
ATOM   4543  C CD2 . LEU C  1 75  ? 25.567  -11.191 -29.838 1.00 27.55  ? 80   LEU A CD2 1 
ATOM   4544  N N   . ASN C  1 76  ? 24.594  -16.495 -29.268 1.00 31.48  ? 81   ASN A N   1 
ATOM   4545  C CA  . ASN C  1 76  ? 23.535  -17.505 -29.251 1.00 39.00  ? 81   ASN A CA  1 
ATOM   4546  C C   . ASN C  1 76  ? 24.119  -18.815 -28.726 1.00 35.85  ? 81   ASN A C   1 
ATOM   4547  O O   . ASN C  1 76  ? 24.665  -19.596 -29.501 1.00 45.53  ? 81   ASN A O   1 
ATOM   4548  C CB  . ASN C  1 76  ? 22.930  -17.693 -30.660 1.00 41.93  ? 81   ASN A CB  1 
ATOM   4549  C CG  . ASN C  1 76  ? 21.974  -16.555 -31.053 1.00 46.34  ? 81   ASN A CG  1 
ATOM   4550  O OD1 . ASN C  1 76  ? 20.821  -16.535 -30.625 1.00 51.12  ? 81   ASN A OD1 1 
ATOM   4551  N ND2 . ASN C  1 76  ? 22.464  -15.593 -31.852 1.00 40.22  ? 81   ASN A ND2 1 
ATOM   4552  N N   . VAL C  1 77  ? 24.057  -19.037 -27.418 1.00 33.02  ? 82   VAL A N   1 
ATOM   4553  C CA  . VAL C  1 77  ? 24.728  -20.206 -26.839 1.00 36.21  ? 82   VAL A CA  1 
ATOM   4554  C C   . VAL C  1 77  ? 23.789  -21.385 -26.649 1.00 37.14  ? 82   VAL A C   1 
ATOM   4555  O O   . VAL C  1 77  ? 22.625  -21.217 -26.254 1.00 39.84  ? 82   VAL A O   1 
ATOM   4556  C CB  . VAL C  1 77  ? 25.404  -19.873 -25.475 1.00 35.63  ? 82   VAL A CB  1 
ATOM   4557  C CG1 . VAL C  1 77  ? 26.392  -18.747 -25.653 1.00 32.46  ? 82   VAL A CG1 1 
ATOM   4558  C CG2 . VAL C  1 77  ? 24.364  -19.555 -24.363 1.00 29.51  ? 82   VAL A CG2 1 
ATOM   4559  N N   . PRO C  1 78  ? 24.321  -22.598 -26.843 1.00 35.05  ? 83   PRO A N   1 
ATOM   4560  C CA  . PRO C  1 78  ? 23.461  -23.757 -26.613 1.00 35.81  ? 83   PRO A CA  1 
ATOM   4561  C C   . PRO C  1 78  ? 23.332  -24.016 -25.128 1.00 40.31  ? 83   PRO A C   1 
ATOM   4562  O O   . PRO C  1 78  ? 24.080  -23.431 -24.325 1.00 35.32  ? 83   PRO A O   1 
ATOM   4563  C CB  . PRO C  1 78  ? 24.219  -24.893 -27.283 1.00 33.32  ? 83   PRO A CB  1 
ATOM   4564  C CG  . PRO C  1 78  ? 25.673  -24.479 -27.137 1.00 35.39  ? 83   PRO A CG  1 
ATOM   4565  C CD  . PRO C  1 78  ? 25.679  -22.976 -27.275 1.00 33.06  ? 83   PRO A CD  1 
ATOM   4566  N N   . GLU C  1 79  A 22.408  -24.916 -24.803 1.00 46.36  ? 83   GLU A N   1 
ATOM   4567  C CA  . GLU C  1 79  A 22.109  -25.378 -23.449 1.00 42.15  ? 83   GLU A CA  1 
ATOM   4568  C C   . GLU C  1 79  A 23.394  -25.755 -22.695 1.00 38.34  ? 83   GLU A C   1 
ATOM   4569  O O   . GLU C  1 79  A 24.303  -26.392 -23.245 1.00 41.39  ? 83   GLU A O   1 
ATOM   4570  C CB  . GLU C  1 79  A 21.128  -26.565 -23.555 1.00 43.94  ? 83   GLU A CB  1 
ATOM   4571  C CG  . GLU C  1 79  A 20.699  -27.246 -22.259 1.00 55.22  ? 83   GLU A CG  1 
ATOM   4572  C CD  . GLU C  1 79  A 19.625  -28.334 -22.474 1.00 60.55  ? 83   GLU A CD  1 
ATOM   4573  O OE1 . GLU C  1 79  A 19.119  -28.474 -23.611 1.00 56.57  ? 83   GLU A OE1 1 
ATOM   4574  O OE2 . GLU C  1 79  A 19.274  -29.027 -21.486 1.00 67.36  ? 83   GLU A OE2 1 
ATOM   4575  N N   . TRP C  1 80  ? 23.485  -25.359 -21.437 1.00 36.23  ? 84   TRP A N   1 
ATOM   4576  C CA  . TRP C  1 80  ? 24.704  -25.630 -20.694 1.00 40.75  ? 84   TRP A CA  1 
ATOM   4577  C C   . TRP C  1 80  ? 24.427  -26.448 -19.423 1.00 39.15  ? 84   TRP A C   1 
ATOM   4578  O O   . TRP C  1 80  ? 23.277  -26.558 -18.980 1.00 43.31  ? 84   TRP A O   1 
ATOM   4579  C CB  . TRP C  1 80  ? 25.397  -24.313 -20.342 1.00 36.88  ? 84   TRP A CB  1 
ATOM   4580  C CG  . TRP C  1 80  ? 24.534  -23.453 -19.461 1.00 40.92  ? 84   TRP A CG  1 
ATOM   4581  C CD1 . TRP C  1 80  ? 24.374  -23.561 -18.105 1.00 44.34  ? 84   TRP A CD1 1 
ATOM   4582  C CD2 . TRP C  1 80  ? 23.711  -22.347 -19.873 1.00 40.19  ? 84   TRP A CD2 1 
ATOM   4583  N NE1 . TRP C  1 80  ? 23.495  -22.599 -17.653 1.00 44.62  ? 84   TRP A NE1 1 
ATOM   4584  C CE2 . TRP C  1 80  ? 23.081  -21.838 -18.718 1.00 41.33  ? 84   TRP A CE2 1 
ATOM   4585  C CE3 . TRP C  1 80  ? 23.443  -21.742 -21.105 1.00 35.61  ? 84   TRP A CE3 1 
ATOM   4586  C CZ2 . TRP C  1 80  ? 22.201  -20.756 -18.764 1.00 38.35  ? 84   TRP A CZ2 1 
ATOM   4587  C CZ3 . TRP C  1 80  ? 22.572  -20.669 -21.141 1.00 39.50  ? 84   TRP A CZ3 1 
ATOM   4588  C CH2 . TRP C  1 80  ? 21.960  -20.189 -19.980 1.00 36.45  ? 84   TRP A CH2 1 
ATOM   4589  N N   . SER C  1 81  ? 25.490  -26.990 -18.831 1.00 37.83  ? 85   SER A N   1 
ATOM   4590  C CA  . SER C  1 81  ? 25.385  -27.769 -17.590 1.00 42.66  ? 85   SER A CA  1 
ATOM   4591  C C   . SER C  1 81  ? 25.835  -26.930 -16.396 1.00 46.72  ? 85   SER A C   1 
ATOM   4592  O O   . SER C  1 81  ? 25.259  -27.005 -15.321 1.00 52.45  ? 85   SER A O   1 
ATOM   4593  C CB  . SER C  1 81  ? 26.233  -29.045 -17.665 1.00 44.63  ? 85   SER A CB  1 
ATOM   4594  O OG  . SER C  1 81  ? 27.580  -28.742 -18.020 1.00 45.29  ? 85   SER A OG  1 
ATOM   4595  N N   . TYR C  1 82  ? 26.852  -26.105 -16.604 1.00 45.72  ? 86   TYR A N   1 
ATOM   4596  C CA  . TYR C  1 82  ? 27.280  -25.155 -15.594 1.00 40.07  ? 86   TYR A CA  1 
ATOM   4597  C C   . TYR C  1 82  ? 28.050  -24.070 -16.325 1.00 40.37  ? 86   TYR A C   1 
ATOM   4598  O O   . TYR C  1 82  ? 28.310  -24.211 -17.530 1.00 42.87  ? 86   TYR A O   1 
ATOM   4599  C CB  . TYR C  1 82  ? 28.129  -25.837 -14.517 1.00 40.43  ? 86   TYR A CB  1 
ATOM   4600  C CG  . TYR C  1 82  ? 29.449  -26.421 -14.985 1.00 42.73  ? 86   TYR A CG  1 
ATOM   4601  C CD1 . TYR C  1 82  ? 29.491  -27.679 -15.610 1.00 39.84  ? 86   TYR A CD1 1 
ATOM   4602  C CD2 . TYR C  1 82  ? 30.669  -25.759 -14.728 1.00 36.92  ? 86   TYR A CD2 1 
ATOM   4603  C CE1 . TYR C  1 82  ? 30.704  -28.247 -16.029 1.00 37.97  ? 86   TYR A CE1 1 
ATOM   4604  C CE2 . TYR C  1 82  ? 31.889  -26.319 -15.133 1.00 38.29  ? 86   TYR A CE2 1 
ATOM   4605  C CZ  . TYR C  1 82  ? 31.898  -27.568 -15.790 1.00 43.47  ? 86   TYR A CZ  1 
ATOM   4606  O OH  . TYR C  1 82  ? 33.089  -28.150 -16.206 1.00 38.33  ? 86   TYR A OH  1 
ATOM   4607  N N   . ILE C  1 83  ? 28.412  -23.005 -15.613 1.00 37.40  ? 87   ILE A N   1 
ATOM   4608  C CA  . ILE C  1 83  ? 29.069  -21.841 -16.209 1.00 34.60  ? 87   ILE A CA  1 
ATOM   4609  C C   . ILE C  1 83  ? 30.429  -21.631 -15.548 1.00 36.12  ? 87   ILE A C   1 
ATOM   4610  O O   . ILE C  1 83  ? 30.542  -21.787 -14.325 1.00 39.33  ? 87   ILE A O   1 
ATOM   4611  C CB  . ILE C  1 83  ? 28.187  -20.575 -16.056 1.00 33.32  ? 87   ILE A CB  1 
ATOM   4612  C CG1 . ILE C  1 83  ? 26.847  -20.772 -16.759 1.00 37.38  ? 87   ILE A CG1 1 
ATOM   4613  C CG2 . ILE C  1 83  ? 28.861  -19.352 -16.607 1.00 32.51  ? 87   ILE A CG2 1 
ATOM   4614  C CD1 . ILE C  1 83  ? 25.912  -19.592 -16.647 1.00 36.66  ? 87   ILE A CD1 1 
ATOM   4615  N N   . VAL C  1 84  ? 31.455  -21.319 -16.351 1.00 37.64  ? 88   VAL A N   1 
ATOM   4616  C CA  . VAL C  1 84  ? 32.825  -21.055 -15.857 1.00 38.88  ? 88   VAL A CA  1 
ATOM   4617  C C   . VAL C  1 84  ? 33.273  -19.626 -16.185 1.00 36.42  ? 88   VAL A C   1 
ATOM   4618  O O   . VAL C  1 84  ? 33.175  -19.186 -17.322 1.00 34.59  ? 88   VAL A O   1 
ATOM   4619  C CB  . VAL C  1 84  ? 33.862  -22.058 -16.450 1.00 40.42  ? 88   VAL A CB  1 
ATOM   4620  C CG1 . VAL C  1 84  ? 35.273  -21.720 -15.981 1.00 39.15  ? 88   VAL A CG1 1 
ATOM   4621  C CG2 . VAL C  1 84  ? 33.506  -23.504 -16.089 1.00 38.96  ? 88   VAL A CG2 1 
ATOM   4622  N N   . GLU C  1 85  ? 33.776  -18.915 -15.179 1.00 41.70  ? 89   GLU A N   1 
ATOM   4623  C CA  . GLU C  1 85  ? 34.137  -17.503 -15.303 1.00 37.09  ? 89   GLU A CA  1 
ATOM   4624  C C   . GLU C  1 85  ? 35.446  -17.217 -14.594 1.00 39.91  ? 89   GLU A C   1 
ATOM   4625  O O   . GLU C  1 85  ? 35.702  -17.797 -13.548 1.00 53.43  ? 89   GLU A O   1 
ATOM   4626  C CB  . GLU C  1 85  ? 33.011  -16.635 -14.722 1.00 37.10  ? 89   GLU A CB  1 
ATOM   4627  C CG  . GLU C  1 85  ? 33.174  -15.123 -14.887 1.00 42.24  ? 89   GLU A CG  1 
ATOM   4628  C CD  . GLU C  1 85  ? 32.134  -14.339 -14.088 1.00 43.19  ? 89   GLU A CD  1 
ATOM   4629  O OE1 . GLU C  1 85  ? 32.018  -14.603 -12.865 1.00 43.00  ? 89   GLU A OE1 1 
ATOM   4630  O OE2 . GLU C  1 85  ? 31.424  -13.489 -14.695 1.00 35.41  ? 89   GLU A OE2 1 
ATOM   4631  N N   . LYS C  1 86  ? 36.275  -16.327 -15.129 1.00 44.32  ? 90   LYS A N   1 
ATOM   4632  C CA  . LYS C  1 86  ? 37.538  -15.966 -14.465 1.00 48.29  ? 90   LYS A CA  1 
ATOM   4633  C C   . LYS C  1 86  ? 37.307  -15.007 -13.299 1.00 48.15  ? 90   LYS A C   1 
ATOM   4634  O O   . LYS C  1 86  ? 36.211  -14.470 -13.138 1.00 48.98  ? 90   LYS A O   1 
ATOM   4635  C CB  . LYS C  1 86  ? 38.525  -15.342 -15.459 1.00 45.16  ? 90   LYS A CB  1 
ATOM   4636  C CG  . LYS C  1 86  ? 39.249  -16.365 -16.337 1.00 46.61  ? 90   LYS A CG  1 
ATOM   4637  C CD  . LYS C  1 86  ? 40.118  -15.658 -17.360 1.00 48.61  ? 90   LYS A CD  1 
ATOM   4638  C CE  . LYS C  1 86  ? 41.016  -16.599 -18.183 1.00 55.18  ? 90   LYS A CE  1 
ATOM   4639  N NZ  . LYS C  1 86  ? 40.291  -17.591 -19.024 1.00 52.85  ? 90   LYS A NZ  1 
ATOM   4640  N N   . ILE C  1 87  ? 38.335  -14.823 -12.474 1.00 50.32  ? 91   ILE A N   1 
ATOM   4641  C CA  . ILE C  1 87  ? 38.252  -13.960 -11.301 1.00 49.49  ? 91   ILE A CA  1 
ATOM   4642  C C   . ILE C  1 87  ? 38.100  -12.514 -11.719 1.00 50.22  ? 91   ILE A C   1 
ATOM   4643  O O   . ILE C  1 87  ? 37.319  -11.770 -11.137 1.00 55.40  ? 91   ILE A O   1 
ATOM   4644  C CB  . ILE C  1 87  ? 39.505  -14.041 -10.396 1.00 51.55  ? 91   ILE A CB  1 
ATOM   4645  C CG1 . ILE C  1 87  ? 40.310  -15.308 -10.657 1.00 55.75  ? 91   ILE A CG1 1 
ATOM   4646  C CG2 . ILE C  1 87  ? 39.118  -13.925 -8.946  1.00 52.41  ? 91   ILE A CG2 1 
ATOM   4647  C CD1 . ILE C  1 87  ? 41.783  -15.173 -10.289 1.00 54.50  ? 91   ILE A CD1 1 
ATOM   4648  N N   . ASN C  1 88  ? 38.897  -12.108 -12.700 1.00 46.45  ? 92   ASN A N   1 
ATOM   4649  C CA  . ASN C  1 88  ? 38.876  -10.722 -13.166 1.00 54.55  ? 92   ASN A CA  1 
ATOM   4650  C C   . ASN C  1 88  ? 38.788  -10.623 -14.710 1.00 48.81  ? 92   ASN A C   1 
ATOM   4651  O O   . ASN C  1 88  ? 39.758  -10.232 -15.361 1.00 49.64  ? 92   ASN A O   1 
ATOM   4652  C CB  . ASN C  1 88  ? 40.138  -10.013 -12.640 1.00 58.69  ? 92   ASN A CB  1 
ATOM   4653  C CG  . ASN C  1 88  ? 40.111  -8.498  -12.819 1.00 68.56  ? 92   ASN A CG  1 
ATOM   4654  O OD1 . ASN C  1 88  ? 39.046  -7.865  -12.833 1.00 69.69  ? 92   ASN A OD1 1 
ATOM   4655  N ND2 . ASN C  1 88  ? 41.301  -7.906  -12.952 1.00 69.61  ? 92   ASN A ND2 1 
ATOM   4656  N N   . PRO C  1 89  ? 37.627  -10.976 -15.298 1.00 41.66  ? 93   PRO A N   1 
ATOM   4657  C CA  . PRO C  1 89  ? 37.490  -10.999 -16.759 1.00 41.93  ? 93   PRO A CA  1 
ATOM   4658  C C   . PRO C  1 89  ? 37.779  -9.631  -17.391 1.00 42.68  ? 93   PRO A C   1 
ATOM   4659  O O   . PRO C  1 89  ? 37.581  -8.609  -16.746 1.00 44.02  ? 93   PRO A O   1 
ATOM   4660  C CB  . PRO C  1 89  ? 36.024  -11.422 -16.974 1.00 40.32  ? 93   PRO A CB  1 
ATOM   4661  C CG  . PRO C  1 89  ? 35.646  -12.145 -15.716 1.00 40.13  ? 93   PRO A CG  1 
ATOM   4662  C CD  . PRO C  1 89  ? 36.379  -11.388 -14.630 1.00 43.39  ? 93   PRO A CD  1 
ATOM   4663  N N   . ALA C  1 90  ? 38.270  -9.626  -18.625 1.00 44.88  ? 94   ALA A N   1 
ATOM   4664  C CA  . ALA C  1 90  ? 38.674  -8.396  -19.318 1.00 43.38  ? 94   ALA A CA  1 
ATOM   4665  C C   . ALA C  1 90  ? 37.497  -7.746  -20.066 1.00 37.74  ? 94   ALA A C   1 
ATOM   4666  O O   . ALA C  1 90  ? 37.516  -6.539  -20.344 1.00 34.94  ? 94   ALA A O   1 
ATOM   4667  C CB  . ALA C  1 90  ? 39.839  -8.677  -20.291 1.00 46.69  ? 94   ALA A CB  1 
ATOM   4668  N N   . ASN C  1 91  ? 36.540  -8.561  -20.501 1.00 33.62  ? 95   ASN A N   1 
ATOM   4669  C CA  . ASN C  1 91  ? 35.376  -8.019  -21.197 1.00 37.28  ? 95   ASN A CA  1 
ATOM   4670  C C   . ASN C  1 91  ? 34.128  -8.027  -20.319 1.00 39.02  ? 95   ASN A C   1 
ATOM   4671  O O   . ASN C  1 91  ? 33.416  -9.054  -20.204 1.00 36.41  ? 95   ASN A O   1 
ATOM   4672  C CB  . ASN C  1 91  ? 35.142  -8.789  -22.474 1.00 36.84  ? 95   ASN A CB  1 
ATOM   4673  C CG  . ASN C  1 91  ? 36.349  -8.776  -23.350 1.00 37.68  ? 95   ASN A CG  1 
ATOM   4674  O OD1 . ASN C  1 91  ? 37.022  -7.736  -23.515 1.00 31.37  ? 95   ASN A OD1 1 
ATOM   4675  N ND2 . ASN C  1 91  ? 36.688  -9.952  -23.870 1.00 36.81  ? 95   ASN A ND2 1 
ATOM   4676  N N   . ASP C  1 92  ? 33.897  -6.877  -19.687 1.00 37.53  ? 96   ASP A N   1 
ATOM   4677  C CA  . ASP C  1 92  ? 32.829  -6.687  -18.723 1.00 32.95  ? 96   ASP A CA  1 
ATOM   4678  C C   . ASP C  1 92  ? 31.934  -5.572  -19.267 1.00 32.25  ? 96   ASP A C   1 
ATOM   4679  O O   . ASP C  1 92  ? 31.575  -5.601  -20.448 1.00 32.56  ? 96   ASP A O   1 
ATOM   4680  C CB  . ASP C  1 92  ? 33.432  -6.324  -17.359 1.00 34.38  ? 96   ASP A CB  1 
ATOM   4681  C CG  . ASP C  1 92  ? 32.397  -6.281  -16.229 1.00 34.41  ? 96   ASP A CG  1 
ATOM   4682  O OD1 . ASP C  1 92  ? 31.603  -7.234  -16.083 1.00 33.36  ? 96   ASP A OD1 1 
ATOM   4683  O OD2 . ASP C  1 92  ? 32.357  -5.247  -15.517 1.00 32.09  ? 96   ASP A OD2 1 
ATOM   4684  N N   . LEU C  1 93  A 31.666  -4.547  -18.455 1.00 31.00  ? 96   LEU A N   1 
ATOM   4685  C CA  . LEU C  1 93  A 30.993  -3.340  -18.932 1.00 34.67  ? 96   LEU A CA  1 
ATOM   4686  C C   . LEU C  1 93  A 32.034  -2.455  -19.640 1.00 33.67  ? 96   LEU A C   1 
ATOM   4687  O O   . LEU C  1 93  A 32.905  -1.855  -18.994 1.00 31.31  ? 96   LEU A O   1 
ATOM   4688  C CB  . LEU C  1 93  A 30.332  -2.581  -17.774 1.00 29.59  ? 96   LEU A CB  1 
ATOM   4689  C CG  . LEU C  1 93  A 29.280  -3.333  -16.958 1.00 30.53  ? 96   LEU A CG  1 
ATOM   4690  C CD1 . LEU C  1 93  A 28.931  -2.558  -15.681 1.00 25.67  ? 96   LEU A CD1 1 
ATOM   4691  C CD2 . LEU C  1 93  A 28.050  -3.570  -17.782 1.00 20.75  ? 96   LEU A CD2 1 
ATOM   4692  N N   . CYS C  1 94  ? 31.957  -2.408  -20.967 1.00 26.93  ? 97   CYS A N   1 
ATOM   4693  C CA  . CYS C  1 94  ? 32.949  -1.693  -21.755 1.00 30.44  ? 97   CYS A CA  1 
ATOM   4694  C C   . CYS C  1 94  ? 32.773  -0.171  -21.603 1.00 30.63  ? 97   CYS A C   1 
ATOM   4695  O O   . CYS C  1 94  ? 33.752  0.562   -21.501 1.00 32.98  ? 97   CYS A O   1 
ATOM   4696  C CB  . CYS C  1 94  ? 32.880  -2.133  -23.225 1.00 31.58  ? 97   CYS A CB  1 
ATOM   4697  S SG  . CYS C  1 94  ? 31.185  -2.143  -23.971 1.00 29.37  ? 97   CYS A SG  1 
ATOM   4698  N N   . TYR C  1 95  ? 31.531  0.307   -21.588 1.00 27.79  ? 98   TYR A N   1 
ATOM   4699  C CA  . TYR C  1 95  ? 31.269  1.696   -21.211 1.00 25.89  ? 98   TYR A CA  1 
ATOM   4700  C C   . TYR C  1 95  ? 31.211  1.768   -19.686 1.00 29.91  ? 98   TYR A C   1 
ATOM   4701  O O   . TYR C  1 95  ? 30.490  0.991   -19.061 1.00 32.99  ? 98   TYR A O   1 
ATOM   4702  C CB  . TYR C  1 95  ? 29.959  2.191   -21.829 1.00 24.55  ? 98   TYR A CB  1 
ATOM   4703  C CG  . TYR C  1 95  ? 29.841  3.696   -21.847 1.00 31.19  ? 98   TYR A CG  1 
ATOM   4704  C CD1 . TYR C  1 95  ? 29.700  4.420   -20.651 1.00 26.76  ? 98   TYR A CD1 1 
ATOM   4705  C CD2 . TYR C  1 95  ? 29.879  4.406   -23.047 1.00 24.61  ? 98   TYR A CD2 1 
ATOM   4706  C CE1 . TYR C  1 95  ? 29.592  5.799   -20.653 1.00 25.35  ? 98   TYR A CE1 1 
ATOM   4707  C CE2 . TYR C  1 95  ? 29.787  5.795   -23.058 1.00 25.76  ? 98   TYR A CE2 1 
ATOM   4708  C CZ  . TYR C  1 95  ? 29.647  6.486   -21.863 1.00 28.75  ? 98   TYR A CZ  1 
ATOM   4709  O OH  . TYR C  1 95  ? 29.529  7.864   -21.878 1.00 26.47  ? 98   TYR A OH  1 
ATOM   4710  N N   . PRO C  1 96  ? 31.996  2.670   -19.070 1.00 30.97  ? 99   PRO A N   1 
ATOM   4711  C CA  . PRO C  1 96  ? 32.051  2.626   -17.596 1.00 24.29  ? 99   PRO A CA  1 
ATOM   4712  C C   . PRO C  1 96  ? 30.699  2.899   -16.909 1.00 25.35  ? 99   PRO A C   1 
ATOM   4713  O O   . PRO C  1 96  ? 29.937  3.765   -17.360 1.00 23.07  ? 99   PRO A O   1 
ATOM   4714  C CB  . PRO C  1 96  ? 33.073  3.727   -17.241 1.00 21.46  ? 99   PRO A CB  1 
ATOM   4715  C CG  . PRO C  1 96  ? 33.130  4.637   -18.471 1.00 28.57  ? 99   PRO A CG  1 
ATOM   4716  C CD  . PRO C  1 96  ? 32.863  3.723   -19.650 1.00 30.31  ? 99   PRO A CD  1 
ATOM   4717  N N   . GLY C  1 97  ? 30.441  2.217   -15.788 1.00 24.43  ? 100  GLY A N   1 
ATOM   4718  C CA  . GLY C  1 97  ? 29.194  2.396   -15.053 1.00 25.49  ? 100  GLY A CA  1 
ATOM   4719  C C   . GLY C  1 97  ? 28.879  1.209   -14.143 1.00 34.77  ? 100  GLY A C   1 
ATOM   4720  O O   . GLY C  1 97  ? 29.810  0.589   -13.596 1.00 34.15  ? 100  GLY A O   1 
ATOM   4721  N N   . ASN C  1 98  ? 27.593  0.873   -13.975 1.00 28.46  ? 101  ASN A N   1 
ATOM   4722  C CA  . ASN C  1 98  ? 27.217  -0.210  -13.058 1.00 30.71  ? 101  ASN A CA  1 
ATOM   4723  C C   . ASN C  1 98  ? 25.981  -0.957  -13.548 1.00 31.44  ? 101  ASN A C   1 
ATOM   4724  O O   . ASN C  1 98  ? 25.243  -0.456  -14.403 1.00 26.30  ? 101  ASN A O   1 
ATOM   4725  C CB  . ASN C  1 98  ? 26.989  0.352   -11.646 1.00 25.47  ? 101  ASN A CB  1 
ATOM   4726  C CG  . ASN C  1 98  ? 25.769  1.275   -11.574 1.00 30.97  ? 101  ASN A CG  1 
ATOM   4727  O OD1 . ASN C  1 98  ? 25.731  2.307   -12.252 1.00 33.76  ? 101  ASN A OD1 1 
ATOM   4728  N ND2 . ASN C  1 98  ? 24.814  0.959   -10.695 1.00 26.67  ? 101  ASN A ND2 1 
ATOM   4729  N N   . PHE C  1 99  ? 25.817  -2.174  -13.022 1.00 27.56  ? 102  PHE A N   1 
ATOM   4730  C CA  . PHE C  1 99  ? 24.760  -3.119  -13.371 1.00 25.40  ? 102  PHE A CA  1 
ATOM   4731  C C   . PHE C  1 99  ? 23.953  -3.437  -12.118 1.00 32.44  ? 102  PHE A C   1 
ATOM   4732  O O   . PHE C  1 99  ? 24.384  -4.194  -11.255 1.00 34.90  ? 102  PHE A O   1 
ATOM   4733  C CB  . PHE C  1 99  ? 25.372  -4.393  -13.960 1.00 27.35  ? 102  PHE A CB  1 
ATOM   4734  C CG  . PHE C  1 99  ? 24.410  -5.273  -14.715 1.00 27.60  ? 102  PHE A CG  1 
ATOM   4735  C CD1 . PHE C  1 99  ? 23.401  -5.961  -14.055 1.00 36.09  ? 102  PHE A CD1 1 
ATOM   4736  C CD2 . PHE C  1 99  ? 24.564  -5.491  -16.057 1.00 26.09  ? 102  PHE A CD2 1 
ATOM   4737  C CE1 . PHE C  1 99  ? 22.525  -6.811  -14.764 1.00 35.26  ? 102  PHE A CE1 1 
ATOM   4738  C CE2 . PHE C  1 99  ? 23.701  -6.325  -16.746 1.00 26.59  ? 102  PHE A CE2 1 
ATOM   4739  C CZ  . PHE C  1 99  ? 22.688  -6.975  -16.110 1.00 21.60  ? 102  PHE A CZ  1 
ATOM   4740  N N   . ASN C  1 100 ? 22.756  -2.898  -12.046 1.00 36.29  ? 103  ASN A N   1 
ATOM   4741  C CA  . ASN C  1 100 ? 21.903  -3.007  -10.872 1.00 31.30  ? 103  ASN A CA  1 
ATOM   4742  C C   . ASN C  1 100 ? 21.482  -4.421  -10.439 1.00 29.44  ? 103  ASN A C   1 
ATOM   4743  O O   . ASN C  1 100 ? 21.024  -5.208  -11.266 1.00 27.84  ? 103  ASN A O   1 
ATOM   4744  C CB  . ASN C  1 100 ? 20.655  -2.225  -11.187 1.00 33.29  ? 103  ASN A CB  1 
ATOM   4745  C CG  . ASN C  1 100 ? 20.153  -1.498  -10.044 1.00 34.62  ? 103  ASN A CG  1 
ATOM   4746  O OD1 . ASN C  1 100 ? 20.663  -0.421  -9.711  1.00 35.75  ? 103  ASN A OD1 1 
ATOM   4747  N ND2 . ASN C  1 100 ? 19.147  -2.071  -9.388  1.00 35.32  ? 103  ASN A ND2 1 
ATOM   4748  N N   . ASP C  1 101 ? 21.587  -4.728  -9.146  1.00 35.11  ? 104  ASP A N   1 
ATOM   4749  C CA  . ASP C  1 101 ? 21.170  -6.044  -8.622  1.00 34.49  ? 104  ASP A CA  1 
ATOM   4750  C C   . ASP C  1 101 ? 21.836  -7.194  -9.364  1.00 31.70  ? 104  ASP A C   1 
ATOM   4751  O O   . ASP C  1 101 ? 21.210  -8.247  -9.615  1.00 26.21  ? 104  ASP A O   1 
ATOM   4752  C CB  . ASP C  1 101 ? 19.640  -6.216  -8.705  1.00 29.83  ? 104  ASP A CB  1 
ATOM   4753  C CG  . ASP C  1 101 ? 18.908  -5.513  -7.569  1.00 39.64  ? 104  ASP A CG  1 
ATOM   4754  O OD1 . ASP C  1 101 ? 19.425  -5.520  -6.430  1.00 46.90  ? 104  ASP A OD1 1 
ATOM   4755  O OD2 . ASP C  1 101 ? 17.818  -4.953  -7.813  1.00 41.78  ? 104  ASP A OD2 1 
ATOM   4756  N N   . TYR C  1 102 ? 23.103  -6.979  -9.712  1.00 28.55  ? 105  TYR A N   1 
ATOM   4757  C CA  . TYR C  1 102 ? 23.869  -7.952  -10.485 1.00 27.72  ? 105  TYR A CA  1 
ATOM   4758  C C   . TYR C  1 102 ? 23.959  -9.304  -9.791  1.00 26.84  ? 105  TYR A C   1 
ATOM   4759  O O   . TYR C  1 102 ? 23.759  -10.345 -10.442 1.00 24.25  ? 105  TYR A O   1 
ATOM   4760  C CB  . TYR C  1 102 ? 25.276  -7.401  -10.765 1.00 24.49  ? 105  TYR A CB  1 
ATOM   4761  C CG  . TYR C  1 102 ? 26.126  -8.185  -11.742 1.00 24.59  ? 105  TYR A CG  1 
ATOM   4762  C CD1 . TYR C  1 102 ? 25.648  -8.579  -12.983 1.00 22.14  ? 105  TYR A CD1 1 
ATOM   4763  C CD2 . TYR C  1 102 ? 27.441  -8.500  -11.422 1.00 27.08  ? 105  TYR A CD2 1 
ATOM   4764  C CE1 . TYR C  1 102 ? 26.461  -9.278  -13.867 1.00 21.07  ? 105  TYR A CE1 1 
ATOM   4765  C CE2 . TYR C  1 102 ? 28.249  -9.188  -12.293 1.00 23.75  ? 105  TYR A CE2 1 
ATOM   4766  C CZ  . TYR C  1 102 ? 27.765  -9.567  -13.515 1.00 24.66  ? 105  TYR A CZ  1 
ATOM   4767  O OH  . TYR C  1 102 ? 28.614  -10.263 -14.354 1.00 24.61  ? 105  TYR A OH  1 
ATOM   4768  N N   . GLU C  1 103 ? 24.216  -9.293  -8.472  1.00 25.37  ? 106  GLU A N   1 
ATOM   4769  C CA  . GLU C  1 103 ? 24.465  -10.547 -7.764  1.00 23.44  ? 106  GLU A CA  1 
ATOM   4770  C C   . GLU C  1 103 ? 23.188  -11.358 -7.628  1.00 24.46  ? 106  GLU A C   1 
ATOM   4771  O O   . GLU C  1 103 ? 23.219  -12.586 -7.740  1.00 24.85  ? 106  GLU A O   1 
ATOM   4772  C CB  . GLU C  1 103 ? 25.094  -10.302 -6.386  1.00 21.96  ? 106  GLU A CB  1 
ATOM   4773  C CG  . GLU C  1 103 ? 26.556  -9.876  -6.407  1.00 20.47  ? 106  GLU A CG  1 
ATOM   4774  C CD  . GLU C  1 103 ? 26.724  -8.393  -6.759  1.00 28.39  ? 106  GLU A CD  1 
ATOM   4775  O OE1 . GLU C  1 103 ? 25.808  -7.607  -6.435  1.00 29.29  ? 106  GLU A OE1 1 
ATOM   4776  O OE2 . GLU C  1 103 ? 27.757  -8.005  -7.359  1.00 29.38  ? 106  GLU A OE2 1 
ATOM   4777  N N   . GLU C  1 104 ? 22.055  -10.677 -7.467  1.00 26.47  ? 107  GLU A N   1 
ATOM   4778  C CA  . GLU C  1 104 ? 20.757  -11.373 -7.443  1.00 28.22  ? 107  GLU A CA  1 
ATOM   4779  C C   . GLU C  1 104 ? 20.435  -12.025 -8.798  1.00 30.02  ? 107  GLU A C   1 
ATOM   4780  O O   . GLU C  1 104 ? 19.921  -13.156 -8.835  1.00 26.72  ? 107  GLU A O   1 
ATOM   4781  C CB  . GLU C  1 104 ? 19.625  -10.392 -7.044  1.00 26.74  ? 107  GLU A CB  1 
ATOM   4782  C CG  . GLU C  1 104 ? 19.480  -10.127 -5.533  1.00 25.96  ? 107  GLU A CG  1 
ATOM   4783  C CD  . GLU C  1 104 ? 18.882  -11.330 -4.748  1.00 28.17  ? 107  GLU A CD  1 
ATOM   4784  O OE1 . GLU C  1 104 ? 17.783  -11.840 -5.136  1.00 27.47  ? 107  GLU A OE1 1 
ATOM   4785  O OE2 . GLU C  1 104 ? 19.538  -11.788 -3.776  1.00 26.82  ? 107  GLU A OE2 1 
ATOM   4786  N N   . LEU C  1 105 ? 20.787  -11.338 -9.897  1.00 30.24  ? 108  LEU A N   1 
ATOM   4787  C CA  . LEU C  1 105 ? 20.589  -11.887 -11.235 1.00 24.69  ? 108  LEU A CA  1 
ATOM   4788  C C   . LEU C  1 105 ? 21.483  -13.100 -11.477 1.00 30.91  ? 108  LEU A C   1 
ATOM   4789  O O   . LEU C  1 105 ? 21.051  -14.061 -12.134 1.00 28.88  ? 108  LEU A O   1 
ATOM   4790  C CB  . LEU C  1 105 ? 20.827  -10.817 -12.319 1.00 26.98  ? 108  LEU A CB  1 
ATOM   4791  C CG  . LEU C  1 105 ? 20.820  -11.296 -13.795 1.00 26.35  ? 108  LEU A CG  1 
ATOM   4792  C CD1 . LEU C  1 105 ? 19.443  -11.864 -14.209 1.00 21.18  ? 108  LEU A CD1 1 
ATOM   4793  C CD2 . LEU C  1 105 ? 21.289  -10.207 -14.795 1.00 18.92  ? 108  LEU A CD2 1 
ATOM   4794  N N   . LYS C  1 106 ? 22.729  -13.051 -10.997 1.00 27.11  ? 109  LYS A N   1 
ATOM   4795  C CA  . LYS C  1 106 ? 23.631  -14.192 -11.150 1.00 27.36  ? 109  LYS A CA  1 
ATOM   4796  C C   . LYS C  1 106 ? 23.059  -15.396 -10.366 1.00 29.04  ? 109  LYS A C   1 
ATOM   4797  O O   . LYS C  1 106 ? 23.199  -16.549 -10.782 1.00 33.59  ? 109  LYS A O   1 
ATOM   4798  C CB  . LYS C  1 106 ? 25.057  -13.842 -10.676 1.00 31.90  ? 109  LYS A CB  1 
ATOM   4799  C CG  . LYS C  1 106 ? 26.048  -13.174 -11.704 1.00 26.47  ? 109  LYS A CG  1 
ATOM   4800  C CD  . LYS C  1 106 ? 27.212  -12.560 -10.883 1.00 31.25  ? 109  LYS A CD  1 
ATOM   4801  C CE  . LYS C  1 106 ? 28.568  -12.411 -11.559 1.00 31.43  ? 109  LYS A CE  1 
ATOM   4802  N NZ  . LYS C  1 106 ? 29.381  -13.654 -11.641 1.00 35.04  ? 109  LYS A NZ  1 
ATOM   4803  N N   . HIS C  1 107 ? 22.396  -15.129 -9.240  1.00 32.83  ? 110  HIS A N   1 
ATOM   4804  C CA  . HIS C  1 107 ? 21.802  -16.205 -8.423  1.00 33.84  ? 110  HIS A CA  1 
ATOM   4805  C C   . HIS C  1 107 ? 20.628  -16.863 -9.130  1.00 29.68  ? 110  HIS A C   1 
ATOM   4806  O O   . HIS C  1 107 ? 20.448  -18.077 -9.083  1.00 27.92  ? 110  HIS A O   1 
ATOM   4807  C CB  . HIS C  1 107 ? 21.348  -15.681 -7.046  1.00 28.64  ? 110  HIS A CB  1 
ATOM   4808  C CG  . HIS C  1 107 ? 20.596  -16.695 -6.235  1.00 28.31  ? 110  HIS A CG  1 
ATOM   4809  N ND1 . HIS C  1 107 ? 21.211  -17.572 -5.367  1.00 32.73  ? 110  HIS A ND1 1 
ATOM   4810  C CD2 . HIS C  1 107 ? 19.271  -16.965 -6.157  1.00 28.67  ? 110  HIS A CD2 1 
ATOM   4811  C CE1 . HIS C  1 107 ? 20.302  -18.347 -4.806  1.00 31.49  ? 110  HIS A CE1 1 
ATOM   4812  N NE2 . HIS C  1 107 ? 19.115  -18.002 -5.272  1.00 27.38  ? 110  HIS A NE2 1 
ATOM   4813  N N   . LEU C  1 108 ? 19.838  -16.035 -9.789  1.00 30.73  ? 111  LEU A N   1 
ATOM   4814  C CA  . LEU C  1 108 ? 18.693  -16.487 -10.583 1.00 35.03  ? 111  LEU A CA  1 
ATOM   4815  C C   . LEU C  1 108 ? 19.185  -17.442 -11.706 1.00 34.77  ? 111  LEU A C   1 
ATOM   4816  O O   . LEU C  1 108 ? 18.550  -18.451 -12.059 1.00 34.44  ? 111  LEU A O   1 
ATOM   4817  C CB  . LEU C  1 108 ? 17.976  -15.248 -11.144 1.00 35.01  ? 111  LEU A CB  1 
ATOM   4818  C CG  . LEU C  1 108 ? 16.487  -15.268 -11.428 1.00 34.64  ? 111  LEU A CG  1 
ATOM   4819  C CD1 . LEU C  1 108 ? 15.845  -15.583 -10.117 1.00 27.85  ? 111  LEU A CD1 1 
ATOM   4820  C CD2 . LEU C  1 108 ? 16.015  -13.916 -11.918 1.00 34.66  ? 111  LEU A CD2 1 
ATOM   4821  N N   . LEU C  1 109 ? 20.370  -17.113 -12.212 1.00 34.69  ? 112  LEU A N   1 
ATOM   4822  C CA  . LEU C  1 109 ? 21.025  -17.798 -13.325 1.00 38.73  ? 112  LEU A CA  1 
ATOM   4823  C C   . LEU C  1 109 ? 21.429  -19.231 -12.987 1.00 39.51  ? 112  LEU A C   1 
ATOM   4824  O O   . LEU C  1 109 ? 21.706  -20.041 -13.867 1.00 43.43  ? 112  LEU A O   1 
ATOM   4825  C CB  . LEU C  1 109 ? 22.252  -16.984 -13.765 1.00 37.40  ? 112  LEU A CB  1 
ATOM   4826  C CG  . LEU C  1 109 ? 22.856  -17.162 -15.156 1.00 41.02  ? 112  LEU A CG  1 
ATOM   4827  C CD1 . LEU C  1 109 ? 21.773  -17.137 -16.211 1.00 39.63  ? 112  LEU A CD1 1 
ATOM   4828  C CD2 . LEU C  1 109 ? 23.841  -16.037 -15.434 1.00 32.88  ? 112  LEU A CD2 1 
ATOM   4829  N N   . SER C  1 110 ? 21.488  -19.559 -11.713 1.00 40.73  ? 113  SER A N   1 
ATOM   4830  C CA  . SER C  1 110 ? 21.919  -20.895 -11.374 1.00 39.99  ? 113  SER A CA  1 
ATOM   4831  C C   . SER C  1 110 ? 20.738  -21.865 -11.280 1.00 42.99  ? 113  SER A C   1 
ATOM   4832  O O   . SER C  1 110 ? 20.888  -23.014 -10.869 1.00 47.59  ? 113  SER A O   1 
ATOM   4833  C CB  . SER C  1 110 ? 22.723  -20.846 -10.082 1.00 41.33  ? 113  SER A CB  1 
ATOM   4834  O OG  . SER C  1 110 ? 21.842  -20.687 -9.008  1.00 52.06  ? 113  SER A OG  1 
ATOM   4835  N N   . ARG C  1 111 ? 19.567  -21.440 -11.735 1.00 47.71  ? 114  ARG A N   1 
ATOM   4836  C CA  . ARG C  1 111 ? 18.447  -22.380 -11.833 1.00 47.41  ? 114  ARG A CA  1 
ATOM   4837  C C   . ARG C  1 111 ? 18.035  -22.475 -13.306 1.00 44.97  ? 114  ARG A C   1 
ATOM   4838  O O   . ARG C  1 111 ? 16.944  -22.981 -13.628 1.00 42.72  ? 114  ARG A O   1 
ATOM   4839  C CB  . ARG C  1 111 ? 17.236  -21.943 -10.997 1.00 48.82  ? 114  ARG A CB  1 
ATOM   4840  C CG  . ARG C  1 111 ? 17.519  -21.557 -9.544  1.00 64.24  ? 114  ARG A CG  1 
ATOM   4841  C CD  . ARG C  1 111 ? 17.947  -22.718 -8.642  1.00 73.60  ? 114  ARG A CD  1 
ATOM   4842  N NE  . ARG C  1 111 ? 18.289  -22.235 -7.291  1.00 76.48  ? 114  ARG A NE  1 
ATOM   4843  C CZ  . ARG C  1 111 ? 17.460  -22.196 -6.243  1.00 72.82  ? 114  ARG A CZ  1 
ATOM   4844  N NH1 . ARG C  1 111 ? 16.210  -22.650 -6.341  1.00 73.05  ? 114  ARG A NH1 1 
ATOM   4845  N NH2 . ARG C  1 111 ? 17.895  -21.723 -5.074  1.00 56.63  ? 114  ARG A NH2 1 
ATOM   4846  N N   . ILE C  1 112 ? 18.906  -21.980 -14.190 1.00 38.04  ? 115  ILE A N   1 
ATOM   4847  C CA  . ILE C  1 112 ? 18.581  -21.871 -15.605 1.00 38.38  ? 115  ILE A CA  1 
ATOM   4848  C C   . ILE C  1 112 ? 19.627  -22.606 -16.445 1.00 36.77  ? 115  ILE A C   1 
ATOM   4849  O O   . ILE C  1 112 ? 20.828  -22.494 -16.188 1.00 38.96  ? 115  ILE A O   1 
ATOM   4850  C CB  . ILE C  1 112 ? 18.499  -20.383 -16.021 1.00 38.76  ? 115  ILE A CB  1 
ATOM   4851  C CG1 . ILE C  1 112 ? 17.379  -19.693 -15.246 1.00 35.90  ? 115  ILE A CG1 1 
ATOM   4852  C CG2 . ILE C  1 112 ? 18.349  -20.205 -17.555 1.00 30.55  ? 115  ILE A CG2 1 
ATOM   4853  C CD1 . ILE C  1 112 ? 17.299  -18.188 -15.482 1.00 30.96  ? 115  ILE A CD1 1 
ATOM   4854  N N   . ASN C  1 113 ? 19.171  -23.372 -17.432 1.00 37.66  ? 116  ASN A N   1 
ATOM   4855  C CA  . ASN C  1 113 ? 20.093  -24.104 -18.313 1.00 45.68  ? 116  ASN A CA  1 
ATOM   4856  C C   . ASN C  1 113 ? 20.073  -23.623 -19.762 1.00 40.12  ? 116  ASN A C   1 
ATOM   4857  O O   . ASN C  1 113 ? 20.967  -23.961 -20.545 1.00 37.65  ? 116  ASN A O   1 
ATOM   4858  C CB  . ASN C  1 113 ? 19.808  -25.608 -18.280 1.00 45.96  ? 116  ASN A CB  1 
ATOM   4859  C CG  . ASN C  1 113 ? 20.095  -26.218 -16.931 1.00 48.79  ? 116  ASN A CG  1 
ATOM   4860  O OD1 . ASN C  1 113 ? 19.190  -26.742 -16.282 1.00 51.05  ? 116  ASN A OD1 1 
ATOM   4861  N ND2 . ASN C  1 113 ? 21.350  -26.149 -16.491 1.00 49.56  ? 116  ASN A ND2 1 
ATOM   4862  N N   . HIS C  1 114 ? 19.031  -22.887 -20.142 1.00 42.05  ? 117  HIS A N   1 
ATOM   4863  C CA  . HIS C  1 114 ? 18.970  -22.414 -21.530 1.00 46.23  ? 117  HIS A CA  1 
ATOM   4864  C C   . HIS C  1 114 ? 18.101  -21.168 -21.772 1.00 36.59  ? 117  HIS A C   1 
ATOM   4865  O O   . HIS C  1 114 ? 16.937  -21.091 -21.359 1.00 31.12  ? 117  HIS A O   1 
ATOM   4866  C CB  . HIS C  1 114 ? 18.490  -23.520 -22.457 1.00 41.01  ? 117  HIS A CB  1 
ATOM   4867  C CG  . HIS C  1 114 ? 18.823  -23.265 -23.891 1.00 44.51  ? 117  HIS A CG  1 
ATOM   4868  N ND1 . HIS C  1 114 ? 18.008  -23.658 -24.933 1.00 41.58  ? 117  HIS A ND1 1 
ATOM   4869  C CD2 . HIS C  1 114 ? 19.922  -22.701 -24.455 1.00 45.68  ? 117  HIS A CD2 1 
ATOM   4870  C CE1 . HIS C  1 114 ? 18.577  -23.313 -26.078 1.00 43.77  ? 117  HIS A CE1 1 
ATOM   4871  N NE2 . HIS C  1 114 ? 19.740  -22.735 -25.818 1.00 38.01  ? 117  HIS A NE2 1 
ATOM   4872  N N   . PHE C  1 115 ? 18.698  -20.213 -22.465 1.00 35.99  ? 118  PHE A N   1 
ATOM   4873  C CA  . PHE C  1 115 ? 18.022  -19.004 -22.908 1.00 39.55  ? 118  PHE A CA  1 
ATOM   4874  C C   . PHE C  1 115 ? 17.711  -19.165 -24.396 1.00 41.36  ? 118  PHE A C   1 
ATOM   4875  O O   . PHE C  1 115 ? 18.488  -19.782 -25.133 1.00 35.07  ? 118  PHE A O   1 
ATOM   4876  C CB  . PHE C  1 115 ? 18.935  -17.794 -22.710 1.00 34.77  ? 118  PHE A CB  1 
ATOM   4877  C CG  . PHE C  1 115 ? 18.962  -17.234 -21.318 1.00 27.37  ? 118  PHE A CG  1 
ATOM   4878  C CD1 . PHE C  1 115 ? 17.801  -17.016 -20.612 1.00 29.06  ? 118  PHE A CD1 1 
ATOM   4879  C CD2 . PHE C  1 115 ? 20.179  -16.907 -20.720 1.00 34.07  ? 118  PHE A CD2 1 
ATOM   4880  C CE1 . PHE C  1 115 ? 17.838  -16.457 -19.339 1.00 28.40  ? 118  PHE A CE1 1 
ATOM   4881  C CE2 . PHE C  1 115 ? 20.228  -16.363 -19.424 1.00 28.90  ? 118  PHE A CE2 1 
ATOM   4882  C CZ  . PHE C  1 115 ? 19.058  -16.134 -18.745 1.00 24.11  ? 118  PHE A CZ  1 
ATOM   4883  N N   . GLU C  1 116 ? 16.633  -18.531 -24.847 1.00 46.10  ? 119  GLU A N   1 
ATOM   4884  C CA  . GLU C  1 116 ? 16.304  -18.425 -26.275 1.00 39.48  ? 119  GLU A CA  1 
ATOM   4885  C C   . GLU C  1 116 ? 16.010  -16.970 -26.597 1.00 33.80  ? 119  GLU A C   1 
ATOM   4886  O O   . GLU C  1 116 ? 14.970  -16.439 -26.229 1.00 37.63  ? 119  GLU A O   1 
ATOM   4887  C CB  . GLU C  1 116 ? 15.099  -19.318 -26.603 1.00 48.88  ? 119  GLU A CB  1 
ATOM   4888  C CG  . GLU C  1 116 ? 14.606  -19.351 -28.070 1.00 59.12  ? 119  GLU A CG  1 
ATOM   4889  C CD  . GLU C  1 116 ? 13.414  -20.321 -28.268 1.00 68.01  ? 119  GLU A CD  1 
ATOM   4890  O OE1 . GLU C  1 116 ? 13.549  -21.528 -27.937 1.00 69.13  ? 119  GLU A OE1 1 
ATOM   4891  O OE2 . GLU C  1 116 ? 12.335  -19.872 -28.725 1.00 64.37  ? 119  GLU A OE2 1 
ATOM   4892  N N   . LYS C  1 117 ? 16.930  -16.329 -27.301 1.00 37.42  ? 120  LYS A N   1 
ATOM   4893  C CA  . LYS C  1 117 ? 16.853  -14.886 -27.531 1.00 36.11  ? 120  LYS A CA  1 
ATOM   4894  C C   . LYS C  1 117 ? 15.770  -14.481 -28.510 1.00 32.45  ? 120  LYS A C   1 
ATOM   4895  O O   . LYS C  1 117 ? 15.590  -15.131 -29.524 1.00 39.85  ? 120  LYS A O   1 
ATOM   4896  C CB  . LYS C  1 117 ? 18.208  -14.377 -28.012 1.00 30.33  ? 120  LYS A CB  1 
ATOM   4897  C CG  . LYS C  1 117 ? 18.425  -12.910 -27.711 1.00 37.18  ? 120  LYS A CG  1 
ATOM   4898  C CD  . LYS C  1 117 ? 19.917  -12.608 -27.636 1.00 38.50  ? 120  LYS A CD  1 
ATOM   4899  C CE  . LYS C  1 117 ? 20.577  -12.297 -28.945 1.00 33.84  ? 120  LYS A CE  1 
ATOM   4900  N NZ  . LYS C  1 117 ? 22.053  -12.186 -28.661 1.00 37.59  ? 120  LYS A NZ  1 
ATOM   4901  N N   . ILE C  1 118 ? 15.006  -13.445 -28.185 1.00 33.29  ? 121  ILE A N   1 
ATOM   4902  C CA  . ILE C  1 118 ? 14.066  -12.910 -29.160 1.00 35.13  ? 121  ILE A CA  1 
ATOM   4903  C C   . ILE C  1 118 ? 14.111  -11.371 -29.239 1.00 36.79  ? 121  ILE A C   1 
ATOM   4904  O O   . ILE C  1 118 ? 14.566  -10.672 -28.316 1.00 36.24  ? 121  ILE A O   1 
ATOM   4905  C CB  . ILE C  1 118 ? 12.621  -13.334 -28.868 1.00 38.99  ? 121  ILE A CB  1 
ATOM   4906  C CG1 . ILE C  1 118 ? 11.965  -12.446 -27.817 1.00 34.11  ? 121  ILE A CG1 1 
ATOM   4907  C CG2 . ILE C  1 118 ? 12.528  -14.850 -28.576 1.00 38.22  ? 121  ILE A CG2 1 
ATOM   4908  C CD1 . ILE C  1 118 ? 10.467  -12.710 -27.730 1.00 36.47  ? 121  ILE A CD1 1 
ATOM   4909  N N   . GLN C  1 119 ? 13.610  -10.851 -30.349 1.00 36.46  ? 122  GLN A N   1 
ATOM   4910  C CA  . GLN C  1 119 ? 13.575  -9.418  -30.591 1.00 29.54  ? 122  GLN A CA  1 
ATOM   4911  C C   . GLN C  1 119 ? 12.315  -8.739  -30.104 1.00 34.23  ? 122  GLN A C   1 
ATOM   4912  O O   . GLN C  1 119 ? 11.210  -9.232  -30.298 1.00 33.55  ? 122  GLN A O   1 
ATOM   4913  C CB  . GLN C  1 119 ? 13.723  -9.141  -32.061 1.00 28.72  ? 122  GLN A CB  1 
ATOM   4914  C CG  . GLN C  1 119 ? 13.674  -7.683  -32.398 1.00 37.25  ? 122  GLN A CG  1 
ATOM   4915  C CD  . GLN C  1 119 ? 13.793  -7.463  -33.902 1.00 38.51  ? 122  GLN A CD  1 
ATOM   4916  O OE1 . GLN C  1 119 ? 12.782  -7.335  -34.595 1.00 30.85  ? 122  GLN A OE1 1 
ATOM   4917  N NE2 . GLN C  1 119 ? 15.028  -7.430  -34.410 1.00 32.37  ? 122  GLN A NE2 1 
ATOM   4918  N N   . ILE C  1 120 ? 12.488  -7.604  -29.449 1.00 33.61  ? 123  ILE A N   1 
ATOM   4919  C CA  . ILE C  1 120 ? 11.356  -6.867  -28.976 1.00 34.35  ? 123  ILE A CA  1 
ATOM   4920  C C   . ILE C  1 120 ? 11.120  -5.606  -29.822 1.00 38.21  ? 123  ILE A C   1 
ATOM   4921  O O   . ILE C  1 120 ? 9.987   -5.301  -30.203 1.00 40.47  ? 123  ILE A O   1 
ATOM   4922  C CB  . ILE C  1 120 ? 11.591  -6.483  -27.518 1.00 37.83  ? 123  ILE A CB  1 
ATOM   4923  C CG1 . ILE C  1 120 ? 11.220  -7.656  -26.634 1.00 35.65  ? 123  ILE A CG1 1 
ATOM   4924  C CG2 . ILE C  1 120 ? 10.823  -5.222  -27.111 1.00 29.52  ? 123  ILE A CG2 1 
ATOM   4925  C CD1 . ILE C  1 120 ? 11.541  -7.368  -25.255 1.00 33.95  ? 123  ILE A CD1 1 
ATOM   4926  N N   . THR C  1 121 ? 12.197  -4.934  -30.199 1.00 31.01  ? 124  THR A N   1 
ATOM   4927  C CA  . THR C  1 121 ? 12.088  -3.747  -31.032 1.00 33.79  ? 124  THR A CA  1 
ATOM   4928  C C   . THR C  1 121 ? 13.158  -3.701  -32.121 1.00 36.10  ? 124  THR A C   1 
ATOM   4929  O O   . THR C  1 121 ? 14.367  -3.631  -31.829 1.00 34.02  ? 124  THR A O   1 
ATOM   4930  C CB  . THR C  1 121 ? 12.136  -2.475  -30.160 1.00 35.86  ? 124  THR A CB  1 
ATOM   4931  O OG1 . THR C  1 121 ? 10.959  -2.430  -29.341 1.00 40.77  ? 124  THR A OG1 1 
ATOM   4932  C CG2 . THR C  1 121 ? 12.155  -1.218  -30.995 1.00 31.93  ? 124  THR A CG2 1 
ATOM   4933  N N   . PRO C  1 122 ? 12.711  -3.774  -33.387 1.00 33.00  ? 125  PRO A N   1 
ATOM   4934  C CA  . PRO C  1 122 ? 13.611  -3.725  -34.537 1.00 32.70  ? 125  PRO A CA  1 
ATOM   4935  C C   . PRO C  1 122 ? 14.369  -2.400  -34.545 1.00 32.45  ? 125  PRO A C   1 
ATOM   4936  O O   . PRO C  1 122 ? 13.778  -1.358  -34.229 1.00 30.99  ? 125  PRO A O   1 
ATOM   4937  C CB  . PRO C  1 122 ? 12.661  -3.820  -35.742 1.00 30.38  ? 125  PRO A CB  1 
ATOM   4938  C CG  . PRO C  1 122 ? 11.329  -4.231  -35.190 1.00 29.46  ? 125  PRO A CG  1 
ATOM   4939  C CD  . PRO C  1 122 ? 11.293  -3.740  -33.790 1.00 35.21  ? 125  PRO A CD  1 
ATOM   4940  N N   . LYS C  1 123 A 15.653  -2.446  -34.890 1.00 33.01  ? 125  LYS A N   1 
ATOM   4941  C CA  . LYS C  1 123 A 16.491  -1.246  -34.911 1.00 35.52  ? 125  LYS A CA  1 
ATOM   4942  C C   . LYS C  1 123 A 16.015  -0.187  -35.919 1.00 33.47  ? 125  LYS A C   1 
ATOM   4943  O O   . LYS C  1 123 A 16.237  1.005   -35.706 1.00 32.39  ? 125  LYS A O   1 
ATOM   4944  C CB  . LYS C  1 123 A 17.948  -1.624  -35.224 1.00 33.53  ? 125  LYS A CB  1 
ATOM   4945  C CG  . LYS C  1 123 A 18.962  -0.515  -34.960 1.00 36.01  ? 125  LYS A CG  1 
ATOM   4946  C CD  . LYS C  1 123 A 20.397  -0.985  -35.200 1.00 43.94  ? 125  LYS A CD  1 
ATOM   4947  C CE  . LYS C  1 123 A 21.407  0.169   -35.097 1.00 44.71  ? 125  LYS A CE  1 
ATOM   4948  N NZ  . LYS C  1 123 A 21.607  0.633   -33.696 1.00 41.53  ? 125  LYS A NZ  1 
ATOM   4949  N N   . ASN C  1 124 B 15.300  -0.606  -36.962 1.00 33.03  ? 125  ASN A N   1 
ATOM   4950  C CA  . ASN C  1 124 B 14.805  0.351   -37.946 1.00 35.17  ? 125  ASN A CA  1 
ATOM   4951  C C   . ASN C  1 124 B 13.357  0.746   -37.677 1.00 38.58  ? 125  ASN A C   1 
ATOM   4952  O O   . ASN C  1 124 B 12.656  1.161   -38.604 1.00 37.30  ? 125  ASN A O   1 
ATOM   4953  C CB  . ASN C  1 124 B 14.922  -0.199  -39.379 1.00 37.18  ? 125  ASN A CB  1 
ATOM   4954  C CG  . ASN C  1 124 B 13.869  -1.271  -39.700 1.00 44.74  ? 125  ASN A CG  1 
ATOM   4955  O OD1 . ASN C  1 124 B 13.325  -1.928  -38.801 1.00 42.35  ? 125  ASN A OD1 1 
ATOM   4956  N ND2 . ASN C  1 124 B 13.575  -1.439  -40.992 1.00 40.01  ? 125  ASN A ND2 1 
ATOM   4957  N N   . SER C  1 125 ? 12.915  0.661   -36.421 1.00 33.54  ? 126  SER A N   1 
ATOM   4958  C CA  . SER C  1 125 ? 11.533  1.006   -36.123 1.00 35.40  ? 126  SER A CA  1 
ATOM   4959  C C   . SER C  1 125 ? 11.483  2.387   -35.479 1.00 37.94  ? 126  SER A C   1 
ATOM   4960  O O   . SER C  1 125 ? 10.392  2.932   -35.259 1.00 38.39  ? 126  SER A O   1 
ATOM   4961  C CB  . SER C  1 125 ? 10.859  -0.029  -35.195 1.00 35.04  ? 126  SER A CB  1 
ATOM   4962  O OG  . SER C  1 125 ? 11.256  0.101   -33.836 1.00 36.21  ? 126  SER A OG  1 
ATOM   4963  N N   . TRP C  1 126 ? 12.657  2.945   -35.177 1.00 33.07  ? 127  TRP A N   1 
ATOM   4964  C CA  . TRP C  1 126 ? 12.741  4.263   -34.542 1.00 37.08  ? 127  TRP A CA  1 
ATOM   4965  C C   . TRP C  1 126 ? 12.775  5.321   -35.653 1.00 39.27  ? 127  TRP A C   1 
ATOM   4966  O O   . TRP C  1 126 ? 13.810  5.516   -36.305 1.00 39.99  ? 127  TRP A O   1 
ATOM   4967  C CB  . TRP C  1 126 ? 13.986  4.362   -33.630 1.00 31.62  ? 127  TRP A CB  1 
ATOM   4968  C CG  . TRP C  1 126 ? 14.053  3.271   -32.575 1.00 37.20  ? 127  TRP A CG  1 
ATOM   4969  C CD1 . TRP C  1 126 ? 14.815  2.118   -32.612 1.00 36.59  ? 127  TRP A CD1 1 
ATOM   4970  C CD2 . TRP C  1 126 ? 13.368  3.253   -31.317 1.00 29.74  ? 127  TRP A CD2 1 
ATOM   4971  N NE1 . TRP C  1 126 ? 14.610  1.386   -31.469 1.00 31.68  ? 127  TRP A NE1 1 
ATOM   4972  C CE2 . TRP C  1 126 ? 13.725  2.059   -30.661 1.00 28.90  ? 127  TRP A CE2 1 
ATOM   4973  C CE3 . TRP C  1 126 ? 12.469  4.117   -30.697 1.00 30.47  ? 127  TRP A CE3 1 
ATOM   4974  C CZ2 . TRP C  1 126 ? 13.207  1.711   -29.419 1.00 24.54  ? 127  TRP A CZ2 1 
ATOM   4975  C CZ3 . TRP C  1 126 ? 11.960  3.767   -29.457 1.00 34.73  ? 127  TRP A CZ3 1 
ATOM   4976  C CH2 . TRP C  1 126 ? 12.331  2.576   -28.835 1.00 26.49  ? 127  TRP A CH2 1 
ATOM   4977  N N   . SER C  1 127 ? 11.640  5.952   -35.938 1.00 35.31  ? 128  SER A N   1 
ATOM   4978  C CA  . SER C  1 127 ? 11.607  6.826   -37.106 1.00 40.57  ? 128  SER A CA  1 
ATOM   4979  C C   . SER C  1 127 ? 11.698  8.308   -36.705 1.00 42.91  ? 128  SER A C   1 
ATOM   4980  O O   . SER C  1 127 ? 11.850  9.178   -37.573 1.00 46.26  ? 128  SER A O   1 
ATOM   4981  C CB  . SER C  1 127 ? 10.363  6.546   -37.971 1.00 41.67  ? 128  SER A CB  1 
ATOM   4982  O OG  . SER C  1 127 ? 9.151   6.567   -37.228 1.00 48.76  ? 128  SER A OG  1 
ATOM   4983  N N   . ASP C  1 128 ? 11.654  8.583   -35.401 1.00 35.73  ? 129  ASP A N   1 
ATOM   4984  C CA  . ASP C  1 128 ? 11.781  9.952   -34.906 1.00 35.06  ? 129  ASP A CA  1 
ATOM   4985  C C   . ASP C  1 128 ? 12.975  10.160  -33.951 1.00 32.87  ? 129  ASP A C   1 
ATOM   4986  O O   . ASP C  1 128 ? 13.067  11.183  -33.280 1.00 29.33  ? 129  ASP A O   1 
ATOM   4987  C CB  . ASP C  1 128 ? 10.485  10.375  -34.214 1.00 35.94  ? 129  ASP A CB  1 
ATOM   4988  C CG  . ASP C  1 128 ? 9.310   10.441  -35.169 1.00 43.94  ? 129  ASP A CG  1 
ATOM   4989  O OD1 . ASP C  1 128 ? 9.524   10.770  -36.358 1.00 45.47  ? 129  ASP A OD1 1 
ATOM   4990  O OD2 . ASP C  1 128 ? 8.170   10.163  -34.733 1.00 52.10  ? 129  ASP A OD2 1 
ATOM   4991  N N   . HIS C  1 129 ? 13.862  9.176   -33.872 1.00 33.42  ? 130  HIS A N   1 
ATOM   4992  C CA  . HIS C  1 129 ? 15.066  9.259   -33.047 1.00 32.89  ? 130  HIS A CA  1 
ATOM   4993  C C   . HIS C  1 129 ? 16.247  8.656   -33.811 1.00 33.55  ? 130  HIS A C   1 
ATOM   4994  O O   . HIS C  1 129 ? 16.038  7.858   -34.720 1.00 33.67  ? 130  HIS A O   1 
ATOM   4995  C CB  . HIS C  1 129 ? 14.843  8.519   -31.712 1.00 29.26  ? 130  HIS A CB  1 
ATOM   4996  C CG  . HIS C  1 129 ? 13.612  8.964   -30.986 1.00 29.04  ? 130  HIS A CG  1 
ATOM   4997  N ND1 . HIS C  1 129 ? 12.345  8.564   -31.362 1.00 27.28  ? 130  HIS A ND1 1 
ATOM   4998  C CD2 . HIS C  1 129 ? 13.447  9.809   -29.934 1.00 32.05  ? 130  HIS A CD2 1 
ATOM   4999  C CE1 . HIS C  1 129 ? 11.455  9.133   -30.565 1.00 31.47  ? 130  HIS A CE1 1 
ATOM   5000  N NE2 . HIS C  1 129 ? 12.096  9.891   -29.687 1.00 31.61  ? 130  HIS A NE2 1 
ATOM   5001  N N   . GLU C  1 130 ? 17.473  9.020   -33.449 1.00 31.87  ? 131  GLU A N   1 
ATOM   5002  C CA  . GLU C  1 130 ? 18.663  8.401   -34.039 1.00 30.83  ? 131  GLU A CA  1 
ATOM   5003  C C   . GLU C  1 130 ? 19.116  7.209   -33.167 1.00 35.95  ? 131  GLU A C   1 
ATOM   5004  O O   . GLU C  1 130 ? 19.327  7.359   -31.949 1.00 31.05  ? 131  GLU A O   1 
ATOM   5005  C CB  . GLU C  1 130 ? 19.787  9.424   -34.219 1.00 30.44  ? 131  GLU A CB  1 
ATOM   5006  C CG  . GLU C  1 130 ? 19.525  10.478  -35.289 1.00 40.86  ? 131  GLU A CG  1 
ATOM   5007  C CD  . GLU C  1 130 ? 19.752  9.930   -36.719 1.00 51.02  ? 131  GLU A CD  1 
ATOM   5008  O OE1 . GLU C  1 130 ? 20.515  8.940   -36.867 1.00 53.54  ? 131  GLU A OE1 1 
ATOM   5009  O OE2 . GLU C  1 130 ? 19.195  10.495  -37.693 1.00 47.15  ? 131  GLU A OE2 1 
ATOM   5010  N N   . ALA C  1 131 ? 19.188  6.025   -33.779 1.00 28.28  ? 132  ALA A N   1 
ATOM   5011  C CA  . ALA C  1 131 ? 19.485  4.792   -33.066 1.00 23.45  ? 132  ALA A CA  1 
ATOM   5012  C C   . ALA C  1 131 ? 20.810  4.172   -33.464 1.00 29.73  ? 132  ALA A C   1 
ATOM   5013  O O   . ALA C  1 131 ? 20.844  3.035   -33.928 1.00 42.14  ? 132  ALA A O   1 
ATOM   5014  C CB  . ALA C  1 131 ? 18.368  3.797   -33.281 1.00 26.15  ? 132  ALA A CB  1 
ATOM   5015  N N   . SER C  1 132 ? 21.905  4.893   -33.263 1.00 33.65  ? 133  SER A N   1 
ATOM   5016  C CA  . SER C  1 132 ? 23.203  4.414   -33.725 1.00 28.32  ? 133  SER A CA  1 
ATOM   5017  C C   . SER C  1 132 ? 24.368  4.832   -32.852 1.00 28.60  ? 133  SER A C   1 
ATOM   5018  O O   . SER C  1 132 ? 25.493  4.889   -33.339 1.00 30.31  ? 133  SER A O   1 
ATOM   5019  C CB  . SER C  1 132 ? 23.451  4.950   -35.127 1.00 28.65  ? 133  SER A CB  1 
ATOM   5020  O OG  . SER C  1 132 ? 23.281  6.364   -35.092 1.00 29.13  ? 133  SER A OG  1 
ATOM   5021  N N   . GLY C  1 133 ? 24.101  5.096   -31.571 1.00 31.37  ? 134  GLY A N   1 
ATOM   5022  C CA  . GLY C  1 133 ? 25.114  5.533   -30.626 1.00 23.59  ? 134  GLY A CA  1 
ATOM   5023  C C   . GLY C  1 133 ? 26.209  4.513   -30.460 1.00 24.01  ? 134  GLY A C   1 
ATOM   5024  O O   . GLY C  1 133 ? 25.940  3.319   -30.471 1.00 26.13  ? 134  GLY A O   1 
ATOM   5025  N N   . VAL C  1 134 ? 27.431  4.999   -30.264 1.00 26.90  ? 135  VAL A N   1 
ATOM   5026  C CA  . VAL C  1 134 ? 28.661  4.212   -30.381 1.00 25.23  ? 135  VAL A CA  1 
ATOM   5027  C C   . VAL C  1 134 ? 29.748  4.901   -29.498 1.00 26.81  ? 135  VAL A C   1 
ATOM   5028  O O   . VAL C  1 134 ? 29.638  6.095   -29.210 1.00 26.43  ? 135  VAL A O   1 
ATOM   5029  C CB  . VAL C  1 134 ? 29.041  4.139   -31.894 1.00 27.37  ? 135  VAL A CB  1 
ATOM   5030  C CG1 . VAL C  1 134 ? 30.443  4.581   -32.139 1.00 30.38  ? 135  VAL A CG1 1 
ATOM   5031  C CG2 . VAL C  1 134 ? 28.746  2.786   -32.476 1.00 24.05  ? 135  VAL A CG2 1 
ATOM   5032  N N   . SER C  1 135 ? 30.740  4.171   -28.996 1.00 27.92  ? 136  SER A N   1 
ATOM   5033  C CA  . SER C  1 135 ? 31.774  4.785   -28.127 1.00 29.07  ? 136  SER A CA  1 
ATOM   5034  C C   . SER C  1 135 ? 33.124  4.106   -28.244 1.00 30.48  ? 136  SER A C   1 
ATOM   5035  O O   . SER C  1 135 ? 33.184  2.897   -28.441 1.00 30.66  ? 136  SER A O   1 
ATOM   5036  C CB  . SER C  1 135 ? 31.360  4.761   -26.648 1.00 30.59  ? 136  SER A CB  1 
ATOM   5037  O OG  . SER C  1 135 ? 32.442  5.110   -25.775 1.00 27.86  ? 136  SER A OG  1 
ATOM   5038  N N   . SER C  1 136 ? 34.203  4.864   -28.055 1.00 30.42  ? 137  SER A N   1 
ATOM   5039  C CA  . SER C  1 136 ? 35.555  4.287   -28.107 1.00 29.56  ? 137  SER A CA  1 
ATOM   5040  C C   . SER C  1 136 ? 35.871  3.393   -26.885 1.00 32.07  ? 137  SER A C   1 
ATOM   5041  O O   . SER C  1 136 ? 36.814  2.607   -26.928 1.00 37.72  ? 137  SER A O   1 
ATOM   5042  C CB  . SER C  1 136 ? 36.622  5.394   -28.211 1.00 33.14  ? 137  SER A CB  1 
ATOM   5043  O OG  . SER C  1 136 ? 36.697  6.185   -27.018 1.00 38.61  ? 137  SER A OG  1 
ATOM   5044  N N   . ALA C  1 137 ? 35.077  3.457   -25.816 1.00 34.55  ? 138  ALA A N   1 
ATOM   5045  C CA  . ALA C  1 137 ? 35.323  2.572   -24.677 1.00 30.48  ? 138  ALA A CA  1 
ATOM   5046  C C   . ALA C  1 137 ? 34.856  1.164   -25.007 1.00 35.52  ? 138  ALA A C   1 
ATOM   5047  O O   . ALA C  1 137 ? 35.143  0.211   -24.258 1.00 35.85  ? 138  ALA A O   1 
ATOM   5048  C CB  . ALA C  1 137 ? 34.625  3.058   -23.476 1.00 31.01  ? 138  ALA A CB  1 
ATOM   5049  N N   . CYS C  1 138 ? 34.122  1.055   -26.119 1.00 33.03  ? 139  CYS A N   1 
ATOM   5050  C CA  . CYS C  1 138 ? 33.587  -0.214  -26.630 1.00 35.18  ? 139  CYS A CA  1 
ATOM   5051  C C   . CYS C  1 138 ? 34.019  -0.499  -28.073 1.00 32.62  ? 139  CYS A C   1 
ATOM   5052  O O   . CYS C  1 138 ? 33.201  -0.392  -28.978 1.00 29.22  ? 139  CYS A O   1 
ATOM   5053  C CB  . CYS C  1 138 ? 32.052  -0.191  -26.565 1.00 31.13  ? 139  CYS A CB  1 
ATOM   5054  S SG  . CYS C  1 138 ? 31.363  -0.256  -24.877 1.00 46.33  ? 139  CYS A SG  1 
ATOM   5055  N N   . PRO C  1 139 ? 35.297  -0.877  -28.291 1.00 37.09  ? 140  PRO A N   1 
ATOM   5056  C CA  . PRO C  1 139 ? 35.831  -1.114  -29.646 1.00 34.65  ? 140  PRO A CA  1 
ATOM   5057  C C   . PRO C  1 139 ? 35.421  -2.459  -30.237 1.00 33.86  ? 140  PRO A C   1 
ATOM   5058  O O   . PRO C  1 139 ? 35.239  -3.393  -29.470 1.00 38.09  ? 140  PRO A O   1 
ATOM   5059  C CB  . PRO C  1 139 ? 37.349  -1.090  -29.424 1.00 31.84  ? 140  PRO A CB  1 
ATOM   5060  C CG  . PRO C  1 139 ? 37.523  -1.595  -28.033 1.00 31.97  ? 140  PRO A CG  1 
ATOM   5061  C CD  . PRO C  1 139 ? 36.338  -1.056  -27.253 1.00 37.82  ? 140  PRO A CD  1 
ATOM   5062  N N   . TYR C  1 140 ? 35.320  -2.576  -31.558 1.00 30.15  ? 141  TYR A N   1 
ATOM   5063  C CA  . TYR C  1 140 ? 35.024  -3.875  -32.150 1.00 33.84  ? 141  TYR A CA  1 
ATOM   5064  C C   . TYR C  1 140 ? 36.226  -4.360  -32.991 1.00 43.25  ? 141  TYR A C   1 
ATOM   5065  O O   . TYR C  1 140 ? 37.078  -5.110  -32.499 1.00 54.27  ? 141  TYR A O   1 
ATOM   5066  C CB  . TYR C  1 140 ? 33.777  -3.830  -33.020 1.00 32.81  ? 141  TYR A CB  1 
ATOM   5067  C CG  . TYR C  1 140 ? 33.464  -5.138  -33.722 1.00 29.65  ? 141  TYR A CG  1 
ATOM   5068  C CD1 . TYR C  1 140 ? 33.429  -6.346  -33.035 1.00 28.55  ? 141  TYR A CD1 1 
ATOM   5069  C CD2 . TYR C  1 140 ? 33.285  -5.166  -35.102 1.00 32.96  ? 141  TYR A CD2 1 
ATOM   5070  C CE1 . TYR C  1 140 ? 33.157  -7.544  -33.693 1.00 27.77  ? 141  TYR A CE1 1 
ATOM   5071  C CE2 . TYR C  1 140 ? 33.019  -6.351  -35.781 1.00 30.07  ? 141  TYR A CE2 1 
ATOM   5072  C CZ  . TYR C  1 140 ? 32.955  -7.538  -35.078 1.00 35.91  ? 141  TYR A CZ  1 
ATOM   5073  O OH  . TYR C  1 140 ? 32.684  -8.715  -35.759 1.00 37.84  ? 141  TYR A OH  1 
ATOM   5074  N N   . GLN C  1 141 ? 36.343  -3.946  -34.239 1.00 36.26  ? 142  GLN A N   1 
ATOM   5075  C CA  . GLN C  1 141 ? 37.509  -4.431  -34.984 1.00 36.84  ? 142  GLN A CA  1 
ATOM   5076  C C   . GLN C  1 141 ? 38.381  -3.209  -35.273 1.00 43.69  ? 142  GLN A C   1 
ATOM   5077  O O   . GLN C  1 141 ? 38.659  -2.879  -36.429 1.00 44.14  ? 142  GLN A O   1 
ATOM   5078  C CB  . GLN C  1 141 ? 37.102  -5.156  -36.287 1.00 30.52  ? 142  GLN A CB  1 
ATOM   5079  C CG  . GLN C  1 141 ? 36.520  -6.574  -36.126 1.00 27.02  ? 142  GLN A CG  1 
ATOM   5080  C CD  . GLN C  1 141 ? 36.049  -7.231  -37.450 1.00 32.32  ? 142  GLN A CD  1 
ATOM   5081  O OE1 . GLN C  1 141 ? 35.980  -6.594  -38.507 1.00 34.11  ? 142  GLN A OE1 1 
ATOM   5082  N NE2 . GLN C  1 141 ? 35.667  -8.504  -37.368 1.00 36.90  ? 142  GLN A NE2 1 
ATOM   5083  N N   . GLY C  1 142 ? 38.802  -2.522  -34.215 1.00 37.60  ? 143  GLY A N   1 
ATOM   5084  C CA  . GLY C  1 142 ? 39.597  -1.332  -34.411 1.00 31.40  ? 143  GLY A CA  1 
ATOM   5085  C C   . GLY C  1 142 ? 38.770  -0.062  -34.544 1.00 42.70  ? 143  GLY A C   1 
ATOM   5086  O O   . GLY C  1 142 ? 39.334  1.022   -34.758 1.00 47.10  ? 143  GLY A O   1 
ATOM   5087  N N   . ARG C  1 143 ? 37.443  -0.179  -34.474 1.00 40.27  ? 144  ARG A N   1 
ATOM   5088  C CA  . ARG C  1 143 ? 36.600  1.022   -34.538 1.00 40.58  ? 144  ARG A CA  1 
ATOM   5089  C C   . ARG C  1 143 ? 35.640  1.130   -33.342 1.00 37.38  ? 144  ARG A C   1 
ATOM   5090  O O   . ARG C  1 143 ? 35.460  0.153   -32.585 1.00 34.50  ? 144  ARG A O   1 
ATOM   5091  C CB  . ARG C  1 143 ? 35.795  1.087   -35.861 1.00 32.54  ? 144  ARG A CB  1 
ATOM   5092  C CG  . ARG C  1 143 ? 34.645  0.110   -35.974 1.00 35.16  ? 144  ARG A CG  1 
ATOM   5093  C CD  . ARG C  1 143 ? 33.910  0.207   -37.329 1.00 38.77  ? 144  ARG A CD  1 
ATOM   5094  N NE  . ARG C  1 143 ? 32.706  -0.631  -37.338 1.00 37.95  ? 144  ARG A NE  1 
ATOM   5095  C CZ  . ARG C  1 143 ? 32.673  -1.904  -37.751 1.00 34.32  ? 144  ARG A CZ  1 
ATOM   5096  N NH1 . ARG C  1 143 ? 33.759  -2.479  -38.264 1.00 27.35  ? 144  ARG A NH1 1 
ATOM   5097  N NH2 . ARG C  1 143 ? 31.534  -2.592  -37.700 1.00 31.27  ? 144  ARG A NH2 1 
ATOM   5098  N N   . SER C  1 144 ? 35.006  2.302   -33.196 1.00 32.11  ? 145  SER A N   1 
ATOM   5099  C CA  . SER C  1 144 ? 34.053  2.532   -32.100 1.00 33.16  ? 145  SER A CA  1 
ATOM   5100  C C   . SER C  1 144 ? 32.716  1.759   -32.323 1.00 33.54  ? 145  SER A C   1 
ATOM   5101  O O   . SER C  1 144 ? 32.157  1.740   -33.445 1.00 30.47  ? 145  SER A O   1 
ATOM   5102  C CB  . SER C  1 144 ? 33.761  4.028   -31.953 1.00 29.06  ? 145  SER A CB  1 
ATOM   5103  O OG  . SER C  1 144 ? 34.910  4.782   -31.631 1.00 29.94  ? 145  SER A OG  1 
ATOM   5104  N N   . SER C  1 145 ? 32.204  1.135   -31.257 1.00 27.32  ? 146  SER A N   1 
ATOM   5105  C CA  . SER C  1 145 ? 31.005  0.281   -31.358 1.00 25.09  ? 146  SER A CA  1 
ATOM   5106  C C   . SER C  1 145 ? 30.091  0.451   -30.131 1.00 29.28  ? 146  SER A C   1 
ATOM   5107  O O   . SER C  1 145 ? 30.164  1.479   -29.453 1.00 29.22  ? 146  SER A O   1 
ATOM   5108  C CB  . SER C  1 145 ? 31.414  -1.187  -31.535 1.00 24.22  ? 146  SER A CB  1 
ATOM   5109  O OG  . SER C  1 145 ? 30.298  -1.989  -31.848 1.00 22.21  ? 146  SER A OG  1 
ATOM   5110  N N   . PHE C  1 146 ? 29.248  -0.543  -29.833 1.00 25.32  ? 147  PHE A N   1 
ATOM   5111  C CA  . PHE C  1 146 ? 28.356  -0.466  -28.671 1.00 25.03  ? 147  PHE A CA  1 
ATOM   5112  C C   . PHE C  1 146 ? 27.801  -1.838  -28.303 1.00 23.68  ? 147  PHE A C   1 
ATOM   5113  O O   . PHE C  1 146 ? 28.017  -2.782  -29.021 1.00 18.98  ? 147  PHE A O   1 
ATOM   5114  C CB  . PHE C  1 146 ? 27.200  0.535   -28.913 1.00 25.01  ? 147  PHE A CB  1 
ATOM   5115  C CG  . PHE C  1 146 ? 26.445  0.931   -27.648 1.00 27.13  ? 147  PHE A CG  1 
ATOM   5116  C CD1 . PHE C  1 146 ? 27.076  1.653   -26.629 1.00 27.37  ? 147  PHE A CD1 1 
ATOM   5117  C CD2 . PHE C  1 146 ? 25.087  0.609   -27.493 1.00 27.63  ? 147  PHE A CD2 1 
ATOM   5118  C CE1 . PHE C  1 146 ? 26.371  2.024   -25.457 1.00 25.46  ? 147  PHE A CE1 1 
ATOM   5119  C CE2 . PHE C  1 146 ? 24.367  0.965   -26.307 1.00 22.72  ? 147  PHE A CE2 1 
ATOM   5120  C CZ  . PHE C  1 146 ? 25.012  1.673   -25.302 1.00 22.61  ? 147  PHE A CZ  1 
ATOM   5121  N N   . PHE C  1 147 ? 27.156  -1.940  -27.134 1.00 25.81  ? 148  PHE A N   1 
ATOM   5122  C CA  . PHE C  1 147 ? 26.418  -3.139  -26.741 1.00 25.01  ? 148  PHE A CA  1 
ATOM   5123  C C   . PHE C  1 147 ? 25.427  -3.486  -27.823 1.00 21.99  ? 148  PHE A C   1 
ATOM   5124  O O   . PHE C  1 147 ? 24.762  -2.601  -28.344 1.00 19.47  ? 148  PHE A O   1 
ATOM   5125  C CB  . PHE C  1 147 ? 25.641  -2.978  -25.418 1.00 23.84  ? 148  PHE A CB  1 
ATOM   5126  C CG  . PHE C  1 147 ? 26.494  -2.684  -24.210 1.00 24.82  ? 148  PHE A CG  1 
ATOM   5127  C CD1 . PHE C  1 147 ? 27.163  -3.707  -23.548 1.00 22.93  ? 148  PHE A CD1 1 
ATOM   5128  C CD2 . PHE C  1 147 ? 26.589  -1.378  -23.710 1.00 22.85  ? 148  PHE A CD2 1 
ATOM   5129  C CE1 . PHE C  1 147 ? 27.938  -3.429  -22.422 1.00 23.96  ? 148  PHE A CE1 1 
ATOM   5130  C CE2 . PHE C  1 147 ? 27.374  -1.090  -22.594 1.00 22.68  ? 148  PHE A CE2 1 
ATOM   5131  C CZ  . PHE C  1 147 ? 28.038  -2.126  -21.939 1.00 23.91  ? 148  PHE A CZ  1 
ATOM   5132  N N   . ARG C  1 148 ? 25.298  -4.783  -28.091 1.00 21.44  ? 149  ARG A N   1 
ATOM   5133  C CA  . ARG C  1 148 ? 24.466  -5.311  -29.158 1.00 21.16  ? 149  ARG A CA  1 
ATOM   5134  C C   . ARG C  1 148 ? 22.981  -5.584  -28.794 1.00 22.73  ? 149  ARG A C   1 
ATOM   5135  O O   . ARG C  1 148 ? 22.123  -5.635  -29.695 1.00 23.49  ? 149  ARG A O   1 
ATOM   5136  C CB  . ARG C  1 148 ? 25.133  -6.605  -29.679 1.00 21.46  ? 149  ARG A CB  1 
ATOM   5137  C CG  . ARG C  1 148 ? 26.636  -6.406  -30.026 1.00 24.82  ? 149  ARG A CG  1 
ATOM   5138  C CD  . ARG C  1 148 ? 26.993  -7.214  -31.244 1.00 28.51  ? 149  ARG A CD  1 
ATOM   5139  N NE  . ARG C  1 148 ? 28.396  -7.183  -31.674 1.00 34.16  ? 149  ARG A NE  1 
ATOM   5140  C CZ  . ARG C  1 148 ? 28.899  -6.286  -32.527 1.00 33.76  ? 149  ARG A CZ  1 
ATOM   5141  N NH1 . ARG C  1 148 ? 28.125  -5.302  -32.978 1.00 28.29  ? 149  ARG A NH1 1 
ATOM   5142  N NH2 . ARG C  1 148 ? 30.180  -6.349  -32.907 1.00 26.41  ? 149  ARG A NH2 1 
ATOM   5143  N N   . ASN C  1 149 ? 22.660  -5.711  -27.499 1.00 21.39  ? 150  ASN A N   1 
ATOM   5144  C CA  . ASN C  1 149 ? 21.305  -6.126  -27.098 1.00 23.15  ? 150  ASN A CA  1 
ATOM   5145  C C   . ASN C  1 149 ? 20.396  -4.994  -26.602 1.00 23.31  ? 150  ASN A C   1 
ATOM   5146  O O   . ASN C  1 149 ? 19.179  -5.196  -26.349 1.00 20.09  ? 150  ASN A O   1 
ATOM   5147  C CB  . ASN C  1 149 ? 21.392  -7.231  -26.035 1.00 23.78  ? 150  ASN A CB  1 
ATOM   5148  C CG  . ASN C  1 149 ? 21.925  -8.542  -26.608 1.00 31.38  ? 150  ASN A CG  1 
ATOM   5149  O OD1 . ASN C  1 149 ? 21.551  -8.936  -27.718 1.00 33.24  ? 150  ASN A OD1 1 
ATOM   5150  N ND2 . ASN C  1 149 ? 22.810  -9.215  -25.864 1.00 29.78  ? 150  ASN A ND2 1 
ATOM   5151  N N   . VAL C  1 150 ? 20.973  -3.801  -26.519 1.00 16.69  ? 151  VAL A N   1 
ATOM   5152  C CA  . VAL C  1 150 ? 20.225  -2.612  -26.143 1.00 19.35  ? 151  VAL A CA  1 
ATOM   5153  C C   . VAL C  1 150 ? 20.626  -1.529  -27.112 1.00 17.51  ? 151  VAL A C   1 
ATOM   5154  O O   . VAL C  1 150 ? 21.679  -1.645  -27.717 1.00 18.53  ? 151  VAL A O   1 
ATOM   5155  C CB  . VAL C  1 150 ? 20.532  -2.183  -24.653 1.00 18.56  ? 151  VAL A CB  1 
ATOM   5156  C CG1 . VAL C  1 150 ? 20.031  -3.233  -23.683 1.00 17.97  ? 151  VAL A CG1 1 
ATOM   5157  C CG2 . VAL C  1 150 ? 22.041  -1.988  -24.456 1.00 17.19  ? 151  VAL A CG2 1 
ATOM   5158  N N   . VAL C  1 151 ? 19.839  -0.467  -27.254 1.00 19.88  ? 152  VAL A N   1 
ATOM   5159  C CA  . VAL C  1 151 ? 20.161  0.585   -28.229 1.00 22.04  ? 152  VAL A CA  1 
ATOM   5160  C C   . VAL C  1 151 ? 20.295  2.000   -27.632 1.00 22.40  ? 152  VAL A C   1 
ATOM   5161  O O   . VAL C  1 151 ? 19.521  2.390   -26.775 1.00 24.60  ? 152  VAL A O   1 
ATOM   5162  C CB  . VAL C  1 151 ? 19.118  0.599   -29.371 1.00 25.93  ? 152  VAL A CB  1 
ATOM   5163  C CG1 . VAL C  1 151 ? 19.430  1.708   -30.392 1.00 29.88  ? 152  VAL A CG1 1 
ATOM   5164  C CG2 . VAL C  1 151 ? 19.093  -0.772  -30.075 1.00 26.10  ? 152  VAL A CG2 1 
ATOM   5165  N N   . TRP C  1 152 ? 21.323  2.744   -28.041 1.00 25.12  ? 153  TRP A N   1 
ATOM   5166  C CA  . TRP C  1 152 ? 21.505  4.137   -27.608 1.00 25.21  ? 153  TRP A CA  1 
ATOM   5167  C C   . TRP C  1 152 ? 20.754  5.157   -28.522 1.00 26.88  ? 153  TRP A C   1 
ATOM   5168  O O   . TRP C  1 152 ? 21.243  5.474   -29.610 1.00 26.76  ? 153  TRP A O   1 
ATOM   5169  C CB  . TRP C  1 152 ? 22.997  4.461   -27.585 1.00 25.14  ? 153  TRP A CB  1 
ATOM   5170  C CG  . TRP C  1 152 ? 23.368  5.692   -26.818 1.00 27.24  ? 153  TRP A CG  1 
ATOM   5171  C CD1 . TRP C  1 152 ? 22.515  6.624   -26.271 1.00 24.54  ? 153  TRP A CD1 1 
ATOM   5172  C CD2 . TRP C  1 152 ? 24.698  6.127   -26.501 1.00 24.33  ? 153  TRP A CD2 1 
ATOM   5173  N NE1 . TRP C  1 152 ? 23.241  7.607   -25.629 1.00 22.18  ? 153  TRP A NE1 1 
ATOM   5174  C CE2 . TRP C  1 152 ? 24.581  7.327   -25.751 1.00 25.24  ? 153  TRP A CE2 1 
ATOM   5175  C CE3 . TRP C  1 152 ? 25.975  5.617   -26.770 1.00 24.70  ? 153  TRP A CE3 1 
ATOM   5176  C CZ2 . TRP C  1 152 ? 25.705  8.029   -25.259 1.00 23.58  ? 153  TRP A CZ2 1 
ATOM   5177  C CZ3 . TRP C  1 152 ? 27.100  6.321   -26.282 1.00 29.11  ? 153  TRP A CZ3 1 
ATOM   5178  C CH2 . TRP C  1 152 ? 26.946  7.513   -25.522 1.00 25.55  ? 153  TRP A CH2 1 
ATOM   5179  N N   . LEU C  1 153 ? 19.594  5.658   -28.077 1.00 25.12  ? 154  LEU A N   1 
ATOM   5180  C CA  . LEU C  1 153 ? 18.787  6.634   -28.821 1.00 23.25  ? 154  LEU A CA  1 
ATOM   5181  C C   . LEU C  1 153 ? 19.176  8.101   -28.562 1.00 28.59  ? 154  LEU A C   1 
ATOM   5182  O O   . LEU C  1 153 ? 19.413  8.491   -27.435 1.00 35.25  ? 154  LEU A O   1 
ATOM   5183  C CB  . LEU C  1 153 ? 17.309  6.452   -28.495 1.00 18.27  ? 154  LEU A CB  1 
ATOM   5184  C CG  . LEU C  1 153 ? 16.755  5.045   -28.708 1.00 22.98  ? 154  LEU A CG  1 
ATOM   5185  C CD1 . LEU C  1 153 ? 15.409  4.905   -28.057 1.00 22.07  ? 154  LEU A CD1 1 
ATOM   5186  C CD2 . LEU C  1 153 ? 16.656  4.670   -30.175 1.00 24.60  ? 154  LEU A CD2 1 
ATOM   5187  N N   . THR C  1 154 ? 19.243  8.908   -29.614 1.00 27.64  ? 155  THR A N   1 
ATOM   5188  C CA  . THR C  1 154 ? 19.550  10.329  -29.468 1.00 32.11  ? 155  THR A CA  1 
ATOM   5189  C C   . THR C  1 154 ? 18.597  11.187  -30.312 1.00 30.91  ? 155  THR A C   1 
ATOM   5190  O O   . THR C  1 154 ? 17.813  10.670  -31.101 1.00 34.24  ? 155  THR A O   1 
ATOM   5191  C CB  . THR C  1 154 ? 21.041  10.641  -29.840 1.00 33.46  ? 155  THR A CB  1 
ATOM   5192  O OG1 . THR C  1 154 ? 21.339  10.145  -31.154 1.00 32.16  ? 155  THR A OG1 1 
ATOM   5193  C CG2 . THR C  1 154 ? 22.001  9.986   -28.817 1.00 24.81  ? 155  THR A CG2 1 
ATOM   5194  N N   . LYS C  1 155 ? 18.691  12.498  -30.171 1.00 33.14  ? 156  LYS A N   1 
ATOM   5195  C CA  . LYS C  1 155 ? 17.786  13.393  -30.894 1.00 34.35  ? 156  LYS A CA  1 
ATOM   5196  C C   . LYS C  1 155 ? 18.001  13.313  -32.398 1.00 38.82  ? 156  LYS A C   1 
ATOM   5197  O O   . LYS C  1 155 ? 19.109  13.011  -32.903 1.00 33.20  ? 156  LYS A O   1 
ATOM   5198  C CB  . LYS C  1 155 ? 17.955  14.843  -30.400 1.00 34.48  ? 156  LYS A CB  1 
ATOM   5199  C CG  . LYS C  1 155 ? 19.239  15.511  -30.844 1.00 30.25  ? 156  LYS A CG  1 
ATOM   5200  C CD  . LYS C  1 155 ? 19.384  16.896  -30.222 1.00 41.31  ? 156  LYS A CD  1 
ATOM   5201  C CE  . LYS C  1 155 ? 20.675  17.595  -30.691 1.00 41.78  ? 156  LYS A CE  1 
ATOM   5202  N NZ  . LYS C  1 155 ? 20.866  18.926  -30.021 1.00 43.25  ? 156  LYS A NZ  1 
ATOM   5203  N N   . LYS C  1 156 ? 16.893  13.503  -33.103 1.00 44.36  ? 157  LYS A N   1 
ATOM   5204  C CA  . LYS C  1 156 ? 16.885  13.530  -34.556 1.00 41.74  ? 157  LYS A CA  1 
ATOM   5205  C C   . LYS C  1 156 ? 16.318  14.861  -34.981 1.00 46.77  ? 157  LYS A C   1 
ATOM   5206  O O   . LYS C  1 156 ? 15.291  15.323  -34.441 1.00 46.35  ? 157  LYS A O   1 
ATOM   5207  C CB  . LYS C  1 156 ? 16.074  12.401  -35.145 1.00 37.07  ? 157  LYS A CB  1 
ATOM   5208  C CG  . LYS C  1 156 ? 15.930  12.433  -36.659 1.00 36.18  ? 157  LYS A CG  1 
ATOM   5209  C CD  . LYS C  1 156 ? 15.173  11.191  -37.040 1.00 38.38  ? 157  LYS A CD  1 
ATOM   5210  C CE  . LYS C  1 156 ? 14.814  11.111  -38.495 1.00 45.03  ? 157  LYS A CE  1 
ATOM   5211  N NZ  . LYS C  1 156 ? 14.021  9.851   -38.672 1.00 42.37  ? 157  LYS A NZ  1 
ATOM   5212  N N   . ASP C  1 157 ? 17.009  15.462  -35.946 1.00 48.09  ? 158  ASP A N   1 
ATOM   5213  C CA  . ASP C  1 157 ? 16.844  16.866  -36.280 1.00 52.59  ? 158  ASP A CA  1 
ATOM   5214  C C   . ASP C  1 157 ? 17.185  17.652  -35.000 1.00 58.72  ? 158  ASP A C   1 
ATOM   5215  O O   . ASP C  1 157 ? 18.323  17.545  -34.491 1.00 57.01  ? 158  ASP A O   1 
ATOM   5216  C CB  . ASP C  1 157 ? 15.438  17.125  -36.832 1.00 45.94  ? 158  ASP A CB  1 
ATOM   5217  C CG  . ASP C  1 157 ? 15.149  16.275  -38.111 1.00 59.99  ? 158  ASP A CG  1 
ATOM   5218  O OD1 . ASP C  1 157 ? 16.077  16.042  -38.936 1.00 47.62  ? 158  ASP A OD1 1 
ATOM   5219  O OD2 . ASP C  1 157 ? 13.990  15.825  -38.283 1.00 62.86  ? 158  ASP A OD2 1 
ATOM   5220  N N   . ASN C  1 158 ? 16.237  18.375  -34.422 1.00 46.10  ? 159  ASN A N   1 
ATOM   5221  C CA  . ASN C  1 158 ? 16.554  18.971  -33.133 1.00 46.23  ? 159  ASN A CA  1 
ATOM   5222  C C   . ASN C  1 158 ? 15.457  18.673  -32.145 1.00 44.35  ? 159  ASN A C   1 
ATOM   5223  O O   . ASN C  1 158 ? 15.024  19.540  -31.387 1.00 47.15  ? 159  ASN A O   1 
ATOM   5224  C CB  . ASN C  1 158 ? 16.791  20.482  -33.254 1.00 49.14  ? 159  ASN A CB  1 
ATOM   5225  C CG  . ASN C  1 158 ? 18.268  20.826  -33.378 1.00 51.72  ? 159  ASN A CG  1 
ATOM   5226  O OD1 . ASN C  1 158 ? 18.983  20.930  -32.384 1.00 56.80  ? 159  ASN A OD1 1 
ATOM   5227  N ND2 . ASN C  1 158 ? 18.729  20.991  -34.598 1.00 47.68  ? 159  ASN A ND2 1 
ATOM   5228  N N   . ALA C  1 159 ? 15.004  17.429  -32.156 1.00 40.30  ? 160  ALA A N   1 
ATOM   5229  C CA  . ALA C  1 159 ? 13.916  17.042  -31.281 1.00 39.70  ? 160  ALA A CA  1 
ATOM   5230  C C   . ALA C  1 159 ? 14.095  15.634  -30.770 1.00 40.68  ? 160  ALA A C   1 
ATOM   5231  O O   . ALA C  1 159 ? 14.763  14.799  -31.409 1.00 37.67  ? 160  ALA A O   1 
ATOM   5232  C CB  . ALA C  1 159 ? 12.588  17.161  -31.991 1.00 35.01  ? 160  ALA A CB  1 
ATOM   5233  N N   . TYR C  1 160 ? 13.487  15.406  -29.607 1.00 35.88  ? 161  TYR A N   1 
ATOM   5234  C CA  . TYR C  1 160 ? 13.358  14.102  -28.991 1.00 30.55  ? 161  TYR A CA  1 
ATOM   5235  C C   . TYR C  1 160 ? 11.905  14.011  -28.516 1.00 34.24  ? 161  TYR A C   1 
ATOM   5236  O O   . TYR C  1 160 ? 11.583  14.352  -27.369 1.00 35.90  ? 161  TYR A O   1 
ATOM   5237  C CB  . TYR C  1 160 ? 14.361  13.955  -27.830 1.00 29.18  ? 161  TYR A CB  1 
ATOM   5238  C CG  . TYR C  1 160 ? 14.573  12.532  -27.318 1.00 29.43  ? 161  TYR A CG  1 
ATOM   5239  C CD1 . TYR C  1 160 ? 13.564  11.840  -26.662 1.00 27.18  ? 161  TYR A CD1 1 
ATOM   5240  C CD2 . TYR C  1 160 ? 15.780  11.877  -27.522 1.00 28.87  ? 161  TYR A CD2 1 
ATOM   5241  C CE1 . TYR C  1 160 ? 13.764  10.551  -26.212 1.00 29.02  ? 161  TYR A CE1 1 
ATOM   5242  C CE2 . TYR C  1 160 ? 15.983  10.590  -27.084 1.00 23.67  ? 161  TYR A CE2 1 
ATOM   5243  C CZ  . TYR C  1 160 ? 14.973  9.935   -26.430 1.00 26.29  ? 161  TYR A CZ  1 
ATOM   5244  O OH  . TYR C  1 160 ? 15.175  8.664   -25.966 1.00 26.30  ? 161  TYR A OH  1 
ATOM   5245  N N   . PRO C  1 161 ? 11.010  13.580  -29.411 1.00 34.97  ? 162  PRO A N   1 
ATOM   5246  C CA  . PRO C  1 161 ? 9.593   13.390  -29.087 1.00 31.08  ? 162  PRO A CA  1 
ATOM   5247  C C   . PRO C  1 161 ? 9.406   12.361  -27.978 1.00 32.71  ? 162  PRO A C   1 
ATOM   5248  O O   . PRO C  1 161 ? 10.296  11.541  -27.754 1.00 35.64  ? 162  PRO A O   1 
ATOM   5249  C CB  . PRO C  1 161 ? 8.994   12.887  -30.404 1.00 27.64  ? 162  PRO A CB  1 
ATOM   5250  C CG  . PRO C  1 161 ? 9.954   13.251  -31.437 1.00 33.94  ? 162  PRO A CG  1 
ATOM   5251  C CD  . PRO C  1 161 ? 11.302  13.257  -30.815 1.00 37.45  ? 162  PRO A CD  1 
ATOM   5252  N N   . THR C  1 162 ? 8.272   12.383  -27.295 1.00 32.73  ? 163  THR A N   1 
ATOM   5253  C CA  . THR C  1 162 ? 8.059   11.429  -26.213 1.00 30.93  ? 163  THR A CA  1 
ATOM   5254  C C   . THR C  1 162 ? 7.798   10.012  -26.735 1.00 32.47  ? 163  THR A C   1 
ATOM   5255  O O   . THR C  1 162 ? 7.002   9.818   -27.648 1.00 34.19  ? 163  THR A O   1 
ATOM   5256  C CB  . THR C  1 162 ? 6.911   11.883  -25.295 1.00 28.54  ? 163  THR A CB  1 
ATOM   5257  O OG1 . THR C  1 162 ? 7.324   13.082  -24.620 1.00 37.44  ? 163  THR A OG1 1 
ATOM   5258  C CG2 . THR C  1 162 ? 6.568   10.803  -24.256 1.00 31.50  ? 163  THR A CG2 1 
ATOM   5259  N N   . ILE C  1 163 ? 8.528   9.047   -26.177 1.00 30.48  ? 164  ILE A N   1 
ATOM   5260  C CA  . ILE C  1 163 ? 8.415   7.642   -26.526 1.00 29.59  ? 164  ILE A CA  1 
ATOM   5261  C C   . ILE C  1 163 ? 7.460   6.893   -25.623 1.00 33.38  ? 164  ILE A C   1 
ATOM   5262  O O   . ILE C  1 163 ? 7.569   6.973   -24.403 1.00 39.14  ? 164  ILE A O   1 
ATOM   5263  C CB  . ILE C  1 163 ? 9.786   6.957   -26.499 1.00 32.89  ? 164  ILE A CB  1 
ATOM   5264  C CG1 . ILE C  1 163 ? 10.677  7.584   -27.592 1.00 31.14  ? 164  ILE A CG1 1 
ATOM   5265  C CG2 . ILE C  1 163 ? 9.621   5.441   -26.702 1.00 30.77  ? 164  ILE A CG2 1 
ATOM   5266  C CD1 . ILE C  1 163 ? 12.114  7.041   -27.706 1.00 26.64  ? 164  ILE A CD1 1 
ATOM   5267  N N   . LYS C  1 164 ? 6.518   6.181   -26.240 1.00 31.89  ? 165  LYS A N   1 
ATOM   5268  C CA  . LYS C  1 164 ? 5.560   5.305   -25.559 1.00 29.25  ? 165  LYS A CA  1 
ATOM   5269  C C   . LYS C  1 164 ? 5.600   4.002   -26.299 1.00 27.56  ? 165  LYS A C   1 
ATOM   5270  O O   . LYS C  1 164 ? 5.168   3.933   -27.440 1.00 37.35  ? 165  LYS A O   1 
ATOM   5271  C CB  . LYS C  1 164 ? 4.145   5.871   -25.591 1.00 28.46  ? 165  LYS A CB  1 
ATOM   5272  C CG  . LYS C  1 164 ? 3.973   7.178   -24.825 1.00 35.92  ? 165  LYS A CG  1 
ATOM   5273  C CD  . LYS C  1 164 ? 2.552   7.722   -24.964 1.00 39.49  ? 165  LYS A CD  1 
ATOM   5274  C CE  . LYS C  1 164 ? 2.422   9.103   -24.316 1.00 49.14  ? 165  LYS A CE  1 
ATOM   5275  N NZ  . LYS C  1 164 ? 1.073   9.716   -24.541 1.00 59.37  ? 165  LYS A NZ  1 
ATOM   5276  N N   . ARG C  1 165 ? 6.152   2.969   -25.697 1.00 32.49  ? 166  ARG A N   1 
ATOM   5277  C CA  . ARG C  1 165 ? 6.358   1.724   -26.412 1.00 27.90  ? 166  ARG A CA  1 
ATOM   5278  C C   . ARG C  1 165 ? 5.749   0.635   -25.513 1.00 36.56  ? 166  ARG A C   1 
ATOM   5279  O O   . ARG C  1 165 ? 5.606   0.862   -24.302 1.00 40.08  ? 166  ARG A O   1 
ATOM   5280  C CB  . ARG C  1 165 ? 7.843   1.526   -26.709 1.00 24.46  ? 166  ARG A CB  1 
ATOM   5281  C CG  . ARG C  1 165 ? 8.159   0.448   -27.714 1.00 35.72  ? 166  ARG A CG  1 
ATOM   5282  C CD  . ARG C  1 165 ? 8.752   0.987   -29.061 1.00 33.80  ? 166  ARG A CD  1 
ATOM   5283  N NE  . ARG C  1 165 ? 8.275   2.311   -29.450 1.00 33.68  ? 166  ARG A NE  1 
ATOM   5284  C CZ  . ARG C  1 165 ? 8.682   2.978   -30.534 1.00 36.62  ? 166  ARG A CZ  1 
ATOM   5285  N NH1 . ARG C  1 165 ? 9.576   2.437   -31.373 1.00 36.99  ? 166  ARG A NH1 1 
ATOM   5286  N NH2 . ARG C  1 165 ? 8.206   4.202   -30.781 1.00 31.92  ? 166  ARG A NH2 1 
ATOM   5287  N N   . SER C  1 166 ? 5.264   -0.472  -26.087 1.00 37.97  ? 167  SER A N   1 
ATOM   5288  C CA  . SER C  1 166 ? 4.623   -1.523  -25.275 1.00 34.95  ? 167  SER A CA  1 
ATOM   5289  C C   . SER C  1 166 ? 4.866   -2.948  -25.745 1.00 36.72  ? 167  SER A C   1 
ATOM   5290  O O   . SER C  1 166 ? 5.103   -3.170  -26.925 1.00 41.61  ? 167  SER A O   1 
ATOM   5291  C CB  . SER C  1 166 ? 3.132   -1.306  -25.230 1.00 35.32  ? 167  SER A CB  1 
ATOM   5292  O OG  . SER C  1 166 ? 2.549   -2.403  -24.586 1.00 44.76  ? 167  SER A OG  1 
ATOM   5293  N N   . TYR C  1 167 ? 4.819   -3.919  -24.835 1.00 33.76  ? 168  TYR A N   1 
ATOM   5294  C CA  . TYR C  1 167 ? 4.954   -5.313  -25.257 1.00 33.47  ? 168  TYR A CA  1 
ATOM   5295  C C   . TYR C  1 167 ? 4.178   -6.254  -24.334 1.00 39.70  ? 168  TYR A C   1 
ATOM   5296  O O   . TYR C  1 167 ? 4.313   -6.157  -23.105 1.00 46.11  ? 168  TYR A O   1 
ATOM   5297  C CB  . TYR C  1 167 ? 6.432   -5.713  -25.327 1.00 31.28  ? 168  TYR A CB  1 
ATOM   5298  C CG  . TYR C  1 167 ? 6.655   -7.156  -25.689 1.00 31.87  ? 168  TYR A CG  1 
ATOM   5299  C CD1 . TYR C  1 167 ? 6.450   -8.170  -24.763 1.00 38.84  ? 168  TYR A CD1 1 
ATOM   5300  C CD2 . TYR C  1 167 ? 7.079   -7.513  -26.951 1.00 31.88  ? 168  TYR A CD2 1 
ATOM   5301  C CE1 . TYR C  1 167 ? 6.640   -9.506  -25.101 1.00 39.52  ? 168  TYR A CE1 1 
ATOM   5302  C CE2 . TYR C  1 167 ? 7.276   -8.846  -27.300 1.00 33.31  ? 168  TYR A CE2 1 
ATOM   5303  C CZ  . TYR C  1 167 ? 7.055   -9.838  -26.366 1.00 38.46  ? 168  TYR A CZ  1 
ATOM   5304  O OH  . TYR C  1 167 ? 7.253   -11.171 -26.676 1.00 45.76  ? 168  TYR A OH  1 
ATOM   5305  N N   . ASN C  1 168 ? 3.399   -7.174  -24.916 1.00 36.54  ? 169  ASN A N   1 
ATOM   5306  C CA  . ASN C  1 168 ? 2.664   -8.203  -24.170 1.00 33.79  ? 169  ASN A CA  1 
ATOM   5307  C C   . ASN C  1 168 ? 3.323   -9.573  -24.337 1.00 32.65  ? 169  ASN A C   1 
ATOM   5308  O O   . ASN C  1 168 ? 3.470   -10.087 -25.425 1.00 38.25  ? 169  ASN A O   1 
ATOM   5309  C CB  . ASN C  1 168 ? 1.191   -8.244  -24.619 1.00 36.98  ? 169  ASN A CB  1 
ATOM   5310  C CG  . ASN C  1 168 ? 0.319   -9.214  -23.785 1.00 51.00  ? 169  ASN A CG  1 
ATOM   5311  O OD1 . ASN C  1 168 ? 0.631   -10.404 -23.657 1.00 51.77  ? 169  ASN A OD1 1 
ATOM   5312  N ND2 . ASN C  1 168 ? -0.802  -8.710  -23.252 1.00 56.37  ? 169  ASN A ND2 1 
ATOM   5313  N N   . ASN C  1 169 ? 3.703   -10.196 -23.239 1.00 42.60  ? 170  ASN A N   1 
ATOM   5314  C CA  . ASN C  1 169 ? 4.349   -11.496 -23.343 1.00 40.72  ? 170  ASN A CA  1 
ATOM   5315  C C   . ASN C  1 169 ? 3.361   -12.612 -23.668 1.00 47.82  ? 170  ASN A C   1 
ATOM   5316  O O   . ASN C  1 169 ? 2.864   -13.277 -22.756 1.00 48.89  ? 170  ASN A O   1 
ATOM   5317  C CB  . ASN C  1 169 ? 5.096   -11.810 -22.050 1.00 31.94  ? 170  ASN A CB  1 
ATOM   5318  C CG  . ASN C  1 169 ? 5.869   -13.112 -22.127 1.00 39.67  ? 170  ASN A CG  1 
ATOM   5319  O OD1 . ASN C  1 169 ? 6.029   -13.697 -23.197 1.00 38.83  ? 170  ASN A OD1 1 
ATOM   5320  N ND2 . ASN C  1 169 ? 6.381   -13.562 -20.986 1.00 45.21  ? 170  ASN A ND2 1 
ATOM   5321  N N   . THR C  1 170 ? 3.090   -12.846 -24.955 1.00 45.86  ? 171  THR A N   1 
ATOM   5322  C CA  . THR C  1 170 ? 2.120   -13.885 -25.314 1.00 42.18  ? 171  THR A CA  1 
ATOM   5323  C C   . THR C  1 170 ? 2.734   -15.287 -25.335 1.00 46.40  ? 171  THR A C   1 
ATOM   5324  O O   . THR C  1 170 ? 2.063   -16.233 -25.729 1.00 58.27  ? 171  THR A O   1 
ATOM   5325  C CB  . THR C  1 170 ? 1.456   -13.627 -26.701 1.00 44.42  ? 171  THR A CB  1 
ATOM   5326  O OG1 . THR C  1 170 ? 2.420   -13.734 -27.761 1.00 54.65  ? 171  THR A OG1 1 
ATOM   5327  C CG2 . THR C  1 170 ? 0.769   -12.270 -26.746 1.00 41.50  ? 171  THR A CG2 1 
ATOM   5328  N N   . ASN C  1 171 ? 3.988   -15.435 -24.902 1.00 49.44  ? 172  ASN A N   1 
ATOM   5329  C CA  . ASN C  1 171 ? 4.650   -16.759 -24.839 1.00 47.81  ? 172  ASN A CA  1 
ATOM   5330  C C   . ASN C  1 171 ? 4.273   -17.507 -23.588 1.00 49.67  ? 172  ASN A C   1 
ATOM   5331  O O   . ASN C  1 171 ? 3.762   -16.919 -22.635 1.00 55.19  ? 172  ASN A O   1 
ATOM   5332  C CB  . ASN C  1 171 ? 6.189   -16.658 -24.879 1.00 47.51  ? 172  ASN A CB  1 
ATOM   5333  C CG  . ASN C  1 171 ? 6.715   -15.937 -26.098 1.00 49.98  ? 172  ASN A CG  1 
ATOM   5334  O OD1 . ASN C  1 171 ? 6.880   -16.543 -27.162 1.00 52.33  ? 172  ASN A OD1 1 
ATOM   5335  N ND2 . ASN C  1 171 ? 6.966   -14.628 -25.959 1.00 44.73  ? 172  ASN A ND2 1 
ATOM   5336  N N   . GLN C  1 172 ? 4.539   -18.803 -23.572 1.00 51.54  ? 173  GLN A N   1 
ATOM   5337  C CA  . GLN C  1 172 ? 4.208   -19.599 -22.398 1.00 56.58  ? 173  GLN A CA  1 
ATOM   5338  C C   . GLN C  1 172 ? 5.233   -19.388 -21.294 1.00 57.01  ? 173  GLN A C   1 
ATOM   5339  O O   . GLN C  1 172 ? 4.887   -19.372 -20.108 1.00 54.52  ? 173  GLN A O   1 
ATOM   5340  C CB  . GLN C  1 172 ? 4.113   -21.080 -22.767 1.00 60.55  ? 173  GLN A CB  1 
ATOM   5341  C CG  . GLN C  1 172 ? 3.022   -21.363 -23.791 1.00 63.93  ? 173  GLN A CG  1 
ATOM   5342  C CD  . GLN C  1 172 ? 1.672   -20.822 -23.346 1.00 70.82  ? 173  GLN A CD  1 
ATOM   5343  O OE1 . GLN C  1 172 ? 1.076   -21.330 -22.388 1.00 65.44  ? 173  GLN A OE1 1 
ATOM   5344  N NE2 . GLN C  1 172 ? 1.190   -19.772 -24.027 1.00 71.56  ? 173  GLN A NE2 1 
ATOM   5345  N N   . GLU C  1 173 ? 6.478   -19.146 -21.701 1.00 55.27  ? 174  GLU A N   1 
ATOM   5346  C CA  . GLU C  1 173 ? 7.583   -18.977 -20.766 1.00 48.28  ? 174  GLU A CA  1 
ATOM   5347  C C   . GLU C  1 173 ? 7.803   -17.522 -20.368 1.00 43.04  ? 174  GLU A C   1 
ATOM   5348  O O   . GLU C  1 173 ? 7.192   -16.618 -20.937 1.00 44.11  ? 174  GLU A O   1 
ATOM   5349  C CB  . GLU C  1 173 ? 8.863   -19.586 -21.355 1.00 46.35  ? 174  GLU A CB  1 
ATOM   5350  C CG  . GLU C  1 173 ? 9.104   -19.308 -22.825 1.00 53.15  ? 174  GLU A CG  1 
ATOM   5351  C CD  . GLU C  1 173 ? 8.423   -20.318 -23.753 1.00 60.99  ? 174  GLU A CD  1 
ATOM   5352  O OE1 . GLU C  1 173 ? 8.842   -21.501 -23.762 1.00 63.50  ? 174  GLU A OE1 1 
ATOM   5353  O OE2 . GLU C  1 173 ? 7.505   -19.910 -24.505 1.00 59.79  ? 174  GLU A OE2 1 
ATOM   5354  N N   . ASP C  1 174 ? 8.582   -17.327 -19.301 1.00 42.47  ? 175  ASP A N   1 
ATOM   5355  C CA  . ASP C  1 174 ? 8.933   -15.998 -18.780 1.00 40.16  ? 175  ASP A CA  1 
ATOM   5356  C C   . ASP C  1 174 ? 10.062  -15.330 -19.572 1.00 36.11  ? 175  ASP A C   1 
ATOM   5357  O O   . ASP C  1 174 ? 10.929  -16.020 -20.139 1.00 33.92  ? 175  ASP A O   1 
ATOM   5358  C CB  . ASP C  1 174 ? 9.358   -16.095 -17.309 1.00 42.75  ? 175  ASP A CB  1 
ATOM   5359  C CG  . ASP C  1 174 ? 8.213   -16.473 -16.378 1.00 48.92  ? 175  ASP A CG  1 
ATOM   5360  O OD1 . ASP C  1 174 ? 7.034   -16.174 -16.715 1.00 44.94  ? 175  ASP A OD1 1 
ATOM   5361  O OD2 . ASP C  1 174 ? 8.517   -17.096 -15.324 1.00 44.88  ? 175  ASP A OD2 1 
ATOM   5362  N N   . LEU C  1 175 ? 10.088  -13.995 -19.523 1.00 33.80  ? 176  LEU A N   1 
ATOM   5363  C CA  . LEU C  1 175 ? 11.048  -13.164 -20.259 1.00 33.23  ? 176  LEU A CA  1 
ATOM   5364  C C   . LEU C  1 175 ? 12.017  -12.380 -19.366 1.00 34.85  ? 176  LEU A C   1 
ATOM   5365  O O   . LEU C  1 175 ? 11.572  -11.600 -18.510 1.00 36.03  ? 176  LEU A O   1 
ATOM   5366  C CB  . LEU C  1 175 ? 10.284  -12.147 -21.097 1.00 32.76  ? 176  LEU A CB  1 
ATOM   5367  C CG  . LEU C  1 175 ? 10.054  -12.311 -22.579 1.00 34.33  ? 176  LEU A CG  1 
ATOM   5368  C CD1 . LEU C  1 175 ? 9.371   -11.051 -23.035 1.00 36.43  ? 176  LEU A CD1 1 
ATOM   5369  C CD2 . LEU C  1 175 ? 11.359  -12.564 -23.344 1.00 34.49  ? 176  LEU A CD2 1 
ATOM   5370  N N   . LEU C  1 176 ? 13.322  -12.498 -19.635 1.00 33.30  ? 177  LEU A N   1 
ATOM   5371  C CA  . LEU C  1 176 ? 14.343  -11.650 -18.993 1.00 28.24  ? 177  LEU A CA  1 
ATOM   5372  C C   . LEU C  1 176 ? 14.606  -10.438 -19.854 1.00 29.74  ? 177  LEU A C   1 
ATOM   5373  O O   . LEU C  1 176 ? 15.248  -10.573 -20.924 1.00 26.38  ? 177  LEU A O   1 
ATOM   5374  C CB  . LEU C  1 176 ? 15.656  -12.429 -18.793 1.00 26.51  ? 177  LEU A CB  1 
ATOM   5375  C CG  . LEU C  1 176 ? 16.908  -11.637 -18.373 1.00 28.72  ? 177  LEU A CG  1 
ATOM   5376  C CD1 . LEU C  1 176 ? 16.767  -10.978 -17.013 1.00 20.71  ? 177  LEU A CD1 1 
ATOM   5377  C CD2 . LEU C  1 176 ? 18.206  -12.472 -18.447 1.00 25.99  ? 177  LEU A CD2 1 
ATOM   5378  N N   . VAL C  1 177 ? 14.161  -9.266  -19.382 1.00 24.20  ? 178  VAL A N   1 
ATOM   5379  C CA  . VAL C  1 177 ? 14.274  -8.013  -20.143 1.00 23.26  ? 178  VAL A CA  1 
ATOM   5380  C C   . VAL C  1 177 ? 15.284  -7.023  -19.505 1.00 29.32  ? 178  VAL A C   1 
ATOM   5381  O O   . VAL C  1 177 ? 15.245  -6.799  -18.282 1.00 28.78  ? 178  VAL A O   1 
ATOM   5382  C CB  . VAL C  1 177 ? 12.865  -7.353  -20.277 1.00 25.81  ? 178  VAL A CB  1 
ATOM   5383  C CG1 . VAL C  1 177 ? 12.879  -6.109  -21.157 1.00 25.01  ? 178  VAL A CG1 1 
ATOM   5384  C CG2 . VAL C  1 177 ? 11.853  -8.367  -20.800 1.00 30.02  ? 178  VAL A CG2 1 
ATOM   5385  N N   . LEU C  1 178 ? 16.157  -6.418  -20.332 1.00 24.81  ? 179  LEU A N   1 
ATOM   5386  C CA  . LEU C  1 178 ? 17.214  -5.521  -19.854 1.00 23.19  ? 179  LEU A CA  1 
ATOM   5387  C C   . LEU C  1 178 ? 17.120  -4.104  -20.485 1.00 23.74  ? 179  LEU A C   1 
ATOM   5388  O O   . LEU C  1 178 ? 16.894  -3.977  -21.677 1.00 27.33  ? 179  LEU A O   1 
ATOM   5389  C CB  . LEU C  1 178 ? 18.574  -6.132  -20.192 1.00 26.70  ? 179  LEU A CB  1 
ATOM   5390  C CG  . LEU C  1 178 ? 18.892  -7.608  -19.946 1.00 24.37  ? 179  LEU A CG  1 
ATOM   5391  C CD1 . LEU C  1 178 ? 20.019  -7.980  -20.881 1.00 23.78  ? 179  LEU A CD1 1 
ATOM   5392  C CD2 . LEU C  1 178 ? 19.362  -7.801  -18.577 1.00 20.66  ? 179  LEU A CD2 1 
ATOM   5393  N N   . TRP C  1 179 ? 17.398  -3.047  -19.726 1.00 24.52  ? 180  TRP A N   1 
ATOM   5394  C CA  . TRP C  1 179 ? 17.371  -1.679  -20.290 1.00 24.37  ? 180  TRP A CA  1 
ATOM   5395  C C   . TRP C  1 179 ? 18.253  -0.794  -19.463 1.00 22.50  ? 180  TRP A C   1 
ATOM   5396  O O   . TRP C  1 179 ? 18.775  -1.262  -18.465 1.00 23.54  ? 180  TRP A O   1 
ATOM   5397  C CB  . TRP C  1 179 ? 15.952  -1.100  -20.336 1.00 26.36  ? 180  TRP A CB  1 
ATOM   5398  C CG  . TRP C  1 179 ? 15.335  -0.849  -18.979 1.00 27.09  ? 180  TRP A CG  1 
ATOM   5399  C CD1 . TRP C  1 179 ? 15.358  0.325   -18.257 1.00 24.77  ? 180  TRP A CD1 1 
ATOM   5400  C CD2 . TRP C  1 179 ? 14.585  -1.791  -18.198 1.00 22.72  ? 180  TRP A CD2 1 
ATOM   5401  N NE1 . TRP C  1 179 ? 14.679  0.154   -17.071 1.00 23.73  ? 180  TRP A NE1 1 
ATOM   5402  C CE2 . TRP C  1 179 ? 14.203  -1.135  -17.005 1.00 24.05  ? 180  TRP A CE2 1 
ATOM   5403  C CE3 . TRP C  1 179 ? 14.220  -3.133  -18.382 1.00 25.74  ? 180  TRP A CE3 1 
ATOM   5404  C CZ2 . TRP C  1 179 ? 13.448  -1.779  -16.001 1.00 22.59  ? 180  TRP A CZ2 1 
ATOM   5405  C CZ3 . TRP C  1 179 ? 13.475  -3.783  -17.377 1.00 24.01  ? 180  TRP A CZ3 1 
ATOM   5406  C CH2 . TRP C  1 179 ? 13.098  -3.099  -16.207 1.00 22.88  ? 180  TRP A CH2 1 
ATOM   5407  N N   . GLY C  1 180 ? 18.462  0.455   -19.869 1.00 19.42  ? 181  GLY A N   1 
ATOM   5408  C CA  . GLY C  1 180 ? 19.414  1.292   -19.150 1.00 21.33  ? 181  GLY A CA  1 
ATOM   5409  C C   . GLY C  1 180 ? 19.180  2.792   -19.188 1.00 21.87  ? 181  GLY A C   1 
ATOM   5410  O O   . GLY C  1 180 ? 18.306  3.252   -19.918 1.00 23.47  ? 181  GLY A O   1 
ATOM   5411  N N   . ILE C  1 181 ? 19.988  3.560   -18.448 1.00 19.51  ? 182  ILE A N   1 
ATOM   5412  C CA  . ILE C  1 181 ? 19.945  5.027   -18.533 1.00 20.17  ? 182  ILE A CA  1 
ATOM   5413  C C   . ILE C  1 181 ? 21.391  5.615   -18.634 1.00 24.00  ? 182  ILE A C   1 
ATOM   5414  O O   . ILE C  1 181 ? 22.313  5.083   -18.022 1.00 29.28  ? 182  ILE A O   1 
ATOM   5415  C CB  . ILE C  1 181 ? 19.170  5.648   -17.318 1.00 22.37  ? 182  ILE A CB  1 
ATOM   5416  C CG1 . ILE C  1 181 ? 19.194  7.179   -17.406 1.00 26.16  ? 182  ILE A CG1 1 
ATOM   5417  C CG2 . ILE C  1 181 ? 19.784  5.201   -15.945 1.00 24.00  ? 182  ILE A CG2 1 
ATOM   5418  C CD1 . ILE C  1 181 ? 18.515  7.978   -16.217 1.00 21.02  ? 182  ILE A CD1 1 
ATOM   5419  N N   . HIS C  1 182 ? 21.594  6.667   -19.443 1.00 23.22  ? 183  HIS A N   1 
ATOM   5420  C CA  . HIS C  1 182 ? 22.886  7.363   -19.557 1.00 24.71  ? 183  HIS A CA  1 
ATOM   5421  C C   . HIS C  1 182 ? 22.962  8.657   -18.694 1.00 29.51  ? 183  HIS A C   1 
ATOM   5422  O O   . HIS C  1 182 ? 22.129  9.580   -18.839 1.00 28.16  ? 183  HIS A O   1 
ATOM   5423  C CB  . HIS C  1 182 ? 23.168  7.789   -20.988 1.00 24.59  ? 183  HIS A CB  1 
ATOM   5424  C CG  . HIS C  1 182 ? 24.495  8.469   -21.165 1.00 27.76  ? 183  HIS A CG  1 
ATOM   5425  N ND1 . HIS C  1 182 ? 24.619  9.739   -21.691 1.00 29.58  ? 183  HIS A ND1 1 
ATOM   5426  C CD2 . HIS C  1 182 ? 25.763  8.018   -20.966 1.00 27.46  ? 183  HIS A CD2 1 
ATOM   5427  C CE1 . HIS C  1 182 ? 25.902  10.062  -21.758 1.00 29.36  ? 183  HIS A CE1 1 
ATOM   5428  N NE2 . HIS C  1 182 ? 26.618  9.035   -21.328 1.00 26.49  ? 183  HIS A NE2 1 
ATOM   5429  N N   . HIS C  1 183 ? 23.999  8.735   -17.859 1.00 28.78  ? 184  HIS A N   1 
ATOM   5430  C CA  . HIS C  1 183 ? 24.303  9.910   -17.028 1.00 31.97  ? 184  HIS A CA  1 
ATOM   5431  C C   . HIS C  1 183 ? 25.422  10.765  -17.637 1.00 34.55  ? 184  HIS A C   1 
ATOM   5432  O O   . HIS C  1 183 ? 26.587  10.380  -17.582 1.00 35.74  ? 184  HIS A O   1 
ATOM   5433  C CB  . HIS C  1 183 ? 24.728  9.472   -15.621 1.00 28.95  ? 184  HIS A CB  1 
ATOM   5434  C CG  . HIS C  1 183 ? 23.708  8.642   -14.901 1.00 33.10  ? 184  HIS A CG  1 
ATOM   5435  N ND1 . HIS C  1 183 ? 22.570  9.187   -14.339 1.00 29.33  ? 184  HIS A ND1 1 
ATOM   5436  C CD2 . HIS C  1 183 ? 23.652  7.310   -14.642 1.00 33.51  ? 184  HIS A CD2 1 
ATOM   5437  C CE1 . HIS C  1 183 ? 21.863  8.232   -13.759 1.00 24.57  ? 184  HIS A CE1 1 
ATOM   5438  N NE2 . HIS C  1 183 ? 22.496  7.083   -13.928 1.00 29.66  ? 184  HIS A NE2 1 
ATOM   5439  N N   . PRO C  1 184 ? 25.076  11.921  -18.230 1.00 33.69  ? 185  PRO A N   1 
ATOM   5440  C CA  . PRO C  1 184 ? 26.091  12.786  -18.844 1.00 36.80  ? 185  PRO A CA  1 
ATOM   5441  C C   . PRO C  1 184 ? 26.994  13.531  -17.832 1.00 42.32  ? 185  PRO A C   1 
ATOM   5442  O O   . PRO C  1 184 ? 26.824  13.420  -16.621 1.00 37.96  ? 185  PRO A O   1 
ATOM   5443  C CB  . PRO C  1 184 ? 25.247  13.788  -19.651 1.00 38.09  ? 185  PRO A CB  1 
ATOM   5444  C CG  . PRO C  1 184 ? 23.871  13.209  -19.722 1.00 32.03  ? 185  PRO A CG  1 
ATOM   5445  C CD  . PRO C  1 184 ? 23.712  12.420  -18.472 1.00 30.67  ? 185  PRO A CD  1 
ATOM   5446  N N   . ASN C  1 185 ? 27.951  14.303  -18.335 1.00 45.31  ? 186  ASN A N   1 
ATOM   5447  C CA  . ASN C  1 185 ? 28.879  15.017  -17.460 1.00 45.64  ? 186  ASN A CA  1 
ATOM   5448  C C   . ASN C  1 185 ? 28.462  16.488  -17.186 1.00 49.40  ? 186  ASN A C   1 
ATOM   5449  O O   . ASN C  1 185 ? 28.767  17.041  -16.124 1.00 48.83  ? 186  ASN A O   1 
ATOM   5450  C CB  . ASN C  1 185 ? 30.291  14.973  -18.058 1.00 49.46  ? 186  ASN A CB  1 
ATOM   5451  C CG  . ASN C  1 185 ? 31.297  15.787  -17.246 1.00 57.12  ? 186  ASN A CG  1 
ATOM   5452  O OD1 . ASN C  1 185 ? 31.812  15.324  -16.212 1.00 54.90  ? 186  ASN A OD1 1 
ATOM   5453  N ND2 . ASN C  1 185 ? 31.576  17.014  -17.707 1.00 53.24  ? 186  ASN A ND2 1 
ATOM   5454  N N   . ASP C  1 186 ? 27.771  17.112  -18.143 1.00 50.98  ? 187  ASP A N   1 
ATOM   5455  C CA  . ASP C  1 186 ? 27.305  18.494  -18.008 1.00 45.98  ? 187  ASP A CA  1 
ATOM   5456  C C   . ASP C  1 186 ? 26.123  18.834  -18.913 1.00 46.47  ? 187  ASP A C   1 
ATOM   5457  O O   . ASP C  1 186 ? 25.836  18.120  -19.870 1.00 45.43  ? 187  ASP A O   1 
ATOM   5458  C CB  . ASP C  1 186 ? 28.460  19.457  -18.283 1.00 46.21  ? 187  ASP A CB  1 
ATOM   5459  C CG  . ASP C  1 186 ? 29.129  19.212  -19.628 1.00 50.67  ? 187  ASP A CG  1 
ATOM   5460  O OD1 . ASP C  1 186 ? 28.490  19.382  -20.698 1.00 50.53  ? 187  ASP A OD1 1 
ATOM   5461  O OD2 . ASP C  1 186 ? 30.321  18.842  -19.598 1.00 51.54  ? 187  ASP A OD2 1 
ATOM   5462  N N   . ALA C  1 187 ? 25.488  19.971  -18.643 1.00 50.45  ? 188  ALA A N   1 
ATOM   5463  C CA  . ALA C  1 187 ? 24.233  20.345  -19.292 1.00 43.79  ? 188  ALA A CA  1 
ATOM   5464  C C   . ALA C  1 187 ? 24.355  20.477  -20.804 1.00 48.11  ? 188  ALA A C   1 
ATOM   5465  O O   . ALA C  1 187 ? 23.376  20.290  -21.549 1.00 42.31  ? 188  ALA A O   1 
ATOM   5466  C CB  . ALA C  1 187 ? 23.718  21.639  -18.705 1.00 35.90  ? 188  ALA A CB  1 
ATOM   5467  N N   . THR C  1 188 ? 25.564  20.785  -21.253 1.00 44.06  ? 189  THR A N   1 
ATOM   5468  C CA  . THR C  1 188 ? 25.789  21.028  -22.663 1.00 45.57  ? 189  THR A CA  1 
ATOM   5469  C C   . THR C  1 188 ? 25.673  19.690  -23.411 1.00 44.00  ? 189  THR A C   1 
ATOM   5470  O O   . THR C  1 188 ? 25.001  19.586  -24.444 1.00 41.49  ? 189  THR A O   1 
ATOM   5471  C CB  . THR C  1 188 ? 27.192  21.682  -22.899 1.00 54.53  ? 189  THR A CB  1 
ATOM   5472  O OG1 . THR C  1 188 ? 27.345  22.837  -22.060 1.00 51.71  ? 189  THR A OG1 1 
ATOM   5473  C CG2 . THR C  1 188 ? 27.410  22.054  -24.373 1.00 46.14  ? 189  THR A CG2 1 
ATOM   5474  N N   . GLU C  1 189 ? 26.319  18.662  -22.859 1.00 49.38  ? 190  GLU A N   1 
ATOM   5475  C CA  . GLU C  1 189 ? 26.253  17.310  -23.403 1.00 42.00  ? 190  GLU A CA  1 
ATOM   5476  C C   . GLU C  1 189 ? 24.815  16.767  -23.379 1.00 39.51  ? 190  GLU A C   1 
ATOM   5477  O O   . GLU C  1 189 ? 24.371  16.169  -24.366 1.00 38.59  ? 190  GLU A O   1 
ATOM   5478  C CB  . GLU C  1 189 ? 27.220  16.403  -22.618 1.00 41.22  ? 190  GLU A CB  1 
ATOM   5479  C CG  . GLU C  1 189 ? 27.261  14.908  -22.989 1.00 40.98  ? 190  GLU A CG  1 
ATOM   5480  C CD  . GLU C  1 189 ? 28.237  14.138  -22.101 1.00 47.60  ? 190  GLU A CD  1 
ATOM   5481  O OE1 . GLU C  1 189 ? 29.219  14.736  -21.612 1.00 57.87  ? 190  GLU A OE1 1 
ATOM   5482  O OE2 . GLU C  1 189 ? 28.029  12.942  -21.857 1.00 47.82  ? 190  GLU A OE2 1 
ATOM   5483  N N   . GLN C  1 190 ? 24.069  17.029  -22.302 1.00 33.96  ? 191  GLN A N   1 
ATOM   5484  C CA  . GLN C  1 190 ? 22.671  16.584  -22.213 1.00 35.64  ? 191  GLN A CA  1 
ATOM   5485  C C   . GLN C  1 190 ? 21.822  17.170  -23.364 1.00 38.63  ? 191  GLN A C   1 
ATOM   5486  O O   . GLN C  1 190 ? 20.916  16.527  -23.898 1.00 38.17  ? 191  GLN A O   1 
ATOM   5487  C CB  . GLN C  1 190 ? 22.079  16.965  -20.856 1.00 32.31  ? 191  GLN A CB  1 
ATOM   5488  C CG  . GLN C  1 190 ? 20.550  16.861  -20.732 1.00 29.67  ? 191  GLN A CG  1 
ATOM   5489  C CD  . GLN C  1 190 ? 19.988  15.455  -20.525 1.00 31.00  ? 191  GLN A CD  1 
ATOM   5490  O OE1 . GLN C  1 190 ? 20.689  14.510  -20.129 1.00 30.25  ? 191  GLN A OE1 1 
ATOM   5491  N NE2 . GLN C  1 190 ? 18.696  15.322  -20.778 1.00 30.99  ? 191  GLN A NE2 1 
ATOM   5492  N N   . THR C  1 191 ? 22.136  18.392  -23.755 1.00 36.74  ? 192  THR A N   1 
ATOM   5493  C CA  . THR C  1 191 ? 21.371  19.077  -24.784 1.00 38.88  ? 192  THR A CA  1 
ATOM   5494  C C   . THR C  1 191 ? 21.845  18.629  -26.162 1.00 38.05  ? 192  THR A C   1 
ATOM   5495  O O   . THR C  1 191 ? 21.070  18.531  -27.125 1.00 36.74  ? 192  THR A O   1 
ATOM   5496  C CB  . THR C  1 191 ? 21.520  20.619  -24.628 1.00 39.42  ? 192  THR A CB  1 
ATOM   5497  O OG1 . THR C  1 191 ? 20.275  21.171  -24.180 1.00 43.18  ? 192  THR A OG1 1 
ATOM   5498  C CG2 . THR C  1 191 ? 21.994  21.293  -25.943 1.00 35.66  ? 192  THR A CG2 1 
ATOM   5499  N N   . ARG C  1 192 ? 23.126  18.298  -26.220 1.00 37.00  ? 193  ARG A N   1 
ATOM   5500  C CA  . ARG C  1 192 ? 23.744  17.874  -27.451 1.00 35.62  ? 193  ARG A CA  1 
ATOM   5501  C C   . ARG C  1 192 ? 23.220  16.504  -27.857 1.00 37.24  ? 193  ARG A C   1 
ATOM   5502  O O   . ARG C  1 192 ? 23.093  16.209  -29.045 1.00 42.33  ? 193  ARG A O   1 
ATOM   5503  C CB  . ARG C  1 192 ? 25.257  17.828  -27.259 1.00 37.79  ? 193  ARG A CB  1 
ATOM   5504  C CG  . ARG C  1 192 ? 26.024  17.315  -28.443 1.00 37.42  ? 193  ARG A CG  1 
ATOM   5505  C CD  . ARG C  1 192 ? 27.515  17.113  -28.121 1.00 42.43  ? 193  ARG A CD  1 
ATOM   5506  N NE  . ARG C  1 192 ? 28.134  16.322  -29.188 1.00 53.92  ? 193  ARG A NE  1 
ATOM   5507  C CZ  . ARG C  1 192 ? 28.190  14.990  -29.228 1.00 50.30  ? 193  ARG A CZ  1 
ATOM   5508  N NH1 . ARG C  1 192 ? 27.694  14.260  -28.235 1.00 40.84  ? 193  ARG A NH1 1 
ATOM   5509  N NH2 . ARG C  1 192 ? 28.764  14.382  -30.267 1.00 54.92  ? 193  ARG A NH2 1 
ATOM   5510  N N   . LEU C  1 193 ? 22.881  15.685  -26.863 1.00 32.62  ? 194  LEU A N   1 
ATOM   5511  C CA  . LEU C  1 193 ? 22.467  14.310  -27.100 1.00 28.39  ? 194  LEU A CA  1 
ATOM   5512  C C   . LEU C  1 193 ? 20.939  14.138  -27.163 1.00 32.90  ? 194  LEU A C   1 
ATOM   5513  O O   . LEU C  1 193 ? 20.422  13.427  -28.040 1.00 30.08  ? 194  LEU A O   1 
ATOM   5514  C CB  . LEU C  1 193 ? 23.043  13.415  -26.005 1.00 33.00  ? 194  LEU A CB  1 
ATOM   5515  C CG  . LEU C  1 193 ? 24.556  13.171  -25.994 1.00 31.19  ? 194  LEU A CG  1 
ATOM   5516  C CD1 . LEU C  1 193 ? 24.971  12.267  -24.844 1.00 26.96  ? 194  LEU A CD1 1 
ATOM   5517  C CD2 . LEU C  1 193 ? 25.033  12.612  -27.302 1.00 37.17  ? 194  LEU A CD2 1 
ATOM   5518  N N   . TYR C  1 194 ? 20.211  14.795  -26.251 1.00 34.43  ? 195  TYR A N   1 
ATOM   5519  C CA  . TYR C  1 194 ? 18.762  14.542  -26.117 1.00 32.63  ? 195  TYR A CA  1 
ATOM   5520  C C   . TYR C  1 194 ? 17.817  15.787  -26.222 1.00 32.94  ? 195  TYR A C   1 
ATOM   5521  O O   . TYR C  1 194 ? 16.599  15.656  -26.108 1.00 27.86  ? 195  TYR A O   1 
ATOM   5522  C CB  . TYR C  1 194 ? 18.506  13.792  -24.805 1.00 30.08  ? 195  TYR A CB  1 
ATOM   5523  C CG  . TYR C  1 194 ? 19.530  12.696  -24.552 1.00 32.79  ? 195  TYR A CG  1 
ATOM   5524  C CD1 . TYR C  1 194 ? 19.569  11.548  -25.357 1.00 30.83  ? 195  TYR A CD1 1 
ATOM   5525  C CD2 . TYR C  1 194 ? 20.434  12.786  -23.484 1.00 29.28  ? 195  TYR A CD2 1 
ATOM   5526  C CE1 . TYR C  1 194 ? 20.512  10.544  -25.132 1.00 28.39  ? 195  TYR A CE1 1 
ATOM   5527  C CE2 . TYR C  1 194 ? 21.372  11.790  -23.248 1.00 25.66  ? 195  TYR A CE2 1 
ATOM   5528  C CZ  . TYR C  1 194 ? 21.406  10.670  -24.068 1.00 29.09  ? 195  TYR A CZ  1 
ATOM   5529  O OH  . TYR C  1 194 ? 22.336  9.670   -23.831 1.00 28.30  ? 195  TYR A OH  1 
ATOM   5530  N N   . GLN C  1 195 ? 18.381  16.980  -26.423 1.00 37.00  ? 196  GLN A N   1 
ATOM   5531  C CA  . GLN C  1 195 ? 17.600  18.210  -26.664 1.00 38.29  ? 196  GLN A CA  1 
ATOM   5532  C C   . GLN C  1 195 ? 16.827  18.720  -25.441 1.00 34.75  ? 196  GLN A C   1 
ATOM   5533  O O   . GLN C  1 195 ? 16.999  19.863  -25.034 1.00 36.06  ? 196  GLN A O   1 
ATOM   5534  C CB  . GLN C  1 195 ? 16.637  17.996  -27.838 1.00 41.74  ? 196  GLN A CB  1 
ATOM   5535  C CG  . GLN C  1 195 ? 15.927  19.231  -28.297 1.00 39.69  ? 196  GLN A CG  1 
ATOM   5536  C CD  . GLN C  1 195 ? 16.888  20.236  -28.872 1.00 44.40  ? 196  GLN A CD  1 
ATOM   5537  O OE1 . GLN C  1 195 ? 17.854  19.877  -29.552 1.00 50.60  ? 196  GLN A OE1 1 
ATOM   5538  N NE2 . GLN C  1 195 ? 16.626  21.507  -28.617 1.00 44.99  ? 196  GLN A NE2 1 
ATOM   5539  N N   . ASN C  1 196 ? 15.980  17.878  -24.864 1.00 33.41  ? 197  ASN A N   1 
ATOM   5540  C CA  . ASN C  1 196 ? 15.269  18.234  -23.634 1.00 34.57  ? 197  ASN A CA  1 
ATOM   5541  C C   . ASN C  1 196 ? 16.205  18.216  -22.423 1.00 34.77  ? 197  ASN A C   1 
ATOM   5542  O O   . ASN C  1 196 ? 16.894  17.222  -22.182 1.00 34.90  ? 197  ASN A O   1 
ATOM   5543  C CB  . ASN C  1 196 ? 14.102  17.262  -23.397 1.00 28.06  ? 197  ASN A CB  1 
ATOM   5544  C CG  . ASN C  1 196 ? 13.300  17.008  -24.652 1.00 36.15  ? 197  ASN A CG  1 
ATOM   5545  O OD1 . ASN C  1 196 ? 13.167  17.903  -25.496 1.00 43.56  ? 197  ASN A OD1 1 
ATOM   5546  N ND2 . ASN C  1 196 ? 12.833  15.766  -24.835 1.00 31.49  ? 197  ASN A ND2 1 
ATOM   5547  N N   . PRO C  1 197 ? 16.185  19.294  -21.618 1.00 42.30  ? 198  PRO A N   1 
ATOM   5548  C CA  . PRO C  1 197 ? 17.049  19.448  -20.427 1.00 38.21  ? 198  PRO A CA  1 
ATOM   5549  C C   . PRO C  1 197 ? 16.572  18.654  -19.208 1.00 34.74  ? 198  PRO A C   1 
ATOM   5550  O O   . PRO C  1 197 ? 17.406  18.220  -18.418 1.00 38.73  ? 198  PRO A O   1 
ATOM   5551  C CB  . PRO C  1 197 ? 16.983  20.950  -20.142 1.00 39.00  ? 198  PRO A CB  1 
ATOM   5552  C CG  . PRO C  1 197 ? 15.635  21.352  -20.654 1.00 44.45  ? 198  PRO A CG  1 
ATOM   5553  C CD  . PRO C  1 197 ? 15.367  20.497  -21.867 1.00 35.26  ? 198  PRO A CD  1 
ATOM   5554  N N   . THR C  1 198 ? 15.263  18.412  -19.107 1.00 32.95  ? 199  THR A N   1 
ATOM   5555  C CA  . THR C  1 198 ? 14.673  17.776  -17.940 1.00 32.94  ? 199  THR A CA  1 
ATOM   5556  C C   . THR C  1 198 ? 13.973  16.478  -18.322 1.00 28.56  ? 199  THR A C   1 
ATOM   5557  O O   . THR C  1 198 ? 12.855  16.525  -18.818 1.00 36.02  ? 199  THR A O   1 
ATOM   5558  C CB  . THR C  1 198 ? 13.605  18.708  -17.304 1.00 38.07  ? 199  THR A CB  1 
ATOM   5559  O OG1 . THR C  1 198 ? 14.117  20.041  -17.128 1.00 40.56  ? 199  THR A OG1 1 
ATOM   5560  C CG2 . THR C  1 198 ? 13.089  18.124  -16.006 1.00 30.94  ? 199  THR A CG2 1 
ATOM   5561  N N   . THR C  1 199 ? 14.567  15.319  -18.045 1.00 28.97  ? 200  THR A N   1 
ATOM   5562  C CA  . THR C  1 199 ? 14.063  14.073  -18.646 1.00 27.92  ? 200  THR A CA  1 
ATOM   5563  C C   . THR C  1 199 ? 13.767  12.928  -17.654 1.00 32.36  ? 200  THR A C   1 
ATOM   5564  O O   . THR C  1 199 ? 14.202  12.986  -16.499 1.00 33.05  ? 200  THR A O   1 
ATOM   5565  C CB  . THR C  1 199 ? 15.076  13.570  -19.661 1.00 28.32  ? 200  THR A CB  1 
ATOM   5566  O OG1 . THR C  1 199 ? 16.300  13.308  -18.975 1.00 26.04  ? 200  THR A OG1 1 
ATOM   5567  C CG2 . THR C  1 199 ? 15.312  14.626  -20.773 1.00 28.11  ? 200  THR A CG2 1 
ATOM   5568  N N   . TYR C  1 200 ? 13.111  11.856  -18.123 1.00 31.63  ? 201  TYR A N   1 
ATOM   5569  C CA  . TYR C  1 200 ? 12.697  10.730  -17.264 1.00 28.41  ? 201  TYR A CA  1 
ATOM   5570  C C   . TYR C  1 200 ? 12.513  9.379   -17.997 1.00 31.05  ? 201  TYR A C   1 
ATOM   5571  O O   . TYR C  1 200 ? 12.367  9.329   -19.209 1.00 27.89  ? 201  TYR A O   1 
ATOM   5572  C CB  . TYR C  1 200 ? 11.378  11.073  -16.553 1.00 29.54  ? 201  TYR A CB  1 
ATOM   5573  C CG  . TYR C  1 200 ? 10.180  11.096  -17.483 1.00 29.85  ? 201  TYR A CG  1 
ATOM   5574  C CD1 . TYR C  1 200 ? 9.869   12.241  -18.210 1.00 34.89  ? 201  TYR A CD1 1 
ATOM   5575  C CD2 . TYR C  1 200 ? 9.364   9.970   -17.648 1.00 34.73  ? 201  TYR A CD2 1 
ATOM   5576  C CE1 . TYR C  1 200 ? 8.781   12.275  -19.101 1.00 35.36  ? 201  TYR A CE1 1 
ATOM   5577  C CE2 . TYR C  1 200 ? 8.270   9.992   -18.525 1.00 35.13  ? 201  TYR A CE2 1 
ATOM   5578  C CZ  . TYR C  1 200 ? 7.993   11.152  -19.245 1.00 36.45  ? 201  TYR A CZ  1 
ATOM   5579  O OH  . TYR C  1 200 ? 6.924   11.203  -20.095 1.00 40.52  ? 201  TYR A OH  1 
ATOM   5580  N N   . ILE C  1 201 ? 12.496  8.280   -17.244 1.00 30.30  ? 202  ILE A N   1 
ATOM   5581  C CA  . ILE C  1 201 ? 12.112  6.990   -17.806 1.00 30.96  ? 202  ILE A CA  1 
ATOM   5582  C C   . ILE C  1 201 ? 11.116  6.313   -16.867 1.00 31.74  ? 202  ILE A C   1 
ATOM   5583  O O   . ILE C  1 201 ? 11.410  6.119   -15.704 1.00 34.94  ? 202  ILE A O   1 
ATOM   5584  C CB  . ILE C  1 201 ? 13.344  6.079   -18.034 1.00 32.76  ? 202  ILE A CB  1 
ATOM   5585  C CG1 . ILE C  1 201 ? 14.339  6.750   -18.985 1.00 26.10  ? 202  ILE A CG1 1 
ATOM   5586  C CG2 . ILE C  1 201 ? 12.958  4.711   -18.556 1.00 22.42  ? 202  ILE A CG2 1 
ATOM   5587  C CD1 . ILE C  1 201 ? 15.661  5.948   -19.135 1.00 25.86  ? 202  ILE A CD1 1 
ATOM   5588  N N   . SER C  1 202 ? 9.948   5.931   -17.385 1.00 36.39  ? 203  SER A N   1 
ATOM   5589  C CA  . SER C  1 202 ? 8.923   5.241   -16.601 1.00 31.57  ? 203  SER A CA  1 
ATOM   5590  C C   . SER C  1 202 ? 8.864   3.808   -17.073 1.00 34.92  ? 203  SER A C   1 
ATOM   5591  O O   . SER C  1 202 ? 8.778   3.582   -18.278 1.00 32.85  ? 203  SER A O   1 
ATOM   5592  C CB  . SER C  1 202 ? 7.541   5.866   -16.827 1.00 29.38  ? 203  SER A CB  1 
ATOM   5593  O OG  . SER C  1 202 ? 7.369   7.080   -16.140 1.00 39.68  ? 203  SER A OG  1 
ATOM   5594  N N   . VAL C  1 203 ? 8.844   2.836   -16.163 1.00 34.16  ? 204  VAL A N   1 
ATOM   5595  C CA  . VAL C  1 203 ? 8.678   1.448   -16.596 1.00 34.36  ? 204  VAL A CA  1 
ATOM   5596  C C   . VAL C  1 203 ? 7.622   0.784   -15.706 1.00 35.38  ? 204  VAL A C   1 
ATOM   5597  O O   . VAL C  1 203 ? 7.743   0.762   -14.484 1.00 35.20  ? 204  VAL A O   1 
ATOM   5598  C CB  . VAL C  1 203 ? 10.038  0.646   -16.565 1.00 36.56  ? 204  VAL A CB  1 
ATOM   5599  C CG1 . VAL C  1 203 ? 9.879   -0.774  -17.152 1.00 32.74  ? 204  VAL A CG1 1 
ATOM   5600  C CG2 . VAL C  1 203 ? 11.142  1.384   -17.327 1.00 34.08  ? 204  VAL A CG2 1 
ATOM   5601  N N   . GLY C  1 204 ? 6.604   0.207   -16.333 1.00 36.47  ? 205  GLY A N   1 
ATOM   5602  C CA  . GLY C  1 204 ? 5.509   -0.377  -15.599 1.00 30.15  ? 205  GLY A CA  1 
ATOM   5603  C C   . GLY C  1 204 ? 5.180   -1.773  -16.059 1.00 35.16  ? 205  GLY A C   1 
ATOM   5604  O O   . GLY C  1 204 ? 5.288   -2.108  -17.237 1.00 35.92  ? 205  GLY A O   1 
ATOM   5605  N N   . THR C  1 205 ? 4.738   -2.579  -15.106 1.00 34.67  ? 206  THR A N   1 
ATOM   5606  C CA  . THR C  1 205 ? 4.473   -3.997  -15.310 1.00 40.66  ? 206  THR A CA  1 
ATOM   5607  C C   . THR C  1 205 ? 3.272   -4.282  -14.372 1.00 44.87  ? 206  THR A C   1 
ATOM   5608  O O   . THR C  1 205 ? 2.711   -3.316  -13.827 1.00 43.09  ? 206  THR A O   1 
ATOM   5609  C CB  . THR C  1 205 ? 5.791   -4.814  -15.060 1.00 40.25  ? 206  THR A CB  1 
ATOM   5610  O OG1 . THR C  1 205 ? 6.243   -5.361  -16.311 1.00 38.40  ? 206  THR A OG1 1 
ATOM   5611  C CG2 . THR C  1 205 ? 5.681   -5.921  -14.002 1.00 33.25  ? 206  THR A CG2 1 
ATOM   5612  N N   . SER C  1 206 ? 2.760   -5.507  -14.249 1.00 43.41  ? 207  SER A N   1 
ATOM   5613  C CA  . SER C  1 206 ? 1.740   -5.701  -13.199 1.00 43.47  ? 207  SER A CA  1 
ATOM   5614  C C   . SER C  1 206 ? 2.325   -5.507  -11.768 1.00 48.71  ? 207  SER A C   1 
ATOM   5615  O O   . SER C  1 206 ? 1.599   -5.092  -10.841 1.00 45.46  ? 207  SER A O   1 
ATOM   5616  C CB  . SER C  1 206 ? 1.099   -7.082  -13.283 1.00 37.85  ? 207  SER A CB  1 
ATOM   5617  O OG  . SER C  1 206 ? 2.050   -8.084  -12.983 1.00 39.69  ? 207  SER A OG  1 
ATOM   5618  N N   . THR C  1 207 ? 3.636   -5.752  -11.610 1.00 44.09  ? 208  THR A N   1 
