data_6YED
# 
_entry.id   6YED 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.342 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   6YED         
WWPDB D_1292107499 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB '6YE0 contains the same protein complexed with putrescine' 6YE0 unspecified 
PDB '6YE6 contains the same protein complexed with agmatine'   6YE6 unspecified 
PDB '6YE7 contains the same protein complexed with cadaverine' 6YE7 unspecified 
PDB '6YE8 contains the same protein complexed with spermidine' 6YE8 unspecified 
PDB '6YEC contains the same protein complexed with spermine'   6YEC unspecified 
PDB '6YEB contains the same protein in its closed apo state'   6YEB 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                        6YED 
_pdbx_database_status.recvd_initial_deposition_date   2020-03-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Shanmugaratnam, S.' 1 0000-0002-2614-6046 
'Kroeger, P.'        2 0000-0001-8486-7485 
'Hocker, B.'         3 0000-0002-8250-9462 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            29 
_citation.language                  ? 
_citation.page_first                433 
_citation.page_last                 ? 
_citation.title                     
'A comprehensive binding study illustrates ligand recognition in the periplasmic binding protein PotF.' 
_citation.year                      2021 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2020.12.005 
_citation.pdbx_database_id_PubMed   33406388 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kroger, P.'         1 ? 
primary 'Shanmugaratnam, S.' 2 ? 
primary 'Ferruz, N.'         3 ? 
primary 'Schweimer, K.'      4 ? 
primary 'Hocker, B.'         5 ? 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   111.593 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6YED 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.220 
_cell.length_a_esd                 ? 
_cell.length_b                     53.450 
_cell.length_b_esd                 ? 
_cell.length_c                     88.130 
_cell.length_c_esd                 ? 
_cell.volume                       333841.241 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         6YED 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_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 'Putrescine-binding periplasmic protein' 39370.531 2   ? ? ? ? 
2 non-polymer syn 'TRIETHYLENE GLYCOL'                     150.173   1   ? ? ? ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                  106.120   6   ? ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                           62.068    15  ? ? ? ? 
5 non-polymer syn 'CHLORIDE ION'                           35.453    3   ? ? ? ? 
6 water       nat water                                    18.015    307 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;AEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLTAGVFQPLDKSKL
PEWKNLDPELLKLVAKHDPDNKFAMPYMWATTGIGYNVDKVKAVLGENAPVDSWDLILKPENLEKLKSCGVSFLDAPEEV
FATVLNYLGKDPNSTKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQASNRAKEAKNGVNVSF
SIPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKAATPLVSAEVRENPGIYPPADVRAKLF
TLKVQDPKIDRVRTRAWTKVKSGKLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLTAGVFQPLDKSKL
PEWKNLDPELLKLVAKHDPDNKFAMPYMWATTGIGYNVDKVKAVLGENAPVDSWDLILKPENLEKLKSCGVSFLDAPEEV
FATVLNYLGKDPNSTKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQASNRAKEAKNGVNVSF
SIPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKAATPLVSAEVRENPGIYPPADVRAKLF
TLKVQDPKIDRVRTRAWTKVKSGKLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
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   GLU n 
1 3   GLN n 
1 4   LYS n 
1 5   THR n 
1 6   LEU n 
1 7   HIS n 
1 8   ILE n 
1 9   TYR n 
1 10  ASN n 
1 11  TRP n 
1 12  SER n 
1 13  ASP n 
1 14  TYR n 
1 15  ILE n 
1 16  ALA n 
1 17  PRO n 
1 18  ASP n 
1 19  THR n 
1 20  VAL n 
1 21  ALA n 
1 22  ASN n 
1 23  PHE n 
1 24  GLU n 
1 25  LYS n 
1 26  GLU n 
1 27  THR n 
1 28  GLY n 
1 29  ILE n 
1 30  LYS n 
1 31  VAL n 
1 32  VAL n 
1 33  TYR n 
1 34  ASP n 
1 35  VAL n 
1 36  PHE n 
1 37  ASP n 
1 38  SER n 
1 39  ASN n 
1 40  GLU n 
1 41  VAL n 
1 42  LEU n 
1 43  GLU n 
1 44  GLY n 
1 45  LYS n 
1 46  LEU n 
1 47  MET n 
1 48  ALA n 
1 49  GLY n 
1 50  SER n 
1 51  THR n 
1 52  GLY n 
1 53  PHE n 
1 54  ASP n 
1 55  LEU n 
1 56  VAL n 
1 57  VAL n 
1 58  PRO n 
1 59  SER n 
1 60  ALA n 
1 61  SER n 
1 62  PHE n 
1 63  LEU n 
1 64  GLU n 
1 65  ARG n 
1 66  GLN n 
1 67  LEU n 
1 68  THR n 
1 69  ALA n 
1 70  GLY n 
1 71  VAL n 
1 72  PHE n 
1 73  GLN n 
1 74  PRO n 
1 75  LEU n 
1 76  ASP n 
1 77  LYS n 
1 78  SER n 
1 79  LYS n 
1 80  LEU n 
1 81  PRO n 
1 82  GLU n 
1 83  TRP n 
1 84  LYS n 
1 85  ASN n 
1 86  LEU n 
1 87  ASP n 
1 88  PRO n 
1 89  GLU n 
1 90  LEU n 
1 91  LEU n 
1 92  LYS n 
1 93  LEU n 
1 94  VAL n 
1 95  ALA n 
1 96  LYS n 
1 97  HIS n 
1 98  ASP n 
1 99  PRO n 
1 100 ASP n 
1 101 ASN n 
1 102 LYS n 
1 103 PHE n 
1 104 ALA n 
1 105 MET n 
1 106 PRO n 
1 107 TYR n 
1 108 MET n 
1 109 TRP n 
1 110 ALA n 
1 111 THR n 
1 112 THR n 
1 113 GLY n 
1 114 ILE n 
1 115 GLY n 
1 116 TYR n 
1 117 ASN n 
1 118 VAL n 
1 119 ASP n 
1 120 LYS n 
1 121 VAL n 
1 122 LYS n 
1 123 ALA n 
1 124 VAL n 
1 125 LEU n 
1 126 GLY n 
1 127 GLU n 
1 128 ASN n 
1 129 ALA n 
1 130 PRO n 
1 131 VAL n 
1 132 ASP n 
1 133 SER n 
1 134 TRP n 
1 135 ASP n 
1 136 LEU n 
1 137 ILE n 
1 138 LEU n 
1 139 LYS n 
1 140 PRO n 
1 141 GLU n 
1 142 ASN n 
1 143 LEU n 
1 144 GLU n 
1 145 LYS n 
1 146 LEU n 
1 147 LYS n 
1 148 SER n 
1 149 CYS n 
1 150 GLY n 
1 151 VAL n 
1 152 SER n 
1 153 PHE n 
1 154 LEU n 
1 155 ASP n 
1 156 ALA n 
1 157 PRO n 
1 158 GLU n 
1 159 GLU n 
1 160 VAL n 
1 161 PHE n 
1 162 ALA n 
1 163 THR n 
1 164 VAL n 
1 165 LEU n 
1 166 ASN n 
1 167 TYR n 
1 168 LEU n 
1 169 GLY n 
1 170 LYS n 
1 171 ASP n 
1 172 PRO n 
1 173 ASN n 
1 174 SER n 
1 175 THR n 
1 176 LYS n 
1 177 ALA n 
1 178 ASP n 
1 179 ASP n 
1 180 TYR n 
1 181 THR n 
1 182 GLY n 
1 183 PRO n 
1 184 ALA n 
1 185 THR n 
1 186 ASP n 
1 187 LEU n 
1 188 LEU n 
1 189 LEU n 
1 190 LYS n 
1 191 LEU n 
1 192 ARG n 
1 193 PRO n 
1 194 ASN n 
1 195 ILE n 
1 196 ARG n 
1 197 TYR n 
1 198 PHE n 
1 199 HIS n 
1 200 SER n 
1 201 SER n 
1 202 GLN n 
1 203 TYR n 
1 204 ILE n 
1 205 ASN n 
1 206 ASP n 
1 207 LEU n 
1 208 ALA n 
1 209 ASN n 
1 210 GLY n 
1 211 ASP n 
1 212 ILE n 
1 213 CYS n 
1 214 VAL n 
1 215 ALA n 
1 216 ILE n 
1 217 GLY n 
1 218 TRP n 
1 219 ALA n 
1 220 GLY n 
1 221 ASP n 
1 222 VAL n 
1 223 TRP n 
1 224 GLN n 
1 225 ALA n 
1 226 SER n 
1 227 ASN n 
1 228 ARG n 
1 229 ALA n 
1 230 LYS n 
1 231 GLU n 
1 232 ALA n 
1 233 LYS n 
1 234 ASN n 
1 235 GLY n 
1 236 VAL n 
1 237 ASN n 
1 238 VAL n 
1 239 SER n 
1 240 PHE n 
1 241 SER n 
1 242 ILE n 
1 243 PRO n 
1 244 LYS n 
1 245 GLU n 
1 246 GLY n 
1 247 ALA n 
1 248 MET n 
1 249 ALA n 
1 250 PHE n 
1 251 PHE n 
1 252 ASP n 
1 253 VAL n 
1 254 PHE n 
1 255 ALA n 
1 256 MET n 
1 257 PRO n 
1 258 ALA n 
1 259 ASP n 
1 260 ALA n 
1 261 LYS n 
1 262 ASN n 
1 263 LYS n 
1 264 ASP n 
1 265 GLU n 
1 266 ALA n 
1 267 TYR n 
1 268 GLN n 
1 269 PHE n 
1 270 LEU n 
1 271 ASN n 
1 272 TYR n 
1 273 LEU n 
1 274 LEU n 
1 275 ARG n 
1 276 PRO n 
1 277 ASP n 
1 278 VAL n 
1 279 VAL n 
1 280 ALA n 
1 281 HIS n 
1 282 ILE n 
1 283 SER n 
1 284 ASP n 
1 285 HIS n 
1 286 VAL n 
1 287 PHE n 
1 288 TYR n 
1 289 ALA n 
1 290 ASN n 
1 291 ALA n 
1 292 ASN n 
1 293 LYS n 
1 294 ALA n 
1 295 ALA n 
1 296 THR n 
1 297 PRO n 
1 298 LEU n 
1 299 VAL n 
1 300 SER n 
1 301 ALA n 
1 302 GLU n 
1 303 VAL n 
1 304 ARG n 
1 305 GLU n 
1 306 ASN n 
1 307 PRO n 
1 308 GLY n 
1 309 ILE n 
1 310 TYR n 
1 311 PRO n 
1 312 PRO n 
1 313 ALA n 
1 314 ASP n 
1 315 VAL n 
1 316 ARG n 
1 317 ALA n 
1 318 LYS n 
1 319 LEU n 
1 320 PHE n 
1 321 THR n 
1 322 LEU n 
1 323 LYS n 
1 324 VAL n 
1 325 GLN n 
1 326 ASP n 
1 327 PRO n 
1 328 LYS n 
1 329 ILE n 
1 330 ASP n 
1 331 ARG n 
1 332 VAL n 
1 333 ARG n 
1 334 THR n 
1 335 ARG n 
1 336 ALA n 
1 337 TRP n 
1 338 THR n 
1 339 LYS n 
1 340 VAL n 
1 341 LYS n 
1 342 SER n 
1 343 GLY n 
1 344 LYS n 
1 345 LEU n 
1 346 GLU n 
1 347 HIS n 
1 348 HIS n 
1 349 HIS n 
1 350 HIS n 
1 351 HIS n 
1 352 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   352 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'potF, b0854, JW0838' 
_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      'Escherichia coli K12' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     83333 
_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      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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                       'pET21b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POTF_ECOLI 
_struct_ref.pdbx_db_accession          P31133 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLTAGVFQPLDKSKL
PEWKNLDPELLKLVAKHDPDNKFAMPYMWATTGIGYNVDKVKAVLGENAPVDSWDLILKPENLEKLKSCGVSFLDAPEEV
FATVLNYLGKDPNSTKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQASNRAKEAKNGVNVSF
SIPKEGAMAFFDVFAMPADAKNKDEAYQFLNYLLRPDVVAHISDHVFYANANKAATPLVSAEVRENPGIYPPADVRAKLF
TLKVQDPKIDRVRTRAWTKVKSGK
;
_struct_ref.pdbx_align_begin           27 
# 
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 6YED A 1 ? 344 ? P31133 27 ? 370 ? 27 370 
2 1 6YED B 1 ? 344 ? P31133 27 ? 370 ? 27 370 
# 
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 6YED LEU A 345 ? UNP P31133 ? ? 'expression tag' 371 1  
1 6YED GLU A 346 ? UNP P31133 ? ? 'expression tag' 372 2  
1 6YED HIS A 347 ? UNP P31133 ? ? 'expression tag' 373 3  
1 6YED HIS A 348 ? UNP P31133 ? ? 'expression tag' 374 4  
1 6YED HIS A 349 ? UNP P31133 ? ? 'expression tag' 375 5  
1 6YED HIS A 350 ? UNP P31133 ? ? 'expression tag' 376 6  
1 6YED HIS A 351 ? UNP P31133 ? ? 'expression tag' 377 7  
1 6YED HIS A 352 ? UNP P31133 ? ? 'expression tag' 378 8  
2 6YED LEU B 345 ? UNP P31133 ? ? 'expression tag' 371 9  
2 6YED GLU B 346 ? UNP P31133 ? ? 'expression tag' 372 10 
2 6YED HIS B 347 ? UNP P31133 ? ? 'expression tag' 373 11 
2 6YED HIS B 348 ? UNP P31133 ? ? 'expression tag' 374 12 
2 6YED HIS B 349 ? UNP P31133 ? ? 'expression tag' 375 13 
2 6YED HIS B 350 ? UNP P31133 ? ? 'expression tag' 376 14 
2 6YED HIS B 351 ? UNP P31133 ? ? 'expression tag' 377 15 
2 6YED HIS B 352 ? UNP P31133 ? ? 'expression tag' 378 16 
# 
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 
CL  non-polymer         . 'CHLORIDE ION'          ?                 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE                ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL          'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ?                 'C4 H10 O3'      106.120 
PGE non-polymer         . 'TRIETHYLENE GLYCOL'    ?                 'C6 H14 O4'      150.173 
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 
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                   6YED 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.12 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         41.98 
_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              7.2 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Tris pH 7.2, 0.2 M NaCl, 35% PEG 3000' 
_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.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-07-12 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'DCM Si(111)' 
_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   0.9184 
_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                        'BESSY BEAMLINE 14.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9184 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   14.1 
_diffrn_source.pdbx_synchrotron_site       BESSY 
# 
_reflns.B_iso_Wilson_estimate            29.95 
_reflns.entry_id                         6YED 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.18 
_reflns.d_resolution_low                 45.90 
_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                       67443 
_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             99.95 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  10.9 
_reflns.pdbx_Rmerge_I_obs                0.1565 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            13.39 
_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                  0.1642 
_reflns.pdbx_Rpim_I_all                  0.04914 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     0.997 
_reflns.pdbx_CC_star                     0.999 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  2.18 
_reflns_shell.d_res_low                   2.258 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         4.65 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           3433 
_reflns_shell.percent_possible_all        99.91 
_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                0.9698 
_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             9.7 
_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             1.023 
_reflns_shell.pdbx_Rpim_I_all             0.3195 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                0.871 
_reflns_shell.pdbx_CC_star                0.965 
_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                               43.22 
_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                                 6YED 
_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                            2.18 
_refine.ls_d_res_low                             45.90 
_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                     67443 
_refine.ls_number_reflns_R_free                  3852 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.92 
_refine.ls_percent_reflns_R_free                 5.71 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2303 
_refine.ls_R_factor_R_free                       0.2730 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2277 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_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                          1.35 
_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                      1A99 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            'Random selection' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 29.6271 
_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                            0.3091 
_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.details                          ? 
_refine_hist.d_res_high                       2.18 
_refine_hist.d_res_low                        45.90 
_refine_hist.number_atoms_solvent             307 
_refine_hist.number_atoms_total               5782 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5360 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         115 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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' ? 0.0019  ? 5613 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.4961  ? 7594 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0426  ? 830  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0034  ? 977  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.5881 ? 776  ? f_dihedral_angle_d ? ? 
# 
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_R_complete 
_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' 2.18 2.21  . . 138 2270 99.18  . . . 0.3314 . 0.3106 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.21 2.23  . . 145 2284 99.71  . . . 0.3773 . 0.3396 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.23 2.26  . . 108 2248 99.83  . . . 0.3380 . 0.3260 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.26 2.29  . . 154 2216 99.96  . . . 0.3706 . 0.3315 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.29 2.33  . . 132 2354 100.00 . . . 0.3906 . 0.3205 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.33 2.36  . . 132 2228 100.00 . . . 0.3341 . 0.3136 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.36 2.40  . . 135 2295 100.00 . . . 0.3676 . 0.2969 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.40 2.44  . . 147 2312 100.00 . . . 0.2881 . 0.2803 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.44 2.48  . . 149 2184 100.00 . . . 0.2576 . 0.2730 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.48 2.53  . . 119 2344 100.00 . . . 0.3204 . 0.2737 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.53 2.57  . . 138 2276 100.00 . . . 0.3613 . 0.2736 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.57 2.63  . . 153 2209 100.00 . . . 0.2939 . 0.2880 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.63 2.68  . . 132 2301 99.92  . . . 0.3298 . 0.2730 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.68 2.75  . . 129 2293 100.00 . . . 0.4077 . 0.2726 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.75 2.81  . . 156 2260 99.96  . . . 0.3080 . 0.2736 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.82 2.89  . . 149 2244 100.00 . . . 0.3358 . 0.2605 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.89 2.98  . . 109 2322 100.00 . . . 0.3292 . 0.2726 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.98 3.07  . . 161 2207 99.87  . . . 0.3191 . 0.2636 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.07 3.18  . . 130 2282 99.96  . . . 0.2858 . 0.2497 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.18 3.31  . . 137 2297 100.00 . . . 0.2796 . 0.2211 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.31 3.46  . . 135 2299 100.00 . . . 0.2882 . 0.2256 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.46 3.64  . . 124 2244 100.00 . . . 0.2581 . 0.2066 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.64 3.87  . . 154 2275 100.00 . . . 0.2534 . 0.2025 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.87 4.17  . . 133 2250 99.92  . . . 0.2133 . 0.1844 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.17 4.59  . . 154 2258 99.88  . . . 0.2032 . 0.1624 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.59 5.25  . . 138 2291 100.00 . . . 0.2008 . 0.1523 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 5.25 6.61  . . 140 2272 99.92  . . . 0.2504 . 0.1938 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 6.62 45.90 . . 121 2276 99.71  . . . 0.1752 . 0.1569 . . . . . . . . . . . 
# 
_struct.entry_id                     6YED 
_struct.title                        
;E.coli's Putrescine receptor PotF in its open apo state
;
_struct.pdbx_descriptor              'Putrescine-binding periplasmic protein' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        6YED 
_struct_keywords.text            'Periplasmic binding protein, E.coli, open apo, TRANSPORT PROTEIN' 
_struct_keywords.pdbx_keywords   'TRANSPORT 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 1 ? 
C  N N 2 ? 
D  N N 3 ? 
E  N N 3 ? 
F  N N 4 ? 
G  N N 4 ? 
H  N N 4 ? 
I  N N 4 ? 
J  N N 4 ? 
K  N N 4 ? 
L  N N 4 ? 
M  N N 4 ? 
N  N N 4 ? 
O  N N 4 ? 
P  N N 4 ? 
Q  N N 5 ? 
R  N N 5 ? 
S  N N 3 ? 
T  N N 3 ? 
U  N N 3 ? 
V  N N 3 ? 
W  N N 4 ? 
X  N N 4 ? 
Y  N N 4 ? 
Z  N N 4 ? 
AA N N 5 ? 
BA N N 6 ? 
CA N N 6 ? 
# 
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 ASP A 18  ? GLY A 28  ? ASP A 44  GLY A 54  1 ? 11 
HELX_P HELX_P2  AA2 SER A 38  ? GLY A 49  ? SER A 64  GLY A 75  1 ? 12 
HELX_P HELX_P3  AA3 SER A 59  ? GLN A 66  ? SER A 85  GLN A 92  1 ? 8  
HELX_P HELX_P4  AA4 ASP A 76  ? LEU A 86  ? ASP A 102 LEU A 112 5 ? 11 
HELX_P HELX_P5  AA5 ASP A 87  ? ALA A 95  ? ASP A 113 ALA A 121 1 ? 9  
HELX_P HELX_P6  AA6 LYS A 96  ? HIS A 97  ? LYS A 122 HIS A 123 5 ? 2  
HELX_P HELX_P7  AA7 ASP A 98  ? LYS A 102 ? ASP A 124 LYS A 128 5 ? 5  
HELX_P HELX_P8  AA8 VAL A 118 ? GLY A 126 ? VAL A 144 GLY A 152 1 ? 9  
HELX_P HELX_P9  AA9 TRP A 134 ? LYS A 139 ? TRP A 160 LYS A 165 1 ? 6  
HELX_P HELX_P10 AB1 LYS A 139 ? LYS A 147 ? LYS A 165 LYS A 173 1 ? 9  
HELX_P HELX_P11 AB2 ALA A 156 ? LEU A 168 ? ALA A 182 LEU A 194 1 ? 13 
HELX_P HELX_P12 AB3 LYS A 176 ? GLY A 182 ? LYS A 202 GLY A 208 1 ? 7  
HELX_P HELX_P13 AB4 GLY A 182 ? ARG A 192 ? GLY A 208 ARG A 218 1 ? 11 
HELX_P HELX_P14 AB5 PRO A 193 ? ILE A 195 ? PRO A 219 ILE A 221 5 ? 3  
HELX_P HELX_P15 AB6 SER A 201 ? ASN A 209 ? SER A 227 ASN A 235 1 ? 9  
HELX_P HELX_P16 AB7 ALA A 219 ? LYS A 233 ? ALA A 245 LYS A 259 1 ? 15 
HELX_P HELX_P17 AB8 ASN A 262 ? LEU A 274 ? ASN A 288 LEU A 300 1 ? 13 
HELX_P HELX_P18 AB9 ARG A 275 ? PHE A 287 ? ARG A 301 PHE A 313 1 ? 13 
HELX_P HELX_P19 AC1 ALA A 295 ? VAL A 299 ? ALA A 321 VAL A 325 5 ? 5  
HELX_P HELX_P20 AC2 SER A 300 ? GLU A 305 ? SER A 326 GLU A 331 1 ? 6  
HELX_P HELX_P21 AC3 PRO A 312 ? ALA A 317 ? PRO A 338 ALA A 343 1 ? 6  
HELX_P HELX_P22 AC4 ASP A 326 ? SER A 342 ? ASP A 352 SER A 368 1 ? 17 
HELX_P HELX_P23 AC5 ASP B 18  ? GLY B 28  ? ASP B 44  GLY B 54  1 ? 11 
HELX_P HELX_P24 AC6 SER B 38  ? GLY B 49  ? SER B 64  GLY B 75  1 ? 12 
HELX_P HELX_P25 AC7 SER B 59  ? GLN B 66  ? SER B 85  GLN B 92  1 ? 8  
HELX_P HELX_P26 AC8 ASP B 76  ? LEU B 86  ? ASP B 102 LEU B 112 5 ? 11 
HELX_P HELX_P27 AC9 ASP B 87  ? LYS B 96  ? ASP B 113 LYS B 122 1 ? 10 
HELX_P HELX_P28 AD1 ASP B 98  ? LYS B 102 ? ASP B 124 LYS B 128 5 ? 5  
HELX_P HELX_P29 AD2 VAL B 118 ? LEU B 125 ? VAL B 144 LEU B 151 1 ? 8  
HELX_P HELX_P30 AD3 TRP B 134 ? LYS B 139 ? TRP B 160 LYS B 165 1 ? 6  
HELX_P HELX_P31 AD4 LYS B 139 ? LYS B 147 ? LYS B 165 LYS B 173 1 ? 9  
HELX_P HELX_P32 AD5 ALA B 156 ? LEU B 168 ? ALA B 182 LEU B 194 1 ? 13 
HELX_P HELX_P33 AD6 LYS B 176 ? GLY B 182 ? LYS B 202 GLY B 208 1 ? 7  
HELX_P HELX_P34 AD7 GLY B 182 ? ARG B 192 ? GLY B 208 ARG B 218 1 ? 11 
HELX_P HELX_P35 AD8 PRO B 193 ? ILE B 195 ? PRO B 219 ILE B 221 5 ? 3  
HELX_P HELX_P36 AD9 SER B 201 ? ASN B 209 ? SER B 227 ASN B 235 1 ? 9  
HELX_P HELX_P37 AE1 ALA B 219 ? LYS B 233 ? ALA B 245 LYS B 259 1 ? 15 
HELX_P HELX_P38 AE2 ASN B 262 ? ARG B 275 ? ASN B 288 ARG B 301 1 ? 14 
HELX_P HELX_P39 AE3 ARG B 275 ? PHE B 287 ? ARG B 301 PHE B 313 1 ? 13 
HELX_P HELX_P40 AE4 ALA B 295 ? VAL B 299 ? ALA B 321 VAL B 325 5 ? 5  
HELX_P HELX_P41 AE5 SER B 300 ? GLU B 305 ? SER B 326 GLU B 331 1 ? 6  
HELX_P HELX_P42 AE6 PRO B 312 ? ALA B 317 ? PRO B 338 ALA B 343 1 ? 6  
HELX_P HELX_P43 AE7 ASP B 326 ? LYS B 341 ? ASP B 352 LYS B 367 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 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 149 SG A ? ? 1_555 A CYS 213 SG A ? A CYS 175 A CYS 239 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
disulf2 disulf ? ? B CYS 149 SG A ? ? 1_555 B CYS 213 SG A ? B CYS 175 B CYS 239 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
AA4 ? 3 ? 
AA5 ? 5 ? 
AA6 ? 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 ? parallel      
AA1 2 3 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 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 LYS A 30  ? PHE A 36  ? LYS A 56  PHE A 62  
AA1 2 THR A 5   ? TRP A 11  ? THR A 31  TRP A 37  
AA1 3 LEU A 55  ? VAL A 56  ? LEU A 81  VAL A 82  
AA2 1 TYR A 197 ? PHE A 198 ? TYR A 223 PHE A 224 
AA2 2 VAL A 151 ? PHE A 153 ? VAL A 177 PHE A 179 
AA2 3 VAL A 214 ? TRP A 218 ? VAL A 240 TRP A 244 
AA2 4 ALA A 104 ? ASN A 117 ? ALA A 130 ASN A 143 
AA2 5 MET A 248 ? ALA A 255 ? MET A 274 ALA A 281 
AA3 1 VAL A 238 ? SER A 241 ? VAL A 264 SER A 267 
AA3 2 ALA A 104 ? ASN A 117 ? ALA A 130 ASN A 143 
AA3 3 ALA A 289 ? ASN A 290 ? ALA A 315 ASN A 316 
AA4 1 LYS B 30  ? PHE B 36  ? LYS B 56  PHE B 62  
AA4 2 THR B 5   ? TRP B 11  ? THR B 31  TRP B 37  
AA4 3 LEU B 55  ? VAL B 56  ? LEU B 81  VAL B 82  
AA5 1 TYR B 197 ? PHE B 198 ? TYR B 223 PHE B 224 
AA5 2 VAL B 151 ? PHE B 153 ? VAL B 177 PHE B 179 
AA5 3 VAL B 214 ? TRP B 218 ? VAL B 240 TRP B 244 
AA5 4 MET B 105 ? ASN B 117 ? MET B 131 ASN B 143 
AA5 5 MET B 248 ? PHE B 254 ? MET B 274 PHE B 280 
AA6 1 VAL B 238 ? SER B 241 ? VAL B 264 SER B 267 
AA6 2 MET B 105 ? ASN B 117 ? MET B 131 ASN B 143 
AA6 3 ALA B 289 ? ASN B 290 ? ALA B 315 ASN B 316 
# 
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 VAL A 32  ? O VAL A 58  N LEU A 6   ? N LEU A 32  
AA1 2 3 N TYR A 9   ? N TYR A 35  O LEU A 55  ? O LEU A 81  
AA2 1 2 O TYR A 197 ? O TYR A 223 N PHE A 153 ? N PHE A 179 
AA2 2 3 N SER A 152 ? N SER A 178 O ILE A 216 ? O ILE A 242 
AA2 3 4 O GLY A 217 ? O GLY A 243 N GLY A 113 ? N GLY A 139 
AA2 4 5 N TYR A 107 ? N TYR A 133 O ASP A 252 ? O ASP A 278 
AA3 1 2 O SER A 239 ? O SER A 265 N TYR A 116 ? N TYR A 142 
AA3 2 3 N TRP A 109 ? N TRP A 135 O ALA A 289 ? O ALA A 315 
AA4 1 2 O VAL B 32  ? O VAL B 58  N LEU B 6   ? N LEU B 32  
AA4 2 3 N TYR B 9   ? N TYR B 35  O LEU B 55  ? O LEU B 81  
AA5 1 2 O TYR B 197 ? O TYR B 223 N PHE B 153 ? N PHE B 179 
AA5 2 3 N SER B 152 ? N SER B 178 O VAL B 214 ? O VAL B 240 
AA5 3 4 O GLY B 217 ? O GLY B 243 N GLY B 113 ? N GLY B 139 
AA5 4 5 N MET B 105 ? N MET B 131 O PHE B 254 ? O PHE B 280 
AA6 1 2 O SER B 241 ? O SER B 267 N ILE B 114 ? N ILE B 140 
AA6 2 3 N TRP B 109 ? N TRP B 135 O ALA B 289 ? O ALA B 315 
# 
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 PGE 401 ? 2 'binding site for residue PGE A 401' 
AC2 Software A PEG 402 ? 2 'binding site for residue PEG A 402' 
AC3 Software A PEG 403 ? 8 'binding site for residue PEG A 403' 
AC4 Software A EDO 404 ? 8 'binding site for residue EDO A 404' 
AC5 Software A EDO 405 ? 7 'binding site for residue EDO A 405' 
AC6 Software A EDO 406 ? 2 'binding site for residue EDO A 406' 
AC7 Software A EDO 407 ? 5 'binding site for residue EDO A 407' 
AC8 Software A EDO 408 ? 5 'binding site for residue EDO A 408' 
AC9 Software A EDO 409 ? 5 'binding site for residue EDO A 409' 
AD1 Software A EDO 410 ? 3 'binding site for residue EDO A 410' 
AD2 Software A EDO 411 ? 6 'binding site for residue EDO A 411' 
AD3 Software A EDO 412 ? 4 'binding site for residue EDO A 412' 
AD4 Software A EDO 413 ? 5 'binding site for residue EDO A 413' 
AD5 Software A EDO 414 ? 4 'binding site for residue EDO A 414' 
AD6 Software A CL  415 ? 2 'binding site for residue CL A 415'  
AD7 Software A CL  416 ? 1 'binding site for residue CL A 416'  
AD8 Software B PEG 401 ? 4 'binding site for residue PEG B 401' 
AD9 Software B PEG 402 ? 3 'binding site for residue PEG B 402' 
AE1 Software B PEG 403 ? 6 'binding site for residue PEG B 403' 
AE2 Software B PEG 404 ? 6 'binding site for residue PEG B 404' 
AE3 Software B EDO 405 ? 6 'binding site for residue EDO B 405' 
AE4 Software B EDO 406 ? 2 'binding site for residue EDO B 406' 
AE5 Software B EDO 407 ? 3 'binding site for residue EDO B 407' 
AE6 Software B EDO 408 ? 5 'binding site for residue EDO B 408' 
AE7 Software B CL  409 ? 2 'binding site for residue CL B 409'  
# 
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 2 GLY A  220 ? GLY A 246 . ? 1_555 ? 