ATOM   5619  C CA  . THR C  1 207 ? 4.300   -5.651  -10.301 1.00 38.14  ? 208  THR A CA  1 
ATOM   5620  C C   . THR C  1 207 ? 5.413   -4.602  -10.218 1.00 39.32  ? 208  THR A C   1 
ATOM   5621  O O   . THR C  1 207 ? 5.845   -4.277  -9.124  1.00 45.66  ? 208  THR A O   1 
ATOM   5622  C CB  . THR C  1 207 ? 4.938   -6.997  -9.856  1.00 39.69  ? 208  THR A CB  1 
ATOM   5623  O OG1 . THR C  1 207 ? 6.097   -7.298  -10.653 1.00 37.74  ? 208  THR A OG1 1 
ATOM   5624  C CG2 . THR C  1 207 ? 3.915   -8.137  -9.887  1.00 37.28  ? 208  THR A CG2 1 
ATOM   5625  N N   . LEU C  1 208 ? 5.916   -4.112  -11.347 1.00 39.06  ? 209  LEU A N   1 
ATOM   5626  C CA  . LEU C  1 208 ? 6.996   -3.117  -11.344 1.00 32.34  ? 209  LEU A CA  1 
ATOM   5627  C C   . LEU C  1 208 ? 6.462   -1.688  -11.596 1.00 33.24  ? 209  LEU A C   1 
ATOM   5628  O O   . LEU C  1 208 ? 5.710   -1.491  -12.530 1.00 37.97  ? 209  LEU A O   1 
ATOM   5629  C CB  . LEU C  1 208 ? 8.032   -3.507  -12.405 1.00 35.68  ? 209  LEU A CB  1 
ATOM   5630  C CG  . LEU C  1 208 ? 9.189   -2.556  -12.739 1.00 38.32  ? 209  LEU A CG  1 
ATOM   5631  C CD1 . LEU C  1 208 ? 10.195  -2.471  -11.623 1.00 34.99  ? 209  LEU A CD1 1 
ATOM   5632  C CD2 . LEU C  1 208 ? 9.877   -2.901  -14.075 1.00 32.73  ? 209  LEU A CD2 1 
ATOM   5633  N N   . ASN C  1 209 ? 6.882   -0.685  -10.824 1.00 33.72  ? 210  ASN A N   1 
ATOM   5634  C CA  . ASN C  1 209 ? 6.432   0.711   -11.032 1.00 31.52  ? 210  ASN A CA  1 
ATOM   5635  C C   . ASN C  1 209 ? 7.595   1.696   -10.862 1.00 35.85  ? 210  ASN A C   1 
ATOM   5636  O O   . ASN C  1 209 ? 7.694   2.398   -9.836  1.00 35.02  ? 210  ASN A O   1 
ATOM   5637  C CB  . ASN C  1 209 ? 5.282   1.069   -10.050 1.00 31.70  ? 210  ASN A CB  1 
ATOM   5638  C CG  . ASN C  1 209 ? 4.717   2.492   -10.256 1.00 36.00  ? 210  ASN A CG  1 
ATOM   5639  O OD1 . ASN C  1 209 ? 4.910   3.098   -11.298 1.00 41.37  ? 210  ASN A OD1 1 
ATOM   5640  N ND2 . ASN C  1 209 ? 4.040   3.022   -9.248  1.00 32.10  ? 210  ASN A ND2 1 
ATOM   5641  N N   . GLN C  1 210 ? 8.413   1.831   -11.911 1.00 31.77  ? 211  GLN A N   1 
ATOM   5642  C CA  . GLN C  1 210 ? 9.705   2.517   -11.799 1.00 29.57  ? 211  GLN A CA  1 
ATOM   5643  C C   . GLN C  1 210 ? 9.800   3.888   -12.477 1.00 31.94  ? 211  GLN A C   1 
ATOM   5644  O O   . GLN C  1 210 ? 9.193   4.133   -13.508 1.00 36.30  ? 211  GLN A O   1 
ATOM   5645  C CB  . GLN C  1 210 ? 10.768  1.594   -12.358 1.00 27.50  ? 211  GLN A CB  1 
ATOM   5646  C CG  . GLN C  1 210 ? 12.171  2.158   -12.582 1.00 28.72  ? 211  GLN A CG  1 
ATOM   5647  C CD  . GLN C  1 210 ? 13.057  1.076   -13.204 1.00 32.61  ? 211  GLN A CD  1 
ATOM   5648  O OE1 . GLN C  1 210 ? 13.509  1.188   -14.340 1.00 27.12  ? 211  GLN A OE1 1 
ATOM   5649  N NE2 . GLN C  1 210 ? 13.197  -0.032  -12.492 1.00 33.70  ? 211  GLN A NE2 1 
ATOM   5650  N N   . LYS C  1 211 ? 10.573  4.781   -11.876 1.00 34.68  ? 212  LYS A N   1 
ATOM   5651  C CA  . LYS C  1 211 ? 10.848  6.087   -12.453 1.00 32.67  ? 212  LYS A CA  1 
ATOM   5652  C C   . LYS C  1 211 ? 12.318  6.517   -12.242 1.00 34.33  ? 212  LYS A C   1 
ATOM   5653  O O   . LYS C  1 211 ? 12.780  6.661   -11.088 1.00 33.62  ? 212  LYS A O   1 
ATOM   5654  C CB  . LYS C  1 211 ? 9.906   7.124   -11.849 1.00 34.76  ? 212  LYS A CB  1 
ATOM   5655  C CG  . LYS C  1 211 ? 10.126  8.527   -12.390 1.00 38.05  ? 212  LYS A CG  1 
ATOM   5656  C CD  . LYS C  1 211 ? 8.799   9.221   -12.604 1.00 41.34  ? 212  LYS A CD  1 
ATOM   5657  C CE  . LYS C  1 211 ? 8.986   10.597  -13.221 1.00 46.86  ? 212  LYS A CE  1 
ATOM   5658  N NZ  . LYS C  1 211 ? 7.672   11.308  -13.396 1.00 51.58  ? 212  LYS A NZ  1 
ATOM   5659  N N   . LEU C  1 212 ? 13.035  6.709   -13.359 1.00 33.44  ? 213  LEU A N   1 
ATOM   5660  C CA  . LEU C  1 212 ? 14.453  7.123   -13.382 1.00 28.52  ? 213  LEU A CA  1 
ATOM   5661  C C   . LEU C  1 212 ? 14.652  8.517   -13.934 1.00 23.17  ? 213  LEU A C   1 
ATOM   5662  O O   . LEU C  1 212 ? 14.034  8.896   -14.915 1.00 30.68  ? 213  LEU A O   1 
ATOM   5663  C CB  . LEU C  1 212 ? 15.336  6.158   -14.214 1.00 26.84  ? 213  LEU A CB  1 
ATOM   5664  C CG  . LEU C  1 212 ? 15.550  4.654   -14.000 1.00 25.47  ? 213  LEU A CG  1 
ATOM   5665  C CD1 . LEU C  1 212 ? 15.195  4.218   -12.585 1.00 23.95  ? 213  LEU A CD1 1 
ATOM   5666  C CD2 . LEU C  1 212 ? 14.947  3.754   -15.040 1.00 20.36  ? 213  LEU A CD2 1 
ATOM   5667  N N   . VAL C  1 213 ? 15.593  9.246   -13.356 1.00 27.64  ? 214  VAL A N   1 
ATOM   5668  C CA  . VAL C  1 213 ? 15.921  10.618  -13.773 1.00 26.93  ? 214  VAL A CA  1 
ATOM   5669  C C   . VAL C  1 213 ? 17.442  10.691  -13.803 1.00 28.17  ? 214  VAL A C   1 
ATOM   5670  O O   . VAL C  1 213 ? 18.095  10.227  -12.867 1.00 26.80  ? 214  VAL A O   1 
ATOM   5671  C CB  . VAL C  1 213 ? 15.306  11.698  -12.787 1.00 21.06  ? 214  VAL A CB  1 
ATOM   5672  C CG1 . VAL C  1 213 ? 15.678  13.096  -13.175 1.00 19.27  ? 214  VAL A CG1 1 
ATOM   5673  C CG2 . VAL C  1 213 ? 13.793  11.585  -12.733 1.00 21.54  ? 214  VAL A CG2 1 
ATOM   5674  N N   . PRO C  1 214 ? 18.020  11.259  -14.884 1.00 33.81  ? 215  PRO A N   1 
ATOM   5675  C CA  . PRO C  1 214 ? 19.492  11.287  -15.025 1.00 30.32  ? 215  PRO A CA  1 
ATOM   5676  C C   . PRO C  1 214 ? 20.159  12.118  -13.929 1.00 28.45  ? 215  PRO A C   1 
ATOM   5677  O O   . PRO C  1 214 ? 19.541  13.053  -13.425 1.00 28.97  ? 215  PRO A O   1 
ATOM   5678  C CB  . PRO C  1 214 ? 19.717  11.947  -16.393 1.00 22.53  ? 215  PRO A CB  1 
ATOM   5679  C CG  . PRO C  1 214 ? 18.421  11.862  -17.091 1.00 27.36  ? 215  PRO A CG  1 
ATOM   5680  C CD  . PRO C  1 214 ? 17.343  11.890  -16.031 1.00 25.80  ? 215  PRO A CD  1 
ATOM   5681  N N   . LYS C  1 215 ? 21.391  11.762  -13.567 1.00 33.66  ? 216  LYS A N   1 
ATOM   5682  C CA  . LYS C  1 215 ? 22.201  12.511  -12.613 1.00 26.66  ? 216  LYS A CA  1 
ATOM   5683  C C   . LYS C  1 215 ? 23.371  13.171  -13.285 1.00 32.46  ? 216  LYS A C   1 
ATOM   5684  O O   . LYS C  1 215 ? 24.409  12.521  -13.412 1.00 37.81  ? 216  LYS A O   1 
ATOM   5685  C CB  . LYS C  1 215 ? 22.754  11.598  -11.537 1.00 23.75  ? 216  LYS A CB  1 
ATOM   5686  C CG  . LYS C  1 215 ? 21.758  11.020  -10.582 1.00 27.60  ? 216  LYS A CG  1 
ATOM   5687  C CD  . LYS C  1 215 ? 22.503  10.269  -9.485  1.00 26.05  ? 216  LYS A CD  1 
ATOM   5688  C CE  . LYS C  1 215 ? 21.694  9.112   -8.991  1.00 26.76  ? 216  LYS A CE  1 
ATOM   5689  N NZ  . LYS C  1 215 ? 22.611  8.028   -8.524  1.00 38.20  ? 216  LYS A NZ  1 
ATOM   5690  N N   . ILE C  1 216 ? 23.247  14.461  -13.612 1.00 33.18  ? 217  ILE A N   1 
ATOM   5691  C CA  . ILE C  1 216 ? 24.253  15.205  -14.401 1.00 34.08  ? 217  ILE A CA  1 
ATOM   5692  C C   . ILE C  1 216 ? 25.272  15.951  -13.531 1.00 38.48  ? 217  ILE A C   1 
ATOM   5693  O O   . ILE C  1 216 ? 24.925  16.926  -12.860 1.00 43.74  ? 217  ILE A O   1 
ATOM   5694  C CB  . ILE C  1 216 ? 23.543  16.209  -15.356 1.00 31.07  ? 217  ILE A CB  1 
ATOM   5695  C CG1 . ILE C  1 216 ? 22.571  15.445  -16.266 1.00 33.74  ? 217  ILE A CG1 1 
ATOM   5696  C CG2 . ILE C  1 216 ? 24.552  16.985  -16.190 1.00 38.95  ? 217  ILE A CG2 1 
ATOM   5697  C CD1 . ILE C  1 216 ? 21.713  16.310  -17.191 1.00 36.28  ? 217  ILE A CD1 1 
ATOM   5698  N N   . ALA C  1 217 ? 26.540  15.538  -13.608 1.00 41.81  ? 218  ALA A N   1 
ATOM   5699  C CA  . ALA C  1 217 ? 27.573  15.974  -12.653 1.00 38.27  ? 218  ALA A CA  1 
ATOM   5700  C C   . ALA C  1 217 ? 29.021  15.666  -13.101 1.00 44.37  ? 218  ALA A C   1 
ATOM   5701  O O   . ALA C  1 217 ? 29.245  15.029  -14.136 1.00 47.88  ? 218  ALA A O   1 
ATOM   5702  C CB  . ALA C  1 217 ? 27.301  15.325  -11.312 1.00 36.04  ? 218  ALA A CB  1 
ATOM   5703  N N   . THR C  1 218 ? 30.003  16.059  -12.293 1.00 39.51  ? 219  THR A N   1 
ATOM   5704  C CA  . THR C  1 218 ? 31.417  15.979  -12.686 1.00 36.89  ? 219  THR A CA  1 
ATOM   5705  C C   . THR C  1 218 ? 32.120  14.794  -12.052 1.00 37.68  ? 219  THR A C   1 
ATOM   5706  O O   . THR C  1 218 ? 32.027  14.636  -10.843 1.00 47.32  ? 219  THR A O   1 
ATOM   5707  C CB  . THR C  1 218 ? 32.155  17.276  -12.294 1.00 43.94  ? 219  THR A CB  1 
ATOM   5708  O OG1 . THR C  1 218 ? 31.593  18.383  -13.016 1.00 51.89  ? 219  THR A OG1 1 
ATOM   5709  C CG2 . THR C  1 218 ? 33.650  17.188  -12.585 1.00 38.33  ? 219  THR A CG2 1 
ATOM   5710  N N   . ARG C  1 219 ? 32.767  13.934  -12.858 1.00 38.47  ? 220  ARG A N   1 
ATOM   5711  C CA  . ARG C  1 219 ? 33.444  12.717  -12.359 1.00 38.02  ? 220  ARG A CA  1 
ATOM   5712  C C   . ARG C  1 219 ? 34.818  12.449  -12.955 1.00 39.07  ? 220  ARG A C   1 
ATOM   5713  O O   . ARG C  1 219 ? 35.138  12.949  -14.028 1.00 38.25  ? 220  ARG A O   1 
ATOM   5714  C CB  . ARG C  1 219 ? 32.609  11.463  -12.634 1.00 39.76  ? 220  ARG A CB  1 
ATOM   5715  C CG  . ARG C  1 219 ? 31.168  11.645  -12.413 1.00 37.33  ? 220  ARG A CG  1 
ATOM   5716  C CD  . ARG C  1 219 ? 30.340  10.575  -13.022 1.00 32.02  ? 220  ARG A CD  1 
ATOM   5717  N NE  . ARG C  1 219 ? 28.980  11.073  -12.980 1.00 38.85  ? 220  ARG A NE  1 
ATOM   5718  C CZ  . ARG C  1 219 ? 28.258  11.411  -14.041 1.00 37.26  ? 220  ARG A CZ  1 
ATOM   5719  N NH1 . ARG C  1 219 ? 28.721  11.184  -15.265 1.00 32.87  ? 220  ARG A NH1 1 
ATOM   5720  N NH2 . ARG C  1 219 ? 27.032  11.889  -13.860 1.00 32.64  ? 220  ARG A NH2 1 
ATOM   5721  N N   . SER C  1 220 ? 35.594  11.594  -12.289 1.00 35.54  ? 221  SER A N   1 
ATOM   5722  C CA  . SER C  1 220 ? 36.901  11.194  -12.803 1.00 37.13  ? 221  SER A CA  1 
ATOM   5723  C C   . SER C  1 220 ? 36.817  10.517  -14.152 1.00 35.00  ? 221  SER A C   1 
ATOM   5724  O O   . SER C  1 220 ? 35.791  9.956   -14.521 1.00 31.23  ? 221  SER A O   1 
ATOM   5725  C CB  . SER C  1 220 ? 37.608  10.261  -11.815 1.00 37.71  ? 221  SER A CB  1 
ATOM   5726  O OG  . SER C  1 220 ? 37.624  10.833  -10.521 1.00 46.25  ? 221  SER A OG  1 
ATOM   5727  N N   . LYS C  1 221 ? 37.912  10.539  -14.887 1.00 37.30  ? 222  LYS A N   1 
ATOM   5728  C CA  . LYS C  1 221 ? 37.870  9.884   -16.176 1.00 40.86  ? 222  LYS A CA  1 
ATOM   5729  C C   . LYS C  1 221 ? 38.247  8.441   -15.988 1.00 37.82  ? 222  LYS A C   1 
ATOM   5730  O O   . LYS C  1 221 ? 39.205  8.110   -15.286 1.00 41.03  ? 222  LYS A O   1 
ATOM   5731  C CB  . LYS C  1 221 ? 38.748  10.591  -17.213 1.00 39.64  ? 222  LYS A CB  1 
ATOM   5732  C CG  . LYS C  1 221 ? 38.289  12.034  -17.364 1.00 38.82  ? 222  LYS A CG  1 
ATOM   5733  C CD  . LYS C  1 221 ? 38.908  12.754  -18.547 1.00 50.33  ? 222  LYS A CD  1 
ATOM   5734  C CE  . LYS C  1 221 ? 38.694  14.252  -18.367 1.00 57.29  ? 222  LYS A CE  1 
ATOM   5735  N NZ  . LYS C  1 221 ? 37.900  14.837  -19.476 1.00 69.30  ? 222  LYS A NZ  1 
ATOM   5736  N N   . VAL C  1 222 ? 37.443  7.581   -16.590 1.00 35.90  ? 223  VAL A N   1 
ATOM   5737  C CA  . VAL C  1 222 ? 37.716  6.164   -16.597 1.00 37.06  ? 223  VAL A CA  1 
ATOM   5738  C C   . VAL C  1 222 ? 37.827  5.768   -18.056 1.00 37.66  ? 223  VAL A C   1 
ATOM   5739  O O   . VAL C  1 222 ? 36.892  6.016   -18.815 1.00 39.21  ? 223  VAL A O   1 
ATOM   5740  C CB  . VAL C  1 222 ? 36.609  5.355   -15.900 1.00 31.20  ? 223  VAL A CB  1 
ATOM   5741  C CG1 . VAL C  1 222 ? 36.899  3.881   -15.987 1.00 26.29  ? 223  VAL A CG1 1 
ATOM   5742  C CG2 . VAL C  1 222 ? 36.407  5.824   -14.458 1.00 29.22  ? 223  VAL A CG2 1 
ATOM   5743  N N   . LYS C  1 223 ? 38.978  5.230   -18.465 1.00 32.08  ? 224  LYS A N   1 
ATOM   5744  C CA  . LYS C  1 223 ? 39.201  4.929   -19.871 1.00 36.40  ? 224  LYS A CA  1 
ATOM   5745  C C   . LYS C  1 223 ? 38.918  6.151   -20.755 1.00 39.67  ? 224  LYS A C   1 
ATOM   5746  O O   . LYS C  1 223 ? 38.345  6.036   -21.819 1.00 42.93  ? 224  LYS A O   1 
ATOM   5747  C CB  . LYS C  1 223 ? 38.323  3.745   -20.276 1.00 35.31  ? 224  LYS A CB  1 
ATOM   5748  C CG  . LYS C  1 223 ? 38.715  2.438   -19.583 1.00 37.51  ? 224  LYS A CG  1 
ATOM   5749  C CD  . LYS C  1 223 ? 37.644  1.353   -19.780 1.00 34.57  ? 224  LYS A CD  1 
ATOM   5750  C CE  . LYS C  1 223 ? 37.299  1.149   -21.233 1.00 37.76  ? 224  LYS A CE  1 
ATOM   5751  N NZ  . LYS C  1 223 ? 36.339  0.008   -21.443 1.00 46.12  ? 224  LYS A NZ  1 
ATOM   5752  N N   . GLY C  1 224 ? 39.293  7.321   -20.256 1.00 42.39  ? 225  GLY A N   1 
ATOM   5753  C CA  . GLY C  1 224 ? 39.178  8.582   -20.959 1.00 37.37  ? 225  GLY A CA  1 
ATOM   5754  C C   . GLY C  1 224 ? 37.814  9.229   -20.864 1.00 41.55  ? 225  GLY A C   1 
ATOM   5755  O O   . GLY C  1 224 ? 37.644  10.386  -21.267 1.00 46.15  ? 225  GLY A O   1 
ATOM   5756  N N   . LEU C  1 225 ? 36.868  8.540   -20.234 1.00 39.86  ? 226  LEU A N   1 
ATOM   5757  C CA  . LEU C  1 225 ? 35.485  9.028   -20.204 1.00 37.89  ? 226  LEU A CA  1 
ATOM   5758  C C   . LEU C  1 225 ? 35.034  9.414   -18.795 1.00 38.41  ? 226  LEU A C   1 
ATOM   5759  O O   . LEU C  1 225 ? 35.525  8.875   -17.798 1.00 36.49  ? 226  LEU A O   1 
ATOM   5760  C CB  . LEU C  1 225 ? 34.524  7.958   -20.766 1.00 32.74  ? 226  LEU A CB  1 
ATOM   5761  C CG  . LEU C  1 225 ? 34.772  7.449   -22.195 1.00 38.98  ? 226  LEU A CG  1 
ATOM   5762  C CD1 . LEU C  1 225 ? 33.614  6.577   -22.712 1.00 35.54  ? 226  LEU A CD1 1 
ATOM   5763  C CD2 . LEU C  1 225 ? 35.052  8.586   -23.139 1.00 36.04  ? 226  LEU A CD2 1 
ATOM   5764  N N   . SER C  1 226 ? 34.104  10.365  -18.738 1.00 37.50  ? 227  SER A N   1 
ATOM   5765  C CA  . SER C  1 226 ? 33.480  10.789  -17.498 1.00 33.12  ? 227  SER A CA  1 
ATOM   5766  C C   . SER C  1 226 ? 31.984  10.512  -17.454 1.00 35.86  ? 227  SER A C   1 
ATOM   5767  O O   . SER C  1 226 ? 31.330  10.855  -16.476 1.00 41.28  ? 227  SER A O   1 
ATOM   5768  C CB  . SER C  1 226 ? 33.713  12.275  -17.277 1.00 37.09  ? 227  SER A CB  1 
ATOM   5769  O OG  . SER C  1 226 ? 35.076  12.510  -16.997 1.00 38.48  ? 227  SER A OG  1 
ATOM   5770  N N   . GLY C  1 227 ? 31.427  9.946   -18.523 1.00 34.64  ? 228  GLY A N   1 
ATOM   5771  C CA  . GLY C  1 227 ? 30.011  9.604   -18.537 1.00 30.32  ? 228  GLY A CA  1 
ATOM   5772  C C   . GLY C  1 227 ? 29.794  8.253   -17.899 1.00 28.82  ? 228  GLY A C   1 
ATOM   5773  O O   . GLY C  1 227 ? 30.746  7.496   -17.776 1.00 31.11  ? 228  GLY A O   1 
ATOM   5774  N N   . ARG C  1 228 ? 28.562  7.932   -17.513 1.00 27.29  ? 229  ARG A N   1 
ATOM   5775  C CA  . ARG C  1 228 ? 28.287  6.627   -16.905 1.00 29.06  ? 229  ARG A CA  1 
ATOM   5776  C C   . ARG C  1 228 ? 27.004  6.038   -17.478 1.00 29.11  ? 229  ARG A C   1 
ATOM   5777  O O   . ARG C  1 228 ? 26.109  6.781   -17.909 1.00 25.13  ? 229  ARG A O   1 
ATOM   5778  C CB  . ARG C  1 228 ? 28.176  6.736   -15.388 1.00 28.56  ? 229  ARG A CB  1 
ATOM   5779  C CG  . ARG C  1 228 ? 29.426  7.257   -14.704 1.00 27.63  ? 229  ARG A CG  1 
ATOM   5780  C CD  . ARG C  1 228 ? 30.612  6.318   -14.828 1.00 26.37  ? 229  ARG A CD  1 
ATOM   5781  N NE  . ARG C  1 228 ? 31.692  6.754   -13.954 1.00 33.13  ? 229  ARG A NE  1 
ATOM   5782  C CZ  . ARG C  1 228 ? 32.737  7.480   -14.344 1.00 37.49  ? 229  ARG A CZ  1 
ATOM   5783  N NH1 . ARG C  1 228 ? 32.859  7.812   -15.636 1.00 34.67  ? 229  ARG A NH1 1 
ATOM   5784  N NH2 . ARG C  1 228 ? 33.664  7.859   -13.446 1.00 30.23  ? 229  ARG A NH2 1 
ATOM   5785  N N   . MET C  1 229 ? 26.929  4.705   -17.500 1.00 26.26  ? 230  MET A N   1 
ATOM   5786  C CA  . MET C  1 229 ? 25.701  4.018   -17.899 1.00 24.02  ? 230  MET A CA  1 
ATOM   5787  C C   . MET C  1 229 ? 25.302  3.057   -16.805 1.00 27.09  ? 230  MET A C   1 
ATOM   5788  O O   . MET C  1 229 ? 26.122  2.271   -16.335 1.00 27.89  ? 230  MET A O   1 
ATOM   5789  C CB  . MET C  1 229 ? 25.870  3.257   -19.222 1.00 23.43  ? 230  MET A CB  1 
ATOM   5790  C CG  . MET C  1 229 ? 26.165  4.186   -20.381 1.00 31.48  ? 230  MET A CG  1 
ATOM   5791  S SD  . MET C  1 229 ? 25.474  3.713   -21.964 1.00 32.29  ? 230  MET A SD  1 
ATOM   5792  C CE  . MET C  1 229 ? 25.742  5.266   -22.871 1.00 30.31  ? 230  MET A CE  1 
ATOM   5793  N N   . GLU C  1 230 ? 24.021  3.103   -16.446 1.00 25.79  ? 231  GLU A N   1 
ATOM   5794  C CA  . GLU C  1 230 ? 23.448  2.270   -15.413 1.00 27.25  ? 231  GLU A CA  1 
ATOM   5795  C C   . GLU C  1 230 ? 22.354  1.329   -15.973 1.00 25.08  ? 231  GLU A C   1 
ATOM   5796  O O   . GLU C  1 230 ? 21.364  1.788   -16.547 1.00 24.71  ? 231  GLU A O   1 
ATOM   5797  C CB  . GLU C  1 230 ? 22.883  3.165   -14.322 1.00 25.20  ? 231  GLU A CB  1 
ATOM   5798  C CG  . GLU C  1 230 ? 22.610  2.445   -13.052 1.00 28.43  ? 231  GLU A CG  1 
ATOM   5799  C CD  . GLU C  1 230 ? 22.069  3.367   -11.980 1.00 34.48  ? 231  GLU A CD  1 
ATOM   5800  O OE1 . GLU C  1 230 ? 21.908  4.579   -12.261 1.00 36.55  ? 231  GLU A OE1 1 
ATOM   5801  O OE2 . GLU C  1 230 ? 21.797  2.876   -10.862 1.00 36.48  ? 231  GLU A OE2 1 
ATOM   5802  N N   . PHE C  1 231 ? 22.519  0.018   -15.787 1.00 24.47  ? 232  PHE A N   1 
ATOM   5803  C CA  . PHE C  1 231 ? 21.594  -0.946  -16.383 1.00 23.55  ? 232  PHE A CA  1 
ATOM   5804  C C   . PHE C  1 231 ? 20.646  -1.644  -15.383 1.00 22.38  ? 232  PHE A C   1 
ATOM   5805  O O   . PHE C  1 231 ? 21.002  -1.874  -14.217 1.00 22.92  ? 232  PHE A O   1 
ATOM   5806  C CB  . PHE C  1 231 ? 22.411  -1.968  -17.174 1.00 21.07  ? 232  PHE A CB  1 
ATOM   5807  C CG  . PHE C  1 231 ? 23.044  -1.395  -18.436 1.00 23.76  ? 232  PHE A CG  1 
ATOM   5808  C CD1 . PHE C  1 231 ? 22.290  -1.230  -19.594 1.00 21.53  ? 232  PHE A CD1 1 
ATOM   5809  C CD2 . PHE C  1 231 ? 24.382  -1.020  -18.462 1.00 27.30  ? 232  PHE A CD2 1 
ATOM   5810  C CE1 . PHE C  1 231 ? 22.855  -0.723  -20.769 1.00 22.84  ? 232  PHE A CE1 1 
ATOM   5811  C CE2 . PHE C  1 231 ? 24.963  -0.480  -19.635 1.00 24.65  ? 232  PHE A CE2 1 
ATOM   5812  C CZ  . PHE C  1 231 ? 24.197  -0.334  -20.785 1.00 24.56  ? 232  PHE A CZ  1 
ATOM   5813  N N   . PHE C  1 232 ? 19.455  -2.009  -15.872 1.00 22.19  ? 233  PHE A N   1 
ATOM   5814  C CA  . PHE C  1 232 ? 18.356  -2.548  -15.055 1.00 22.63  ? 233  PHE A CA  1 
ATOM   5815  C C   . PHE C  1 232 ? 17.742  -3.790  -15.660 1.00 18.82  ? 233  PHE A C   1 
ATOM   5816  O O   . PHE C  1 232 ? 17.913  -4.025  -16.847 1.00 21.69  ? 233  PHE A O   1 
ATOM   5817  C CB  . PHE C  1 232 ? 17.257  -1.508  -14.869 1.00 19.49  ? 233  PHE A CB  1 
ATOM   5818  C CG  . PHE C  1 232 ? 17.682  -0.343  -14.071 1.00 24.89  ? 233  PHE A CG  1 
ATOM   5819  C CD1 . PHE C  1 232 ? 18.303  0.740   -14.675 1.00 26.66  ? 233  PHE A CD1 1 
ATOM   5820  C CD2 . PHE C  1 232 ? 17.509  -0.338  -12.686 1.00 28.63  ? 233  PHE A CD2 1 
ATOM   5821  C CE1 . PHE C  1 232 ? 18.712  1.841   -13.915 1.00 28.53  ? 233  PHE A CE1 1 
ATOM   5822  C CE2 . PHE C  1 232 ? 17.927  0.742   -11.915 1.00 28.59  ? 233  PHE A CE2 1 
ATOM   5823  C CZ  . PHE C  1 232 ? 18.532  1.843   -12.537 1.00 26.98  ? 233  PHE A CZ  1 
ATOM   5824  N N   . TRP C  1 233 ? 17.022  -4.574  -14.852 1.00 20.90  ? 234  TRP A N   1 
ATOM   5825  C CA  . TRP C  1 233 ? 16.378  -5.804  -15.343 1.00 27.07  ? 234  TRP A CA  1 
ATOM   5826  C C   . TRP C  1 233 ? 15.106  -6.200  -14.584 1.00 25.06  ? 234  TRP A C   1 
ATOM   5827  O O   . TRP C  1 233 ? 14.921  -5.862  -13.420 1.00 22.34  ? 234  TRP A O   1 
ATOM   5828  C CB  . TRP C  1 233 ? 17.355  -7.009  -15.313 1.00 23.34  ? 234  TRP A CB  1 
ATOM   5829  C CG  . TRP C  1 233 ? 17.825  -7.412  -13.928 1.00 24.79  ? 234  TRP A CG  1 
ATOM   5830  C CD1 . TRP C  1 233 ? 18.859  -6.868  -13.229 1.00 25.50  ? 234  TRP A CD1 1 
ATOM   5831  C CD2 . TRP C  1 233 ? 17.275  -8.445  -13.088 1.00 24.77  ? 234  TRP A CD2 1 
ATOM   5832  N NE1 . TRP C  1 233 ? 18.995  -7.496  -12.014 1.00 26.31  ? 234  TRP A NE1 1 
ATOM   5833  C CE2 . TRP C  1 233 ? 18.028  -8.461  -11.898 1.00 24.58  ? 234  TRP A CE2 1 
ATOM   5834  C CE3 . TRP C  1 233 ? 16.223  -9.362  -13.234 1.00 27.48  ? 234  TRP A CE3 1 
ATOM   5835  C CZ2 . TRP C  1 233 ? 17.756  -9.342  -10.852 1.00 22.13  ? 234  TRP A CZ2 1 
ATOM   5836  C CZ3 . TRP C  1 233 ? 15.954  -10.241 -12.197 1.00 24.65  ? 234  TRP A CZ3 1 
ATOM   5837  C CH2 . TRP C  1 233 ? 16.721  -10.222 -11.022 1.00 26.68  ? 234  TRP A CH2 1 
ATOM   5838  N N   . THR C  1 234 ? 14.267  -6.978  -15.265 1.00 29.95  ? 235  THR A N   1 
ATOM   5839  C CA  . THR C  1 234 ? 13.066  -7.571  -14.686 1.00 29.11  ? 235  THR A CA  1 
ATOM   5840  C C   . THR C  1 234 ? 12.700  -8.864  -15.421 1.00 27.81  ? 235  THR A C   1 
ATOM   5841  O O   . THR C  1 234 ? 13.062  -9.046  -16.579 1.00 25.88  ? 235  THR A O   1 
ATOM   5842  C CB  . THR C  1 234 ? 11.855  -6.616  -14.750 1.00 26.40  ? 235  THR A CB  1 
ATOM   5843  O OG1 . THR C  1 234 ? 10.913  -7.000  -13.744 1.00 28.95  ? 235  THR A OG1 1 
ATOM   5844  C CG2 . THR C  1 234 ? 11.162  -6.692  -16.107 1.00 24.98  ? 235  THR A CG2 1 
ATOM   5845  N N   . ILE C  1 235 ? 11.941  -9.726  -14.746 1.00 31.78  ? 236  ILE A N   1 
ATOM   5846  C CA  . ILE C  1 235 ? 11.372  -10.934 -15.344 1.00 30.92  ? 236  ILE A CA  1 
ATOM   5847  C C   . ILE C  1 235 ? 9.900   -10.631 -15.608 1.00 31.94  ? 236  ILE A C   1 
ATOM   5848  O O   . ILE C  1 235 ? 9.165   -10.245 -14.691 1.00 28.37  ? 236  ILE A O   1 
ATOM   5849  C CB  . ILE C  1 235 ? 11.495  -12.184 -14.440 1.00 30.74  ? 236  ILE A CB  1 
ATOM   5850  C CG1 . ILE C  1 235 ? 12.958  -12.529 -14.161 1.00 30.05  ? 236  ILE A CG1 1 
ATOM   5851  C CG2 . ILE C  1 235 ? 10.758  -13.388 -15.062 1.00 30.90  ? 236  ILE A CG2 1 
ATOM   5852  C CD1 . ILE C  1 235 ? 13.705  -13.087 -15.329 1.00 28.25  ? 236  ILE A CD1 1 
ATOM   5853  N N   . LEU C  1 236 ? 9.507   -10.704 -16.878 1.00 32.71  ? 237  LEU A N   1 
ATOM   5854  C CA  . LEU C  1 236 ? 8.122   -10.468 -17.287 1.00 35.03  ? 237  LEU A CA  1 
ATOM   5855  C C   . LEU C  1 236 ? 7.319   -11.790 -17.317 1.00 39.84  ? 237  LEU A C   1 
ATOM   5856  O O   . LEU C  1 236 ? 7.628   -12.697 -18.099 1.00 39.44  ? 237  LEU A O   1 
ATOM   5857  C CB  . LEU C  1 236 ? 8.070   -9.803  -18.655 1.00 35.78  ? 237  LEU A CB  1 
ATOM   5858  C CG  . LEU C  1 236 ? 6.665   -9.360  -19.077 1.00 39.89  ? 237  LEU A CG  1 
ATOM   5859  C CD1 . LEU C  1 236 ? 6.149   -8.263  -18.155 1.00 38.18  ? 237  LEU A CD1 1 
ATOM   5860  C CD2 . LEU C  1 236 ? 6.610   -8.929  -20.536 1.00 37.14  ? 237  LEU A CD2 1 
ATOM   5861  N N   . LYS C  1 237 ? 6.318   -11.911 -16.448 1.00 40.51  ? 238  LYS A N   1 
ATOM   5862  C CA  . LYS C  1 237 ? 5.523   -13.134 -16.376 1.00 38.19  ? 238  LYS A CA  1 
ATOM   5863  C C   . LYS C  1 237 ? 4.744   -13.404 -17.669 1.00 41.63  ? 238  LYS A C   1 
ATOM   5864  O O   . LYS C  1 237 ? 4.320   -12.466 -18.362 1.00 42.06  ? 238  LYS A O   1 
ATOM   5865  C CB  . LYS C  1 237 ? 4.553   -13.051 -15.185 1.00 42.45  ? 238  LYS A CB  1 
ATOM   5866  C CG  . LYS C  1 237 ? 5.209   -12.914 -13.796 1.00 36.66  ? 238  LYS A CG  1 
ATOM   5867  C CD  . LYS C  1 237 ? 6.240   -14.004 -13.534 1.00 37.98  ? 238  LYS A CD  1 
ATOM   5868  C CE  . LYS C  1 237 ? 5.603   -15.326 -13.107 1.00 48.06  ? 238  LYS A CE  1 
ATOM   5869  N NZ  . LYS C  1 237 ? 6.616   -16.438 -13.066 1.00 57.07  ? 238  LYS A NZ  1 
ATOM   5870  N N   . SER C  1 238 ? 4.538   -14.687 -17.969 1.00 41.86  ? 239  SER A N   1 
ATOM   5871  C CA  . SER C  1 238 ? 3.727   -15.104 -19.109 1.00 39.89  ? 239  SER A CA  1 
ATOM   5872  C C   . SER C  1 238 ? 2.351   -14.483 -19.016 1.00 44.51  ? 239  SER A C   1 
ATOM   5873  O O   . SER C  1 238 ? 1.707   -14.589 -17.972 1.00 44.06  ? 239  SER A O   1 
ATOM   5874  C CB  . SER C  1 238 ? 3.600   -16.624 -19.154 1.00 40.69  ? 239  SER A CB  1 
ATOM   5875  O OG  . SER C  1 238 ? 2.867   -17.038 -20.291 1.00 48.22  ? 239  SER A OG  1 
ATOM   5876  N N   . ASN C  1 239 ? 1.916   -13.860 -20.112 1.00 41.97  ? 240  ASN A N   1 
ATOM   5877  C CA  . ASN C  1 239 ? 0.618   -13.190 -20.231 1.00 39.97  ? 240  ASN A CA  1 
ATOM   5878  C C   . ASN C  1 239 ? 0.559   -11.787 -19.562 1.00 41.52  ? 240  ASN A C   1 
ATOM   5879  O O   . ASN C  1 239 ? -0.507  -11.158 -19.545 1.00 42.19  ? 240  ASN A O   1 
ATOM   5880  C CB  . ASN C  1 239 ? -0.469  -14.113 -19.648 1.00 45.72  ? 240  ASN A CB  1 
ATOM   5881  C CG  . ASN C  1 239 ? -1.800  -14.033 -20.377 1.00 59.90  ? 240  ASN A CG  1 
ATOM   5882  O OD1 . ASN C  1 239 ? -2.757  -13.407 -19.898 1.00 65.95  ? 240  ASN A OD1 1 
ATOM   5883  N ND2 . ASN C  1 239 ? -1.890  -14.727 -21.509 1.00 58.70  ? 240  ASN A ND2 1 
ATOM   5884  N N   . ASP C  1 240 ? 1.699   -11.242 -19.115 1.00 40.47  ? 241  ASP A N   1 
ATOM   5885  C CA  . ASP C  1 240 ? 1.735   -9.855  -18.589 1.00 35.96  ? 241  ASP A CA  1 
ATOM   5886  C C   . ASP C  1 240 ? 2.296   -8.901  -19.648 1.00 43.07  ? 241  ASP A C   1 
ATOM   5887  O O   . ASP C  1 240 ? 2.814   -9.332  -20.689 1.00 42.68  ? 241  ASP A O   1 
ATOM   5888  C CB  . ASP C  1 240 ? 2.573   -9.760  -17.294 1.00 30.07  ? 241  ASP A CB  1 
ATOM   5889  C CG  . ASP C  1 240 ? 2.350   -8.431  -16.502 1.00 37.87  ? 241  ASP A CG  1 
ATOM   5890  O OD1 . ASP C  1 240 ? 1.320   -7.730  -16.692 1.00 41.73  ? 241  ASP A OD1 1 
ATOM   5891  O OD2 . ASP C  1 240 ? 3.235   -8.073  -15.688 1.00 36.27  ? 241  ASP A OD2 1 
ATOM   5892  N N   . ALA C  1 241 ? 2.241   -7.602  -19.373 1.00 42.88  ? 242  ALA A N   1 
ATOM   5893  C CA  . ALA C  1 241 ? 2.691   -6.621  -20.349 1.00 45.27  ? 242  ALA A CA  1 
ATOM   5894  C C   . ALA C  1 241 ? 3.636   -5.609  -19.707 1.00 46.04  ? 242  ALA A C   1 
ATOM   5895  O O   . ALA C  1 241 ? 3.460   -5.260  -18.532 1.00 44.12  ? 242  ALA A O   1 
ATOM   5896  C CB  . ALA C  1 241 ? 1.477   -5.901  -20.963 1.00 43.24  ? 242  ALA A CB  1 
ATOM   5897  N N   . ILE C  1 242 ? 4.594   -5.095  -20.490 1.00 43.36  ? 243  ILE A N   1 
ATOM   5898  C CA  . ILE C  1 242 ? 5.529   -4.079  -19.984 1.00 38.97  ? 243  ILE A CA  1 
ATOM   5899  C C   . ILE C  1 242 ? 5.330   -2.775  -20.750 1.00 34.04  ? 243  ILE A C   1 
ATOM   5900  O O   . ILE C  1 242 ? 5.027   -2.792  -21.937 1.00 42.35  ? 243  ILE A O   1 
ATOM   5901  C CB  . ILE C  1 242 ? 6.998   -4.537  -20.090 1.00 37.67  ? 243  ILE A CB  1 
ATOM   5902  C CG1 . ILE C  1 242 ? 7.926   -3.615  -19.301 1.00 32.72  ? 243  ILE A CG1 1 
ATOM   5903  C CG2 . ILE C  1 242 ? 7.436   -4.613  -21.538 1.00 40.34  ? 243  ILE A CG2 1 
ATOM   5904  C CD1 . ILE C  1 242 ? 9.324   -4.149  -19.204 1.00 30.64  ? 243  ILE A CD1 1 
ATOM   5905  N N   . ASN C  1 243 ? 5.403   -1.651  -20.049 1.00 33.23  ? 244  ASN A N   1 
ATOM   5906  C CA  . ASN C  1 243 ? 5.174   -0.355  -20.661 1.00 35.55  ? 244  ASN A CA  1 
ATOM   5907  C C   . ASN C  1 243 ? 6.333   0.608   -20.415 1.00 38.78  ? 244  ASN A C   1 
ATOM   5908  O O   . ASN C  1 243 ? 6.715   0.820   -19.248 1.00 37.06  ? 244  ASN A O   1 
ATOM   5909  C CB  . ASN C  1 243 ? 3.860   0.248   -20.144 1.00 41.53  ? 244  ASN A CB  1 
ATOM   5910  C CG  . ASN C  1 243 ? 2.645   -0.595  -20.535 1.00 51.02  ? 244  ASN A CG  1 
ATOM   5911  O OD1 . ASN C  1 243 ? 2.106   -0.446  -21.641 1.00 54.49  ? 244  ASN A OD1 1 
ATOM   5912  N ND2 . ASN C  1 243 ? 2.200   -1.474  -19.625 1.00 48.73  ? 244  ASN A ND2 1 
ATOM   5913  N N   . PHE C  1 244 ? 6.894   1.179   -21.493 1.00 30.77  ? 245  PHE A N   1 
ATOM   5914  C CA  . PHE C  1 244 ? 7.985   2.162   -21.367 1.00 26.70  ? 245  PHE A CA  1 
ATOM   5915  C C   . PHE C  1 244 ? 7.572   3.577   -21.788 1.00 31.85  ? 245  PHE A C   1 
ATOM   5916  O O   . PHE C  1 244 ? 6.901   3.757   -22.826 1.00 35.67  ? 245  PHE A O   1 
ATOM   5917  C CB  . PHE C  1 244 ? 9.183   1.758   -22.220 1.00 29.16  ? 245  PHE A CB  1 
ATOM   5918  C CG  . PHE C  1 244 ? 9.821   0.428   -21.857 1.00 29.53  ? 245  PHE A CG  1 
ATOM   5919  C CD1 . PHE C  1 244 ? 10.759  0.341   -20.838 1.00 24.31  ? 245  PHE A CD1 1 
ATOM   5920  C CD2 . PHE C  1 244 ? 9.528   -0.723  -22.609 1.00 28.08  ? 245  PHE A CD2 1 
ATOM   5921  C CE1 . PHE C  1 244 ? 11.385  -0.886  -20.549 1.00 26.99  ? 245  PHE A CE1 1 
ATOM   5922  C CE2 . PHE C  1 244 ? 10.131  -1.962  -22.322 1.00 26.62  ? 245  PHE A CE2 1 
ATOM   5923  C CZ  . PHE C  1 244 ? 11.059  -2.047  -21.293 1.00 21.81  ? 245  PHE A CZ  1 
ATOM   5924  N N   . GLU C  1 245 ? 7.975   4.585   -21.019 1.00 27.60  ? 246  GLU A N   1 
ATOM   5925  C CA  . GLU C  1 245 ? 7.805   5.973   -21.457 1.00 33.10  ? 246  GLU A CA  1 
ATOM   5926  C C   . GLU C  1 245 ? 8.999   6.876   -21.091 1.00 34.75  ? 246  GLU A C   1 
ATOM   5927  O O   . GLU C  1 245 ? 9.467   6.869   -19.940 1.00 34.27  ? 246  GLU A O   1 
ATOM   5928  C CB  . GLU C  1 245 ? 6.497   6.584   -20.915 1.00 31.01  ? 246  GLU A CB  1 
ATOM   5929  C CG  . GLU C  1 245 ? 6.304   8.037   -21.455 1.00 36.55  ? 246  GLU A CG  1 
ATOM   5930  C CD  . GLU C  1 245 ? 4.983   8.704   -21.059 1.00 41.96  ? 246  GLU A CD  1 
ATOM   5931  O OE1 . GLU C  1 245 ? 3.946   8.002   -20.998 1.00 45.42  ? 246  GLU A OE1 1 
ATOM   5932  O OE2 . GLU C  1 245 ? 4.993   9.933   -20.803 1.00 39.21  ? 246  GLU A OE2 1 
ATOM   5933  N N   . SER C  1 246 ? 9.473   7.657   -22.066 1.00 30.31  ? 247  SER A N   1 
ATOM   5934  C CA  . SER C  1 246 ? 10.686  8.468   -21.909 1.00 29.32  ? 247  SER A CA  1 
ATOM   5935  C C   . SER C  1 246 ? 10.778  9.660   -22.850 1.00 33.02  ? 247  SER A C   1 
ATOM   5936  O O   . SER C  1 246 ? 10.383  9.560   -24.019 1.00 34.63  ? 247  SER A O   1 
ATOM   5937  C CB  . SER C  1 246 ? 11.928  7.615   -22.149 1.00 26.34  ? 247  SER A CB  1 
ATOM   5938  O OG  . SER C  1 246 ? 13.109  8.383   -21.952 1.00 27.82  ? 247  SER A OG  1 
ATOM   5939  N N   . ASN C  1 247 ? 11.339  10.767  -22.360 1.00 29.07  ? 248  ASN A N   1 
ATOM   5940  C CA  . ASN C  1 247 ? 11.666  11.913  -23.224 1.00 29.87  ? 248  ASN A CA  1 
ATOM   5941  C C   . ASN C  1 247 ? 13.148  12.235  -23.254 1.00 29.83  ? 248  ASN A C   1 
ATOM   5942  O O   . ASN C  1 247 ? 13.491  13.402  -23.482 1.00 27.58  ? 248  ASN A O   1 
ATOM   5943  C CB  . ASN C  1 247 ? 10.931  13.164  -22.773 1.00 28.43  ? 248  ASN A CB  1 
ATOM   5944  C CG  . ASN C  1 247 ? 11.383  13.615  -21.378 1.00 35.45  ? 248  ASN A CG  1 
ATOM   5945  O OD1 . ASN C  1 247 ? 11.765  12.781  -20.536 1.00 28.79  ? 248  ASN A OD1 1 
ATOM   5946  N ND2 . ASN C  1 247 ? 11.387  14.930  -21.143 1.00 32.20  ? 248  ASN A ND2 1 
ATOM   5947  N N   . GLY C  1 248 ? 14.006  11.221  -23.037 1.00 28.08  ? 249  GLY A N   1 
ATOM   5948  C CA  . GLY C  1 248 ? 15.458  11.377  -23.120 1.00 25.67  ? 249  GLY A CA  1 
ATOM   5949  C C   . GLY C  1 248 ? 16.267  10.439  -22.204 1.00 30.09  ? 249  GLY A C   1 
ATOM   5950  O O   . GLY C  1 248 ? 15.736  9.878   -21.230 1.00 24.14  ? 249  GLY A O   1 
ATOM   5951  N N   . ASN C  1 249 ? 17.543  10.244  -22.550 1.00 29.19  ? 250  ASN A N   1 
ATOM   5952  C CA  . ASN C  1 249 ? 18.515  9.435   -21.782 1.00 28.03  ? 250  ASN A CA  1 
ATOM   5953  C C   . ASN C  1 249 ? 18.261  7.932   -21.729 1.00 25.42  ? 250  ASN A C   1 
ATOM   5954  O O   . ASN C  1 249 ? 18.879  7.242   -20.922 1.00 21.33  ? 250  ASN A O   1 
ATOM   5955  C CB  . ASN C  1 249 ? 18.643  9.923   -20.337 1.00 26.45  ? 250  ASN A CB  1 
ATOM   5956  C CG  . ASN C  1 249 ? 19.066  11.375  -20.237 1.00 28.83  ? 250  ASN A CG  1 
ATOM   5957  O OD1 . ASN C  1 249 ? 18.250  12.277  -20.385 1.00 27.42  ? 250  ASN A OD1 1 
ATOM   5958  N ND2 . ASN C  1 249 ? 20.359  11.604  -19.962 1.00 26.24  ? 250  ASN A ND2 1 
ATOM   5959  N N   . PHE C  1 250 ? 17.421  7.439   -22.636 1.00 22.84  ? 251  PHE A N   1 
ATOM   5960  C CA  . PHE C  1 250 ? 16.885  6.071   -22.585 1.00 22.98  ? 251  PHE A CA  1 
ATOM   5961  C C   . PHE C  1 250 ? 17.727  5.123   -23.418 1.00 21.24  ? 251  PHE A C   1 
ATOM   5962  O O   . PHE C  1 250 ? 18.018  5.411   -24.572 1.00 24.30  ? 251  PHE A O   1 
ATOM   5963  C CB  . PHE C  1 250 ? 15.413  6.079   -23.054 1.00 21.28  ? 251  PHE A CB  1 
ATOM   5964  C CG  . PHE C  1 250 ? 14.712  4.738   -23.009 1.00 23.35  ? 251  PHE A CG  1 
ATOM   5965  C CD1 . PHE C  1 250 ? 15.015  3.777   -22.033 1.00 21.90  ? 251  PHE A CD1 1 
ATOM   5966  C CD2 . PHE C  1 250 ? 13.718  4.441   -23.978 1.00 22.85  ? 251  PHE A CD2 1 
ATOM   5967  C CE1 . PHE C  1 250 ? 14.328  2.530   -22.017 1.00 23.80  ? 251  PHE A CE1 1 
ATOM   5968  C CE2 . PHE C  1 250 ? 13.037  3.221   -23.985 1.00 19.58  ? 251  PHE A CE2 1 
ATOM   5969  C CZ  . PHE C  1 250 ? 13.335  2.253   -22.996 1.00 23.44  ? 251  PHE A CZ  1 
ATOM   5970  N N   . ILE C  1 251 ? 18.200  4.040   -22.819 1.00 19.05  ? 252  ILE A N   1 
ATOM   5971  C CA  . ILE C  1 251 ? 18.881  3.013   -23.600 1.00 20.93  ? 252  ILE A CA  1 
ATOM   5972  C C   . ILE C  1 251 ? 17.938  1.815   -23.790 1.00 24.33  ? 252  ILE A C   1 
ATOM   5973  O O   . ILE C  1 251 ? 17.782  0.979   -22.875 1.00 23.07  ? 252  ILE A O   1 
ATOM   5974  C CB  . ILE C  1 251 ? 20.201  2.686   -22.936 1.00 21.38  ? 252  ILE A CB  1 
ATOM   5975  C CG1 . ILE C  1 251 ? 21.042  3.958   -23.022 1.00 22.28  ? 252  ILE A CG1 1 
ATOM   5976  C CG2 . ILE C  1 251 ? 20.918  1.567   -23.642 1.00 17.07  ? 252  ILE A CG2 1 
ATOM   5977  C CD1 . ILE C  1 251 ? 22.069  4.052   -21.989 1.00 24.30  ? 252  ILE A CD1 1 
ATOM   5978  N N   . ALA C  1 252 ? 17.300  1.738   -24.973 1.00 18.80  ? 253  ALA A N   1 
ATOM   5979  C CA  . ALA C  1 252 ? 16.106  0.885   -25.090 1.00 20.05  ? 253  ALA A CA  1 
ATOM   5980  C C   . ALA C  1 252 ? 16.458  -0.546  -25.326 1.00 19.57  ? 253  ALA A C   1 
ATOM   5981  O O   . ALA C  1 252 ? 17.567  -0.825  -25.761 1.00 22.84  ? 253  ALA A O   1 
ATOM   5982  C CB  . ALA C  1 252 ? 15.198  1.368   -26.179 1.00 19.39  ? 253  ALA A CB  1 
ATOM   5983  N N   . PRO C  1 253 ? 15.545  -1.467  -24.960 1.00 21.31  ? 254  PRO A N   1 
ATOM   5984  C CA  . PRO C  1 253 ? 15.698  -2.892  -25.290 1.00 19.87  ? 254  PRO A CA  1 
ATOM   5985  C C   . PRO C  1 253 ? 15.644  -3.103  -26.791 1.00 26.31  ? 254  PRO A C   1 
ATOM   5986  O O   . PRO C  1 253 ? 14.776  -2.505  -27.441 1.00 30.66  ? 254  PRO A O   1 
ATOM   5987  C CB  . PRO C  1 253 ? 14.483  -3.561  -24.609 1.00 18.38  ? 254  PRO A CB  1 
ATOM   5988  C CG  . PRO C  1 253 ? 14.084  -2.628  -23.527 1.00 19.43  ? 254  PRO A CG  1 
ATOM   5989  C CD  . PRO C  1 253 ? 14.454  -1.232  -23.983 1.00 22.08  ? 254  PRO A CD  1 
ATOM   5990  N N   . GLU C  1 254 ? 16.524  -3.946  -27.327 1.00 28.10  ? 255  GLU A N   1 
ATOM   5991  C CA  . GLU C  1 254 ? 16.342  -4.462  -28.683 1.00 29.37  ? 255  GLU A CA  1 
ATOM   5992  C C   . GLU C  1 254 ? 16.044  -5.967  -28.614 1.00 31.26  ? 255  GLU A C   1 
ATOM   5993  O O   . GLU C  1 254 ? 15.065  -6.434  -29.197 1.00 33.39  ? 255  GLU A O   1 
ATOM   5994  C CB  . GLU C  1 254 ? 17.563  -4.207  -29.566 1.00 27.92  ? 255  GLU A CB  1 
ATOM   5995  C CG  . GLU C  1 254 ? 17.373  -4.818  -30.958 1.00 31.09  ? 255  GLU A CG  1 
ATOM   5996  C CD  . GLU C  1 254 ? 18.428  -4.380  -31.957 1.00 35.31  ? 255  GLU A CD  1 
ATOM   5997  O OE1 . GLU C  1 254 ? 18.595  -3.155  -32.174 1.00 40.36  ? 255  GLU A OE1 1 
ATOM   5998  O OE2 . GLU C  1 254 ? 19.117  -5.269  -32.497 1.00 35.43  ? 255  GLU A OE2 1 
ATOM   5999  N N   . ASN C  1 255 ? 16.859  -6.705  -27.861 1.00 29.14  ? 256  ASN A N   1 
ATOM   6000  C CA  . ASN C  1 255 ? 16.670  -8.149  -27.653 1.00 26.64  ? 256  ASN A CA  1 
ATOM   6001  C C   . ASN C  1 255 ? 16.383  -8.502  -26.171 1.00 29.92  ? 256  ASN A C   1 
ATOM   6002  O O   . ASN C  1 255 ? 16.759  -7.752  -25.263 1.00 28.02  ? 256  ASN A O   1 
ATOM   6003  C CB  . ASN C  1 255 ? 17.908  -8.905  -28.158 1.00 27.30  ? 256  ASN A CB  1 
ATOM   6004  C CG  . ASN C  1 255 ? 18.143  -8.714  -29.659 1.00 31.47  ? 256  ASN A CG  1 
ATOM   6005  O OD1 . ASN C  1 255 ? 17.185  -8.721  -30.437 1.00 28.67  ? 256  ASN A OD1 1 
ATOM   6006  N ND2 . ASN C  1 255 ? 19.414  -8.525  -30.070 1.00 28.53  ? 256  ASN A ND2 1 
ATOM   6007  N N   . ALA C  1 256 ? 15.668  -9.603  -25.937 1.00 30.03  ? 257  ALA A N   1 
ATOM   6008  C CA  . ALA C  1 256 ? 15.382  -10.104 -24.589 1.00 23.01  ? 257  ALA A CA  1 
ATOM   6009  C C   . ALA C  1 256 ? 15.513  -11.629 -24.568 1.00 29.12  ? 257  ALA A C   1 
ATOM   6010  O O   . ALA C  1 256 ? 15.715  -12.240 -25.620 1.00 29.82  ? 257  ALA A O   1 
ATOM   6011  C CB  . ALA C  1 256 ? 14.003  -9.687  -24.147 1.00 24.51  ? 257  ALA A CB  1 
ATOM   6012  N N   . TYR C  1 257 ? 15.400  -12.252 -23.393 1.00 30.53  ? 258  TYR A N   1 
ATOM   6013  C CA  . TYR C  1 257 ? 15.640  -13.709 -23.283 1.00 31.97  ? 258  TYR A CA  1 
ATOM   6014  C C   . TYR C  1 257 ? 14.458  -14.535 -22.712 1.00 35.28  ? 258  TYR A C   1 
ATOM   6015  O O   . TYR C  1 257 ? 13.975  -14.242 -21.593 1.00 30.65  ? 258  TYR A O   1 
ATOM   6016  C CB  . TYR C  1 257 ? 16.886  -13.973 -22.418 1.00 26.27  ? 258  TYR A CB  1 
ATOM   6017  C CG  . TYR C  1 257 ? 18.199  -13.394 -22.917 1.00 26.98  ? 258  TYR A CG  1 
ATOM   6018  C CD1 . TYR C  1 257 ? 18.545  -12.071 -22.658 1.00 25.76  ? 258  TYR A CD1 1 
ATOM   6019  C CD2 . TYR C  1 257 ? 19.127  -14.192 -23.597 1.00 29.08  ? 258  TYR A CD2 1 
ATOM   6020  C CE1 . TYR C  1 257 ? 19.766  -11.533 -23.104 1.00 27.97  ? 258  TYR A CE1 1 
ATOM   6021  C CE2 . TYR C  1 257 ? 20.355  -13.673 -24.023 1.00 26.91  ? 258  TYR A CE2 1 
ATOM   6022  C CZ  . TYR C  1 257 ? 20.669  -12.345 -23.776 1.00 30.51  ? 258  TYR A CZ  1 
ATOM   6023  O OH  . TYR C  1 257 ? 21.876  -11.819 -24.211 1.00 32.86  ? 258  TYR A OH  1 
ATOM   6024  N N   . LYS C  1 258 ? 14.023  -15.564 -23.463 1.00 33.53  ? 259  LYS A N   1 
ATOM   6025  C CA  . LYS C  1 258 ? 13.004  -16.497 -22.969 1.00 35.59  ? 259  LYS A CA  1 
ATOM   6026  C C   . LYS C  1 258 ? 13.675  -17.628 -22.233 1.00 35.73  ? 259  LYS A C   1 
ATOM   6027  O O   . LYS C  1 258 ? 14.503  -18.352 -22.805 1.00 37.47  ? 259  LYS A O   1 
ATOM   6028  C CB  . LYS C  1 258 ? 12.169  -17.098 -24.085 1.00 36.65  ? 259  LYS A CB  1 
ATOM   6029  C CG  . LYS C  1 258 ? 11.373  -16.117 -24.915 1.00 51.73  ? 259  LYS A CG  1 
ATOM   6030  C CD  . LYS C  1 258 ? 10.336  -16.876 -25.724 1.00 49.53  ? 259  LYS A CD  1 
ATOM   6031  C CE  . LYS C  1 258 ? 10.984  -17.869 -26.650 1.00 47.29  ? 259  LYS A CE  1 
ATOM   6032  N NZ  . LYS C  1 258 ? 9.908   -18.483 -27.459 1.00 53.52  ? 259  LYS A NZ  1 
ATOM   6033  N N   . ILE C  1 259 ? 13.260  -17.825 -20.994 1.00 29.97  ? 260  ILE A N   1 
ATOM   6034  C CA  . ILE C  1 259 ? 13.843  -18.872 -20.166 1.00 38.24  ? 260  ILE A CA  1 
ATOM   6035  C C   . ILE C  1 259 ? 13.154  -20.188 -20.554 1.00 36.48  ? 260  ILE A C   1 
ATOM   6036  O O   . ILE C  1 259 ? 12.012  -20.449 -20.164 1.00 37.26  ? 260  ILE A O   1 
ATOM   6037  C CB  . ILE C  1 259 ? 13.676  -18.540 -18.625 1.00 36.01  ? 260  ILE A CB  1 
ATOM   6038  C CG1 . ILE C  1 259 ? 14.291  -17.170 -18.302 1.00 33.61  ? 260  ILE A CG1 1 
ATOM   6039  C CG2 . ILE C  1 259 ? 14.310  -19.622 -17.767 1.00 34.08  ? 260  ILE A CG2 1 
ATOM   6040  C CD1 . ILE C  1 259 ? 13.684  -16.450 -17.134 1.00 27.79  ? 260  ILE A CD1 1 
ATOM   6041  N N   . VAL C  1 260 A 13.858  -20.999 -21.340 1.00 35.56  ? 260  VAL A N   1 
ATOM   6042  C CA  . VAL C  1 260 A 13.252  -22.157 -21.989 1.00 42.22  ? 260  VAL A CA  1 
ATOM   6043  C C   . VAL C  1 260 A 13.556  -23.467 -21.260 1.00 46.78  ? 260  VAL A C   1 
ATOM   6044  O O   . VAL C  1 260 A 12.781  -24.422 -21.351 1.00 43.52  ? 260  VAL A O   1 
ATOM   6045  C CB  . VAL C  1 260 A 13.653  -22.269 -23.492 1.00 41.16  ? 260  VAL A CB  1 
ATOM   6046  C CG1 . VAL C  1 260 A 13.038  -21.133 -24.290 1.00 38.86  ? 260  VAL A CG1 1 
ATOM   6047  C CG2 . VAL C  1 260 A 15.166  -22.332 -23.694 1.00 41.38  ? 260  VAL A CG2 1 
ATOM   6048  N N   . LYS C  1 261 ? 14.679  -23.532 -20.552 1.00 44.54  ? 261  LYS A N   1 
ATOM   6049  C CA  . LYS C  1 261 ? 14.985  -24.754 -19.832 1.00 40.86  ? 261  LYS A CA  1 
ATOM   6050  C C   . LYS C  1 261 ? 15.455  -24.410 -18.408 1.00 47.14  ? 261  LYS A C   1 
ATOM   6051  O O   . LYS C  1 261 ? 16.377  -23.611 -18.201 1.00 43.31  ? 261  LYS A O   1 
ATOM   6052  C CB  . LYS C  1 261 ? 16.046  -25.555 -20.588 1.00 42.97  ? 261  LYS A CB  1 
ATOM   6053  C CG  . LYS C  1 261 ? 16.293  -26.944 -20.012 1.00 51.70  ? 261  LYS A CG  1 
ATOM   6054  C CD  . LYS C  1 261 ? 15.956  -28.029 -21.069 1.00 59.35  ? 261  LYS A CD  1 
ATOM   6055  C CE  . LYS C  1 261 ? 16.194  -29.460 -20.564 1.00 58.96  ? 261  LYS A CE  1 
ATOM   6056  N NZ  . LYS C  1 261 ? 15.082  -29.881 -19.638 1.00 57.26  ? 261  LYS A NZ  1 
ATOM   6057  N N   . LYS C  1 262 ? 14.797  -25.018 -17.421 1.00 53.63  ? 262  LYS A N   1 
ATOM   6058  C CA  . LYS C  1 262 ? 15.162  -24.825 -16.021 1.00 46.36  ? 262  LYS A CA  1 
ATOM   6059  C C   . LYS C  1 262 ? 15.808  -26.072 -15.417 1.00 49.83  ? 262  LYS A C   1 
ATOM   6060  O O   . LYS C  1 262 ? 15.491  -27.196 -15.811 1.00 57.05  ? 262  LYS A O   1 
ATOM   6061  C CB  . LYS C  1 262 ? 13.913  -24.437 -15.247 1.00 44.72  ? 262  LYS A CB  1 
ATOM   6062  C CG  . LYS C  1 262 ? 13.481  -23.019 -15.559 1.00 50.10  ? 262  LYS A CG  1 
ATOM   6063  C CD  . LYS C  1 262 ? 12.324  -22.537 -14.714 1.00 50.59  ? 262  LYS A CD  1 
ATOM   6064  C CE  . LYS C  1 262 ? 12.064  -21.062 -15.005 1.00 57.53  ? 262  LYS A CE  1 
ATOM   6065  N NZ  . LYS C  1 262 ? 10.943  -20.496 -14.211 1.00 74.40  ? 262  LYS A NZ  1 
ATOM   6066  N N   . GLY C  1 263 ? 16.698  -25.877 -14.450 1.00 48.24  ? 263  GLY A N   1 
ATOM   6067  C CA  . GLY C  1 263 ? 17.387  -26.993 -13.831 1.00 50.16  ? 263  GLY A CA  1 
ATOM   6068  C C   . GLY C  1 263 ? 18.489  -26.569 -12.881 1.00 51.47  ? 263  GLY A C   1 
ATOM   6069  O O   . GLY C  1 263 ? 18.529  -25.421 -12.452 1.00 55.66  ? 263  GLY A O   1 
ATOM   6070  N N   . ASP C  1 264 ? 19.386  -27.497 -12.551 1.00 55.95  ? 264  ASP A N   1 
ATOM   6071  C CA  . ASP C  1 264 ? 20.505  -27.211 -11.647 1.00 53.57  ? 264  ASP A CA  1 
ATOM   6072  C C   . ASP C  1 264 ? 21.800  -26.775 -12.356 1.00 56.26  ? 264  ASP A C   1 
ATOM   6073  O O   . ASP C  1 264 ? 22.297  -27.447 -13.275 1.00 56.25  ? 264  ASP A O   1 
ATOM   6074  C CB  . ASP C  1 264 ? 20.762  -28.434 -10.763 1.00 53.67  ? 264  ASP A CB  1 
ATOM   6075  C CG  . ASP C  1 264 ? 19.784  -28.512 -9.577  1.00 72.65  ? 264  ASP A CG  1 
ATOM   6076  O OD1 . ASP C  1 264 ? 19.101  -27.496 -9.279  1.00 68.13  ? 264  ASP A OD1 1 
ATOM   6077  O OD2 . ASP C  1 264 ? 19.697  -29.592 -8.947  1.00 76.87  ? 264  ASP A OD2 1 
ATOM   6078  N N   . SER C  1 265 ? 22.339  -25.638 -11.930 1.00 47.93  ? 265  SER A N   1 
ATOM   6079  C CA  . SER C  1 265 ? 23.591  -25.144 -12.489 1.00 44.00  ? 265  SER A CA  1 
ATOM   6080  C C   . SER C  1 265 ? 24.299  -24.288 -11.451 1.00 43.61  ? 265  SER A C   1 
ATOM   6081  O O   . SER C  1 265 ? 23.753  -24.002 -10.391 1.00 39.72  ? 265  SER A O   1 
ATOM   6082  C CB  . SER C  1 265 ? 23.352  -24.343 -13.776 1.00 48.26  ? 265  SER A CB  1 
ATOM   6083  O OG  . SER C  1 265 ? 24.566  -23.801 -14.284 1.00 47.43  ? 265  SER A OG  1 
ATOM   6084  N N   . THR C  1 266 ? 25.501  -23.844 -11.772 1.00 42.93  ? 266  THR A N   1 
ATOM   6085  C CA  . THR C  1 266 ? 26.240  -22.998 -10.857 1.00 34.52  ? 266  THR A CA  1 
ATOM   6086  C C   . THR C  1 266 ? 27.227  -22.192 -11.685 1.00 35.46  ? 266  THR A C   1 
ATOM   6087  O O   . THR C  1 266 ? 27.444  -22.499 -12.859 1.00 35.81  ? 266  THR A O   1 
ATOM   6088  C CB  . THR C  1 266 ? 26.963  -23.826 -9.798  1.00 29.92  ? 266  THR A CB  1 
ATOM   6089  O OG1 . THR C  1 266 ? 27.539  -22.963 -8.819  1.00 39.37  ? 266  THR A OG1 1 
ATOM   6090  C CG2 . THR C  1 266 ? 28.067  -24.639 -10.424 1.00 36.31  ? 266  THR A CG2 1 
ATOM   6091  N N   . ILE C  1 267 ? 27.813  -21.162 -11.086 1.00 34.78  ? 267  ILE A N   1 
ATOM   6092  C CA  . ILE C  1 267 ? 28.870  -20.407 -11.745 1.00 35.47  ? 267  ILE A CA  1 
ATOM   6093  C C   . ILE C  1 267 ? 30.208  -20.617 -11.030 1.00 37.62  ? 267  ILE A C   1 
ATOM   6094  O O   . ILE C  1 267 ? 30.388  -20.174 -9.892  1.00 34.28  ? 267  ILE A O   1 
ATOM   6095  C CB  . ILE C  1 267 ? 28.525  -18.914 -11.787 1.00 34.17  ? 267  ILE A CB  1 
ATOM   6096  C CG1 . ILE C  1 267 ? 27.107  -18.724 -12.348 1.00 32.18  ? 267  ILE A CG1 1 
ATOM   6097  C CG2 . ILE C  1 267 ? 29.609  -18.126 -12.520 1.00 29.93  ? 267  ILE A CG2 1 
ATOM   6098  C CD1 . ILE C  1 267 ? 26.666  -17.278 -12.448 1.00 32.14  ? 267  ILE A CD1 1 
ATOM   6099  N N   . MET C  1 268 ? 31.143  -21.275 -11.717 1.00 39.89  ? 268  MET A N   1 
ATOM   6100  C CA  . MET C  1 268 ? 32.457  -21.582 -11.149 1.00 40.40  ? 268  MET A CA  1 
ATOM   6101  C C   . MET C  1 268 ? 33.530  -20.540 -11.474 1.00 40.80  ? 268  MET A C   1 
ATOM   6102  O O   . MET C  1 268 ? 33.658  -20.127 -12.629 1.00 47.04  ? 268  MET A O   1 
ATOM   6103  C CB  . MET C  1 268 ? 32.933  -22.955 -11.655 1.00 44.49  ? 268  MET A CB  1 
ATOM   6104  C CG  . MET C  1 268 ? 32.645  -24.109 -10.713 1.00 52.98  ? 268  MET A CG  1 
ATOM   6105  S SD  . MET C  1 268 ? 33.035  -25.702 -11.466 1.00 46.61  ? 268  MET A SD  1 
ATOM   6106  C CE  . MET C  1 268 ? 34.479  -25.167 -12.367 1.00 44.18  ? 268  MET A CE  1 
ATOM   6107  N N   . LYS C  1 269 ? 34.342  -20.178 -10.481 1.00 40.27  ? 269  LYS A N   1 
ATOM   6108  C CA  . LYS C  1 269 ? 35.484  -19.274 -10.674 1.00 44.69  ? 269  LYS A CA  1 
ATOM   6109  C C   . LYS C  1 269 ? 36.788  -20.061 -10.860 1.00 51.25  ? 269  LYS A C   1 
ATOM   6110  O O   . LYS C  1 269 ? 37.237  -20.775 -9.949  1.00 48.40  ? 269  LYS A O   1 
ATOM   6111  C CB  . LYS C  1 269 ? 35.630  -18.323 -9.495  1.00 44.18  ? 269  LYS A CB  1 
ATOM   6112  C CG  . LYS C  1 269 ? 34.448  -17.433 -9.309  1.00 45.55  ? 269  LYS A CG  1 
ATOM   6113  C CD  . LYS C  1 269 ? 34.310  -16.438 -10.424 1.00 49.38  ? 269  LYS A CD  1 
ATOM   6114  C CE  . LYS C  1 269 ? 33.092  -15.597 -10.129 1.00 49.79  ? 269  LYS A CE  1 
ATOM   6115  N NZ  . LYS C  1 269 ? 31.932  -16.561 -9.947  1.00 45.94  ? 269  LYS A NZ  1 
ATOM   6116  N N   . SER C  1 270 ? 37.383  -19.931 -12.046 1.00 53.77  ? 270  SER A N   1 
ATOM   6117  C CA  . SER C  1 270 ? 38.550  -20.714 -12.427 1.00 48.75  ? 270  SER A CA  1 
ATOM   6118  C C   . SER C  1 270 ? 39.346  -20.075 -13.556 1.00 55.38  ? 270  SER A C   1 
ATOM   6119  O O   . SER C  1 270 ? 38.805  -19.300 -14.342 1.00 57.56  ? 270  SER A O   1 
ATOM   6120  C CB  . SER C  1 270 ? 38.095  -22.115 -12.847 1.00 44.69  ? 270  SER A CB  1 
ATOM   6121  O OG  . SER C  1 270 ? 39.177  -22.854 -13.363 1.00 48.37  ? 270  SER A OG  1 
ATOM   6122  N N   . GLU C  1 271 ? 40.628  -20.410 -13.650 1.00 58.86  ? 271  GLU A N   1 
ATOM   6123  C CA  . GLU C  1 271 ? 41.468  -19.923 -14.751 1.00 54.86  ? 271  GLU A CA  1 
ATOM   6124  C C   . GLU C  1 271 ? 41.657  -20.933 -15.897 1.00 57.35  ? 271  GLU A C   1 
ATOM   6125  O O   . GLU C  1 271 ? 42.255  -20.601 -16.918 1.00 62.43  ? 271  GLU A O   1 
ATOM   6126  C CB  . GLU C  1 271 ? 42.846  -19.516 -14.232 1.00 52.75  ? 271  GLU A CB  1 
ATOM   6127  C CG  . GLU C  1 271 ? 42.792  -18.402 -13.234 1.00 62.48  ? 271  GLU A CG  1 
ATOM   6128  C CD  . GLU C  1 271 ? 42.189  -17.158 -13.845 1.00 66.38  ? 271  GLU A CD  1 
ATOM   6129  O OE1 . GLU C  1 271 ? 42.650  -16.767 -14.944 1.00 61.78  ? 271  GLU A OE1 1 
ATOM   6130  O OE2 . GLU C  1 271 ? 41.255  -16.585 -13.228 1.00 64.07  ? 271  GLU A OE2 1 
ATOM   6131  N N   . LEU C  1 272 ? 41.164  -22.157 -15.731 1.00 53.59  ? 272  LEU A N   1 
ATOM   6132  C CA  . LEU C  1 272 ? 41.394  -23.209 -16.718 1.00 54.94  ? 272  LEU A CA  1 
ATOM   6133  C C   . LEU C  1 272 ? 40.568  -23.043 -17.989 1.00 59.26  ? 272  LEU A C   1 
ATOM   6134  O O   . LEU C  1 272 ? 39.654  -22.232 -18.049 1.00 60.26  ? 272  LEU A O   1 
ATOM   6135  C CB  . LEU C  1 272 ? 41.100  -24.575 -16.097 1.00 51.72  ? 272  LEU A CB  1 
ATOM   6136  C CG  . LEU C  1 272 ? 41.763  -24.785 -14.732 1.00 54.81  ? 272  LEU A CG  1 
ATOM   6137  C CD1 . LEU C  1 272 ? 41.421  -26.174 -14.164 1.00 49.94  ? 272  LEU A CD1 1 
ATOM   6138  C CD2 . LEU C  1 272 ? 43.275  -24.527 -14.766 1.00 45.56  ? 272  LEU A CD2 1 
ATOM   6139  N N   . GLU C  1 273 ? 40.868  -23.868 -18.984 1.00 65.71  ? 273  GLU A N   1 
ATOM   6140  C CA  . GLU C  1 273 ? 40.134  -23.885 -20.244 1.00 63.62  ? 273  GLU A CA  1 
ATOM   6141  C C   . GLU C  1 273 ? 39.659  -25.303 -20.499 1.00 57.97  ? 273  GLU A C   1 
ATOM   6142  O O   . GLU C  1 273 ? 40.075  -26.223 -19.798 1.00 63.11  ? 273  GLU A O   1 
ATOM   6143  C CB  . GLU C  1 273 ? 41.015  -23.413 -21.401 1.00 65.42  ? 273  GLU A CB  1 
ATOM   6144  C CG  . GLU C  1 273 ? 41.455  -21.950 -21.344 1.00 70.79  ? 273  GLU A CG  1 
ATOM   6145  C CD  . GLU C  1 273 ? 40.312  -20.975 -21.607 1.00 75.76  ? 273  GLU A CD  1 
ATOM   6146  O OE1 . GLU C  1 273 ? 39.313  -21.377 -22.257 1.00 76.27  ? 273  GLU A OE1 1 
ATOM   6147  O OE2 . GLU C  1 273 ? 40.433  -19.795 -21.196 1.00 72.67  ? 273  GLU A OE2 1 
ATOM   6148  N N   . TYR C  1 274 ? 38.810  -25.487 -21.506 1.00 52.11  ? 274  TYR A N   1 
ATOM   6149  C CA  . TYR C  1 274 ? 38.223  -26.799 -21.797 1.00 55.81  ? 274  TYR A CA  1 
ATOM   6150  C C   . TYR C  1 274 ? 39.288  -27.897 -21.922 1.00 55.06  ? 274  TYR A C   1 
ATOM   6151  O O   . TYR C  1 274 ? 40.441  -27.611 -22.263 1.00 52.43  ? 274  TYR A O   1 
ATOM   6152  C CB  . TYR C  1 274 ? 37.410  -26.712 -23.076 1.00 52.68  ? 274  TYR A CB  1 
ATOM   6153  C CG  . TYR C  1 274 ? 36.451  -27.842 -23.350 1.00 53.30  ? 274  TYR A CG  1 
ATOM   6154  C CD1 . TYR C  1 274 ? 35.600  -28.319 -22.369 1.00 50.20  ? 274  TYR A CD1 1 
ATOM   6155  C CD2 . TYR C  1 274 ? 36.363  -28.393 -24.623 1.00 58.90  ? 274  TYR A CD2 1 
ATOM   6156  C CE1 . TYR C  1 274 ? 34.700  -29.335 -22.646 1.00 53.69  ? 274  TYR A CE1 1 
ATOM   6157  C CE2 . TYR C  1 274 ? 35.475  -29.402 -24.913 1.00 54.56  ? 274  TYR A CE2 1 
ATOM   6158  C CZ  . TYR C  1 274 ? 34.641  -29.871 -23.929 1.00 58.01  ? 274  TYR A CZ  1 
ATOM   6159  O OH  . TYR C  1 274 ? 33.750  -30.880 -24.242 1.00 55.78  ? 274  TYR A OH  1 
ATOM   6160  N N   . GLY C  1 275 ? 38.912  -29.138 -21.607 1.00 57.26  ? 275  GLY A N   1 
ATOM   6161  C CA  . GLY C  1 275 ? 39.861  -30.243 -21.615 1.00 56.84  ? 275  GLY A CA  1 
ATOM   6162  C C   . GLY C  1 275 ? 39.461  -31.475 -22.417 1.00 62.61  ? 275  GLY A C   1 
ATOM   6163  O O   . GLY C  1 275 ? 40.130  -32.501 -22.336 1.00 67.56  ? 275  GLY A O   1 
ATOM   6164  N N   . ASP C  1 276 ? 38.373  -31.379 -23.180 1.00 64.00  ? 276  ASP A N   1 
ATOM   6165  C CA  . ASP C  1 276 ? 37.873  -32.490 -23.995 1.00 65.84  ? 276  ASP A CA  1 
ATOM   6166  C C   . ASP C  1 276 ? 37.787  -33.787 -23.223 1.00 66.97  ? 276  ASP A C   1 
ATOM   6167  O O   . ASP C  1 276 ? 38.124  -34.847 -23.738 1.00 76.41  ? 276  ASP A O   1 
ATOM   6168  C CB  . ASP C  1 276 ? 38.728  -32.708 -25.237 1.00 70.27  ? 276  ASP A CB  1 
ATOM   6169  C CG  . ASP C  1 276 ? 38.542  -31.626 -26.257 1.00 72.99  ? 276  ASP A CG  1 
ATOM   6170  O OD1 . ASP C  1 276 ? 37.582  -31.737 -27.060 1.00 70.24  ? 276  ASP A OD1 1 
ATOM   6171  O OD2 . ASP C  1 276 ? 39.351  -30.676 -26.248 1.00 74.54  ? 276  ASP A OD2 1 
ATOM   6172  N N   . CYS C  1 277 ? 37.331  -33.698 -21.987 1.00 63.20  ? 277  CYS A N   1 
ATOM   6173  C CA  . CYS C  1 277 ? 37.197  -34.868 -21.146 1.00 60.35  ? 277  CYS A CA  1 
ATOM   6174  C C   . CYS C  1 277 ? 35.748  -34.945 -20.693 1.00 59.00  ? 277  CYS A C   1 
ATOM   6175  O O   . CYS C  1 277 ? 34.923  -34.122 -21.098 1.00 58.83  ? 277  CYS A O   1 
ATOM   6176  C CB  . CYS C  1 277 ? 38.156  -34.786 -19.955 1.00 63.65  ? 277  CYS A CB  1 
ATOM   6177  S SG  . CYS C  1 277 ? 38.039  -33.222 -19.001 1.00 71.86  ? 277  CYS A SG  1 
ATOM   6178  N N   . ASN C  1 278 ? 35.433  -35.934 -19.869 1.00 56.56  ? 278  ASN A N   1 
ATOM   6179  C CA  . ASN C  1 278 ? 34.089  -36.076 -19.350 1.00 49.95  ? 278  ASN A CA  1 
ATOM   6180  C C   . ASN C  1 278 ? 34.102  -36.594 -17.915 1.00 56.62  ? 278  ASN A C   1 
ATOM   6181  O O   . ASN C  1 278 ? 34.935  -37.442 -17.577 1.00 52.69  ? 278  ASN A O   1 
ATOM   6182  C CB  . ASN C  1 278 ? 33.288  -37.006 -20.249 1.00 48.81  ? 278  ASN A CB  1 
ATOM   6183  C CG  . ASN C  1 278 ? 31.820  -37.010 -19.913 1.00 57.39  ? 278  ASN A CG  1 
ATOM   6184  O OD1 . ASN C  1 278 ? 31.316  -36.065 -19.306 1.00 59.17  ? 278  ASN A OD1 1 
ATOM   6185  N ND2 . ASN C  1 278 ? 31.118  -38.077 -20.295 1.00 58.88  ? 278  ASN A ND2 1 
ATOM   6186  N N   . THR C  1 279 ? 33.166  -36.110 -17.092 1.00 52.08  ? 279  THR A N   1 
ATOM   6187  C CA  . THR C  1 279 ? 33.099  -36.482 -15.676 1.00 51.07  ? 279  THR A CA  1 
ATOM   6188  C C   . THR C  1 279 ? 31.663  -36.384 -15.136 1.00 55.34  ? 279  THR A C   1 
ATOM   6189  O O   . THR C  1 279 ? 30.759  -35.890 -15.814 1.00 58.08  ? 279  THR A O   1 
ATOM   6190  C CB  . THR C  1 279 ? 34.052  -35.580 -14.808 1.00 51.36  ? 279  THR A CB  1 
ATOM   6191  O OG1 . THR C  1 279 ? 34.138  -36.074 -13.464 1.00 53.90  ? 279  THR A OG1 1 
ATOM   6192  C CG2 . THR C  1 279 ? 33.578  -34.142 -14.773 1.00 50.10  ? 279  THR A CG2 1 
ATOM   6193  N N   . LYS C  1 280 ? 31.458  -36.862 -13.913 1.00 56.29  ? 280  LYS A N   1 
ATOM   6194  C CA  . LYS C  1 280 ? 30.170  -36.720 -13.231 1.00 58.69  ? 280  LYS A CA  1 
ATOM   6195  C C   . LYS C  1 280 ? 30.351  -35.957 -11.933 1.00 52.11  ? 280  LYS A C   1 
ATOM   6196  O O   . LYS C  1 280 ? 29.416  -35.823 -11.141 1.00 52.93  ? 280  LYS A O   1 
ATOM   6197  C CB  . LYS C  1 280 ? 29.503  -38.071 -12.968 1.00 62.32  ? 280  LYS A CB  1 
ATOM   6198  C CG  . LYS C  1 280 ? 28.813  -38.640 -14.184 1.00 70.14  ? 280  LYS A CG  1 
ATOM   6199  C CD  . LYS C  1 280 ? 27.890  -39.790 -13.804 1.00 76.18  ? 280  LYS A CD  1 
ATOM   6200  C CE  . LYS C  1 280 ? 28.500  -41.129 -14.159 1.00 78.61  ? 280  LYS A CE  1 
ATOM   6201  N NZ  . LYS C  1 280 ? 27.488  -42.212 -14.081 1.00 79.43  ? 280  LYS A NZ  1 
ATOM   6202  N N   . CYS C  1 281 ? 31.580  -35.491 -11.723 1.00 51.16  ? 281  CYS A N   1 
ATOM   6203  C CA  . CYS C  1 281 ? 31.922  -34.647 -10.584 1.00 51.11  ? 281  CYS A CA  1 
ATOM   6204  C C   . CYS C  1 281 ? 33.046  -33.662 -10.933 1.00 49.52  ? 281  CYS A C   1 
ATOM   6205  O O   . CYS C  1 281 ? 34.196  -34.052 -11.164 1.00 45.06  ? 281  CYS A O   1 
ATOM   6206  C CB  . CYS C  1 281 ? 32.332  -35.502 -9.393  1.00 48.84  ? 281  CYS A CB  1 
ATOM   6207  S SG  . CYS C  1 281 ? 32.713  -34.509 -7.966  1.00 64.46  ? 281  CYS A SG  1 
ATOM   6208  N N   . GLN C  1 282 ? 32.711  -32.376 -10.893 1.00 50.17  ? 282  GLN A N   1 
ATOM   6209  C CA  . GLN C  1 282 ? 33.602  -31.318 -11.337 1.00 42.28  ? 282  GLN A CA  1 
ATOM   6210  C C   . GLN C  1 282 ? 33.883  -30.288 -10.248 1.00 43.05  ? 282  GLN A C   1 
ATOM   6211  O O   . GLN C  1 282 ? 32.965  -29.883 -9.545  1.00 47.50  ? 282  GLN A O   1 
ATOM   6212  C CB  . GLN C  1 282 ? 32.993  -30.640 -12.558 1.00 43.57  ? 282  GLN A CB  1 
ATOM   6213  C CG  . GLN C  1 282 ? 33.866  -29.553 -13.163 1.00 43.19  ? 282  GLN A CG  1 
ATOM   6214  C CD  . GLN C  1 282 ? 35.158  -30.105 -13.729 1.00 42.90  ? 282  GLN A CD  1 
ATOM   6215  O OE1 . GLN C  1 282 ? 35.162  -30.890 -14.690 1.00 41.91  ? 282  GLN A OE1 1 
ATOM   6216  N NE2 . GLN C  1 282 ? 36.269  -29.688 -13.138 1.00 38.45  ? 282  GLN A NE2 1 
ATOM   6217  N N   . THR C  1 283 ? 35.149  -29.878 -10.115 1.00 40.56  ? 283  THR A N   1 
ATOM   6218  C CA  . THR C  1 283 ? 35.559  -28.836 -9.171  1.00 41.06  ? 283  THR A CA  1 
ATOM   6219  C C   . THR C  1 283 ? 36.300  -27.736 -9.941  1.00 44.64  ? 283  THR A C   1 
ATOM   6220  O O   . THR C  1 283 ? 36.743  -27.968 -11.068 1.00 42.15  ? 283  THR A O   1 
ATOM   6221  C CB  . THR C  1 283 ? 36.480  -29.389 -8.058  1.00 45.41  ? 283  THR A CB  1 
ATOM   6222  O OG1 . THR C  1 283 ? 37.863  -29.261 -8.442  1.00 45.14  ? 283  THR A OG1 1 
ATOM   6223  C CG2 . THR C  1 283 ? 36.114  -30.836 -7.709  1.00 39.56  ? 283  THR A CG2 1 
ATOM   6224  N N   . PRO C  1 284 ? 36.449  -26.540 -9.339  1.00 46.62  ? 284  PRO A N   1 
ATOM   6225  C CA  . PRO C  1 284 ? 37.089  -25.463 -10.111 1.00 47.34  ? 284  PRO A CA  1 
ATOM   6226  C C   . PRO C  1 284 ? 38.537  -25.738 -10.571 1.00 48.58  ? 284  PRO A C   1 
ATOM   6227  O O   . PRO C  1 284 ? 39.017  -25.028 -11.464 1.00 43.70  ? 284  PRO A O   1 
ATOM   6228  C CB  . PRO C  1 284 ? 37.050  -24.265 -9.135  1.00 47.24  ? 284  PRO A CB  1 
ATOM   6229  C CG  . PRO C  1 284 ? 35.891  -24.558 -8.220  1.00 46.52  ? 284  PRO A CG  1 
ATOM   6230  C CD  . PRO C  1 284 ? 35.892  -26.048 -8.057  1.00 43.28  ? 284  PRO A CD  1 
ATOM   6231  N N   . ILE C  1 285 ? 39.217  -26.741 -10.001 1.00 47.43  ? 285  ILE A N   1 
ATOM   6232  C CA  . ILE C  1 285 ? 40.625  -26.959 -10.345 1.00 38.91  ? 285  ILE A CA  1 
ATOM   6233  C C   . ILE C  1 285 ? 40.898  -28.317 -11.005 1.00 41.95  ? 285  ILE A C   1 
ATOM   6234  O O   . ILE C  1 285 ? 42.060  -28.655 -11.295 1.00 38.77  ? 285  ILE A O   1 
ATOM   6235  C CB  . ILE C  1 285 ? 41.534  -26.817 -9.094  1.00 41.37  ? 285  ILE A CB  1 
ATOM   6236  C CG1 . ILE C  1 285 ? 41.358  -28.009 -8.139  1.00 46.57  ? 285  ILE A CG1 1 
ATOM   6237  C CG2 . ILE C  1 285 ? 41.276  -25.478 -8.377  1.00 36.23  ? 285  ILE A CG2 1 
ATOM   6238  C CD1 . ILE C  1 285 ? 42.253  -27.933 -6.894  1.00 41.77  ? 285  ILE A CD1 1 
ATOM   6239  N N   . GLY C  1 286 ? 39.835  -29.082 -11.262 1.00 40.97  ? 286  GLY A N   1 
ATOM   6240  C CA  . GLY C  1 286 ? 39.976  -30.408 -11.847 1.00 41.65  ? 286  GLY A CA  1 
ATOM   6241  C C   . GLY C  1 286 ? 38.812  -31.330 -11.533 1.00 39.66  ? 286  GLY A C   1 
ATOM   6242  O O   . GLY C  1 286 ? 38.073  -31.090 -10.585 1.00 38.26  ? 286  GLY A O   1 
ATOM   6243  N N   . ALA C  1 287 ? 38.661  -32.395 -12.318 1.00 40.53  ? 287  ALA A N   1 
ATOM   6244  C CA  . ALA C  1 287 ? 37.521  -33.297 -12.188 1.00 45.22  ? 287  ALA A CA  1 
ATOM   6245  C C   . ALA C  1 287 ? 37.878  -34.507 -11.315 1.00 51.70  ? 287  ALA A C   1 
ATOM   6246  O O   . ALA C  1 287 ? 39.059  -34.732 -11.009 1.00 48.00  ? 287  ALA A O   1 
ATOM   6247  C CB  . ALA C  1 287 ? 37.038  -33.747 -13.558 1.00 38.97  ? 287  ALA A CB  1 
ATOM   6248  N N   . ILE C  1 288 ? 36.851  -35.246 -10.879 1.00 53.34  ? 288  ILE A N   1 
ATOM   6249  C CA  . ILE C  1 288 ? 37.023  -36.378 -9.953  1.00 52.66  ? 288  ILE A CA  1 
ATOM   6250  C C   . ILE C  1 288 ? 36.395  -37.661 -10.504 1.00 57.76  ? 288  ILE A C   1 
ATOM   6251  O O   . ILE C  1 288 ? 35.207  -37.707 -10.844 1.00 53.50  ? 288  ILE A O   1 
ATOM   6252  C CB  . ILE C  1 288 ? 36.401  -36.100 -8.556  1.00 52.27  ? 288  ILE A CB  1 
ATOM   6253  C CG1 . ILE C  1 288 ? 37.186  -35.030 -7.788  1.00 53.17  ? 288  ILE A CG1 1 
ATOM   6254  C CG2 . ILE C  1 288 ? 36.326  -37.377 -7.727  1.00 55.07  ? 288  ILE A CG2 1 
ATOM   6255  C CD1 . ILE C  1 288 ? 36.490  -34.570 -6.486  1.00 44.35  ? 288  ILE A CD1 1 
ATOM   6256  N N   . ASN C  1 289 ? 37.219  -38.699 -10.597 1.00 62.10  ? 289  ASN A N   1 
ATOM   6257  C CA  . ASN C  1 289 ? 36.754  -40.030 -10.936 1.00 62.71  ? 289  ASN A CA  1 
ATOM   6258  C C   . ASN C  1 289 ? 37.226  -40.938 -9.813  1.00 65.92  ? 289  ASN A C   1 
ATOM   6259  O O   . ASN C  1 289 ? 38.374  -41.406 -9.803  1.00 62.81  ? 289  ASN A O   1 
ATOM   6260  C CB  . ASN C  1 289 ? 37.289  -40.491 -12.288 1.00 57.22  ? 289  ASN A CB  1 
ATOM   6261  C CG  . ASN C  1 289 ? 36.636  -41.779 -12.758 1.00 74.28  ? 289  ASN A CG  1 
ATOM   6262  O OD1 . ASN C  1 289 ? 35.551  -42.141 -12.285 1.00 78.47  ? 289  ASN A OD1 1 
ATOM   6263  N ND2 . ASN C  1 289 ? 37.296  -42.489 -13.682 1.00 71.16  ? 289  ASN A ND2 1 
ATOM   6264  N N   . SER C  1 290 ? 36.339  -41.163 -8.852  1.00 62.92  ? 290  SER A N   1 
ATOM   6265  C CA  . SER C  1 290 ? 36.722  -41.823 -7.619  1.00 60.34  ? 290  SER A CA  1 
ATOM   6266  C C   . SER C  1 290 ? 35.525  -42.579 -7.065  1.00 58.70  ? 290  SER A C   1 
ATOM   6267  O O   . SER C  1 290 ? 34.383  -42.350 -7.470  1.00 53.17  ? 290  SER A O   1 
ATOM   6268  C CB  . SER C  1 290 ? 37.245  -40.782 -6.616  1.00 61.29  ? 290  SER A CB  1 
ATOM   6269  O OG  . SER C  1 290 ? 37.726  -41.346 -5.414  1.00 53.79  ? 290  SER A OG  1 
ATOM   6270  N N   . SER C  1 291 ? 35.787  -43.479 -6.128  1.00 66.46  ? 291  SER A N   1 
ATOM   6271  C CA  . SER C  1 291 ? 34.716  -44.241 -5.506  1.00 67.15  ? 291  SER A CA  1 
ATOM   6272  C C   . SER C  1 291 ? 34.789  -44.096 -4.002  1.00 66.97  ? 291  SER A C   1 
ATOM   6273  O O   . SER C  1 291 ? 33.928  -44.595 -3.277  1.00 68.53  ? 291  SER A O   1 
ATOM   6274  C CB  . SER C  1 291 ? 34.795  -45.711 -5.911  1.00 68.53  ? 291  SER A CB  1 
ATOM   6275  O OG  . SER C  1 291 ? 33.522  -46.178 -6.313  1.00 75.75  ? 291  SER A OG  1 
ATOM   6276  N N   . MET C  1 292 ? 35.813  -43.382 -3.545  1.00 62.50  ? 292  MET A N   1 
ATOM   6277  C CA  . MET C  1 292 ? 35.966  -43.106 -2.133  1.00 63.54  ? 292  MET A CA  1 
ATOM   6278  C C   . MET C  1 292 ? 34.767  -42.322 -1.621  1.00 69.14  ? 292  MET A C   1 
ATOM   6279  O O   . MET C  1 292 ? 34.149  -41.552 -2.372  1.00 65.63  ? 292  MET A O   1 
ATOM   6280  C CB  . MET C  1 292 ? 37.269  -42.346 -1.878  1.00 64.37  ? 292  MET A CB  1 
ATOM   6281  C CG  . MET C  1 292 ? 38.506  -42.968 -2.497  1.00 63.42  ? 292  MET A CG  1 
ATOM   6282  S SD  . MET C  1 292 ? 39.295  -44.124 -1.343  1.00 68.02  ? 292  MET A SD  1 
ATOM   6283  C CE  . MET C  1 292 ? 38.096  -45.464 -1.248  1.00 64.19  ? 292  MET A CE  1 
ATOM   6284  N N   . PRO C  1 293 ? 34.410  -42.538 -0.342  1.00 69.63  ? 293  PRO A N   1 
ATOM   6285  C CA  . PRO C  1 293 ? 33.269  -41.821 0.239   1.00 66.23  ? 293  PRO A CA  1 
ATOM   6286  C C   . PRO C  1 293 ? 33.642  -40.384 0.591   1.00 58.91  ? 293  PRO A C   1 
ATOM   6287  O O   . PRO C  1 293 ? 32.760  -39.586 0.886   1.00 60.19  ? 293  PRO A O   1 
ATOM   6288  C CB  . PRO C  1 293 ? 32.931  -42.649 1.487   1.00 67.18  ? 293  PRO A CB  1 
ATOM   6289  C CG  . PRO C  1 293 ? 34.241  -43.276 1.881   1.00 66.31  ? 293  PRO A CG  1 
ATOM   6290  C CD  . PRO C  1 293 ? 34.951  -43.561 0.575   1.00 67.01  ? 293  PRO A CD  1 
ATOM   6291  N N   . PHE C  1 294 ? 34.932  -40.071 0.558   1.00 56.39  ? 294  PHE A N   1 
ATOM   6292  C CA  . PHE C  1 294 ? 35.399  -38.713 0.817   1.00 62.96  ? 294  PHE A CA  1 
ATOM   6293  C C   . PHE C  1 294 ? 36.393  -38.254 -0.264  1.00 60.97  ? 294  PHE A C   1 
ATOM   6294  O O   . PHE C  1 294 ? 36.921  -39.075 -1.024  1.00 59.93  ? 294  PHE A O   1 
ATOM   6295  C CB  . PHE C  1 294 ? 36.050  -38.593 2.197   1.00 58.24  ? 294  PHE A CB  1 
ATOM   6296  C CG  . PHE C  1 294 ? 35.104  -38.805 3.337   1.00 61.36  ? 294  PHE A CG  1 
ATOM   6297  C CD1 . PHE C  1 294 ? 34.141  -37.857 3.640   1.00 65.95  ? 294  PHE A CD1 1 
ATOM   6298  C CD2 . PHE C  1 294 ? 35.208  -39.927 4.145   1.00 65.06  ? 294  PHE A CD2 1 
ATOM   6299  C CE1 . PHE C  1 294 ? 33.261  -38.045 4.709   1.00 66.89  ? 294  PHE A CE1 1 
ATOM   6300  C CE2 . PHE C  1 294 ? 34.340  -40.119 5.216   1.00 64.85  ? 294  PHE A CE2 1 
ATOM   6301  C CZ  . PHE C  1 294 ? 33.364  -39.175 5.495   1.00 64.39  ? 294  PHE A CZ  1 
ATOM   6302  N N   . HIS C  1 295 ? 36.589  -36.938 -0.355  1.00 52.69  ? 295  HIS A N   1 
ATOM   6303  C CA  . HIS C  1 295 ? 37.653  -36.339 -1.165  1.00 53.57  ? 295  HIS A CA  1 
ATOM   6304  C C   . HIS C  1 295 ? 38.119  -35.082 -0.456  1.00 49.92  ? 295  HIS A C   1 
ATOM   6305  O O   . HIS C  1 295 ? 37.456  -34.613 0.466   1.00 51.49  ? 295  HIS A O   1 
ATOM   6306  C CB  . HIS C  1 295 ? 37.188  -36.017 -2.590  1.00 51.93  ? 295  HIS A CB  1 
ATOM   6307  C CG  . HIS C  1 295 ? 36.338  -34.790 -2.675  1.00 56.58  ? 295  HIS A CG  1 
ATOM   6308  N ND1 . HIS C  1 295 ? 36.867  -33.514 -2.715  1.00 54.17  ? 295  HIS A ND1 1 
ATOM   6309  C CD2 . HIS C  1 295 ? 34.990  -34.644 -2.724  1.00 56.26  ? 295  HIS A CD2 1 
ATOM   6310  C CE1 . HIS C  1 295 ? 35.879  -32.637 -2.774  1.00 52.96  ? 295  HIS A CE1 1 
ATOM   6311  N NE2 . HIS C  1 295 ? 34.732  -33.296 -2.780  1.00 55.25  ? 295  HIS A NE2 1 
ATOM   6312  N N   . ASN C  1 296 ? 39.253  -34.533 -0.874  1.00 47.13  ? 296  ASN A N   1 
ATOM   6313  C CA  . ASN C  1 296 ? 39.781  -33.338 -0.220  1.00 47.72  ? 296  ASN A CA  1 
ATOM   6314  C C   . ASN C  1 296 ? 40.354  -32.312 -1.219  1.00 45.26  ? 296  ASN A C   1 
ATOM   6315  O O   . ASN C  1 296 ? 41.282  -31.569 -0.892  1.00 41.64  ? 296  ASN A O   1 
ATOM   6316  C CB  . ASN C  1 296 ? 40.829  -33.720 0.842   1.00 43.38  ? 296  ASN A CB  1 
ATOM   6317  C CG  . ASN C  1 296 ? 42.169  -34.143 0.241   1.00 47.99  ? 296  ASN A CG  1 
ATOM   6318  O OD1 . ASN C  1 296 ? 42.238  -34.578 -0.909  1.00 50.37  ? 296  ASN A OD1 1 
ATOM   6319  N ND2 . ASN C  1 296 ? 43.244  -34.000 1.019   1.00 42.61  ? 296  ASN A ND2 1 
ATOM   6320  N N   . ILE C  1 297 ? 39.790  -32.280 -2.430  1.00 45.97  ? 297  ILE A N   1 
ATOM   6321  C CA  . ILE C  1 297 ? 40.290  -31.415 -3.504  1.00 45.62  ? 297  ILE A CA  1 
ATOM   6322  C C   . ILE C  1 297 ? 39.818  -29.952 -3.406  1.00 51.55  ? 297  ILE A C   1 
ATOM   6323  O O   . ILE C  1 297 ? 40.630  -29.008 -3.408  1.00 49.69  ? 297  ILE A O   1 
ATOM   6324  C CB  . ILE C  1 297 ? 39.844  -31.903 -4.896  1.00 42.17  ? 297  ILE A CB  1 
ATOM   6325  C CG1 . ILE C  1 297 ? 40.504  -33.225 -5.287  1.00 50.88  ? 297  ILE A CG1 1 
ATOM   6326  C CG2 . ILE C  1 297 ? 40.143  -30.837 -5.935  1.00 44.07  ? 297  ILE A CG2 1 
ATOM   6327  C CD1 . ILE C  1 297 ? 39.688  -34.426 -4.986  1.00 45.76  ? 297  ILE A CD1 1 
ATOM   6328  N N   . HIS C  1 298 ? 38.498  -29.784 -3.278  1.00 50.49  ? 298  HIS A N   1 
ATOM   6329  C CA  . HIS C  1 298 ? 37.860  -28.470 -3.291  1.00 44.56  ? 298  HIS A CA  1 
ATOM   6330  C C   . HIS C  1 298 ? 36.461  -28.627 -2.705  1.00 40.00  ? 298  HIS A C   1 
ATOM   6331  O O   . HIS C  1 298 ? 35.837  -29.671 -2.914  1.00 38.56  ? 298  HIS A O   1 
ATOM   6332  C CB  . HIS C  1 298 ? 37.777  -27.912 -4.731  1.00 43.33  ? 298  HIS A CB  1 
ATOM   6333  C CG  . HIS C  1 298 ? 37.700  -26.419 -4.789  1.00 42.72  ? 298  HIS A CG  1 
ATOM   6334  N ND1 . HIS C  1 298 ? 36.590  -25.705 -4.379  1.00 44.34  ? 298  HIS A ND1 1 
ATOM   6335  C CD2 . HIS C  1 298 ? 38.613  -25.502 -5.190  1.00 37.89  ? 298  HIS A CD2 1 
ATOM   6336  C CE1 . HIS C  1 298 ? 36.829  -24.412 -4.516  1.00 41.98  ? 298  HIS A CE1 1 
ATOM   6337  N NE2 . HIS C  1 298 ? 38.047  -24.263 -5.009  1.00 43.27  ? 298  HIS A NE2 1 
ATOM   6338  N N   . PRO C  1 299 ? 35.978  -27.615 -1.955  1.00 39.11  ? 299  PRO A N   1 
ATOM   6339  C CA  . PRO C  1 299 ? 34.645  -27.615 -1.329  1.00 37.14  ? 299  PRO A CA  1 
ATOM   6340  C C   . PRO C  1 299 ? 33.492  -27.327 -2.271  1.00 39.75  ? 299  PRO A C   1 
ATOM   6341  O O   . PRO C  1 299 ? 32.361  -27.710 -1.958  1.00 37.94  ? 299  PRO A O   1 
ATOM   6342  C CB  . PRO C  1 299 ? 34.735  -26.487 -0.302  1.00 39.32  ? 299  PRO A CB  1 
ATOM   6343  C CG  . PRO C  1 299 ? 35.800  -25.602 -0.788  1.00 42.71  ? 299  PRO A CG  1 
ATOM   6344  C CD  . PRO C  1 299 ? 36.816  -26.525 -1.429  1.00 45.17  ? 299  PRO A CD  1 
ATOM   6345  N N   . LEU C  1 300 ? 33.763  -26.669 -3.398  1.00 42.27  ? 300  LEU A N   1 
ATOM   6346  C CA  . LEU C  1 300 ? 32.710  -26.375 -4.389  1.00 39.84  ? 300  LEU A CA  1 
ATOM   6347  C C   . LEU C  1 300 ? 32.703  -27.342 -5.576  1.00 40.93  ? 300  LEU A C   1 
ATOM   6348  O O   . LEU C  1 300 ? 33.502  -27.203 -6.501  1.00 41.25  ? 300  LEU A O   1 
ATOM   6349  C CB  . LEU C  1 300 ? 32.824  -24.953 -4.911  1.00 31.91  ? 300  LEU A CB  1 
ATOM   6350  C CG  . LEU C  1 300 ? 32.664  -23.842 -3.894  1.00 36.93  ? 300  LEU A CG  1 
ATOM   6351  C CD1 . LEU C  1 300 ? 32.762  -22.489 -4.581  1.00 32.98  ? 300  LEU A CD1 1 
ATOM   6352  C CD2 . LEU C  1 300 ? 31.335  -24.011 -3.187  1.00 43.26  ? 300  LEU A CD2 1 
ATOM   6353  N N   . THR C  1 301 ? 31.811  -28.326 -5.544  1.00 40.99  ? 301  THR A N   1 
ATOM   6354  C CA  . THR C  1 301 ? 31.736  -29.324 -6.607  1.00 39.38  ? 301  THR A CA  1 
ATOM   6355  C C   . THR C  1 301 ? 30.354  -29.244 -7.259  1.00 36.32  ? 301  THR A C   1 
ATOM   6356  O O   . THR C  1 301 ? 29.482  -28.570 -6.730  1.00 37.52  ? 301  THR A O   1 
ATOM   6357  C CB  . THR C  1 301 ? 31.996  -30.765 -6.054  1.00 46.40  ? 301  THR A CB  1 
ATOM   6358  O OG1 . THR C  1 301 ? 30.845  -31.248 -5.343  1.00 37.08  ? 301  THR A OG1 1 
ATOM   6359  C CG2 . THR C  1 301 ? 33.235  -30.791 -5.134  1.00 41.84  ? 301  THR A CG2 1 
ATOM   6360  N N   . ILE C  1 302 ? 30.156  -29.877 -8.414  1.00 34.24  ? 302  ILE A N   1 
ATOM   6361  C CA  . ILE C  1 302 ? 28.803  -30.040 -8.956  1.00 38.91  ? 302  ILE A CA  1 
ATOM   6362  C C   . ILE C  1 302 ? 28.683  -31.429 -9.604  1.00 47.36  ? 302  ILE A C   1 
ATOM   6363  O O   . ILE C  1 302 ? 29.640  -31.945 -10.210 1.00 45.32  ? 302  ILE A O   1 
ATOM   6364  C CB  . ILE C  1 302 ? 28.392  -28.931 -9.988  1.00 41.81  ? 302  ILE A CB  1 
ATOM   6365  C CG1 . ILE C  1 302 ? 26.886  -29.067 -10.297 1.00 43.15  ? 302  ILE A CG1 1 
ATOM   6366  C CG2 . ILE C  1 302 ? 29.242  -28.999 -11.275 1.00 36.46  ? 302  ILE A CG2 1 
ATOM   6367  C CD1 . ILE C  1 302 ? 26.296  -28.072 -11.280 1.00 39.12  ? 302  ILE A CD1 1 
ATOM   6368  N N   . GLY C  1 303 ? 27.512  -32.043 -9.457  1.00 45.44  ? 303  GLY A N   1 
ATOM   6369  C CA  . GLY C  1 303 ? 27.314  -33.390 -9.955  1.00 49.39  ? 303  GLY A CA  1 
ATOM   6370  C C   . GLY C  1 303 ? 27.226  -34.384 -8.808  1.00 58.13  ? 303  GLY A C   1 
ATOM   6371  O O   . GLY C  1 303 ? 26.950  -34.003 -7.665  1.00 51.55  ? 303  GLY A O   1 
ATOM   6372  N N   . GLU C  1 304 ? 27.475  -35.658 -9.115  1.00 62.11  ? 304  GLU A N   1 
ATOM   6373  C CA  . GLU C  1 304 ? 27.390  -36.736 -8.129  1.00 64.64  ? 304  GLU A CA  1 
ATOM   6374  C C   . GLU C  1 304 ? 28.752  -36.991 -7.453  1.00 64.07  ? 304  GLU A C   1 
ATOM   6375  O O   . GLU C  1 304 ? 29.599  -37.684 -8.011  1.00 65.20  ? 304  GLU A O   1 
ATOM   6376  C CB  . GLU C  1 304 ? 26.861  -37.998 -8.804  1.00 60.87  ? 304  GLU A CB  1 
ATOM   6377  C CG  . GLU C  1 304 ? 26.470  -39.104 -7.836  1.00 83.79  ? 304  GLU A CG  1 
ATOM   6378  C CD  . GLU C  1 304 ? 25.863  -40.319 -8.531  1.00 93.27  ? 304  GLU A CD  1 
ATOM   6379  O OE1 . GLU C  1 304 ? 25.785  -40.322 -9.784  1.00 92.34  ? 304  GLU A OE1 1 
ATOM   6380  O OE2 . GLU C  1 304 ? 25.433  -41.251 -7.811  1.00 97.15  ? 304  GLU A OE2 1 
ATOM   6381  N N   . CYS C  1 305 ? 28.964  -36.409 -6.271  1.00 59.01  ? 305  CYS A N   1 
ATOM   6382  C CA  . CYS C  1 305 ? 30.299  -36.343 -5.672  1.00 58.62  ? 305  CYS A CA  1 
ATOM   6383  C C   . CYS C  1 305 ? 30.445  -36.966 -4.296  1.00 64.13  ? 305  CYS A C   1 
ATOM   6384  O O   . CYS C  1 305 ? 29.467  -37.081 -3.554  1.00 68.18  ? 305  CYS A O   1 
ATOM   6385  C CB  . CYS C  1 305 ? 30.757  -34.878 -5.563  1.00 61.59  ? 305  CYS A CB  1 
ATOM   6386  S SG  . CYS C  1 305 ? 30.916  -33.957 -7.132  1.00 70.62  ? 305  CYS A SG  1 
ATOM   6387  N N   . PRO C  1 306 ? 31.693  -37.324 -3.932  1.00 62.91  ? 306  PRO A N   1 
ATOM   6388  C CA  . PRO C  1 306 ? 32.029  -37.667 -2.552  1.00 59.38  ? 306  PRO A CA  1 
ATOM   6389  C C   . PRO C  1 306 ? 31.820  -36.469 -1.647  1.00 60.11  ? 306  PRO A C   1 
ATOM   6390  O O   . PRO C  1 306 ? 31.614  -35.369 -2.140  1.00 67.34  ? 306  PRO A O   1 
ATOM   6391  C CB  . PRO C  1 306 ? 33.514  -38.039 -2.630  1.00 55.65  ? 306  PRO A CB  1 
ATOM   6392  C CG  . PRO C  1 306 ? 33.720  -38.451 -4.015  1.00 53.77  ? 306  PRO A CG  1 
ATOM   6393  C CD  . PRO C  1 306 ? 32.825  -37.586 -4.837  1.00 62.65  ? 306  PRO A CD  1 
ATOM   6394  N N   . LYS C  1 307 ? 31.895  -36.663 -0.341  1.00 57.24  ? 307  LYS A N   1 
ATOM   6395  C CA  . LYS C  1 307 ? 31.723  -35.549 0.567   1.00 56.98  ? 307  LYS A CA  1 
ATOM   6396  C C   . LYS C  1 307 ? 33.084  -34.943 0.847   1.00 55.24  ? 307  LYS A C   1 
ATOM   6397  O O   . LYS C  1 307 ? 34.068  -35.661 0.950   1.00 57.02  ? 307  LYS A O   1 
ATOM   6398  C CB  . LYS C  1 307 ? 31.021  -35.992 1.860   1.00 67.05  ? 307  LYS A CB  1 
ATOM   6399  C CG  . LYS C  1 307 ? 29.572  -36.497 1.671   1.00 71.07  ? 307  LYS A CG  1 
ATOM   6400  C CD  . LYS C  1 307 ? 28.697  -35.468 0.933   1.00 75.58  ? 307  LYS A CD  1 
ATOM   6401  C CE  . LYS C  1 307 ? 27.347  -36.045 0.550   1.00 71.87  ? 307  LYS A CE  1 
ATOM   6402  N NZ  . LYS C  1 307 ? 27.502  -37.146 -0.429  1.00 73.19  ? 307  LYS A NZ  1 
ATOM   6403  N N   . TYR C  1 308 ? 33.134  -33.619 0.956   1.00 53.78  ? 308  TYR A N   1 
ATOM   6404  C CA  . TYR C  1 308 ? 34.386  -32.903 1.126   1.00 48.83  ? 308  TYR A CA  1 
ATOM   6405  C C   . TYR C  1 308 ? 34.818  -32.787 2.582   1.00 50.52  ? 308  TYR A C   1 
ATOM   6406  O O   . TYR C  1 308 ? 34.023  -32.457 3.463   1.00 49.95  ? 308  TYR A O   1 
ATOM   6407  C CB  . TYR C  1 308 ? 34.279  -31.508 0.508   1.00 47.08  ? 308  TYR A CB  1 
ATOM   6408  C CG  . TYR C  1 308 ? 35.467  -30.639 0.834   1.00 46.19  ? 308  TYR A CG  1 
ATOM   6409  C CD1 . TYR C  1 308 ? 36.703  -30.828 0.196   1.00 44.85  ? 308  TYR A CD1 1 
ATOM   6410  C CD2 . TYR C  1 308 ? 35.356  -29.619 1.769   1.00 44.74  ? 308  TYR A CD2 1 
ATOM   6411  C CE1 . TYR C  1 308 ? 37.801  -30.025 0.504   1.00 39.97  ? 308  TYR A CE1 1 
ATOM   6412  C CE2 . TYR C  1 308 ? 36.440  -28.807 2.076   1.00 46.39  ? 308  TYR A CE2 1 
ATOM   6413  C CZ  . TYR C  1 308 ? 37.658  -29.019 1.443   1.00 41.97  ? 308  TYR A CZ  1 
ATOM   6414  O OH  . TYR C  1 308 ? 38.724  -28.217 1.765   1.00 44.18  ? 308  TYR A OH  1 
ATOM   6415  N N   . VAL C  1 309 ? 36.106  -33.036 2.811   1.00 48.36  ? 309  VAL A N   1 
ATOM   6416  C CA  . VAL C  1 309 ? 36.722  -32.920 4.126   1.00 45.97  ? 309  VAL A CA  1 
ATOM   6417  C C   . VAL C  1 309 ? 38.101  -32.278 3.950   1.00 46.72  ? 309  VAL A C   1 
ATOM   6418  O O   . VAL C  1 309 ? 38.659  -32.340 2.856   1.00 43.71  ? 309  VAL A O   1 
ATOM   6419  C CB  . VAL C  1 309 ? 36.851  -34.308 4.802   1.00 47.15  ? 309  VAL A CB  1 
ATOM   6420  C CG1 . VAL C  1 309 ? 37.411  -34.187 6.206   1.00 54.25  ? 309  VAL A CG1 1 
ATOM   6421  C CG2 . VAL C  1 309 ? 35.519  -34.998 4.854   1.00 48.27  ? 309  VAL A CG2 1 
ATOM   6422  N N   . LYS C  1 310 ? 38.639  -31.665 5.009   1.00 47.62  ? 310  LYS A N   1 
ATOM   6423  C CA  . LYS C  1 310 ? 39.978  -31.062 4.979   1.00 48.50  ? 310  LYS A CA  1 
ATOM   6424  C C   . LYS C  1 310 ? 41.138  -31.956 5.477   1.00 54.74  ? 310  LYS A C   1 
ATOM   6425  O O   . LYS C  1 310 ? 42.140  -31.432 5.989   1.00 60.29  ? 310  LYS A O   1 
ATOM   6426  C CB  . LYS C  1 310 ? 40.013  -29.796 5.823   1.00 47.16  ? 310  LYS A CB  1 
ATOM   6427  C CG  . LYS C  1 310 ? 39.312  -28.611 5.295   1.00 45.15  ? 310  LYS A CG  1 
ATOM   6428  C CD  . LYS C  1 310 ? 39.773  -27.438 6.126   1.00 46.55  ? 310  LYS A CD  1 
ATOM   6429  C CE  . LYS C  1 310 ? 38.756  -26.337 6.179   1.00 53.91  ? 310  LYS A CE  1 
ATOM   6430  N NZ  . LYS C  1 310 ? 39.135  -25.420 7.289   1.00 60.20  ? 310  LYS A NZ  1 
ATOM   6431  N N   . SER C  1 311 ? 41.008  -33.277 5.380   1.00 57.33  ? 311  SER A N   1 
ATOM   6432  C CA  . SER C  1 311 ? 42.044  -34.173 5.911   1.00 61.00  ? 311  SER A CA  1 
ATOM   6433  C C   . SER C  1 311 ? 43.169  -34.438 4.903   1.00 61.36  ? 311  SER A C   1 
ATOM   6434  O O   . SER C  1 311 ? 42.923  -34.500 3.694   1.00 60.99  ? 311  SER A O   1 
ATOM   6435  C CB  . SER C  1 311 ? 41.424  -35.511 6.329   1.00 59.50  ? 311  SER A CB  1 
ATOM   6436  O OG  . SER C  1 311 ? 40.344  -35.325 7.221   1.00 59.20  ? 311  SER A OG  1 
ATOM   6437  N N   . ASN C  1 312 ? 44.388  -34.650 5.399   1.00 60.19  ? 312  ASN A N   1 
ATOM   6438  C CA  . ASN C  1 312 ? 45.477  -35.046 4.513   1.00 59.94  ? 312  ASN A CA  1 
ATOM   6439  C C   . ASN C  1 312 ? 45.459  -36.552 4.282   1.00 62.00  ? 312  ASN A C   1 
ATOM   6440  O O   . ASN C  1 312 ? 45.831  -37.022 3.206   1.00 58.96  ? 312  ASN A O   1 
ATOM   6441  C CB  . ASN C  1 312 ? 46.835  -34.631 5.084   1.00 64.96  ? 312  ASN A CB  1 
ATOM   6442  C CG  . ASN C  1 312 ? 47.002  -33.124 5.185   1.00 74.95  ? 312  ASN A CG  1 
ATOM   6443  O OD1 . ASN C  1 312 ? 46.412  -32.363 4.410   1.00 73.95  ? 312  ASN A OD1 1 
ATOM   6444  N ND2 . ASN C  1 312 ? 47.809  -32.682 6.150   1.00 73.61  ? 312  ASN A ND2 1 
ATOM   6445  N N   . ARG C  1 313 ? 44.967  -37.289 5.277   1.00 63.43  ? 313  ARG A N   1 
ATOM   6446  C CA  . ARG C  1 313 ? 44.910  -38.747 5.227   1.00 63.49  ? 313  ARG A CA  1 
ATOM   6447  C C   . ARG C  1 313 ? 43.723  -39.284 6.019   1.00 59.95  ? 313  ARG A C   1 
ATOM   6448  O O   . ARG C  1 313 ? 43.435  -38.812 7.123   1.00 56.41  ? 313  ARG A O   1 
ATOM   6449  C CB  . ARG C  1 313 ? 46.214  -39.349 5.774   1.00 73.27  ? 313  ARG A CB  1 
ATOM   6450  C CG  . ARG C  1 313 ? 46.462  -40.804 5.369   1.00 76.98  ? 313  ARG A CG  1 
ATOM   6451  C CD  . ARG C  1 313 ? 47.862  -41.275 5.783   1.00 81.85  ? 313  ARG A CD  1 
ATOM   6452  N NE  . ARG C  1 313 ? 48.125  -42.660 5.381   1.00 90.13  ? 313  ARG A NE  1 
ATOM   6453  C CZ  . ARG C  1 313 ? 48.091  -43.707 6.204   1.00 84.86  ? 313  ARG A CZ  1 
ATOM   6454  N NH1 . ARG C  1 313 ? 47.818  -43.536 7.493   1.00 75.28  ? 313  ARG A NH1 1 
ATOM   6455  N NH2 . ARG C  1 313 ? 48.348  -44.928 5.741   1.00 81.63  ? 313  ARG A NH2 1 
ATOM   6456  N N   . LEU C  1 314 ? 43.071  -40.309 5.479   1.00 64.03  ? 314  LEU A N   1 
ATOM   6457  C CA  . LEU C  1 314 ? 41.965  -40.956 6.181   1.00 65.97  ? 314  LEU A CA  1 
ATOM   6458  C C   . LEU C  1 314 ? 41.929  -42.442 5.901   1.00 70.60  ? 314  LEU A C   1 
ATOM   6459  O O   . LEU C  1 314 ? 41.364  -42.862 4.883   1.00 68.93  ? 314  LEU A O   1 
ATOM   6460  C CB  . LEU C  1 314 ? 40.631  -40.352 5.761   1.00 64.48  ? 314  LEU A CB  1 
ATOM   6461  C CG  . LEU C  1 314 ? 39.595  -40.076 6.842   1.00 64.73  ? 314  LEU A CG  1 
ATOM   6462  C CD1 . LEU C  1 314 ? 40.173  -39.091 7.843   1.00 60.85  ? 314  LEU A CD1 1 
ATOM   6463  C CD2 . LEU C  1 314 ? 38.323  -39.522 6.211   1.00 62.41  ? 314  LEU A CD2 1 
ATOM   6464  N N   . VAL C  1 315 ? 42.511  -43.234 6.806   1.00 72.39  ? 315  VAL A N   1 
ATOM   6465  C CA  . VAL C  1 315 ? 42.564  -44.690 6.625   1.00 74.82  ? 315  VAL A CA  1 
ATOM   6466  C C   . VAL C  1 315 ? 42.024  -45.468 7.838   1.00 69.61  ? 315  VAL A C   1 
ATOM   6467  O O   . VAL C  1 315 ? 42.350  -45.166 8.996   1.00 66.05  ? 315  VAL A O   1 
ATOM   6468  C CB  . VAL C  1 315 ? 43.997  -45.159 6.304   1.00 71.42  ? 315  VAL A CB  1 
ATOM   6469  C CG1 . VAL C  1 315 ? 44.975  -44.568 7.286   1.00 70.05  ? 315  VAL A CG1 1 
ATOM   6470  C CG2 . VAL C  1 315 ? 44.066  -46.666 6.325   1.00 71.97  ? 315  VAL A CG2 1 
ATOM   6471  N N   . LEU C  1 316 ? 41.198  -46.471 7.540   1.00 68.38  ? 316  LEU A N   1 
ATOM   6472  C CA  . LEU C  1 316 ? 40.492  -47.273 8.539   1.00 68.67  ? 316  LEU A CA  1 
ATOM   6473  C C   . LEU C  1 316 ? 41.184  -48.608 8.799   1.00 71.83  ? 316  LEU A C   1 
ATOM   6474  O O   . LEU C  1 316 ? 41.512  -49.328 7.855   1.00 73.28  ? 316  LEU A O   1 
ATOM   6475  C CB  . LEU C  1 316 ? 39.061  -47.562 8.070   1.00 58.93  ? 316  LEU A CB  1 
ATOM   6476  C CG  . LEU C  1 316 ? 37.947  -46.562 8.336   1.00 55.54  ? 316  LEU A CG  1 
ATOM   6477  C CD1 . LEU C  1 316 ? 36.714  -46.916 7.525   1.00 54.35  ? 316  LEU A CD1 1 
ATOM   6478  C CD2 . LEU C  1 316 ? 37.628  -46.512 9.815   1.00 63.03  ? 316  LEU A CD2 1 
ATOM   6479  N N   . ALA C  1 317 ? 41.370  -48.958 10.069  1.00 70.11  ? 317  ALA A N   1 
ATOM   6480  C CA  . ALA C  1 317 ? 41.903  -50.272 10.398  1.00 69.28  ? 317  ALA A CA  1 
ATOM   6481  C C   . ALA C  1 317 ? 40.817  -51.316 10.169  1.00 66.82  ? 317  ALA A C   1 
ATOM   6482  O O   . ALA C  1 317 ? 39.729  -51.208 10.734  1.00 64.63  ? 317  ALA A O   1 
ATOM   6483  C CB  . ALA C  1 317 ? 42.410  -50.316 11.842  1.00 64.93  ? 317  ALA A CB  1 
ATOM   6484  N N   . THR C  1 318 ? 41.126  -52.323 9.346   1.00 72.56  ? 318  THR A N   1 
ATOM   6485  C CA  . THR C  1 318 ? 40.221  -53.450 9.074   1.00 77.73  ? 318  THR A CA  1 
ATOM   6486  C C   . THR C  1 318 ? 40.786  -54.770 9.611   1.00 83.35  ? 318  THR A C   1 
ATOM   6487  O O   . THR C  1 318 ? 40.038  -55.633 10.085  1.00 82.82  ? 318  THR A O   1 
ATOM   6488  C CB  . THR C  1 318 ? 39.938  -53.644 7.553   1.00 71.62  ? 318  THR A CB  1 
ATOM   6489  O OG1 . THR C  1 318 ? 41.174  -53.659 6.823   1.00 67.46  ? 318  THR A OG1 1 
ATOM   6490  C CG2 . THR C  1 318 ? 39.042  -52.550 7.017   1.00 73.30  ? 318  THR A CG2 1 
ATOM   6491  N N   . GLY C  1 319 ? 42.105  -54.926 9.536   1.00 85.26  ? 319  GLY A N   1 
ATOM   6492  C CA  . GLY C  1 319 ? 42.740  -56.132 10.030  1.00 85.51  ? 319  GLY A CA  1 
ATOM   6493  C C   . GLY C  1 319 ? 43.214  -55.938 11.454  1.00 81.08  ? 319  GLY A C   1 
ATOM   6494  O O   . GLY C  1 319 ? 42.703  -55.075 12.172  1.00 78.25  ? 319  GLY A O   1 
ATOM   6495  N N   . LEU C  1 320 ? 44.224  -56.703 11.850  1.00 83.19  ? 320  LEU A N   1 
ATOM   6496  C CA  . LEU C  1 320 ? 44.736  -56.621 13.209  1.00 83.59  ? 320  LEU A CA  1 
ATOM   6497  C C   . LEU C  1 320 ? 46.193  -56.182 13.232  1.00 82.34  ? 320  LEU A C   1 
ATOM   6498  O O   . LEU C  1 320 ? 46.826  -56.031 12.184  1.00 83.82  ? 320  LEU A O   1 
ATOM   6499  C CB  . LEU C  1 320 ? 44.559  -57.968 13.920  1.00 85.68  ? 320  LEU A CB  1 
ATOM   6500  C CG  . LEU C  1 320 ? 45.062  -59.223 13.205  1.00 85.95  ? 320  LEU A CG  1 
ATOM   6501  C CD1 . LEU C  1 320 ? 46.449  -59.581 13.725  1.00 88.06  ? 320  LEU A CD1 1 
ATOM   6502  C CD2 . LEU C  1 320 ? 44.086  -60.398 13.334  1.00 83.87  ? 320  LEU A CD2 1 
ATOM   6503  N N   . ARG C  1 321 ? 46.712  -55.991 14.439  1.00 80.84  ? 321  ARG A N   1 
ATOM   6504  C CA  . ARG C  1 321 ? 48.052  -55.459 14.639  1.00 80.54  ? 321  ARG A CA  1 
ATOM   6505  C C   . ARG C  1 321 ? 49.114  -56.414 14.096  1.00 88.53  ? 321  ARG A C   1 
ATOM   6506  O O   . ARG C  1 321 ? 49.040  -57.628 14.300  1.00 89.90  ? 321  ARG A O   1 
ATOM   6507  C CB  . ARG C  1 321 ? 48.272  -55.172 16.122  1.00 75.79  ? 321  ARG A CB  1 
ATOM   6508  C CG  . ARG C  1 321 ? 49.497  -54.349 16.424  1.00 76.46  ? 321  ARG A CG  1 
ATOM   6509  C CD  . ARG C  1 321 ? 49.643  -54.183 17.911  1.00 66.91  ? 321  ARG A CD  1 
ATOM   6510  N NE  . ARG C  1 321 ? 50.267  -52.915 18.264  1.00 70.74  ? 321  ARG A NE  1 
ATOM   6511  C CZ  . ARG C  1 321 ? 49.680  -51.962 18.988  1.00 77.11  ? 321  ARG A CZ  1 
ATOM   6512  N NH1 . ARG C  1 321 ? 48.440  -52.113 19.448  1.00 72.77  ? 321  ARG A NH1 1 
ATOM   6513  N NH2 . ARG C  1 321 ? 50.338  -50.850 19.259  1.00 78.45  ? 321  ARG A NH2 1 
ATOM   6514  N N   . ASN C  1 322 ? 50.085  -55.862 13.374  1.00 90.84  ? 322  ASN A N   1 
ATOM   6515  C CA  . ASN C  1 322 ? 51.084  -56.680 12.693  1.00 94.67  ? 322  ASN A CA  1 
ATOM   6516  C C   . ASN C  1 322 ? 52.374  -56.797 13.502  1.00 103.36 ? 322  ASN A C   1 
ATOM   6517  O O   . ASN C  1 322 ? 52.924  -55.792 13.978  1.00 99.52  ? 322  ASN A O   1 
ATOM   6518  C CB  . ASN C  1 322 ? 51.390  -56.115 11.306  1.00 95.76  ? 322  ASN A CB  1 
ATOM   6519  C CG  . ASN C  1 322 ? 51.746  -57.199 10.304  1.00 98.33  ? 322  ASN A CG  1 
ATOM   6520  O OD1 . ASN C  1 322 ? 52.230  -58.271 10.677  1.00 101.18 ? 322  ASN A OD1 1 
ATOM   6521  N ND2 . ASN C  1 322 ? 51.504  -56.927 9.020   1.00 94.14  ? 322  ASN A ND2 1 
ATOM   6522  N N   . SER C  1 323 ? 52.852  -58.035 13.637  1.00 111.18 ? 323  SER A N   1 
ATOM   6523  C CA  . SER C  1 323 ? 54.032  -58.345 14.445  1.00 112.80 ? 323  SER A CA  1 
ATOM   6524  C C   . SER C  1 323 ? 55.320  -57.796 13.841  1.00 113.33 ? 323  SER A C   1 
ATOM   6525  O O   . SER C  1 323 ? 55.611  -58.021 12.660  1.00 110.76 ? 323  SER A O   1 
ATOM   6526  C CB  . SER C  1 323 ? 54.159  -59.865 14.631  1.00 107.77 ? 323  SER A CB  1 
ATOM   6527  O OG  . SER C  1 323 ? 54.150  -60.542 13.381  1.00 102.68 ? 323  SER A OG  1 
ATOM   6528  N N   . PRO C  1 324 ? 56.103  -57.086 14.670  1.00 114.76 ? 324  PRO A N   1 
ATOM   6529  C CA  . PRO C  1 324 ? 57.369  -56.450 14.281  1.00 118.56 ? 324  PRO A CA  1 
ATOM   6530  C C   . PRO C  1 324 ? 58.392  -57.426 13.691  1.00 118.59 ? 324  PRO A C   1 
ATOM   6531  O O   . PRO C  1 324 ? 58.266  -58.637 13.873  1.00 121.41 ? 324  PRO A O   1 
ATOM   6532  C CB  . PRO C  1 324 ? 57.876  -55.862 15.601  1.00 114.86 ? 324  PRO A CB  1 
ATOM   6533  C CG  . PRO C  1 324 ? 56.625  -55.568 16.373  1.00 111.71 ? 324  PRO A CG  1 
ATOM   6534  C CD  . PRO C  1 324 ? 55.668  -56.674 16.020  1.00 110.74 ? 324  PRO A CD  1 
ATOM   6535  N N   . GLY D  2 1   ? 47.637  -55.843 24.538  1.00 90.37  ? 1    GLY B N   1 
ATOM   6536  C CA  . GLY D  2 1   ? 46.286  -55.429 24.195  1.00 88.50  ? 1    GLY B CA  1 
ATOM   6537  C C   . GLY D  2 1   ? 45.386  -55.232 25.405  1.00 84.48  ? 1    GLY B C   1 
ATOM   6538  O O   . GLY D  2 1   ? 45.845  -55.303 26.555  1.00 84.65  ? 1    GLY B O   1 
ATOM   6539  N N   . LEU D  2 2   ? 44.101  -54.979 25.148  1.00 77.55  ? 2    LEU B N   1 
ATOM   6540  C CA  . LEU D  2 2   ? 43.143  -54.696 26.220  1.00 79.47  ? 2    LEU B CA  1 
ATOM   6541  C C   . LEU D  2 2   ? 42.584  -56.006 26.785  1.00 78.23  ? 2    LEU B C   1 
ATOM   6542  O O   . LEU D  2 2   ? 41.663  -56.015 27.604  1.00 76.52  ? 2    LEU B O   1 
ATOM   6543  C CB  . LEU D  2 2   ? 41.999  -53.809 25.701  1.00 72.78  ? 2    LEU B CB  1 
ATOM   6544  C CG  . LEU D  2 2   ? 41.298  -52.871 26.689  1.00 62.81  ? 2    LEU B CG  1 
ATOM   6545  C CD1 . LEU D  2 2   ? 42.289  -51.846 27.201  1.00 62.78  ? 2    LEU B CD1 1 
ATOM   6546  C CD2 . LEU D  2 2   ? 40.099  -52.191 26.047  1.00 61.78  ? 2    LEU B CD2 1 
ATOM   6547  N N   . PHE D  2 3   ? 43.179  -57.106 26.343  1.00 82.02  ? 3    PHE B N   1 
ATOM   6548  C CA  . PHE D  2 3   ? 42.642  -58.447 26.537  1.00 80.51  ? 3    PHE B CA  1 
ATOM   6549  C C   . PHE D  2 3   ? 43.798  -59.395 26.849  1.00 78.42  ? 3    PHE B C   1 
ATOM   6550  O O   . PHE D  2 3   ? 43.603  -60.460 27.434  1.00 78.42  ? 3    PHE B O   1 
ATOM   6551  C CB  . PHE D  2 3   ? 41.817  -58.884 25.328  1.00 75.80  ? 3    PHE B CB  1 
ATOM   6552  C CG  . PHE D  2 3   ? 40.459  -58.233 25.270  1.00 75.88  ? 3    PHE B CG  1 
ATOM   6553  C CD1 . PHE D  2 3   ? 39.464  -58.590 26.174  1.00 75.66  ? 3    PHE B CD1 1 
ATOM   6554  C CD2 . PHE D  2 3   ? 40.188  -57.233 24.347  1.00 80.62  ? 3    PHE B CD2 1 
ATOM   6555  C CE1 . PHE D  2 3   ? 38.208  -57.985 26.141  1.00 75.78  ? 3    PHE B CE1 1 
ATOM   6556  C CE2 . PHE D  2 3   ? 38.937  -56.619 24.308  1.00 80.05  ? 3    PHE B CE2 1 
ATOM   6557  C CZ  . PHE D  2 3   ? 37.945  -56.998 25.207  1.00 78.67  ? 3    PHE B CZ  1 
ATOM   6558  N N   . GLY D  2 4   ? 44.993  -59.003 26.412  1.00 81.11  ? 4    GLY B N   1 
ATOM   6559  C CA  . GLY D  2 4   ? 46.217  -59.713 26.743  1.00 85.22  ? 4    GLY B CA  1 
ATOM   6560  C C   . GLY D  2 4   ? 46.674  -60.785 25.774  1.00 84.59  ? 4    GLY B C   1 
ATOM   6561  O O   . GLY D  2 4   ? 47.739  -61.374 25.957  1.00 83.01  ? 4    GLY B O   1 
ATOM   6562  N N   . ALA D  2 5   ? 45.900  -61.013 24.720  1.00 81.68  ? 5    ALA B N   1 
ATOM   6563  C CA  . ALA D  2 5   ? 46.226  -62.069 23.780  1.00 77.95  ? 5    ALA B CA  1 
ATOM   6564  C C   . ALA D  2 5   ? 47.254  -61.550 22.763  1.00 88.38  ? 5    ALA B C   1 
ATOM   6565  O O   . ALA D  2 5   ? 48.428  -61.901 22.875  1.00 92.63  ? 5    ALA B O   1 
ATOM   6566  C CB  . ALA D  2 5   ? 44.973  -62.588 23.101  1.00 68.00  ? 5    ALA B CB  1 
ATOM   6567  N N   . ILE D  2 6   ? 46.849  -60.709 21.803  1.00 90.04  ? 6    ILE B N   1 
ATOM   6568  C CA  . ILE D  2 6   ? 47.800  -60.158 20.816  1.00 88.75  ? 6    ILE B CA  1 
ATOM   6569  C C   . ILE D  2 6   ? 48.908  -59.355 21.506  1.00 90.91  ? 6    ILE B C   1 
ATOM   6570  O O   . ILE D  2 6   ? 48.632  -58.520 22.380  1.00 88.73  ? 6    ILE B O   1 
ATOM   6571  C CB  . ILE D  2 6   ? 47.111  -59.245 19.745  1.00 83.74  ? 6    ILE B CB  1 
ATOM   6572  C CG1 . ILE D  2 6   ? 46.344  -60.066 18.706  1.00 77.66  ? 6    ILE B CG1 1 
ATOM   6573  C CG2 . ILE D  2 6   ? 48.147  -58.453 18.971  1.00 79.41  ? 6    ILE B CG2 1 
ATOM   6574  C CD1 . ILE D  2 6   ? 45.007  -60.558 19.155  1.00 76.17  ? 6    ILE B CD1 1 
ATOM   6575  N N   . ALA D  2 7   ? 50.155  -59.662 21.131  1.00 92.14  ? 7    ALA B N   1 
ATOM   6576  C CA  . ALA D  2 7   ? 51.361  -59.082 21.731  1.00 91.36  ? 7    ALA B CA  1 
ATOM   6577  C C   . ALA D  2 7   ? 51.345  -59.233 23.249  1.00 93.08  ? 7    ALA B C   1 
ATOM   6578  O O   . ALA D  2 7   ? 51.859  -58.376 23.971  1.00 91.21  ? 7    ALA B O   1 
ATOM   6579  C CB  . ALA D  2 7   ? 51.517  -57.614 21.333  1.00 89.07  ? 7    ALA B CB  1 
ATOM   6580  N N   . GLY D  2 8   ? 50.744  -60.325 23.722  1.00 94.97  ? 8    GLY B N   1 
ATOM   6581  C CA  . GLY D  2 8   ? 50.608  -60.576 25.148  1.00 93.65  ? 8    GLY B CA  1 
ATOM   6582  C C   . GLY D  2 8   ? 51.132  -61.941 25.562  1.00 96.60  ? 8    GLY B C   1 
ATOM   6583  O O   . GLY D  2 8   ? 52.303  -62.241 25.328  1.00 98.58  ? 8    GLY B O   1 
ATOM   6584  N N   . PHE D  2 9   ? 50.277  -62.790 26.134  1.00 95.29  ? 9    PHE B N   1 
ATOM   6585  C CA  . PHE D  2 9   ? 50.743  -64.103 26.587  1.00 95.61  ? 9    PHE B CA  1 
ATOM   6586  C C   . PHE D  2 9   ? 51.024  -65.020 25.410  1.00 94.35  ? 9    PHE B C   1 
ATOM   6587  O O   . PHE D  2 9   ? 51.813  -65.957 25.524  1.00 100.08 ? 9    PHE B O   1 
ATOM   6588  C CB  . PHE D  2 9   ? 49.739  -64.760 27.550  1.00 92.77  ? 9    PHE B CB  1 
ATOM   6589  C CG  . PHE D  2 9   ? 48.460  -65.220 26.901  1.00 87.62  ? 9    PHE B CG  1 
ATOM   6590  C CD1 . PHE D  2 9   ? 48.369  -66.469 26.304  1.00 87.48  ? 9    PHE B CD1 1 
ATOM   6591  C CD2 . PHE D  2 9   ? 47.333  -64.417 26.933  1.00 85.50  ? 9    PHE B CD2 1 
ATOM   6592  C CE1 . PHE D  2 9   ? 47.189  -66.889 25.721  1.00 85.90  ? 9    PHE B CE1 1 
ATOM   6593  C CE2 . PHE D  2 9   ? 46.151  -64.833 26.359  1.00 80.12  ? 9    PHE B CE2 1 
ATOM   6594  C CZ  . PHE D  2 9   ? 46.080  -66.071 25.751  1.00 82.46  ? 9    PHE B CZ  1 
ATOM   6595  N N   . ILE D  2 10  ? 50.373  -64.747 24.286  1.00 89.59  ? 10   ILE B N   1 
ATOM   6596  C CA  . ILE D  2 10  ? 50.769  -65.330 23.016  1.00 91.51  ? 10   ILE B CA  1 
ATOM   6597  C C   . ILE D  2 10  ? 51.530  -64.243 22.257  1.00 98.94  ? 10   ILE B C   1 
ATOM   6598  O O   . ILE D  2 10  ? 51.000  -63.154 22.029  1.00 101.78 ? 10   ILE B O   1 
ATOM   6599  C CB  . ILE D  2 10  ? 49.561  -65.854 22.221  1.00 85.73  ? 10   ILE B CB  1 
ATOM   6600  C CG1 . ILE D  2 10  ? 49.799  -65.706 20.717  1.00 89.88  ? 10   ILE B CG1 1 
ATOM   6601  C CG2 . ILE D  2 10  ? 48.290  -65.153 22.657  1.00 84.54  ? 10   ILE B CG2 1 
ATOM   6602  C CD1 . ILE D  2 10  ? 48.604  -66.078 19.872  1.00 88.71  ? 10   ILE B CD1 1 
ATOM   6603  N N   . GLU D  2 11  ? 52.776  -64.528 21.886  1.00 97.67  ? 11   GLU B N   1 
ATOM   6604  C CA  . GLU D  2 11  ? 53.628  -63.530 21.233  1.00 97.92  ? 11   GLU B CA  1 
ATOM   6605  C C   . GLU D  2 11  ? 53.683  -63.704 19.719  1.00 98.31  ? 11   GLU B C   1 
ATOM   6606  O O   . GLU D  2 11  ? 53.856  -64.815 19.221  1.00 103.80 ? 11   GLU B O   1 
ATOM   6607  C CB  . GLU D  2 11  ? 55.055  -63.591 21.791  1.00 93.75  ? 11   GLU B CB  1 
ATOM   6608  C CG  . GLU D  2 11  ? 55.199  -63.328 23.277  1.00 92.00  ? 11   GLU B CG  1 
ATOM   6609  C CD  . GLU D  2 11  ? 56.642  -63.467 23.742  1.00 91.84  ? 11   GLU B CD  1 
ATOM   6610  O OE1 . GLU D  2 11  ? 57.459  -64.030 22.984  1.00 97.08  ? 11   GLU B OE1 1 
ATOM   6611  O OE2 . GLU D  2 11  ? 56.965  -63.014 24.859  1.00 92.53  ? 11   GLU B OE2 1 
ATOM   6612  N N   . GLY D  2 12  ? 53.517  -62.606 18.988  1.00 95.00  ? 12   GLY B N   1 
ATOM   6613  C CA  . GLY D  2 12  ? 53.671  -62.640 17.546  1.00 96.97  ? 12   GLY B CA  1 
ATOM   6614  C C   . GLY D  2 12  ? 52.600  -63.432 16.817  1.00 99.76  ? 12   GLY B C   1 
ATOM   6615  O O   . GLY D  2 12  ? 51.907  -64.265 17.415  1.00 92.33  ? 12   GLY B O   1 
ATOM   6616  N N   . GLY D  2 13  ? 52.453  -63.156 15.520  1.00 99.25  ? 13   GLY B N   1 
ATOM   6617  C CA  . GLY D  2 13  ? 51.493  -63.857 14.687  1.00 91.65  ? 13   GLY B CA  1 
ATOM   6618  C C   . GLY D  2 13  ? 52.225  -64.814 13.778  1.00 93.38  ? 13   GLY B C   1 
ATOM   6619  O O   . GLY D  2 13  ? 53.456  -64.775 13.698  1.00 93.05  ? 13   GLY B O   1 
ATOM   6620  N N   . TRP D  2 14  ? 51.470  -65.663 13.086  1.00 94.15  ? 14   TRP B N   1 
ATOM   6621  C CA  . TRP D  2 14  ? 52.056  -66.695 12.228  1.00 99.02  ? 14   TRP B CA  1 
ATOM   6622  C C   . TRP D  2 14  ? 51.989  -66.379 10.736  1.00 99.51  ? 14   TRP B C   1 
ATOM   6623  O O   . TRP D  2 14  ? 50.920  -66.454 10.121  1.00 96.32  ? 14   TRP B O   1 
ATOM   6624  C CB  . TRP D  2 14  ? 51.378  -68.043 12.471  1.00 98.79  ? 14   TRP B CB  1 
ATOM   6625  C CG  . TRP D  2 14  ? 51.440  -68.480 13.875  1.00 93.93  ? 14   TRP B CG  1 
ATOM   6626  C CD1 . TRP D  2 14  ? 52.425  -68.205 14.783  1.00 89.49  ? 14   TRP B CD1 1 
ATOM   6627  C CD2 . TRP D  2 14  ? 50.470  -69.273 14.554  1.00 94.23  ? 14   TRP B CD2 1 
ATOM   6628  N NE1 . TRP D  2 14  ? 52.121  -68.781 15.990  1.00 92.76  ? 14   TRP B NE1 1 
ATOM   6629  C CE2 . TRP D  2 14  ? 50.925  -69.444 15.877  1.00 97.79  ? 14   TRP B CE2 1 
ATOM   6630  C CE3 . TRP D  2 14  ? 49.256  -69.855 14.173  1.00 97.45  ? 14   TRP B CE3 1 
ATOM   6631  C CZ2 . TRP D  2 14  ? 50.207  -70.175 16.825  1.00 99.83  ? 14   TRP B CZ2 1 
ATOM   6632  C CZ3 . TRP D  2 14  ? 48.544  -70.578 15.111  1.00 98.07  ? 14   TRP B CZ3 1 
ATOM   6633  C CH2 . TRP D  2 14  ? 49.019  -70.729 16.423  1.00 100.17 ? 14   TRP B CH2 1 
ATOM   6634  N N   . GLN D  2 15  ? 53.147  -66.084 10.152  1.00 99.85  ? 15   GLN B N   1 
ATOM   6635  C CA  . GLN D  2 15  ? 53.246  -65.797 8.727   1.00 99.07  ? 15   GLN B CA  1 
ATOM   6636  C C   . GLN D  2 15  ? 52.795  -67.024 7.912   1.00 98.57  ? 15   GLN B C   1 
ATOM   6637  O O   . GLN D  2 15  ? 52.390  -66.908 6.753   1.00 99.39  ? 15   GLN B O   1 
ATOM   6638  C CB  . GLN D  2 15  ? 54.682  -65.384 8.401   1.00 92.80  ? 15   GLN B CB  1 
ATOM   6639  C CG  . GLN D  2 15  ? 55.089  -64.087 9.109   1.00 95.84  ? 15   GLN B CG  1 
ATOM   6640  C CD  . GLN D  2 15  ? 56.574  -63.797 9.013   1.00 101.69 ? 15   GLN B CD  1 
ATOM   6641  O OE1 . GLN D  2 15  ? 57.381  -64.714 8.867   1.00 109.62 ? 15   GLN B OE1 1 
ATOM   6642  N NE2 . GLN D  2 15  ? 56.945  -62.522 9.121   1.00 93.14  ? 15   GLN B NE2 1 
ATOM   6643  N N   . GLY D  2 16  ? 52.835  -68.193 8.549   1.00 97.92  ? 16   GLY B N   1 
ATOM   6644  C CA  . GLY D  2 16  ? 52.456  -69.447 7.920   1.00 99.35  ? 16   GLY B CA  1 
ATOM   6645  C C   . GLY D  2 16  ? 50.958  -69.667 8.010   1.00 100.16 ? 16   GLY B C   1 
ATOM   6646  O O   . GLY D  2 16  ? 50.405  -70.595 7.412   1.00 95.79  ? 16   GLY B O   1 
ATOM   6647  N N   . MET D  2 17  ? 50.303  -68.801 8.778   1.00 101.49 ? 17   MET B N   1 
ATOM   6648  C CA  . MET D  2 17  ? 48.855  -68.841 8.949   1.00 103.21 ? 17   MET B CA  1 
ATOM   6649  C C   . MET D  2 17  ? 48.200  -67.897 7.937   1.00 104.94 ? 17   MET B C   1 
ATOM   6650  O O   . MET D  2 17  ? 48.179  -66.687 8.133   1.00 106.27 ? 17   MET B O   1 
ATOM   6651  C CB  . MET D  2 17  ? 48.511  -68.450 10.397  1.00 99.20  ? 17   MET B CB  1 
ATOM   6652  C CG  . MET D  2 17  ? 47.042  -68.343 10.742  1.00 102.52 ? 17   MET B CG  1 
ATOM   6653  S SD  . MET D  2 17  ? 46.158  -69.902 10.811  1.00 115.43 ? 17   MET B SD  1 
ATOM   6654  C CE  . MET D  2 17  ? 44.521  -69.271 11.116  1.00 102.87 ? 17   MET B CE  1 
ATOM   6655  N N   . VAL D  2 18  ? 47.698  -68.451 6.835   1.00 105.43 ? 18   VAL B N   1 
ATOM   6656  C CA  . VAL D  2 18  ? 47.209  -67.620 5.733   1.00 105.25 ? 18   VAL B CA  1 
ATOM   6657  C C   . VAL D  2 18  ? 45.822  -68.057 5.220   1.00 107.02 ? 18   VAL B C   1 
ATOM   6658  O O   . VAL D  2 18  ? 45.539  -67.941 4.029   1.00 110.68 ? 18   VAL B O   1 
ATOM   6659  C CB  . VAL D  2 18  ? 48.218  -67.610 4.540   1.00 104.80 ? 18   VAL B CB  1 
ATOM   6660  C CG1 . VAL D  2 18  ? 48.148  -66.280 3.790   1.00 102.32 ? 18   VAL B CG1 1 
ATOM   6661  C CG2 . VAL D  2 18  ? 49.649  -67.847 5.020   1.00 98.11  ? 18   VAL B CG2 1 
ATOM   6662  N N   . ASP D  2 19  ? 44.962  -68.572 6.093   1.00 106.14 ? 19   ASP B N   1 
ATOM   6663  C CA  . ASP D  2 19  ? 43.641  -69.024 5.639   1.00 108.97 ? 19   ASP B CA  1 
ATOM   6664  C C   . ASP D  2 19  ? 42.500  -68.278 6.346   1.00 110.64 ? 19   ASP B C   1 
ATOM   6665  O O   . ASP D  2 19  ? 41.334  -68.364 5.950   1.00 110.30 ? 19   ASP B O   1 
ATOM   6666  C CB  . ASP D  2 19  ? 43.498  -70.536 5.861   1.00 114.77 ? 19   ASP B CB  1 
ATOM   6667  C CG  . ASP D  2 19  ? 42.342  -71.152 5.069   1.00 118.18 ? 19   ASP B CG  1 
ATOM   6668  O OD1 . ASP D  2 19  ? 41.556  -70.416 4.437   1.00 114.52 ? 19   ASP B OD1 1 
ATOM   6669  O OD2 . ASP D  2 19  ? 42.225  -72.396 5.078   1.00 122.69 ? 19   ASP B OD2 1 
ATOM   6670  N N   . GLY D  2 20  ? 42.837  -67.550 7.403   1.00 108.58 ? 20   GLY B N   1 
ATOM   6671  C CA  . GLY D  2 20  ? 41.841  -66.815 8.158   1.00 95.70  ? 20   GLY B CA  1 
ATOM   6672  C C   . GLY D  2 20  ? 42.505  -65.772 9.022   1.00 98.41  ? 20   GLY B C   1 
ATOM   6673  O O   . GLY D  2 20  ? 43.663  -65.414 8.807   1.00 98.64  ? 20   GLY B O   1 
ATOM   6674  N N   . TRP D  2 21  ? 41.764  -65.271 9.997   1.00 97.67  ? 21   TRP B N   1 
ATOM   6675  C CA  . TRP D  2 21  ? 42.294  -64.267 10.903  1.00 98.38  ? 21   TRP B CA  1 
ATOM   6676  C C   . TRP D  2 21  ? 42.795  -64.919 12.186  1.00 99.28  ? 21   TRP B C   1 
ATOM   6677  O O   . TRP D  2 21  ? 43.846  -64.544 12.721  1.00 94.22  ? 21   TRP B O   1 
ATOM   6678  C CB  . TRP D  2 21  ? 41.225  -63.223 11.225  1.00 100.48 ? 21   TRP B CB  1 
ATOM   6679  C CG  . TRP D  2 21  ? 41.202  -62.004 10.340  1.00 97.46  ? 21   TRP B CG  1 
ATOM   6680  C CD1 . TRP D  2 21  ? 42.256  -61.442 9.670   1.00 96.89  ? 21   TRP B CD1 1 
ATOM   6681  C CD2 . TRP D  2 21  ? 40.056  -61.205 10.027  1.00 101.07 ? 21   TRP B CD2 1 
ATOM   6682  N NE1 . TRP D  2 21  ? 41.835  -60.334 8.972   1.00 96.11  ? 21   TRP B NE1 1 
ATOM   6683  C CE2 . TRP D  2 21  ? 40.487  -60.170 9.172   1.00 104.57 ? 21   TRP B CE2 1 
ATOM   6684  C CE3 . TRP D  2 21  ? 38.702  -61.263 10.390  1.00 98.29  ? 21   TRP B CE3 1 
ATOM   6685  C CZ2 . TRP D  2 21  ? 39.610  -59.201 8.675   1.00 104.84 ? 21   TRP B CZ2 1 
ATOM   6686  C CZ3 . TRP D  2 21  ? 37.835  -60.298 9.894   1.00 94.53  ? 21   TRP B CZ3 1 
ATOM   6687  C CH2 . TRP D  2 21  ? 38.291  -59.283 9.049   1.00 95.45  ? 21   TRP B CH2 1 
ATOM   6688  N N   . TYR D  2 22  ? 42.043  -65.908 12.665  1.00 99.60  ? 22   TYR B N   1 
ATOM   6689  C CA  . TYR D  2 22  ? 42.392  -66.599 13.900  1.00 101.74 ? 22   TYR B CA  1 
ATOM   6690  C C   . TYR D  2 22  ? 42.466  -68.113 13.695  1.00 104.06 ? 22   TYR B C   1 
ATOM   6691  O O   . TYR D  2 22  ? 41.718  -68.671 12.883  1.00 101.38 ? 22   TYR B O   1 
ATOM   6692  C CB  . TYR D  2 22  ? 41.363  -66.289 14.990  1.00 100.36 ? 22   TYR B CB  1 
ATOM   6693  C CG  . TYR D  2 22  ? 40.687  -64.936 14.869  1.00 95.88  ? 22   TYR B CG  1 
ATOM   6694  C CD1 . TYR D  2 22  ? 41.377  -63.754 15.138  1.00 88.40  ? 22   TYR B CD1 1 