2   AC1 2 HOH BA .   ? HOH A 588 . ? 1_555 ? 
3   AC2 2 GLU A  89  ? GLU A 115 . ? 1_555 ? 
4   AC2 2 LYS A  92  ? LYS A 118 . ? 1_555 ? 
5   AC3 8 ASN A  166 ? ASN A 192 . ? 1_555 ? 
6   AC3 8 ASP A  171 ? ASP A 197 . ? 1_555 ? 
7   AC3 8 PRO A  172 ? PRO A 198 . ? 1_555 ? 
8   AC3 8 ASN A  173 ? ASN A 199 . ? 1_555 ? 
9   AC3 8 LYS A  318 ? LYS A 344 . ? 1_555 ? 
10  AC3 8 PHE A  320 ? PHE A 346 . ? 1_555 ? 
11  AC3 8 LYS A  323 ? LYS A 349 . ? 1_555 ? 
12  AC3 8 HOH BA .   ? HOH A 583 . ? 1_555 ? 
13  AC4 8 TRP A  109 ? TRP A 135 . ? 1_555 ? 
14  AC4 8 ALA A  110 ? ALA A 136 . ? 1_555 ? 
15  AC4 8 ILE A  242 ? ILE A 268 . ? 1_555 ? 
16  AC4 8 TYR A  288 ? TYR A 314 . ? 1_555 ? 
17  AC4 8 ALA A  289 ? ALA A 315 . ? 1_555 ? 
18  AC4 8 ILE A  309 ? ILE A 335 . ? 1_555 ? 
19  AC4 8 HOH BA .   ? HOH A 515 . ? 1_555 ? 
20  AC4 8 HOH BA .   ? HOH A 625 . ? 1_555 ? 
21  AC5 7 HIS A  7   ? HIS A 33  . ? 1_555 ? 
22  AC5 7 VAL A  32  ? VAL A 58  . ? 1_555 ? 
23  AC5 7 ASP A  34  ? ASP A 60  . ? 1_555 ? 
24  AC5 7 LEU A  168 ? LEU A 194 . ? 1_545 ? 
25  AC5 7 PRO A  183 ? PRO A 209 . ? 1_545 ? 
26  AC5 7 HOH BA .   ? HOH A 504 . ? 1_555 ? 
27  AC5 7 HOH BA .   ? HOH A 602 . ? 1_555 ? 
28  AC6 2 PRO A  17  ? PRO A 43  . ? 1_555 ? 
29  AC6 2 ALA A  21  ? ALA A 47  . ? 1_555 ? 
30  AC7 5 ALA A  60  ? ALA A 86  . ? 1_555 ? 
31  AC7 5 SER A  61  ? SER A 87  . ? 1_555 ? 
32  AC7 5 HIS A  97  ? HIS A 123 . ? 1_555 ? 
33  AC7 5 PHE A  250 ? PHE A 276 . ? 1_555 ? 
34  AC7 5 PHE A  251 ? PHE A 277 . ? 1_555 ? 
35  AC8 5 LYS A  84  ? LYS A 110 . ? 1_555 ? 
36  AC8 5 ASN A  85  ? ASN A 111 . ? 1_555 ? 
37  AC8 5 LEU A  86  ? LEU A 112 . ? 1_555 ? 
38  AC8 5 PRO A  88  ? PRO A 114 . ? 1_555 ? 
39  AC8 5 LYS A  293 ? LYS A 319 . ? 1_555 ? 
40  AC9 5 GLU A  89  ? GLU A 115 . ? 1_555 ? 
41  AC9 5 LYS A  293 ? LYS A 319 . ? 1_555 ? 
42  AC9 5 ALA A  313 ? ALA A 339 . ? 1_555 ? 
43  AC9 5 ARG A  316 ? ARG A 342 . ? 1_555 ? 
44  AC9 5 HOH BA .   ? HOH A 540 . ? 1_555 ? 
45  AD1 3 ASP A  155 ? ASP A 181 . ? 1_555 ? 
46  AD1 3 PRO A  157 ? PRO A 183 . ? 1_555 ? 
47  AD1 3 GLU A  158 ? GLU A 184 . ? 1_555 ? 
48  AD2 6 LYS A  244 ? LYS A 270 . ? 1_555 ? 
49  AD2 6 PRO A  307 ? PRO A 333 . ? 1_555 ? 
50  AD2 6 PRO A  312 ? PRO A 338 . ? 1_555 ? 
51  AD2 6 VAL A  315 ? VAL A 341 . ? 1_555 ? 
52  AD2 6 HOH BA .   ? HOH A 605 . ? 1_555 ? 
53  AD2 6 HOH BA .   ? HOH A 613 . ? 1_555 ? 
54  AD3 4 ARG A  192 ? ARG A 218 . ? 1_555 ? 
55  AD3 4 ARG A  196 ? ARG A 222 . ? 1_555 ? 
56  AD3 4 TYR A  197 ? TYR A 223 . ? 1_555 ? 
57  AD3 4 PHE A  198 ? PHE A 224 . ? 1_555 ? 
58  AD4 5 PRO A  88  ? PRO A 114 . ? 1_555 ? 
59  AD4 5 LEU A  91  ? LEU A 117 . ? 1_555 ? 
60  AD4 5 LYS A  92  ? LYS A 118 . ? 1_555 ? 
61  AD4 5 ASN A  101 ? ASN A 127 . ? 1_555 ? 
62  AD4 5 EDO P  .   ? EDO A 414 . ? 1_555 ? 
63  AD5 4 ALA A  95  ? ALA A 121 . ? 1_555 ? 
64  AD5 4 PRO A  99  ? PRO A 125 . ? 1_555 ? 
65  AD5 4 ASP A  100 ? ASP A 126 . ? 1_555 ? 
66  AD5 4 EDO O  .   ? EDO A 413 . ? 1_555 ? 
67  AD6 2 TRP A  11  ? TRP A 37  . ? 1_555 ? 
68  AD6 2 HOH BA .   ? HOH A 507 . ? 1_555 ? 
69  AD7 1 GLU A  159 ? GLU A 185 . ? 1_555 ? 
70  AD8 4 ASN B  39  ? ASN B 65  . ? 1_555 ? 
71  AD8 4 ASP B  221 ? ASP B 247 . ? 1_555 ? 
72  AD8 4 PEG T  .   ? PEG B 402 . ? 1_555 ? 
73  AD8 4 EDO Z  .   ? EDO B 408 . ? 1_555 ? 
74  AD9 3 TRP B  218 ? TRP B 244 . ? 1_555 ? 
75  AD9 3 PEG S  .   ? PEG B 401 . ? 1_555 ? 
76  AD9 3 HOH CA .   ? HOH B 520 . ? 1_555 ? 
77  AE1 6 ASN B  22  ? ASN B 48  . ? 1_555 ? 
78  AE1 6 GLU B  26  ? GLU B 52  . ? 1_555 ? 
79  AE1 6 TYR B  272 ? TYR B 298 . ? 1_555 ? 
80  AE1 6 ARG B  275 ? ARG B 301 . ? 1_555 ? 
81  AE1 6 ASP B  277 ? ASP B 303 . ? 1_555 ? 
82  AE1 6 VAL B  278 ? VAL B 304 . ? 1_555 ? 
83  AE2 6 PRO A  297 ? PRO A 323 . ? 1_555 ? 
84  AE2 6 ASP B  284 ? ASP B 310 . ? 1_555 ? 
85  AE2 6 SER B  300 ? SER B 326 . ? 1_555 ? 
86  AE2 6 ALA B  301 ? ALA B 327 . ? 1_555 ? 
87  AE2 6 HOH CA .   ? HOH B 504 . ? 1_555 ? 
88  AE2 6 HOH CA .   ? HOH B 531 . ? 1_555 ? 
89  AE3 6 TRP B  109 ? TRP B 135 . ? 1_555 ? 
90  AE3 6 ALA B  110 ? ALA B 136 . ? 1_555 ? 
91  AE3 6 ILE B  242 ? ILE B 268 . ? 1_555 ? 
92  AE3 6 ALA B  289 ? ALA B 315 . ? 1_555 ? 
93  AE3 6 ILE B  309 ? ILE B 335 . ? 1_555 ? 
94  AE3 6 HOH CA .   ? HOH B 538 . ? 1_555 ? 
95  AE4 2 LYS B  293 ? LYS B 319 . ? 1_555 ? 
96  AE4 2 HOH CA .   ? HOH B 541 . ? 1_555 ? 
97  AE5 3 ASP B  87  ? ASP B 113 . ? 1_555 ? 
98  AE5 3 THR B  296 ? THR B 322 . ? 1_555 ? 
99  AE5 3 ARG B  316 ? ARG B 342 . ? 1_555 ? 
100 AE6 5 GLY B  220 ? GLY B 246 . ? 1_555 ? 
101 AE6 5 PHE B  250 ? PHE B 276 . ? 1_555 ? 
102 AE6 5 TYR B  288 ? TYR B 314 . ? 1_555 ? 
103 AE6 5 PEG S  .   ? PEG B 401 . ? 1_555 ? 
104 AE6 5 CL  AA .   ? CL  B 409 . ? 1_555 ? 
105 AE7 2 ASP B  252 ? ASP B 278 . ? 1_555 ? 
106 AE7 2 EDO Z  .   ? EDO B 408 . ? 1_555 ? 
# 
_atom_sites.entry_id                    6YED 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.013120 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005193 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018709 
_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]   0.012203 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . GLN A  1 3   ? -6.60641  -46.17031 34.63625  1.000 66.03216  ? 29  GLN A N   1 
ATOM   2    C  CA  . GLN A  1 3   ? -6.13191  -45.84479 33.29639  1.000 65.80990  ? 29  GLN A CA  1 
ATOM   3    C  C   . GLN A  1 3   ? -6.14992  -44.33809 33.05659  1.000 61.79992  ? 29  GLN A C   1 
ATOM   4    O  O   . GLN A  1 3   ? -5.59790  -43.85188 32.06962  1.000 61.84399  ? 29  GLN A O   1 
ATOM   5    C  CB  . GLN A  1 3   ? -6.98009  -46.55557 32.23874  1.000 68.92592  ? 29  GLN A CB  1 
ATOM   6    C  CG  . GLN A  1 3   ? -6.75264  -48.05726 32.16251  1.000 71.41557  ? 29  GLN A CG  1 
ATOM   7    C  CD  . GLN A  1 3   ? -7.17289  -48.64366 30.82808  1.000 73.24307  ? 29  GLN A CD  1 
ATOM   8    O  OE1 . GLN A  1 3   ? -7.56449  -49.80786 30.74395  1.000 74.85439  ? 29  GLN A OE1 1 
ATOM   9    N  NE2 . GLN A  1 3   ? -7.09205  -47.83768 29.77559  1.000 72.53552  ? 29  GLN A NE2 1 
ATOM   10   N  N   . LYS A  1 4   ? -6.78836  -43.60451 33.96557  1.000 59.09863  ? 30  LYS A N   1 
ATOM   11   C  CA  . LYS A  1 4   ? -6.88084  -42.15454 33.84206  1.000 56.19997  ? 30  LYS A CA  1 
ATOM   12   C  C   . LYS A  1 4   ? -5.52796  -41.52069 34.14723  1.000 51.35912  ? 30  LYS A C   1 
ATOM   13   O  O   . LYS A  1 4   ? -4.98547  -41.69464 35.24367  1.000 51.34740  ? 30  LYS A O   1 
ATOM   14   C  CB  . LYS A  1 4   ? -7.95646  -41.61593 34.78144  1.000 57.75844  ? 30  LYS A CB  1 
ATOM   15   C  CG  . LYS A  1 4   ? -9.24128  -42.43079 34.77770  1.000 60.79459  ? 30  LYS A CG  1 
ATOM   16   C  CD  . LYS A  1 4   ? -10.45661 -41.55134 34.53463  1.000 62.48839  ? 30  LYS A CD  1 
ATOM   17   C  CE  . LYS A  1 4   ? -11.16098 -41.20973 35.83764  1.000 63.87597  ? 30  LYS A CE  1 
ATOM   18   N  NZ  . LYS A  1 4   ? -12.50088 -40.60413 35.60198  1.000 65.82316  ? 30  LYS A NZ  1 
ATOM   19   N  N   . THR A  1 5   ? -4.98791  -40.77984 33.18083  1.000 48.67723  ? 31  THR A N   1 
ATOM   20   C  CA  . THR A  1 5   ? -3.64811  -40.21648 33.27136  1.000 45.17559  ? 31  THR A CA  1 
ATOM   21   C  C   . THR A  1 5   ? -3.70118  -38.71594 33.01814  1.000 40.90264  ? 31  THR A C   1 
ATOM   22   O  O   . THR A  1 5   ? -4.49729  -38.24365 32.20152  1.000 41.31351  ? 31  THR A O   1 
ATOM   23   C  CB  . THR A  1 5   ? -2.70139  -40.89759 32.26294  1.000 45.78313  ? 31  THR A CB  1 
ATOM   24   O  OG1 . THR A  1 5   ? -2.55928  -42.28216 32.60179  1.000 47.59405  ? 31  THR A OG1 1 
ATOM   25   C  CG2 . THR A  1 5   ? -1.32615  -40.24781 32.26722  1.000 45.25196  ? 31  THR A CG2 1 
ATOM   26   N  N   . LEU A  1 6   ? -2.85947  -37.97044 33.73398  1.000 37.54225  ? 32  LEU A N   1 
ATOM   27   C  CA  . LEU A  1 6   ? -2.72482  -36.53268 33.53776  1.000 34.28704  ? 32  LEU A CA  1 
ATOM   28   C  C   . LEU A  1 6   ? -1.29147  -36.13447 33.85779  1.000 32.72767  ? 32  LEU A C   1 
ATOM   29   O  O   . LEU A  1 6   ? -0.78412  -36.46279 34.93387  1.000 31.95833  ? 32  LEU A O   1 
ATOM   30   C  CB  . LEU A  1 6   ? -3.71055  -35.76090 34.42055  1.000 33.16991  ? 32  LEU A CB  1 
ATOM   31   C  CG  . LEU A  1 6   ? -3.61468  -34.23576 34.40396  1.000 25.43978  ? 32  LEU A CG  1 
ATOM   32   C  CD1 . LEU A  1 6   ? -3.82687  -33.69485 33.00160  1.000 25.78573  ? 32  LEU A CD1 1 
ATOM   33   C  CD2 . LEU A  1 6   ? -4.62619  -33.64467 35.36488  1.000 29.01043  ? 32  LEU A CD2 1 
ATOM   34   N  N   . HIS A  1 7   ? -0.64626  -35.43067 32.92856  1.000 32.72537  ? 33  HIS A N   1 
ATOM   35   C  CA  . HIS A  1 7   ? 0.76519   -35.07546 33.03718  1.000 32.55022  ? 33  HIS A CA  1 
ATOM   36   C  C   . HIS A  1 7   ? 0.89535   -33.56080 33.11696  1.000 31.91944  ? 33  HIS A C   1 
ATOM   37   O  O   . HIS A  1 7   ? 0.55286   -32.85487 32.16214  1.000 32.00114  ? 33  HIS A O   1 
ATOM   38   C  CB  . HIS A  1 7   ? 1.55557   -35.62421 31.84716  1.000 35.31459  ? 33  HIS A CB  1 
ATOM   39   C  CG  . HIS A  1 7   ? 3.02119   -35.77576 32.11073  1.000 40.24023  ? 33  HIS A CG  1 
ATOM   40   N  ND1 . HIS A  1 7   ? 3.90805   -36.21207 31.15014  1.000 42.73024  ? 33  HIS A ND1 1 
ATOM   41   C  CD2 . HIS A  1 7   ? 3.75573   -35.54911 33.22541  1.000 41.11076  ? 33  HIS A CD2 1 
ATOM   42   C  CE1 . HIS A  1 7   ? 5.12539   -36.24905 31.66179  1.000 42.25284  ? 33  HIS A CE1 1 
ATOM   43   N  NE2 . HIS A  1 7   ? 5.06060   -35.85119 32.91966  1.000 41.40388  ? 33  HIS A NE2 1 
ATOM   44   N  N   . ILE A  1 8   ? 1.40403   -33.06710 34.24514  1.000 30.57421  ? 34  ILE A N   1 
ATOM   45   C  CA  . ILE A  1 8   ? 1.48947   -31.63826 34.52321  1.000 28.82504  ? 34  ILE A CA  1 
ATOM   46   C  C   . ILE A  1 8   ? 2.95381   -31.24039 34.65523  1.000 27.90846  ? 34  ILE A C   1 
ATOM   47   O  O   . ILE A  1 8   ? 3.77059   -32.00356 35.18289  1.000 25.97392  ? 34  ILE A O   1 
ATOM   48   C  CB  . ILE A  1 8   ? 0.70386   -31.26631 35.79938  1.000 28.15631  ? 34  ILE A CB  1 
ATOM   49   C  CG1 . ILE A  1 8   ? -0.71166  -31.84377 35.73996  1.000 29.39957  ? 34  ILE A CG1 1 
ATOM   50   C  CG2 . ILE A  1 8   ? 0.64817   -29.75663 35.98431  1.000 25.86569  ? 34  ILE A CG2 1 
ATOM   51   C  CD1 . ILE A  1 8   ? -1.55854  -31.50861 36.94764  1.000 29.26304  ? 34  ILE A CD1 1 
ATOM   52   N  N   . TYR A  1 9   ? 3.27924   -30.04043 34.17286  1.000 27.52636  ? 35  TYR A N   1 
ATOM   53   C  CA  . TYR A  1 9   ? 4.61824   -29.46789 34.26984  1.000 26.80914  ? 35  TYR A CA  1 
ATOM   54   C  C   . TYR A  1 9   ? 4.49655   -28.07399 34.86799  1.000 23.83604  ? 35  TYR A C   1 
ATOM   55   O  O   . TYR A  1 9   ? 3.90787   -27.18171 34.24869  1.000 20.16096  ? 35  TYR A O   1 
ATOM   56   C  CB  . TYR A  1 9   ? 5.29148   -29.41108 32.89494  1.000 30.50256  ? 35  TYR A CB  1 
ATOM   57   C  CG  . TYR A  1 9   ? 6.80141   -29.51246 32.92286  1.000 31.73948  ? 35  TYR A CG  1 
ATOM   58   C  CD1 . TYR A  1 9   ? 7.45199   -30.29296 33.87050  1.000 30.05332  ? 35  TYR A CD1 1 
ATOM   59   C  CD2 . TYR A  1 9   ? 7.57618   -28.83269 31.99107  1.000 31.34048  ? 35  TYR A CD2 1 
ATOM   60   C  CE1 . TYR A  1 9   ? 8.83375   -30.38832 33.89109  1.000 31.29021  ? 35  TYR A CE1 1 
ATOM   61   C  CE2 . TYR A  1 9   ? 8.95523   -28.92197 32.00340  1.000 31.91324  ? 35  TYR A CE2 1 
ATOM   62   C  CZ  . TYR A  1 9   ? 9.57923   -29.70019 32.95453  1.000 33.69117  ? 35  TYR A CZ  1 
ATOM   63   O  OH  . TYR A  1 9   ? 10.95290  -29.78868 32.96711  1.000 36.19185  ? 35  TYR A OH  1 
ATOM   64   N  N   . ASN A  1 10  ? 5.05500   -27.88448 36.06258  1.000 23.78766  ? 36  ASN A N   1 
ATOM   65   C  CA  . ASN A  1 10  ? 4.87229   -26.65258 36.81746  1.000 22.62435  ? 36  ASN A CA  1 
ATOM   66   C  C   . ASN A  1 10  ? 6.17937   -26.28027 37.50566  1.000 23.51749  ? 36  ASN A C   1 
ATOM   67   O  O   . ASN A  1 10  ? 7.12588   -27.06823 37.55789  1.000 24.80777  ? 36  ASN A O   1 
ATOM   68   C  CB  . ASN A  1 10  ? 3.73830   -26.80397 37.84371  1.000 21.00965  ? 36  ASN A CB  1 
ATOM   69   C  CG  . ASN A  1 10  ? 3.28770   -25.47764 38.42483  1.000 21.28301  ? 36  ASN A CG  1 
ATOM   70   O  OD1 . ASN A  1 10  ? 3.72345   -24.41324 37.98666  1.000 21.86749  ? 36  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A  1 10  ? 2.40533   -25.53640 39.41523  1.000 17.94732  ? 36  ASN A ND2 1 
ATOM   72   N  N   . TRP A  1 11  ? 6.23178   -25.05428 38.02262  1.000 23.26237  ? 37  TRP A N   1 
ATOM   73   C  CA  . TRP A  1 11  ? 7.34788   -24.64997 38.86561  1.000 24.98503  ? 37  TRP A CA  1 
ATOM   74   C  C   . TRP A  1 11  ? 7.38195   -25.49675 40.13241  1.000 24.86502  ? 37  TRP A C   1 
ATOM   75   O  O   . TRP A  1 11  ? 6.35918   -26.01660 40.58708  1.000 22.26828  ? 37  TRP A O   1 
ATOM   76   C  CB  . TRP A  1 11  ? 7.23333   -23.17227 39.24697  1.000 25.03248  ? 37  TRP A CB  1 
ATOM   77   C  CG  . TRP A  1 11  ? 7.49492   -22.20355 38.13722  1.000 27.32641  ? 37  TRP A CG  1 
ATOM   78   C  CD1 . TRP A  1 11  ? 6.59380   -21.73951 37.22449  1.000 27.91698  ? 37  TRP A CD1 1 
ATOM   79   C  CD2 . TRP A  1 11  ? 8.73783   -21.55582 37.83932  1.000 30.29205  ? 37  TRP A CD2 1 
ATOM   80   N  NE1 . TRP A  1 11  ? 7.20076   -20.85213 36.36915  1.000 29.81418  ? 37  TRP A NE1 1 
ATOM   81   C  CE2 . TRP A  1 11  ? 8.51727   -20.72181 36.72547  1.000 30.41068  ? 37  TRP A CE2 1 
ATOM   82   C  CE3 . TRP A  1 11  ? 10.01724  -21.60526 38.40246  1.000 32.25670  ? 37  TRP A CE3 1 
ATOM   83   C  CZ2 . TRP A  1 11  ? 9.52791   -19.94383 36.16334  1.000 32.11941  ? 37  TRP A CZ2 1 
ATOM   84   C  CZ3 . TRP A  1 11  ? 11.01939  -20.83188 37.84305  1.000 32.43647  ? 37  TRP A CZ3 1 
ATOM   85   C  CH2 . TRP A  1 11  ? 10.76883  -20.01266 36.73516  1.000 32.55491  ? 37  TRP A CH2 1 
ATOM   86   N  N   . SER A  1 12  ? 8.57381   -25.63181 40.70647  1.000 26.13724  ? 38  SER A N   1 
ATOM   87   C  CA  . SER A  1 12  ? 8.70322   -26.31035 41.98760  1.000 28.13126  ? 38  SER A CA  1 
ATOM   88   C  C   . SER A  1 12  ? 8.06191   -25.47531 43.08811  1.000 26.07539  ? 38  SER A C   1 
ATOM   89   O  O   . SER A  1 12  ? 8.17082   -24.24586 43.09776  1.000 26.16455  ? 38  SER A O   1 
ATOM   90   C  CB  . SER A  1 12  ? 10.17421  -26.56819 42.31356  1.000 32.23916  ? 38  SER A CB  1 
ATOM   91   O  OG  . SER A  1 12  ? 10.79313  -27.35366 41.30981  1.000 38.40767  ? 38  SER A OG  1 
ATOM   92   N  N   . ASP A  1 13  ? 7.37908   -26.15458 44.01176  1.000 26.71441  ? 39  ASP A N   1 
ATOM   93   C  CA  . ASP A  1 13  ? 6.73435   -25.50797 45.15716  1.000 30.06598  ? 39  ASP A CA  1 
ATOM   94   C  C   . ASP A  1 13  ? 5.79396   -24.38976 44.70936  1.000 28.42363  ? 39  ASP A C   1 
ATOM   95   O  O   . ASP A  1 13  ? 5.65129   -23.36070 45.37330  1.000 28.30747  ? 39  ASP A O   1 
ATOM   96   C  CB  . ASP A  1 13  ? 7.77713   -24.98479 46.14782  1.000 33.36498  ? 39  ASP A CB  1 
ATOM   97   C  CG  . ASP A  1 13  ? 7.21029   -24.78374 47.54053  1.000 38.24724  ? 39  ASP A CG  1 
ATOM   98   O  OD1 . ASP A  1 13  ? 6.58638   -25.72532 48.07361  1.000 40.93668  ? 39  ASP A OD1 1 
ATOM   99   O  OD2 . ASP A  1 13  ? 7.38970   -23.68293 48.10231  1.000 40.59537  ? 39  ASP A OD2 1 
ATOM   100  N  N   . TYR A  1 14  ? 5.14755   -24.59313 43.56169  1.000 26.43114  ? 40  TYR A N   1 
ATOM   101  C  CA  . TYR A  1 14  ? 4.19788   -23.63588 43.00896  1.000 25.75106  ? 40  TYR A CA  1 
ATOM   102  C  C   . TYR A  1 14  ? 2.76392   -24.14226 43.12326  1.000 26.29501  ? 40  TYR A C   1 
ATOM   103  O  O   . TYR A  1 14  ? 1.89758   -23.77010 42.32835  1.000 27.94199  ? 40  TYR A O   1 
ATOM   104  C  CB  . TYR A  1 14  ? 4.54058   -23.32151 41.55471  1.000 24.64327  ? 40  TYR A CB  1 
ATOM   105  C  CG  . TYR A  1 14  ? 4.08317   -21.95661 41.09243  1.000 24.52152  ? 40  TYR A CG  1 
ATOM   106  C  CD1 . TYR A  1 14  ? 3.94847   -20.90510 41.99031  1.000 24.12058  ? 40  TYR A CD1 1 
ATOM   107  C  CD2 . TYR A  1 14  ? 3.79748   -21.71653 39.75514  1.000 23.62064  ? 40  TYR A CD2 1 
ATOM   108  C  CE1 . TYR A  1 14  ? 3.53393   -19.65457 41.56877  1.000 23.41533  ? 40  TYR A CE1 1 
ATOM   109  C  CE2 . TYR A  1 14  ? 3.38390   -20.47110 39.32464  1.000 21.03860  ? 40  TYR A CE2 1 
ATOM   110  C  CZ  . TYR A  1 14  ? 3.25402   -19.44434 40.23445  1.000 22.80793  ? 40  TYR A CZ  1 
ATOM   111  O  OH  . TYR A  1 14  ? 2.84385   -18.20220 39.80786  1.000 23.35009  ? 40  TYR A OH  1 
ATOM   112  N  N   . ILE A  1 15  ? 2.50909   -25.00163 44.10867  1.000 25.24711  ? 41  ILE A N   1 
ATOM   113  C  CA  . ILE A  1 15  ? 1.17989   -25.55180 44.34399  1.000 25.54410  ? 41  ILE A CA  1 
ATOM   114  C  C   . ILE A  1 15  ? 1.11808   -25.96850 45.80462  1.000 26.01975  ? 41  ILE A C   1 
ATOM   115  O  O   . ILE A  1 15  ? 2.14703   -26.19267 46.44541  1.000 26.47883  ? 41  ILE A O   1 
ATOM   116  C  CB  . ILE A  1 15  ? 0.88282   -26.73969 43.39150  1.000 25.85190  ? 41  ILE A CB  1 
ATOM   117  C  CG1 . ILE A  1 15  ? -0.60722  -26.80042 43.05025  1.000 25.69737  ? 41  ILE A CG1 1 
ATOM   118  C  CG2 . ILE A  1 15  ? 1.35510   -28.05663 43.99666  1.000 25.66543  ? 41  ILE A CG2 1 
ATOM   119  C  CD1 . ILE A  1 15  ? -0.94100  -27.79301 41.95520  1.000 25.73158  ? 41  ILE A CD1 1 
ATOM   120  N  N   . ALA A  1 16  ? -0.09450  -26.05290 46.34371  1.000 26.07039  ? 42  ALA A N   1 
ATOM   121  C  CA  . ALA A  1 16  ? -0.25179  -26.49311 47.71808  1.000 29.99648  ? 42  ALA A CA  1 
ATOM   122  C  C   . ALA A  1 16  ? 0.15727   -27.96037 47.84472  1.000 33.28014  ? 42  ALA A C   1 
ATOM   123  O  O   . ALA A  1 16  ? -0.02990  -28.74743 46.91278  1.000 34.58600  ? 42  ALA A O   1 
ATOM   124  C  CB  . ALA A  1 16  ? -1.69167  -26.30354 48.18507  1.000 31.05524  ? 42  ALA A CB  1 
ATOM   125  N  N   . PRO A  1 17  ? 0.72595   -28.35046 48.98854  1.000 34.43657  ? 43  PRO A N   1 
ATOM   126  C  CA  . PRO A  1 17  ? 1.27379   -29.71281 49.11066  1.000 34.52355  ? 43  PRO A CA  1 
ATOM   127  C  C   . PRO A  1 17  ? 0.25433   -30.82160 48.90668  1.000 34.87754  ? 43  PRO A C   1 
ATOM   128  O  O   . PRO A  1 17  ? 0.65368   -31.95139 48.59902  1.000 35.04637  ? 43  PRO A O   1 
ATOM   129  C  CB  . PRO A  1 17  ? 1.83981   -29.73523 50.53779  1.000 35.09776  ? 43  PRO A CB  1 
ATOM   130  C  CG  . PRO A  1 17  ? 2.10300   -28.30198 50.86411  1.000 34.71510  ? 43  PRO A CG  1 
ATOM   131  C  CD  . PRO A  1 17  ? 1.01900   -27.52704 50.17429  1.000 34.69981  ? 43  PRO A CD  1 
ATOM   132  N  N   . ASP A  1 18  ? -1.04214  -30.54689 49.05712  1.000 35.05753  ? 44  ASP A N   1 
ATOM   133  C  CA  . ASP A  1 18  ? -2.05999  -31.58810 48.97130  1.000 35.46075  ? 44  ASP A CA  1 
ATOM   134  C  C   . ASP A  1 18  ? -3.04193  -31.38091 47.82369  1.000 34.11406  ? 44  ASP A C   1 
ATOM   135  O  O   . ASP A  1 18  ? -4.05227  -32.08995 47.75858  1.000 36.74135  ? 44  ASP A O   1 
ATOM   136  C  CB  . ASP A  1 18  ? -2.82512  -31.69128 50.29477  1.000 39.87733  ? 44  ASP A CB  1 
ATOM   137  C  CG  . ASP A  1 18  ? -3.32606  -30.34712 50.78615  1.000 42.23074  ? 44  ASP A CG  1 
ATOM   138  O  OD1 . ASP A  1 18  ? -2.64072  -29.33014 50.54796  1.000 41.90538  ? 44  ASP A OD1 1 
ATOM   139  O  OD2 . ASP A  1 18  ? -4.40581  -30.30846 51.41312  1.000 44.38999  ? 44  ASP A OD2 1 
ATOM   140  N  N   . THR A  1 19  ? -2.77555  -30.44047 46.91413  1.000 29.99334  ? 45  THR A N   1 
ATOM   141  C  CA  . THR A  1 19  ? -3.70089  -30.19516 45.80978  1.000 28.36967  ? 45  THR A CA  1 
ATOM   142  C  C   . THR A  1 19  ? -3.81953  -31.41784 44.90649  1.000 27.41207  ? 45  THR A C   1 
ATOM   143  O  O   . THR A  1 19  ? -4.92703  -31.89846 44.62837  1.000 26.86196  ? 45  THR A O   1 
ATOM   144  C  CB  . THR A  1 19  ? -3.24503  -28.97913 45.00169  1.000 25.87446  ? 45  THR A CB  1 
ATOM   145  O  OG1 . THR A  1 19  ? -3.14468  -27.83919 45.86233  1.000 24.15139  ? 45  THR A OG1 1 
ATOM   146  C  CG2 . THR A  1 19  ? -4.23400  -28.67839 43.88561  1.000 26.70196  ? 45  THR A CG2 1 
ATOM   147  N  N   . VAL A  1 20  ? -2.68047  -31.93360 44.43807  1.000 26.18951  ? 46  VAL A N   1 
ATOM   148  C  CA  . VAL A  1 20  ? -2.69114  -33.07308 43.52552  1.000 29.06279  ? 46  VAL A CA  1 
ATOM   149  C  C   . VAL A  1 20  ? -3.28366  -34.29967 44.20695  1.000 32.59091  ? 46  VAL A C   1 
ATOM   150  O  O   . VAL A  1 20  ? -4.03629  -35.06491 43.59288  1.000 33.83761  ? 46  VAL A O   1 
ATOM   151  C  CB  . VAL A  1 20  ? -1.26931  -33.34594 42.99947  1.000 28.39208  ? 46  VAL A CB  1 
ATOM   152  C  CG1 . VAL A  1 20  ? -1.25357  -34.58524 42.11897  1.000 29.61871  ? 46  VAL A CG1 1 
ATOM   153  C  CG2 . VAL A  1 20  ? -0.74510  -32.13789 42.23686  1.000 21.97604  ? 46  VAL A CG2 1 
ATOM   154  N  N   . ALA A  1 21  ? -2.96146  -34.50321 45.48692  1.000 33.15318  ? 47  ALA A N   1 
ATOM   155  C  CA  . ALA A  1 21  ? -3.48424  -35.66213 46.20403  1.000 34.73607  ? 47  ALA A CA  1 
ATOM   156  C  C   . ALA A  1 21  ? -5.00060  -35.59504 46.33339  1.000 37.33890  ? 47  ALA A C   1 
ATOM   157  O  O   . ALA A  1 21  ? -5.69287  -36.60206 46.13993  1.000 39.08623  ? 47  ALA A O   1 
ATOM   158  C  CB  . ALA A  1 21  ? -2.83089  -35.76646 47.58140  1.000 34.01394  ? 47  ALA A CB  1 
ATOM   159  N  N   . ASN A  1 22  ? -5.53628  -34.41510 46.65714  1.000 37.57320  ? 48  ASN A N   1 
ATOM   160  C  CA  . ASN A  1 22  ? -6.98479  -34.26698 46.75530  1.000 38.46371  ? 48  ASN A CA  1 
ATOM   161  C  C   . ASN A  1 22  ? -7.65198  -34.46405 45.40032  1.000 38.44298  ? 48  ASN A C   1 
ATOM   162  O  O   . ASN A  1 22  ? -8.69851  -35.11853 45.30796  1.000 40.07759  ? 48  ASN A O   1 
ATOM   163  C  CB  . ASN A  1 22  ? -7.33845  -32.89701 47.33357  1.000 37.13629  ? 48  ASN A CB  1 
ATOM   164  C  CG  . ASN A  1 22  ? -6.77842  -32.68907 48.72571  1.000 37.27704  ? 48  ASN A CG  1 
ATOM   165  O  OD1 . ASN A  1 22  ? -6.53392  -33.64687 49.45900  1.000 37.70780  ? 48  ASN A OD1 1 
ATOM   166  N  ND2 . ASN A  1 22  ? -6.56581  -31.43099 49.09560  1.000 36.31179  ? 48  ASN A ND2 1 
ATOM   167  N  N   . PHE A  1 23  ? -7.06091  -33.90912 44.33722  1.000 37.85581  ? 49  PHE A N   1 
ATOM   168  C  CA  . PHE A  1 23  ? -7.62351  -34.10231 43.00372  1.000 38.46585  ? 49  PHE A CA  1 
ATOM   169  C  C   . PHE A  1 23  ? -7.63576  -35.57739 42.61935  1.000 40.84890  ? 49  PHE A C   1 
ATOM   170  O  O   . PHE A  1 23  ? -8.61314  -36.06874 42.04162  1.000 42.29430  ? 49  PHE A O   1 
ATOM   171  C  CB  . PHE A  1 23  ? -6.83939  -33.28516 41.97633  1.000 36.40094  ? 49  PHE A CB  1 
ATOM   172  C  CG  . PHE A  1 23  ? -7.31447  -33.47306 40.56263  1.000 35.30411  ? 49  PHE A CG  1 
ATOM   173  C  CD1 . PHE A  1 23  ? -8.42039  -32.78398 40.09328  1.000 34.67714  ? 49  PHE A CD1 1 
ATOM   174  C  CD2 . PHE A  1 23  ? -6.65503  -34.33715 39.70280  1.000 35.50033  ? 49  PHE A CD2 1 
ATOM   175  C  CE1 . PHE A  1 23  ? -8.86203  -32.95485 38.79486  1.000 35.10719  ? 49  PHE A CE1 1 
ATOM   176  C  CE2 . PHE A  1 23  ? -7.09198  -34.51202 38.40250  1.000 35.71906  ? 49  PHE A CE2 1 
ATOM   177  C  CZ  . PHE A  1 23  ? -8.19642  -33.81903 37.94820  1.000 35.73006  ? 49  PHE A CZ  1 
ATOM   178  N  N   . GLU A  1 24  ? -6.56056  -36.30098 42.93987  1.000 41.72753  ? 50  GLU A N   1 
ATOM   179  C  CA  . GLU A  1 24  ? -6.49410  -37.72384 42.62200  1.000 43.70308  ? 50  GLU A CA  1 
ATOM   180  C  C   . GLU A  1 24  ? -7.52618  -38.51285 43.41730  1.000 46.32106  ? 50  GLU A C   1 
ATOM   181  O  O   . GLU A  1 24  ? -8.21549  -39.38170 42.86986  1.000 47.01335  ? 50  GLU A O   1 
ATOM   182  C  CB  . GLU A  1 24  ? -5.08759  -38.25765 42.89609  1.000 43.36694  ? 50  GLU A CB  1 
ATOM   183  C  CG  . GLU A  1 24  ? -4.02590  -37.76614 41.92906  1.000 43.42880  ? 50  GLU A CG  1 
ATOM   184  C  CD  . GLU A  1 24  ? -2.64612  -38.29071 42.27058  1.000 46.01868  ? 50  GLU A CD  1 
ATOM   185  O  OE1 . GLU A  1 24  ? -2.18997  -38.06699 43.41173  1.000 46.79813  ? 50  GLU A OE1 1 
ATOM   186  O  OE2 . GLU A  1 24  ? -2.01934  -38.93012 41.39953  1.000 46.98890  ? 50  GLU A OE2 1 
ATOM   187  N  N   . LYS A  1 25  ? -7.64315  -38.22588 44.71675  1.000 46.66368  ? 51  LYS A N   1 
ATOM   188  C  CA  . LYS A  1 25  ? -8.60629  -38.94067 45.54669  1.000 48.69886  ? 51  LYS A CA  1 
ATOM   189  C  C   . LYS A  1 25  ? -10.03795 -38.66790 45.10675  1.000 48.55404  ? 51  LYS A C   1 
ATOM   190  O  O   . LYS A  1 25  ? -10.89146 -39.55884 45.18734  1.000 50.60028  ? 51  LYS A O   1 
ATOM   191  C  CB  . LYS A  1 25  ? -8.41975  -38.55792 47.01574  1.000 49.20920  ? 51  LYS A CB  1 
ATOM   192  C  CG  . LYS A  1 25  ? -9.20143  -39.42490 47.99165  1.000 51.77701  ? 51  LYS A CG  1 
ATOM   193  C  CD  . LYS A  1 25  ? -10.03087 -38.57892 48.94747  1.000 53.19409  ? 51  LYS A CD  1 
ATOM   194  C  CE  . LYS A  1 25  ? -11.22005 -37.94428 48.24204  1.000 53.21238  ? 51  LYS A CE  1 