ATOM   6695  C CD2 . TYR D  2 22  ? 39.340  -64.849 14.511  1.00 92.67  ? 22   TYR B CD2 1 
ATOM   6696  C CE1 . TYR D  2 22  ? 40.749  -62.524 15.035  1.00 85.59  ? 22   TYR B CE1 1 
ATOM   6697  C CE2 . TYR D  2 22  ? 38.705  -63.628 14.408  1.00 87.71  ? 22   TYR B CE2 1 
ATOM   6698  C CZ  . TYR D  2 22  ? 39.412  -62.466 14.671  1.00 86.42  ? 22   TYR B CZ  1 
ATOM   6699  O OH  . TYR D  2 22  ? 38.779  -61.242 14.572  1.00 85.85  ? 22   TYR B OH  1 
ATOM   6700  N N   . GLY D  2 23  ? 43.329  -68.782 14.460  1.00 104.03 ? 23   GLY B N   1 
ATOM   6701  C CA  . GLY D  2 23  ? 43.458  -70.224 14.330  1.00 108.15 ? 23   GLY B CA  1 
ATOM   6702  C C   . GLY D  2 23  ? 44.454  -70.970 15.205  1.00 106.65 ? 23   GLY B C   1 
ATOM   6703  O O   . GLY D  2 23  ? 44.805  -70.534 16.311  1.00 100.28 ? 23   GLY B O   1 
ATOM   6704  N N   . TYR D  2 24  ? 44.921  -72.101 14.671  1.00 106.71 ? 24   TYR B N   1 
ATOM   6705  C CA  . TYR D  2 24  ? 45.701  -73.088 15.414  1.00 106.71 ? 24   TYR B CA  1 
ATOM   6706  C C   . TYR D  2 24  ? 47.038  -73.474 14.771  1.00 109.78 ? 24   TYR B C   1 
ATOM   6707  O O   . TYR D  2 24  ? 47.151  -73.571 13.549  1.00 110.10 ? 24   TYR B O   1 
ATOM   6708  C CB  . TYR D  2 24  ? 44.886  -74.368 15.594  1.00 97.38  ? 24   TYR B CB  1 
ATOM   6709  C CG  . TYR D  2 24  ? 43.437  -74.153 15.934  1.00 99.15  ? 24   TYR B CG  1 
ATOM   6710  C CD1 . TYR D  2 24  ? 42.491  -73.928 14.938  1.00 102.61 ? 24   TYR B CD1 1 
ATOM   6711  C CD2 . TYR D  2 24  ? 43.004  -74.197 17.250  1.00 99.59  ? 24   TYR B CD2 1 
ATOM   6712  C CE1 . TYR D  2 24  ? 41.148  -73.736 15.251  1.00 102.55 ? 24   TYR B CE1 1 
ATOM   6713  C CE2 . TYR D  2 24  ? 41.665  -74.016 17.574  1.00 97.68  ? 24   TYR B CE2 1 
ATOM   6714  C CZ  . TYR D  2 24  ? 40.738  -73.788 16.572  1.00 96.73  ? 24   TYR B CZ  1 
ATOM   6715  O OH  . TYR D  2 24  ? 39.406  -73.612 16.893  1.00 87.36  ? 24   TYR B OH  1 
ATOM   6716  N N   . HIS D  2 25  ? 48.043  -73.708 15.610  1.00 108.54 ? 25   HIS B N   1 
ATOM   6717  C CA  . HIS D  2 25  ? 49.279  -74.352 15.176  1.00 108.25 ? 25   HIS B CA  1 
ATOM   6718  C C   . HIS D  2 25  ? 49.249  -75.717 15.843  1.00 111.70 ? 25   HIS B C   1 
ATOM   6719  O O   . HIS D  2 25  ? 49.405  -75.820 17.064  1.00 111.52 ? 25   HIS B O   1 
ATOM   6720  C CB  . HIS D  2 25  ? 50.514  -73.533 15.600  1.00 105.66 ? 25   HIS B CB  1 
ATOM   6721  C CG  . HIS D  2 25  ? 51.831  -74.090 15.144  1.00 104.29 ? 25   HIS B CG  1 
ATOM   6722  N ND1 . HIS D  2 25  ? 53.031  -73.694 15.700  1.00 98.06  ? 25   HIS B ND1 1 
ATOM   6723  C CD2 . HIS D  2 25  ? 52.144  -74.986 14.178  1.00 107.07 ? 25   HIS B CD2 1 
ATOM   6724  C CE1 . HIS D  2 25  ? 54.022  -74.332 15.105  1.00 102.43 ? 25   HIS B CE1 1 
ATOM   6725  N NE2 . HIS D  2 25  ? 53.512  -75.122 14.176  1.00 106.78 ? 25   HIS B NE2 1 
ATOM   6726  N N   . HIS D  2 26  ? 49.055  -76.766 15.045  1.00 113.11 ? 26   HIS B N   1 
ATOM   6727  C CA  . HIS D  2 26  ? 48.910  -78.115 15.590  1.00 111.36 ? 26   HIS B CA  1 
ATOM   6728  C C   . HIS D  2 26  ? 50.161  -78.944 15.342  1.00 112.45 ? 26   HIS B C   1 
ATOM   6729  O O   . HIS D  2 26  ? 50.811  -78.822 14.303  1.00 115.05 ? 26   HIS B O   1 
ATOM   6730  C CB  . HIS D  2 26  ? 47.644  -78.792 15.019  1.00 106.75 ? 26   HIS B CB  1 
ATOM   6731  C CG  . HIS D  2 26  ? 47.854  -80.208 14.567  1.00 117.10 ? 26   HIS B CG  1 
ATOM   6732  N ND1 . HIS D  2 26  ? 48.490  -80.518 13.381  1.00 117.57 ? 26   HIS B ND1 1 
ATOM   6733  C CD2 . HIS D  2 26  ? 47.522  -81.394 15.133  1.00 117.32 ? 26   HIS B CD2 1 
ATOM   6734  C CE1 . HIS D  2 26  ? 48.534  -81.830 13.232  1.00 114.34 ? 26   HIS B CE1 1 
ATOM   6735  N NE2 . HIS D  2 26  ? 47.960  -82.387 14.285  1.00 119.11 ? 26   HIS B NE2 1 
ATOM   6736  N N   . SER D  2 27  ? 50.494  -79.770 16.331  1.00 109.34 ? 27   SER B N   1 
ATOM   6737  C CA  . SER D  2 27  ? 51.710  -80.579 16.316  1.00 109.47 ? 27   SER B CA  1 
ATOM   6738  C C   . SER D  2 27  ? 51.505  -81.952 16.962  1.00 107.17 ? 27   SER B C   1 
ATOM   6739  O O   . SER D  2 27  ? 51.725  -82.106 18.162  1.00 108.68 ? 27   SER B O   1 
ATOM   6740  C CB  . SER D  2 27  ? 52.844  -79.823 17.032  1.00 106.81 ? 27   SER B CB  1 
ATOM   6741  O OG  . SER D  2 27  ? 54.064  -80.552 17.032  1.00 101.37 ? 27   SER B OG  1 
ATOM   6742  N N   . ASN D  2 28  ? 51.090  -82.948 16.188  1.00 104.93 ? 28   ASN B N   1 
ATOM   6743  C CA  . ASN D  2 28  ? 50.976  -84.303 16.729  1.00 103.07 ? 28   ASN B CA  1 
ATOM   6744  C C   . ASN D  2 28  ? 51.840  -85.260 15.901  1.00 110.80 ? 28   ASN B C   1 
ATOM   6745  O O   . ASN D  2 28  ? 52.825  -84.831 15.286  1.00 109.49 ? 28   ASN B O   1 
ATOM   6746  C CB  . ASN D  2 28  ? 49.510  -84.784 16.807  1.00 101.18 ? 28   ASN B CB  1 
ATOM   6747  C CG  . ASN D  2 28  ? 48.884  -85.088 15.445  1.00 104.51 ? 28   ASN B CG  1 
ATOM   6748  O OD1 . ASN D  2 28  ? 49.369  -84.658 14.396  1.00 111.09 ? 28   ASN B OD1 1 
ATOM   6749  N ND2 . ASN D  2 28  ? 47.799  -85.857 15.464  1.00 93.76  ? 28   ASN B ND2 1 
ATOM   6750  N N   . GLU D  2 29  ? 51.498  -86.549 15.922  1.00 113.46 ? 29   GLU B N   1 
ATOM   6751  C CA  . GLU D  2 29  ? 52.267  -87.596 15.232  1.00 112.86 ? 29   GLU B CA  1 
ATOM   6752  C C   . GLU D  2 29  ? 52.316  -87.370 13.730  1.00 111.34 ? 29   GLU B C   1 
ATOM   6753  O O   . GLU D  2 29  ? 53.371  -87.499 13.107  1.00 111.76 ? 29   GLU B O   1 
ATOM   6754  C CB  . GLU D  2 29  ? 51.654  -88.974 15.497  1.00 109.83 ? 29   GLU B CB  1 
ATOM   6755  C CG  . GLU D  2 29  ? 51.593  -89.357 16.962  1.00 116.41 ? 29   GLU B CG  1 
ATOM   6756  C CD  . GLU D  2 29  ? 50.468  -88.639 17.686  1.00 112.66 ? 29   GLU B CD  1 
ATOM   6757  O OE1 . GLU D  2 29  ? 49.669  -87.952 17.007  1.00 115.05 ? 29   GLU B OE1 1 
ATOM   6758  O OE2 . GLU D  2 29  ? 50.394  -88.737 18.926  1.00 112.02 ? 29   GLU B OE2 1 
ATOM   6759  N N   . GLN D  2 30  ? 51.161  -87.034 13.161  1.00 110.35 ? 30   GLN B N   1 
ATOM   6760  C CA  . GLN D  2 30  ? 51.074  -86.598 11.775  1.00 107.41 ? 30   GLN B CA  1 
ATOM   6761  C C   . GLN D  2 30  ? 51.588  -85.164 11.635  1.00 112.20 ? 30   GLN B C   1 
ATOM   6762  O O   . GLN D  2 30  ? 50.812  -84.227 11.389  1.00 105.88 ? 30   GLN B O   1 
ATOM   6763  C CB  . GLN D  2 30  ? 49.641  -86.703 11.237  1.00 102.81 ? 30   GLN B CB  1 
ATOM   6764  C CG  . GLN D  2 30  ? 49.090  -88.117 11.062  1.00 89.71  ? 30   GLN B CG  1 
ATOM   6765  C CD  . GLN D  2 30  ? 48.472  -88.688 12.317  1.00 96.65  ? 30   GLN B CD  1 
ATOM   6766  O OE1 . GLN D  2 30  ? 48.988  -88.501 13.420  1.00 103.64 ? 30   GLN B OE1 1 
ATOM   6767  N NE2 . GLN D  2 30  ? 47.334  -89.360 12.159  1.00 84.53  ? 30   GLN B NE2 1 
ATOM   6768  N N   . GLY D  2 31  ? 52.896  -85.008 11.847  1.00 114.83 ? 31   GLY B N   1 
ATOM   6769  C CA  . GLY D  2 31  ? 53.603  -83.754 11.638  1.00 116.89 ? 31   GLY B CA  1 
ATOM   6770  C C   . GLY D  2 31  ? 53.085  -82.485 12.293  1.00 115.12 ? 31   GLY B C   1 
ATOM   6771  O O   . GLY D  2 31  ? 52.367  -82.520 13.294  1.00 113.65 ? 31   GLY B O   1 
ATOM   6772  N N   . SER D  2 32  ? 53.455  -81.358 11.686  1.00 114.50 ? 32   SER B N   1 
ATOM   6773  C CA  . SER D  2 32  ? 53.116  -80.028 12.169  1.00 110.91 ? 32   SER B CA  1 
ATOM   6774  C C   . SER D  2 32  ? 51.964  -79.482 11.333  1.00 114.45 ? 32   SER B C   1 
ATOM   6775  O O   . SER D  2 32  ? 51.276  -80.250 10.649  1.00 114.55 ? 32   SER B O   1 
ATOM   6776  C CB  . SER D  2 32  ? 54.330  -79.092 12.073  1.00 108.73 ? 32   SER B CB  1 
ATOM   6777  O OG  . SER D  2 32  ? 55.427  -79.558 12.840  1.00 103.01 ? 32   SER B OG  1 
ATOM   6778  N N   . GLY D  2 33  ? 51.717  -78.176 11.418  1.00 114.80 ? 33   GLY B N   1 
ATOM   6779  C CA  . GLY D  2 33  ? 50.709  -77.563 10.568  1.00 114.65 ? 33   GLY B CA  1 
ATOM   6780  C C   . GLY D  2 33  ? 50.007  -76.313 11.075  1.00 112.94 ? 33   GLY B C   1 
ATOM   6781  O O   . GLY D  2 33  ? 50.094  -75.971 12.258  1.00 109.55 ? 33   GLY B O   1 
ATOM   6782  N N   . TYR D  2 34  ? 49.324  -75.626 10.155  1.00 110.97 ? 34   TYR B N   1 
ATOM   6783  C CA  . TYR D  2 34  ? 48.484  -74.470 10.468  1.00 100.11 ? 34   TYR B CA  1 
ATOM   6784  C C   . TYR D  2 34  ? 47.020  -74.761 10.100  1.00 101.59 ? 34   TYR B C   1 
ATOM   6785  O O   . TYR D  2 34  ? 46.746  -75.633 9.275   1.00 97.27  ? 34   TYR B O   1 
ATOM   6786  C CB  . TYR D  2 34  ? 49.001  -73.230 9.753   1.00 93.60  ? 34   TYR B CB  1 
ATOM   6787  C CG  . TYR D  2 34  ? 50.346  -72.769 10.267  1.00 90.19  ? 34   TYR B CG  1 
ATOM   6788  C CD1 . TYR D  2 34  ? 50.466  -72.170 11.508  1.00 95.55  ? 34   TYR B CD1 1 
ATOM   6789  C CD2 . TYR D  2 34  ? 51.496  -72.936 9.512   1.00 91.97  ? 34   TYR B CD2 1 
ATOM   6790  C CE1 . TYR D  2 34  ? 51.695  -71.742 11.984  1.00 96.49  ? 34   TYR B CE1 1 
ATOM   6791  C CE2 . TYR D  2 34  ? 52.730  -72.510 9.977   1.00 89.83  ? 34   TYR B CE2 1 
ATOM   6792  C CZ  . TYR D  2 34  ? 52.824  -71.915 11.214  1.00 92.41  ? 34   TYR B CZ  1 
ATOM   6793  O OH  . TYR D  2 34  ? 54.048  -71.489 11.689  1.00 90.17  ? 34   TYR B OH  1 
ATOM   6794  N N   . ALA D  2 35  ? 46.085  -74.079 10.760  1.00 106.34 ? 35   ALA B N   1 
ATOM   6795  C CA  . ALA D  2 35  ? 44.650  -74.268 10.510  1.00 106.86 ? 35   ALA B CA  1 
ATOM   6796  C C   . ALA D  2 35  ? 43.811  -73.052 10.950  1.00 111.93 ? 35   ALA B C   1 
ATOM   6797  O O   . ALA D  2 35  ? 44.029  -72.500 12.028  1.00 115.99 ? 35   ALA B O   1 
ATOM   6798  C CB  . ALA D  2 35  ? 44.153  -75.535 11.205  1.00 97.79  ? 35   ALA B CB  1 
ATOM   6799  N N   . ALA D  2 36  ? 42.874  -72.620 10.109  1.00 109.07 ? 36   ALA B N   1 
ATOM   6800  C CA  . ALA D  2 36  ? 42.027  -71.468 10.432  1.00 104.80 ? 36   ALA B CA  1 
ATOM   6801  C C   . ALA D  2 36  ? 40.666  -71.869 11.015  1.00 103.41 ? 36   ALA B C   1 
ATOM   6802  O O   . ALA D  2 36  ? 40.016  -72.784 10.504  1.00 99.29  ? 36   ALA B O   1 
ATOM   6803  C CB  . ALA D  2 36  ? 41.833  -70.605 9.194   1.00 106.07 ? 36   ALA B CB  1 
ATOM   6804  N N   . ASP D  2 37  ? 40.240  -71.192 12.084  1.00 99.07  ? 37   ASP B N   1 
ATOM   6805  C CA  . ASP D  2 37  ? 38.881  -71.378 12.603  1.00 96.53  ? 37   ASP B CA  1 
ATOM   6806  C C   . ASP D  2 37  ? 37.894  -70.568 11.775  1.00 96.10  ? 37   ASP B C   1 
ATOM   6807  O O   . ASP D  2 37  ? 37.834  -69.342 11.890  1.00 96.61  ? 37   ASP B O   1 
ATOM   6808  C CB  . ASP D  2 37  ? 38.767  -70.983 14.078  1.00 98.70  ? 37   ASP B CB  1 
ATOM   6809  C CG  . ASP D  2 37  ? 37.402  -71.359 14.682  1.00 96.71  ? 37   ASP B CG  1 
ATOM   6810  O OD1 . ASP D  2 37  ? 36.807  -72.375 14.252  1.00 98.26  ? 37   ASP B OD1 1 
ATOM   6811  O OD2 . ASP D  2 37  ? 36.916  -70.629 15.575  1.00 89.07  ? 37   ASP B OD2 1 
ATOM   6812  N N   . LYS D  2 38  ? 37.143  -71.259 10.922  1.00 98.44  ? 38   LYS B N   1 
ATOM   6813  C CA  . LYS D  2 38  ? 36.244  -70.606 9.970   1.00 102.32 ? 38   LYS B CA  1 
ATOM   6814  C C   . LYS D  2 38  ? 35.071  -69.845 10.607  1.00 99.63  ? 38   LYS B C   1 
ATOM   6815  O O   . LYS D  2 38  ? 34.793  -68.708 10.222  1.00 99.29  ? 38   LYS B O   1 
ATOM   6816  C CB  . LYS D  2 38  ? 35.700  -71.644 8.972   1.00 100.43 ? 38   LYS B CB  1 
ATOM   6817  C CG  . LYS D  2 38  ? 34.672  -71.089 7.986   1.00 97.76  ? 38   LYS B CG  1 
ATOM   6818  C CD  . LYS D  2 38  ? 34.150  -72.150 7.013   1.00 94.02  ? 38   LYS B CD  1 
ATOM   6819  C CE  . LYS D  2 38  ? 33.018  -71.582 6.161   1.00 87.57  ? 38   LYS B CE  1 
ATOM   6820  N NZ  . LYS D  2 38  ? 32.588  -72.478 5.054   1.00 81.31  ? 38   LYS B NZ  1 
ATOM   6821  N N   . GLU D  2 39  ? 34.397  -70.465 11.575  1.00 98.92  ? 39   GLU B N   1 
ATOM   6822  C CA  . GLU D  2 39  ? 33.164  -69.913 12.144  1.00 101.56 ? 39   GLU B CA  1 
ATOM   6823  C C   . GLU D  2 39  ? 33.294  -68.493 12.736  1.00 105.54 ? 39   GLU B C   1 
ATOM   6824  O O   . GLU D  2 39  ? 32.478  -67.606 12.439  1.00 102.39 ? 39   GLU B O   1 
ATOM   6825  C CB  . GLU D  2 39  ? 32.622  -70.875 13.212  1.00 104.01 ? 39   GLU B CB  1 
ATOM   6826  C CG  . GLU D  2 39  ? 31.303  -70.427 13.854  1.00 108.12 ? 39   GLU B CG  1 
ATOM   6827  C CD  . GLU D  2 39  ? 31.512  -69.500 15.054  1.00 114.85 ? 39   GLU B CD  1 
ATOM   6828  O OE1 . GLU D  2 39  ? 32.672  -69.402 15.525  1.00 118.86 ? 39   GLU B OE1 1 
ATOM   6829  O OE2 . GLU D  2 39  ? 30.529  -68.869 15.520  1.00 112.44 ? 39   GLU B OE2 1 
ATOM   6830  N N   . SER D  2 40  ? 34.328  -68.286 13.554  1.00 103.82 ? 40   SER B N   1 
ATOM   6831  C CA  . SER D  2 40  ? 34.538  -67.021 14.261  1.00 100.87 ? 40   SER B CA  1 
ATOM   6832  C C   . SER D  2 40  ? 35.057  -65.906 13.341  1.00 97.15  ? 40   SER B C   1 
ATOM   6833  O O   . SER D  2 40  ? 34.855  -64.715 13.606  1.00 94.40  ? 40   SER B O   1 
ATOM   6834  C CB  . SER D  2 40  ? 35.493  -67.241 15.443  1.00 89.89  ? 40   SER B CB  1 
ATOM   6835  O OG  . SER D  2 40  ? 36.793  -67.595 15.005  1.00 87.93  ? 40   SER B OG  1 
ATOM   6836  N N   . THR D  2 41  ? 35.708  -66.305 12.254  1.00 95.22  ? 41   THR B N   1 
ATOM   6837  C CA  . THR D  2 41  ? 36.214  -65.365 11.264  1.00 96.36  ? 41   THR B CA  1 
ATOM   6838  C C   . THR D  2 41  ? 35.071  -64.781 10.421  1.00 94.58  ? 41   THR B C   1 
ATOM   6839  O O   . THR D  2 41  ? 35.162  -63.640 9.977   1.00 92.05  ? 41   THR B O   1 
ATOM   6840  C CB  . THR D  2 41  ? 37.256  -66.025 10.338  1.00 97.25  ? 41   THR B CB  1 
ATOM   6841  O OG1 . THR D  2 41  ? 37.108  -67.448 10.401  1.00 97.56  ? 41   THR B OG1 1 
ATOM   6842  C CG2 . THR D  2 41  ? 38.675  -65.649 10.760  1.00 88.62  ? 41   THR B CG2 1 
ATOM   6843  N N   . GLN D  2 42  ? 34.008  -65.551 10.188  1.00 92.77  ? 42   GLN B N   1 
ATOM   6844  C CA  . GLN D  2 42  ? 32.878  -65.028 9.412   1.00 94.96  ? 42   GLN B CA  1 
ATOM   6845  C C   . GLN D  2 42  ? 32.166  -63.931 10.202  1.00 95.16  ? 42   GLN B C   1 
ATOM   6846  O O   . GLN D  2 42  ? 31.820  -62.880 9.655   1.00 92.15  ? 42   GLN B O   1 
ATOM   6847  C CB  . GLN D  2 42  ? 31.879  -66.134 9.028   1.00 96.74  ? 42   GLN B CB  1 
ATOM   6848  C CG  . GLN D  2 42  ? 30.697  -65.649 8.136   1.00 95.34  ? 42   GLN B CG  1 
ATOM   6849  C CD  . GLN D  2 42  ? 31.139  -64.946 6.842   1.00 93.83  ? 42   GLN B CD  1 
ATOM   6850  O OE1 . GLN D  2 42  ? 32.122  -65.340 6.214   1.00 96.12  ? 42   GLN B OE1 1 
ATOM   6851  N NE2 . GLN D  2 42  ? 30.408  -63.902 6.448   1.00 83.24  ? 42   GLN B NE2 1 
ATOM   6852  N N   . LYS D  2 43  ? 31.964  -64.171 11.494  1.00 98.88  ? 43   LYS B N   1 
ATOM   6853  C CA  . LYS D  2 43  ? 31.352  -63.173 12.360  1.00 95.27  ? 43   LYS B CA  1 
ATOM   6854  C C   . LYS D  2 43  ? 32.279  -61.967 12.495  1.00 88.01  ? 43   LYS B C   1 
ATOM   6855  O O   . LYS D  2 43  ? 31.837  -60.861 12.807  1.00 82.91  ? 43   LYS B O   1 
ATOM   6856  C CB  . LYS D  2 43  ? 31.026  -63.780 13.725  1.00 94.45  ? 43   LYS B CB  1 
ATOM   6857  C CG  . LYS D  2 43  ? 30.017  -64.917 13.643  1.00 98.29  ? 43   LYS B CG  1 
ATOM   6858  C CD  . LYS D  2 43  ? 29.677  -65.467 15.017  1.00 100.43 ? 43   LYS B CD  1 
ATOM   6859  C CE  . LYS D  2 43  ? 28.515  -66.451 14.947  1.00 100.62 ? 43   LYS B CE  1 
ATOM   6860  N NZ  . LYS D  2 43  ? 27.255  -65.821 14.466  1.00 98.82  ? 43   LYS B NZ  1 
ATOM   6861  N N   . ALA D  2 44  ? 33.566  -62.191 12.248  1.00 83.56  ? 44   ALA B N   1 
ATOM   6862  C CA  . ALA D  2 44  ? 34.538  -61.114 12.291  1.00 86.54  ? 44   ALA B CA  1 
ATOM   6863  C C   . ALA D  2 44  ? 34.578  -60.306 10.974  1.00 92.26  ? 44   ALA B C   1 
ATOM   6864  O O   . ALA D  2 44  ? 34.676  -59.078 11.017  1.00 93.23  ? 44   ALA B O   1 
ATOM   6865  C CB  . ALA D  2 44  ? 35.907  -61.663 12.622  1.00 88.03  ? 44   ALA B CB  1 
ATOM   6866  N N   . ILE D  2 45  ? 34.513  -60.959 9.811   1.00 90.17  ? 45   ILE B N   1 
ATOM   6867  C CA  . ILE D  2 45  ? 34.441  -60.189 8.565   1.00 88.42  ? 45   ILE B CA  1 
ATOM   6868  C C   . ILE D  2 45  ? 33.077  -59.512 8.443   1.00 87.13  ? 45   ILE B C   1 
ATOM   6869  O O   . ILE D  2 45  ? 32.985  -58.418 7.897   1.00 92.96  ? 45   ILE B O   1 
ATOM   6870  C CB  . ILE D  2 45  ? 34.703  -61.018 7.272   1.00 91.60  ? 45   ILE B CB  1 
ATOM   6871  C CG1 . ILE D  2 45  ? 34.103  -62.425 7.350   1.00 94.80  ? 45   ILE B CG1 1 
ATOM   6872  C CG2 . ILE D  2 45  ? 36.191  -61.047 6.938   1.00 91.32  ? 45   ILE B CG2 1 
ATOM   6873  C CD1 . ILE D  2 45  ? 34.416  -63.294 6.127   1.00 91.83  ? 45   ILE B CD1 1 
ATOM   6874  N N   . ASP D  2 46  ? 32.021  -60.155 8.937   1.00 85.47  ? 46   ASP B N   1 
ATOM   6875  C CA  . ASP D  2 46  ? 30.695  -59.537 8.916   1.00 86.02  ? 46   ASP B CA  1 
ATOM   6876  C C   . ASP D  2 46  ? 30.658  -58.301 9.829   1.00 85.99  ? 46   ASP B C   1 
ATOM   6877  O O   . ASP D  2 46  ? 29.974  -57.312 9.538   1.00 83.18  ? 46   ASP B O   1 
ATOM   6878  C CB  . ASP D  2 46  ? 29.613  -60.533 9.351   1.00 84.41  ? 46   ASP B CB  1 
ATOM   6879  C CG  . ASP D  2 46  ? 29.345  -61.603 8.312   1.00 90.88  ? 46   ASP B CG  1 
ATOM   6880  O OD1 . ASP D  2 46  ? 29.781  -61.443 7.147   1.00 90.63  ? 46   ASP B OD1 1 
ATOM   6881  O OD2 . ASP D  2 46  ? 28.673  -62.598 8.664   1.00 91.84  ? 46   ASP B OD2 1 
ATOM   6882  N N   . GLY D  2 47  ? 31.406  -58.366 10.930  1.00 86.93  ? 47   GLY B N   1 
ATOM   6883  C CA  . GLY D  2 47  ? 31.432  -57.297 11.913  1.00 79.72  ? 47   GLY B CA  1 
ATOM   6884  C C   . GLY D  2 47  ? 32.115  -56.041 11.419  1.00 78.24  ? 47   GLY B C   1 
ATOM   6885  O O   . GLY D  2 47  ? 31.618  -54.938 11.637  1.00 80.87  ? 47   GLY B O   1 
ATOM   6886  N N   . VAL D  2 48  ? 33.247  -56.199 10.743  1.00 76.43  ? 48   VAL B N   1 
ATOM   6887  C CA  . VAL D  2 48  ? 33.996  -55.042 10.268  1.00 77.54  ? 48   VAL B CA  1 
ATOM   6888  C C   . VAL D  2 48  ? 33.301  -54.458 9.027   1.00 77.52  ? 48   VAL B C   1 
ATOM   6889  O O   . VAL D  2 48  ? 33.318  -53.240 8.809   1.00 71.53  ? 48   VAL B O   1 
ATOM   6890  C CB  . VAL D  2 48  ? 35.467  -55.402 9.946   1.00 72.26  ? 48   VAL B CB  1 
ATOM   6891  C CG1 . VAL D  2 48  ? 36.229  -54.174 9.481   1.00 71.75  ? 48   VAL B CG1 1 
ATOM   6892  C CG2 . VAL D  2 48  ? 36.151  -55.981 11.164  1.00 71.69  ? 48   VAL B CG2 1 
ATOM   6893  N N   . THR D  2 49  ? 32.671  -55.334 8.240   1.00 76.87  ? 49   THR B N   1 
ATOM   6894  C CA  . THR D  2 49  ? 31.977  -54.942 7.012   1.00 76.59  ? 49   THR B CA  1 
ATOM   6895  C C   . THR D  2 49  ? 30.692  -54.178 7.311   1.00 79.02  ? 49   THR B C   1 
ATOM   6896  O O   . THR D  2 49  ? 30.337  -53.244 6.593   1.00 80.74  ? 49   THR B O   1 
ATOM   6897  C CB  . THR D  2 49  ? 31.627  -56.180 6.134   1.00 78.47  ? 49   THR B CB  1 
ATOM   6898  O OG1 . THR D  2 49  ? 32.831  -56.858 5.758   1.00 81.10  ? 49   THR B OG1 1 
ATOM   6899  C CG2 . THR D  2 49  ? 30.884  -55.772 4.865   1.00 78.31  ? 49   THR B CG2 1 
ATOM   6900  N N   . ASN D  2 50  ? 30.008  -54.551 8.387   1.00 81.23  ? 50   ASN B N   1 
ATOM   6901  C CA  . ASN D  2 50  ? 28.855  -53.785 8.840   1.00 78.18  ? 50   ASN B CA  1 
ATOM   6902  C C   . ASN D  2 50  ? 29.283  -52.424 9.360   1.00 77.34  ? 50   ASN B C   1 
ATOM   6903  O O   . ASN D  2 50  ? 28.603  -51.421 9.140   1.00 75.94  ? 50   ASN B O   1 
ATOM   6904  C CB  . ASN D  2 50  ? 28.088  -54.543 9.912   1.00 74.74  ? 50   ASN B CB  1 
ATOM   6905  C CG  . ASN D  2 50  ? 27.221  -55.635 9.334   1.00 82.58  ? 50   ASN B CG  1 
ATOM   6906  O OD1 . ASN D  2 50  ? 26.013  -55.454 9.172   1.00 88.36  ? 50   ASN B OD1 1 
ATOM   6907  N ND2 . ASN D  2 50  ? 27.829  -56.769 9.001   1.00 80.16  ? 50   ASN B ND2 1 
ATOM   6908  N N   . LYS D  2 51  ? 30.415  -52.407 10.057  1.00 75.63  ? 51   LYS B N   1 
ATOM   6909  C CA  . LYS D  2 51  ? 30.947  -51.180 10.628  1.00 75.86  ? 51   LYS B CA  1 
ATOM   6910  C C   . LYS D  2 51  ? 31.210  -50.146 9.551   1.00 76.11  ? 51   LYS B C   1 
ATOM   6911  O O   . LYS D  2 51  ? 30.805  -48.991 9.689   1.00 80.55  ? 51   LYS B O   1 
ATOM   6912  C CB  . LYS D  2 51  ? 32.237  -51.453 11.406  1.00 73.76  ? 51   LYS B CB  1 
ATOM   6913  C CG  . LYS D  2 51  ? 32.907  -50.189 11.912  1.00 66.58  ? 51   LYS B CG  1 
ATOM   6914  C CD  . LYS D  2 51  ? 34.201  -50.478 12.638  1.00 61.92  ? 51   LYS B CD  1 
ATOM   6915  C CE  . LYS D  2 51  ? 33.895  -51.111 13.986  1.00 64.22  ? 51   LYS B CE  1 
ATOM   6916  N NZ  . LYS D  2 51  ? 35.044  -51.046 14.919  1.00 66.35  ? 51   LYS B NZ  1 
ATOM   6917  N N   . VAL D  2 52  ? 31.910  -50.558 8.496   1.00 76.54  ? 52   VAL B N   1 
ATOM   6918  C CA  . VAL D  2 52  ? 32.282  -49.639 7.425   1.00 78.18  ? 52   VAL B CA  1 
ATOM   6919  C C   . VAL D  2 52  ? 31.051  -49.202 6.612   1.00 75.44  ? 52   VAL B C   1 
ATOM   6920  O O   . VAL D  2 52  ? 31.013  -48.100 6.078   1.00 76.83  ? 52   VAL B O   1 
ATOM   6921  C CB  . VAL D  2 52  ? 33.369  -50.249 6.487   1.00 75.09  ? 52   VAL B CB  1 
ATOM   6922  C CG1 . VAL D  2 52  ? 34.621  -50.607 7.290   1.00 67.15  ? 52   VAL B CG1 1 
ATOM   6923  C CG2 . VAL D  2 52  ? 32.837  -51.449 5.718   1.00 71.92  ? 52   VAL B CG2 1 
ATOM   6924  N N   . ASN D  2 53  ? 30.031  -50.046 6.534   1.00 74.35  ? 53   ASN B N   1 
ATOM   6925  C CA  . ASN D  2 53  ? 28.828  -49.646 5.822   1.00 75.61  ? 53   ASN B CA  1 
ATOM   6926  C C   . ASN D  2 53  ? 28.050  -48.624 6.671   1.00 79.06  ? 53   ASN B C   1 
ATOM   6927  O O   . ASN D  2 53  ? 27.535  -47.635 6.147   1.00 79.36  ? 53   ASN B O   1 
ATOM   6928  C CB  . ASN D  2 53  ? 27.942  -50.867 5.497   1.00 77.73  ? 53   ASN B CB  1 
ATOM   6929  C CG  . ASN D  2 53  ? 28.611  -51.867 4.540   1.00 81.41  ? 53   ASN B CG  1 
ATOM   6930  O OD1 . ASN D  2 53  ? 29.608  -51.558 3.878   1.00 83.69  ? 53   ASN B OD1 1 
ATOM   6931  N ND2 . ASN D  2 53  ? 28.033  -53.068 4.445   1.00 74.57  ? 53   ASN B ND2 1 
ATOM   6932  N N   . SER D  2 54  ? 28.004  -48.862 7.985   1.00 82.33  ? 54   SER B N   1 
ATOM   6933  C CA  . SER D  2 54  ? 27.363  -47.971 8.960   1.00 77.68  ? 54   SER B CA  1 
ATOM   6934  C C   . SER D  2 54  ? 28.057  -46.622 9.032   1.00 79.71  ? 54   SER B C   1 
ATOM   6935  O O   . SER D  2 54  ? 27.427  -45.599 9.305   1.00 78.47  ? 54   SER B O   1 
ATOM   6936  C CB  . SER D  2 54  ? 27.356  -48.596 10.363  1.00 76.61  ? 54   SER B CB  1 
ATOM   6937  O OG  . SER D  2 54  ? 26.437  -49.669 10.469  1.00 79.76  ? 54   SER B OG  1 
ATOM   6938  N N   . ILE D  2 55  ? 29.372  -46.650 8.835   1.00 81.91  ? 55   ILE B N   1 
ATOM   6939  C CA  . ILE D  2 55  ? 30.220  -45.463 8.917   1.00 81.25  ? 55   ILE B CA  1 
ATOM   6940  C C   . ILE D  2 55  ? 30.061  -44.554 7.692   1.00 83.29  ? 55   ILE B C   1 
ATOM   6941  O O   . ILE D  2 55  ? 30.151  -43.328 7.804   1.00 84.59  ? 55   ILE B O   1 
ATOM   6942  C CB  . ILE D  2 55  ? 31.728  -45.870 9.074   1.00 83.20  ? 55   ILE B CB  1 
ATOM   6943  C CG1 . ILE D  2 55  ? 32.454  -44.979 10.082  1.00 81.98  ? 55   ILE B CG1 1 
ATOM   6944  C CG2 . ILE D  2 55  ? 32.473  -45.882 7.729   1.00 77.97  ? 55   ILE B CG2 1 
ATOM   6945  C CD1 . ILE D  2 55  ? 32.663  -45.628 11.428  1.00 74.88  ? 55   ILE B CD1 1 
ATOM   6946  N N   . ILE D  2 56  ? 29.820  -45.164 6.531   1.00 84.87  ? 56   ILE B N   1 
ATOM   6947  C CA  . ILE D  2 56  ? 29.674  -44.439 5.272   1.00 82.62  ? 56   ILE B CA  1 
ATOM   6948  C C   . ILE D  2 56  ? 28.300  -43.799 5.079   1.00 82.43  ? 56   ILE B C   1 
ATOM   6949  O O   . ILE D  2 56  ? 28.197  -42.613 4.776   1.00 84.00  ? 56   ILE B O   1 
ATOM   6950  C CB  . ILE D  2 56  ? 29.966  -45.388 4.083   1.00 79.77  ? 56   ILE B CB  1 
ATOM   6951  C CG1 . ILE D  2 56  ? 31.449  -45.777 4.086   1.00 72.15  ? 56   ILE B CG1 1 
ATOM   6952  C CG2 . ILE D  2 56  ? 29.549  -44.754 2.760   1.00 73.66  ? 56   ILE B CG2 1 
ATOM   6953  C CD1 . ILE D  2 56  ? 31.812  -46.822 3.080   1.00 65.97  ? 56   ILE B CD1 1 
ATOM   6954  N N   . ASP D  2 57  ? 27.245  -44.573 5.300   1.00 83.61  ? 57   ASP B N   1 
ATOM   6955  C CA  . ASP D  2 57  ? 25.893  -44.073 5.091   1.00 86.66  ? 57   ASP B CA  1 
ATOM   6956  C C   . ASP D  2 57  ? 25.476  -43.080 6.187   1.00 89.84  ? 57   ASP B C   1 
ATOM   6957  O O   . ASP D  2 57  ? 24.515  -42.332 6.007   1.00 92.49  ? 57   ASP B O   1 
ATOM   6958  C CB  . ASP D  2 57  ? 24.890  -45.228 5.006   1.00 85.79  ? 57   ASP B CB  1 
ATOM   6959  C CG  . ASP D  2 57  ? 24.452  -45.719 6.374   1.00 91.64  ? 57   ASP B CG  1 
ATOM   6960  O OD1 . ASP D  2 57  ? 25.335  -46.044 7.202   1.00 91.44  ? 57   ASP B OD1 1 
ATOM   6961  O OD2 . ASP D  2 57  ? 23.223  -45.759 6.629   1.00 94.30  ? 57   ASP B OD2 1 
ATOM   6962  N N   . LYS D  2 58  ? 26.181  -43.074 7.320   1.00 84.69  ? 58   LYS B N   1 
ATOM   6963  C CA  . LYS D  2 58  ? 25.870  -42.121 8.385   1.00 80.49  ? 58   LYS B CA  1 
ATOM   6964  C C   . LYS D  2 58  ? 26.405  -40.735 8.021   1.00 86.50  ? 58   LYS B C   1 
ATOM   6965  O O   . LYS D  2 58  ? 26.113  -39.742 8.692   1.00 82.53  ? 58   LYS B O   1 
ATOM   6966  C CB  . LYS D  2 58  ? 26.460  -42.569 9.728   1.00 81.78  ? 58   LYS B CB  1 
ATOM   6967  C CG  . LYS D  2 58  ? 25.575  -43.491 10.537  1.00 80.50  ? 58   LYS B CG  1 
ATOM   6968  C CD  . LYS D  2 58  ? 24.181  -42.933 10.655  1.00 71.85  ? 58   LYS B CD  1 
ATOM   6969  C CE  . LYS D  2 58  ? 23.310  -43.855 11.456  1.00 63.35  ? 58   LYS B CE  1 
ATOM   6970  N NZ  . LYS D  2 58  ? 21.893  -43.633 11.091  1.00 66.21  ? 58   LYS B NZ  1 
ATOM   6971  N N   . MET D  2 59  ? 27.186  -40.677 6.947   1.00 87.48  ? 59   MET B N   1 
ATOM   6972  C CA  . MET D  2 59  ? 27.835  -39.444 6.527   1.00 83.18  ? 59   MET B CA  1 
ATOM   6973  C C   . MET D  2 59  ? 27.300  -38.972 5.181   1.00 80.67  ? 59   MET B C   1 
ATOM   6974  O O   . MET D  2 59  ? 27.744  -37.947 4.672   1.00 80.03  ? 59   MET B O   1 
ATOM   6975  C CB  . MET D  2 59  ? 29.349  -39.655 6.411   1.00 83.44  ? 59   MET B CB  1 
ATOM   6976  C CG  . MET D  2 59  ? 30.066  -40.085 7.684   1.00 77.17  ? 59   MET B CG  1 
ATOM   6977  S SD  . MET D  2 59  ? 30.337  -38.728 8.828   1.00 92.58  ? 59   MET B SD  1 
ATOM   6978  C CE  . MET D  2 59  ? 31.125  -37.517 7.762   1.00 70.65  ? 59   MET B CE  1 
ATOM   6979  N N   . ASN D  2 60  ? 26.352  -39.715 4.605   1.00 80.98  ? 60   ASN B N   1 
ATOM   6980  C CA  . ASN D  2 60  ? 25.863  -39.408 3.258   1.00 86.05  ? 60   ASN B CA  1 
ATOM   6981  C C   . ASN D  2 60  ? 25.041  -38.113 3.231   1.00 88.56  ? 60   ASN B C   1 
ATOM   6982  O O   . ASN D  2 60  ? 24.978  -37.425 2.200   1.00 91.91  ? 60   ASN B O   1 
ATOM   6983  C CB  . ASN D  2 60  ? 25.056  -40.586 2.670   1.00 86.11  ? 60   ASN B CB  1 
ATOM   6984  C CG  . ASN D  2 60  ? 23.690  -40.771 3.322   1.00 90.65  ? 60   ASN B CG  1 
ATOM   6985  O OD1 . ASN D  2 60  ? 23.477  -40.415 4.483   1.00 93.08  ? 60   ASN B OD1 1 
ATOM   6986  N ND2 . ASN D  2 60  ? 22.760  -41.358 2.571   1.00 85.53  ? 60   ASN B ND2 1 
ATOM   6987  N N   . THR D  2 61  ? 24.422  -37.777 4.362   1.00 82.62  ? 61   THR B N   1 
ATOM   6988  C CA  . THR D  2 61  ? 23.752  -36.491 4.500   1.00 76.91  ? 61   THR B CA  1 
ATOM   6989  C C   . THR D  2 61  ? 24.653  -35.537 5.280   1.00 76.17  ? 61   THR B C   1 
ATOM   6990  O O   . THR D  2 61  ? 24.747  -35.578 6.507   1.00 74.28  ? 61   THR B O   1 
ATOM   6991  C CB  . THR D  2 61  ? 22.392  -36.613 5.195   1.00 81.76  ? 61   THR B CB  1 
ATOM   6992  O OG1 . THR D  2 61  ? 22.016  -35.333 5.717   1.00 78.34  ? 61   THR B OG1 1 
ATOM   6993  C CG2 . THR D  2 61  ? 22.448  -37.637 6.334   1.00 85.19  ? 61   THR B CG2 1 
ATOM   6994  N N   . GLN D  2 62  ? 25.326  -34.679 4.533   1.00 80.35  ? 62   GLN B N   1 
ATOM   6995  C CA  . GLN D  2 62  ? 26.344  -33.802 5.082   1.00 72.59  ? 62   GLN B CA  1 
ATOM   6996  C C   . GLN D  2 62  ? 26.396  -32.495 4.283   1.00 71.43  ? 62   GLN B C   1 
ATOM   6997  O O   . GLN D  2 62  ? 26.031  -32.464 3.102   1.00 75.08  ? 62   GLN B O   1 
ATOM   6998  C CB  . GLN D  2 62  ? 27.697  -34.519 5.087   1.00 68.71  ? 62   GLN B CB  1 
ATOM   6999  C CG  . GLN D  2 62  ? 28.919  -33.607 4.983   1.00 70.46  ? 62   GLN B CG  1 
ATOM   7000  C CD  . GLN D  2 62  ? 30.221  -34.373 5.093   1.00 75.81  ? 62   GLN B CD  1 
ATOM   7001  O OE1 . GLN D  2 62  ? 30.240  -35.513 5.574   1.00 77.13  ? 62   GLN B OE1 1 
ATOM   7002  N NE2 . GLN D  2 62  ? 31.320  -33.753 4.661   1.00 67.42  ? 62   GLN B NE2 1 
ATOM   7003  N N   . PHE D  2 63  ? 26.842  -31.426 4.938   1.00 63.48  ? 63   PHE B N   1 
ATOM   7004  C CA  . PHE D  2 63  ? 26.836  -30.087 4.366   1.00 62.61  ? 63   PHE B CA  1 
ATOM   7005  C C   . PHE D  2 63  ? 27.546  -29.958 3.027   1.00 63.94  ? 63   PHE B C   1 
ATOM   7006  O O   . PHE D  2 63  ? 28.678  -30.410 2.848   1.00 71.04  ? 63   PHE B O   1 
ATOM   7007  C CB  . PHE D  2 63  ? 27.470  -29.117 5.348   1.00 58.32  ? 63   PHE B CB  1 
ATOM   7008  C CG  . PHE D  2 63  ? 27.485  -27.712 4.867   1.00 57.25  ? 63   PHE B CG  1 
ATOM   7009  C CD1 . PHE D  2 63  ? 26.360  -26.905 5.017   1.00 58.22  ? 63   PHE B CD1 1 
ATOM   7010  C CD2 . PHE D  2 63  ? 28.628  -27.183 4.276   1.00 52.66  ? 63   PHE B CD2 1 
ATOM   7011  C CE1 . PHE D  2 63  ? 26.369  -25.580 4.578   1.00 56.29  ? 63   PHE B CE1 1 
ATOM   7012  C CE2 . PHE D  2 63  ? 28.657  -25.865 3.837   1.00 55.46  ? 63   PHE B CE2 1 
ATOM   7013  C CZ  . PHE D  2 63  ? 27.520  -25.054 3.989   1.00 51.88  ? 63   PHE B CZ  1 
ATOM   7014  N N   . GLU D  2 64  ? 26.883  -29.273 2.108   1.00 60.01  ? 64   GLU B N   1 
ATOM   7015  C CA  . GLU D  2 64  ? 27.442  -29.018 0.802   1.00 55.78  ? 64   GLU B CA  1 
ATOM   7016  C C   . GLU D  2 64  ? 27.530  -27.510 0.620   1.00 54.20  ? 64   GLU B C   1 
ATOM   7017  O O   . GLU D  2 64  ? 26.536  -26.795 0.804   1.00 55.51  ? 64   GLU B O   1 
ATOM   7018  C CB  . GLU D  2 64  ? 26.570  -29.662 -0.287  1.00 57.75  ? 64   GLU B CB  1 
ATOM   7019  C CG  . GLU D  2 64  ? 26.355  -31.168 -0.087  1.00 71.50  ? 64   GLU B CG  1 
ATOM   7020  C CD  . GLU D  2 64  ? 25.705  -31.872 -1.281  1.00 84.35  ? 64   GLU B CD  1 
ATOM   7021  O OE1 . GLU D  2 64  ? 25.195  -31.176 -2.192  1.00 84.37  ? 64   GLU B OE1 1 
ATOM   7022  O OE2 . GLU D  2 64  ? 25.704  -33.129 -1.293  1.00 82.76  ? 64   GLU B OE2 1 
ATOM   7023  N N   . ALA D  2 65  ? 28.709  -27.024 0.248   1.00 48.10  ? 65   ALA B N   1 
ATOM   7024  C CA  . ALA D  2 65  ? 28.914  -25.588 0.082   1.00 48.76  ? 65   ALA B CA  1 
ATOM   7025  C C   . ALA D  2 65  ? 28.390  -25.125 -1.285  1.00 49.48  ? 65   ALA B C   1 
ATOM   7026  O O   . ALA D  2 65  ? 28.467  -25.864 -2.263  1.00 46.92  ? 65   ALA B O   1 
ATOM   7027  C CB  . ALA D  2 65  ? 30.391  -25.237 0.240   1.00 44.04  ? 65   ALA B CB  1 
ATOM   7028  N N   . VAL D  2 66  ? 27.838  -23.911 -1.333  1.00 53.53  ? 66   VAL B N   1 
ATOM   7029  C CA  . VAL D  2 66  ? 27.369  -23.282 -2.580  1.00 51.65  ? 66   VAL B CA  1 
ATOM   7030  C C   . VAL D  2 66  ? 28.075  -21.941 -2.773  1.00 48.55  ? 66   VAL B C   1 
ATOM   7031  O O   . VAL D  2 66  ? 28.264  -21.199 -1.803  1.00 52.87  ? 66   VAL B O   1 
ATOM   7032  C CB  . VAL D  2 66  ? 25.818  -23.012 -2.555  1.00 52.47  ? 66   VAL B CB  1 
ATOM   7033  C CG1 . VAL D  2 66  ? 25.303  -22.549 -3.932  1.00 39.07  ? 66   VAL B CG1 1 
ATOM   7034  C CG2 . VAL D  2 66  ? 25.031  -24.226 -2.012  1.00 49.74  ? 66   VAL B CG2 1 
ATOM   7035  N N   . GLY D  2 67  ? 28.463  -21.600 -3.995  1.00 42.11  ? 67   GLY B N   1 
ATOM   7036  C CA  . GLY D  2 67  ? 29.081  -20.295 -4.192  1.00 42.52  ? 67   GLY B CA  1 
ATOM   7037  C C   . GLY D  2 67  ? 28.006  -19.209 -4.165  1.00 45.57  ? 67   GLY B C   1 
ATOM   7038  O O   . GLY D  2 67  ? 26.949  -19.384 -4.784  1.00 46.00  ? 67   GLY B O   1 
ATOM   7039  N N   . ARG D  2 68  ? 28.237  -18.118 -3.430  1.00 40.30  ? 68   ARG B N   1 
ATOM   7040  C CA  . ARG D  2 68  ? 27.339  -16.949 -3.462  1.00 34.87  ? 68   ARG B CA  1 
ATOM   7041  C C   . ARG D  2 68  ? 28.181  -15.701 -3.554  1.00 34.91  ? 68   ARG B C   1 
ATOM   7042  O O   . ARG D  2 68  ? 29.221  -15.607 -2.879  1.00 41.48  ? 68   ARG B O   1 
ATOM   7043  C CB  . ARG D  2 68  ? 26.450  -16.854 -2.214  1.00 39.51  ? 68   ARG B CB  1 
ATOM   7044  C CG  . ARG D  2 68  ? 25.587  -18.048 -1.929  1.00 39.98  ? 68   ARG B CG  1 
ATOM   7045  C CD  . ARG D  2 68  ? 24.787  -17.855 -0.662  1.00 34.77  ? 68   ARG B CD  1 
ATOM   7046  N NE  . ARG D  2 68  ? 24.045  -19.073 -0.385  1.00 34.16  ? 68   ARG B NE  1 
ATOM   7047  C CZ  . ARG D  2 68  ? 24.532  -20.072 0.341   1.00 41.94  ? 68   ARG B CZ  1 
ATOM   7048  N NH1 . ARG D  2 68  ? 25.742  -19.973 0.886   1.00 43.02  ? 68   ARG B NH1 1 
ATOM   7049  N NH2 . ARG D  2 68  ? 23.819  -21.172 0.528   1.00 43.67  ? 68   ARG B NH2 1 
ATOM   7050  N N   . GLU D  2 69  ? 27.698  -14.701 -4.282  1.00 29.01  ? 69   GLU B N   1 
ATOM   7051  C CA  . GLU D  2 69  ? 28.485  -13.491 -4.469  1.00 27.71  ? 69   GLU B CA  1 
ATOM   7052  C C   . GLU D  2 69  ? 27.849  -12.267 -3.793  1.00 25.80  ? 69   GLU B C   1 
ATOM   7053  O O   . GLU D  2 69  ? 26.625  -12.211 -3.601  1.00 24.36  ? 69   GLU B O   1 
ATOM   7054  C CB  . GLU D  2 69  ? 28.684  -13.228 -5.960  1.00 33.88  ? 69   GLU B CB  1 
ATOM   7055  C CG  . GLU D  2 69  ? 28.882  -14.489 -6.778  1.00 39.31  ? 69   GLU B CG  1 
ATOM   7056  C CD  . GLU D  2 69  ? 29.801  -14.274 -7.968  1.00 46.81  ? 69   GLU B CD  1 
ATOM   7057  O OE1 . GLU D  2 69  ? 30.929  -13.761 -7.767  1.00 49.99  ? 69   GLU B OE1 1 
ATOM   7058  O OE2 . GLU D  2 69  ? 29.384  -14.609 -9.099  1.00 46.66  ? 69   GLU B OE2 1 
ATOM   7059  N N   . PHE D  2 70  ? 28.687  -11.300 -3.415  1.00 24.43  ? 70   PHE B N   1 
ATOM   7060  C CA  . PHE D  2 70  ? 28.224  -10.124 -2.689  1.00 25.87  ? 70   PHE B CA  1 
ATOM   7061  C C   . PHE D  2 70  ? 28.951  -8.886  -3.176  1.00 25.07  ? 70   PHE B C   1 
ATOM   7062  O O   . PHE D  2 70  ? 30.153  -8.948  -3.417  1.00 27.65  ? 70   PHE B O   1 
ATOM   7063  C CB  . PHE D  2 70  ? 28.454  -10.331 -1.174  1.00 24.03  ? 70   PHE B CB  1 
ATOM   7064  C CG  . PHE D  2 70  ? 27.717  -11.527 -0.610  1.00 22.45  ? 70   PHE B CG  1 
ATOM   7065  C CD1 . PHE D  2 70  ? 28.305  -12.790 -0.610  1.00 27.40  ? 70   PHE B CD1 1 
ATOM   7066  C CD2 . PHE D  2 70  ? 26.416  -11.400 -0.134  1.00 20.75  ? 70   PHE B CD2 1 
ATOM   7067  C CE1 . PHE D  2 70  ? 27.611  -13.926 -0.112  1.00 28.97  ? 70   PHE B CE1 1 
ATOM   7068  C CE2 . PHE D  2 70  ? 25.705  -12.519 0.359   1.00 25.34  ? 70   PHE B CE2 1 
ATOM   7069  C CZ  . PHE D  2 70  ? 26.306  -13.789 0.374   1.00 26.62  ? 70   PHE B CZ  1 
ATOM   7070  N N   . ASN D  2 71  ? 28.287  -7.732  -3.222  1.00 24.67  ? 71   ASN B N   1 
ATOM   7071  C CA  . ASN D  2 71  ? 28.989  -6.529  -3.677  1.00 25.54  ? 71   ASN B CA  1 
ATOM   7072  C C   . ASN D  2 71  ? 29.751  -5.814  -2.541  1.00 30.51  ? 71   ASN B C   1 
ATOM   7073  O O   . ASN D  2 71  ? 29.851  -6.313  -1.404  1.00 29.37  ? 71   ASN B O   1 
ATOM   7074  C CB  . ASN D  2 71  ? 28.006  -5.584  -4.374  1.00 24.89  ? 71   ASN B CB  1 
ATOM   7075  C CG  . ASN D  2 71  ? 26.983  -4.993  -3.428  1.00 31.26  ? 71   ASN B CG  1 
ATOM   7076  O OD1 . ASN D  2 71  ? 27.324  -4.361  -2.416  1.00 28.38  ? 71   ASN B OD1 1 
ATOM   7077  N ND2 . ASN D  2 71  ? 25.708  -5.262  -3.713  1.00 31.44  ? 71   ASN B ND2 1 
ATOM   7078  N N   . ASN D  2 72  ? 30.294  -4.650  -2.845  1.00 27.35  ? 72   ASN B N   1 
ATOM   7079  C CA  . ASN D  2 72  ? 31.245  -4.027  -1.946  1.00 29.42  ? 72   ASN B CA  1 
ATOM   7080  C C   . ASN D  2 72  ? 30.659  -3.430  -0.665  1.00 30.76  ? 72   ASN B C   1 
ATOM   7081  O O   . ASN D  2 72  ? 31.400  -3.182  0.301   1.00 32.39  ? 72   ASN B O   1 
ATOM   7082  C CB  . ASN D  2 72  ? 32.002  -2.935  -2.703  1.00 35.45  ? 72   ASN B CB  1 
ATOM   7083  C CG  . ASN D  2 72  ? 33.258  -2.501  -1.983  1.00 41.38  ? 72   ASN B CG  1 
ATOM   7084  O OD1 . ASN D  2 72  ? 33.996  -3.331  -1.402  1.00 43.14  ? 72   ASN B OD1 1 
ATOM   7085  N ND2 . ASN D  2 72  ? 33.490  -1.188  -1.966  1.00 31.70  ? 72   ASN B ND2 1 
ATOM   7086  N N   . LEU D  2 73  ? 29.344  -3.236  -0.631  1.00 27.59  ? 73   LEU B N   1 
ATOM   7087  C CA  . LEU D  2 73  ? 28.694  -2.744  0.582   1.00 23.31  ? 73   LEU B CA  1 
ATOM   7088  C C   . LEU D  2 73  ? 27.799  -3.846  1.192   1.00 25.34  ? 73   LEU B C   1 
ATOM   7089  O O   . LEU D  2 73  ? 26.826  -3.565  1.907   1.00 27.75  ? 73   LEU B O   1 
ATOM   7090  C CB  . LEU D  2 73  ? 27.900  -1.467  0.282   1.00 21.86  ? 73   LEU B CB  1 
ATOM   7091  C CG  . LEU D  2 73  ? 28.706  -0.159  0.117   1.00 25.93  ? 73   LEU B CG  1 
ATOM   7092  C CD1 . LEU D  2 73  ? 27.922  0.997   -0.599  1.00 19.34  ? 73   LEU B CD1 1 
ATOM   7093  C CD2 . LEU D  2 73  ? 29.189  0.329   1.456   1.00 24.28  ? 73   LEU B CD2 1 
ATOM   7094  N N   . GLU D  2 74  ? 28.172  -5.098  0.928   1.00 22.85  ? 74   GLU B N   1 
ATOM   7095  C CA  . GLU D  2 74  ? 27.585  -6.264  1.568   1.00 22.86  ? 74   GLU B CA  1 
ATOM   7096  C C   . GLU D  2 74  ? 28.703  -7.063  2.301   1.00 25.28  ? 74   GLU B C   1 
ATOM   7097  O O   . GLU D  2 74  ? 28.672  -8.300  2.353   1.00 23.60  ? 74   GLU B O   1 
ATOM   7098  C CB  . GLU D  2 74  ? 26.855  -7.152  0.527   1.00 23.06  ? 74   GLU B CB  1 
ATOM   7099  C CG  . GLU D  2 74  ? 25.523  -6.552  0.021   1.00 25.51  ? 74   GLU B CG  1 
ATOM   7100  C CD  . GLU D  2 74  ? 24.843  -7.294  -1.183  1.00 31.95  ? 74   GLU B CD  1 
ATOM   7101  O OE1 . GLU D  2 74  ? 25.535  -7.860  -2.092  1.00 26.15  ? 74   GLU B OE1 1 
ATOM   7102  O OE2 . GLU D  2 74  ? 23.579  -7.283  -1.195  1.00 27.95  ? 74   GLU B OE2 1 
ATOM   7103  N N   . ARG D  2 75  ? 29.680  -6.363  2.890   1.00 25.49  ? 75   ARG B N   1 
ATOM   7104  C CA  . ARG D  2 75  ? 30.803  -7.076  3.512   1.00 25.97  ? 75   ARG B CA  1 
ATOM   7105  C C   . ARG D  2 75  ? 30.339  -7.880  4.716   1.00 26.50  ? 75   ARG B C   1 
ATOM   7106  O O   . ARG D  2 75  ? 30.857  -8.949  4.956   1.00 28.68  ? 75   ARG B O   1 
ATOM   7107  C CB  . ARG D  2 75  ? 31.946  -6.137  3.933   1.00 27.65  ? 75   ARG B CB  1 
ATOM   7108  C CG  . ARG D  2 75  ? 32.673  -5.459  2.775   1.00 26.65  ? 75   ARG B CG  1 
ATOM   7109  C CD  . ARG D  2 75  ? 33.114  -6.489  1.772   1.00 33.34  ? 75   ARG B CD  1 
ATOM   7110  N NE  . ARG D  2 75  ? 33.912  -5.975  0.660   1.00 42.40  ? 75   ARG B NE  1 
ATOM   7111  C CZ  . ARG D  2 75  ? 33.996  -6.611  -0.509  1.00 40.00  ? 75   ARG B CZ  1 
ATOM   7112  N NH1 . ARG D  2 75  ? 33.281  -7.731  -0.681  1.00 35.52  ? 75   ARG B NH1 1 
ATOM   7113  N NH2 . ARG D  2 75  ? 34.736  -6.118  -1.510  1.00 30.34  ? 75   ARG B NH2 1 
ATOM   7114  N N   . ARG D  2 76  ? 29.361  -7.371  5.464   1.00 26.83  ? 76   ARG B N   1 
ATOM   7115  C CA  . ARG D  2 76  ? 28.835  -8.085  6.627   1.00 24.70  ? 76   ARG B CA  1 
ATOM   7116  C C   . ARG D  2 76  ? 28.196  -9.431  6.272   1.00 25.79  ? 76   ARG B C   1 
ATOM   7117  O O   . ARG D  2 76  ? 28.473  -10.435 6.929   1.00 27.07  ? 76   ARG B O   1 
ATOM   7118  C CB  . ARG D  2 76  ? 27.803  -7.234  7.364   1.00 22.13  ? 76   ARG B CB  1 
ATOM   7119  C CG  . ARG D  2 76  ? 28.365  -6.051  8.109   1.00 20.36  ? 76   ARG B CG  1 
ATOM   7120  C CD  . ARG D  2 76  ? 27.235  -5.172  8.660   1.00 21.14  ? 76   ARG B CD  1 
ATOM   7121  N NE  . ARG D  2 76  ? 26.410  -4.627  7.586   1.00 24.09  ? 76   ARG B NE  1 
ATOM   7122  C CZ  . ARG D  2 76  ? 25.142  -4.242  7.726   1.00 26.04  ? 76   ARG B CZ  1 
ATOM   7123  N NH1 . ARG D  2 76  ? 24.540  -4.295  8.916   1.00 25.95  ? 76   ARG B NH1 1 
ATOM   7124  N NH2 . ARG D  2 76  ? 24.476  -3.786  6.668   1.00 23.51  ? 76   ARG B NH2 1 
ATOM   7125  N N   . ILE D  2 77  ? 27.346  -9.476  5.248   1.00 25.70  ? 77   ILE B N   1 
ATOM   7126  C CA  . ILE D  2 77  ? 26.709  -10.757 4.950   1.00 29.77  ? 77   ILE B CA  1 
ATOM   7127  C C   . ILE D  2 77  ? 27.655  -11.665 4.152   1.00 30.37  ? 77   ILE B C   1 
ATOM   7128  O O   . ILE D  2 77  ? 27.549  -12.907 4.254   1.00 27.93  ? 77   ILE B O   1 
ATOM   7129  C CB  . ILE D  2 77  ? 25.331  -10.595 4.216   1.00 23.51  ? 77   ILE B CB  1 
ATOM   7130  C CG1 . ILE D  2 77  ? 25.469  -9.724  2.992   1.00 28.78  ? 77   ILE B CG1 1 
ATOM   7131  C CG2 . ILE D  2 77  ? 24.292  -9.937  5.127   1.00 20.82  ? 77   ILE B CG2 1 
ATOM   7132  C CD1 . ILE D  2 77  ? 24.121  -9.549  2.253   1.00 29.33  ? 77   ILE B CD1 1 
ATOM   7133  N N   . GLU D  2 78  ? 28.620  -11.069 3.439   1.00 27.44  ? 78   GLU B N   1 
ATOM   7134  C CA  . GLU D  2 78  ? 29.665  -11.864 2.774   1.00 28.88  ? 78   GLU B CA  1 
ATOM   7135  C C   . GLU D  2 78  ? 30.456  -12.672 3.803   1.00 34.16  ? 78   GLU B C   1 
ATOM   7136  O O   . GLU D  2 78  ? 30.770  -13.876 3.595   1.00 29.19  ? 78   GLU B O   1 
ATOM   7137  C CB  . GLU D  2 78  ? 30.640  -10.964 2.014   1.00 26.19  ? 78   GLU B CB  1 
ATOM   7138  C CG  . GLU D  2 78  ? 31.833  -11.692 1.382   1.00 24.51  ? 78   GLU B CG  1 
ATOM   7139  C CD  . GLU D  2 78  ? 32.753  -10.724 0.638   1.00 40.29  ? 78   GLU B CD  1 
ATOM   7140  O OE1 . GLU D  2 78  ? 33.234  -9.765  1.282   1.00 45.10  ? 78   GLU B OE1 1 
ATOM   7141  O OE2 . GLU D  2 78  ? 32.928  -10.851 -0.604  1.00 38.53  ? 78   GLU B OE2 1 
ATOM   7142  N N   . ASN D  2 79  ? 30.743  -11.992 4.918   1.00 28.51  ? 79   ASN B N   1 
ATOM   7143  C CA  . ASN D  2 79  ? 31.492  -12.537 6.041   1.00 28.17  ? 79   ASN B CA  1 
ATOM   7144  C C   . ASN D  2 79  ? 30.682  -13.581 6.806   1.00 31.84  ? 79   ASN B C   1 
ATOM   7145  O O   . ASN D  2 79  ? 31.208  -14.631 7.178   1.00 33.88  ? 79   ASN B O   1 
ATOM   7146  C CB  . ASN D  2 79  ? 31.901  -11.390 6.963   1.00 31.83  ? 79   ASN B CB  1 
ATOM   7147  C CG  . ASN D  2 79  ? 32.837  -11.820 8.074   1.00 39.62  ? 79   ASN B CG  1 
ATOM   7148  O OD1 . ASN D  2 79  ? 32.467  -11.782 9.243   1.00 42.31  ? 79   ASN B OD1 1 
ATOM   7149  N ND2 . ASN D  2 79  ? 34.062  -12.186 7.723   1.00 42.82  ? 79   ASN B ND2 1 
ATOM   7150  N N   . LEU D  2 80  ? 29.389  -13.312 6.982   1.00 29.35  ? 80   LEU B N   1 
ATOM   7151  C CA  . LEU D  2 80  ? 28.467  -14.285 7.556   1.00 29.21  ? 80   LEU B CA  1 
ATOM   7152  C C   . LEU D  2 80  ? 28.446  -15.594 6.729   1.00 33.06  ? 80   LEU B C   1 
ATOM   7153  O O   . LEU D  2 80  ? 28.532  -16.699 7.283   1.00 29.82  ? 80   LEU B O   1 
ATOM   7154  C CB  . LEU D  2 80  ? 27.061  -13.677 7.668   1.00 26.17  ? 80   LEU B CB  1 
ATOM   7155  C CG  . LEU D  2 80  ? 26.041  -14.335 8.608   1.00 29.83  ? 80   LEU B CG  1 
ATOM   7156  C CD1 . LEU D  2 80  ? 24.952  -13.370 9.060   1.00 24.92  ? 80   LEU B CD1 1 
ATOM   7157  C CD2 . LEU D  2 80  ? 25.400  -15.555 7.923   1.00 30.07  ? 80   LEU B CD2 1 
ATOM   7158  N N   . ASN D  2 81  ? 28.323  -15.460 5.413   1.00 28.26  ? 81   ASN B N   1 
ATOM   7159  C CA  . ASN D  2 81  ? 28.275  -16.609 4.530   1.00 30.43  ? 81   ASN B CA  1 
ATOM   7160  C C   . ASN D  2 81  ? 29.543  -17.473 4.666   1.00 30.38  ? 81   ASN B C   1 
ATOM   7161  O O   . ASN D  2 81  ? 29.486  -18.708 4.688   1.00 30.84  ? 81   ASN B O   1 
ATOM   7162  C CB  . ASN D  2 81  ? 28.098  -16.127 3.093   1.00 31.63  ? 81   ASN B CB  1 
ATOM   7163  C CG  . ASN D  2 81  ? 27.918  -17.255 2.108   1.00 31.33  ? 81   ASN B CG  1 
ATOM   7164  O OD1 . ASN D  2 81  ? 26.836  -17.815 1.979   1.00 34.92  ? 81   ASN B OD1 1 
ATOM   7165  N ND2 . ASN D  2 81  ? 28.978  -17.584 1.391   1.00 34.60  ? 81   ASN B ND2 1 
ATOM   7166  N N   . LYS D  2 82  ? 30.683  -16.805 4.780   1.00 32.10  ? 82   LYS B N   1 
ATOM   7167  C CA  . LYS D  2 82  ? 31.983  -17.472 4.877   1.00 34.02  ? 82   LYS B CA  1 
ATOM   7168  C C   . LYS D  2 82  ? 32.162  -18.219 6.200   1.00 38.41  ? 82   LYS B C   1 
ATOM   7169  O O   . LYS D  2 82  ? 32.621  -19.352 6.201   1.00 39.46  ? 82   LYS B O   1 
ATOM   7170  C CB  . LYS D  2 82  ? 33.108  -16.443 4.689   1.00 36.17  ? 82   LYS B CB  1 
ATOM   7171  C CG  . LYS D  2 82  ? 34.537  -16.940 4.888   1.00 35.78  ? 82   LYS B CG  1 
ATOM   7172  C CD  . LYS D  2 82  ? 34.956  -17.977 3.852   1.00 56.84  ? 82   LYS B CD  1 
ATOM   7173  C CE  . LYS D  2 82  ? 36.419  -17.785 3.428   1.00 63.08  ? 82   LYS B CE  1 
ATOM   7174  N NZ  . LYS D  2 82  ? 37.245  -17.175 4.529   1.00 54.23  ? 82   LYS B NZ  1 
ATOM   7175  N N   . LYS D  2 83  ? 31.767  -17.608 7.315   1.00 34.46  ? 83   LYS B N   1 
ATOM   7176  C CA  . LYS D  2 83  ? 31.899  -18.244 8.628   1.00 37.11  ? 83   LYS B CA  1 
ATOM   7177  C C   . LYS D  2 83  ? 30.972  -19.442 8.812   1.00 36.38  ? 83   LYS B C   1 
ATOM   7178  O O   . LYS D  2 83  ? 31.317  -20.421 9.482   1.00 41.10  ? 83   LYS B O   1 
ATOM   7179  C CB  . LYS D  2 83  ? 31.603  -17.228 9.727   1.00 36.21  ? 83   LYS B CB  1 
ATOM   7180  C CG  . LYS D  2 83  ? 32.709  -16.240 9.923   1.00 44.66  ? 83   LYS B CG  1 
ATOM   7181  C CD  . LYS D  2 83  ? 33.902  -16.890 10.609  1.00 61.46  ? 83   LYS B CD  1 
ATOM   7182  C CE  . LYS D  2 83  ? 33.512  -17.390 12.015  1.00 59.22  ? 83   LYS B CE  1 
ATOM   7183  N NZ  . LYS D  2 83  ? 34.665  -17.993 12.777  1.00 58.79  ? 83   LYS B NZ  1 
ATOM   7184  N N   . MET D  2 84  ? 29.802  -19.360 8.199   1.00 31.76  ? 84   MET B N   1 
ATOM   7185  C CA  . MET D  2 84  ? 28.831  -20.419 8.280   1.00 34.06  ? 84   MET B CA  1 
ATOM   7186  C C   . MET D  2 84  ? 29.293  -21.641 7.500   1.00 40.83  ? 84   MET B C   1 
ATOM   7187  O O   . MET D  2 84  ? 29.179  -22.770 7.981   1.00 37.32  ? 84   MET B O   1 
ATOM   7188  C CB  . MET D  2 84  ? 27.493  -19.937 7.734   1.00 30.95  ? 84   MET B CB  1 
ATOM   7189  C CG  . MET D  2 84  ? 26.372  -20.931 7.895   1.00 38.72  ? 84   MET B CG  1 
ATOM   7190  S SD  . MET D  2 84  ? 25.284  -20.985 6.460   1.00 44.29  ? 84   MET B SD  1 
ATOM   7191  C CE  . MET D  2 84  ? 26.200  -22.050 5.384   1.00 50.16  ? 84   MET B CE  1 
ATOM   7192  N N   . GLU D  2 85  ? 29.812  -21.407 6.290   1.00 42.24  ? 85   GLU B N   1 
ATOM   7193  C CA  . GLU D  2 85  ? 30.273  -22.507 5.449   1.00 43.75  ? 85   GLU B CA  1 
ATOM   7194  C C   . GLU D  2 85  ? 31.591  -23.114 5.981   1.00 43.91  ? 85   GLU B C   1 
ATOM   7195  O O   . GLU D  2 85  ? 31.712  -24.335 6.058   1.00 44.24  ? 85   GLU B O   1 
ATOM   7196  C CB  . GLU D  2 85  ? 30.398  -22.055 3.978   1.00 43.89  ? 85   GLU B CB  1 
ATOM   7197  C CG  . GLU D  2 85  ? 29.028  -21.767 3.304   1.00 45.64  ? 85   GLU B CG  1 
ATOM   7198  C CD  . GLU D  2 85  ? 29.003  -21.937 1.776   1.00 50.42  ? 85   GLU B CD  1 
ATOM   7199  O OE1 . GLU D  2 85  ? 30.015  -21.634 1.105   1.00 53.32  ? 85   GLU B OE1 1 
ATOM   7200  O OE2 . GLU D  2 85  ? 27.952  -22.363 1.242   1.00 49.00  ? 85   GLU B OE2 1 
ATOM   7201  N N   . ASP D  2 86  ? 32.557  -22.278 6.361   1.00 39.45  ? 86   ASP B N   1 
ATOM   7202  C CA  . ASP D  2 86  ? 33.771  -22.747 7.046   1.00 40.41  ? 86   ASP B CA  1 
ATOM   7203  C C   . ASP D  2 86  ? 33.393  -23.466 8.347   1.00 47.85  ? 86   ASP B C   1 
ATOM   7204  O O   . ASP D  2 86  ? 34.031  -24.441 8.748   1.00 49.86  ? 86   ASP B O   1 
ATOM   7205  C CB  . ASP D  2 86  ? 34.719  -21.579 7.374   1.00 39.67  ? 86   ASP B CB  1 
ATOM   7206  C CG  . ASP D  2 86  ? 35.503  -21.073 6.153   1.00 52.59  ? 86   ASP B CG  1 
ATOM   7207  O OD1 . ASP D  2 86  ? 35.244  -21.529 5.010   1.00 51.62  ? 86   ASP B OD1 1 
ATOM   7208  O OD2 . ASP D  2 86  ? 36.367  -20.183 6.342   1.00 53.86  ? 86   ASP B OD2 1 
ATOM   7209  N N   . GLY D  2 87  ? 32.357  -22.967 9.015   1.00 44.15  ? 87   GLY B N   1 
ATOM   7210  C CA  . GLY D  2 87  ? 31.933  -23.544 10.267  1.00 37.95  ? 87   GLY B CA  1 
ATOM   7211  C C   . GLY D  2 87  ? 31.431  -24.965 10.113  1.00 44.04  ? 87   GLY B C   1 
ATOM   7212  O O   . GLY D  2 87  ? 31.765  -25.817 10.926  1.00 49.67  ? 87   GLY B O   1 
ATOM   7213  N N   . PHE D  2 88  ? 30.629  -25.232 9.087   1.00 42.97  ? 88   PHE B N   1 
ATOM   7214  C CA  . PHE D  2 88  ? 30.094  -26.576 8.897   1.00 46.78  ? 88   PHE B CA  1 
ATOM   7215  C C   . PHE D  2 88  ? 31.184  -27.533 8.411   1.00 50.96  ? 88   PHE B C   1 
ATOM   7216  O O   . PHE D  2 88  ? 31.138  -28.733 8.717   1.00 54.53  ? 88   PHE B O   1 
ATOM   7217  C CB  . PHE D  2 88  ? 28.889  -26.592 7.922   1.00 46.03  ? 88   PHE B CB  1 
ATOM   7218  C CG  . PHE D  2 88  ? 27.581  -26.178 8.563   1.00 49.88  ? 88   PHE B CG  1 
ATOM   7219  C CD1 . PHE D  2 88  ? 26.994  -26.972 9.562   1.00 45.01  ? 88   PHE B CD1 1 
ATOM   7220  C CD2 . PHE D  2 88  ? 26.920  -25.012 8.158   1.00 48.27  ? 88   PHE B CD2 1 
ATOM   7221  C CE1 . PHE D  2 88  ? 25.788  -26.595 10.179  1.00 37.17  ? 88   PHE B CE1 1 
ATOM   7222  C CE2 . PHE D  2 88  ? 25.703  -24.629 8.758   1.00 44.90  ? 88   PHE B CE2 1 
ATOM   7223  C CZ  . PHE D  2 88  ? 25.137  -25.431 9.773   1.00 39.40  ? 88   PHE B CZ  1 
ATOM   7224  N N   . LEU D  2 89  ? 32.167  -27.019 7.675   1.00 47.78  ? 89   LEU B N   1 
ATOM   7225  C CA  . LEU D  2 89  ? 33.214  -27.887 7.167   1.00 47.53  ? 89   LEU B CA  1 
ATOM   7226  C C   . LEU D  2 89  ? 34.138  -28.343 8.293   1.00 46.50  ? 89   LEU B C   1 
ATOM   7227  O O   . LEU D  2 89  ? 34.530  -29.507 8.310   1.00 47.21  ? 89   LEU B O   1 
ATOM   7228  C CB  . LEU D  2 89  ? 34.032  -27.193 6.057   1.00 46.76  ? 89   LEU B CB  1 
ATOM   7229  C CG  . LEU D  2 89  ? 33.278  -26.915 4.735   1.00 59.77  ? 89   LEU B CG  1 
ATOM   7230  C CD1 . LEU D  2 89  ? 34.116  -26.149 3.679   1.00 55.38  ? 89   LEU B CD1 1 
ATOM   7231  C CD2 . LEU D  2 89  ? 32.671  -28.191 4.111   1.00 56.87  ? 89   LEU B CD2 1 
ATOM   7232  N N   . ASP D  2 90  ? 34.411  -27.487 9.278   1.00 42.57  ? 90   ASP B N   1 
ATOM   7233  C CA  . ASP D  2 90  ? 35.267  -27.908 10.395  1.00 47.13  ? 90   ASP B CA  1 
ATOM   7234  C C   . ASP D  2 90  ? 34.541  -28.940 11.266  1.00 51.44  ? 90   ASP B C   1 
ATOM   7235  O O   . ASP D  2 90  ? 35.163  -29.885 11.764  1.00 49.78  ? 90   ASP B O   1 
ATOM   7236  C CB  . ASP D  2 90  ? 35.723  -26.723 11.270  1.00 46.64  ? 90   ASP B CB  1 
ATOM   7237  C CG  . ASP D  2 90  ? 36.709  -25.793 10.553  1.00 54.35  ? 90   ASP B CG  1 
ATOM   7238  O OD1 . ASP D  2 90  ? 37.279  -26.184 9.509   1.00 54.35  ? 90   ASP B OD1 1 
ATOM   7239  O OD2 . ASP D  2 90  ? 36.963  -24.685 11.069  1.00 55.58  ? 90   ASP B OD2 1 
ATOM   7240  N N   . VAL D  2 91  ? 33.226  -28.765 11.412  1.00 49.62  ? 91   VAL B N   1 
ATOM   7241  C CA  . VAL D  2 91  ? 32.390  -29.666 12.191  1.00 46.41  ? 91   VAL B CA  1 
ATOM   7242  C C   . VAL D  2 91  ? 32.377  -31.064 11.579  1.00 48.16  ? 91   VAL B C   1 
ATOM   7243  O O   . VAL D  2 91  ? 32.602  -32.045 12.284  1.00 48.48  ? 91   VAL B O   1 
ATOM   7244  C CB  . VAL D  2 91  ? 30.940  -29.129 12.296  1.00 40.42  ? 91   VAL B CB  1 
ATOM   7245  C CG1 . VAL D  2 91  ? 30.005  -30.197 12.779  1.00 29.64  ? 91   VAL B CG1 1 
ATOM   7246  C CG2 . VAL D  2 91  ? 30.881  -27.894 13.200  1.00 41.53  ? 91   VAL B CG2 1 
ATOM   7247  N N   . TRP D  2 92  ? 32.155  -31.165 10.272  1.00 45.56  ? 92   TRP B N   1 
ATOM   7248  C CA  . TRP D  2 92  ? 32.091  -32.482 9.634   1.00 45.44  ? 92   TRP B CA  1 
ATOM   7249  C C   . TRP D  2 92  ? 33.484  -33.117 9.394   1.00 47.39  ? 92   TRP B C   1 
ATOM   7250  O O   . TRP D  2 92  ? 33.594  -34.336 9.262   1.00 48.37  ? 92   TRP B O   1 
ATOM   7251  C CB  . TRP D  2 92  ? 31.331  -32.374 8.320   1.00 46.64  ? 92   TRP B CB  1 
ATOM   7252  C CG  . TRP D  2 92  ? 29.865  -32.232 8.502   1.00 45.47  ? 92   TRP B CG  1 
ATOM   7253  C CD1 . TRP D  2 92  ? 29.133  -31.101 8.324   1.00 46.70  ? 92   TRP B CD1 1 
ATOM   7254  C CD2 . TRP D  2 92  ? 28.940  -33.255 8.879   1.00 47.50  ? 92   TRP B CD2 1 
ATOM   7255  N NE1 . TRP D  2 92  ? 27.809  -31.352 8.571   1.00 47.64  ? 92   TRP B NE1 1 
ATOM   7256  C CE2 . TRP D  2 92  ? 27.664  -32.669 8.916   1.00 45.72  ? 92   TRP B CE2 1 
ATOM   7257  C CE3 . TRP D  2 92  ? 29.069  -34.607 9.212   1.00 51.23  ? 92   TRP B CE3 1 
ATOM   7258  C CZ2 . TRP D  2 92  ? 26.519  -33.389 9.269   1.00 45.52  ? 92   TRP B CZ2 1 
ATOM   7259  C CZ3 . TRP D  2 92  ? 27.934  -35.319 9.557   1.00 47.84  ? 92   TRP B CZ3 1 
ATOM   7260  C CH2 . TRP D  2 92  ? 26.675  -34.708 9.583   1.00 46.31  ? 92   TRP B CH2 1 
ATOM   7261  N N   . THR D  2 93  ? 34.536  -32.296 9.356   1.00 43.21  ? 93   THR B N   1 
ATOM   7262  C CA  . THR D  2 93  ? 35.910  -32.785 9.268   1.00 41.73  ? 93   THR B CA  1 
ATOM   7263  C C   . THR D  2 93  ? 36.289  -33.368 10.624  1.00 49.83  ? 93   THR B C   1 
ATOM   7264  O O   . THR D  2 93  ? 36.926  -34.421 10.712  1.00 50.01  ? 93   THR B O   1 
ATOM   7265  C CB  . THR D  2 93  ? 36.921  -31.659 8.881   1.00 45.44  ? 93   THR B CB  1 
ATOM   7266  O OG1 . THR D  2 93  ? 36.837  -31.383 7.478   1.00 49.26  ? 93   THR B OG1 1 
ATOM   7267  C CG2 . THR D  2 93  ? 38.343  -32.069 9.164   1.00 45.25  ? 93   THR B CG2 1 
ATOM   7268  N N   . TYR D  2 94  ? 35.889  -32.677 11.689  1.00 48.31  ? 94   TYR B N   1 
ATOM   7269  C CA  . TYR D  2 94  ? 36.090  -33.186 13.042  1.00 49.13  ? 94   TYR B CA  1 
ATOM   7270  C C   . TYR D  2 94  ? 35.319  -34.482 13.261  1.00 52.71  ? 94   TYR B C   1 
ATOM   7271  O O   . TYR D  2 94  ? 35.842  -35.435 13.838  1.00 50.71  ? 94   TYR B O   1 
ATOM   7272  C CB  . TYR D  2 94  ? 35.661  -32.153 14.080  1.00 42.48  ? 94   TYR B CB  1 
ATOM   7273  C CG  . TYR D  2 94  ? 35.566  -32.684 15.490  1.00 48.10  ? 94   TYR B CG  1 
ATOM   7274  C CD1 . TYR D  2 94  ? 34.418  -33.337 15.938  1.00 46.63  ? 94   TYR B CD1 1 
ATOM   7275  C CD2 . TYR D  2 94  ? 36.621  -32.516 16.388  1.00 56.12  ? 94   TYR B CD2 1 
ATOM   7276  C CE1 . TYR D  2 94  ? 34.326  -33.821 17.224  1.00 49.34  ? 94   TYR B CE1 1 
ATOM   7277  C CE2 . TYR D  2 94  ? 36.538  -32.993 17.688  1.00 55.34  ? 94   TYR B CE2 1 
ATOM   7278  C CZ  . TYR D  2 94  ? 35.386  -33.642 18.101  1.00 53.88  ? 94   TYR B CZ  1 
ATOM   7279  O OH  . TYR D  2 94  ? 35.283  -34.116 19.393  1.00 61.76  ? 94   TYR B OH  1 
ATOM   7280  N N   . ASN D  2 95  ? 34.064  -34.497 12.816  1.00 49.91  ? 95   ASN B N   1 
ATOM   7281  C CA  . ASN D  2 95  ? 33.211  -35.655 12.994  1.00 44.60  ? 95   ASN B CA  1 
ATOM   7282  C C   . ASN D  2 95  ? 33.793  -36.872 12.299  1.00 50.49  ? 95   ASN B C   1 
ATOM   7283  O O   . ASN D  2 95  ? 33.673  -37.982 12.794  1.00 52.34  ? 95   ASN B O   1 
ATOM   7284  C CB  . ASN D  2 95  ? 31.807  -35.415 12.424  1.00 44.69  ? 95   ASN B CB  1 
ATOM   7285  C CG  . ASN D  2 95  ? 30.840  -34.769 13.410  1.00 42.55  ? 95   ASN B CG  1 
ATOM   7286  O OD1 . ASN D  2 95  ? 31.203  -34.314 14.497  1.00 36.02  ? 95   ASN B OD1 1 
ATOM   7287  N ND2 . ASN D  2 95  ? 29.571  -34.767 13.029  1.00 46.73  ? 95   ASN B ND2 1 
ATOM   7288  N N   . ALA D  2 96  ? 34.438  -36.660 11.155  1.00 52.83  ? 96   ALA B N   1 
ATOM   7289  C CA  . ALA D  2 96  ? 34.915  -37.782 10.360  1.00 52.28  ? 96   ALA B CA  1 
ATOM   7290  C C   . ALA D  2 96  ? 36.238  -38.307 10.903  1.00 49.44  ? 96   ALA B C   1 
ATOM   7291  O O   . ALA D  2 96  ? 36.453  -39.508 10.951  1.00 51.64  ? 96   ALA B O   1 
ATOM   7292  C CB  . ALA D  2 96  ? 35.046  -37.380 8.906   1.00 52.42  ? 96   ALA B CB  1 
ATOM   7293  N N   . GLU D  2 97  ? 37.117  -37.416 11.326  1.00 49.24  ? 97   GLU B N   1 
ATOM   7294  C CA  . GLU D  2 97  ? 38.393  -37.839 11.894  1.00 55.82  ? 97   GLU B CA  1 
ATOM   7295  C C   . GLU D  2 97  ? 38.238  -38.563 13.240  1.00 58.06  ? 97   GLU B C   1 
ATOM   7296  O O   . GLU D  2 97  ? 38.892  -39.575 13.483  1.00 62.95  ? 97   GLU B O   1 
ATOM   7297  C CB  . GLU D  2 97  ? 39.314  -36.642 12.072  1.00 52.23  ? 97   GLU B CB  1 
ATOM   7298  C CG  . GLU D  2 97  ? 39.831  -36.103 10.773  1.00 52.54  ? 97   GLU B CG  1 
ATOM   7299  C CD  . GLU D  2 97  ? 40.714  -34.904 10.988  1.00 58.36  ? 97   GLU B CD  1 
ATOM   7300  O OE1 . GLU D  2 97  ? 40.734  -34.391 12.132  1.00 61.14  ? 97   GLU B OE1 1 
ATOM   7301  O OE2 . GLU D  2 97  ? 41.363  -34.464 10.015  1.00 57.00  ? 97   GLU B OE2 1 
ATOM   7302  N N   . LEU D  2 98  ? 37.397  -38.026 14.118  1.00 57.56  ? 98   LEU B N   1 
ATOM   7303  C CA  . LEU D  2 98  ? 37.220  -38.581 15.454  1.00 52.48  ? 98   LEU B CA  1 
ATOM   7304  C C   . LEU D  2 98  ? 36.537  -39.944 15.407  1.00 53.81  ? 98   LEU B C   1 
ATOM   7305  O O   . LEU D  2 98  ? 36.825  -40.814 16.220  1.00 53.33  ? 98   LEU B O   1 
ATOM   7306  C CB  . LEU D  2 98  ? 36.394  -37.631 16.329  1.00 45.65  ? 98   LEU B CB  1 
ATOM   7307  C CG  . LEU D  2 98  ? 36.320  -38.050 17.803  1.00 58.03  ? 98   LEU B CG  1 
ATOM   7308  C CD1 . LEU D  2 98  ? 37.614  -37.633 18.493  1.00 56.63  ? 98   LEU B CD1 1 
ATOM   7309  C CD2 . LEU D  2 98  ? 35.069  -37.556 18.581  1.00 53.82  ? 98   LEU B CD2 1 
ATOM   7310  N N   . LEU D  2 99  ? 35.654  -40.139 14.438  1.00 48.86  ? 99   LEU B N   1 
ATOM   7311  C CA  . LEU D  2 99  ? 34.912  -41.397 14.337  1.00 56.43  ? 99   LEU B CA  1 
ATOM   7312  C C   . LEU D  2 99  ? 35.796  -42.546 13.841  1.00 59.61  ? 99   LEU B C   1 
ATOM   7313  O O   . LEU D  2 99  ? 35.615  -43.701 14.234  1.00 58.41  ? 99   LEU B O   1 
ATOM   7314  C CB  . LEU D  2 99  ? 33.711  -41.238 13.405  1.00 58.85  ? 99   LEU B CB  1 
ATOM   7315  C CG  . LEU D  2 99  ? 32.927  -42.509 13.085  1.00 61.62  ? 99   LEU B CG  1 
ATOM   7316  C CD1 . LEU D  2 99  ? 32.277  -43.039 14.339  1.00 61.85  ? 99   LEU B CD1 1 
ATOM   7317  C CD2 . LEU D  2 99  ? 31.879  -42.233 12.024  1.00 64.67  ? 99   LEU B CD2 1 
ATOM   7318  N N   . VAL D  2 100 ? 36.713  -42.215 12.935  1.00 61.31  ? 100  VAL B N   1 
ATOM   7319  C CA  . VAL D  2 100 ? 37.714  -43.142 12.420  1.00 59.96  ? 100  VAL B CA  1 
ATOM   7320  C C   . VAL D  2 100 ? 38.793  -43.426 13.492  1.00 59.55  ? 100  VAL B C   1 
ATOM   7321  O O   . VAL D  2 100 ? 39.254  -44.556 13.642  1.00 65.68  ? 100  VAL B O   1 
ATOM   7322  C CB  . VAL D  2 100 ? 38.348  -42.589 11.132  1.00 51.19  ? 100  VAL B CB  1 
ATOM   7323  C CG1 . VAL D  2 100 ? 39.563  -43.411 10.710  1.00 51.87  ? 100  VAL B CG1 1 
ATOM   7324  C CG2 . VAL D  2 100 ? 37.317  -42.589 10.037  1.00 50.99  ? 100  VAL B CG2 1 
ATOM   7325  N N   . LEU D  2 101 ? 39.188  -42.395 14.230  1.00 52.45  ? 101  LEU B N   1 
ATOM   7326  C CA  . LEU D  2 101 ? 40.139  -42.537 15.326  1.00 57.51  ? 101  LEU B CA  1 
ATOM   7327  C C   . LEU D  2 101 ? 39.587  -43.465 16.411  1.00 65.47  ? 101  LEU B C   1 
ATOM   7328  O O   . LEU D  2 101 ? 40.308  -44.283 16.987  1.00 67.32  ? 101  LEU B O   1 
ATOM   7329  C CB  . LEU D  2 101 ? 40.462  -41.167 15.928  1.00 55.04  ? 101  LEU B CB  1 
ATOM   7330  C CG  . LEU D  2 101 ? 41.943  -40.879 16.149  1.00 61.15  ? 101  LEU B CG  1 
ATOM   7331  C CD1 . LEU D  2 101 ? 42.774  -41.532 15.049  1.00 59.24  ? 101  LEU B CD1 1 
ATOM   7332  C CD2 . LEU D  2 101 ? 42.213  -39.375 16.209  1.00 59.87  ? 101  LEU B CD2 1 
ATOM   7333  N N   . MET D  2 102 ? 38.302  -43.310 16.699  1.00 63.57  ? 102  MET B N   1 
ATOM   7334  C CA  . MET D  2 102 ? 37.649  -44.101 17.719  1.00 57.57  ? 102  MET B CA  1 
ATOM   7335  C C   . MET D  2 102 ? 37.414  -45.540 17.290  1.00 60.31  ? 102  MET B C   1 
ATOM   7336  O O   . MET D  2 102 ? 37.665  -46.463 18.046  1.00 64.71  ? 102  MET B O   1 
ATOM   7337  C CB  . MET D  2 102 ? 36.324  -43.457 18.091  1.00 59.32  ? 102  MET B CB  1 
ATOM   7338  C CG  . MET D  2 102 ? 36.462  -42.216 18.937  1.00 55.62  ? 102  MET B CG  1 
ATOM   7339  S SD  . MET D  2 102 ? 34.823  -41.719 19.437  1.00 52.21  ? 102  MET B SD  1 
ATOM   7340  C CE  . MET D  2 102 ? 35.209  -40.878 20.975  1.00 54.36  ? 102  MET B CE  1 
ATOM   7341  N N   . GLU D  2 103 ? 36.947  -45.733 16.067  1.00 62.14  ? 103  GLU B N   1 
ATOM   7342  C CA  . GLU D  2 103 ? 36.563  -47.068 15.630  1.00 62.90  ? 103  GLU B CA  1 
ATOM   7343  C C   . GLU D  2 103 ? 37.750  -47.902 15.169  1.00 65.59  ? 103  GLU B C   1 
ATOM   7344  O O   . GLU D  2 103 ? 37.632  -49.116 15.021  1.00 68.61  ? 103  GLU B O   1 
ATOM   7345  C CB  . GLU D  2 103 ? 35.512  -46.985 14.531  1.00 61.89  ? 103  GLU B CB  1 
ATOM   7346  C CG  . GLU D  2 103 ? 34.144  -46.496 15.030  1.00 69.95  ? 103  GLU B CG  1 
ATOM   7347  C CD  . GLU D  2 103 ? 33.542  -47.366 16.130  1.00 64.77  ? 103  GLU B CD  1 
ATOM   7348  O OE1 . GLU D  2 103 ? 33.646  -48.607 16.035  1.00 63.64  ? 103  GLU B OE1 1 
ATOM   7349  O OE2 . GLU D  2 103 ? 32.945  -46.807 17.077  1.00 69.35  ? 103  GLU B OE2 1 
ATOM   7350  N N   . ASN D  2 104 ? 38.883  -47.259 14.913  1.00 67.32  ? 104  ASN B N   1 
ATOM   7351  C CA  . ASN D  2 104 ? 40.109  -48.014 14.692  1.00 65.43  ? 104  ASN B CA  1 
ATOM   7352  C C   . ASN D  2 104 ? 40.486  -48.758 15.967  1.00 69.50  ? 104  ASN B C   1 
ATOM   7353  O O   . ASN D  2 104 ? 40.676  -49.979 15.963  1.00 68.31  ? 104  ASN B O   1 
ATOM   7354  C CB  . ASN D  2 104 ? 41.274  -47.097 14.296  1.00 61.00  ? 104  ASN B CB  1 
ATOM   7355  C CG  . ASN D  2 104 ? 41.292  -46.772 12.824  1.00 62.50  ? 104  ASN B CG  1 
ATOM   7356  O OD1 . ASN D  2 104 ? 40.409  -47.187 12.075  1.00 62.53  ? 104  ASN B OD1 1 
ATOM   7357  N ND2 . ASN D  2 104 ? 42.318  -46.045 12.394  1.00 58.94  ? 104  ASN B ND2 1 
ATOM   7358  N N   . GLU D  2 105 ? 40.539  -48.011 17.066  1.00 64.64  ? 105  GLU B N   1 
ATOM   7359  C CA  . GLU D  2 105 ? 40.962  -48.557 18.340  1.00 69.05  ? 105  GLU B CA  1 
ATOM   7360  C C   . GLU D  2 105 ? 40.057  -49.713 18.770  1.00 68.23  ? 105  GLU B C   1 
ATOM   7361  O O   . GLU D  2 105 ? 40.538  -50.696 19.330  1.00 65.54  ? 105  GLU B O   1 
ATOM   7362  C CB  . GLU D  2 105 ? 40.990  -47.465 19.407  1.00 73.77  ? 105  GLU B CB  1 
ATOM   7363  C CG  . GLU D  2 105 ? 41.781  -47.849 20.636  1.00 73.39  ? 105  GLU B CG  1 
ATOM   7364  C CD  . GLU D  2 105 ? 41.117  -47.399 21.908  1.00 85.97  ? 105  GLU B CD  1 
ATOM   7365  O OE1 . GLU D  2 105 ? 39.928  -47.010 21.856  1.00 90.11  ? 105  GLU B OE1 1 
ATOM   7366  O OE2 . GLU D  2 105 ? 41.785  -47.436 22.963  1.00 98.48  ? 105  GLU B OE2 1 
ATOM   7367  N N   . ARG D  2 106 ? 38.762  -49.611 18.469  1.00 66.59  ? 106  ARG B N   1 
ATOM   7368  C CA  . ARG D  2 106 ? 37.806  -50.649 18.848  1.00 65.65  ? 106  ARG B CA  1 
ATOM   7369  C C   . ARG D  2 106 ? 37.909  -51.850 17.916  1.00 65.84  ? 106  ARG B C   1 
ATOM   7370  O O   . ARG D  2 106 ? 37.595  -52.974 18.304  1.00 70.39  ? 106  ARG B O   1 
ATOM   7371  C CB  . ARG D  2 106 ? 36.364  -50.115 18.844  1.00 66.15  ? 106  ARG B CB  1 
ATOM   7372  C CG  . ARG D  2 106 ? 35.996  -49.218 20.034  1.00 72.01  ? 106  ARG B CG  1 
ATOM   7373  C CD  . ARG D  2 106 ? 34.508  -48.828 20.023  1.00 75.28  ? 106  ARG B CD  1 
ATOM   7374  N NE  . ARG D  2 106 ? 33.637  -49.936 20.438  1.00 86.18  ? 106  ARG B NE  1 
ATOM   7375  C CZ  . ARG D  2 106 ? 33.317  -50.224 21.704  1.00 81.38  ? 106  ARG B CZ  1 
ATOM   7376  N NH1 . ARG D  2 106 ? 33.791  -49.480 22.702  1.00 81.53  ? 106  ARG B NH1 1 
ATOM   7377  N NH2 . ARG D  2 106 ? 32.519  -51.258 21.976  1.00 71.19  ? 106  ARG B NH2 1 
ATOM   7378  N N   . THR D  2 107 ? 38.321  -51.601 16.679  1.00 65.90  ? 107  THR B N   1 
ATOM   7379  C CA  . THR D  2 107 ? 38.507  -52.662 15.698  1.00 66.71  ? 107  THR B CA  1 
ATOM   7380  C C   . THR D  2 107 ? 39.700  -53.538 16.095  1.00 68.90  ? 107  THR B C   1 
ATOM   7381  O O   . THR D  2 107 ? 39.676  -54.757 15.922  1.00 69.12  ? 107  THR B O   1 
ATOM   7382  C CB  . THR D  2 107 ? 38.699  -52.088 14.281  1.00 63.49  ? 107  THR B CB  1 
ATOM   7383  O OG1 . THR D  2 107 ? 37.437  -51.619 13.791  1.00 66.26  ? 107  THR B OG1 1 
ATOM   7384  C CG2 . THR D  2 107 ? 39.241  -53.143 13.324  1.00 63.69  ? 107  THR B CG2 1 
ATOM   7385  N N   . LEU D  2 108 ? 40.757  -52.912 16.601  1.00 64.51  ? 108  LEU B N   1 
ATOM   7386  C CA  . LEU D  2 108 ? 41.919  -53.657 17.058  1.00 64.80  ? 108  LEU B CA  1 
ATOM   7387  C C   . LEU D  2 108 ? 41.607  -54.483 18.315  1.00 69.71  ? 108  LEU B C   1 
ATOM   7388  O O   . LEU D  2 108 ? 42.058  -55.622 18.453  1.00 70.42  ? 108  LEU B O   1 
ATOM   7389  C CB  . LEU D  2 108 ? 43.091  -52.708 17.324  1.00 68.86  ? 108  LEU B CB  1 
ATOM   7390  C CG  . LEU D  2 108 ? 43.692  -52.025 16.092  1.00 65.01  ? 108  LEU B CG  1 
ATOM   7391  C CD1 . LEU D  2 108 ? 44.857  -51.133 16.497  1.00 61.47  ? 108  LEU B CD1 1 
ATOM   7392  C CD2 . LEU D  2 108 ? 44.128  -53.050 15.053  1.00 67.55  ? 108  LEU B CD2 1 
ATOM   7393  N N   . ASP D  2 109 ? 40.815  -53.911 19.217  1.00 70.82  ? 109  ASP B N   1 
ATOM   7394  C CA  . ASP D  2 109 ? 40.411  -54.606 20.431  1.00 67.17  ? 109  ASP B CA  1 
ATOM   7395  C C   . ASP D  2 109 ? 39.342  -55.682 20.162  1.00 69.80  ? 109  ASP B C   1 
ATOM   7396  O O   . ASP D  2 109 ? 39.120  -56.559 20.994  1.00 68.39  ? 109  ASP B O   1 
ATOM   7397  C CB  . ASP D  2 109 ? 39.895  -53.596 21.460  1.00 64.73  ? 109  ASP B CB  1 
ATOM   7398  C CG  . ASP D  2 109 ? 41.007  -52.737 22.037  1.00 74.25  ? 109  ASP B CG  1 
ATOM   7399  O OD1 . ASP D  2 109 ? 42.185  -53.156 21.929  1.00 76.19  ? 109  ASP B OD1 1 
ATOM   7400  O OD2 . ASP D  2 109 ? 40.705  -51.657 22.605  1.00 75.00  ? 109  ASP B OD2 1 
ATOM   7401  N N   . PHE D  2 110 ? 38.681  -55.608 19.005  1.00 67.04  ? 110  PHE B N   1 
ATOM   7402  C CA  . PHE D  2 110 ? 37.666  -56.598 18.620  1.00 67.54  ? 110  PHE B CA  1 
ATOM   7403  C C   . PHE D  2 110 ? 38.384  -57.881 18.212  1.00 72.53  ? 110  PHE B C   1 
ATOM   7404  O O   . PHE D  2 110 ? 37.894  -58.978 18.464  1.00 72.12  ? 110  PHE B O   1 
ATOM   7405  C CB  . PHE D  2 110 ? 36.780  -56.078 17.478  1.00 68.48  ? 110  PHE B CB  1 
ATOM   7406  C CG  . PHE D  2 110 ? 35.727  -57.064 16.988  1.00 62.64  ? 110  PHE B CG  1 
ATOM   7407  C CD1 . PHE D  2 110 ? 34.663  -57.432 17.798  1.00 63.12  ? 110  PHE B CD1 1 
ATOM   7408  C CD2 . PHE D  2 110 ? 35.775  -57.569 15.697  1.00 61.33  ? 110  PHE B CD2 1 
ATOM   7409  C CE1 . PHE D  2 110 ? 33.683  -58.310 17.333  1.00 64.83  ? 110  PHE B CE1 1 
ATOM   7410  C CE2 . PHE D  2 110 ? 34.805  -58.453 15.233  1.00 65.31  ? 110  PHE B CE2 1 
ATOM   7411  C CZ  . PHE D  2 110 ? 33.762  -58.823 16.049  1.00 61.63  ? 110  PHE B CZ  1 
ATOM   7412  N N   . HIS D  2 111 ? 39.519  -57.730 17.528  1.00 70.00  ? 111  HIS B N   1 
ATOM   7413  C CA  . HIS D  2 111 ? 40.364  -58.866 17.176  1.00 73.30  ? 111  HIS B CA  1 
ATOM   7414  C C   . HIS D  2 111 ? 41.003  -59.513 18.422  1.00 75.55  ? 111  HIS B C   1 
ATOM   7415  O O   . HIS D  2 111 ? 41.064  -60.746 18.533  1.00 74.76  ? 111  HIS B O   1 
ATOM   7416  C CB  . HIS D  2 111 ? 41.457  -58.442 16.184  1.00 75.66  ? 111  HIS B CB  1 
ATOM   7417  C CG  . HIS D  2 111 ? 40.958  -58.166 14.795  1.00 80.72  ? 111  HIS B CG  1 
ATOM   7418  N ND1 . HIS D  2 111 ? 40.047  -58.979 14.152  1.00 79.83  ? 111  HIS B ND1 1 
ATOM   7419  C CD2 . HIS D  2 111 ? 41.269  -57.182 13.916  1.00 77.24  ? 111  HIS B CD2 1 
ATOM   7420  C CE1 . HIS D  2 111 ? 39.809  -58.500 12.943  1.00 82.38  ? 111  HIS B CE1 1 
ATOM   7421  N NE2 . HIS D  2 111 ? 40.540  -57.411 12.774  1.00 78.93  ? 111  HIS B NE2 1 
ATOM   7422  N N   . ASP D  2 112 ? 41.468  -58.680 19.353  1.00 69.91  ? 112  ASP B N   1 
ATOM   7423  C CA  . ASP D  2 112 ? 42.109  -59.165 20.573  1.00 70.17  ? 112  ASP B CA  1 
ATOM   7424  C C   . ASP D  2 112 ? 41.121  -59.976 21.423  1.00 72.49  ? 112  ASP B C   1 
ATOM   7425  O O   . ASP D  2 112 ? 41.457  -61.031 21.952  1.00 72.35  ? 112  ASP B O   1 
ATOM   7426  C CB  . ASP D  2 112 ? 42.675  -57.987 21.377  1.00 75.04  ? 112  ASP B CB  1 
ATOM   7427  C CG  . ASP D  2 112 ? 43.707  -58.417 22.416  1.00 80.39  ? 112  ASP B CG  1 
ATOM   7428  O OD1 . ASP D  2 112 ? 43.831  -59.627 22.663  1.00 78.78  ? 112  ASP B OD1 1 
ATOM   7429  O OD2 . ASP D  2 112 ? 44.390  -57.544 22.997  1.00 83.65  ? 112  ASP B OD2 1 
ATOM   7430  N N   . SER D  2 113 ? 39.893  -59.482 21.530  1.00 75.24  ? 113  SER B N   1 
ATOM   7431  C CA  . SER D  2 113 ? 38.830  -60.174 22.259  1.00 74.32  ? 113  SER B CA  1 
ATOM   7432  C C   . SER D  2 113 ? 38.467  -61.500 21.600  1.00 72.67  ? 113  SER B C   1 
ATOM   7433  O O   . SER D  2 113 ? 38.123  -62.468 22.275  1.00 71.96  ? 113  SER B O   1 
ATOM   7434  C CB  . SER D  2 113 ? 37.590  -59.272 22.357  1.00 72.38  ? 113  SER B CB  1 
ATOM   7435  O OG  . SER D  2 113 ? 36.441  -59.978 22.785  1.00 69.60  ? 113  SER B OG  1 
ATOM   7436  N N   . ASN D  2 114 ? 38.568  -61.543 20.277  1.00 71.20  ? 114  ASN B N   1 
ATOM   7437  C CA  . ASN D  2 114 ? 38.154  -62.716 19.529  1.00 71.36  ? 114  ASN B CA  1 
ATOM   7438  C C   . ASN D  2 114 ? 39.163  -63.851 19.642  1.00 74.72  ? 114  ASN B C   1 
ATOM   7439  O O   . ASN D  2 114 ? 38.787  -65.025 19.631  1.00 68.72  ? 114  ASN B O   1 
ATOM   7440  C CB  . ASN D  2 114 ? 37.928  -62.331 18.072  1.00 69.71  ? 114  ASN B CB  1 
ATOM   7441  C CG  . ASN D  2 114 ? 36.617  -61.603 17.872  1.00 68.90  ? 114  ASN B CG  1 
ATOM   7442  O OD1 . ASN D  2 114 ? 35.744  -61.656 18.733  1.00 68.84  ? 114  ASN B OD1 1 
ATOM   7443  N ND2 . ASN D  2 114 ? 36.480  -60.897 16.751  1.00 69.70  ? 114  ASN B ND2 1 
ATOM   7444  N N   . VAL D  2 115 ? 40.436  -63.493 19.796  1.00 75.70  ? 115  VAL B N   1 
ATOM   7445  C CA  . VAL D  2 115 ? 41.489  -64.481 20.024  1.00 75.85  ? 115  VAL B CA  1 
ATOM   7446  C C   . VAL D  2 115 ? 41.384  -65.075 21.427  1.00 74.54  ? 115  VAL B C   1 
ATOM   7447  O O   . VAL D  2 115 ? 41.413  -66.294 21.591  1.00 79.99  ? 115  VAL B O   1 
ATOM   7448  C CB  . VAL D  2 115 ? 42.897  -63.881 19.836  1.00 72.63  ? 115  VAL B CB  1 
ATOM   7449  C CG1 . VAL D  2 115 ? 43.943  -64.720 20.560  1.00 72.70  ? 115  VAL B CG1 1 
ATOM   7450  C CG2 . VAL D  2 115 ? 43.221  -63.775 18.365  1.00 78.94  ? 115  VAL B CG2 1 
ATOM   7451  N N   . LYS D  2 116 ? 41.233  -64.213 22.429  1.00 73.22  ? 116  LYS B N   1 
ATOM   7452  C CA  . LYS D  2 116 ? 41.133  -64.671 23.810  1.00 73.77  ? 116  LYS B CA  1 
ATOM   7453  C C   . LYS D  2 116 ? 39.920  -65.567 23.994  1.00 73.11  ? 116  LYS B C   1 
ATOM   7454  O O   . LYS D  2 116 ? 39.997  -66.557 24.705  1.00 76.55  ? 116  LYS B O   1 
ATOM   7455  C CB  . LYS D  2 116 ? 41.054  -63.496 24.794  1.00 72.76  ? 116  LYS B CB  1 
ATOM   7456  C CG  . LYS D  2 116 ? 40.952  -63.948 26.248  1.00 73.46  ? 116  LYS B CG  1 
ATOM   7457  C CD  . LYS D  2 116 ? 40.898  -62.793 27.241  1.00 79.72  ? 116  LYS B CD  1 
ATOM   7458  C CE  . LYS D  2 116 ? 40.960  -63.312 28.675  1.00 75.52  ? 116  LYS B CE  1 
ATOM   7459  N NZ  . LYS D  2 116 ? 39.625  -63.726 29.198  1.00 77.68  ? 116  LYS B NZ  1 
ATOM   7460  N N   . ASN D  2 117 ? 38.805  -65.236 23.353  1.00 73.54  ? 117  ASN B N   1 
ATOM   7461  C CA  . ASN D  2 117 ? 37.607  -66.061 23.486  1.00 74.68  ? 117  ASN B CA  1 
ATOM   7462  C C   . ASN D  2 117 ? 37.815  -67.426 22.825  1.00 76.21  ? 117  ASN B C   1 
ATOM   7463  O O   . ASN D  2 117 ? 37.260  -68.440 23.265  1.00 77.75  ? 117  ASN B O   1 
ATOM   7464  C CB  . ASN D  2 117 ? 36.378  -65.359 22.891  1.00 74.03  ? 117  ASN B CB  1 
ATOM   7465  C CG  . ASN D  2 117 ? 35.878  -64.193 23.752  1.00 77.41  ? 117  ASN B CG  1 
ATOM   7466  O OD1 . ASN D  2 117 ? 36.490  -63.829 24.759  1.00 78.50  ? 117  ASN B OD1 1 
ATOM   7467  N ND2 . ASN D  2 117 ? 34.749  -63.613 23.356  1.00 78.72  ? 117  ASN B ND2 1 
ATOM   7468  N N   . LEU D  2 118 ? 38.633  -67.444 21.778  1.00 74.30  ? 118  LEU B N   1 
ATOM   7469  C CA  . LEU D  2 118 ? 38.974  -68.688 21.099  1.00 76.20  ? 118  LEU B CA  1 
ATOM   7470  C C   . LEU D  2 118 ? 39.903  -69.551 21.957  1.00 79.81  ? 118  LEU B C   1 
ATOM   7471  O O   . LEU D  2 118 ? 39.735  -70.769 22.039  1.00 80.20  ? 118  LEU B O   1 
ATOM   7472  C CB  . LEU D  2 118 ? 39.637  -68.399 19.750  1.00 77.32  ? 118  LEU B CB  1 
ATOM   7473  C CG  . LEU D  2 118 ? 39.923  -69.624 18.878  1.00 74.84  ? 118  LEU B CG  1 
ATOM   7474  C CD1 . LEU D  2 118 ? 38.618  -70.231 18.396  1.00 76.25  ? 118  LEU B CD1 1 
ATOM   7475  C CD2 . LEU D  2 118 ? 40.821  -69.265 17.710  1.00 79.97  ? 118  LEU B CD2 1 
ATOM   7476  N N   . TYR D  2 119 ? 40.875  -68.913 22.602  1.00 75.86  ? 119  TYR B N   1 
ATOM   7477  C CA  . TYR D  2 119 ? 41.774  -69.608 23.513  1.00 79.56  ? 119  TYR B CA  1 
ATOM   7478  C C   . TYR D  2 119 ? 41.002  -70.246 24.666  1.00 78.69  ? 119  TYR B C   1 
ATOM   7479  O O   . TYR D  2 119 ? 41.231  -71.394 25.025  1.00 80.59  ? 119  TYR B O   1 
ATOM   7480  C CB  . TYR D  2 119 ? 42.822  -68.646 24.064  1.00 78.44  ? 119  TYR B CB  1 
ATOM   7481  C CG  . TYR D  2 119 ? 43.736  -69.262 25.099  1.00 82.57  ? 119  TYR B CG  1 
ATOM   7482  C CD1 . TYR D  2 119 ? 43.404  -69.241 26.452  1.00 79.18  ? 119  TYR B CD1 1 
ATOM   7483  C CD2 . TYR D  2 119 ? 44.934  -69.856 24.727  1.00 83.27  ? 119  TYR B CD2 1 
ATOM   7484  C CE1 . TYR D  2 119 ? 44.233  -69.799 27.399  1.00 82.65  ? 119  TYR B CE1 1 
ATOM   7485  C CE2 . TYR D  2 119 ? 45.776  -70.415 25.670  1.00 87.80  ? 119  TYR B CE2 1 
ATOM   7486  C CZ  . TYR D  2 119 ? 45.421  -70.385 27.006  1.00 87.28  ? 119  TYR B CZ  1 
ATOM   7487  O OH  . TYR D  2 119 ? 46.255  -70.945 27.950  1.00 90.70  ? 119  TYR B OH  1 
ATOM   7488  N N   . ASP D  2 120 ? 40.089  -69.481 25.246  1.00 79.94  ? 120  ASP B N   1 
ATOM   7489  C CA  . ASP D  2 120 ? 39.278  -69.960 26.351  1.00 81.91  ? 120  ASP B CA  1 
ATOM   7490  C C   . ASP D  2 120 ? 38.310  -71.030 25.844  1.00 80.18  ? 120  ASP B C   1 
ATOM   7491  O O   . ASP D  2 120 ? 37.821  -71.850 26.632  1.00 78.33  ? 120  ASP B O   1 
ATOM   7492  C CB  . ASP D  2 120 ? 38.504  -68.791 27.002  1.00 78.49  ? 120  ASP B CB  1 
ATOM   7493  C CG  . ASP D  2 120 ? 39.385  -67.896 27.879  1.00 73.50  ? 120  ASP B CG  1 
ATOM   7494  O OD1 . ASP D  2 120 ? 40.562  -68.233 28.130  1.00 75.65  ? 120  ASP B OD1 1 
ATOM   7495  O OD2 . ASP D  2 120 ? 38.896  -66.824 28.294  1.00 81.18  ? 120  ASP B OD2 1 
ATOM   7496  N N   . LYS D  2 121 ? 38.067  -71.045 24.529  1.00 76.47  ? 121  LYS B N   1 
ATOM   7497  C CA  . LYS D  2 121 ? 37.129  -72.011 23.940  1.00 84.07  ? 121  LYS B CA  1 
ATOM   7498  C C   . LYS D  2 121 ? 37.686  -73.443 24.010  1.00 86.19  ? 121  LYS B C   1 
ATOM   7499  O O   . LYS D  2 121 ? 36.923  -74.401 24.187  1.00 83.86  ? 121  LYS B O   1 
ATOM   7500  C CB  . LYS D  2 121 ? 36.782  -71.659 22.484  1.00 80.78  ? 121  LYS B CB  1 
ATOM   7501  C CG  . LYS D  2 121 ? 35.901  -72.723 21.810  1.00 85.03  ? 121  LYS B CG  1 
ATOM   7502  C CD  . LYS D  2 121 ? 35.912  -72.648 20.288  1.00 88.47  ? 121  LYS B CD  1 
ATOM   7503  C CE  . LYS D  2 121 ? 35.075  -73.783 19.689  1.00 89.30  ? 121  LYS B CE  1 
ATOM   7504  N NZ  . LYS D  2 121 ? 34.985  -73.730 18.202  1.00 86.83  ? 121  LYS B NZ  1 
ATOM   7505  N N   . VAL D  2 122 ? 39.004  -73.591 23.851  1.00 82.94  ? 122  VAL B N   1 
ATOM   7506  C CA  . VAL D  2 122 ? 39.622  -74.911 23.942  1.00 83.72  ? 122  VAL B CA  1 
ATOM   7507  C C   . VAL D  2 122 ? 40.052  -75.213 25.387  1.00 86.41  ? 122  VAL B C   1 
ATOM   7508  O O   . VAL D  2 122 ? 39.958  -76.357 25.831  1.00 87.06  ? 122  VAL B O   1 
ATOM   7509  C CB  . VAL D  2 122 ? 40.845  -75.062 22.993  1.00 80.33  ? 122  VAL B CB  1 
ATOM   7510  C CG1 . VAL D  2 122 ? 40.379  -75.267 21.561  1.00 80.61  ? 122  VAL B CG1 1 
ATOM   7511  C CG2 . VAL D  2 122 ? 41.756  -73.864 23.073  1.00 82.73  ? 122  VAL B CG2 1 
ATOM   7512  N N   . ARG D  2 123 ? 40.496  -74.192 26.122  1.00 81.28  ? 123  ARG B N   1 
ATOM   7513  C CA  . ARG D  2 123 ? 40.908  -74.375 27.513  1.00 80.28  ? 123  ARG B CA  1 
ATOM   7514  C C   . ARG D  2 123 ? 39.766  -74.826 28.440  1.00 78.59  ? 123  ARG B C   1 
ATOM   7515  O O   . ARG D  2 123 ? 39.991  -75.594 29.371  1.00 78.33  ? 123  ARG B O   1 
ATOM   7516  C CB  . ARG D  2 123 ? 41.515  -73.082 28.058  1.00 82.42  ? 123  ARG B CB  1 
ATOM   7517  C CG  . ARG D  2 123 ? 41.977  -73.174 29.511  1.00 80.60  ? 123  ARG B CG  1 
ATOM   7518  C CD  . ARG D  2 123 ? 42.289  -71.802 30.086  1.00 85.48  ? 123  ARG B CD  1 
ATOM   7519  N NE  . ARG D  2 123 ? 41.087  -70.971 30.109  1.00 88.23  ? 123  ARG B NE  1 
ATOM   7520  C CZ  . ARG D  2 123 ? 40.179  -70.990 31.083  1.00 83.83  ? 123  ARG B CZ  1 
ATOM   7521  N NH1 . ARG D  2 123 ? 40.332  -71.797 32.125  1.00 80.40  ? 123  ARG B NH1 1 
ATOM   7522  N NH2 . ARG D  2 123 ? 39.110  -70.208 31.009  1.00 80.74  ? 123  ARG B NH2 1 
ATOM   7523  N N   . LEU D  2 124 ? 38.542  -74.382 28.174  1.00 77.72  ? 124  LEU B N   1 
ATOM   7524  C CA  . LEU D  2 124 ? 37.400  -74.763 29.012  1.00 79.20  ? 124  LEU B CA  1 
ATOM   7525  C C   . LEU D  2 124 ? 36.924  -76.172 28.680  1.00 83.07  ? 124  LEU B C   1 
ATOM   7526  O O   . LEU D  2 124 ? 36.150  -76.782 29.426  1.00 83.65  ? 124  LEU B O   1 
ATOM   7527  C CB  . LEU D  2 124 ? 36.234  -73.779 28.845  1.00 80.50  ? 124  LEU B CB  1 
ATOM   7528  C CG  . LEU D  2 124 ? 36.291  -72.452 29.611  1.00 83.76  ? 124  LEU B CG  1 
ATOM   7529  C CD1 . LEU D  2 124 ? 35.228  -71.491 29.098  1.00 79.91  ? 124  LEU B CD1 1 
ATOM   7530  C CD2 . LEU D  2 124 ? 36.158  -72.666 31.114  1.00 80.84  ? 124  LEU B CD2 1 
ATOM   7531  N N   . GLN D  2 125 ? 37.377  -76.667 27.534  1.00 86.49  ? 125  GLN B N   1 
ATOM   7532  C CA  . GLN D  2 125 ? 36.965  -77.968 27.020  1.00 89.24  ? 125  GLN B CA  1 
ATOM   7533  C C   . GLN D  2 125 ? 37.928  -79.078 27.462  1.00 84.17  ? 125  GLN B C   1 
ATOM   7534  O O   . GLN D  2 125 ? 37.505  -80.206 27.719  1.00 79.21  ? 125  GLN B O   1 
ATOM   7535  C CB  . GLN D  2 125 ? 36.842  -77.916 25.499  1.00 83.80  ? 125  GLN B CB  1 
ATOM   7536  C CG  . GLN D  2 125 ? 35.600  -78.618 24.997  1.00 85.61  ? 125  GLN B CG  1 
ATOM   7537  C CD  . GLN D  2 125 ? 35.351  -78.387 23.521  1.00 96.11  ? 125  GLN B CD  1 
ATOM   7538  O OE1 . GLN D  2 125 ? 36.086  -77.650 22.854  1.00 92.06  ? 125  GLN B OE1 1 
ATOM   7539  N NE2 . GLN D  2 125 ? 34.296  -79.007 23.004  1.00 99.13  ? 125  GLN B NE2 1 
ATOM   7540  N N   . LEU D  2 126 ? 39.221  -78.753 27.517  1.00 80.95  ? 126  LEU B N   1 
ATOM   7541  C CA  . LEU D  2 126 ? 40.256  -79.724 27.849  1.00 78.46  ? 126  LEU B CA  1 
ATOM   7542  C C   . LEU D  2 126 ? 40.425  -79.967 29.350  1.00 81.18  ? 126  LEU B C   1 
ATOM   7543  O O   . LEU D  2 126 ? 40.380  -81.110 29.808  1.00 81.93  ? 126  LEU B O   1 
ATOM   7544  C CB  . LEU D  2 126 ? 41.603  -79.266 27.290  1.00 73.96  ? 126  LEU B CB  1 
ATOM   7545  C CG  . LEU D  2 126 ? 41.771  -79.011 25.798  1.00 77.39  ? 126  LEU B CG  1 
ATOM   7546  C CD1 . LEU D  2 126 ? 43.238  -78.792 25.494  1.00 79.94  ? 126  LEU B CD1 1 
ATOM   7547  C CD2 . LEU D  2 126 ? 41.217  -80.153 24.966  1.00 78.63  ? 126  LEU B CD2 1 
ATOM   7548  N N   . ARG D  2 127 ? 40.552  -78.880 30.109  1.00 82.83  ? 127  ARG B N   1 
ATOM   7549  C CA  . ARG D  2 127 ? 40.887  -78.927 31.536  1.00 77.67  ? 127  ARG B CA  1 
ATOM   7550  C C   . ARG D  2 127 ? 42.197  -79.684 31.781  1.00 77.29  ? 127  ARG B C   1 
ATOM   7551  O O   . ARG D  2 127 ? 43.243  -79.354 31.206  1.00 71.15  ? 127  ARG B O   1 
ATOM   7552  C CB  . ARG D  2 127 ? 39.772  -79.578 32.348  1.00 76.52  ? 127  ARG B CB  1 
ATOM   7553  C CG  . ARG D  2 127 ? 38.390  -79.143 31.975  1.00 75.71  ? 127  ARG B CG  1 
ATOM   7554  C CD  . ARG D  2 127 ? 37.429  -80.236 32.327  1.00 81.86  ? 127  ARG B CD  1 
ATOM   7555  N NE  . ARG D  2 127 ? 36.049  -79.837 32.108  1.00 87.36  ? 127  ARG B NE  1 
ATOM   7556  C CZ  . ARG D  2 127 ? 35.299  -80.291 31.113  1.00 90.37  ? 127  ARG B CZ  1 
ATOM   7557  N NH1 . ARG D  2 127 ? 35.799  -81.159 30.246  1.00 87.55  ? 127  ARG B NH1 1 
ATOM   7558  N NH2 . ARG D  2 127 ? 34.046  -79.879 30.988  1.00 95.30  ? 127  ARG B NH2 1 
ATOM   7559  N N   . ASP D  2 128 ? 42.134  -80.685 32.660  1.00 79.75  ? 128  ASP B N   1 
ATOM   7560  C CA  . ASP D  2 128 ? 43.319  -81.449 33.062  1.00 80.28  ? 128  ASP B CA  1 
ATOM   7561  C C   . ASP D  2 128 ? 43.707  -82.607 32.116  1.00 82.13  ? 128  ASP B C   1 
ATOM   7562  O O   . ASP D  2 128 ? 44.483  -83.484 32.500  1.00 80.85  ? 128  ASP B O   1 
ATOM   7563  C CB  . ASP D  2 128 ? 43.145  -81.968 34.498  1.00 81.83  ? 128  ASP B CB  1 
ATOM   7564  C CG  . ASP D  2 128 ? 41.824  -82.682 34.722  1.00 80.07  ? 128  ASP B CG  1 
ATOM   7565  O OD1 . ASP D  2 128 ? 40.960  -82.660 33.815  1.00 79.94  ? 128  ASP B OD1 1 
ATOM   7566  O OD2 . ASP D  2 128 ? 41.650  -83.243 35.831  1.00 74.56  ? 128  ASP B OD2 1 
ATOM   7567  N N   . ASN D  2 129 ? 43.184  -82.596 30.886  1.00 84.58  ? 129  ASN B N   1 
ATOM   7568  C CA  . ASN D  2 129 ? 43.641  -83.519 29.845  1.00 81.64  ? 129  ASN B CA  1 
ATOM   7569  C C   . ASN D  2 129 ? 44.786  -82.890 29.069  1.00 85.62  ? 129  ASN B C   1 
ATOM   7570  O O   . ASN D  2 129 ? 45.333  -83.507 28.155  1.00 91.17  ? 129  ASN B O   1 
ATOM   7571  C CB  . ASN D  2 129 ? 42.520  -83.884 28.861  1.00 81.88  ? 129  ASN B CB  1 
ATOM   7572  C CG  . ASN D  2 129 ? 41.477  -84.816 29.454  1.00 87.52  ? 129  ASN B CG  1 
ATOM   7573  O OD1 . ASN D  2 129 ? 41.457  -85.077 30.659  1.00 89.54  ? 129  ASN B OD1 1 
ATOM   7574  N ND2 . ASN D  2 129 ? 40.597  -85.328 28.596  1.00 84.79  ? 129  ASN B ND2 1 
ATOM   7575  N N   . ALA D  2 130 ? 45.136  -81.661 29.448  1.00 82.92  ? 130  ALA B N   1 
ATOM   7576  C CA  . ALA D  2 130 ? 46.258  -80.937 28.863  1.00 80.87  ? 130  ALA B CA  1 
ATOM   7577  C C   . ALA D  2 130 ? 46.813  -79.927 29.861  1.00 82.70  ? 130  ALA B C   1 
ATOM   7578  O O   . ALA D  2 130 ? 46.180  -79.630 30.877  1.00 82.05  ? 130  ALA B O   1 
ATOM   7579  C CB  . ALA D  2 130 ? 45.833  -80.240 27.600  1.00 82.69  ? 130  ALA B CB  1 
ATOM   7580  N N   . LYS D  2 131 ? 47.986  -79.386 29.555  1.00 82.63  ? 131  LYS B N   1 
ATOM   7581  C CA  . LYS D  2 131 ? 48.600  -78.366 30.397  1.00 90.31  ? 131  LYS B CA  1 
ATOM   7582  C C   . LYS D  2 131 ? 48.813  -77.045 29.650  1.00 94.95  ? 131  LYS B C   1 
ATOM   7583  O O   . LYS D  2 131 ? 49.224  -77.044 28.487  1.00 92.44  ? 131  LYS B O   1 
ATOM   7584  C CB  . LYS D  2 131 ? 49.930  -78.868 30.952  1.00 89.74  ? 131  LYS B CB  1 
ATOM   7585  C CG  . LYS D  2 131 ? 50.912  -79.312 29.885  1.00 94.64  ? 131  LYS B CG  1 
ATOM   7586  C CD  . LYS D  2 131 ? 52.253  -79.656 30.504  1.00 98.90  ? 131  LYS B CD  1 
ATOM   7587  C CE  . LYS D  2 131 ? 52.826  -78.454 31.239  1.00 95.88  ? 131  LYS B CE  1 
ATOM   7588  N NZ  . LYS D  2 131 ? 54.108  -78.758 31.948  1.00 94.21  ? 131  LYS B NZ  1 
ATOM   7589  N N   . GLU D  2 132 ? 48.561  -75.927 30.331  1.00 96.66  ? 132  GLU B N   1 
ATOM   7590  C CA  . GLU D  2 132 ? 48.833  -74.609 29.759  1.00 92.49  ? 132  GLU B CA  1 
ATOM   7591  C C   . GLU D  2 132 ? 50.319  -74.344 29.872  1.00 89.81  ? 132  GLU B C   1 
ATOM   7592  O O   . GLU D  2 132 ? 50.867  -74.239 30.966  1.00 95.14  ? 132  GLU B O   1 
ATOM   7593  C CB  . GLU D  2 132 ? 48.055  -73.492 30.468  1.00 93.34  ? 132  GLU B CB  1 
ATOM   7594  C CG  . GLU D  2 132 ? 46.556  -73.703 30.583  1.00 96.27  ? 132  GLU B CG  1 
ATOM   7595  C CD  . GLU D  2 132 ? 45.830  -72.450 31.036  1.00 95.23  ? 132  GLU B CD  1 
ATOM   7596  O OE1 . GLU D  2 132 ? 46.327  -71.339 30.760  1.00 90.05  ? 132  GLU B OE1 1 
ATOM   7597  O OE2 . GLU D  2 132 ? 44.773  -72.581 31.689  1.00 99.29  ? 132  GLU B OE2 1 
ATOM   7598  N N   . LEU D  2 133 ? 50.972  -74.277 28.727  1.00 90.88  ? 133  LEU B N   1 
ATOM   7599  C CA  . LEU D  2 133 ? 52.402  -74.041 28.678  1.00 94.35  ? 133  LEU B CA  1 
ATOM   7600  C C   . LEU D  2 133 ? 52.721  -72.565 28.972  1.00 99.07  ? 133  LEU B C   1 
ATOM   7601  O O   . LEU D  2 133 ? 53.812  -72.238 29.451  1.00 100.13 ? 133  LEU B O   1 
ATOM   7602  C CB  . LEU D  2 133 ? 52.938  -74.492 27.321  1.00 95.92  ? 133  LEU B CB  1 
ATOM   7603  C CG  . LEU D  2 133 ? 52.933  -76.030 27.238  1.00 99.82  ? 133  LEU B CG  1 
ATOM   7604  C CD1 . LEU D  2 133 ? 53.021  -76.550 25.798  1.00 96.16  ? 133  LEU B CD1 1 
ATOM   7605  C CD2 . LEU D  2 133 ? 54.025  -76.640 28.116  1.00 94.96  ? 133  LEU B CD2 1 
ATOM   7606  N N   . GLY D  2 134 ? 51.755  -71.686 28.693  1.00 98.66  ? 134  GLY B N   1 
ATOM   7607  C CA  . GLY D  2 134 ? 51.867  -70.269 29.012  1.00 97.10  ? 134  GLY B CA  1 
ATOM   7608  C C   . GLY D  2 134 ? 52.177  -69.374 27.824  1.00 97.60  ? 134  GLY B C   1 
ATOM   7609  O O   . GLY D  2 134 ? 52.547  -68.203 27.985  1.00 94.86  ? 134  GLY B O   1 
ATOM   7610  N N   . ASN D  2 135 ? 51.992  -69.921 26.627  1.00 93.37  ? 135  ASN B N   1 
ATOM   7611  C CA  . ASN D  2 135 ? 52.263  -69.195 25.397  1.00 90.34  ? 135  ASN B CA  1 
ATOM   7612  C C   . ASN D  2 135 ? 51.150  -69.386 24.372  1.00 92.05  ? 135  ASN B C   1 
ATOM   7613  O O   . ASN D  2 135 ? 51.312  -69.058 23.196  1.00 90.57  ? 135  ASN B O   1 
ATOM   7614  C CB  . ASN D  2 135 ? 53.571  -69.679 24.792  1.00 90.23  ? 135  ASN B CB  1 
ATOM   7615  C CG  . ASN D  2 135 ? 53.494  -71.135 24.367  1.00 95.67  ? 135  ASN B CG  1 
ATOM   7616  O OD1 . ASN D  2 135 ? 52.650  -71.891 24.859  1.00 92.08  ? 135  ASN B OD1 1 
ATOM   7617  N ND2 . ASN D  2 135 ? 54.346  -71.528 23.422  1.00 97.89  ? 135  ASN B ND2 1 
ATOM   7618  N N   . GLY D  2 136 ? 50.020  -69.919 24.824  1.00 90.81  ? 136  GLY B N   1 
ATOM   7619  C CA  . GLY D  2 136 ? 48.889  -70.148 23.953  1.00 83.38  ? 136  GLY B CA  1 
ATOM   7620  C C   . GLY D  2 136 ? 48.802  -71.600 23.530  1.00 91.75  ? 136  GLY B C   1 
ATOM   7621  O O   . GLY D  2 136 ? 47.828  -72.006 22.886  1.00 89.68  ? 136  GLY B O   1 
ATOM   7622  N N   . CYS D  2 137 ? 49.799  -72.394 23.925  1.00 95.15  ? 137  CYS B N   1 
ATOM   7623  C CA  . CYS D  2 137 ? 49.880  -73.793 23.493  1.00 96.77  ? 137  CYS B CA  1 
ATOM   7624  C C   . CYS D  2 137 ? 49.403  -74.766 24.563  1.00 94.12  ? 137  CYS B C   1 
ATOM   7625  O O   . CYS D  2 137 ? 49.667  -74.582 25.749  1.00 92.96  ? 137  CYS B O   1 
ATOM   7626  C CB  . CYS D  2 137 ? 51.315  -74.158 23.103  1.00 96.90  ? 137  CYS B CB  1 
ATOM   7627  S SG  . CYS D  2 137 ? 51.955  -73.393 21.604  1.00 100.81 ? 137  CYS B SG  1 
ATOM   7628  N N   . PHE D  2 138 ? 48.732  -75.825 24.121  1.00 94.62  ? 138  PHE B N   1 
ATOM   7629  C CA  . PHE D  2 138 ? 48.257  -76.872 25.018  1.00 94.30  ? 138  PHE B CA  1 
ATOM   7630  C C   . PHE D  2 138 ? 48.916  -78.219 24.712  1.00 99.28  ? 138  PHE B C   1 
ATOM   7631  O O   . PHE D  2 138 ? 48.726  -78.770 23.633  1.00 101.93 ? 138  PHE B O   1 
ATOM   7632  C CB  . PHE D  2 138 ? 46.735  -76.998 24.919  1.00 90.27  ? 138  PHE B CB  1 
ATOM   7633  C CG  . PHE D  2 138 ? 45.995  -75.812 25.466  1.00 93.90  ? 138  PHE B CG  1 
ATOM   7634  C CD1 . PHE D  2 138 ? 46.625  -74.921 26.323  1.00 92.36  ? 138  PHE B CD1 1 
ATOM   7635  C CD2 . PHE D  2 138 ? 44.667  -75.589 25.128  1.00 95.22  ? 138  PHE B CD2 1 
ATOM   7636  C CE1 . PHE D  2 138 ? 45.951  -73.827 26.832  1.00 92.31  ? 138  PHE B CE1 1 
ATOM   7637  C CE2 . PHE D  2 138 ? 43.980  -74.494 25.640  1.00 92.50  ? 138  PHE B CE2 1 
ATOM   7638  C CZ  . PHE D  2 138 ? 44.624  -73.613 26.492  1.00 90.25  ? 138  PHE B CZ  1 
ATOM   7639  N N   . GLU D  2 139 ? 49.652  -78.755 25.687  1.00 102.75 ? 139  GLU B N   1 
ATOM   7640  C CA  . GLU D  2 139 ? 50.304  -80.069 25.587  1.00 98.32  ? 139  GLU B CA  1 
ATOM   7641  C C   . GLU D  2 139 ? 49.467  -81.161 26.244  1.00 94.08  ? 139  GLU B C   1 
ATOM   7642  O O   . GLU D  2 139 ? 49.234  -81.117 27.456  1.00 92.81  ? 139  GLU B O   1 
ATOM   7643  C CB  . GLU D  2 139 ? 51.698  -80.028 26.223  1.00 97.74  ? 139  GLU B CB  1 
ATOM   7644  C CG  . GLU D  2 139 ? 52.521  -81.295 26.013  1.00 99.80  ? 139  GLU B CG  1 
ATOM   7645  C CD  . GLU D  2 139 ? 53.928  -81.188 26.593  1.00 105.68 ? 139  GLU B CD  1 
ATOM   7646  O OE1 . GLU D  2 139 ? 54.081  -80.702 27.739  1.00 96.02  ? 139  GLU B OE1 1 
ATOM   7647  O OE2 . GLU D  2 139 ? 54.884  -81.583 25.889  1.00 113.37 ? 139  GLU B OE2 1 
ATOM   7648  N N   . PHE D  2 140 ? 48.988  -82.119 25.450  1.00 95.07  ? 140  PHE B N   1 
ATOM   7649  C CA  . PHE D  2 140 ? 48.073  -83.130 25.983  1.00 98.54  ? 140  PHE B CA  1 
ATOM   7650  C C   . PHE D  2 140 ? 48.778  -84.134 26.918  1.00 99.59  ? 140  PHE B C   1 
ATOM   7651  O O   . PHE D  2 140 ? 49.995  -84.345 26.827  1.00 100.16 ? 140  PHE B O   1 
ATOM   7652  C CB  . PHE D  2 140 ? 47.406  -83.927 24.844  1.00 96.11  ? 140  PHE B CB  1 
ATOM   7653  C CG  . PHE D  2 140 ? 46.475  -83.130 23.955  1.00 98.53  ? 140  PHE B CG  1 
ATOM   7654  C CD1 . PHE D  2 140 ? 46.967  -82.388 22.891  1.00 99.86  ? 140  PHE B CD1 1 
ATOM   7655  C CD2 . PHE D  2 140 ? 45.096  -83.196 24.137  1.00 96.75  ? 140  PHE B CD2 1 
ATOM   7656  C CE1 . PHE D  2 140 ? 46.107  -81.682 22.059  1.00 95.89  ? 140  PHE B CE1 1 
ATOM   7657  C CE2 . PHE D  2 140 ? 44.232  -82.498 23.309  1.00 92.20  ? 140  PHE B CE2 1 
ATOM   7658  C CZ  . PHE D  2 140 ? 44.740  -81.738 22.268  1.00 90.62  ? 140  PHE B CZ  1 
ATOM   7659  N N   . TYR D  2 141 ? 47.985  -84.776 27.781  1.00 95.64  ? 141  TYR B N   1 
ATOM   7660  C CA  . TYR D  2 141 ? 48.461  -85.798 28.721  1.00 95.95  ? 141  TYR B CA  1 
ATOM   7661  C C   . TYR D  2 141 ? 48.152  -87.138 28.088  1.00 96.22  ? 141  TYR B C   1 
ATOM   7662  O O   . TYR D  2 141 ? 48.204  -88.192 28.717  1.00 95.29  ? 141  TYR B O   1 
ATOM   7663  C CB  . TYR D  2 141 ? 47.812  -85.666 30.111  1.00 91.92  ? 141  TYR B CB  1 
ATOM   7664  C CG  . TYR D  2 141 ? 48.459  -84.620 31.000  1.00 90.08  ? 141  TYR B CG  1 
ATOM   7665  C CD1 . TYR D  2 141 ? 49.845  -84.497 31.054  1.00 87.56  ? 141  TYR B CD1 1 
ATOM   7666  C CD2 . TYR D  2 141 ? 47.691  -83.753 31.775  1.00 84.26  ? 141  TYR B CD2 1 
ATOM   7667  C CE1 . TYR D  2 141 ? 50.450  -83.550 31.855  1.00 88.51  ? 141  TYR B CE1 1 
ATOM   7668  C CE2 . TYR D  2 141 ? 48.290  -82.795 32.576  1.00 82.72  ? 141  TYR B CE2 1 
ATOM   7669  C CZ  . TYR D  2 141 ? 49.671  -82.704 32.617  1.00 85.19  ? 141  TYR B CZ  1 
ATOM   7670  O OH  . TYR D  2 141 ? 50.287  -81.767 33.410  1.00 80.63  ? 141  TYR B OH  1 
ATOM   7671  N N   . HIS D  2 142 ? 47.787  -87.059 26.820  1.00 98.57  ? 142  HIS B N   1 
ATOM   7672  C CA  . HIS D  2 142 ? 47.579  -88.224 25.999  1.00 96.06  ? 142  HIS B CA  1 
ATOM   7673  C C   . HIS D  2 142 ? 47.996  -87.853 24.590  1.00 96.59  ? 142  HIS B C   1 
ATOM   7674  O O   . HIS D  2 142 ? 48.564  -86.784 24.361  1.00 93.45  ? 142  HIS B O   1 
ATOM   7675  C CB  . HIS D  2 142 ? 46.114  -88.677 26.060  1.00 92.34  ? 142  HIS B CB  1 
ATOM   7676  C CG  . HIS D  2 142 ? 45.135  -87.622 25.645  1.00 96.97  ? 142  HIS B CG  1 
ATOM   7677  N ND1 . HIS D  2 142 ? 44.884  -87.311 24.325  1.00 97.14  ? 142  HIS B ND1 1 
ATOM   7678  C CD2 . HIS D  2 142 ? 44.337  -86.810 26.382  1.00 95.79  ? 142  HIS B CD2 1 
ATOM   7679  C CE1 . HIS D  2 142 ? 43.980  -86.349 24.267  1.00 96.12  ? 142  HIS B CE1 1 
ATOM   7680  N NE2 . HIS D  2 142 ? 43.630  -86.028 25.500  1.00 95.94  ? 142  HIS B NE2 1 
ATOM   7681  N N   . ARG D  2 143 ? 47.736  -88.742 23.645  1.00 98.78  ? 143  ARG B N   1 
ATOM   7682  C CA  . ARG D  2 143 ? 48.033  -88.434 22.264  1.00 99.20  ? 143  ARG B CA  1 
ATOM   7683  C C   . ARG D  2 143 ? 46.753  -88.190 21.500  1.00 97.44  ? 143  ARG B C   1 
ATOM   7684  O O   . ARG D  2 143 ? 45.741  -88.862 21.712  1.00 92.31  ? 143  ARG B O   1 
ATOM   7685  C CB  . ARG D  2 143 ? 48.909  -89.514 21.627  1.00 100.18 ? 143  ARG B CB  1 
ATOM   7686  C CG  . ARG D  2 143 ? 50.352  -89.285 22.022  1.00 103.31 ? 143  ARG B CG  1 
ATOM   7687  C CD  . ARG D  2 143 ? 51.375  -90.222 21.409  1.00 100.51 ? 143  ARG B CD  1 
ATOM   7688  N NE  . ARG D  2 143 ? 52.702  -89.632 21.611  1.00 102.18 ? 143  ARG B NE  1 
ATOM   7689  C CZ  . ARG D  2 143 ? 53.370  -89.636 22.767  1.00 105.18 ? 143  ARG B CZ  1 
ATOM   7690  N NH1 . ARG D  2 143 ? 52.846  -90.234 23.842  1.00 105.69 ? 143  ARG B NH1 1 
ATOM   7691  N NH2 . ARG D  2 143 ? 54.571  -89.048 22.852  1.00 109.30 ? 143  ARG B NH2 1 
ATOM   7692  N N   . CYS D  2 144 ? 46.814  -87.211 20.608  1.00 99.82  ? 144  CYS B N   1 
ATOM   7693  C CA  . CYS D  2 144 ? 45.641  -86.805 19.863  1.00 103.88 ? 144  CYS B CA  1 
ATOM   7694  C C   . CYS D  2 144 ? 45.936  -86.886 18.371  1.00 103.58 ? 144  CYS B C   1 
ATOM   7695  O O   . CYS D  2 144 ? 46.812  -86.184 17.855  1.00 100.20 ? 144  CYS B O   1 
ATOM   7696  C CB  . CYS D  2 144 ? 45.233  -85.385 20.280  1.00 100.84 ? 144  CYS B CB  1 
ATOM   7697  S SG  . CYS D  2 144 ? 43.528  -84.927 19.882  1.00 98.04  ? 144  CYS B SG  1 
ATOM   7698  N N   . ASP D  2 145 ? 45.182  -87.738 17.681  1.00 107.19 ? 145  ASP B N   1 
ATOM   7699  C CA  . ASP D  2 145 ? 45.361  -87.938 16.249  1.00 108.68 ? 145  ASP B CA  1 
ATOM   7700  C C   . ASP D  2 145 ? 44.841  -86.732 15.477  1.00 108.27 ? 145  ASP B C   1 
ATOM   7701  O O   . ASP D  2 145 ? 44.704  -85.647 16.029  1.00 106.51 ? 145  ASP B O   1 
ATOM   7702  C CB  . ASP D  2 145 ? 44.637  -89.210 15.787  1.00 107.76 ? 145  ASP B CB  1 
ATOM   7703  C CG  . ASP D  2 145 ? 43.188  -89.265 16.257  1.00 106.67 ? 145  ASP B CG  1 
ATOM   7704  O OD1 . ASP D  2 145 ? 42.890  -88.729 17.345  1.00 107.30 ? 145  ASP B OD1 1 
ATOM   7705  O OD2 . ASP D  2 145 ? 42.345  -89.829 15.527  1.00 104.48 ? 145  ASP B OD2 1 
ATOM   7706  N N   . ASN D  2 146 ? 44.548  -86.926 14.198  1.00 109.64 ? 146  ASN B N   1 
ATOM   7707  C CA  . ASN D  2 146 ? 43.925  -85.878 13.404  1.00 105.78 ? 146  ASN B CA  1 
ATOM   7708  C C   . ASN D  2 146 ? 42.413  -86.125 13.256  1.00 108.41 ? 146  ASN B C   1 
ATOM   7709  O O   . ASN D  2 146 ? 41.847  -86.033 12.165  1.00 111.51 ? 146  ASN B O   1 
ATOM   7710  C CB  . ASN D  2 146 ? 44.630  -85.753 12.048  1.00 102.83 ? 146  ASN B CB  1 
ATOM   7711  C CG  . ASN D  2 146 ? 46.100  -85.347 12.189  1.00 100.07 ? 146  ASN B CG  1 
ATOM   7712  O OD1 . ASN D  2 146 ? 46.690  -85.467 13.265  1.00 99.01  ? 146  ASN B OD1 1 
ATOM   7713  N ND2 . ASN D  2 146 ? 46.687  -84.850 11.106  1.00 101.09 ? 146  ASN B ND2 1 
ATOM   7714  N N   . GLU D  2 147 ? 41.781  -86.461 14.377  1.00 106.50 ? 147  GLU B N   1 
ATOM   7715  C CA  . GLU D  2 147 ? 40.331  -86.604 14.469  1.00 110.51 ? 147  GLU B CA  1 
ATOM   7716  C C   . GLU D  2 147 ? 39.894  -86.215 15.877  1.00 116.32 ? 147  GLU B C   1 
ATOM   7717  O O   . GLU D  2 147 ? 38.705  -85.996 16.156  1.00 116.18 ? 147  GLU B O   1 
ATOM   7718  C CB  . GLU D  2 147 ? 39.878  -88.032 14.165  1.00 113.15 ? 147  GLU B CB  1 
ATOM   7719  C CG  . GLU D  2 147 ? 38.377  -88.127 13.901  1.00 117.93 ? 147  GLU B CG  1 
ATOM   7720  C CD  . GLU D  2 147 ? 37.908  -89.526 13.560  1.00 119.28 ? 147  GLU B CD  1 
ATOM   7721  O OE1 . GLU D  2 147 ? 38.757  -90.442 13.461  1.00 114.35 ? 147  GLU B OE1 1 
ATOM   7722  O OE2 . GLU D  2 147 ? 36.680  -89.701 13.399  1.00 118.18 ? 147  GLU B OE2 1 
ATOM   7723  N N   . CYS D  2 148 ? 40.880  -86.135 16.763  1.00 113.68 ? 148  CYS B N   1 
ATOM   7724  C CA  . CYS D  2 148 ? 40.688  -85.575 18.089  1.00 111.22 ? 148  CYS B CA  1 
ATOM   7725  C C   . CYS D  2 148 ? 40.757  -84.057 17.963  1.00 104.34 ? 148  CYS B C   1 
ATOM   7726  O O   . CYS D  2 148 ? 39.876  -83.343 18.441  1.00 101.04 ? 148  CYS B O   1 
ATOM   7727  C CB  . CYS D  2 148 ? 41.739  -86.111 19.065  1.00 111.64 ? 148  CYS B CB  1 
ATOM   7728  S SG  . CYS D  2 148 ? 41.713  -85.355 20.696  1.00 106.58 ? 148  CYS B SG  1 
ATOM   7729  N N   . MET D  2 149 ? 41.820  -83.592 17.302  1.00 102.97 ? 149  MET B N   1 
ATOM   7730  C CA  . MET D  2 149 ? 42.046  -82.181 17.007  1.00 100.18 ? 149  MET B CA  1 
ATOM   7731  C C   . MET D  2 149 ? 40.814  -81.488 16.421  1.00 104.88 ? 149  MET B C   1 
ATOM   7732  O O   . MET D  2 149 ? 40.538  -80.335 16.743  1.00 104.35 ? 149  MET B O   1 
ATOM   7733  C CB  . MET D  2 149 ? 43.211  -82.030 16.025  1.00 96.49  ? 149  MET B CB  1 
ATOM   7734  C CG  . MET D  2 149 ? 44.520  -82.658 16.463  1.00 89.73  ? 149  MET B CG  1 
ATOM   7735  S SD  . MET D  2 149 ? 45.209  -81.964 17.964  1.00 87.34  ? 149  MET B SD  1 
ATOM   7736  C CE  . MET D  2 149 ? 46.933  -82.423 17.863  1.00 95.19  ? 149  MET B CE  1 
ATOM   7737  N N   . GLU D  2 150 ? 40.100  -82.184 15.538  1.00 106.62 ? 150  GLU B N   1 
ATOM   7738  C CA  . GLU D  2 150 ? 38.893  -81.640 14.916  1.00 104.51 ? 150  GLU B CA  1 
ATOM   7739  C C   . GLU D  2 150 ? 37.733  -81.457 15.878  1.00 105.56 ? 150  GLU B C   1 
ATOM   7740  O O   . GLU D  2 150 ? 36.953  -80.514 15.740  1.00 106.59 ? 150  GLU B O   1 
ATOM   7741  C CB  . GLU D  2 150 ? 38.446  -82.521 13.751  1.00 108.45 ? 150  GLU B CB  1 
ATOM   7742  C CG  . GLU D  2 150 ? 39.063  -82.100 12.430  1.00 110.84 ? 150  GLU B CG  1 
ATOM   7743  C CD  . GLU D  2 150 ? 39.121  -80.589 12.280  1.00 107.78 ? 150  GLU B CD  1 
ATOM   7744  O OE1 . GLU D  2 150 ? 38.054  -79.939 12.273  1.00 109.68 ? 150  GLU B OE1 1 
ATOM   7745  O OE2 . GLU D  2 150 ? 40.241  -80.049 12.186  1.00 106.61 ? 150  GLU B OE2 1 
ATOM   7746  N N   . SER D  2 151 ? 37.618  -82.364 16.844  1.00 108.80 ? 151  SER B N   1 
ATOM   7747  C CA  . SER D  2 151 ? 36.501  -82.348 17.792  1.00 108.34 ? 151  SER B CA  1 
ATOM   7748  C C   . SER D  2 151 ? 36.554  -81.133 18.733  1.00 102.79 ? 151  SER B C   1 
ATOM   7749  O O   . SER D  2 151 ? 35.534  -80.734 19.298  1.00 98.54  ? 151  SER B O   1 
ATOM   7750  C CB  . SER D  2 151 ? 36.461  -83.660 18.593  1.00 103.21 ? 151  SER B CB  1 
ATOM   7751  O OG  . SER D  2 151 ? 37.376  -83.646 19.671  1.00 105.17 ? 151  SER B OG  1 
ATOM   7752  N N   . VAL D  2 152 ? 37.741  -80.559 18.915  1.00 99.46  ? 152  VAL B N   1 
ATOM   7753  C CA  . VAL D  2 152 ? 37.856  -79.368 19.742  1.00 101.42 ? 152  VAL B CA  1 
ATOM   7754  C C   . VAL D  2 152 ? 37.519  -78.141 18.886  1.00 102.02 ? 152  VAL B C   1 
ATOM   7755  O O   . VAL D  2 152 ? 36.886  -77.195 19.362  1.00 100.38 ? 152  VAL B O   1 
ATOM   7756  C CB  . VAL D  2 152 ? 39.277  -79.225 20.399  1.00 100.05 ? 152  VAL B CB  1 
ATOM   7757  C CG1 . VAL D  2 152 ? 39.624  -80.461 21.206  1.00 99.34  ? 152  VAL B CG1 1 
ATOM   7758  C CG2 . VAL D  2 152 ? 40.371  -78.952 19.377  1.00 93.12  ? 152  VAL B CG2 1 
ATOM   7759  N N   . ARG D  2 153 ? 37.905  -78.185 17.613  1.00 102.29 ? 153  ARG B N   1 
ATOM   7760  C CA  . ARG D  2 153 ? 37.698  -77.070 16.692  1.00 101.14 ? 153  ARG B CA  1 
ATOM   7761  C C   . ARG D  2 153 ? 36.232  -76.913 16.268  1.00 102.82 ? 153  ARG B C   1 
ATOM   7762  O O   . ARG D  2 153 ? 35.826  -75.830 15.838  1.00 109.49 ? 153  ARG B O   1 
ATOM   7763  C CB  . ARG D  2 153 ? 38.611  -77.218 15.472  1.00 100.64 ? 153  ARG B CB  1 
ATOM   7764  C CG  . ARG D  2 153 ? 40.075  -76.921 15.795  1.00 100.09 ? 153  ARG B CG  1 
ATOM   7765  C CD  . ARG D  2 153 ? 40.984  -77.006 14.571  1.00 103.03 ? 153  ARG B CD  1 
ATOM   7766  N NE  . ARG D  2 153 ? 41.255  -78.377 14.160  1.00 106.61 ? 153  ARG B NE  1 
ATOM   7767  C CZ  . ARG D  2 153 ? 42.421  -78.793 13.674  1.00 105.89 ? 153  ARG B CZ  1 
ATOM   7768  N NH1 . ARG D  2 153 ? 43.425  -77.935 13.523  1.00 104.54 ? 153  ARG B NH1 1 
ATOM   7769  N NH2 . ARG D  2 153 ? 42.577  -80.065 13.330  1.00 101.48 ? 153  ARG B NH2 1 
ATOM   7770  N N   . ASN D  2 154 ? 35.443  -77.983 16.360  1.00 98.22  ? 154  ASN B N   1 