ATOM   195  N  NZ  . LYS A  1 25  ? -12.03273 -37.10245 49.16298  1.000 53.42615  ? 51  LYS A NZ  1 
ATOM   196  N  N   . GLU A  1 26  ? -10.32101 -37.45297 44.63232  1.000 46.60051  ? 52  GLU A N   1 
ATOM   197  C  CA  . GLU A  1 26  ? -11.68663 -37.12028 44.24375  1.000 46.19665  ? 52  GLU A CA  1 
ATOM   198  C  C   . GLU A  1 26  ? -12.03349 -37.65881 42.86018  1.000 46.20855  ? 52  GLU A C   1 
ATOM   199  O  O   . GLU A  1 26  ? -13.13987 -38.16918 42.65214  1.000 46.59674  ? 52  GLU A O   1 
ATOM   200  C  CB  . GLU A  1 26  ? -11.88981 -35.60566 44.28890  1.000 45.47871  ? 52  GLU A CB  1 
ATOM   201  C  CG  . GLU A  1 26  ? -13.25241 -35.15042 43.79450  1.000 46.66761  ? 52  GLU A CG  1 
ATOM   202  C  CD  . GLU A  1 26  ? -13.46487 -33.65996 43.95936  1.000 47.43699  ? 52  GLU A CD  1 
ATOM   203  O  OE1 . GLU A  1 26  ? -12.62438 -33.00638 44.61188  1.000 46.33942  ? 52  GLU A OE1 1 
ATOM   204  O  OE2 . GLU A  1 26  ? -14.47354 -33.14175 43.43637  1.000 49.01704  ? 52  GLU A OE2 1 
ATOM   205  N  N   . THR A  1 27  ? -11.10766 -37.56139 41.90491  1.000 44.75439  ? 53  THR A N   1 
ATOM   206  C  CA  . THR A  1 27  ? -11.40280 -37.91100 40.52178  1.000 43.94985  ? 53  THR A CA  1 
ATOM   207  C  C   . THR A  1 27  ? -10.97219 -39.31959 40.13658  1.000 44.49141  ? 53  THR A C   1 
ATOM   208  O  O   . THR A  1 27  ? -11.48660 -39.85502 39.14857  1.000 45.69670  ? 53  THR A O   1 
ATOM   209  C  CB  . THR A  1 27  ? -10.73144 -36.91399 39.56904  1.000 41.28123  ? 53  THR A CB  1 
ATOM   210  O  OG1 . THR A  1 27  ? -9.32029  -36.89144 39.81647  1.000 39.70370  ? 53  THR A OG1 1 
ATOM   211  C  CG2 . THR A  1 27  ? -11.29728 -35.51801 39.77633  1.000 39.53981  ? 53  THR A CG2 1 
ATOM   212  N  N   . GLY A  1 28  ? -10.05257 -39.93007 40.87972  1.000 44.72299  ? 54  GLY A N   1 
ATOM   213  C  CA  . GLY A  1 28  ? -9.52594  -41.22476 40.50065  1.000 45.44344  ? 54  GLY A CA  1 
ATOM   214  C  C   . GLY A  1 28  ? -8.49308  -41.19054 39.39860  1.000 45.04679  ? 54  GLY A C   1 
ATOM   215  O  O   . GLY A  1 28  ? -8.11096  -42.25276 38.89444  1.000 44.60166  ? 54  GLY A O   1 
ATOM   216  N  N   . ILE A  1 29  ? -8.03262  -40.00794 39.00861  1.000 43.88734  ? 55  ILE A N   1 
ATOM   217  C  CA  . ILE A  1 29  ? -7.03127  -39.84700 37.96181  1.000 42.10752  ? 55  ILE A CA  1 
ATOM   218  C  C   . ILE A  1 29  ? -5.64780  -39.95879 38.58384  1.000 41.18244  ? 55  ILE A C   1 
ATOM   219  O  O   . ILE A  1 29  ? -5.41610  -39.48711 39.70252  1.000 41.78101  ? 55  ILE A O   1 
ATOM   220  C  CB  . ILE A  1 29  ? -7.21310  -38.49600 37.24241  1.000 40.50247  ? 55  ILE A CB  1 
ATOM   221  C  CG1 . ILE A  1 29  ? -8.63745  -38.36693 36.69924  1.000 41.71678  ? 55  ILE A CG1 1 
ATOM   222  C  CG2 . ILE A  1 29  ? -6.19635  -38.33268 36.12155  1.000 39.22665  ? 55  ILE A CG2 1 
ATOM   223  C  CD1 . ILE A  1 29  ? -8.94555  -37.00477 36.11585  1.000 42.01401  ? 55  ILE A CD1 1 
ATOM   224  N  N   . LYS A  1 30  ? -4.72448  -40.59445 37.86584  1.000 40.74059  ? 56  LYS A N   1 
ATOM   225  C  CA  . LYS A  1 30  ? -3.32839  -40.66566 38.28390  1.000 39.87046  ? 56  LYS A CA  1 
ATOM   226  C  C   . LYS A  1 30  ? -2.58133  -39.49685 37.65223  1.000 36.65279  ? 56  LYS A C   1 
ATOM   227  O  O   . LYS A  1 30  ? -2.38806  -39.46012 36.43255  1.000 36.09283  ? 56  LYS A O   1 
ATOM   228  C  CB  . LYS A  1 30  ? -2.70337  -41.99889 37.88321  1.000 42.67223  ? 56  LYS A CB  1 
ATOM   229  C  CG  . LYS A  1 30  ? -1.24555  -42.13654 38.29471  1.000 44.16237  ? 56  LYS A CG  1 
ATOM   230  C  CD  . LYS A  1 30  ? -0.39993  -42.71214 37.17089  1.000 46.79083  ? 56  LYS A CD  1 
ATOM   231  C  CE  . LYS A  1 30  ? -0.57130  -44.21785 37.06677  1.000 49.69583  ? 56  LYS A CE  1 
ATOM   232  N  NZ  . LYS A  1 30  ? 0.09782   -44.92880 38.19086  1.000 50.74704  ? 56  LYS A NZ  1 
ATOM   233  N  N   . VAL A  1 31  ? -2.16273  -38.54389 38.47872  1.000 34.35371  ? 57  VAL A N   1 
ATOM   234  C  CA  . VAL A  1 31  ? -1.50045  -37.33166 38.01318  1.000 32.38364  ? 57  VAL A CA  1 
ATOM   235  C  C   . VAL A  1 31  ? 0.00537   -37.53449 38.10275  1.000 32.22071  ? 57  VAL A C   1 
ATOM   236  O  O   . VAL A  1 31  ? 0.53598   -37.85680 39.17281  1.000 31.94034  ? 57  VAL A O   1 
ATOM   237  C  CB  . VAL A  1 31  ? -1.93915  -36.10394 38.82625  1.000 31.48473  ? 57  VAL A CB  1 
ATOM   238  C  CG1 . VAL A  1 31  ? -1.14162  -34.87954 38.40548  1.000 29.08926  ? 57  VAL A CG1 1 
ATOM   239  C  CG2 . VAL A  1 31  ? -3.43066  -35.85947 38.65613  1.000 32.58008  ? 57  VAL A CG2 1 
ATOM   240  N  N   . VAL A  1 32  ? 0.69221   -37.34910 36.98032  1.000 31.36029  ? 58  VAL A N   1 
ATOM   241  C  CA  . VAL A  1 32  ? 2.14906   -37.35061 36.93172  1.000 29.70381  ? 58  VAL A CA  1 
ATOM   242  C  C   . VAL A  1 32  ? 2.58055   -35.89104 37.01233  1.000 27.69120  ? 58  VAL A C   1 
ATOM   243  O  O   . VAL A  1 32  ? 2.49212   -35.14744 36.03135  1.000 26.67158  ? 58  VAL A O   1 
ATOM   244  C  CB  . VAL A  1 32  ? 2.67890   -38.03658 35.67004  1.000 29.94387  ? 58  VAL A CB  1 
ATOM   245  C  CG1 . VAL A  1 32  ? 4.19464   -38.12855 35.71750  1.000 29.51822  ? 58  VAL A CG1 1 
ATOM   246  C  CG2 . VAL A  1 32  ? 2.06243   -39.41831 35.52059  1.000 29.54886  ? 58  VAL A CG2 1 
ATOM   247  N  N   . TYR A  1 33  ? 3.04385   -35.47624 38.18896  1.000 27.02573  ? 59  TYR A N   1 
ATOM   248  C  CA  . TYR A  1 33  ? 3.35569   -34.07674 38.47182  1.000 27.13907  ? 59  TYR A CA  1 
ATOM   249  C  C   . TYR A  1 33  ? 4.87042   -33.89884 38.44850  1.000 28.18859  ? 59  TYR A C   1 
ATOM   250  O  O   . TYR A  1 33  ? 5.56674   -34.27510 39.39489  1.000 29.41011  ? 59  TYR A O   1 
ATOM   251  C  CB  . TYR A  1 33  ? 2.76088   -33.66135 39.81381  1.000 27.15181  ? 59  TYR A CB  1 
ATOM   252  C  CG  . TYR A  1 33  ? 2.74697   -32.16938 40.05894  1.000 26.68915  ? 59  TYR A CG  1 
ATOM   253  C  CD1 . TYR A  1 33  ? 1.72986   -31.37077 39.55080  1.000 26.20341  ? 59  TYR A CD1 1 
ATOM   254  C  CD2 . TYR A  1 33  ? 3.74393   -31.56124 40.80963  1.000 25.99842  ? 59  TYR A CD2 1 
ATOM   255  C  CE1 . TYR A  1 33  ? 1.71142   -30.00692 39.77729  1.000 23.30058  ? 59  TYR A CE1 1 
ATOM   256  C  CE2 . TYR A  1 33  ? 3.73359   -30.19927 41.04148  1.000 24.61861  ? 59  TYR A CE2 1 
ATOM   257  C  CZ  . TYR A  1 33  ? 2.71576   -29.42744 40.52346  1.000 23.37188  ? 59  TYR A CZ  1 
ATOM   258  O  OH  . TYR A  1 33  ? 2.70380   -28.07111 40.75335  1.000 23.41205  ? 59  TYR A OH  1 
ATOM   259  N  N   . ASP A  1 34  ? 5.37754   -33.32243 37.36292  1.000 27.43854  ? 60  ASP A N   1 
ATOM   260  C  CA  . ASP A  1 34  ? 6.79140   -33.01531 37.21648  1.000 26.85196  ? 60  ASP A CA  1 
ATOM   261  C  C   . ASP A  1 34  ? 7.01431   -31.51783 37.37954  1.000 27.12373  ? 60  ASP A C   1 
ATOM   262  O  O   . ASP A  1 34  ? 6.13802   -30.70531 37.06982  1.000 25.87317  ? 60  ASP A O   1 
ATOM   263  C  CB  . ASP A  1 34  ? 7.32077   -33.47595 35.85572  1.000 27.56030  ? 60  ASP A CB  1 
ATOM   264  C  CG  . ASP A  1 34  ? 7.38142   -34.98381 35.73621  1.000 29.65898  ? 60  ASP A CG  1 
ATOM   265  O  OD1 . ASP A  1 34  ? 7.51138   -35.65914 36.77902  1.000 30.50445  ? 60  ASP A OD1 1 
ATOM   266  O  OD2 . ASP A  1 34  ? 7.30013   -35.49342 34.59938  1.000 29.81133  ? 60  ASP A OD2 1 
ATOM   267  N  N   . VAL A  1 35  ? 8.20162   -31.15738 37.86763  1.000 27.46390  ? 61  VAL A N   1 
ATOM   268  C  CA  . VAL A  1 35  ? 8.52392   -29.77231 38.17443  1.000 28.13093  ? 61  VAL A CA  1 
ATOM   269  C  C   . VAL A  1 35  ? 9.79672   -29.36473 37.44474  1.000 29.09137  ? 61  VAL A C   1 
ATOM   270  O  O   . VAL A  1 35  ? 10.61472  -30.19783 37.04755  1.000 30.13359  ? 61  VAL A O   1 
ATOM   271  C  CB  . VAL A  1 35  ? 8.68112   -29.53138 39.69142  1.000 28.20199  ? 61  VAL A CB  1 
ATOM   272  C  CG1 . VAL A  1 35  ? 7.36457   -29.78841 40.41069  1.000 27.42752  ? 61  VAL A CG1 1 
ATOM   273  C  CG2 . VAL A  1 35  ? 9.79184   -30.40456 40.25646  1.000 29.00764  ? 61  VAL A CG2 1 
ATOM   274  N  N   . PHE A  1 36  ? 9.94849   -28.05340 37.26983  1.000 29.12573  ? 62  PHE A N   1 
ATOM   275  C  CA  . PHE A  1 36  ? 11.15950  -27.45870 36.72717  1.000 31.51145  ? 62  PHE A CA  1 
ATOM   276  C  C   . PHE A  1 36  ? 11.55947  -26.27163 37.59164  1.000 32.25585  ? 62  PHE A C   1 
ATOM   277  O  O   . PHE A  1 36  ? 10.71181  -25.61620 38.20420  1.000 28.94373  ? 62  PHE A O   1 
ATOM   278  C  CB  . PHE A  1 36  ? 10.97476  -27.01283 35.26581  1.000 32.66608  ? 62  PHE A CB  1 
ATOM   279  C  CG  . PHE A  1 36  ? 9.81104   -26.08304 35.05195  1.000 31.34520  ? 62  PHE A CG  1 
ATOM   280  C  CD1 . PHE A  1 36  ? 9.96011   -24.71365 35.20969  1.000 30.39780  ? 62  PHE A CD1 1 
ATOM   281  C  CD2 . PHE A  1 36  ? 8.57194   -26.57749 34.67973  1.000 31.49401  ? 62  PHE A CD2 1 
ATOM   282  C  CE1 . PHE A  1 36  ? 8.89397   -23.85726 35.01067  1.000 29.79778  ? 62  PHE A CE1 1 
ATOM   283  C  CE2 . PHE A  1 36  ? 7.50181   -25.72509 34.47656  1.000 30.87468  ? 62  PHE A CE2 1 
ATOM   284  C  CZ  . PHE A  1 36  ? 7.66340   -24.36364 34.64462  1.000 30.32454  ? 62  PHE A CZ  1 
ATOM   285  N  N   . ASP A  1 37  ? 12.86167  -26.00120 37.63786  1.000 34.63994  ? 63  ASP A N   1 
ATOM   286  C  CA  . ASP A  1 37  ? 13.40158  -24.91141 38.43859  1.000 36.67204  ? 63  ASP A CA  1 
ATOM   287  C  C   . ASP A  1 37  ? 13.81482  -23.70766 37.60351  1.000 37.75497  ? 63  ASP A C   1 
ATOM   288  O  O   . ASP A  1 37  ? 14.32635  -22.73125 38.16018  1.000 38.15042  ? 63  ASP A O   1 
ATOM   289  C  CB  . ASP A  1 37  ? 14.59724  -25.40482 39.26020  1.000 38.77826  ? 63  ASP A CB  1 
ATOM   290  C  CG  . ASP A  1 37  ? 14.20457  -26.44194 40.29396  1.000 40.64395  ? 63  ASP A CG  1 
ATOM   291  O  OD1 . ASP A  1 37  ? 13.28368  -26.16852 41.09248  1.000 41.32812  ? 63  ASP A OD1 1 
ATOM   292  O  OD2 . ASP A  1 37  ? 14.81449  -27.53184 40.30624  1.000 42.37802  ? 63  ASP A OD2 1 
ATOM   293  N  N   . SER A  1 38  ? 13.60309  -23.74922 36.29022  1.000 39.02422  ? 64  SER A N   1 
ATOM   294  C  CA  . SER A  1 38  ? 13.99306  -22.65718 35.41167  1.000 40.85146  ? 64  SER A CA  1 
ATOM   295  C  C   . SER A  1 38  ? 13.04659  -22.61439 34.22163  1.000 42.10930  ? 64  SER A C   1 
ATOM   296  O  O   . SER A  1 38  ? 12.68574  -23.65735 33.66956  1.000 42.37389  ? 64  SER A O   1 
ATOM   297  C  CB  . SER A  1 38  ? 15.44217  -22.81557 34.93627  1.000 43.52821  ? 64  SER A CB  1 
ATOM   298  O  OG  . SER A  1 38  ? 15.62493  -22.24318 33.65346  1.000 45.06052  ? 64  SER A OG  1 
ATOM   299  N  N   . ASN A  1 39  ? 12.64970  -21.40018 33.83227  1.000 41.49808  ? 65  ASN A N   1 
ATOM   300  C  CA  . ASN A  1 39  ? 11.73622  -21.23552 32.70739  1.000 44.24393  ? 65  ASN A CA  1 
ATOM   301  C  C   . ASN A  1 39  ? 12.37241  -21.62636 31.38004  1.000 45.56796  ? 65  ASN A C   1 
ATOM   302  O  O   . ASN A  1 39  ? 11.64716  -21.95625 30.43274  1.000 46.59639  ? 65  ASN A O   1 
ATOM   303  C  CB  . ASN A  1 39  ? 11.23756  -19.78990 32.64620  1.000 45.84404  ? 65  ASN A CB  1 
ATOM   304  C  CG  . ASN A  1 39  ? 12.24009  -18.85249 32.00114  1.000 49.52422  ? 65  ASN A CG  1 
ATOM   305  O  OD1 . ASN A  1 39  ? 12.10429  -18.48640 30.83439  1.000 52.09706  ? 65  ASN A OD1 1 
ATOM   306  N  ND2 . ASN A  1 39  ? 13.25560  -18.45859 32.76122  1.000 50.00965  ? 65  ASN A ND2 1 
ATOM   307  N  N   . GLU A  1 40  ? 13.70555  -21.59796 31.29292  1.000 45.02018  ? 66  GLU A N   1 
ATOM   308  C  CA  . GLU A  1 40  ? 14.37728  -21.98165 30.05603  1.000 43.83195  ? 66  GLU A CA  1 
ATOM   309  C  C   . GLU A  1 40  ? 14.07011  -23.42649 29.68782  1.000 43.56422  ? 66  GLU A C   1 
ATOM   310  O  O   . GLU A  1 40  ? 13.83797  -23.73772 28.51473  1.000 45.98134  ? 66  GLU A O   1 
ATOM   311  C  CB  . GLU A  1 40  ? 15.88635  -21.77408 30.18885  1.000 44.21408  ? 66  GLU A CB  1 
ATOM   312  C  CG  . GLU A  1 40  ? 16.31986  -20.31799 30.20945  1.000 46.40355  ? 66  GLU A CG  1 
ATOM   313  C  CD  . GLU A  1 40  ? 16.74565  -19.85626 31.58944  1.000 48.41515  ? 66  GLU A CD  1 
ATOM   314  O  OE1 . GLU A  1 40  ? 17.04958  -18.65538 31.74859  1.000 48.52825  ? 66  GLU A OE1 1 
ATOM   315  O  OE2 . GLU A  1 40  ? 16.77755  -20.69423 32.51520  1.000 48.74202  ? 66  GLU A OE2 1 
ATOM   316  N  N   . VAL A  1 41  ? 14.05813  -24.32116 30.67891  1.000 42.06972  ? 67  VAL A N   1 
ATOM   317  C  CA  . VAL A  1 41  ? 13.77880  -25.73147 30.41531  1.000 43.08635  ? 67  VAL A CA  1 
ATOM   318  C  C   . VAL A  1 41  ? 12.38022  -25.89580 29.83301  1.000 43.60250  ? 67  VAL A C   1 
ATOM   319  O  O   . VAL A  1 41  ? 12.18735  -26.55717 28.80312  1.000 45.63225  ? 67  VAL A O   1 
ATOM   320  C  CB  . VAL A  1 41  ? 13.95402  -26.56005 31.70119  1.000 43.74199  ? 67  VAL A CB  1 
ATOM   321  C  CG1 . VAL A  1 41  ? 13.42736  -27.97360 31.50271  1.000 44.08674  ? 67  VAL A CG1 1 
ATOM   322  C  CG2 . VAL A  1 41  ? 15.41421  -26.58114 32.12634  1.000 44.32139  ? 67  VAL A CG2 1 
ATOM   323  N  N   . LEU A  1 42  ? 11.38393  -25.29121 30.48598  1.000 41.64243  ? 68  LEU A N   1 
ATOM   324  C  CA  . LEU A  1 42  ? 10.00564  -25.41017 30.02225  1.000 38.29023  ? 68  LEU A CA  1 
ATOM   325  C  C   . LEU A  1 42  ? 9.84384   -24.83426 28.62219  1.000 36.68891  ? 68  LEU A C   1 
ATOM   326  O  O   . LEU A  1 42  ? 9.20404   -25.44527 27.75939  1.000 35.53213  ? 68  LEU A O   1 
ATOM   327  C  CB  . LEU A  1 42  ? 9.05773   -24.71219 30.99751  1.000 35.16567  ? 68  LEU A CB  1 
ATOM   328  C  CG  . LEU A  1 42  ? 7.64332   -24.48644 30.45535  1.000 34.60400  ? 68  LEU A CG  1 
ATOM   329  C  CD1 . LEU A  1 42  ? 6.91040   -25.80965 30.28102  1.000 33.31113  ? 68  LEU A CD1 1 
ATOM   330  C  CD2 . LEU A  1 42  ? 6.85648   -23.54365 31.34700  1.000 34.47414  ? 68  LEU A CD2 1 
ATOM   331  N  N   . GLU A  1 43  ? 10.42152  -23.65572 28.37530  1.000 35.92223  ? 69  GLU A N   1 
ATOM   332  C  CA  . GLU A  1 43  ? 10.24172  -23.01698 27.07495  1.000 38.57926  ? 69  GLU A CA  1 
ATOM   333  C  C   . GLU A  1 43  ? 10.94676  -23.79416 25.96786  1.000 39.42364  ? 69  GLU A C   1 
ATOM   334  O  O   . GLU A  1 43  ? 10.39940  -23.95107 24.86810  1.000 39.82518  ? 69  GLU A O   1 
ATOM   335  C  CB  . GLU A  1 43  ? 10.73146  -21.57109 27.13250  1.000 39.84983  ? 69  GLU A CB  1 
ATOM   336  C  CG  . GLU A  1 43  ? 9.88103   -20.68970 28.03573  1.000 40.63633  ? 69  GLU A CG  1 
ATOM   337  C  CD  . GLU A  1 43  ? 10.54132  -19.36666 28.36055  1.000 42.66474  ? 69  GLU A CD  1 
ATOM   338  O  OE1 . GLU A  1 43  ? 11.72014  -19.18114 27.99079  1.000 43.38637  ? 69  GLU A OE1 1 
ATOM   339  O  OE2 . GLU A  1 43  ? 9.88139   -18.51326 28.99116  1.000 41.87201  ? 69  GLU A OE2 1 
ATOM   340  N  N   . GLY A  1 44  ? 12.15257  -24.30042 26.23855  1.000 38.71768  ? 70  GLY A N   1 
ATOM   341  C  CA  . GLY A  1 44  ? 12.84066  -25.10737 25.24632  1.000 39.33951  ? 70  GLY A CA  1 
ATOM   342  C  C   . GLY A  1 44  ? 12.10459  -26.39477 24.93528  1.000 40.23495  ? 70  GLY A C   1 
ATOM   343  O  O   . GLY A  1 44  ? 11.99957  -26.79514 23.77257  1.000 42.31461  ? 70  GLY A O   1 
ATOM   344  N  N   . LYS A  1 45  ? 11.57235  -27.05660 25.96739  1.000 39.09948  ? 71  LYS A N   1 
ATOM   345  C  CA  . LYS A  1 45  ? 10.79754  -28.26937 25.72912  1.000 40.34774  ? 71  LYS A CA  1 
ATOM   346  C  C   . LYS A  1 45  ? 9.52618   -27.96718 24.94513  1.000 40.31133  ? 71  LYS A C   1 
ATOM   347  O  O   . LYS A  1 45  ? 9.16074   -28.71919 24.03421  1.000 42.12408  ? 71  LYS A O   1 
ATOM   348  C  CB  . LYS A  1 45  ? 10.46639  -28.95204 27.05565  1.000 39.93611  ? 71  LYS A CB  1 
ATOM   349  C  CG  . LYS A  1 45  ? 11.64621  -29.67106 27.68793  1.000 41.18017  ? 71  LYS A CG  1 
ATOM   350  C  CD  . LYS A  1 45  ? 11.30008  -30.20063 29.06873  1.000 41.60872  ? 71  LYS A CD  1 
ATOM   351  C  CE  . LYS A  1 45  ? 12.43411  -31.04037 29.63382  1.000 42.51151  ? 71  LYS A CE  1 
ATOM   352  N  NZ  . LYS A  1 45  ? 12.08405  -31.62738 30.95653  1.000 41.80485  ? 71  LYS A NZ  1 
ATOM   353  N  N   . LEU A  1 46  ? 8.84972   -26.86198 25.27075  1.000 39.23292  ? 72  LEU A N   1 
ATOM   354  C  CA  . LEU A  1 46  ? 7.60831   -26.52227 24.58347  1.000 39.78925  ? 72  LEU A CA  1 
ATOM   355  C  C   . LEU A  1 46  ? 7.85593   -26.18779 23.11873  1.000 43.68547  ? 72  LEU A C   1 
ATOM   356  O  O   . LEU A  1 46  ? 7.07499   -26.58639 22.24680  1.000 43.89166  ? 72  LEU A O   1 
ATOM   357  C  CB  . LEU A  1 46  ? 6.91826   -25.35482 25.28848  1.000 36.90925  ? 72  LEU A CB  1 
ATOM   358  C  CG  . LEU A  1 46  ? 6.10631   -25.69470 26.53932  1.000 34.97246  ? 72  LEU A CG  1 
ATOM   359  C  CD1 . LEU A  1 46  ? 5.50833   -24.43509 27.14810  1.000 33.73186  ? 72  LEU A CD1 1 
ATOM   360  C  CD2 . LEU A  1 46  ? 5.01967   -26.70861 26.21490  1.000 34.93948  ? 72  LEU A CD2 1 
ATOM   361  N  N   . MET A  1 47  ? 8.93120   -25.45461 22.82430  1.000 46.42550  ? 73  MET A N   1 
ATOM   362  C  CA  . MET A  1 47  ? 9.23078   -25.13105 21.43559  1.000 51.60915  ? 73  MET A CA  1 
ATOM   363  C  C   . MET A  1 47  ? 9.87128   -26.29262 20.68733  1.000 53.92771  ? 73  MET A C   1 
ATOM   364  O  O   . MET A  1 47  ? 9.89219   -26.27755 19.45179  1.000 55.17489  ? 73  MET A O   1 
ATOM   365  C  CB  . MET A  1 47  ? 10.12860  -23.89508 21.35778  1.000 54.35552  ? 73  MET A CB  1 
ATOM   366  C  CG  . MET A  1 47  ? 9.35040   -22.58735 21.31716  1.000 58.04775  ? 73  MET A CG  1 
ATOM   367  S  SD  . MET A  1 47  ? 10.39134  -21.11590 21.26734  1.000 63.22150  ? 73  MET A SD  1 
ATOM   368  C  CE  . MET A  1 47  ? 11.80336  -21.65585 22.22678  1.000 64.74192  ? 73  MET A CE  1 
ATOM   369  N  N   . ALA A  1 48  ? 10.38872  -27.29611 21.39989  1.000 54.82196  ? 74  ALA A N   1 
ATOM   370  C  CA  . ALA A  1 48  ? 10.85976  -28.50447 20.73405  1.000 56.29158  ? 74  ALA A CA  1 
ATOM   371  C  C   . ALA A  1 48  ? 9.70529   -29.40094 20.30513  1.000 59.68233  ? 74  ALA A C   1 
ATOM   372  O  O   . ALA A  1 48  ? 9.82944   -30.13388 19.31747  1.000 64.90257  ? 74  ALA A O   1 
ATOM   373  C  CB  . ALA A  1 48  ? 11.81361  -29.27553 21.64775  1.000 54.52151  ? 74  ALA A CB  1 
ATOM   374  N  N   . GLY A  1 49  ? 8.58724   -29.35825 21.02592  1.000 57.39565  ? 75  GLY A N   1 
ATOM   375  C  CA  . GLY A  1 49  ? 7.41075   -30.12213 20.67258  1.000 56.02081  ? 75  GLY A CA  1 
ATOM   376  C  C   . GLY A  1 49  ? 7.40914   -31.52187 21.26181  1.000 53.30654  ? 75  GLY A C   1 
ATOM   377  O  O   . GLY A  1 49  ? 8.42314   -32.04541 21.73000  1.000 53.71116  ? 75  GLY A O   1 
ATOM   378  N  N   . SER A  1 50  ? 6.22341   -32.13304 21.23178  1.000 48.06887  ? 76  SER A N   1 
ATOM   379  C  CA  . SER A  1 50  ? 6.01154   -33.50377 21.70114  1.000 46.82166  ? 76  SER A CA  1 
ATOM   380  C  C   . SER A  1 50  ? 6.53806   -33.69218 23.12262  1.000 43.10693  ? 76  SER A C   1 
ATOM   381  O  O   . SER A  1 50  ? 7.30313   -34.61328 23.41684  1.000 42.63929  ? 76  SER A O   1 
ATOM   382  C  CB  . SER A  1 50  ? 6.64191   -34.51308 20.74032  1.000 49.30141  ? 76  SER A CB  1 
ATOM   383  O  OG  . SER A  1 50  ? 5.72209   -34.89378 19.73111  1.000 52.92614  ? 76  SER A OG  1 
ATOM   384  N  N   . THR A  1 51  ? 6.11000   -32.79970 24.01631  1.000 39.47154  ? 77  THR A N   1 
ATOM   385  C  CA  . THR A  1 51  ? 6.57911   -32.82571 25.39552  1.000 35.82829  ? 77  THR A CA  1 
ATOM   386  C  C   . THR A  1 51  ? 5.94813   -33.94096 26.21703  1.000 35.37449  ? 77  THR A C   1 
ATOM   387  O  O   . THR A  1 51  ? 6.52263   -34.34181 27.23515  1.000 36.82747  ? 77  THR A O   1 
ATOM   388  C  CB  . THR A  1 51  ? 6.29771   -31.48382 26.07404  1.000 32.34665  ? 77  THR A CB  1 
ATOM   389  O  OG1 . THR A  1 51  ? 4.89565   -31.37106 26.34853  1.000 30.92743  ? 77  THR A OG1 1 
ATOM   390  C  CG2 . THR A  1 51  ? 6.72154   -30.33729 25.17748  1.000 31.89869  ? 77  THR A CG2 1 
ATOM   391  N  N   . GLY A  1 52  ? 4.78993   -34.44857 25.80458  1.000 34.00105  ? 78  GLY A N   1 
ATOM   392  C  CA  . GLY A  1 52  ? 4.07966   -35.43147 26.59376  1.000 34.27665  ? 78  GLY A CA  1 
ATOM   393  C  C   . GLY A  1 52  ? 3.29841   -34.86768 27.75742  1.000 33.28458  ? 78  GLY A C   1 
ATOM   394  O  O   . GLY A  1 52  ? 2.74819   -35.64378 28.54717  1.000 35.58888  ? 78  GLY A O   1 
ATOM   395  N  N   . PHE A  1 53  ? 3.23205   -33.54607 27.89128  1.000 29.84950  ? 79  PHE A N   1 
ATOM   396  C  CA  . PHE A  1 53  ? 2.49887   -32.89795 28.96863  1.000 30.14789  ? 79  PHE A CA  1 
ATOM   397  C  C   . PHE A  1 53  ? 1.09972   -32.52213 28.50019  1.000 30.48697  ? 79  PHE A C   1 
ATOM   398  O  O   . PHE A  1 53  ? 0.90544   -32.11175 27.35188  1.000 31.12308  ? 79  PHE A O   1 
ATOM   399  C  CB  . PHE A  1 53  ? 3.22876   -31.64358 29.45553  1.000 30.57594  ? 79  PHE A CB  1 
ATOM   400  C  CG  . PHE A  1 53  ? 4.57596   -31.91707 30.05913  1.000 32.82174  ? 79  PHE A CG  1 
ATOM   401  C  CD1 . PHE A  1 53  ? 4.70127   -32.73674 31.16775  1.000 33.75015  ? 79  PHE A CD1 1 
ATOM   402  C  CD2 . PHE A  1 53  ? 5.71731   -31.34553 29.52271  1.000 34.91583  ? 79  PHE A CD2 1 
ATOM   403  C  CE1 . PHE A  1 53  ? 5.94159   -32.98558 31.72556  1.000 34.72860  ? 79  PHE A CE1 1 
ATOM   404  C  CE2 . PHE A  1 53  ? 6.95975   -31.59208 30.07438  1.000 35.97828  ? 79  PHE A CE2 1 
ATOM   405  C  CZ  . PHE A  1 53  ? 7.07189   -32.41314 31.17726  1.000 35.45001  ? 79  PHE A CZ  1 
ATOM   406  N  N   . ASP A  1 54  ? 0.12679   -32.66368 29.39869  1.000 29.52924  ? 80  ASP A N   1 
ATOM   407  C  CA  . ASP A  1 54  ? -1.23103  -32.21076 29.12745  1.000 30.09608  ? 80  ASP A CA  1 
ATOM   408  C  C   . ASP A  1 54  ? -1.46829  -30.78305 29.59557  1.000 30.29140  ? 80  ASP A C   1 
ATOM   409  O  O   . ASP A  1 54  ? -2.26040  -30.05933 28.98095  1.000 29.76041  ? 80  ASP A O   1 
ATOM   410  C  CB  . ASP A  1 54  ? -2.24419  -33.14146 29.79811  1.000 32.78797  ? 80  ASP A CB  1 
ATOM   411  C  CG  . ASP A  1 54  ? -2.08066  -34.58530 29.37051  1.000 36.73206  ? 80  ASP A CG  1 
ATOM   412  O  OD1 . ASP A  1 54  ? -2.19247  -34.86389 28.15851  1.000 38.30002  ? 80  ASP A OD1 1 
ATOM   413  O  OD2 . ASP A  1 54  ? -1.83744  -35.44131 30.24698  1.000 38.04722  ? 80  ASP A OD2 1 
ATOM   414  N  N   . LEU A  1 55  ? -0.80159  -30.36586 30.66987  1.000 28.49108  ? 81  LEU A N   1 
ATOM   415  C  CA  . LEU A  1 55  ? -0.90685  -29.01024 31.18582  1.000 26.89215  ? 81  LEU A CA  1 
ATOM   416  C  C   . LEU A  1 55  ? 0.48074   -28.50928 31.55260  1.000 26.20129  ? 81  LEU A C   1 
ATOM   417  O  O   . LEU A  1 55  ? 1.27581   -29.24059 32.14955  1.000 28.10726  ? 81  LEU A O   1 
ATOM   418  C  CB  . LEU A  1 55  ? -1.82918  -28.93978 32.41018  1.000 25.68074  ? 81  LEU A CB  1 
ATOM   419  C  CG  . LEU A  1 55  ? -3.32188  -29.17821 32.17342  1.000 25.92666  ? 81  LEU A CG  1 
ATOM   420  C  CD1 . LEU A  1 55  ? -4.09029  -29.09731 33.48483  1.000 23.24618  ? 81  LEU A CD1 1 
ATOM   421  C  CD2 . LEU A  1 55  ? -3.87333  -28.18330 31.16353  1.000 25.80713  ? 81  LEU A CD2 1 
ATOM   422  N  N   . VAL A  1 56  ? 0.76757   -27.26112 31.18461  1.000 25.50706  ? 82  VAL A N   1 
ATOM   423  C  CA  . VAL A  1 56  ? 2.02862   -26.61240 31.51092  1.000 25.37037  ? 82  VAL A CA  1 
ATOM   424  C  C   . VAL A  1 56  ? 1.72493   -25.23845 32.09004  1.000 24.86715  ? 82  VAL A C   1 
ATOM   425  O  O   . VAL A  1 56  ? 0.64265   -24.68117 31.89593  1.000 25.30027  ? 82  VAL A O   1 
ATOM   426  C  CB  . VAL A  1 56  ? 2.96211   -26.49017 30.28778  1.000 25.58146  ? 82  VAL A CB  1 
ATOM   427  C  CG1 . VAL A  1 56  ? 3.51948   -27.85454 29.90754  1.000 25.67085  ? 82  VAL A CG1 1 
ATOM   428  C  CG2 . VAL A  1 56  ? 2.22072   -25.86354 29.11630  1.000 26.72240  ? 82  VAL A CG2 1 
ATOM   429  N  N   . VAL A  1 57  ? 2.69805   -24.69546 32.81523  1.000 25.53352  ? 83  VAL A N   1 
ATOM   430  C  CA  . VAL A  1 57  ? 2.52975   -23.39738 33.46470  1.000 26.46028  ? 83  VAL A CA  1 
ATOM   431  C  C   . VAL A  1 57  ? 3.60302   -22.43129 32.97502  1.000 26.98493  ? 83  VAL A C   1 
ATOM   432  O  O   . VAL A  1 57  ? 4.59321   -22.19560 33.68341  1.000 25.50902  ? 83  VAL A O   1 
ATOM   433  C  CB  . VAL A  1 57  ? 2.56560   -23.53102 34.99551  1.000 27.42298  ? 83  VAL A CB  1 
ATOM   434  C  CG1 . VAL A  1 57  ? 2.08107   -22.24526 35.65265  1.000 29.23084  ? 83  VAL A CG1 1 
ATOM   435  C  CG2 . VAL A  1 57  ? 1.71875   -24.71202 35.44403  1.000 27.48500  ? 83  VAL A CG2 1 
ATOM   436  N  N   . PRO A  1 58  ? 3.45887   -21.85465 31.78655  1.000 28.68172  ? 84  PRO A N   1 
ATOM   437  C  CA  . PRO A  1 58  ? 4.42326   -20.86271 31.31263  1.000 27.78152  ? 84  PRO A CA  1 
ATOM   438  C  C   . PRO A  1 58  ? 4.00649   -19.44965 31.70561  1.000 26.19967  ? 84  PRO A C   1 
ATOM   439  O  O   . PRO A  1 58  ? 2.92437   -19.21543 32.24733  1.000 24.47774  ? 84  PRO A O   1 
ATOM   440  C  CB  . PRO A  1 58  ? 4.37147   -21.04510 29.79183  1.000 28.71884  ? 84  PRO A CB  1 