ATOM   7771  C CA  . ASN D  2 154 ? 34.007  -77.849 16.134  1.00 98.81  ? 154  ASN B CA  1 
ATOM   7772  C C   . ASN D  2 154 ? 33.289  -77.960 17.477  1.00 100.75 ? 154  ASN B C   1 
ATOM   7773  O O   . ASN D  2 154 ? 32.062  -78.045 17.542  1.00 103.72 ? 154  ASN B O   1 
ATOM   7774  C CB  . ASN D  2 154 ? 33.470  -78.892 15.130  1.00 107.50 ? 154  ASN B CB  1 
ATOM   7775  C CG  . ASN D  2 154 ? 33.766  -80.345 15.528  1.00 106.09 ? 154  ASN B CG  1 
ATOM   7776  O OD1 . ASN D  2 154 ? 33.270  -80.841 16.539  1.00 103.45 ? 154  ASN B OD1 1 
ATOM   7777  N ND2 . ASN D  2 154 ? 34.558  -81.036 14.708  1.00 109.41 ? 154  ASN B ND2 1 
ATOM   7778  N N   . GLY D  2 155 ? 34.074  -77.954 18.550  1.00 102.35 ? 155  GLY B N   1 
ATOM   7779  C CA  . GLY D  2 155 ? 33.544  -77.944 19.903  1.00 101.77 ? 155  GLY B CA  1 
ATOM   7780  C C   . GLY D  2 155 ? 32.696  -79.139 20.307  1.00 103.02 ? 155  GLY B C   1 
ATOM   7781  O O   . GLY D  2 155 ? 31.597  -78.960 20.836  1.00 105.65 ? 155  GLY B O   1 
ATOM   7782  N N   . THR D  2 156 ? 33.204  -80.349 20.067  1.00 104.48 ? 156  THR B N   1 
ATOM   7783  C CA  . THR D  2 156 ? 32.509  -81.592 20.440  1.00 107.03 ? 156  THR B CA  1 
ATOM   7784  C C   . THR D  2 156 ? 33.356  -82.520 21.328  1.00 110.56 ? 156  THR B C   1 
ATOM   7785  O O   . THR D  2 156 ? 32.840  -83.529 21.828  1.00 109.38 ? 156  THR B O   1 
ATOM   7786  C CB  . THR D  2 156 ? 32.058  -82.402 19.201  1.00 102.36 ? 156  THR B CB  1 
ATOM   7787  O OG1 . THR D  2 156 ? 33.122  -82.443 18.242  1.00 105.17 ? 156  THR B OG1 1 
ATOM   7788  C CG2 . THR D  2 156 ? 30.823  -81.787 18.566  1.00 101.28 ? 156  THR B CG2 1 
ATOM   7789  N N   . TYR D  2 157 ? 34.637  -82.173 21.503  1.00 107.71 ? 157  TYR B N   1 
ATOM   7790  C CA  . TYR D  2 157 ? 35.616  -82.939 22.293  1.00 103.14 ? 157  TYR B CA  1 
ATOM   7791  C C   . TYR D  2 157 ? 35.016  -83.619 23.524  1.00 108.19 ? 157  TYR B C   1 
ATOM   7792  O O   . TYR D  2 157 ? 34.644  -82.961 24.499  1.00 106.38 ? 157  TYR B O   1 
ATOM   7793  C CB  . TYR D  2 157 ? 36.760  -82.008 22.712  1.00 100.23 ? 157  TYR B CB  1 
ATOM   7794  C CG  . TYR D  2 157 ? 37.839  -82.611 23.599  1.00 102.97 ? 157  TYR B CG  1 
ATOM   7795  C CD1 . TYR D  2 157 ? 38.925  -83.298 23.055  1.00 101.82 ? 157  TYR B CD1 1 
ATOM   7796  C CD2 . TYR D  2 157 ? 37.797  -82.449 24.987  1.00 104.29 ? 157  TYR B CD2 1 
ATOM   7797  C CE1 . TYR D  2 157 ? 39.929  -83.830 23.870  1.00 100.44 ? 157  TYR B CE1 1 
ATOM   7798  C CE2 . TYR D  2 157 ? 38.792  -82.979 25.812  1.00 99.07  ? 157  TYR B CE2 1 
ATOM   7799  C CZ  . TYR D  2 157 ? 39.855  -83.668 25.248  1.00 100.97 ? 157  TYR B CZ  1 
ATOM   7800  O OH  . TYR D  2 157 ? 40.836  -84.188 26.066  1.00 94.95  ? 157  TYR B OH  1 
ATOM   7801  N N   . ASP D  2 158 ? 34.935  -84.949 23.455  1.00 111.33 ? 158  ASP B N   1 
ATOM   7802  C CA  . ASP D  2 158 ? 34.354  -85.768 24.518  1.00 110.73 ? 158  ASP B CA  1 
ATOM   7803  C C   . ASP D  2 158 ? 35.389  -85.950 25.627  1.00 109.02 ? 158  ASP B C   1 
ATOM   7804  O O   . ASP D  2 158 ? 36.377  -86.673 25.465  1.00 107.61 ? 158  ASP B O   1 
ATOM   7805  C CB  . ASP D  2 158 ? 33.903  -87.124 23.950  1.00 110.37 ? 158  ASP B CB  1 
ATOM   7806  C CG  . ASP D  2 158 ? 32.887  -87.836 24.835  1.00 111.17 ? 158  ASP B CG  1 
ATOM   7807  O OD1 . ASP D  2 158 ? 32.785  -87.516 26.042  1.00 110.60 ? 158  ASP B OD1 1 
ATOM   7808  O OD2 . ASP D  2 158 ? 32.185  -88.726 24.306  1.00 111.59 ? 158  ASP B OD2 1 
ATOM   7809  N N   . TYR D  2 159 ? 35.173  -85.259 26.742  1.00 105.10 ? 159  TYR B N   1 
ATOM   7810  C CA  . TYR D  2 159 ? 36.166  -85.224 27.809  1.00 105.56 ? 159  TYR B CA  1 
ATOM   7811  C C   . TYR D  2 159 ? 36.329  -86.558 28.557  1.00 105.04 ? 159  TYR B C   1 
ATOM   7812  O O   . TYR D  2 159 ? 37.444  -87.092 28.604  1.00 102.86 ? 159  TYR B O   1 
ATOM   7813  C CB  . TYR D  2 159 ? 35.841  -84.103 28.807  1.00 99.50  ? 159  TYR B CB  1 
ATOM   7814  C CG  . TYR D  2 159 ? 36.669  -84.154 30.072  1.00 92.63  ? 159  TYR B CG  1 
ATOM   7815  C CD1 . TYR D  2 159 ? 37.999  -83.748 30.062  1.00 87.97  ? 159  TYR B CD1 1 
ATOM   7816  C CD2 . TYR D  2 159 ? 36.134  -84.626 31.264  1.00 91.55  ? 159  TYR B CD2 1 
ATOM   7817  C CE1 . TYR D  2 159 ? 38.766  -83.788 31.203  1.00 85.63  ? 159  TYR B CE1 1 
ATOM   7818  C CE2 . TYR D  2 159 ? 36.898  -84.673 32.414  1.00 87.60  ? 159  TYR B CE2 1 
ATOM   7819  C CZ  . TYR D  2 159 ? 38.216  -84.253 32.376  1.00 84.36  ? 159  TYR B CZ  1 
ATOM   7820  O OH  . TYR D  2 159 ? 38.994  -84.282 33.511  1.00 78.86  ? 159  TYR B OH  1 
ATOM   7821  N N   . PRO D  2 160 ? 35.226  -87.114 29.124  1.00 105.84 ? 160  PRO B N   1 
ATOM   7822  C CA  . PRO D  2 160 ? 35.398  -88.307 29.968  1.00 105.70 ? 160  PRO B CA  1 
ATOM   7823  C C   . PRO D  2 160 ? 35.949  -89.528 29.235  1.00 104.82 ? 160  PRO B C   1 
ATOM   7824  O O   . PRO D  2 160 ? 36.464  -90.443 29.881  1.00 104.23 ? 160  PRO B O   1 
ATOM   7825  C CB  . PRO D  2 160 ? 33.972  -88.589 30.469  1.00 105.12 ? 160  PRO B CB  1 
ATOM   7826  C CG  . PRO D  2 160 ? 33.250  -87.298 30.331  1.00 103.31 ? 160  PRO B CG  1 
ATOM   7827  C CD  . PRO D  2 160 ? 33.809  -86.704 29.079  1.00 105.28 ? 160  PRO B CD  1 
ATOM   7828  N N   . GLN D  2 161 ? 35.816  -89.543 27.912  1.00 104.90 ? 161  GLN B N   1 
ATOM   7829  C CA  . GLN D  2 161 ? 36.279  -90.657 27.090  1.00 108.31 ? 161  GLN B CA  1 
ATOM   7830  C C   . GLN D  2 161 ? 37.813  -90.729 26.997  1.00 106.30 ? 161  GLN B C   1 
ATOM   7831  O O   . GLN D  2 161 ? 38.365  -91.715 26.501  1.00 110.95 ? 161  GLN B O   1 
ATOM   7832  C CB  . GLN D  2 161 ? 35.669  -90.557 25.683  1.00 111.61 ? 161  GLN B CB  1 
ATOM   7833  C CG  . GLN D  2 161 ? 35.912  -91.770 24.790  1.00 111.56 ? 161  GLN B CG  1 
ATOM   7834  C CD  . GLN D  2 161 ? 35.312  -91.620 23.410  1.00 111.49 ? 161  GLN B CD  1 
ATOM   7835  O OE1 . GLN D  2 161 ? 34.465  -90.756 23.179  1.00 110.25 ? 161  GLN B OE1 1 
ATOM   7836  N NE2 . GLN D  2 161 ? 35.752  -92.464 22.479  1.00 113.28 ? 161  GLN B NE2 1 
ATOM   7837  N N   . TYR D  2 162 ? 38.509  -89.701 27.478  1.00 101.12 ? 162  TYR B N   1 
ATOM   7838  C CA  . TYR D  2 162 ? 39.970  -89.702 27.389  1.00 102.30 ? 162  TYR B CA  1 
ATOM   7839  C C   . TYR D  2 162 ? 40.613  -89.281 28.704  1.00 99.97  ? 162  TYR B C   1 
ATOM   7840  O O   . TYR D  2 162 ? 41.835  -89.149 28.804  1.00 98.72  ? 162  TYR B O   1 
ATOM   7841  C CB  . TYR D  2 162 ? 40.422  -88.822 26.217  1.00 101.23 ? 162  TYR B CB  1 
ATOM   7842  C CG  . TYR D  2 162 ? 39.830  -89.358 24.933  1.00 112.39 ? 162  TYR B CG  1 
ATOM   7843  C CD1 . TYR D  2 162 ? 40.436  -90.412 24.255  1.00 114.91 ? 162  TYR B CD1 1 
ATOM   7844  C CD2 . TYR D  2 162 ? 38.640  -88.849 24.425  1.00 114.06 ? 162  TYR B CD2 1 
ATOM   7845  C CE1 . TYR D  2 162 ? 39.880  -90.934 23.101  1.00 113.75 ? 162  TYR B CE1 1 
ATOM   7846  C CE2 . TYR D  2 162 ? 38.078  -89.362 23.271  1.00 114.00 ? 162  TYR B CE2 1 
ATOM   7847  C CZ  . TYR D  2 162 ? 38.703  -90.402 22.614  1.00 112.95 ? 162  TYR B CZ  1 
ATOM   7848  O OH  . TYR D  2 162 ? 38.147  -90.910 21.465  1.00 115.13 ? 162  TYR B OH  1 
ATOM   7849  N N   . SER D  2 163 ? 39.768  -89.084 29.711  1.00 99.15  ? 163  SER B N   1 
ATOM   7850  C CA  . SER D  2 163 ? 40.190  -88.608 31.024  1.00 100.14 ? 163  SER B CA  1 
ATOM   7851  C C   . SER D  2 163 ? 41.152  -89.550 31.769  1.00 103.08 ? 163  SER B C   1 
ATOM   7852  O O   . SER D  2 163 ? 42.042  -89.092 32.492  1.00 99.87  ? 163  SER B O   1 
ATOM   7853  C CB  . SER D  2 163 ? 38.951  -88.346 31.884  1.00 94.70  ? 163  SER B CB  1 
ATOM   7854  O OG  . SER D  2 163 ? 38.060  -89.447 31.847  1.00 97.82  ? 163  SER B OG  1 
ATOM   7855  N N   . GLU D  2 164 ? 40.986  -90.857 31.572  1.00 107.28 ? 164  GLU B N   1 
ATOM   7856  C CA  . GLU D  2 164 ? 41.735  -91.871 32.326  1.00 104.37 ? 164  GLU B CA  1 
ATOM   7857  C C   . GLU D  2 164 ? 43.195  -91.938 31.866  1.00 100.52 ? 164  GLU B C   1 
ATOM   7858  O O   . GLU D  2 164 ? 44.107  -91.916 32.695  1.00 97.13  ? 164  GLU B O   1 
ATOM   7859  C CB  . GLU D  2 164 ? 41.072  -93.257 32.206  1.00 103.94 ? 164  GLU B CB  1 
ATOM   7860  C CG  . GLU D  2 164 ? 41.009  -93.853 30.790  1.00 114.08 ? 164  GLU B CG  1 
ATOM   7861  C CD  . GLU D  2 164 ? 40.122  -93.073 29.836  1.00 107.57 ? 164  GLU B CD  1 
ATOM   7862  O OE1 . GLU D  2 164 ? 39.178  -92.404 30.316  1.00 104.86 ? 164  GLU B OE1 1 
ATOM   7863  O OE2 . GLU D  2 164 ? 40.396  -93.113 28.612  1.00 106.54 ? 164  GLU B OE2 1 
ATOM   7864  N N   . GLU D  2 165 ? 43.400  -92.061 30.554  1.00 98.83  ? 165  GLU B N   1 
ATOM   7865  C CA  . GLU D  2 165 ? 44.731  -92.095 29.958  1.00 95.14  ? 165  GLU B CA  1 
ATOM   7866  C C   . GLU D  2 165 ? 45.559  -90.886 30.374  1.00 100.69 ? 165  GLU B C   1 
ATOM   7867  O O   . GLU D  2 165 ? 46.755  -91.006 30.670  1.00 99.11  ? 165  GLU B O   1 
ATOM   7868  C CB  . GLU D  2 165 ? 44.629  -92.128 28.435  1.00 90.72  ? 165  GLU B CB  1 
ATOM   7869  C CG  . GLU D  2 165 ? 45.973  -92.054 27.734  1.00 80.83  ? 165  GLU B CG  1 
ATOM   7870  C CD  . GLU D  2 165 ? 45.833  -92.064 26.233  1.00 83.29  ? 165  GLU B CD  1 
ATOM   7871  O OE1 . GLU D  2 165 ? 44.681  -92.175 25.751  1.00 81.39  ? 165  GLU B OE1 1 
ATOM   7872  O OE2 . GLU D  2 165 ? 46.871  -91.954 25.539  1.00 84.16  ? 165  GLU B OE2 1 
ATOM   7873  N N   . ALA D  2 166 ? 44.906  -89.722 30.378  1.00 101.96 ? 166  ALA B N   1 
ATOM   7874  C CA  . ALA D  2 166 ? 45.524  -88.473 30.812  1.00 99.49  ? 166  ALA B CA  1 
ATOM   7875  C C   . ALA D  2 166 ? 45.847  -88.522 32.313  1.00 95.15  ? 166  ALA B C   1 
ATOM   7876  O O   . ALA D  2 166 ? 46.956  -88.172 32.730  1.00 91.76  ? 166  ALA B O   1 
ATOM   7877  C CB  . ALA D  2 166 ? 44.615  -87.292 30.484  1.00 96.23  ? 166  ALA B CB  1 
ATOM   7878  N N   . ARG D  2 167 ? 44.865  -88.936 33.112  1.00 94.22  ? 167  ARG B N   1 
ATOM   7879  C CA  . ARG D  2 167 ? 45.025  -89.052 34.561  1.00 93.79  ? 167  ARG B CA  1 
ATOM   7880  C C   . ARG D  2 167 ? 46.171  -89.999 34.940  1.00 95.52  ? 167  ARG B C   1 
ATOM   7881  O O   . ARG D  2 167 ? 46.933  -89.721 35.866  1.00 91.80  ? 167  ARG B O   1 
ATOM   7882  C CB  . ARG D  2 167 ? 43.710  -89.515 35.198  1.00 96.50  ? 167  ARG B CB  1 
ATOM   7883  C CG  . ARG D  2 167 ? 43.732  -89.641 36.719  1.00 101.83 ? 167  ARG B CG  1 
ATOM   7884  C CD  . ARG D  2 167 ? 42.344  -89.997 37.243  1.00 106.66 ? 167  ARG B CD  1 
ATOM   7885  N NE  . ARG D  2 167 ? 41.886  -91.313 36.809  1.00 109.42 ? 167  ARG B NE  1 
ATOM   7886  C CZ  . ARG D  2 167 ? 40.611  -91.618 36.588  1.00 110.61 ? 167  ARG B CZ  1 
ATOM   7887  N NH1 . ARG D  2 167 ? 39.671  -90.693 36.746  1.00 111.40 ? 167  ARG B NH1 1 
ATOM   7888  N NH2 . ARG D  2 167 ? 40.273  -92.837 36.190  1.00 111.73 ? 167  ARG B NH2 1 
ATOM   7889  N N   . LEU D  2 168 ? 46.274  -91.120 34.224  1.00 98.57  ? 168  LEU B N   1 
ATOM   7890  C CA  . LEU D  2 168 ? 47.360  -92.086 34.416  1.00 96.62  ? 168  LEU B CA  1 
ATOM   7891  C C   . LEU D  2 168 ? 48.726  -91.468 34.095  1.00 96.79  ? 168  LEU B C   1 
ATOM   7892  O O   . LEU D  2 168 ? 49.674  -91.608 34.865  1.00 96.61  ? 168  LEU B O   1 
ATOM   7893  C CB  . LEU D  2 168 ? 47.131  -93.333 33.547  1.00 94.86  ? 168  LEU B CB  1 
ATOM   7894  C CG  . LEU D  2 168 ? 46.139  -94.376 34.080  1.00 94.93  ? 168  LEU B CG  1 
ATOM   7895  C CD1 . LEU D  2 168 ? 46.116  -95.649 33.240  1.00 83.78  ? 168  LEU B CD1 1 
ATOM   7896  C CD2 . LEU D  2 168 ? 46.441  -94.692 35.534  1.00 97.05  ? 168  LEU B CD2 1 
ATOM   7897  N N   . LYS D  2 169 ? 48.796  -90.780 32.955  1.00 95.27  ? 169  LYS B N   1 
ATOM   7898  C CA  . LYS D  2 169 ? 50.024  -90.196 32.407  1.00 91.85  ? 169  LYS B CA  1 
ATOM   7899  C C   . LYS D  2 169 ? 50.553  -89.084 33.322  1.00 92.86  ? 169  LYS B C   1 
ATOM   7900  O O   . LYS D  2 169 ? 51.766  -88.859 33.434  1.00 88.77  ? 169  LYS B O   1 
ATOM   7901  C CB  . LYS D  2 169 ? 49.746  -89.656 30.998  1.00 91.21  ? 169  LYS B CB  1 
ATOM   7902  C CG  . LYS D  2 169 ? 50.927  -89.041 30.248  1.00 86.24  ? 169  LYS B CG  1 
ATOM   7903  C CD  . LYS D  2 169 ? 52.003  -90.077 29.972  1.00 79.87  ? 169  LYS B CD  1 
ATOM   7904  C CE  . LYS D  2 169 ? 53.041  -89.570 28.993  1.00 72.29  ? 169  LYS B CE  1 
ATOM   7905  N NZ  . LYS D  2 169 ? 53.787  -88.402 29.514  1.00 82.31  ? 169  LYS B NZ  1 
ATOM   7906  N N   . ARG D  2 170 ? 49.613  -88.353 33.917  1.00 94.09  ? 170  ARG B N   1 
ATOM   7907  C CA  . ARG D  2 170 ? 49.908  -87.237 34.812  1.00 95.58  ? 170  ARG B CA  1 
ATOM   7908  C C   . ARG D  2 170 ? 50.374  -87.684 36.214  1.00 98.45  ? 170  ARG B C   1 
ATOM   7909  O O   . ARG D  2 170 ? 51.157  -86.989 36.868  1.00 97.45  ? 170  ARG B O   1 
ATOM   7910  C CB  . ARG D  2 170 ? 48.656  -86.351 34.921  1.00 91.51  ? 170  ARG B CB  1 
ATOM   7911  C CG  . ARG D  2 170 ? 48.840  -85.041 35.658  1.00 91.04  ? 170  ARG B CG  1 
ATOM   7912  C CD  . ARG D  2 170 ? 47.596  -84.161 35.547  1.00 86.80  ? 170  ARG B CD  1 
ATOM   7913  N NE  . ARG D  2 170 ? 46.483  -84.582 36.397  1.00 83.41  ? 170  ARG B NE  1 
ATOM   7914  C CZ  . ARG D  2 170 ? 45.356  -85.124 35.946  1.00 76.37  ? 170  ARG B CZ  1 
ATOM   7915  N NH1 . ARG D  2 170 ? 45.195  -85.326 34.650  1.00 83.96  ? 170  ARG B NH1 1 
ATOM   7916  N NH2 . ARG D  2 170 ? 44.392  -85.467 36.788  1.00 72.85  ? 170  ARG B NH2 1 
ATOM   7917  N N   . GLU D  2 171 ? 49.895  -88.845 36.664  1.00 100.23 ? 171  GLU B N   1 
ATOM   7918  C CA  . GLU D  2 171 ? 50.369  -89.467 37.906  1.00 99.37  ? 171  GLU B CA  1 
ATOM   7919  C C   . GLU D  2 171 ? 51.766  -90.060 37.707  1.00 101.07 ? 171  GLU B C   1 
ATOM   7920  O O   . GLU D  2 171 ? 52.564  -90.101 38.644  1.00 98.79  ? 171  GLU B O   1 
ATOM   7921  C CB  . GLU D  2 171 ? 49.386  -90.541 38.402  1.00 95.82  ? 171  GLU B CB  1 
ATOM   7922  C CG  . GLU D  2 171 ? 48.032  -89.992 38.858  1.00 96.09  ? 171  GLU B CG  1 
ATOM   7923  C CD  . GLU D  2 171 ? 47.031  -91.081 39.221  1.00 104.20 ? 171  GLU B CD  1 
ATOM   7924  O OE1 . GLU D  2 171 ? 47.302  -92.267 38.938  1.00 106.62 ? 171  GLU B OE1 1 
ATOM   7925  O OE2 . GLU D  2 171 ? 45.963  -90.752 39.784  1.00 105.84 ? 171  GLU B OE2 1 
ATOM   7926  N N   . GLU D  2 172 ? 52.040  -90.534 36.486  1.00 99.29  ? 172  GLU B N   1 
ATOM   7927  C CA  . GLU D  2 172 ? 53.361  -91.054 36.122  1.00 97.14  ? 172  GLU B CA  1 
ATOM   7928  C C   . GLU D  2 172 ? 54.398  -89.944 36.197  1.00 101.67 ? 172  GLU B C   1 
ATOM   7929  O O   . GLU D  2 172 ? 55.553  -90.168 36.580  1.00 101.21 ? 172  GLU B O   1 
ATOM   7930  C CB  . GLU D  2 172 ? 53.369  -91.646 34.701  1.00 91.84  ? 172  GLU B CB  1 
ATOM   7931  C CG  . GLU D  2 172 ? 52.403  -92.796 34.452  1.00 94.20  ? 172  GLU B CG  1 
ATOM   7932  C CD  . GLU D  2 172 ? 52.344  -93.237 32.983  1.00 94.21  ? 172  GLU B CD  1 
ATOM   7933  O OE1 . GLU D  2 172 ? 53.094  -92.669 32.143  1.00 90.25  ? 172  GLU B OE1 1 
ATOM   7934  O OE2 . GLU D  2 172 ? 51.537  -94.154 32.679  1.00 93.11  ? 172  GLU B OE2 1 
ATOM   7935  N N   . ILE D  2 173 ? 53.962  -88.740 35.843  1.00 102.92 ? 173  ILE B N   1 
ATOM   7936  C CA  . ILE D  2 173 ? 54.807  -87.556 35.916  1.00 107.51 ? 173  ILE B CA  1 
ATOM   7937  C C   . ILE D  2 173 ? 54.889  -87.079 37.376  1.00 110.11 ? 173  ILE B C   1 
ATOM   7938  O O   . ILE D  2 173 ? 55.917  -86.544 37.810  1.00 111.87 ? 173  ILE B O   1 
ATOM   7939  C CB  . ILE D  2 173 ? 54.288  -86.435 34.960  1.00 99.59  ? 173  ILE B CB  1 
ATOM   7940  C CG1 . ILE D  2 173 ? 54.506  -86.860 33.501  1.00 95.93  ? 173  ILE B CG1 1 
ATOM   7941  C CG2 . ILE D  2 173 ? 54.997  -85.115 35.219  1.00 93.70  ? 173  ILE B CG2 1 
ATOM   7942  C CD1 . ILE D  2 173 ? 53.843  -85.978 32.456  1.00 86.17  ? 173  ILE B CD1 1 
ATOM   7943  N N   . SER D  2 174 ? 53.823  -87.316 38.142  1.00 109.93 ? 174  SER B N   1 
ATOM   7944  C CA  . SER D  2 174 ? 53.775  -86.896 39.547  1.00 114.74 ? 174  SER B CA  1 
ATOM   7945  C C   . SER D  2 174 ? 54.331  -87.969 40.508  1.00 113.31 ? 174  SER B C   1 
ATOM   7946  O O   . SER D  2 174 ? 53.884  -88.087 41.653  1.00 112.44 ? 174  SER B O   1 
ATOM   7947  C CB  . SER D  2 174 ? 52.334  -86.529 39.934  1.00 110.08 ? 174  SER B CB  1 
ATOM   7948  O OG  . SER D  2 174 ? 52.283  -85.884 41.197  1.00 112.35 ? 174  SER B OG  1 
ATOM   7949  N N   . GLY D  2 175 ? 55.319  -88.730 40.041  1.00 110.97 ? 175  GLY B N   1 
ATOM   7950  C CA  . GLY D  2 175 ? 55.946  -89.762 40.849  1.00 110.45 ? 175  GLY B CA  1 
ATOM   7951  C C   . GLY D  2 175 ? 57.461  -89.697 40.804  1.00 109.08 ? 175  GLY B C   1 
ATOM   7952  O O   . GLY D  2 175 ? 58.044  -89.254 39.813  1.00 107.45 ? 175  GLY B O   1 
ATOM   7953  N N   . ASP E  1 2   ? 27.290  -90.481 40.415  1.00 118.44 ? 8    ASP E N   1 
ATOM   7954  C CA  . ASP E  1 2   ? 26.183  -89.718 39.847  1.00 119.32 ? 8    ASP E CA  1 
ATOM   7955  C C   . ASP E  1 2   ? 26.507  -88.223 39.803  1.00 120.85 ? 8    ASP E C   1 
ATOM   7956  O O   . ASP E  1 2   ? 27.470  -87.774 40.431  1.00 119.49 ? 8    ASP E O   1 
ATOM   7957  C CB  . ASP E  1 2   ? 24.888  -89.971 40.645  1.00 116.87 ? 8    ASP E CB  1 
ATOM   7958  C CG  . ASP E  1 2   ? 24.808  -89.160 41.944  1.00 111.53 ? 8    ASP E CG  1 
ATOM   7959  O OD1 . ASP E  1 2   ? 25.845  -88.952 42.613  1.00 109.77 ? 8    ASP E OD1 1 
ATOM   7960  O OD2 . ASP E  1 2   ? 23.686  -88.738 42.303  1.00 108.89 ? 8    ASP E OD2 1 
ATOM   7961  N N   . PRO E  1 3   ? 25.746  -87.457 39.001  1.00 123.59 ? 9    PRO E N   1 
ATOM   7962  C CA  . PRO E  1 3   ? 25.746  -86.001 39.175  1.00 121.39 ? 9    PRO E CA  1 
ATOM   7963  C C   . PRO E  1 3   ? 25.493  -85.609 40.644  1.00 116.50 ? 9    PRO E C   1 
ATOM   7964  O O   . PRO E  1 3   ? 24.544  -86.106 41.260  1.00 113.17 ? 9    PRO E O   1 
ATOM   7965  C CB  . PRO E  1 3   ? 24.593  -85.542 38.272  1.00 121.11 ? 9    PRO E CB  1 
ATOM   7966  C CG  . PRO E  1 3   ? 24.409  -86.652 37.249  1.00 116.43 ? 9    PRO E CG  1 
ATOM   7967  C CD  . PRO E  1 3   ? 25.210  -87.855 37.686  1.00 118.23 ? 9    PRO E CD  1 
ATOM   7968  N N   . GLY E  1 4   ? 26.331  -84.733 41.193  1.00 112.06 ? 10   GLY E N   1 
ATOM   7969  C CA  . GLY E  1 4   ? 26.147  -84.248 42.551  1.00 108.39 ? 10   GLY E CA  1 
ATOM   7970  C C   . GLY E  1 4   ? 25.357  -82.953 42.615  1.00 105.21 ? 10   GLY E C   1 
ATOM   7971  O O   . GLY E  1 4   ? 24.434  -82.738 41.825  1.00 104.64 ? 10   GLY E O   1 
ATOM   7972  N N   . ASP E  1 5   ? 25.703  -82.086 43.562  1.00 105.43 ? 11   ASP E N   1 
ATOM   7973  C CA  . ASP E  1 5   ? 25.005  -80.810 43.674  1.00 102.35 ? 11   ASP E CA  1 
ATOM   7974  C C   . ASP E  1 5   ? 25.645  -79.779 42.755  1.00 92.72  ? 11   ASP E C   1 
ATOM   7975  O O   . ASP E  1 5   ? 26.861  -79.766 42.548  1.00 89.31  ? 11   ASP E O   1 
ATOM   7976  C CB  . ASP E  1 5   ? 25.012  -80.305 45.123  1.00 103.54 ? 11   ASP E CB  1 
ATOM   7977  C CG  . ASP E  1 5   ? 24.342  -81.269 46.087  1.00 100.46 ? 11   ASP E CG  1 
ATOM   7978  O OD1 . ASP E  1 5   ? 23.664  -82.211 45.619  1.00 97.46  ? 11   ASP E OD1 1 
ATOM   7979  O OD2 . ASP E  1 5   ? 24.513  -81.086 47.312  1.00 96.28  ? 11   ASP E OD2 1 
ATOM   7980  N N   . GLN E  1 6   ? 24.806  -78.911 42.209  1.00 94.66  ? 12   GLN E N   1 
ATOM   7981  C CA  . GLN E  1 6   ? 25.260  -77.881 41.291  1.00 93.90  ? 12   GLN E CA  1 
ATOM   7982  C C   . GLN E  1 6   ? 24.789  -76.482 41.665  1.00 88.29  ? 12   GLN E C   1 
ATOM   7983  O O   . GLN E  1 6   ? 23.879  -76.299 42.476  1.00 87.70  ? 12   GLN E O   1 
ATOM   7984  C CB  . GLN E  1 6   ? 24.794  -78.204 39.869  1.00 89.93  ? 12   GLN E CB  1 
ATOM   7985  C CG  . GLN E  1 6   ? 25.521  -79.362 39.224  1.00 90.00  ? 12   GLN E CG  1 
ATOM   7986  C CD  . GLN E  1 6   ? 25.405  -79.333 37.717  1.00 87.67  ? 12   GLN E CD  1 
ATOM   7987  O OE1 . GLN E  1 6   ? 24.605  -78.575 37.162  1.00 79.33  ? 12   GLN E OE1 1 
ATOM   7988  N NE2 . GLN E  1 6   ? 26.213  -80.145 37.043  1.00 84.56  ? 12   GLN E NE2 1 
ATOM   7989  N N   . ILE E  1 7   ? 25.405  -75.501 41.023  1.00 85.31  ? 13   ILE E N   1 
ATOM   7990  C CA  . ILE E  1 7   ? 24.925  -74.129 41.044  1.00 84.48  ? 13   ILE E CA  1 
ATOM   7991  C C   . ILE E  1 7   ? 25.391  -73.530 39.722  1.00 80.37  ? 13   ILE E C   1 
ATOM   7992  O O   . ILE E  1 7   ? 26.533  -73.747 39.297  1.00 76.43  ? 13   ILE E O   1 
ATOM   7993  C CB  . ILE E  1 7   ? 25.435  -73.328 42.284  1.00 80.66  ? 13   ILE E CB  1 
ATOM   7994  C CG1 . ILE E  1 7   ? 24.606  -72.055 42.480  1.00 75.75  ? 13   ILE E CG1 1 
ATOM   7995  C CG2 . ILE E  1 7   ? 26.938  -73.030 42.203  1.00 75.27  ? 13   ILE E CG2 1 
ATOM   7996  C CD1 . ILE E  1 7   ? 24.910  -71.316 43.773  1.00 70.67  ? 13   ILE E CD1 1 
ATOM   7997  N N   . CYS E  1 8   ? 24.484  -72.823 39.049  1.00 85.41  ? 14   CYS E N   1 
ATOM   7998  C CA  . CYS E  1 8   ? 24.768  -72.286 37.716  1.00 80.63  ? 14   CYS E CA  1 
ATOM   7999  C C   . CYS E  1 8   ? 24.445  -70.799 37.588  1.00 78.96  ? 14   CYS E C   1 
ATOM   8000  O O   . CYS E  1 8   ? 23.532  -70.292 38.241  1.00 80.22  ? 14   CYS E O   1 
ATOM   8001  C CB  . CYS E  1 8   ? 23.989  -73.079 36.665  1.00 74.36  ? 14   CYS E CB  1 
ATOM   8002  S SG  . CYS E  1 8   ? 24.476  -74.830 36.579  1.00 74.36  ? 14   CYS E SG  1 
ATOM   8003  N N   . ILE E  1 9   ? 25.192  -70.118 36.721  1.00 81.73  ? 15   ILE E N   1 
ATOM   8004  C CA  . ILE E  1 9   ? 25.005  -68.688 36.465  1.00 78.44  ? 15   ILE E CA  1 
ATOM   8005  C C   . ILE E  1 9   ? 24.388  -68.456 35.089  1.00 75.14  ? 15   ILE E C   1 
ATOM   8006  O O   . ILE E  1 9   ? 24.847  -69.025 34.105  1.00 77.75  ? 15   ILE E O   1 
ATOM   8007  C CB  . ILE E  1 9   ? 26.343  -67.929 36.563  1.00 77.87  ? 15   ILE E CB  1 
ATOM   8008  C CG1 . ILE E  1 9   ? 26.924  -68.076 37.971  1.00 76.74  ? 15   ILE E CG1 1 
ATOM   8009  C CG2 . ILE E  1 9   ? 26.160  -66.463 36.221  1.00 72.23  ? 15   ILE E CG2 1 
ATOM   8010  C CD1 . ILE E  1 9   ? 28.250  -68.801 37.999  1.00 76.50  ? 15   ILE E CD1 1 
ATOM   8011  N N   . GLY E  1 10  ? 23.368  -67.602 35.022  1.00 78.61  ? 16   GLY E N   1 
ATOM   8012  C CA  . GLY E  1 10  ? 22.682  -67.320 33.772  1.00 75.09  ? 16   GLY E CA  1 
ATOM   8013  C C   . GLY E  1 10  ? 21.915  -66.014 33.813  1.00 73.75  ? 16   GLY E C   1 
ATOM   8014  O O   . GLY E  1 10  ? 21.918  -65.328 34.837  1.00 73.14  ? 16   GLY E O   1 
ATOM   8015  N N   . TYR E  1 11  ? 21.227  -65.696 32.716  1.00 71.62  ? 17   TYR E N   1 
ATOM   8016  C CA  . TYR E  1 11  ? 20.573  -64.400 32.550  1.00 72.20  ? 17   TYR E CA  1 
ATOM   8017  C C   . TYR E  1 11  ? 19.116  -64.479 32.119  1.00 73.58  ? 17   TYR E C   1 
ATOM   8018  O O   . TYR E  1 11  ? 18.621  -65.547 31.791  1.00 77.71  ? 17   TYR E O   1 
ATOM   8019  C CB  . TYR E  1 11  ? 21.343  -63.548 31.543  1.00 68.80  ? 17   TYR E CB  1 
ATOM   8020  C CG  . TYR E  1 11  ? 21.739  -64.245 30.264  1.00 67.47  ? 17   TYR E CG  1 
ATOM   8021  C CD1 . TYR E  1 11  ? 22.928  -64.975 30.193  1.00 68.26  ? 17   TYR E CD1 1 
ATOM   8022  C CD2 . TYR E  1 11  ? 20.960  -64.141 29.113  1.00 70.17  ? 17   TYR E CD2 1 
ATOM   8023  C CE1 . TYR E  1 11  ? 23.325  -65.599 29.021  1.00 67.99  ? 17   TYR E CE1 1 
ATOM   8024  C CE2 . TYR E  1 11  ? 21.348  -64.763 27.922  1.00 67.63  ? 17   TYR E CE2 1 
ATOM   8025  C CZ  . TYR E  1 11  ? 22.535  -65.492 27.888  1.00 70.26  ? 17   TYR E CZ  1 
ATOM   8026  O OH  . TYR E  1 11  ? 22.947  -66.120 26.729  1.00 73.57  ? 17   TYR E OH  1 
ATOM   8027  N N   . HIS E  1 12  ? 18.445  -63.328 32.124  1.00 73.00  ? 18   HIS E N   1 
ATOM   8028  C CA  . HIS E  1 12  ? 17.011  -63.223 31.837  1.00 73.89  ? 18   HIS E CA  1 
ATOM   8029  C C   . HIS E  1 12  ? 16.606  -63.455 30.374  1.00 77.78  ? 18   HIS E C   1 
ATOM   8030  O O   . HIS E  1 12  ? 17.346  -63.104 29.450  1.00 77.69  ? 18   HIS E O   1 
ATOM   8031  C CB  . HIS E  1 12  ? 16.504  -61.847 32.258  1.00 73.88  ? 18   HIS E CB  1 
ATOM   8032  C CG  . HIS E  1 12  ? 15.022  -61.691 32.132  1.00 74.97  ? 18   HIS E CG  1 
ATOM   8033  N ND1 . HIS E  1 12  ? 14.132  -62.565 32.716  1.00 77.33  ? 18   HIS E ND1 1 
ATOM   8034  C CD2 . HIS E  1 12  ? 14.274  -60.790 31.452  1.00 77.45  ? 18   HIS E CD2 1 
ATOM   8035  C CE1 . HIS E  1 12  ? 12.897  -62.191 32.430  1.00 79.63  ? 18   HIS E CE1 1 
ATOM   8036  N NE2 . HIS E  1 12  ? 12.955  -61.121 31.658  1.00 79.49  ? 18   HIS E NE2 1 
ATOM   8037  N N   . ALA E  1 13  ? 15.436  -64.064 30.176  1.00 75.87  ? 19   ALA E N   1 
ATOM   8038  C CA  . ALA E  1 13  ? 14.816  -64.152 28.851  1.00 76.80  ? 19   ALA E CA  1 
ATOM   8039  C C   . ALA E  1 13  ? 13.296  -63.977 28.953  1.00 77.99  ? 19   ALA E C   1 
ATOM   8040  O O   . ALA E  1 13  ? 12.720  -64.091 30.038  1.00 75.47  ? 19   ALA E O   1 
ATOM   8041  C CB  . ALA E  1 13  ? 15.164  -65.478 28.169  1.00 75.50  ? 19   ALA E CB  1 
ATOM   8042  N N   . ASN E  1 14  ? 12.669  -63.645 27.824  1.00 76.80  ? 20   ASN E N   1 
ATOM   8043  C CA  . ASN E  1 14  ? 11.216  -63.459 27.738  1.00 75.27  ? 20   ASN E CA  1 
ATOM   8044  C C   . ASN E  1 14  ? 10.724  -63.733 26.323  1.00 78.90  ? 20   ASN E C   1 
ATOM   8045  O O   . ASN E  1 14  ? 11.439  -64.331 25.504  1.00 81.35  ? 20   ASN E O   1 
ATOM   8046  C CB  . ASN E  1 14  ? 10.788  -62.047 28.178  1.00 80.98  ? 20   ASN E CB  1 
ATOM   8047  C CG  . ASN E  1 14  ? 11.498  -60.932 27.401  1.00 81.26  ? 20   ASN E CG  1 
ATOM   8048  O OD1 . ASN E  1 14  ? 11.736  -61.040 26.198  1.00 84.57  ? 20   ASN E OD1 1 
ATOM   8049  N ND2 . ASN E  1 14  ? 11.820  -59.845 28.096  1.00 73.47  ? 20   ASN E ND2 1 
ATOM   8050  N N   . ASN E  1 15  ? 9.497   -63.298 26.046  1.00 81.72  ? 21   ASN E N   1 
ATOM   8051  C CA  . ASN E  1 15  ? 8.893   -63.463 24.724  1.00 84.66  ? 21   ASN E CA  1 
ATOM   8052  C C   . ASN E  1 15  ? 8.800   -62.158 23.940  1.00 85.48  ? 21   ASN E C   1 
ATOM   8053  O O   . ASN E  1 15  ? 7.936   -62.007 23.071  1.00 85.69  ? 21   ASN E O   1 
ATOM   8054  C CB  . ASN E  1 15  ? 7.501   -64.083 24.851  1.00 86.78  ? 21   ASN E CB  1 
ATOM   8055  C CG  . ASN E  1 15  ? 7.555   -65.591 25.079  1.00 91.60  ? 21   ASN E CG  1 
ATOM   8056  O OD1 . ASN E  1 15  ? 7.819   -66.363 24.150  1.00 93.97  ? 21   ASN E OD1 1 
ATOM   8057  N ND2 . ASN E  1 15  ? 7.280   -66.019 26.314  1.00 92.99  ? 21   ASN E ND2 1 
ATOM   8058  N N   . SER E  1 16  ? 9.699   -61.225 24.241  1.00 84.21  ? 22   SER E N   1 
ATOM   8059  C CA  . SER E  1 16  ? 9.681   -59.903 23.627  1.00 82.37  ? 22   SER E CA  1 
ATOM   8060  C C   . SER E  1 16  ? 10.097  -59.950 22.159  1.00 81.73  ? 22   SER E C   1 
ATOM   8061  O O   . SER E  1 16  ? 10.794  -60.869 21.716  1.00 83.94  ? 22   SER E O   1 
ATOM   8062  C CB  . SER E  1 16  ? 10.583  -58.946 24.413  1.00 81.73  ? 22   SER E CB  1 
ATOM   8063  O OG  . SER E  1 16  ? 10.450  -57.607 23.972  1.00 83.71  ? 22   SER E OG  1 
ATOM   8064  N N   . THR E  1 17  ? 9.702   -58.919 21.424  1.00 79.60  ? 23   THR E N   1 
ATOM   8065  C CA  . THR E  1 17  ? 9.981   -58.847 19.999  1.00 86.24  ? 23   THR E CA  1 
ATOM   8066  C C   . THR E  1 17  ? 10.648  -57.517 19.631  1.00 84.29  ? 23   THR E C   1 
ATOM   8067  O O   . THR E  1 17  ? 10.856  -57.223 18.451  1.00 86.07  ? 23   THR E O   1 
ATOM   8068  C CB  . THR E  1 17  ? 8.675   -59.025 19.163  1.00 85.95  ? 23   THR E CB  1 
ATOM   8069  O OG1 . THR E  1 17  ? 7.580   -58.367 19.818  1.00 83.46  ? 23   THR E OG1 1 
ATOM   8070  C CG2 . THR E  1 17  ? 8.342   -60.501 18.989  1.00 79.81  ? 23   THR E CG2 1 
ATOM   8071  N N   . GLU E  1 18  ? 11.007  -56.731 20.643  1.00 76.54  ? 24   GLU E N   1 
ATOM   8072  C CA  . GLU E  1 18  ? 11.652  -55.446 20.417  1.00 71.83  ? 24   GLU E CA  1 
ATOM   8073  C C   . GLU E  1 18  ? 13.025  -55.618 19.768  1.00 73.95  ? 24   GLU E C   1 
ATOM   8074  O O   . GLU E  1 18  ? 13.755  -56.565 20.074  1.00 73.24  ? 24   GLU E O   1 
ATOM   8075  C CB  . GLU E  1 18  ? 11.804  -54.683 21.731  1.00 71.23  ? 24   GLU E CB  1 
ATOM   8076  C CG  . GLU E  1 18  ? 10.494  -54.281 22.383  1.00 81.73  ? 24   GLU E CG  1 
ATOM   8077  C CD  . GLU E  1 18  ? 9.495   -53.716 21.400  1.00 94.03  ? 24   GLU E CD  1 
ATOM   8078  O OE1 . GLU E  1 18  ? 9.819   -52.717 20.716  1.00 99.10  ? 24   GLU E OE1 1 
ATOM   8079  O OE2 . GLU E  1 18  ? 8.382   -54.277 21.308  1.00 101.72 ? 24   GLU E OE2 1 
ATOM   8080  N N   . GLN E  1 19  ? 13.359  -54.708 18.853  1.00 72.69  ? 25   GLN E N   1 
ATOM   8081  C CA  . GLN E  1 19  ? 14.632  -54.757 18.139  1.00 68.11  ? 25   GLN E CA  1 
ATOM   8082  C C   . GLN E  1 19  ? 15.379  -53.437 18.292  1.00 62.43  ? 25   GLN E C   1 
ATOM   8083  O O   . GLN E  1 19  ? 14.787  -52.362 18.350  1.00 66.18  ? 25   GLN E O   1 
ATOM   8084  C CB  . GLN E  1 19  ? 14.437  -55.093 16.662  1.00 70.15  ? 25   GLN E CB  1 
ATOM   8085  C CG  . GLN E  1 19  ? 13.711  -56.399 16.410  1.00 74.27  ? 25   GLN E CG  1 
ATOM   8086  C CD  . GLN E  1 19  ? 13.420  -56.623 14.938  1.00 80.24  ? 25   GLN E CD  1 
ATOM   8087  O OE1 . GLN E  1 19  ? 13.478  -55.694 14.127  1.00 85.87  ? 25   GLN E OE1 1 
ATOM   8088  N NE2 . GLN E  1 19  ? 13.098  -57.859 14.586  1.00 77.87  ? 25   GLN E NE2 1 
ATOM   8089  N N   . VAL E  1 20  ? 16.693  -53.542 18.368  1.00 60.30  ? 26   VAL E N   1 
ATOM   8090  C CA  . VAL E  1 20  ? 17.553  -52.399 18.524  1.00 51.05  ? 26   VAL E CA  1 
ATOM   8091  C C   . VAL E  1 20  ? 18.646  -52.451 17.450  1.00 56.56  ? 26   VAL E C   1 
ATOM   8092  O O   . VAL E  1 20  ? 18.938  -53.528 16.934  1.00 59.47  ? 26   VAL E O   1 
ATOM   8093  C CB  . VAL E  1 20  ? 18.124  -52.421 19.962  1.00 53.75  ? 26   VAL E CB  1 
ATOM   8094  C CG1 . VAL E  1 20  ? 19.644  -52.417 19.986  1.00 50.65  ? 26   VAL E CG1 1 
ATOM   8095  C CG2 . VAL E  1 20  ? 17.513  -51.314 20.816  1.00 52.63  ? 26   VAL E CG2 1 
ATOM   8096  N N   . ASP E  1 21  ? 19.267  -51.317 17.118  1.00 54.15  ? 27   ASP E N   1 
ATOM   8097  C CA  . ASP E  1 21  ? 20.357  -51.319 16.138  1.00 54.37  ? 27   ASP E CA  1 
ATOM   8098  C C   . ASP E  1 21  ? 21.680  -50.960 16.799  1.00 51.69  ? 27   ASP E C   1 
ATOM   8099  O O   . ASP E  1 21  ? 21.699  -50.238 17.791  1.00 53.02  ? 27   ASP E O   1 
ATOM   8100  C CB  . ASP E  1 21  ? 20.043  -50.359 14.991  1.00 55.37  ? 27   ASP E CB  1 
ATOM   8101  C CG  . ASP E  1 21  ? 19.038  -50.934 13.998  1.00 61.37  ? 27   ASP E CG  1 
ATOM   8102  O OD1 . ASP E  1 21  ? 18.396  -51.966 14.283  1.00 62.62  ? 27   ASP E OD1 1 
ATOM   8103  O OD2 . ASP E  1 21  ? 18.825  -50.299 12.950  1.00 71.89  ? 27   ASP E OD2 1 
ATOM   8104  N N   . THR E  1 22  ? 22.779  -51.416 16.204  1.00 51.19  ? 28   THR E N   1 
ATOM   8105  C CA  . THR E  1 22  ? 24.132  -51.174 16.710  1.00 52.37  ? 28   THR E CA  1 
ATOM   8106  C C   . THR E  1 22  ? 24.972  -50.752 15.511  1.00 58.44  ? 28   THR E C   1 
ATOM   8107  O O   . THR E  1 22  ? 24.475  -50.756 14.388  1.00 60.33  ? 28   THR E O   1 
ATOM   8108  C CB  . THR E  1 22  ? 24.702  -52.475 17.433  1.00 57.55  ? 28   THR E CB  1 
ATOM   8109  O OG1 . THR E  1 22  ? 24.337  -52.462 18.825  1.00 59.38  ? 28   THR E OG1 1 
ATOM   8110  C CG2 . THR E  1 22  ? 26.220  -52.646 17.344  1.00 53.87  ? 28   THR E CG2 1 
ATOM   8111  N N   . ILE E  1 23  ? 26.212  -50.332 15.734  1.00 58.12  ? 29   ILE E N   1 
ATOM   8112  C CA  . ILE E  1 23  ? 27.078  -49.914 14.642  1.00 61.29  ? 29   ILE E CA  1 
ATOM   8113  C C   . ILE E  1 23  ? 27.655  -51.127 13.875  1.00 66.90  ? 29   ILE E C   1 
ATOM   8114  O O   . ILE E  1 23  ? 28.028  -51.016 12.707  1.00 67.68  ? 29   ILE E O   1 
ATOM   8115  C CB  . ILE E  1 23  ? 28.219  -49.027 15.192  1.00 64.69  ? 29   ILE E CB  1 
ATOM   8116  C CG1 . ILE E  1 23  ? 29.591  -49.679 14.993  1.00 65.88  ? 29   ILE E CG1 1 
ATOM   8117  C CG2 . ILE E  1 23  ? 27.975  -48.723 16.676  1.00 63.45  ? 29   ILE E CG2 1 
ATOM   8118  C CD1 . ILE E  1 23  ? 30.680  -48.700 14.657  1.00 65.35  ? 29   ILE E CD1 1 
ATOM   8119  N N   . MET E  1 24  ? 27.691  -52.288 14.534  1.00 70.90  ? 30   MET E N   1 
ATOM   8120  C CA  . MET E  1 24  ? 28.233  -53.523 13.958  1.00 66.23  ? 30   MET E CA  1 
ATOM   8121  C C   . MET E  1 24  ? 27.131  -54.492 13.536  1.00 64.75  ? 30   MET E C   1 
ATOM   8122  O O   . MET E  1 24  ? 27.392  -55.470 12.840  1.00 69.44  ? 30   MET E O   1 
ATOM   8123  C CB  . MET E  1 24  ? 29.157  -54.225 14.966  1.00 70.01  ? 30   MET E CB  1 
ATOM   8124  C CG  . MET E  1 24  ? 30.665  -54.037 14.748  1.00 69.43  ? 30   MET E CG  1 
ATOM   8125  S SD  . MET E  1 24  ? 31.697  -55.185 15.709  1.00 72.96  ? 30   MET E SD  1 
ATOM   8126  C CE  . MET E  1 24  ? 33.026  -54.096 16.229  1.00 67.49  ? 30   MET E CE  1 
ATOM   8127  N N   . GLU E  1 25  ? 25.910  -54.240 13.996  1.00 62.09  ? 31   GLU E N   1 
ATOM   8128  C CA  . GLU E  1 25  ? 24.831  -55.206 13.846  1.00 63.19  ? 31   GLU E CA  1 
ATOM   8129  C C   . GLU E  1 25  ? 23.427  -54.595 13.950  1.00 66.10  ? 31   GLU E C   1 
ATOM   8130  O O   . GLU E  1 25  ? 23.150  -53.818 14.872  1.00 65.79  ? 31   GLU E O   1 
ATOM   8131  C CB  . GLU E  1 25  ? 25.027  -56.277 14.915  1.00 69.39  ? 31   GLU E CB  1 
ATOM   8132  C CG  . GLU E  1 25  ? 24.122  -57.479 14.890  1.00 67.26  ? 31   GLU E CG  1 
ATOM   8133  C CD  . GLU E  1 25  ? 24.437  -58.404 16.068  1.00 76.17  ? 31   GLU E CD  1 
ATOM   8134  O OE1 . GLU E  1 25  ? 25.416  -58.113 16.806  1.00 72.44  ? 31   GLU E OE1 1 
ATOM   8135  O OE2 . GLU E  1 25  ? 23.713  -59.409 16.261  1.00 73.75  ? 31   GLU E OE2 1 
ATOM   8136  N N   . LYS E  1 26  ? 22.545  -54.968 13.026  1.00 62.19  ? 32   LYS E N   1 
ATOM   8137  C CA  . LYS E  1 26  ? 21.180  -54.435 12.969  1.00 64.81  ? 32   LYS E CA  1 
ATOM   8138  C C   . LYS E  1 26  ? 20.130  -55.428 13.475  1.00 70.04  ? 32   LYS E C   1 
ATOM   8139  O O   . LYS E  1 26  ? 20.380  -56.637 13.541  1.00 71.47  ? 32   LYS E O   1 
ATOM   8140  C CB  . LYS E  1 26  ? 20.803  -53.993 11.540  1.00 68.11  ? 32   LYS E CB  1 
ATOM   8141  C CG  . LYS E  1 26  ? 21.471  -52.721 11.006  1.00 71.10  ? 32   LYS E CG  1 
ATOM   8142  C CD  . LYS E  1 26  ? 22.988  -52.758 10.966  1.00 69.94  ? 32   LYS E CD  1 
ATOM   8143  C CE  . LYS E  1 26  ? 23.543  -51.336 11.048  1.00 73.75  ? 32   LYS E CE  1 
ATOM   8144  N NZ  . LYS E  1 26  ? 25.010  -51.310 11.360  1.00 77.40  ? 32   LYS E NZ  1 
ATOM   8145  N N   . ASN E  1 27  ? 18.968  -54.891 13.855  1.00 68.64  ? 33   ASN E N   1 
ATOM   8146  C CA  . ASN E  1 27  ? 17.816  -55.679 14.289  1.00 69.77  ? 33   ASN E CA  1 
ATOM   8147  C C   . ASN E  1 27  ? 18.159  -56.719 15.357  1.00 71.64  ? 33   ASN E C   1 
ATOM   8148  O O   . ASN E  1 27  ? 17.916  -57.913 15.183  1.00 68.66  ? 33   ASN E O   1 
ATOM   8149  C CB  . ASN E  1 27  ? 17.169  -56.366 13.084  1.00 79.93  ? 33   ASN E CB  1 
ATOM   8150  C CG  . ASN E  1 27  ? 16.400  -55.401 12.201  1.00 83.59  ? 33   ASN E CG  1 
ATOM   8151  O OD1 . ASN E  1 27  ? 16.051  -54.298 12.629  1.00 79.84  ? 33   ASN E OD1 1 
ATOM   8152  N ND2 . ASN E  1 27  ? 16.148  -55.813 10.948  1.00 92.71  ? 33   ASN E ND2 1 
ATOM   8153  N N   . VAL E  1 28  ? 18.724  -56.257 16.463  1.00 70.47  ? 34   VAL E N   1 
ATOM   8154  C CA  . VAL E  1 28  ? 19.063  -57.141 17.564  1.00 65.33  ? 34   VAL E CA  1 
ATOM   8155  C C   . VAL E  1 28  ? 17.892  -57.242 18.526  1.00 68.91  ? 34   VAL E C   1 
ATOM   8156  O O   . VAL E  1 28  ? 17.462  -56.242 19.110  1.00 66.30  ? 34   VAL E O   1 
ATOM   8157  C CB  . VAL E  1 28  ? 20.305  -56.646 18.306  1.00 64.01  ? 34   VAL E CB  1 
ATOM   8158  C CG1 . VAL E  1 28  ? 20.419  -57.314 19.675  1.00 60.74  ? 34   VAL E CG1 1 
ATOM   8159  C CG2 . VAL E  1 28  ? 21.546  -56.884 17.456  1.00 64.48  ? 34   VAL E CG2 1 
ATOM   8160  N N   . THR E  1 29  ? 17.385  -58.454 18.710  1.00 69.75  ? 35   THR E N   1 
ATOM   8161  C CA  . THR E  1 29  ? 16.223  -58.621 19.556  1.00 67.48  ? 35   THR E CA  1 
ATOM   8162  C C   . THR E  1 29  ? 16.639  -58.544 21.008  1.00 66.30  ? 35   THR E C   1 
ATOM   8163  O O   . THR E  1 29  ? 17.672  -59.079 21.391  1.00 64.60  ? 35   THR E O   1 
ATOM   8164  C CB  . THR E  1 29  ? 15.517  -59.943 19.289  1.00 69.79  ? 35   THR E CB  1 
ATOM   8165  O OG1 . THR E  1 29  ? 15.408  -60.141 17.872  1.00 73.33  ? 35   THR E OG1 1 
ATOM   8166  C CG2 . THR E  1 29  ? 14.123  -59.930 19.926  1.00 69.02  ? 35   THR E CG2 1 
ATOM   8167  N N   . VAL E  1 30  ? 15.843  -57.847 21.807  1.00 67.94  ? 36   VAL E N   1 
ATOM   8168  C CA  . VAL E  1 30  ? 16.228  -57.537 23.175  1.00 70.25  ? 36   VAL E CA  1 
ATOM   8169  C C   . VAL E  1 30  ? 15.049  -57.754 24.120  1.00 72.04  ? 36   VAL E C   1 
ATOM   8170  O O   . VAL E  1 30  ? 13.893  -57.763 23.697  1.00 70.69  ? 36   VAL E O   1 
ATOM   8171  C CB  . VAL E  1 30  ? 16.761  -56.088 23.317  1.00 67.82  ? 36   VAL E CB  1 
ATOM   8172  C CG1 . VAL E  1 30  ? 18.130  -55.948 22.646  1.00 59.98  ? 36   VAL E CG1 1 
ATOM   8173  C CG2 . VAL E  1 30  ? 15.759  -55.084 22.764  1.00 68.10  ? 36   VAL E CG2 1 
ATOM   8174  N N   . THR E  1 31  ? 15.361  -57.944 25.399  1.00 68.11  ? 37   THR E N   1 
ATOM   8175  C CA  . THR E  1 31  ? 14.355  -58.221 26.413  1.00 71.42  ? 37   THR E CA  1 
ATOM   8176  C C   . THR E  1 31  ? 13.565  -56.950 26.737  1.00 76.32  ? 37   THR E C   1 
ATOM   8177  O O   . THR E  1 31  ? 12.348  -56.994 26.938  1.00 75.17  ? 37   THR E O   1 
ATOM   8178  C CB  . THR E  1 31  ? 15.005  -58.809 27.715  1.00 77.53  ? 37   THR E CB  1 
ATOM   8179  O OG1 . THR E  1 31  ? 15.687  -57.781 28.448  1.00 74.69  ? 37   THR E OG1 1 
ATOM   8180  C CG2 . THR E  1 31  ? 16.007  -59.920 27.380  1.00 73.00  ? 37   THR E CG2 1 
ATOM   8181  N N   . HIS E  1 32  ? 14.273  -55.822 26.798  1.00 78.23  ? 38   HIS E N   1 
ATOM   8182  C CA  . HIS E  1 32  ? 13.666  -54.518 27.093  1.00 78.40  ? 38   HIS E CA  1 
ATOM   8183  C C   . HIS E  1 32  ? 14.270  -53.396 26.232  1.00 70.99  ? 38   HIS E C   1 
ATOM   8184  O O   . HIS E  1 32  ? 15.487  -53.324 26.038  1.00 66.60  ? 38   HIS E O   1 
ATOM   8185  C CB  . HIS E  1 32  ? 13.810  -54.182 28.589  1.00 78.30  ? 38   HIS E CB  1 
ATOM   8186  C CG  . HIS E  1 32  ? 13.203  -55.209 29.499  1.00 79.10  ? 38   HIS E CG  1 
ATOM   8187  N ND1 . HIS E  1 32  ? 13.819  -56.409 29.784  1.00 75.50  ? 38   HIS E ND1 1 
ATOM   8188  C CD2 . HIS E  1 32  ? 12.025  -55.223 30.167  1.00 81.32  ? 38   HIS E CD2 1 
ATOM   8189  C CE1 . HIS E  1 32  ? 13.053  -57.113 30.597  1.00 76.40  ? 38   HIS E CE1 1 
ATOM   8190  N NE2 . HIS E  1 32  ? 11.958  -56.416 30.844  1.00 77.33  ? 38   HIS E NE2 1 
ATOM   8191  N N   . ALA E  1 33  ? 13.407  -52.533 25.706  1.00 73.65  ? 39   ALA E N   1 
ATOM   8192  C CA  . ALA E  1 33  ? 13.846  -51.379 24.920  1.00 69.93  ? 39   ALA E CA  1 
ATOM   8193  C C   . ALA E  1 33  ? 12.968  -50.167 25.247  1.00 65.60  ? 39   ALA E C   1 
ATOM   8194  O O   . ALA E  1 33  ? 11.875  -50.318 25.792  1.00 66.02  ? 39   ALA E O   1 
ATOM   8195  C CB  . ALA E  1 33  ? 13.810  -51.700 23.426  1.00 63.72  ? 39   ALA E CB  1 
ATOM   8196  N N   . GLN E  1 34  ? 13.448  -48.967 24.932  1.00 64.37  ? 40   GLN E N   1 
ATOM   8197  C CA  . GLN E  1 34  ? 12.678  -47.748 25.183  1.00 60.59  ? 40   GLN E CA  1 
ATOM   8198  C C   . GLN E  1 34  ? 12.604  -46.851 23.944  1.00 62.13  ? 40   GLN E C   1 
ATOM   8199  O O   . GLN E  1 34  ? 13.634  -46.441 23.398  1.00 61.93  ? 40   GLN E O   1 
ATOM   8200  C CB  . GLN E  1 34  ? 13.276  -46.971 26.361  1.00 58.77  ? 40   GLN E CB  1 
ATOM   8201  C CG  . GLN E  1 34  ? 12.566  -45.659 26.650  1.00 62.34  ? 40   GLN E CG  1 
ATOM   8202  C CD  . GLN E  1 34  ? 13.123  -44.923 27.862  1.00 64.07  ? 40   GLN E CD  1 
ATOM   8203  O OE1 . GLN E  1 34  ? 13.855  -45.491 28.676  1.00 65.03  ? 40   GLN E OE1 1 
ATOM   8204  N NE2 . GLN E  1 34  ? 12.791  -43.641 27.972  1.00 58.85  ? 40   GLN E NE2 1 
ATOM   8205  N N   . ASP E  1 35  ? 11.381  -46.583 23.485  1.00 68.11  ? 41   ASP E N   1 
ATOM   8206  C CA  . ASP E  1 35  ? 11.126  -45.646 22.384  1.00 65.33  ? 41   ASP E CA  1 
ATOM   8207  C C   . ASP E  1 35  ? 11.314  -44.197 22.861  1.00 63.24  ? 41   ASP E C   1 
ATOM   8208  O O   . ASP E  1 35  ? 10.830  -43.826 23.923  1.00 61.29  ? 41   ASP E O   1 
ATOM   8209  C CB  . ASP E  1 35  ? 9.700   -45.824 21.855  1.00 60.07  ? 41   ASP E CB  1 
ATOM   8210  C CG  . ASP E  1 35  ? 9.470   -45.125 20.532  1.00 67.09  ? 41   ASP E CG  1 
ATOM   8211  O OD1 . ASP E  1 35  ? 10.383  -44.431 20.042  1.00 68.63  ? 41   ASP E OD1 1 
ATOM   8212  O OD2 . ASP E  1 35  ? 8.347   -45.230 20.002  1.00 69.80  ? 41   ASP E OD2 1 
ATOM   8213  N N   . ILE E  1 36  ? 11.975  -43.365 22.063  1.00 65.50  ? 42   ILE E N   1 
ATOM   8214  C CA  . ILE E  1 36  ? 12.173  -41.965 22.444  1.00 64.61  ? 42   ILE E CA  1 
ATOM   8215  C C   . ILE E  1 36  ? 11.759  -40.975 21.347  1.00 63.23  ? 42   ILE E C   1 
ATOM   8216  O O   . ILE E  1 36  ? 12.110  -39.803 21.413  1.00 62.50  ? 42   ILE E O   1 
ATOM   8217  C CB  . ILE E  1 36  ? 13.637  -41.700 22.825  1.00 59.92  ? 42   ILE E CB  1 
ATOM   8218  C CG1 . ILE E  1 36  ? 14.542  -42.102 21.667  1.00 60.34  ? 42   ILE E CG1 1 
ATOM   8219  C CG2 . ILE E  1 36  ? 14.016  -42.471 24.091  1.00 60.79  ? 42   ILE E CG2 1 
ATOM   8220  C CD1 . ILE E  1 36  ? 16.001  -41.887 21.923  1.00 57.62  ? 42   ILE E CD1 1 
ATOM   8221  N N   . LEU E  1 37  ? 10.993  -41.444 20.363  1.00 59.97  ? 43   LEU E N   1 
ATOM   8222  C CA  . LEU E  1 37  ? 10.564  -40.607 19.246  1.00 57.35  ? 43   LEU E CA  1 
ATOM   8223  C C   . LEU E  1 37  ? 9.038   -40.551 19.111  1.00 58.32  ? 43   LEU E C   1 
ATOM   8224  O O   . LEU E  1 37  ? 8.396   -41.557 18.802  1.00 59.82  ? 43   LEU E O   1 
ATOM   8225  C CB  . LEU E  1 37  ? 11.175  -41.121 17.936  1.00 61.65  ? 43   LEU E CB  1 
ATOM   8226  C CG  . LEU E  1 37  ? 10.828  -40.386 16.639  1.00 56.40  ? 43   LEU E CG  1 
ATOM   8227  C CD1 . LEU E  1 37  ? 11.481  -39.020 16.627  1.00 51.74  ? 43   LEU E CD1 1 
ATOM   8228  C CD2 . LEU E  1 37  ? 11.243  -41.192 15.421  1.00 57.94  ? 43   LEU E CD2 1 
ATOM   8229  N N   . GLU E  1 38  ? 8.465   -39.370 19.337  1.00 58.02  ? 44   GLU E N   1 
ATOM   8230  C CA  . GLU E  1 38  ? 7.027   -39.154 19.150  1.00 58.56  ? 44   GLU E CA  1 
ATOM   8231  C C   . GLU E  1 38  ? 6.704   -38.994 17.660  1.00 56.35  ? 44   GLU E C   1 
ATOM   8232  O O   . GLU E  1 38  ? 7.312   -38.174 16.978  1.00 53.74  ? 44   GLU E O   1 
ATOM   8233  C CB  . GLU E  1 38  ? 6.560   -37.927 19.941  1.00 58.90  ? 44   GLU E CB  1 
ATOM   8234  C CG  . GLU E  1 38  ? 5.096   -37.567 19.739  1.00 58.97  ? 44   GLU E CG  1 
ATOM   8235  C CD  . GLU E  1 38  ? 4.157   -38.675 20.180  1.00 62.08  ? 44   GLU E CD  1 
ATOM   8236  O OE1 . GLU E  1 38  ? 3.335   -39.122 19.348  1.00 60.27  ? 44   GLU E OE1 1 
ATOM   8237  O OE2 . GLU E  1 38  ? 4.239   -39.091 21.360  1.00 67.27  ? 44   GLU E OE2 1 
ATOM   8238  N N   . LYS E  1 39  ? 5.746   -39.781 17.170  1.00 56.46  ? 45   LYS E N   1 
ATOM   8239  C CA  . LYS E  1 39  ? 5.452   -39.853 15.741  1.00 52.09  ? 45   LYS E CA  1 
ATOM   8240  C C   . LYS E  1 39  ? 3.992   -39.555 15.402  1.00 55.55  ? 45   LYS E C   1 
ATOM   8241  O O   . LYS E  1 39  ? 3.563   -39.766 14.259  1.00 51.86  ? 45   LYS E O   1 
ATOM   8242  C CB  . LYS E  1 39  ? 5.821   -41.234 15.212  1.00 47.41  ? 45   LYS E CB  1 
ATOM   8243  C CG  . LYS E  1 39  ? 7.306   -41.520 15.294  1.00 56.15  ? 45   LYS E CG  1 
ATOM   8244  C CD  . LYS E  1 39  ? 7.639   -42.978 14.968  1.00 59.85  ? 45   LYS E CD  1 
ATOM   8245  C CE  . LYS E  1 39  ? 7.305   -43.937 16.117  1.00 56.45  ? 45   LYS E CE  1 
ATOM   8246  N NZ  . LYS E  1 39  ? 7.862   -43.501 17.433  1.00 61.28  ? 45   LYS E NZ  1 
ATOM   8247  N N   . THR E  1 40  ? 3.237   -39.061 16.386  1.00 54.35  ? 46   THR E N   1 
ATOM   8248  C CA  . THR E  1 40  ? 1.801   -38.858 16.208  1.00 54.49  ? 46   THR E CA  1 
ATOM   8249  C C   . THR E  1 40  ? 1.353   -37.440 16.563  1.00 52.58  ? 46   THR E C   1 
ATOM   8250  O O   . THR E  1 40  ? 1.839   -36.856 17.534  1.00 51.04  ? 46   THR E O   1 
ATOM   8251  C CB  . THR E  1 40  ? 0.986   -39.870 17.089  1.00 55.13  ? 46   THR E CB  1 
ATOM   8252  O OG1 . THR E  1 40  ? 1.015   -39.474 18.472  1.00 56.41  ? 46   THR E OG1 1 
ATOM   8253  C CG2 . THR E  1 40  ? 1.541   -41.299 16.947  1.00 44.64  ? 46   THR E CG2 1 
ATOM   8254  N N   . HIS E  1 41  ? 0.396   -36.911 15.799  1.00 55.59  ? 47   HIS E N   1 
ATOM   8255  C CA  . HIS E  1 41  ? -0.199  -35.601 16.092  1.00 56.87  ? 47   HIS E CA  1 
ATOM   8256  C C   . HIS E  1 41  ? -1.721  -35.687 15.937  1.00 53.82  ? 47   HIS E C   1 
ATOM   8257  O O   . HIS E  1 41  ? -2.216  -36.633 15.330  1.00 53.24  ? 47   HIS E O   1 
ATOM   8258  C CB  . HIS E  1 41  ? 0.388   -34.524 15.176  1.00 51.40  ? 47   HIS E CB  1 
ATOM   8259  C CG  . HIS E  1 41  ? 0.107   -34.736 13.720  1.00 50.02  ? 47   HIS E CG  1 
ATOM   8260  N ND1 . HIS E  1 41  ? -0.975  -34.170 13.077  1.00 50.71  ? 47   HIS E ND1 1 
ATOM   8261  C CD2 . HIS E  1 41  ? 0.762   -35.462 12.782  1.00 54.86  ? 47   HIS E CD2 1 
ATOM   8262  C CE1 . HIS E  1 41  ? -0.964  -34.521 11.802  1.00 50.81  ? 47   HIS E CE1 1 
ATOM   8263  N NE2 . HIS E  1 41  ? 0.076   -35.311 11.598  1.00 52.90  ? 47   HIS E NE2 1 
ATOM   8264  N N   . ASN E  1 42  ? -2.462  -34.712 16.459  1.00 54.50  ? 48   ASN E N   1 
ATOM   8265  C CA  . ASN E  1 42  ? -3.925  -34.809 16.420  1.00 54.46  ? 48   ASN E CA  1 
ATOM   8266  C C   . ASN E  1 42  ? -4.615  -34.141 15.229  1.00 56.14  ? 48   ASN E C   1 
ATOM   8267  O O   . ASN E  1 42  ? -5.835  -34.155 15.166  1.00 64.53  ? 48   ASN E O   1 
ATOM   8268  C CB  . ASN E  1 42  ? -4.544  -34.227 17.685  1.00 53.12  ? 48   ASN E CB  1 
ATOM   8269  C CG  . ASN E  1 42  ? -4.611  -32.732 17.653  1.00 60.61  ? 48   ASN E CG  1 
ATOM   8270  O OD1 . ASN E  1 42  ? -3.752  -32.064 17.073  1.00 63.62  ? 48   ASN E OD1 1 
ATOM   8271  N ND2 . ASN E  1 42  ? -5.651  -32.183 18.265  1.00 66.00  ? 48   ASN E ND2 1 
ATOM   8272  N N   . GLY E  1 43  ? -3.862  -33.495 14.341  1.00 55.05  ? 49   GLY E N   1 
ATOM   8273  C CA  . GLY E  1 43  ? -4.434  -32.914 13.130  1.00 52.40  ? 49   GLY E CA  1 
ATOM   8274  C C   . GLY E  1 43  ? -5.355  -31.710 13.314  1.00 55.13  ? 49   GLY E C   1 
ATOM   8275  O O   . GLY E  1 43  ? -6.133  -31.356 12.428  1.00 58.40  ? 49   GLY E O   1 
ATOM   8276  N N   . LYS E  1 44  ? -5.270  -31.053 14.457  1.00 55.30  ? 50   LYS E N   1 
ATOM   8277  C CA  . LYS E  1 44  ? -6.133  -29.914 14.686  1.00 56.12  ? 50   LYS E CA  1 
ATOM   8278  C C   . LYS E  1 44  ? -5.352  -28.678 15.152  1.00 59.08  ? 50   LYS E C   1 
ATOM   8279  O O   . LYS E  1 44  ? -4.200  -28.784 15.591  1.00 58.80  ? 50   LYS E O   1 
ATOM   8280  C CB  . LYS E  1 44  ? -7.197  -30.299 15.711  1.00 62.70  ? 50   LYS E CB  1 
ATOM   8281  C CG  . LYS E  1 44  ? -8.023  -31.506 15.286  1.00 60.83  ? 50   LYS E CG  1 
ATOM   8282  C CD  . LYS E  1 44  ? -9.043  -31.897 16.352  1.00 67.50  ? 50   LYS E CD  1 
ATOM   8283  C CE  . LYS E  1 44  ? -10.008 -30.761 16.654  1.00 74.73  ? 50   LYS E CE  1 
ATOM   8284  N NZ  . LYS E  1 44  ? -10.985 -30.505 15.545  1.00 82.89  ? 50   LYS E NZ  1 
ATOM   8285  N N   . LEU E  1 45  ? -5.994  -27.510 15.056  1.00 59.98  ? 51   LEU E N   1 
ATOM   8286  C CA  . LEU E  1 45  ? -5.451  -26.256 15.583  1.00 54.93  ? 51   LEU E CA  1 
ATOM   8287  C C   . LEU E  1 45  ? -6.119  -25.929 16.917  1.00 54.33  ? 51   LEU E C   1 
ATOM   8288  O O   . LEU E  1 45  ? -7.338  -25.735 16.966  1.00 55.12  ? 51   LEU E O   1 
ATOM   8289  C CB  . LEU E  1 45  ? -5.661  -25.098 14.592  1.00 51.53  ? 51   LEU E CB  1 
ATOM   8290  C CG  . LEU E  1 45  ? -4.937  -25.077 13.249  1.00 49.34  ? 51   LEU E CG  1 
ATOM   8291  C CD1 . LEU E  1 45  ? -5.335  -23.844 12.481  1.00 48.70  ? 51   LEU E CD1 1 
ATOM   8292  C CD2 . LEU E  1 45  ? -3.447  -25.102 13.439  1.00 47.20  ? 51   LEU E CD2 1 
ATOM   8293  N N   . CYS E  1 46  ? -5.317  -25.834 17.980  1.00 53.29  ? 52   CYS E N   1 
ATOM   8294  C CA  . CYS E  1 46  ? -5.831  -25.708 19.345  1.00 52.05  ? 52   CYS E CA  1 
ATOM   8295  C C   . CYS E  1 46  ? -5.370  -24.445 20.035  1.00 52.53  ? 52   CYS E C   1 
ATOM   8296  O O   . CYS E  1 46  ? -4.536  -23.704 19.508  1.00 52.29  ? 52   CYS E O   1 
ATOM   8297  C CB  . CYS E  1 46  ? -5.384  -26.904 20.176  1.00 53.22  ? 52   CYS E CB  1 
ATOM   8298  S SG  . CYS E  1 46  ? -5.515  -28.471 19.288  1.00 63.46  ? 52   CYS E SG  1 
ATOM   8299  N N   . ASN E  1 47  ? -5.907  -24.207 21.228  1.00 55.23  ? 53   ASN E N   1 
ATOM   8300  C CA  . ASN E  1 47  ? -5.382  -23.159 22.099  1.00 49.93  ? 53   ASN E CA  1 
ATOM   8301  C C   . ASN E  1 47  ? -3.989  -23.536 22.582  1.00 50.78  ? 53   ASN E C   1 
ATOM   8302  O O   . ASN E  1 47  ? -3.648  -24.722 22.649  1.00 50.65  ? 53   ASN E O   1 
ATOM   8303  C CB  . ASN E  1 47  ? -6.287  -22.920 23.305  1.00 54.54  ? 53   ASN E CB  1 
ATOM   8304  C CG  . ASN E  1 47  ? -7.603  -22.258 22.950  1.00 57.04  ? 53   ASN E CG  1 
ATOM   8305  O OD1 . ASN E  1 47  ? -8.027  -22.229 21.797  1.00 61.22  ? 53   ASN E OD1 1 
ATOM   8306  N ND2 . ASN E  1 47  ? -8.248  -21.695 23.956  1.00 55.30  ? 53   ASN E ND2 1 
ATOM   8307  N N   . LEU E  1 48  ? -3.176  -22.536 22.897  1.00 49.82  ? 54   LEU E N   1 
ATOM   8308  C CA  . LEU E  1 48  ? -1.882  -22.798 23.507  1.00 50.77  ? 54   LEU E CA  1 
ATOM   8309  C C   . LEU E  1 48  ? -2.007  -22.458 24.972  1.00 54.92  ? 54   LEU E C   1 
ATOM   8310  O O   . LEU E  1 48  ? -2.189  -21.282 25.309  1.00 53.12  ? 54   LEU E O   1 
ATOM   8311  C CB  . LEU E  1 48  ? -0.770  -21.978 22.859  1.00 48.83  ? 54   LEU E CB  1 
ATOM   8312  C CG  . LEU E  1 48  ? 0.660   -22.427 23.189  1.00 50.08  ? 54   LEU E CG  1 
ATOM   8313  C CD1 . LEU E  1 48  ? 1.024   -23.766 22.550  1.00 42.14  ? 54   LEU E CD1 1 
ATOM   8314  C CD2 . LEU E  1 48  ? 1.671   -21.339 22.814  1.00 48.56  ? 54   LEU E CD2 1 
ATOM   8315  N N   . ASP E  1 49  ? -1.890  -23.474 25.837  1.00 55.53  ? 55   ASP E N   1 
ATOM   8316  C CA  . ASP E  1 49  ? -2.326  -23.349 27.231  1.00 59.34  ? 55   ASP E CA  1 
ATOM   8317  C C   . ASP E  1 49  ? -3.776  -22.878 27.247  1.00 55.72  ? 55   ASP E C   1 
ATOM   8318  O O   . ASP E  1 49  ? -4.648  -23.522 26.684  1.00 53.09  ? 55   ASP E O   1 
ATOM   8319  C CB  . ASP E  1 49  ? -1.440  -22.384 28.034  1.00 61.85  ? 55   ASP E CB  1 
ATOM   8320  C CG  . ASP E  1 49  ? -0.320  -23.094 28.781  1.00 72.17  ? 55   ASP E CG  1 
ATOM   8321  O OD1 . ASP E  1 49  ? -0.516  -24.262 29.193  1.00 73.73  ? 55   ASP E OD1 1 
ATOM   8322  O OD2 . ASP E  1 49  ? 0.761   -22.480 28.945  1.00 76.51  ? 55   ASP E OD2 1 
ATOM   8323  N N   . GLY E  1 50  A -4.047  -21.742 27.866  1.00 50.62  ? 55   GLY E N   1 
ATOM   8324  C CA  . GLY E  1 50  A -5.424  -21.291 27.867  1.00 61.55  ? 55   GLY E CA  1 
ATOM   8325  C C   . GLY E  1 50  A -5.839  -20.436 26.672  1.00 60.86  ? 55   GLY E C   1 
ATOM   8326  O O   . GLY E  1 50  A -7.036  -20.225 26.440  1.00 61.60  ? 55   GLY E O   1 
ATOM   8327  N N   . VAL E  1 51  ? -4.866  -19.995 25.881  1.00 50.85  ? 56   VAL E N   1 
ATOM   8328  C CA  . VAL E  1 51  ? -5.069  -18.842 25.010  1.00 51.86  ? 56   VAL E CA  1 
ATOM   8329  C C   . VAL E  1 51  ? -5.426  -19.230 23.572  1.00 51.89  ? 56   VAL E C   1 
ATOM   8330  O O   . VAL E  1 51  ? -4.773  -20.080 22.969  1.00 53.85  ? 56   VAL E O   1 
ATOM   8331  C CB  . VAL E  1 51  ? -3.813  -17.949 25.023  1.00 50.59  ? 56   VAL E CB  1 
ATOM   8332  C CG1 . VAL E  1 51  ? -4.089  -16.610 24.339  1.00 50.54  ? 56   VAL E CG1 1 
ATOM   8333  C CG2 . VAL E  1 51  ? -3.369  -17.718 26.447  1.00 41.61  ? 56   VAL E CG2 1 
ATOM   8334  N N   . LYS E  1 52  ? -6.498  -18.635 23.053  1.00 47.80  ? 57   LYS E N   1 
ATOM   8335  C CA  . LYS E  1 52  ? -6.970  -18.922 21.698  1.00 51.81  ? 57   LYS E CA  1 
ATOM   8336  C C   . LYS E  1 52  ? -6.143  -18.180 20.626  1.00 51.73  ? 57   LYS E C   1 
ATOM   8337  O O   . LYS E  1 52  ? -5.771  -17.003 20.796  1.00 49.35  ? 57   LYS E O   1 
ATOM   8338  C CB  . LYS E  1 52  ? -8.459  -18.566 21.567  1.00 54.28  ? 57   LYS E CB  1 
ATOM   8339  C CG  . LYS E  1 52  ? -9.045  -18.847 20.190  1.00 58.68  ? 57   LYS E CG  1 
ATOM   8340  C CD  . LYS E  1 52  ? -10.546 -18.591 20.135  1.00 62.91  ? 57   LYS E CD  1 
ATOM   8341  C CE  . LYS E  1 52  ? -11.088 -18.772 18.708  1.00 59.25  ? 57   LYS E CE  1 
ATOM   8342  N NZ  . LYS E  1 52  ? -10.455 -19.937 18.037  1.00 56.13  ? 57   LYS E NZ  1 
ATOM   8343  N N   . PRO E  1 53  ? -5.853  -18.867 19.513  1.00 45.24  ? 58   PRO E N   1 
ATOM   8344  C CA  . PRO E  1 53  ? -5.100  -18.195 18.452  1.00 47.90  ? 58   PRO E CA  1 
ATOM   8345  C C   . PRO E  1 53  ? -5.934  -17.189 17.637  1.00 49.65  ? 58   PRO E C   1 
ATOM   8346  O O   . PRO E  1 53  ? -7.160  -17.320 17.574  1.00 48.67  ? 58   PRO E O   1 
ATOM   8347  C CB  . PRO E  1 53  ? -4.637  -19.368 17.574  1.00 46.09  ? 58   PRO E CB  1 
ATOM   8348  C CG  . PRO E  1 53  ? -5.680  -20.440 17.798  1.00 50.05  ? 58   PRO E CG  1 
ATOM   8349  C CD  . PRO E  1 53  ? -6.041  -20.309 19.246  1.00 48.77  ? 58   PRO E CD  1 
ATOM   8350  N N   . LEU E  1 54  ? -5.270  -16.204 17.026  1.00 43.46  ? 59   LEU E N   1 
ATOM   8351  C CA  . LEU E  1 54  ? -5.925  -15.345 16.048  1.00 45.25  ? 59   LEU E CA  1 
ATOM   8352  C C   . LEU E  1 54  ? -5.922  -16.070 14.716  1.00 43.86  ? 59   LEU E C   1 
ATOM   8353  O O   . LEU E  1 54  ? -4.904  -16.139 14.045  1.00 48.36  ? 59   LEU E O   1 
ATOM   8354  C CB  . LEU E  1 54  ? -5.226  -13.984 15.919  1.00 42.91  ? 59   LEU E CB  1 
ATOM   8355  C CG  . LEU E  1 54  ? -5.686  -13.110 14.738  1.00 45.24  ? 59   LEU E CG  1 
ATOM   8356  C CD1 . LEU E  1 54  ? -7.180  -12.853 14.807  1.00 41.80  ? 59   LEU E CD1 1 
ATOM   8357  C CD2 . LEU E  1 54  ? -4.925  -11.764 14.646  1.00 40.45  ? 59   LEU E CD2 1 
ATOM   8358  N N   . ILE E  1 55  ? -7.066  -16.611 14.333  1.00 41.88  ? 60   ILE E N   1 
ATOM   8359  C CA  . ILE E  1 55  ? -7.157  -17.345 13.084  1.00 47.72  ? 60   ILE E CA  1 
ATOM   8360  C C   . ILE E  1 55  ? -7.815  -16.454 12.037  1.00 53.29  ? 60   ILE E C   1 
ATOM   8361  O O   . ILE E  1 55  ? -9.044  -16.273 12.016  1.00 54.16  ? 60   ILE E O   1 
ATOM   8362  C CB  . ILE E  1 55  ? -7.921  -18.674 13.253  1.00 49.79  ? 60   ILE E CB  1 
ATOM   8363  C CG1 . ILE E  1 55  ? -7.179  -19.579 14.242  1.00 52.79  ? 60   ILE E CG1 1 
ATOM   8364  C CG2 . ILE E  1 55  ? -8.045  -19.403 11.943  1.00 45.70  ? 60   ILE E CG2 1 
ATOM   8365  C CD1 . ILE E  1 55  ? -7.793  -20.973 14.401  1.00 55.50  ? 60   ILE E CD1 1 
ATOM   8366  N N   . LEU E  1 56  ? -6.964  -15.870 11.190  1.00 54.58  ? 61   LEU E N   1 
ATOM   8367  C CA  . LEU E  1 56  ? -7.419  -15.104 10.045  1.00 51.88  ? 61   LEU E CA  1 
ATOM   8368  C C   . LEU E  1 56  ? -8.018  -16.162 9.131   1.00 53.10  ? 61   LEU E C   1 
ATOM   8369  O O   . LEU E  1 56  ? -7.592  -17.318 9.170   1.00 55.35  ? 61   LEU E O   1 
ATOM   8370  C CB  . LEU E  1 56  ? -6.252  -14.319 9.402   1.00 47.59  ? 61   LEU E CB  1 
ATOM   8371  C CG  . LEU E  1 56  ? -5.297  -13.492 10.300  1.00 44.20  ? 61   LEU E CG  1 
ATOM   8372  C CD1 . LEU E  1 56  ? -4.025  -13.011 9.573   1.00 37.96  ? 61   LEU E CD1 1 
ATOM   8373  C CD2 . LEU E  1 56  ? -6.009  -12.300 10.964  1.00 42.31  ? 61   LEU E CD2 1 
ATOM   8374  N N   . ARG E  1 57  ? -8.997  -15.814 8.312   1.00 54.32  ? 62   ARG E N   1 
ATOM   8375  C CA  . ARG E  1 57  ? -9.592  -16.866 7.494   1.00 59.48  ? 62   ARG E CA  1 
ATOM   8376  C C   . ARG E  1 57  ? -9.005  -16.833 6.119   1.00 56.91  ? 62   ARG E C   1 
ATOM   8377  O O   . ARG E  1 57  ? -8.017  -17.507 5.826   1.00 53.47  ? 62   ARG E O   1 
ATOM   8378  C CB  . ARG E  1 57  ? -11.115 -16.718 7.389   1.00 66.49  ? 62   ARG E CB  1 
ATOM   8379  C CG  . ARG E  1 57  ? -11.932 -17.174 8.590   1.00 67.05  ? 62   ARG E CG  1 
ATOM   8380  C CD  . ARG E  1 57  ? -13.437 -17.102 8.251   1.00 75.44  ? 62   ARG E CD  1 
ATOM   8381  N NE  . ARG E  1 57  ? -14.269 -16.796 9.412   1.00 75.53  ? 62   ARG E NE  1 
ATOM   8382  C CZ  . ARG E  1 57  ? -14.689 -17.708 10.285  1.00 78.86  ? 62   ARG E CZ  1 
ATOM   8383  N NH1 . ARG E  1 57  ? -14.377 -18.987 10.106  1.00 79.98  ? 62   ARG E NH1 1 
ATOM   8384  N NH2 . ARG E  1 57  ? -15.433 -17.347 11.330  1.00 76.97  ? 62   ARG E NH2 1 
ATOM   8385  N N   . ASP E  1 58  ? -9.663  -16.040 5.285   1.00 54.85  ? 63   ASP E N   1 
ATOM   8386  C CA  . ASP E  1 58  ? -9.241  -15.781 3.935   1.00 52.71  ? 63   ASP E CA  1 
ATOM   8387  C C   . ASP E  1 58  ? -8.686  -14.368 3.910   1.00 49.96  ? 63   ASP E C   1 
ATOM   8388  O O   . ASP E  1 58  ? -8.650  -13.729 2.864   1.00 57.97  ? 63   ASP E O   1 
ATOM   8389  C CB  . ASP E  1 58  ? -10.406 -15.937 2.954   1.00 56.11  ? 63   ASP E CB  1 
ATOM   8390  C CG  . ASP E  1 58  ? -11.028 -17.321 2.996   1.00 62.33  ? 63   ASP E CG  1 
ATOM   8391  O OD1 . ASP E  1 58  ? -10.368 -18.300 2.566   1.00 63.87  ? 63   ASP E OD1 1 
ATOM   8392  O OD2 . ASP E  1 58  ? -12.193 -17.421 3.448   1.00 64.24  ? 63   ASP E OD2 1 
ATOM   8393  N N   . CYS E  1 59  ? -8.305  -13.864 5.075   1.00 47.36  ? 64   CYS E N   1 
ATOM   8394  C CA  . CYS E  1 59  ? -7.692  -12.549 5.158   1.00 47.34  ? 64   CYS E CA  1 
ATOM   8395  C C   . CYS E  1 59  ? -6.205  -12.735 5.397   1.00 48.88  ? 64   CYS E C   1 
ATOM   8396  O O   . CYS E  1 59  ? -5.802  -13.717 6.033   1.00 52.33  ? 64   CYS E O   1 
ATOM   8397  C CB  . CYS E  1 59  ? -8.320  -11.707 6.267   1.00 50.83  ? 64   CYS E CB  1 
ATOM   8398  S SG  . CYS E  1 59  ? -9.900  -10.923 5.808   1.00 67.99  ? 64   CYS E SG  1 
ATOM   8399  N N   . SER E  1 60  ? -5.395  -11.834 4.839   1.00 43.45  ? 65   SER E N   1 
ATOM   8400  C CA  . SER E  1 60  ? -3.956  -11.808 5.089   1.00 38.20  ? 65   SER E CA  1 
ATOM   8401  C C   . SER E  1 60  ? -3.697  -10.796 6.193   1.00 36.90  ? 65   SER E C   1 
ATOM   8402  O O   . SER E  1 60  ? -4.603  -10.027 6.537   1.00 37.25  ? 65   SER E O   1 
ATOM   8403  C CB  . SER E  1 60  ? -3.181  -11.405 3.841   1.00 42.76  ? 65   SER E CB  1 
ATOM   8404  O OG  . SER E  1 60  ? -3.377  -10.021 3.582   1.00 44.37  ? 65   SER E OG  1 
ATOM   8405  N N   . VAL E  1 61  ? -2.455  -10.737 6.688   1.00 34.97  ? 66   VAL E N   1 
ATOM   8406  C CA  . VAL E  1 61  ? -2.079  -9.778  7.742   1.00 32.96  ? 66   VAL E CA  1 
ATOM   8407  C C   . VAL E  1 61  ? -2.278  -8.340  7.297   1.00 31.17  ? 66   VAL E C   1 
ATOM   8408  O O   . VAL E  1 61  ? -2.748  -7.508  8.065   1.00 35.65  ? 66   VAL E O   1 
ATOM   8409  C CB  . VAL E  1 61  ? -0.611  -9.976  8.210   1.00 31.33  ? 66   VAL E CB  1 
ATOM   8410  C CG1 . VAL E  1 61  ? -0.089  -8.744  8.917   1.00 22.60  ? 66   VAL E CG1 1 
ATOM   8411  C CG2 . VAL E  1 61  ? -0.486  -11.229 9.093   1.00 30.61  ? 66   VAL E CG2 1 
ATOM   8412  N N   . ALA E  1 62  ? -1.905  -8.035  6.061   1.00 35.95  ? 67   ALA E N   1 
ATOM   8413  C CA  . ALA E  1 62  ? -2.115  -6.692  5.552   1.00 35.01  ? 67   ALA E CA  1 
ATOM   8414  C C   . ALA E  1 62  ? -3.603  -6.381  5.505   1.00 35.42  ? 67   ALA E C   1 
ATOM   8415  O O   . ALA E  1 62  ? -4.012  -5.278  5.875   1.00 31.63  ? 67   ALA E O   1 
ATOM   8416  C CB  . ALA E  1 62  ? -1.490  -6.521  4.192   1.00 39.05  ? 67   ALA E CB  1 
ATOM   8417  N N   . GLY E  1 63  ? -4.412  -7.353  5.068   1.00 39.45  ? 68   GLY E N   1 
ATOM   8418  C CA  . GLY E  1 63  ? -5.852  -7.138  4.980   1.00 40.15  ? 68   GLY E CA  1 
ATOM   8419  C C   . GLY E  1 63  ? -6.415  -6.792  6.346   1.00 44.69  ? 68   GLY E C   1 
ATOM   8420  O O   . GLY E  1 63  ? -7.107  -5.755  6.516   1.00 41.70  ? 68   GLY E O   1 
ATOM   8421  N N   . TRP E  1 64  ? -6.050  -7.612  7.336   1.00 40.05  ? 69   TRP E N   1 
ATOM   8422  C CA  . TRP E  1 64  ? -6.440  -7.363  8.717   1.00 35.41  ? 69   TRP E CA  1 
ATOM   8423  C C   . TRP E  1 64  ? -5.983  -5.951  9.171   1.00 37.10  ? 69   TRP E C   1 
ATOM   8424  O O   . TRP E  1 64  ? -6.818  -5.139  9.568   1.00 40.65  ? 69   TRP E O   1 
ATOM   8425  C CB  . TRP E  1 64  ? -5.865  -8.461  9.609   1.00 36.72  ? 69   TRP E CB  1 
ATOM   8426  C CG  . TRP E  1 64  ? -5.795  -8.087  11.071  1.00 47.41  ? 69   TRP E CG  1 
ATOM   8427  C CD1 . TRP E  1 64  ? -6.702  -7.352  11.785  1.00 43.57  ? 69   TRP E CD1 1 
ATOM   8428  C CD2 . TRP E  1 64  ? -4.745  -8.420  11.987  1.00 43.11  ? 69   TRP E CD2 1 
ATOM   8429  N NE1 . TRP E  1 64  ? -6.279  -7.211  13.082  1.00 41.70  ? 69   TRP E NE1 1 
ATOM   8430  C CE2 . TRP E  1 64  ? -5.081  -7.858  13.231  1.00 40.44  ? 69   TRP E CE2 1 
ATOM   8431  C CE3 . TRP E  1 64  ? -3.560  -9.152  11.875  1.00 41.46  ? 69   TRP E CE3 1 
ATOM   8432  C CZ2 . TRP E  1 64  ? -4.270  -7.997  14.359  1.00 43.59  ? 69   TRP E CZ2 1 
ATOM   8433  C CZ3 . TRP E  1 64  ? -2.751  -9.287  13.002  1.00 38.07  ? 69   TRP E CZ3 1 
ATOM   8434  C CH2 . TRP E  1 64  ? -3.110  -8.716  14.221  1.00 38.55  ? 69   TRP E CH2 1 
ATOM   8435  N N   . LEU E  1 65  ? -4.692  -5.628  9.076   1.00 33.03  ? 70   LEU E N   1 
ATOM   8436  C CA  . LEU E  1 65  ? -4.203  -4.363  9.648   1.00 37.83  ? 70   LEU E CA  1 
ATOM   8437  C C   . LEU E  1 65  ? -4.672  -3.091  8.970   1.00 38.49  ? 70   LEU E C   1 
ATOM   8438  O O   . LEU E  1 65  ? -4.806  -2.050  9.626   1.00 36.45  ? 70   LEU E O   1 
ATOM   8439  C CB  . LEU E  1 65  ? -2.675  -4.331  9.710   1.00 33.30  ? 70   LEU E CB  1 
ATOM   8440  C CG  . LEU E  1 65  ? -2.093  -5.219  10.814  1.00 44.09  ? 70   LEU E CG  1 
ATOM   8441  C CD1 . LEU E  1 65  ? -0.579  -5.079  10.851  1.00 35.58  ? 70   LEU E CD1 1 
ATOM   8442  C CD2 . LEU E  1 65  ? -2.732  -4.902  12.195  1.00 34.89  ? 70   LEU E CD2 1 
ATOM   8443  N N   . LEU E  1 66  ? -4.814  -3.144  7.650   1.00 40.58  ? 71   LEU E N   1 
ATOM   8444  C CA  . LEU E  1 66  ? -5.293  -1.993  6.896   1.00 38.66  ? 71   LEU E CA  1 
ATOM   8445  C C   . LEU E  1 66  ? -6.821  -1.903  6.991   1.00 41.57  ? 71   LEU E C   1 
ATOM   8446  O O   . LEU E  1 66  ? -7.400  -0.805  6.926   1.00 36.03  ? 71   LEU E O   1 
ATOM   8447  C CB  . LEU E  1 66  ? -4.818  -2.078  5.445   1.00 40.63  ? 71   LEU E CB  1 
ATOM   8448  C CG  . LEU E  1 66  ? -3.356  -1.644  5.223   1.00 41.00  ? 71   LEU E CG  1 
ATOM   8449  C CD1 . LEU E  1 66  ? -2.853  -1.980  3.805   1.00 30.02  ? 71   LEU E CD1 1 
ATOM   8450  C CD2 . LEU E  1 66  ? -3.182  -0.142  5.522   1.00 32.83  ? 71   LEU E CD2 1 
ATOM   8451  N N   . GLY E  1 67  ? -7.470  -3.056  7.178   1.00 39.38  ? 72   GLY E N   1 
ATOM   8452  C CA  . GLY E  1 67  ? -8.911  -3.063  7.332   1.00 39.92  ? 72   GLY E CA  1 
ATOM   8453  C C   . GLY E  1 67  ? -9.635  -3.137  5.998   1.00 49.90  ? 72   GLY E C   1 
ATOM   8454  O O   . GLY E  1 67  ? -10.487 -2.274  5.665   1.00 49.74  ? 72   GLY E O   1 
ATOM   8455  N N   . ASN E  1 68  ? -9.264  -4.146  5.218   1.00 42.04  ? 73   ASN E N   1 
ATOM   8456  C CA  . ASN E  1 68  ? -10.025 -4.527  4.054   1.00 45.03  ? 73   ASN E CA  1 
ATOM   8457  C C   . ASN E  1 68  ? -11.458 -4.680  4.528   1.00 53.09  ? 73   ASN E C   1 
ATOM   8458  O O   . ASN E  1 68  ? -11.702 -5.371  5.517   1.00 58.26  ? 73   ASN E O   1 
ATOM   8459  C CB  . ASN E  1 68  ? -9.469  -5.837  3.481   1.00 49.90  ? 73   ASN E CB  1 
ATOM   8460  C CG  . ASN E  1 68  ? -10.121 -6.263  2.168   1.00 47.44  ? 73   ASN E CG  1 
ATOM   8461  O OD1 . ASN E  1 68  ? -11.332 -6.164  1.977   1.00 46.98  ? 73   ASN E OD1 1 
ATOM   8462  N ND2 . ASN E  1 68  ? -9.306  -6.795  1.276   1.00 46.30  ? 73   ASN E ND2 1 
ATOM   8463  N N   . PRO E  1 69  ? -12.413 -4.021  3.848   1.00 56.58  ? 74   PRO E N   1 
ATOM   8464  C CA  . PRO E  1 69  ? -13.831 -4.071  4.233   1.00 56.46  ? 74   PRO E CA  1 
ATOM   8465  C C   . PRO E  1 69  ? -14.380 -5.510  4.312   1.00 64.83  ? 74   PRO E C   1 
ATOM   8466  O O   . PRO E  1 69  ? -15.436 -5.732  4.921   1.00 68.97  ? 74   PRO E O   1 
ATOM   8467  C CB  . PRO E  1 69  ? -14.526 -3.274  3.127   1.00 54.55  ? 74   PRO E CB  1 
ATOM   8468  C CG  . PRO E  1 69  ? -13.474 -2.370  2.599   1.00 49.80  ? 74   PRO E CG  1 
ATOM   8469  C CD  . PRO E  1 69  ? -12.180 -3.107  2.716   1.00 53.53  ? 74   PRO E CD  1 
ATOM   8470  N N   . MET E  1 70  ? -13.688 -6.470  3.703   1.00 57.14  ? 75   MET E N   1 
ATOM   8471  C CA  . MET E  1 70  ? -14.118 -7.860  3.768   1.00 58.81  ? 75   MET E CA  1 
ATOM   8472  C C   . MET E  1 70  ? -13.512 -8.651  4.943   1.00 58.97  ? 75   MET E C   1 
ATOM   8473  O O   . MET E  1 70  ? -13.649 -9.872  5.015   1.00 59.78  ? 75   MET E O   1 
ATOM   8474  C CB  . MET E  1 70  ? -13.786 -8.545  2.451   1.00 53.97  ? 75   MET E CB  1 
ATOM   8475  C CG  . MET E  1 70  ? -14.587 -7.941  1.335   1.00 62.27  ? 75   MET E CG  1 
ATOM   8476  S SD  . MET E  1 70  ? -16.272 -8.554  1.297   1.00 78.15  ? 75   MET E SD  1 
ATOM   8477  C CE  . MET E  1 70  ? -16.994 -7.537  0.004   1.00 62.56  ? 75   MET E CE  1 
ATOM   8478  N N   . CYS E  1 71  ? -12.822 -7.958  5.840   1.00 57.76  ? 76   CYS E N   1 
ATOM   8479  C CA  . CYS E  1 71  ? -12.165 -8.597  6.977   1.00 60.11  ? 76   CYS E CA  1 
ATOM   8480  C C   . CYS E  1 71  ? -12.717 -8.013  8.274   1.00 60.58  ? 76   CYS E C   1 
ATOM   8481  O O   . CYS E  1 71  ? -12.034 -7.990  9.312   1.00 54.55  ? 76   CYS E O   1 
ATOM   8482  C CB  . CYS E  1 71  ? -10.647 -8.378  6.937   1.00 57.99  ? 76   CYS E CB  1 
ATOM   8483  S SG  . CYS E  1 71  ? -9.759  -8.904  5.471   1.00 58.51  ? 76   CYS E SG  1 
ATOM   8484  N N   . ASP E  1 72  ? -13.957 -7.546  8.215   1.00 61.69  ? 77   ASP E N   1 
ATOM   8485  C CA  . ASP E  1 72  ? -14.546 -6.812  9.329   1.00 61.55  ? 77   ASP E CA  1 
ATOM   8486  C C   . ASP E  1 72  ? -14.709 -7.673  10.593  1.00 59.89  ? 77   ASP E C   1 
ATOM   8487  O O   . ASP E  1 72  ? -14.989 -7.150  11.678  1.00 59.89  ? 77   ASP E O   1 
ATOM   8488  C CB  . ASP E  1 72  ? -15.884 -6.206  8.883   1.00 69.19  ? 77   ASP E CB  1 
ATOM   8489  C CG  . ASP E  1 72  ? -15.703 -4.956  8.011   1.00 69.38  ? 77   ASP E CG  1 
ATOM   8490  O OD1 . ASP E  1 72  ? -14.616 -4.336  8.052   1.00 65.27  ? 77   ASP E OD1 1 
ATOM   8491  O OD2 . ASP E  1 72  ? -16.638 -4.619  7.254   1.00 72.25  ? 77   ASP E OD2 1 
ATOM   8492  N N   . GLU E  1 73  ? -14.516 -8.987  10.456  1.00 55.13  ? 78   GLU E N   1 
ATOM   8493  C CA  . GLU E  1 73  ? -14.493 -9.872  11.611  1.00 50.77  ? 78   GLU E CA  1 
ATOM   8494  C C   . GLU E  1 73  ? -13.392 -9.470  12.597  1.00 54.49  ? 78   GLU E C   1 
ATOM   8495  O O   . GLU E  1 73  ? -13.536 -9.621  13.825  1.00 52.74  ? 78   GLU E O   1 
ATOM   8496  C CB  . GLU E  1 73  ? -14.264 -11.321 11.183  1.00 49.60  ? 78   GLU E CB  1 
ATOM   8497  C CG  . GLU E  1 73  ? -14.231 -12.279 12.380  1.00 53.53  ? 78   GLU E CG  1 
ATOM   8498  C CD  . GLU E  1 73  ? -14.019 -13.729 11.988  1.00 58.60  ? 78   GLU E CD  1 
ATOM   8499  O OE1 . GLU E  1 73  ? -14.011 -14.004 10.765  1.00 54.88  ? 78   GLU E OE1 1 
ATOM   8500  O OE2 . GLU E  1 73  ? -13.866 -14.584 12.907  1.00 59.57  ? 78   GLU E OE2 1 
ATOM   8501  N N   . PHE E  1 74  ? -12.324 -8.899  12.046  1.00 51.67  ? 79   PHE E N   1 
ATOM   8502  C CA  . PHE E  1 74  ? -11.107 -8.644  12.785  1.00 46.59  ? 79   PHE E CA  1 
ATOM   8503  C C   . PHE E  1 74  ? -10.907 -7.179  13.128  1.00 46.91  ? 79   PHE E C   1 
ATOM   8504  O O   . PHE E  1 74  ? -9.784  -6.763  13.454  1.00 45.61  ? 79   PHE E O   1 
ATOM   8505  C CB  . PHE E  1 74  ? -9.905  -9.158  11.972  1.00 39.74  ? 79   PHE E CB  1 
ATOM   8506  C CG  . PHE E  1 74  ? -10.064 -10.569 11.473  1.00 47.49  ? 79   PHE E CG  1 
ATOM   8507  C CD1 . PHE E  1 74  ? -9.920  -11.648 12.341  1.00 50.40  ? 79   PHE E CD1 1 
ATOM   8508  C CD2 . PHE E  1 74  ? -10.372 -10.828 10.146  1.00 50.03  ? 79   PHE E CD2 1 
ATOM   8509  C CE1 . PHE E  1 74  ? -10.058 -12.964 11.884  1.00 50.43  ? 79   PHE E CE1 1 
ATOM   8510  C CE2 . PHE E  1 74  ? -10.523 -12.143 9.690   1.00 47.28  ? 79   PHE E CE2 1 
ATOM   8511  C CZ  . PHE E  1 74  ? -10.363 -13.205 10.559  1.00 45.23  ? 79   PHE E CZ  1 
ATOM   8512  N N   . LEU E  1 75  ? -11.985 -6.404  13.142  1.00 43.46  ? 80   LEU E N   1 
ATOM   8513  C CA  . LEU E  1 75  ? -11.812 -4.988  13.442  1.00 48.09  ? 80   LEU E CA  1 
ATOM   8514  C C   . LEU E  1 75  ? -11.278 -4.807  14.855  1.00 52.16  ? 80   LEU E C   1 
ATOM   8515  O O   . LEU E  1 75  ? -10.529 -3.859  15.111  1.00 53.24  ? 80   LEU E O   1 
ATOM   8516  C CB  . LEU E  1 75  ? -13.116 -4.189  13.254  1.00 48.75  ? 80   LEU E CB  1 
ATOM   8517  C CG  . LEU E  1 75  ? -13.421 -3.750  11.814  1.00 54.47  ? 80   LEU E CG  1 
ATOM   8518  C CD1 . LEU E  1 75  ? -14.839 -4.071  11.449  1.00 62.19  ? 80   LEU E CD1 1 
ATOM   8519  C CD2 . LEU E  1 75  ? -13.161 -2.263  11.595  1.00 49.47  ? 80   LEU E CD2 1 
ATOM   8520  N N   . ASN E  1 76  ? -11.624 -5.732  15.753  1.00 46.91  ? 81   ASN E N   1 
ATOM   8521  C CA  . ASN E  1 76  ? -11.144 -5.653  17.122  1.00 48.38  ? 81   ASN E CA  1 
ATOM   8522  C C   . ASN E  1 76  ? -10.940 -7.018  17.766  1.00 55.11  ? 81   ASN E C   1 
ATOM   8523  O O   . ASN E  1 76  ? -11.869 -7.593  18.341  1.00 60.71  ? 81   ASN E O   1 
ATOM   8524  C CB  . ASN E  1 76  ? -12.096 -4.820  17.959  1.00 45.85  ? 81   ASN E CB  1 
ATOM   8525  C CG  . ASN E  1 76  ? -11.977 -3.354  17.652  1.00 51.70  ? 81   ASN E CG  1 
ATOM   8526  O OD1 . ASN E  1 76  ? -11.026 -2.685  18.084  1.00 52.48  ? 81   ASN E OD1 1 
ATOM   8527  N ND2 . ASN E  1 76  ? -12.935 -2.837  16.888  1.00 44.26  ? 81   ASN E ND2 1 
ATOM   8528  N N   . VAL E  1 77  ? -9.719  -7.534  17.661  1.00 48.70  ? 82   VAL E N   1 
ATOM   8529  C CA  . VAL E  1 77  ? -9.434  -8.874  18.130  1.00 47.32  ? 82   VAL E CA  1 
ATOM   8530  C C   . VAL E  1 77  ? -8.904  -8.835  19.582  1.00 46.73  ? 82   VAL E C   1 
ATOM   8531  O O   . VAL E  1 77  ? -8.398  -7.805  20.047  1.00 44.39  ? 82   VAL E O   1 
ATOM   8532  C CB  . VAL E  1 77  ? -8.438  -9.595  17.178  1.00 43.46  ? 82   VAL E CB  1 
ATOM   8533  C CG1 . VAL E  1 77  ? -8.985  -9.582  15.740  1.00 39.65  ? 82   VAL E CG1 1 
ATOM   8534  C CG2 . VAL E  1 77  ? -7.071  -8.957  17.239  1.00 35.01  ? 82   VAL E CG2 1 
ATOM   8535  N N   . PRO E  1 78  ? -9.140  -9.922  20.335  1.00 45.73  ? 83   PRO E N   1 
ATOM   8536  C CA  . PRO E  1 78  ? -8.598  -10.125 21.687  1.00 45.32  ? 83   PRO E CA  1 
ATOM   8537  C C   . PRO E  1 78  ? -7.163  -10.666 21.669  1.00 44.91  ? 83   PRO E C   1 
ATOM   8538  O O   . PRO E  1 78  ? -6.677  -11.038 20.587  1.00 45.45  ? 83   PRO E O   1 
ATOM   8539  C CB  . PRO E  1 78  ? -9.544  -11.171 22.277  1.00 45.82  ? 83   PRO E CB  1 
ATOM   8540  C CG  . PRO E  1 78  ? -9.990  -11.976 21.061  1.00 42.73  ? 83   PRO E CG  1 
ATOM   8541  C CD  . PRO E  1 78  ? -10.086 -10.989 19.946  1.00 38.54  ? 83   PRO E CD  1 
ATOM   8542  N N   . GLU E  1 79  A -6.530  -10.728 22.840  1.00 37.60  ? 83   GLU E N   1 
ATOM   8543  C CA  . GLU E  1 79  A -5.199  -11.304 23.016  1.00 36.94  ? 83   GLU E CA  1 
ATOM   8544  C C   . GLU E  1 79  A -5.102  -12.685 22.358  1.00 41.41  ? 83   GLU E C   1 
ATOM   8545  O O   . GLU E  1 79  A -6.071  -13.451 22.402  1.00 47.23  ? 83   GLU E O   1 
ATOM   8546  C CB  . GLU E  1 79  A -4.863  -11.405 24.502  1.00 35.88  ? 83   GLU E CB  1 
ATOM   8547  C CG  . GLU E  1 79  A -3.537  -12.101 24.791  1.00 36.46  ? 83   GLU E CG  1 
ATOM   8548  C CD  . GLU E  1 79  A -3.182  -12.200 26.287  1.00 44.48  ? 83   GLU E CD  1 
ATOM   8549  O OE1 . GLU E  1 79  A -3.850  -11.573 27.156  1.00 44.14  ? 83   GLU E OE1 1 
ATOM   8550  O OE2 . GLU E  1 79  A -2.256  -12.983 26.588  1.00 39.90  ? 83   GLU E OE2 1 
ATOM   8551  N N   . TRP E  1 80  ? -3.970  -12.973 21.694  1.00 42.47  ? 84   TRP E N   1 
ATOM   8552  C CA  . TRP E  1 80  ? -3.767  -14.255 20.989  1.00 43.78  ? 84   TRP E CA  1 
ATOM   8553  C C   . TRP E  1 80  ? -2.468  -14.982 21.433  1.00 41.43  ? 84   TRP E C   1 
ATOM   8554  O O   . TRP E  1 80  ? -1.565  -14.359 22.000  1.00 38.43  ? 84   TRP E O   1 
ATOM   8555  C CB  . TRP E  1 80  ? -3.754  -14.023 19.471  1.00 39.66  ? 84   TRP E CB  1 
ATOM   8556  C CG  . TRP E  1 80  ? -2.576  -13.169 18.974  1.00 42.36  ? 84   TRP E CG  1 
ATOM   8557  C CD1 . TRP E  1 80  ? -1.309  -13.603 18.683  1.00 41.75  ? 84   TRP E CD1 1 
ATOM   8558  C CD2 . TRP E  1 80  ? -2.575  -11.758 18.724  1.00 34.90  ? 84   TRP E CD2 1 
ATOM   8559  N NE1 . TRP E  1 80  ? -0.527  -12.549 18.278  1.00 34.36  ? 84   TRP E NE1 1 
ATOM   8560  C CE2 . TRP E  1 80  ? -1.280  -11.407 18.297  1.00 33.83  ? 84   TRP E CE2 1 
ATOM   8561  C CE3 . TRP E  1 80  ? -3.538  -10.754 18.841  1.00 38.99  ? 84   TRP E CE3 1 
ATOM   8562  C CZ2 . TRP E  1 80  ? -0.925  -10.092 17.980  1.00 32.91  ? 84   TRP E CZ2 1 
ATOM   8563  C CZ3 . TRP E  1 80  ? -3.180  -9.446  18.519  1.00 40.03  ? 84   TRP E CZ3 1 
ATOM   8564  C CH2 . TRP E  1 80  ? -1.887  -9.132  18.088  1.00 32.36  ? 84   TRP E CH2 1 
ATOM   8565  N N   . SER E  1 81  ? -2.362  -16.271 21.100  1.00 42.20  ? 85   SER E N   1 
ATOM   8566  C CA  . SER E  1 81  ? -1.221  -17.127 21.473  1.00 44.23  ? 85   SER E CA  1 
ATOM   8567  C C   . SER E  1 81  ? -0.284  -17.339 20.292  1.00 49.26  ? 85   SER E C   1 
ATOM   8568  O O   . SER E  1 81  ? 0.920   -17.580 20.476  1.00 50.65  ? 85   SER E O   1 
ATOM   8569  C CB  . SER E  1 81  ? -1.687  -18.491 21.974  1.00 44.98  ? 85   SER E CB  1 
ATOM   8570  O OG  . SER E  1 81  ? -2.495  -19.105 20.990  1.00 49.03  ? 85   SER E OG  1 
ATOM   8571  N N   . TYR E  1 82  ? -0.872  -17.357 19.094  1.00 45.93  ? 86   TYR E N   1 
ATOM   8572  C CA  . TYR E  1 82  ? -0.134  -17.350 17.832  1.00 39.19  ? 86   TYR E CA  1 
ATOM   8573  C C   . TYR E  1 82  ? -1.077  -16.911 16.709  1.00 39.75  ? 86   TYR E C   1 
ATOM   8574  O O   . TYR E  1 82  ? -2.254  -16.682 16.962  1.00 42.66  ? 86   TYR E O   1 
ATOM   8575  C CB  . TYR E  1 82  ? 0.500   -18.722 17.561  1.00 40.75  ? 86   TYR E CB  1 
ATOM   8576  C CG  . TYR E  1 82  ? -0.467  -19.876 17.434  1.00 45.51  ? 86   TYR E CG  1 
ATOM   8577  C CD1 . TYR E  1 82  ? -0.970  -20.508 18.575  1.00 45.90  ? 86   TYR E CD1 1 
ATOM   8578  C CD2 . TYR E  1 82  ? -0.834  -20.378 16.187  1.00 41.63  ? 86   TYR E CD2 1 
ATOM   8579  C CE1 . TYR E  1 82  ? -1.840  -21.570 18.486  1.00 42.04  ? 86   TYR E CE1 1 
ATOM   8580  C CE2 . TYR E  1 82  ? -1.704  -21.451 16.087  1.00 44.11  ? 86   TYR E CE2 1 
ATOM   8581  C CZ  . TYR E  1 82  ? -2.200  -22.045 17.248  1.00 46.32  ? 86   TYR E CZ  1 
ATOM   8582  O OH  . TYR E  1 82  ? -3.068  -23.110 17.174  1.00 48.10  ? 86   TYR E OH  1 
ATOM   8583  N N   . ILE E  1 83  ? -0.561  -16.748 15.489  1.00 37.40  ? 87   ILE E N   1 
ATOM   8584  C CA  . ILE E  1 83  ? -1.362  -16.266 14.364  1.00 34.49  ? 87   ILE E CA  1 
ATOM   8585  C C   . ILE E  1 83  ? -1.383  -17.310 13.254  1.00 39.29  ? 87   ILE E C   1 
ATOM   8586  O O   . ILE E  1 83  ? -0.342  -17.894 12.902  1.00 37.46  ? 87   ILE E O   1 
ATOM   8587  C CB  . ILE E  1 83  ? -0.828  -14.913 13.814  1.00 34.85  ? 87   ILE E CB  1 
ATOM   8588  C CG1 . ILE E  1 83  ? -0.998  -13.804 14.857  1.00 40.24  ? 87   ILE E CG1 1 
ATOM   8589  C CG2 . ILE E  1 83  ? -1.585  -14.486 12.596  1.00 34.30  ? 87   ILE E CG2 1 
ATOM   8590  C CD1 . ILE E  1 83  ? -0.492  -12.418 14.406  1.00 35.51  ? 87   ILE E CD1 1 
ATOM   8591  N N   . VAL E  1 84  ? -2.573  -17.549 12.697  1.00 40.59  ? 88   VAL E N   1 
ATOM   8592  C CA  . VAL E  1 84  ? -2.708  -18.514 11.603  1.00 40.22  ? 88   VAL E CA  1 
ATOM   8593  C C   . VAL E  1 84  ? -3.160  -17.757 10.352  1.00 41.41  ? 88   VAL E C   1 
ATOM   8594  O O   . VAL E  1 84  ? -4.147  -17.017 10.362  1.00 41.59  ? 88   VAL E O   1 
ATOM   8595  C CB  . VAL E  1 84  ? -3.707  -19.654 11.933  1.00 43.58  ? 88   VAL E CB  1 
ATOM   8596  C CG1 . VAL E  1 84  ? -3.871  -20.589 10.730  1.00 40.08  ? 88   VAL E CG1 1 
ATOM   8597  C CG2 . VAL E  1 84  ? -3.279  -20.433 13.187  1.00 35.35  ? 88   VAL E CG2 1 
ATOM   8598  N N   . GLU E  1 85  ? -2.417  -17.963 9.274   1.00 42.66  ? 89   GLU E N   1 
ATOM   8599  C CA  . GLU E  1 85  ? -2.609  -17.263 8.017   1.00 41.33  ? 89   GLU E CA  1 
ATOM   8600  C C   . GLU E  1 85  ? -2.523  -18.337 6.946   1.00 41.97  ? 89   GLU E C   1 
ATOM   8601  O O   . GLU E  1 85  ? -1.766  -19.290 7.085   1.00 48.55  ? 89   GLU E O   1 
ATOM   8602  C CB  . GLU E  1 85  ? -1.545  -16.163 7.823   1.00 41.46  ? 89   GLU E CB  1 
ATOM   8603  C CG  . GLU E  1 85  ? -1.725  -15.302 6.568   1.00 44.73  ? 89   GLU E CG  1 
ATOM   8604  C CD  . GLU E  1 85  ? -0.523  -14.407 6.236   1.00 41.81  ? 89   GLU E CD  1 
ATOM   8605  O OE1 . GLU E  1 85  ? 0.623   -14.902 6.191   1.00 43.69  ? 89   GLU E OE1 1 
ATOM   8606  O OE2 . GLU E  1 85  ? -0.733  -13.211 5.959   1.00 46.36  ? 89   GLU E OE2 1 
ATOM   8607  N N   . LYS E  1 86  ? -3.331  -18.221 5.906   1.00 44.83  ? 90   LYS E N   1 
ATOM   8608  C CA  . LYS E  1 86  ? -3.291  -19.190 4.817   1.00 50.00  ? 90   LYS E CA  1 
ATOM   8609  C C   . LYS E  1 86  ? -2.115  -18.907 3.886   1.00 51.90  ? 90   LYS E C   1 
ATOM   8610  O O   . LYS E  1 86  ? -1.528  -17.826 3.924   1.00 54.55  ? 90   LYS E O   1 
ATOM   8611  C CB  . LYS E  1 86  ? -4.605  -19.159 4.044   1.00 48.35  ? 90   LYS E CB  1 
ATOM   8612  C CG  . LYS E  1 86  ? -5.727  -19.908 4.732   1.00 52.06  ? 90   LYS E CG  1 
ATOM   8613  C CD  . LYS E  1 86  ? -7.059  -19.734 4.015   1.00 51.86  ? 90   LYS E CD  1 
ATOM   8614  C CE  . LYS E  1 86  ? -8.149  -20.626 4.613   1.00 54.69  ? 90   LYS E CE  1 
ATOM   8615  N NZ  . LYS E  1 86  ? -8.408  -20.320 6.044   1.00 62.44  ? 90   LYS E NZ  1 
ATOM   8616  N N   . ILE E  1 87  ? -1.788  -19.869 3.033   1.00 54.41  ? 91   ILE E N   1 
ATOM   8617  C CA  . ILE E  1 87  ? -0.667  -19.717 2.116   1.00 54.01  ? 91   ILE E CA  1 
ATOM   8618  C C   . ILE E  1 87  ? -0.933  -18.607 1.101   1.00 56.86  ? 91   ILE E C   1 
ATOM   8619  O O   . ILE E  1 87  ? -0.085  -17.746 0.903   1.00 63.69  ? 91   ILE E O   1 
ATOM   8620  C CB  . ILE E  1 87  ? -0.360  -21.034 1.385   1.00 48.41  ? 91   ILE E CB  1 
ATOM   8621  C CG1 . ILE E  1 87  ? 0.116   -22.083 2.395   1.00 51.91  ? 91   ILE E CG1 1 
ATOM   8622  C CG2 . ILE E  1 87  ? 0.719   -20.830 0.382   1.00 44.90  ? 91   ILE E CG2 1 
ATOM   8623  C CD1 . ILE E  1 87  ? 0.661   -23.380 1.771   1.00 50.74  ? 91   ILE E CD1 1 
ATOM   8624  N N   . ASN E  1 88  ? -2.123  -18.586 0.509   1.00 53.64  ? 92   ASN E N   1 
ATOM   8625  C CA  . ASN E  1 88  ? -2.465  -17.579 -0.502  1.00 55.97  ? 92   ASN E CA  1 
ATOM   8626  C C   . ASN E  1 88  ? -3.813  -16.930 -0.176  1.00 57.66  ? 92   ASN E C   1 
ATOM   8627  O O   . ASN E  1 88  ? -4.804  -17.170 -0.875  1.00 59.78  ? 92   ASN E O   1 
ATOM   8628  C CB  . ASN E  1 88  ? -2.480  -18.228 -1.905  1.00 61.33  ? 92   ASN E CB  1 
ATOM   8629  C CG  . ASN E  1 88  ? -2.591  -17.209 -3.053  1.00 68.16  ? 92   ASN E CG  1 
ATOM   8630  O OD1 . ASN E  1 88  ? -2.188  -16.055 -2.925  1.00 71.83  ? 92   ASN E OD1 1 
ATOM   8631  N ND2 . ASN E  1 88  ? -3.110  -17.661 -4.198  1.00 72.36  ? 92   ASN E ND2 1 
ATOM   8632  N N   . PRO E  1 89  ? -3.843  -16.075 0.869   1.00 59.56  ? 93   PRO E N   1 
ATOM   8633  C CA  . PRO E  1 89  ? -5.082  -15.478 1.404   1.00 54.33  ? 93   PRO E CA  1 
ATOM   8634  C C   . PRO E  1 89  ? -5.876  -14.740 0.324   1.00 52.80  ? 93   PRO E C   1 
ATOM   8635  O O   . PRO E  1 89  ? -5.239  -14.238 -0.585  1.00 59.42  ? 93   PRO E O   1 
ATOM   8636  C CB  . PRO E  1 89  ? -4.562  -14.494 2.466   1.00 50.26  ? 93   PRO E CB  1 
ATOM   8637  C CG  . PRO E  1 89  ? -3.197  -15.011 2.837   1.00 53.59  ? 93   PRO E CG  1 
ATOM   8638  C CD  . PRO E  1 89  ? -2.643  -15.554 1.556   1.00 57.10  ? 93   PRO E CD  1 
ATOM   8639  N N   . ALA E  1 90  ? -7.207  -14.679 0.397   1.00 47.34  ? 94   ALA E N   1 
ATOM   8640  C CA  . ALA E  1 90  ? -7.971  -14.070 -0.688  1.00 45.80  ? 94   ALA E CA  1 
ATOM   8641  C C   . ALA E  1 90  ? -8.167  -12.584 -0.485  1.00 53.48  ? 94   ALA E C   1 
ATOM   8642  O O   . ALA E  1 90  ? -8.104  -11.796 -1.429  1.00 56.39  ? 94   ALA E O   1 
ATOM   8643  C CB  . ALA E  1 90  ? -9.319  -14.743 -0.831  1.00 48.99  ? 94   ALA E CB  1 
ATOM   8644  N N   . ASN E  1 91  ? -8.369  -12.186 0.758   1.00 48.16  ? 95   ASN E N   1 
ATOM   8645  C CA  . ASN E  1 91  ? -8.624  -10.789 1.038   1.00 50.38  ? 95   ASN E CA  1 
ATOM   8646  C C   . ASN E  1 91  ? -7.389  -10.086 1.552   1.00 53.13  ? 95   ASN E C   1 
ATOM   8647  O O   . ASN E  1 91  ? -7.104  -10.133 2.752   1.00 52.94  ? 95   ASN E O   1 
ATOM   8648  C CB  . ASN E  1 91  ? -9.766  -10.672 2.037   1.00 52.16  ? 95   ASN E CB  1 
ATOM   8649  C CG  . ASN E  1 91  ? -11.058 -11.249 1.500   1.00 55.02  ? 95   ASN E CG  1 
ATOM   8650  O OD1 . ASN E  1 91  ? -11.413 -11.019 0.343   1.00 55.33  ? 95   ASN E OD1 1 
ATOM   8651  N ND2 . ASN E  1 91  ? -11.755 -12.024 2.325   1.00 58.95  ? 95   ASN E ND2 1 
ATOM   8652  N N   . ASP E  1 92  ? -6.662  -9.446  0.634   1.00 44.91  ? 96   ASP E N   1 
ATOM   8653  C CA  . ASP E  1 92  ? -5.383  -8.817  0.940   1.00 44.82  ? 96   ASP E CA  1 
ATOM   8654  C C   . ASP E  1 92  ? -5.480  -7.319  0.650   1.00 47.42  ? 96   ASP E C   1 
ATOM   8655  O O   . ASP E  1 92  ? -6.362  -6.615  1.172   1.00 42.79  ? 96   ASP E O   1 
ATOM   8656  C CB  . ASP E  1 92  ? -4.255  -9.477  0.123   1.00 46.98  ? 96   ASP E CB  1 
ATOM   8657  C CG  . ASP E  1 92  ? -2.843  -9.005  0.530   1.00 51.47  ? 96   ASP E CG  1 
ATOM   8658  O OD1 . ASP E  1 92  ? -2.521  -8.957  1.736   1.00 56.50  ? 96   ASP E OD1 1 
ATOM   8659  O OD2 . ASP E  1 92  ? -2.041  -8.672  -0.369  1.00 57.51  ? 96   ASP E OD2 1 
ATOM   8660  N N   . LEU E  1 93  A -4.601  -6.834  -0.214  1.00 45.49  ? 96   LEU E N   1 
ATOM   8661  C CA  . LEU E  1 93  A -4.729  -5.478  -0.701  1.00 47.46  ? 96   LEU E CA  1 
ATOM   8662  C C   . LEU E  1 93  A -5.814  -5.479  -1.795  1.00 50.93  ? 96   LEU E C   1 
ATOM   8663  O O   . LEU E  1 93  A -5.598  -6.004  -2.893  1.00 49.14  ? 96   LEU E O   1 
ATOM   8664  C CB  . LEU E  1 93  A -3.383  -4.997  -1.231  1.00 44.41  ? 96   LEU E CB  1 
ATOM   8665  C CG  . LEU E  1 93  A -2.267  -5.057  -0.192  1.00 39.13  ? 96   LEU E CG  1 
ATOM   8666  C CD1 . LEU E  1 93  A -0.902  -4.837  -0.838  1.00 43.49  ? 96   LEU E CD1 1 
ATOM   8667  C CD2 . LEU E  1 93  A -2.523  -3.996  0.840   1.00 33.76  ? 96   LEU E CD2 1 
ATOM   8668  N N   . CYS E  1 94  ? -6.997  -4.946  -1.483  1.00 51.57  ? 97   CYS E N   1 
ATOM   8669  C CA  . CYS E  1 94  ? -8.108  -4.987  -2.446  1.00 56.72  ? 97   CYS E CA  1 
ATOM   8670  C C   . CYS E  1 94  ? -7.848  -4.008  -3.605  1.00 51.14  ? 97   CYS E C   1 
ATOM   8671  O O   . CYS E  1 94  ? -8.037  -4.344  -4.765  1.00 50.56  ? 97   CYS E O   1 
ATOM   8672  C CB  . CYS E  1 94  ? -9.461  -4.707  -1.759  1.00 50.72  ? 97   CYS E CB  1 
ATOM   8673  S SG  . CYS E  1 94  ? -9.559  -3.232  -0.647  1.00 60.89  ? 97   CYS E SG  1 
ATOM   8674  N N   . TYR E  1 95  ? -7.367  -2.818  -3.277  1.00 49.89  ? 98   TYR E N   1 
ATOM   8675  C CA  . TYR E  1 95  ? -6.843  -1.899  -4.273  1.00 50.99  ? 98   TYR E CA  1 
ATOM   8676  C C   . TYR E  1 95  ? -5.394  -2.290  -4.555  1.00 51.09  ? 98   TYR E C   1 
ATOM   8677  O O   . TYR E  1 95  ? -4.595  -2.384  -3.618  1.00 53.60  ? 98   TYR E O   1 
ATOM   8678  C CB  . TYR E  1 95  ? -6.897  -0.454  -3.773  1.00 48.33  ? 98   TYR E CB  1 
ATOM   8679  C CG  . TYR E  1 95  ? -6.836  0.585   -4.863  1.00 51.73  ? 98   TYR E CG  1 
ATOM   8680  C CD1 . TYR E  1 95  ? -5.705  0.741   -5.638  1.00 48.19  ? 98   TYR E CD1 1 
ATOM   8681  C CD2 . TYR E  1 95  ? -7.895  1.449   -5.072  1.00 56.06  ? 98   TYR E CD2 1 
ATOM   8682  C CE1 . TYR E  1 95  ? -5.645  1.698   -6.624  1.00 52.82  ? 98   TYR E CE1 1 
ATOM   8683  C CE2 . TYR E  1 95  ? -7.845  2.423   -6.050  1.00 57.82  ? 98   TYR E CE2 1 
ATOM   8684  C CZ  . TYR E  1 95  ? -6.715  2.546   -6.829  1.00 56.30  ? 98   TYR E CZ  1 
ATOM   8685  O OH  . TYR E  1 95  ? -6.657  3.525   -7.805  1.00 49.43  ? 98   TYR E OH  1 
ATOM   8686  N N   . PRO E  1 96  ? -5.041  -2.487  -5.838  1.00 46.03  ? 99   PRO E N   1 
ATOM   8687  C CA  . PRO E  1 96  ? -3.716  -2.984  -6.198  1.00 40.60  ? 99   PRO E CA  1 
ATOM   8688  C C   . PRO E  1 96  ? -2.556  -2.085  -5.729  1.00 42.18  ? 99   PRO E C   1 
ATOM   8689  O O   . PRO E  1 96  ? -2.676  -0.837  -5.646  1.00 44.69  ? 99   PRO E O   1 
ATOM   8690  C CB  . PRO E  1 96  ? -3.784  -3.025  -7.737  1.00 49.15  ? 99   PRO E CB  1 
ATOM   8691  C CG  . PRO E  1 96  ? -5.223  -3.156  -8.053  1.00 42.47  ? 99   PRO E CG  1 
ATOM   8692  C CD  . PRO E  1 96  ? -5.874  -2.279  -7.039  1.00 46.82  ? 99   PRO E CD  1 
ATOM   8693  N N   . GLY E  1 97  ? -1.438  -2.725  -5.401  1.00 35.47  ? 100  GLY E N   1 
ATOM   8694  C CA  . GLY E  1 97  ? -0.265  -1.993  -4.953  1.00 38.12  ? 100  GLY E CA  1 
ATOM   8695  C C   . GLY E  1 97  ? 0.692   -2.823  -4.114  1.00 37.43  ? 100  GLY E C   1 
ATOM   8696  O O   . GLY E  1 97  ? 0.808   -4.034  -4.313  1.00 35.29  ? 100  GLY E O   1 
ATOM   8697  N N   . ASN E  1 98  ? 1.373   -2.180  -3.166  1.00 39.67  ? 101  ASN E N   1 
ATOM   8698  C CA  . ASN E  1 98  ? 2.336   -2.893  -2.330  1.00 39.83  ? 101  ASN E CA  1 
ATOM   8699  C C   . ASN E  1 98  ? 2.478   -2.334  -0.896  1.00 38.83  ? 101  ASN E C   1 
ATOM   8700  O O   . ASN E  1 98  ? 2.161   -1.158  -0.607  1.00 31.62  ? 101  ASN E O   1 
ATOM   8701  C CB  . ASN E  1 98  ? 3.702   -2.886  -3.026  1.00 37.71  ? 101  ASN E CB  1 
ATOM   8702  C CG  . ASN E  1 98  ? 4.334   -1.497  -3.066  1.00 41.83  ? 101  ASN E CG  1 
ATOM   8703  O OD1 . ASN E  1 98  ? 3.806   -0.573  -3.696  1.00 46.53  ? 101  ASN E OD1 1 
ATOM   8704  N ND2 . ASN E  1 98  ? 5.494   -1.355  -2.417  1.00 40.65  ? 101  ASN E ND2 1 
ATOM   8705  N N   . PHE E  1 99  ? 3.014   -3.185  -0.025  1.00 35.64  ? 102  PHE E N   1 
ATOM   8706  C CA  . PHE E  1 99  ? 3.185   -2.877  1.387   1.00 31.02  ? 102  PHE E CA  1 
ATOM   8707  C C   . PHE E  1 99  ? 4.674   -2.838  1.749   1.00 32.76  ? 102  PHE E C   1 
ATOM   8708  O O   . PHE E  1 99  ? 5.350   -3.866  1.820   1.00 32.57  ? 102  PHE E O   1 
ATOM   8709  C CB  . PHE E  1 99  ? 2.460   -3.924  2.217   1.00 37.68  ? 102  PHE E CB  1 
ATOM   8710  C CG  . PHE E  1 99  ? 2.114   -3.486  3.630   1.00 41.82  ? 102  PHE E CG  1 
ATOM   8711  C CD1 . PHE E  1 99  ? 3.102   -3.295  4.585   1.00 39.48  ? 102  PHE E CD1 1 
ATOM   8712  C CD2 . PHE E  1 99  ? 0.790   -3.342  4.011   1.00 37.38  ? 102  PHE E CD2 1 
ATOM   8713  C CE1 . PHE E  1 99  ? 2.781   -2.927  5.881   1.00 41.17  ? 102  PHE E CE1 1 
ATOM   8714  C CE2 . PHE E  1 99  ? 0.464   -2.984  5.303   1.00 42.22  ? 102  PHE E CE2 1 
ATOM   8715  C CZ  . PHE E  1 99  ? 1.462   -2.764  6.238   1.00 43.97  ? 102  PHE E CZ  1 
ATOM   8716  N N   . ASN E  1 100 ? 5.179   -1.638  1.979   1.00 32.18  ? 103  ASN E N   1 
ATOM   8717  C CA  . ASN E  1 100 ? 6.593   -1.407  2.261   1.00 31.31  ? 103  ASN E CA  1 
ATOM   8718  C C   . ASN E  1 100 ? 7.174   -2.076  3.529   1.00 34.45  ? 103  ASN E C   1 
ATOM   8719  O O   . ASN E  1 100 ? 6.566   -2.031  4.594   1.00 32.85  ? 103  ASN E O   1 
ATOM   8720  C CB  . ASN E  1 100 ? 6.800   0.086   2.351   1.00 30.25  ? 103  ASN E CB  1 
ATOM   8721  C CG  . ASN E  1 100 ? 8.099   0.504   1.791   1.00 40.36  ? 103  ASN E CG  1 
ATOM   8722  O OD1 . ASN E  1 100 ? 8.279   0.534   0.547   1.00 42.75  ? 103  ASN E OD1 1 
ATOM   8723  N ND2 . ASN E  1 100 ? 9.033   0.863   2.679   1.00 35.11  ? 103  ASN E ND2 1 
ATOM   8724  N N   . ASP E  1 101 ? 8.338   -2.718  3.380   1.00 35.26  ? 104  ASP E N   1 
ATOM   8725  C CA  . ASP E  1 101 ? 9.024   -3.417  4.466   1.00 29.38  ? 104  ASP E CA  1 
ATOM   8726  C C   . ASP E  1 101 ? 8.113   -4.390  5.167   1.00 28.72  ? 104  ASP E C   1 
ATOM   8727  O O   . ASP E  1 101 ? 8.217   -4.573  6.393   1.00 26.30  ? 104  ASP E O   1 
ATOM   8728  C CB  . ASP E  1 101 ? 9.623   -2.429  5.484   1.00 29.04  ? 104  ASP E CB  1 
ATOM   8729  C CG  . ASP E  1 101 ? 10.983  -1.893  5.051   1.00 29.11  ? 104  ASP E CG  1 
ATOM   8730  O OD1 . ASP E  1 101 ? 11.786  -2.664  4.476   1.00 34.57  ? 104  ASP E OD1 1 
ATOM   8731  O OD2 . ASP E  1 101 ? 11.254  -0.707  5.266   1.00 31.90  ? 104  ASP E OD2 1 
ATOM   8732  N N   . TYR E  1 102 ? 7.259   -5.038  4.380   1.00 26.73  ? 105  TYR E N   1 
ATOM   8733  C CA  . TYR E  1 102 ? 6.264   -5.951  4.916   1.00 27.30  ? 105  TYR E CA  1 
ATOM   8734  C C   . TYR E  1 102 ? 6.873   -7.080  5.758   1.00 29.74  ? 105  TYR E C   1 
ATOM   8735  O O   . TYR E  1 102 ? 6.374   -7.351  6.859   1.00 32.26  ? 105  TYR E O   1 
ATOM   8736  C CB  . TYR E  1 102 ? 5.449   -6.522  3.754   1.00 28.21  ? 105  TYR E CB  1 
ATOM   8737  C CG  . TYR E  1 102 ? 4.192   -7.319  4.087   1.00 36.47  ? 105  TYR E CG  1 
ATOM   8738  C CD1 . TYR E  1 102 ? 3.227   -6.835  4.964   1.00 35.91  ? 105  TYR E CD1 1 
ATOM   8739  C CD2 . TYR E  1 102 ? 3.952   -8.549  3.471   1.00 34.83  ? 105  TYR E CD2 1 
ATOM   8740  C CE1 . TYR E  1 102 ? 2.076   -7.579  5.233   1.00 30.51  ? 105  TYR E CE1 1 
ATOM   8741  C CE2 . TYR E  1 102 ? 2.816   -9.277  3.730   1.00 33.31  ? 105  TYR E CE2 1 
ATOM   8742  C CZ  . TYR E  1 102 ? 1.885   -8.794  4.608   1.00 33.52  ? 105  TYR E CZ  1 
ATOM   8743  O OH  . TYR E  1 102 ? 0.755   -9.548  4.851   1.00 36.20  ? 105  TYR E OH  1 
ATOM   8744  N N   . GLU E  1 103 ? 7.955   -7.706  5.283   1.00 28.29  ? 106  GLU E N   1 
ATOM   8745  C CA  . GLU E  1 103 ? 8.532   -8.889  5.950   1.00 27.31  ? 106  GLU E CA  1 
ATOM   8746  C C   . GLU E  1 103 ? 9.218   -8.493  7.275   1.00 31.14  ? 106  GLU E C   1 
ATOM   8747  O O   . GLU E  1 103 ? 9.308   -9.309  8.203   1.00 27.63  ? 106  GLU E O   1 
ATOM   8748  C CB  . GLU E  1 103 ? 9.518   -9.625  5.037   1.00 22.57  ? 106  GLU E CB  1 
ATOM   8749  C CG  . GLU E  1 103 ? 8.861   -10.394 3.886   1.00 25.49  ? 106  GLU E CG  1 
ATOM   8750  C CD  . GLU E  1 103 ? 8.419   -9.471  2.737   1.00 30.68  ? 106  GLU E CD  1 
ATOM   8751  O OE1 . GLU E  1 103 ? 9.071   -8.404  2.548   1.00 28.89  ? 106  GLU E OE1 1 
ATOM   8752  O OE2 . GLU E  1 103 ? 7.432   -9.805  2.025   1.00 29.42  ? 106  GLU E OE2 1 
ATOM   8753  N N   . GLU E  1 104 ? 9.739   -7.265  7.349   1.00 27.90  ? 107  GLU E N   1 
ATOM   8754  C CA  . GLU E  1 104 ? 10.269  -6.752  8.616   1.00 25.64  ? 107  GLU E CA  1 
ATOM   8755  C C   . GLU E  1 104 ? 9.149   -6.516  9.643   1.00 30.04  ? 107  GLU E C   1 
ATOM   8756  O O   . GLU E  1 104 ? 9.345   -6.769  10.858  1.00 27.53  ? 107  GLU E O   1 
ATOM   8757  C CB  . GLU E  1 104 ? 11.059  -5.431  8.417   1.00 22.24  ? 107  GLU E CB  1 
ATOM   8758  C CG  . GLU E  1 104 ? 12.472  -5.636  7.914   1.00 25.90  ? 107  GLU E CG  1 
ATOM   8759  C CD  . GLU E  1 104 ? 13.371  -6.319  8.956   1.00 29.74  ? 107  GLU E CD  1 
ATOM   8760  O OE1 . GLU E  1 104 ? 13.438  -5.830  10.113  1.00 29.25  ? 107  GLU E OE1 1 
ATOM   8761  O OE2 . GLU E  1 104 ? 13.972  -7.369  8.618   1.00 26.20  ? 107  GLU E OE2 1 
ATOM   8762  N N   . LEU E  1 105 ? 7.993   -6.032  9.155   1.00 29.69  ? 108  LEU E N   1 
ATOM   8763  C CA  . LEU E  1 105 ? 6.808   -5.840  9.997   1.00 27.05  ? 108  LEU E CA  1 
ATOM   8764  C C   . LEU E  1 105 ? 6.271   -7.171  10.500  1.00 28.79  ? 108  LEU E C   1 
ATOM   8765  O O   . LEU E  1 105 ? 5.956   -7.303  11.691  1.00 23.40  ? 108  LEU E O   1 
ATOM   8766  C CB  . LEU E  1 105 ? 5.692   -5.096  9.241   1.00 24.96  ? 108  LEU E CB  1 
ATOM   8767  C CG  . LEU E  1 105 ? 4.309   -5.062  9.938   1.00 27.45  ? 108  LEU E CG  1 
ATOM   8768  C CD1 . LEU E  1 105 ? 4.286   -4.301  11.286  1.00 22.41  ? 108  LEU E CD1 1 
ATOM   8769  C CD2 . LEU E  1 105 ? 3.197   -4.533  9.001   1.00 29.26  ? 108  LEU E CD2 1 
ATOM   8770  N N   . LYS E  1 106 ? 6.227   -8.167  9.608   1.00 28.29  ? 109  LYS E N   1 
ATOM   8771  C CA  . LYS E  1 106 ? 5.743   -9.467  9.995   1.00 26.16  ? 109  LYS E CA  1 
ATOM   8772  C C   . LYS E  1 106 ? 6.674   -10.022 11.068  1.00 28.09  ? 109  LYS E C   1 
ATOM   8773  O O   . LYS E  1 106 ? 6.220   -10.664 12.003  1.00 32.24  ? 109  LYS E O   1 
ATOM   8774  C CB  . LYS E  1 106 ? 5.681   -10.414 8.797   1.00 32.89  ? 109  LYS E CB  1 
ATOM   8775  C CG  . LYS E  1 106 ? 4.421   -10.376 7.957   1.00 33.46  ? 109  LYS E CG  1 
ATOM   8776  C CD  . LYS E  1 106 ? 4.692   -11.104 6.651   1.00 35.14  ? 109  LYS E CD  1 
ATOM   8777  C CE  . LYS E  1 106 ? 3.443   -11.675 6.036   1.00 40.39  ? 109  LYS E CE  1 
ATOM   8778  N NZ  . LYS E  1 106 ? 3.035   -12.927 6.721   1.00 47.70  ? 109  LYS E NZ  1 
ATOM   8779  N N   . HIS E  1 107 ? 7.969   -9.741  10.965  1.00 26.21  ? 110  HIS E N   1 
ATOM   8780  C CA  . HIS E  1 107 ? 8.913   -10.243 11.962  1.00 29.24  ? 110  HIS E CA  1 
ATOM   8781  C C   . HIS E  1 107 ? 8.671   -9.573  13.321  1.00 32.04  ? 110  HIS E C   1 
ATOM   8782  O O   . HIS E  1 107 ? 8.733   -10.235 14.362  1.00 33.46  ? 110  HIS E O   1 
ATOM   8783  C CB  . HIS E  1 107 ? 10.357  -10.002 11.520  1.00 27.81  ? 110  HIS E CB  1 
ATOM   8784  C CG  . HIS E  1 107 ? 11.383  -10.476 12.507  1.00 32.16  ? 110  HIS E CG  1 
ATOM   8785  N ND1 . HIS E  1 107 ? 11.929  -11.743 12.461  1.00 31.07  ? 110  HIS E ND1 1 
ATOM   8786  C CD2 . HIS E  1 107 ? 11.960  -9.853  13.565  1.00 31.00  ? 110  HIS E CD2 1 
ATOM   8787  C CE1 . HIS E  1 107 ? 12.799  -11.876 13.448  1.00 34.11  ? 110  HIS E CE1 1 
ATOM   8788  N NE2 . HIS E  1 107 ? 12.833  -10.747 14.135  1.00 30.23  ? 110  HIS E NE2 1 
ATOM   8789  N N   . LEU E  1 108 ? 8.373   -8.272  13.288  1.00 27.18  ? 111  LEU E N   1 
ATOM   8790  C CA  . LEU E  1 108 ? 8.022   -7.478  14.477  1.00 29.15  ? 111  LEU E CA  1 
ATOM   8791  C C   . LEU E  1 108 ? 6.810   -8.043  15.228  1.00 34.30  ? 111  LEU E C   1 
ATOM   8792  O O   . LEU E  1 108 ? 6.760   -8.059  16.466  1.00 34.94  ? 111  LEU E O   1 
ATOM   8793  C CB  . LEU E  1 108 ? 7.724   -6.040  14.044  1.00 27.93  ? 111  LEU E CB  1 
ATOM   8794  C CG  . LEU E  1 108 ? 7.708   -4.909  15.053  1.00 31.83  ? 111  LEU E CG  1 
ATOM   8795  C CD1 . LEU E  1 108 ? 9.051   -4.913  15.706  1.00 40.05  ? 111  LEU E CD1 1 
ATOM   8796  C CD2 . LEU E  1 108 ? 7.490   -3.586  14.342  1.00 22.23  ? 111  LEU E CD2 1 
ATOM   8797  N N   . LEU E  1 109 ? 5.850   -8.526  14.446  1.00 33.95  ? 112  LEU E N   1 
ATOM   8798  C CA  . LEU E  1 109 ? 4.587   -9.070  14.930  1.00 35.24  ? 112  LEU E CA  1 
ATOM   8799  C C   . LEU E  1 109 ? 4.806   -10.383 15.712  1.00 37.28  ? 112  LEU E C   1 
ATOM   8800  O O   . LEU E  1 109 ? 3.949   -10.827 16.469  1.00 39.74  ? 112  LEU E O   1 
ATOM   8801  C CB  . LEU E  1 109 ? 3.621   -9.283  13.743  1.00 33.08  ? 112  LEU E CB  1 
ATOM   8802  C CG  . LEU E  1 109 ? 2.098   -9.412  13.915  1.00 34.64  ? 112  LEU E CG  1 
ATOM   8803  C CD1 . LEU E  1 109 ? 1.513   -8.284  14.783  1.00 34.10  ? 112  LEU E CD1 1 
ATOM   8804  C CD2 . LEU E  1 109 ? 1.354   -9.493  12.563  1.00 33.30  ? 112  LEU E CD2 1 
ATOM   8805  N N   . SER E  1 110 ? 5.953   -11.017 15.551  1.00 38.64  ? 113  SER E N   1 
ATOM   8806  C CA  . SER E  1 110 ? 6.139   -12.281 16.250  1.00 42.75  ? 113  SER E CA  1 
ATOM   8807  C C   . SER E  1 110 ? 6.687   -12.023 17.639  1.00 38.27  ? 113  SER E C   1 
ATOM   8808  O O   . SER E  1 110 ? 7.140   -12.946 18.321  1.00 43.22  ? 113  SER E O   1 
ATOM   8809  C CB  . SER E  1 110 ? 7.091   -13.202 15.477  1.00 44.64  ? 113  SER E CB  1 
ATOM   8810  O OG  . SER E  1 110 ? 8.439   -12.800 15.692  1.00 45.50  ? 113  SER E OG  1 
ATOM   8811  N N   . ARG E  1 111 ? 6.655   -10.767 18.062  1.00 35.69  ? 114  ARG E N   1 
ATOM   8812  C CA  . ARG E  1 111 ? 7.020   -10.446 19.436  1.00 42.46  ? 114  ARG E CA  1 
ATOM   8813  C C   . ARG E  1 111 ? 5.850   -9.778  20.151  1.00 38.03  ? 114  ARG E C   1 
ATOM   8814  O O   . ARG E  1 111 ? 6.046   -9.125  21.165  1.00 38.84  ? 114  ARG E O   1 
ATOM   8815  C CB  . ARG E  1 111 ? 8.258   -9.550  19.485  1.00 46.28  ? 114  ARG E CB  1 
ATOM   8816  C CG  . ARG E  1 111 ? 9.382   -10.088 18.636  1.00 48.15  ? 114  ARG E CG  1 
ATOM   8817  C CD  . ARG E  1 111 ? 9.889   -11.411 19.179  1.00 61.50  ? 114  ARG E CD  1 
ATOM   8818  N NE  . ARG E  1 111 ? 10.885  -11.980 18.267  1.00 74.47  ? 114  ARG E NE  1 
ATOM   8819  C CZ  . ARG E  1 111 ? 12.209  -11.854 18.374  1.00 76.98  ? 114  ARG E CZ  1 
ATOM   8820  N NH1 . ARG E  1 111 ? 12.764  -11.225 19.415  1.00 73.47  ? 114  ARG E NH1 1 
ATOM   8821  N NH2 . ARG E  1 111 ? 12.984  -12.411 17.448  1.00 64.81  ? 114  ARG E NH2 1 
ATOM   8822  N N   . ILE E  1 112 ? 4.656   -9.908  19.567  1.00 39.81  ? 115  ILE E N   1 
ATOM   8823  C CA  . ILE E  1 112 ? 3.424   -9.248  20.026  1.00 39.33  ? 115  ILE E CA  1 
ATOM   8824  C C   . ILE E  1 112 ? 2.259   -10.256 20.234  1.00 40.13  ? 115  ILE E C   1 
ATOM   8825  O O   . ILE E  1 112 ? 2.050   -11.143 19.393  1.00 37.96  ? 115  ILE E O   1 
ATOM   8826  C CB  . ILE E  1 112 ? 2.996   -8.165  19.015  1.00 34.06  ? 115  ILE E CB  1 
ATOM   8827  C CG1 . ILE E  1 112 ? 4.030   -7.041  18.981  1.00 35.44  ? 115  ILE E CG1 1 
ATOM   8828  C CG2 . ILE E  1 112 ? 1.616   -7.622  19.346  1.00 31.88  ? 115  ILE E CG2 1 
ATOM   8829  C CD1 . ILE E  1 112 ? 3.761   -5.953  17.919  1.00 26.32  ? 115  ILE E CD1 1 
ATOM   8830  N N   . ASN E  1 113 ? 1.517   -10.111 21.342  1.00 37.90  ? 116  ASN E N   1 
ATOM   8831  C CA  . ASN E  1 113 ? 0.359   -10.975 21.678  1.00 39.31  ? 116  ASN E CA  1 
ATOM   8832  C C   . ASN E  1 113 ? -0.998  -10.243 21.671  1.00 34.88  ? 116  ASN E C   1 
ATOM   8833  O O   . ASN E  1 113 ? -2.039  -10.886 21.597  1.00 33.36  ? 116  ASN E O   1 
ATOM   8834  C CB  . ASN E  1 113 ? 0.535   -11.606 23.080  1.00 43.65  ? 116  ASN E CB  1 
ATOM   8835  C CG  . ASN E  1 113 ? 1.692   -12.591 23.163  1.00 39.58  ? 116  ASN E CG  1 
ATOM   8836  O OD1 . ASN E  1 113 ? 2.653   -12.344 23.892  1.00 45.12  ? 116  ASN E OD1 1 
ATOM   8837  N ND2 . ASN E  1 113 ? 1.577   -13.724 22.488  1.00 36.63  ? 116  ASN E ND2 1 
ATOM   8838  N N   . HIS E  1 114 ? -0.984  -8.913  21.776  1.00 31.48  ? 117  HIS E N   1 
ATOM   8839  C CA  . HIS E  1 114 ? -2.225  -8.145  21.835  1.00 31.27  ? 117  HIS E CA  1 
ATOM   8840  C C   . HIS E  1 114 ? -2.128  -6.677  21.379  1.00 32.10  ? 117  HIS E C   1 
ATOM   8841  O O   . HIS E  1 114 ? -1.266  -5.906  21.839  1.00 31.45  ? 117  HIS E O   1 
ATOM   8842  C CB  . HIS E  1 114 ? -2.777  -8.152  23.261  1.00 40.05  ? 117  HIS E CB  1 
ATOM   8843  C CG  . HIS E  1 114 ? -4.208  -7.715  23.349  1.00 42.13  ? 117  HIS E CG  1 
ATOM   8844  N ND1 . HIS E  1 114 ? -4.708  -7.008  24.423  1.00 39.41  ? 117  HIS E ND1 1 
ATOM   8845  C CD2 . HIS E  1 114 ? -5.251  -7.916  22.505  1.00 42.55  ? 117  HIS E CD2 1 