ATOM   441  C  CG  . PRO A  1 58  ? 2.94235   -21.40255 29.53782  1.000 30.49464  ? 84  PRO A CG  1 
ATOM   442  C  CD  . PRO A  1 58  ? 2.46277   -22.18139 30.74955  1.000 30.10429  ? 84  PRO A CD  1 
ATOM   443  N  N   . SER A  1 59  ? 4.89874   -18.50616 31.42195  1.000 26.61435  ? 85  SER A N   1 
ATOM   444  C  CA  . SER A  1 59  ? 4.56653   -17.10158 31.59512  1.000 26.18848  ? 85  SER A CA  1 
ATOM   445  C  C   . SER A  1 59  ? 3.61800   -16.65298 30.49021  1.000 27.42303  ? 85  SER A C   1 
ATOM   446  O  O   . SER A  1 59  ? 3.59505   -17.21805 29.39303  1.000 30.64899  ? 85  SER A O   1 
ATOM   447  C  CB  . SER A  1 59  ? 5.82953   -16.24156 31.58050  1.000 25.14949  ? 85  SER A CB  1 
ATOM   448  O  OG  . SER A  1 59  ? 6.62360   -16.52258 30.44131  1.000 26.38661  ? 85  SER A OG  1 
ATOM   449  N  N   . ALA A  1 60  ? 2.81964   -15.62698 30.79198  1.000 26.45606  ? 86  ALA A N   1 
ATOM   450  C  CA  . ALA A  1 60  ? 1.89204   -15.11089 29.79200  1.000 30.60365  ? 86  ALA A CA  1 
ATOM   451  C  C   . ALA A  1 60  ? 2.62617   -14.44136 28.63690  1.000 32.69793  ? 86  ALA A C   1 
ATOM   452  O  O   . ALA A  1 60  ? 2.12092   -14.43023 27.50915  1.000 35.34454  ? 86  ALA A O   1 
ATOM   453  C  CB  . ALA A  1 60  ? 0.90681   -14.13684 30.43706  1.000 29.88793  ? 86  ALA A CB  1 
ATOM   454  N  N   . SER A  1 61  ? 3.81871   -13.89468 28.88992  1.000 31.64182  ? 87  SER A N   1 
ATOM   455  C  CA  . SER A  1 61  ? 4.57803   -13.24791 27.82305  1.000 33.05197  ? 87  SER A CA  1 
ATOM   456  C  C   . SER A  1 61  ? 5.13082   -14.27003 26.83583  1.000 32.97673  ? 87  SER A C   1 
ATOM   457  O  O   . SER A  1 61  ? 5.12602   -14.03474 25.62160  1.000 35.14201  ? 87  SER A O   1 
ATOM   458  C  CB  . SER A  1 61  ? 5.70661   -12.40587 28.41822  1.000 34.76124  ? 87  SER A CB  1 
ATOM   459  O  OG  . SER A  1 61  ? 6.41962   -13.13025 29.40531  1.000 36.09350  ? 87  SER A OG  1 
ATOM   460  N  N   . PHE A  1 62  ? 5.61243   -15.41098 27.33450  1.000 31.97000  ? 88  PHE A N   1 
ATOM   461  C  CA  . PHE A  1 62  ? 6.05155   -16.47609 26.43800  1.000 34.58639  ? 88  PHE A CA  1 
ATOM   462  C  C   . PHE A  1 62  ? 4.88661   -17.00782 25.61171  1.000 36.15956  ? 88  PHE A C   1 
ATOM   463  O  O   . PHE A  1 62  ? 5.01987   -17.23204 24.40072  1.000 38.80246  ? 88  PHE A O   1 
ATOM   464  C  CB  . PHE A  1 62  ? 6.70341   -17.60006 27.24418  1.000 36.05727  ? 88  PHE A CB  1 
ATOM   465  C  CG  . PHE A  1 62  ? 7.01760   -18.82596 26.43505  1.000 38.68402  ? 88  PHE A CG  1 
ATOM   466  C  CD1 . PHE A  1 62  ? 8.11322   -18.85026 25.58848  1.000 40.53679  ? 88  PHE A CD1 1 
ATOM   467  C  CD2 . PHE A  1 62  ? 6.22197   -19.95612 26.52654  1.000 38.72451  ? 88  PHE A CD2 1 
ATOM   468  C  CE1 . PHE A  1 62  ? 8.40697   -19.97666 24.84445  1.000 42.70913  ? 88  PHE A CE1 1 
ATOM   469  C  CE2 . PHE A  1 62  ? 6.51020   -21.08599 25.78437  1.000 41.50305  ? 88  PHE A CE2 1 
ATOM   470  C  CZ  . PHE A  1 62  ? 7.60430   -21.09633 24.94285  1.000 42.73595  ? 88  PHE A CZ  1 
ATOM   471  N  N   . LEU A  1 63  ? 3.73189   -17.20758 26.25180  1.000 36.42321  ? 89  LEU A N   1 
ATOM   472  C  CA  . LEU A  1 63  ? 2.54101   -17.63783 25.52755  1.000 38.12349  ? 89  LEU A CA  1 
ATOM   473  C  C   . LEU A  1 63  ? 2.14363   -16.61763 24.46728  1.000 42.76156  ? 89  LEU A C   1 
ATOM   474  O  O   . LEU A  1 63  ? 1.68329   -16.98720 23.38055  1.000 43.37162  ? 89  LEU A O   1 
ATOM   475  C  CB  . LEU A  1 63  ? 1.39592   -17.87549 26.51249  1.000 34.41186  ? 89  LEU A CB  1 
ATOM   476  C  CG  . LEU A  1 63  ? 0.00449   -18.15344 25.94417  1.000 33.57370  ? 89  LEU A CG  1 
ATOM   477  C  CD1 . LEU A  1 63  ? -0.60967  -19.36973 26.61771  1.000 32.06410  ? 89  LEU A CD1 1 
ATOM   478  C  CD2 . LEU A  1 63  ? -0.89026  -16.93791 26.11524  1.000 33.59259  ? 89  LEU A CD2 1 
ATOM   479  N  N   . GLU A  1 64  ? 2.31519   -15.32696 24.76538  1.000 46.06576  ? 90  GLU A N   1 
ATOM   480  C  CA  . GLU A  1 64  ? 2.06219   -14.29564 23.76406  1.000 50.55071  ? 90  GLU A CA  1 
ATOM   481  C  C   . GLU A  1 64  ? 3.03641   -14.41269 22.59960  1.000 52.39963  ? 90  GLU A C   1 
ATOM   482  O  O   . GLU A  1 64  ? 2.64310   -14.29285 21.43309  1.000 54.04002  ? 90  GLU A O   1 
ATOM   483  C  CB  . GLU A  1 64  ? 2.15741   -12.90983 24.40204  1.000 51.94593  ? 90  GLU A CB  1 
ATOM   484  C  CG  . GLU A  1 64  ? 2.13856   -11.76618 23.40059  1.000 57.69097  ? 90  GLU A CG  1 
ATOM   485  C  CD  . GLU A  1 64  ? 2.03387   -10.40878 24.06608  1.000 61.74347  ? 90  GLU A CD  1 
ATOM   486  O  OE1 . GLU A  1 64  ? 2.39452   -10.29828 25.25704  1.000 61.48705  ? 90  GLU A OE1 1 
ATOM   487  O  OE2 . GLU A  1 64  ? 1.59032   -9.45169  23.39770  1.000 63.88600  ? 90  GLU A OE2 1 
ATOM   488  N  N   . ARG A  1 65  ? 4.31580   -14.64281 22.89971  1.000 53.17424  ? 91  ARG A N   1 
ATOM   489  C  CA  . ARG A  1 65  ? 5.30783   -14.83256 21.84775  1.000 55.14750  ? 91  ARG A CA  1 
ATOM   490  C  C   . ARG A  1 65  ? 5.02619   -16.07074 21.00743  1.000 56.57024  ? 91  ARG A C   1 
ATOM   491  O  O   . ARG A  1 65  ? 5.46906   -16.13871 19.85545  1.000 58.34671  ? 91  ARG A O   1 
ATOM   492  C  CB  . ARG A  1 65  ? 6.71088   -14.92957 22.45066  1.000 54.93410  ? 91  ARG A CB  1 
ATOM   493  C  CG  . ARG A  1 65  ? 7.26358   -13.61361 22.96996  1.000 54.13383  ? 91  ARG A CG  1 
ATOM   494  C  CD  . ARG A  1 65  ? 8.76892   -13.69262 23.17228  1.000 54.27223  ? 91  ARG A CD  1 
ATOM   495  N  NE  . ARG A  1 65  ? 9.13913   -14.71200 24.14989  1.000 53.48273  ? 91  ARG A NE  1 
ATOM   496  C  CZ  . ARG A  1 65  ? 9.19565   -14.50416 25.46136  1.000 52.27374  ? 91  ARG A CZ  1 
ATOM   497  N  NH1 . ARG A  1 65  ? 8.90493   -13.30980 25.95885  1.000 51.88416  ? 91  ARG A NH1 1 
ATOM   498  N  NH2 . ARG A  1 65  ? 9.54277   -15.49067 26.27651  1.000 51.66476  ? 91  ARG A NH2 1 
ATOM   499  N  N   . GLN A  1 66  ? 4.30293   -17.04874 21.55358  1.000 55.45531  ? 92  GLN A N   1 
ATOM   500  C  CA  . GLN A  1 66  ? 4.02247   -18.29903 20.85732  1.000 55.10826  ? 92  GLN A CA  1 
ATOM   501  C  C   . GLN A  1 66  ? 2.55280   -18.43135 20.45867  1.000 54.35002  ? 92  GLN A C   1 
ATOM   502  O  O   . GLN A  1 66  ? 2.00034   -19.53391 20.46842  1.000 54.36799  ? 92  GLN A O   1 
ATOM   503  C  CB  . GLN A  1 66  ? 4.44415   -19.48469 21.72237  1.000 53.50750  ? 92  GLN A CB  1 
ATOM   504  C  CG  . GLN A  1 66  ? 5.89722   -19.45299 22.15811  1.000 52.93339  ? 92  GLN A CG  1 
ATOM   505  C  CD  . GLN A  1 66  ? 6.85546   -19.66024 21.00371  1.000 55.29308  ? 92  GLN A CD  1 
ATOM   506  O  OE1 . GLN A  1 66  ? 6.51246   -20.28763 20.00184  1.000 56.44339  ? 92  GLN A OE1 1 
ATOM   507  N  NE2 . GLN A  1 66  ? 8.06594   -19.13158 21.13794  1.000 56.30697  ? 92  GLN A NE2 1 
ATOM   508  N  N   . LEU A  1 67  ? 1.91070   -17.32194 20.08569  1.000 53.32240  ? 93  LEU A N   1 
ATOM   509  C  CA  . LEU A  1 67  ? 0.47638   -17.35353 19.81479  1.000 53.28583  ? 93  LEU A CA  1 
ATOM   510  C  C   . LEU A  1 67  ? 0.14198   -17.98524 18.46784  1.000 55.32573  ? 93  LEU A C   1 
ATOM   511  O  O   . LEU A  1 67  ? -0.93036  -18.58308 18.32272  1.000 56.16455  ? 93  LEU A O   1 
ATOM   512  C  CB  . LEU A  1 67  ? -0.10476  -15.93992 19.88084  1.000 53.84795  ? 93  LEU A CB  1 
ATOM   513  C  CG  . LEU A  1 67  ? -0.43502  -15.40692 21.27666  1.000 51.21693  ? 93  LEU A CG  1 
ATOM   514  C  CD1 . LEU A  1 67  ? -0.79181  -13.92937 21.21929  1.000 51.83098  ? 93  LEU A CD1 1 
ATOM   515  C  CD2 . LEU A  1 67  ? -1.55947  -16.21022 21.91087  1.000 49.67956  ? 93  LEU A CD2 1 
ATOM   516  N  N   . THR A  1 68  ? 1.02606   -17.86715 17.47818  1.000 54.67424  ? 94  THR A N   1 
ATOM   517  C  CA  . THR A  1 68  ? 0.75712   -18.36879 16.13687  1.000 55.94109  ? 94  THR A CA  1 
ATOM   518  C  C   . THR A  1 68  ? 1.55874   -19.61423 15.78487  1.000 56.59010  ? 94  THR A C   1 
ATOM   519  O  O   . THR A  1 68  ? 1.42650   -20.12117 14.66552  1.000 58.06970  ? 94  THR A O   1 
ATOM   520  C  CB  . THR A  1 68  ? 1.03418   -17.27683 15.09567  1.000 55.63050  ? 94  THR A CB  1 
ATOM   521  O  OG1 . THR A  1 68  ? 2.44242   -17.01819 15.03420  1.000 54.50916  ? 94  THR A OG1 1 
ATOM   522  C  CG2 . THR A  1 68  ? 0.30334   -15.99348 15.46026  1.000 55.31434  ? 94  THR A CG2 1 
ATOM   523  N  N   . ALA A  1 69  ? 2.37860   -20.12412 16.70167  1.000 56.39209  ? 95  ALA A N   1 
ATOM   524  C  CA  . ALA A  1 69  ? 3.22664   -21.27401 16.41448  1.000 59.05412  ? 95  ALA A CA  1 
ATOM   525  C  C   . ALA A  1 69  ? 2.50580   -22.60741 16.56791  1.000 59.46164  ? 95  ALA A C   1 
ATOM   526  O  O   . ALA A  1 69  ? 3.12395   -23.65306 16.33982  1.000 59.55687  ? 95  ALA A O   1 
ATOM   527  C  CB  . ALA A  1 69  ? 4.46331   -21.25159 17.31678  1.000 59.45582  ? 95  ALA A CB  1 
ATOM   528  N  N   . GLY A  1 70  ? 1.22838   -22.60191 16.94111  1.000 57.14137  ? 96  GLY A N   1 
ATOM   529  C  CA  . GLY A  1 70  ? 0.50040   -23.84406 17.12179  1.000 57.02344  ? 96  GLY A CA  1 
ATOM   530  C  C   . GLY A  1 70  ? 0.99496   -24.69346 18.27006  1.000 52.81250  ? 96  GLY A C   1 
ATOM   531  O  O   . GLY A  1 70  ? 0.81813   -25.91543 18.25095  1.000 51.33668  ? 96  GLY A O   1 
ATOM   532  N  N   . VAL A  1 71  ? 1.61302   -24.07563 19.27649  1.000 49.44039  ? 97  VAL A N   1 
ATOM   533  C  CA  . VAL A  1 71  ? 2.15759   -24.83704 20.39453  1.000 46.42938  ? 97  VAL A CA  1 
ATOM   534  C  C   . VAL A  1 71  ? 1.07701   -25.15540 21.42386  1.000 44.10931  ? 97  VAL A C   1 
ATOM   535  O  O   . VAL A  1 71  ? 1.09666   -26.22938 22.03718  1.000 43.06908  ? 97  VAL A O   1 
ATOM   536  C  CB  . VAL A  1 71  ? 3.33473   -24.06765 21.02003  1.000 45.47898  ? 97  VAL A CB  1 
ATOM   537  C  CG1 . VAL A  1 71  ? 2.95482   -22.61767 21.23437  1.000 45.65149  ? 97  VAL A CG1 1 
ATOM   538  C  CG2 . VAL A  1 71  ? 3.77939   -24.70910 22.32790  1.000 44.03972  ? 97  VAL A CG2 1 
ATOM   539  N  N   . PHE A  1 72  ? 0.11598   -24.25756 21.61862  1.000 43.26158  ? 98  PHE A N   1 
ATOM   540  C  CA  . PHE A  1 72  ? -0.92736  -24.43136 22.61662  1.000 39.59897  ? 98  PHE A CA  1 
ATOM   541  C  C   . PHE A  1 72  ? -2.27505  -24.67788 21.95114  1.000 38.28656  ? 98  PHE A C   1 
ATOM   542  O  O   . PHE A  1 72  ? -2.51342  -24.26545 20.81257  1.000 39.23950  ? 98  PHE A O   1 
ATOM   543  C  CB  . PHE A  1 72  ? -1.02154  -23.20858 23.53406  1.000 35.25801  ? 98  PHE A CB  1 
ATOM   544  C  CG  . PHE A  1 72  ? 0.23198   -22.93959 24.31270  1.000 35.48009  ? 98  PHE A CG  1 
ATOM   545  C  CD1 . PHE A  1 72  ? 0.65147   -23.81761 25.29763  1.000 35.54332  ? 98  PHE A CD1 1 
ATOM   546  C  CD2 . PHE A  1 72  ? 0.98965   -21.80776 24.06318  1.000 35.93361  ? 98  PHE A CD2 1 
ATOM   547  C  CE1 . PHE A  1 72  ? 1.80482   -23.57404 26.01776  1.000 35.57701  ? 98  PHE A CE1 1 
ATOM   548  C  CE2 . PHE A  1 72  ? 2.14470   -21.55821 24.77966  1.000 35.42252  ? 98  PHE A CE2 1 
ATOM   549  C  CZ  . PHE A  1 72  ? 2.55243   -22.44241 25.75867  1.000 35.26054  ? 98  PHE A CZ  1 
ATOM   550  N  N   . GLN A  1 73  ? -3.15769  -25.35693 22.68465  1.000 37.98215  ? 99  GLN A N   1 
ATOM   551  C  CA  . GLN A  1 73  ? -4.51389  -25.67206 22.25699  1.000 39.76074  ? 99  GLN A CA  1 
ATOM   552  C  C   . GLN A  1 73  ? -5.48125  -24.63275 22.79706  1.000 40.05928  ? 99  GLN A C   1 
ATOM   553  O  O   . GLN A  1 73  ? -5.40469  -24.28577 23.98535  1.000 37.24840  ? 99  GLN A O   1 
ATOM   554  C  CB  . GLN A  1 73  ? -4.91547  -27.06092 22.74818  1.000 41.71043  ? 99  GLN A CB  1 
ATOM   555  C  CG  . GLN A  1 73  ? -6.40327  -27.23957 23.01236  1.000 43.07478  ? 99  GLN A CG  1 
ATOM   556  C  CD  . GLN A  1 73  ? -7.17188  -27.64934 21.77245  1.000 45.32675  ? 99  GLN A CD  1 
ATOM   557  O  OE1 . GLN A  1 73  ? -6.76969  -28.56409 21.05442  1.000 47.83704  ? 99  GLN A OE1 1 
ATOM   558  N  NE2 . GLN A  1 73  ? -8.28810  -26.97652 21.51737  1.000 44.26495  ? 99  GLN A NE2 1 
ATOM   559  N  N   . PRO A  1 74  ? -6.38520  -24.10566 21.97303  1.000 41.53661  ? 100 PRO A N   1 
ATOM   560  C  CA  . PRO A  1 74  ? -7.36924  -23.14017 22.48089  1.000 40.83480  ? 100 PRO A CA  1 
ATOM   561  C  C   . PRO A  1 74  ? -8.29311  -23.78727 23.50295  1.000 39.73431  ? 100 PRO A C   1 
ATOM   562  O  O   . PRO A  1 74  ? -8.86210  -24.85527 23.26552  1.000 39.62793  ? 100 PRO A O   1 