ATOM   8846  C CE1 . HIS E  1 114 ? -5.992  -6.768  24.219  1.00 43.03  ? 117  HIS E CE1 1 
ATOM   8847  N NE2 . HIS E  1 114 ? -6.345  -7.307  23.065  1.00 40.75  ? 117  HIS E NE2 1 
ATOM   8848  N N   . PHE E  1 115 ? -3.040  -6.313  20.478  1.00 35.44  ? 118  PHE E N   1 
ATOM   8849  C CA  . PHE E  1 115 ? -3.237  -4.937  20.004  1.00 38.32  ? 118  PHE E CA  1 
ATOM   8850  C C   . PHE E  1 115 ? -4.492  -4.327  20.603  1.00 36.71  ? 118  PHE E C   1 
ATOM   8851  O O   . PHE E  1 115 ? -5.462  -5.047  20.872  1.00 48.08  ? 118  PHE E O   1 
ATOM   8852  C CB  . PHE E  1 115 ? -3.361  -4.901  18.475  1.00 37.64  ? 118  PHE E CB  1 
ATOM   8853  C CG  . PHE E  1 115 ? -2.054  -4.876  17.746  1.00 34.76  ? 118  PHE E CG  1 
ATOM   8854  C CD1 . PHE E  1 115 ? -1.012  -4.053  18.183  1.00 36.41  ? 118  PHE E CD1 1 
ATOM   8855  C CD2 . PHE E  1 115 ? -1.877  -5.638  16.596  1.00 35.30  ? 118  PHE E CD2 1 
ATOM   8856  C CE1 . PHE E  1 115 ? 0.196   -4.012  17.503  1.00 31.56  ? 118  PHE E CE1 1 
ATOM   8857  C CE2 . PHE E  1 115 ? -0.685  -5.593  15.899  1.00 32.32  ? 118  PHE E CE2 1 
ATOM   8858  C CZ  . PHE E  1 115 ? 0.355   -4.781  16.360  1.00 32.30  ? 118  PHE E CZ  1 
ATOM   8859  N N   . GLU E  1 116 ? -4.513  -3.007  20.736  1.00 36.41  ? 119  GLU E N   1 
ATOM   8860  C CA  . GLU E  1 116 ? -5.751  -2.289  21.085  1.00 44.97  ? 119  GLU E CA  1 
ATOM   8861  C C   . GLU E  1 116 ? -5.981  -1.149  20.095  1.00 44.50  ? 119  GLU E C   1 
ATOM   8862  O O   . GLU E  1 116 ? -5.203  -0.189  20.082  1.00 42.13  ? 119  GLU E O   1 
ATOM   8863  C CB  . GLU E  1 116 ? -5.721  -1.693  22.501  1.00 46.15  ? 119  GLU E CB  1 
ATOM   8864  C CG  . GLU E  1 116 ? -7.066  -0.993  22.830  1.00 59.18  ? 119  GLU E CG  1 
ATOM   8865  C CD  . GLU E  1 116 ? -7.153  -0.316  24.206  1.00 65.76  ? 119  GLU E CD  1 
ATOM   8866  O OE1 . GLU E  1 116 ? -6.892  -0.993  25.236  1.00 68.04  ? 119  GLU E OE1 1 
ATOM   8867  O OE2 . GLU E  1 116 ? -7.526  0.894   24.233  1.00 53.02  ? 119  GLU E OE2 1 
ATOM   8868  N N   . LYS E  1 117 ? -7.006  -1.256  19.242  1.00 37.88  ? 120  LYS E N   1 
ATOM   8869  C CA  . LYS E  1 117 ? -7.183  -0.227  18.200  1.00 44.34  ? 120  LYS E CA  1 
ATOM   8870  C C   . LYS E  1 117 ? -7.732  1.109   18.735  1.00 43.18  ? 120  LYS E C   1 
ATOM   8871  O O   . LYS E  1 117 ? -8.691  1.106   19.512  1.00 48.39  ? 120  LYS E O   1 
ATOM   8872  C CB  . LYS E  1 117 ? -8.113  -0.732  17.097  1.00 42.65  ? 120  LYS E CB  1 
ATOM   8873  C CG  . LYS E  1 117 ? -7.832  -0.091  15.753  1.00 43.35  ? 120  LYS E CG  1 
ATOM   8874  C CD  . LYS E  1 117 ? -8.499  -0.888  14.648  1.00 46.14  ? 120  LYS E CD  1 
ATOM   8875  C CE  . LYS E  1 117 ? -9.933  -0.412  14.427  1.00 44.12  ? 120  LYS E CE  1 
ATOM   8876  N NZ  . LYS E  1 117 ? -10.712 -1.261  13.485  1.00 44.88  ? 120  LYS E NZ  1 
ATOM   8877  N N   . ILE E  1 118 ? -7.158  2.242   18.322  1.00 38.38  ? 121  ILE E N   1 
ATOM   8878  C CA  . ILE E  1 118 ? -7.777  3.534   18.649  1.00 38.25  ? 121  ILE E CA  1 
ATOM   8879  C C   . ILE E  1 118 ? -7.920  4.473   17.436  1.00 48.42  ? 121  ILE E C   1 
ATOM   8880  O O   . ILE E  1 118 ? -7.191  4.358   16.447  1.00 47.93  ? 121  ILE E O   1 
ATOM   8881  C CB  . ILE E  1 118 ? -6.991  4.287   19.728  1.00 45.70  ? 121  ILE E CB  1 
ATOM   8882  C CG1 . ILE E  1 118 ? -5.699  4.876   19.186  1.00 38.33  ? 121  ILE E CG1 1 
ATOM   8883  C CG2 . ILE E  1 118 ? -6.720  3.400   20.947  1.00 50.10  ? 121  ILE E CG2 1 
ATOM   8884  C CD1 . ILE E  1 118 ? -5.048  5.780   20.217  1.00 40.45  ? 121  ILE E CD1 1 
ATOM   8885  N N   . GLN E  1 119 ? -8.855  5.420   17.519  1.00 54.04  ? 122  GLN E N   1 
ATOM   8886  C CA  . GLN E  1 119 ? -9.053  6.381   16.435  1.00 46.62  ? 122  GLN E CA  1 
ATOM   8887  C C   . GLN E  1 119 ? -8.190  7.584   16.742  1.00 45.45  ? 122  GLN E C   1 
ATOM   8888  O O   . GLN E  1 119 ? -8.253  8.112   17.848  1.00 51.48  ? 122  GLN E O   1 
ATOM   8889  C CB  . GLN E  1 119 ? -10.526 6.791   16.298  1.00 45.61  ? 122  GLN E CB  1 
ATOM   8890  C CG  . GLN E  1 119 ? -10.785 7.752   15.125  1.00 57.56  ? 122  GLN E CG  1 
ATOM   8891  C CD  . GLN E  1 119 ? -12.252 8.164   14.957  1.00 56.89  ? 122  GLN E CD  1 
ATOM   8892  O OE1 . GLN E  1 119 ? -12.657 9.241   15.400  1.00 49.54  ? 122  GLN E OE1 1 
ATOM   8893  N NE2 . GLN E  1 119 ? -13.053 7.292   14.324  1.00 55.88  ? 122  GLN E NE2 1 
ATOM   8894  N N   . ILE E  1 120 ? -7.367  8.001   15.781  1.00 48.82  ? 123  ILE E N   1 
ATOM   8895  C CA  . ILE E  1 120 ? -6.463  9.145   15.977  1.00 49.82  ? 123  ILE E CA  1 
ATOM   8896  C C   . ILE E  1 120 ? -6.867  10.368  15.144  1.00 49.97  ? 123  ILE E C   1 
ATOM   8897  O O   . ILE E  1 120 ? -6.523  11.505  15.489  1.00 51.99  ? 123  ILE E O   1 
ATOM   8898  C CB  . ILE E  1 120 ? -4.967  8.778   15.711  1.00 51.00  ? 123  ILE E CB  1 
ATOM   8899  C CG1 . ILE E  1 120 ? -4.787  8.070   14.379  1.00 43.58  ? 123  ILE E CG1 1 
ATOM   8900  C CG2 . ILE E  1 120 ? -4.416  7.868   16.826  1.00 47.32  ? 123  ILE E CG2 1 
ATOM   8901  C CD1 . ILE E  1 120 ? -3.339  7.822   14.072  1.00 37.08  ? 123  ILE E CD1 1 
ATOM   8902  N N   . THR E  1 121 ? -7.536  10.139  14.016  1.00 54.88  ? 124  THR E N   1 
ATOM   8903  C CA  . THR E  1 121 ? -8.079  11.254  13.239  1.00 55.53  ? 124  THR E CA  1 
ATOM   8904  C C   . THR E  1 121 ? -9.527  10.922  12.835  1.00 56.48  ? 124  THR E C   1 
ATOM   8905  O O   . THR E  1 121 ? -9.783  9.959   12.086  1.00 56.21  ? 124  THR E O   1 
ATOM   8906  C CB  . THR E  1 121 ? -7.207  11.585  11.979  1.00 55.16  ? 124  THR E CB  1 
ATOM   8907  O OG1 . THR E  1 121 ? -5.897  12.014  12.377  1.00 51.81  ? 124  THR E OG1 1 
ATOM   8908  C CG2 . THR E  1 121 ? -7.834  12.710  11.150  1.00 62.08  ? 124  THR E CG2 1 
ATOM   8909  N N   . PRO E  1 122 ? -10.487 11.683  13.403  1.00 58.94  ? 125  PRO E N   1 
ATOM   8910  C CA  . PRO E  1 122 ? -11.923 11.570  13.105  1.00 65.40  ? 125  PRO E CA  1 
ATOM   8911  C C   . PRO E  1 122 ? -12.226 11.919  11.631  1.00 69.23  ? 125  PRO E C   1 
ATOM   8912  O O   . PRO E  1 122 ? -11.686 12.885  11.073  1.00 62.75  ? 125  PRO E O   1 
ATOM   8913  C CB  . PRO E  1 122 ? -12.571 12.590  14.064  1.00 59.89  ? 125  PRO E CB  1 
ATOM   8914  C CG  . PRO E  1 122 ? -11.479 13.521  14.451  1.00 60.50  ? 125  PRO E CG  1 
ATOM   8915  C CD  . PRO E  1 122 ? -10.217 12.709  14.431  1.00 63.28  ? 125  PRO E CD  1 
ATOM   8916  N N   . LYS E  1 123 A -13.116 11.151  11.015  1.00 74.01  ? 125  LYS E N   1 
ATOM   8917  C CA  . LYS E  1 123 A -13.436 11.330  9.597   1.00 75.38  ? 125  LYS E CA  1 
ATOM   8918  C C   . LYS E  1 123 A -14.049 12.715  9.310   1.00 74.66  ? 125  LYS E C   1 
ATOM   8919  O O   . LYS E  1 123 A -14.048 13.193  8.170   1.00 71.07  ? 125  LYS E O   1 
ATOM   8920  C CB  . LYS E  1 123 A -14.375 10.212  9.147   1.00 67.93  ? 125  LYS E CB  1 
ATOM   8921  C CG  . LYS E  1 123 A -14.477 10.038  7.666   1.00 64.85  ? 125  LYS E CG  1 
ATOM   8922  C CD  . LYS E  1 123 A -15.337 8.835   7.369   1.00 71.96  ? 125  LYS E CD  1 
ATOM   8923  C CE  . LYS E  1 123 A -15.576 8.669   5.872   1.00 71.17  ? 125  LYS E CE  1 
ATOM   8924  N NZ  . LYS E  1 123 A -14.346 8.211   5.174   1.00 64.43  ? 125  LYS E NZ  1 
ATOM   8925  N N   . ASN E  1 124 B -14.560 13.347  10.361  1.00 72.32  ? 125  ASN E N   1 
ATOM   8926  C CA  . ASN E  1 124 B -15.206 14.649  10.269  1.00 69.77  ? 125  ASN E CA  1 
ATOM   8927  C C   . ASN E  1 124 B -14.282 15.791  10.634  1.00 69.26  ? 125  ASN E C   1 
ATOM   8928  O O   . ASN E  1 124 B -14.719 16.854  11.086  1.00 67.67  ? 125  ASN E O   1 
ATOM   8929  C CB  . ASN E  1 124 B -16.432 14.654  11.167  1.00 74.61  ? 125  ASN E CB  1 
ATOM   8930  C CG  . ASN E  1 124 B -17.317 13.456  10.916  1.00 82.44  ? 125  ASN E CG  1 
ATOM   8931  O OD1 . ASN E  1 124 B -17.630 13.138  9.763   1.00 76.82  ? 125  ASN E OD1 1 
ATOM   8932  N ND2 . ASN E  1 124 B -17.690 12.753  11.986  1.00 83.34  ? 125  ASN E ND2 1 
ATOM   8933  N N   . SER E  1 125 ? -12.993 15.566  10.437  1.00 68.50  ? 126  SER E N   1 
ATOM   8934  C CA  . SER E  1 125 ? -12.002 16.578  10.757  1.00 66.44  ? 126  SER E CA  1 
ATOM   8935  C C   . SER E  1 125 ? -11.462 17.213  9.473   1.00 62.14  ? 126  SER E C   1 
ATOM   8936  O O   . SER E  1 125 ? -10.771 18.222  9.518   1.00 62.09  ? 126  SER E O   1 
ATOM   8937  C CB  . SER E  1 125 ? -10.872 15.957  11.591  1.00 65.48  ? 126  SER E CB  1 
ATOM   8938  O OG  . SER E  1 125 ? -9.757  16.824  11.686  1.00 73.18  ? 126  SER E OG  1 
ATOM   8939  N N   . TRP E  1 126 ? -11.801 16.624  8.330   1.00 61.57  ? 127  TRP E N   1 
ATOM   8940  C CA  . TRP E  1 126 ? -11.354 17.139  7.037   1.00 62.47  ? 127  TRP E CA  1 
ATOM   8941  C C   . TRP E  1 126 ? -12.398 18.090  6.475   1.00 62.85  ? 127  TRP E C   1 
ATOM   8942  O O   . TRP E  1 126 ? -13.372 17.664  5.828   1.00 64.31  ? 127  TRP E O   1 
ATOM   8943  C CB  . TRP E  1 126 ? -11.085 15.996  6.048   1.00 58.54  ? 127  TRP E CB  1 
ATOM   8944  C CG  . TRP E  1 126 ? -10.149 14.938  6.599   1.00 59.17  ? 127  TRP E CG  1 
ATOM   8945  C CD1 . TRP E  1 126 ? -10.484 13.682  7.026   1.00 55.74  ? 127  TRP E CD1 1 
ATOM   8946  C CD2 . TRP E  1 126 ? -8.744  15.075  6.827   1.00 51.33  ? 127  TRP E CD2 1 
ATOM   8947  N NE1 . TRP E  1 126 ? -9.365  13.022  7.472   1.00 54.02  ? 127  TRP E NE1 1 
ATOM   8948  C CE2 . TRP E  1 126 ? -8.287  13.857  7.362   1.00 50.41  ? 127  TRP E CE2 1 
ATOM   8949  C CE3 . TRP E  1 126 ? -7.825  16.106  6.616   1.00 49.03  ? 127  TRP E CE3 1 
ATOM   8950  C CZ2 . TRP E  1 126 ? -6.956  13.646  7.689   1.00 56.14  ? 127  TRP E CZ2 1 
ATOM   8951  C CZ3 . TRP E  1 126 ? -6.507  15.895  6.939   1.00 48.99  ? 127  TRP E CZ3 1 
ATOM   8952  C CH2 . TRP E  1 126 ? -6.081  14.680  7.472   1.00 55.41  ? 127  TRP E CH2 1 
ATOM   8953  N N   . SER E  1 127 ? -12.173 19.379  6.688   1.00 60.94  ? 128  SER E N   1 
ATOM   8954  C CA  . SER E  1 127 ? -13.192 20.376  6.391   1.00 68.49  ? 128  SER E CA  1 
ATOM   8955  C C   . SER E  1 127 ? -12.975 21.113  5.061   1.00 67.82  ? 128  SER E C   1 
ATOM   8956  O O   . SER E  1 127 ? -13.866 21.821  4.590   1.00 60.71  ? 128  SER E O   1 
ATOM   8957  C CB  . SER E  1 127 ? -13.260 21.395  7.540   1.00 67.12  ? 128  SER E CB  1 
ATOM   8958  O OG  . SER E  1 127 ? -13.884 20.833  8.691   1.00 74.39  ? 128  SER E OG  1 
ATOM   8959  N N   . ASP E  1 128 ? -11.817 20.905  4.435   1.00 69.50  ? 129  ASP E N   1 
ATOM   8960  C CA  . ASP E  1 128 ? -11.520 21.544  3.157   1.00 60.49  ? 129  ASP E CA  1 
ATOM   8961  C C   . ASP E  1 128 ? -11.214 20.499  2.083   1.00 58.16  ? 129  ASP E C   1 
ATOM   8962  O O   . ASP E  1 128 ? -10.775 20.833  0.976   1.00 57.00  ? 129  ASP E O   1 
ATOM   8963  C CB  . ASP E  1 128 ? -10.348 22.507  3.327   1.00 56.44  ? 129  ASP E CB  1 
ATOM   8964  C CG  . ASP E  1 128 ? -10.658 23.623  4.304   1.00 67.80  ? 129  ASP E CG  1 
ATOM   8965  O OD1 . ASP E  1 128 ? -11.831 24.054  4.379   1.00 71.92  ? 129  ASP E OD1 1 
ATOM   8966  O OD2 . ASP E  1 128 ? -9.732  24.050  5.025   1.00 69.37  ? 129  ASP E OD2 1 
ATOM   8967  N N   . HIS E  1 129 ? -11.452 19.231  2.416   1.00 58.69  ? 130  HIS E N   1 
ATOM   8968  C CA  . HIS E  1 129 ? -11.243 18.135  1.470   1.00 58.77  ? 130  HIS E CA  1 
ATOM   8969  C C   . HIS E  1 129 ? -12.414 17.163  1.561   1.00 53.15  ? 130  HIS E C   1 
ATOM   8970  O O   . HIS E  1 129 ? -13.122 17.138  2.556   1.00 58.60  ? 130  HIS E O   1 
ATOM   8971  C CB  . HIS E  1 129 ? -9.906  17.405  1.740   1.00 51.68  ? 130  HIS E CB  1 
ATOM   8972  C CG  . HIS E  1 129 ? -8.703  18.309  1.776   1.00 51.61  ? 130  HIS E CG  1 
ATOM   8973  N ND1 . HIS E  1 129 ? -8.404  19.118  2.854   1.00 50.97  ? 130  HIS E ND1 1 
ATOM   8974  C CD2 . HIS E  1 129 ? -7.722  18.525  0.863   1.00 51.55  ? 130  HIS E CD2 1 
ATOM   8975  C CE1 . HIS E  1 129 ? -7.291  19.792  2.601   1.00 48.00  ? 130  HIS E CE1 1 
ATOM   8976  N NE2 . HIS E  1 129 ? -6.858  19.452  1.399   1.00 42.68  ? 130  HIS E NE2 1 
ATOM   8977  N N   . GLU E  1 130 ? -12.608 16.360  0.524   1.00 54.82  ? 131  GLU E N   1 
ATOM   8978  C CA  . GLU E  1 130 ? -13.632 15.322  0.536   1.00 61.20  ? 131  GLU E CA  1 
ATOM   8979  C C   . GLU E  1 130 ? -13.017 14.046  1.087   1.00 60.21  ? 131  GLU E C   1 
ATOM   8980  O O   . GLU E  1 130 ? -12.156 13.442  0.448   1.00 57.25  ? 131  GLU E O   1 
ATOM   8981  C CB  . GLU E  1 130 ? -14.179 15.071  -0.883  1.00 59.96  ? 131  GLU E CB  1 
ATOM   8982  C CG  . GLU E  1 130 ? -14.970 16.233  -1.475  1.00 69.28  ? 131  GLU E CG  1 
ATOM   8983  C CD  . GLU E  1 130 ? -16.402 16.298  -0.972  1.00 75.30  ? 131  GLU E CD  1 
ATOM   8984  O OE1 . GLU E  1 130 ? -16.950 15.223  -0.612  1.00 76.61  ? 131  GLU E OE1 1 
ATOM   8985  O OE2 . GLU E  1 130 ? -16.959 17.423  -0.918  1.00 72.00  ? 131  GLU E OE2 1 
ATOM   8986  N N   . ALA E  1 131 ? -13.501 13.589  2.233   1.00 63.53  ? 132  ALA E N   1 
ATOM   8987  C CA  . ALA E  1 131 ? -12.892 12.424  2.857   1.00 54.91  ? 132  ALA E CA  1 
ATOM   8988  C C   . ALA E  1 131 ? -13.843 11.257  2.754   1.00 52.78  ? 132  ALA E C   1 
ATOM   8989  O O   . ALA E  1 131 ? -14.241 10.686  3.758   1.00 63.54  ? 132  ALA E O   1 
ATOM   8990  C CB  . ALA E  1 131 ? -12.538 12.705  4.304   1.00 53.85  ? 132  ALA E CB  1 
ATOM   8991  N N   . SER E  1 132 ? -14.176 10.885  1.527   1.00 47.71  ? 133  SER E N   1 
ATOM   8992  C CA  . SER E  1 132 ? -15.137 9.826   1.292   1.00 53.93  ? 133  SER E CA  1 
ATOM   8993  C C   . SER E  1 132 ? -14.772 9.014   0.057   1.00 54.95  ? 133  SER E C   1 
ATOM   8994  O O   . SER E  1 132 ? -15.646 8.441   -0.593  1.00 58.28  ? 133  SER E O   1 
ATOM   8995  C CB  . SER E  1 132 ? -16.543 10.418  1.133   1.00 64.38  ? 133  SER E CB  1 
ATOM   8996  O OG  . SER E  1 132 ? -16.576 11.443  0.147   1.00 69.46  ? 133  SER E OG  1 
ATOM   8997  N N   . GLY E  1 133 ? -13.479 8.955   -0.256  1.00 48.57  ? 134  GLY E N   1 
ATOM   8998  C CA  . GLY E  1 133 ? -13.011 8.210   -1.414  1.00 47.67  ? 134  GLY E CA  1 
ATOM   8999  C C   . GLY E  1 133 ? -13.314 6.723   -1.364  1.00 50.63  ? 134  GLY E C   1 
ATOM   9000  O O   . GLY E  1 133 ? -13.168 6.064   -0.331  1.00 51.94  ? 134  GLY E O   1 
ATOM   9001  N N   . VAL E  1 134 ? -13.645 6.168   -2.519  1.00 53.33  ? 135  VAL E N   1 
ATOM   9002  C CA  . VAL E  1 134 ? -14.276 4.861   -2.574  1.00 52.84  ? 135  VAL E CA  1 
ATOM   9003  C C   . VAL E  1 134 ? -13.951 4.189   -3.914  1.00 56.09  ? 135  VAL E C   1 
ATOM   9004  O O   . VAL E  1 134 ? -13.587 4.872   -4.872  1.00 56.50  ? 135  VAL E O   1 
ATOM   9005  C CB  . VAL E  1 134 ? -15.804 5.037   -2.340  1.00 54.54  ? 135  VAL E CB  1 
ATOM   9006  C CG1 . VAL E  1 134 ? -16.648 4.410   -3.442  1.00 51.00  ? 135  VAL E CG1 1 
ATOM   9007  C CG2 . VAL E  1 134 ? -16.190 4.552   -0.968  1.00 50.17  ? 135  VAL E CG2 1 
ATOM   9008  N N   . SER E  1 135 ? -14.004 2.861   -3.971  1.00 53.81  ? 136  SER E N   1 
ATOM   9009  C CA  . SER E  1 135 ? -13.655 2.153   -5.195  1.00 52.83  ? 136  SER E CA  1 
ATOM   9010  C C   . SER E  1 135 ? -14.438 0.850   -5.390  1.00 59.14  ? 136  SER E C   1 
ATOM   9011  O O   . SER E  1 135 ? -14.760 0.145   -4.429  1.00 52.67  ? 136  SER E O   1 
ATOM   9012  C CB  . SER E  1 135 ? -12.155 1.847   -5.213  1.00 51.96  ? 136  SER E CB  1 
ATOM   9013  O OG  . SER E  1 135 ? -11.847 0.952   -6.276  1.00 57.38  ? 136  SER E OG  1 
ATOM   9014  N N   . SER E  1 136 ? -14.690 0.498   -6.645  1.00 53.98  ? 137  SER E N   1 
ATOM   9015  C CA  . SER E  1 136 ? -15.450 -0.703  -6.926  1.00 53.60  ? 137  SER E CA  1 
ATOM   9016  C C   . SER E  1 136 ? -14.618 -1.966  -6.664  1.00 54.60  ? 137  SER E C   1 
ATOM   9017  O O   . SER E  1 136 ? -15.154 -3.076  -6.606  1.00 53.50  ? 137  SER E O   1 
ATOM   9018  C CB  . SER E  1 136 ? -15.970 -0.662  -8.366  1.00 57.06  ? 137  SER E CB  1 
ATOM   9019  O OG  . SER E  1 136 ? -14.912 -0.712  -9.311  1.00 67.48  ? 137  SER E OG  1 
ATOM   9020  N N   . ALA E  1 137 ? -13.308 -1.798  -6.508  1.00 53.26  ? 138  ALA E N   1 
ATOM   9021  C CA  . ALA E  1 137 ? -12.439 -2.928  -6.196  1.00 54.57  ? 138  ALA E CA  1 
ATOM   9022  C C   . ALA E  1 137 ? -12.495 -3.281  -4.712  1.00 57.23  ? 138  ALA E C   1 
ATOM   9023  O O   . ALA E  1 137 ? -12.099 -4.366  -4.288  1.00 58.07  ? 138  ALA E O   1 
ATOM   9024  C CB  . ALA E  1 137 ? -11.023 -2.614  -6.597  1.00 55.08  ? 138  ALA E CB  1 
ATOM   9025  N N   . CYS E  1 138 ? -13.046 -2.374  -3.927  1.00 56.10  ? 139  CYS E N   1 
ATOM   9026  C CA  . CYS E  1 138 ? -13.167 -2.599  -2.503  1.00 56.79  ? 139  CYS E CA  1 
ATOM   9027  C C   . CYS E  1 138 ? -14.640 -2.523  -2.080  1.00 56.69  ? 139  CYS E C   1 
ATOM   9028  O O   . CYS E  1 138 ? -15.067 -1.538  -1.479  1.00 49.68  ? 139  CYS E O   1 
ATOM   9029  C CB  . CYS E  1 138 ? -12.303 -1.577  -1.738  1.00 56.56  ? 139  CYS E CB  1 
ATOM   9030  S SG  . CYS E  1 138 ? -10.474 -1.828  -1.891  1.00 76.01  ? 139  CYS E SG  1 
ATOM   9031  N N   . PRO E  1 139 ? -15.423 -3.576  -2.392  1.00 54.71  ? 140  PRO E N   1 
ATOM   9032  C CA  . PRO E  1 139 ? -16.865 -3.583  -2.098  1.00 56.16  ? 140  PRO E CA  1 
ATOM   9033  C C   . PRO E  1 139 ? -17.197 -3.858  -0.626  1.00 58.68  ? 140  PRO E C   1 
ATOM   9034  O O   . PRO E  1 139 ? -16.393 -4.506  0.048   1.00 60.91  ? 140  PRO E O   1 
ATOM   9035  C CB  . PRO E  1 139 ? -17.382 -4.728  -2.970  1.00 45.60  ? 140  PRO E CB  1 
ATOM   9036  C CG  . PRO E  1 139 ? -16.240 -5.672  -3.023  1.00 51.64  ? 140  PRO E CG  1 
ATOM   9037  C CD  . PRO E  1 139 ? -14.999 -4.820  -3.059  1.00 55.40  ? 140  PRO E CD  1 
ATOM   9038  N N   . TYR E  1 140 ? -18.349 -3.379  -0.145  1.00 54.29  ? 141  TYR E N   1 
ATOM   9039  C CA  . TYR E  1 140 ? -18.784 -3.684  1.214   1.00 53.30  ? 141  TYR E CA  1 
ATOM   9040  C C   . TYR E  1 140 ? -20.097 -4.466  1.242   1.00 62.16  ? 141  TYR E C   1 
ATOM   9041  O O   . TYR E  1 140 ? -20.094 -5.703  1.301   1.00 69.65  ? 141  TYR E O   1 
ATOM   9042  C CB  . TYR E  1 140 ? -18.887 -2.388  2.044   1.00 56.93  ? 141  TYR E CB  1 
ATOM   9043  C CG  . TYR E  1 140 ? -19.426 -2.560  3.460   1.00 56.26  ? 141  TYR E CG  1 
ATOM   9044  C CD1 . TYR E  1 140 ? -19.071 -3.660  4.237   1.00 56.72  ? 141  TYR E CD1 1 
ATOM   9045  C CD2 . TYR E  1 140 ? -20.210 -1.575  4.048   1.00 53.28  ? 141  TYR E CD2 1 
ATOM   9046  C CE1 . TYR E  1 140 ? -19.546 -3.812  5.525   1.00 56.65  ? 141  TYR E CE1 1 
ATOM   9047  C CE2 . TYR E  1 140 ? -20.677 -1.704  5.346   1.00 48.99  ? 141  TYR E CE2 1 
ATOM   9048  C CZ  . TYR E  1 140 ? -20.350 -2.827  6.084   1.00 57.81  ? 141  TYR E CZ  1 
ATOM   9049  O OH  . TYR E  1 140 ? -20.830 -2.976  7.383   1.00 53.43  ? 141  TYR E OH  1 
ATOM   9050  N N   . GLN E  1 141 ? -21.220 -3.760  1.222   1.00 62.13  ? 142  GLN E N   1 
ATOM   9051  C CA  . GLN E  1 141 ? -22.514 -4.436  1.223   1.00 54.93  ? 142  GLN E CA  1 
ATOM   9052  C C   . GLN E  1 141 ? -23.290 -4.094  -0.016  1.00 57.74  ? 142  GLN E C   1 
ATOM   9053  O O   . GLN E  1 141 ? -24.335 -3.443  0.067   1.00 56.83  ? 142  GLN E O   1 
ATOM   9054  C CB  . GLN E  1 141 ? -23.328 -4.103  2.471   1.00 53.92  ? 142  GLN E CB  1 
ATOM   9055  C CG  . GLN E  1 141 ? -22.885 -4.872  3.705   1.00 50.95  ? 142  GLN E CG  1 
ATOM   9056  C CD  . GLN E  1 141 ? -23.663 -4.482  4.942   1.00 47.07  ? 142  GLN E CD  1 
ATOM   9057  O OE1 . GLN E  1 141 ? -24.372 -3.481  4.955   1.00 49.97  ? 142  GLN E OE1 1 
ATOM   9058  N NE2 . GLN E  1 141 ? -23.548 -5.282  5.985   1.00 44.65  ? 142  GLN E NE2 1 
ATOM   9059  N N   . GLY E  1 142 ? -22.731 -4.476  -1.164  1.00 60.79  ? 143  GLY E N   1 
ATOM   9060  C CA  . GLY E  1 142 ? -23.344 -4.234  -2.459  1.00 57.74  ? 143  GLY E CA  1 
ATOM   9061  C C   . GLY E  1 142 ? -22.971 -2.892  -3.058  1.00 57.50  ? 143  GLY E C   1 
ATOM   9062  O O   . GLY E  1 142 ? -23.336 -2.595  -4.201  1.00 60.56  ? 143  GLY E O   1 
ATOM   9063  N N   . ARG E  1 143 ? -22.215 -2.098  -2.300  1.00 54.75  ? 144  ARG E N   1 
ATOM   9064  C CA  . ARG E  1 143 ? -21.781 -0.786  -2.759  1.00 50.68  ? 144  ARG E CA  1 
ATOM   9065  C C   . ARG E  1 143 ? -20.240 -0.647  -2.713  1.00 50.37  ? 144  ARG E C   1 
ATOM   9066  O O   . ARG E  1 143 ? -19.541 -1.468  -2.133  1.00 55.74  ? 144  ARG E O   1 
ATOM   9067  C CB  . ARG E  1 143 ? -22.467 0.314   -1.919  1.00 49.57  ? 144  ARG E CB  1 
ATOM   9068  C CG  . ARG E  1 143 ? -21.958 0.523   -0.475  1.00 47.99  ? 144  ARG E CG  1 
ATOM   9069  C CD  . ARG E  1 143 ? -22.854 1.543   0.265   1.00 45.93  ? 144  ARG E CD  1 
ATOM   9070  N NE  . ARG E  1 143 ? -22.324 2.029   1.546   1.00 47.84  ? 144  ARG E NE  1 
ATOM   9071  C CZ  . ARG E  1 143 ? -22.515 1.474   2.749   1.00 42.09  ? 144  ARG E CZ  1 
ATOM   9072  N NH1 . ARG E  1 143 ? -23.214 0.359   2.894   1.00 41.52  ? 144  ARG E NH1 1 
ATOM   9073  N NH2 . ARG E  1 143 ? -21.975 2.038   3.821   1.00 40.33  ? 144  ARG E NH2 1 
ATOM   9074  N N   . SER E  1 144 ? -19.713 0.376   -3.358  1.00 45.46  ? 145  SER E N   1 
ATOM   9075  C CA  . SER E  1 144 ? -18.276 0.596   -3.376  1.00 50.88  ? 145  SER E CA  1 
ATOM   9076  C C   . SER E  1 144 ? -17.748 1.199   -2.048  1.00 54.05  ? 145  SER E C   1 
ATOM   9077  O O   . SER E  1 144 ? -18.354 2.104   -1.447  1.00 45.73  ? 145  SER E O   1 
ATOM   9078  C CB  . SER E  1 144 ? -17.919 1.473   -4.578  1.00 53.38  ? 145  SER E CB  1 
ATOM   9079  O OG  . SER E  1 144 ? -18.260 0.798   -5.782  1.00 55.00  ? 145  SER E OG  1 
ATOM   9080  N N   . SER E  1 145 ? -16.596 0.700   -1.610  1.00 56.88  ? 146  SER E N   1 
ATOM   9081  C CA  . SER E  1 145 ? -16.058 1.042   -0.292  1.00 56.78  ? 146  SER E CA  1 
ATOM   9082  C C   . SER E  1 145 ? -14.531 1.273   -0.326  1.00 56.38  ? 146  SER E C   1 
ATOM   9083  O O   . SER E  1 145 ? -14.003 1.699   -1.364  1.00 50.24  ? 146  SER E O   1 
ATOM   9084  C CB  . SER E  1 145 ? -16.426 -0.058  0.716   1.00 48.36  ? 146  SER E CB  1 
ATOM   9085  O OG  . SER E  1 145 ? -16.102 0.340   2.023   1.00 47.72  ? 146  SER E OG  1 
ATOM   9086  N N   . PHE E  1 146 ? -13.866 1.085   0.827   1.00 54.05  ? 147  PHE E N   1 
ATOM   9087  C CA  . PHE E  1 146 ? -12.409 1.280   0.987   1.00 49.75  ? 147  PHE E CA  1 
ATOM   9088  C C   . PHE E  1 146 ? -11.860 0.753   2.343   1.00 48.67  ? 147  PHE E C   1 
ATOM   9089  O O   . PHE E  1 146 ? -12.631 0.453   3.258   1.00 50.12  ? 147  PHE E O   1 
ATOM   9090  C CB  . PHE E  1 146 ? -12.099 2.767   0.841   1.00 46.72  ? 147  PHE E CB  1 
ATOM   9091  C CG  . PHE E  1 146 ? -10.664 3.088   0.586   1.00 42.92  ? 147  PHE E CG  1 
ATOM   9092  C CD1 . PHE E  1 146 ? -10.057 2.740   -0.609  1.00 47.26  ? 147  PHE E CD1 1 
ATOM   9093  C CD2 . PHE E  1 146 ? -9.949  3.825   1.504   1.00 41.91  ? 147  PHE E CD2 1 
ATOM   9094  C CE1 . PHE E  1 146 ? -8.735  3.090   -0.857  1.00 47.50  ? 147  PHE E CE1 1 
ATOM   9095  C CE2 . PHE E  1 146 ? -8.636  4.174   1.268   1.00 45.53  ? 147  PHE E CE2 1 
ATOM   9096  C CZ  . PHE E  1 146 ? -8.023  3.809   0.096   1.00 44.25  ? 147  PHE E CZ  1 
ATOM   9097  N N   . PHE E  1 147 ? -10.534 0.700   2.485   1.00 48.73  ? 148  PHE E N   1 
ATOM   9098  C CA  . PHE E  1 147 ? -9.881  0.366   3.764   1.00 48.30  ? 148  PHE E CA  1 
ATOM   9099  C C   . PHE E  1 147 ? -10.369 1.244   4.940   1.00 47.77  ? 148  PHE E C   1 
ATOM   9100  O O   . PHE E  1 147 ? -10.386 2.482   4.855   1.00 44.09  ? 148  PHE E O   1 
ATOM   9101  C CB  . PHE E  1 147 ? -8.357  0.512   3.636   1.00 40.90  ? 148  PHE E CB  1 
ATOM   9102  C CG  . PHE E  1 147 ? -7.761  -0.322  2.545   1.00 44.97  ? 148  PHE E CG  1 
ATOM   9103  C CD1 . PHE E  1 147 ? -7.550  -1.666  2.726   1.00 40.62  ? 148  PHE E CD1 1 
ATOM   9104  C CD2 . PHE E  1 147 ? -7.399  0.253   1.330   1.00 49.60  ? 148  PHE E CD2 1 
ATOM   9105  C CE1 . PHE E  1 147 ? -6.997  -2.438  1.721   1.00 41.86  ? 148  PHE E CE1 1 
ATOM   9106  C CE2 . PHE E  1 147 ? -6.841  -0.518  0.315   1.00 45.84  ? 148  PHE E CE2 1 
ATOM   9107  C CZ  . PHE E  1 147 ? -6.640  -1.867  0.519   1.00 45.14  ? 148  PHE E CZ  1 
ATOM   9108  N N   . ARG E  1 148 ? -10.638 0.623   6.080   1.00 45.17  ? 149  ARG E N   1 
ATOM   9109  C CA  . ARG E  1 148 ? -11.272 1.376   7.145   1.00 43.65  ? 149  ARG E CA  1 
ATOM   9110  C C   . ARG E  1 148 ? -10.291 2.137   8.000   1.00 45.30  ? 149  ARG E C   1 
ATOM   9111  O O   . ARG E  1 148 ? -10.697 3.068   8.702   1.00 52.23  ? 149  ARG E O   1 
ATOM   9112  C CB  . ARG E  1 148 ? -12.081 0.445   8.034   1.00 43.60  ? 149  ARG E CB  1 
ATOM   9113  C CG  . ARG E  1 148 ? -13.007 -0.433  7.260   1.00 51.41  ? 149  ARG E CG  1 
ATOM   9114  C CD  . ARG E  1 148 ? -14.259 -0.750  8.034   1.00 57.38  ? 149  ARG E CD  1 
ATOM   9115  N NE  . ARG E  1 148 ? -15.082 -1.660  7.249   1.00 64.33  ? 149  ARG E NE  1 
ATOM   9116  C CZ  . ARG E  1 148 ? -15.994 -1.251  6.370   1.00 64.11  ? 149  ARG E CZ  1 
ATOM   9117  N NH1 . ARG E  1 148 ? -16.201 0.053   6.184   1.00 62.89  ? 149  ARG E NH1 1 
ATOM   9118  N NH2 . ARG E  1 148 ? -16.699 -2.140  5.679   1.00 62.79  ? 149  ARG E NH2 1 
ATOM   9119  N N   . ASN E  1 149 ? -9.007  1.793   7.946   1.00 41.46  ? 150  ASN E N   1 
ATOM   9120  C CA  . ASN E  1 149 ? -8.097  2.404   8.911   1.00 42.53  ? 150  ASN E CA  1 
ATOM   9121  C C   . ASN E  1 149 ? -7.321  3.558   8.338   1.00 45.41  ? 150  ASN E C   1 
ATOM   9122  O O   . ASN E  1 149 ? -6.694  4.329   9.082   1.00 43.33  ? 150  ASN E O   1 
ATOM   9123  C CB  . ASN E  1 149 ? -7.142  1.351   9.465   1.00 41.32  ? 150  ASN E CB  1 
ATOM   9124  C CG  . ASN E  1 149 ? -7.849  0.350   10.348  1.00 42.46  ? 150  ASN E CG  1 
ATOM   9125  O OD1 . ASN E  1 149 ? -8.706  0.726   11.160  1.00 42.15  ? 150  ASN E OD1 1 
ATOM   9126  N ND2 . ASN E  1 149 ? -7.524  -0.932  10.181  1.00 37.60  ? 150  ASN E ND2 1 
ATOM   9127  N N   . VAL E  1 150 ? -7.469  3.745   7.032   1.00 40.78  ? 151  VAL E N   1 
ATOM   9128  C CA  . VAL E  1 150 ? -6.872  4.883   6.355   1.00 43.75  ? 151  VAL E CA  1 
ATOM   9129  C C   . VAL E  1 150 ? -7.968  5.525   5.515   1.00 47.81  ? 151  VAL E C   1 
ATOM   9130  O O   . VAL E  1 150 ? -8.888  4.835   5.031   1.00 46.49  ? 151  VAL E O   1 
ATOM   9131  C CB  . VAL E  1 150 ? -5.684  4.461   5.433   1.00 49.87  ? 151  VAL E CB  1 
ATOM   9132  C CG1 . VAL E  1 150 ? -4.495  3.952   6.244   1.00 44.89  ? 151  VAL E CG1 1 
ATOM   9133  C CG2 . VAL E  1 150 ? -6.130  3.393   4.424   1.00 44.71  ? 151  VAL E CG2 1 
ATOM   9134  N N   . VAL E  1 151 ? -7.829  6.822   5.266   1.00 44.83  ? 152  VAL E N   1 
ATOM   9135  C CA  . VAL E  1 151 ? -8.886  7.567   4.587   1.00 47.06  ? 152  VAL E CA  1 
ATOM   9136  C C   . VAL E  1 151 ? -8.396  8.235   3.284   1.00 45.46  ? 152  VAL E C   1 
ATOM   9137  O O   . VAL E  1 151 ? -7.370  8.939   3.273   1.00 42.33  ? 152  VAL E O   1 
ATOM   9138  C CB  . VAL E  1 151 ? -9.507  8.639   5.560   1.00 50.21  ? 152  VAL E CB  1 
ATOM   9139  C CG1 . VAL E  1 151 ? -8.429  9.554   6.181   1.00 42.46  ? 152  VAL E CG1 1 
ATOM   9140  C CG2 . VAL E  1 151 ? -10.590 9.454   4.868   1.00 50.79  ? 152  VAL E CG2 1 
ATOM   9141  N N   . TRP E  1 152 ? -9.166  8.038   2.207   1.00 44.13  ? 153  TRP E N   1 
ATOM   9142  C CA  . TRP E  1 152 ? -8.871  8.623   0.889   1.00 41.70  ? 153  TRP E CA  1 
ATOM   9143  C C   . TRP E  1 152 ? -9.413  10.050  0.684   1.00 40.85  ? 153  TRP E C   1 
ATOM   9144  O O   . TRP E  1 152 ? -10.571 10.232  0.319   1.00 39.19  ? 153  TRP E O   1 
ATOM   9145  C CB  . TRP E  1 152 ? -9.435  7.685   -0.192  1.00 42.97  ? 153  TRP E CB  1 
ATOM   9146  C CG  . TRP E  1 152 ? -8.957  7.932   -1.609  1.00 45.20  ? 153  TRP E CG  1 
ATOM   9147  C CD1 . TRP E  1 152 ? -8.224  9.003   -2.070  1.00 43.01  ? 153  TRP E CD1 1 
ATOM   9148  C CD2 . TRP E  1 152 ? -9.181  7.083   -2.749  1.00 42.71  ? 153  TRP E CD2 1 
ATOM   9149  N NE1 . TRP E  1 152 ? -7.982  8.863   -3.422  1.00 42.15  ? 153  TRP E NE1 1 
ATOM   9150  C CE2 . TRP E  1 152 ? -8.561  7.698   -3.861  1.00 43.01  ? 153  TRP E CE2 1 
ATOM   9151  C CE3 . TRP E  1 152 ? -9.845  5.866   -2.936  1.00 41.97  ? 153  TRP E CE3 1 
ATOM   9152  C CZ2 . TRP E  1 152 ? -8.581  7.126   -5.135  1.00 43.64  ? 153  TRP E CZ2 1 
ATOM   9153  C CZ3 . TRP E  1 152 ? -9.868  5.303   -4.201  1.00 40.80  ? 153  TRP E CZ3 1 
ATOM   9154  C CH2 . TRP E  1 152 ? -9.242  5.933   -5.283  1.00 48.10  ? 153  TRP E CH2 1 
ATOM   9155  N N   . LEU E  1 153 ? -8.539  11.045  0.850   1.00 43.57  ? 154  LEU E N   1 
ATOM   9156  C CA  . LEU E  1 153 ? -8.875  12.470  0.651   1.00 48.92  ? 154  LEU E CA  1 
ATOM   9157  C C   . LEU E  1 153 ? -8.724  12.936  -0.824  1.00 57.74  ? 154  LEU E C   1 
ATOM   9158  O O   . LEU E  1 153 ? -7.716  12.618  -1.479  1.00 56.30  ? 154  LEU E O   1 
ATOM   9159  C CB  . LEU E  1 153 ? -7.979  13.358  1.520   1.00 43.55  ? 154  LEU E CB  1 
ATOM   9160  C CG  . LEU E  1 153 ? -7.834  13.105  3.025   1.00 49.90  ? 154  LEU E CG  1 
ATOM   9161  C CD1 . LEU E  1 153 ? -6.655  13.910  3.581   1.00 55.07  ? 154  LEU E CD1 1 
ATOM   9162  C CD2 . LEU E  1 153 ? -9.099  13.441  3.789   1.00 47.10  ? 154  LEU E CD2 1 
ATOM   9163  N N   . THR E  1 154 ? -9.711  13.697  -1.323  1.00 54.22  ? 155  THR E N   1 
ATOM   9164  C CA  . THR E  1 154 ? -9.701  14.266  -2.680  1.00 53.47  ? 155  THR E CA  1 
ATOM   9165  C C   . THR E  1 154 ? -10.076 15.760  -2.658  1.00 56.93  ? 155  THR E C   1 
ATOM   9166  O O   . THR E  1 154 ? -10.448 16.276  -1.611  1.00 58.73  ? 155  THR E O   1 
ATOM   9167  C CB  . THR E  1 154 ? -10.688 13.561  -3.604  1.00 49.26  ? 155  THR E CB  1 
ATOM   9168  O OG1 . THR E  1 154 ? -12.000 13.660  -3.045  1.00 54.88  ? 155  THR E OG1 1 
ATOM   9169  C CG2 . THR E  1 154 ? -10.293 12.107  -3.820  1.00 47.03  ? 155  THR E CG2 1 
ATOM   9170  N N   . LYS E  1 155 ? -10.025 16.447  -3.804  1.00 59.15  ? 156  LYS E N   1 
ATOM   9171  C CA  . LYS E  1 155 ? -10.345 17.887  -3.828  1.00 61.78  ? 156  LYS E CA  1 
ATOM   9172  C C   . LYS E  1 155 ? -11.823 18.205  -3.496  1.00 58.95  ? 156  LYS E C   1 
ATOM   9173  O O   . LYS E  1 155 ? -12.738 17.426  -3.807  1.00 59.79  ? 156  LYS E O   1 
ATOM   9174  C CB  . LYS E  1 155 ? -10.006 18.503  -5.186  1.00 61.44  ? 156  LYS E CB  1 
ATOM   9175  C CG  . LYS E  1 155 ? -10.984 18.172  -6.300  1.00 59.69  ? 156  LYS E CG  1 
ATOM   9176  C CD  . LYS E  1 155 ? -10.538 18.853  -7.585  1.00 61.38  ? 156  LYS E CD  1 
ATOM   9177  C CE  . LYS E  1 155 ? -11.518 18.623  -8.719  1.00 61.75  ? 156  LYS E CE  1 
ATOM   9178  N NZ  . LYS E  1 155 ? -11.016 19.259  -9.957  1.00 57.57  ? 156  LYS E NZ  1 
ATOM   9179  N N   . LYS E  1 156 ? -12.046 19.355  -2.865  1.00 58.58  ? 157  LYS E N   1 
ATOM   9180  C CA  . LYS E  1 156 ? -13.401 19.793  -2.500  1.00 63.18  ? 157  LYS E CA  1 
ATOM   9181  C C   . LYS E  1 156 ? -13.732 21.119  -3.153  1.00 63.68  ? 157  LYS E C   1 
ATOM   9182  O O   . LYS E  1 156 ? -12.948 22.070  -3.045  1.00 60.45  ? 157  LYS E O   1 
ATOM   9183  C CB  . LYS E  1 156 ? -13.544 19.935  -0.990  1.00 62.44  ? 157  LYS E CB  1 
ATOM   9184  C CG  . LYS E  1 156 ? -14.881 20.502  -0.557  1.00 64.35  ? 157  LYS E CG  1 
ATOM   9185  C CD  . LYS E  1 156 ? -14.979 20.493  0.956   1.00 65.31  ? 157  LYS E CD  1 
ATOM   9186  C CE  . LYS E  1 156 ? -16.235 21.160  1.454   1.00 60.29  ? 157  LYS E CE  1 
ATOM   9187  N NZ  . LYS E  1 156 ? -16.241 21.135  2.933   1.00 66.92  ? 157  LYS E NZ  1 
ATOM   9188  N N   . ASP E  1 157 ? -14.920 21.187  -3.764  1.00 65.96  ? 158  ASP E N   1 
ATOM   9189  C CA  . ASP E  1 157 ? -15.248 22.220  -4.753  1.00 67.37  ? 158  ASP E CA  1 
ATOM   9190  C C   . ASP E  1 157 ? -14.237 22.004  -5.874  1.00 70.37  ? 158  ASP E C   1 
ATOM   9191  O O   . ASP E  1 157 ? -14.265 20.952  -6.539  1.00 69.27  ? 158  ASP E O   1 
ATOM   9192  C CB  . ASP E  1 157 ? -15.209 23.644  -4.170  1.00 65.00  ? 158  ASP E CB  1 
ATOM   9193  C CG  . ASP E  1 157 ? -16.222 23.845  -3.032  1.00 66.86  ? 158  ASP E CG  1 
ATOM   9194  O OD1 . ASP E  1 157 ? -17.339 23.284  -3.106  1.00 60.57  ? 158  ASP E OD1 1 
ATOM   9195  O OD2 . ASP E  1 157 ? -15.897 24.559  -2.056  1.00 69.39  ? 158  ASP E OD2 1 
ATOM   9196  N N   . ASN E  1 158 ? -13.325 22.954  -6.065  1.00 61.72  ? 159  ASN E N   1 
ATOM   9197  C CA  . ASN E  1 158 ? -12.230 22.723  -7.000  1.00 65.76  ? 159  ASN E CA  1 
ATOM   9198  C C   . ASN E  1 158 ? -10.855 23.018  -6.442  1.00 66.53  ? 159  ASN E C   1 
ATOM   9199  O O   . ASN E  1 158 ? -10.016 23.609  -7.131  1.00 64.56  ? 159  ASN E O   1 
ATOM   9200  C CB  . ASN E  1 158 ? -12.434 23.544  -8.267  1.00 67.45  ? 159  ASN E CB  1 
ATOM   9201  C CG  . ASN E  1 158 ? -13.039 22.736  -9.372  1.00 67.27  ? 159  ASN E CG  1 
ATOM   9202  O OD1 . ASN E  1 158 ? -13.665 21.700  -9.134  1.00 69.00  ? 159  ASN E OD1 1 
ATOM   9203  N ND2 . ASN E  1 158 ? -12.829 23.179  -10.599 1.00 79.19  ? 159  ASN E ND2 1 
ATOM   9204  N N   . ALA E  1 159 ? -10.615 22.588  -5.206  1.00 66.23  ? 160  ALA E N   1 
ATOM   9205  C CA  . ALA E  1 159 ? -9.353  22.897  -4.541  1.00 69.21  ? 160  ALA E CA  1 
ATOM   9206  C C   . ALA E  1 159 ? -8.845  21.781  -3.632  1.00 66.28  ? 160  ALA E C   1 
ATOM   9207  O O   . ALA E  1 159 ? -9.617  20.921  -3.191  1.00 65.88  ? 160  ALA E O   1 
ATOM   9208  C CB  . ALA E  1 159 ? -9.489  24.192  -3.745  1.00 61.74  ? 160  ALA E CB  1 
ATOM   9209  N N   . TYR E  1 160 ? -7.525  21.773  -3.430  1.00 63.62  ? 161  TYR E N   1 
ATOM   9210  C CA  . TYR E  1 160 ? -6.857  20.923  -2.440  1.00 57.01  ? 161  TYR E CA  1 
ATOM   9211  C C   . TYR E  1 160 ? -5.756  21.710  -1.722  1.00 52.31  ? 161  TYR E C   1 
ATOM   9212  O O   . TYR E  1 160 ? -4.594  21.683  -2.138  1.00 49.59  ? 161  TYR E O   1 
ATOM   9213  C CB  . TYR E  1 160 ? -6.273  19.678  -3.113  1.00 54.10  ? 161  TYR E CB  1 
ATOM   9214  C CG  . TYR E  1 160 ? -5.848  18.519  -2.210  1.00 48.76  ? 161  TYR E CG  1 
ATOM   9215  C CD1 . TYR E  1 160 ? -4.783  18.648  -1.312  1.00 47.00  ? 161  TYR E CD1 1 
ATOM   9216  C CD2 . TYR E  1 160 ? -6.467  17.268  -2.324  1.00 53.49  ? 161  TYR E CD2 1 
ATOM   9217  C CE1 . TYR E  1 160 ? -4.375  17.578  -0.520  1.00 46.78  ? 161  TYR E CE1 1 
ATOM   9218  C CE2 . TYR E  1 160 ? -6.069  16.187  -1.541  1.00 50.34  ? 161  TYR E CE2 1 
ATOM   9219  C CZ  . TYR E  1 160 ? -5.022  16.351  -0.642  1.00 45.23  ? 161  TYR E CZ  1 
ATOM   9220  O OH  . TYR E  1 160 ? -4.618  15.279  0.122   1.00 47.34  ? 161  TYR E OH  1 
ATOM   9221  N N   . PRO E  1 161 ? -6.111  22.404  -0.634  1.00 54.00  ? 162  PRO E N   1 
ATOM   9222  C CA  . PRO E  1 161 ? -5.124  23.134  0.175   1.00 51.66  ? 162  PRO E CA  1 
ATOM   9223  C C   . PRO E  1 161 ? -4.034  22.223  0.764   1.00 48.88  ? 162  PRO E C   1 
ATOM   9224  O O   . PRO E  1 161 ? -4.221  20.998  0.865   1.00 43.28  ? 162  PRO E O   1 
ATOM   9225  C CB  . PRO E  1 161 ? -5.966  23.738  1.316   1.00 43.10  ? 162  PRO E CB  1 
ATOM   9226  C CG  . PRO E  1 161 ? -7.373  23.673  0.857   1.00 46.04  ? 162  PRO E CG  1 
ATOM   9227  C CD  . PRO E  1 161 ? -7.472  22.495  -0.072  1.00 56.39  ? 162  PRO E CD  1 
ATOM   9228  N N   . THR E  1 162 ? -2.919  22.841  1.152   1.00 49.01  ? 163  THR E N   1 
ATOM   9229  C CA  . THR E  1 162 ? -1.805  22.148  1.791   1.00 49.19  ? 163  THR E CA  1 
ATOM   9230  C C   . THR E  1 162 ? -2.184  21.749  3.205   1.00 50.48  ? 163  THR E C   1 
ATOM   9231  O O   . THR E  1 162 ? -2.603  22.597  3.993   1.00 53.74  ? 163  THR E O   1 
ATOM   9232  C CB  . THR E  1 162 ? -0.527  23.030  1.840   1.00 51.56  ? 163  THR E CB  1 
ATOM   9233  O OG1 . THR E  1 162 ? 0.030   23.148  0.515   1.00 54.74  ? 163  THR E OG1 1 
ATOM   9234  C CG2 . THR E  1 162 ? 0.521   22.420  2.773   1.00 47.73  ? 163  THR E CG2 1 
ATOM   9235  N N   . ILE E  1 163 ? -2.007  20.465  3.520   1.00 45.77  ? 164  ILE E N   1 
ATOM   9236  C CA  . ILE E  1 163 ? -2.329  19.911  4.834   1.00 43.65  ? 164  ILE E CA  1 
ATOM   9237  C C   . ILE E  1 163 ? -1.096  19.952  5.767   1.00 47.67  ? 164  ILE E C   1 
ATOM   9238  O O   . ILE E  1 163 ? -0.021  19.507  5.382   1.00 50.13  ? 164  ILE E O   1 
ATOM   9239  C CB  . ILE E  1 163 ? -2.824  18.461  4.703   1.00 35.57  ? 164  ILE E CB  1 
ATOM   9240  C CG1 . ILE E  1 163 ? -4.055  18.366  3.809   1.00 40.12  ? 164  ILE E CG1 1 
ATOM   9241  C CG2 . ILE E  1 163 ? -3.116  17.887  6.036   1.00 44.23  ? 164  ILE E CG2 1 
ATOM   9242  C CD1 . ILE E  1 163 ? -4.544  16.951  3.606   1.00 39.89  ? 164  ILE E CD1 1 
ATOM   9243  N N   . LYS E  1 164 ? -1.235  20.522  6.966   1.00 49.99  ? 165  LYS E N   1 
ATOM   9244  C CA  . LYS E  1 164 ? -0.180  20.463  7.989   1.00 48.95  ? 165  LYS E CA  1 
ATOM   9245  C C   . LYS E  1 164 ? -0.805  20.001  9.299   1.00 56.56  ? 165  LYS E C   1 
ATOM   9246  O O   . LYS E  1 164 ? -1.466  20.753  10.021  1.00 63.32  ? 165  LYS E O   1 
ATOM   9247  C CB  . LYS E  1 164 ? 0.531   21.803  8.169   1.00 47.48  ? 165  LYS E CB  1 
ATOM   9248  C CG  . LYS E  1 164 ? 1.417   22.161  7.010   1.00 55.18  ? 165  LYS E CG  1 
ATOM   9249  C CD  . LYS E  1 164 ? 2.088   23.513  7.178   1.00 57.52  ? 165  LYS E CD  1 
ATOM   9250  C CE  . LYS E  1 164 ? 2.895   23.843  5.923   1.00 63.37  ? 165  LYS E CE  1 
ATOM   9251  N NZ  . LYS E  1 164 ? 3.457   25.225  5.907   1.00 72.51  ? 165  LYS E NZ  1 
ATOM   9252  N N   . ARG E  1 165 ? -0.555  18.745  9.606   1.00 55.28  ? 166  ARG E N   1 
ATOM   9253  C CA  . ARG E  1 165 ? -1.227  18.090  10.693  1.00 56.50  ? 166  ARG E CA  1 
ATOM   9254  C C   . ARG E  1 165 ? -0.207  17.381  11.575  1.00 56.20  ? 166  ARG E C   1 
ATOM   9255  O O   . ARG E  1 165 ? 0.839   16.923  11.101  1.00 55.27  ? 166  ARG E O   1 
ATOM   9256  C CB  . ARG E  1 165 ? -2.270  17.137  10.111  1.00 48.52  ? 166  ARG E CB  1 
ATOM   9257  C CG  . ARG E  1 165 ? -3.224  16.570  11.098  1.00 58.28  ? 166  ARG E CG  1 
ATOM   9258  C CD  . ARG E  1 165 ? -4.342  15.868  10.360  1.00 67.20  ? 166  ARG E CD  1 
ATOM   9259  N NE  . ARG E  1 165 ? -5.342  16.817  9.876   1.00 66.99  ? 166  ARG E NE  1 
ATOM   9260  C CZ  . ARG E  1 165 ? -6.496  17.062  10.503  1.00 65.49  ? 166  ARG E CZ  1 
ATOM   9261  N NH1 . ARG E  1 165 ? -6.803  16.411  11.620  1.00 61.48  ? 166  ARG E NH1 1 
ATOM   9262  N NH2 . ARG E  1 165 ? -7.356  17.944  10.007  1.00 63.89  ? 166  ARG E NH2 1 
ATOM   9263  N N   . SER E  1 166 ? -0.501  17.294  12.862  1.00 52.39  ? 167  SER E N   1 
ATOM   9264  C CA  . SER E  1 166 ? 0.431   16.677  13.774  1.00 46.21  ? 167  SER E CA  1 
ATOM   9265  C C   . SER E  1 166 ? -0.361  15.823  14.763  1.00 48.91  ? 167  SER E C   1 
ATOM   9266  O O   . SER E  1 166 ? -1.548  16.063  14.989  1.00 46.55  ? 167  SER E O   1 
ATOM   9267  C CB  . SER E  1 166 ? 1.273   17.745  14.470  1.00 46.70  ? 167  SER E CB  1 
ATOM   9268  O OG  . SER E  1 166 ? 2.095   17.186  15.474  1.00 49.56  ? 167  SER E OG  1 
ATOM   9269  N N   . TYR E  1 167 ? 0.294   14.799  15.310  1.00 52.25  ? 168  TYR E N   1 
ATOM   9270  C CA  . TYR E  1 167 ? -0.298  13.922  16.331  1.00 50.47  ? 168  TYR E CA  1 
ATOM   9271  C C   . TYR E  1 167 ? 0.793   13.568  17.367  1.00 52.02  ? 168  TYR E C   1 
ATOM   9272  O O   . TYR E  1 167 ? 1.896   13.147  17.017  1.00 49.61  ? 168  TYR E O   1 
ATOM   9273  C CB  . TYR E  1 167 ? -0.903  12.642  15.710  1.00 37.14  ? 168  TYR E CB  1 
ATOM   9274  C CG  . TYR E  1 167 ? -1.405  11.681  16.761  1.00 46.19  ? 168  TYR E CG  1 
ATOM   9275  C CD1 . TYR E  1 167 ? -0.524  10.871  17.475  1.00 49.61  ? 168  TYR E CD1 1 
ATOM   9276  C CD2 . TYR E  1 167 ? -2.751  11.594  17.063  1.00 48.23  ? 168  TYR E CD2 1 
ATOM   9277  C CE1 . TYR E  1 167 ? -0.971  10.008  18.466  1.00 49.93  ? 168  TYR E CE1 1 
ATOM   9278  C CE2 . TYR E  1 167 ? -3.206  10.744  18.051  1.00 45.30  ? 168  TYR E CE2 1 
ATOM   9279  C CZ  . TYR E  1 167 ? -2.307  9.951   18.748  1.00 49.63  ? 168  TYR E CZ  1 
ATOM   9280  O OH  . TYR E  1 167 ? -2.736  9.082   19.725  1.00 52.13  ? 168  TYR E OH  1 
ATOM   9281  N N   . ASN E  1 168 ? 0.477   13.737  18.644  1.00 53.06  ? 169  ASN E N   1 
ATOM   9282  C CA  . ASN E  1 168 ? 1.408   13.395  19.706  1.00 47.69  ? 169  ASN E CA  1 
ATOM   9283  C C   . ASN E  1 168 ? 0.927   12.131  20.408  1.00 48.36  ? 169  ASN E C   1 
ATOM   9284  O O   . ASN E  1 168 ? -0.212  12.081  20.870  1.00 47.93  ? 169  ASN E O   1 
ATOM   9285  C CB  . ASN E  1 168 ? 1.542   14.565  20.679  1.00 47.89  ? 169  ASN E CB  1 
ATOM   9286  C CG  . ASN E  1 168 ? 2.606   14.342  21.730  1.00 52.84  ? 169  ASN E CG  1 
ATOM   9287  O OD1 . ASN E  1 168 ? 2.574   13.361  22.457  1.00 53.55  ? 169  ASN E OD1 1 
ATOM   9288  N ND2 . ASN E  1 168 ? 3.559   15.258  21.815  1.00 60.12  ? 169  ASN E ND2 1 
ATOM   9289  N N   . ASN E  1 169 ? 1.775   11.100  20.459  1.00 46.76  ? 170  ASN E N   1 
ATOM   9290  C CA  . ASN E  1 169 ? 1.388   9.845   21.105  1.00 46.45  ? 170  ASN E CA  1 
ATOM   9291  C C   . ASN E  1 169 ? 1.435   9.939   22.629  1.00 46.97  ? 170  ASN E C   1 
ATOM   9292  O O   . ASN E  1 169 ? 2.434   9.565   23.262  1.00 40.77  ? 170  ASN E O   1 
ATOM   9293  C CB  . ASN E  1 169 ? 2.276   8.690   20.669  1.00 43.69  ? 170  ASN E CB  1 
ATOM   9294  C CG  . ASN E  1 169 ? 1.773   7.361   21.211  1.00 48.69  ? 170  ASN E CG  1 
ATOM   9295  O OD1 . ASN E  1 169 ? 0.626   7.274   21.676  1.00 45.42  ? 170  ASN E OD1 1 
ATOM   9296  N ND2 . ASN E  1 169 ? 2.619   6.322   21.165  1.00 46.78  ? 170  ASN E ND2 1 
ATOM   9297  N N   . THR E  1 170 ? 0.325   10.406  23.192  1.00 45.89  ? 171  THR E N   1 
ATOM   9298  C CA  . THR E  1 170 ? 0.195   10.640  24.618  1.00 44.11  ? 171  THR E CA  1 
ATOM   9299  C C   . THR E  1 170 ? -0.166  9.354   25.350  1.00 50.64  ? 171  THR E C   1 
ATOM   9300  O O   . THR E  1 170 ? -0.402  9.369   26.560  1.00 51.13  ? 171  THR E O   1 
ATOM   9301  C CB  . THR E  1 170 ? -0.881  11.694  24.900  1.00 44.28  ? 171  THR E CB  1 
ATOM   9302  O OG1 . THR E  1 170 ? -2.156  11.205  24.445  1.00 49.01  ? 171  THR E OG1 1 
ATOM   9303  C CG2 . THR E  1 170 ? -0.546  12.998  24.190  1.00 38.17  ? 171  THR E CG2 1 
ATOM   9304  N N   . ASN E  1 171 ? -0.164  8.235   24.628  1.00 48.56  ? 172  ASN E N   1 
ATOM   9305  C CA  . ASN E  1 171 ? -0.425  6.963   25.263  1.00 41.92  ? 172  ASN E CA  1 
ATOM   9306  C C   . ASN E  1 171 ? 0.843   6.487   25.945  1.00 48.15  ? 172  ASN E C   1 
ATOM   9307  O O   . ASN E  1 171 ? 1.952   6.926   25.605  1.00 40.61  ? 172  ASN E O   1 
ATOM   9308  C CB  . ASN E  1 171 ? -0.873  5.917   24.252  1.00 38.98  ? 172  ASN E CB  1 
ATOM   9309  C CG  . ASN E  1 171 ? -2.037  6.377   23.427  1.00 47.47  ? 172  ASN E CG  1 
ATOM   9310  O OD1 . ASN E  1 171 ? -3.190  6.284   23.850  1.00 49.48  ? 172  ASN E OD1 1 
ATOM   9311  N ND2 . ASN E  1 171 ? -1.745  6.899   22.232  1.00 47.20  ? 172  ASN E ND2 1 
ATOM   9312  N N   . GLN E  1 172 ? 0.666   5.554   26.881  1.00 50.63  ? 173  GLN E N   1 
ATOM   9313  C CA  . GLN E  1 172 ? 1.770   4.966   27.623  1.00 46.75  ? 173  GLN E CA  1 
ATOM   9314  C C   . GLN E  1 172 ? 2.505   3.945   26.746  1.00 46.76  ? 173  GLN E C   1 
ATOM   9315  O O   . GLN E  1 172 ? 3.753   3.864   26.746  1.00 42.60  ? 173  GLN E O   1 
ATOM   9316  C CB  . GLN E  1 172 ? 1.222   4.289   28.893  1.00 44.99  ? 173  GLN E CB  1 
ATOM   9317  C CG  . GLN E  1 172 ? 2.288   3.802   29.869  1.00 41.09  ? 173  GLN E CG  1 
ATOM   9318  C CD  . GLN E  1 172 ? 3.019   4.957   30.547  1.00 45.30  ? 173  GLN E CD  1 
ATOM   9319  O OE1 . GLN E  1 172 ? 2.422   6.019   30.794  1.00 39.37  ? 173  GLN E OE1 1 
ATOM   9320  N NE2 . GLN E  1 172 ? 4.317   4.757   30.852  1.00 39.27  ? 173  GLN E NE2 1 
ATOM   9321  N N   . GLU E  1 173 ? 1.721   3.266   25.907  1.00 40.60  ? 174  GLU E N   1 
ATOM   9322  C CA  . GLU E  1 173 ? 2.230   2.198   25.059  1.00 40.72  ? 174  GLU E CA  1 
ATOM   9323  C C   . GLU E  1 173 ? 2.707   2.744   23.702  1.00 40.87  ? 174  GLU E C   1 
ATOM   9324  O O   . GLU E  1 173 ? 2.474   3.917   23.365  1.00 42.63  ? 174  GLU E O   1 
ATOM   9325  C CB  . GLU E  1 173 ? 1.137   1.112   24.876  1.00 41.64  ? 174  GLU E CB  1 
ATOM   9326  C CG  . GLU E  1 173 ? -0.276  1.644   24.571  1.00 43.44  ? 174  GLU E CG  1 
ATOM   9327  C CD  . GLU E  1 173 ? -1.151  1.987   25.821  1.00 51.42  ? 174  GLU E CD  1 
ATOM   9328  O OE1 . GLU E  1 173 ? -1.653  1.067   26.517  1.00 41.19  ? 174  GLU E OE1 1 
ATOM   9329  O OE2 . GLU E  1 173 ? -1.315  3.201   26.114  1.00 45.81  ? 174  GLU E OE2 1 
ATOM   9330  N N   . ASP E  1 174 ? 3.471   1.939   22.970  1.00 40.53  ? 175  ASP E N   1 
ATOM   9331  C CA  . ASP E  1 174 ? 3.920   2.347   21.635  1.00 37.28  ? 175  ASP E CA  1 
ATOM   9332  C C   . ASP E  1 174 ? 2.806   2.142   20.587  1.00 38.26  ? 175  ASP E C   1 
ATOM   9333  O O   . ASP E  1 174 ? 1.927   1.267   20.761  1.00 37.55  ? 175  ASP E O   1 
ATOM   9334  C CB  . ASP E  1 174 ? 5.195   1.600   21.230  1.00 34.41  ? 175  ASP E CB  1 
ATOM   9335  C CG  . ASP E  1 174 ? 6.404   2.032   22.048  1.00 40.66  ? 175  ASP E CG  1 
ATOM   9336  O OD1 . ASP E  1 174 ? 6.364   3.160   22.590  1.00 40.41  ? 175  ASP E OD1 1 
ATOM   9337  O OD2 . ASP E  1 174 ? 7.408   1.284   22.103  1.00 40.64  ? 175  ASP E OD2 1 
ATOM   9338  N N   . LEU E  1 175 ? 2.865   2.931   19.503  1.00 37.92  ? 176  LEU E N   1 
ATOM   9339  C CA  . LEU E  1 175 ? 1.838   2.920   18.433  1.00 40.47  ? 176  LEU E CA  1 
ATOM   9340  C C   . LEU E  1 175 ? 2.309   2.406   17.075  1.00 36.88  ? 176  LEU E C   1 
ATOM   9341  O O   . LEU E  1 175 ? 3.320   2.912   16.551  1.00 38.08  ? 176  LEU E O   1 
ATOM   9342  C CB  . LEU E  1 175 ? 1.289   4.336   18.176  1.00 36.99  ? 176  LEU E CB  1 
ATOM   9343  C CG  . LEU E  1 175 ? -0.093  4.790   18.619  1.00 36.49  ? 176  LEU E CG  1 
ATOM   9344  C CD1 . LEU E  1 175 ? -0.354  6.178   18.055  1.00 39.75  ? 176  LEU E CD1 1 
ATOM   9345  C CD2 . LEU E  1 175 ? -1.130  3.809   18.143  1.00 36.04  ? 176  LEU E CD2 1 
ATOM   9346  N N   . LEU E  1 176 ? 1.543   1.489   16.471  1.00 32.15  ? 177  LEU E N   1 
ATOM   9347  C CA  . LEU E  1 176 ? 1.766   1.155   15.047  1.00 34.53  ? 177  LEU E CA  1 
ATOM   9348  C C   . LEU E  1 176 ? 0.885   2.055   14.173  1.00 34.65  ? 177  LEU E C   1 
ATOM   9349  O O   . LEU E  1 176 ? -0.339  1.874   14.138  1.00 32.60  ? 177  LEU E O   1 
ATOM   9350  C CB  . LEU E  1 176 ? 1.469   -0.320  14.749  1.00 27.88  ? 177  LEU E CB  1 
ATOM   9351  C CG  . LEU E  1 176 ? 1.454   -0.737  13.268  1.00 36.45  ? 177  LEU E CG  1 
ATOM   9352  C CD1 . LEU E  1 176 ? 2.823   -0.521  12.612  1.00 33.04  ? 177  LEU E CD1 1 
ATOM   9353  C CD2 . LEU E  1 176 ? 0.957   -2.193  13.046  1.00 27.36  ? 177  LEU E CD2 1 
ATOM   9354  N N   . VAL E  1 177 ? 1.519   2.986   13.446  1.00 27.91  ? 178  VAL E N   1 
ATOM   9355  C CA  . VAL E  1 177 ? 0.803   3.952   12.610  1.00 32.59  ? 178  VAL E CA  1 
ATOM   9356  C C   . VAL E  1 177 ? 0.972   3.619   11.091  1.00 35.80  ? 178  VAL E C   1 
ATOM   9357  O O   . VAL E  1 177 ? 2.085   3.403   10.606  1.00 34.63  ? 178  VAL E O   1 
ATOM   9358  C CB  . VAL E  1 177 ? 1.299   5.409   12.921  1.00 33.16  ? 178  VAL E CB  1 
ATOM   9359  C CG1 . VAL E  1 177 ? 0.493   6.453   12.178  1.00 29.78  ? 178  VAL E CG1 1 
ATOM   9360  C CG2 . VAL E  1 177 ? 1.284   5.707   14.434  1.00 28.75  ? 178  VAL E CG2 1 
ATOM   9361  N N   . LEU E  1 178 ? -0.125  3.640   10.333  1.00 35.31  ? 179  LEU E N   1 
ATOM   9362  C CA  . LEU E  1 178 ? -0.102  3.241   8.916   1.00 35.36  ? 179  LEU E CA  1 
ATOM   9363  C C   . LEU E  1 178 ? -0.501  4.422   8.015   1.00 37.35  ? 179  LEU E C   1 
ATOM   9364  O O   . LEU E  1 178 ? -1.258  5.296   8.436   1.00 38.87  ? 179  LEU E O   1 
ATOM   9365  C CB  . LEU E  1 178 ? -1.052  2.064   8.660   1.00 30.46  ? 179  LEU E CB  1 
ATOM   9366  C CG  . LEU E  1 178 ? -1.051  0.832   9.570   1.00 33.86  ? 179  LEU E CG  1 
ATOM   9367  C CD1 . LEU E  1 178 ? -2.371  0.084   9.423   1.00 34.41  ? 179  LEU E CD1 1 
ATOM   9368  C CD2 . LEU E  1 178 ? 0.090   -0.109  9.238   1.00 30.83  ? 179  LEU E CD2 1 
ATOM   9369  N N   . TRP E  1 179 ? 0.076   4.503   6.819   1.00 35.22  ? 180  TRP E N   1 
ATOM   9370  C CA  . TRP E  1 179 ? -0.339  5.522   5.864   1.00 33.45  ? 180  TRP E CA  1 
ATOM   9371  C C   . TRP E  1 179 ? -0.004  5.144   4.415   1.00 40.29  ? 180  TRP E C   1 
ATOM   9372  O O   . TRP E  1 179 ? 0.715   4.170   4.166   1.00 38.44  ? 180  TRP E O   1 
ATOM   9373  C CB  . TRP E  1 179 ? 0.272   6.863   6.231   1.00 32.48  ? 180  TRP E CB  1 
ATOM   9374  C CG  . TRP E  1 179 ? 1.759   7.010   6.086   1.00 37.60  ? 180  TRP E CG  1 
ATOM   9375  C CD1 . TRP E  1 179 ? 2.426   7.524   5.012   1.00 35.58  ? 180  TRP E CD1 1 
ATOM   9376  C CD2 . TRP E  1 179 ? 2.764   6.706   7.075   1.00 38.56  ? 180  TRP E CD2 1 
ATOM   9377  N NE1 . TRP E  1 179 ? 3.779   7.556   5.264   1.00 38.00  ? 180  TRP E NE1 1 
ATOM   9378  C CE2 . TRP E  1 179 ? 4.014   7.054   6.521   1.00 40.51  ? 180  TRP E CE2 1 
ATOM   9379  C CE3 . TRP E  1 179 ? 2.725   6.179   8.372   1.00 36.99  ? 180  TRP E CE3 1 
ATOM   9380  C CZ2 . TRP E  1 179 ? 5.220   6.887   7.225   1.00 37.09  ? 180  TRP E CZ2 1 
ATOM   9381  C CZ3 . TRP E  1 179 ? 3.920   6.013   9.067   1.00 35.69  ? 180  TRP E CZ3 1 
ATOM   9382  C CH2 . TRP E  1 179 ? 5.148   6.367   8.493   1.00 35.68  ? 180  TRP E CH2 1 
ATOM   9383  N N   . GLY E  1 180 ? -0.499  5.929   3.459   1.00 36.81  ? 181  GLY E N   1 
ATOM   9384  C CA  . GLY E  1 180 ? -0.358  5.550   2.074   1.00 38.53  ? 181  GLY E CA  1 
ATOM   9385  C C   . GLY E  1 180 ? -0.236  6.705   1.104   1.00 40.61  ? 181  GLY E C   1 
ATOM   9386  O O   . GLY E  1 180 ? -0.410  7.872   1.479   1.00 37.40  ? 181  GLY E O   1 
ATOM   9387  N N   . ILE E  1 181 ? 0.077   6.352   -0.147  1.00 37.72  ? 182  ILE E N   1 
ATOM   9388  C CA  . ILE E  1 181 ? 0.173   7.292   -1.256  1.00 39.16  ? 182  ILE E CA  1 
ATOM   9389  C C   . ILE E  1 181 ? -0.440  6.671   -2.533  1.00 40.74  ? 182  ILE E C   1 
ATOM   9390  O O   . ILE E  1 181 ? -0.326  5.458   -2.768  1.00 37.73  ? 182  ILE E O   1 
ATOM   9391  C CB  . ILE E  1 181 ? 1.630   7.699   -1.492  1.00 38.95  ? 182  ILE E CB  1 
ATOM   9392  C CG1 . ILE E  1 181 ? 1.731   8.696   -2.640  1.00 46.57  ? 182  ILE E CG1 1 
ATOM   9393  C CG2 . ILE E  1 181 ? 2.483   6.469   -1.786  1.00 40.92  ? 182  ILE E CG2 1 
ATOM   9394  C CD1 . ILE E  1 181 ? 3.160   9.115   -2.943  1.00 44.83  ? 182  ILE E CD1 1 
ATOM   9395  N N   . HIS E  1 182 ? -1.136  7.494   -3.318  1.00 40.56  ? 183  HIS E N   1 
ATOM   9396  C CA  . HIS E  1 182 ? -1.769  7.031   -4.557  1.00 41.21  ? 183  HIS E CA  1 
ATOM   9397  C C   . HIS E  1 182 ? -0.985  7.425   -5.810  1.00 39.88  ? 183  HIS E C   1 
ATOM   9398  O O   . HIS E  1 182 ? -0.659  8.607   -6.013  1.00 42.16  ? 183  HIS E O   1 
ATOM   9399  C CB  . HIS E  1 182 ? -3.210  7.557   -4.635  1.00 41.94  ? 183  HIS E CB  1 
ATOM   9400  C CG  . HIS E  1 182 ? -3.956  7.125   -5.864  1.00 44.64  ? 183  HIS E CG  1 
ATOM   9401  N ND1 . HIS E  1 182 ? -4.641  8.012   -6.672  1.00 40.94  ? 183  HIS E ND1 1 
ATOM   9402  C CD2 . HIS E  1 182 ? -4.106  5.902   -6.435  1.00 42.74  ? 183  HIS E CD2 1 
ATOM   9403  C CE1 . HIS E  1 182 ? -5.195  7.351   -7.675  1.00 42.22  ? 183  HIS E CE1 1 
ATOM   9404  N NE2 . HIS E  1 182 ? -4.885  6.070   -7.556  1.00 41.68  ? 183  HIS E NE2 1 
ATOM   9405  N N   . HIS E  1 183 ? -0.684  6.421   -6.633  1.00 35.10  ? 184  HIS E N   1 
ATOM   9406  C CA  . HIS E  1 183 ? -0.029  6.621   -7.928  1.00 37.80  ? 184  HIS E CA  1 
ATOM   9407  C C   . HIS E  1 183 ? -1.078  6.522   -9.017  1.00 38.15  ? 184  HIS E C   1 
ATOM   9408  O O   . HIS E  1 183 ? -1.520  5.415   -9.353  1.00 38.50  ? 184  HIS E O   1 
ATOM   9409  C CB  . HIS E  1 183 ? 1.071   5.569   -8.192  1.00 35.48  ? 184  HIS E CB  1 
ATOM   9410  C CG  . HIS E  1 183 ? 2.110   5.494   -7.118  1.00 37.51  ? 184  HIS E CG  1 
ATOM   9411  N ND1 . HIS E  1 183 ? 3.085   6.459   -6.956  1.00 35.44  ? 184  HIS E ND1 1 
ATOM   9412  C CD2 . HIS E  1 183 ? 2.322   4.573   -6.144  1.00 35.53  ? 184  HIS E CD2 1 
ATOM   9413  C CE1 . HIS E  1 183 ? 3.848   6.136   -5.923  1.00 36.16  ? 184  HIS E CE1 1 
ATOM   9414  N NE2 . HIS E  1 183 ? 3.409   4.995   -5.415  1.00 34.96  ? 184  HIS E NE2 1 
ATOM   9415  N N   . PRO E  1 184 ? -1.479  7.672   -9.575  1.00 40.22  ? 185  PRO E N   1 
ATOM   9416  C CA  . PRO E  1 184 ? -2.482  7.749   -10.651 1.00 46.93  ? 185  PRO E CA  1 
ATOM   9417  C C   . PRO E  1 184 ? -1.952  7.201   -11.998 1.00 51.25  ? 185  PRO E C   1 
ATOM   9418  O O   . PRO E  1 184 ? -0.812  6.708   -12.070 1.00 45.91  ? 185  PRO E O   1 
ATOM   9419  C CB  . PRO E  1 184 ? -2.773  9.258   -10.760 1.00 45.44  ? 185  PRO E CB  1 
ATOM   9420  C CG  . PRO E  1 184 ? -2.171  9.878   -9.534  1.00 41.33  ? 185  PRO E CG  1 
ATOM   9421  C CD  . PRO E  1 184 ? -1.016  9.009   -9.161  1.00 37.60  ? 185  PRO E CD  1 
ATOM   9422  N N   . ASN E  1 185 ? -2.807  7.234   -13.024 1.00 54.23  ? 186  ASN E N   1 
ATOM   9423  C CA  . ASN E  1 185 ? -2.502  6.739   -14.377 1.00 53.76  ? 186  ASN E CA  1 
ATOM   9424  C C   . ASN E  1 185 ? -2.135  7.818   -15.396 1.00 55.29  ? 186  ASN E C   1 
ATOM   9425  O O   . ASN E  1 185 ? -1.453  7.535   -16.380 1.00 58.10  ? 186  ASN E O   1 
ATOM   9426  C CB  . ASN E  1 185 ? -3.677  5.951   -14.920 1.00 53.28  ? 186  ASN E CB  1 
ATOM   9427  C CG  . ASN E  1 185 ? -4.198  4.962   -13.924 1.00 54.77  ? 186  ASN E CG  1 
ATOM   9428  O OD1 . ASN E  1 185 ? -3.815  3.793   -13.941 1.00 55.14  ? 186  ASN E OD1 1 
ATOM   9429  N ND2 . ASN E  1 185 ? -5.065  5.424   -13.024 1.00 61.82  ? 186  ASN E ND2 1 
ATOM   9430  N N   . ASP E  1 186 ? -2.654  9.029   -15.211 1.00 54.91  ? 187  ASP E N   1 
ATOM   9431  C CA  . ASP E  1 186 ? -2.321  10.131  -16.107 1.00 56.75  ? 187  ASP E CA  1 
ATOM   9432  C C   . ASP E  1 186 ? -2.572  11.484  -15.445 1.00 55.82  ? 187  ASP E C   1 
ATOM   9433  O O   . ASP E  1 186 ? -3.196  11.556  -14.383 1.00 56.11  ? 187  ASP E O   1 
ATOM   9434  C CB  . ASP E  1 186 ? -3.098  10.013  -17.421 1.00 55.66  ? 187  ASP E CB  1 
ATOM   9435  C CG  . ASP E  1 186 ? -4.594  9.956   -17.216 1.00 59.93  ? 187  ASP E CG  1 
ATOM   9436  O OD1 . ASP E  1 186 ? -5.167  10.951  -16.713 1.00 59.85  ? 187  ASP E OD1 1 
ATOM   9437  O OD2 . ASP E  1 186 ? -5.195  8.915   -17.570 1.00 63.63  ? 187  ASP E OD2 1 
ATOM   9438  N N   . ALA E  1 187 ? -2.066  12.547  -16.070 1.00 52.89  ? 188  ALA E N   1 
ATOM   9439  C CA  . ALA E  1 187 ? -2.107  13.888  -15.488 1.00 52.85  ? 188  ALA E CA  1 
ATOM   9440  C C   . ALA E  1 187 ? -3.537  14.394  -15.293 1.00 54.15  ? 188  ALA E C   1 
ATOM   9441  O O   . ALA E  1 187 ? -3.795  15.267  -14.450 1.00 52.27  ? 188  ALA E O   1 
ATOM   9442  C CB  . ALA E  1 187 ? -1.313  14.853  -16.345 1.00 41.26  ? 188  ALA E CB  1 
ATOM   9443  N N   . THR E  1 188 ? -4.445  13.859  -16.108 1.00 54.29  ? 189  THR E N   1 
ATOM   9444  C CA  . THR E  1 188 ? -5.849  14.268  -16.126 1.00 58.72  ? 189  THR E CA  1 
ATOM   9445  C C   . THR E  1 188 ? -6.600  13.734  -14.917 1.00 57.08  ? 189  THR E C   1 
ATOM   9446  O O   . THR E  1 188 ? -7.324  14.478  -14.242 1.00 58.12  ? 189  THR E O   1 
ATOM   9447  C CB  . THR E  1 188 ? -6.550  13.789  -17.418 1.00 60.40  ? 189  THR E CB  1 
ATOM   9448  O OG1 . THR E  1 188 ? -5.853  14.312  -18.551 1.00 59.48  ? 189  THR E OG1 1 
ATOM   9449  C CG2 . THR E  1 188 ? -7.994  14.260  -17.467 1.00 63.07  ? 189  THR E CG2 1 
ATOM   9450  N N   . GLU E  1 189 ? -6.416  12.443  -14.652 1.00 56.86  ? 190  GLU E N   1 
ATOM   9451  C CA  . GLU E  1 189 ? -6.953  11.809  -13.453 1.00 54.56  ? 190  GLU E CA  1 
ATOM   9452  C C   . GLU E  1 189 ? -6.371  12.488  -12.213 1.00 50.93  ? 190  GLU E C   1 
ATOM   9453  O O   . GLU E  1 189 ? -7.077  12.743  -11.242 1.00 53.41  ? 190  GLU E O   1 
ATOM   9454  C CB  . GLU E  1 189 ? -6.623  10.320  -13.455 1.00 52.30  ? 190  GLU E CB  1 
ATOM   9455  C CG  . GLU E  1 189 ? -6.986  9.581   -12.182 1.00 56.97  ? 190  GLU E CG  1 
ATOM   9456  C CD  . GLU E  1 189 ? -6.572  8.107   -12.235 1.00 61.72  ? 190  GLU E CD  1 
ATOM   9457  O OE1 . GLU E  1 189 ? -6.558  7.531   -13.342 1.00 60.90  ? 190  GLU E OE1 1 
ATOM   9458  O OE2 . GLU E  1 189 ? -6.208  7.535   -11.180 1.00 63.70  ? 190  GLU E OE2 1 
ATOM   9459  N N   . GLN E  1 190 ? -5.092  12.834  -12.287 1.00 47.19  ? 191  GLN E N   1 
ATOM   9460  C CA  . GLN E  1 190 ? -4.413  13.545  -11.218 1.00 52.27  ? 191  GLN E CA  1 
ATOM   9461  C C   . GLN E  1 190 ? -5.117  14.875  -10.917 1.00 52.48  ? 191  GLN E C   1 
ATOM   9462  O O   . GLN E  1 190 ? -5.107  15.370  -9.792  1.00 52.80  ? 191  GLN E O   1 
ATOM   9463  C CB  . GLN E  1 190 ? -2.942  13.797  -11.579 1.00 48.66  ? 191  GLN E CB  1 
ATOM   9464  C CG  . GLN E  1 190 ? -2.214  14.799  -10.642 1.00 47.91  ? 191  GLN E CG  1 
ATOM   9465  C CD  . GLN E  1 190 ? -1.807  14.207  -9.273  1.00 49.24  ? 191  GLN E CD  1 
ATOM   9466  O OE1 . GLN E  1 190 ? -1.742  12.974  -9.084  1.00 40.82  ? 191  GLN E OE1 1 
ATOM   9467  N NE2 . GLN E  1 190 ? -1.523  15.096  -8.319  1.00 40.78  ? 191  GLN E NE2 1 
ATOM   9468  N N   . THR E  1 191 ? -5.680  15.493  -11.941 1.00 56.40  ? 192  THR E N   1 
ATOM   9469  C CA  . THR E  1 191 ? -6.298  16.792  -11.731 1.00 60.42  ? 192  THR E CA  1 
ATOM   9470  C C   . THR E  1 191 ? -7.755  16.691  -11.231 1.00 55.04  ? 192  THR E C   1 
ATOM   9471  O O   . THR E  1 191 ? -8.203  17.532  -10.431 1.00 49.93  ? 192  THR E O   1 
ATOM   9472  C CB  . THR E  1 191 ? -6.226  17.633  -13.040 1.00 57.79  ? 192  THR E CB  1 
ATOM   9473  O OG1 . THR E  1 191 ? -6.638  16.823  -14.150 1.00 57.61  ? 192  THR E OG1 1 
ATOM   9474  C CG2 . THR E  1 191 ? -4.793  18.109  -13.279 1.00 51.29  ? 192  THR E CG2 1 
ATOM   9475  N N   . ARG E  1 192 ? -8.479  15.654  -11.659 1.00 49.25  ? 193  ARG E N   1 
ATOM   9476  C CA  . ARG E  1 192 ? -9.864  15.534  -11.220 1.00 54.60  ? 193  ARG E CA  1 
ATOM   9477  C C   . ARG E  1 192 ? -9.946  15.138  -9.747  1.00 64.54  ? 193  ARG E C   1 
ATOM   9478  O O   . ARG E  1 192 ? -10.917 15.493  -9.064  1.00 70.06  ? 193  ARG E O   1 
ATOM   9479  C CB  . ARG E  1 192 ? -10.668 14.554  -12.081 1.00 54.50  ? 193  ARG E CB  1 
ATOM   9480  C CG  . ARG E  1 192 ? -9.981  13.294  -12.508 1.00 55.09  ? 193  ARG E CG  1 
ATOM   9481  C CD  . ARG E  1 192 ? -11.015 12.300  -13.049 1.00 57.54  ? 193  ARG E CD  1 
ATOM   9482  N NE  . ARG E  1 192 ? -12.231 12.313  -12.229 1.00 66.30  ? 193  ARG E NE  1 
ATOM   9483  C CZ  . ARG E  1 192 ? -12.597 11.334  -11.398 1.00 68.28  ? 193  ARG E CZ  1 
ATOM   9484  N NH1 . ARG E  1 192 ? -11.852 10.240  -11.292 1.00 71.55  ? 193  ARG E NH1 1 
ATOM   9485  N NH2 . ARG E  1 192 ? -13.717 11.436  -10.682 1.00 57.84  ? 193  ARG E NH2 1 
ATOM   9486  N N   . LEU E  1 193 ? -8.934  14.426  -9.248  1.00 59.06  ? 194  LEU E N   1 
ATOM   9487  C CA  . LEU E  1 193 ? -8.969  13.965  -7.864  1.00 52.78  ? 194  LEU E CA  1 
ATOM   9488  C C   . LEU E  1 193 ? -8.300  14.958  -6.925  1.00 51.87  ? 194  LEU E C   1 
ATOM   9489  O O   . LEU E  1 193 ? -8.841  15.254  -5.858  1.00 57.13  ? 194  LEU E O   1 
ATOM   9490  C CB  . LEU E  1 193 ? -8.317  12.583  -7.704  1.00 47.36  ? 194  LEU E CB  1 
ATOM   9491  C CG  . LEU E  1 193 ? -9.060  11.311  -8.123  1.00 50.12  ? 194  LEU E CG  1 
ATOM   9492  C CD1 . LEU E  1 193 ? -9.515  11.352  -9.551  1.00 55.60  ? 194  LEU E CD1 1 
ATOM   9493  C CD2 . LEU E  1 193 ? -8.201  10.082  -7.898  1.00 48.30  ? 194  LEU E CD2 1 
ATOM   9494  N N   . TYR E  1 194 ? -7.163  15.518  -7.317  1.00 48.30  ? 195  TYR E N   1 
ATOM   9495  C CA  . TYR E  1 194 ? -6.377  16.285  -6.354  1.00 51.43  ? 195  TYR E CA  1 
ATOM   9496  C C   . TYR E  1 194 ? -6.051  17.700  -6.828  1.00 51.99  ? 195  TYR E C   1 
ATOM   9497  O O   . TYR E  1 194 ? -5.503  18.509  -6.066  1.00 51.65  ? 195  TYR E O   1 
ATOM   9498  C CB  . TYR E  1 194 ? -5.075  15.532  -6.052  1.00 45.45  ? 195  TYR E CB  1 
ATOM   9499  C CG  . TYR E  1 194 ? -5.249  14.045  -5.859  1.00 41.68  ? 195  TYR E CG  1 
ATOM   9500  C CD1 . TYR E  1 194 ? -5.797  13.521  -4.699  1.00 42.39  ? 195  TYR E CD1 1 
ATOM   9501  C CD2 . TYR E  1 194 ? -4.898  13.164  -6.863  1.00 47.14  ? 195  TYR E CD2 1 
ATOM   9502  C CE1 . TYR E  1 194 ? -5.952  12.145  -4.539  1.00 40.09  ? 195  TYR E CE1 1 
ATOM   9503  C CE2 . TYR E  1 194 ? -5.062  11.801  -6.715  1.00 46.94  ? 195  TYR E CE2 1 
ATOM   9504  C CZ  . TYR E  1 194 ? -5.588  11.294  -5.554  1.00 40.65  ? 195  TYR E CZ  1 
ATOM   9505  O OH  . TYR E  1 194 ? -5.737  9.927   -5.444  1.00 40.47  ? 195  TYR E OH  1 
ATOM   9506  N N   . GLN E  1 195 ? -6.421  17.990  -8.074  1.00 56.97  ? 196  GLN E N   1 
ATOM   9507  C CA  . GLN E  1 195 ? -6.291  19.321  -8.690  1.00 59.78  ? 196  GLN E CA  1 
ATOM   9508  C C   . GLN E  1 195 ? -4.843  19.736  -8.994  1.00 60.63  ? 196  GLN E C   1 
ATOM   9509  O O   . GLN E  1 195 ? -4.520  20.022  -10.154 1.00 62.62  ? 196  GLN E O   1 
ATOM   9510  C CB  . GLN E  1 195 ? -6.966  20.389  -7.810  1.00 62.68  ? 196  GLN E CB  1 
ATOM   9511  C CG  . GLN E  1 195 ? -7.089  21.769  -8.448  1.00 63.78  ? 196  GLN E CG  1 
ATOM   9512  C CD  . GLN E  1 195 ? -8.047  21.785  -9.635  1.00 68.76  ? 196  GLN E CD  1 
ATOM   9513  O OE1 . GLN E  1 195 ? -9.098  21.133  -9.615  1.00 71.24  ? 196  GLN E OE1 1 
ATOM   9514  N NE2 . GLN E  1 195 ? -7.684  22.530  -10.680 1.00 71.39  ? 196  GLN E NE2 1 
ATOM   9515  N N   . ASN E  1 196 ? -3.960  19.731  -7.992  1.00 59.09  ? 197  ASN E N   1 
ATOM   9516  C CA  . ASN E  1 196 ? -2.559  20.107  -8.234  1.00 56.34  ? 197  ASN E CA  1 
ATOM   9517  C C   . ASN E  1 196 ? -1.762  19.066  -9.033  1.00 54.98  ? 197  ASN E C   1 
ATOM   9518  O O   . ASN E  1 196 ? -1.807  17.867  -8.746  1.00 54.18  ? 197  ASN E O   1 
ATOM   9519  C CB  . ASN E  1 196 ? -1.837  20.391  -6.915  1.00 58.58  ? 197  ASN E CB  1 
ATOM   9520  C CG  . ASN E  1 196 ? -2.650  21.250  -5.975  1.00 53.00  ? 197  ASN E CG  1 
ATOM   9521  O OD1 . ASN E  1 196 ? -3.453  22.072  -6.410  1.00 59.57  ? 197  ASN E OD1 1 
ATOM   9522  N ND2 . ASN E  1 196 ? -2.421  21.086  -4.681  1.00 46.06  ? 197  ASN E ND2 1 
ATOM   9523  N N   . PRO E  1 197 ? -0.999  19.543  -10.033 1.00 60.34  ? 198  PRO E N   1 
ATOM   9524  C CA  . PRO E  1 197 ? -0.279  18.637  -10.936 1.00 58.56  ? 198  PRO E CA  1 
ATOM   9525  C C   . PRO E  1 197 ? 0.972   18.036  -10.314 1.00 50.03  ? 198  PRO E C   1 
ATOM   9526  O O   . PRO E  1 197 ? 1.293   16.911  -10.656 1.00 44.93  ? 198  PRO E O   1 
ATOM   9527  C CB  . PRO E  1 197 ? 0.105   19.558  -12.102 1.00 54.40  ? 198  PRO E CB  1 
ATOM   9528  C CG  . PRO E  1 197 ? 0.264   20.913  -11.449 1.00 44.21  ? 198  PRO E CG  1 
ATOM   9529  C CD  . PRO E  1 197 ? -0.767  20.966  -10.364 1.00 48.52  ? 198  PRO E CD  1 
ATOM   9530  N N   . THR E  1 198 ? 1.626   18.766  -9.405  1.00 50.00  ? 199  THR E N   1 
ATOM   9531  C CA  . THR E  1 198 ? 2.886   18.340  -8.785  1.00 53.06  ? 199  THR E CA  1 
ATOM   9532  C C   . THR E  1 198 ? 2.809   18.283  -7.246  1.00 51.33  ? 199  THR E C   1 
ATOM   9533  O O   . THR E  1 198 ? 2.822   19.316  -6.565  1.00 53.17  ? 199  THR E O   1 
ATOM   9534  C CB  . THR E  1 198 ? 4.063   19.275  -9.193  1.00 55.13  ? 199  THR E CB  1 
ATOM   9535  O OG1 . THR E  1 198 ? 4.213   19.271  -10.618 1.00 55.72  ? 199  THR E OG1 1 
ATOM   9536  C CG2 . THR E  1 198 ? 5.375   18.812  -8.566  1.00 50.81  ? 199  THR E CG2 1 
ATOM   9537  N N   . THR E  1 199 ? 2.769   17.068  -6.706  1.00 50.85  ? 200  THR E N   1 
ATOM   9538  C CA  . THR E  1 199 ? 2.491   16.855  -5.287  1.00 48.87  ? 200  THR E CA  1 
ATOM   9539  C C   . THR E  1 199 ? 3.591   16.070  -4.574  1.00 48.31  ? 200  THR E C   1 
ATOM   9540  O O   . THR E  1 199 ? 4.468   15.487  -5.211  1.00 47.94  ? 200  THR E O   1 
ATOM   9541  C CB  . THR E  1 199 ? 1.190   16.097  -5.101  1.00 46.51  ? 200  THR E CB  1 
ATOM   9542  O OG1 . THR E  1 199 ? 1.278   14.853  -5.811  1.00 48.63  ? 200  THR E OG1 1 
ATOM   9543  C CG2 . THR E  1 199 ? 0.033   16.904  -5.650  1.00 47.88  ? 200  THR E CG2 1 
ATOM   9544  N N   . TYR E  1 200 ? 3.504   16.043  -3.248  1.00 47.15  ? 201  TYR E N   1 
ATOM   9545  C CA  . TYR E  1 200 ? 4.483   15.394  -2.383  1.00 43.22  ? 201  TYR E CA  1 
ATOM   9546  C C   . TYR E  1 200 ? 3.836   15.054  -1.047  1.00 44.32  ? 201  TYR E C   1 
ATOM   9547  O O   . TYR E  1 200 ? 2.816   15.635  -0.678  1.00 45.49  ? 201  TYR E O   1 
ATOM   9548  C CB  . TYR E  1 200 ? 5.686   16.302  -2.155  1.00 47.82  ? 201  TYR E CB  1 
ATOM   9549  C CG  . TYR E  1 200 ? 5.361   17.489  -1.264  1.00 48.78  ? 201  TYR E CG  1 
ATOM   9550  C CD1 . TYR E  1 200 ? 4.790   18.644  -1.804  1.00 42.83  ? 201  TYR E CD1 1 
ATOM   9551  C CD2 . TYR E  1 200 ? 5.630   17.463  0.110   1.00 45.14  ? 201  TYR E CD2 1 
ATOM   9552  C CE1 . TYR E  1 200 ? 4.484   19.731  -1.016  1.00 41.70  ? 201  TYR E CE1 1 
ATOM   9553  C CE2 . TYR E  1 200 ? 5.332   18.562  0.914   1.00 41.02  ? 201  TYR E CE2 1 
ATOM   9554  C CZ  . TYR E  1 200 ? 4.756   19.686  0.339   1.00 43.82  ? 201  TYR E CZ  1 
ATOM   9555  O OH  . TYR E  1 200 ? 4.444   20.773  1.109   1.00 47.38  ? 201  TYR E OH  1 
ATOM   9556  N N   . ILE E  1 201 ? 4.456   14.150  -0.298  1.00 45.21  ? 202  ILE E N   1 
ATOM   9557  C CA  . ILE E  1 201 ? 4.031   13.846  1.070   1.00 37.26  ? 202  ILE E CA  1 
ATOM   9558  C C   . ILE E  1 201 ? 5.248   13.845  1.987   1.00 36.87  ? 202  ILE E C   1 
ATOM   9559  O O   . ILE E  1 201 ? 6.188   13.098  1.742   1.00 35.53  ? 202  ILE E O   1 
ATOM   9560  C CB  . ILE E  1 201 ? 3.355   12.462  1.136   1.00 32.01  ? 202  ILE E CB  1 
ATOM   9561  C CG1 . ILE E  1 201 ? 2.182   12.383  0.177   1.00 30.53  ? 202  ILE E CG1 1 
ATOM   9562  C CG2 . ILE E  1 201 ? 2.929   12.130  2.544   1.00 32.23  ? 202  ILE E CG2 1 
ATOM   9563  C CD1 . ILE E  1 201 ? 1.598   11.016  0.087   1.00 35.23  ? 202  ILE E CD1 1 
ATOM   9564  N N   . SER E  1 202 ? 5.246   14.652  3.042   1.00 36.00  ? 203  SER E N   1 
ATOM   9565  C CA  . SER E  1 202 ? 6.347   14.597  4.009   1.00 39.15  ? 203  SER E CA  1 
ATOM   9566  C C   . SER E  1 202 ? 5.900   13.973  5.325   1.00 42.11  ? 203  SER E C   1 
ATOM   9567  O O   . SER E  1 202 ? 4.812   14.266  5.812   1.00 43.29  ? 203  SER E O   1 
ATOM   9568  C CB  . SER E  1 202 ? 6.936   15.977  4.296   1.00 38.60  ? 203  SER E CB  1 
ATOM   9569  O OG  . SER E  1 202 ? 7.921   16.315  3.350   1.00 40.01  ? 203  SER E OG  1 
ATOM   9570  N N   . VAL E  1 203 ? 6.741   13.107  5.887   1.00 36.53  ? 204  VAL E N   1 
ATOM   9571  C CA  . VAL E  1 203 ? 6.476   12.497  7.191   1.00 35.47  ? 204  VAL E CA  1 
ATOM   9572  C C   . VAL E  1 203 ? 7.723   12.583  8.079   1.00 39.41  ? 204  VAL E C   1 
ATOM   9573  O O   . VAL E  1 203 ? 8.813   12.189  7.655   1.00 39.37  ? 204  VAL E O   1 
ATOM   9574  C CB  . VAL E  1 203 ? 6.025   11.033  7.043   1.00 34.32  ? 204  VAL E CB  1 
ATOM   9575  C CG1 . VAL E  1 203 ? 5.690   10.421  8.392   1.00 38.00  ? 204  VAL E CG1 1 
ATOM   9576  C CG2 . VAL E  1 203 ? 4.847   10.925  6.100   1.00 36.06  ? 204  VAL E CG2 1 
ATOM   9577  N N   . GLY E  1 204 ? 7.566   13.125  9.292   1.00 36.52  ? 205  GLY E N   1 
ATOM   9578  C CA  . GLY E  1 204 ? 8.677   13.312  10.214  1.00 38.85  ? 205  GLY E CA  1 
ATOM   9579  C C   . GLY E  1 204 ? 8.420   12.854  11.647  1.00 43.15  ? 205  GLY E C   1 
ATOM   9580  O O   . GLY E  1 204 ? 7.307   12.958  12.170  1.00 45.51  ? 205  GLY E O   1 
ATOM   9581  N N   . THR E  1 205 ? 9.479   12.393  12.301  1.00 44.40  ? 206  THR E N   1 
ATOM   9582  C CA  . THR E  1 205 ? 9.409   11.781  13.630  1.00 42.82  ? 206  THR E CA  1 
ATOM   9583  C C   . THR E  1 205 ? 10.732  12.149  14.310  1.00 44.76  ? 206  THR E C   1 
ATOM   9584  O O   . THR E  1 205 ? 11.514  12.900  13.742  1.00 54.65  ? 206  THR E O   1 
ATOM   9585  C CB  . THR E  1 205 ? 9.122   10.227  13.483  1.00 44.06  ? 206  THR E CB  1 
ATOM   9586  O OG1 . THR E  1 205 ? 7.852   9.904   14.056  1.00 47.43  ? 206  THR E OG1 1 
ATOM   9587  C CG2 . THR E  1 205 ? 10.187  9.312   14.059  1.00 43.08  ? 206  THR E CG2 1 
ATOM   9588  N N   . SER E  1 206 ? 10.980  11.728  15.534  1.00 47.14  ? 207  SER E N   1 
ATOM   9589  C CA  . SER E  1 206 ? 12.306  11.948  16.114  1.00 48.02  ? 207  SER E CA  1 
ATOM   9590  C C   . SER E  1 206 ? 13.435  11.181  15.395  1.00 45.42  ? 207  SER E C   1 
ATOM   9591  O O   . SER E  1 206 ? 14.591  11.577  15.465  1.00 50.17  ? 207  SER E O   1 
ATOM   9592  C CB  . SER E  1 206 ? 12.278  11.604  17.600  1.00 48.15  ? 207  SER E CB  1 
ATOM   9593  O OG  . SER E  1 206 ? 11.962  10.243  17.781  1.00 48.64  ? 207  SER E OG  1 
ATOM   9594  N N   . THR E  1 207 ? 13.089  10.095  14.704  1.00 45.27  ? 208  THR E N   1 
ATOM   9595  C CA  . THR E  1 207 ? 14.049  9.244   13.991  1.00 42.07  ? 208  THR E CA  1 
ATOM   9596  C C   . THR E  1 207 ? 13.799  9.130   12.493  1.00 45.14  ? 208  THR E C   1 
ATOM   9597  O O   . THR E  1 207 ? 14.687  8.694   11.760  1.00 41.83  ? 208  THR E O   1 
ATOM   9598  C CB  . THR E  1 207 ? 14.031  7.785   14.526  1.00 43.32  ? 208  THR E CB  1 
ATOM   9599  O OG1 . THR E  1 207 ? 12.724  7.244   14.340  1.00 43.14  ? 208  THR E OG1 1 
ATOM   9600  C CG2 . THR E  1 207 ? 14.340  7.722   15.992  1.00 41.23  ? 208  THR E CG2 1 
ATOM   9601  N N   . LEU E  1 208 ? 12.582  9.467   12.056  1.00 45.53  ? 209  LEU E N   1 
ATOM   9602  C CA  . LEU E  1 208 ? 12.160  9.337   10.650  1.00 39.71  ? 209  LEU E CA  1 
ATOM   9603  C C   . LEU E  1 208 ? 12.165  10.675  9.901   1.00 42.09  ? 209  LEU E C   1 
ATOM   9604  O O   . LEU E  1 208 ? 11.723  11.691  10.446  1.00 48.42  ? 209  LEU E O   1 
ATOM   9605  C CB  . LEU E  1 208 ? 10.765  8.687   10.572  1.00 36.42  ? 209  LEU E CB  1 
ATOM   9606  C CG  . LEU E  1 208 ? 10.133  8.595   9.174   1.00 40.81  ? 209  LEU E CG  1 
ATOM   9607  C CD1 . LEU E  1 208 ? 10.912  7.641   8.303   1.00 35.73  ? 209  LEU E CD1 1 
ATOM   9608  C CD2 . LEU E  1 208 ? 8.652   8.156   9.200   1.00 37.76  ? 209  LEU E CD2 1 
ATOM   9609  N N   . ASN E  1 209 ? 12.682  10.681  8.671   1.00 37.41  ? 210  ASN E N   1 
ATOM   9610  C CA  . ASN E  1 209 ? 12.699  11.874  7.820   1.00 36.50  ? 210  ASN E CA  1 
ATOM   9611  C C   . ASN E  1 209 ? 12.391  11.442  6.381   1.00 40.12  ? 210  ASN E C   1 
ATOM   9612  O O   . ASN E  1 209 ? 13.307  11.201  5.598   1.00 48.71  ? 210  ASN E O   1 
ATOM   9613  C CB  . ASN E  1 209 ? 14.063  12.592  7.930   1.00 42.19  ? 210  ASN E CB  1 
ATOM   9614  C CG  . ASN E  1 209 ? 14.121  13.948  7.176   1.00 42.69  ? 210  ASN E CG  1 
ATOM   9615  O OD1 . ASN E  1 209 ? 13.098  14.532  6.808   1.00 44.21  ? 210  ASN E OD1 1 
ATOM   9616  N ND2 . ASN E  1 209 ? 15.335  14.472  7.011   1.00 41.14  ? 210  ASN E ND2 1 
ATOM   9617  N N   . GLN E  1 210 ? 11.103  11.311  6.055   1.00 37.89  ? 211  GLN E N   1 
ATOM   9618  C CA  . GLN E  1 210 ? 10.630  10.712  4.792   1.00 34.32  ? 211  GLN E CA  1 
ATOM   9619  C C   . GLN E  1 210 ? 9.986   11.707  3.811   1.00 37.58  ? 211  GLN E C   1 
ATOM   9620  O O   . GLN E  1 210 ? 9.354   12.683  4.230   1.00 39.71  ? 211  GLN E O   1 
ATOM   9621  C CB  . GLN E  1 210 ? 9.642   9.604   5.110   1.00 34.59  ? 211  GLN E CB  1 
ATOM   9622  C CG  . GLN E  1 210 ? 8.835   9.091   3.941   1.00 38.55  ? 211  GLN E CG  1 
ATOM   9623  C CD  . GLN E  1 210 ? 7.883   7.981   4.356   1.00 38.66  ? 211  GLN E CD  1 
ATOM   9624  O OE1 . GLN E  1 210 ? 6.668   8.160   4.369   1.00 38.22  ? 211  GLN E OE1 1 
ATOM   9625  N NE2 . GLN E  1 210 ? 8.435   6.811   4.654   1.00 41.41  ? 211  GLN E NE2 1 
ATOM   9626  N N   . LYS E  1 211 ? 10.167  11.475  2.509   1.00 39.55  ? 212  LYS E N   1 
ATOM   9627  C CA  . LYS E  1 211 ? 9.526   12.299  1.479   1.00 36.53  ? 212  LYS E CA  1 
ATOM   9628  C C   . LYS E  1 211 ? 9.071   11.479  0.271   1.00 35.44  ? 212  LYS E C   1 
ATOM   9629  O O   . LYS E  1 211 ? 9.887   10.871  -0.405  1.00 42.67  ? 212  LYS E O   1 
ATOM   9630  C CB  . LYS E  1 211 ? 10.470  13.411  1.022   1.00 36.48  ? 212  LYS E CB  1 
ATOM   9631  C CG  . LYS E  1 211 ? 9.873   14.293  -0.081  1.00 40.01  ? 212  LYS E CG  1 
ATOM   9632  C CD  . LYS E  1 211 ? 10.247  15.745  0.119   1.00 36.06  ? 212  LYS E CD  1 
ATOM   9633  C CE  . LYS E  1 211 ? 9.598   16.639  -0.908  1.00 46.08  ? 212  LYS E CE  1 
ATOM   9634  N NZ  . LYS E  1 211 ? 10.011  18.061  -0.698  1.00 61.77  ? 212  LYS E NZ  1 
ATOM   9635  N N   . LEU E  1 212 ? 7.772   11.473  -0.007  1.00 34.88  ? 213  LEU E N   1 
ATOM   9636  C CA  . LEU E  1 212 ? 7.232   10.672  -1.104  1.00 36.91  ? 213  LEU E CA  1 
ATOM   9637  C C   . LEU E  1 212 ? 6.709   11.560  -2.248  1.00 40.98  ? 213  LEU E C   1 
ATOM   9638  O O   . LEU E  1 212 ? 6.190   12.658  -2.020  1.00 42.49  ? 213  LEU E O   1 
ATOM   9639  C CB  . LEU E  1 212 ? 6.117   9.754   -0.600  1.00 33.86  ? 213  LEU E CB  1 
ATOM   9640  C CG  . LEU E  1 212 ? 6.443   8.950   0.668   1.00 37.54  ? 213  LEU E CG  1 
ATOM   9641  C CD1 . LEU E  1 212 ? 5.232   8.160   1.209   1.00 37.10  ? 213  LEU E CD1 1 
ATOM   9642  C CD2 . LEU E  1 212 ? 7.633   8.048   0.469   1.00 40.38  ? 213  LEU E CD2 1 
ATOM   9643  N N   . VAL E  1 213 ? 6.873   11.089  -3.480  1.00 37.64  ? 214  VAL E N   1 
ATOM   9644  C CA  . VAL E  1 213 ? 6.388   11.806  -4.661  1.00 37.85  ? 214  VAL E CA  1 
ATOM   9645  C C   . VAL E  1 213 ? 5.701   10.768  -5.548  1.00 38.16  ? 214  VAL E C   1 
ATOM   9646  O O   . VAL E  1 213 ? 6.194   9.637   -5.667  1.00 38.35  ? 214  VAL E O   1 
ATOM   9647  C CB  . VAL E  1 213 ? 7.533   12.529  -5.402  1.00 37.25  ? 214  VAL E CB  1 
ATOM   9648  C CG1 . VAL E  1 213 ? 7.015   13.242  -6.612  1.00 33.58  ? 214  VAL E CG1 1 
ATOM   9649  C CG2 . VAL E  1 213 ? 8.216   13.529  -4.469  1.00 38.74  ? 214  VAL E CG2 1 
ATOM   9650  N N   . PRO E  1 214 ? 4.505   11.097  -6.078  1.00 37.13  ? 215  PRO E N   1 
ATOM   9651  C CA  . PRO E  1 214 ? 3.734   10.135  -6.894  1.00 34.96  ? 215  PRO E CA  1 
ATOM   9652  C C   . PRO E  1 214 ? 4.401   9.804   -8.245  1.00 37.89  ? 215  PRO E C   1 
ATOM   9653  O O   . PRO E  1 214 ? 5.022   10.664  -8.884  1.00 33.83  ? 215  PRO E O   1 
ATOM   9654  C CB  . PRO E  1 214 ? 2.404   10.857  -7.146  1.00 34.02  ? 215  PRO E CB  1 
ATOM   9655  C CG  . PRO E  1 214 ? 2.357   11.982  -6.169  1.00 40.39  ? 215  PRO E CG  1 
ATOM   9656  C CD  . PRO E  1 214 ? 3.784   12.372  -5.898  1.00 36.94  ? 215  PRO E CD  1 
ATOM   9657  N N   . LYS E  1 215 ? 4.202   8.580   -8.705  1.00 34.73  ? 216  LYS E N   1 
ATOM   9658  C CA  . LYS E  1 215 ? 4.698   8.180   -10.001 1.00 37.19  ? 216  LYS E CA  1 
ATOM   9659  C C   . LYS E  1 215 ? 3.530   7.976   -11.001 1.00 41.68  ? 216  LYS E C   1 
ATOM   9660  O O   . LYS E  1 215 ? 2.892   6.921   -11.039 1.00 38.22  ? 216  LYS E O   1 
ATOM   9661  C CB  . LYS E  1 215 ? 5.535   6.916   -9.839  1.00 29.65  ? 216  LYS E CB  1 
ATOM   9662  C CG  . LYS E  1 215 ? 6.796   7.164   -9.059  1.00 30.04  ? 216  LYS E CG  1 
ATOM   9663  C CD  . LYS E  1 215 ? 7.612   5.895   -8.973  1.00 35.65  ? 216  LYS E CD  1 
ATOM   9664  C CE  . LYS E  1 215 ? 7.658   5.366   -7.540  1.00 40.90  ? 216  LYS E CE  1 
ATOM   9665  N NZ  . LYS E  1 215 ? 8.062   3.909   -7.466  1.00 42.08  ? 216  LYS E NZ  1 
ATOM   9666  N N   . ILE E  1 216 ? 3.304   8.972   -11.854 1.00 41.64  ? 217  ILE E N   1 
ATOM   9667  C CA  . ILE E  1 216 ? 2.159   8.955   -12.765 1.00 42.71  ? 217  ILE E CA  1 
ATOM   9668  C C   . ILE E  1 216 ? 2.603   8.263   -14.053 1.00 45.51  ? 217  ILE E C   1 
ATOM   9669  O O   . ILE E  1 216 ? 3.562   8.721   -14.691 1.00 55.99  ? 217  ILE E O   1 
ATOM   9670  C CB  . ILE E  1 216 ? 1.656   10.387  -13.065 1.00 43.57  ? 217  ILE E CB  1 
ATOM   9671  C CG1 . ILE E  1 216 ? 1.402   11.148  -11.763 1.00 42.87  ? 217  ILE E CG1 1 
ATOM   9672  C CG2 . ILE E  1 216 ? 0.424   10.351  -13.946 1.00 47.72  ? 217  ILE E CG2 1 
ATOM   9673  C CD1 . ILE E  1 216 ? 1.008   12.598  -11.919 1.00 40.21  ? 217  ILE E CD1 1 
ATOM   9674  N N   . ALA E  1 217 ? 1.961   7.141   -14.402 1.00 44.35  ? 218  ALA E N   1 
ATOM   9675  C CA  . ALA E  1 217 ? 2.439   6.276   -15.502 1.00 50.20  ? 218  ALA E CA  1 
ATOM   9676  C C   . ALA E  1 217 ? 1.437   5.198   -15.988 1.00 52.57  ? 218  ALA E C   1 
ATOM   9677  O O   . ALA E  1 217 ? 0.357   5.022   -15.419 1.00 53.66  ? 218  ALA E O   1 
ATOM   9678  C CB  . ALA E  1 217 ? 3.761   5.594   -15.084 1.00 46.95  ? 218  ALA E CB  1 
ATOM   9679  N N   . THR E  1 218 ? 1.855   4.441   -17.004 1.00 51.48  ? 219  THR E N   1 
ATOM   9680  C CA  . THR E  1 218 ? 1.012   3.479   -17.711 1.00 43.34  ? 219  THR E CA  1 
ATOM   9681  C C   . THR E  1 218 ? 1.312   2.036   -17.271 1.00 47.91  ? 219  THR E C   1 
ATOM   9682  O O   . THR E  1 218 ? 2.413   1.531   -17.511 1.00 47.55  ? 219  THR E O   1 
ATOM   9683  C CB  . THR E  1 218 ? 1.259   3.628   -19.255 1.00 46.56  ? 219  THR E CB  1 
ATOM   9684  O OG1 . THR E  1 218 ? 0.932   4.959   -19.673 1.00 58.85  ? 219  THR E OG1 1 
ATOM   9685  C CG2 . THR E  1 218 ? 0.476   2.616   -20.096 1.00 40.26  ? 219  THR E CG2 1 
ATOM   9686  N N   . ARG E  1 219 ? 0.318   1.344   -16.699 1.00 46.82  ? 220  ARG E N   1 
ATOM   9687  C CA  . ARG E  1 219 ? 0.541   -0.015  -16.186 1.00 44.52  ? 220  ARG E CA  1 
ATOM   9688  C C   . ARG E  1 219 ? -0.589  -0.943  -16.572 1.00 46.40  ? 220  ARG E C   1 
ATOM   9689  O O   . ARG E  1 219 ? -1.700  -0.494  -16.851 1.00 46.97  ? 220  ARG E O   1 
ATOM   9690  C CB  . ARG E  1 219 ? 0.661   -0.047  -14.643 1.00 47.96  ? 220  ARG E CB  1 
ATOM   9691  C CG  . ARG E  1 219 ? 1.446   1.069   -14.014 1.00 45.78  ? 220  ARG E CG  1 
ATOM   9692  C CD  . ARG E  1 219 ? 1.153   1.276   -12.513 1.00 44.44  ? 220  ARG E CD  1 
ATOM   9693  N NE  . ARG E  1 219 ? 1.751   2.555   -12.159 1.00 40.77  ? 220  ARG E NE  1 
ATOM   9694  C CZ  . ARG E  1 219 ? 1.071   3.659   -11.902 1.00 39.95  ? 220  ARG E CZ  1 
ATOM   9695  N NH1 . ARG E  1 219 ? -0.259  3.622   -11.867 1.00 45.46  ? 220  ARG E NH1 1 
ATOM   9696  N NH2 . ARG E  1 219 ? 1.726   4.789   -11.660 1.00 32.71  ? 220  ARG E NH2 1 
ATOM   9697  N N   . SER E  1 220 ? -0.308  -2.240  -16.466 1.00 45.28  ? 221  SER E N   1 
ATOM   9698  C CA  . SER E  1 220 ? -1.289  -3.291  -16.655 1.00 49.95  ? 221  SER E CA  1 
ATOM   9699  C C   . SER E  1 220 ? -2.491  -3.087  -15.718 1.00 56.42  ? 221  SER E C   1 
ATOM   9700  O O   . SER E  1 220 ? -2.387  -2.382  -14.708 1.00 56.71  ? 221  SER E O   1 
ATOM   9701  C CB  . SER E  1 220 ? -0.659  -4.662  -16.355 1.00 51.43  ? 221  SER E CB  1 
ATOM   9702  O OG  . SER E  1 220 ? 0.577   -4.861  -17.018 1.00 46.52  ? 221  SER E OG  1 
ATOM   9703  N N   . LYS E  1 221 ? -3.631  -3.683  -16.063 1.00 60.17  ? 222  LYS E N   1 
ATOM   9704  C CA  . LYS E  1 221 ? -4.821  -3.640  -15.206 1.00 57.65  ? 222  LYS E CA  1 
ATOM   9705  C C   . LYS E  1 221 ? -4.770  -4.818  -14.244 1.00 54.70  ? 222  LYS E C   1 
ATOM   9706  O O   . LYS E  1 221 ? -4.521  -5.944  -14.670 1.00 54.64  ? 222  LYS E O   1 
ATOM   9707  C CB  . LYS E  1 221 ? -6.123  -3.705  -16.020 1.00 57.06  ? 222  LYS E CB  1 
ATOM   9708  C CG  . LYS E  1 221 ? -6.402  -2.566  -16.983 1.00 59.87  ? 222  LYS E CG  1 
ATOM   9709  C CD  . LYS E  1 221 ? -7.901  -2.469  -17.276 1.00 64.08  ? 222  LYS E CD  1 
ATOM   9710  C CE  . LYS E  1 221 ? -8.237  -1.265  -18.154 1.00 65.46  ? 222  LYS E CE  1 
ATOM   9711  N NZ  . LYS E  1 221 ? -9.704  -0.993  -18.225 1.00 59.61  ? 222  LYS E NZ  1 
ATOM   9712  N N   . VAL E  1 222 ? -4.993  -4.554  -12.957 1.00 51.83  ? 223  VAL E N   1 
ATOM   9713  C CA  . VAL E  1 222 ? -5.118  -5.617  -11.957 1.00 52.38  ? 223  VAL E CA  1 
ATOM   9714  C C   . VAL E  1 222 ? -6.466  -5.459  -11.277 1.00 56.43  ? 223  VAL E C   1 
ATOM   9715  O O   . VAL E  1 222 ? -6.749  -4.392  -10.715 1.00 60.05  ? 223  VAL E O   1 
ATOM   9716  C CB  . VAL E  1 222 ? -3.997  -5.590  -10.900 1.00 53.03  ? 223  VAL E CB  1 
ATOM   9717  C CG1 . VAL E  1 222 ? -4.174  -6.743  -9.924  1.00 55.63  ? 223  VAL E CG1 1 
ATOM   9718  C CG2 . VAL E  1 222 ? -2.628  -5.666  -11.557 1.00 53.53  ? 223  VAL E CG2 1 
ATOM   9719  N N   . LYS E  1 223 ? -7.299  -6.502  -11.347 1.00 56.70  ? 224  LYS E N   1 
ATOM   9720  C CA  . LYS E  1 223 ? -8.709  -6.422  -10.920 1.00 66.48  ? 224  LYS E CA  1 
ATOM   9721  C C   . LYS E  1 223 ? -9.437  -5.246  -11.590 1.00 64.84  ? 224  LYS E C   1 
ATOM   9722  O O   . LYS E  1 223 ? -10.251 -4.570  -10.954 1.00 67.26  ? 224  LYS E O   1 
ATOM   9723  C CB  . LYS E  1 223 ? -8.843  -6.267  -9.394  1.00 65.25  ? 224  LYS E CB  1 
ATOM   9724  C CG  . LYS E  1 223 ? -8.366  -7.440  -8.565  1.00 67.16  ? 224  LYS E CG  1 
ATOM   9725  C CD  . LYS E  1 223 ? -8.408  -7.070  -7.093  1.00 69.07  ? 224  LYS E CD  1 
ATOM   9726  C CE  . LYS E  1 223 ? -9.818  -6.592  -6.705  1.00 69.09  ? 224  LYS E CE  1 
ATOM   9727  N NZ  . LYS E  1 223 ? -10.033 -6.332  -5.243  1.00 53.94  ? 224  LYS E NZ  1 
ATOM   9728  N N   . GLY E  1 224 ? -9.123  -4.998  -12.860 1.00 62.05  ? 225  GLY E N   1 
ATOM   9729  C CA  . GLY E  1 224 ? -9.759  -3.947  -13.640 1.00 62.52  ? 225  GLY E CA  1 
ATOM   9730  C C   . GLY E  1 224 ? -9.171  -2.561  -13.452 1.00 59.87  ? 225  GLY E C   1 
ATOM   9731  O O   . GLY E  1 224 ? -9.604  -1.612  -14.113 1.00 64.01  ? 225  GLY E O   1 
ATOM   9732  N N   . LEU E  1 225 ? -8.195  -2.441  -12.553 1.00 56.67  ? 226  LEU E N   1 
ATOM   9733  C CA  . LEU E  1 225 ? -7.551  -1.153  -12.283 1.00 60.89  ? 226  LEU E CA  1 
ATOM   9734  C C   . LEU E  1 225 ? -6.054  -1.162  -12.606 1.00 58.26  ? 226  LEU E C   1 
ATOM   9735  O O   . LEU E  1 225 ? -5.363  -2.175  -12.442 1.00 53.80  ? 226  LEU E O   1 
ATOM   9736  C CB  . LEU E  1 225 ? -7.733  -0.726  -10.821 1.00 62.35  ? 226  LEU E CB  1 
ATOM   9737  C CG  . LEU E  1 225 ? -9.122  -0.467  -10.246 1.00 63.13  ? 226  LEU E CG  1 
ATOM   9738  C CD1 . LEU E  1 225 ? -9.764  -1.775  -9.850  1.00 65.04  ? 226  LEU E CD1 1 
ATOM   9739  C CD2 . LEU E  1 225 ? -9.033  0.477   -9.049  1.00 56.01  ? 226  LEU E CD2 1 
ATOM   9740  N N   . SER E  1 226 ? -5.558  -0.009  -13.037 1.00 50.26  ? 227  SER E N   1 
ATOM   9741  C CA  . SER E  1 226 ? -4.147  0.148   -13.317 1.00 49.66  ? 227  SER E CA  1 
ATOM   9742  C C   . SER E  1 226 ? -3.552  1.197   -12.391 1.00 49.18  ? 227  SER E C   1 
ATOM   9743  O O   . SER E  1 226 ? -2.376  1.540   -12.509 1.00 48.89  ? 227  SER E O   1 
ATOM   9744  C CB  . SER E  1 226 ? -3.918  0.501   -14.788 1.00 52.57  ? 227  SER E CB  1 
ATOM   9745  O OG  . SER E  1 226 ? -4.587  1.695   -15.120 1.00 60.25  ? 227  SER E OG  1 
ATOM   9746  N N   . GLY E  1 227 ? -4.372  1.727   -11.484 1.00 50.54  ? 228  GLY E N   1 
ATOM   9747  C CA  . GLY E  1 227 ? -3.884  2.693   -10.515 1.00 45.35  ? 228  GLY E CA  1 
ATOM   9748  C C   . GLY E  1 227 ? -3.182  1.930   -9.409  1.00 41.77  ? 228  GLY E C   1 
ATOM   9749  O O   . GLY E  1 227 ? -3.328  0.713   -9.315  1.00 43.97  ? 228  GLY E O   1 
ATOM   9750  N N   . ARG E  1 228 ? -2.385  2.608   -8.591  1.00 40.65  ? 229  ARG E N   1 
ATOM   9751  C CA  . ARG E  1 228 ? -1.686  1.875   -7.525  1.00 47.45  ? 229  ARG E CA  1 
ATOM   9752  C C   . ARG E  1 228 ? -1.683  2.561   -6.183  1.00 37.94  ? 229  ARG E C   1 
ATOM   9753  O O   . ARG E  1 228 ? -1.651  3.788   -6.108  1.00 41.05  ? 229  ARG E O   1 
ATOM   9754  C CB  . ARG E  1 228 ? -0.231  1.604   -7.916  1.00 45.56  ? 229  ARG E CB  1 
ATOM   9755  C CG  . ARG E  1 228 ? -0.078  0.726   -9.111  1.00 40.83  ? 229  ARG E CG  1 
ATOM   9756  C CD  . ARG E  1 228 ? -0.578  -0.634  -8.808  1.00 36.60  ? 229  ARG E CD  1 
ATOM   9757  N NE  . ARG E  1 228 ? -0.241  -1.510  -9.907  1.00 47.71  ? 229  ARG E NE  1 
ATOM   9758  C CZ  . ARG E  1 228 ? -1.077  -1.781  -10.895 1.00 50.40  ? 229  ARG E CZ  1 
ATOM   9759  N NH1 . ARG E  1 228 ? -2.285  -1.219  -10.894 1.00 45.81  ? 229  ARG E NH1 1 
ATOM   9760  N NH2 . ARG E  1 228 ? -0.703  -2.601  -11.875 1.00 50.35  ? 229  ARG E NH2 1 
ATOM   9761  N N   . MET E  1 229 ? -1.658  1.756   -5.126  1.00 39.17  ? 230  MET E N   1 
ATOM   9762  C CA  . MET E  1 229 ? -1.523  2.299   -3.761  1.00 46.32  ? 230  MET E CA  1 
ATOM   9763  C C   . MET E  1 229 ? -0.306  1.660   -3.068  1.00 39.46  ? 230  MET E C   1 
ATOM   9764  O O   . MET E  1 229 ? -0.139  0.432   -3.084  1.00 37.19  ? 230  MET E O   1 
ATOM   9765  C CB  . MET E  1 229 ? -2.805  2.050   -2.933  1.00 48.38  ? 230  MET E CB  1 
ATOM   9766  C CG  . MET E  1 229 ? -4.096  2.733   -3.449  1.00 48.96  ? 230  MET E CG  1 
ATOM   9767  S SD  . MET E  1 229 ? -4.675  4.195   -2.543  1.00 57.27  ? 230  MET E SD  1 
ATOM   9768  C CE  . MET E  1 229 ? -6.208  4.559   -3.407  1.00 49.17  ? 230  MET E CE  1 
ATOM   9769  N N   . GLU E  1 230 ? 0.536   2.495   -2.462  1.00 40.16  ? 231  GLU E N   1 
ATOM   9770  C CA  . GLU E  1 230 ? 1.755   2.024   -1.786  1.00 39.87  ? 231  GLU E CA  1 
ATOM   9771  C C   . GLU E  1 230 ? 1.699   2.392   -0.306  1.00 34.36  ? 231  GLU E C   1 
ATOM   9772  O O   . GLU E  1 230 ? 1.602   3.567   0.009   1.00 38.72  ? 231  GLU E O   1 
ATOM   9773  C CB  . GLU E  1 230 ? 2.992   2.652   -2.444  1.00 41.49  ? 231  GLU E CB  1 
ATOM   9774  C CG  . GLU E  1 230 ? 4.340   1.978   -2.158  1.00 40.46  ? 231  GLU E CG  1 
ATOM   9775  C CD  . GLU E  1 230 ? 5.514   2.668   -2.853  1.00 43.05  ? 231  GLU E CD  1 
ATOM   9776  O OE1 . GLU E  1 230 ? 5.305   3.676   -3.581  1.00 37.39  ? 231  GLU E OE1 1 
ATOM   9777  O OE2 . GLU E  1 230 ? 6.654   2.215   -2.624  1.00 46.77  ? 231  GLU E OE2 1 
ATOM   9778  N N   . PHE E  1 231 ? 1.787   1.423   0.601   1.00 34.25  ? 232  PHE E N   1 
ATOM   9779  C CA  . PHE E  1 231 ? 1.607   1.745   2.027   1.00 33.93  ? 232  PHE E CA  1 
ATOM   9780  C C   . PHE E  1 231 ? 2.887   1.677   2.876   1.00 36.23  ? 232  PHE E C   1 
ATOM   9781  O O   . PHE E  1 231 ? 3.811   0.948   2.547   1.00 37.83  ? 232  PHE E O   1 
ATOM   9782  C CB  . PHE E  1 231 ? 0.528   0.846   2.637   1.00 28.24  ? 232  PHE E CB  1 
ATOM   9783  C CG  . PHE E  1 231 ? -0.858  1.124   2.082   1.00 36.21  ? 232  PHE E CG  1 
ATOM   9784  C CD1 . PHE E  1 231 ? -1.557  2.267   2.461   1.00 40.91  ? 232  PHE E CD1 1 
ATOM   9785  C CD2 . PHE E  1 231 ? -1.477  0.234   1.221   1.00 36.60  ? 232  PHE E CD2 1 
ATOM   9786  C CE1 . PHE E  1 231 ? -2.828  2.536   1.943   1.00 37.57  ? 232  PHE E CE1 1 
ATOM   9787  C CE2 . PHE E  1 231 ? -2.746  0.498   0.719   1.00 38.27  ? 232  PHE E CE2 1 
ATOM   9788  C CZ  . PHE E  1 231 ? -3.414  1.647   1.080   1.00 33.27  ? 232  PHE E CZ  1 
ATOM   9789  N N   . PHE E  1 232 ? 2.934   2.449   3.964   1.00 34.72  ? 233  PHE E N   1 
ATOM   9790  C CA  . PHE E  1 232 ? 4.125   2.572   4.793   1.00 29.38  ? 233  PHE E CA  1 
ATOM   9791  C C   . PHE E  1 232 ? 3.726   2.404   6.233   1.00 35.90  ? 233  PHE E C   1 
ATOM   9792  O O   . PHE E  1 232 ? 2.544   2.457   6.531   1.00 36.61  ? 233  PHE E O   1 
ATOM   9793  C CB  . PHE E  1 232 ? 4.796   3.924   4.593   1.00 33.98  ? 233  PHE E CB  1 
ATOM   9794  C CG  . PHE E  1 232 ? 5.365   4.110   3.219   1.00 42.50  ? 233  PHE E CG  1 
ATOM   9795  C CD1 . PHE E  1 232 ? 4.559   4.542   2.167   1.00 41.20  ? 233  PHE E CD1 1 
ATOM   9796  C CD2 . PHE E  1 232 ? 6.698   3.844   2.964   1.00 38.78  ? 233  PHE E CD2 1 
ATOM   9797  C CE1 . PHE E  1 232 ? 5.070   4.706   0.910   1.00 34.74  ? 233  PHE E CE1 1 
ATOM   9798  C CE2 . PHE E  1 232 ? 7.205   4.004   1.685   1.00 39.22  ? 233  PHE E CE2 1 
ATOM   9799  C CZ  . PHE E  1 232 ? 6.390   4.438   0.671   1.00 36.26  ? 233  PHE E CZ  1 
ATOM   9800  N N   . TRP E  1 233 ? 4.695   2.170   7.120   1.00 38.33  ? 234  TRP E N   1 
ATOM   9801  C CA  . TRP E  1 233 ? 4.425   2.047   8.554   1.00 32.15  ? 234  TRP E CA  1 
ATOM   9802  C C   . TRP E  1 233 ? 5.589   2.535   9.401   1.00 32.83  ? 234  TRP E C   1 
ATOM   9803  O O   . TRP E  1 233 ? 6.717   2.651   8.928   1.00 34.10  ? 234  TRP E O   1 
ATOM   9804  C CB  . TRP E  1 233 ? 4.095   0.604   8.933   1.00 26.78  ? 234  TRP E CB  1 
ATOM   9805  C CG  . TRP E  1 233 ? 5.196   -0.357  8.685   1.00 29.10  ? 234  TRP E CG  1 
ATOM   9806  C CD1 . TRP E  1 233 ? 5.477   -0.989  7.506   1.00 32.28  ? 234  TRP E CD1 1 
ATOM   9807  C CD2 . TRP E  1 233 ? 6.186   -0.807  9.625   1.00 28.38  ? 234  TRP E CD2 1 
ATOM   9808  N NE1 . TRP E  1 233 ? 6.574   -1.812  7.657   1.00 24.82  ? 234  TRP E NE1 1 
ATOM   9809  C CE2 . TRP E  1 233 ? 7.030   -1.718  8.945   1.00 26.48  ? 234  TRP E CE2 1 
ATOM   9810  C CE3 . TRP E  1 233 ? 6.438   -0.539  10.981  1.00 30.21  ? 234  TRP E CE3 1 
ATOM   9811  C CZ2 . TRP E  1 233 ? 8.112   -2.365  9.576   1.00 24.84  ? 234  TRP E CZ2 1 
ATOM   9812  C CZ3 . TRP E  1 233 ? 7.517   -1.183  11.602  1.00 24.31  ? 234  TRP E CZ3 1 
ATOM   9813  C CH2 . TRP E  1 233 ? 8.334   -2.086  10.894  1.00 19.91  ? 234  TRP E CH2 1 
ATOM   9814  N N   . THR E  1 234 ? 5.306   2.872   10.650  1.00 33.68  ? 235  THR E N   1 
ATOM   9815  C CA  . THR E  1 234 ? 6.356   3.221   11.598  1.00 31.85  ? 235  THR E CA  1 
ATOM   9816  C C   . THR E  1 234 ? 5.886   2.940   13.017  1.00 35.62  ? 235  THR E C   1 
ATOM   9817  O O   . THR E  1 234 ? 4.676   2.872   13.294  1.00 35.13  ? 235  THR E O   1 
ATOM   9818  C CB  . THR E  1 234 ? 6.796   4.705   11.464  1.00 37.46  ? 235  THR E CB  1 
ATOM   9819  O OG1 . THR E  1 234 ? 8.115   4.858   12.007  1.00 34.74  ? 235  THR E OG1 1 
ATOM   9820  C CG2 . THR E  1 234 ? 5.852   5.630   12.216  1.00 30.79  ? 235  THR E CG2 1 
ATOM   9821  N N   . ILE E  1 235 ? 6.840   2.782   13.927  1.00 36.67  ? 236  ILE E N   1 
ATOM   9822  C CA  . ILE E  1 235 ? 6.476   2.637   15.334  1.00 39.05  ? 236  ILE E CA  1 
ATOM   9823  C C   . ILE E  1 235 ? 6.777   3.962   16.042  1.00 36.14  ? 236  ILE E C   1 
ATOM   9824  O O   . ILE E  1 235 ? 7.937   4.379   16.181  1.00 32.59  ? 236  ILE E O   1 
ATOM   9825  C CB  . ILE E  1 235 ? 7.219   1.464   16.009  1.00 37.28  ? 236  ILE E CB  1 
ATOM   9826  C CG1 . ILE E  1 235 ? 6.868   0.147   15.307  1.00 30.88  ? 236  ILE E CG1 1 
ATOM   9827  C CG2 . ILE E  1 235 ? 6.888   1.406   17.501  1.00 34.15  ? 236  ILE E CG2 1 
ATOM   9828  C CD1 . ILE E  1 235 ? 5.475   -0.314  15.566  1.00 30.59  ? 236  ILE E CD1 1 
ATOM   9829  N N   . LEU E  1 236 ? 5.706   4.612   16.487  1.00 33.92  ? 237  LEU E N   1 
ATOM   9830  C CA  . LEU E  1 236 ? 5.821   5.878   17.176  1.00 38.53  ? 237  LEU E CA  1 
ATOM   9831  C C   . LEU E  1 236 ? 5.968   5.630   18.687  1.00 39.52  ? 237  LEU E C   1 
ATOM   9832  O O   . LEU E  1 236 ? 5.040   5.127   19.351  1.00 36.78  ? 237  LEU E O   1 
ATOM   9833  C CB  . LEU E  1 236 ? 4.607   6.751   16.865  1.00 39.86  ? 237  LEU E CB  1 
ATOM   9834  C CG  . LEU E  1 236 ? 4.625   8.178   17.394  1.00 38.57  ? 237  LEU E CG  1 
ATOM   9835  C CD1 . LEU E  1 236 ? 5.771   8.975   16.804  1.00 36.34  ? 237  LEU E CD1 1 
ATOM   9836  C CD2 . LEU E  1 236 ? 3.288   8.817   17.094  1.00 36.36  ? 237  LEU E CD2 1 
ATOM   9837  N N   . LYS E  1 237 ? 7.148   5.965   19.213  1.00 40.19  ? 238  LYS E N   1 
ATOM   9838  C CA  . LYS E  1 237 ? 7.425   5.798   20.646  1.00 42.30  ? 238  LYS E CA  1 
ATOM   9839  C C   . LYS E  1 237 ? 6.435   6.625   21.504  1.00 43.57  ? 238  LYS E C   1 
ATOM   9840  O O   . LYS E  1 237 ? 5.899   7.660   21.048  1.00 44.08  ? 238  LYS E O   1 
ATOM   9841  C CB  . LYS E  1 237 ? 8.872   6.226   20.974  1.00 35.35  ? 238  LYS E CB  1 
ATOM   9842  C CG  . LYS E  1 237 ? 9.975   5.415   20.302  1.00 36.84  ? 238  LYS E CG  1 
ATOM   9843  C CD  . LYS E  1 237 ? 9.806   3.917   20.547  1.00 45.67  ? 238  LYS E CD  1 
ATOM   9844  C CE  . LYS E  1 237 ? 10.987  3.102   20.014  1.00 55.65  ? 238  LYS E CE  1 
ATOM   9845  N NZ  . LYS E  1 237 ? 10.735  1.616   20.151  1.00 58.70  ? 238  LYS E NZ  1 
ATOM   9846  N N   . SER E  1 238 ? 6.178   6.155   22.724  1.00 41.59  ? 239  SER E N   1 
ATOM   9847  C CA  . SER E  1 238 ? 5.341   6.888   23.681  1.00 44.07  ? 239  SER E CA  1 
ATOM   9848  C C   . SER E  1 238 ? 5.901   8.280   23.880  1.00 45.72  ? 239  SER E C   1 
ATOM   9849  O O   . SER E  1 238 ? 7.125   8.448   24.025  1.00 44.89  ? 239  SER E O   1 
ATOM   9850  C CB  . SER E  1 238 ? 5.258   6.174   25.040  1.00 44.59  ? 239  SER E CB  1 
ATOM   9851  O OG  . SER E  1 238 ? 4.382   6.851   25.936  1.00 41.51  ? 239  SER E OG  1 
ATOM   9852  N N   . ASN E  1 239 ? 5.009   9.269   23.805  1.00 41.49  ? 240  ASN E N   1 
ATOM   9853  C CA  . ASN E  1 239 ? 5.365   10.667  24.015  1.00 49.19  ? 240  ASN E CA  1 
ATOM   9854  C C   . ASN E  1 239 ? 6.154   11.292  22.842  1.00 50.79  ? 240  ASN E C   1 
ATOM   9855  O O   . ASN E  1 239 ? 6.765   12.345  23.008  1.00 51.55  ? 240  ASN E O   1 
ATOM   9856  C CB  . ASN E  1 239 ? 6.147   10.847  25.328  1.00 51.21  ? 240  ASN E CB  1 
ATOM   9857  C CG  . ASN E  1 239 ? 5.856   12.173  25.999  1.00 61.62  ? 240  ASN E CG  1 
ATOM   9858  O OD1 . ASN E  1 239 ? 4.701   12.635  26.033  1.00 57.40  ? 240  ASN E OD1 1 
ATOM   9859  N ND2 . ASN E  1 239 ? 6.908   12.815  26.506  1.00 66.12  ? 240  ASN E ND2 1 
ATOM   9860  N N   . ASP E  1 240 ? 6.185   10.630  21.682  1.00 50.17  ? 241  ASP E N   1 
ATOM   9861  C CA  . ASP E  1 240 ? 6.743   11.247  20.473  1.00 49.06  ? 241  ASP E CA  1 
ATOM   9862  C C   . ASP E  1 240 ? 5.619   11.726  19.539  1.00 46.99  ? 241  ASP E C   1 
ATOM   9863  O O   . ASP E  1 240 ? 4.447   11.381  19.712  1.00 45.87  ? 241  ASP E O   1 
ATOM   9864  C CB  . ASP E  1 240 ? 7.671   10.273  19.737  1.00 44.52  ? 241  ASP E CB  1 
ATOM   9865  C CG  . ASP E  1 240 ? 8.515   10.957  18.648  1.00 51.07  ? 241  ASP E CG  1 
ATOM   9866  O OD1 . ASP E  1 240 ? 8.663   12.211  18.669  1.00 48.69  ? 241  ASP E OD1 1 
ATOM   9867  O OD2 . ASP E  1 240 ? 9.028   10.219  17.767  1.00 51.51  ? 241  ASP E OD2 1 
ATOM   9868  N N   . ALA E  1 241 ? 5.978   12.476  18.510  1.00 47.49  ? 242  ALA E N   1 
ATOM   9869  C CA  . ALA E  1 241 ? 4.958   12.998  17.621  1.00 50.41  ? 242  ALA E CA  1 
ATOM   9870  C C   . ALA E  1 241 ? 5.283   12.738  16.162  1.00 44.52  ? 242  ALA E C   1 
ATOM   9871  O O   . ALA E  1 241 ? 6.446   12.749  15.758  1.00 45.38  ? 242  ALA E O   1 
ATOM   9872  C CB  . ALA E  1 241 ? 4.780   14.489  17.851  1.00 53.56  ? 242  ALA E CB  1 
ATOM   9873  N N   . ILE E  1 242 ? 4.230   12.543  15.379  1.00 41.68  ? 243  ILE E N   1 
ATOM   9874  C CA  . ILE E  1 242 ? 4.367   12.346  13.945  1.00 47.60  ? 243  ILE E CA  1 
ATOM   9875  C C   . ILE E  1 242 ? 3.704   13.525  13.211  1.00 43.41  ? 243  ILE E C   1 
ATOM   9876  O O   . ILE E  1 242 ? 2.613   13.972  13.565  1.00 38.57  ? 243  ILE E O   1 
ATOM   9877  C CB  . ILE E  1 242 ? 3.779   10.983  13.507  1.00 39.36  ? 243  ILE E CB  1 
ATOM   9878  C CG1 . ILE E  1 242 ? 4.018   10.760  12.019  1.00 39.59  ? 243  ILE E CG1 1 
ATOM   9879  C CG2 . ILE E  1 242 ? 2.287   10.891  13.782  1.00 32.50  ? 243  ILE E CG2 1 
ATOM   9880  C CD1 . ILE E  1 242 ? 3.603   9.350   11.550  1.00 36.25  ? 243  ILE E CD1 1 
ATOM   9881  N N   . ASN E  1 243 ? 4.389   14.010  12.181  1.00 46.04  ? 244  ASN E N   1 
ATOM   9882  C CA  . ASN E  1 243 ? 3.973   15.196  11.445  1.00 44.00  ? 244  ASN E CA  1 
ATOM   9883  C C   . ASN E  1 243 ? 3.794   14.892  9.965   1.00 44.10  ? 244  ASN E C   1 
ATOM   9884  O O   . ASN E  1 243 ? 4.679   14.313  9.329   1.00 40.81  ? 244  ASN E O   1 
ATOM   9885  C CB  . ASN E  1 243 ? 5.003   16.309  11.647  1.00 47.38  ? 244  ASN E CB  1 
ATOM   9886  C CG  . ASN E  1 243 ? 5.131   16.717  13.120  1.00 59.10  ? 244  ASN E CG  1 
ATOM   9887  O OD1 . ASN E  1 243 ? 4.391   17.580  13.603  1.00 59.44  ? 244  ASN E OD1 1 
ATOM   9888  N ND2 . ASN E  1 243 ? 6.050   16.064  13.846  1.00 58.21  ? 244  ASN E ND2 1 
ATOM   9889  N N   . PHE E  1 244 ? 2.619   15.231  9.443   1.00 45.68  ? 245  PHE E N   1 
ATOM   9890  C CA  . PHE E  1 244 ? 2.303   15.069  8.022   1.00 42.09  ? 245  PHE E CA  1 
ATOM   9891  C C   . PHE E  1 244 ? 2.179   16.413  7.298   1.00 43.43  ? 245  PHE E C   1 
ATOM   9892  O O   . PHE E  1 244 ? 1.521   17.322  7.795   1.00 43.73  ? 245  PHE E O   1 
ATOM   9893  C CB  . PHE E  1 244 ? 0.996   14.316  7.847   1.00 39.49  ? 245  PHE E CB  1 
ATOM   9894  C CG  . PHE E  1 244 ? 1.024   12.913  8.346   1.00 39.95  ? 245  PHE E CG  1 
ATOM   9895  C CD1 . PHE E  1 244 ? 1.509   11.882  7.546   1.00 45.45  ? 245  PHE E CD1 1 
ATOM   9896  C CD2 . PHE E  1 244 ? 0.563   12.610  9.602   1.00 40.53  ? 245  PHE E CD2 1 
ATOM   9897  C CE1 . PHE E  1 244 ? 1.522   10.567  8.003   1.00 41.73  ? 245  PHE E CE1 1 
ATOM   9898  C CE2 . PHE E  1 244 ? 0.573   11.305  10.066  1.00 36.76  ? 245  PHE E CE2 1 
ATOM   9899  C CZ  . PHE E  1 244 ? 1.050   10.284  9.266   1.00 38.86  ? 245  PHE E CZ  1 
ATOM   9900  N N   . GLU E  1 245 ? 2.766   16.510  6.103   1.00 49.45  ? 246  GLU E N   1 
ATOM   9901  C CA  . GLU E  1 245 ? 2.590   17.663  5.205   1.00 40.66  ? 246  GLU E CA  1 
ATOM   9902  C C   . GLU E  1 245 ? 2.372   17.157  3.769   1.00 42.70  ? 246  GLU E C   1 
ATOM   9903  O O   . GLU E  1 245 ? 3.168   16.353  3.252   1.00 40.67  ? 246  GLU E O   1 
ATOM   9904  C CB  . GLU E  1 245 ? 3.801   18.606  5.265   1.00 38.45  ? 246  GLU E CB  1 
ATOM   9905  C CG  . GLU E  1 245 ? 3.605   19.868  4.422   1.00 47.32  ? 246  GLU E CG  1 
ATOM   9906  C CD  . GLU E  1 245 ? 4.765   20.852  4.481   1.00 50.09  ? 246  GLU E CD  1 
ATOM   9907  O OE1 . GLU E  1 245 ? 5.409   21.029  5.538   1.00 56.09  ? 246  GLU E OE1 1 
ATOM   9908  O OE2 . GLU E  1 245 ? 5.054   21.441  3.426   1.00 55.02  ? 246  GLU E OE2 1 
ATOM   9909  N N   . SER E  1 246 ? 1.294   17.624  3.131   1.00 42.49  ? 247  SER E N   1 
ATOM   9910  C CA  . SER E  1 246 ? 0.918   17.120  1.808   1.00 42.77  ? 247  SER E CA  1 
ATOM   9911  C C   . SER E  1 246 ? 0.021   18.020  0.971   1.00 44.05  ? 247  SER E C   1 
ATOM   9912  O O   . SER E  1 246 ? -0.961  18.572  1.466   1.00 42.97  ? 247  SER E O   1 
ATOM   9913  C CB  . SER E  1 246 ? 0.207   15.778  1.953   1.00 38.79  ? 247  SER E CB  1 
ATOM   9914  O OG  . SER E  1 246 ? -0.108  15.215  0.680   1.00 41.48  ? 247  SER E OG  1 
ATOM   9915  N N   . ASN E  1 247 ? 0.298   18.081  -0.330  1.00 48.90  ? 248  ASN E N   1 
ATOM   9916  C CA  . ASN E  1 247 ? -0.613  18.764  -1.258  1.00 50.07  ? 248  ASN E CA  1 
ATOM   9917  C C   . ASN E  1 247 ? -1.192  17.830  -2.336  1.00 42.56  ? 248  ASN E C   1 
ATOM   9918  O O   . ASN E  1 247 ? -1.536  18.273  -3.436  1.00 46.23  ? 248  ASN E O   1 
ATOM   9919  C CB  . ASN E  1 247 ? 0.078   19.980  -1.908  1.00 51.60  ? 248  ASN E CB  1 
ATOM   9920  C CG  . ASN E  1 247 ? 1.199   19.593  -2.862  1.00 54.38  ? 248  ASN E CG  1 
ATOM   9921  O OD1 . ASN E  1 247 ? 1.843   18.549  -2.705  1.00 52.46  ? 248  ASN E OD1 1 
ATOM   9922  N ND2 . ASN E  1 247 ? 1.442   20.446  -3.855  1.00 52.90  ? 248  ASN E ND2 1 
ATOM   9923  N N   . GLY E  1 248 ? -1.318  16.547  -2.003  1.00 36.14  ? 249  GLY E N   1 
ATOM   9924  C CA  . GLY E  1 248 ? -2.006  15.604  -2.866  1.00 36.92  ? 249  GLY E CA  1 
ATOM   9925  C C   . GLY E  1 248 ? -1.553  14.153  -2.802  1.00 40.91  ? 249  GLY E C   1 
ATOM   9926  O O   . GLY E  1 248 ? -0.448  13.857  -2.358  1.00 43.47  ? 249  GLY E O   1 
ATOM   9927  N N   . ASN E  1 249 ? -2.428  13.242  -3.222  1.00 42.19  ? 250  ASN E N   1 
ATOM   9928  C CA  . ASN E  1 249 ? -2.103  11.820  -3.319  1.00 41.83  ? 250  ASN E CA  1 
ATOM   9929  C C   . ASN E  1 249 ? -1.886  11.160  -1.966  1.00 39.96  ? 250  ASN E C   1 
ATOM   9930  O O   . ASN E  1 249 ? -1.302  10.082  -1.900  1.00 40.24  ? 250  ASN E O   1 
ATOM   9931  C CB  . ASN E  1 249 ? -0.860  11.632  -4.182  1.00 44.17  ? 250  ASN E CB  1 
ATOM   9932  C CG  . ASN E  1 249 ? -0.983  12.331  -5.508  1.00 42.66  ? 250  ASN E CG  1 
ATOM   9933  O OD1 . ASN E  1 249 ? -0.789  13.543  -5.589  1.00 37.46  ? 250  ASN E OD1 1 
ATOM   9934  N ND2 . ASN E  1 249 ? -1.322  11.577  -6.556  1.00 43.03  ? 250  ASN E ND2 1 
ATOM   9935  N N   . PHE E  1 250 ? -2.375  11.810  -0.904  1.00 41.54  ? 251  PHE E N   1 
ATOM   9936  C CA  . PHE E  1 250 ? -2.138  11.412  0.489   1.00 40.44  ? 251  PHE E CA  1 
ATOM   9937  C C   . PHE E  1 250 ? -3.253  10.524  1.003   1.00 40.45  ? 251  PHE E C   1 
ATOM   9938  O O   . PHE E  1 250 ? -4.390  10.958  1.069   1.00 51.89  ? 251  PHE E O   1 
ATOM   9939  C CB  . PHE E  1 250 ? -2.006  12.666  1.374   1.00 42.31  ? 251  PHE E CB  1 
ATOM   9940  C CG  . PHE E  1 250 ? -1.730  12.375  2.837   1.00 42.90  ? 251  PHE E CG  1 
ATOM   9941  C CD1 . PHE E  1 250 ? -1.046  11.219  3.228   1.00 46.23  ? 251  PHE E CD1 1 
ATOM   9942  C CD2 . PHE E  1 250 ? -2.077  13.302  3.821   1.00 45.20  ? 251  PHE E CD2 1 
ATOM   9943  C CE1 . PHE E  1 250 ? -0.776  10.961  4.580   1.00 40.89  ? 251  PHE E CE1 1 
ATOM   9944  C CE2 . PHE E  1 250 ? -1.800  13.059  5.178   1.00 41.89  ? 251  PHE E CE2 1 
ATOM   9945  C CZ  . PHE E  1 250 ? -1.147  11.892  5.552   1.00 42.02  ? 251  PHE E CZ  1 
ATOM   9946  N N   . ILE E  1 251 ? -2.922  9.297   1.396   1.00 40.09  ? 252  ILE E N   1 
ATOM   9947  C CA  . ILE E  1 251 ? -3.894  8.418   2.035   1.00 39.00  ? 252  ILE E CA  1 
ATOM   9948  C C   . ILE E  1 251 ? -3.628  8.511   3.551   1.00 42.82  ? 252  ILE E C   1 
ATOM   9949  O O   . ILE E  1 251 ? -2.663  7.930   4.059   1.00 39.17  ? 252  ILE E O   1 
ATOM   9950  C CB  . ILE E  1 251 ? -3.783  6.968   1.535   1.00 34.99  ? 252  ILE E CB  1 
ATOM   9951  C CG1 . ILE E  1 251 ? -3.941  6.905   0.016   1.00 47.21  ? 252  ILE E CG1 1 
ATOM   9952  C CG2 . ILE E  1 251 ? -4.807  6.077   2.195   1.00 36.04  ? 252  ILE E CG2 1 
ATOM   9953  C CD1 . ILE E  1 251 ? -5.231  7.478   -0.496  1.00 48.12  ? 252  ILE E CD1 1 
ATOM   9954  N N   . ALA E  1 252 ? -4.454  9.288   4.256   1.00 40.61  ? 253  ALA E N   1 
ATOM   9955  C CA  . ALA E  1 252 ? -4.173  9.670   5.642   1.00 37.77  ? 253  ALA E CA  1 
ATOM   9956  C C   . ALA E  1 252 ? -4.617  8.581   6.652   1.00 36.57  ? 253  ALA E C   1 
ATOM   9957  O O   . ALA E  1 252 ? -5.474  7.735   6.339   1.00 36.84  ? 253  ALA E O   1 
ATOM   9958  C CB  . ALA E  1 252 ? -4.838  10.992  5.956   1.00 35.12  ? 253  ALA E CB  1 
ATOM   9959  N N   . PRO E  1 253 ? -3.984  8.560   7.844   1.00 33.13  ? 254  PRO E N   1 
ATOM   9960  C CA  . PRO E  1 253 ? -4.366  7.669   8.957   1.00 36.06  ? 254  PRO E CA  1 
ATOM   9961  C C   . PRO E  1 253 ? -5.763  7.952   9.506   1.00 38.14  ? 254  PRO E C   1 
ATOM   9962  O O   . PRO E  1 253 ? -6.112  9.125   9.614   1.00 42.10  ? 254  PRO E O   1 
ATOM   9963  C CB  . PRO E  1 253 ? -3.342  7.991   10.051  1.00 29.09  ? 254  PRO E CB  1 
ATOM   9964  C CG  . PRO E  1 253 ? -2.213  8.612   9.363   1.00 37.33  ? 254  PRO E CG  1 
ATOM   9965  C CD  . PRO E  1 253 ? -2.749  9.309   8.141   1.00 32.44  ? 254  PRO E CD  1 
ATOM   9966  N N   . GLU E  1 254 ? -6.550  6.925   9.818   1.00 38.54  ? 255  GLU E N   1 
ATOM   9967  C CA  . GLU E  1 254 ? -7.716  7.131   10.690  1.00 48.05  ? 255  GLU E CA  1 
ATOM   9968  C C   . GLU E  1 254 ? -7.576  6.365   12.041  1.00 49.03  ? 255  GLU E C   1 
ATOM   9969  O O   . GLU E  1 254 ? -7.704  6.951   13.124  1.00 42.94  ? 255  GLU E O   1 
ATOM   9970  C CB  . GLU E  1 254 ? -9.002  6.731   9.973   1.00 45.76  ? 255  GLU E CB  1 
ATOM   9971  C CG  . GLU E  1 254 ? -10.261 6.934   10.812  1.00 55.61  ? 255  GLU E CG  1 
ATOM   9972  C CD  . GLU E  1 254 ? -11.545 6.806   9.991   1.00 72.79  ? 255  GLU E CD  1 
ATOM   9973  O OE1 . GLU E  1 254 ? -11.706 7.564   8.999   1.00 76.27  ? 255  GLU E OE1 1 
ATOM   9974  O OE2 . GLU E  1 254 ? -12.365 5.908   10.307  1.00 71.45  ? 255  GLU E OE2 1 
ATOM   9975  N N   . ASN E  1 255 ? -7.258  5.073   11.966  1.00 47.31  ? 256  ASN E N   1 
ATOM   9976  C CA  . ASN E  1 255 ? -7.056  4.269   13.164  1.00 42.96  ? 256  ASN E CA  1 
ATOM   9977  C C   . ASN E  1 255 ? -5.611  3.748   13.302  1.00 44.58  ? 256  ASN E C   1 
ATOM   9978  O O   . ASN E  1 255 ? -4.985  3.357   12.313  1.00 43.56  ? 256  ASN E O   1 
ATOM   9979  C CB  . ASN E  1 255 ? -8.019  3.081   13.160  1.00 40.45  ? 256  ASN E CB  1 
ATOM   9980  C CG  . ASN E  1 255 ? -9.472  3.505   13.093  1.00 43.31  ? 256  ASN E CG  1 
ATOM   9981  O OD1 . ASN E  1 255 ? -9.875  4.497   13.696  1.00 48.30  ? 256  ASN E OD1 1 
ATOM   9982  N ND2 . ASN E  1 255 ? -10.272 2.732   12.380  1.00 45.18  ? 256  ASN E ND2 1 
ATOM   9983  N N   . ALA E  1 256 ? -5.143  3.620   14.545  1.00 40.14  ? 257  ALA E N   1 
ATOM   9984  C CA  . ALA E  1 256 ? -3.794  3.134   14.816  1.00 38.44  ? 257  ALA E CA  1 
ATOM   9985  C C   . ALA E  1 256 ? -3.810  2.050   15.911  1.00 42.10  ? 257  ALA E C   1 
ATOM   9986  O O   . ALA E  1 256 ? -4.854  1.809   16.519  1.00 45.92  ? 257  ALA E O   1 
ATOM   9987  C CB  . ALA E  1 256 ? -2.907  4.300   15.221  1.00 38.85  ? 257  ALA E CB  1 
ATOM   9988  N N   . TYR E  1 257 ? -2.685  1.368   16.143  1.00 42.38  ? 258  TYR E N   1 
ATOM   9989  C CA  . TYR E  1 257 ? -2.677  0.238   17.098  1.00 40.91  ? 258  TYR E CA  1 
ATOM   9990  C C   . TYR E  1 257 ? -1.673  0.405   18.241  1.00 38.33  ? 258  TYR E C   1 
ATOM   9991  O O   . TYR E  1 257 ? -0.470  0.597   18.007  1.00 34.54  ? 258  TYR E O   1 
ATOM   9992  C CB  . TYR E  1 257 ? -2.388  -1.073  16.396  1.00 33.40  ? 258  TYR E CB  1 
ATOM   9993  C CG  . TYR E  1 257 ? -3.351  -1.488  15.322  1.00 37.04  ? 258  TYR E CG  1 
ATOM   9994  C CD1 . TYR E  1 257 ? -3.237  -0.990  14.021  1.00 37.92  ? 258  TYR E CD1 1 
ATOM   9995  C CD2 . TYR E  1 257 ? -4.307  -2.458  15.572  1.00 36.65  ? 258  TYR E CD2 1 
ATOM   9996  C CE1 . TYR E  1 257 ? -4.102  -1.420  13.015  1.00 37.48  ? 258  TYR E CE1 1 
ATOM   9997  C CE2 . TYR E  1 257 ? -5.166  -2.896  14.581  1.00 38.25  ? 258  TYR E CE2 1 
ATOM   9998  C CZ  . TYR E  1 257 ? -5.063  -2.375  13.308  1.00 39.69  ? 258  TYR E CZ  1 
ATOM   9999  O OH  . TYR E  1 257 ? -5.932  -2.818  12.342  1.00 42.34  ? 258  TYR E OH  1 
ATOM   10000 N N   . LYS E  1 258 ? -2.192  0.285   19.464  1.00 38.10  ? 259  LYS E N   1 
ATOM   10001 C CA  . LYS E  1 258 ? -1.407  0.353   20.688  1.00 35.77  ? 259  LYS E CA  1 
ATOM   10002 C C   . LYS E  1 258 ? -0.832  -1.005  21.056  1.00 34.19  ? 259  LYS E C   1 
ATOM   10003 O O   . LYS E  1 258 ? -1.568  -2.002  21.136  1.00 34.44  ? 259  LYS E O   1 
ATOM   10004 C CB  . LYS E  1 258 ? -2.282  0.869   21.840  1.00 46.22  ? 259  LYS E CB  1 
ATOM   10005 C CG  . LYS E  1 258 ? -2.832  2.290   21.651  1.00 49.64  ? 259  LYS E CG  1 
ATOM   10006 C CD  . LYS E  1 258 ? -3.407  2.906   22.956  1.00 47.73  ? 259  LYS E CD  1 
ATOM   10007 C CE  . LYS E  1 258 ? -4.586  2.121   23.496  1.00 50.92  ? 259  LYS E CE  1 
ATOM   10008 N NZ  . LYS E  1 258 ? -5.226  2.821   24.651  1.00 50.14  ? 259  LYS E NZ  1 
ATOM   10009 N N   . ILE E  1 259 ? 0.483   -1.055  21.268  1.00 33.97  ? 260  ILE E N   1 
ATOM   10010 C CA  . ILE E  1 259 ? 1.114   -2.319  21.644  1.00 34.31  ? 260  ILE E CA  1 
ATOM   10011 C C   . ILE E  1 259 ? 0.966   -2.523  23.140  1.00 36.71  ? 260  ILE E C   1 
ATOM   10012 O O   . ILE E  1 259 ? 1.643   -1.877  23.940  1.00 35.99  ? 260  ILE E O   1 
ATOM   10013 C CB  . ILE E  1 259 ? 2.599   -2.396  21.228  1.00 36.18  ? 260  ILE E CB  1 
ATOM   10014 C CG1 . ILE E  1 259 ? 2.712   -2.408  19.701  1.00 39.09  ? 260  ILE E CG1 1 
ATOM   10015 C CG2 . ILE E  1 259 ? 3.219   -3.699  21.733  1.00 31.73  ? 260  ILE E CG2 1 
ATOM   10016 C CD1 . ILE E  1 259 ? 4.036   -1.933  19.148  1.00 35.33  ? 260  ILE E CD1 1 
ATOM   10017 N N   . VAL E  1 260 A 0.069   -3.441  23.498  1.00 41.88  ? 260  VAL E N   1 
ATOM   10018 C CA  . VAL E  1 260 A -0.405  -3.602  24.874  1.00 38.23  ? 260  VAL E CA  1 
ATOM   10019 C C   . VAL E  1 260 A 0.337   -4.714  25.612  1.00 39.21  ? 260  VAL E C   1 
ATOM   10020 O O   . VAL E  1 260 A 0.641   -4.592  26.805  1.00 38.25  ? 260  VAL E O   1 
ATOM   10021 C CB  . VAL E  1 260 A -1.938  -3.917  24.868  1.00 38.39  ? 260  VAL E CB  1 
ATOM   10022 C CG1 . VAL E  1 260 A -2.411  -4.504  26.207  1.00 42.19  ? 260  VAL E CG1 1 
ATOM   10023 C CG2 . VAL E  1 260 A -2.722  -2.682  24.478  1.00 33.58  ? 260  VAL E CG2 1 
ATOM   10024 N N   . LYS E  1 261 ? 0.650   -5.781  24.881  1.00 35.71  ? 261  LYS E N   1 
ATOM   10025 C CA  . LYS E  1 261 ? 1.399   -6.906  25.419  1.00 34.17  ? 261  LYS E CA  1 
ATOM   10026 C C   . LYS E  1 261 ? 2.385   -7.506  24.395  1.00 37.14  ? 261  LYS E C   1 
ATOM   10027 O O   . LYS E  1 261 ? 1.981   -7.916  23.295  1.00 36.63  ? 261  LYS E O   1 
ATOM   10028 C CB  . LYS E  1 261 ? 0.433   -7.991  25.890  1.00 31.90  ? 261  LYS E CB  1 
ATOM   10029 C CG  . LYS E  1 261 ? 1.104   -9.238  26.439  1.00 32.16  ? 261  LYS E CG  1 
ATOM   10030 C CD  . LYS E  1 261 ? 0.103   -10.163 27.130  1.00 36.43  ? 261  LYS E CD  1 
ATOM   10031 C CE  . LYS E  1 261 ? 0.748   -11.507 27.501  1.00 35.29  ? 261  LYS E CE  1 
ATOM   10032 N NZ  . LYS E  1 261 ? -0.261  -12.508 27.943  1.00 33.12  ? 261  LYS E NZ  1 
ATOM   10033 N N   . LYS E  1 262 ? 3.654   -7.607  24.788  1.00 36.62  ? 262  LYS E N   1 
ATOM   10034 C CA  . LYS E  1 262 ? 4.677   -8.293  24.003  1.00 34.26  ? 262  LYS E CA  1 
ATOM   10035 C C   . LYS E  1 262 ? 5.040   -9.650  24.650  1.00 37.23  ? 262  LYS E C   1 
ATOM   10036 O O   . LYS E  1 262 ? 4.914   -9.804  25.857  1.00 39.50  ? 262  LYS E O   1 
ATOM   10037 C CB  . LYS E  1 262 ? 5.924   -7.432  23.870  1.00 30.66  ? 262  LYS E CB  1 
ATOM   10038 C CG  . LYS E  1 262 ? 5.845   -6.329  22.855  1.00 37.34  ? 262  LYS E CG  1 
ATOM   10039 C CD  . LYS E  1 262 ? 7.224   -5.704  22.692  1.00 45.02  ? 262  LYS E CD  1 
ATOM   10040 C CE  . LYS E  1 262 ? 7.755   -5.278  24.073  1.00 51.50  ? 262  LYS E CE  1 
ATOM   10041 N NZ  . LYS E  1 262 ? 8.935   -4.353  24.060  1.00 58.93  ? 262  LYS E NZ  1 
ATOM   10042 N N   . GLY E  1 263 ? 5.506   -10.610 23.853  1.00 37.08  ? 263  GLY E N   1 
ATOM   10043 C CA  . GLY E  1 263 ? 5.831   -11.944 24.336  1.00 39.20  ? 263  GLY E CA  1 
ATOM   10044 C C   . GLY E  1 263 ? 6.237   -12.895 23.213  1.00 47.26  ? 263  GLY E C   1 
ATOM   10045 O O   . GLY E  1 263 ? 6.658   -12.460 22.140  1.00 53.26  ? 263  GLY E O   1 
ATOM   10046 N N   . ASP E  1 264 ? 6.124   -14.197 23.447  1.00 48.63  ? 264  ASP E N   1 
ATOM   10047 C CA  . ASP E  1 264 ? 6.473   -15.167 22.416  1.00 51.32  ? 264  ASP E CA  1 
ATOM   10048 C C   . ASP E  1 264 ? 5.292   -15.485 21.512  1.00 51.75  ? 264  ASP E C   1 
ATOM   10049 O O   . ASP E  1 264 ? 4.197   -15.846 21.968  1.00 47.62  ? 264  ASP E O   1 
ATOM   10050 C CB  . ASP E  1 264 ? 7.006   -16.455 23.042  1.00 62.22  ? 264  ASP E CB  1 
ATOM   10051 C CG  . ASP E  1 264 ? 8.462   -16.342 23.435  1.00 74.08  ? 264  ASP E CG  1 
ATOM   10052 O OD1 . ASP E  1 264 ? 9.104   -15.374 22.971  1.00 78.20  ? 264  ASP E OD1 1 
ATOM   10053 O OD2 . ASP E  1 264 ? 8.956   -17.204 24.203  1.00 80.90  ? 264  ASP E OD2 1 
ATOM   10054 N N   . SER E  1 265 ? 5.526   -15.355 20.214  1.00 47.70  ? 265  SER E N   1 
ATOM   10055 C CA  . SER E  1 265 ? 4.484   -15.640 19.255  1.00 44.81  ? 265  SER E CA  1 
ATOM   10056 C C   . SER E  1 265 ? 5.128   -16.061 17.931  1.00 44.57  ? 265  SER E C   1 
ATOM   10057 O O   . SER E  1 265 ? 6.350   -15.997 17.767  1.00 44.54  ? 265  SER E O   1 
ATOM   10058 C CB  . SER E  1 265 ? 3.586   -14.403 19.093  1.00 36.72  ? 265  SER E CB  1 
ATOM   10059 O OG  . SER E  1 265 ? 2.549   -14.618 18.160  1.00 38.56  ? 265  SER E OG  1 
ATOM   10060 N N   . THR E  1 266 ? 4.311   -16.464 16.975  1.00 37.91  ? 266  THR E N   1 
ATOM   10061 C CA  . THR E  1 266 ? 4.827   -16.823 15.674  1.00 38.08  ? 266  THR E CA  1 
ATOM   10062 C C   . THR E  1 266 ? 3.689   -16.657 14.698  1.00 41.14  ? 266  THR E C   1 
ATOM   10063 O O   . THR E  1 266 ? 2.552   -16.450 15.116  1.00 39.43  ? 266  THR E O   1 
ATOM   10064 C CB  . THR E  1 266 ? 5.380   -18.267 15.623  1.00 36.09  ? 266  THR E CB  1 
ATOM   10065 O OG1 . THR E  1 266 ? 6.057   -18.470 14.387  1.00 30.84  ? 266  THR E OG1 1 
ATOM   10066 C CG2 . THR E  1 266 ? 4.277   -19.300 15.757  1.00 34.56  ? 266  THR E CG2 1 
ATOM   10067 N N   . ILE E  1 267 ? 4.004   -16.690 13.406  1.00 38.97  ? 267  ILE E N   1 
ATOM   10068 C CA  . ILE E  1 267 ? 2.985   -16.713 12.372  1.00 34.75  ? 267  ILE E CA  1 
ATOM   10069 C C   . ILE E  1 267 ? 3.063   -18.082 11.673  1.00 36.91  ? 267  ILE E C   1 
ATOM   10070 O O   . ILE E  1 267 ? 4.068   -18.403 11.032  1.00 35.74  ? 267  ILE E O   1 
ATOM   10071 C CB  . ILE E  1 267 ? 3.172   -15.535 11.373  1.00 33.94  ? 267  ILE E CB  1 
ATOM   10072 C CG1 . ILE E  1 267 ? 3.069   -14.208 12.101  1.00 30.30  ? 267  ILE E CG1 1 
ATOM   10073 C CG2 . ILE E  1 267 ? 2.115   -15.535 10.250  1.00 34.35  ? 267  ILE E CG2 1 
ATOM   10074 C CD1 . ILE E  1 267 ? 3.209   -13.017 11.164  1.00 31.83  ? 267  ILE E CD1 1 
ATOM   10075 N N   . MET E  1 268 ? 2.026   -18.905 11.835  1.00 41.47  ? 268  MET E N   1 
ATOM   10076 C CA  . MET E  1 268 ? 1.999   -20.230 11.193  1.00 42.57  ? 268  MET E CA  1 
ATOM   10077 C C   . MET E  1 268 ? 1.254   -20.206 9.846   1.00 41.34  ? 268  MET E C   1 
ATOM   10078 O O   . MET E  1 268 ? 0.241   -19.523 9.674   1.00 40.12  ? 268  MET E O   1 
ATOM   10079 C CB  . MET E  1 268 ? 1.382   -21.275 12.133  1.00 43.69  ? 268  MET E CB  1 
ATOM   10080 C CG  . MET E  1 268 ? 2.393   -22.122 12.909  1.00 48.57  ? 268  MET E CG  1 
ATOM   10081 S SD  . MET E  1 268 ? 1.679   -23.105 14.276  1.00 52.70  ? 268  MET E SD  1 
ATOM   10082 C CE  . MET E  1 268 ? 0.105   -23.557 13.586  1.00 45.41  ? 268  MET E CE  1 
ATOM   10083 N N   . LYS E  1 269 ? 1.797   -20.933 8.880   1.00 47.13  ? 269  LYS E N   1 
ATOM   10084 C CA  . LYS E  1 269 ? 1.131   -21.131 7.600   1.00 46.86  ? 269  LYS E CA  1 
ATOM   10085 C C   . LYS E  1 269 ? 0.350   -22.450 7.597   1.00 47.82  ? 269  LYS E C   1 
ATOM   10086 O O   . LYS E  1 269 ? 0.932   -23.541 7.652   1.00 46.98  ? 269  LYS E O   1 
ATOM   10087 C CB  . LYS E  1 269 ? 2.148   -21.115 6.474   1.00 43.11  ? 269  LYS E CB  1 
ATOM   10088 C CG  . LYS E  1 269 ? 2.807   -19.795 6.209   1.00 44.24  ? 269  LYS E CG  1 
ATOM   10089 C CD  . LYS E  1 269 ? 1.790   -18.863 5.575   1.00 57.59  ? 269  LYS E CD  1 
ATOM   10090 C CE  . LYS E  1 269 ? 2.389   -17.526 5.138   1.00 53.38  ? 269  LYS E CE  1 
ATOM   10091 N NZ  . LYS E  1 269 ? 1.502   -16.857 4.131   1.00 47.19  ? 269  LYS E NZ  1 
ATOM   10092 N N   . SER E  1 270 ? -0.974  -22.345 7.547   1.00 50.11  ? 270  SER E N   1 
ATOM   10093 C CA  . SER E  1 270 ? -1.820  -23.532 7.600   1.00 51.99  ? 270  SER E CA  1 
ATOM   10094 C C   . SER E  1 270 ? -3.190  -23.264 6.962   1.00 56.12  ? 270  SER E C   1 
ATOM   10095 O O   . SER E  1 270 ? -3.717  -22.140 7.001   1.00 55.36  ? 270  SER E O   1 
ATOM   10096 C CB  . SER E  1 270 ? -1.986  -24.001 9.049   1.00 49.78  ? 270  SER E CB  1 
ATOM   10097 O OG  . SER E  1 270 ? -2.885  -25.089 9.131   1.00 53.33  ? 270  SER E OG  1 
ATOM   10098 N N   . GLU E  1 271 ? -3.779  -24.321 6.409   1.00 59.74  ? 271  GLU E N   1 
ATOM   10099 C CA  . GLU E  1 271 ? -5.076  -24.223 5.756   1.00 58.76  ? 271  GLU E CA  1 
ATOM   10100 C C   . GLU E  1 271 ? -6.170  -24.698 6.690   1.00 59.21  ? 271  GLU E C   1 
ATOM   10101 O O   . GLU E  1 271 ? -7.354  -24.532 6.394   1.00 66.20  ? 271  GLU E O   1 
ATOM   10102 C CB  . GLU E  1 271 ? -5.105  -25.050 4.463   1.00 59.47  ? 271  GLU E CB  1 
ATOM   10103 C CG  . GLU E  1 271 ? -4.052  -24.649 3.427   1.00 62.16  ? 271  GLU E CG  1 
ATOM   10104 C CD  . GLU E  1 271 ? -4.196  -23.206 2.961   1.00 67.49  ? 271  GLU E CD  1 
ATOM   10105 O OE1 . GLU E  1 271 ? -5.313  -22.798 2.560   1.00 70.36  ? 271  GLU E OE1 1 
ATOM   10106 O OE2 . GLU E  1 271 ? -3.183  -22.472 3.028   1.00 64.83  ? 271  GLU E OE2 1 
ATOM   10107 N N   . LEU E  1 272 ? -5.769  -25.241 7.839   1.00 54.46  ? 272  LEU E N   1 
ATOM   10108 C CA  . LEU E  1 272 ? -6.710  -25.845 8.771   1.00 55.18  ? 272  LEU E CA  1 
ATOM   10109 C C   . LEU E  1 272 ? -7.562  -24.761 9.447   1.00 57.58  ? 272  LEU E C   1 
ATOM   10110 O O   . LEU E  1 272 ? -7.274  -23.570 9.318   1.00 53.58  ? 272  LEU E O   1 
ATOM   10111 C CB  . LEU E  1 272 ? -5.948  -26.691 9.820   1.00 57.73  ? 272  LEU E CB  1 
ATOM   10112 C CG  . LEU E  1 272 ? -4.907  -27.722 9.312   1.00 59.81  ? 272  LEU E CG  1 
ATOM   10113 C CD1 . LEU E  1 272 ? -4.189  -28.524 10.416  1.00 44.70  ? 272  LEU E CD1 1 
ATOM   10114 C CD2 . LEU E  1 272 ? -5.520  -28.664 8.292   1.00 54.59  ? 272  LEU E CD2 1 
ATOM   10115 N N   . GLU E  1 273 ? -8.598  -25.175 10.177  1.00 63.29  ? 273  GLU E N   1 
ATOM   10116 C CA  . GLU E  1 273 ? -9.439  -24.228 10.917  1.00 62.37  ? 273  GLU E CA  1 
ATOM   10117 C C   . GLU E  1 273 ? -9.540  -24.642 12.372  1.00 62.64  ? 273  GLU E C   1 
ATOM   10118 O O   . GLU E  1 273 ? -9.075  -25.720 12.749  1.00 63.61  ? 273  GLU E O   1 
ATOM   10119 C CB  . GLU E  1 273 ? -10.836 -24.118 10.301  1.00 66.57  ? 273  GLU E CB  1 
ATOM   10120 C CG  . GLU E  1 273 ? -10.829 -23.517 8.896   1.00 73.12  ? 273  GLU E CG  1 
ATOM   10121 C CD  . GLU E  1 273 ? -12.213 -23.126 8.389   1.00 84.98  ? 273  GLU E CD  1 
ATOM   10122 O OE1 . GLU E  1 273 ? -13.197 -23.841 8.702   1.00 85.05  ? 273  GLU E OE1 1 
ATOM   10123 O OE2 . GLU E  1 273 ? -12.307 -22.097 7.673   1.00 81.68  ? 273  GLU E OE2 1 
ATOM   10124 N N   . TYR E  1 274 ? -10.134 -23.776 13.187  1.00 63.72  ? 274  TYR E N   1 
ATOM   10125 C CA  . TYR E  1 274 ? -10.210 -24.005 14.622  1.00 57.64  ? 274  TYR E CA  1 
ATOM   10126 C C   . TYR E  1 274 ? -10.793 -25.375 14.966  1.00 66.95  ? 274  TYR E C   1 
ATOM   10127 O O   . TYR E  1 274 ? -11.596 -25.924 14.207  1.00 69.92  ? 274  TYR E O   1 
ATOM   10128 C CB  . TYR E  1 274 ? -11.030 -22.904 15.261  1.00 59.98  ? 274  TYR E CB  1 
ATOM   10129 C CG  . TYR E  1 274 ? -10.907 -22.848 16.757  1.00 61.75  ? 274  TYR E CG  1 
ATOM   10130 C CD1 . TYR E  1 274 ? -9.669  -22.929 17.374  1.00 56.37  ? 274  TYR E CD1 1 
ATOM   10131 C CD2 . TYR E  1 274 ? -12.034 -22.698 17.552  1.00 67.88  ? 274  TYR E CD2 1 
ATOM   10132 C CE1 . TYR E  1 274 ? -9.555  -22.874 18.740  1.00 63.14  ? 274  TYR E CE1 1 
ATOM   10133 C CE2 . TYR E  1 274 ? -11.935 -22.641 18.930  1.00 70.40  ? 274  TYR E CE2 1 
ATOM   10134 C CZ  . TYR E  1 274 ? -10.692 -22.728 19.522  1.00 70.68  ? 274  TYR E CZ  1 
ATOM   10135 O OH  . TYR E  1 274 ? -10.589 -22.662 20.895  1.00 66.25  ? 274  TYR E OH  1 
ATOM   10136 N N   . GLY E  1 275 ? -10.365 -25.943 16.090  1.00 65.69  ? 275  GLY E N   1 
ATOM   10137 C CA  . GLY E  1 275 ? -10.796 -27.279 16.461  1.00 69.12  ? 275  GLY E CA  1 
ATOM   10138 C C   . GLY E  1 275 ? -11.341 -27.444 17.873  1.00 73.37  ? 275  GLY E C   1 
ATOM   10139 O O   . GLY E  1 275 ? -11.587 -28.571 18.319  1.00 76.92  ? 275  GLY E O   1 
ATOM   10140 N N   . ASP E  1 276 ? -11.523 -26.330 18.581  1.00 74.46  ? 276  ASP E N   1 
ATOM   10141 C CA  . ASP E  1 276 ? -12.025 -26.344 19.961  1.00 73.74  ? 276  ASP E CA  1 
ATOM   10142 C C   . ASP E  1 276 ? -11.308 -27.331 20.870  1.00 70.63  ? 276  ASP E C   1 
ATOM   10143 O O   . ASP E  1 276 ? -11.946 -27.993 21.675  1.00 75.01  ? 276  ASP E O   1 
ATOM   10144 C CB  . ASP E  1 276 ? -13.527 -26.625 19.995  1.00 72.79  ? 276  ASP E CB  1 
ATOM   10145 C CG  . ASP E  1 276 ? -14.344 -25.448 19.510  1.00 78.25  ? 276  ASP E CG  1 
ATOM   10146 O OD1 . ASP E  1 276 ? -14.628 -24.559 20.352  1.00 78.67  ? 276  ASP E OD1 1 
ATOM   10147 O OD2 . ASP E  1 276 ? -14.680 -25.405 18.302  1.00 75.36  ? 276  ASP E OD2 1 
ATOM   10148 N N   . CYS E  1 277 ? -9.986  -27.405 20.758  1.00 67.76  ? 277  CYS E N   1 
ATOM   10149 C CA  . CYS E  1 277 ? -9.205  -28.323 21.576  1.00 65.93  ? 277  CYS E CA  1 
ATOM   10150 C C   . CYS E  1 277 ? -8.155  -27.554 22.376  1.00 60.74  ? 277  CYS E C   1 
ATOM   10151 O O   . CYS E  1 277 ? -8.127  -26.315 22.361  1.00 61.42  ? 277  CYS E O   1 
ATOM   10152 C CB  . CYS E  1 277 ? -8.540  -29.397 20.705  1.00 67.20  ? 277  CYS E CB  1 
ATOM   10153 S SG  . CYS E  1 277 ? -7.543  -28.757 19.304  1.00 83.32  ? 277  CYS E SG  1 
ATOM   10154 N N   . ASN E  1 278 ? -7.314  -28.277 23.105  1.00 57.69  ? 278  ASN E N   1 
ATOM   10155 C CA  . ASN E  1 278 ? -6.258  -27.616 23.855  1.00 55.07  ? 278  ASN E CA  1 
ATOM   10156 C C   . ASN E  1 278 ? -4.970  -28.439 23.870  1.00 56.80  ? 278  ASN E C   1 
ATOM   10157 O O   . ASN E  1 278 ? -5.010  -29.678 23.856  1.00 57.76  ? 278  ASN E O   1 
ATOM   10158 C CB  . ASN E  1 278 ? -6.708  -27.315 25.282  1.00 56.29  ? 278  ASN E CB  1 
ATOM   10159 C CG  . ASN E  1 278 ? -5.770  -26.365 25.986  1.00 57.74  ? 278  ASN E CG  1 
ATOM   10160 O OD1 . ASN E  1 278 ? -5.049  -25.623 25.330  1.00 58.82  ? 278  ASN E OD1 1 
ATOM   10161 N ND2 . ASN E  1 278 ? -5.756  -26.390 27.315  1.00 57.51  ? 278  ASN E ND2 1 
ATOM   10162 N N   . THR E  1 279 ? -3.832  -27.737 23.849  1.00 56.42  ? 279  THR E N   1 
ATOM   10163 C CA  . THR E  1 279 ? -2.513  -28.365 23.810  1.00 50.03  ? 279  THR E CA  1 
ATOM   10164 C C   . THR E  1 279 ? -1.428  -27.451 24.400  1.00 50.47  ? 279  THR E C   1 
ATOM   10165 O O   . THR E  1 279 ? -1.680  -26.289 24.750  1.00 48.31  ? 279  THR E O   1 
ATOM   10166 C CB  . THR E  1 279 ? -2.129  -28.752 22.368  1.00 51.89  ? 279  THR E CB  1 
ATOM   10167 O OG1 . THR E  1 279 ? -0.957  -29.583 22.372  1.00 55.29  ? 279  THR E OG1 1 
ATOM   10168 C CG2 . THR E  1 279 ? -1.898  -27.501 21.520  1.00 50.92  ? 279  THR E CG2 1 
ATOM   10169 N N   . LYS E  1 280 ? -0.221  -27.990 24.521  1.00 51.75  ? 280  LYS E N   1 
ATOM   10170 C CA  . LYS E  1 280 ? 0.919   -27.202 24.964  1.00 50.13  ? 280  LYS E CA  1 
ATOM   10171 C C   . LYS E  1 280 ? 2.017   -27.207 23.899  1.00 53.33  ? 280  LYS E C   1 
ATOM   10172 O O   . LYS E  1 280 ? 3.085   -26.618 24.078  1.00 51.04  ? 280  LYS E O   1 
ATOM   10173 C CB  . LYS E  1 280 ? 1.464   -27.742 26.289  1.00 55.30  ? 280  LYS E CB  1 
ATOM   10174 C CG  . LYS E  1 280 ? 0.599   -27.383 27.491  1.00 65.18  ? 280  LYS E CG  1 
ATOM   10175 C CD  . LYS E  1 280 ? 1.321   -27.615 28.821  1.00 69.36  ? 280  LYS E CD  1 
ATOM   10176 C CE  . LYS E  1 280 ? 2.506   -26.647 28.969  1.00 69.77  ? 280  LYS E CE  1 
ATOM   10177 N NZ  . LYS E  1 280 ? 2.898   -26.375 30.381  1.00 68.11  ? 280  LYS E NZ  1 
ATOM   10178 N N   . CYS E  1 281 ? 1.745   -27.861 22.778  1.00 51.78  ? 281  CYS E N   1 
ATOM   10179 C CA  . CYS E  1 281 ? 2.704   -27.889 21.693  1.00 51.18  ? 281  CYS E CA  1 
ATOM   10180 C C   . CYS E  1 281 ? 1.957   -27.964 20.377  1.00 51.99  ? 281  CYS E C   1 
ATOM   10181 O O   . CYS E  1 281 ? 1.224   -28.920 20.124  1.00 55.63  ? 281  CYS E O   1 
ATOM   10182 C CB  . CYS E  1 281 ? 3.665   -29.067 21.849  1.00 53.13  ? 281  CYS E CB  1 
ATOM   10183 S SG  . CYS E  1 281 ? 4.980   -29.124 20.587  1.00 59.56  ? 281  CYS E SG  1 
ATOM   10184 N N   . GLN E  1 282 ? 2.151   -26.945 19.547  1.00 51.69  ? 282  GLN E N   1 
ATOM   10185 C CA  . GLN E  1 282 ? 1.405   -26.790 18.295  1.00 51.22  ? 282  GLN E CA  1 
ATOM   10186 C C   . GLN E  1 282 ? 2.335   -26.694 17.083  1.00 50.47  ? 282  GLN E C   1 
ATOM   10187 O O   . GLN E  1 282 ? 3.367   -26.018 17.150  1.00 48.50  ? 282  GLN E O   1 
ATOM   10188 C CB  . GLN E  1 282 ? 0.516   -25.537 18.371  1.00 51.52  ? 282  GLN E CB  1 
ATOM   10189 C CG  . GLN E  1 282 ? -0.368  -25.309 17.160  1.00 49.99  ? 282  GLN E CG  1 
ATOM   10190 C CD  . GLN E  1 282 ? -1.438  -26.354 17.033  1.00 50.18  ? 282  GLN E CD  1 
ATOM   10191 O OE1 . GLN E  1 282 ? -2.341  -26.434 17.862  1.00 50.85  ? 282  GLN E OE1 1 
ATOM   10192 N NE2 . GLN E  1 282 ? -1.334  -27.180 16.006  1.00 52.31  ? 282  GLN E NE2 1 
ATOM   10193 N N   . THR E  1 283 ? 1.977   -27.387 15.999  1.00 48.60  ? 283  THR E N   1 
ATOM   10194 C CA  . THR E  1 283 ? 2.687   -27.285 14.730  1.00 50.61  ? 283  THR E CA  1 
ATOM   10195 C C   . THR E  1 283 ? 1.642   -26.910 13.668  1.00 54.49  ? 283  THR E C   1 
ATOM   10196 O O   . THR E  1 283 ? 0.440   -27.069 13.917  1.00 54.30  ? 283  THR E O   1 
ATOM   10197 C CB  . THR E  1 283 ? 3.406   -28.599 14.361  1.00 51.39  ? 283  THR E CB  1 
ATOM   10198 O OG1 . THR E  1 283 ? 2.542   -29.437 13.581  1.00 51.72  ? 283  THR E OG1 1 
ATOM   10199 C CG2 . THR E  1 283 ? 3.908   -29.317 15.618  1.00 49.58  ? 283  THR E CG2 1 
ATOM   10200 N N   . PRO E  1 284 ? 2.078   -26.423 12.484  1.00 52.42  ? 284  PRO E N   1 
ATOM   10201 C CA  . PRO E  1 284 ? 1.090   -26.007 11.476  1.00 52.29  ? 284  PRO E CA  1 
ATOM   10202 C C   . PRO E  1 284 ? 0.126   -27.110 11.035  1.00 51.55  ? 284  PRO E C   1 
ATOM   10203 O O   . PRO E  1 284 ? -0.934  -26.747 10.514  1.00 51.44  ? 284  PRO E O   1 
ATOM   10204 C CB  . PRO E  1 284 ? 1.963   -25.569 10.283  1.00 45.70  ? 284  PRO E CB  1 
ATOM   10205 C CG  . PRO E  1 284 ? 3.233   -25.185 10.872  1.00 45.96  ? 284  PRO E CG  1 
ATOM   10206 C CD  . PRO E  1 284 ? 3.449   -26.102 12.047  1.00 50.49  ? 284  PRO E CD  1 
ATOM   10207 N N   . ILE E  1 285 ? 0.434   -28.389 11.292  1.00 48.58  ? 285  ILE E N   1 
ATOM   10208 C CA  . ILE E  1 285 ? -0.416  -29.490 10.811  1.00 51.03  ? 285  ILE E CA  1 
ATOM   10209 C C   . ILE E  1 285 ? -1.086  -30.293 11.917  1.00 53.06  ? 285  ILE E C   1 
ATOM   10210 O O   . ILE E  1 285 ? -1.752  -31.281 11.619  1.00 56.95  ? 285  ILE E O   1 
ATOM   10211 C CB  . ILE E  1 285 ? 0.368   -30.525 9.931   1.00 48.96  ? 285  ILE E CB  1 
ATOM   10212 C CG1 . ILE E  1 285 ? 1.374   -31.292 10.785  1.00 51.39  ? 285  ILE E CG1 1 
ATOM   10213 C CG2 . ILE E  1 285 ? 1.081   -29.865 8.777   1.00 43.92  ? 285  ILE E CG2 1 
ATOM   10214 C CD1 . ILE E  1 285 ? 2.186   -32.288 10.011  1.00 47.85  ? 285  ILE E CD1 1 
ATOM   10215 N N   . GLY E  1 286 ? -0.915  -29.888 13.177  1.00 49.99  ? 286  GLY E N   1 
ATOM   10216 C CA  . GLY E  1 286 ? -1.514  -30.606 14.295  1.00 50.63  ? 286  GLY E CA  1 
ATOM   10217 C C   . GLY E  1 286 ? -0.784  -30.419 15.623  1.00 55.58  ? 286  GLY E C   1 
ATOM   10218 O O   . GLY E  1 286 ? 0.375   -30.006 15.644  1.00 55.95  ? 286  GLY E O   1 
ATOM   10219 N N   . ALA E  1 287 ? -1.455  -30.711 16.734  1.00 51.04  ? 287  ALA E N   1 
ATOM   10220 C CA  . ALA E  1 287 ? -0.863  -30.499 18.047  1.00 50.10  ? 287  ALA E CA  1 
ATOM   10221 C C   . ALA E  1 287 ? -0.256  -31.789 18.624  1.00 55.10  ? 287  ALA E C   1 
ATOM   10222 O O   . ALA E  1 287 ? -0.571  -32.895 18.166  1.00 51.56  ? 287  ALA E O   1 
ATOM   10223 C CB  . ALA E  1 287 ? -1.890  -29.937 18.989  1.00 50.20  ? 287  ALA E CB  1 
ATOM   10224 N N   . ILE E  1 288 ? 0.589   -31.629 19.649  1.00 53.77  ? 288  ILE E N   1 
ATOM   10225 C CA  . ILE E  1 288 ? 1.344   -32.735 20.254  1.00 57.80  ? 288  ILE E CA  1 
ATOM   10226 C C   . ILE E  1 288 ? 1.144   -32.835 21.784  1.00 61.20  ? 288  ILE E C   1 
ATOM   10227 O O   . ILE E  1 288 ? 1.365   -31.862 22.514  1.00 62.75  ? 288  ILE E O   1 
ATOM   10228 C CB  . ILE E  1 288 ? 2.857   -32.590 19.969  1.00 57.12  ? 288  ILE E CB  1 
ATOM   10229 C CG1 . ILE E  1 288 ? 3.157   -32.792 18.486  1.00 51.46  ? 288  ILE E CG1 1 
ATOM   10230 C CG2 . ILE E  1 288 ? 3.670   -33.567 20.822  1.00 54.79  ? 288  ILE E CG2 1 
ATOM   10231 C CD1 . ILE E  1 288 ? 4.592   -32.450 18.114  1.00 51.20  ? 288  ILE E CD1 1 
ATOM   10232 N N   . ASN E  1 289 ? 0.743   -34.016 22.257  1.00 59.24  ? 289  ASN E N   1 
ATOM   10233 C CA  . ASN E  1 289 ? 0.627   -34.306 23.692  1.00 63.08  ? 289  ASN E CA  1 
ATOM   10234 C C   . ASN E  1 289 ? 1.509   -35.529 23.917  1.00 60.97  ? 289  ASN E C   1 
ATOM   10235 O O   . ASN E  1 289 ? 1.125   -36.649 23.571  1.00 62.22  ? 289  ASN E O   1 
ATOM   10236 C CB  . ASN E  1 289 ? -0.850  -34.548 24.108  1.00 63.82  ? 289  ASN E CB  1 
ATOM   10237 C CG  . ASN E  1 289 ? -1.077  -34.556 25.640  1.00 70.05  ? 289  ASN E CG  1 
ATOM   10238 O OD1 . ASN E  1 289 ? -0.266  -34.055 26.420  1.00 72.82  ? 289  ASN E OD1 1 
ATOM   10239 N ND2 . ASN E  1 289 ? -2.221  -35.094 26.058  1.00 72.46  ? 289  ASN E ND2 1 
ATOM   10240 N N   . SER E  1 290 ? 2.726   -35.307 24.409  1.00 57.50  ? 290  SER E N   1 
ATOM   10241 C CA  . SER E  1 290 ? 3.721   -36.374 24.466  1.00 57.08  ? 290  SER E CA  1 
ATOM   10242 C C   . SER E  1 290 ? 4.705   -36.247 25.633  1.00 63.87  ? 290  SER E C   1 
ATOM   10243 O O   . SER E  1 290 ? 4.804   -35.198 26.273  1.00 62.14  ? 290  SER E O   1 
ATOM   10244 C CB  . SER E  1 290 ? 4.507   -36.414 23.157  1.00 56.77  ? 290  SER E CB  1 
ATOM   10245 O OG  . SER E  1 290 ? 5.448   -37.475 23.140  1.00 62.46  ? 290  SER E OG  1 
ATOM   10246 N N   . SER E  1 291 ? 5.445   -37.323 25.888  1.00 61.80  ? 291  SER E N   1 
ATOM   10247 C CA  . SER E  1 291 ? 6.482   -37.324 26.921  1.00 68.90  ? 291  SER E CA  1 
ATOM   10248 C C   . SER E  1 291 ? 7.850   -37.737 26.358  1.00 66.84  ? 291  SER E C   1 
ATOM   10249 O O   . SER E  1 291 ? 8.851   -37.745 27.075  1.00 73.84  ? 291  SER E O   1 
ATOM   10250 C CB  . SER E  1 291 ? 6.088   -38.251 28.079  1.00 73.48  ? 291  SER E CB  1 
ATOM   10251 O OG  . SER E  1 291 ? 5.757   -39.553 27.614  1.00 68.98  ? 291  SER E OG  1 
ATOM   10252 N N   . MET E  1 292 ? 7.874   -38.081 25.074  1.00 63.40  ? 292  MET E N   1 
ATOM   10253 C CA  . MET E  1 292 ? 9.100   -38.425 24.367  1.00 61.31  ? 292  MET E CA  1 
ATOM   10254 C C   . MET E  1 292 ? 10.041  -37.207 24.305  1.00 62.29  ? 292  MET E C   1 
ATOM   10255 O O   . MET E  1 292 ? 9.581   -36.064 24.201  1.00 56.58  ? 292  MET E O   1 
ATOM   10256 C CB  . MET E  1 292 ? 8.762   -38.873 22.945  1.00 61.17  ? 292  MET E CB  1 
ATOM   10257 C CG  . MET E  1 292 ? 7.571   -39.793 22.832  1.00 56.72  ? 292  MET E CG  1 
ATOM   10258 S SD  . MET E  1 292 ? 7.995   -41.519 22.969  1.00 68.85  ? 292  MET E SD  1 
ATOM   10259 C CE  . MET E  1 292 ? 6.713   -42.254 21.944  1.00 59.65  ? 292  MET E CE  1 
ATOM   10260 N N   . PRO E  1 293 ? 11.363  -37.440 24.350  1.00 64.30  ? 293  PRO E N   1 
ATOM   10261 C CA  . PRO E  1 293 ? 12.322  -36.334 24.238  1.00 55.68  ? 293  PRO E CA  1 
ATOM   10262 C C   . PRO E  1 293 ? 12.559  -35.887 22.797  1.00 54.85  ? 293  PRO E C   1 
ATOM   10263 O O   . PRO E  1 293 ? 13.177  -34.852 22.595  1.00 59.87  ? 293  PRO E O   1 
ATOM   10264 C CB  . PRO E  1 293 ? 13.597  -36.917 24.858  1.00 52.98  ? 293  PRO E CB  1 
ATOM   10265 C CG  . PRO E  1 293 ? 13.494  -38.361 24.629  1.00 56.36  ? 293  PRO E CG  1 
ATOM   10266 C CD  . PRO E  1 293 ? 12.025  -38.696 24.746  1.00 62.76  ? 293  PRO E CD  1 
ATOM   10267 N N   . PHE E  1 294 ? 12.102  -36.664 21.821  1.00 55.12  ? 294  PHE E N   1 
ATOM   10268 C CA  . PHE E  1 294 ? 12.236  -36.294 20.409  1.00 57.75  ? 294  PHE E CA  1 
ATOM   10269 C C   . PHE E  1 294 ? 10.893  -36.445 19.672  1.00 56.53  ? 294  PHE E C   1 
ATOM   10270 O O   . PHE E  1 294 ? 10.028  -37.208 20.095  1.00 57.51  ? 294  PHE E O   1 
ATOM   10271 C CB  . PHE E  1 294 ? 13.299  -37.158 19.700  1.00 55.68  ? 294  PHE E CB  1 
ATOM   10272 C CG  . PHE E  1 294 ? 14.715  -36.931 20.180  1.00 59.39  ? 294  PHE E CG  1 
ATOM   10273 C CD1 . PHE E  1 294 ? 15.414  -35.779 19.826  1.00 58.71  ? 294  PHE E CD1 1 
ATOM   10274 C CD2 . PHE E  1 294 ? 15.359  -37.885 20.969  1.00 59.81  ? 294  PHE E CD2 1 
ATOM   10275 C CE1 . PHE E  1 294 ? 16.725  -35.576 20.262  1.00 57.59  ? 294  PHE E CE1 1 
ATOM   10276 C CE2 . PHE E  1 294 ? 16.670  -37.697 21.402  1.00 55.67  ? 294  PHE E CE2 1 
ATOM   10277 C CZ  . PHE E  1 294 ? 17.355  -36.542 21.050  1.00 57.15  ? 294  PHE E CZ  1 
ATOM   10278 N N   . HIS E  1 295 ? 10.740  -35.732 18.557  1.00 53.90  ? 295  HIS E N   1 
ATOM   10279 C CA  . HIS E  1 295 ? 9.594   -35.912 17.664  1.00 52.39  ? 295  HIS E CA  1 
ATOM   10280 C C   . HIS E  1 295 ? 10.020  -35.656 16.221  1.00 50.16  ? 295  HIS E C   1 
ATOM   10281 O O   . HIS E  1 295 ? 11.132  -35.173 15.977  1.00 47.97  ? 295  HIS E O   1 
ATOM   10282 C CB  . HIS E  1 295 ? 8.420   -35.004 18.077  1.00 51.57  ? 295  HIS E CB  1 
ATOM   10283 C CG  . HIS E  1 295 ? 8.565   -33.567 17.667  1.00 53.03  ? 295  HIS E CG  1 
ATOM   10284 N ND1 . HIS E  1 295 ? 8.220   -33.106 16.411  1.00 51.08  ? 295  HIS E ND1 1 
ATOM   10285 C CD2 . HIS E  1 295 ? 9.004   -32.484 18.358  1.00 50.47  ? 295  HIS E CD2 1 
ATOM   10286 C CE1 . HIS E  1 295 ? 8.441   -31.803 16.347  1.00 50.06  ? 295  HIS E CE1 1 
ATOM   10287 N NE2 . HIS E  1 295 ? 8.917   -31.401 17.512  1.00 53.40  ? 295  HIS E NE2 1 
ATOM   10288 N N   . ASN E  1 296 ? 9.154   -36.010 15.269  1.00 49.61  ? 296  ASN E N   1 
ATOM   10289 C CA  . ASN E  1 296 ? 9.471   -35.850 13.850  1.00 44.26  ? 296  ASN E CA  1 
ATOM   10290 C C   . ASN E  1 296 ? 8.289   -35.352 13.011  1.00 43.18  ? 296  ASN E C   1 
ATOM   10291 O O   . ASN E  1 296 ? 8.230   -35.601 11.808  1.00 45.30  ? 296  ASN E O   1 
ATOM   10292 C CB  . ASN E  1 296 ? 10.024  -37.171 13.287  1.00 47.03  ? 296  ASN E CB  1 
ATOM   10293 C CG  . ASN E  1 296 ? 8.933   -38.243 13.004  1.00 48.62  ? 296  ASN E CG  1 
ATOM   10294 O OD1 . ASN E  1 296 ? 7.815   -38.213 13.535  1.00 47.87  ? 296  ASN E OD1 1 
ATOM   10295 N ND2 . ASN E  1 296 ? 9.303   -39.224 12.193  1.00 44.81  ? 296  ASN E ND2 1 
ATOM   10296 N N   . ILE E  1 297 ? 7.379   -34.604 13.634  1.00 45.70  ? 297  ILE E N   1 
ATOM   10297 C CA  . ILE E  1 297 ? 6.151   -34.143 12.961  1.00 48.60  ? 297  ILE E CA  1 
ATOM   10298 C C   . ILE E  1 297 ? 6.350   -32.909 12.051  1.00 49.17  ? 297  ILE E C   1 
ATOM   10299 O O   . ILE E  1 297 ? 5.867   -32.882 10.922  1.00 50.58  ? 297  ILE E O   1 
ATOM   10300 C CB  . ILE E  1 297 ? 5.034   -33.848 13.999  1.00 48.04  ? 297  ILE E CB  1 
ATOM   10301 C CG1 . ILE E  1 297 ? 4.461   -35.163 14.523  1.00 50.77  ? 297  ILE E CG1 1 
ATOM   10302 C CG2 . ILE E  1 297 ? 3.885   -33.057 13.371  1.00 50.68  ? 297  ILE E CG2 1 
ATOM   10303 C CD1 . ILE E  1 297 ? 5.130   -35.642 15.764  1.00 54.50  ? 297  ILE E CD1 1 
ATOM   10304 N N   . HIS E  1 298 ? 7.034   -31.887 12.562  1.00 47.31  ? 298  HIS E N   1 
ATOM   10305 C CA  . HIS E  1 298 ? 7.279   -30.648 11.833  1.00 45.05  ? 298  HIS E CA  1 
ATOM   10306 C C   . HIS E  1 298 ? 8.388   -29.874 12.560  1.00 46.14  ? 298  HIS E C   1 
ATOM   10307 O O   . HIS E  1 298 ? 8.538   -30.001 13.771  1.00 43.99  ? 298  HIS E O   1 
ATOM   10308 C CB  . HIS E  1 298 ? 5.991   -29.823 11.715  1.00 49.64  ? 298  HIS E CB  1 
ATOM   10309 C CG  . HIS E  1 298 ? 6.018   -28.805 10.614  1.00 49.25  ? 298  HIS E CG  1 
ATOM   10310 N ND1 . HIS E  1 298 ? 6.761   -27.646 10.689  1.00 49.17  ? 298  HIS E ND1 1 
ATOM   10311 C CD2 . HIS E  1 298 ? 5.414   -28.787 9.402   1.00 47.24  ? 298  HIS E CD2 1 
ATOM   10312 C CE1 . HIS E  1 298 ? 6.596   -26.949 9.578   1.00 46.72  ? 298  HIS E CE1 1 
ATOM   10313 N NE2 . HIS E  1 298 ? 5.787   -27.622 8.780   1.00 41.75  ? 298  HIS E NE2 1 
ATOM   10314 N N   . PRO E  1 299 ? 9.240   -29.165 11.814  1.00 44.31  ? 299  PRO E N   1 
ATOM   10315 C CA  . PRO E  1 299 ? 10.300  -28.373 12.455  1.00 44.43  ? 299  PRO E CA  1 
ATOM   10316 C C   . PRO E  1 299 ? 9.814   -27.058 13.038  1.00 45.28  ? 299  PRO E C   1 
ATOM   10317 O O   . PRO E  1 299 ? 10.460  -26.511 13.933  1.00 49.08  ? 299  PRO E O   1 
ATOM   10318 C CB  . PRO E  1 299 ? 11.298  -28.128 11.321  1.00 43.30  ? 299  PRO E CB  1 
ATOM   10319 C CG  . PRO E  1 299 ? 10.504  -28.316 10.070  1.00 49.81  ? 299  PRO E CG  1 
ATOM   10320 C CD  . PRO E  1 299 ? 9.515   -29.404 10.392  1.00 43.16  ? 299  PRO E CD  1 
ATOM   10321 N N   . LEU E  1 300 ? 8.671   -26.577 12.575  1.00 45.01  ? 300  LEU E N   1 
ATOM   10322 C CA  . LEU E  1 300 ? 8.142   -25.302 13.068  1.00 47.40  ? 300  LEU E CA  1 
ATOM   10323 C C   . LEU E  1 300 ? 7.089   -25.507 14.169  1.00 45.20  ? 300  LEU E C   1 
ATOM   10324 O O   . LEU E  1 300 ? 5.922   -25.799 13.896  1.00 44.12  ? 300  LEU E O   1 
ATOM   10325 C CB  . LEU E  1 300 ? 7.559   -24.491 11.901  1.00 46.19  ? 300  LEU E CB  1 
ATOM   10326 C CG  . LEU E  1 300 ? 8.598   -24.171 10.820  1.00 44.67  ? 300  LEU E CG  1 
ATOM   10327 C CD1 . LEU E  1 300 ? 8.011   -23.351 9.666   1.00 34.05  ? 300  LEU E CD1 1 
ATOM   10328 C CD2 . LEU E  1 300 ? 9.795   -23.462 11.465  1.00 43.35  ? 300  LEU E CD2 1 
ATOM   10329 N N   . THR E  1 301 ? 7.525   -25.408 15.420  1.00 44.70  ? 301  THR E N   1 
ATOM   10330 C CA  . THR E  1 301 ? 6.622   -25.603 16.546  1.00 43.82  ? 301  THR E CA  1 
ATOM   10331 C C   . THR E  1 301 ? 6.600   -24.381 17.446  1.00 40.98  ? 301  THR E C   1 
ATOM   10332 O O   . THR E  1 301 ? 7.495   -23.541 17.370  1.00 41.73  ? 301  THR E O   1 
ATOM   10333 C CB  . THR E  1 301 ? 7.020   -26.838 17.375  1.00 45.55  ? 301  THR E CB  1 
ATOM   10334 O OG1 . THR E  1 301 ? 8.202   -26.553 18.124  1.00 42.37  ? 301  THR E OG1 1 
ATOM   10335 C CG2 . THR E  1 301 ? 7.281   -28.041 16.458  1.00 49.10  ? 301  THR E CG2 1 
ATOM   10336 N N   . ILE E  1 302 ? 5.598   -24.303 18.318  1.00 42.35  ? 302  ILE E N   1 
ATOM   10337 C CA  . ILE E  1 302 ? 5.583   -23.298 19.387  1.00 42.55  ? 302  ILE E CA  1 
ATOM   10338 C C   . ILE E  1 302 ? 5.058   -23.944 20.663  1.00 45.36  ? 302  ILE E C   1 
ATOM   10339 O O   . ILE E  1 302 ? 4.163   -24.798 20.625  1.00 45.31  ? 302  ILE E O   1 
ATOM   10340 C CB  . ILE E  1 302 ? 4.710   -22.040 19.067  1.00 40.83  ? 302  ILE E CB  1 
ATOM   10341 C CG1 . ILE E  1 302 ? 4.963   -20.957 20.130  1.00 35.29  ? 302  ILE E CG1 1 
ATOM   10342 C CG2 . ILE E  1 302 ? 3.215   -22.392 18.975  1.00 39.20  ? 302  ILE E CG2 1 
ATOM   10343 C CD1 . ILE E  1 302 ? 4.165   -19.685 19.970  1.00 40.30  ? 302  ILE E CD1 1 
ATOM   10344 N N   . GLY E  1 303 ? 5.631   -23.545 21.794  1.00 48.08  ? 303  GLY E N   1 
ATOM   10345 C CA  . GLY E  1 303 ? 5.252   -24.115 23.071  1.00 50.98  ? 303  GLY E CA  1 
ATOM   10346 C C   . GLY E  1 303 ? 6.321   -24.993 23.680  1.00 48.78  ? 303  GLY E C   1 
ATOM   10347 O O   . GLY E  1 303 ? 7.495   -24.870 23.347  1.00 50.85  ? 303  GLY E O   1 
ATOM   10348 N N   . GLU E  1 304 ? 5.911   -25.864 24.596  1.00 50.54  ? 304  GLU E N   1 
ATOM   10349 C CA  . GLU E  1 304 ? 6.837   -26.758 25.273  1.00 53.52  ? 304  GLU E CA  1 
ATOM   10350 C C   . GLU E  1 304 ? 6.932   -28.062 24.498  1.00 50.86  ? 304  GLU E C   1 
ATOM   10351 O O   . GLU E  1 304 ? 6.067   -28.920 24.656  1.00 55.71  ? 304  GLU E O   1 
ATOM   10352 C CB  . GLU E  1 304 ? 6.400   -27.043 26.714  1.00 55.97  ? 304  GLU E CB  1 
ATOM   10353 C CG  . GLU E  1 304 ? 7.479   -27.808 27.488  1.00 65.39  ? 304  GLU E CG  1 
ATOM   10354 C CD  . GLU E  1 304 ? 7.102   -28.149 28.921  1.00 76.25  ? 304  GLU E CD  1 
ATOM   10355 O OE1 . GLU E  1 304 ? 6.047   -28.792 29.133  1.00 75.72  ? 304  GLU E OE1 1 
ATOM   10356 O OE2 . GLU E  1 304 ? 7.884   -27.804 29.836  1.00 87.93  ? 304  GLU E OE2 1 
ATOM   10357 N N   . CYS E  1 305 ? 7.958   -28.208 23.659  1.00 47.07  ? 305  CYS E N   1 
ATOM   10358 C CA  . CYS E  1 305 ? 8.015   -29.321 22.699  1.00 51.54  ? 305  CYS E CA  1 
ATOM   10359 C C   . CYS E  1 305 ? 9.226   -30.246 22.842  1.00 50.65  ? 305  CYS E C   1 
ATOM   10360 O O   . CYS E  1 305 ? 10.262  -29.859 23.390  1.00 50.72  ? 305  CYS E O   1 
ATOM   10361 C CB  . CYS E  1 305 ? 7.999   -28.780 21.265  1.00 52.54  ? 305  CYS E CB  1 
ATOM   10362 S SG  . CYS E  1 305 ? 6.535   -27.825 20.862  1.00 63.58  ? 305  CYS E SG  1 
ATOM   10363 N N   . PRO E  1 306 ? 9.104   -31.474 22.315  1.00 51.03  ? 306  PRO E N   1 
ATOM   10364 C CA  . PRO E  1 306 ? 10.251  -32.368 22.140  1.00 52.40  ? 306  PRO E CA  1 
ATOM   10365 C C   . PRO E  1 306 ? 11.274  -31.766 21.170  1.00 58.02  ? 306  PRO E C   1 
ATOM   10366 O O   . PRO E  1 306 ? 10.981  -30.748 20.543  1.00 61.89  ? 306  PRO E O   1 
ATOM   10367 C CB  . PRO E  1 306 ? 9.618   -33.634 21.545  1.00 50.06  ? 306  PRO E CB  1 
ATOM   10368 C CG  . PRO E  1 306 ? 8.221   -33.594 21.967  1.00 46.96  ? 306  PRO E CG  1 
ATOM   10369 C CD  . PRO E  1 306 ? 7.839   -32.148 21.973  1.00 51.13  ? 306  PRO E CD  1 
ATOM   10370 N N   . LYS E  1 307 ? 12.438  -32.386 21.023  1.00 54.86  ? 307  LYS E N   1 
ATOM   10371 C CA  . LYS E  1 307 ? 13.428  -31.858 20.107  1.00 56.91  ? 307  LYS E CA  1 
ATOM   10372 C C   . LYS E  1 307 ? 13.134  -32.479 18.743  1.00 56.62  ? 307  LYS E C   1 
ATOM   10373 O O   . LYS E  1 307 ? 12.733  -33.635 18.682  1.00 56.48  ? 307  LYS E O   1 
ATOM   10374 C CB  . LYS E  1 307 ? 14.850  -32.178 20.580  1.00 56.36  ? 307  LYS E CB  1 
ATOM   10375 C CG  . LYS E  1 307 ? 15.183  -31.598 21.955  1.00 63.50  ? 307  LYS E CG  1 
ATOM   10376 C CD  . LYS E  1 307 ? 14.862  -30.102 22.093  1.00 65.59  ? 307  LYS E CD  1 
ATOM   10377 C CE  . LYS E  1 307 ? 15.809  -29.225 21.299  1.00 71.03  ? 307  LYS E CE  1 
ATOM   10378 N NZ  . LYS E  1 307 ? 15.662  -27.777 21.624  1.00 73.64  ? 307  LYS E NZ  1 
ATOM   10379 N N   . TYR E  1 308 ? 13.283  -31.709 17.662  1.00 55.65  ? 308  TYR E N   1 
ATOM   10380 C CA  . TYR E  1 308 ? 12.936  -32.202 16.332  1.00 47.29  ? 308  TYR E CA  1 
ATOM   10381 C C   . TYR E  1 308 ? 14.126  -32.903 15.669  1.00 46.78  ? 308  TYR E C   1 
ATOM   10382 O O   . TYR E  1 308 ? 15.252  -32.418 15.750  1.00 42.50  ? 308  TYR E O   1 
ATOM   10383 C CB  . TYR E  1 308 ? 12.438  -31.066 15.426  1.00 40.51  ? 308  TYR E CB  1 
ATOM   10384 C CG  . TYR E  1 308 ? 12.144  -31.545 14.014  1.00 44.24  ? 308  TYR E CG  1 
ATOM   10385 C CD1 . TYR E  1 308 ? 10.959  -32.226 13.717  1.00 45.73  ? 308  TYR E CD1 1 
ATOM   10386 C CD2 . TYR E  1 308 ? 13.064  -31.377 13.003  1.00 39.78  ? 308  TYR E CD2 1 
ATOM   10387 C CE1 . TYR E  1 308 ? 10.697  -32.694 12.452  1.00 40.99  ? 308  TYR E CE1 1 
ATOM   10388 C CE2 . TYR E  1 308 ? 12.813  -31.839 11.733  1.00 48.33  ? 308  TYR E CE2 1 
ATOM   10389 C CZ  . TYR E  1 308 ? 11.626  -32.500 11.453  1.00 45.77  ? 308  TYR E CZ  1 
ATOM   10390 O OH  . TYR E  1 308 ? 11.389  -32.959 10.168  1.00 33.34  ? 308  TYR E OH  1 
ATOM   10391 N N   . VAL E  1 309 ? 13.869  -34.047 15.029  1.00 44.20  ? 309  VAL E N   1 
ATOM   10392 C CA  . VAL E  1 309 ? 14.883  -34.746 14.231  1.00 45.28  ? 309  VAL E CA  1 
ATOM   10393 C C   . VAL E  1 309 ? 14.233  -35.311 12.955  1.00 44.13  ? 309  VAL E C   1 
ATOM   10394 O O   . VAL E  1 309 ? 13.009  -35.447 12.891  1.00 45.53  ? 309  VAL E O   1 
ATOM   10395 C CB  . VAL E  1 309 ? 15.592  -35.882 15.035  1.00 44.59  ? 309  VAL E CB  1 
ATOM   10396 C CG1 . VAL E  1 309 ? 16.441  -35.283 16.159  1.00 35.90  ? 309  VAL E CG1 1 
ATOM   10397 C CG2 . VAL E  1 309 ? 14.589  -36.890 15.584  1.00 39.77  ? 309  VAL E CG2 1 
ATOM   10398 N N   . LYS E  1 310 ? 15.038  -35.602 11.934  1.00 43.43  ? 310  LYS E N   1 
ATOM   10399 C CA  . LYS E  1 310 ? 14.514  -36.183 10.691  1.00 48.17  ? 310  LYS E CA  1 
ATOM   10400 C C   . LYS E  1 310 ? 14.555  -37.719 10.639  1.00 57.04  ? 310  LYS E C   1 
ATOM   10401 O O   . LYS E  1 310 ? 14.644  -38.303 9.550   1.00 58.22  ? 310  LYS E O   1 
ATOM   10402 C CB  . LYS E  1 310 ? 15.277  -35.646 9.480   1.00 46.95  ? 310  LYS E CB  1 
ATOM   10403 C CG  . LYS E  1 310 ? 14.968  -34.227 9.130   1.00 51.25  ? 310  LYS E CG  1 
ATOM   10404 C CD  . LYS E  1 310 ? 15.488  -33.881 7.753   1.00 46.69  ? 310  LYS E CD  1 
ATOM   10405 C CE  . LYS E  1 310 ? 16.943  -33.485 7.799   1.00 54.75  ? 310  LYS E CE  1 
ATOM   10406 N NZ  . LYS E  1 310 ? 17.475  -33.158 6.419   1.00 57.78  ? 310  LYS E NZ  1 
ATOM   10407 N N   . SER E  1 311 ? 14.537  -38.363 11.808  1.00 57.26  ? 311  SER E N   1 
ATOM   10408 C CA  . SER E  1 311 ? 14.621  -39.824 11.898  1.00 54.10  ? 311  SER E CA  1 
ATOM   10409 C C   . SER E  1 311 ? 13.256  -40.492 11.849  1.00 57.01  ? 311  SER E C   1 
ATOM   10410 O O   . SER E  1 311 ? 12.255  -39.920 12.302  1.00 52.54  ? 311  SER E O   1 
ATOM   10411 C CB  . SER E  1 311 ? 15.340  -40.253 13.179  1.00 53.66  ? 311  SER E CB  1 
ATOM   10412 O OG  . SER E  1 311 ? 16.615  -39.653 13.282  1.00 52.95  ? 311  SER E OG  1 
ATOM   10413 N N   . ASN E  1 312 ? 13.232  -41.712 11.314  1.00 59.74  ? 312  ASN E N   1 
ATOM   10414 C CA  . ASN E  1 312 ? 12.027  -42.542 11.325  1.00 61.03  ? 312  ASN E CA  1 
ATOM   10415 C C   . ASN E  1 312 ? 11.904  -43.352 12.629  1.00 61.09  ? 312  ASN E C   1 
ATOM   10416 O O   . ASN E  1 312 ? 10.794  -43.622 13.106  1.00 63.82  ? 312  ASN E O   1 
ATOM   10417 C CB  . ASN E  1 312 ? 12.034  -43.495 10.125  1.00 62.82  ? 312  ASN E CB  1 
ATOM   10418 C CG  . ASN E  1 312 ? 12.032  -42.763 8.789   1.00 71.00  ? 312  ASN E CG  1 
ATOM   10419 O OD1 . ASN E  1 312 ? 11.524  -41.643 8.670   1.00 66.71  ? 312  ASN E OD1 1 
ATOM   10420 N ND2 . ASN E  1 312 ? 12.623  -43.393 7.776   1.00 69.67  ? 312  ASN E ND2 1 
ATOM   10421 N N   . ARG E  1 313 ? 13.047  -43.690 13.228  1.00 55.77  ? 313  ARG E N   1 
ATOM   10422 C CA  . ARG E  1 313 ? 13.071  -44.497 14.450  1.00 60.71  ? 313  ARG E CA  1 
ATOM   10423 C C   . ARG E  1 313 ? 14.232  -44.204 15.392  1.00 58.06  ? 313  ARG E C   1 
ATOM   10424 O O   . ARG E  1 313 ? 15.379  -44.045 14.966  1.00 53.59  ? 313  ARG E O   1 
ATOM   10425 C CB  . ARG E  1 313 ? 13.108  -45.985 14.100  1.00 66.53  ? 313  ARG E CB  1 
ATOM   10426 C CG  . ARG E  1 313 ? 11.744  -46.608 13.922  1.00 71.83  ? 313  ARG E CG  1 
ATOM   10427 C CD  . ARG E  1 313 ? 11.832  -48.110 13.689  1.00 72.88  ? 313  ARG E CD  1 
ATOM   10428 N NE  . ARG E  1 313 ? 12.252  -48.819 14.893  1.00 78.21  ? 313  ARG E NE  1 
ATOM   10429 C CZ  . ARG E  1 313 ? 11.410  -49.299 15.803  1.00 82.01  ? 313  ARG E CZ  1 
ATOM   10430 N NH1 . ARG E  1 313 ? 10.102  -49.099 15.665  1.00 80.79  ? 313  ARG E NH1 1 
ATOM   10431 N NH2 . ARG E  1 313 ? 11.878  -49.942 16.869  1.00 82.19  ? 313  ARG E NH2 1 
ATOM   10432 N N   . LEU E  1 314 ? 13.929  -44.217 16.685  1.00 57.67  ? 314  LEU E N   1 
ATOM   10433 C CA  . LEU E  1 314 ? 14.940  -44.037 17.719  1.00 55.65  ? 314  LEU E CA  1 
ATOM   10434 C C   . LEU E  1 314 ? 14.617  -44.874 18.952  1.00 54.93  ? 314  LEU E C   1 
ATOM   10435 O O   . LEU E  1 314 ? 13.802  -44.480 19.794  1.00 55.57  ? 314  LEU E O   1 
ATOM   10436 C CB  . LEU E  1 314 ? 15.063  -42.565 18.108  1.00 56.02  ? 314  LEU E CB  1 
ATOM   10437 C CG  . LEU E  1 314 ? 16.093  -41.706 17.377  1.00 50.86  ? 314  LEU E CG  1 
ATOM   10438 C CD1 . LEU E  1 314 ? 16.318  -40.407 18.146  1.00 54.74  ? 314  LEU E CD1 1 
ATOM   10439 C CD2 . LEU E  1 314 ? 17.387  -42.454 17.207  1.00 42.37  ? 314  LEU E CD2 1 
ATOM   10440 N N   . VAL E  1 315 ? 15.263  -46.032 19.052  1.00 51.77  ? 315  VAL E N   1 
ATOM   10441 C CA  . VAL E  1 315 ? 15.015  -46.938 20.166  1.00 57.65  ? 315  VAL E CA  1 
ATOM   10442 C C   . VAL E  1 315 ? 16.315  -47.291 20.933  1.00 52.45  ? 315  VAL E C   1 
ATOM   10443 O O   . VAL E  1 315 ? 17.350  -47.614 20.338  1.00 49.26  ? 315  VAL E O   1 
ATOM   10444 C CB  . VAL E  1 315 ? 14.314  -48.226 19.659  1.00 58.87  ? 315  VAL E CB  1 
ATOM   10445 C CG1 . VAL E  1 315 ? 15.040  -48.784 18.438  1.00 62.28  ? 315  VAL E CG1 1 
ATOM   10446 C CG2 . VAL E  1 315 ? 14.227  -49.267 20.760  1.00 59.21  ? 315  VAL E CG2 1 
ATOM   10447 N N   . LEU E  1 316 ? 16.248  -47.186 22.259  1.00 50.30  ? 316  LEU E N   1 
ATOM   10448 C CA  . LEU E  1 316 ? 17.408  -47.404 23.123  1.00 58.55  ? 316  LEU E CA  1 
ATOM   10449 C C   . LEU E  1 316 ? 17.403  -48.749 23.838  1.00 59.93  ? 316  LEU E C   1 
ATOM   10450 O O   . LEU E  1 316 ? 16.420  -49.117 24.492  1.00 61.15  ? 316  LEU E O   1 
ATOM   10451 C CB  . LEU E  1 316 ? 17.511  -46.291 24.164  1.00 56.28  ? 316  LEU E CB  1 
ATOM   10452 C CG  . LEU E  1 316 ? 18.301  -45.076 23.705  1.00 53.18  ? 316  LEU E CG  1 
ATOM   10453 C CD1 . LEU E  1 316 ? 18.088  -43.925 24.674  1.00 59.43  ? 316  LEU E CD1 1 
ATOM   10454 C CD2 . LEU E  1 316 ? 19.778  -45.451 23.597  1.00 48.45  ? 316  LEU E CD2 1 
ATOM   10455 N N   . ALA E  1 317 ? 18.535  -49.441 23.784  1.00 58.84  ? 317  ALA E N   1 
ATOM   10456 C CA  . ALA E  1 317 ? 18.664  -50.710 24.489  1.00 62.24  ? 317  ALA E CA  1 
ATOM   10457 C C   . ALA E  1 317 ? 18.768  -50.487 25.999  1.00 64.05  ? 317  ALA E C   1 
ATOM   10458 O O   . ALA E  1 317 ? 19.672  -49.787 26.471  1.00 60.95  ? 317  ALA E O   1 
ATOM   10459 C CB  . ALA E  1 317 ? 19.881  -51.499 23.969  1.00 53.44  ? 317  ALA E CB  1 
ATOM   10460 N N   . THR E  1 318 ? 17.863  -51.131 26.743  1.00 65.79  ? 318  THR E N   1 
ATOM   10461 C CA  . THR E  1 318 ? 17.854  -51.073 28.199  1.00 63.98  ? 318  THR E CA  1 
ATOM   10462 C C   . THR E  1 318 ? 18.202  -52.441 28.791  1.00 69.75  ? 318  THR E C   1 
ATOM   10463 O O   . THR E  1 318 ? 18.942  -52.539 29.775  1.00 68.91  ? 318  THR E O   1 
ATOM   10464 C CB  . THR E  1 318 ? 16.472  -50.650 28.739  1.00 63.96  ? 318  THR E CB  1 
ATOM   10465 O OG1 . THR E  1 318 ? 15.455  -51.451 28.126  1.00 65.78  ? 318  THR E OG1 1 
ATOM   10466 C CG2 . THR E  1 318 ? 16.196  -49.192 28.453  1.00 66.78  ? 318  THR E CG2 1 
ATOM   10467 N N   . GLY E  1 319 ? 17.703  -53.494 28.148  1.00 69.99  ? 319  GLY E N   1 
ATOM   10468 C CA  . GLY E  1 319 ? 17.927  -54.862 28.593  1.00 71.61  ? 319  GLY E CA  1 
ATOM   10469 C C   . GLY E  1 319 ? 19.086  -55.555 27.908  1.00 64.85  ? 319  GLY E C   1 
ATOM   10470 O O   . GLY E  1 319 ? 20.056  -54.917 27.532  1.00 64.77  ? 319  GLY E O   1 
ATOM   10471 N N   . LEU E  1 320 ? 19.010  -56.872 27.788  1.00 64.44  ? 320  LEU E N   1 
ATOM   10472 C CA  . LEU E  1 320 ? 20.057  -57.615 27.098  1.00 68.46  ? 320  LEU E CA  1 
ATOM   10473 C C   . LEU E  1 320 ? 19.488  -58.382 25.893  1.00 66.24  ? 320  LEU E C   1 
ATOM   10474 O O   . LEU E  1 320 ? 18.287  -58.331 25.627  1.00 67.09  ? 320  LEU E O   1 
ATOM   10475 C CB  . LEU E  1 320 ? 20.771  -58.551 28.072  1.00 65.47  ? 320  LEU E CB  1 
ATOM   10476 C CG  . LEU E  1 320 ? 19.832  -59.396 28.921  1.00 69.50  ? 320  LEU E CG  1 
ATOM   10477 C CD1 . LEU E  1 320 ? 19.624  -60.745 28.269  1.00 71.64  ? 320  LEU E CD1 1 
ATOM   10478 C CD2 . LEU E  1 320 ? 20.393  -59.556 30.331  1.00 69.82  ? 320  LEU E CD2 1 
ATOM   10479 N N   . ARG E  1 321 ? 20.361  -59.051 25.147  1.00 63.04  ? 321  ARG E N   1 
ATOM   10480 C CA  . ARG E  1 321 ? 19.953  -59.797 23.957  1.00 63.75  ? 321  ARG E CA  1 
ATOM   10481 C C   . ARG E  1 321 ? 19.039  -60.981 24.296  1.00 69.28  ? 321  ARG E C   1 
ATOM   10482 O O   . ARG E  1 321 ? 19.337  -61.772 25.199  1.00 66.93  ? 321  ARG E O   1 
ATOM   10483 C CB  . ARG E  1 321 ? 21.184  -60.303 23.221  1.00 59.93  ? 321  ARG E CB  1 
ATOM   10484 C CG  . ARG E  1 321 ? 20.900  -60.871 21.854  1.00 69.61  ? 321  ARG E CG  1 
ATOM   10485 C CD  . ARG E  1 321 ? 22.181  -61.422 21.252  1.00 75.72  ? 321  ARG E CD  1 
ATOM   10486 N NE  . ARG E  1 321 ? 23.211  -60.391 21.164  1.00 74.94  ? 321  ARG E NE  1 
ATOM   10487 C CZ  . ARG E  1 321 ? 23.600  -59.833 20.021  1.00 75.95  ? 321  ARG E CZ  1 
ATOM   10488 N NH1 . ARG E  1 321 ? 23.038  -60.215 18.880  1.00 67.54  ? 321  ARG E NH1 1 
ATOM   10489 N NH2 . ARG E  1 321 ? 24.549  -58.897 20.020  1.00 75.22  ? 321  ARG E NH2 1 
ATOM   10490 N N   . ASN E  1 322 ? 17.945  -61.129 23.553  1.00 69.94  ? 322  ASN E N   1 
ATOM   10491 C CA  . ASN E  1 322 ? 16.960  -62.147 23.900  1.00 76.49  ? 322  ASN E CA  1 
ATOM   10492 C C   . ASN E  1 322 ? 17.079  -63.466 23.142  1.00 81.48  ? 322  ASN E C   1 
ATOM   10493 O O   . ASN E  1 322 ? 17.054  -63.507 21.904  1.00 76.92  ? 322  ASN E O   1 
ATOM   10494 C CB  . ASN E  1 322 ? 15.553  -61.612 23.670  1.00 75.27  ? 322  ASN E CB  1 
ATOM   10495 C CG  . ASN E  1 322 ? 14.552  -62.194 24.628  1.00 70.99  ? 322  ASN E CG  1 
ATOM   10496 O OD1 . ASN E  1 322 ? 14.741  -63.281 25.166  1.00 73.30  ? 322  ASN E OD1 1 
ATOM   10497 N ND2 . ASN E  1 322 ? 13.457  -61.485 24.821  1.00 74.38  ? 322  ASN E ND2 1 
ATOM   10498 N N   . SER E  1 323 ? 17.156  -64.542 23.926  1.00 92.39  ? 323  SER E N   1 
ATOM   10499 C CA  . SER E  1 323 ? 17.272  -65.911 23.428  1.00 92.62  ? 323  SER E CA  1 
ATOM   10500 C C   . SER E  1 323 ? 15.940  -66.418 22.840  1.00 91.20  ? 323  SER E C   1 
ATOM   10501 O O   . SER E  1 323 ? 14.893  -66.344 23.508  1.00 87.17  ? 323  SER E O   1 
ATOM   10502 C CB  . SER E  1 323 ? 17.744  -66.835 24.565  1.00 89.04  ? 323  SER E CB  1 
ATOM   10503 O OG  . SER E  1 323 ? 18.780  -66.234 25.335  1.00 81.22  ? 323  SER E OG  1 
ATOM   10504 N N   . PRO E  1 324 ? 15.988  -66.972 21.608  1.00 94.07  ? 324  PRO E N   1 
ATOM   10505 C CA  . PRO E  1 324 ? 14.810  -67.482 20.883  1.00 97.81  ? 324  PRO E CA  1 
ATOM   10506 C C   . PRO E  1 324 ? 14.039  -68.567 21.644  1.00 97.27  ? 324  PRO E C   1 
ATOM   10507 O O   . PRO E  1 324 ? 12.825  -68.684 21.454  1.00 95.47  ? 324  PRO E O   1 
ATOM   10508 C CB  . PRO E  1 324 ? 15.409  -68.053 19.589  1.00 90.47  ? 324  PRO E CB  1 
ATOM   10509 C CG  . PRO E  1 324 ? 16.844  -68.314 19.910  1.00 93.11  ? 324  PRO E CG  1 
ATOM   10510 C CD  . PRO E  1 324 ? 17.235  -67.215 20.858  1.00 92.46  ? 324  PRO E CD  1 
ATOM   10511 N N   . GLY F  2 1   ? 29.489  -61.278 22.265  1.00 55.29  ? 1    GLY F N   1 
ATOM   10512 C CA  . GLY F  2 1   ? 30.012  -60.086 22.907  1.00 61.07  ? 1    GLY F CA  1 
ATOM   10513 C C   . GLY F  2 1   ? 31.524  -60.092 23.057  1.00 68.06  ? 1    GLY F C   1 
ATOM   10514 O O   . GLY F  2 1   ? 32.206  -61.028 22.632  1.00 66.68  ? 1    GLY F O   1 
ATOM   10515 N N   . LEU F  2 2   ? 32.040  -59.050 23.704  1.00 73.07  ? 2    LEU F N   1 
ATOM   10516 C CA  . LEU F  2 2   ? 33.482  -58.835 23.846  1.00 73.01  ? 2    LEU F CA  1 
ATOM   10517 C C   . LEU F  2 2   ? 34.084  -59.581 25.032  1.00 75.57  ? 2    LEU F C   1 
ATOM   10518 O O   . LEU F  2 2   ? 35.258  -59.382 25.370  1.00 76.18  ? 2    LEU F O   1 
ATOM   10519 C CB  . LEU F  2 2   ? 33.771  -57.340 24.009  1.00 71.42  ? 2    LEU F CB  1 
ATOM   10520 C CG  . LEU F  2 2   ? 33.558  -56.435 22.805  1.00 69.51  ? 2    LEU F CG  1 
ATOM   10521 C CD1 . LEU F  2 2   ? 34.015  -55.036 23.146  1.00 68.98  ? 2    LEU F CD1 1 
ATOM   10522 C CD2 . LEU F  2 2   ? 34.334  -56.971 21.622  1.00 64.62  ? 2    LEU F CD2 1 
ATOM   10523 N N   . PHE F  2 3   ? 33.289  -60.465 25.632  1.00 76.96  ? 3    PHE F N   1 
ATOM   10524 C CA  . PHE F  2 3   ? 33.603  -61.026 26.941  1.00 75.62  ? 3    PHE F CA  1 
ATOM   10525 C C   . PHE F  2 3   ? 33.352  -62.539 26.929  1.00 81.21  ? 3    PHE F C   1 
ATOM   10526 O O   . PHE F  2 3   ? 33.946  -63.279 27.720  1.00 83.67  ? 3    PHE F O   1 
ATOM   10527 C CB  . PHE F  2 3   ? 32.819  -60.310 28.047  1.00 70.41  ? 3    PHE F CB  1 
ATOM   10528 C CG  . PHE F  2 3   ? 33.332  -58.921 28.320  1.00 70.74  ? 3    PHE F CG  1 
ATOM   10529 C CD1 . PHE F  2 3   ? 34.585  -58.729 28.889  1.00 69.09  ? 3    PHE F CD1 1 
ATOM   10530 C CD2 . PHE F  2 3   ? 32.578  -57.804 27.989  1.00 71.26  ? 3    PHE F CD2 1 
ATOM   10531 C CE1 . PHE F  2 3   ? 35.081  -57.447 29.116  1.00 68.05  ? 3    PHE F CE1 1 
ATOM   10532 C CE2 . PHE F  2 3   ? 33.062  -56.518 28.228  1.00 65.95  ? 3    PHE F CE2 1 
ATOM   10533 C CZ  . PHE F  2 3   ? 34.314  -56.340 28.790  1.00 62.70  ? 3    PHE F CZ  1 
ATOM   10534 N N   . GLY F  2 4   ? 32.450  -62.994 26.058  1.00 80.32  ? 4    GLY F N   1 
ATOM   10535 C CA  . GLY F  2 4   ? 32.286  -64.419 25.853  1.00 79.27  ? 4    GLY F CA  1 
ATOM   10536 C C   . GLY F  2 4   ? 31.278  -65.101 26.750  1.00 77.06  ? 4    GLY F C   1 
ATOM   10537 O O   . GLY F  2 4   ? 31.099  -66.315 26.677  1.00 77.81  ? 4    GLY F O   1 
ATOM   10538 N N   . ALA F  2 5   ? 30.636  -64.337 27.619  1.00 73.82  ? 5    ALA F N   1 
ATOM   10539 C CA  . ALA F  2 5   ? 29.706  -64.938 28.557  1.00 75.05  ? 5    ALA F CA  1 
ATOM   10540 C C   . ALA F  2 5   ? 28.322  -65.117 27.910  1.00 72.06  ? 5    ALA F C   1 
ATOM   10541 O O   . ALA F  2 5   ? 27.970  -66.232 27.541  1.00 71.60  ? 5    ALA F O   1 
ATOM   10542 C CB  . ALA F  2 5   ? 29.618  -64.104 29.827  1.00 65.78  ? 5    ALA F CB  1 
ATOM   10543 N N   . ILE F  2 6   ? 27.546  -64.043 27.763  1.00 71.33  ? 6    ILE F N   1 
ATOM   10544 C CA  . ILE F  2 6   ? 26.226  -64.138 27.126  1.00 68.62  ? 6    ILE F CA  1 
ATOM   10545 C C   . ILE F  2 6   ? 26.357  -64.611 25.664  1.00 73.19  ? 6    ILE F C   1 
ATOM   10546 O O   . ILE F  2 6   ? 27.162  -64.065 24.894  1.00 72.13  ? 6    ILE F O   1 
ATOM   10547 C CB  . ILE F  2 6   ? 25.475  -62.791 27.182  1.00 60.90  ? 6    ILE F CB  1 
ATOM   10548 C CG1 . ILE F  2 6   ? 25.157  -62.423 28.631  1.00 61.44  ? 6    ILE F CG1 1 
ATOM   10549 C CG2 . ILE F  2 6   ? 24.212  -62.833 26.317  1.00 60.78  ? 6    ILE F CG2 1 
ATOM   10550 C CD1 . ILE F  2 6   ? 24.452  -61.098 28.788  1.00 60.84  ? 6    ILE F CD1 1 
ATOM   10551 N N   . ALA F  2 7   ? 25.570  -65.627 25.297  1.00 71.86  ? 7    ALA F N   1 
ATOM   10552 C CA  . ALA F  2 7   ? 25.658  -66.284 23.981  1.00 73.69  ? 7    ALA F CA  1 
ATOM   10553 C C   . ALA F  2 7   ? 27.082  -66.793 23.661  1.00 75.71  ? 7    ALA F C   1 
ATOM   10554 O O   . ALA F  2 7   ? 27.501  -66.848 22.494  1.00 73.63  ? 7    ALA F O   1 
ATOM   10555 C CB  . ALA F  2 7   ? 25.167  -65.337 22.878  1.00 65.02  ? 7    ALA F CB  1 
ATOM   10556 N N   . GLY F  2 8   ? 27.807  -67.175 24.710  1.00 75.73  ? 8    GLY F N   1 
ATOM   10557 C CA  . GLY F  2 8   ? 29.176  -67.651 24.598  1.00 74.65  ? 8    GLY F CA  1 
ATOM   10558 C C   . GLY F  2 8   ? 29.334  -68.983 25.313  1.00 78.96  ? 8    GLY F C   1 
ATOM   10559 O O   . GLY F  2 8   ? 28.661  -69.953 24.958  1.00 81.11  ? 8    GLY F O   1 
ATOM   10560 N N   . PHE F  2 9   ? 30.190  -69.029 26.337  1.00 78.41  ? 9    PHE F N   1 
ATOM   10561 C CA  . PHE F  2 9   ? 30.407  -70.273 27.078  1.00 78.81  ? 9    PHE F CA  1 
ATOM   10562 C C   . PHE F  2 9   ? 29.171  -70.552 27.920  1.00 77.38  ? 9    PHE F C   1 
ATOM   10563 O O   . PHE F  2 9   ? 28.903  -71.698 28.280  1.00 78.90  ? 9    PHE F O   1 
ATOM   10564 C CB  . PHE F  2 9   ? 31.688  -70.221 27.935  1.00 77.95  ? 9    PHE F CB  1 
ATOM   10565 C CG  . PHE F  2 9   ? 31.597  -69.337 29.158  1.00 82.61  ? 9    PHE F CG  1 
ATOM   10566 C CD1 . PHE F  2 9   ? 31.132  -69.836 30.373  1.00 80.92  ? 9    PHE F CD1 1 
ATOM   10567 C CD2 . PHE F  2 9   ? 31.995  -68.011 29.097  1.00 81.45  ? 9    PHE F CD2 1 
ATOM   10568 C CE1 . PHE F  2 9   ? 31.062  -69.024 31.501  1.00 74.99  ? 9    PHE F CE1 1 
ATOM   10569 C CE2 . PHE F  2 9   ? 31.922  -67.195 30.220  1.00 78.56  ? 9    PHE F CE2 1 
ATOM   10570 C CZ  . PHE F  2 9   ? 31.453  -67.706 31.421  1.00 74.58  ? 9    PHE F CZ  1 
ATOM   10571 N N   . ILE F  2 10  ? 28.405  -69.503 28.202  1.00 76.91  ? 10   ILE F N   1 
ATOM   10572 C CA  . ILE F  2 10  ? 27.051  -69.681 28.712  1.00 80.07  ? 10   ILE F CA  1 
ATOM   10573 C C   . ILE F  2 10  ? 26.099  -69.528 27.542  1.00 82.54  ? 10   ILE F C   1 
ATOM   10574 O O   . ILE F  2 10  ? 26.105  -68.516 26.836  1.00 81.75  ? 10   ILE F O   1 
ATOM   10575 C CB  . ILE F  2 10  ? 26.653  -68.664 29.803  1.00 77.71  ? 10   ILE F CB  1 
ATOM   10576 C CG1 . ILE F  2 10  ? 27.702  -68.598 30.907  1.00 75.60  ? 10   ILE F CG1 1 
ATOM   10577 C CG2 . ILE F  2 10  ? 25.257  -68.994 30.359  1.00 69.42  ? 10   ILE F CG2 1 
ATOM   10578 C CD1 . ILE F  2 10  ? 27.293  -67.709 32.070  1.00 74.97  ? 10   ILE F CD1 1 
ATOM   10579 N N   . GLU F  2 11  ? 25.309  -70.562 27.313  1.00 89.41  ? 11   GLU F N   1 
ATOM   10580 C CA  . GLU F  2 11  ? 24.377  -70.553 26.209  1.00 87.97  ? 11   GLU F CA  1 
ATOM   10581 C C   . GLU F  2 11  ? 22.928  -70.300 26.656  1.00 88.62  ? 11   GLU F C   1 
ATOM   10582 O O   . GLU F  2 11  ? 22.429  -70.970 27.569  1.00 92.06  ? 11   GLU F O   1 
ATOM   10583 C CB  . GLU F  2 11  ? 24.503  -71.878 25.472  1.00 87.47  ? 11   GLU F CB  1 
ATOM   10584 C CG  . GLU F  2 11  ? 23.584  -72.009 24.306  1.00 103.14 ? 11   GLU F CG  1 
ATOM   10585 C CD  . GLU F  2 11  ? 23.573  -73.413 23.751  1.00 107.51 ? 11   GLU F CD  1 
ATOM   10586 O OE1 . GLU F  2 11  ? 24.255  -74.288 24.350  1.00 110.82 ? 11   GLU F OE1 1 
ATOM   10587 O OE2 . GLU F  2 11  ? 22.879  -73.628 22.723  1.00 110.90 ? 11   GLU F OE2 1 
ATOM   10588 N N   . GLY F  2 12  ? 22.265  -69.339 26.008  1.00 80.94  ? 12   GLY F N   1 
ATOM   10589 C CA  . GLY F  2 12  ? 20.847  -69.071 26.234  1.00 85.26  ? 12   GLY F CA  1 
ATOM   10590 C C   . GLY F  2 12  ? 20.439  -68.514 27.595  1.00 80.92  ? 12   GLY F C   1 
ATOM   10591 O O   . GLY F  2 12  ? 21.141  -68.692 28.595  1.00 81.64  ? 12   GLY F O   1 
ATOM   10592 N N   . GLY F  2 13  ? 19.281  -67.863 27.650  1.00 74.55  ? 13   GLY F N   1 
ATOM   10593 C CA  . GLY F  2 13  ? 18.817  -67.320 28.910  1.00 74.29  ? 13   GLY F CA  1 
ATOM   10594 C C   . GLY F  2 13  ? 17.690  -68.156 29.478  1.00 81.56  ? 13   GLY F C   1 
ATOM   10595 O O   . GLY F  2 13  ? 17.155  -69.027 28.794  1.00 88.23  ? 13   GLY F O   1 
ATOM   10596 N N   . TRP F  2 14  ? 17.326  -67.879 30.727  1.00 82.63  ? 14   TRP F N   1 
ATOM   10597 C CA  . TRP F  2 14  ? 16.293  -68.627 31.445  1.00 85.36  ? 14   TRP F CA  1 
ATOM   10598 C C   . TRP F  2 14  ? 14.970  -67.856 31.528  1.00 81.18  ? 14   TRP F C   1 
ATOM   10599 O O   . TRP F  2 14  ? 14.848  -66.904 32.309  1.00 80.73  ? 14   TRP F O   1 
ATOM   10600 C CB  . TRP F  2 14  ? 16.770  -68.962 32.866  1.00 84.46  ? 14   TRP F CB  1 
ATOM   10601 C CG  . TRP F  2 14  ? 18.056  -69.746 32.947  1.00 83.90  ? 14   TRP F CG  1 
ATOM   10602 C CD1 . TRP F  2 14  ? 18.522  -70.677 32.052  1.00 83.39  ? 14   TRP F CD1 1 
ATOM   10603 C CD2 . TRP F  2 14  ? 19.046  -69.656 33.982  1.00 82.67  ? 14   TRP F CD2 1 
ATOM   10604 N NE1 . TRP F  2 14  ? 19.739  -71.174 32.475  1.00 74.96  ? 14   TRP F NE1 1 
ATOM   10605 C CE2 . TRP F  2 14  ? 20.081  -70.560 33.653  1.00 78.02  ? 14   TRP F CE2 1 
ATOM   10606 C CE3 . TRP F  2 14  ? 19.158  -68.896 35.153  1.00 78.39  ? 14   TRP F CE3 1 
ATOM   10607 C CZ2 . TRP F  2 14  ? 21.209  -70.718 34.451  1.00 72.88  ? 14   TRP F CZ2 1 
ATOM   10608 C CZ3 . TRP F  2 14  ? 20.274  -69.055 35.938  1.00 76.99  ? 14   TRP F CZ3 1 
ATOM   10609 C CH2 . TRP F  2 14  ? 21.284  -69.963 35.588  1.00 77.68  ? 14   TRP F CH2 1 
ATOM   10610 N N   . GLN F  2 15  ? 13.973  -68.287 30.757  1.00 77.74  ? 15   GLN F N   1 
ATOM   10611 C CA  . GLN F  2 15  ? 12.661  -67.651 30.800  1.00 81.13  ? 15   GLN F CA  1 
ATOM   10612 C C   . GLN F  2 15  ? 11.997  -67.800 32.170  1.00 85.28  ? 15   GLN F C   1 
ATOM   10613 O O   . GLN F  2 15  ? 11.167  -66.972 32.562  1.00 83.23  ? 15   GLN F O   1 
ATOM   10614 C CB  . GLN F  2 15  ? 11.743  -68.217 29.697  1.00 79.94  ? 15   GLN F CB  1 
ATOM   10615 C CG  . GLN F  2 15  ? 12.192  -67.863 28.264  1.00 83.82  ? 15   GLN F CG  1 
ATOM   10616 C CD  . GLN F  2 15  ? 11.411  -68.577 27.154  1.00 82.90  ? 15   GLN F CD  1 
ATOM   10617 O OE1 . GLN F  2 15  ? 10.896  -69.686 27.326  1.00 86.80  ? 15   GLN F OE1 1 
ATOM   10618 N NE2 . GLN F  2 15  ? 11.283  -67.905 26.019  1.00 79.68  ? 15   GLN F NE2 1 
ATOM   10619 N N   . GLY F  2 16  ? 12.425  -68.801 32.936  1.00 86.20  ? 16   GLY F N   1 
ATOM   10620 C CA  . GLY F  2 16  ? 11.777  -69.088 34.201  1.00 86.34  ? 16   GLY F CA  1 
ATOM   10621 C C   . GLY F  2 16  ? 12.268  -68.189 35.309  1.00 85.36  ? 16   GLY F C   1 
ATOM   10622 O O   . GLY F  2 16  ? 11.667  -68.112 36.380  1.00 85.20  ? 16   GLY F O   1 
ATOM   10623 N N   . MET F  2 17  ? 13.338  -67.460 35.031  1.00 82.88  ? 17   MET F N   1 
ATOM   10624 C CA  . MET F  2 17  ? 13.857  -66.523 36.009  1.00 91.41  ? 17   MET F CA  1 
ATOM   10625 C C   . MET F  2 17  ? 13.292  -65.116 35.772  1.00 90.58  ? 17   MET F C   1 
ATOM   10626 O O   . MET F  2 17  ? 13.703  -64.422 34.845  1.00 88.04  ? 17   MET F O   1 
ATOM   10627 C CB  . MET F  2 17  ? 15.379  -66.507 35.971  1.00 89.61  ? 17   MET F CB  1 
ATOM   10628 C CG  . MET F  2 17  ? 15.973  -65.498 36.923  1.00 85.03  ? 17   MET F CG  1 
ATOM   10629 S SD  . MET F  2 17  ? 17.754  -65.528 36.852  1.00 82.38  ? 17   MET F SD  1 
ATOM   10630 C CE  . MET F  2 17  ? 18.094  -63.962 37.597  1.00 79.93  ? 17   MET F CE  1 
ATOM   10631 N N   . VAL F  2 18  ? 12.354  -64.696 36.619  1.00 86.47  ? 18   VAL F N   1 
ATOM   10632 C CA  . VAL F  2 18  ? 11.605  -63.469 36.363  1.00 89.98  ? 18   VAL F CA  1 
ATOM   10633 C C   . VAL F  2 18  ? 11.677  -62.469 37.525  1.00 91.39  ? 18   VAL F C   1 
ATOM   10634 O O   . VAL F  2 18  ? 10.720  -61.730 37.781  1.00 92.17  ? 18   VAL F O   1 
ATOM   10635 C CB  . VAL F  2 18  ? 10.107  -63.782 36.070  1.00 91.69  ? 18   VAL F CB  1 
ATOM   10636 C CG1 . VAL F  2 18  ? 9.524   -62.766 35.086  1.00 94.96  ? 18   VAL F CG1 1 
ATOM   10637 C CG2 . VAL F  2 18  ? 9.938   -65.197 35.529  1.00 86.76  ? 18   VAL F CG2 1 
ATOM   10638 N N   . ASP F  2 19  ? 12.802  -62.450 38.237  1.00 88.31  ? 19   ASP F N   1 
ATOM   10639 C CA  . ASP F  2 19  ? 12.965  -61.510 39.350  1.00 89.07  ? 19   ASP F CA  1 
ATOM   10640 C C   . ASP F  2 19  ? 14.169  -60.581 39.128  1.00 84.82  ? 19   ASP F C   1 
ATOM   10641 O O   . ASP F  2 19  ? 14.354  -59.607 39.866  1.00 81.67  ? 19   ASP F O   1 
ATOM   10642 C CB  . ASP F  2 19  ? 13.062  -62.246 40.712  1.00 92.40  ? 19   ASP F CB  1 
ATOM   10643 C CG  . ASP F  2 19  ? 14.111  -63.364 40.733  1.00 93.82  ? 19   ASP F CG  1 
ATOM   10644 O OD1 . ASP F  2 19  ? 14.488  -63.874 39.648  1.00 95.10  ? 19   ASP F OD1 1 
ATOM   10645 O OD2 . ASP F  2 19  ? 14.546  -63.740 41.853  1.00 86.18  ? 19   ASP F OD2 1 
ATOM   10646 N N   . GLY F  2 20  ? 14.991  -60.892 38.124  1.00 84.36  ? 20   GLY F N   1 
ATOM   10647 C CA  . GLY F  2 20  ? 16.138  -60.057 37.800  1.00 82.12  ? 20   GLY F CA  1 
ATOM   10648 C C   . GLY F  2 20  ? 16.749  -60.291 36.429  1.00 77.15  ? 20   GLY F C   1 
ATOM   10649 O O   . GLY F  2 20  ? 16.171  -60.976 35.585  1.00 76.89  ? 20   GLY F O   1 
ATOM   10650 N N   . TRP F  2 21  ? 17.937  -59.733 36.215  1.00 76.02  ? 21   TRP F N   1 
ATOM   10651 C CA  . TRP F  2 21  ? 18.620  -59.855 34.928  1.00 76.79  ? 21   TRP F CA  1 
ATOM   10652 C C   . TRP F  2 21  ? 19.678  -60.955 34.946  1.00 75.59  ? 21   TRP F C   1 
ATOM   10653 O O   . TRP F  2 21  ? 19.828  -61.703 33.976  1.00 73.52  ? 21   TRP F O   1 
ATOM   10654 C CB  . TRP F  2 21  ? 19.264  -58.517 34.525  1.00 77.75  ? 21   TRP F CB  1 
ATOM   10655 C CG  . TRP F  2 21  ? 18.369  -57.600 33.694  1.00 78.86  ? 21   TRP F CG  1 
ATOM   10656 C CD1 . TRP F  2 21  ? 17.319  -57.972 32.881  1.00 77.36  ? 21   TRP F CD1 1 
ATOM   10657 C CD2 . TRP F  2 21  ? 18.469  -56.172 33.581  1.00 75.11  ? 21   TRP F CD2 1 
ATOM   10658 N NE1 . TRP F  2 21  ? 16.762  -56.861 32.288  1.00 71.71  ? 21   TRP F NE1 1 
ATOM   10659 C CE2 . TRP F  2 21  ? 17.444  -55.746 32.703  1.00 73.00  ? 21   TRP F CE2 1 
ATOM   10660 C CE3 . TRP F  2 21  ? 19.320  -55.210 34.144  1.00 72.53  ? 21   TRP F CE3 1 
ATOM   10661 C CZ2 . TRP F  2 21  ? 17.252  -54.401 32.377  1.00 72.77  ? 21   TRP F CZ2 1 
ATOM   10662 C CZ3 . TRP F  2 21  ? 19.127  -53.875 33.814  1.00 72.46  ? 21   TRP F CZ3 1 
ATOM   10663 C CH2 . TRP F  2 21  ? 18.102  -53.485 32.938  1.00 71.51  ? 21   TRP F CH2 1 
ATOM   10664 N N   . TYR F  2 22  ? 20.411  -61.044 36.053  1.00 72.67  ? 22   TYR F N   1 
ATOM   10665 C CA  . TYR F  2 22  ? 21.444  -62.062 36.207  1.00 74.30  ? 22   TYR F CA  1 
ATOM   10666 C C   . TYR F  2 22  ? 21.182  -62.852 37.494  1.00 81.04  ? 22   TYR F C   1 
ATOM   10667 O O   . TYR F  2 22  ? 20.651  -62.295 38.459  1.00 86.47  ? 22   TYR F O   1 
ATOM   10668 C CB  . TYR F  2 22  ? 22.837  -61.441 36.288  1.00 74.07  ? 22   TYR F CB  1 
ATOM   10669 C CG  . TYR F  2 22  ? 23.041  -60.116 35.582  1.00 76.19  ? 22   TYR F CG  1 
ATOM   10670 C CD1 . TYR F  2 22  ? 23.081  -60.023 34.188  1.00 69.65  ? 22   TYR F CD1 1 
ATOM   10671 C CD2 . TYR F  2 22  ? 23.255  -58.957 36.326  1.00 72.39  ? 22   TYR F CD2 1 
ATOM   10672 C CE1 . TYR F  2 22  ? 23.294  -58.799 33.565  1.00 65.71  ? 22   TYR F CE1 1 
ATOM   10673 C CE2 . TYR F  2 22  ? 23.471  -57.738 35.715  1.00 71.17  ? 22   TYR F CE2 1 
ATOM   10674 C CZ  . TYR F  2 22  ? 23.491  -57.661 34.337  1.00 68.02  ? 22   TYR F CZ  1 
ATOM   10675 O OH  . TYR F  2 22  ? 23.708  -56.432 33.751  1.00 66.53  ? 22   TYR F OH  1 
ATOM   10676 N N   . GLY F  2 23  ? 21.562  -64.129 37.542  1.00 81.93  ? 23   GLY F N   1 
ATOM   10677 C CA  . GLY F  2 23  ? 21.352  -64.893 38.765  1.00 84.36  ? 23   GLY F CA  1 
ATOM   10678 C C   . GLY F  2 23  ? 21.801  -66.343 38.807  1.00 82.04  ? 23   GLY F C   1 
ATOM   10679 O O   . GLY F  2 23  ? 22.710  -66.747 38.075  1.00 80.28  ? 23   GLY F O   1 
ATOM   10680 N N   . TYR F  2 24  ? 21.168  -67.123 39.684  1.00 84.61  ? 24   TYR F N   1 
ATOM   10681 C CA  . TYR F  2 24  ? 21.623  -68.483 39.965  1.00 83.64  ? 24   TYR F CA  1 
ATOM   10682 C C   . TYR F  2 24  ? 20.507  -69.515 39.850  1.00 85.35  ? 24   TYR F C   1 
ATOM   10683 O O   . TYR F  2 24  ? 19.353  -69.259 40.214  1.00 85.25  ? 24   TYR F O   1 
ATOM   10684 C CB  . TYR F  2 24  ? 22.226  -68.598 41.367  1.00 78.73  ? 24   TYR F CB  1 
ATOM   10685 C CG  . TYR F  2 24  ? 23.098  -67.455 41.831  1.00 76.89  ? 24   TYR F CG  1 
ATOM   10686 C CD1 . TYR F  2 24  ? 22.532  -66.331 42.421  1.00 76.21  ? 24   TYR F CD1 1 
ATOM   10687 C CD2 . TYR F  2 24  ? 24.485  -67.517 41.729  1.00 75.59  ? 24   TYR F CD2 1 
ATOM   10688 C CE1 . TYR F  2 24  ? 23.311  -65.288 42.877  1.00 77.52  ? 24   TYR F CE1 1 
ATOM   10689 C CE2 . TYR F  2 24  ? 25.280  -66.470 42.185  1.00 76.88  ? 24   TYR F CE2 1 
ATOM   10690 C CZ  . TYR F  2 24  ? 24.681  -65.354 42.758  1.00 76.71  ? 24   TYR F CZ  1 
ATOM   10691 O OH  . TYR F  2 24  ? 25.433  -64.294 43.216  1.00 76.58  ? 24   TYR F OH  1 
ATOM   10692 N N   . HIS F  2 25  ? 20.870  -70.684 39.333  1.00 86.70  ? 25   HIS F N   1 
ATOM   10693 C CA  . HIS F  2 25  ? 20.035  -71.881 39.404  1.00 89.76  ? 25   HIS F CA  1 
ATOM   10694 C C   . HIS F  2 25  ? 20.695  -72.961 40.271  1.00 89.49  ? 25   HIS F C   1 
ATOM   10695 O O   . HIS F  2 25  ? 21.781  -73.443 39.928  1.00 86.54  ? 25   HIS F O   1 
ATOM   10696 C CB  . HIS F  2 25  ? 19.757  -72.440 38.016  1.00 86.07  ? 25   HIS F CB  1 
ATOM   10697 C CG  . HIS F  2 25  ? 18.881  -73.649 38.034  1.00 91.48  ? 25   HIS F CG  1 
ATOM   10698 N ND1 . HIS F  2 25  ? 17.520  -73.576 38.242  1.00 91.95  ? 25   HIS F ND1 1 
ATOM   10699 C CD2 . HIS F  2 25  ? 19.174  -74.964 37.907  1.00 91.53  ? 25   HIS F CD2 1 
ATOM   10700 C CE1 . HIS F  2 25  ? 17.010  -74.794 38.224  1.00 95.73  ? 25   HIS F CE1 1 
ATOM   10701 N NE2 . HIS F  2 25  ? 17.993  -75.655 38.022  1.00 95.99  ? 25   HIS F NE2 1 
ATOM   10702 N N   . HIS F  2 26  ? 20.065  -73.333 41.390  1.00 94.40  ? 26   HIS F N   1 
ATOM   10703 C CA  . HIS F  2 26  ? 20.683  -74.303 42.308  1.00 95.89  ? 26   HIS F CA  1 
ATOM   10704 C C   . HIS F  2 26  ? 20.003  -75.643 42.162  1.00 93.12  ? 26   HIS F C   1 
ATOM   10705 O O   . HIS F  2 26  ? 18.798  -75.715 41.912  1.00 96.12  ? 26   HIS F O   1 
ATOM   10706 C CB  . HIS F  2 26  ? 20.601  -73.861 43.782  1.00 93.90  ? 26   HIS F CB  1 
ATOM   10707 C CG  . HIS F  2 26  ? 19.222  -73.923 44.370  1.00 96.50  ? 26   HIS F CG  1 
ATOM   10708 N ND1 . HIS F  2 26  ? 18.233  -73.009 44.073  1.00 99.12  ? 26   HIS F ND1 1 
ATOM   10709 C CD2 . HIS F  2 26  ? 18.677  -74.784 45.265  1.00 101.70 ? 26   HIS F CD2 1 
ATOM   10710 C CE1 . HIS F  2 26  ? 17.137  -73.310 44.748  1.00 100.53 ? 26   HIS F CE1 1 
ATOM   10711 N NE2 . HIS F  2 26  ? 17.380  -74.382 45.480  1.00 103.38 ? 26   HIS F NE2 1 
ATOM   10712 N N   . SER F  2 27  ? 20.776  -76.705 42.347  1.00 91.18  ? 27   SER F N   1 
ATOM   10713 C CA  . SER F  2 27  ? 20.250  -78.052 42.175  1.00 99.88  ? 27   SER F CA  1 
ATOM   10714 C C   . SER F  2 27  ? 20.791  -78.973 43.266  1.00 99.05  ? 27   SER F C   1 
ATOM   10715 O O   . SER F  2 27  ? 21.850  -79.585 43.117  1.00 97.33  ? 27   SER F O   1 
ATOM   10716 C CB  . SER F  2 27  ? 20.601  -78.591 40.782  1.00 97.30  ? 27   SER F CB  1 
ATOM   10717 O OG  . SER F  2 27  ? 20.068  -79.889 40.566  1.00 90.40  ? 27   SER F OG  1 
ATOM   10718 N N   . ASN F  2 28  ? 20.075  -79.025 44.385  1.00 98.87  ? 28   ASN F N   1 
ATOM   10719 C CA  . ASN F  2 28  ? 20.410  -79.935 45.475  1.00 102.88 ? 28   ASN F CA  1 
ATOM   10720 C C   . ASN F  2 28  ? 19.218  -80.816 45.868  1.00 106.28 ? 28   ASN F C   1 
ATOM   10721 O O   . ASN F  2 28  ? 18.261  -80.951 45.099  1.00 103.77 ? 28   ASN F O   1 
ATOM   10722 C CB  . ASN F  2 28  ? 20.920  -79.138 46.677  1.00 99.29  ? 28   ASN F CB  1 
ATOM   10723 C CG  . ASN F  2 28  ? 19.832  -78.302 47.336  1.00 100.79 ? 28   ASN F CG  1 
ATOM   10724 O OD1 . ASN F  2 28  ? 18.771  -78.055 46.756  1.00 101.99 ? 28   ASN F OD1 1 
ATOM   10725 N ND2 . ASN F  2 28  ? 20.105  -77.840 48.546  1.00 102.08 ? 28   ASN F ND2 1 
ATOM   10726 N N   . GLU F  2 29  ? 19.287  -81.404 47.065  1.00 107.26 ? 29   GLU F N   1 
ATOM   10727 C CA  . GLU F  2 29  ? 18.241  -82.295 47.588  1.00 105.07 ? 29   GLU F CA  1 
ATOM   10728 C C   . GLU F  2 29  ? 16.913  -81.590 47.812  1.00 106.67 ? 29   GLU F C   1 
ATOM   10729 O O   . GLU F  2 29  ? 15.853  -82.143 47.510  1.00 109.90 ? 29   GLU F O   1 
ATOM   10730 C CB  . GLU F  2 29  ? 18.704  -82.972 48.886  1.00 99.44  ? 29   GLU F CB  1 
ATOM   10731 C CG  . GLU F  2 29  ? 19.874  -83.933 48.689  1.00 105.14 ? 29   GLU F CG  1 
ATOM   10732 C CD  . GLU F  2 29  ? 21.193  -83.224 48.448  1.00 111.23 ? 29   GLU F CD  1 
ATOM   10733 O OE1 . GLU F  2 29  ? 21.225  -81.973 48.564  1.00 108.61 ? 29   GLU F OE1 1 
ATOM   10734 O OE2 . GLU F  2 29  ? 22.184  -83.919 48.109  1.00 108.82 ? 29   GLU F OE2 1 
ATOM   10735 N N   . GLN F  2 30  ? 16.963  -80.378 48.352  1.00 105.58 ? 30   GLN F N   1 
ATOM   10736 C CA  . GLN F  2 30  ? 15.762  -79.554 48.435  1.00 109.02 ? 30   GLN F CA  1 
ATOM   10737 C C   . GLN F  2 30  ? 15.444  -78.977 47.044  1.00 111.63 ? 30   GLN F C   1 
ATOM   10738 O O   . GLN F  2 30  ? 15.486  -77.755 46.834  1.00 106.02 ? 30   GLN F O   1 
ATOM   10739 C CB  . GLN F  2 30  ? 15.936  -78.412 49.442  1.00 111.28 ? 30   GLN F CB  1 
ATOM   10740 C CG  . GLN F  2 30  ? 16.149  -78.803 50.911  1.00 106.09 ? 30   GLN F CG  1 
ATOM   10741 C CD  . GLN F  2 30  ? 17.617  -79.056 51.249  1.00 103.76 ? 30   GLN F CD  1 
ATOM   10742 O OE1 . GLN F  2 30  ? 18.358  -79.658 50.466  1.00 101.16 ? 30   GLN F OE1 1 
ATOM   10743 N NE2 . GLN F  2 30  ? 18.054  -78.540 52.396  1.00 98.50  ? 30   GLN F NE2 1 
ATOM   10744 N N   . GLY F  2 31  ? 15.143  -79.873 46.106  1.00 109.85 ? 31   GLY F N   1 
ATOM   10745 C CA  . GLY F  2 31  ? 14.747  -79.531 44.750  1.00 105.68 ? 31   GLY F CA  1 
ATOM   10746 C C   . GLY F  2 31  ? 15.628  -78.551 43.990  1.00 106.17 ? 31   GLY F C   1 
ATOM   10747 O O   . GLY F  2 31  ? 16.791  -78.318 44.331  1.00 101.82 ? 31   GLY F O   1 
ATOM   10748 N N   . SER F  2 32  ? 15.052  -77.983 42.936  1.00 107.34 ? 32   SER F N   1 
ATOM   10749 C CA  . SER F  2 32  ? 15.735  -77.008 42.107  1.00 96.04  ? 32   SER F CA  1 
ATOM   10750 C C   . SER F  2 32  ? 15.115  -75.659 42.377  1.00 97.24  ? 32   SER F C   1 
ATOM   10751 O O   . SER F  2 32  ? 14.372  -75.489 43.347  1.00 95.20  ? 32   SER F O   1 
ATOM   10752 C CB  . SER F  2 32  ? 15.632  -77.364 40.628  1.00 94.19  ? 32   SER F CB  1 
ATOM   10753 O OG  . SER F  2 32  ? 16.226  -78.621 40.382  1.00 94.29  ? 32   SER F OG  1 
ATOM   10754 N N   . GLY F  2 33  ? 15.399  -74.705 41.502  1.00 100.15 ? 33   GLY F N   1 
ATOM   10755 C CA  . GLY F  2 33  ? 14.809  -73.385 41.619  1.00 101.62 ? 33   GLY F CA  1 
ATOM   10756 C C   . GLY F  2 33  ? 15.671  -72.318 40.984  1.00 95.30  ? 33   GLY F C   1 
ATOM   10757 O O   . GLY F  2 33  ? 16.845  -72.555 40.684  1.00 94.35  ? 33   GLY F O   1 
ATOM   10758 N N   . TYR F  2 34  ? 15.092  -71.137 40.793  1.00 93.50  ? 34   TYR F N   1 
ATOM   10759 C CA  . TYR F  2 34  ? 15.841  -70.012 40.252  1.00 91.16  ? 34   TYR F CA  1 
ATOM   10760 C C   . TYR F  2 34  ? 15.985  -68.946 41.317  1.00 85.69  ? 34   TYR F C   1 
ATOM   10761 O O   . TYR F  2 34  ? 15.135  -68.809 42.189  1.00 80.70  ? 34   TYR F O   1 
ATOM   10762 C CB  . TYR F  2 34  ? 15.150  -69.430 39.011  1.00 86.05  ? 34   TYR F CB  1 
ATOM   10763 C CG  . TYR F  2 34  ? 15.160  -70.348 37.807  1.00 91.64  ? 34   TYR F CG  1 
ATOM   10764 C CD1 . TYR F  2 34  ? 16.341  -70.585 37.103  1.00 91.12  ? 34   TYR F CD1 1 
ATOM   10765 C CD2 . TYR F  2 34  ? 13.991  -70.966 37.359  1.00 92.40  ? 34   TYR F CD2 1 
ATOM   10766 C CE1 . TYR F  2 34  ? 16.364  -71.423 35.995  1.00 87.67  ? 34   TYR F CE1 1 
ATOM   10767 C CE2 . TYR F  2 34  ? 14.005  -71.807 36.245  1.00 85.45  ? 34   TYR F CE2 1 
ATOM   10768 C CZ  . TYR F  2 34  ? 15.197  -72.030 35.572  1.00 87.54  ? 34   TYR F CZ  1 
ATOM   10769 O OH  . TYR F  2 34  ? 15.236  -72.860 34.473  1.00 95.26  ? 34   TYR F OH  1 
ATOM   10770 N N   . ALA F  2 35  ? 17.056  -68.171 41.220  1.00 89.64  ? 35   ALA F N   1 
ATOM   10771 C CA  . ALA F  2 35  ? 17.324  -67.117 42.189  1.00 94.59  ? 35   ALA F CA  1 
ATOM   10772 C C   . ALA F  2 35  ? 18.163  -66.016 41.542  1.00 91.08  ? 35   ALA F C   1 
ATOM   10773 O O   . ALA F  2 35  ? 19.190  -66.287 40.919  1.00 88.67  ? 35   ALA F O   1 
ATOM   10774 C CB  . ALA F  2 35  ? 18.036  -67.688 43.422  1.00 85.22  ? 35   ALA F CB  1 
ATOM   10775 N N   . ALA F  2 36  ? 17.723  -64.773 41.718  1.00 92.53  ? 36   ALA F N   1 
ATOM   10776 C CA  . ALA F  2 36  ? 18.376  -63.617 41.115  1.00 87.66  ? 36   ALA F CA  1 
ATOM   10777 C C   . ALA F  2 36  ? 19.343  -62.976 42.073  1.00 86.03  ? 36   ALA F C   1 
ATOM   10778 O O   . ALA F  2 36  ? 19.029  -62.818 43.253  1.00 90.92  ? 36   ALA F O   1 
ATOM   10779 C CB  . ALA F  2 36  ? 17.349  -62.592 40.670  1.00 86.71  ? 36   ALA F CB  1 
ATOM   10780 N N   . ASP F  2 37  ? 20.521  -62.612 41.577  1.00 82.11  ? 37   ASP F N   1 
ATOM   10781 C CA  . ASP F  2 37  ? 21.434  -61.823 42.392  1.00 87.74  ? 37   ASP F CA  1 
ATOM   10782 C C   . ASP F  2 37  ? 20.975  -60.370 42.364  1.00 86.32  ? 37   ASP F C   1 
ATOM   10783 O O   . ASP F  2 37  ? 21.169  -59.670 41.372  1.00 87.84  ? 37   ASP F O   1 
ATOM   10784 C CB  . ASP F  2 37  ? 22.887  -61.940 41.919  1.00 82.78  ? 37   ASP F CB  1 
ATOM   10785 C CG  . ASP F  2 37  ? 23.863  -61.287 42.894  1.00 84.84  ? 37   ASP F CG  1 
ATOM   10786 O OD1 . ASP F  2 37  ? 23.574  -61.273 44.112  1.00 88.71  ? 37   ASP F OD1 1 
ATOM   10787 O OD2 . ASP F  2 37  ? 24.916  -60.785 42.450  1.00 85.04  ? 37   ASP F OD2 1 
ATOM   10788 N N   . LYS F  2 38  ? 20.357  -59.936 43.459  1.00 86.45  ? 38   LYS F N   1 
ATOM   10789 C CA  . LYS F  2 38  ? 19.752  -58.615 43.548  1.00 84.65  ? 38   LYS F CA  1 
ATOM   10790 C C   . LYS F  2 38  ? 20.809  -57.535 43.400  1.00 88.06  ? 38   LYS F C   1 
ATOM   10791 O O   . LYS F  2 38  ? 20.602  -56.538 42.709  1.00 89.34  ? 38   LYS F O   1 
ATOM   10792 C CB  . LYS F  2 38  ? 19.020  -58.443 44.886  1.00 86.91  ? 38   LYS F CB  1 
ATOM   10793 C CG  . LYS F  2 38  ? 17.966  -59.502 45.218  1.00 92.36  ? 38   LYS F CG  1 
ATOM   10794 C CD  . LYS F  2 38  ? 16.806  -59.492 44.232  1.00 91.98  ? 38   LYS F CD  1 
ATOM   10795 C CE  . LYS F  2 38  ? 15.891  -58.297 44.486  1.00 91.84  ? 38   LYS F CE  1 
ATOM   10796 N NZ  . LYS F  2 38  ? 14.720  -58.292 43.566  1.00 95.20  ? 38   LYS F NZ  1 
ATOM   10797 N N   . GLU F  2 39  ? 21.936  -57.741 44.070  1.00 86.64  ? 39   GLU F N   1 
ATOM   10798 C CA  . GLU F  2 39  ? 22.989  -56.743 44.170  1.00 84.37  ? 39   GLU F CA  1 
ATOM   10799 C C   . GLU F  2 39  ? 23.525  -56.272 42.796  1.00 86.16  ? 39   GLU F C   1 
ATOM   10800 O O   . GLU F  2 39  ? 23.624  -55.061 42.534  1.00 85.76  ? 39   GLU F O   1 
ATOM   10801 C CB  . GLU F  2 39  ? 24.110  -57.330 45.044  1.00 86.59  ? 39   GLU F CB  1 
ATOM   10802 C CG  . GLU F  2 39  ? 25.277  -56.414 45.402  1.00 88.02  ? 39   GLU F CG  1 
ATOM   10803 C CD  . GLU F  2 39  ? 26.379  -56.402 44.357  1.00 95.34  ? 39   GLU F CD  1 
ATOM   10804 O OE1 . GLU F  2 39  ? 26.334  -57.236 43.420  1.00 96.02  ? 39   GLU F OE1 1 
ATOM   10805 O OE2 . GLU F  2 39  ? 27.312  -55.580 44.502  1.00 97.30  ? 39   GLU F OE2 1 
ATOM   10806 N N   . SER F  2 40  ? 23.846  -57.218 41.915  1.00 83.72  ? 40   SER F N   1 
ATOM   10807 C CA  . SER F  2 40  ? 24.420  -56.876 40.614  1.00 78.15  ? 40   SER F CA  1 
ATOM   10808 C C   . SER F  2 40  ? 23.388  -56.369 39.596  1.00 77.38  ? 40   SER F C   1 
ATOM   10809 O O   . SER F  2 40  ? 23.743  -55.622 38.682  1.00 71.37  ? 40   SER F O   1 
ATOM   10810 C CB  . SER F  2 40  ? 25.165  -58.076 40.024  1.00 76.04  ? 40   SER F CB  1 
ATOM   10811 O OG  . SER F  2 40  ? 24.267  -59.112 39.677  1.00 76.08  ? 40   SER F OG  1 
ATOM   10812 N N   . THR F  2 41  ? 22.124  -56.775 39.743  1.00 78.72  ? 41   THR F N   1 
ATOM   10813 C CA  . THR F  2 41  ? 21.068  -56.300 38.834  1.00 79.88  ? 41   THR F CA  1 
ATOM   10814 C C   . THR F  2 41  ? 20.680  -54.860 39.147  1.00 74.82  ? 41   THR F C   1 
ATOM   10815 O O   . THR F  2 41  ? 20.315  -54.103 38.250  1.00 73.15  ? 41   THR F O   1 
ATOM   10816 C CB  . THR F  2 41  ? 19.752  -57.165 38.875  1.00 81.13  ? 41   THR F CB  1 
ATOM   10817 O OG1 . THR F  2 41  ? 19.110  -57.046 40.155  1.00 81.81  ? 41   THR F OG1 1 
ATOM   10818 C CG2 . THR F  2 41  ? 20.014  -58.635 38.536  1.00 76.04  ? 41   THR F CG2 1 
ATOM   10819 N N   . GLN F  2 42  ? 20.736  -54.491 40.424  1.00 79.19  ? 42   GLN F N   1 
ATOM   10820 C CA  . GLN F  2 42  ? 20.378  -53.136 40.833  1.00 79.59  ? 42   GLN F CA  1 
ATOM   10821 C C   . GLN F  2 42  ? 21.422  -52.127 40.359  1.00 76.24  ? 42   GLN F C   1 
ATOM   10822 O O   . GLN F  2 42  ? 21.066  -51.058 39.858  1.00 76.18  ? 42   GLN F O   1 
ATOM   10823 C CB  . GLN F  2 42  ? 20.205  -53.046 42.354  1.00 75.39  ? 42   GLN F CB  1 
ATOM   10824 C CG  . GLN F  2 42  ? 19.693  -51.696 42.800  1.00 72.72  ? 42   GLN F CG  1 
ATOM   10825 C CD  . GLN F  2 42  ? 18.403  -51.330 42.088  1.00 76.75  ? 42   GLN F CD  1 
ATOM   10826 O OE1 . GLN F  2 42  ? 18.371  -50.392 41.287  1.00 77.83  ? 42   GLN F OE1 1 
ATOM   10827 N NE2 . GLN F  2 42  ? 17.336  -52.081 42.361  1.00 68.50  ? 42   GLN F NE2 1 
ATOM   10828 N N   . LYS F  2 43  ? 22.703  -52.468 40.518  1.00 72.94  ? 43   LYS F N   1 
ATOM   10829 C CA  . LYS F  2 43  ? 23.787  -51.604 40.051  1.00 73.63  ? 43   LYS F CA  1 
ATOM   10830 C C   . LYS F  2 43  ? 23.793  -51.550 38.521  1.00 75.73  ? 43   LYS F C   1 
ATOM   10831 O O   . LYS F  2 43  ? 24.321  -50.615 37.915  1.00 77.08  ? 43   LYS F O   1 
ATOM   10832 C CB  . LYS F  2 43  ? 25.139  -52.070 40.605  1.00 76.60  ? 43   LYS F CB  1 
ATOM   10833 C CG  . LYS F  2 43  ? 26.090  -52.643 39.581  1.00 79.11  ? 43   LYS F CG  1 
ATOM   10834 C CD  . LYS F  2 43  ? 27.539  -52.551 40.055  1.00 81.39  ? 43   LYS F CD  1 
ATOM   10835 C CE  . LYS F  2 43  ? 28.444  -53.488 39.243  1.00 87.93  ? 43   LYS F CE  1 
ATOM   10836 N NZ  . LYS F  2 43  ? 28.196  -53.417 37.762  1.00 77.76  ? 43   LYS F NZ  1 
ATOM   10837 N N   . ALA F  2 44  ? 23.186  -52.556 37.906  1.00 76.11  ? 44   ALA F N   1 
ATOM   10838 C CA  . ALA F  2 44  ? 23.060  -52.614 36.461  1.00 72.07  ? 44   ALA F CA  1 
ATOM   10839 C C   . ALA F  2 44  ? 21.891  -51.732 36.007  1.00 74.39  ? 44   ALA F C   1 
ATOM   10840 O O   . ALA F  2 44  ? 21.973  -51.091 34.964  1.00 79.91  ? 44   ALA F O   1 
ATOM   10841 C CB  . ALA F  2 44  ? 22.874  -54.051 35.988  1.00 71.30  ? 44   ALA F CB  1 
ATOM   10842 N N   . ILE F  2 45  ? 20.799  -51.712 36.768  1.00 73.71  ? 45   ILE F N   1 
ATOM   10843 C CA  . ILE F  2 45  ? 19.667  -50.828 36.460  1.00 75.47  ? 45   ILE F CA  1 
ATOM   10844 C C   . ILE F  2 45  ? 20.040  -49.353 36.693  1.00 75.08  ? 45   ILE F C   1 
ATOM   10845 O O   . ILE F  2 45  ? 19.621  -48.465 35.937  1.00 75.10  ? 45   ILE F O   1 
ATOM   10846 C CB  . ILE F  2 45  ? 18.407  -51.187 37.308  1.00 78.09  ? 45   ILE F CB  1 
ATOM   10847 C CG1 . ILE F  2 45  ? 17.743  -52.460 36.773  1.00 79.25  ? 45   ILE F CG1 1 
ATOM   10848 C CG2 . ILE F  2 45  ? 17.391  -50.041 37.323  1.00 73.85  ? 45   ILE F CG2 1 
ATOM   10849 C CD1 . ILE F  2 45  ? 16.413  -52.796 37.441  1.00 83.88  ? 45   ILE F CD1 1 
ATOM   10850 N N   . ASP F  2 46  ? 20.850  -49.104 37.721  1.00 72.54  ? 46   ASP F N   1 
ATOM   10851 C CA  . ASP F  2 46  ? 21.330  -47.760 38.028  1.00 72.03  ? 46   ASP F CA  1 
ATOM   10852 C C   . ASP F  2 46  ? 22.283  -47.224 36.930  1.00 70.96  ? 46   ASP F C   1 
ATOM   10853 O O   . ASP F  2 46  ? 22.319  -46.029 36.641  1.00 67.06  ? 46   ASP F O   1 
ATOM   10854 C CB  . ASP F  2 46  ? 22.026  -47.749 39.397  1.00 75.36  ? 46   ASP F CB  1 
ATOM   10855 C CG  . ASP F  2 46  ? 21.050  -47.909 40.566  1.00 75.90  ? 46   ASP F CG  1 
ATOM   10856 O OD1 . ASP F  2 46  ? 19.823  -47.758 40.365  1.00 76.82  ? 46   ASP F OD1 1 
ATOM   10857 O OD2 . ASP F  2 46  ? 21.525  -48.170 41.695  1.00 77.06  ? 46   ASP F OD2 1 
ATOM   10858 N N   . GLY F  2 47  ? 23.067  -48.107 36.330  1.00 69.54  ? 47   GLY F N   1 
ATOM   10859 C CA  . GLY F  2 47  ? 23.987  -47.684 35.292  1.00 69.10  ? 47   GLY F CA  1 
ATOM   10860 C C   . GLY F  2 47  ? 23.251  -47.281 34.022  1.00 70.50  ? 47   GLY F C   1 
ATOM   10861 O O   . GLY F  2 47  ? 23.585  -46.275 33.390  1.00 66.11  ? 47   GLY F O   1 
ATOM   10862 N N   . VAL F  2 48  ? 22.231  -48.065 33.661  1.00 71.74  ? 48   VAL F N   1 
ATOM   10863 C CA  . VAL F  2 48  ? 21.476  -47.859 32.424  1.00 67.62  ? 48   VAL F CA  1 
ATOM   10864 C C   . VAL F  2 48  ? 20.520  -46.675 32.549  1.00 65.28  ? 48   VAL F C   1 
ATOM   10865 O O   . VAL F  2 48  ? 20.325  -45.918 31.599  1.00 62.86  ? 48   VAL F O   1 
ATOM   10866 C CB  . VAL F  2 48  ? 20.679  -49.140 32.042  1.00 63.32  ? 48   VAL F CB  1 
ATOM   10867 C CG1 . VAL F  2 48  ? 19.882  -48.941 30.756  1.00 64.85  ? 48   VAL F CG1 1 
ATOM   10868 C CG2 . VAL F  2 48  ? 21.619  -50.303 31.881  1.00 62.97  ? 48   VAL F CG2 1 
ATOM   10869 N N   . THR F  2 49  ? 19.971  -46.480 33.741  1.00 66.93  ? 49   THR F N   1 
ATOM   10870 C CA  . THR F  2 49  ? 19.040  -45.388 33.962  1.00 66.33  ? 49   THR F CA  1 
ATOM   10871 C C   . THR F  2 49  ? 19.793  -44.067 33.931  1.00 67.97  ? 49   THR F C   1 
ATOM   10872 O O   . THR F  2 49  ? 19.264  -43.049 33.477  1.00 68.08  ? 49   THR F O   1 
ATOM   10873 C CB  . THR F  2 49  ? 18.313  -45.529 35.311  1.00 69.85  ? 49   THR F CB  1 
ATOM   10874 O OG1 . THR F  2 49  ? 17.611  -46.779 35.346  1.00 78.24  ? 49   THR F OG1 1 
ATOM   10875 C CG2 . THR F  2 49  ? 17.330  -44.381 35.527  1.00 68.42  ? 49   THR F CG2 1 
ATOM   10876 N N   . ASN F  2 50  ? 21.039  -44.099 34.399  1.00 66.65  ? 50   ASN F N   1 
ATOM   10877 C CA  . ASN F  2 50  ? 21.923  -42.940 34.318  1.00 67.38  ? 50   ASN F CA  1 
ATOM   10878 C C   . ASN F  2 50  ? 22.285  -42.626 32.867  1.00 66.05  ? 50   ASN F C   1 
ATOM   10879 O O   . ASN F  2 50  ? 22.304  -41.466 32.455  1.00 66.07  ? 50   ASN F O   1 
ATOM   10880 C CB  . ASN F  2 50  ? 23.196  -43.170 35.149  1.00 64.86  ? 50   ASN F CB  1 
ATOM   10881 C CG  . ASN F  2 50  ? 22.967  -42.989 36.651  1.00 77.79  ? 50   ASN F CG  1 
ATOM   10882 O OD1 . ASN F  2 50  ? 22.086  -42.234 37.069  1.00 84.14  ? 50   ASN F OD1 1 
ATOM   10883 N ND2 . ASN F  2 50  ? 23.743  -43.710 37.467  1.00 74.62  ? 50   ASN F ND2 1 
ATOM   10884 N N   . LYS F  2 51  ? 22.557  -43.669 32.093  1.00 65.79  ? 51   LYS F N   1 
ATOM   10885 C CA  . LYS F  2 51  ? 22.909  -43.501 30.696  1.00 61.87  ? 51   LYS F CA  1 
ATOM   10886 C C   . LYS F  2 51  ? 21.783  -42.827 29.897  1.00 61.26  ? 51   LYS F C   1 
ATOM   10887 O O   . LYS F  2 51  ? 22.012  -41.829 29.213  1.00 60.15  ? 51   LYS F O   1 
ATOM   10888 C CB  . LYS F  2 51  ? 23.261  -44.848 30.069  1.00 58.53  ? 51   LYS F CB  1 
ATOM   10889 C CG  . LYS F  2 51  ? 23.524  -44.738 28.587  1.00 57.02  ? 51   LYS F CG  1 
ATOM   10890 C CD  . LYS F  2 51  ? 23.791  -46.070 27.962  1.00 51.82  ? 51   LYS F CD  1 
ATOM   10891 C CE  . LYS F  2 51  ? 25.140  -46.589 28.370  1.00 50.51  ? 51   LYS F CE  1 
ATOM   10892 N NZ  . LYS F  2 51  ? 25.541  -47.645 27.419  1.00 53.66  ? 51   LYS F NZ  1 
ATOM   10893 N N   . VAL F  2 52  ? 20.564  -43.345 30.034  1.00 61.82  ? 52   VAL F N   1 
ATOM   10894 C CA  . VAL F  2 52  ? 19.425  -42.879 29.241  1.00 65.24  ? 52   VAL F CA  1 
ATOM   10895 C C   . VAL F  2 52  ? 19.054  -41.425 29.574  1.00 71.68  ? 52   VAL F C   1 
ATOM   10896 O O   . VAL F  2 52  ? 18.623  -40.659 28.695  1.00 73.00  ? 52   VAL F O   1 
ATOM   10897 C CB  . VAL F  2 52  ? 18.198  -43.803 29.470  1.00 66.53  ? 52   VAL F CB  1 
ATOM   10898 C CG1 . VAL F  2 52  ? 16.933  -43.243 28.810  1.00 67.46  ? 52   VAL F CG1 1 
ATOM   10899 C CG2 . VAL F  2 52  ? 18.502  -45.213 28.969  1.00 65.26  ? 52   VAL F CG2 1 
ATOM   10900 N N   . ASN F  2 53  ? 19.274  -41.036 30.828  1.00 68.02  ? 53   ASN F N   1 
ATOM   10901 C CA  . ASN F  2 53  ? 19.040  -39.667 31.274  1.00 66.63  ? 53   ASN F CA  1 
ATOM   10902 C C   . ASN F  2 53  ? 20.142  -38.739 30.782  1.00 66.61  ? 53   ASN F C   1 
ATOM   10903 O O   . ASN F  2 53  ? 19.889  -37.572 30.489  1.00 67.64  ? 53   ASN F O   1 
ATOM   10904 C CB  . ASN F  2 53  ? 18.924  -39.623 32.795  1.00 66.76  ? 53   ASN F CB  1 
ATOM   10905 C CG  . ASN F  2 53  ? 17.698  -40.355 33.299  1.00 69.53  ? 53   ASN F CG  1 
ATOM   10906 O OD1 . ASN F  2 53  ? 16.751  -40.598 32.544  1.00 69.61  ? 53   ASN F OD1 1 
ATOM   10907 N ND2 . ASN F  2 53  ? 17.727  -40.757 34.564  1.00 65.49  ? 53   ASN F ND2 1 
ATOM   10908 N N   . SER F  2 54  ? 21.367  -39.264 30.737  1.00 65.63  ? 54   SER F N   1 
ATOM   10909 C CA  . SER F  2 54  ? 22.526  -38.532 30.223  1.00 67.44  ? 54   SER F CA  1 
ATOM   10910 C C   . SER F  2 54  ? 22.374  -38.205 28.738  1.00 71.42  ? 54   SER F C   1 
ATOM   10911 O O   . SER F  2 54  ? 22.819  -37.147 28.286  1.00 75.82  ? 54   SER F O   1 
ATOM   10912 C CB  . SER F  2 54  ? 23.827  -39.330 30.430  1.00 64.72  ? 54   SER F CB  1 
ATOM   10913 O OG  . SER F  2 54  ? 24.248  -39.355 31.783  1.00 63.93  ? 54   SER F OG  1 
ATOM   10914 N N   . ILE F  2 55  ? 21.753  -39.119 27.991  1.00 65.00  ? 55   ILE F N   1 
ATOM   10915 C CA  . ILE F  2 55  ? 21.555  -38.965 26.555  1.00 62.33  ? 55   ILE F CA  1 
ATOM   10916 C C   . ILE F  2 55  ? 20.450  -37.918 26.300  1.00 68.63  ? 55   ILE F C   1 
ATOM   10917 O O   . ILE F  2 55  ? 20.493  -37.172 25.315  1.00 69.00  ? 55   ILE F O   1 
ATOM   10918 C CB  . ILE F  2 55  ? 21.198  -40.331 25.886  1.00 62.14  ? 55   ILE F CB  1 
ATOM   10919 C CG1 . ILE F  2 55  ? 22.365  -41.321 26.016  1.00 59.61  ? 55   ILE F CG1 1 
ATOM   10920 C CG2 . ILE F  2 55  ? 20.817  -40.146 24.421  1.00 56.98  ? 55   ILE F CG2 1 
ATOM   10921 C CD1 . ILE F  2 55  ? 22.050  -42.742 25.589  1.00 52.20  ? 55   ILE F CD1 1 
ATOM   10922 N N   . ILE F  2 56  ? 19.479  -37.851 27.211  1.00 66.04  ? 56   ILE F N   1 
ATOM   10923 C CA  . ILE F  2 56  ? 18.384  -36.884 27.121  1.00 69.65  ? 56   ILE F CA  1 
ATOM   10924 C C   . ILE F  2 56  ? 18.849  -35.469 27.532  1.00 74.96  ? 56   ILE F C   1 
ATOM   10925 O O   . ILE F  2 56  ? 18.485  -34.466 26.903  1.00 75.73  ? 56   ILE F O   1 
ATOM   10926 C CB  . ILE F  2 56  ? 17.182  -37.312 27.985  1.00 70.08  ? 56   ILE F CB  1 
ATOM   10927 C CG1 . ILE F  2 56  ? 16.536  -38.572 27.406  1.00 66.38  ? 56   ILE F CG1 1 
ATOM   10928 C CG2 . ILE F  2 56  ? 16.153  -36.182 28.095  1.00 61.09  ? 56   ILE F CG2 1 
ATOM   10929 C CD1 . ILE F  2 56  ? 15.421  -39.133 28.275  1.00 68.72  ? 56   ILE F CD1 1 
ATOM   10930 N N   . ASP F  2 57  ? 19.634  -35.392 28.604  1.00 73.91  ? 57   ASP F N   1 
ATOM   10931 C CA  . ASP F  2 57  ? 20.152  -34.112 29.090  1.00 75.82  ? 57   ASP F CA  1 
ATOM   10932 C C   . ASP F  2 57  ? 21.241  -33.521 28.195  1.00 73.19  ? 57   ASP F C   1 
ATOM   10933 O O   . ASP F  2 57  ? 21.509  -32.327 28.270  1.00 73.74  ? 57   ASP F O   1 
ATOM   10934 C CB  . ASP F  2 57  ? 20.709  -34.275 30.504  1.00 73.35  ? 57   ASP F CB  1 
ATOM   10935 C CG  . ASP F  2 57  ? 19.633  -34.571 31.516  1.00 84.41  ? 57   ASP F CG  1 
ATOM   10936 O OD1 . ASP F  2 57  ? 18.529  -33.994 31.378  1.00 87.05  ? 57   ASP F OD1 1 
ATOM   10937 O OD2 . ASP F  2 57  ? 19.881  -35.390 32.434  1.00 88.23  ? 57   ASP F OD2 1 
ATOM   10938 N N   . LYS F  2 58  ? 21.888  -34.358 27.380  1.00 73.64  ? 58   LYS F N   1 
ATOM   10939 C CA  . LYS F  2 58  ? 22.903  -33.877 26.434  1.00 76.11  ? 58   LYS F CA  1 
ATOM   10940 C C   . LYS F  2 58  ? 22.273  -33.276 25.169  1.00 78.15  ? 58   LYS F C   1 
ATOM   10941 O O   . LYS F  2 58  ? 22.972  -32.684 24.348  1.00 75.47  ? 58   LYS F O   1 
ATOM   10942 C CB  . LYS F  2 58  ? 23.878  -34.993 26.026  1.00 70.48  ? 58   LYS F CB  1 
ATOM   10943 C CG  . LYS F  2 58  ? 25.049  -35.189 26.977  1.00 71.55  ? 58   LYS F CG  1 
ATOM   10944 C CD  . LYS F  2 58  ? 25.737  -33.869 27.325  1.00 71.14  ? 58   LYS F CD  1 
ATOM   10945 C CE  . LYS F  2 58  ? 26.886  -34.092 28.308  1.00 58.16  ? 58   LYS F CE  1 
ATOM   10946 N NZ  . LYS F  2 58  ? 27.178  -32.883 29.137  1.00 53.57  ? 58   LYS F NZ  1 
ATOM   10947 N N   . MET F  2 59  ? 20.959  -33.437 25.013  1.00 78.79  ? 59   MET F N   1 
ATOM   10948 C CA  . MET F  2 59  ? 20.268  -32.999 23.805  1.00 77.03  ? 59   MET F CA  1 
ATOM   10949 C C   . MET F  2 59  ? 19.282  -31.873 24.091  1.00 78.19  ? 59   MET F C   1 
ATOM   10950 O O   . MET F  2 59  ? 18.608  -31.392 23.180  1.00 84.47  ? 59   MET F O   1 
ATOM   10951 C CB  . MET F  2 59  ? 19.529  -34.176 23.161  1.00 73.41  ? 59   MET F CB  1 
ATOM   10952 C CG  . MET F  2 59  ? 20.445  -35.313 22.784  1.00 68.26  ? 59   MET F CG  1 
ATOM   10953 S SD  . MET F  2 59  ? 21.341  -34.841 21.317  1.00 72.70  ? 59   MET F SD  1 
ATOM   10954 C CE  . MET F  2 59  ? 22.365  -36.284 21.042  1.00 57.63  ? 59   MET F CE  1 
ATOM   10955 N N   . ASN F  2 60  ? 19.205  -31.442 25.346  1.00 79.07  ? 60   ASN F N   1 
ATOM   10956 C CA  . ASN F  2 60  ? 18.211  -30.442 25.725  1.00 84.50  ? 60   ASN F CA  1 
ATOM   10957 C C   . ASN F  2 60  ? 18.509  -29.079 25.100  1.00 80.14  ? 60   ASN F C   1 
ATOM   10958 O O   . ASN F  2 60  ? 17.589  -28.313 24.799  1.00 80.32  ? 60   ASN F O   1 
ATOM   10959 C CB  . ASN F  2 60  ? 18.115  -30.312 27.259  1.00 78.83  ? 60   ASN F CB  1 
ATOM   10960 C CG  . ASN F  2 60  ? 19.357  -29.679 27.881  1.00 80.28  ? 60   ASN F CG  1 
ATOM   10961 O OD1 . ASN F  2 60  ? 20.462  -29.812 27.358  1.00 80.80  ? 60   ASN F OD1 1 
ATOM   10962 N ND2 . ASN F  2 60  ? 19.171  -28.962 28.989  1.00 80.53  ? 60   ASN F ND2 1 
ATOM   10963 N N   . THR F  2 61  ? 19.789  -28.792 24.877  1.00 78.28  ? 61   THR F N   1 
ATOM   10964 C CA  . THR F  2 61  ? 20.170  -27.586 24.154  1.00 79.66  ? 61   THR F CA  1 
ATOM   10965 C C   . THR F  2 61  ? 20.524  -27.970 22.722  1.00 77.01  ? 61   THR F C   1 
ATOM   10966 O O   . THR F  2 61  ? 21.615  -28.466 22.438  1.00 74.06  ? 61   THR F O   1 
ATOM   10967 C CB  . THR F  2 61  ? 21.353  -26.840 24.808  1.00 77.20  ? 61   THR F CB  1 
ATOM   10968 O OG1 . THR F  2 61  ? 21.111  -26.668 26.209  1.00 82.14  ? 61   THR F OG1 1 
ATOM   10969 C CG2 . THR F  2 61  ? 21.513  -25.462 24.174  1.00 72.21  ? 61   THR F CG2 1 
ATOM   10970 N N   . GLN F  2 62  ? 19.583  -27.730 21.823  1.00 71.61  ? 62   GLN F N   1 
ATOM   10971 C CA  . GLN F  2 62  ? 19.707  -28.176 20.453  1.00 69.05  ? 62   GLN F CA  1 
ATOM   10972 C C   . GLN F  2 62  ? 19.014  -27.140 19.563  1.00 67.76  ? 62   GLN F C   1 
ATOM   10973 O O   . GLN F  2 62  ? 18.101  -26.442 20.011  1.00 70.37  ? 62   GLN F O   1 
ATOM   10974 C CB  . GLN F  2 62  ? 19.089  -29.571 20.300  1.00 63.14  ? 62   GLN F CB  1 
ATOM   10975 C CG  . GLN F  2 62  ? 18.572  -29.885 18.906  1.00 64.79  ? 62   GLN F CG  1 
ATOM   10976 C CD  . GLN F  2 62  ? 17.979  -31.284 18.778  1.00 68.30  ? 62   GLN F CD  1 
ATOM   10977 O OE1 . GLN F  2 62  ? 16.886  -31.449 18.229  1.00 65.51  ? 62   GLN F OE1 1 
ATOM   10978 N NE2 . GLN F  2 62  ? 18.691  -32.294 19.280  1.00 67.75  ? 62   GLN F NE2 1 
ATOM   10979 N N   . PHE F  2 63  ? 19.465  -27.024 18.319  1.00 59.85  ? 63   PHE F N   1 
ATOM   10980 C CA  . PHE F  2 63  ? 18.970  -25.993 17.398  1.00 63.57  ? 63   PHE F CA  1 
ATOM   10981 C C   . PHE F  2 63  ? 17.459  -26.019 17.176  1.00 59.98  ? 63   PHE F C   1 
ATOM   10982 O O   . PHE F  2 63  ? 16.865  -27.085 17.048  1.00 60.36  ? 63   PHE F O   1 
ATOM   10983 C CB  . PHE F  2 63  ? 19.685  -26.115 16.063  1.00 54.57  ? 63   PHE F CB  1 
ATOM   10984 C CG  . PHE F  2 63  ? 19.274  -25.091 15.075  1.00 50.89  ? 63   PHE F CG  1 
ATOM   10985 C CD1 . PHE F  2 63  ? 19.834  -23.815 15.111  1.00 47.61  ? 63   PHE F CD1 1 
ATOM   10986 C CD2 . PHE F  2 63  ? 18.358  -25.407 14.073  1.00 50.59  ? 63   PHE F CD2 1 
ATOM   10987 C CE1 . PHE F  2 63  ? 19.468  -22.840 14.175  1.00 46.57  ? 63   PHE F CE1 1 
ATOM   10988 C CE2 . PHE F  2 63  ? 17.990  -24.448 13.123  1.00 54.58  ? 63   PHE F CE2 1 
ATOM   10989 C CZ  . PHE F  2 63  ? 18.545  -23.151 13.184  1.00 47.25  ? 63   PHE F CZ  1 
ATOM   10990 N N   . GLU F  2 64  ? 16.840  -24.841 17.182  1.00 56.31  ? 64   GLU F N   1 
ATOM   10991 C CA  . GLU F  2 64  ? 15.416  -24.728 16.903  1.00 56.60  ? 64   GLU F CA  1 
ATOM   10992 C C   . GLU F  2 64  ? 15.140  -23.774 15.733  1.00 58.01  ? 64   GLU F C   1 
ATOM   10993 O O   . GLU F  2 64  ? 15.547  -22.609 15.778  1.00 61.92  ? 64   GLU F O   1 
ATOM   10994 C CB  . GLU F  2 64  ? 14.666  -24.261 18.164  1.00 61.98  ? 64   GLU F CB  1 
ATOM   10995 C CG  . GLU F  2 64  ? 14.857  -25.180 19.389  1.00 72.98  ? 64   GLU F CG  1 
ATOM   10996 C CD  . GLU F  2 64  ? 13.910  -24.867 20.553  1.00 81.22  ? 64   GLU F CD  1 
ATOM   10997 O OE1 . GLU F  2 64  ? 13.256  -23.803 20.538  1.00 81.27  ? 64   GLU F OE1 1 
ATOM   10998 O OE2 . GLU F  2 64  ? 13.822  -25.691 21.490  1.00 86.15  ? 64   GLU F OE2 1 
ATOM   10999 N N   . ALA F  2 65  ? 14.394  -24.239 14.725  1.00 59.45  ? 65   ALA F N   1 
ATOM   11000 C CA  . ALA F  2 65  ? 14.104  -23.422 13.537  1.00 53.26  ? 65   ALA F CA  1 
ATOM   11001 C C   . ALA F  2 65  ? 12.946  -22.460 13.791  1.00 60.39  ? 65   ALA F C   1 
ATOM   11002 O O   . ALA F  2 65  ? 11.964  -22.799 14.468  1.00 60.99  ? 65   ALA F O   1 
ATOM   11003 C CB  . ALA F  2 65  ? 13.778  -24.297 12.357  1.00 42.60  ? 65   ALA F CB  1 
ATOM   11004 N N   . VAL F  2 66  ? 13.078  -21.250 13.256  1.00 56.80  ? 66   VAL F N   1 
ATOM   11005 C CA  . VAL F  2 66  ? 12.009  -20.265 13.316  1.00 53.90  ? 66   VAL F CA  1 
ATOM   11006 C C   . VAL F  2 66  ? 11.750  -19.773 11.894  1.00 53.36  ? 66   VAL F C   1 
ATOM   11007 O O   . VAL F  2 66  ? 12.688  -19.582 11.122  1.00 57.54  ? 66   VAL F O   1 
ATOM   11008 C CB  . VAL F  2 66  ? 12.366  -19.096 14.274  1.00 54.66  ? 66   VAL F CB  1 
ATOM   11009 C CG1 . VAL F  2 66  ? 13.608  -18.395 13.809  1.00 48.75  ? 66   VAL F CG1 1 
ATOM   11010 C CG2 . VAL F  2 66  ? 11.190  -18.113 14.420  1.00 57.95  ? 66   VAL F CG2 1 
ATOM   11011 N N   . GLY F  2 67  ? 10.485  -19.549 11.547  1.00 53.54  ? 67   GLY F N   1 
ATOM   11012 C CA  . GLY F  2 67  ? 10.132  -19.114 10.204  1.00 49.21  ? 67   GLY F CA  1 
ATOM   11013 C C   . GLY F  2 67  ? 10.486  -17.664 9.936   1.00 55.51  ? 67   GLY F C   1 
ATOM   11014 O O   . GLY F  2 67  ? 10.237  -16.805 10.785  1.00 62.94  ? 67   GLY F O   1 
ATOM   11015 N N   . ARG F  2 68  ? 11.073  -17.396 8.767   1.00 51.68  ? 68   ARG F N   1 
ATOM   11016 C CA  . ARG F  2 68  ? 11.378  -16.033 8.324   1.00 41.60  ? 68   ARG F CA  1 
ATOM   11017 C C   . ARG F  2 68  ? 10.909  -15.855 6.899   1.00 39.24  ? 68   ARG F C   1 
ATOM   11018 O O   . ARG F  2 68  ? 10.914  -16.810 6.124   1.00 37.54  ? 68   ARG F O   1 
ATOM   11019 C CB  . ARG F  2 68  ? 12.878  -15.752 8.407   1.00 40.80  ? 68   ARG F CB  1 
ATOM   11020 C CG  . ARG F  2 68  ? 13.471  -15.956 9.783   1.00 40.71  ? 68   ARG F CG  1 
ATOM   11021 C CD  . ARG F  2 68  ? 14.963  -15.719 9.808   1.00 35.81  ? 68   ARG F CD  1 
ATOM   11022 N NE  . ARG F  2 68  ? 15.513  -15.950 11.139  1.00 37.42  ? 68   ARG F NE  1 
ATOM   11023 C CZ  . ARG F  2 68  ? 15.980  -17.111 11.603  1.00 37.84  ? 68   ARG F CZ  1 
ATOM   11024 N NH1 . ARG F  2 68  ? 16.022  -18.199 10.855  1.00 32.87  ? 68   ARG F NH1 1 
ATOM   11025 N NH2 . ARG F  2 68  ? 16.440  -17.166 12.844  1.00 41.60  ? 68   ARG F NH2 1 
ATOM   11026 N N   . GLU F  2 69  ? 10.480  -14.652 6.541   1.00 37.80  ? 69   GLU F N   1 
ATOM   11027 C CA  . GLU F  2 69  ? 10.019  -14.435 5.170   1.00 31.08  ? 69   GLU F CA  1 
ATOM   11028 C C   . GLU F  2 69  ? 10.929  -13.467 4.424   1.00 27.91  ? 69   GLU F C   1 
ATOM   11029 O O   . GLU F  2 69  ? 11.552  -12.605 5.041   1.00 29.34  ? 69   GLU F O   1 
ATOM   11030 C CB  . GLU F  2 69  ? 8.566   -13.947 5.175   1.00 36.34  ? 69   GLU F CB  1 
ATOM   11031 C CG  . GLU F  2 69  ? 7.735   -14.688 6.209   1.00 44.87  ? 69   GLU F CG  1 
ATOM   11032 C CD  . GLU F  2 69  ? 6.276   -14.917 5.821   1.00 47.13  ? 69   GLU F CD  1 
ATOM   11033 O OE1 . GLU F  2 69  ? 6.021   -15.423 4.702   1.00 47.30  ? 69   GLU F OE1 1 
ATOM   11034 O OE2 . GLU F  2 69  ? 5.391   -14.647 6.675   1.00 48.66  ? 69   GLU F OE2 1 
ATOM   11035 N N   . PHE F  2 70  ? 11.014  -13.600 3.098   1.00 31.48  ? 70   PHE F N   1 
ATOM   11036 C CA  . PHE F  2 70  ? 11.912  -12.752 2.302   1.00 27.23  ? 70   PHE F CA  1 
ATOM   11037 C C   . PHE F  2 70  ? 11.181  -12.349 1.063   1.00 25.86  ? 70   PHE F C   1 
ATOM   11038 O O   . PHE F  2 70  ? 10.381  -13.117 0.567   1.00 29.65  ? 70   PHE F O   1 
ATOM   11039 C CB  . PHE F  2 70  ? 13.225  -13.481 1.969   1.00 25.95  ? 70   PHE F CB  1 
ATOM   11040 C CG  . PHE F  2 70  ? 13.986  -13.882 3.188   1.00 29.30  ? 70   PHE F CG  1 
ATOM   11041 C CD1 . PHE F  2 70  ? 14.857  -12.979 3.796   1.00 27.17  ? 70   PHE F CD1 1 
ATOM   11042 C CD2 . PHE F  2 70  ? 13.786  -15.133 3.776   1.00 29.85  ? 70   PHE F CD2 1 
ATOM   11043 C CE1 . PHE F  2 70  ? 15.535  -13.319 4.966   1.00 26.66  ? 70   PHE F CE1 1 
ATOM   11044 C CE2 . PHE F  2 70  ? 14.461  -15.488 4.939   1.00 27.85  ? 70   PHE F CE2 1 
ATOM   11045 C CZ  . PHE F  2 70  ? 15.332  -14.584 5.537   1.00 28.85  ? 70   PHE F CZ  1 
ATOM   11046 N N   . ASN F  2 71  ? 11.457  -11.167 0.526   1.00 28.54  ? 71   ASN F N   1 
ATOM   11047 C CA  . ASN F  2 71  ? 10.734  -10.778 -0.676  1.00 27.58  ? 71   ASN F CA  1 
ATOM   11048 C C   . ASN F  2 71  ? 11.422  -11.338 -1.936  1.00 30.93  ? 71   ASN F C   1 
ATOM   11049 O O   . ASN F  2 71  ? 12.379  -12.092 -1.832  1.00 31.78  ? 71   ASN F O   1 
ATOM   11050 C CB  . ASN F  2 71  ? 10.559  -9.243  -0.770  1.00 24.77  ? 71   ASN F CB  1 
ATOM   11051 C CG  . ASN F  2 71  ? 11.860  -8.493  -1.035  1.00 26.00  ? 71   ASN F CG  1 
ATOM   11052 O OD1 . ASN F  2 71  ? 12.629  -8.851  -1.925  1.00 30.31  ? 71   ASN F OD1 1 
ATOM   11053 N ND2 . ASN F  2 71  ? 12.043  -7.370  -0.350  1.00 27.11  ? 71   ASN F ND2 1 
ATOM   11054 N N   . ASN F  2 72  ? 10.925  -10.956 -3.111  1.00 29.07  ? 72   ASN F N   1 
ATOM   11055 C CA  . ASN F  2 72  ? 11.304  -11.537 -4.383  1.00 30.70  ? 72   ASN F CA  1 
ATOM   11056 C C   . ASN F  2 72  ? 12.718  -11.126 -4.839  1.00 36.47  ? 72   ASN F C   1 
ATOM   11057 O O   . ASN F  2 72  ? 13.243  -11.696 -5.802  1.00 38.23  ? 72   ASN F O   1 
ATOM   11058 C CB  . ASN F  2 72  ? 10.264  -11.117 -5.444  1.00 40.32  ? 72   ASN F CB  1 
ATOM   11059 C CG  . ASN F  2 72  ? 10.289  -11.986 -6.715  1.00 50.90  ? 72   ASN F CG  1 
ATOM   11060 O OD1 . ASN F  2 72  ? 10.424  -13.226 -6.661  1.00 52.08  ? 72   ASN F OD1 1 
ATOM   11061 N ND2 . ASN F  2 72  ? 10.181  -11.323 -7.878  1.00 51.38  ? 72   ASN F ND2 1 
ATOM   11062 N N   . LEU F  2 73  ? 13.312  -10.103 -4.209  1.00 34.35  ? 73   LEU F N   1 
ATOM   11063 C CA  . LEU F  2 73  ? 14.695  -9.710  -4.527  1.00 28.42  ? 73   LEU F CA  1 
ATOM   11064 C C   . LEU F  2 73  ? 15.668  -9.914  -3.348  1.00 30.95  ? 73   LEU F C   1 
ATOM   11065 O O   . LEU F  2 73  ? 16.752  -9.290  -3.294  1.00 26.47  ? 73   LEU F O   1 
ATOM   11066 C CB  . LEU F  2 73  ? 14.741  -8.255  -5.024  1.00 24.64  ? 73   LEU F CB  1 
ATOM   11067 C CG  . LEU F  2 73  ? 14.345  -8.025  -6.500  1.00 31.17  ? 73   LEU F CG  1 
ATOM   11068 C CD1 . LEU F  2 73  ? 14.017  -6.581  -6.824  1.00 21.13  ? 73   LEU F CD1 1 
ATOM   11069 C CD2 . LEU F  2 73  ? 15.459  -8.482  -7.450  1.00 28.40  ? 73   LEU F CD2 1 
ATOM   11070 N N   . GLU F  2 74  ? 15.312  -10.853 -2.467  1.00 25.23  ? 74   GLU F N   1 
ATOM   11071 C CA  . GLU F  2 74  ? 16.190  -11.288 -1.378  1.00 28.61  ? 74   GLU F CA  1 
ATOM   11072 C C   . GLU F  2 74  ? 16.474  -12.781 -1.512  1.00 30.33  ? 74   GLU F C   1 
ATOM   11073 O O   . GLU F  2 74  ? 16.501  -13.502 -0.499  1.00 30.75  ? 74   GLU F O   1 
ATOM   11074 C CB  . GLU F  2 74  ? 15.546  -10.989 -0.005  1.00 27.85  ? 74   GLU F CB  1 
ATOM   11075 C CG  . GLU F  2 74  ? 15.549  -9.495  0.374   1.00 30.32  ? 74   GLU F CG  1 
ATOM   11076 C CD  . GLU F  2 74  ? 14.680  -9.116  1.603   1.00 30.18  ? 74   GLU F CD  1 
ATOM   11077 O OE1 . GLU F  2 74  ? 13.597  -9.732  1.819   1.00 28.88  ? 74   GLU F OE1 1 
ATOM   11078 O OE2 . GLU F  2 74  ? 15.094  -8.172  2.332   1.00 27.58  ? 74   GLU F OE2 1 
ATOM   11079 N N   . ARG F  2 75  ? 16.644  -13.254 -2.753  1.00 24.72  ? 75   ARG F N   1 
ATOM   11080 C CA  . ARG F  2 75  ? 16.802  -14.693 -2.999  1.00 28.72  ? 75   ARG F CA  1 
ATOM   11081 C C   . ARG F  2 75  ? 18.094  -15.300 -2.441  1.00 27.62  ? 75   ARG F C   1 
ATOM   11082 O O   . ARG F  2 75  ? 18.061  -16.436 -1.957  1.00 29.18  ? 75   ARG F O   1 
ATOM   11083 C CB  . ARG F  2 75  ? 16.733  -15.000 -4.502  1.00 29.36  ? 75   ARG F CB  1 
ATOM   11084 C CG  . ARG F  2 75  ? 15.371  -14.756 -5.167  1.00 32.34  ? 75   ARG F CG  1 
ATOM   11085 C CD  . ARG F  2 75  ? 14.309  -15.538 -4.502  1.00 36.03  ? 75   ARG F CD  1 
ATOM   11086 N NE  . ARG F  2 75  ? 13.010  -15.427 -5.157  1.00 46.12  ? 75   ARG F NE  1 
ATOM   11087 C CZ  . ARG F  2 75  ? 11.861  -15.772 -4.569  1.00 49.08  ? 75   ARG F CZ  1 
ATOM   11088 N NH1 . ARG F  2 75  ? 11.867  -16.250 -3.328  1.00 48.59  ? 75   ARG F NH1 1 
ATOM   11089 N NH2 . ARG F  2 75  ? 10.707  -15.663 -5.222  1.00 51.57  ? 75   ARG F NH2 1 
ATOM   11090 N N   . ARG F  2 76  ? 19.208  -14.558 -2.498  1.00 22.04  ? 76   ARG F N   1 
ATOM   11091 C CA  . ARG F  2 76  ? 20.496  -15.053 -1.991  1.00 24.31  ? 76   ARG F CA  1 
ATOM   11092 C C   . ARG F  2 76  ? 20.462  -15.363 -0.488  1.00 29.84  ? 76   ARG F C   1 
ATOM   11093 O O   . ARG F  2 76  ? 20.934  -16.426 -0.065  1.00 30.78  ? 76   ARG F O   1 
ATOM   11094 C CB  . ARG F  2 76  ? 21.626  -14.060 -2.275  1.00 21.72  ? 76   ARG F CB  1 
ATOM   11095 C CG  . ARG F  2 76  ? 22.087  -13.982 -3.734  1.00 21.68  ? 76   ARG F CG  1 
ATOM   11096 C CD  . ARG F  2 76  ? 23.074  -12.830 -3.926  1.00 19.47  ? 76   ARG F CD  1 
ATOM   11097 N NE  . ARG F  2 76  ? 22.426  -11.562 -3.660  1.00 18.29  ? 76   ARG F NE  1 
ATOM   11098 C CZ  . ARG F  2 76  ? 23.056  -10.480 -3.213  1.00 24.75  ? 76   ARG F CZ  1 
ATOM   11099 N NH1 . ARG F  2 76  ? 24.366  -10.540 -2.960  1.00 26.77  ? 76   ARG F NH1 1 
ATOM   11100 N NH2 . ARG F  2 76  ? 22.376  -9.353  -2.972  1.00 15.15  ? 76   ARG F NH2 1 
ATOM   11101 N N   . ILE F  2 77  ? 19.901  -14.452 0.310   1.00 23.76  ? 77   ILE F N   1 
ATOM   11102 C CA  . ILE F  2 77  ? 19.812  -14.665 1.725   1.00 25.69  ? 77   ILE F CA  1 
ATOM   11103 C C   . ILE F  2 77  ? 18.636  -15.582 2.101   1.00 34.09  ? 77   ILE F C   1 
ATOM   11104 O O   . ILE F  2 77  ? 18.659  -16.193 3.177   1.00 33.63  ? 77   ILE F O   1 
ATOM   11105 C CB  . ILE F  2 77  ? 19.697  -13.342 2.503   1.00 24.91  ? 77   ILE F CB  1 
ATOM   11106 C CG1 . ILE F  2 77  ? 18.462  -12.571 2.056   1.00 24.97  ? 77   ILE F CG1 1 
ATOM   11107 C CG2 . ILE F  2 77  ? 20.999  -12.520 2.386   1.00 23.41  ? 77   ILE F CG2 1 
ATOM   11108 C CD1 . ILE F  2 77  ? 18.240  -11.235 2.816   1.00 24.71  ? 77   ILE F CD1 1 
ATOM   11109 N N   . GLU F  2 78  ? 17.609  -15.681 1.255   1.00 31.54  ? 78   GLU F N   1 
ATOM   11110 C CA  . GLU F  2 78  ? 16.588  -16.704 1.486   1.00 30.46  ? 78   GLU F CA  1 
ATOM   11111 C C   . GLU F  2 78  ? 17.198  -18.092 1.389   1.00 33.25  ? 78   GLU F C   1 
ATOM   11112 O O   . GLU F  2 78  ? 16.848  -19.007 2.142   1.00 38.69  ? 78   GLU F O   1 
ATOM   11113 C CB  . GLU F  2 78  ? 15.443  -16.580 0.506   1.00 30.67  ? 78   GLU F CB  1 
ATOM   11114 C CG  . GLU F  2 78  ? 14.477  -17.760 0.544   1.00 28.79  ? 78   GLU F CG  1 
ATOM   11115 C CD  . GLU F  2 78  ? 13.288  -17.564 -0.388  1.00 46.22  ? 78   GLU F CD  1 
ATOM   11116 O OE1 . GLU F  2 78  ? 13.497  -17.218 -1.581  1.00 47.54  ? 78   GLU F OE1 1 
ATOM   11117 O OE2 . GLU F  2 78  ? 12.142  -17.771 0.072   1.00 44.81  ? 78   GLU F OE2 1 
ATOM   11118 N N   . ASN F  2 79  ? 18.109  -18.244 0.442   1.00 31.44  ? 79   ASN F N   1 
ATOM   11119 C CA  . ASN F  2 79  ? 18.830  -19.493 0.250   1.00 35.15  ? 79   ASN F CA  1 
ATOM   11120 C C   . ASN F  2 79  ? 19.830  -19.743 1.399   1.00 37.17  ? 79   ASN F C   1 
ATOM   11121 O O   . ASN F  2 79  ? 19.995  -20.878 1.851   1.00 38.96  ? 79   ASN F O   1 
ATOM   11122 C CB  . ASN F  2 79  ? 19.565  -19.461 -1.102  1.00 35.85  ? 79   ASN F CB  1 
ATOM   11123 C CG  . ASN F  2 79  ? 20.183  -20.786 -1.461  1.00 39.20  ? 79   ASN F CG  1 
ATOM   11124 O OD1 . ASN F  2 79  ? 21.411  -20.911 -1.519  1.00 40.64  ? 79   ASN F OD1 1 
ATOM   11125 N ND2 . ASN F  2 79  ? 19.343  -21.780 -1.732  1.00 39.90  ? 79   ASN F ND2 1 
ATOM   11126 N N   . LEU F  2 80  ? 20.483  -18.676 1.868   1.00 32.87  ? 80   LEU F N   1 
ATOM   11127 C CA  . LEU F  2 80  ? 21.381  -18.760 3.016   1.00 33.26  ? 80   LEU F CA  1 
ATOM   11128 C C   . LEU F  2 80  ? 20.636  -19.237 4.257   1.00 36.14  ? 80   LEU F C   1 
ATOM   11129 O O   . LEU F  2 80  ? 21.079  -20.159 4.928   1.00 42.13  ? 80   LEU F O   1 
ATOM   11130 C CB  . LEU F  2 80  ? 22.045  -17.404 3.284   1.00 35.67  ? 80   LEU F CB  1 
ATOM   11131 C CG  . LEU F  2 80  ? 23.349  -17.293 4.085   1.00 32.72  ? 80   LEU F CG  1 
ATOM   11132 C CD1 . LEU F  2 80  ? 24.025  -15.984 3.790   1.00 28.56  ? 80   LEU F CD1 1 
ATOM   11133 C CD2 . LEU F  2 80  ? 23.097  -17.388 5.556   1.00 35.75  ? 80   LEU F CD2 1 
ATOM   11134 N N   . ASN F  2 81  ? 19.502  -18.616 4.550   1.00 29.77  ? 81   ASN F N   1 
ATOM   11135 C CA  . ASN F  2 81  ? 18.721  -18.954 5.724   1.00 32.57  ? 81   ASN F CA  1 
ATOM   11136 C C   . ASN F  2 81  ? 18.283  -20.425 5.733   1.00 39.69  ? 81   ASN F C   1 
ATOM   11137 O O   . ASN F  2 81  ? 18.420  -21.125 6.742   1.00 38.10  ? 81   ASN F O   1 
ATOM   11138 C CB  . ASN F  2 81  ? 17.495  -18.026 5.790   1.00 33.02  ? 81   ASN F CB  1 
ATOM   11139 C CG  . ASN F  2 81  ? 16.586  -18.327 6.969   1.00 33.22  ? 81   ASN F CG  1 
ATOM   11140 O OD1 . ASN F  2 81  ? 16.860  -17.954 8.114   1.00 30.99  ? 81   ASN F OD1 1 
ATOM   11141 N ND2 . ASN F  2 81  ? 15.483  -19.015 6.684   1.00 28.49  ? 81   ASN F ND2 1 
ATOM   11142 N N   . LYS F  2 82  ? 17.847  -20.897 4.572   1.00 36.54  ? 82   LYS F N   1 
ATOM   11143 C CA  . LYS F  2 82  ? 17.322  -22.240 4.410   1.00 38.67  ? 82   LYS F CA  1 
ATOM   11144 C C   . LYS F  2 82  ? 18.409  -23.277 4.627   1.00 39.86  ? 82   LYS F C   1 
ATOM   11145 O O   . LYS F  2 82  ? 18.190  -24.284 5.292   1.00 40.56  ? 82   LYS F O   1 
ATOM   11146 C CB  . LYS F  2 82  ? 16.729  -22.395 2.999   1.00 38.77  ? 82   LYS F CB  1 
ATOM   11147 C CG  . LYS F  2 82  ? 16.205  -23.770 2.645   1.00 38.82  ? 82   LYS F CG  1 
ATOM   11148 C CD  . LYS F  2 82  ? 15.750  -23.805 1.175   1.00 62.39  ? 82   LYS F CD  1 
ATOM   11149 C CE  . LYS F  2 82  ? 15.264  -25.187 0.733   1.00 68.53  ? 82   LYS F CE  1 
ATOM   11150 N NZ  . LYS F  2 82  ? 14.123  -25.631 1.594   1.00 77.02  ? 82   LYS F NZ  1 
ATOM   11151 N N   . LYS F  2 83  ? 19.583  -23.019 4.068   1.00 35.28  ? 83   LYS F N   1 
ATOM   11152 C CA  . LYS F  2 83  ? 20.688  -23.952 4.186   1.00 40.31  ? 83   LYS F CA  1 
ATOM   11153 C C   . LYS F  2 83  ? 21.280  -24.006 5.590   1.00 40.64  ? 83   LYS F C   1 
ATOM   11154 O O   . LYS F  2 83  ? 21.752  -25.050 6.022   1.00 40.78  ? 83   LYS F O   1 
ATOM   11155 C CB  . LYS F  2 83  ? 21.785  -23.620 3.160   1.00 43.39  ? 83   LYS F CB  1 
ATOM   11156 C CG  . LYS F  2 83  ? 21.437  -24.057 1.736   1.00 40.51  ? 83   LYS F CG  1 
ATOM   11157 C CD  . LYS F  2 83  ? 22.683  -24.202 0.886   1.00 51.92  ? 83   LYS F CD  1 
ATOM   11158 C CE  . LYS F  2 83  ? 23.865  -24.772 1.680   1.00 56.14  ? 83   LYS F CE  1 
ATOM   11159 N NZ  . LYS F  2 83  ? 25.180  -24.070 1.404   1.00 55.65  ? 83   LYS F NZ  1 
ATOM   11160 N N   . MET F  2 84  ? 21.243  -22.886 6.300   1.00 39.51  ? 84   MET F N   1 
ATOM   11161 C CA  . MET F  2 84  ? 21.778  -22.837 7.647   1.00 40.80  ? 84   MET F CA  1 
ATOM   11162 C C   . MET F  2 84  ? 20.918  -23.662 8.602   1.00 42.44  ? 84   MET F C   1 
ATOM   11163 O O   . MET F  2 84  ? 21.432  -24.423 9.428   1.00 38.78  ? 84   MET F O   1 
ATOM   11164 C CB  . MET F  2 84  ? 21.829  -21.398 8.152   1.00 41.18  ? 84   MET F CB  1 
ATOM   11165 C CG  . MET F  2 84  ? 22.470  -21.284 9.510   1.00 40.46  ? 84   MET F CG  1 
ATOM   11166 S SD  . MET F  2 84  ? 21.528  -20.150 10.539  1.00 51.19  ? 84   MET F SD  1 
ATOM   11167 C CE  . MET F  2 84  ? 20.230  -21.242 11.076  1.00 41.81  ? 84   MET F CE  1 
ATOM   11168 N N   . GLU F  2 85  ? 19.606  -23.507 8.461   1.00 37.88  ? 85   GLU F N   1 
ATOM   11169 C CA  . GLU F  2 85  ? 18.662  -24.227 9.283   1.00 41.46  ? 85   GLU F CA  1 
ATOM   11170 C C   . GLU F  2 85  ? 18.633  -25.721 8.924   1.00 46.17  ? 85   GLU F C   1 
ATOM   11171 O O   . GLU F  2 85  ? 18.642  -26.574 9.818   1.00 45.68  ? 85   GLU F O   1 
ATOM   11172 C CB  . GLU F  2 85  ? 17.272  -23.609 9.137   1.00 42.96  ? 85   GLU F CB  1 
ATOM   11173 C CG  . GLU F  2 85  ? 17.162  -22.205 9.734   1.00 43.14  ? 85   GLU F CG  1 
ATOM   11174 C CD  . GLU F  2 85  ? 15.746  -21.874 10.149  1.00 50.77  ? 85   GLU F CD  1 
ATOM   11175 O OE1 . GLU F  2 85  ? 14.828  -22.344 9.432   1.00 51.55  ? 85   GLU F OE1 1 
ATOM   11176 O OE2 . GLU F  2 85  ? 15.561  -21.163 11.178  1.00 48.40  ? 85   GLU F OE2 1 
ATOM   11177 N N   . ASP F  2 86  ? 18.606  -26.037 7.629   1.00 39.77  ? 86   ASP F N   1 
ATOM   11178 C CA  . ASP F  2 86  ? 18.713  -27.428 7.188   1.00 40.05  ? 86   ASP F CA  1 
ATOM   11179 C C   . ASP F  2 86  ? 20.041  -28.041 7.650   1.00 44.87  ? 86   ASP F C   1 
ATOM   11180 O O   . ASP F  2 86  ? 20.118  -29.232 7.969   1.00 44.61  ? 86   ASP F O   1 
ATOM   11181 C CB  . ASP F  2 86  ? 18.593  -27.535 5.666   1.00 43.83  ? 86   ASP F CB  1 
ATOM   11182 C CG  . ASP F  2 86  ? 17.155  -27.348 5.157   1.00 54.69  ? 86   ASP F CG  1 
ATOM   11183 O OD1 . ASP F  2 86  ? 16.264  -26.994 5.967   1.00 53.71  ? 86   ASP F OD1 1 
ATOM   11184 O OD2 . ASP F  2 86  ? 16.930  -27.525 3.927   1.00 63.85  ? 86   ASP F OD2 1 
ATOM   11185 N N   . GLY F  2 87  ? 21.089  -27.218 7.665   1.00 43.92  ? 87   GLY F N   1 
ATOM   11186 C CA  . GLY F  2 87  ? 22.420  -27.657 8.065   1.00 38.46  ? 87   GLY F CA  1 
ATOM   11187 C C   . GLY F  2 87  ? 22.479  -28.108 9.523   1.00 45.57  ? 87   GLY F C   1 
ATOM   11188 O O   . GLY F  2 87  ? 23.113  -29.111 9.837   1.00 47.47  ? 87   GLY F O   1 
ATOM   11189 N N   . PHE F  2 88  ? 21.830  -27.367 10.416  1.00 41.05  ? 88   PHE F N   1 
ATOM   11190 C CA  . PHE F  2 88  ? 21.806  -27.728 11.822  1.00 40.79  ? 88   PHE F CA  1 
ATOM   11191 C C   . PHE F  2 88  ? 20.923  -28.964 12.061  1.00 45.29  ? 88   PHE F C   1 
ATOM   11192 O O   . PHE F  2 88  ? 21.193  -29.761 12.959  1.00 41.76  ? 88   PHE F O   1 
ATOM   11193 C CB  . PHE F  2 88  ? 21.306  -26.549 12.661  1.00 38.60  ? 88   PHE F CB  1 
ATOM   11194 C CG  . PHE F  2 88  ? 22.351  -25.508 12.924  1.00 39.74  ? 88   PHE F CG  1 
ATOM   11195 C CD1 . PHE F  2 88  ? 23.419  -25.773 13.773  1.00 37.92  ? 88   PHE F CD1 1 
ATOM   11196 C CD2 . PHE F  2 88  ? 22.290  -24.274 12.296  1.00 40.42  ? 88   PHE F CD2 1 
ATOM   11197 C CE1 . PHE F  2 88  ? 24.408  -24.810 14.016  1.00 35.73  ? 88   PHE F CE1 1 
ATOM   11198 C CE2 . PHE F  2 88  ? 23.274  -23.303 12.527  1.00 45.28  ? 88   PHE F CE2 1 
ATOM   11199 C CZ  . PHE F  2 88  ? 24.338  -23.580 13.402  1.00 40.07  ? 88   PHE F CZ  1 
ATOM   11200 N N   . LEU F  2 89  ? 19.885  -29.136 11.249  1.00 42.98  ? 89   LEU F N   1 
ATOM   11201 C CA  . LEU F  2 89  ? 18.983  -30.264 11.430  1.00 44.21  ? 89   LEU F CA  1 
ATOM   11202 C C   . LEU F  2 89  ? 19.671  -31.567 11.006  1.00 47.95  ? 89   LEU F C   1 
ATOM   11203 O O   . LEU F  2 89  ? 19.381  -32.628 11.552  1.00 49.75  ? 89   LEU F O   1 
ATOM   11204 C CB  . LEU F  2 89  ? 17.687  -30.042 10.649  1.00 47.98  ? 89   LEU F CB  1 
ATOM   11205 C CG  . LEU F  2 89  ? 16.826  -28.859 11.140  1.00 55.45  ? 89   LEU F CG  1 
ATOM   11206 C CD1 . LEU F  2 89  ? 15.642  -28.650 10.210  1.00 61.33  ? 89   LEU F CD1 1 
ATOM   11207 C CD2 . LEU F  2 89  ? 16.326  -28.971 12.601  1.00 44.31  ? 89   LEU F CD2 1 
ATOM   11208 N N   . ASP F  2 90  ? 20.572  -31.492 10.027  1.00 46.87  ? 90   ASP F N   1 
ATOM   11209 C CA  . ASP F  2 90  ? 21.352  -32.666 9.617   1.00 44.44  ? 90   ASP F CA  1 
ATOM   11210 C C   . ASP F  2 90  ? 22.420  -33.061 10.660  1.00 46.58  ? 90   ASP F C   1 
ATOM   11211 O O   . ASP F  2 90  ? 22.694  -34.242 10.868  1.00 48.43  ? 90   ASP F O   1 
ATOM   11212 C CB  . ASP F  2 90  ? 22.010  -32.405 8.266   1.00 44.01  ? 90   ASP F CB  1 
ATOM   11213 C CG  . ASP F  2 90  ? 20.993  -32.335 7.110   1.00 55.05  ? 90   ASP F CG  1 
ATOM   11214 O OD1 . ASP F  2 90  ? 19.870  -32.850 7.280   1.00 49.43  ? 90   ASP F OD1 1 
ATOM   11215 O OD2 . ASP F  2 90  ? 21.311  -31.749 6.038   1.00 51.24  ? 90   ASP F OD2 1 
ATOM   11216 N N   . VAL F  2 91  ? 23.037  -32.064 11.287  1.00 45.54  ? 91   VAL F N   1 
ATOM   11217 C CA  . VAL F  2 91  ? 24.047  -32.267 12.330  1.00 44.07  ? 91   VAL F CA  1 
ATOM   11218 C C   . VAL F  2 91  ? 23.462  -32.890 13.605  1.00 47.47  ? 91   VAL F C   1 
ATOM   11219 O O   . VAL F  2 91  ? 24.024  -33.836 14.165  1.00 46.12  ? 91   VAL F O   1 
ATOM   11220 C CB  . VAL F  2 91  ? 24.745  -30.931 12.678  1.00 39.61  ? 91   VAL F CB  1 
ATOM   11221 C CG1 . VAL F  2 91  ? 25.521  -31.012 13.988  1.00 36.76  ? 91   VAL F CG1 1 
ATOM   11222 C CG2 . VAL F  2 91  ? 25.631  -30.509 11.539  1.00 39.32  ? 91   VAL F CG2 1 
ATOM   11223 N N   . TRP F  2 92  ? 22.334  -32.367 14.069  1.00 43.89  ? 92   TRP F N   1 
ATOM   11224 C CA  . TRP F  2 92  ? 21.760  -32.891 15.290  1.00 46.32  ? 92   TRP F CA  1 
ATOM   11225 C C   . TRP F  2 92  ? 21.047  -34.238 15.058  1.00 45.58  ? 92   TRP F C   1 
ATOM   11226 O O   . TRP F  2 92  ? 20.857  -35.007 15.988  1.00 41.61  ? 92   TRP F O   1 
ATOM   11227 C CB  . TRP F  2 92  ? 20.816  -31.867 15.918  1.00 46.78  ? 92   TRP F CB  1 
ATOM   11228 C CG  . TRP F  2 92  ? 21.543  -30.746 16.645  1.00 51.44  ? 92   TRP F CG  1 
ATOM   11229 C CD1 . TRP F  2 92  ? 21.651  -29.441 16.251  1.00 49.59  ? 92   TRP F CD1 1 
ATOM   11230 C CD2 . TRP F  2 92  ? 22.279  -30.849 17.879  1.00 49.86  ? 92   TRP F CD2 1 
ATOM   11231 N NE1 . TRP F  2 92  ? 22.387  -28.727 17.166  1.00 46.90  ? 92   TRP F NE1 1 
ATOM   11232 C CE2 . TRP F  2 92  ? 22.790  -29.568 18.170  1.00 47.97  ? 92   TRP F CE2 1 
ATOM   11233 C CE3 . TRP F  2 92  ? 22.552  -31.900 18.761  1.00 48.37  ? 92   TRP F CE3 1 
ATOM   11234 C CZ2 . TRP F  2 92  ? 23.553  -29.308 19.315  1.00 48.31  ? 92   TRP F CZ2 1 
ATOM   11235 C CZ3 . TRP F  2 92  ? 23.312  -31.640 19.897  1.00 46.45  ? 92   TRP F CZ3 1 
ATOM   11236 C CH2 . TRP F  2 92  ? 23.804  -30.355 20.160  1.00 48.14  ? 92   TRP F CH2 1 
ATOM   11237 N N   . THR F  2 93  ? 20.682  -34.532 13.818  1.00 46.14  ? 93   THR F N   1 
ATOM   11238 C CA  . THR F  2 93  ? 20.086  -35.823 13.503  1.00 42.44  ? 93   THR F CA  1 
ATOM   11239 C C   . THR F  2 93  ? 21.194  -36.872 13.529  1.00 42.34  ? 93   THR F C   1 
ATOM   11240 O O   . THR F  2 93  ? 21.010  -37.968 14.054  1.00 42.58  ? 93   THR F O   1 
ATOM   11241 C CB  . THR F  2 93  ? 19.351  -35.810 12.122  1.00 41.49  ? 93   THR F CB  1 
ATOM   11242 O OG1 . THR F  2 93  ? 18.124  -35.075 12.228  1.00 43.58  ? 93   THR F OG1 1 
ATOM   11243 C CG2 . THR F  2 93  ? 19.021  -37.217 11.646  1.00 38.63  ? 93   THR F CG2 1 
ATOM   11244 N N   . TYR F  2 94  ? 22.353  -36.524 12.981  1.00 42.54  ? 94   TYR F N   1 
ATOM   11245 C CA  . TYR F  2 94  ? 23.532  -37.394 13.031  1.00 43.40  ? 94   TYR F CA  1 
ATOM   11246 C C   . TYR F  2 94  ? 23.985  -37.631 14.470  1.00 44.25  ? 94   TYR F C   1 
ATOM   11247 O O   . TYR F  2 94  ? 24.311  -38.750 14.844  1.00 48.20  ? 94   TYR F O   1 
ATOM   11248 C CB  . TYR F  2 94  ? 24.682  -36.794 12.200  1.00 46.74  ? 94   TYR F CB  1 
ATOM   11249 C CG  . TYR F  2 94  ? 26.069  -37.429 12.362  1.00 46.70  ? 94   TYR F CG  1 
ATOM   11250 C CD1 . TYR F  2 94  ? 26.909  -37.056 13.413  1.00 48.18  ? 94   TYR F CD1 1 
ATOM   11251 C CD2 . TYR F  2 94  ? 26.559  -38.352 11.428  1.00 45.69  ? 94   TYR F CD2 1 
ATOM   11252 C CE1 . TYR F  2 94  ? 28.176  -37.608 13.555  1.00 49.98  ? 94   TYR F CE1 1 
ATOM   11253 C CE2 . TYR F  2 94  ? 27.832  -38.909 11.555  1.00 47.55  ? 94   TYR F CE2 1 
ATOM   11254 C CZ  . TYR F  2 94  ? 28.636  -38.532 12.626  1.00 55.05  ? 94   TYR F CZ  1 
ATOM   11255 O OH  . TYR F  2 94  ? 29.904  -39.062 12.794  1.00 56.19  ? 94   TYR F OH  1 
ATOM   11256 N N   . ASN F  2 95  ? 24.008  -36.584 15.278  1.00 42.78  ? 95   ASN F N   1 
ATOM   11257 C CA  . ASN F  2 95  ? 24.478  -36.722 16.647  1.00 39.88  ? 95   ASN F CA  1 
ATOM   11258 C C   . ASN F  2 95  ? 23.628  -37.689 17.487  1.00 46.77  ? 95   ASN F C   1 
ATOM   11259 O O   . ASN F  2 95  ? 24.169  -38.465 18.292  1.00 43.73  ? 95   ASN F O   1 
ATOM   11260 C CB  . ASN F  2 95  ? 24.505  -35.345 17.300  1.00 39.96  ? 95   ASN F CB  1 
ATOM   11261 C CG  . ASN F  2 95  ? 25.780  -34.593 17.001  1.00 43.43  ? 95   ASN F CG  1 
ATOM   11262 O OD1 . ASN F  2 95  ? 26.611  -35.061 16.226  1.00 44.29  ? 95   ASN F OD1 1 
ATOM   11263 N ND2 . ASN F  2 95  ? 25.908  -33.389 17.548  1.00 42.11  ? 95   ASN F ND2 1 
ATOM   11264 N N   . ALA F  2 96  ? 22.312  -37.682 17.250  1.00 45.23  ? 96   ALA F N   1 
ATOM   11265 C CA  . ALA F  2 96  ? 21.380  -38.484 18.041  1.00 40.51  ? 96   ALA F CA  1 
ATOM   11266 C C   . ALA F  2 96  ? 21.365  -39.911 17.530  1.00 39.80  ? 96   ALA F C   1 
ATOM   11267 O O   . ALA F  2 96  ? 21.372  -40.831 18.318  1.00 42.49  ? 96   ALA F O   1 
ATOM   11268 C CB  . ALA F  2 96  ? 19.973  -37.891 18.009  1.00 31.94  ? 96   ALA F CB  1 
ATOM   11269 N N   . GLU F  2 97  ? 21.406  -40.096 16.215  1.00 40.29  ? 97   GLU F N   1 
ATOM   11270 C CA  . GLU F  2 97  ? 21.389  -41.440 15.655  1.00 43.37  ? 97   GLU F CA  1 
ATOM   11271 C C   . GLU F  2 97  ? 22.665  -42.191 16.017  1.00 47.88  ? 97   GLU F C   1 
ATOM   11272 O O   . GLU F  2 97  ? 22.607  -43.350 16.432  1.00 50.08  ? 97   GLU F O   1 
ATOM   11273 C CB  . GLU F  2 97  ? 21.217  -41.408 14.136  1.00 39.17  ? 97   GLU F CB  1 
ATOM   11274 C CG  . GLU F  2 97  ? 19.838  -40.987 13.727  1.00 39.81  ? 97   GLU F CG  1 
ATOM   11275 C CD  . GLU F  2 97  ? 19.616  -40.988 12.231  1.00 42.77  ? 97   GLU F CD  1 
ATOM   11276 O OE1 . GLU F  2 97  ? 20.586  -41.117 11.452  1.00 50.47  ? 97   GLU F OE1 1 
ATOM   11277 O OE2 . GLU F  2 97  ? 18.446  -40.870 11.825  1.00 45.23  ? 97   GLU F OE2 1 
ATOM   11278 N N   . LEU F  2 98  ? 23.807  -41.529 15.861  1.00 42.90  ? 98   LEU F N   1 
ATOM   11279 C CA  . LEU F  2 98  ? 25.099  -42.150 16.143  1.00 45.30  ? 98   LEU F CA  1 
ATOM   11280 C C   . LEU F  2 98  ? 25.328  -42.421 17.637  1.00 49.45  ? 98   LEU F C   1 
ATOM   11281 O O   . LEU F  2 98  ? 26.047  -43.351 18.005  1.00 49.56  ? 98   LEU F O   1 
ATOM   11282 C CB  . LEU F  2 98  ? 26.238  -41.273 15.627  1.00 45.45  ? 98   LEU F CB  1 
ATOM   11283 C CG  . LEU F  2 98  ? 27.640  -41.876 15.718  1.00 50.04  ? 98   LEU F CG  1 
ATOM   11284 C CD1 . LEU F  2 98  ? 27.837  -42.853 14.575  1.00 52.39  ? 98   LEU F CD1 1 
ATOM   11285 C CD2 . LEU F  2 98  ? 28.746  -40.814 15.749  1.00 43.45  ? 98   LEU F CD2 1 
ATOM   11286 N N   . LEU F  2 99  ? 24.749  -41.595 18.502  1.00 47.59  ? 99   LEU F N   1 
ATOM   11287 C CA  . LEU F  2 99  ? 24.983  -41.760 19.928  1.00 44.92  ? 99   LEU F CA  1 
ATOM   11288 C C   . LEU F  2 99  ? 24.228  -42.994 20.370  1.00 50.60  ? 99   LEU F C   1 
ATOM   11289 O O   . LEU F  2 99  ? 24.717  -43.790 21.162  1.00 51.49  ? 99   LEU F O   1 
ATOM   11290 C CB  . LEU F  2 99  ? 24.542  -40.515 20.713  1.00 46.97  ? 99   LEU F CB  1 
ATOM   11291 C CG  . LEU F  2 99  ? 24.572  -40.505 22.249  1.00 53.79  ? 99   LEU F CG  1 
ATOM   11292 C CD1 . LEU F  2 99  ? 25.991  -40.635 22.812  1.00 48.51  ? 99   LEU F CD1 1 
ATOM   11293 C CD2 . LEU F  2 99  ? 23.912  -39.236 22.778  1.00 51.08  ? 99   LEU F CD2 1 
ATOM   11294 N N   . VAL F  2 100 ? 23.063  -43.189 19.773  1.00 50.97  ? 100  VAL F N   1 
ATOM   11295 C CA  . VAL F  2 100 ? 22.238  -44.335 20.090  1.00 50.96  ? 100  VAL F CA  1 
ATOM   11296 C C   . VAL F  2 100 ? 22.878  -45.645 19.625  1.00 49.35  ? 100  VAL F C   1 
ATOM   11297 O O   . VAL F  2 100 ? 22.940  -46.603 20.381  1.00 55.03  ? 100  VAL F O   1 
ATOM   11298 C CB  . VAL F  2 100 ? 20.842  -44.156 19.448  1.00 50.76  ? 100  VAL F CB  1 
ATOM   11299 C CG1 . VAL F  2 100 ? 20.070  -45.476 19.417  1.00 52.02  ? 100  VAL F CG1 1 
ATOM   11300 C CG2 . VAL F  2 100 ? 20.074  -43.059 20.175  1.00 41.11  ? 100  VAL F CG2 1 
ATOM   11301 N N   . LEU F  2 101 ? 23.428  -45.665 18.422  1.00 47.94  ? 101  LEU F N   1 
ATOM   11302 C CA  . LEU F  2 101 ? 24.123  -46.853 17.941  1.00 53.38  ? 101  LEU F CA  1 
ATOM   11303 C C   . LEU F  2 101 ? 25.318  -47.180 18.824  1.00 53.25  ? 101  LEU F C   1 
ATOM   11304 O O   . LEU F  2 101 ? 25.539  -48.340 19.164  1.00 54.76  ? 101  LEU F O   1 
ATOM   11305 C CB  . LEU F  2 101 ? 24.588  -46.675 16.488  1.00 46.78  ? 101  LEU F CB  1 
ATOM   11306 C CG  . LEU F  2 101 ? 23.708  -47.352 15.439  1.00 51.06  ? 101  LEU F CG  1 
ATOM   11307 C CD1 . LEU F  2 101 ? 22.285  -47.422 15.918  1.00 48.64  ? 101  LEU F CD1 1 
ATOM   11308 C CD2 . LEU F  2 101 ? 23.774  -46.618 14.112  1.00 60.01  ? 101  LEU F CD2 1 
ATOM   11309 N N   . MET F  2 102 ? 26.062  -46.160 19.232  1.00 47.97  ? 102  MET F N   1 
ATOM   11310 C CA  . MET F  2 102 ? 27.253  -46.411 20.018  1.00 51.49  ? 102  MET F CA  1 
ATOM   11311 C C   . MET F  2 102 ? 26.902  -46.935 21.399  1.00 56.31  ? 102  MET F C   1 
ATOM   11312 O O   . MET F  2 102 ? 27.520  -47.888 21.879  1.00 58.23  ? 102  MET F O   1 
ATOM   11313 C CB  . MET F  2 102 ? 28.109  -45.152 20.149  1.00 49.87  ? 102  MET F CB  1 
ATOM   11314 C CG  . MET F  2 102 ? 28.916  -44.816 18.921  1.00 53.82  ? 102  MET F CG  1 
ATOM   11315 S SD  . MET F  2 102 ? 30.058  -43.455 19.246  1.00 58.41  ? 102  MET F SD  1 
ATOM   11316 C CE  . MET F  2 102 ? 31.375  -43.814 18.075  1.00 56.69  ? 102  MET F CE  1 
ATOM   11317 N N   . GLU F  2 103 ? 25.895  -46.341 22.028  1.00 55.31  ? 103  GLU F N   1 
ATOM   11318 C CA  . GLU F  2 103 ? 25.587  -46.699 23.403  1.00 56.61  ? 103  GLU F CA  1 
ATOM   11319 C C   . GLU F  2 103 ? 24.745  -47.976 23.455  1.00 57.64  ? 103  GLU F C   1 
ATOM   11320 O O   . GLU F  2 103 ? 24.738  -48.674 24.474  1.00 59.78  ? 103  GLU F O   1 
ATOM   11321 C CB  . GLU F  2 103 ? 24.879  -45.540 24.124  1.00 48.59  ? 103  GLU F CB  1 
ATOM   11322 C CG  . GLU F  2 103 ? 25.794  -44.353 24.366  1.00 50.80  ? 103  GLU F CG  1 
ATOM   11323 C CD  . GLU F  2 103 ? 27.040  -44.739 25.146  1.00 59.72  ? 103  GLU F CD  1 
ATOM   11324 O OE1 . GLU F  2 103 ? 26.917  -45.522 26.107  1.00 57.15  ? 103  GLU F OE1 1 
ATOM   11325 O OE2 . GLU F  2 103 ? 28.152  -44.296 24.773  1.00 65.47  ? 103  GLU F OE2 1 
ATOM   11326 N N   . ASN F  2 104 ? 24.095  -48.318 22.346  1.00 53.08  ? 104  ASN F N   1 
ATOM   11327 C CA  . ASN F  2 104 ? 23.434  -49.614 22.252  1.00 55.45  ? 104  ASN F CA  1 
ATOM   11328 C C   . ASN F  2 104 ? 24.466  -50.728 22.333  1.00 56.22  ? 104  ASN F C   1 
ATOM   11329 O O   . ASN F  2 104 ? 24.328  -51.655 23.137  1.00 58.36  ? 104  ASN F O   1 
ATOM   11330 C CB  . ASN F  2 104 ? 22.624  -49.727 20.955  1.00 52.00  ? 104  ASN F CB  1 
ATOM   11331 C CG  . ASN F  2 104 ? 21.229  -49.145 21.084  1.00 53.13  ? 104  ASN F CG  1 
ATOM   11332 O OD1 . ASN F  2 104 ? 20.834  -48.660 22.152  1.00 49.74  ? 104  ASN F OD1 1 
ATOM   11333 N ND2 . ASN F  2 104 ? 20.482  -49.157 19.979  1.00 54.59  ? 104  ASN F ND2 1 
ATOM   11334 N N   . GLU F  2 105 ? 25.510  -50.610 21.518  1.00 56.72  ? 105  GLU F N   1 
ATOM   11335 C CA  . GLU F  2 105 ? 26.566  -51.602 21.465  1.00 55.70  ? 105  GLU F CA  1 
ATOM   11336 C C   . GLU F  2 105 ? 27.261  -51.768 22.830  1.00 59.27  ? 105  GLU F C   1 
ATOM   11337 O O   . GLU F  2 105 ? 27.664  -52.871 23.206  1.00 58.65  ? 105  GLU F O   1 
ATOM   11338 C CB  . GLU F  2 105 ? 27.613  -51.228 20.420  1.00 52.83  ? 105  GLU F CB  1 
ATOM   11339 C CG  . GLU F  2 105 ? 28.504  -52.411 20.064  1.00 66.60  ? 105  GLU F CG  1 
ATOM   11340 C CD  . GLU F  2 105 ? 29.976  -52.065 19.987  1.00 69.01  ? 105  GLU F CD  1 
ATOM   11341 O OE1 . GLU F  2 105 ? 30.358  -50.965 20.444  1.00 62.68  ? 105  GLU F OE1 1 
ATOM   11342 O OE2 . GLU F  2 105 ? 30.751  -52.920 19.504  1.00 79.66  ? 105  GLU F OE2 1 
ATOM   11343 N N   . ARG F  2 106 ? 27.427  -50.672 23.563  1.00 58.57  ? 106  ARG F N   1 
ATOM   11344 C CA  . ARG F  2 106 ? 28.122  -50.751 24.843  1.00 58.74  ? 106  ARG F CA  1 
ATOM   11345 C C   . ARG F  2 106 ? 27.212  -51.267 25.942  1.00 57.94  ? 106  ARG F C   1 
ATOM   11346 O O   . ARG F  2 106 ? 27.667  -51.918 26.883  1.00 55.33  ? 106  ARG F O   1 
ATOM   11347 C CB  . ARG F  2 106 ? 28.703  -49.390 25.215  1.00 55.69  ? 106  ARG F CB  1 
ATOM   11348 C CG  . ARG F  2 106 ? 29.897  -49.102 24.363  1.00 64.35  ? 106  ARG F CG  1 
ATOM   11349 C CD  . ARG F  2 106 ? 30.591  -47.801 24.673  1.00 74.43  ? 106  ARG F CD  1 
ATOM   11350 N NE  . ARG F  2 106 ? 31.616  -47.546 23.657  1.00 81.68  ? 106  ARG F NE  1 
ATOM   11351 C CZ  . ARG F  2 106 ? 31.338  -47.221 22.388  1.00 82.48  ? 106  ARG F CZ  1 
ATOM   11352 N NH1 . ARG F  2 106 ? 30.078  -47.123 21.973  1.00 75.39  ? 106  ARG F NH1 1 
ATOM   11353 N NH2 . ARG F  2 106 ? 32.314  -47.005 21.516  1.00 88.21  ? 106  ARG F NH2 1 
ATOM   11354 N N   . THR F  2 107 ? 25.922  -51.000 25.801  1.00 54.24  ? 107  THR F N   1 
ATOM   11355 C CA  . THR F  2 107 ? 24.964  -51.462 26.773  1.00 53.57  ? 107  THR F CA  1 
ATOM   11356 C C   . THR F  2 107 ? 24.918  -52.990 26.712  1.00 58.69  ? 107  THR F C   1 
ATOM   11357 O O   . THR F  2 107 ? 24.890  -53.658 27.738  1.00 57.80  ? 107  THR F O   1 
ATOM   11358 C CB  . THR F  2 107 ? 23.574  -50.866 26.514  1.00 53.45  ? 107  THR F CB  1 
ATOM   11359 O OG1 . THR F  2 107 ? 23.581  -49.479 26.871  1.00 49.64  ? 107  THR F OG1 1 
ATOM   11360 C CG2 . THR F  2 107 ? 22.489  -51.610 27.317  1.00 54.02  ? 107  THR F CG2 1 
ATOM   11361 N N   . LEU F  2 108 ? 24.958  -53.536 25.503  1.00 56.57  ? 108  LEU F N   1 
ATOM   11362 C CA  . LEU F  2 108 ? 24.927  -54.980 25.323  1.00 55.18  ? 108  LEU F CA  1 
ATOM   11363 C C   . LEU F  2 108 ? 26.200  -55.639 25.868  1.00 57.53  ? 108  LEU F C   1 
ATOM   11364 O O   . LEU F  2 108 ? 26.126  -56.694 26.495  1.00 57.02  ? 108  LEU F O   1 
ATOM   11365 C CB  . LEU F  2 108 ? 24.720  -55.317 23.840  1.00 52.22  ? 108  LEU F CB  1 
ATOM   11366 C CG  . LEU F  2 108 ? 23.350  -54.939 23.248  1.00 58.00  ? 108  LEU F CG  1 
ATOM   11367 C CD1 . LEU F  2 108 ? 23.230  -55.264 21.758  1.00 51.55  ? 108  LEU F CD1 1 
ATOM   11368 C CD2 . LEU F  2 108 ? 22.221  -55.619 24.023  1.00 53.76  ? 108  LEU F CD2 1 
ATOM   11369 N N   . ASP F  2 109 ? 27.354  -55.005 25.665  1.00 57.89  ? 109  ASP F N   1 
ATOM   11370 C CA  . ASP F  2 109 ? 28.612  -55.524 26.209  1.00 57.15  ? 109  ASP F CA  1 
ATOM   11371 C C   . ASP F  2 109 ? 28.715  -55.299 27.714  1.00 57.86  ? 109  ASP F C   1 
ATOM   11372 O O   . ASP F  2 109 ? 29.571  -55.895 28.359  1.00 60.96  ? 109  ASP F O   1 
ATOM   11373 C CB  . ASP F  2 109 ? 29.840  -54.898 25.523  1.00 58.18  ? 109  ASP F CB  1 
ATOM   11374 C CG  . ASP F  2 109 ? 30.084  -55.443 24.116  1.00 67.71  ? 109  ASP F CG  1 
ATOM   11375 O OD1 . ASP F  2 109 ? 29.588  -56.545 23.805  1.00 73.18  ? 109  ASP F OD1 1 
ATOM   11376 O OD2 . ASP F  2 109 ? 30.786  -54.771 23.319  1.00 75.30  ? 109  ASP F OD2 1 
ATOM   11377 N N   . PHE F  2 110 ? 27.870  -54.422 28.263  1.00 59.76  ? 110  PHE F N   1 
ATOM   11378 C CA  . PHE F  2 110 ? 27.850  -54.141 29.708  1.00 58.68  ? 110  PHE F CA  1 
ATOM   11379 C C   . PHE F  2 110 ? 27.218  -55.309 30.458  1.00 60.87  ? 110  PHE F C   1 
ATOM   11380 O O   . PHE F  2 110 ? 27.679  -55.688 31.533  1.00 60.95  ? 110  PHE F O   1 
ATOM   11381 C CB  . PHE F  2 110 ? 27.094  -52.839 30.000  1.00 54.74  ? 110  PHE F CB  1 
ATOM   11382 C CG  . PHE F  2 110 ? 26.929  -52.515 31.480  1.00 54.54  ? 110  PHE F CG  1 
ATOM   11383 C CD1 . PHE F  2 110 ? 28.028  -52.230 32.279  1.00 53.58  ? 110  PHE F CD1 1 
ATOM   11384 C CD2 . PHE F  2 110 ? 25.659  -52.411 32.047  1.00 54.52  ? 110  PHE F CD2 1 
ATOM   11385 C CE1 . PHE F  2 110 ? 27.862  -51.912 33.633  1.00 51.29  ? 110  PHE F CE1 1 
ATOM   11386 C CE2 . PHE F  2 110 ? 25.493  -52.078 33.380  1.00 49.19  ? 110  PHE F CE2 1 
ATOM   11387 C CZ  . PHE F  2 110 ? 26.592  -51.830 34.173  1.00 45.19  ? 110  PHE F CZ  1 
ATOM   11388 N N   . HIS F  2 111 ? 26.154  -55.866 29.889  1.00 59.16  ? 111  HIS F N   1 
ATOM   11389 C CA  . HIS F  2 111 ? 25.530  -57.057 30.432  1.00 57.22  ? 111  HIS F CA  1 
ATOM   11390 C C   . HIS F  2 111 ? 26.468  -58.251 30.286  1.00 58.93  ? 111  HIS F C   1 
ATOM   11391 O O   . HIS F  2 111 ? 26.571  -59.084 31.189  1.00 62.63  ? 111  HIS F O   1 
ATOM   11392 C CB  . HIS F  2 111 ? 24.196  -57.310 29.745  1.00 62.88  ? 111  HIS F CB  1 
ATOM   11393 C CG  . HIS F  2 111 ? 23.151  -56.297 30.093  1.00 65.50  ? 111  HIS F CG  1 
ATOM   11394 N ND1 . HIS F  2 111 ? 22.953  -55.842 31.379  1.00 64.22  ? 111  HIS F ND1 1 
ATOM   11395 C CD2 . HIS F  2 111 ? 22.253  -55.639 29.321  1.00 67.42  ? 111  HIS F CD2 1 
ATOM   11396 C CE1 . HIS F  2 111 ? 21.976  -54.952 31.385  1.00 65.87  ? 111  HIS F CE1 1 
ATOM   11397 N NE2 . HIS F  2 111 ? 21.534  -54.810 30.149  1.00 64.99  ? 111  HIS F NE2 1 
ATOM   11398 N N   . ASP F  2 112 ? 27.158  -58.331 29.149  1.00 59.78  ? 112  ASP F N   1 
ATOM   11399 C CA  . ASP F  2 112 ? 28.084  -59.436 28.900  1.00 63.08  ? 112  ASP F CA  1 
ATOM   11400 C C   . ASP F  2 112 ? 29.218  -59.438 29.928  1.00 65.23  ? 112  ASP F C   1 
ATOM   11401 O O   . ASP F  2 112 ? 29.589  -60.481 30.470  1.00 62.47  ? 112  ASP F O   1 
ATOM   11402 C CB  . ASP F  2 112 ? 28.666  -59.357 27.480  1.00 57.57  ? 112  ASP F CB  1 
ATOM   11403 C CG  . ASP F  2 112 ? 29.337  -60.662 27.039  1.00 70.74  ? 112  ASP F CG  1 
ATOM   11404 O OD1 . ASP F  2 112 ? 28.995  -61.735 27.576  1.00 73.45  ? 112  ASP F OD1 1 
ATOM   11405 O OD2 . ASP F  2 112 ? 30.224  -60.619 26.161  1.00 75.04  ? 112  ASP F OD2 1 
ATOM   11406 N N   . SER F  2 113 ? 29.753  -58.259 30.218  1.00 67.04  ? 113  SER F N   1 
ATOM   11407 C CA  . SER F  2 113 ? 30.793  -58.146 31.230  1.00 68.27  ? 113  SER F CA  1 
ATOM   11408 C C   . SER F  2 113 ? 30.244  -58.506 32.615  1.00 65.84  ? 113  SER F C   1 
ATOM   11409 O O   . SER F  2 113 ? 30.963  -59.053 33.461  1.00 59.99  ? 113  SER F O   1 
ATOM   11410 C CB  . SER F  2 113 ? 31.388  -56.739 31.247  1.00 62.60  ? 113  SER F CB  1 
ATOM   11411 O OG  . SER F  2 113 ? 32.202  -56.563 32.394  1.00 65.39  ? 113  SER F OG  1 
ATOM   11412 N N   . ASN F  2 114 ? 28.967  -58.200 32.835  1.00 60.64  ? 114  ASN F N   1 
ATOM   11413 C CA  . ASN F  2 114 ? 28.369  -58.406 34.143  1.00 63.01  ? 114  ASN F CA  1 
ATOM   11414 C C   . ASN F  2 114 ? 28.044  -59.885 34.399  1.00 62.91  ? 114  ASN F C   1 
ATOM   11415 O O   . ASN F  2 114 ? 28.118  -60.347 35.534  1.00 59.40  ? 114  ASN F O   1 
ATOM   11416 C CB  . ASN F  2 114 ? 27.103  -57.546 34.306  1.00 60.50  ? 114  ASN F CB  1 
ATOM   11417 C CG  . ASN F  2 114 ? 27.411  -56.076 34.570  1.00 57.11  ? 114  ASN F CG  1 
ATOM   11418 O OD1 . ASN F  2 114 ? 28.546  -55.708 34.888  1.00 52.55  ? 114  ASN F OD1 1 
ATOM   11419 N ND2 . ASN F  2 114 ? 26.381  -55.234 34.485  1.00 58.79  ? 114  ASN F ND2 1 
ATOM   11420 N N   . VAL F  2 115 ? 27.738  -60.641 33.350  1.00 61.24  ? 115  VAL F N   1 
ATOM   11421 C CA  . VAL F  2 115 ? 27.485  -62.056 33.552  1.00 60.64  ? 115  VAL F CA  1 
ATOM   11422 C C   . VAL F  2 115 ? 28.806  -62.764 33.919  1.00 60.22  ? 115  VAL F C   1 
ATOM   11423 O O   . VAL F  2 115 ? 28.852  -63.492 34.906  1.00 59.89  ? 115  VAL F O   1 
ATOM   11424 C CB  . VAL F  2 115 ? 26.830  -62.712 32.310  1.00 60.69  ? 115  VAL F CB  1 
ATOM   11425 C CG1 . VAL F  2 115 ? 26.991  -64.217 32.354  1.00 57.25  ? 115  VAL F CG1 1 
ATOM   11426 C CG2 . VAL F  2 115 ? 25.350  -62.358 32.232  1.00 55.93  ? 115  VAL F CG2 1 
ATOM   11427 N N   . LYS F  2 116 ? 29.877  -62.510 33.162  1.00 59.74  ? 116  LYS F N   1 
ATOM   11428 C CA  . LYS F  2 116 ? 31.197  -63.122 33.414  1.00 60.44  ? 116  LYS F CA  1 
ATOM   11429 C C   . LYS F  2 116 ? 31.834  -62.755 34.772  1.00 60.88  ? 116  LYS F C   1 
ATOM   11430 O O   . LYS F  2 116 ? 32.498  -63.583 35.395  1.00 64.50  ? 116  LYS F O   1 
ATOM   11431 C CB  . LYS F  2 116 ? 32.174  -62.766 32.281  1.00 60.78  ? 116  LYS F CB  1 
ATOM   11432 C CG  . LYS F  2 116 ? 33.595  -63.333 32.465  1.00 65.03  ? 116  LYS F CG  1 
ATOM   11433 C CD  . LYS F  2 116 ? 34.505  -62.994 31.293  1.00 72.82  ? 116  LYS F CD  1 
ATOM   11434 C CE  . LYS F  2 116 ? 35.877  -63.661 31.400  1.00 65.32  ? 116  LYS F CE  1 
ATOM   11435 N NZ  . LYS F  2 116 ? 36.850  -62.862 32.184  1.00 57.87  ? 116  LYS F NZ  1 
ATOM   11436 N N   . ASN F  2 117 ? 31.670  -61.511 35.209  1.00 62.89  ? 117  ASN F N   1 
ATOM   11437 C CA  . ASN F  2 117 ? 32.219  -61.073 36.493  1.00 64.06  ? 117  ASN F CA  1 
ATOM   11438 C C   . ASN F  2 117 ? 31.524  -61.764 37.666  1.00 67.49  ? 117  ASN F C   1 
ATOM   11439 O O   . ASN F  2 117 ? 32.135  -61.985 38.715  1.00 68.28  ? 117  ASN F O   1 
ATOM   11440 C CB  . ASN F  2 117 ? 32.116  -59.550 36.637  1.00 64.80  ? 117  ASN F CB  1 
ATOM   11441 C CG  . ASN F  2 117 ? 33.132  -58.806 35.780  1.00 68.34  ? 117  ASN F CG  1 
ATOM   11442 O OD1 . ASN F  2 117 ? 33.891  -59.411 35.021  1.00 69.13  ? 117  ASN F OD1 1 
ATOM   11443 N ND2 . ASN F  2 117 ? 33.134  -57.484 35.886  1.00 72.29  ? 117  ASN F ND2 1 
ATOM   11444 N N   . LEU F  2 118 ? 30.246  -62.094 37.479  1.00 65.87  ? 118  LEU F N   1 
ATOM   11445 C CA  . LEU F  2 118 ? 29.477  -62.841 38.466  1.00 63.49  ? 118  LEU F CA  1 
ATOM   11446 C C   . LEU F  2 118 ? 29.970  -64.290 38.502  1.00 69.46  ? 118  LEU F C   1 
ATOM   11447 O O   . LEU F  2 118 ? 30.091  -64.884 39.573  1.00 68.16  ? 118  LEU F O   1 
ATOM   11448 C CB  . LEU F  2 118 ? 27.981  -62.796 38.137  1.00 63.09  ? 118  LEU F CB  1 
ATOM   11449 C CG  . LEU F  2 118 ? 27.034  -63.437 39.155  1.00 72.61  ? 118  LEU F CG  1 
ATOM   11450 C CD1 . LEU F  2 118 ? 27.019  -62.619 40.433  1.00 73.73  ? 118  LEU F CD1 1 
ATOM   11451 C CD2 . LEU F  2 118 ? 25.622  -63.596 38.608  1.00 69.80  ? 118  LEU F CD2 1 
ATOM   11452 N N   . TYR F  2 119 ? 30.247  -64.844 37.318  1.00 65.08  ? 119  TYR F N   1 
ATOM   11453 C CA  . TYR F  2 119 ? 30.800  -66.182 37.190  1.00 63.97  ? 119  TYR F CA  1 
ATOM   11454 C C   . TYR F  2 119 ? 32.179  -66.284 37.854  1.00 69.47  ? 119  TYR F C   1 
ATOM   11455 O O   . TYR F  2 119 ? 32.414  -67.229 38.604  1.00 73.96  ? 119  TYR F O   1 
ATOM   11456 C CB  . TYR F  2 119 ? 30.872  -66.600 35.711  1.00 70.20  ? 119  TYR F CB  1 
ATOM   11457 C CG  . TYR F  2 119 ? 31.521  -67.959 35.453  1.00 71.00  ? 119  TYR F CG  1 
ATOM   11458 C CD1 . TYR F  2 119 ? 30.760  -69.131 35.419  1.00 73.52  ? 119  TYR F CD1 1 
ATOM   11459 C CD2 . TYR F  2 119 ? 32.893  -68.066 35.240  1.00 67.17  ? 119  TYR F CD2 1 
ATOM   11460 C CE1 . TYR F  2 119 ? 31.355  -70.374 35.181  1.00 74.84  ? 119  TYR F CE1 1 
ATOM   11461 C CE2 . TYR F  2 119 ? 33.496  -69.296 35.003  1.00 74.59  ? 119  TYR F CE2 1 
ATOM   11462 C CZ  . TYR F  2 119 ? 32.728  -70.446 34.974  1.00 76.14  ? 119  TYR F CZ  1 
ATOM   11463 O OH  . TYR F  2 119 ? 33.345  -71.660 34.745  1.00 71.25  ? 119  TYR F OH  1 
ATOM   11464 N N   . ASP F  2 120 ? 33.085  -65.335 37.601  1.00 65.64  ? 120  ASP F N   1 
ATOM   11465 C CA  . ASP F  2 120 ? 34.412  -65.381 38.243  1.00 69.69  ? 120  ASP F CA  1 
ATOM   11466 C C   . ASP F  2 120 ? 34.335  -65.110 39.749  1.00 74.56  ? 120  ASP F C   1 
ATOM   11467 O O   . ASP F  2 120 ? 35.278  -65.405 40.489  1.00 71.59  ? 120  ASP F O   1 
ATOM   11468 C CB  . ASP F  2 120 ? 35.399  -64.398 37.598  1.00 68.70  ? 120  ASP F CB  1 
ATOM   11469 C CG  . ASP F  2 120 ? 35.986  -64.919 36.297  1.00 76.39  ? 120  ASP F CG  1 
ATOM   11470 O OD1 . ASP F  2 120 ? 35.721  -66.091 35.953  1.00 80.06  ? 120  ASP F OD1 1 
ATOM   11471 O OD2 . ASP F  2 120 ? 36.735  -64.171 35.632  1.00 77.12  ? 120  ASP F OD2 1 
ATOM   11472 N N   . LYS F  2 121 ? 33.215  -64.532 40.184  1.00 72.94  ? 121  LYS F N   1 
ATOM   11473 C CA  . LYS F  2 121 ? 32.969  -64.230 41.589  1.00 70.61  ? 121  LYS F CA  1 
ATOM   11474 C C   . LYS F  2 121 ? 32.792  -65.534 42.347  1.00 76.26  ? 121  LYS F C   1 
ATOM   11475 O O   . LYS F  2 121 ? 33.196  -65.664 43.507  1.00 78.11  ? 121  LYS F O   1 
ATOM   11476 C CB  . LYS F  2 121 ? 31.724  -63.350 41.749  1.00 71.86  ? 121  LYS F CB  1 
ATOM   11477 C CG  . LYS F  2 121 ? 31.287  -63.131 43.188  1.00 79.25  ? 121  LYS F CG  1 
ATOM   11478 C CD  . LYS F  2 121 ? 29.829  -62.678 43.264  1.00 80.58  ? 121  LYS F CD  1 
ATOM   11479 C CE  . LYS F  2 121 ? 29.362  -62.546 44.715  1.00 84.06  ? 121  LYS F CE  1 
ATOM   11480 N NZ  . LYS F  2 121 ? 27.966  -62.043 44.815  1.00 80.83  ? 121  LYS F NZ  1 
ATOM   11481 N N   . VAL F  2 122 ? 32.181  -66.501 41.670  1.00 72.38  ? 122  VAL F N   1 
ATOM   11482 C CA  . VAL F  2 122 ? 31.920  -67.793 42.267  1.00 72.85  ? 122  VAL F CA  1 
ATOM   11483 C C   . VAL F  2 122 ? 33.099  -68.736 42.062  1.00 73.28  ? 122  VAL F C   1 
ATOM   11484 O O   . VAL F  2 122 ? 33.464  -69.468 42.977  1.00 78.50  ? 122  VAL F O   1 
ATOM   11485 C CB  . VAL F  2 122 ? 30.639  -68.421 41.677  1.00 72.81  ? 122  VAL F CB  1 
ATOM   11486 C CG1 . VAL F  2 122 ? 30.399  -69.797 42.261  1.00 76.39  ? 122  VAL F CG1 1 
ATOM   11487 C CG2 . VAL F  2 122 ? 29.444  -67.521 41.941  1.00 74.27  ? 122  VAL F CG2 1 
ATOM   11488 N N   . ARG F  2 123 ? 33.739  -68.659 40.895  1.00 73.75  ? 123  ARG F N   1 
ATOM   11489 C CA  . ARG F  2 123 ? 34.892  -69.508 40.573  1.00 74.29  ? 123  ARG F CA  1 
ATOM   11490 C C   . ARG F  2 123 ? 36.042  -69.256 41.532  1.00 71.12  ? 123  ARG F C   1 
ATOM   11491 O O   . ARG F  2 123 ? 36.831  -70.150 41.814  1.00 73.23  ? 123  ARG F O   1 
ATOM   11492 C CB  . ARG F  2 123 ? 35.377  -69.265 39.132  1.00 78.25  ? 123  ARG F CB  1 
ATOM   11493 C CG  . ARG F  2 123 ? 36.589  -70.122 38.694  1.00 78.32  ? 123  ARG F CG  1 
ATOM   11494 C CD  . ARG F  2 123 ? 37.208  -69.633 37.376  1.00 81.88  ? 123  ARG F CD  1 
ATOM   11495 N NE  . ARG F  2 123 ? 37.808  -68.299 37.474  1.00 79.66  ? 123  ARG F NE  1 
ATOM   11496 C CZ  . ARG F  2 123 ? 39.060  -68.056 37.865  1.00 76.68  ? 123  ARG F CZ  1 
ATOM   11497 N NH1 . ARG F  2 123 ? 39.876  -69.055 38.183  1.00 83.36  ? 123  ARG F NH1 1 
ATOM   11498 N NH2 . ARG F  2 123 ? 39.507  -66.809 37.923  1.00 71.84  ? 123  ARG F NH2 1 
ATOM   11499 N N   . LEU F  2 124 ? 36.131  -68.024 42.018  1.00 74.29  ? 124  LEU F N   1 
ATOM   11500 C CA  . LEU F  2 124 ? 37.197  -67.626 42.924  1.00 75.36  ? 124  LEU F CA  1 
ATOM   11501 C C   . LEU F  2 124 ? 36.973  -68.069 44.357  1.00 76.22  ? 124  LEU F C   1 
ATOM   11502 O O   . LEU F  2 124 ? 37.921  -68.154 45.137  1.00 79.87  ? 124  LEU F O   1 
ATOM   11503 C CB  . LEU F  2 124 ? 37.370  -66.105 42.873  1.00 77.31  ? 124  LEU F CB  1 
ATOM   11504 C CG  . LEU F  2 124 ? 38.217  -65.605 41.701  1.00 76.63  ? 124  LEU F CG  1 
ATOM   11505 C CD1 . LEU F  2 124 ? 38.064  -64.111 41.487  1.00 77.53  ? 124  LEU F CD1 1 
ATOM   11506 C CD2 . LEU F  2 124 ? 39.677  -65.938 41.966  1.00 79.55  ? 124  LEU F CD2 1 
ATOM   11507 N N   . GLN F  2 125 ? 35.738  -68.417 44.692  1.00 78.24  ? 125  GLN F N   1 
ATOM   11508 C CA  . GLN F  2 125 ? 35.425  -68.758 46.070  1.00 80.01  ? 125  GLN F CA  1 
ATOM   11509 C C   . GLN F  2 125 ? 35.629  -70.245 46.311  1.00 85.64  ? 125  GLN F C   1 
ATOM   11510 O O   . GLN F  2 125 ? 36.199  -70.649 47.331  1.00 87.27  ? 125  GLN F O   1 
ATOM   11511 C CB  . GLN F  2 125 ? 33.981  -68.370 46.410  1.00 79.20  ? 125  GLN F CB  1 
ATOM   11512 C CG  . GLN F  2 125 ? 33.738  -66.873 46.600  1.00 78.65  ? 125  GLN F CG  1 
ATOM   11513 C CD  . GLN F  2 125 ? 32.294  -66.567 46.966  1.00 83.62  ? 125  GLN F CD  1 
ATOM   11514 O OE1 . GLN F  2 125 ? 31.904  -66.659 48.134  1.00 81.81  ? 125  GLN F OE1 1 
ATOM   11515 N NE2 . GLN F  2 125 ? 31.488  -66.213 45.964  1.00 84.02  ? 125  GLN F NE2 1 
ATOM   11516 N N   . LEU F  2 126 ? 35.194  -71.050 45.346  1.00 81.06  ? 126  LEU F N   1 
ATOM   11517 C CA  . LEU F  2 126 ? 35.215  -72.498 45.487  1.00 80.81  ? 126  LEU F CA  1 
ATOM   11518 C C   . LEU F  2 126 ? 36.567  -73.128 45.136  1.00 83.23  ? 126  LEU F C   1 
ATOM   11519 O O   . LEU F  2 126 ? 37.057  -73.968 45.887  1.00 86.71  ? 126  LEU F O   1 
ATOM   11520 C CB  . LEU F  2 126 ? 34.077  -73.135 44.666  1.00 78.62  ? 126  LEU F CB  1 
ATOM   11521 C CG  . LEU F  2 126 ? 32.580  -72.870 44.966  1.00 75.92  ? 126  LEU F CG  1 
ATOM   11522 C CD1 . LEU F  2 126 ? 32.245  -71.539 45.638  1.00 77.07  ? 126  LEU F CD1 1 
ATOM   11523 C CD2 . LEU F  2 126 ? 31.720  -73.059 43.722  1.00 71.84  ? 126  LEU F CD2 1 
ATOM   11524 N N   . ARG F  2 127 ? 37.158  -72.732 44.009  1.00 86.04  ? 127  ARG F N   1 
ATOM   11525 C CA  . ARG F  2 127 ? 38.417  -73.312 43.497  1.00 90.28  ? 127  ARG F CA  1 
ATOM   11526 C C   . ARG F  2 127 ? 38.342  -74.842 43.470  1.00 90.54  ? 127  ARG F C   1 
ATOM   11527 O O   . ARG F  2 127 ? 37.458  -75.401 42.822  1.00 91.96  ? 127  ARG F O   1 
ATOM   11528 C CB  . ARG F  2 127 ? 39.675  -72.828 44.252  1.00 87.30  ? 127  ARG F CB  1 
ATOM   11529 C CG  . ARG F  2 127 ? 39.620  -72.625 45.738  1.00 82.71  ? 127  ARG F CG  1 
ATOM   11530 C CD  . ARG F  2 127 ? 40.723  -71.692 46.139  1.00 88.52  ? 127  ARG F CD  1 
ATOM   11531 N NE  . ARG F  2 127 ? 40.841  -71.556 47.585  1.00 96.67  ? 127  ARG F NE  1 
ATOM   11532 C CZ  . ARG F  2 127 ? 41.754  -70.792 48.174  1.00 97.73  ? 127  ARG F CZ  1 
ATOM   11533 N NH1 . ARG F  2 127 ? 42.608  -70.110 47.426  1.00 100.80 ? 127  ARG F NH1 1 
ATOM   11534 N NH2 . ARG F  2 127 ? 41.818  -70.705 49.498  1.00 89.78  ? 127  ARG F NH2 1 
ATOM   11535 N N   . ASP F  2 128 ? 39.267  -75.522 44.150  1.00 94.86  ? 128  ASP F N   1 
ATOM   11536 C CA  . ASP F  2 128 ? 39.333  -76.986 44.074  1.00 90.41  ? 128  ASP F CA  1 
ATOM   11537 C C   . ASP F  2 128 ? 38.324  -77.718 44.975  1.00 89.13  ? 128  ASP F C   1 
ATOM   11538 O O   . ASP F  2 128 ? 38.482  -78.912 45.234  1.00 95.02  ? 128  ASP F O   1 
ATOM   11539 C CB  . ASP F  2 128 ? 40.749  -77.478 44.407  1.00 88.34  ? 128  ASP F CB  1 
ATOM   11540 C CG  . ASP F  2 128 ? 41.282  -76.918 45.716  1.00 92.79  ? 128  ASP F CG  1 
ATOM   11541 O OD1 . ASP F  2 128 ? 40.481  -76.466 46.566  1.00 93.50  ? 128  ASP F OD1 1 
ATOM   11542 O OD2 . ASP F  2 128 ? 42.515  -76.966 45.910  1.00 93.29  ? 128  ASP F OD2 1 
ATOM   11543 N N   . ASN F  2 129 ? 37.312  -77.000 45.462  1.00 88.40  ? 129  ASN F N   1 
ATOM   11544 C CA  . ASN F  2 129 ? 36.164  -77.601 46.149  1.00 85.85  ? 129  ASN F CA  1 
ATOM   11545 C C   . ASN F  2 129 ? 35.011  -77.847 45.165  1.00 88.11  ? 129  ASN F C   1 
ATOM   11546 O O   . ASN F  2 129 ? 33.915  -78.258 45.564  1.00 85.96  ? 129  ASN F O   1 
ATOM   11547 C CB  . ASN F  2 129 ? 35.672  -76.712 47.297  1.00 84.51  ? 129  ASN F CB  1 
ATOM   11548 C CG  . ASN F  2 129 ? 36.652  -76.636 48.447  1.00 85.25  ? 129  ASN F CG  1 
ATOM   11549 O OD1 . ASN F  2 129 ? 37.798  -77.073 48.342  1.00 84.23  ? 129  ASN F OD1 1 
ATOM   11550 N ND2 . ASN F  2 129 ? 36.204  -76.070 49.556  1.00 88.21  ? 129  ASN F ND2 1 
ATOM   11551 N N   . ALA F  2 130 ? 35.242  -77.512 43.893  1.00 88.22  ? 130  ALA F N   1 
ATOM   11552 C CA  . ALA F  2 130 ? 34.274  -77.748 42.818  1.00 84.74  ? 130  ALA F CA  1 
ATOM   11553 C C   . ALA F  2 130 ? 34.971  -77.859 41.454  1.00 89.17  ? 130  ALA F C   1 
ATOM   11554 O O   . ALA F  2 130 ? 36.171  -77.588 41.340  1.00 86.60  ? 130  ALA F O   1 
ATOM   11555 C CB  . ALA F  2 130 ? 33.232  -76.664 42.793  1.00 84.03  ? 130  ALA F CB  1 
ATOM   11556 N N   . LYS F  2 131 ? 34.214  -78.268 40.431  1.00 94.30  ? 131  LYS F N   1 
ATOM   11557 C CA  . LYS F  2 131 ? 34.726  -78.398 39.059  1.00 92.02  ? 131  LYS F CA  1 
ATOM   11558 C C   . LYS F  2 131 ? 34.032  -77.497 38.040  1.00 89.18  ? 131  LYS F C   1 
ATOM   11559 O O   . LYS F  2 131 ? 32.812  -77.329 38.077  1.00 87.66  ? 131  LYS F O   1 
ATOM   11560 C CB  . LYS F  2 131 ? 34.602  -79.844 38.583  1.00 89.01  ? 131  LYS F CB  1 
ATOM   11561 C CG  . LYS F  2 131 ? 35.418  -80.809 39.391  1.00 96.51  ? 131  LYS F CG  1 
ATOM   11562 C CD  . LYS F  2 131 ? 35.457  -82.168 38.723  1.00 101.72 ? 131  LYS F CD  1 
ATOM   11563 C CE  . LYS F  2 131 ? 34.060  -82.735 38.525  1.00 100.98 ? 131  LYS F CE  1 
ATOM   11564 N NZ  . LYS F  2 131 ? 34.105  -84.084 37.874  1.00 102.76 ? 131  LYS F NZ  1 
ATOM   11565 N N   . GLU F  2 132 ? 34.817  -76.920 37.133  1.00 90.24  ? 132  GLU F N   1 
ATOM   11566 C CA  . GLU F  2 132 ? 34.250  -76.153 36.028  1.00 91.30  ? 132  GLU F CA  1 
ATOM   11567 C C   . GLU F  2 132 ? 33.822  -77.090 34.919  1.00 86.35  ? 132  GLU F C   1 
ATOM   11568 O O   . GLU F  2 132 ? 34.658  -77.713 34.262  1.00 88.32  ? 132  GLU F O   1 
ATOM   11569 C CB  . GLU F  2 132 ? 35.242  -75.123 35.473  1.00 90.60  ? 132  GLU F CB  1 
ATOM   11570 C CG  . GLU F  2 132 ? 35.840  -74.181 36.500  1.00 90.94  ? 132  GLU F CG  1 
ATOM   11571 C CD  . GLU F  2 132 ? 36.570  -73.020 35.849  1.00 90.96  ? 132  GLU F CD  1 
ATOM   11572 O OE1 . GLU F  2 132 ? 36.193  -72.642 34.715  1.00 82.73  ? 132  GLU F OE1 1 
ATOM   11573 O OE2 . GLU F  2 132 ? 37.524  -72.499 36.467  1.00 89.71  ? 132  GLU F OE2 1 
ATOM   11574 N N   . LEU F  2 133 ? 32.518  -77.182 34.710  1.00 83.67  ? 133  LEU F N   1 
ATOM   11575 C CA  . LEU F  2 133 ? 31.992  -78.031 33.657  1.00 86.76  ? 133  LEU F CA  1 
ATOM   11576 C C   . LEU F  2 133 ? 32.220  -77.393 32.287  1.00 88.04  ? 133  LEU F C   1 
ATOM   11577 O O   . LEU F  2 133 ? 32.363  -78.095 31.285  1.00 86.18  ? 133  LEU F O   1 
ATOM   11578 C CB  . LEU F  2 133 ? 30.500  -78.316 33.881  1.00 88.03  ? 133  LEU F CB  1 
ATOM   11579 C CG  . LEU F  2 133 ? 30.095  -79.349 34.949  1.00 88.18  ? 133  LEU F CG  1 
ATOM   11580 C CD1 . LEU F  2 133 ? 30.445  -78.918 36.363  1.00 86.90  ? 133  LEU F CD1 1 
ATOM   11581 C CD2 . LEU F  2 133 ? 28.606  -79.667 34.846  1.00 83.76  ? 133  LEU F CD2 1 
ATOM   11582 N N   . GLY F  2 134 ? 32.273  -76.063 32.251  1.00 88.33  ? 134  GLY F N   1 
ATOM   11583 C CA  . GLY F  2 134 ? 32.570  -75.352 31.021  1.00 82.37  ? 134  GLY F CA  1 
ATOM   11584 C C   . GLY F  2 134 ? 31.344  -74.756 30.352  1.00 79.76  ? 134  GLY F C   1 
ATOM   11585 O O   . GLY F  2 134 ? 31.393  -74.390 29.176  1.00 78.21  ? 134  GLY F O   1 
ATOM   11586 N N   . ASN F  2 135 ? 30.244  -74.663 31.098  1.00 82.35  ? 135  ASN F N   1 
ATOM   11587 C CA  . ASN F  2 135 ? 28.993  -74.101 30.577  1.00 80.67  ? 135  ASN F CA  1 
ATOM   11588 C C   . ASN F  2 135 ? 28.328  -73.140 31.575  1.00 75.43  ? 135  ASN F C   1 
ATOM   11589 O O   . ASN F  2 135 ? 27.136  -72.846 31.479  1.00 69.70  ? 135  ASN F O   1 
ATOM   11590 C CB  . ASN F  2 135 ? 28.016  -75.217 30.195  1.00 74.01  ? 135  ASN F CB  1 
ATOM   11591 C CG  . ASN F  2 135 ? 27.568  -76.044 31.388  1.00 77.33  ? 135  ASN F CG  1 
ATOM   11592 O OD1 . ASN F  2 135 ? 28.224  -76.071 32.439  1.00 78.08  ? 135  ASN F OD1 1 
ATOM   11593 N ND2 . ASN F  2 135 ? 26.443  -76.735 31.226  1.00 73.12  ? 135  ASN F ND2 1 
ATOM   11594 N N   . GLY F  2 136 ? 29.100  -72.677 32.551  1.00 73.58  ? 136  GLY F N   1 
ATOM   11595 C CA  . GLY F  2 136 ? 28.582  -71.753 33.539  1.00 77.03  ? 136  GLY F CA  1 
ATOM   11596 C C   . GLY F  2 136 ? 28.262  -72.452 34.843  1.00 82.53  ? 136  GLY F C   1 
ATOM   11597 O O   . GLY F  2 136 ? 27.877  -71.800 35.822  1.00 77.10  ? 136  GLY F O   1 
ATOM   11598 N N   . CYS F  2 137 ? 28.425  -73.781 34.848  1.00 86.86  ? 137  CYS F N   1 
ATOM   11599 C CA  . CYS F  2 137 ? 28.081  -74.622 36.003  1.00 79.89  ? 137  CYS F CA  1 
ATOM   11600 C C   . CYS F  2 137 ? 29.273  -75.077 36.841  1.00 82.04  ? 137  CYS F C   1 
ATOM   11601 O O   . CYS F  2 137 ? 30.371  -75.316 36.321  1.00 84.69  ? 137  CYS F O   1 
ATOM   11602 C CB  . CYS F  2 137 ? 27.296  -75.863 35.562  1.00 80.32  ? 137  CYS F CB  1 
ATOM   11603 S SG  . CYS F  2 137 ? 25.577  -75.594 35.030  1.00 76.17  ? 137  CYS F SG  1 
ATOM   11604 N N   . PHE F  2 138 ? 29.031  -75.169 38.148  1.00 81.46  ? 138  PHE F N   1 
ATOM   11605 C CA  . PHE F  2 138 ? 29.998  -75.687 39.113  1.00 87.53  ? 138  PHE F CA  1 
ATOM   11606 C C   . PHE F  2 138 ? 29.456  -76.956 39.787  1.00 88.71  ? 138  PHE F C   1 
ATOM   11607 O O   . PHE F  2 138 ? 28.406  -76.916 40.439  1.00 88.05  ? 138  PHE F O   1 
ATOM   11608 C CB  . PHE F  2 138 ? 30.314  -74.648 40.192  1.00 85.01  ? 138  PHE F CB  1 
ATOM   11609 C CG  . PHE F  2 138 ? 31.022  -73.431 39.682  1.00 85.15  ? 138  PHE F CG  1 
ATOM   11610 C CD1 . PHE F  2 138 ? 32.363  -73.485 39.327  1.00 85.62  ? 138  PHE F CD1 1 
ATOM   11611 C CD2 . PHE F  2 138 ? 30.353  -72.214 39.596  1.00 83.78  ? 138  PHE F CD2 1 
ATOM   11612 C CE1 . PHE F  2 138 ? 33.022  -72.348 38.862  1.00 82.41  ? 138  PHE F CE1 1 
ATOM   11613 C CE2 . PHE F  2 138 ? 31.004  -71.074 39.135  1.00 82.12  ? 138  PHE F CE2 1 
ATOM   11614 C CZ  . PHE F  2 138 ? 32.341  -71.142 38.772  1.00 77.02  ? 138  PHE F CZ  1 
ATOM   11615 N N   . GLU F  2 139 ? 30.161  -78.076 39.627  1.00 88.69  ? 139  GLU F N   1 
ATOM   11616 C CA  . GLU F  2 139 ? 29.803  -79.315 40.327  1.00 91.29  ? 139  GLU F CA  1 
ATOM   11617 C C   . GLU F  2 139 ? 30.667  -79.483 41.569  1.00 85.27  ? 139  GLU F C   1 
ATOM   11618 O O   . GLU F  2 139 ? 31.882  -79.648 41.464  1.00 81.35  ? 139  GLU F O   1 
ATOM   11619 C CB  . GLU F  2 139 ? 29.946  -80.535 39.424  1.00 87.01  ? 139  GLU F CB  1 
ATOM   11620 C CG  . GLU F  2 139 ? 29.425  -81.808 40.062  1.00 87.66  ? 139  GLU F CG  1 
ATOM   11621 C CD  . GLU F  2 139 ? 29.523  -83.008 39.140  1.00 97.29  ? 139  GLU F CD  1 
ATOM   11622 O OE1 . GLU F  2 139 ? 30.579  -83.181 38.489  1.00 93.92  ? 139  GLU F OE1 1 
ATOM   11623 O OE2 . GLU F  2 139 ? 28.540  -83.780 39.068  1.00 102.64 ? 139  GLU F OE2 1 
ATOM   11624 N N   . PHE F  2 140 ? 30.046  -79.438 42.744  1.00 87.09  ? 140  PHE F N   1 
ATOM   11625 C CA  . PHE F  2 140 ? 30.811  -79.436 43.990  1.00 94.02  ? 140  PHE F CA  1 
ATOM   11626 C C   . PHE F  2 140 ? 31.486  -80.775 44.290  1.00 93.99  ? 140  PHE F C   1 
ATOM   11627 O O   . PHE F  2 140 ? 31.117  -81.814 43.739  1.00 94.42  ? 140  PHE F O   1 
ATOM   11628 C CB  . PHE F  2 140 ? 29.910  -79.129 45.192  1.00 95.30  ? 140  PHE F CB  1 
ATOM   11629 C CG  . PHE F  2 140 ? 29.279  -77.766 45.185  1.00 97.58  ? 140  PHE F CG  1 
ATOM   11630 C CD1 . PHE F  2 140 ? 28.098  -77.542 44.493  1.00 92.98  ? 140  PHE F CD1 1 
ATOM   11631 C CD2 . PHE F  2 140 ? 29.829  -76.729 45.932  1.00 97.45  ? 140  PHE F CD2 1 
ATOM   11632 C CE1 . PHE F  2 140 ? 27.497  -76.303 44.514  1.00 93.59  ? 140  PHE F CE1 1 
ATOM   11633 C CE2 . PHE F  2 140 ? 29.236  -75.482 45.958  1.00 94.66  ? 140  PHE F CE2 1 
ATOM   11634 C CZ  . PHE F  2 140 ? 28.066  -75.267 45.252  1.00 98.48  ? 140  PHE F CZ  1 
ATOM   11635 N N   . TYR F  2 141 ? 32.486  -80.726 45.167  1.00 94.83  ? 141  TYR F N   1 
ATOM   11636 C CA  . TYR F  2 141 ? 33.170  -81.921 45.654  1.00 95.37  ? 141  TYR F CA  1 
ATOM   11637 C C   . TYR F  2 141 ? 32.633  -82.273 47.040  1.00 96.04  ? 141  TYR F C   1 
ATOM   11638 O O   . TYR F  2 141 ? 33.181  -83.141 47.720  1.00 97.99  ? 141  TYR F O   1 
ATOM   11639 C CB  . TYR F  2 141 ? 34.683  -81.723 45.743  1.00 95.88  ? 141  TYR F CB  1 
ATOM   11640 C CG  . TYR F  2 141 ? 35.476  -81.850 44.458  1.00 97.82  ? 141  TYR F CG  1 
ATOM   11641 C CD1 . TYR F  2 141 ? 35.181  -82.832 43.517  1.00 95.97  ? 141  TYR F CD1 1 
ATOM   11642 C CD2 . TYR F  2 141 ? 36.568  -81.025 44.224  1.00 94.61  ? 141  TYR F CD2 1 
ATOM   11643 C CE1 . TYR F  2 141 ? 35.934  -82.960 42.362  1.00 96.14  ? 141  TYR F CE1 1 
ATOM   11644 C CE2 . TYR F  2 141 ? 37.321  -81.141 43.076  1.00 96.81  ? 141  TYR F CE2 1 
ATOM   11645 C CZ  . TYR F  2 141 ? 37.006  -82.111 42.150  1.00 98.19  ? 141  TYR F CZ  1 
ATOM   11646 O OH  . TYR F  2 141 ? 37.773  -82.221 41.012  1.00 91.89  ? 141  TYR F OH  1 
ATOM   11647 N N   . HIS F  2 142 ? 31.575  -81.579 47.456  1.00 95.91  ? 142  HIS F N   1 
ATOM   11648 C CA  . HIS F  2 142 ? 30.900  -81.858 48.723  1.00 91.70  ? 142  HIS F CA  1 
ATOM   11649 C C   . HIS F  2 142 ? 29.407  -81.570 48.595  1.00 92.34  ? 142  HIS F C   1 
ATOM   11650 O O   . HIS F  2 142 ? 28.900  -81.414 47.483  1.00 92.83  ? 142  HIS F O   1 
ATOM   11651 C CB  . HIS F  2 142 ? 31.535  -81.071 49.888  1.00 92.32  ? 142  HIS F CB  1 
ATOM   11652 C CG  . HIS F  2 142 ? 31.520  -79.578 49.725  1.00 99.63  ? 142  HIS F CG  1 
ATOM   11653 N ND1 . HIS F  2 142 ? 32.525  -78.887 49.078  1.00 95.84  ? 142  HIS F ND1 1 
ATOM   11654 C CD2 . HIS F  2 142 ? 30.650  -78.639 50.176  1.00 97.86  ? 142  HIS F CD2 1 
ATOM   11655 C CE1 . HIS F  2 142 ? 32.259  -77.593 49.110  1.00 93.04  ? 142  HIS F CE1 1 
ATOM   11656 N NE2 . HIS F  2 142 ? 31.128  -77.415 49.771  1.00 93.63  ? 142  HIS F NE2 1 
ATOM   11657 N N   . ARG F  2 143 ? 28.708  -81.490 49.724  1.00 95.21  ? 143  ARG F N   1 
ATOM   11658 C CA  . ARG F  2 143 ? 27.263  -81.265 49.708  1.00 97.27  ? 143  ARG F CA  1 
ATOM   11659 C C   . ARG F  2 143 ? 26.920  -79.818 50.006  1.00 97.57  ? 143  ARG F C   1 
ATOM   11660 O O   . ARG F  2 143 ? 27.541  -79.186 50.868  1.00 94.34  ? 143  ARG F O   1 
ATOM   11661 C CB  . ARG F  2 143 ? 26.565  -82.149 50.743  1.00 92.44  ? 143  ARG F CB  1 
ATOM   11662 C CG  . ARG F  2 143 ? 26.483  -83.610 50.397  1.00 92.80  ? 143  ARG F CG  1 
ATOM   11663 C CD  . ARG F  2 143 ? 25.755  -84.357 51.502  1.00 90.55  ? 143  ARG F CD  1 
ATOM   11664 N NE  . ARG F  2 143 ? 25.461  -85.740 51.143  1.00 88.89  ? 143  ARG F NE  1 
ATOM   11665 C CZ  . ARG F  2 143 ? 26.371  -86.708 51.144  1.00 83.61  ? 143  ARG F CZ  1 
ATOM   11666 N NH1 . ARG F  2 143 ? 27.630  -86.440 51.464  1.00 86.12  ? 143  ARG F NH1 1 
ATOM   11667 N NH2 . ARG F  2 143 ? 26.029  -87.940 50.814  1.00 83.93  ? 143  ARG F NH2 1 
ATOM   11668 N N   . CYS F  2 144 ? 25.924  -79.303 49.288  1.00 99.73  ? 144  CYS F N   1 
ATOM   11669 C CA  . CYS F  2 144 ? 25.474  -77.930 49.480  1.00 101.33 ? 144  CYS F CA  1 
ATOM   11670 C C   . CYS F  2 144 ? 23.969  -77.919 49.726  1.00 98.09  ? 144  CYS F C   1 
ATOM   11671 O O   . CYS F  2 144 ? 23.184  -78.244 48.834  1.00 96.74  ? 144  CYS F O   1 
ATOM   11672 C CB  . CYS F  2 144 ? 25.824  -77.064 48.259  1.00 101.70 ? 144  CYS F CB  1 
ATOM   11673 S SG  . CYS F  2 144 ? 26.916  -75.638 48.586  1.00 106.03 ? 144  CYS F SG  1 
ATOM   11674 N N   . ASP F  2 145 ? 23.578  -77.518 50.934  1.00 101.09 ? 145  ASP F N   1 
ATOM   11675 C CA  . ASP F  2 145 ? 22.168  -77.433 51.323  1.00 105.45 ? 145  ASP F CA  1 
ATOM   11676 C C   . ASP F  2 145 ? 21.522  -76.192 50.708  1.00 101.87 ? 145  ASP F C   1 
ATOM   11677 O O   . ASP F  2 145 ? 21.985  -75.693 49.687  1.00 102.23 ? 145  ASP F O   1 
ATOM   11678 C CB  . ASP F  2 145 ? 22.020  -77.434 52.857  1.00 103.98 ? 145  ASP F CB  1 
ATOM   11679 C CG  . ASP F  2 145 ? 22.935  -76.424 53.547  1.00 103.73 ? 145  ASP F CG  1 
ATOM   11680 O OD1 . ASP F  2 145 ? 23.387  -75.468 52.888  1.00 104.15 ? 145  ASP F OD1 1 
ATOM   11681 O OD2 . ASP F  2 145 ? 23.198  -76.585 54.758  1.00 103.81 ? 145  ASP F OD2 1 
ATOM   11682 N N   . ASN F  2 146 ? 20.438  -75.710 51.303  1.00 98.06  ? 146  ASN F N   1 
ATOM   11683 C CA  . ASN F  2 146 ? 19.896  -74.431 50.880  1.00 96.76  ? 146  ASN F CA  1 
ATOM   11684 C C   . ASN F  2 146 ? 20.363  -73.343 51.838  1.00 101.72 ? 146  ASN F C   1 
ATOM   11685 O O   . ASN F  2 146 ? 19.607  -72.431 52.173  1.00 110.69 ? 146  ASN F O   1 
ATOM   11686 C CB  . ASN F  2 146 ? 18.366  -74.472 50.826  1.00 95.08  ? 146  ASN F CB  1 
ATOM   11687 C CG  . ASN F  2 146 ? 17.848  -75.437 49.792  1.00 97.49  ? 146  ASN F CG  1 
ATOM   11688 O OD1 . ASN F  2 146 ? 18.579  -76.302 49.317  1.00 98.86  ? 146  ASN F OD1 1 
ATOM   11689 N ND2 . ASN F  2 146 ? 16.583  -75.283 49.420  1.00 97.84  ? 146  ASN F ND2 1 
ATOM   11690 N N   . GLU F  2 147 ? 21.626  -73.429 52.251  1.00 99.62  ? 147  GLU F N   1 
ATOM   11691 C CA  . GLU F  2 147 ? 22.231  -72.421 53.121  1.00 102.99 ? 147  GLU F CA  1 
ATOM   11692 C C   . GLU F  2 147 ? 23.733  -72.385 52.851  1.00 95.28  ? 147  GLU F C   1 
ATOM   11693 O O   . GLU F  2 147 ? 24.446  -71.479 53.282  1.00 91.57  ? 147  GLU F O   1 
ATOM   11694 C CB  . GLU F  2 147 ? 21.920  -72.727 54.594  1.00 106.24 ? 147  GLU F CB  1 
ATOM   11695 C CG  . GLU F  2 147 ? 22.118  -71.560 55.559  1.00 112.10 ? 147  GLU F CG  1 
ATOM   11696 C CD  . GLU F  2 147 ? 21.686  -71.895 56.982  1.00 118.41 ? 147  GLU F CD  1 
ATOM   11697 O OE1 . GLU F  2 147 ? 21.173  -73.017 57.198  1.00 117.07 ? 147  GLU F OE1 1 
ATOM   11698 O OE2 . GLU F  2 147 ? 21.848  -71.034 57.881  1.00 123.90 ? 147  GLU F OE2 1 
ATOM   11699 N N   . CYS F  2 148 ? 24.195  -73.409 52.141  1.00 97.61  ? 148  CYS F N   1 
ATOM   11700 C CA  . CYS F  2 148 ? 25.529  -73.441 51.563  1.00 98.36  ? 148  CYS F CA  1 
ATOM   11701 C C   . CYS F  2 148 ? 25.460  -72.640 50.248  1.00 98.74  ? 148  CYS F C   1 
ATOM   11702 O O   . CYS F  2 148 ? 26.261  -71.724 50.026  1.00 96.61  ? 148  CYS F O   1 
ATOM   11703 C CB  . CYS F  2 148 ? 25.991  -74.892 51.349  1.00 97.43  ? 148  CYS F CB  1 
ATOM   11704 S SG  . CYS F  2 148 ? 27.557  -75.158 50.468  1.00 104.18 ? 148  CYS F SG  1 
ATOM   11705 N N   . MET F  2 149 ? 24.491  -72.991 49.392  1.00 97.06  ? 149  MET F N   1 
ATOM   11706 C CA  . MET F  2 149 ? 24.193  -72.247 48.161  1.00 92.40  ? 149  MET F CA  1 
ATOM   11707 C C   . MET F  2 149 ? 24.066  -70.755 48.433  1.00 90.31  ? 149  MET F C   1 
ATOM   11708 O O   . MET F  2 149 ? 24.509  -69.921 47.641  1.00 82.47  ? 149  MET F O   1 
ATOM   11709 C CB  . MET F  2 149 ? 22.888  -72.734 47.530  1.00 90.66  ? 149  MET F CB  1 
ATOM   11710 C CG  . MET F  2 149 ? 22.845  -74.195 47.195  1.00 91.16  ? 149  MET F CG  1 
ATOM   11711 S SD  . MET F  2 149 ? 24.044  -74.693 45.953  1.00 103.41 ? 149  MET F SD  1 
ATOM   11712 C CE  . MET F  2 149 ? 23.309  -76.243 45.434  1.00 99.43  ? 149  MET F CE  1 
ATOM   11713 N N   . GLU F  2 150 ? 23.429  -70.443 49.559  1.00 91.68  ? 150  GLU F N   1 
ATOM   11714 C CA  . GLU F  2 150 ? 23.232  -69.073 49.994  1.00 90.77  ? 150  GLU F CA  1 
ATOM   11715 C C   . GLU F  2 150 ? 24.551  -68.393 50.373  1.00 90.20  ? 150  GLU F C   1 
ATOM   11716 O O   . GLU F  2 150 ? 24.718  -67.189 50.156  1.00 90.44  ? 150  GLU F O   1 
ATOM   11717 C CB  . GLU F  2 150 ? 22.257  -69.023 51.170  1.00 89.72  ? 150  GLU F CB  1 
ATOM   11718 C CG  . GLU F  2 150 ? 21.922  -67.612 51.611  1.00 88.94  ? 150  GLU F CG  1 
ATOM   11719 C CD  . GLU F  2 150 ? 21.248  -66.796 50.520  1.00 90.74  ? 150  GLU F CD  1 
ATOM   11720 O OE1 . GLU F  2 150 ? 20.715  -67.391 49.558  1.00 91.65  ? 150  GLU F OE1 1 
ATOM   11721 O OE2 . GLU F  2 150 ? 21.282  -65.552 50.611  1.00 91.38  ? 150  GLU F OE2 1 
ATOM   11722 N N   . SER F  2 151 ? 25.482  -69.150 50.946  1.00 87.55  ? 151  SER F N   1 
ATOM   11723 C CA  . SER F  2 151 ? 26.749  -68.559 51.370  1.00 90.02  ? 151  SER F CA  1 
ATOM   11724 C C   . SER F  2 151 ? 27.586  -68.143 50.155  1.00 91.25  ? 151  SER F C   1 
ATOM   11725 O O   . SER F  2 151 ? 28.433  -67.251 50.247  1.00 90.91  ? 151  SER F O   1 
ATOM   11726 C CB  . SER F  2 151 ? 27.548  -69.527 52.247  1.00 86.06  ? 151  SER F CB  1 
ATOM   11727 O OG  . SER F  2 151 ? 28.284  -70.447 51.461  1.00 84.87  ? 151  SER F OG  1 
ATOM   11728 N N   . VAL F  2 152 ? 27.341  -68.793 49.019  1.00 87.67  ? 152  VAL F N   1 
ATOM   11729 C CA  . VAL F  2 152 ? 28.049  -68.480 47.781  1.00 88.28  ? 152  VAL F CA  1 
ATOM   11730 C C   . VAL F  2 152 ? 27.402  -67.283 47.070  1.00 87.85  ? 152  VAL F C   1 
ATOM   11731 O O   . VAL F  2 152 ? 28.100  -66.466 46.452  1.00 83.74  ? 152  VAL F O   1 
ATOM   11732 C CB  . VAL F  2 152 ? 28.074  -69.685 46.822  1.00 20.00  ? 152  VAL F CB  1 
ATOM   11733 C CG1 . VAL F  2 152 ? 28.704  -69.295 45.494  1.00 20.00  ? 152  VAL F CG1 1 
ATOM   11734 C CG2 . VAL F  2 152 ? 28.821  -70.851 47.452  1.00 20.00  ? 152  VAL F CG2 1 
ATOM   11735 N N   . ARG F  2 153 ? 26.075  -67.170 47.189  1.00 88.25  ? 153  ARG F N   1 
ATOM   11736 C CA  . ARG F  2 153 ? 25.327  -66.088 46.544  1.00 86.30  ? 153  ARG F CA  1 
ATOM   11737 C C   . ARG F  2 153 ? 25.572  -64.732 47.208  1.00 88.35  ? 153  ARG F C   1 
ATOM   11738 O O   . ARG F  2 153 ? 25.473  -63.686 46.548  1.00 84.25  ? 153  ARG F O   1 
ATOM   11739 C CB  . ARG F  2 153 ? 23.822  -66.379 46.558  1.00 79.69  ? 153  ARG F CB  1 
ATOM   11740 C CG  . ARG F  2 153 ? 23.392  -67.471 45.607  1.00 80.73  ? 153  ARG F CG  1 
ATOM   11741 C CD  . ARG F  2 153 ? 21.882  -67.646 45.611  1.00 80.00  ? 153  ARG F CD  1 
ATOM   11742 N NE  . ARG F  2 153 ? 21.401  -68.309 46.816  1.00 86.57  ? 153  ARG F NE  1 
ATOM   11743 C CZ  . ARG F  2 153 ? 20.398  -69.179 46.831  1.00 92.43  ? 153  ARG F CZ  1 
ATOM   11744 N NH1 . ARG F  2 153 ? 19.776  -69.494 45.700  1.00 94.24  ? 153  ARG F NH1 1 
ATOM   11745 N NH2 . ARG F  2 153 ? 20.021  -69.740 47.974  1.00 95.45  ? 153  ARG F NH2 1 
ATOM   11746 N N   . ASN F  2 154 ? 25.906  -64.744 48.500  1.00 87.97  ? 154  ASN F N   1 
ATOM   11747 C CA  . ASN F  2 154 ? 26.273  -63.506 49.183  1.00 85.40  ? 154  ASN F CA  1 
ATOM   11748 C C   . ASN F  2 154 ? 27.763  -63.419 49.504  1.00 84.86  ? 154  ASN F C   1 
ATOM   11749 O O   . ASN F  2 154 ? 28.199  -62.498 50.190  1.00 89.51  ? 154  ASN F O   1 
ATOM   11750 C CB  . ASN F  2 154 ? 25.430  -63.304 50.460  1.00 82.58  ? 154  ASN F CB  1 
ATOM   11751 C CG  . ASN F  2 154 ? 25.460  -64.496 51.405  1.00 89.16  ? 154  ASN F CG  1 
ATOM   11752 O OD1 . ASN F  2 154 ? 26.511  -64.865 51.930  1.00 93.12  ? 154  ASN F OD1 1 
ATOM   11753 N ND2 . ASN F  2 154 ? 24.287  -65.067 51.672  1.00 87.49  ? 154  ASN F ND2 1 
ATOM   11754 N N   . GLY F  2 155 ? 28.543  -64.356 48.969  1.00 83.89  ? 155  GLY F N   1 
ATOM   11755 C CA  . GLY F  2 155 ? 29.992  -64.346 49.117  1.00 85.00  ? 155  GLY F CA  1 
ATOM   11756 C C   . GLY F  2 155 ? 30.540  -64.479 50.533  1.00 88.89  ? 155  GLY F C   1 
ATOM   11757 O O   . GLY F  2 155 ? 31.419  -63.717 50.940  1.00 86.59  ? 155  GLY F O   1 
ATOM   11758 N N   . THR F  2 156 ? 30.049  -65.477 51.267  1.00 92.74  ? 156  THR F N   1 
ATOM   11759 C CA  . THR F  2 156 ? 30.478  -65.741 52.642  1.00 90.89  ? 156  THR F CA  1 
ATOM   11760 C C   . THR F  2 156 ? 31.014  -67.172 52.763  1.00 94.01  ? 156  THR F C   1 
ATOM   11761 O O   . THR F  2 156 ? 31.469  -67.580 53.836  1.00 94.32  ? 156  THR F O   1 
ATOM   11762 C CB  . THR F  2 156 ? 29.340  -65.535 53.654  1.00 84.49  ? 156  THR F CB  1 
ATOM   11763 O OG1 . THR F  2 156 ? 28.151  -66.167 53.174  1.00 89.43  ? 156  THR F OG1 1 
ATOM   11764 C CG2 . THR F  2 156 ? 29.077  -64.061 53.865  1.00 80.73  ? 156  THR F CG2 1 
ATOM   11765 N N   . TYR F  2 157 ? 30.873  -67.940 51.679  1.00 92.69  ? 157  TYR F N   1 
ATOM   11766 C CA  . TYR F  2 157 ? 31.369  -69.320 51.574  1.00 93.75  ? 157  TYR F CA  1 
ATOM   11767 C C   . TYR F  2 157 ? 32.736  -69.579 52.226  1.00 98.62  ? 157  TYR F C   1 
ATOM   11768 O O   . TYR F  2 157 ? 33.777  -69.130 51.726  1.00 94.82  ? 157  TYR F O   1 
ATOM   11769 C CB  . TYR F  2 157 ? 31.437  -69.739 50.102  1.00 93.16  ? 157  TYR F CB  1 
ATOM   11770 C CG  . TYR F  2 157 ? 32.034  -71.117 49.879  1.00 94.21  ? 157  TYR F CG  1 
ATOM   11771 C CD1 . TYR F  2 157 ? 31.311  -72.275 50.170  1.00 93.57  ? 157  TYR F CD1 1 
ATOM   11772 C CD2 . TYR F  2 157 ? 33.328  -71.258 49.375  1.00 92.04  ? 157  TYR F CD2 1 
ATOM   11773 C CE1 . TYR F  2 157 ? 31.866  -73.538 49.964  1.00 89.18  ? 157  TYR F CE1 1 
ATOM   11774 C CE2 . TYR F  2 157 ? 33.889  -72.511 49.170  1.00 88.97  ? 157  TYR F CE2 1 
ATOM   11775 C CZ  . TYR F  2 157 ? 33.154  -73.645 49.464  1.00 86.48  ? 157  TYR F CZ  1 
ATOM   11776 O OH  . TYR F  2 157 ? 33.718  -74.883 49.248  1.00 89.28  ? 157  TYR F OH  1 
ATOM   11777 N N   . ASP F  2 158 ? 32.715  -70.334 53.323  1.00 99.72  ? 158  ASP F N   1 
ATOM   11778 C CA  . ASP F  2 158 ? 33.916  -70.685 54.084  1.00 100.28 ? 158  ASP F CA  1 
ATOM   11779 C C   . ASP F  2 158 ? 34.685  -71.852 53.444  1.00 96.94  ? 158  ASP F C   1 
ATOM   11780 O O   . ASP F  2 158 ? 34.233  -72.993 53.495  1.00 94.61  ? 158  ASP F O   1 
ATOM   11781 C CB  . ASP F  2 158 ? 33.514  -71.033 55.527  1.00 98.01  ? 158  ASP F CB  1 
ATOM   11782 C CG  . ASP F  2 158 ? 34.681  -71.002 56.490  1.00 97.32  ? 158  ASP F CG  1 
ATOM   11783 O OD1 . ASP F  2 158 ? 35.835  -71.112 56.034  1.00 96.94  ? 158  ASP F OD1 1 
ATOM   11784 O OD2 . ASP F  2 158 ? 34.446  -70.855 57.708  1.00 96.77  ? 158  ASP F OD2 1 
ATOM   11785 N N   . TYR F  2 159 ? 35.846  -71.565 52.849  1.00 96.72  ? 159  TYR F N   1 
ATOM   11786 C CA  . TYR F  2 159 ? 36.598  -72.578 52.088  1.00 97.91  ? 159  TYR F CA  1 
ATOM   11787 C C   . TYR F  2 159 ? 37.180  -73.748 52.923  1.00 101.93 ? 159  TYR F C   1 
ATOM   11788 O O   . TYR F  2 159 ? 36.913  -74.913 52.593  1.00 99.80  ? 159  TYR F O   1 
ATOM   11789 C CB  . TYR F  2 159 ? 37.726  -71.915 51.278  1.00 95.04  ? 159  TYR F CB  1 
ATOM   11790 C CG  . TYR F  2 159 ? 38.762  -72.889 50.728  1.00 96.47  ? 159  TYR F CG  1 
ATOM   11791 C CD1 . TYR F  2 159 ? 38.466  -73.725 49.653  1.00 93.87  ? 159  TYR F CD1 1 
ATOM   11792 C CD2 . TYR F  2 159 ? 40.044  -72.960 51.278  1.00 97.30  ? 159  TYR F CD2 1 
ATOM   11793 C CE1 . TYR F  2 159 ? 39.416  -74.611 49.151  1.00 95.58  ? 159  TYR F CE1 1 
ATOM   11794 C CE2 . TYR F  2 159 ? 40.998  -73.841 50.782  1.00 94.06  ? 159  TYR F CE2 1 
ATOM   11795 C CZ  . TYR F  2 159 ? 40.677  -74.663 49.721  1.00 95.05  ? 159  TYR F CZ  1 
ATOM   11796 O OH  . TYR F  2 159 ? 41.619  -75.537 49.222  1.00 93.60  ? 159  TYR F OH  1 
ATOM   11797 N N   . PRO F  2 160 ? 37.982  -73.462 53.983  1.00 100.65 ? 160  PRO F N   1 
ATOM   11798 C CA  . PRO F  2 160 ? 38.605  -74.581 54.715  1.00 96.69  ? 160  PRO F CA  1 
ATOM   11799 C C   . PRO F  2 160 ? 37.586  -75.495 55.396  1.00 93.27  ? 160  PRO F C   1 
ATOM   11800 O O   . PRO F  2 160 ? 37.919  -76.626 55.742  1.00 90.86  ? 160  PRO F O   1 
ATOM   11801 C CB  . PRO F  2 160 ? 39.490  -73.879 55.751  1.00 99.65  ? 160  PRO F CB  1 
ATOM   11802 C CG  . PRO F  2 160 ? 38.882  -72.540 55.927  1.00 100.03 ? 160  PRO F CG  1 
ATOM   11803 C CD  . PRO F  2 160 ? 38.363  -72.163 54.570  1.00 98.43  ? 160  PRO F CD  1 
ATOM   11804 N N   . GLN F  2 161 ? 36.366  -74.991 55.581  1.00 94.73  ? 161  GLN F N   1 
ATOM   11805 C CA  . GLN F  2 161 ? 35.278  -75.734 56.203  1.00 91.45  ? 161  GLN F CA  1 
ATOM   11806 C C   . GLN F  2 161 ? 34.821  -76.903 55.324  1.00 92.19  ? 161  GLN F C   1 
ATOM   11807 O O   . GLN F  2 161 ? 34.053  -77.757 55.763  1.00 90.89  ? 161  GLN F O   1 
ATOM   11808 C CB  . GLN F  2 161 ? 34.088  -74.801 56.461  1.00 90.76  ? 161  GLN F CB  1 
ATOM   11809 C CG  . GLN F  2 161 ? 32.924  -75.427 57.229  1.00 91.35  ? 161  GLN F CG  1 
ATOM   11810 C CD  . GLN F  2 161 ? 31.748  -74.481 57.391  1.00 96.06  ? 161  GLN F CD  1 
ATOM   11811 O OE1 . GLN F  2 161 ? 31.879  -73.267 57.217  1.00 98.11  ? 161  GLN F OE1 1 
ATOM   11812 N NE2 . GLN F  2 161 ? 30.579  -75.040 57.687  1.00 92.71  ? 161  GLN F NE2 1 
ATOM   11813 N N   . TYR F  2 162 ? 35.302  -76.954 54.084  1.00 94.48  ? 162  TYR F N   1 
ATOM   11814 C CA  . TYR F  2 162 ? 34.884  -78.012 53.172  1.00 94.04  ? 162  TYR F CA  1 
ATOM   11815 C C   . TYR F  2 162 ? 36.094  -78.601 52.450  1.00 91.64  ? 162  TYR F C   1 
ATOM   11816 O O   . TYR F  2 162 ? 35.955  -79.517 51.632  1.00 89.43  ? 162  TYR F O   1 
ATOM   11817 C CB  . TYR F  2 162 ? 33.883  -77.465 52.145  1.00 94.15  ? 162  TYR F CB  1 
ATOM   11818 C CG  . TYR F  2 162 ? 32.645  -76.813 52.738  1.00 95.16  ? 162  TYR F CG  1 
ATOM   11819 C CD1 . TYR F  2 162 ? 31.534  -77.564 53.123  1.00 97.77  ? 162  TYR F CD1 1 
ATOM   11820 C CD2 . TYR F  2 162 ? 32.585  -75.430 52.894  1.00 93.92  ? 162  TYR F CD2 1 
ATOM   11821 C CE1 . TYR F  2 162 ? 30.401  -76.945 53.663  1.00 98.27  ? 162  TYR F CE1 1 
ATOM   11822 C CE2 . TYR F  2 162 ? 31.467  -74.806 53.427  1.00 95.56  ? 162  TYR F CE2 1 
ATOM   11823 C CZ  . TYR F  2 162 ? 30.382  -75.564 53.809  1.00 98.65  ? 162  TYR F CZ  1 
ATOM   11824 O OH  . TYR F  2 162 ? 29.282  -74.929 54.337  1.00 100.13 ? 162  TYR F OH  1 
ATOM   11825 N N   . SER F  2 163 ? 37.278  -78.085 52.782  1.00 88.54  ? 163  SER F N   1 
ATOM   11826 C CA  . SER F  2 163 ? 38.526  -78.447 52.103  1.00 92.84  ? 163  SER F CA  1 
ATOM   11827 C C   . SER F  2 163 ? 38.854  -79.943 52.258  1.00 95.44  ? 163  SER F C   1 
ATOM   11828 O O   . SER F  2 163 ? 39.388  -80.587 51.348  1.00 93.82  ? 163  SER F O   1 
ATOM   11829 C CB  . SER F  2 163 ? 39.675  -77.578 52.649  1.00 92.97  ? 163  SER F CB  1 
ATOM   11830 O OG  . SER F  2 163 ? 40.749  -77.449 51.729  1.00 92.74  ? 163  SER F OG  1 
ATOM   11831 N N   . GLU F  2 164 ? 38.523  -80.476 53.428  1.00 97.63  ? 164  GLU F N   1 
ATOM   11832 C CA  . GLU F  2 164 ? 38.808  -81.857 53.788  1.00 93.03  ? 164  GLU F CA  1 
ATOM   11833 C C   . GLU F  2 164 ? 37.828  -82.839 53.132  1.00 94.20  ? 164  GLU F C   1 
ATOM   11834 O O   . GLU F  2 164 ? 38.253  -83.778 52.456  1.00 97.33  ? 164  GLU F O   1 
ATOM   11835 C CB  . GLU F  2 164 ? 38.810  -82.011 55.320  1.00 94.87  ? 164  GLU F CB  1 
ATOM   11836 C CG  . GLU F  2 164 ? 37.508  -81.617 56.034  1.00 95.56  ? 164  GLU F CG  1 
ATOM   11837 C CD  . GLU F  2 164 ? 37.208  -80.120 55.952  1.00 95.00  ? 164  GLU F CD  1 
ATOM   11838 O OE1 . GLU F  2 164 ? 38.165  -79.326 55.805  1.00 96.38  ? 164  GLU F OE1 1 
ATOM   11839 O OE2 . GLU F  2 164 ? 36.019  -79.742 56.014  1.00 91.41  ? 164  GLU F OE2 1 
ATOM   11840 N N   . GLU F  2 165 ? 36.527  -82.618 53.331  1.00 89.81  ? 165  GLU F N   1 
ATOM   11841 C CA  . GLU F  2 165 ? 35.490  -83.472 52.756  1.00 90.58  ? 165  GLU F CA  1 
ATOM   11842 C C   . GLU F  2 165 ? 35.654  -83.580 51.245  1.00 95.07  ? 165  GLU F C   1 
ATOM   11843 O O   . GLU F  2 165 ? 35.490  -84.656 50.662  1.00 94.42  ? 165  GLU F O   1 
ATOM   11844 C CB  . GLU F  2 165 ? 34.091  -82.933 53.106  1.00 89.99  ? 165  GLU F CB  1 
ATOM   11845 C CG  . GLU F  2 165 ? 32.919  -83.710 52.465  1.00 89.50  ? 165  GLU F CG  1 
ATOM   11846 C CD  . GLU F  2 165 ? 31.542  -83.159 52.843  1.00 89.63  ? 165  GLU F CD  1 
ATOM   11847 O OE1 . GLU F  2 165 ? 31.481  -82.201 53.649  1.00 87.34  ? 165  GLU F OE1 1 
ATOM   11848 O OE2 . GLU F  2 165 ? 30.525  -83.687 52.333  1.00 87.70  ? 165  GLU F OE2 1 
ATOM   11849 N N   . ALA F  2 166 ? 35.972  -82.445 50.629  1.00 92.10  ? 166  ALA F N   1 
ATOM   11850 C CA  . ALA F  2 166 ? 36.217  -82.352 49.196  1.00 96.21  ? 166  ALA F CA  1 
ATOM   11851 C C   . ALA F  2 166 ? 37.490  -83.066 48.708  1.00 103.55 ? 166  ALA F C   1 
ATOM   11852 O O   . ALA F  2 166 ? 37.439  -83.827 47.728  1.00 101.41 ? 166  ALA F O   1 
ATOM   11853 C CB  . ALA F  2 166 ? 36.261  -80.886 48.788  1.00 95.01  ? 166  ALA F CB  1 
ATOM   11854 N N   . ARG F  2 167 ? 38.618  -82.815 49.384  1.00 101.83 ? 167  ARG F N   1 
ATOM   11855 C CA  . ARG F  2 167 ? 39.921  -83.354 48.969  1.00 100.45 ? 167  ARG F CA  1 
ATOM   11856 C C   . ARG F  2 167 ? 39.897  -84.881 48.856  1.00 108.46 ? 167  ARG F C   1 
ATOM   11857 O O   . ARG F  2 167 ? 40.467  -85.458 47.921  1.00 108.87 ? 167  ARG F O   1 
ATOM   11858 C CB  . ARG F  2 167 ? 41.029  -82.921 49.935  1.00 97.88  ? 167  ARG F CB  1 
ATOM   11859 C CG  . ARG F  2 167 ? 42.417  -83.371 49.490  1.00 103.75 ? 167  ARG F CG  1 
ATOM   11860 C CD  . ARG F  2 167 ? 43.540  -82.905 50.418  1.00 109.95 ? 167  ARG F CD  1 
ATOM   11861 N NE  . ARG F  2 167 ? 43.460  -83.522 51.743  1.00 119.54 ? 167  ARG F NE  1 
ATOM   11862 C CZ  . ARG F  2 167 ? 43.902  -82.962 52.868  1.00 123.34 ? 167  ARG F CZ  1 
ATOM   11863 N NH1 . ARG F  2 167 ? 44.486  -81.769 52.837  1.00 122.48 ? 167  ARG F NH1 1 
ATOM   11864 N NH2 . ARG F  2 167 ? 43.778  -83.605 54.025  1.00 118.71 ? 167  ARG F NH2 1 
ATOM   11865 N N   . LEU F  2 168 ? 39.227  -85.521 49.813  1.00 109.25 ? 168  LEU F N   1 
ATOM   11866 C CA  . LEU F  2 168 ? 39.032  -86.971 49.816  1.00 108.63 ? 168  LEU F CA  1 
ATOM   11867 C C   . LEU F  2 168 ? 38.245  -87.436 48.580  1.00 109.77 ? 168  LEU F C   1 
ATOM   11868 O O   . LEU F  2 168 ? 38.574  -88.464 47.978  1.00 108.77 ? 168  LEU F O   1 
ATOM   11869 C CB  . LEU F  2 168 ? 38.330  -87.424 51.111  1.00 104.78 ? 168  LEU F CB  1 
ATOM   11870 C CG  . LEU F  2 168 ? 39.137  -87.652 52.405  1.00 99.84  ? 168  LEU F CG  1 
ATOM   11871 C CD1 . LEU F  2 168 ? 39.935  -86.431 52.865  1.00 97.23  ? 168  LEU F CD1 1 
ATOM   11872 C CD2 . LEU F  2 168 ? 38.212  -88.117 53.521  1.00 97.87  ? 168  LEU F CD2 1 
ATOM   11873 N N   . LYS F  2 169 ? 37.195  -86.692 48.228  1.00 108.99 ? 169  LYS F N   1 
ATOM   11874 C CA  . LYS F  2 169 ? 36.290  -87.082 47.144  1.00 109.95 ? 169  LYS F CA  1 
ATOM   11875 C C   . LYS F  2 169 ? 36.976  -87.117 45.777  1.00 113.23 ? 169  LYS F C   1 
ATOM   11876 O O   . LYS F  2 169 ? 36.704  -88.010 44.966  1.00 112.54 ? 169  LYS F O   1 
ATOM   11877 C CB  . LYS F  2 169 ? 35.084  -86.138 47.081  1.00 101.17 ? 169  LYS F CB  1 
ATOM   11878 C CG  . LYS F  2 169 ? 34.123  -86.453 45.940  1.00 105.32 ? 169  LYS F CG  1 
ATOM   11879 C CD  . LYS F  2 169 ? 33.510  -87.838 46.071  1.00 111.34 ? 169  LYS F CD  1 
ATOM   11880 C CE  . LYS F  2 169 ? 32.424  -88.064 45.032  1.00 107.64 ? 169  LYS F CE  1 
ATOM   11881 N NZ  . LYS F  2 169 ? 33.013  -88.037 43.662  1.00 106.77 ? 169  LYS F NZ  1 
ATOM   11882 N N   . ARG F  2 170 ? 37.852  -86.150 45.513  1.00 111.73 ? 170  ARG F N   1 
ATOM   11883 C CA  . ARG F  2 170 ? 38.545  -86.106 44.222  1.00 115.57 ? 170  ARG F CA  1 
ATOM   11884 C C   . ARG F  2 170 ? 39.655  -87.164 44.137  1.00 118.07 ? 170  ARG F C   1 
ATOM   11885 O O   . ARG F  2 170 ? 40.080  -87.535 43.043  1.00 120.35 ? 170  ARG F O   1 
ATOM   11886 C CB  . ARG F  2 170 ? 39.112  -84.711 43.919  1.00 108.88 ? 170  ARG F CB  1 
ATOM   11887 C CG  . ARG F  2 170 ? 39.800  -84.009 45.057  1.00 105.77 ? 170  ARG F CG  1 
ATOM   11888 C CD  . ARG F  2 170 ? 39.957  -82.529 44.740  1.00 98.63  ? 170  ARG F CD  1 
ATOM   11889 N NE  . ARG F  2 170 ? 40.613  -81.822 45.832  1.00 98.12  ? 170  ARG F NE  1 
ATOM   11890 C CZ  . ARG F  2 170 ? 41.894  -81.477 45.828  1.00 96.47  ? 170  ARG F CZ  1 
ATOM   11891 N NH1 . ARG F  2 170 ? 42.656  -81.778 44.785  1.00 98.55  ? 170  ARG F NH1 1 
ATOM   11892 N NH2 . ARG F  2 170 ? 42.413  -80.841 46.868  1.00 94.76  ? 170  ARG F NH2 1 
ATOM   11893 N N   . GLU F  2 171 ? 40.146  -87.615 45.287  1.00 117.99 ? 171  GLU F N   1 
ATOM   11894 C CA  . GLU F  2 171 ? 41.095  -88.724 45.333  1.00 115.10 ? 171  GLU F CA  1 
ATOM   11895 C C   . GLU F  2 171 ? 40.444  -90.063 44.968  1.00 116.42 ? 171  GLU F C   1 
ATOM   11896 O O   . GLU F  2 171 ? 41.096  -90.938 44.399  1.00 115.37 ? 171  GLU F O   1 
ATOM   11897 C CB  . GLU F  2 171 ? 41.710  -88.818 46.715  1.00 113.53 ? 171  GLU F CB  1 
ATOM   11898 C CG  . GLU F  2 171 ? 42.575  -87.649 47.086  1.00 110.48 ? 171  GLU F CG  1 
ATOM   11899 C CD  . GLU F  2 171 ? 43.028  -87.757 48.522  1.00 117.56 ? 171  GLU F CD  1 
ATOM   11900 O OE1 . GLU F  2 171 ? 42.488  -88.629 49.247  1.00 113.70 ? 171  GLU F OE1 1 
ATOM   11901 O OE2 . GLU F  2 171 ? 43.924  -86.984 48.924  1.00 120.93 ? 171  GLU F OE2 1 
ATOM   11902 N N   . GLU F  2 172 ? 39.167  -90.226 45.316  1.00 119.72 ? 172  GLU F N   1 
ATOM   11903 C CA  . GLU F  2 172 ? 38.416  -91.421 44.933  1.00 119.06 ? 172  GLU F CA  1 
ATOM   11904 C C   . GLU F  2 172 ? 38.294  -91.466 43.416  1.00 119.58 ? 172  GLU F C   1 
ATOM   11905 O O   . GLU F  2 172 ? 38.300  -92.537 42.807  1.00 123.10 ? 172  GLU F O   1 
ATOM   11906 C CB  . GLU F  2 172 ? 37.006  -91.424 45.545  1.00 116.36 ? 172  GLU F CB  1 
ATOM   11907 C CG  . GLU F  2 172 ? 36.920  -91.353 47.065  1.00 117.75 ? 172  GLU F CG  1 
ATOM   11908 C CD  . GLU F  2 172 ? 35.481  -91.192 47.550  1.00 122.79 ? 172  GLU F CD  1 
ATOM   11909 O OE1 . GLU F  2 172 ? 34.570  -91.163 46.691  1.00 121.14 ? 172  GLU F OE1 1 
ATOM   11910 O OE2 . GLU F  2 172 ? 35.257  -91.101 48.782  1.00 123.35 ? 172  GLU F OE2 1 
ATOM   11911 N N   . ILE F  2 173 ? 38.179  -90.278 42.822  1.00 121.08 ? 173  ILE F N   1 
ATOM   11912 C CA  . ILE F  2 173 ? 38.081  -90.107 41.375  1.00 121.39 ? 173  ILE F CA  1 
ATOM   11913 C C   . ILE F  2 173 ? 39.446  -90.190 40.700  1.00 119.89 ? 173  ILE F C   1 
ATOM   11914 O O   . ILE F  2 173 ? 39.588  -90.761 39.615  1.00 118.59 ? 173  ILE F O   1 
ATOM   11915 C CB  . ILE F  2 173 ? 37.460  -88.720 41.034  1.00 120.24 ? 173  ILE F CB  1 
ATOM   11916 C CG1 . ILE F  2 173 ? 36.055  -88.575 41.632  1.00 121.07 ? 173  ILE F CG1 1 
ATOM   11917 C CG2 . ILE F  2 173 ? 37.515  -88.440 39.523  1.00 121.30 ? 173  ILE F CG2 1 
ATOM   11918 C CD1 . ILE F  2 173 ? 35.511  -87.153 41.588  1.00 114.76 ? 173  ILE F CD1 1 
ATOM   11919 N N   . SER F  2 174 ? 40.449  -89.628 41.373  1.00 120.60 ? 174  SER F N   1 
ATOM   11920 C CA  . SER F  2 174 ? 41.818  -89.575 40.868  1.00 119.70 ? 174  SER F CA  1 
ATOM   11921 C C   . SER F  2 174 ? 42.664  -90.753 41.372  1.00 120.22 ? 174  SER F C   1 
ATOM   11922 O O   . SER F  2 174 ? 43.866  -90.611 41.600  1.00 119.75 ? 174  SER F O   1 
ATOM   11923 C CB  . SER F  2 174 ? 42.459  -88.232 41.254  1.00 116.40 ? 174  SER F CB  1 
ATOM   11924 O OG  . SER F  2 174 ? 43.679  -88.002 40.573  1.00 110.97 ? 174  SER F OG  1 
ATOM   11925 N N   . GLY F  2 175 ? 42.036  -91.911 41.552  1.00 121.61 ? 175  GLY F N   1 
ATOM   11926 C CA  . GLY F  2 175 ? 42.747  -93.089 42.019  1.00 121.71 ? 175  GLY F CA  1 
ATOM   11927 C C   . GLY F  2 175 ? 42.454  -94.316 41.180  1.00 122.60 ? 175  GLY F C   1 
ATOM   11928 O O   . GLY F  2 175 ? 42.149  -94.205 39.992  1.00 121.53 ? 175  GLY F O   1 
HETATM 11929 C C1  . NAG G  3 .   ? 28.532  -34.119 42.402  1.00 87.48  ? 1001 NAG C C1  1 
HETATM 11930 C C2  . NAG G  3 .   ? 27.063  -33.980 42.819  1.00 86.77  ? 1001 NAG C C2  1 
HETATM 11931 C C3  . NAG G  3 .   ? 26.701  -32.509 43.030  1.00 88.13  ? 1001 NAG C C3  1 
HETATM 11932 C C4  . NAG G  3 .   ? 27.673  -31.856 44.003  1.00 92.00  ? 1001 NAG C C4  1 
HETATM 11933 C C5  . NAG G  3 .   ? 29.110  -32.056 43.518  1.00 90.13  ? 1001 NAG C C5  1 
HETATM 11934 C C6  . NAG G  3 .   ? 30.156  -31.513 44.471  1.00 92.17  ? 1001 NAG C C6  1 
HETATM 11935 C C7  . NAG G  3 .   ? 25.363  -35.607 42.147  1.00 90.07  ? 1001 NAG C C7  1 
HETATM 11936 C C8  . NAG G  3 .   ? 24.515  -36.126 41.025  1.00 91.85  ? 1001 NAG C C8  1 
HETATM 11937 N N2  . NAG G  3 .   ? 26.179  -34.592 41.845  1.00 83.84  ? 1001 NAG C N2  1 
HETATM 11938 O O3  . NAG G  3 .   ? 25.370  -32.414 43.534  1.00 86.63  ? 1001 NAG C O3  1 
HETATM 11939 O O4  . NAG G  3 .   ? 27.383  -30.468 44.130  1.00 94.12  ? 1001 NAG C O4  1 
HETATM 11940 O O5  . NAG G  3 .   ? 29.379  -33.461 43.368  1.00 88.98  ? 1001 NAG C O5  1 
HETATM 11941 O O6  . NAG G  3 .   ? 29.633  -30.539 45.366  1.00 90.74  ? 1001 NAG C O6  1 
HETATM 11942 O O7  . NAG G  3 .   ? 25.312  -36.086 43.280  1.00 92.28  ? 1001 NAG C O7  1 
HETATM 11943 C C1  . NAG H  3 .   ? 45.568  12.626  -10.156 1.00 57.23  ? 1002 NAG C C1  1 
HETATM 11944 C C2  . NAG H  3 .   ? 45.021  12.247  -11.536 1.00 61.23  ? 1002 NAG C C2  1 
HETATM 11945 C C3  . NAG H  3 .   ? 46.071  11.514  -12.377 1.00 64.81  ? 1002 NAG C C3  1 
HETATM 11946 C C4  . NAG H  3 .   ? 47.475  12.099  -12.239 1.00 70.40  ? 1002 NAG C C4  1 
HETATM 11947 C C5  . NAG H  3 .   ? 47.804  12.589  -10.824 1.00 65.49  ? 1002 NAG C C5  1 
HETATM 11948 C C6  . NAG H  3 .   ? 49.055  13.444  -10.751 1.00 67.17  ? 1002 NAG C C6  1 
HETATM 11949 C C7  . NAG H  3 .   ? 42.646  11.754  -11.951 1.00 56.71  ? 1002 NAG C C7  1 
HETATM 11950 C C8  . NAG H  3 .   ? 41.539  10.767  -11.744 1.00 50.27  ? 1002 NAG C C8  1 
HETATM 11951 N N2  . NAG H  3 .   ? 43.825  11.422  -11.418 1.00 55.43  ? 1002 NAG C N2  1 
HETATM 11952 O O3  . NAG H  3 .   ? 45.683  11.697  -13.731 1.00 71.83  ? 1002 NAG C O3  1 
HETATM 11953 O O4  . NAG H  3 .   ? 48.388  11.072  -12.615 1.00 75.10  ? 1002 NAG C O4  1 
HETATM 11954 O O5  . NAG H  3 .   ? 46.730  13.383  -10.311 1.00 56.13  ? 1002 NAG C O5  1 
HETATM 11955 O O6  . NAG H  3 .   ? 49.209  14.320  -11.863 1.00 64.85  ? 1002 NAG C O6  1 
HETATM 11956 O O7  . NAG H  3 .   ? 42.472  12.813  -12.554 1.00 57.75  ? 1002 NAG C O7  1 
HETATM 11957 C C1  . FUL I  4 .   ? 45.670  10.549  -14.591 1.00 75.45  ? 1003 FUL C C1  1 
HETATM 11958 C C2  . FUL I  4 .   ? 44.322  10.548  -15.420 1.00 79.63  ? 1003 FUL C C2  1 
HETATM 11959 O O2  . FUL I  4 .   ? 44.030  11.799  -16.090 1.00 76.66  ? 1003 FUL C O2  1 
HETATM 11960 C C3  . FUL I  4 .   ? 44.330  9.360   -16.391 1.00 80.75  ? 1003 FUL C C3  1 
HETATM 11961 O O3  . FUL I  4 .   ? 43.154  9.308   -17.212 1.00 77.62  ? 1003 FUL C O3  1 
HETATM 11962 C C4  . FUL I  4 .   ? 44.385  8.118   -15.525 1.00 86.78  ? 1003 FUL C C4  1 
HETATM 11963 O O4  . FUL I  4 .   ? 43.306  8.167   -14.539 1.00 76.70  ? 1003 FUL C O4  1 
HETATM 11964 C C5  . FUL I  4 .   ? 45.785  8.114   -14.844 1.00 83.88  ? 1003 FUL C C5  1 
HETATM 11965 C C6  . FUL I  4 .   ? 46.104  6.832   -14.049 1.00 79.45  ? 1003 FUL C C6  1 
HETATM 11966 O O5  . FUL I  4 .   ? 45.978  9.308   -13.972 1.00 72.31  ? 1003 FUL C O5  1 
HETATM 11967 C C1  . NAG J  3 .   ? 49.310  11.542  -13.616 1.00 82.09  ? 1004 NAG C C1  1 
HETATM 11968 C C2  . NAG J  3 .   ? 50.037  10.337  -14.231 1.00 85.11  ? 1004 NAG C C2  1 
HETATM 11969 C C3  . NAG J  3 .   ? 49.726  10.214  -15.723 1.00 87.61  ? 1004 NAG C C3  1 
HETATM 11970 C C4  . NAG J  3 .   ? 50.083  11.498  -16.472 1.00 78.82  ? 1004 NAG C C4  1 
HETATM 11971 C C5  . NAG J  3 .   ? 49.655  12.728  -15.679 1.00 77.62  ? 1004 NAG C C5  1 
HETATM 11972 C C6  . NAG J  3 .   ? 48.975  13.768  -16.534 1.00 74.79  ? 1004 NAG C C6  1 
HETATM 11973 C C7  . NAG J  3 .   ? 52.074  9.839   -12.948 1.00 87.63  ? 1004 NAG C C7  1 
HETATM 11974 C C8  . NAG J  3 .   ? 53.563  9.996   -12.877 1.00 85.86  ? 1004 NAG C C8  1 
HETATM 11975 N N2  . NAG J  3 .   ? 51.476  10.405  -14.003 1.00 86.57  ? 1004 NAG C N2  1 
HETATM 11976 O O3  . NAG J  3 .   ? 48.353  9.870   -15.894 1.00 87.26  ? 1004 NAG C O3  1 
HETATM 11977 O O4  . NAG J  3 .   ? 51.485  11.569  -16.713 1.00 76.91  ? 1004 NAG C O4  1 
HETATM 11978 O O5  . NAG J  3 .   ? 48.715  12.340  -14.670 1.00 79.02  ? 1004 NAG C O5  1 
HETATM 11979 O O6  . NAG J  3 .   ? 48.440  13.185  -17.713 1.00 75.42  ? 1004 NAG C O6  1 
HETATM 11980 O O7  . NAG J  3 .   ? 51.440  9.227   -12.085 1.00 81.17  ? 1004 NAG C O7  1 
HETATM 11981 C C1  . SIA K  5 .   ? 21.722  26.473  17.360  1.00 73.71  ? 1005 SIA C C1  1 
HETATM 11982 C C2  . SIA K  5 .   ? 21.081  27.528  16.443  1.00 79.53  ? 1005 SIA C C2  1 
HETATM 11983 C C3  . SIA K  5 .   ? 22.011  28.753  16.327  1.00 78.82  ? 1005 SIA C C3  1 
HETATM 11984 C C4  . SIA K  5 .   ? 23.195  28.594  15.371  1.00 76.70  ? 1005 SIA C C4  1 
HETATM 11985 C C5  . SIA K  5 .   ? 22.706  28.161  14.000  1.00 68.24  ? 1005 SIA C C5  1 
HETATM 11986 C C6  . SIA K  5 .   ? 21.818  26.915  14.093  1.00 68.91  ? 1005 SIA C C6  1 
HETATM 11987 C C7  . SIA K  5 .   ? 21.096  26.649  12.764  1.00 66.27  ? 1005 SIA C C7  1 
HETATM 11988 C C8  . SIA K  5 .   ? 20.007  25.577  12.901  1.00 63.76  ? 1005 SIA C C8  1 
HETATM 11989 C C9  . SIA K  5 .   ? 19.707  24.934  11.549  1.00 59.58  ? 1005 SIA C C9  1 
HETATM 11990 C C10 . SIA K  5 .   ? 23.933  28.369  11.907  1.00 63.35  ? 1005 SIA C C10 1 
HETATM 11991 C C11 . SIA K  5 .   ? 25.154  27.984  11.112  1.00 50.48  ? 1005 SIA C C11 1 
HETATM 11992 N N5  . SIA K  5 .   ? 23.845  27.875  13.144  1.00 61.39  ? 1005 SIA C N5  1 
HETATM 11993 O O1A . SIA K  5 .   ? 21.647  25.247  17.059  1.00 71.52  ? 1005 SIA C O1A 1 
HETATM 11994 O O1B . SIA K  5 .   ? 22.314  26.842  18.408  1.00 71.36  ? 1005 SIA C O1B 1 
HETATM 11995 O O4  . SIA K  5 .   ? 23.929  29.827  15.249  1.00 77.56  ? 1005 SIA C O4  1 
HETATM 11996 O O6  . SIA K  5 .   ? 20.849  26.890  15.170  1.00 76.21  ? 1005 SIA C O6  1 
HETATM 11997 O O7  . SIA K  5 .   ? 20.538  27.868  12.236  1.00 68.64  ? 1005 SIA C O7  1 
HETATM 11998 O O8  . SIA K  5 .   ? 20.417  24.570  13.843  1.00 59.96  ? 1005 SIA C O8  1 
HETATM 11999 O O9  . SIA K  5 .   ? 18.501  24.149  11.592  1.00 61.13  ? 1005 SIA C O9  1 
HETATM 12000 O O10 . SIA K  5 .   ? 23.057  29.098  11.454  1.00 67.84  ? 1005 SIA C O10 1 
HETATM 12001 C C1  . GAL L  6 .   ? 16.300  26.555  17.793  1.00 77.42  ? 1006 GAL C C1  1 
HETATM 12002 C C2  . GAL L  6 .   ? 17.374  27.388  17.038  1.00 80.49  ? 1006 GAL C C2  1 
HETATM 12003 C C3  . GAL L  6 .   ? 18.837  27.036  17.458  1.00 79.64  ? 1006 GAL C C3  1 
HETATM 12004 C C4  . GAL L  6 .   ? 18.978  26.893  19.055  1.00 81.56  ? 1006 GAL C C4  1 
HETATM 12005 C C5  . GAL L  6 .   ? 17.784  26.114  19.654  1.00 81.12  ? 1006 GAL C C5  1 
HETATM 12006 C C6  . GAL L  6 .   ? 17.776  26.051  21.217  1.00 90.04  ? 1006 GAL C C6  1 
HETATM 12007 O O2  . GAL L  6 .   ? 17.260  27.221  15.624  1.00 76.99  ? 1006 GAL C O2  1 
HETATM 12008 O O3  . GAL L  6 .   ? 19.807  28.037  16.957  1.00 83.24  ? 1006 GAL C O3  1 
HETATM 12009 O O4  . GAL L  6 .   ? 19.174  28.158  19.736  1.00 82.99  ? 1006 GAL C O4  1 
HETATM 12010 O O5  . GAL L  6 .   ? 16.495  26.652  19.202  1.00 79.58  ? 1006 GAL C O5  1 
HETATM 12011 O O6  . GAL L  6 .   ? 16.705  25.246  21.763  1.00 87.47  ? 1006 GAL C O6  1 
HETATM 12012 C C1  . NAG M  3 .   ? 54.334  -41.555 11.132  1.00 105.95 ? 1001 NAG A C1  1 
HETATM 12013 C C2  . NAG M  3 .   ? 55.389  -40.543 11.634  1.00 105.66 ? 1001 NAG A C2  1 
HETATM 12014 C C3  . NAG M  3 .   ? 55.667  -39.484 10.556  1.00 107.07 ? 1001 NAG A C3  1 
HETATM 12015 C C4  . NAG M  3 .   ? 56.046  -40.156 9.241   1.00 105.37 ? 1001 NAG A C4  1 
HETATM 12016 C C5  . NAG M  3 .   ? 54.940  -41.125 8.824   1.00 105.28 ? 1001 NAG A C5  1 
HETATM 12017 C C6  . NAG M  3 .   ? 55.217  -41.847 7.518   1.00 98.54  ? 1001 NAG A C6  1 
HETATM 12018 C C7  . NAG M  3 .   ? 55.730  -39.138 13.641  1.00 101.03 ? 1001 NAG A C7  1 
HETATM 12019 C C8  . NAG M  3 .   ? 55.096  -38.608 14.893  1.00 99.39  ? 1001 NAG A C8  1 
HETATM 12020 N N2  . NAG M  3 .   ? 54.955  -39.923 12.880  1.00 101.71 ? 1001 NAG A N2  1 
HETATM 12021 O O3  . NAG M  3 .   ? 56.707  -38.598 10.964  1.00 107.84 ? 1001 NAG A O3  1 
HETATM 12022 O O4  . NAG M  3 .   ? 56.248  -39.180 8.224   1.00 106.18 ? 1001 NAG A O4  1 
HETATM 12023 O O5  . NAG M  3 .   ? 54.760  -42.119 9.847   1.00 103.96 ? 1001 NAG A O5  1 
HETATM 12024 O O6  . NAG M  3 .   ? 56.245  -42.823 7.621   1.00 90.74  ? 1001 NAG A O6  1 
HETATM 12025 O O7  . NAG M  3 .   ? 56.885  -38.857 13.328  1.00 99.35  ? 1001 NAG A O7  1 
HETATM 12026 C C1  . NAG N  3 .   ? -1.633  -9.806  -22.777 1.00 60.43  ? 1002 NAG A C1  1 
HETATM 12027 C C2  . NAG N  3 .   ? -2.642  -9.033  -21.911 1.00 65.68  ? 1002 NAG A C2  1 
HETATM 12028 C C3  . NAG N  3 .   ? -3.794  -9.942  -21.441 1.00 71.52  ? 1002 NAG A C3  1 
HETATM 12029 C C4  . NAG N  3 .   ? -4.356  -10.810 -22.565 1.00 74.83  ? 1002 NAG A C4  1 
HETATM 12030 C C5  . NAG N  3 .   ? -3.231  -11.495 -23.332 1.00 71.36  ? 1002 NAG A C5  1 
HETATM 12031 C C6  . NAG N  3 .   ? -3.708  -12.341 -24.500 1.00 69.23  ? 1002 NAG A C6  1 
HETATM 12032 C C7  . NAG N  3 .   ? -2.370  -7.329  -20.156 1.00 67.08  ? 1002 NAG A C7  1 
HETATM 12033 C C8  . NAG N  3 .   ? -1.578  -6.916  -18.946 1.00 52.56  ? 1002 NAG A C8  1 
HETATM 12034 N N2  . NAG N  3 .   ? -1.976  -8.456  -20.754 1.00 64.06  ? 1002 NAG A N2  1 
HETATM 12035 O O3  . NAG N  3 .   ? -4.815  -9.091  -20.926 1.00 76.21  ? 1002 NAG A O3  1 
HETATM 12036 O O4  . NAG N  3 .   ? -5.214  -11.811 -22.024 1.00 81.05  ? 1002 NAG A O4  1 
HETATM 12037 O O5  . NAG N  3 .   ? -2.322  -10.505 -23.832 1.00 65.78  ? 1002 NAG A O5  1 
HETATM 12038 O O6  . NAG N  3 .   ? -3.735  -11.702 -25.773 1.00 76.07  ? 1002 NAG A O6  1 
HETATM 12039 O O7  . NAG N  3 .   ? -3.313  -6.658  -20.579 1.00 72.13  ? 1002 NAG A O7  1 
HETATM 12040 C C1  . FUC O  7 .   ? -4.732  -10.658 -25.963 1.00 78.06  ? 1003 FUC A C1  1 
HETATM 12041 C C2  . FUC O  7 .   ? -4.240  -9.621  -27.068 1.00 67.58  ? 1003 FUC A C2  1 
HETATM 12042 C C3  . FUC O  7 .   ? -5.273  -9.335  -28.152 1.00 64.47  ? 1003 FUC A C3  1 
HETATM 12043 C C4  . FUC O  7 .   ? -6.648  -9.183  -27.555 1.00 69.93  ? 1003 FUC A C4  1 
HETATM 12044 C C5  . FUC O  7 .   ? -7.064  -10.549 -27.059 1.00 76.66  ? 1003 FUC A C5  1 
HETATM 12045 C C6  . FUC O  7 .   ? -8.442  -10.532 -26.409 1.00 76.48  ? 1003 FUC A C6  1 
HETATM 12046 O O2  . FUC O  7 .   ? -3.011  -10.016 -27.681 1.00 59.19  ? 1003 FUC A O2  1 
HETATM 12047 O O3  . FUC O  7 .   ? -4.959  -8.107  -28.811 1.00 77.68  ? 1003 FUC A O3  1 
HETATM 12048 O O4  . FUC O  7 .   ? -6.641  -8.231  -26.489 1.00 68.66  ? 1003 FUC A O4  1 
HETATM 12049 O O5  . FUC O  7 .   ? -6.109  -11.143 -26.087 1.00 81.84  ? 1003 FUC A O5  1 
HETATM 12050 C C1  . FUL P  4 .   ? -5.618  -9.704  -19.894 1.00 83.74  ? 1004 FUL A C1  1 
HETATM 12051 C C2  . FUL P  4 .   ? -6.044  -8.766  -18.748 1.00 86.72  ? 1004 FUL A C2  1 
HETATM 12052 O O2  . FUL P  4 .   ? -6.319  -7.398  -19.144 1.00 81.60  ? 1004 FUL A O2  1 
HETATM 12053 C C3  . FUL P  4 .   ? -7.268  -9.422  -18.123 1.00 87.25  ? 1004 FUL A C3  1 
HETATM 12054 O O3  . FUL P  4 .   ? -7.748  -8.623  -17.046 1.00 90.43  ? 1004 FUL A O3  1 
HETATM 12055 C C4  . FUL P  4 .   ? -6.920  -10.882 -17.599 1.00 85.01  ? 1004 FUL A C4  1 
HETATM 12056 O O4  . FUL P  4 .   ? -6.143  -10.824 -16.419 1.00 87.01  ? 1004 FUL A O4  1 
HETATM 12057 C C5  . FUL P  4 .   ? -6.176  -11.739 -18.678 1.00 84.07  ? 1004 FUL A C5  1 
HETATM 12058 C C6  . FUL P  4 .   ? -5.507  -13.013 -18.132 1.00 78.34  ? 1004 FUL A C6  1 
HETATM 12059 O O5  . FUL P  4 .   ? -5.156  -10.967 -19.401 1.00 85.88  ? 1004 FUL A O5  1 
HETATM 12060 C C1  . NAG Q  3 .   ? -6.560  -11.767 -22.571 1.00 86.38  ? 1005 NAG A C1  1 
HETATM 12061 C C2  . NAG Q  3 .   ? -7.343  -12.987 -22.087 1.00 82.72  ? 1005 NAG A C2  1 
HETATM 12062 C C3  . NAG Q  3 .   ? -8.758  -12.581 -21.678 1.00 88.93  ? 1005 NAG A C3  1 
HETATM 12063 C C4  . NAG Q  3 .   ? -9.396  -11.724 -22.763 1.00 93.56  ? 1005 NAG A C4  1 
HETATM 12064 C C5  . NAG Q  3 .   ? -8.562  -10.461 -22.995 1.00 88.98  ? 1005 NAG A C5  1 
HETATM 12065 C C6  . NAG Q  3 .   ? -9.246  -9.187  -22.550 1.00 82.41  ? 1005 NAG A C6  1 
HETATM 12066 C C7  . NAG Q  3 .   ? -6.741  -15.175 -23.009 1.00 82.80  ? 1005 NAG A C7  1 
HETATM 12067 C C8  . NAG Q  3 .   ? -6.891  -16.118 -24.165 1.00 82.27  ? 1005 NAG A C8  1 
HETATM 12068 N N2  . NAG Q  3 .   ? -7.385  -14.012 -23.118 1.00 78.20  ? 1005 NAG A N2  1 
HETATM 12069 O O3  . NAG Q  3 .   ? -8.736  -11.867 -20.447 1.00 91.94  ? 1005 NAG A O3  1 
HETATM 12070 O O4  . NAG Q  3 .   ? -9.449  -12.480 -23.968 1.00 94.22  ? 1005 NAG A O4  1 
HETATM 12071 O O5  . NAG Q  3 .   ? -7.320  -10.550 -22.278 1.00 91.03  ? 1005 NAG A O5  1 
HETATM 12072 O O6  . NAG Q  3 .   ? -9.807  -9.317  -21.252 1.00 86.39  ? 1005 NAG A O6  1 
HETATM 12073 O O7  . NAG Q  3 .   ? -6.063  -15.457 -22.022 1.00 80.07  ? 1005 NAG A O7  1 
HETATM 12074 C C1  . SIA R  5 .   ? 33.095  8.374   -27.419 1.00 45.82  ? 1006 SIA A C1  1 
HETATM 12075 C C2  . SIA R  5 .   ? 32.727  9.796   -27.824 1.00 41.50  ? 1006 SIA A C2  1 
HETATM 12076 C C3  . SIA R  5 .   ? 32.218  9.758   -29.269 1.00 36.99  ? 1006 SIA A C3  1 
HETATM 12077 C C4  . SIA R  5 .   ? 30.864  9.084   -29.453 1.00 36.86  ? 1006 SIA A C4  1 
HETATM 12078 C C5  . SIA R  5 .   ? 29.839  9.674   -28.499 1.00 36.00  ? 1006 SIA A C5  1 
HETATM 12079 C C6  . SIA R  5 .   ? 30.374  9.726   -27.053 1.00 36.81  ? 1006 SIA A C6  1 
HETATM 12080 C C7  . SIA R  5 .   ? 29.351  10.373  -26.090 1.00 35.12  ? 1006 SIA A C7  1 
HETATM 12081 C C8  . SIA R  5 .   ? 29.826  10.509  -24.627 1.00 31.90  ? 1006 SIA A C8  1 
HETATM 12082 C C9  . SIA R  5 .   ? 28.637  10.769  -23.722 1.00 34.79  ? 1006 SIA A C9  1 
HETATM 12083 C C10 . SIA R  5 .   ? 27.378  9.512   -28.747 1.00 32.10  ? 1006 SIA A C10 1 
HETATM 12084 C C11 . SIA R  5 .   ? 26.215  8.573   -28.882 1.00 25.01  ? 1006 SIA A C11 1 
HETATM 12085 N N5  . SIA R  5 .   ? 28.591  8.933   -28.627 1.00 30.75  ? 1006 SIA A N5  1 
HETATM 12086 O O1A . SIA R  5 .   ? 33.984  7.782   -28.096 1.00 42.56  ? 1006 SIA A O1A 1 
HETATM 12087 O O1B . SIA R  5 .   ? 32.513  7.825   -26.434 1.00 42.29  ? 1006 SIA A O1B 1 
HETATM 12088 O O4  . SIA R  5 .   ? 30.418  9.256   -30.808 1.00 39.23  ? 1006 SIA A O4  1 
HETATM 12089 O O6  . SIA R  5 .   ? 31.711  10.309  -26.942 1.00 36.62  ? 1006 SIA A O6  1 
HETATM 12090 O O7  . SIA R  5 .   ? 29.006  11.673  -26.616 1.00 37.21  ? 1006 SIA A O7  1 
HETATM 12091 O O8  . SIA R  5 .   ? 30.510  9.349   -24.139 1.00 28.09  ? 1006 SIA A O8  1 
HETATM 12092 O O9  . SIA R  5 .   ? 29.062  10.780  -22.349 1.00 37.31  ? 1006 SIA A O9  1 
HETATM 12093 O O10 . SIA R  5 .   ? 27.196  10.721  -28.753 1.00 33.82  ? 1006 SIA A O10 1 
HETATM 12094 C C1  . GAL S  6 .   ? 36.098  12.654  -25.344 1.00 70.70  ? 1007 GAL A C1  1 
HETATM 12095 C C2  . GAL S  6 .   ? 34.980  12.337  -26.406 1.00 65.26  ? 1007 GAL A C2  1 
HETATM 12096 C C3  . GAL S  6 .   ? 34.647  10.836  -26.612 1.00 57.17  ? 1007 GAL A C3  1 
HETATM 12097 C C4  . GAL S  6 .   ? 35.967  9.996   -26.683 1.00 59.27  ? 1007 GAL A C4  1 
HETATM 12098 C C5  . GAL S  6 .   ? 36.871  10.361  -25.474 1.00 58.87  ? 1007 GAL A C5  1 
HETATM 12099 C C6  . GAL S  6 .   ? 38.223  9.628   -25.401 1.00 57.88  ? 1007 GAL A C6  1 
HETATM 12100 O O2  . GAL S  6 .   ? 33.754  13.003  -26.110 1.00 64.08  ? 1007 GAL A O2  1 
HETATM 12101 O O3  . GAL S  6 .   ? 33.898  10.653  -27.851 1.00 51.65  ? 1007 GAL A O3  1 
HETATM 12102 O O4  . GAL S  6 .   ? 36.657  10.151  -27.936 1.00 58.15  ? 1007 GAL A O4  1 
HETATM 12103 O O5  . GAL S  6 .   ? 37.182  11.739  -25.421 1.00 63.64  ? 1007 GAL A O5  1 
HETATM 12104 O O6  . GAL S  6 .   ? 39.101  10.027  -26.453 1.00 73.84  ? 1007 GAL A O6  1 
HETATM 12105 C C1  . NAG T  3 .   ? 39.699  14.845  -23.663 1.00 98.40  ? 1008 NAG A C1  1 
HETATM 12106 C C2  . NAG T  3 .   ? 38.249  14.968  -24.131 1.00 92.56  ? 1008 NAG A C2  1 
HETATM 12107 C C3  . NAG T  3 .   ? 38.006  14.000  -25.280 1.00 90.10  ? 1008 NAG A C3  1 
HETATM 12108 C C4  . NAG T  3 .   ? 38.945  14.348  -26.429 1.00 92.01  ? 1008 NAG A C4  1 
HETATM 12109 C C5  . NAG T  3 .   ? 40.379  14.167  -25.929 1.00 96.87  ? 1008 NAG A C5  1 
HETATM 12110 C C6  . NAG T  3 .   ? 41.437  14.477  -26.969 1.00 101.40 ? 1008 NAG A C6  1 
HETATM 12111 C C7  . NAG T  3 .   ? 36.792  15.764  -22.334 1.00 94.60  ? 1008 NAG A C7  1 
HETATM 12112 C C8  . NAG T  3 .   ? 35.806  15.381  -21.272 1.00 95.52  ? 1008 NAG A C8  1 
HETATM 12113 N N2  . NAG T  3 .   ? 37.300  14.759  -23.062 1.00 85.84  ? 1008 NAG A N2  1 
HETATM 12114 O O1  . NAG T  3 .   ? 39.929  15.794  -22.664 1.00 99.22  ? 1008 NAG A O1  1 
HETATM 12115 O O3  . NAG T  3 .   ? 36.619  13.979  -25.626 1.00 91.02  ? 1008 NAG A O3  1 
HETATM 12116 O O4  . NAG T  3 .   ? 38.715  13.544  -27.582 1.00 91.65  ? 1008 NAG A O4  1 
HETATM 12117 O O5  . NAG T  3 .   ? 40.621  15.032  -24.800 1.00 100.86 ? 1008 NAG A O5  1 
HETATM 12118 O O6  . NAG T  3 .   ? 41.206  15.713  -27.633 1.00 104.64 ? 1008 NAG A O6  1 
HETATM 12119 O O7  . NAG T  3 .   ? 37.124  16.932  -22.527 1.00 100.08 ? 1008 NAG A O7  1 
HETATM 12120 C C1  . NAG U  3 .   ? 15.012  -55.176 10.309  1.00 98.64  ? 1001 NAG E C1  1 
HETATM 12121 C C2  . NAG U  3 .   ? 15.080  -55.179 8.771   1.00 95.76  ? 1001 NAG E C2  1 
HETATM 12122 C C3  . NAG U  3 .   ? 13.910  -54.376 8.183   1.00 102.26 ? 1001 NAG E C3  1 
HETATM 12123 C C4  . NAG U  3 .   ? 12.583  -54.873 8.748   1.00 102.59 ? 1001 NAG E C4  1 
HETATM 12124 C C5  . NAG U  3 .   ? 12.613  -54.899 10.277  1.00 102.37 ? 1001 NAG E C5  1 
HETATM 12125 C C6  . NAG U  3 .   ? 11.368  -55.517 10.874  1.00 100.41 ? 1001 NAG E C6  1 
HETATM 12126 C C7  . NAG U  3 .   ? 16.807  -54.695 7.061   1.00 102.71 ? 1001 NAG E C7  1 
HETATM 12127 C C8  . NAG U  3 .   ? 18.162  -54.092 6.822   1.00 96.49  ? 1001 NAG E C8  1 
HETATM 12128 N N2  . NAG U  3 .   ? 16.362  -54.644 8.323   1.00 98.18  ? 1001 NAG E N2  1 
HETATM 12129 O O3  . NAG U  3 .   ? 13.884  -54.477 6.760   1.00 105.25 ? 1001 NAG E O3  1 
HETATM 12130 O O4  . NAG U  3 .   ? 11.515  -54.038 8.309   1.00 98.82  ? 1001 NAG E O4  1 
HETATM 12131 O O5  . NAG U  3 .   ? 13.727  -55.683 10.738  1.00 103.53 ? 1001 NAG E O5  1 
HETATM 12132 O O6  . NAG U  3 .   ? 10.571  -56.138 9.873   1.00 101.18 ? 1001 NAG E O6  1 
HETATM 12133 O O7  . NAG U  3 .   ? 16.144  -55.188 6.149   1.00 101.56 ? 1001 NAG E O7  1 
HETATM 12134 C C1  . NAG V  3 .   ? 4.129   15.182  23.140  1.00 65.54  ? 1002 NAG E C1  1 
HETATM 12135 C C2  . NAG V  3 .   ? 5.418   16.003  23.013  1.00 68.92  ? 1002 NAG E C2  1 
HETATM 12136 C C3  . NAG V  3 .   ? 6.109   16.155  24.374  1.00 74.02  ? 1002 NAG E C3  1 
HETATM 12137 C C4  . NAG V  3 .   ? 5.122   16.537  25.481  1.00 83.23  ? 1002 NAG E C4  1 
HETATM 12138 C C5  . NAG V  3 .   ? 3.838   15.706  25.412  1.00 78.85  ? 1002 NAG E C5  1 
HETATM 12139 C C6  . NAG V  3 .   ? 2.753   16.177  26.364  1.00 78.34  ? 1002 NAG E C6  1 
HETATM 12140 C C7  . NAG V  3 .   ? 7.077   16.021  21.170  1.00 67.10  ? 1002 NAG E C7  1 
HETATM 12141 C C8  . NAG V  3 .   ? 7.919   15.156  20.269  1.00 52.82  ? 1002 NAG E C8  1 
HETATM 12142 N N2  . NAG V  3 .   ? 6.316   15.368  22.056  1.00 69.79  ? 1002 NAG E N2  1 
HETATM 12143 O O3  . NAG V  3 .   ? 7.075   17.188  24.211  1.00 84.11  ? 1002 NAG E O3  1 
HETATM 12144 O O4  . NAG V  3 .   ? 5.716   16.335  26.762  1.00 87.60  ? 1002 NAG E O4  1 
HETATM 12145 O O5  . NAG V  3 .   ? 3.289   15.768  24.090  1.00 65.11  ? 1002 NAG E O5  1 
HETATM 12146 O O6  . NAG V  3 .   ? 2.817   17.572  26.634  1.00 74.29  ? 1002 NAG E O6  1 
HETATM 12147 O O7  . NAG V  3 .   ? 7.094   17.246  21.097  1.00 72.71  ? 1002 NAG E O7  1 
HETATM 12148 C C1  . FUL W  4 .   ? 8.276   17.121  25.019  1.00 91.51  ? 1003 FUL E C1  1 
HETATM 12149 C C2  . FUL W  4 .   ? 9.383   17.938  24.330  1.00 97.86  ? 1003 FUL E C2  1 
HETATM 12150 O O2  . FUL W  4 .   ? 8.919   19.237  23.903  1.00 96.51  ? 1003 FUL E O2  1 
HETATM 12151 C C3  . FUL W  4 .   ? 10.621  18.038  25.254  1.00 101.52 ? 1003 FUL E C3  1 
HETATM 12152 O O3  . FUL W  4 .   ? 11.722  18.674  24.575  1.00 103.76 ? 1003 FUL E O3  1 
HETATM 12153 C C4  . FUL W  4 .   ? 11.087  16.629  25.707  1.00 99.63  ? 1003 FUL E C4  1 
HETATM 12154 O O4  . FUL W  4 .   ? 11.660  15.913  24.609  1.00 108.55 ? 1003 FUL E O4  1 
HETATM 12155 C C5  . FUL W  4 .   ? 9.912   15.829  26.287  1.00 95.40  ? 1003 FUL E C5  1 
HETATM 12156 C C6  . FUL W  4 .   ? 10.274  14.368  26.541  1.00 96.18  ? 1003 FUL E C6  1 
HETATM 12157 O O5  . FUL W  4 .   ? 8.731   15.845  25.403  1.00 90.89  ? 1003 FUL E O5  1 
HETATM 12158 C C1  . NAG X  3 .   ? 5.783   17.558  27.540  1.00 93.48  ? 1004 NAG E C1  1 
HETATM 12159 C C2  . NAG X  3 .   ? 6.628   17.349  28.800  1.00 97.71  ? 1004 NAG E C2  1 
HETATM 12160 C C3  . NAG X  3 .   ? 7.704   18.436  28.915  1.00 103.99 ? 1004 NAG E C3  1 
HETATM 12161 C C4  . NAG X  3 .   ? 7.100   19.832  28.776  1.00 103.10 ? 1004 NAG E C4  1 
HETATM 12162 C C5  . NAG X  3 .   ? 6.214   19.916  27.532  1.00 102.11 ? 1004 NAG E C5  1 
HETATM 12163 C C6  . NAG X  3 .   ? 6.624   21.011  26.571  1.00 100.72 ? 1004 NAG E C6  1 
HETATM 12164 C C7  . NAG X  3 .   ? 5.048   16.265  30.331  1.00 94.63  ? 1004 NAG E C7  1 
HETATM 12165 C C8  . NAG X  3 .   ? 4.240   16.406  31.586  1.00 94.60  ? 1004 NAG E C8  1 
HETATM 12166 N N2  . NAG X  3 .   ? 5.791   17.322  29.991  1.00 98.62  ? 1004 NAG E N2  1 
HETATM 12167 O O3  . NAG X  3 .   ? 8.700   18.233  27.918  1.00 97.40  ? 1004 NAG E O3  1 
HETATM 12168 O O4  . NAG X  3 .   ? 6.352   20.179  29.937  1.00 96.50  ? 1004 NAG E O4  1 
HETATM 12169 O O5  . NAG X  3 .   ? 6.284   18.681  26.803  1.00 98.35  ? 1004 NAG E O5  1 
HETATM 12170 O O6  . NAG X  3 .   ? 7.901   21.544  26.892  1.00 107.14 ? 1004 NAG E O6  1 
HETATM 12171 O O7  . NAG X  3 .   ? 5.034   15.235  29.661  1.00 89.24  ? 1004 NAG E O7  1 
HETATM 12172 C C1  . SIA Y  5 .   ? -13.510 2.922   -9.102  1.00 66.01  ? 1005 SIA E C1  1 
HETATM 12173 C C2  . SIA Y  5 .   ? -13.809 4.185   -9.889  1.00 70.33  ? 1005 SIA E C2  1 
HETATM 12174 C C3  . SIA Y  5 .   ? -14.938 4.921   -9.151  1.00 62.09  ? 1005 SIA E C3  1 
HETATM 12175 C C4  . SIA Y  5 .   ? -14.515 5.608   -7.861  1.00 54.32  ? 1005 SIA E C4  1 
HETATM 12176 C C5  . SIA Y  5 .   ? -13.286 6.468   -8.079  1.00 54.01  ? 1005 SIA E C5  1 
HETATM 12177 C C6  . SIA Y  5 .   ? -12.168 5.591   -8.667  1.00 56.96  ? 1005 SIA E C6  1 
HETATM 12178 C C7  . SIA Y  5 .   ? -10.830 6.324   -8.884  1.00 58.71  ? 1005 SIA E C7  1 
HETATM 12179 C C8  . SIA Y  5 .   ? -9.732  5.474   -9.554  1.00 57.75  ? 1005 SIA E C8  1 
HETATM 12180 C C9  . SIA Y  5 .   ? -8.387  6.222   -9.511  1.00 56.52  ? 1005 SIA E C9  1 
HETATM 12181 C C10 . SIA Y  5 .   ? -12.384 8.282   -6.609  1.00 51.56  ? 1005 SIA E C10 1 
HETATM 12182 C C11 . SIA Y  5 .   ? -12.114 8.701   -5.190  1.00 42.58  ? 1005 SIA E C11 1 
HETATM 12183 N N5  . SIA Y  5 .   ? -12.945 7.078   -6.796  1.00 57.57  ? 1005 SIA E N5  1 
HETATM 12184 O O1A . SIA Y  5 .   ? -12.327 2.509   -9.104  1.00 66.24  ? 1005 SIA E O1A 1 
HETATM 12185 O O1B . SIA Y  5 .   ? -14.425 2.337   -8.468  1.00 67.98  ? 1005 SIA E O1B 1 
HETATM 12186 O O4  . SIA Y  5 .   ? -15.569 6.443   -7.369  1.00 54.03  ? 1005 SIA E O4  1 
HETATM 12187 O O6  . SIA Y  5 .   ? -12.573 4.930   -9.884  1.00 68.33  ? 1005 SIA E O6  1 
HETATM 12188 O O7  . SIA Y  5 .   ? -11.024 7.553   -9.608  1.00 58.68  ? 1005 SIA E O7  1 
HETATM 12189 O O8  . SIA Y  5 .   ? -9.606  4.207   -8.890  1.00 57.56  ? 1005 SIA E O8  1 
HETATM 12190 O O9  . SIA Y  5 .   ? -7.269  5.458   -10.016 1.00 57.31  ? 1005 SIA E O9  1 
HETATM 12191 O O10 . SIA Y  5 .   ? -12.088 9.007   -7.536  1.00 58.58  ? 1005 SIA E O10 1 
HETATM 12192 C C1  . GAL Z  6 .   ? -12.738 2.103   -14.385 1.00 74.99  ? 1006 GAL E C1  1 
HETATM 12193 C C2  . GAL Z  6 .   ? -13.442 3.244   -13.576 1.00 75.59  ? 1006 GAL E C2  1 
HETATM 12194 C C3  . GAL Z  6 .   ? -13.558 2.903   -12.064 1.00 76.74  ? 1006 GAL E C3  1 
HETATM 12195 C C4  . GAL Z  6 .   ? -14.323 1.546   -11.932 1.00 81.47  ? 1006 GAL E C4  1 
HETATM 12196 C C5  . GAL Z  6 .   ? -13.627 0.430   -12.812 1.00 73.54  ? 1006 GAL E C5  1 
HETATM 12197 C C6  . GAL Z  6 .   ? -14.358 -0.942  -12.840 1.00 69.84  ? 1006 GAL E C6  1 
HETATM 12198 O O2  . GAL Z  6 .   ? -12.747 4.473   -13.699 1.00 83.42  ? 1006 GAL E O2  1 
HETATM 12199 O O3  . GAL Z  6 .   ? -14.267 3.949   -11.270 1.00 73.88  ? 1006 GAL E O3  1 
HETATM 12200 O O4  . GAL Z  6 .   ? -15.740 1.705   -12.236 1.00 85.40  ? 1006 GAL E O4  1 
HETATM 12201 O O5  . GAL Z  6 .   ? -13.410 0.840   -14.211 1.00 76.22  ? 1006 GAL E O5  1 
HETATM 12202 O O6  . GAL Z  6 .   ? -13.530 -1.997  -13.333 1.00 60.38  ? 1006 GAL E O6  1 
HETATM 12203 O O   . HOH AA 8 .   ? 46.862  11.169  12.563  1.00 41.27  ? 1101 HOH C O   1 
HETATM 12204 O O   . HOH AA 8 .   ? 37.207  15.644  18.237  1.00 35.95  ? 1102 HOH C O   1 
HETATM 12205 O O   . HOH AA 8 .   ? 36.898  2.760   -3.271  1.00 26.77  ? 1103 HOH C O   1 
HETATM 12206 O O   . HOH AA 8 .   ? 44.865  8.316   25.071  1.00 28.80  ? 1104 HOH C O   1 
HETATM 12207 O O   . HOH AA 8 .   ? 35.800  5.516   31.147  1.00 41.55  ? 1105 HOH C O   1 
HETATM 12208 O O   . HOH AA 8 .   ? 17.642  27.397  -5.739  1.00 43.41  ? 1106 HOH C O   1 
HETATM 12209 O O   . HOH AA 8 .   ? 50.702  12.949  2.846   1.00 48.38  ? 1107 HOH C O   1 
HETATM 12210 O O   . HOH AA 8 .   ? 26.583  24.677  2.669   1.00 35.42  ? 1108 HOH C O   1 
HETATM 12211 O O   . HOH AA 8 .   ? 34.541  1.353   27.781  1.00 34.84  ? 1109 HOH C O   1 
HETATM 12212 O O   . HOH AA 8 .   ? 36.278  3.229   -6.073  1.00 21.48  ? 1110 HOH C O   1 
HETATM 12213 O O   . HOH AA 8 .   ? 24.107  -1.083  4.036   1.00 35.80  ? 1111 HOH C O   1 
HETATM 12214 O O   . HOH AA 8 .   ? 39.955  -0.461  1.874   1.00 38.26  ? 1112 HOH C O   1 
HETATM 12215 O O   . HOH AA 8 .   ? 41.074  -15.416 20.270  1.00 53.92  ? 1113 HOH C O   1 
HETATM 12216 O O   . HOH AA 8 .   ? 19.400  19.742  -10.382 1.00 46.32  ? 1114 HOH C O   1 
HETATM 12217 O O   . HOH AA 8 .   ? 45.905  2.063   1.577   1.00 30.96  ? 1115 HOH C O   1 
HETATM 12218 O O   . HOH AA 8 .   ? 29.045  7.267   27.294  1.00 45.86  ? 1116 HOH C O   1 
HETATM 12219 O O   . HOH AA 8 .   ? 32.740  4.369   23.875  1.00 30.85  ? 1117 HOH C O   1 
HETATM 12220 O O   . HOH AA 8 .   ? 22.215  9.827   -5.349  1.00 23.58  ? 1118 HOH C O   1 
HETATM 12221 O O   . HOH AA 8 .   ? 34.451  -34.433 34.129  1.00 54.66  ? 1119 HOH C O   1 
HETATM 12222 O O   . HOH AA 8 .   ? 30.666  7.446   -11.010 1.00 26.38  ? 1120 HOH C O   1 
HETATM 12223 O O   . HOH AA 8 .   ? 45.551  4.320   19.338  1.00 32.74  ? 1121 HOH C O   1 
HETATM 12224 O O   . HOH AA 8 .   ? 28.167  14.593  22.508  1.00 42.42  ? 1122 HOH C O   1 
HETATM 12225 O O   . HOH AA 8 .   ? 17.622  10.679  5.766   1.00 44.02  ? 1123 HOH C O   1 
HETATM 12226 O O   . HOH AA 8 .   ? 39.074  -4.371  3.900   1.00 40.29  ? 1124 HOH C O   1 
HETATM 12227 O O   . HOH AA 8 .   ? 34.556  -6.399  15.087  1.00 35.77  ? 1125 HOH C O   1 
HETATM 12228 O O   . HOH AA 8 .   ? 38.179  11.700  25.941  1.00 39.10  ? 1126 HOH C O   1 
HETATM 12229 O O   . HOH AA 8 .   ? 25.859  -6.662  4.613   1.00 23.33  ? 1127 HOH C O   1 
HETATM 12230 O O   . HOH AA 8 .   ? 50.031  4.951   31.655  1.00 41.40  ? 1128 HOH C O   1 
HETATM 12231 O O   . HOH AA 8 .   ? 32.586  -15.560 32.682  1.00 42.53  ? 1129 HOH C O   1 
HETATM 12232 O O   . HOH AA 8 .   ? 53.286  -15.360 30.966  1.00 45.02  ? 1130 HOH C O   1 
HETATM 12233 O O   . HOH AA 8 .   ? 34.883  10.696  25.989  1.00 39.40  ? 1131 HOH C O   1 
HETATM 12234 O O   . HOH AA 8 .   ? 17.927  12.320  9.968   1.00 39.26  ? 1132 HOH C O   1 
HETATM 12235 O O   . HOH AA 8 .   ? 25.466  -28.019 43.977  1.00 57.48  ? 1133 HOH C O   1 
HETATM 12236 O O   . HOH AA 8 .   ? 28.361  7.531   -0.513  1.00 26.18  ? 1134 HOH C O   1 
HETATM 12237 O O   . HOH AA 8 .   ? 29.787  4.683   -11.558 1.00 29.53  ? 1135 HOH C O   1 
HETATM 12238 O O   . HOH AA 8 .   ? 23.791  -29.911 42.484  1.00 62.54  ? 1136 HOH C O   1 
HETATM 12239 O O   . HOH AA 8 .   ? 43.901  10.033  13.895  1.00 41.18  ? 1137 HOH C O   1 
HETATM 12240 O O   . HOH AA 8 .   ? 25.403  6.624   15.037  1.00 29.21  ? 1138 HOH C O   1 
HETATM 12241 O O   . HOH AA 8 .   ? 18.308  13.177  0.158   1.00 39.03  ? 1139 HOH C O   1 
HETATM 12242 O O   . HOH AA 8 .   ? 31.476  2.928   -11.738 1.00 31.33  ? 1140 HOH C O   1 
HETATM 12243 O O   . HOH AA 8 .   ? 25.028  -0.397  7.108   1.00 23.82  ? 1141 HOH C O   1 
HETATM 12244 O O   . HOH AA 8 .   ? 32.708  -32.727 33.440  1.00 50.47  ? 1142 HOH C O   1 
HETATM 12245 O O   . HOH AA 8 .   ? 36.870  -5.776  3.800   1.00 44.36  ? 1143 HOH C O   1 
HETATM 12246 O O   . HOH AA 8 .   ? 38.002  12.599  28.616  1.00 47.19  ? 1144 HOH C O   1 
HETATM 12247 O O   . HOH AA 8 .   ? 16.609  9.297   7.300   1.00 41.12  ? 1145 HOH C O   1 
HETATM 12248 O O   . HOH AA 8 .   ? 37.798  -1.279  1.028   1.00 44.86  ? 1146 HOH C O   1 
HETATM 12249 O O   . HOH AA 8 .   ? 57.536  -18.590 31.420  1.00 62.76  ? 1147 HOH C O   1 
HETATM 12250 O O   . HOH BA 8 .   ? 27.267  -27.497 29.701  1.00 47.84  ? 201  HOH D O   1 
HETATM 12251 O O   . HOH BA 8 .   ? 22.930  -5.542  15.963  1.00 28.89  ? 202  HOH D O   1 
HETATM 12252 O O   . HOH BA 8 .   ? 27.008  -13.945 19.416  1.00 44.21  ? 203  HOH D O   1 
HETATM 12253 O O   . HOH BA 8 .   ? 15.598  -5.824  5.611   1.00 29.68  ? 204  HOH D O   1 
HETATM 12254 O O   . HOH BA 8 .   ? 48.959  -31.147 22.191  1.00 63.47  ? 205  HOH D O   1 
HETATM 12255 O O   . HOH BA 8 .   ? 16.507  -9.375  15.615  1.00 25.21  ? 206  HOH D O   1 
HETATM 12256 O O   . HOH BA 8 .   ? 50.642  -31.279 18.123  1.00 70.81  ? 207  HOH D O   1 
HETATM 12257 O O   . HOH CA 8 .   ? 26.948  4.071   -13.046 1.00 30.94  ? 1101 HOH A O   1 
HETATM 12258 O O   . HOH CA 8 .   ? 40.984  -29.467 0.089   1.00 45.45  ? 1102 HOH A O   1 
HETATM 12259 O O   . HOH CA 8 .   ? 38.372  -44.476 -14.333 1.00 68.45  ? 1103 HOH A O   1 
HETATM 12260 O O   . HOH CA 8 .   ? 8.241   -6.362  -10.153 1.00 35.67  ? 1104 HOH A O   1 
HETATM 12261 O O   . HOH CA 8 .   ? 6.946   11.558  -33.208 1.00 52.72  ? 1105 HOH A O   1 
HETATM 12262 O O   . HOH CA 8 .   ? 37.719  -23.788 8.426   1.00 49.85  ? 1106 HOH A O   1 
HETATM 12263 O O   . HOH CA 8 .   ? 37.545  -7.512  -32.578 1.00 37.37  ? 1107 HOH A O   1 
HETATM 12264 O O   . HOH CA 8 .   ? 39.637  -38.155 -8.855  1.00 52.91  ? 1108 HOH A O   1 
HETATM 12265 O O   . HOH CA 8 .   ? 23.676  2.365   -29.898 1.00 25.15  ? 1109 HOH A O   1 
HETATM 12266 O O   . HOH CA 8 .   ? 31.435  10.441  -21.507 1.00 29.74  ? 1110 HOH A O   1 
HETATM 12267 O O   . HOH CA 8 .   ? 36.343  -2.326  -38.316 1.00 35.27  ? 1111 HOH A O   1 
HETATM 12268 O O   . HOH CA 8 .   ? 17.978  7.952   -25.277 1.00 24.63  ? 1112 HOH A O   1 
HETATM 12269 O O   . HOH CA 8 .   ? 28.147  0.326   -18.019 1.00 29.66  ? 1113 HOH A O   1 
HETATM 12270 O O   . HOH CA 8 .   ? 34.506  7.349   -31.031 1.00 36.30  ? 1114 HOH A O   1 
HETATM 12271 O O   . HOH CA 8 .   ? 11.809  -6.035  -11.400 1.00 28.95  ? 1115 HOH A O   1 
HETATM 12272 O O   . HOH CA 8 .   ? 10.896  6.998   -33.002 1.00 35.72  ? 1116 HOH A O   1 
HETATM 12273 O O   . HOH CA 8 .   ? 29.182  -1.711  -34.285 1.00 30.61  ? 1117 HOH A O   1 
HETATM 12274 O O   . HOH CA 8 .   ? 31.340  -21.498 -7.727  1.00 37.36  ? 1118 HOH A O   1 
HETATM 12275 O O   . HOH CA 8 .   ? 31.092  -11.275 -13.152 1.00 31.28  ? 1119 HOH A O   1 
HETATM 12276 O O   . HOH CA 8 .   ? 5.521   -0.815  -28.777 1.00 35.20  ? 1120 HOH A O   1 
HETATM 12277 O O   . HOH CA 8 .   ? 11.752  -4.053  -39.485 1.00 28.00  ? 1121 HOH A O   1 
HETATM 12278 O O   . HOH CA 8 .   ? 28.318  -9.584  -28.005 1.00 32.61  ? 1122 HOH A O   1 
HETATM 12279 O O   . HOH CA 8 .   ? 23.741  -11.922 -26.501 1.00 30.83  ? 1123 HOH A O   1 
HETATM 12280 O O   . HOH CA 8 .   ? 41.487  4.702   -17.447 1.00 44.19  ? 1124 HOH A O   1 
HETATM 12281 O O   . HOH CA 8 .   ? 23.129  20.295  -30.934 1.00 43.84  ? 1125 HOH A O   1 
HETATM 12282 O O   . HOH CA 8 .   ? 15.604  -1.245  -31.032 1.00 34.49  ? 1126 HOH A O   1 
HETATM 12283 O O   . HOH CA 8 .   ? 18.743  -27.924 -26.353 1.00 41.19  ? 1127 HOH A O   1 
HETATM 12284 O O   . HOH CA 8 .   ? 20.987  -7.374  -32.716 1.00 47.47  ? 1128 HOH A O   1 
HETATM 12285 O O   . HOH CA 8 .   ? 34.754  -3.716  -26.691 1.00 34.65  ? 1129 HOH A O   1 
HETATM 12286 O O   . HOH CA 8 .   ? 22.036  -8.157  -6.153  1.00 27.23  ? 1130 HOH A O   1 
HETATM 12287 O O   . HOH CA 8 .   ? 20.195  6.283   -10.762 1.00 33.50  ? 1131 HOH A O   1 
HETATM 12288 O O   . HOH CA 8 .   ? 14.863  -6.881  -10.758 1.00 36.21  ? 1132 HOH A O   1 
HETATM 12289 O O   . HOH CA 8 .   ? 30.363  12.039  -31.733 1.00 40.84  ? 1133 HOH A O   1 
HETATM 12290 O O   . HOH CA 8 .   ? 37.679  3.842   -31.312 1.00 37.77  ? 1134 HOH A O   1 
HETATM 12291 O O   . HOH CA 8 .   ? 12.805  22.670  -17.270 1.00 39.90  ? 1135 HOH A O   1 
HETATM 12292 O O   . HOH CA 8 .   ? 2.555   5.640   -22.091 1.00 38.00  ? 1136 HOH A O   1 
HETATM 12293 O O   . HOH CA 8 .   ? 16.081  -19.394 -4.858  1.00 37.62  ? 1137 HOH A O   1 
HETATM 12294 O O   . HOH CA 8 .   ? 35.483  -5.064  -23.373 1.00 38.21  ? 1138 HOH A O   1 
HETATM 12295 O O   . HOH CA 8 .   ? 17.046  -13.507 -7.510  1.00 29.52  ? 1139 HOH A O   1 
HETATM 12296 O O   . HOH CA 8 .   ? 26.513  -11.695 -26.552 1.00 28.42  ? 1140 HOH A O   1 
HETATM 12297 O O   . HOH CA 8 .   ? 5.660   10.762  -15.570 1.00 49.74  ? 1141 HOH A O   1 
HETATM 12298 O O   . HOH CA 8 .   ? 8.608   -11.047 -11.780 1.00 34.33  ? 1142 HOH A O   1 
HETATM 12299 O O   . HOH CA 8 .   ? 35.132  -4.088  -20.042 1.00 36.50  ? 1143 HOH A O   1 
HETATM 12300 O O   . HOH CA 8 .   ? 22.853  -2.940  -6.988  1.00 36.90  ? 1144 HOH A O   1 
HETATM 12301 O O   . HOH CA 8 .   ? -6.867  -7.745  -31.196 1.00 43.50  ? 1145 HOH A O   1 
HETATM 12302 O O   . HOH CA 8 .   ? 8.225   6.708   -32.631 1.00 43.11  ? 1146 HOH A O   1 
HETATM 12303 O O   . HOH CA 8 .   ? 24.584  3.397   -8.734  1.00 40.79  ? 1147 HOH A O   1 
HETATM 12304 O O   . HOH CA 8 .   ? 4.831   12.147  -12.094 1.00 44.91  ? 1148 HOH A O   1 
HETATM 12305 O O   . HOH CA 8 .   ? 11.449  -9.406  -11.405 1.00 33.02  ? 1149 HOH A O   1 
HETATM 12306 O O   . HOH CA 8 .   ? 12.798  -13.319 -32.979 1.00 41.34  ? 1150 HOH A O   1 
HETATM 12307 O O   . HOH CA 8 .   ? 16.231  -13.227 -32.918 1.00 44.07  ? 1151 HOH A O   1 
HETATM 12308 O O   . HOH CA 8 .   ? 15.253  24.188  -17.889 1.00 45.13  ? 1152 HOH A O   1 
HETATM 12309 O O   . HOH CA 8 .   ? 14.264  -15.781 -33.931 1.00 61.54  ? 1153 HOH A O   1 
HETATM 12310 O O   . HOH CA 8 .   ? 17.437  -15.655 -33.791 1.00 53.28  ? 1154 HOH A O   1 
HETATM 12311 O O   . HOH DA 8 .   ? 46.517  -78.146 33.240  1.00 62.74  ? 201  HOH B O   1 
HETATM 12312 O O   . HOH DA 8 .   ? 31.203  -15.747 1.526   1.00 32.45  ? 202  HOH B O   1 
HETATM 12313 O O   . HOH DA 8 .   ? 33.579  -9.500  4.117   1.00 35.90  ? 203  HOH B O   1 
HETATM 12314 O O   . HOH DA 8 .   ? 31.479  -11.917 -3.092  1.00 28.19  ? 204  HOH B O   1 
HETATM 12315 O O   . HOH DA 8 .   ? 24.414  -4.340  3.775   1.00 27.37  ? 205  HOH B O   1 
HETATM 12316 O O   . HOH DA 8 .   ? 35.284  -3.429  1.654   1.00 39.90  ? 206  HOH B O   1 
HETATM 12317 O O   . HOH DA 8 .   ? 34.194  0.675   0.422   1.00 35.30  ? 207  HOH B O   1 
HETATM 12318 O O   . HOH DA 8 .   ? 19.926  -8.497  0.475   1.00 25.39  ? 208  HOH B O   1 
HETATM 12319 O O   . HOH EA 8 .   ? 1.896   -25.003 31.878  1.00 63.67  ? 1101 HOH E O   1 
HETATM 12320 O O   . HOH EA 8 .   ? 9.229   -66.778 27.258  1.00 82.84  ? 1102 HOH E O   1 
HETATM 12321 O O   . HOH EA 8 .   ? 7.109   5.198   -3.979  1.00 39.21  ? 1103 HOH E O   1 
HETATM 12322 O O   . HOH EA 8 .   ? -13.562 15.437  -4.862  1.00 48.29  ? 1104 HOH E O   1 
HETATM 12323 O O   . HOH EA 8 .   ? -0.296  -38.335 13.931  1.00 54.20  ? 1105 HOH E O   1 
HETATM 12324 O O   . HOH EA 8 .   ? 11.154  -5.464  11.945  1.00 27.59  ? 1106 HOH E O   1 
HETATM 12325 O O   . HOH EA 8 .   ? 3.870   -0.700  24.140  1.00 30.38  ? 1107 HOH E O   1 
HETATM 12326 O O   . HOH EA 8 .   ? -6.963  -20.409 8.150   1.00 50.49  ? 1108 HOH E O   1 
HETATM 12327 O O   . HOH EA 8 .   ? -4.613  -34.175 25.896  1.00 67.25  ? 1109 HOH E O   1 
HETATM 12328 O O   . HOH EA 8 .   ? -8.133  -6.334  15.386  1.00 41.37  ? 1110 HOH E O   1 
HETATM 12329 O O   . HOH EA 8 .   ? 1.734   21.231  -7.944  1.00 49.96  ? 1111 HOH E O   1 
HETATM 12330 O O   . HOH EA 8 .   ? -16.100 19.295  -5.203  1.00 53.89  ? 1112 HOH E O   1 
HETATM 12331 O O   . HOH EA 8 .   ? 13.391  18.891  22.514  1.00 58.40  ? 1113 HOH E O   1 
HETATM 12332 O O   . HOH EA 8 .   ? -12.114 4.532   4.710   1.00 43.70  ? 1114 HOH E O   1 
HETATM 12333 O O   . HOH EA 8 .   ? 0.866   -12.171 4.039   1.00 34.58  ? 1115 HOH E O   1 
HETATM 12334 O O   . HOH EA 8 .   ? -4.039  -36.227 27.771  1.00 63.61  ? 1116 HOH E O   1 
HETATM 12335 O O   . HOH EA 8 .   ? -1.364  -5.479  -5.718  1.00 43.21  ? 1117 HOH E O   1 
HETATM 12336 O O   . HOH EA 8 .   ? -18.869 -4.336  8.877   1.00 49.98  ? 1118 HOH E O   1 
HETATM 12337 O O   . HOH EA 8 .   ? 1.320   -36.003 20.394  1.00 55.27  ? 1119 HOH E O   1 
HETATM 12338 O O   . HOH EA 8 .   ? 9.144   -12.091 8.152   1.00 32.48  ? 1120 HOH E O   1 
HETATM 12339 O O   . HOH EA 8 .   ? 5.889   -12.096 2.548   1.00 42.95  ? 1121 HOH E O   1 
HETATM 12340 O O   . HOH EA 8 .   ? -12.919 -20.180 3.582   1.00 62.03  ? 1122 HOH E O   1 
HETATM 12341 O O   . HOH EA 8 .   ? 9.503   -41.605 25.137  1.00 58.63  ? 1123 HOH E O   1 
HETATM 12342 O O   . HOH EA 8 .   ? 10.097  -3.951  1.492   1.00 33.41  ? 1124 HOH E O   1 
HETATM 12343 O O   . HOH EA 8 .   ? -0.022  -19.632 26.271  1.00 49.97  ? 1125 HOH E O   1 
HETATM 12344 O O   . HOH EA 8 .   ? 8.775   6.489   14.351  1.00 36.45  ? 1126 HOH E O   1 
HETATM 12345 O O   . HOH EA 8 .   ? -14.681 -10.347 7.755   1.00 44.63  ? 1127 HOH E O   1 
HETATM 12346 O O   . HOH EA 8 .   ? -10.918 -8.460  -0.995  1.00 47.77  ? 1128 HOH E O   1 
HETATM 12347 O O   . HOH EA 8 .   ? 2.882   -6.211  -0.148  1.00 39.87  ? 1129 HOH E O   1 
HETATM 12348 O O   . HOH EA 8 .   ? 3.034   -18.305 23.373  1.00 46.28  ? 1130 HOH E O   1 
HETATM 12349 O O   . HOH EA 8 .   ? 18.812  -31.629 4.120   1.00 40.91  ? 1131 HOH E O   1 
HETATM 12350 O O   . HOH EA 8 .   ? -7.527  -13.009 18.393  1.00 45.77  ? 1132 HOH E O   1 
HETATM 12351 O O   . HOH EA 8 .   ? 16.886  -8.041  7.822   1.00 22.50  ? 1133 HOH E O   1 
HETATM 12352 O O   . HOH EA 8 .   ? 11.094  -6.049  4.757   1.00 24.09  ? 1134 HOH E O   1 
HETATM 12353 O O   . HOH EA 8 .   ? 12.434  9.383   1.756   1.00 42.04  ? 1135 HOH E O   1 
HETATM 12354 O O   . HOH EA 8 .   ? 7.776   7.428   -3.814  1.00 35.51  ? 1136 HOH E O   1 
HETATM 12355 O O   . HOH EA 8 .   ? 13.781  7.963   5.110   1.00 46.19  ? 1137 HOH E O   1 
HETATM 12356 O O   . HOH EA 8 .   ? 1.073   -8.021  0.972   1.00 44.54  ? 1138 HOH E O   1 
HETATM 12357 O O   . HOH EA 8 .   ? -14.333 3.070   4.780   1.00 43.09  ? 1139 HOH E O   1 
HETATM 12358 O O   . HOH EA 8 .   ? 3.749   11.636  -16.843 1.00 49.32  ? 1140 HOH E O   1 
HETATM 12359 O O   . HOH EA 8 .   ? 0.692   -18.017 24.492  1.00 45.99  ? 1141 HOH E O   1 
HETATM 12360 O O   . HOH EA 8 .   ? -0.208  -12.669 1.327   1.00 41.86  ? 1142 HOH E O   1 
HETATM 12361 O O   . HOH EA 8 .   ? 0.758   -23.420 33.389  1.00 57.63  ? 1143 HOH E O   1 
HETATM 12362 O O   . HOH FA 8 .   ? 13.426  -20.129 8.847   1.00 42.84  ? 201  HOH F O   1 
HETATM 12363 O O   . HOH FA 8 .   ? 12.532  -14.776 -7.653  1.00 40.64  ? 202  HOH F O   1 
HETATM 12364 O O   . HOH FA 8 .   ? 6.540   -15.113 9.106   1.00 44.12  ? 203  HOH F O   1 
HETATM 12365 O O   . HOH FA 8 .   ? 14.670  -12.333 -8.188  1.00 34.86  ? 204  HOH F O   1 
HETATM 12366 O O   . HOH FA 8 .   ? 15.965  -18.485 -2.329  1.00 35.18  ? 205  HOH F O   1 
HETATM 12367 O O   . HOH FA 8 .   ? 19.581  -8.513  -2.175  1.00 25.07  ? 206  HOH F O   1 
HETATM 12368 O O   . HOH FA 8 .   ? 16.330  -21.028 -1.341  1.00 37.99  ? 207  HOH F O   1 
HETATM 12369 O O   . HOH FA 8 .   ? 13.369  -12.115 -10.053 1.00 40.72  ? 208  HOH F O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   7   ?   ?   ?   C . n 
A 1 2   ASP 2   8   8   ASP ASP C . n 
A 1 3   PRO 3   9   9   PRO PRO C . n 
A 1 4   GLY 4   10  10  GLY GLY C . n 
A 1 5   ASP 5   11  11  ASP ASP C . n 
A 1 6   GLN 6   12  12  GLN GLN C . n 
A 1 7   ILE 7   13  13  ILE ILE C . n 
A 1 8   CYS 8   14  14  CYS CYS C . n 
A 1 9   ILE 9   15  15  ILE ILE C . n 
A 1 10  GLY 10  16  16  GLY GLY C . n 
A 1 11  TYR 11  17  17  TYR TYR C . n 
A 1 12  HIS 12  18  18  HIS HIS C . n 
A 1 13  ALA 13  19  19  ALA ALA C . n 
A 1 14  ASN 14  20  20  ASN ASN C . n 
A 1 15  ASN 15  21  21  ASN ASN C . n 
A 1 16  SER 16  22  22  SER SER C . n 
A 1 17  THR 17  23  23  THR THR C . n 
A 1 18  GLU 18  24  24  GLU GLU C . n 
A 1 19  GLN 19  25  25  GLN GLN C . n 
A 1 20  VAL 20  26  26  VAL VAL C . n 
A 1 21  ASP 21  27  27  ASP ASP C . n 
A 1 22  THR 22  28  28  THR THR C . n 
A 1 23  ILE 23  29  29  ILE ILE C . n 
A 1 24  MET 24  30  30  MET MET C . n 
A 1 25  GLU 25  31  31  GLU GLU C . n 
A 1 26  LYS 26  32  32  LYS LYS C . n 
A 1 27  ASN 27  33  33  ASN ASN C . n 
A 1 28  VAL 28  34  34  VAL VAL C . n 
A 1 29  THR 29  35  35  THR THR C . n 
A 1 30  VAL 30  36  36  VAL VAL C . n 
A 1 31  THR 31  37  37  THR THR C . n 
A 1 32  HIS 32  38  38  HIS HIS C . n 
A 1 33  ALA 33  39  39  ALA ALA C . n 
A 1 34  GLN 34  40  40  GLN GLN C . n 
A 1 35  ASP 35  41  41  ASP ASP C . n 
A 1 36  ILE 36  42  42  ILE ILE C . n 
A 1 37  LEU 37  43  43  LEU LEU C . n 
A 1 38  GLU 38  44  44  GLU GLU C . n 
A 1 39  LYS 39  45  45  LYS LYS C . n 
A 1 40  THR 40  46  46  THR THR C . n 
A 1 41  HIS 41  47  47  HIS HIS C . n 
A 1 42  ASN 42  48  48  ASN ASN C . n 
A 1 43  GLY 43  49  49  GLY GLY C . n 
A 1 44  LYS 44  50  50  LYS LYS C . n 
A 1 45  LEU 45  51  51  LEU LEU C . n 
A 1 46  CYS 46  52  52  CYS CYS C . n 
A 1 47  ASN 47  53  53  ASN ASN C . n 
A 1 48  LEU 48  54  54  LEU LEU C . n 
A 1 49  ASP 49  55  55  ASP ASP C . n 
A 1 50  GLY 50  55  55  GLY GLY C A n 
A 1 51  VAL 51  56  56  VAL VAL C . n 
A 1 52  LYS 52  57  57  LYS LYS C . n 
A 1 53  PRO 53  58  58  PRO PRO C . n 
A 1 54  LEU 54  59  59  LEU LEU C . n 
A 1 55  ILE 55  60  60  ILE ILE C . n 
A 1 56  LEU 56  61  61  LEU LEU C . n 
A 1 57  ARG 57  62  62  ARG ARG C . n 
A 1 58  ASP 58  63  63  ASP ASP C . n 
A 1 59  CYS 59  64  64  CYS CYS C . n 
A 1 60  SER 60  65  65  SER SER C . n 
A 1 61  VAL 61  66  66  VAL VAL C . n 
A 1 62  ALA 62  67  67  ALA ALA C . n 
A 1 63  GLY 63  68  68  GLY GLY C . n 
A 1 64  TRP 64  69  69  TRP TRP C . n 
A 1 65  LEU 65  70  70  LEU LEU C . n 
A 1 66  LEU 66  71  71  LEU LEU C . n 
A 1 67  GLY 67  72  72  GLY GLY C . n 
A 1 68  ASN 68  73  73  ASN ASN C . n 
A 1 69  PRO 69  74  74  PRO PRO C . n 
A 1 70  MET 70  75  75  MET MET C . n 
A 1 71  CYS 71  76  76  CYS CYS C . n 
A 1 72  ASP 72  77  77  ASP ASP C . n 
A 1 73  GLU 73  78  78  GLU GLU C . n 
A 1 74  PHE 74  79  79  PHE PHE C . n 
A 1 75  LEU 75  80  80  LEU LEU C . n 
A 1 76  ASN 76  81  81  ASN ASN C . n 
A 1 77  VAL 77  82  82  VAL VAL C . n 
A 1 78  PRO 78  83  83  PRO PRO C . n 
A 1 79  GLU 79  83  83  GLU GLU C A n 
A 1 80  TRP 80  84  84  TRP TRP C . n 
A 1 81  SER 81  85  85  SER SER C . n 
A 1 82  TYR 82  86  86  TYR TYR C . n 
A 1 83  ILE 83  87  87  ILE ILE C . n 
A 1 84  VAL 84  88  88  VAL VAL C . n 
A 1 85  GLU 85  89  89  GLU GLU C . n 
A 1 86  LYS 86  90  90  LYS LYS C . n 
A 1 87  ILE 87  91  91  ILE ILE C . n 
A 1 88  ASN 88  92  92  ASN ASN C . n 
A 1 89  PRO 89  93  93  PRO PRO C . n 
A 1 90  ALA 90  94  94  ALA ALA C . n 
A 1 91  ASN 91  95  95  ASN ASN C . n 
A 1 92  ASP 92  96  96  ASP ASP C . n 
A 1 93  LEU 93  96  96  LEU LEU C A n 
A 1 94  CYS 94  97  97  CYS CYS C . n 
A 1 95  TYR 95  98  98  TYR TYR C . n 
A 1 96  PRO 96  99  99  PRO PRO C . n 
A 1 97  GLY 97  100 100 GLY GLY C . n 
A 1 98  ASN 98  101 101 ASN ASN C . n 
A 1 99  PHE 99  102 102 PHE PHE C . n 
A 1 100 ASN 100 103 103 ASN ASN C . n 
A 1 101 ASP 101 104 104 ASP ASP C . n 
A 1 102 TYR 102 105 105 TYR TYR C . n 
A 1 103 GLU 103 106 106 GLU GLU C . n 
A 1 104 GLU 104 107 107 GLU GLU C . n 
A 1 105 LEU 105 108 108 LEU LEU C . n 
A 1 106 LYS 106 109 109 LYS LYS C . n 
A 1 107 HIS 107 110 110 HIS HIS C . n 
A 1 108 LEU 108 111 111 LEU LEU C . n 
A 1 109 LEU 109 112 112 LEU LEU C . n 
A 1 110 SER 110 113 113 SER SER C . n 
A 1 111 ARG 111 114 114 ARG ARG C . n 
A 1 112 ILE 112 115 115 ILE ILE C . n 
A 1 113 ASN 113 116 116 ASN ASN C . n 
A 1 114 HIS 114 117 117 HIS HIS C . n 
A 1 115 PHE 115 118 118 PHE PHE C . n 
A 1 116 GLU 116 119 119 GLU GLU C . n 
A 1 117 LYS 117 120 120 LYS LYS C . n 
A 1 118 ILE 118 121 121 ILE ILE C . n 
A 1 119 GLN 119 122 122 GLN GLN C . n 
A 1 120 ILE 120 123 123 ILE ILE C . n 
A 1 121 THR 121 124 124 THR THR C . n 
A 1 122 PRO 122 125 125 PRO PRO C . n 
A 1 123 LYS 123 125 125 LYS LYS C A n 
A 1 124 ASN 124 125 125 ASN ASN C B n 
A 1 125 SER 125 126 126 SER SER C . n 
A 1 126 TRP 126 127 127 TRP TRP C . n 
A 1 127 SER 127 128 128 SER SER C . n 
A 1 128 ASP 128 129 129 ASP ASP C . n 
A 1 129 HIS 129 130 130 HIS HIS C . n 
A 1 130 GLU 130 131 131 GLU GLU C . n 
A 1 131 ALA 131 132 132 ALA ALA C . n 
A 1 132 SER 132 133 133 SER SER C . n 
A 1 133 GLY 133 134 134 GLY GLY C . n 
A 1 134 VAL 134 135 135 VAL VAL C . n 
A 1 135 SER 135 136 136 SER SER C . n 
A 1 136 SER 136 137 137 SER SER C . n 
A 1 137 ALA 137 138 138 ALA ALA C . n 
A 1 138 CYS 138 139 139 CYS CYS C . n 
A 1 139 PRO 139 140 140 PRO PRO C . n 
A 1 140 TYR 140 141 141 TYR TYR C . n 
A 1 141 GLN 141 142 142 GLN GLN C . n 
A 1 142 GLY 142 143 143 GLY GLY C . n 
A 1 143 ARG 143 144 144 ARG ARG C . n 
A 1 144 SER 144 145 145 SER SER C . n 
A 1 145 SER 145 146 146 SER SER C . n 
A 1 146 PHE 146 147 147 PHE PHE C . n 
A 1 147 PHE 147 148 148 PHE PHE C . n 
A 1 148 ARG 148 149 149 ARG ARG C . n 
A 1 149 ASN 149 150 150 ASN ASN C . n 
A 1 150 VAL 150 151 151 VAL VAL C . n 
A 1 151 VAL 151 152 152 VAL VAL C . n 
A 1 152 TRP 152 153 153 TRP TRP C . n 
A 1 153 LEU 153 154 154 LEU LEU C . n 
A 1 154 THR 154 155 155 THR THR C . n 
A 1 155 LYS 155 156 156 LYS LYS C . n 
A 1 156 LYS 156 157 157 LYS LYS C . n 
A 1 157 ASP 157 158 158 ASP ASP C . n 
A 1 158 ASN 158 159 159 ASN ASN C . n 
A 1 159 ALA 159 160 160 ALA ALA C . n 
A 1 160 TYR 160 161 161 TYR TYR C . n 
A 1 161 PRO 161 162 162 PRO PRO C . n 
A 1 162 THR 162 163 163 THR THR C . n 
A 1 163 ILE 163 164 164 ILE ILE C . n 
A 1 164 LYS 164 165 165 LYS LYS C . n 
A 1 165 ARG 165 166 166 ARG ARG C . n 
A 1 166 SER 166 167 167 SER SER C . n 
A 1 167 TYR 167 168 168 TYR TYR C . n 
A 1 168 ASN 168 169 169 ASN ASN C . n 
A 1 169 ASN 169 170 170 ASN ASN C . n 
A 1 170 THR 170 171 171 THR THR C . n 
A 1 171 ASN 171 172 172 ASN ASN C . n 
A 1 172 GLN 172 173 173 GLN GLN C . n 
A 1 173 GLU 173 174 174 GLU GLU C . n 
A 1 174 ASP 174 175 175 ASP ASP C . n 
A 1 175 LEU 175 176 176 LEU LEU C . n 
A 1 176 LEU 176 177 177 LEU LEU C . n 
A 1 177 VAL 177 178 178 VAL VAL C . n 
A 1 178 LEU 178 179 179 LEU LEU C . n 
A 1 179 TRP 179 180 180 TRP TRP C . n 
A 1 180 GLY 180 181 181 GLY GLY C . n 
A 1 181 ILE 181 182 182 ILE ILE C . n 
A 1 182 HIS 182 183 183 HIS HIS C . n 
A 1 183 HIS 183 184 184 HIS HIS C . n 
A 1 184 PRO 184 185 185 PRO PRO C . n 
A 1 185 ASN 185 186 186 ASN ASN C . n 
A 1 186 ASP 186 187 187 ASP ASP C . n 
A 1 187 ALA 187 188 188 ALA ALA C . n 
A 1 188 THR 188 189 189 THR THR C . n 
A 1 189 GLU 189 190 190 GLU GLU C . n 
A 1 190 GLN 190 191 191 GLN GLN C . n 
A 1 191 THR 191 192 192 THR THR C . n 
A 1 192 ARG 192 193 193 ARG ARG C . n 
A 1 193 LEU 193 194 194 LEU LEU C . n 
A 1 194 TYR 194 195 195 TYR TYR C . n 
A 1 195 GLN 195 196 196 GLN GLN C . n 
A 1 196 ASN 196 197 197 ASN ASN C . n 
A 1 197 PRO 197 198 198 PRO PRO C . n 
A 1 198 THR 198 199 199 THR THR C . n 
A 1 199 THR 199 200 200 THR THR C . n 
A 1 200 TYR 200 201 201 TYR TYR C . n 
A 1 201 ILE 201 202 202 ILE ILE C . n 
A 1 202 SER 202 203 203 SER SER C . n 
A 1 203 VAL 203 204 204 VAL VAL C . n 
A 1 204 GLY 204 205 205 GLY GLY C . n 
A 1 205 THR 205 206 206 THR THR C . n 
A 1 206 SER 206 207 207 SER SER C . n 
A 1 207 THR 207 208 208 THR THR C . n 
A 1 208 LEU 208 209 209 LEU LEU C . n 
A 1 209 ASN 209 210 210 ASN ASN C . n 
A 1 210 GLN 210 211 211 GLN GLN C . n 
A 1 211 LYS 211 212 212 LYS LYS C . n 
A 1 212 LEU 212 213 213 LEU LEU C . n 
A 1 213 VAL 213 214 214 VAL VAL C . n 
A 1 214 PRO 214 215 215 PRO PRO C . n 
A 1 215 LYS 215 216 216 LYS LYS C . n 
A 1 216 ILE 216 217 217 ILE ILE C . n 
A 1 217 ALA 217 218 218 ALA ALA C . n 
A 1 218 THR 218 219 219 THR THR C . n 
A 1 219 ARG 219 220 220 ARG ARG C . n 
A 1 220 SER 220 221 221 SER SER C . n 
A 1 221 LYS 221 222 222 LYS LYS C . n 
A 1 222 VAL 222 223 223 VAL VAL C . n 
A 1 223 LYS 223 224 224 LYS LYS C . n 
A 1 224 GLY 224 225 225 GLY GLY C . n 
A 1 225 LEU 225 226 226 LEU LEU C . n 
A 1 226 SER 226 227 227 SER SER C . n 
A 1 227 GLY 227 228 228 GLY GLY C . n 
A 1 228 ARG 228 229 229 ARG ARG C . n 
A 1 229 MET 229 230 230 MET MET C . n 
A 1 230 GLU 230 231 231 GLU GLU C . n 
A 1 231 PHE 231 232 232 PHE PHE C . n 
A 1 232 PHE 232 233 233 PHE PHE C . n 
A 1 233 TRP 233 234 234 TRP TRP C . n 
A 1 234 THR 234 235 235 THR THR C . n 
A 1 235 ILE 235 236 236 ILE ILE C . n 
A 1 236 LEU 236 237 237 LEU LEU C . n 
A 1 237 LYS 237 238 238 LYS LYS C . n 
A 1 238 SER 238 239 239 SER SER C . n 
A 1 239 ASN 239 240 240 ASN ASN C . n 
A 1 240 ASP 240 241 241 ASP ASP C . n 
A 1 241 ALA 241 242 242 ALA ALA C . n 
A 1 242 ILE 242 243 243 ILE ILE C . n 
A 1 243 ASN 243 244 244 ASN ASN C . n 
A 1 244 PHE 244 245 245 PHE PHE C . n 
A 1 245 GLU 245 246 246 GLU GLU C . n 
A 1 246 SER 246 247 247 SER SER C . n 
A 1 247 ASN 247 248 248 ASN ASN C . n 
A 1 248 GLY 248 249 249 GLY GLY C . n 
A 1 249 ASN 249 250 250 ASN ASN C . n 
A 1 250 PHE 250 251 251 PHE PHE C . n 
A 1 251 ILE 251 252 252 ILE ILE C . n 
A 1 252 ALA 252 253 253 ALA ALA C . n 
A 1 253 PRO 253 254 254 PRO PRO C . n 
A 1 254 GLU 254 255 255 GLU GLU C . n 
A 1 255 ASN 255 256 256 ASN ASN C . n 
A 1 256 ALA 256 257 257 ALA ALA C . n 
A 1 257 TYR 257 258 258 TYR TYR C . n 
A 1 258 LYS 258 259 259 LYS LYS C . n 
A 1 259 ILE 259 260 260 ILE ILE C . n 
A 1 260 VAL 260 260 260 VAL VAL C A n 
A 1 261 LYS 261 261 261 LYS LYS C . n 
A 1 262 LYS 262 262 262 LYS LYS C . n 
A 1 263 GLY 263 263 263 GLY GLY C . n 
A 1 264 ASP 264 264 264 ASP ASP C . n 
A 1 265 SER 265 265 265 SER SER C . n 
A 1 266 THR 266 266 266 THR THR C . n 
A 1 267 ILE 267 267 267 ILE ILE C . n 
A 1 268 MET 268 268 268 MET MET C . n 
A 1 269 LYS 269 269 269 LYS LYS C . n 
A 1 270 SER 270 270 270 SER SER C . n 
A 1 271 GLU 271 271 271 GLU GLU C . n 
A 1 272 LEU 272 272 272 LEU LEU C . n 
A 1 273 GLU 273 273 273 GLU GLU C . n 
A 1 274 TYR 274 274 274 TYR TYR C . n 
A 1 275 GLY 275 275 275 GLY GLY C . n 
A 1 276 ASP 276 276 276 ASP ASP C . n 
A 1 277 CYS 277 277 277 CYS CYS C . n 
A 1 278 ASN 278 278 278 ASN ASN C . n 
A 1 279 THR 279 279 279 THR THR C . n 
A 1 280 LYS 280 280 280 LYS LYS C . n 
A 1 281 CYS 281 281 281 CYS CYS C . n 
A 1 282 GLN 282 282 282 GLN GLN C . n 
A 1 283 THR 283 283 283 THR THR C . n 
A 1 284 PRO 284 284 284 PRO PRO C . n 
A 1 285 ILE 285 285 285 ILE ILE C . n 
A 1 286 GLY 286 286 286 GLY GLY C . n 
A 1 287 ALA 287 287 287 ALA ALA C . n 
A 1 288 ILE 288 288 288 ILE ILE C . n 
A 1 289 ASN 289 289 289 ASN ASN C . n 
A 1 290 SER 290 290 290 SER SER C . n 
A 1 291 SER 291 291 291 SER SER C . n 
A 1 292 MET 292 292 292 MET MET C . n 
A 1 293 PRO 293 293 293 PRO PRO C . n 
A 1 294 PHE 294 294 294 PHE PHE C . n 
A 1 295 HIS 295 295 295 HIS HIS C . n 
A 1 296 ASN 296 296 296 ASN ASN C . n 
A 1 297 ILE 297 297 297 ILE ILE C . n 
A 1 298 HIS 298 298 298 HIS HIS C . n 
A 1 299 PRO 299 299 299 PRO PRO C . n 
A 1 300 LEU 300 300 300 LEU LEU C . n 
A 1 301 THR 301 301 301 THR THR C . n 
A 1 302 ILE 302 302 302 ILE ILE C . n 
A 1 303 GLY 303 303 303 GLY GLY C . n 
A 1 304 GLU 304 304 304 GLU GLU C . n 
A 1 305 CYS 305 305 305 CYS CYS C . n 
A 1 306 PRO 306 306 306 PRO PRO C . n 
A 1 307 LYS 307 307 307 LYS LYS C . n 
A 1 308 TYR 308 308 308 TYR TYR C . n 
A 1 309 VAL 309 309 309 VAL VAL C . n 
A 1 310 LYS 310 310 310 LYS LYS C . n 
A 1 311 SER 311 311 311 SER SER C . n 
A 1 312 ASN 312 312 312 ASN ASN C . n 
A 1 313 ARG 313 313 313 ARG ARG C . n 
A 1 314 LEU 314 314 314 LEU LEU C . n 
A 1 315 VAL 315 315 315 VAL VAL C . n 
A 1 316 LEU 316 316 316 LEU LEU C . n 
A 1 317 ALA 317 317 317 ALA ALA C . n 
A 1 318 THR 318 318 318 THR THR C . n 
A 1 319 GLY 319 319 319 GLY GLY C . n 
A 1 320 LEU 320 320 320 LEU LEU C . n 
A 1 321 ARG 321 321 321 ARG ARG C . n 
A 1 322 ASN 322 322 322 ASN ASN C . n 
A 1 323 SER 323 323 323 SER SER C . n 
A 1 324 PRO 324 324 324 PRO PRO C . n 
A 1 325 GLN 325 325 ?   ?   ?   C . n 
A 1 326 GLY 326 326 ?   ?   ?   C . n 
A 1 327 GLU 327 327 ?   ?   ?   C . n 
A 1 328 ARG 328 328 ?   ?   ?   C . n 
A 1 329 ARG 329 329 ?   ?   ?   C . n 
A 1 330 ARG 330 330 ?   ?   ?   C . n 
A 1 331 LYS 331 331 ?   ?   ?   C . n 
A 1 332 LYS 332 332 ?   ?   ?   C . n 
A 1 333 ARG 333 333 ?   ?   ?   C . n 
B 2 1   GLY 1   1   1   GLY GLY D . n 
B 2 2   LEU 2   2   2   LEU LEU D . n 
B 2 3   PHE 3   3   3   PHE PHE D . n 
B 2 4   GLY 4   4   4   GLY GLY D . n 
B 2 5   ALA 5   5   5   ALA ALA D . n 
B 2 6   ILE 6   6   6   ILE ILE D . n 
B 2 7   ALA 7   7   7   ALA ALA D . n 
B 2 8   GLY 8   8   8   GLY GLY D . n 
B 2 9   PHE 9   9   9   PHE PHE D . n 
B 2 10  ILE 10  10  10  ILE ILE D . n 
B 2 11  GLU 11  11  11  GLU GLU D . n 
B 2 12  GLY 12  12  12  GLY GLY D . n 
B 2 13  GLY 13  13  13  GLY GLY D . n 
B 2 14  TRP 14  14  14  TRP TRP D . n 
B 2 15  GLN 15  15  15  GLN GLN D . n 
B 2 16  GLY 16  16  16  GLY GLY D . n 
B 2 17  MET 17  17  17  MET MET D . n 
B 2 18  VAL 18  18  18  VAL VAL D . n 
B 2 19  ASP 19  19  19  ASP ASP D . n 
B 2 20  GLY 20  20  20  GLY GLY D . n 
B 2 21  TRP 21  21  21  TRP TRP D . n 
B 2 22  TYR 22  22  22  TYR TYR D . n 
B 2 23  GLY 23  23  23  GLY GLY D . n 
B 2 24  TYR 24  24  24  TYR TYR D . n 
B 2 25  HIS 25  25  25  HIS HIS D . n 
B 2 26  HIS 26  26  26  HIS HIS D . n 
B 2 27  SER 27  27  27  SER SER D . n 
B 2 28  ASN 28  28  28  ASN ASN D . n 
B 2 29  GLU 29  29  29  GLU GLU D . n 
B 2 30  GLN 30  30  30  GLN GLN D . n 
B 2 31  GLY 31  31  31  GLY GLY D . n 
B 2 32  SER 32  32  32  SER SER D . n 
B 2 33  GLY 33  33  33  GLY GLY D . n 
B 2 34  TYR 34  34  34  TYR TYR D . n 
B 2 35  ALA 35  35  35  ALA ALA D . n 
B 2 36  ALA 36  36  36  ALA ALA D . n 
B 2 37  ASP 37  37  37  ASP ASP D . n 
B 2 38  LYS 38  38  38  LYS LYS D . n 
B 2 39  GLU 39  39  39  GLU GLU D . n 
B 2 40  SER 40  40  40  SER SER D . n 
B 2 41  THR 41  41  41  THR THR D . n 
B 2 42  GLN 42  42  42  GLN GLN D . n 
B 2 43  LYS 43  43  43  LYS LYS D . n 
B 2 44  ALA 44  44  44  ALA ALA D . n 
B 2 45  ILE 45  45  45  ILE ILE D . n 
B 2 46  ASP 46  46  46  ASP ASP D . n 
B 2 47  GLY 47  47  47  GLY GLY D . n 
B 2 48  VAL 48  48  48  VAL VAL D . n 
B 2 49  THR 49  49  49  THR THR D . n 
B 2 50  ASN 50  50  50  ASN ASN D . n 
B 2 51  LYS 51  51  51  LYS LYS D . n 
B 2 52  VAL 52  52  52  VAL VAL D . n 
B 2 53  ASN 53  53  53  ASN ASN D . n 
B 2 54  SER 54  54  54  SER SER D . n 
B 2 55  ILE 55  55  55  ILE ILE D . n 
B 2 56  ILE 56  56  56  ILE ILE D . n 
B 2 57  ASP 57  57  57  ASP ASP D . n 
B 2 58  LYS 58  58  58  LYS LYS D . n 
B 2 59  MET 59  59  59  MET MET D . n 
B 2 60  ASN 60  60  60  ASN ASN D . n 
B 2 61  THR 61  61  61  THR THR D . n 
B 2 62  GLN 62  62  62  GLN GLN D . n 
B 2 63  PHE 63  63  63  PHE PHE D . n 
B 2 64  GLU 64  64  64  GLU GLU D . n 
B 2 65  ALA 65  65  65  ALA ALA D . n 
B 2 66  VAL 66  66  66  VAL VAL D . n 
B 2 67  GLY 67  67  67  GLY GLY D . n 
B 2 68  ARG 68  68  68  ARG ARG D . n 
B 2 69  GLU 69  69  69  GLU GLU D . n 
B 2 70  PHE 70  70  70  PHE PHE D . n 
B 2 71  ASN 71  71  71  ASN ASN D . n 
B 2 72  ASN 72  72  72  ASN ASN D . n 
B 2 73  LEU 73  73  73  LEU LEU D . n 
B 2 74  GLU 74  74  74  GLU GLU D . n 
B 2 75  ARG 75  75  75  ARG ARG D . n 
B 2 76  ARG 76  76  76  ARG ARG D . n 
B 2 77  ILE 77  77  77  ILE ILE D . n 
B 2 78  GLU 78  78  78  GLU GLU D . n 
B 2 79  ASN 79  79  79  ASN ASN D . n 
B 2 80  LEU 80  80  80  LEU LEU D . n 
B 2 81  ASN 81  81  81  ASN ASN D . n 
B 2 82  LYS 82  82  82  LYS LYS D . n 
B 2 83  LYS 83  83  83  LYS LYS D . n 
B 2 84  MET 84  84  84  MET MET D . n 
B 2 85  GLU 85  85  85  GLU GLU D . n 
B 2 86  ASP 86  86  86  ASP ASP D . n 
B 2 87  GLY 87  87  87  GLY GLY D . n 
B 2 88  PHE 88  88  88  PHE PHE D . n 
B 2 89  LEU 89  89  89  LEU LEU D . n 
B 2 90  ASP 90  90  90  ASP ASP D . n 
B 2 91  VAL 91  91  91  VAL VAL D . n 
B 2 92  TRP 92  92  92  TRP TRP D . n 
B 2 93  THR 93  93  93  THR THR D . n 
B 2 94  TYR 94  94  94  TYR TYR D . n 
B 2 95  ASN 95  95  95  ASN ASN D . n 
B 2 96  ALA 96  96  96  ALA ALA D . n 
B 2 97  GLU 97  97  97  GLU GLU D . n 
B 2 98  LEU 98  98  98  LEU LEU D . n 
B 2 99  LEU 99  99  99  LEU LEU D . n 
B 2 100 VAL 100 100 100 VAL VAL D . n 
B 2 101 LEU 101 101 101 LEU LEU D . n 
B 2 102 MET 102 102 102 MET MET D . n 
B 2 103 GLU 103 103 103 GLU GLU D . n 
B 2 104 ASN 104 104 104 ASN ASN D . n 
B 2 105 GLU 105 105 105 GLU GLU D . n 
B 2 106 ARG 106 106 106 ARG ARG D . n 
B 2 107 THR 107 107 107 THR THR D . n 
B 2 108 LEU 108 108 108 LEU LEU D . n 
B 2 109 ASP 109 109 109 ASP ASP D . n 
B 2 110 PHE 110 110 110 PHE PHE D . n 
B 2 111 HIS 111 111 111 HIS HIS D . n 
B 2 112 ASP 112 112 112 ASP ASP D . n 
B 2 113 SER 113 113 113 SER SER D . n 
B 2 114 ASN 114 114 114 ASN ASN D . n 
B 2 115 VAL 115 115 115 VAL VAL D . n 
B 2 116 LYS 116 116 116 LYS LYS D . n 
B 2 117 ASN 117 117 117 ASN ASN D . n 
B 2 118 LEU 118 118 118 LEU LEU D . n 
B 2 119 TYR 119 119 119 TYR TYR D . n 
B 2 120 ASP 120 120 120 ASP ASP D . n 
B 2 121 LYS 121 121 121 LYS LYS D . n 
B 2 122 VAL 122 122 122 VAL VAL D . n 
B 2 123 ARG 123 123 123 ARG ARG D . n 
B 2 124 LEU 124 124 124 LEU LEU D . n 
B 2 125 GLN 125 125 125 GLN GLN D . n 
B 2 126 LEU 126 126 126 LEU LEU D . n 
B 2 127 ARG 127 127 127 ARG ARG D . n 
B 2 128 ASP 128 128 128 ASP ASP D . n 
B 2 129 ASN 129 129 129 ASN ASN D . n 
B 2 130 ALA 130 130 130 ALA ALA D . n 
B 2 131 LYS 131 131 131 LYS LYS D . n 
B 2 132 GLU 132 132 132 GLU GLU D . n 
B 2 133 LEU 133 133 133 LEU LEU D . n 
B 2 134 GLY 134 134 134 GLY GLY D . n 
B 2 135 ASN 135 135 135 ASN ASN D . n 
B 2 136 GLY 136 136 136 GLY GLY D . n 
B 2 137 CYS 137 137 137 CYS CYS D . n 
B 2 138 PHE 138 138 138 PHE PHE D . n 
B 2 139 GLU 139 139 139 GLU GLU D . n 
B 2 140 PHE 140 140 140 PHE PHE D . n 
B 2 141 TYR 141 141 141 TYR TYR D . n 
B 2 142 HIS 142 142 142 HIS HIS D . n 
B 2 143 ARG 143 143 143 ARG ARG D . n 
B 2 144 CYS 144 144 144 CYS CYS D . n 
B 2 145 ASP 145 145 145 ASP ASP D . n 
B 2 146 ASN 146 146 146 ASN ASN D . n 
B 2 147 GLU 147 147 147 GLU GLU D . n 
B 2 148 CYS 148 148 148 CYS CYS D . n 
B 2 149 MET 149 149 149 MET MET D . n 
B 2 150 GLU 150 150 150 GLU GLU D . n 
B 2 151 SER 151 151 151 SER SER D . n 
B 2 152 VAL 152 152 152 VAL VAL D . n 
B 2 153 ARG 153 153 153 ARG ARG D . n 
B 2 154 ASN 154 154 154 ASN ASN D . n 
B 2 155 GLY 155 155 155 GLY GLY D . n 
B 2 156 THR 156 156 156 THR THR D . n 
B 2 157 TYR 157 157 157 TYR TYR D . n 
B 2 158 ASP 158 158 158 ASP ASP D . n 
B 2 159 TYR 159 159 159 TYR TYR D . n 
B 2 160 PRO 160 160 160 PRO PRO D . n 
B 2 161 GLN 161 161 161 GLN GLN D . n 
B 2 162 TYR 162 162 162 TYR TYR D . n 
B 2 163 SER 163 163 163 SER SER D . n 
B 2 164 GLU 164 164 164 GLU GLU D . n 
B 2 165 GLU 165 165 165 GLU GLU D . n 
B 2 166 ALA 166 166 166 ALA ALA D . n 
B 2 167 ARG 167 167 167 ARG ARG D . n 
B 2 168 LEU 168 168 168 LEU LEU D . n 
B 2 169 LYS 169 169 169 LYS LYS D . n 
B 2 170 ARG 170 170 170 ARG ARG D . n 
B 2 171 GLU 171 171 171 GLU GLU D . n 
B 2 172 GLU 172 172 172 GLU GLU D . n 
B 2 173 ILE 173 173 173 ILE ILE D . n 
B 2 174 SER 174 174 174 SER SER D . n 
B 2 175 GLY 175 175 175 GLY GLY D . n 
B 2 176 ARG 176 176 ?   ?   ?   D . n 
B 2 177 LEU 177 177 ?   ?   ?   D . n 
B 2 178 VAL 178 178 ?   ?   ?   D . n 
B 2 179 PRO 179 179 ?   ?   ?   D . n 
B 2 180 ARG 180 180 ?   ?   ?   D . n 
C 1 1   ALA 1   7   ?   ?   ?   A . n 
C 1 2   ASP 2   8   8   ASP ASP A . n 
C 1 3   PRO 3   9   9   PRO PRO A . n 
C 1 4   GLY 4   10  10  GLY GLY A . n 
C 1 5   ASP 5   11  11  ASP ASP A . n 
C 1 6   GLN 6   12  12  GLN GLN A . n 
C 1 7   ILE 7   13  13  ILE ILE A . n 
C 1 8   CYS 8   14  14  CYS CYS A . n 
C 1 9   ILE 9   15  15  ILE ILE A . n 
C 1 10  GLY 10  16  16  GLY GLY A . n 
C 1 11  TYR 11  17  17  TYR TYR A . n 
C 1 12  HIS 12  18  18  HIS HIS A . n 
C 1 13  ALA 13  19  19  ALA ALA A . n 
C 1 14  ASN 14  20  20  ASN ASN A . n 
C 1 15  ASN 15  21  21  ASN ASN A . n 
C 1 16  SER 16  22  22  SER SER A . n 
C 1 17  THR 17  23  23  THR THR A . n 
C 1 18  GLU 18  24  24  GLU GLU A . n 
C 1 19  GLN 19  25  25  GLN GLN A . n 
C 1 20  VAL 20  26  26  VAL VAL A . n 
C 1 21  ASP 21  27  27  ASP ASP A . n 
C 1 22  THR 22  28  28  THR THR A . n 
C 1 23  ILE 23  29  29  ILE ILE A . n 
C 1 24  MET 24  30  30  MET MET A . n 
C 1 25  GLU 25  31  31  GLU GLU A . n 
C 1 26  LYS 26  32  32  LYS LYS A . n 
C 1 27  ASN 27  33  33  ASN ASN A . n 
C 1 28  VAL 28  34  34  VAL VAL A . n 
C 1 29  THR 29  35  35  THR THR A . n 
C 1 30  VAL 30  36  36  VAL VAL A . n 
C 1 31  THR 31  37  37  THR THR A . n 
C 1 32  HIS 32  38  38  HIS HIS A . n 
C 1 33  ALA 33  39  39  ALA ALA A . n 
C 1 34  GLN 34  40  40  GLN GLN A . n 
C 1 35  ASP 35  41  41  ASP ASP A . n 
C 1 36  ILE 36  42  42  ILE ILE A . n 
C 1 37  LEU 37  43  43  LEU LEU A . n 
C 1 38  GLU 38  44  44  GLU GLU A . n 
C 1 39  LYS 39  45  45  LYS LYS A . n 
C 1 40  THR 40  46  46  THR THR A . n 
C 1 41  HIS 41  47  47  HIS HIS A . n 
C 1 42  ASN 42  48  48  ASN ASN A . n 
C 1 43  GLY 43  49  49  GLY GLY A . n 
C 1 44  LYS 44  50  50  LYS LYS A . n 
C 1 45  LEU 45  51  51  LEU LEU A . n 
C 1 46  CYS 46  52  52  CYS CYS A . n 
C 1 47  ASN 47  53  53  ASN ASN A . n 
C 1 48  LEU 48  54  54  LEU LEU A . n 
C 1 49  ASP 49  55  55  ASP ASP A . n 
C 1 50  GLY 50  55  55  GLY GLY A A n 
C 1 51  VAL 51  56  56  VAL VAL A . n 
C 1 52  LYS 52  57  57  LYS LYS A . n 
C 1 53  PRO 53  58  58  PRO PRO A . n 
C 1 54  LEU 54  59  59  LEU LEU A . n 
C 1 55  ILE 55  60  60  ILE ILE A . n 
C 1 56  LEU 56  61  61  LEU LEU A . n 
C 1 57  ARG 57  62  62  ARG ARG A . n 
C 1 58  ASP 58  63  63  ASP ASP A . n 
C 1 59  CYS 59  64  64  CYS CYS A . n 
C 1 60  SER 60  65  65  SER SER A . n 
C 1 61  VAL 61  66  66  VAL VAL A . n 
C 1 62  ALA 62  67  67  ALA ALA A . n 
C 1 63  GLY 63  68  68  GLY GLY A . n 
C 1 64  TRP 64  69  69  TRP TRP A . n 
C 1 65  LEU 65  70  70  LEU LEU A . n 
C 1 66  LEU 66  71  71  LEU LEU A . n 
C 1 67  GLY 67  72  72  GLY GLY A . n 
C 1 68  ASN 68  73  73  ASN ASN A . n 
C 1 69  PRO 69  74  74  PRO PRO A . n 
C 1 70  MET 70  75  75  MET MET A . n 
C 1 71  CYS 71  76  76  CYS CYS A . n 
C 1 72  ASP 72  77  77  ASP ASP A . n 
C 1 73  GLU 73  78  78  GLU GLU A . n 
C 1 74  PHE 74  79  79  PHE PHE A . n 
C 1 75  LEU 75  80  80  LEU LEU A . n 
C 1 76  ASN 76  81  81  ASN ASN A . n 
C 1 77  VAL 77  82  82  VAL VAL A . n 
C 1 78  PRO 78  83  83  PRO PRO A . n 
C 1 79  GLU 79  83  83  GLU GLU A A n 
C 1 80  TRP 80  84  84  TRP TRP A . n 
C 1 81  SER 81  85  85  SER SER A . n 
C 1 82  TYR 82  86  86  TYR TYR A . n 
C 1 83  ILE 83  87  87  ILE ILE A . n 
C 1 84  VAL 84  88  88  VAL VAL A . n 
C 1 85  GLU 85  89  89  GLU GLU A . n 
C 1 86  LYS 86  90  90  LYS LYS A . n 
C 1 87  ILE 87  91  91  ILE ILE A . n 
C 1 88  ASN 88  92  92  ASN ASN A . n 
C 1 89  PRO 89  93  93  PRO PRO A . n 
C 1 90  ALA 90  94  94  ALA ALA A . n 
C 1 91  ASN 91  95  95  ASN ASN A . n 
C 1 92  ASP 92  96  96  ASP ASP A . n 
C 1 93  LEU 93  96  96  LEU LEU A A n 
C 1 94  CYS 94  97  97  CYS CYS A . n 
C 1 95  TYR 95  98  98  TYR TYR A . n 
C 1 96  PRO 96  99  99  PRO PRO A . n 
C 1 97  GLY 97  100 100 GLY GLY A . n 
C 1 98  ASN 98  101 101 ASN ASN A . n 
C 1 99  PHE 99  102 102 PHE PHE A . n 
C 1 100 ASN 100 103 103 ASN ASN A . n 
C 1 101 ASP 101 104 104 ASP ASP A . n 
C 1 102 TYR 102 105 105 TYR TYR A . n 
C 1 103 GLU 103 106 106 GLU GLU A . n 
C 1 104 GLU 104 107 107 GLU GLU A . n 
C 1 105 LEU 105 108 108 LEU LEU A . n 
C 1 106 LYS 106 109 109 LYS LYS A . n 
C 1 107 HIS 107 110 110 HIS HIS A . n 
C 1 108 LEU 108 111 111 LEU LEU A . n 
C 1 109 LEU 109 112 112 LEU LEU A . n 
C 1 110 SER 110 113 113 SER SER A . n 
C 1 111 ARG 111 114 114 ARG ARG A . n 
C 1 112 ILE 112 115 115 ILE ILE A . n 
C 1 113 ASN 113 116 116 ASN ASN A . n 
C 1 114 HIS 114 117 117 HIS HIS A . n 
C 1 115 PHE 115 118 118 PHE PHE A . n 
C 1 116 GLU 116 119 119 GLU GLU A . n 
C 1 117 LYS 117 120 120 LYS LYS A . n 
C 1 118 ILE 118 121 121 ILE ILE A . n 
C 1 119 GLN 119 122 122 GLN GLN A . n 
C 1 120 ILE 120 123 123 ILE ILE A . n 
C 1 121 THR 121 124 124 THR THR A . n 
C 1 122 PRO 122 125 125 PRO PRO A . n 
C 1 123 LYS 123 125 125 LYS LYS A A n 
C 1 124 ASN 124 125 125 ASN ASN A B n 
C 1 125 SER 125 126 126 SER SER A . n 
C 1 126 TRP 126 127 127 TRP TRP A . n 
C 1 127 SER 127 128 128 SER SER A . n 
C 1 128 ASP 128 129 129 ASP ASP A . n 
C 1 129 HIS 129 130 130 HIS HIS A . n 
C 1 130 GLU 130 131 131 GLU GLU A . n 
C 1 131 ALA 131 132 132 ALA ALA A . n 
C 1 132 SER 132 133 133 SER SER A . n 
C 1 133 GLY 133 134 134 GLY GLY A . n 
C 1 134 VAL 134 135 135 VAL VAL A . n 
C 1 135 SER 135 136 136 SER SER A . n 
C 1 136 SER 136 137 137 SER SER A . n 
C 1 137 ALA 137 138 138 ALA ALA A . n 
C 1 138 CYS 138 139 139 CYS CYS A . n 
C 1 139 PRO 139 140 140 PRO PRO A . n 
C 1 140 TYR 140 141 141 TYR TYR A . n 
C 1 141 GLN 141 142 142 GLN GLN A . n 
C 1 142 GLY 142 143 143 GLY GLY A . n 
C 1 143 ARG 143 144 144 ARG ARG A . n 
C 1 144 SER 144 145 145 SER SER A . n 
C 1 145 SER 145 146 146 SER SER A . n 
C 1 146 PHE 146 147 147 PHE PHE A . n 
C 1 147 PHE 147 148 148 PHE PHE A . n 
C 1 148 ARG 148 149 149 ARG ARG A . n 
C 1 149 ASN 149 150 150 ASN ASN A . n 
C 1 150 VAL 150 151 151 VAL VAL A . n 
C 1 151 VAL 151 152 152 VAL VAL A . n 
C 1 152 TRP 152 153 153 TRP TRP A . n 
C 1 153 LEU 153 154 154 LEU LEU A . n 
C 1 154 THR 154 155 155 THR THR A . n 
C 1 155 LYS 155 156 156 LYS LYS A . n 
C 1 156 LYS 156 157 157 LYS LYS A . n 
C 1 157 ASP 157 158 158 ASP ASP A . n 
C 1 158 ASN 158 159 159 ASN ASN A . n 
C 1 159 ALA 159 160 160 ALA ALA A . n 
C 1 160 TYR 160 161 161 TYR TYR A . n 
C 1 161 PRO 161 162 162 PRO PRO A . n 
C 1 162 THR 162 163 163 THR THR A . n 
C 1 163 ILE 163 164 164 ILE ILE A . n 
C 1 164 LYS 164 165 165 LYS LYS A . n 
C 1 165 ARG 165 166 166 ARG ARG A . n 
C 1 166 SER 166 167 167 SER SER A . n 
C 1 167 TYR 167 168 168 TYR TYR A . n 
C 1 168 ASN 168 169 169 ASN ASN A . n 
C 1 169 ASN 169 170 170 ASN ASN A . n 
C 1 170 THR 170 171 171 THR THR A . n 
C 1 171 ASN 171 172 172 ASN ASN A . n 
C 1 172 GLN 172 173 173 GLN GLN A . n 
C 1 173 GLU 173 174 174 GLU GLU A . n 
C 1 174 ASP 174 175 175 ASP ASP A . n 
C 1 175 LEU 175 176 176 LEU LEU A . n 
C 1 176 LEU 176 177 177 LEU LEU A . n 
C 1 177 VAL 177 178 178 VAL VAL A . n 
C 1 178 LEU 178 179 179 LEU LEU A . n 
C 1 179 TRP 179 180 180 TRP TRP A . n 
C 1 180 GLY 180 181 181 GLY GLY A . n 
C 1 181 ILE 181 182 182 ILE ILE A . n 
C 1 182 HIS 182 183 183 HIS HIS A . n 
C 1 183 HIS 183 184 184 HIS HIS A . n 
C 1 184 PRO 184 185 185 PRO PRO A . n 
C 1 185 ASN 185 186 186 ASN ASN A . n 
C 1 186 ASP 186 187 187 ASP ASP A . n 
C 1 187 ALA 187 188 188 ALA ALA A . n 
C 1 188 THR 188 189 189 THR THR A . n 
C 1 189 GLU 189 190 190 GLU GLU A . n 
C 1 190 GLN 190 191 191 GLN GLN A . n 
C 1 191 THR 191 192 192 THR THR A . n 
C 1 192 ARG 192 193 193 ARG ARG A . n 
C 1 193 LEU 193 194 194 LEU LEU A . n 
C 1 194 TYR 194 195 195 TYR TYR A . n 
C 1 195 GLN 195 196 196 GLN GLN A . n 
C 1 196 ASN 196 197 197 ASN ASN A . n 
C 1 197 PRO 197 198 198 PRO PRO A . n 
C 1 198 THR 198 199 199 THR THR A . n 
C 1 199 THR 199 200 200 THR THR A . n 
C 1 200 TYR 200 201 201 TYR TYR A . n 
C 1 201 ILE 201 202 202 ILE ILE A . n 
C 1 202 SER 202 203 203 SER SER A . n 
C 1 203 VAL 203 204 204 VAL VAL A . n 
C 1 204 GLY 204 205 205 GLY GLY A . n 
C 1 205 THR 205 206 206 THR THR A . n 
C 1 206 SER 206 207 207 SER SER A . n 
C 1 207 THR 207 208 208 THR THR A . n 
C 1 208 LEU 208 209 209 LEU LEU A . n 
C 1 209 ASN 209 210 210 ASN ASN A . n 
C 1 210 GLN 210 211 211 GLN GLN A . n 
C 1 211 LYS 211 212 212 LYS LYS A . n 
C 1 212 LEU 212 213 213 LEU LEU A . n 
C 1 213 VAL 213 214 214 VAL VAL A . n 
C 1 214 PRO 214 215 215 PRO PRO A . n 
C 1 215 LYS 215 216 216 LYS LYS A . n 
C 1 216 ILE 216 217 217 ILE ILE A . n 
C 1 217 ALA 217 218 218 ALA ALA A . n 
C 1 218 THR 218 219 219 THR THR A . n 
C 1 219 ARG 219 220 220 ARG ARG A . n 
C 1 220 SER 220 221 221 SER SER A . n 
C 1 221 LYS 221 222 222 LYS LYS A . n 
C 1 222 VAL 222 223 223 VAL VAL A . n 
C 1 223 LYS 223 224 224 LYS LYS A . n 
C 1 224 GLY 224 225 225 GLY GLY A . n 
C 1 225 LEU 225 226 226 LEU LEU A . n 
C 1 226 SER 226 227 227 SER SER A . n 
C 1 227 GLY 227 228 228 GLY GLY A . n 
C 1 228 ARG 228 229 229 ARG ARG A . n 
C 1 229 MET 229 230 230 MET MET A . n 
C 1 230 GLU 230 231 231 GLU GLU A . n 
C 1 231 PHE 231 232 232 PHE PHE A . n 
C 1 232 PHE 232 233 233 PHE PHE A . n 
C 1 233 TRP 233 234 234 TRP TRP A . n 
C 1 234 THR 234 235 235 THR THR A . n 
C 1 235 ILE 235 236 236 ILE ILE A . n 
C 1 236 LEU 236 237 237 LEU LEU A . n 
C 1 237 LYS 237 238 238 LYS LYS A . n 
C 1 238 SER 238 239 239 SER SER A . n 
C 1 239 ASN 239 240 240 ASN ASN A . n 
C 1 240 ASP 240 241 241 ASP ASP A . n 
C 1 241 ALA 241 242 242 ALA ALA A . n 
C 1 242 ILE 242 243 243 ILE ILE A . n 
C 1 243 ASN 243 244 244 ASN ASN A . n 
C 1 244 PHE 244 245 245 PHE PHE A . n 
C 1 245 GLU 245 246 246 GLU GLU A . n 
C 1 246 SER 246 247 247 SER SER A . n 
C 1 247 ASN 247 248 248 ASN ASN A . n 
C 1 248 GLY 248 249 249 GLY GLY A . n 
C 1 249 ASN 249 250 250 ASN ASN A . n 
C 1 250 PHE 250 251 251 PHE PHE A . n 
C 1 251 ILE 251 252 252 ILE ILE A . n 
C 1 252 ALA 252 253 253 ALA ALA A . n 
C 1 253 PRO 253 254 254 PRO PRO A . n 
C 1 254 GLU 254 255 255 GLU GLU A . n 
C 1 255 ASN 255 256 256 ASN ASN A . n 
C 1 256 ALA 256 257 257 ALA ALA A . n 
C 1 257 TYR 257 258 258 TYR TYR A . n 
C 1 258 LYS 258 259 259 LYS LYS A . n 
C 1 259 ILE 259 260 260 ILE ILE A . n 
C 1 260 VAL 260 260 260 VAL VAL A A n 
C 1 261 LYS 261 261 261 LYS LYS A . n 
C 1 262 LYS 262 262 262 LYS LYS A . n 
C 1 263 GLY 263 263 263 GLY GLY A . n 
C 1 264 ASP 264 264 264 ASP ASP A . n 
C 1 265 SER 265 265 265 SER SER A . n 
C 1 266 THR 266 266 266 THR THR A . n 
C 1 267 ILE 267 267 267 ILE ILE A . n 
C 1 268 MET 268 268 268 MET MET A . n 
C 1 269 LYS 269 269 269 LYS LYS A . n 
C 1 270 SER 270 270 270 SER SER A . n 
C 1 271 GLU 271 271 271 GLU GLU A . n 
C 1 272 LEU 272 272 272 LEU LEU A . n 
C 1 273 GLU 273 273 273 GLU GLU A . n 
C 1 274 TYR 274 274 274 TYR TYR A . n 
C 1 275 GLY 275 275 275 GLY GLY A . n 
C 1 276 ASP 276 276 276 ASP ASP A . n 
C 1 277 CYS 277 277 277 CYS CYS A . n 
C 1 278 ASN 278 278 278 ASN ASN A . n 
C 1 279 THR 279 279 279 THR THR A . n 
C 1 280 LYS 280 280 280 LYS LYS A . n 
C 1 281 CYS 281 281 281 CYS CYS A . n 
C 1 282 GLN 282 282 282 GLN GLN A . n 
C 1 283 THR 283 283 283 THR THR A . n 
C 1 284 PRO 284 284 284 PRO PRO A . n 
C 1 285 ILE 285 285 285 ILE ILE A . n 
C 1 286 GLY 286 286 286 GLY GLY A . n 
C 1 287 ALA 287 287 287 ALA ALA A . n 
C 1 288 ILE 288 288 288 ILE ILE A . n 
C 1 289 ASN 289 289 289 ASN ASN A . n 
C 1 290 SER 290 290 290 SER SER A . n 
C 1 291 SER 291 291 291 SER SER A . n 
C 1 292 MET 292 292 292 MET MET A . n 
C 1 293 PRO 293 293 293 PRO PRO A . n 
C 1 294 PHE 294 294 294 PHE PHE A . n 
C 1 295 HIS 295 295 295 HIS HIS A . n 
C 1 296 ASN 296 296 296 ASN ASN A . n 
C 1 297 ILE 297 297 297 ILE ILE A . n 
C 1 298 HIS 298 298 298 HIS HIS A . n 
C 1 299 PRO 299 299 299 PRO PRO A . n 
C 1 300 LEU 300 300 300 LEU LEU A . n 
C 1 301 THR 301 301 301 THR THR A . n 
C 1 302 ILE 302 302 302 ILE ILE A . n 
C 1 303 GLY 303 303 303 GLY GLY A . n 
C 1 304 GLU 304 304 304 GLU GLU A . n 
C 1 305 CYS 305 305 305 CYS CYS A . n 
C 1 306 PRO 306 306 306 PRO PRO A . n 
C 1 307 LYS 307 307 307 LYS LYS A . n 
C 1 308 TYR 308 308 308 TYR TYR A . n 
C 1 309 VAL 309 309 309 VAL VAL A . n 
C 1 310 LYS 310 310 310 LYS LYS A . n 
C 1 311 SER 311 311 311 SER SER A . n 
C 1 312 ASN 312 312 312 ASN ASN A . n 
C 1 313 ARG 313 313 313 ARG ARG A . n 
C 1 314 LEU 314 314 314 LEU LEU A . n 
C 1 315 VAL 315 315 315 VAL VAL A . n 
C 1 316 LEU 316 316 316 LEU LEU A . n 
C 1 317 ALA 317 317 317 ALA ALA A . n 
C 1 318 THR 318 318 318 THR THR A . n 
C 1 319 GLY 319 319 319 GLY GLY A . n 
C 1 320 LEU 320 320 320 LEU LEU A . n 
C 1 321 ARG 321 321 321 ARG ARG A . n 
C 1 322 ASN 322 322 322 ASN ASN A . n 
C 1 323 SER 323 323 323 SER SER A . n 
C 1 324 PRO 324 324 324 PRO PRO A . n 
C 1 325 GLN 325 325 ?   ?   ?   A . n 
C 1 326 GLY 326 326 ?   ?   ?   A . n 
C 1 327 GLU 327 327 ?   ?   ?   A . n 
C 1 328 ARG 328 328 ?   ?   ?   A . n 
C 1 329 ARG 329 329 ?   ?   ?   A . n 
C 1 330 ARG 330 330 ?   ?   ?   A . n 
C 1 331 LYS 331 331 ?   ?   ?   A . n 
C 1 332 LYS 332 332 ?   ?   ?   A . n 
C 1 333 ARG 333 333 ?   ?   ?   A . n 
D 2 1   GLY 1   1   1   GLY GLY B . n 
D 2 2   LEU 2   2   2   LEU LEU B . n 
D 2 3   PHE 3   3   3   PHE PHE B . n 
D 2 4   GLY 4   4   4   GLY GLY B . n 
D 2 5   ALA 5   5   5   ALA ALA B . n 
D 2 6   ILE 6   6   6   ILE ILE B . n 
D 2 7   ALA 7   7   7   ALA ALA B . n 
D 2 8   GLY 8   8   8   GLY GLY B . n 
D 2 9   PHE 9   9   9   PHE PHE B . n 
D 2 10  ILE 10  10  10  ILE ILE B . n 
D 2 11  GLU 11  11  11  GLU GLU B . n 
D 2 12  GLY 12  12  12  GLY GLY B . n 
D 2 13  GLY 13  13  13  GLY GLY B . n 
D 2 14  TRP 14  14  14  TRP TRP B . n 
D 2 15  GLN 15  15  15  GLN GLN B . n 
D 2 16  GLY 16  16  16  GLY GLY B . n 
D 2 17  MET 17  17  17  MET MET B . n 
D 2 18  VAL 18  18  18  VAL VAL B . n 
D 2 19  ASP 19  19  19  ASP ASP B . n 
D 2 20  GLY 20  20  20  GLY GLY B . n 
D 2 21  TRP 21  21  21  TRP TRP B . n 
D 2 22  TYR 22  22  22  TYR TYR B . n 
D 2 23  GLY 23  23  23  GLY GLY B . n 
D 2 24  TYR 24  24  24  TYR TYR B . n 
D 2 25  HIS 25  25  25  HIS HIS B . n 
D 2 26  HIS 26  26  26  HIS HIS B . n 
D 2 27  SER 27  27  27  SER SER B . n 
D 2 28  ASN 28  28  28  ASN ASN B . n 
D 2 29  GLU 29  29  29  GLU GLU B . n 
D 2 30  GLN 30  30  30  GLN GLN B . n 
D 2 31  GLY 31  31  31  GLY GLY B . n 
D 2 32  SER 32  32  32  SER SER B . n 
D 2 33  GLY 33  33  33  GLY GLY B . n 
D 2 34  TYR 34  34  34  TYR TYR B . n 
D 2 35  ALA 35  35  35  ALA ALA B . n 
D 2 36  ALA 36  36  36  ALA ALA B . n 
D 2 37  ASP 37  37  37  ASP ASP B . n 
D 2 38  LYS 38  38  38  LYS LYS B . n 
D 2 39  GLU 39  39  39  GLU GLU B . n 
D 2 40  SER 40  40  40  SER SER B . n 
D 2 41  THR 41  41  41  THR THR B . n 
D 2 42  GLN 42  42  42  GLN GLN B . n 
D 2 43  LYS 43  43  43  LYS LYS B . n 
D 2 44  ALA 44  44  44  ALA ALA B . n 
D 2 45  ILE 45  45  45  ILE ILE B . n 
D 2 46  ASP 46  46  46  ASP ASP B . n 
D 2 47  GLY 47  47  47  GLY GLY B . n 
D 2 48  VAL 48  48  48  VAL VAL B . n 
D 2 49  THR 49  49  49  THR THR B . n 
D 2 50  ASN 50  50  50  ASN ASN B . n 
D 2 51  LYS 51  51  51  LYS LYS B . n 
D 2 52  VAL 52  52  52  VAL VAL B . n 
D 2 53  ASN 53  53  53  ASN ASN B . n 
D 2 54  SER 54  54  54  SER SER B . n 
D 2 55  ILE 55  55  55  ILE ILE B . n 
D 2 56  ILE 56  56  56  ILE ILE B . n 
D 2 57  ASP 57  57  57  ASP ASP B . n 
D 2 58  LYS 58  58  58  LYS LYS B . n 
D 2 59  MET 59  59  59  MET MET B . n 
D 2 60  ASN 60  60  60  ASN ASN B . n 
D 2 61  THR 61  61  61  THR THR B . n 
D 2 62  GLN 62  62  62  GLN GLN B . n 
D 2 63  PHE 63  63  63  PHE PHE B . n 
D 2 64  GLU 64  64  64  GLU GLU B . n 
D 2 65  ALA 65  65  65  ALA ALA B . n 
D 2 66  VAL 66  66  66  VAL VAL B . n 
D 2 67  GLY 67  67  67  GLY GLY B . n 
D 2 68  ARG 68  68  68  ARG ARG B . n 
D 2 69  GLU 69  69  69  GLU GLU B . n 
D 2 70  PHE 70  70  70  PHE PHE B . n 
D 2 71  ASN 71  71  71  ASN ASN B . n 
D 2 72  ASN 72  72  72  ASN ASN B . n 
D 2 73  LEU 73  73  73  LEU LEU B . n 
D 2 74  GLU 74  74  74  GLU GLU B . n 
D 2 75  ARG 75  75  75  ARG ARG B . n 
D 2 76  ARG 76  76  76  ARG ARG B . n 
D 2 77  ILE 77  77  77  ILE ILE B . n 
D 2 78  GLU 78  78  78  GLU GLU B . n 
D 2 79  ASN 79  79  79  ASN ASN B . n 
D 2 80  LEU 80  80  80  LEU LEU B . n 
D 2 81  ASN 81  81  81  ASN ASN B . n 
D 2 82  LYS 82  82  82  LYS LYS B . n 
D 2 83  LYS 83  83  83  LYS LYS B . n 
D 2 84  MET 84  84  84  MET MET B . n 
D 2 85  GLU 85  85  85  GLU GLU B . n 
D 2 86  ASP 86  86  86  ASP ASP B . n 
D 2 87  GLY 87  87  87  GLY GLY B . n 
D 2 88  PHE 88  88  88  PHE PHE B . n 
D 2 89  LEU 89  89  89  LEU LEU B . n 
D 2 90  ASP 90  90  90  ASP ASP B . n 
D 2 91  VAL 91  91  91  VAL VAL B . n 
D 2 92  TRP 92  92  92  TRP TRP B . n 
D 2 93  THR 93  93  93  THR THR B . n 
D 2 94  TYR 94  94  94  TYR TYR B . n 
D 2 95  ASN 95  95  95  ASN ASN B . n 
D 2 96  ALA 96  96  96  ALA ALA B . n 
D 2 97  GLU 97  97  97  GLU GLU B . n 
D 2 98  LEU 98  98  98  LEU LEU B . n 
D 2 99  LEU 99  99  99  LEU LEU B . n 
D 2 100 VAL 100 100 100 VAL VAL B . n 
D 2 101 LEU 101 101 101 LEU LEU B . n 
D 2 102 MET 102 102 102 MET MET B . n 
D 2 103 GLU 103 103 103 GLU GLU B . n 
D 2 104 ASN 104 104 104 ASN ASN B . n 
D 2 105 GLU 105 105 105 GLU GLU B . n 
D 2 106 ARG 106 106 106 ARG ARG B . n 
D 2 107 THR 107 107 107 THR THR B . n 
D 2 108 LEU 108 108 108 LEU LEU B . n 
D 2 109 ASP 109 109 109 ASP ASP B . n 
D 2 110 PHE 110 110 110 PHE PHE B . n 
D 2 111 HIS 111 111 111 HIS HIS B . n 
D 2 112 ASP 112 112 112 ASP ASP B . n 
D 2 113 SER 113 113 113 SER SER B . n 
D 2 114 ASN 114 114 114 ASN ASN B . n 
D 2 115 VAL 115 115 115 VAL VAL B . n 
D 2 116 LYS 116 116 116 LYS LYS B . n 
D 2 117 ASN 117 117 117 ASN ASN B . n 
D 2 118 LEU 118 118 118 LEU LEU B . n 
D 2 119 TYR 119 119 119 TYR TYR B . n 
D 2 120 ASP 120 120 120 ASP ASP B . n 
D 2 121 LYS 121 121 121 LYS LYS B . n 
D 2 122 VAL 122 122 122 VAL VAL B . n 
D 2 123 ARG 123 123 123 ARG ARG B . n 
D 2 124 LEU 124 124 124 LEU LEU B . n 
D 2 125 GLN 125 125 125 GLN GLN B . n 
D 2 126 LEU 126 126 126 LEU LEU B . n 
D 2 127 ARG 127 127 127 ARG ARG B . n 
D 2 128 ASP 128 128 128 ASP ASP B . n 
D 2 129 ASN 129 129 129 ASN ASN B . n 
D 2 130 ALA 130 130 130 ALA ALA B . n 
D 2 131 LYS 131 131 131 LYS LYS B . n 
D 2 132 GLU 132 132 132 GLU GLU B . n 
D 2 133 LEU 133 133 133 LEU LEU B . n 
D 2 134 GLY 134 134 134 GLY GLY B . n 
D 2 135 ASN 135 135 135 ASN ASN B . n 
D 2 136 GLY 136 136 136 GLY GLY B . n 
D 2 137 CYS 137 137 137 CYS CYS B . n 
D 2 138 PHE 138 138 138 PHE PHE B . n 
D 2 139 GLU 139 139 139 GLU GLU B . n 
D 2 140 PHE 140 140 140 PHE PHE B . n 
D 2 141 TYR 141 141 141 TYR TYR B . n 
D 2 142 HIS 142 142 142 HIS HIS B . n 
D 2 143 ARG 143 143 143 ARG ARG B . n 
D 2 144 CYS 144 144 144 CYS CYS B . n 
D 2 145 ASP 145 145 145 ASP ASP B . n 
D 2 146 ASN 146 146 146 ASN ASN B . n 
D 2 147 GLU 147 147 147 GLU GLU B . n 
D 2 148 CYS 148 148 148 CYS CYS B . n 
D 2 149 MET 149 149 149 MET MET B . n 
D 2 150 GLU 150 150 150 GLU GLU B . n 
D 2 151 SER 151 151 151 SER SER B . n 
D 2 152 VAL 152 152 152 VAL VAL B . n 
D 2 153 ARG 153 153 153 ARG ARG B . n 
D 2 154 ASN 154 154 154 ASN ASN B . n 
D 2 155 GLY 155 155 155 GLY GLY B . n 
D 2 156 THR 156 156 156 THR THR B . n 
D 2 157 TYR 157 157 157 TYR TYR B . n 
D 2 158 ASP 158 158 158 ASP ASP B . n 
D 2 159 TYR 159 159 159 TYR TYR B . n 
D 2 160 PRO 160 160 160 PRO PRO B . n 
D 2 161 GLN 161 161 161 GLN GLN B . n 
D 2 162 TYR 162 162 162 TYR TYR B . n 
D 2 163 SER 163 163 163 SER SER B . n 
D 2 164 GLU 164 164 164 GLU GLU B . n 
D 2 165 GLU 165 165 165 GLU GLU B . n 
D 2 166 ALA 166 166 166 ALA ALA B . n 
D 2 167 ARG 167 167 167 ARG ARG B . n 
D 2 168 LEU 168 168 168 LEU LEU B . n 
D 2 169 LYS 169 169 169 LYS LYS B . n 
D 2 170 ARG 170 170 170 ARG ARG B . n 
D 2 171 GLU 171 171 171 GLU GLU B . n 
D 2 172 GLU 172 172 172 GLU GLU B . n 
D 2 173 ILE 173 173 173 ILE ILE B . n 
D 2 174 SER 174 174 174 SER SER B . n 
D 2 175 GLY 175 175 175 GLY GLY B . n 
D 2 176 ARG 176 176 ?   ?   ?   B . n 
D 2 177 LEU 177 177 ?   ?   ?   B . n 
D 2 178 VAL 178 178 ?   ?   ?   B . n 
D 2 179 PRO 179 179 ?   ?   ?   B . n 
D 2 180 ARG 180 180 ?   ?   ?   B . n 
E 1 1   ALA 1   7   ?   ?   ?   E . n 
E 1 2   ASP 2   8   8   ASP ASP E . n 
E 1 3   PRO 3   9   9   PRO PRO E . n 
E 1 4   GLY 4   10  10  GLY GLY E . n 
E 1 5   ASP 5   11  11  ASP ASP E . n 
E 1 6   GLN 6   12  12  GLN GLN E . n 
E 1 7   ILE 7   13  13  ILE ILE E . n 
E 1 8   CYS 8   14  14  CYS CYS E . n 
E 1 9   ILE 9   15  15  ILE ILE E . n 
E 1 10  GLY 10  16  16  GLY GLY E . n 
E 1 11  TYR 11  17  17  TYR TYR E . n 
E 1 12  HIS 12  18  18  HIS HIS E . n 
E 1 13  ALA 13  19  19  ALA ALA E . n 
E 1 14  ASN 14  20  20  ASN ASN E . n 
E 1 15  ASN 15  21  21  ASN ASN E . n 
E 1 16  SER 16  22  22  SER SER E . n 
E 1 17  THR 17  23  23  THR THR E . n 
E 1 18  GLU 18  24  24  GLU GLU E . n 
E 1 19  GLN 19  25  25  GLN GLN E . n 
E 1 20  VAL 20  26  26  VAL VAL E . n 
E 1 21  ASP 21  27  27  ASP ASP E . n 
E 1 22  THR 22  28  28  THR THR E . n 
E 1 23  ILE 23  29  29  ILE ILE E . n 
E 1 24  MET 24  30  30  MET MET E . n 
E 1 25  GLU 25  31  31  GLU GLU E . n 
E 1 26  LYS 26  32  32  LYS LYS E . n 
E 1 27  ASN 27  33  33  ASN ASN E . n 
E 1 28  VAL 28  34  34  VAL VAL E . n 
E 1 29  THR 29  35  35  THR THR E . n 
E 1 30  VAL 30  36  36  VAL VAL E . n 
E 1 31  THR 31  37  37  THR THR E . n 
E 1 32  HIS 32  38  38  HIS HIS E . n 
E 1 33  ALA 33  39  39  ALA ALA E . n 
E 1 34  GLN 34  40  40  GLN GLN E . n 
E 1 35  ASP 35  41  41  ASP ASP E . n 
E 1 36  ILE 36  42  42  ILE ILE E . n 
E 1 37  LEU 37  43  43  LEU LEU E . n 
E 1 38  GLU 38  44  44  GLU GLU E . n 
E 1 39  LYS 39  45  45  LYS LYS E . n 
E 1 40  THR 40  46  46  THR THR E . n 
E 1 41  HIS 41  47  47  HIS HIS E . n 
E 1 42  ASN 42  48  48  ASN ASN E . n 
E 1 43  GLY 43  49  49  GLY GLY E . n 
E 1 44  LYS 44  50  50  LYS LYS E . n 
E 1 45  LEU 45  51  51  LEU LEU E . n 
E 1 46  CYS 46  52  52  CYS CYS E . n 
E 1 47  ASN 47  53  53  ASN ASN E . n 
E 1 48  LEU 48  54  54  LEU LEU E . n 
E 1 49  ASP 49  55  55  ASP ASP E . n 
E 1 50  GLY 50  55  55  GLY GLY E A n 
E 1 51  VAL 51  56  56  VAL VAL E . n 
E 1 52  LYS 52  57  57  LYS LYS E . n 
E 1 53  PRO 53  58  58  PRO PRO E . n 
E 1 54  LEU 54  59  59  LEU LEU E . n 
E 1 55  ILE 55  60  60  ILE ILE E . n 
E 1 56  LEU 56  61  61  LEU LEU E . n 
E 1 57  ARG 57  62  62  ARG ARG E . n 
E 1 58  ASP 58  63  63  ASP ASP E . n 
E 1 59  CYS 59  64  64  CYS CYS E . n 
E 1 60  SER 60  65  65  SER SER E . n 
E 1 61  VAL 61  66  66  VAL VAL E . n 
E 1 62  ALA 62  67  67  ALA ALA E . n 
E 1 63  GLY 63  68  68  GLY GLY E . n 
E 1 64  TRP 64  69  69  TRP TRP E . n 
E 1 65  LEU 65  70  70  LEU LEU E . n 
E 1 66  LEU 66  71  71  LEU LEU E . n 
E 1 67  GLY 67  72  72  GLY GLY E . n 
E 1 68  ASN 68  73  73  ASN ASN E . n 
E 1 69  PRO 69  74  74  PRO PRO E . n 
E 1 70  MET 70  75  75  MET MET E . n 
E 1 71  CYS 71  76  76  CYS CYS E . n 
E 1 72  ASP 72  77  77  ASP ASP E . n 
E 1 73  GLU 73  78  78  GLU GLU E . n 
E 1 74  PHE 74  79  79  PHE PHE E . n 
E 1 75  LEU 75  80  80  LEU LEU E . n 
E 1 76  ASN 76  81  81  ASN ASN E . n 
E 1 77  VAL 77  82  82  VAL VAL E . n 
E 1 78  PRO 78  83  83  PRO PRO E . n 
E 1 79  GLU 79  83  83  GLU GLU E A n 
E 1 80  TRP 80  84  84  TRP TRP E . n 
E 1 81  SER 81  85  85  SER SER E . n 
E 1 82  TYR 82  86  86  TYR TYR E . n 
E 1 83  ILE 83  87  87  ILE ILE E . n 
E 1 84  VAL 84  88  88  VAL VAL E . n 
E 1 85  GLU 85  89  89  GLU GLU E . n 
E 1 86  LYS 86  90  90  LYS LYS E . n 
E 1 87  ILE 87  91  91  ILE ILE E . n 
E 1 88  ASN 88  92  92  ASN ASN E . n 
E 1 89  PRO 89  93  93  PRO PRO E . n 
E 1 90  ALA 90  94  94  ALA ALA E . n 
E 1 91  ASN 91  95  95  ASN ASN E . n 
E 1 92  ASP 92  96  96  ASP ASP E . n 
E 1 93  LEU 93  96  96  LEU LEU E A n 
E 1 94  CYS 94  97  97  CYS CYS E . n 
E 1 95  TYR 95  98  98  TYR TYR E . n 
E 1 96  PRO 96  99  99  PRO PRO E . n 
E 1 97  GLY 97  100 100 GLY GLY E . n 
E 1 98  ASN 98  101 101 ASN ASN E . n 
E 1 99  PHE 99  102 102 PHE PHE E . n 
E 1 100 ASN 100 103 103 ASN ASN E . n 
E 1 101 ASP 101 104 104 ASP ASP E . n 
E 1 102 TYR 102 105 105 TYR TYR E . n 
E 1 103 GLU 103 106 106 GLU GLU E . n 
E 1 104 GLU 104 107 107 GLU GLU E . n 
E 1 105 LEU 105 108 108 LEU LEU E . n 
E 1 106 LYS 106 109 109 LYS LYS E . n 
E 1 107 HIS 107 110 110 HIS HIS E . n 
E 1 108 LEU 108 111 111 LEU LEU E . n 
E 1 109 LEU 109 112 112 LEU LEU E . n 
E 1 110 SER 110 113 113 SER SER E . n 
E 1 111 ARG 111 114 114 ARG ARG E . n 
E 1 112 ILE 112 115 115 ILE ILE E . n 
E 1 113 ASN 113 116 116 ASN ASN E . n 
E 1 114 HIS 114 117 117 HIS HIS E . n 
E 1 115 PHE 115 118 118 PHE PHE E . n 
E 1 116 GLU 116 119 119 GLU GLU E . n 
E 1 117 LYS 117 120 120 LYS LYS E . n 
E 1 118 ILE 118 121 121 ILE ILE E . n 
E 1 119 GLN 119 122 122 GLN GLN E . n 
E 1 120 ILE 120 123 123 ILE ILE E . n 
E 1 121 THR 121 124 124 THR THR E . n 
E 1 122 PRO 122 125 125 PRO PRO E . n 
E 1 123 LYS 123 125 125 LYS LYS E A n 
E 1 124 ASN 124 125 125 ASN ASN E B n 
E 1 125 SER 125 126 126 SER SER E . n 
E 1 126 TRP 126 127 127 TRP TRP E . n 
E 1 127 SER 127 128 128 SER SER E . n 
E 1 128 ASP 128 129 129 ASP ASP E . n 
E 1 129 HIS 129 130 130 HIS HIS E . n 
E 1 130 GLU 130 131 131 GLU GLU E . n 
E 1 131 ALA 131 132 132 ALA ALA E . n 
E 1 132 SER 132 133 133 SER SER E . n 
E 1 133 GLY 133 134 134 GLY GLY E . n 
E 1 134 VAL 134 135 135 VAL VAL E . n 
E 1 135 SER 135 136 136 SER SER E . n 
E 1 136 SER 136 137 137 SER SER E . n 
E 1 137 ALA 137 138 138 ALA ALA E . n 
E 1 138 CYS 138 139 139 CYS CYS E . n 
E 1 139 PRO 139 140 140 PRO PRO E . n 
E 1 140 TYR 140 141 141 TYR TYR E . n 
E 1 141 GLN 141 142 142 GLN GLN E . n 
E 1 142 GLY 142 143 143 GLY GLY E . n 
E 1 143 ARG 143 144 144 ARG ARG E . n 
E 1 144 SER 144 145 145 SER SER E . n 
E 1 145 SER 145 146 146 SER SER E . n 
E 1 146 PHE 146 147 147 PHE PHE E . n 
E 1 147 PHE 147 148 148 PHE PHE E . n 
E 1 148 ARG 148 149 149 ARG ARG E . n 
E 1 149 ASN 149 150 150 ASN ASN E . n 
E 1 150 VAL 150 151 151 VAL VAL E . n 
E 1 151 VAL 151 152 152 VAL VAL E . n 
E 1 152 TRP 152 153 153 TRP TRP E . n 
E 1 153 LEU 153 154 154 LEU LEU E . n 
E 1 154 THR 154 155 155 THR THR E . n 
E 1 155 LYS 155 156 156 LYS LYS E . n 
E 1 156 LYS 156 157 157 LYS LYS E . n 
E 1 157 ASP 157 158 158 ASP ASP E . n 
E 1 158 ASN 158 159 159 ASN ASN E . n 
E 1 159 ALA 159 160 160 ALA ALA E . n 
E 1 160 TYR 160 161 161 TYR TYR E . n 
E 1 161 PRO 161 162 162 PRO PRO E . n 
E 1 162 THR 162 163 163 THR THR E . n 
E 1 163 ILE 163 164 164 ILE ILE E . n 
E 1 164 LYS 164 165 165 LYS LYS E . n 
E 1 165 ARG 165 166 166 ARG ARG E . n 
E 1 166 SER 166 167 167 SER SER E . n 
E 1 167 TYR 167 168 168 TYR TYR E . n 
E 1 168 ASN 168 169 169 ASN ASN E . n 
E 1 169 ASN 169 170 170 ASN ASN E . n 
E 1 170 THR 170 171 171 THR THR E . n 
E 1 171 ASN 171 172 172 ASN ASN E . n 
E 1 172 GLN 172 173 173 GLN GLN E . n 
E 1 173 GLU 173 174 174 GLU GLU E . n 
E 1 174 ASP 174 175 175 ASP ASP E . n 
E 1 175 LEU 175 176 176 LEU LEU E . n 
E 1 176 LEU 176 177 177 LEU LEU E . n 
E 1 177 VAL 177 178 178 VAL VAL E . n 
E 1 178 LEU 178 179 179 LEU LEU E . n 
E 1 179 TRP 179 180 180 TRP TRP E . n 
E 1 180 GLY 180 181 181 GLY GLY E . n 
E 1 181 ILE 181 182 182 ILE ILE E . n 
E 1 182 HIS 182 183 183 HIS HIS E . n 
E 1 183 HIS 183 184 184 HIS HIS E . n 
E 1 184 PRO 184 185 185 PRO PRO E . n 
E 1 185 ASN 185 186 186 ASN ASN E . n 
E 1 186 ASP 186 187 187 ASP ASP E . n 
E 1 187 ALA 187 188 188 ALA ALA E . n 
E 1 188 THR 188 189 189 THR THR E . n 
E 1 189 GLU 189 190 190 GLU GLU E . n 
E 1 190 GLN 190 191 191 GLN GLN E . n 
E 1 191 THR 191 192 192 THR THR E . n 
E 1 192 ARG 192 193 193 ARG ARG E . n 
E 1 193 LEU 193 194 194 LEU LEU E . n 
E 1 194 TYR 194 195 195 TYR TYR E . n 
E 1 195 GLN 195 196 196 GLN GLN E . n 
E 1 196 ASN 196 197 197 ASN ASN E . n 
E 1 197 PRO 197 198 198 PRO PRO E . n 
E 1 198 THR 198 199 199 THR THR E . n 
E 1 199 THR 199 200 200 THR THR E . n 
E 1 200 TYR 200 201 201 TYR TYR E . n 
E 1 201 ILE 201 202 202 ILE ILE E . n 
E 1 202 SER 202 203 203 SER SER E . n 
E 1 203 VAL 203 204 204 VAL VAL E . n 
E 1 204 GLY 204 205 205 GLY GLY E . n 
E 1 205 THR 205 206 206 THR THR E . n 
E 1 206 SER 206 207 207 SER SER E . n 
E 1 207 THR 207 208 208 THR THR E . n 
E 1 208 LEU 208 209 209 LEU LEU E . n 
E 1 209 ASN 209 210 210 ASN ASN E . n 
E 1 210 GLN 210 211 211 GLN GLN E . n 
E 1 211 LYS 211 212 212 LYS LYS E . n 
E 1 212 LEU 212 213 213 LEU LEU E . n 
E 1 213 VAL 213 214 214 VAL VAL E . n 
E 1 214 PRO 214 215 215 PRO PRO E . n 
E 1 215 LYS 215 216 216 LYS LYS E . n 
E 1 216 ILE 216 217 217 ILE ILE E . n 
E 1 217 ALA 217 218 218 ALA ALA E . n 
E 1 218 THR 218 219 219 THR THR E . n 
E 1 219 ARG 219 220 220 ARG ARG E . n 
E 1 220 SER 220 221 221 SER SER E . n 
E 1 221 LYS 221 222 222 LYS LYS E . n 
E 1 222 VAL 222 223 223 VAL VAL E . n 
E 1 223 LYS 223 224 224 LYS LYS E . n 
E 1 224 GLY 224 225 225 GLY GLY E . n 
E 1 225 LEU 225 226 226 LEU LEU E . n 
E 1 226 SER 226 227 227 SER SER E . n 
E 1 227 GLY 227 228 228 GLY GLY E . n 
E 1 228 ARG 228 229 229 ARG ARG E . n 
E 1 229 MET 229 230 230 MET MET E . n 
E 1 230 GLU 230 231 231 GLU GLU E . n 
E 1 231 PHE 231 232 232 PHE PHE E . n 
E 1 232 PHE 232 233 233 PHE PHE E . n 
E 1 233 TRP 233 234 234 TRP TRP E . n 
E 1 234 THR 234 235 235 THR THR E . n 
E 1 235 ILE 235 236 236 ILE ILE E . n 
E 1 236 LEU 236 237 237 LEU LEU E . n 
E 1 237 LYS 237 238 238 LYS LYS E . n 
E 1 238 SER 238 239 239 SER SER E . n 
E 1 239 ASN 239 240 240 ASN ASN E . n 
E 1 240 ASP 240 241 241 ASP ASP E . n 
E 1 241 ALA 241 242 242 ALA ALA E . n 
E 1 242 ILE 242 243 243 ILE ILE E . n 
E 1 243 ASN 243 244 244 ASN ASN E . n 
E 1 244 PHE 244 245 245 PHE PHE E . n 
E 1 245 GLU 245 246 246 GLU GLU E . n 
E 1 246 SER 246 247 247 SER SER E . n 
E 1 247 ASN 247 248 248 ASN ASN E . n 
E 1 248 GLY 248 249 249 GLY GLY E . n 
E 1 249 ASN 249 250 250 ASN ASN E . n 
E 1 250 PHE 250 251 251 PHE PHE E . n 
E 1 251 ILE 251 252 252 ILE ILE E . n 
E 1 252 ALA 252 253 253 ALA ALA E . n 
E 1 253 PRO 253 254 254 PRO PRO E . n 
E 1 254 GLU 254 255 255 GLU GLU E . n 
E 1 255 ASN 255 256 256 ASN ASN E . n 
E 1 256 ALA 256 257 257 ALA ALA E . n 
E 1 257 TYR 257 258 258 TYR TYR E . n 
E 1 258 LYS 258 259 259 LYS LYS E . n 
E 1 259 ILE 259 260 260 ILE ILE E . n 
E 1 260 VAL 260 260 260 VAL VAL E A n 
E 1 261 LYS 261 261 261 LYS LYS E . n 
E 1 262 LYS 262 262 262 LYS LYS E . n 
E 1 263 GLY 263 263 263 GLY GLY E . n 
E 1 264 ASP 264 264 264 ASP ASP E . n 
E 1 265 SER 265 265 265 SER SER E . n 
E 1 266 THR 266 266 266 THR THR E . n 
E 1 267 ILE 267 267 267 ILE ILE E . n 
E 1 268 MET 268 268 268 MET MET E . n 
E 1 269 LYS 269 269 269 LYS LYS E . n 
E 1 270 SER 270 270 270 SER SER E . n 
E 1 271 GLU 271 271 271 GLU GLU E . n 
E 1 272 LEU 272 272 272 LEU LEU E . n 
E 1 273 GLU 273 273 273 GLU GLU E . n 
E 1 274 TYR 274 274 274 TYR TYR E . n 
E 1 275 GLY 275 275 275 GLY GLY E . n 
E 1 276 ASP 276 276 276 ASP ASP E . n 
E 1 277 CYS 277 277 277 CYS CYS E . n 
E 1 278 ASN 278 278 278 ASN ASN E . n 
E 1 279 THR 279 279 279 THR THR E . n 
E 1 280 LYS 280 280 280 LYS LYS E . n 
E 1 281 CYS 281 281 281 CYS CYS E . n 
E 1 282 GLN 282 282 282 GLN GLN E . n 
E 1 283 THR 283 283 283 THR THR E . n 
E 1 284 PRO 284 284 284 PRO PRO E . n 
E 1 285 ILE 285 285 285 ILE ILE E . n 
E 1 286 GLY 286 286 286 GLY GLY E . n 
E 1 287 ALA 287 287 287 ALA ALA E . n 
E 1 288 ILE 288 288 288 ILE ILE E . n 
E 1 289 ASN 289 289 289 ASN ASN E . n 
E 1 290 SER 290 290 290 SER SER E . n 
E 1 291 SER 291 291 291 SER SER E . n 
E 1 292 MET 292 292 292 MET MET E . n 
E 1 293 PRO 293 293 293 PRO PRO E . n 
E 1 294 PHE 294 294 294 PHE PHE E . n 
E 1 295 HIS 295 295 295 HIS HIS E . n 
E 1 296 ASN 296 296 296 ASN ASN E . n 
E 1 297 ILE 297 297 297 ILE ILE E . n 
E 1 298 HIS 298 298 298 HIS HIS E . n 
E 1 299 PRO 299 299 299 PRO PRO E . n 
E 1 300 LEU 300 300 300 LEU LEU E . n 
E 1 301 THR 301 301 301 THR THR E . n 
E 1 302 ILE 302 302 302 ILE ILE E . n 
E 1 303 GLY 303 303 303 GLY GLY E . n 
E 1 304 GLU 304 304 304 GLU GLU E . n 
E 1 305 CYS 305 305 305 CYS CYS E . n 
E 1 306 PRO 306 306 306 PRO PRO E . n 
E 1 307 LYS 307 307 307 LYS LYS E . n 
E 1 308 TYR 308 308 308 TYR TYR E . n 
E 1 309 VAL 309 309 309 VAL VAL E . n 
E 1 310 LYS 310 310 310 LYS LYS E . n 
E 1 311 SER 311 311 311 SER SER E . n 
E 1 312 ASN 312 312 312 ASN ASN E . n 
E 1 313 ARG 313 313 313 ARG ARG E . n 
E 1 314 LEU 314 314 314 LEU LEU E . n 
E 1 315 VAL 315 315 315 VAL VAL E . n 
E 1 316 LEU 316 316 316 LEU LEU E . n 
E 1 317 ALA 317 317 317 ALA ALA E . n 
E 1 318 THR 318 318 318 THR THR E . n 
E 1 319 GLY 319 319 319 GLY GLY E . n 
E 1 320 LEU 320 320 320 LEU LEU E . n 
E 1 321 ARG 321 321 321 ARG ARG E . n 
E 1 322 ASN 322 322 322 ASN ASN E . n 
E 1 323 SER 323 323 323 SER SER E . n 
E 1 324 PRO 324 324 324 PRO PRO E . n 
E 1 325 GLN 325 325 ?   ?   ?   E . n 
E 1 326 GLY 326 326 ?   ?   ?   E . n 
E 1 327 GLU 327 327 ?   ?   ?   E . n 
E 1 328 ARG 328 328 ?   ?   ?   E . n 
E 1 329 ARG 329 329 ?   ?   ?   E . n 
E 1 330 ARG 330 330 ?   ?   ?   E . n 
E 1 331 LYS 331 331 ?   ?   ?   E . n 
E 1 332 LYS 332 332 ?   ?   ?   E . n 
E 1 333 ARG 333 333 ?   ?   ?   E . n 
F 2 1   GLY 1   1   1   GLY GLY F . n 
F 2 2   LEU 2   2   2   LEU LEU F . n 
F 2 3   PHE 3   3   3   PHE PHE F . n 
F 2 4   GLY 4   4   4   GLY GLY F . n 
F 2 5   ALA 5   5   5   ALA ALA F . n 
F 2 6   ILE 6   6   6   ILE ILE F . n 
F 2 7   ALA 7   7   7   ALA ALA F . n 
F 2 8   GLY 8   8   8   GLY GLY F . n 
F 2 9   PHE 9   9   9   PHE PHE F . n 
F 2 10  ILE 10  10  10  ILE ILE F . n 
F 2 11  GLU 11  11  11  GLU GLU F . n 
F 2 12  GLY 12  12  12  GLY GLY F . n 
F 2 13  GLY 13  13  13  GLY GLY F . n 
F 2 14  TRP 14  14  14  TRP TRP F . n 
F 2 15  GLN 15  15  15  GLN GLN F . n 
F 2 16  GLY 16  16  16  GLY GLY F . n 
F 2 17  MET 17  17  17  MET MET F . n 
F 2 18  VAL 18  18  18  VAL VAL F . n 
F 2 19  ASP 19  19  19  ASP ASP F . n 
F 2 20  GLY 20  20  20  GLY GLY F . n 
F 2 21  TRP 21  21  21  TRP TRP F . n 
F 2 22  TYR 22  22  22  TYR TYR F . n 
F 2 23  GLY 23  23  23  GLY GLY F . n 
F 2 24  TYR 24  24  24  TYR TYR F . n 
F 2 25  HIS 25  25  25  HIS HIS F . n 
F 2 26  HIS 26  26  26  HIS HIS F . n 
F 2 27  SER 27  27  27  SER SER F . n 
F 2 28  ASN 28  28  28  ASN ASN F . n 
F 2 29  GLU 29  29  29  GLU GLU F . n 
F 2 30  GLN 30  30  30  GLN GLN F . n 
F 2 31  GLY 31  31  31  GLY GLY F . n 
F 2 32  SER 32  32  32  SER SER F . n 
F 2 33  GLY 33  33  33  GLY GLY F . n 
F 2 34  TYR 34  34  34  TYR TYR F . n 
F 2 35  ALA 35  35  35  ALA ALA F . n 
F 2 36  ALA 36  36  36  ALA ALA F . n 
F 2 37  ASP 37  37  37  ASP ASP F . n 
F 2 38  LYS 38  38  38  LYS LYS F . n 
F 2 39  GLU 39  39  39  GLU GLU F . n 
F 2 40  SER 40  40  40  SER SER F . n 
F 2 41  THR 41  41  41  THR THR F . n 
F 2 42  GLN 42  42  42  GLN GLN F . n 
F 2 43  LYS 43  43  43  LYS LYS F . n 
F 2 44  ALA 44  44  44  ALA ALA F . n 
F 2 45  ILE 45  45  45  ILE ILE F . n 
F 2 46  ASP 46  46  46  ASP ASP F . n 
F 2 47  GLY 47  47  47  GLY GLY F . n 
F 2 48  VAL 48  48  48  VAL VAL F . n 
F 2 49  THR 49  49  49  THR THR F . n 
F 2 50  ASN 50  50  50  ASN ASN F . n 
F 2 51  LYS 51  51  51  LYS LYS F . n 
F 2 52  VAL 52  52  52  VAL VAL F . n 
F 2 53  ASN 53  53  53  ASN ASN F . n 
F 2 54  SER 54  54  54  SER SER F . n 
F 2 55  ILE 55  55  55  ILE ILE F . n 
F 2 56  ILE 56  56  56  ILE ILE F . n 
F 2 57  ASP 57  57  57  ASP ASP F . n 
F 2 58  LYS 58  58  58  LYS LYS F . n 
F 2 59  MET 59  59  59  MET MET F . n 
F 2 60  ASN 60  60  60  ASN ASN F . n 
F 2 61  THR 61  61  61  THR THR F . n 
F 2 62  GLN 62  62  62  GLN GLN F . n 
F 2 63  PHE 63  63  63  PHE PHE F . n 
F 2 64  GLU 64  64  64  GLU GLU F . n 
F 2 65  ALA 65  65  65  ALA ALA F . n 
F 2 66  VAL 66  66  66  VAL VAL F . n 
F 2 67  GLY 67  67  67  GLY GLY F . n 
F 2 68  ARG 68  68  68  ARG ARG F . n 
F 2 69  GLU 69  69  69  GLU GLU F . n 
F 2 70  PHE 70  70  70  PHE PHE F . n 
F 2 71  ASN 71  71  71  ASN ASN F . n 
F 2 72  ASN 72  72  72  ASN ASN F . n 
F 2 73  LEU 73  73  73  LEU LEU F . n 
F 2 74  GLU 74  74  74  GLU GLU F . n 
F 2 75  ARG 75  75  75  ARG ARG F . n 
F 2 76  ARG 76  76  76  ARG ARG F . n 
F 2 77  ILE 77  77  77  ILE ILE F . n 
F 2 78  GLU 78  78  78  GLU GLU F . n 
F 2 79  ASN 79  79  79  ASN ASN F . n 
F 2 80  LEU 80  80  80  LEU LEU F . n 
F 2 81  ASN 81  81  81  ASN ASN F . n 
F 2 82  LYS 82  82  82  LYS LYS F . n 
F 2 83  LYS 83  83  83  LYS LYS F . n 
F 2 84  MET 84  84  84  MET MET F . n 
F 2 85  GLU 85  85  85  GLU GLU F . n 
F 2 86  ASP 86  86  86  ASP ASP F . n 
F 2 87  GLY 87  87  87  GLY GLY F . n 
F 2 88  PHE 88  88  88  PHE PHE F . n 
F 2 89  LEU 89  89  89  LEU LEU F . n 
F 2 90  ASP 90  90  90  ASP ASP F . n 
F 2 91  VAL 91  91  91  VAL VAL F . n 
F 2 92  TRP 92  92  92  TRP TRP F . n 
F 2 93  THR 93  93  93  THR THR F . n 
F 2 94  TYR 94  94  94  TYR TYR F . n 
F 2 95  ASN 95  95  95  ASN ASN F . n 
F 2 96  ALA 96  96  96  ALA ALA F . n 
F 2 97  GLU 97  97  97  GLU GLU F . n 
F 2 98  LEU 98  98  98  LEU LEU F . n 
F 2 99  LEU 99  99  99  LEU LEU F . n 
F 2 100 VAL 100 100 100 VAL VAL F . n 
F 2 101 LEU 101 101 101 LEU LEU F . n 
F 2 102 MET 102 102 102 MET MET F . n 
F 2 103 GLU 103 103 103 GLU GLU F . n 
F 2 104 ASN 104 104 104 ASN ASN F . n 
F 2 105 GLU 105 105 105 GLU GLU F . n 
F 2 106 ARG 106 106 106 ARG ARG F . n 
F 2 107 THR 107 107 107 THR THR F . n 
F 2 108 LEU 108 108 108 LEU LEU F . n 
F 2 109 ASP 109 109 109 ASP ASP F . n 
F 2 110 PHE 110 110 110 PHE PHE F . n 
F 2 111 HIS 111 111 111 HIS HIS F . n 
F 2 112 ASP 112 112 112 ASP ASP F . n 
F 2 113 SER 113 113 113 SER SER F . n 
F 2 114 ASN 114 114 114 ASN ASN F . n 
F 2 115 VAL 115 115 115 VAL VAL F . n 
F 2 116 LYS 116 116 116 LYS LYS F . n 
F 2 117 ASN 117 117 117 ASN ASN F . n 
F 2 118 LEU 118 118 118 LEU LEU F . n 
F 2 119 TYR 119 119 119 TYR TYR F . n 
F 2 120 ASP 120 120 120 ASP ASP F . n 
F 2 121 LYS 121 121 121 LYS LYS F . n 
F 2 122 VAL 122 122 122 VAL VAL F . n 
F 2 123 ARG 123 123 123 ARG ARG F . n 
F 2 124 LEU 124 124 124 LEU LEU F . n 
F 2 125 GLN 125 125 125 GLN GLN F . n 
F 2 126 LEU 126 126 126 LEU LEU F . n 
F 2 127 ARG 127 127 127 ARG ARG F . n 
F 2 128 ASP 128 128 128 ASP ASP F . n 
F 2 129 ASN 129 129 129 ASN ASN F . n 
F 2 130 ALA 130 130 130 ALA ALA F . n 
F 2 131 LYS 131 131 131 LYS LYS F . n 
F 2 132 GLU 132 132 132 GLU GLU F . n 
F 2 133 LEU 133 133 133 LEU LEU F . n 
F 2 134 GLY 134 134 134 GLY GLY F . n 
F 2 135 ASN 135 135 135 ASN ASN F . n 
F 2 136 GLY 136 136 136 GLY GLY F . n 
F 2 137 CYS 137 137 137 CYS CYS F . n 
F 2 138 PHE 138 138 138 PHE PHE F . n 
F 2 139 GLU 139 139 139 GLU GLU F . n 
F 2 140 PHE 140 140 140 PHE PHE F . n 
F 2 141 TYR 141 141 141 TYR TYR F . n 
F 2 142 HIS 142 142 142 HIS HIS F . n 
F 2 143 ARG 143 143 143 ARG ARG F . n 
F 2 144 CYS 144 144 144 CYS CYS F . n 
F 2 145 ASP 145 145 145 ASP ASP F . n 
F 2 146 ASN 146 146 146 ASN ASN F . n 
F 2 147 GLU 147 147 147 GLU GLU F . n 
F 2 148 CYS 148 148 148 CYS CYS F . n 
F 2 149 MET 149 149 149 MET MET F . n 
F 2 150 GLU 150 150 150 GLU GLU F . n 
F 2 151 SER 151 151 151 SER SER F . n 
F 2 152 VAL 152 152 152 VAL VAL F . n 
F 2 153 ARG 153 153 153 ARG ARG F . n 
F 2 154 ASN 154 154 154 ASN ASN F . n 
F 2 155 GLY 155 155 155 GLY GLY F . n 
F 2 156 THR 156 156 156 THR THR F . n 
F 2 157 TYR 157 157 157 TYR TYR F . n 
F 2 158 ASP 158 158 158 ASP ASP F . n 
F 2 159 TYR 159 159 159 TYR TYR F . n 
F 2 160 PRO 160 160 160 PRO PRO F . n 
F 2 161 GLN 161 161 161 GLN GLN F . n 
F 2 162 TYR 162 162 162 TYR TYR F . n 
F 2 163 SER 163 163 163 SER SER F . n 
F 2 164 GLU 164 164 164 GLU GLU F . n 
F 2 165 GLU 165 165 165 GLU GLU F . n 
F 2 166 ALA 166 166 166 ALA ALA F . n 
F 2 167 ARG 167 167 167 ARG ARG F . n 
F 2 168 LEU 168 168 168 LEU LEU F . n 
F 2 169 LYS 169 169 169 LYS LYS F . n 
F 2 170 ARG 170 170 170 ARG ARG F . n 
F 2 171 GLU 171 171 171 GLU GLU F . n 
F 2 172 GLU 172 172 172 GLU GLU F . n 
F 2 173 ILE 173 173 173 ILE ILE F . n 
F 2 174 SER 174 174 174 SER SER F . n 
F 2 175 GLY 175 175 175 GLY GLY F . n 
F 2 176 ARG 176 176 ?   ?   ?   F . n 
F 2 177 LEU 177 177 ?   ?   ?   F . n 
F 2 178 VAL 178 178 ?   ?   ?   F . n 
F 2 179 PRO 179 179 ?   ?   ?   F . n 
F 2 180 ARG 180 180 ?   ?   ?   F . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G  3 NAG 1  1001 1001 NAG NAG C . 
H  3 NAG 1  1002 2001 NAG NAG C . 
I  4 FUL 2  1003 2001 FUL FUC C . 
J  3 NAG 3  1004 2002 NAG NAG C . 
K  5 SIA 1  1005 3001 SIA SIA C . 
L  6 GAL 2  1006 3002 GAL GAL C . 
M  3 NAG 1  1001 1001 NAG NAG A . 
N  3 NAG 1  1002 2001 NAG NAG A . 
O  7 FUC 2  1003 2001 FUC FUC A . 
P  4 FUL 3  1004 2001 FUL FUC A . 
Q  3 NAG 4  1005 2002 NAG NAG A . 
R  5 SIA 1  1006 3001 SIA SIA A . 
S  6 GAL 2  1007 3002 GAL GAL A . 
T  3 NAG 3  1008 3003 NAG NAG A . 
U  3 NAG 1  1001 1001 NAG NAG E . 
V  3 NAG 1  1002 2001 NAG NAG E . 
W  4 FUL 2  1003 2001 FUL FUC E . 
X  3 NAG 3  1004 2002 NAG NAG E . 
Y  5 SIA 1  1005 3001 SIA SIA E . 
Z  6 GAL 2  1006 3002 GAL GAL E . 
AA 8 HOH 1  1101 56   HOH HOH C . 
AA 8 HOH 2  1102 22   HOH HOH C . 
AA 8 HOH 3  1103 36   HOH HOH C . 
AA 8 HOH 4  1104 58   HOH HOH C . 
AA 8 HOH 5  1105 130  HOH HOH C . 
AA 8 HOH 6  1106 14   HOH HOH C . 
AA 8 HOH 7  1107 81   HOH HOH C . 
AA 8 HOH 8  1108 4    HOH HOH C . 
AA 8 HOH 9  1109 12   HOH HOH C . 
AA 8 HOH 10 1110 61   HOH HOH C . 
AA 8 HOH 11 1111 135  HOH HOH C . 
AA 8 HOH 12 1112 33   HOH HOH C . 
AA 8 HOH 13 1113 108  HOH HOH C . 
AA 8 HOH 14 1114 48   HOH HOH C . 
AA 8 HOH 15 1115 37   HOH HOH C . 
AA 8 HOH 16 1116 74   HOH HOH C . 
AA 8 HOH 17 1117 15   HOH HOH C . 
AA 8 HOH 18 1118 155  HOH HOH C . 
AA 8 HOH 19 1119 165  HOH HOH C . 
AA 8 HOH 20 1120 23   HOH HOH C . 
AA 8 HOH 21 1121 25   HOH HOH C . 
AA 8 HOH 22 1122 53   HOH HOH C . 
AA 8 HOH 23 1123 153  HOH HOH C . 
AA 8 HOH 24 1124 95   HOH HOH C . 
AA 8 HOH 25 1125 31   HOH HOH C . 
AA 8 HOH 26 1126 133  HOH HOH C . 
AA 8 HOH 27 1127 16   HOH HOH C . 
AA 8 HOH 28 1128 116  HOH HOH C . 
AA 8 HOH 29 1129 118  HOH HOH C . 
AA 8 HOH 30 1130 159  HOH HOH C . 
AA 8 HOH 31 1131 59   HOH HOH C . 
AA 8 HOH 32 1132 92   HOH HOH C . 
AA 8 HOH 33 1133 52   HOH HOH C . 
AA 8 HOH 34 1134 88   HOH HOH C . 
AA 8 HOH 35 1135 121  HOH HOH C . 
AA 8 HOH 36 1136 139  HOH HOH C . 
AA 8 HOH 37 1137 41   HOH HOH C . 
AA 8 HOH 38 1138 143  HOH HOH C . 
AA 8 HOH 39 1139 154  HOH HOH C . 
AA 8 HOH 40 1140 136  HOH HOH C . 
AA 8 HOH 41 1141 144  HOH HOH C . 
AA 8 HOH 42 1142 166  HOH HOH C . 
AA 8 HOH 43 1143 117  HOH HOH C . 
AA 8 HOH 44 1144 134  HOH HOH C . 
AA 8 HOH 45 1145 167  HOH HOH C . 
AA 8 HOH 46 1146 137  HOH HOH C . 
AA 8 HOH 47 1147 161  HOH HOH C . 
BA 8 HOH 1  201  80   HOH HOH D . 
BA 8 HOH 2  202  19   HOH HOH D . 
BA 8 HOH 3  203  29   HOH HOH D . 
BA 8 HOH 4  204  20   HOH HOH D . 
BA 8 HOH 5  205  68   HOH HOH D . 
BA 8 HOH 6  206  64   HOH HOH D . 
BA 8 HOH 7  207  104  HOH HOH D . 
CA 8 HOH 1  1101 98   HOH HOH A . 
CA 8 HOH 2  1102 71   HOH HOH A . 
CA 8 HOH 3  1103 97   HOH HOH A . 
CA 8 HOH 4  1104 76   HOH HOH A . 
CA 8 HOH 5  1105 69   HOH HOH A . 
CA 8 HOH 6  1106 125  HOH HOH A . 
CA 8 HOH 7  1107 96   HOH HOH A . 
CA 8 HOH 8  1108 21   HOH HOH A . 
CA 8 HOH 9  1109 7    HOH HOH A . 
CA 8 HOH 10 1110 62   HOH HOH A . 
CA 8 HOH 11 1111 9    HOH HOH A . 
CA 8 HOH 12 1112 1    HOH HOH A . 
CA 8 HOH 13 1113 84   HOH HOH A . 
CA 8 HOH 14 1114 75   HOH HOH A . 
CA 8 HOH 15 1115 100  HOH HOH A . 
CA 8 HOH 16 1116 34   HOH HOH A . 
CA 8 HOH 17 1117 87   HOH HOH A . 
CA 8 HOH 18 1118 127  HOH HOH A . 
CA 8 HOH 19 1119 43   HOH HOH A . 
CA 8 HOH 20 1120 78   HOH HOH A . 
CA 8 HOH 21 1121 17   HOH HOH A . 
CA 8 HOH 22 1122 55   HOH HOH A . 
CA 8 HOH 23 1123 3    HOH HOH A . 
CA 8 HOH 24 1124 122  HOH HOH A . 
CA 8 HOH 25 1125 109  HOH HOH A . 
CA 8 HOH 26 1126 77   HOH HOH A . 
CA 8 HOH 27 1127 94   HOH HOH A . 
CA 8 HOH 28 1128 99   HOH HOH A . 
CA 8 HOH 29 1129 110  HOH HOH A . 
CA 8 HOH 30 1130 2    HOH HOH A . 
CA 8 HOH 31 1131 18   HOH HOH A . 
CA 8 HOH 32 1132 131  HOH HOH A . 
CA 8 HOH 33 1133 65   HOH HOH A . 
CA 8 HOH 34 1134 93   HOH HOH A . 
CA 8 HOH 35 1135 123  HOH HOH A . 
CA 8 HOH 36 1136 107  HOH HOH A . 
CA 8 HOH 37 1137 66   HOH HOH A . 
CA 8 HOH 38 1138 28   HOH HOH A . 
CA 8 HOH 39 1139 8    HOH HOH A . 
CA 8 HOH 40 1140 112  HOH HOH A . 
CA 8 HOH 41 1141 82   HOH HOH A . 
CA 8 HOH 42 1142 35   HOH HOH A . 
CA 8 HOH 43 1143 158  HOH HOH A . 
CA 8 HOH 44 1144 156  HOH HOH A . 
CA 8 HOH 45 1145 91   HOH HOH A . 
CA 8 HOH 46 1146 141  HOH HOH A . 
CA 8 HOH 47 1147 157  HOH HOH A . 
CA 8 HOH 48 1148 103  HOH HOH A . 
CA 8 HOH 49 1149 27   HOH HOH A . 
CA 8 HOH 50 1150 162  HOH HOH A . 
CA 8 HOH 51 1151 164  HOH HOH A . 
CA 8 HOH 52 1152 138  HOH HOH A . 
CA 8 HOH 53 1153 163  HOH HOH A . 
CA 8 HOH 54 1154 160  HOH HOH A . 
DA 8 HOH 1  201  115  HOH HOH B . 
DA 8 HOH 2  202  89   HOH HOH B . 
DA 8 HOH 3  203  101  HOH HOH B . 
DA 8 HOH 4  204  24   HOH HOH B . 
DA 8 HOH 5  205  49   HOH HOH B . 
DA 8 HOH 6  206  63   HOH HOH B . 
DA 8 HOH 7  207  105  HOH HOH B . 
DA 8 HOH 8  208  45   HOH HOH B . 
EA 8 HOH 1  1101 44   HOH HOH E . 
EA 8 HOH 2  1102 142  HOH HOH E . 
EA 8 HOH 3  1103 30   HOH HOH E . 
EA 8 HOH 4  1104 6    HOH HOH E . 
EA 8 HOH 5  1105 73   HOH HOH E . 
EA 8 HOH 6  1106 13   HOH HOH E . 
EA 8 HOH 7  1107 11   HOH HOH E . 
EA 8 HOH 8  1108 46   HOH HOH E . 
EA 8 HOH 9  1109 86   HOH HOH E . 
EA 8 HOH 10 1110 10   HOH HOH E . 
EA 8 HOH 11 1111 132  HOH HOH E . 
EA 8 HOH 12 1112 39   HOH HOH E . 
EA 8 HOH 13 1113 83   HOH HOH E . 
EA 8 HOH 14 1114 85   HOH HOH E . 
EA 8 HOH 15 1115 147  HOH HOH E . 
EA 8 HOH 16 1116 57   HOH HOH E . 
EA 8 HOH 17 1117 38   HOH HOH E . 
EA 8 HOH 18 1118 113  HOH HOH E . 
EA 8 HOH 19 1119 54   HOH HOH E . 
EA 8 HOH 20 1120 146  HOH HOH E . 
EA 8 HOH 21 1121 90   HOH HOH E . 
EA 8 HOH 22 1122 129  HOH HOH E . 
EA 8 HOH 23 1123 79   HOH HOH E . 
EA 8 HOH 24 1124 60   HOH HOH E . 
EA 8 HOH 25 1125 102  HOH HOH E . 
EA 8 HOH 26 1126 119  HOH HOH E . 
EA 8 HOH 27 1127 26   HOH HOH E . 
EA 8 HOH 28 1128 120  HOH HOH E . 
EA 8 HOH 29 1129 150  HOH HOH E . 
EA 8 HOH 30 1130 128  HOH HOH E . 
EA 8 HOH 31 1131 111  HOH HOH E . 
EA 8 HOH 32 1132 47   HOH HOH E . 
EA 8 HOH 33 1133 5    HOH HOH E . 
EA 8 HOH 34 1134 145  HOH HOH E . 
EA 8 HOH 35 1135 151  HOH HOH E . 
EA 8 HOH 36 1136 67   HOH HOH E . 
EA 8 HOH 37 1137 152  HOH HOH E . 
EA 8 HOH 38 1138 149  HOH HOH E . 
EA 8 HOH 39 1139 70   HOH HOH E . 
EA 8 HOH 40 1140 106  HOH HOH E . 
EA 8 HOH 41 1141 126  HOH HOH E . 
EA 8 HOH 42 1142 148  HOH HOH E . 
EA 8 HOH 43 1143 140  HOH HOH E . 
FA 8 HOH 1  201  42   HOH HOH F . 
FA 8 HOH 2  202  32   HOH HOH F . 
FA 8 HOH 3  203  124  HOH HOH F . 
FA 8 HOH 4  204  40   HOH HOH F . 
FA 8 HOH 5  205  51   HOH HOH F . 
FA 8 HOH 6  206  50   HOH HOH F . 
FA 8 HOH 7  207  72   HOH HOH F . 
FA 8 HOH 8  208  114  HOH HOH F . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 33460 ? 
1 MORE         -77   ? 
1 'SSA (A^2)'  64670 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2015-12-02 
2 'Structure model' 1 1 2015-12-09 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.8.2_1309 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .          2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .          3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .          4 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   SG 
_pdbx_validate_close_contact.auth_asym_id_1   D 
_pdbx_validate_close_contact.auth_comp_id_1   CYS 
_pdbx_validate_close_contact.auth_seq_id_1    144 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   CB 
_pdbx_validate_close_contact.auth_asym_id_2   D 
_pdbx_validate_close_contact.auth_comp_id_2   CYS 
_pdbx_validate_close_contact.auth_seq_id_2    148 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.07 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP C 55  ? ? 52.18   -122.19 
2  1 ARG C 62  ? ? -101.22 -88.36  
3  1 ASP C 96  ? ? -121.02 -123.24 
4  1 ALA C 132 ? ? -110.98 61.09   
5  1 SER C 133 ? ? -149.42 28.24   
6  1 TYR C 141 ? ? -116.16 -79.45  
7  1 GLN C 142 ? ? -114.32 59.00   
8  1 ASP C 158 ? ? 63.16   -114.40 
9  1 GLN C 196 ? ? 72.50   -55.39  
10 1 PHE D 3   ? ? -138.82 -41.89  
11 1 ALA D 5   ? ? -89.82  -77.06  
12 1 ASN D 28  ? ? -122.36 -161.53 
13 1 SER D 32  ? ? -105.29 -166.48 
14 1 ARG D 127 ? ? 58.19   -127.20 
15 1 ASP D 145 ? ? -73.36  -157.66 
16 1 ASN D 146 ? ? -100.60 42.72   
17 1 GLU D 147 ? ? -151.49 -11.73  
18 1 TYR D 157 ? ? -38.00  108.82  
19 1 SER D 174 ? ? -86.10  32.05   
20 1 ASP A 55  ? ? 54.97   -121.74 
21 1 ARG A 62  ? ? -100.29 -84.58  
22 1 ASP A 96  ? ? -120.25 -127.65 
23 1 ALA A 132 ? ? -114.18 60.63   
24 1 SER A 133 ? ? -147.67 25.43   
25 1 TYR A 141 ? ? -114.56 -84.42  
26 1 GLN A 142 ? ? -114.27 58.44   
27 1 SER A 146 ? ? -141.49 -156.92 
28 1 ASP A 158 ? ? 59.58   -116.44 
29 1 GLN A 196 ? ? 69.98   -56.14  
30 1 PHE B 3   ? ? -140.55 -23.88  
31 1 ALA B 5   ? ? -83.49  -74.38  
32 1 ASN B 28  ? ? -122.61 -156.22 
33 1 SER B 32  ? ? -102.02 -165.04 
34 1 ARG B 127 ? ? 56.20   -126.22 
35 1 ASP B 145 ? ? -72.90  -159.46 
36 1 ASN B 146 ? ? -100.72 45.62   
37 1 GLU B 147 ? ? -148.50 -14.30  
38 1 TYR B 157 ? ? -35.01  109.69  
39 1 SER B 174 ? ? -89.33  32.63   
40 1 ASP E 55  ? ? 53.73   -120.92 
41 1 ARG E 62  ? ? -98.86  -89.28  
42 1 ASP E 96  ? ? -119.29 -122.77 
43 1 ALA E 132 ? ? -109.67 60.31   
44 1 SER E 133 ? ? -145.07 28.11   
45 1 TYR E 141 ? ? -117.61 -86.82  
46 1 GLN E 142 ? ? -119.15 62.49   
47 1 SER E 146 ? ? -139.00 -155.29 
48 1 ASP E 158 ? ? 61.02   -112.73 
49 1 GLN E 196 ? ? 70.69   -55.66  
50 1 ALA F 5   ? ? -84.20  -75.93  
51 1 ASN F 28  ? ? -125.75 -162.00 
52 1 SER F 32  ? ? -108.47 -165.35 
53 1 ARG F 127 ? ? 49.89   -122.82 
54 1 ASP F 145 ? ? -76.50  -156.99 
55 1 ASN F 146 ? ? -98.92  40.21   
56 1 GLU F 147 ? ? -151.84 -13.26  
57 1 TYR F 157 ? ? -38.89  110.34  
58 1 SER F 174 ? ? -93.84  33.28   
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      C 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1147 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.86 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 N 1 C GAL 1006 ? O1 ? K GAL 2 O1 
2 1 N 1 E GAL 1006 ? O1 ? Y GAL 2 O1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 C ALA 7   ? A ALA 1   
2  1 Y 1 C GLN 325 ? A GLN 325 
3  1 Y 1 C GLY 326 ? A GLY 326 
4  1 Y 1 C GLU 327 ? A GLU 327 
5  1 Y 1 C ARG 328 ? A ARG 328 
6  1 Y 1 C ARG 329 ? A ARG 329 
7  1 Y 1 C ARG 330 ? A ARG 330 
8  1 Y 1 C LYS 331 ? A LYS 331 
9  1 Y 1 C LYS 332 ? A LYS 332 
10 1 Y 1 C ARG 333 ? A ARG 333 
11 1 Y 1 D ARG 176 ? B ARG 176 
12 1 Y 1 D LEU 177 ? B LEU 177 
13 1 Y 1 D VAL 178 ? B VAL 178 
14 1 Y 1 D PRO 179 ? B PRO 179 
15 1 Y 1 D ARG 180 ? B ARG 180 
16 1 Y 1 A ALA 7   ? C ALA 1   
17 1 Y 1 A GLN 325 ? C GLN 325 
18 1 Y 1 A GLY 326 ? C GLY 326 
19 1 Y 1 A GLU 327 ? C GLU 327 
20 1 Y 1 A ARG 328 ? C ARG 328 
21 1 Y 1 A ARG 329 ? C ARG 329 
22 1 Y 1 A ARG 330 ? C ARG 330 
23 1 Y 1 A LYS 331 ? C LYS 331 
24 1 Y 1 A LYS 332 ? C LYS 332 
25 1 Y 1 A ARG 333 ? C ARG 333 
26 1 Y 1 B ARG 176 ? D ARG 176 
27 1 Y 1 B LEU 177 ? D LEU 177 
28 1 Y 1 B VAL 178 ? D VAL 178 
29 1 Y 1 B PRO 179 ? D PRO 179 
30 1 Y 1 B ARG 180 ? D ARG 180 
31 1 Y 1 E ALA 7   ? E ALA 1   
32 1 Y 1 E GLN 325 ? E GLN 325 
33 1 Y 1 E GLY 326 ? E GLY 326 
34 1 Y 1 E GLU 327 ? E GLU 327 
35 1 Y 1 E ARG 328 ? E ARG 328 
36 1 Y 1 E ARG 329 ? E ARG 329 
37 1 Y 1 E ARG 330 ? E ARG 330 
38 1 Y 1 E LYS 331 ? E LYS 331 
39 1 Y 1 E LYS 332 ? E LYS 332 
40 1 Y 1 E ARG 333 ? E ARG 333 
41 1 Y 1 F ARG 176 ? F ARG 176 
42 1 Y 1 F LEU 177 ? F LEU 177 
43 1 Y 1 F VAL 178 ? F VAL 178 
44 1 Y 1 F PRO 179 ? F PRO 179 
45 1 Y 1 F ARG 180 ? F ARG 180 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 N-ACETYL-D-GLUCOSAMINE NAG 
4 BETA-L-FUCOSE          FUL 
5 'O-SIALIC ACID'        SIA 
6 BETA-D-GALACTOSE       GAL 
7 ALPHA-L-FUCOSE         FUC 
8 water                  HOH 
# 