ATOM   563  C  CB  . PRO A  1 74  ? -8.12669  -22.70579 21.22018  1.000 42.17055  ? 100 PRO A CB  1 
ATOM   564  C  CG  . PRO A  1 74  ? -7.88111  -23.79216 20.22794  1.000 43.89854  ? 100 PRO A CG  1 
ATOM   565  C  CD  . PRO A  1 74  ? -6.51646  -24.32648 20.52391  1.000 43.12485  ? 100 PRO A CD  1 
ATOM   566  N  N   . LEU A  1 75  ? -8.43662  -23.12698 24.64940  1.000 38.51745  ? 101 LEU A N   1 
ATOM   567  C  CA  . LEU A  1 75  ? -9.20580  -23.68298 25.75593  1.000 39.41139  ? 101 LEU A CA  1 
ATOM   568  C  C   . LEU A  1 75  ? -10.68901 -23.71675 25.40847  1.000 41.94166  ? 101 LEU A C   1 
ATOM   569  O  O   . LEU A  1 75  ? -11.28340 -22.68255 25.08675  1.000 43.52454  ? 101 LEU A O   1 
ATOM   570  C  CB  . LEU A  1 75  ? -8.97384  -22.86304 27.02256  1.000 35.71713  ? 101 LEU A CB  1 
ATOM   571  C  CG  . LEU A  1 75  ? -7.59805  -22.98858 27.67770  1.000 33.99003  ? 101 LEU A CG  1 
ATOM   572  C  CD1 . LEU A  1 75  ? -7.54328  -22.18217 28.96635  1.000 32.08479  ? 101 LEU A CD1 1 
ATOM   573  C  CD2 . LEU A  1 75  ? -7.26023  -24.44832 27.93808  1.000 33.46558  ? 101 LEU A CD2 1 
ATOM   574  N  N   . ASP A  1 76  ? -11.28466 -24.90453 25.47378  1.000 42.41370  ? 102 ASP A N   1 
ATOM   575  C  CA  . ASP A  1 76  ? -12.72636 -25.05793 25.29586  1.000 43.52896  ? 102 ASP A CA  1 
ATOM   576  C  C   . ASP A  1 76  ? -13.42109 -24.48334 26.52265  1.000 42.40366  ? 102 ASP A C   1 
ATOM   577  O  O   . ASP A  1 76  ? -13.47874 -25.12057 27.57671  1.000 40.97242  ? 102 ASP A O   1 
ATOM   578  C  CB  . ASP A  1 76  ? -13.08632 -26.52501 25.08837  1.000 43.28214  ? 102 ASP A CB  1 
ATOM   579  C  CG  . ASP A  1 76  ? -14.47411 -26.71222 24.50010  1.000 43.72392  ? 102 ASP A CG  1 
ATOM   580  O  OD1 . ASP A  1 76  ? -15.37333 -25.90020 24.80468  1.000 42.98965  ? 102 ASP A OD1 1 
ATOM   581  O  OD2 . ASP A  1 76  ? -14.66604 -27.67716 23.73028  1.000 44.36469  ? 102 ASP A OD2 1 
ATOM   582  N  N   . LYS A  1 77  ? -13.95112 -23.26530 26.38804  1.000 43.01769  ? 103 LYS A N   1 
ATOM   583  C  CA  . LYS A  1 77  ? -14.60352 -22.60318 27.51110  1.000 41.60632  ? 103 LYS A CA  1 
ATOM   584  C  C   . LYS A  1 77  ? -15.87453 -23.31605 27.95151  1.000 40.96200  ? 103 LYS A C   1 
ATOM   585  O  O   . LYS A  1 77  ? -16.31813 -23.11548 29.08713  1.000 38.35637  ? 103 LYS A O   1 
ATOM   586  C  CB  . LYS A  1 77  ? -14.92225 -21.15127 27.15163  1.000 42.70097  ? 103 LYS A CB  1 
ATOM   587  C  CG  . LYS A  1 77  ? -13.69258 -20.29449 26.90633  1.000 42.31948  ? 103 LYS A CG  1 
ATOM   588  C  CD  . LYS A  1 77  ? -12.87696 -20.12699 28.17699  1.000 40.44527  ? 103 LYS A CD  1 
ATOM   589  C  CE  . LYS A  1 77  ? -11.46113 -19.66919 27.86781  1.000 39.42530  ? 103 LYS A CE  1 
ATOM   590  N  NZ  . LYS A  1 77  ? -11.44156 -18.45962 26.99928  1.000 40.02063  ? 103 LYS A NZ  1 
ATOM   591  N  N   . SER A  1 78  ? -16.47065 -24.13711 27.08353  1.000 42.47895  ? 104 SER A N   1 
ATOM   592  C  CA  . SER A  1 78  ? -17.68075 -24.85673 27.46433  1.000 44.75187  ? 104 SER A CA  1 
ATOM   593  C  C   . SER A  1 78  ? -17.39131 -25.94756 28.48679  1.000 45.60842  ? 104 SER A C   1 
ATOM   594  O  O   . SER A  1 78  ? -18.28347 -26.32560 29.25391  1.000 45.72785  ? 104 SER A O   1 
ATOM   595  C  CB  . SER A  1 78  ? -18.35106 -25.44925 26.22530  1.000 46.82155  ? 104 SER A CB  1 
ATOM   596  O  OG  . SER A  1 78  ? -17.68284 -26.61997 25.78972  1.000 46.66568  ? 104 SER A OG  1 
ATOM   597  N  N   . LYS A  1 79  ? -16.16265 -26.45774 28.51829  1.000 44.93991  ? 105 LYS A N   1 
ATOM   598  C  CA  . LYS A  1 79  ? -15.75943 -27.47280 29.48090  1.000 44.57416  ? 105 LYS A CA  1 
ATOM   599  C  C   . LYS A  1 79  ? -15.26925 -26.87476 30.79435  1.000 41.60363  ? 105 LYS A C   1 
ATOM   600  O  O   . LYS A  1 79  ? -14.77437 -27.61419 31.65128  1.000 39.98204  ? 105 LYS A O   1 
ATOM   601  C  CB  . LYS A  1 79  ? -14.66840 -28.36829 28.88353  1.000 45.67003  ? 105 LYS A CB  1 
ATOM   602  C  CG  . LYS A  1 79  ? -14.88776 -28.75782 27.42920  1.000 48.93561  ? 105 LYS A CG  1 
ATOM   603  C  CD  . LYS A  1 79  ? -16.23024 -29.43974 27.21704  1.000 51.98264  ? 105 LYS A CD  1 
ATOM   604  C  CE  . LYS A  1 79  ? -16.49067 -29.67917 25.73879  1.000 54.43902  ? 105 LYS A CE  1 
ATOM   605  N  NZ  . LYS A  1 79  ? -17.94451 -29.74787 25.43007  1.000 56.66568  ? 105 LYS A NZ  1 
ATOM   606  N  N   . LEU A  1 80  ? -15.39497 -25.56013 30.97224  1.000 41.11951  ? 106 LEU A N   1 
ATOM   607  C  CA  . LEU A  1 80  ? -14.94456 -24.86884 32.18049  1.000 39.00872  ? 106 LEU A CA  1 
ATOM   608  C  C   . LEU A  1 80  ? -16.07607 -23.98180 32.68237  1.000 40.17034  ? 106 LEU A C   1 
ATOM   609  O  O   . LEU A  1 80  ? -16.05188 -22.75767 32.49434  1.000 39.91450  ? 106 LEU A O   1 
ATOM   610  C  CB  . LEU A  1 80  ? -13.68010 -24.05224 31.90929  1.000 36.56879  ? 106 LEU A CB  1 
ATOM   611  C  CG  . LEU A  1 80  ? -12.47397 -24.83197 31.38045  1.000 36.00300  ? 106 LEU A CG  1 
ATOM   612  C  CD1 . LEU A  1 80  ? -11.40849 -23.88603 30.84802  1.000 35.50298  ? 106 LEU A CD1 1 
ATOM   613  C  CD2 . LEU A  1 80  ? -11.90264 -25.73530 32.46138  1.000 34.05453  ? 106 LEU A CD2 1 
ATOM   614  N  N   . PRO A  1 81  ? -17.08889 -24.56738 33.32762  1.000 42.22706  ? 107 PRO A N   1 
ATOM   615  C  CA  . PRO A  1 81  ? -18.21790 -23.75005 33.80243  1.000 45.02057  ? 107 PRO A CA  1 
ATOM   616  C  C   . PRO A  1 81  ? -17.83221 -22.74244 34.87038  1.000 45.94767  ? 107 PRO A C   1 
ATOM   617  O  O   . PRO A  1 81  ? -18.41013 -21.64889 34.91276  1.000 47.73751  ? 107 PRO A O   1 
ATOM   618  C  CB  . PRO A  1 81  ? -19.20467 -24.79528 34.34561  1.000 46.30013  ? 107 PRO A CB  1 
ATOM   619  C  CG  . PRO A  1 81  ? -18.78630 -26.09257 33.72485  1.000 45.79209  ? 107 PRO A CG  1 
ATOM   620  C  CD  . PRO A  1 81  ? -17.30287 -26.00192 33.57667  1.000 43.15993  ? 107 PRO A CD  1 
ATOM   621  N  N   . GLU A  1 82  ? -16.87209 -23.07116 35.73285  1.000 45.13786  ? 108 GLU A N   1 
ATOM   622  C  CA  . GLU A  1 82  ? -16.46103 -22.18002 36.81100  1.000 44.83055  ? 108 GLU A CA  1 
ATOM   623  C  C   . GLU A  1 82  ? -15.52008 -21.07311 36.34591  1.000 38.94522  ? 108 GLU A C   1 
ATOM   624  O  O   . GLU A  1 82  ? -14.98369 -20.34351 37.18899  1.000 36.90255  ? 108 GLU A O   1 
ATOM   625  C  CB  . GLU A  1 82  ? -15.80495 -22.98475 37.93618  1.000 48.66932  ? 108 GLU A CB  1 
ATOM   626  C  CG  . GLU A  1 82  ? -16.76939 -23.88662 38.69034  1.000 53.60847  ? 108 GLU A CG  1 
ATOM   627  C  CD  . GLU A  1 82  ? -17.08042 -23.37269 40.08286  1.000 58.04563  ? 108 GLU A CD  1 
ATOM   628  O  OE1 . GLU A  1 82  ? -17.71084 -22.29975 40.19498  1.000 59.69786  ? 108 GLU A OE1 1 
ATOM   629  O  OE2 . GLU A  1 82  ? -16.69560 -24.04158 41.06518  1.000 59.12304  ? 108 GLU A OE2 1 
ATOM   630  N  N   . TRP A  1 83  ? -15.31440 -20.93103 35.03269  1.000 37.28963  ? 109 TRP A N   1 
ATOM   631  C  CA  . TRP A  1 83  ? -14.50819 -19.83558 34.50419  1.000 35.41016  ? 109 TRP A CA  1 
ATOM   632  C  C   . TRP A  1 83  ? -15.03269 -18.47475 34.94290  1.000 34.25516  ? 109 TRP A C   1 
ATOM   633  O  O   . TRP A  1 83  ? -14.25986 -17.51169 34.99747  1.000 32.56883  ? 109 TRP A O   1 
ATOM   634  C  CB  . TRP A  1 83  ? -14.46400 -19.91635 32.97508  1.000 36.73555  ? 109 TRP A CB  1 
ATOM   635  C  CG  . TRP A  1 83  ? -13.53437 -18.93277 32.32575  1.000 33.98452  ? 109 TRP A CG  1 
ATOM   636  C  CD1 . TRP A  1 83  ? -13.80722 -17.63440 32.00304  1.000 33.21045  ? 109 TRP A CD1 1 
ATOM   637  C  CD2 . TRP A  1 83  ? -12.18537 -19.17438 31.90675  1.000 31.44730  ? 109 TRP A CD2 1 
ATOM   638  N  NE1 . TRP A  1 83  ? -12.70997 -17.05135 31.41657  1.000 31.24555  ? 109 TRP A NE1 1 
ATOM   639  C  CE2 . TRP A  1 83  ? -11.70129 -17.97579 31.34513  1.000 31.08643  ? 109 TRP A CE2 1 
ATOM   640  C  CE3 . TRP A  1 83  ? -11.33922 -20.28644 31.95508  1.000 28.50139  ? 109 TRP A CE3 1 
ATOM   641  C  CZ2 . TRP A  1 83  ? -10.40937 -17.85826 30.83614  1.000 30.23831  ? 109 TRP A CZ2 1 
ATOM   642  C  CZ3 . TRP A  1 83  ? -10.05813 -20.16778 31.44872  1.000 27.36557  ? 109 TRP A CZ3 1 
ATOM   643  C  CH2 . TRP A  1 83  ? -9.60512  -18.96273 30.89754  1.000 28.28211  ? 109 TRP A CH2 1 
ATOM   644  N  N   . LYS A  1 84  ? -16.32499 -18.37980 35.26765  1.000 34.07844  ? 110 LYS A N   1 
ATOM   645  C  CA  . LYS A  1 84  ? -16.90086 -17.12903 35.74616  1.000 36.44897  ? 110 LYS A CA  1 
ATOM   646  C  C   . LYS A  1 84  ? -16.28015 -16.66458 37.05758  1.000 35.38353  ? 110 LYS A C   1 
ATOM   647  O  O   . LYS A  1 84  ? -16.42007 -15.48904 37.41229  1.000 35.80080  ? 110 LYS A O   1 
ATOM   648  C  CB  . LYS A  1 84  ? -18.41323 -17.28723 35.91621  1.000 41.02578  ? 110 LYS A CB  1 
ATOM   649  C  CG  . LYS A  1 84  ? -18.80852 -18.34135 36.94143  1.000 44.22182  ? 110 LYS A CG  1 
ATOM   650  C  CD  . LYS A  1 84  ? -20.31252 -18.56342 36.96710  1.000 49.05705  ? 110 LYS A CD  1 
ATOM   651  C  CE  . LYS A  1 84  ? -20.75126 -19.21358 38.27110  1.000 52.02759  ? 110 LYS A CE  1 
ATOM   652  N  NZ  . LYS A  1 84  ? -20.93726 -20.68555 38.13206  1.000 53.53328  ? 110 LYS A NZ  1 
ATOM   653  N  N   . ASN A  1 85  ? -15.59955 -17.55490 37.78502  1.000 33.75261  ? 111 ASN A N   1 
ATOM   654  C  CA  . ASN A  1 85  ? -15.00340 -17.17414 39.06051  1.000 31.34843  ? 111 ASN A CA  1 
ATOM   655  C  C   . ASN A  1 85  ? -13.79424 -16.26301 38.89436  1.000 29.72248  ? 111 ASN A C   1 
ATOM   656  O  O   . ASN A  1 85  ? -13.42005 -15.57395 39.84956  1.000 29.16168  ? 111 ASN A O   1 
ATOM   657  C  CB  . ASN A  1 85  ? -14.60042 -18.42204 39.84775  1.000 30.36889  ? 111 ASN A CB  1 
ATOM   658  C  CG  . ASN A  1 85  ? -15.79474 -19.23548 40.30293  1.000 30.71262  ? 111 ASN A CG  1 
ATOM   659  O  OD1 . ASN A  1 85  ? -16.89053 -18.70446 40.48237  1.000 32.63394  ? 111 ASN A OD1 1 
ATOM   660  N  ND2 . ASN A  1 85  ? -15.58776 -20.53287 40.49488  1.000 29.47948  ? 111 ASN A ND2 1 
ATOM   661  N  N   . LEU A  1 86  ? -13.17855 -16.24271 37.71535  1.000 28.55727  ? 112 LEU A N   1 
ATOM   662  C  CA  . LEU A  1 86  ? -11.97788 -15.44603 37.51057  1.000 26.86439  ? 112 LEU A CA  1 
ATOM   663  C  C   . LEU A  1 86  ? -12.30452 -13.95644 37.51693  1.000 28.40518  ? 112 LEU A C   1 
ATOM   664  O  O   . LEU A  1 86  ? -13.37288 -13.52740 37.07325  1.000 29.75940  ? 112 LEU A O   1 
ATOM   665  C  CB  . LEU A  1 86  ? -11.30197 -15.82916 36.19386  1.000 25.85270  ? 112 LEU A CB  1 
ATOM   666  C  CG  . LEU A  1 86  ? -10.74533 -17.25251 36.11778  1.000 25.96061  ? 112 LEU A CG  1 
ATOM   667  C  CD1 . LEU A  1 86  ? -10.45162 -17.64302 34.67764  1.000 25.05766  ? 112 LEU A CD1 1 
ATOM   668  C  CD2 . LEU A  1 86  ? -9.49882  -17.39101 36.97893  1.000 25.86944  ? 112 LEU A CD2 1 
ATOM   669  N  N   . ASP A  1 87  ? -11.36772 -13.16963 38.03058  1.000 29.69411  ? 113 ASP A N   1 
ATOM   670  C  CA  . ASP A  1 87  ? -11.53767 -11.72157 38.09897  1.000 31.29903  ? 113 ASP A CA  1 
ATOM   671  C  C   . ASP A  1 87  ? -11.58930 -11.13929 36.69241  1.000 30.59731  ? 113 ASP A C   1 
ATOM   672  O  O   . ASP A  1 87  ? -10.62680 -11.30088 35.93020  1.000 30.18021  ? 113 ASP A O   1 
ATOM   673  C  CB  . ASP A  1 87  ? -10.39423 -11.09507 38.89594  1.000 31.87156  ? 113 ASP A CB  1 
ATOM   674  C  CG  . ASP A  1 87  ? -10.69562 -9.67334  39.34325  1.000 35.74033  ? 113 ASP A CG  1 
ATOM   675  O  OD1 . ASP A  1 87  ? -11.24916 -8.88997  38.54355  1.000 38.71968  ? 113 ASP A OD1 1 
ATOM   676  O  OD2 . ASP A  1 87  ? -10.37208 -9.33625  40.50122  1.000 36.85339  ? 113 ASP A OD2 1 
ATOM   677  N  N   . PRO A  1 88  ? -12.67387 -10.46370 36.30500  1.000 33.00926  ? 114 PRO A N   1 
ATOM   678  C  CA  . PRO A  1 88  ? -12.72157 -9.87766  34.95553  1.000 33.86860  ? 114 PRO A CA  1 
ATOM   679  C  C   . PRO A  1 88  ? -11.65794 -8.82059  34.72244  1.000 33.39438  ? 114 PRO A C   1 
ATOM   680  O  O   . PRO A  1 88  ? -11.20075 -8.65863  33.58559  1.000 34.50800  ? 114 PRO A O   1 
ATOM   681  C  CB  . PRO A  1 88  ? -14.13782 -9.28842  34.87842  1.000 36.25726  ? 114 PRO A CB  1 
ATOM   682  C  CG  . PRO A  1 88  ? -14.55690 -9.10333  36.30190  1.000 36.76246  ? 114 PRO A CG  1 
ATOM   683  C  CD  . PRO A  1 88  ? -13.90954 -10.21648 37.06605  1.000 34.71607  ? 114 PRO A CD  1 
ATOM   684  N  N   . GLU A  1 89  ? -11.23931 -8.10383  35.76734  1.000 33.19473  ? 115 GLU A N   1 
ATOM   685  C  CA  . GLU A  1 89  ? -10.17706 -7.11366  35.61518  1.000 35.24158  ? 115 GLU A CA  1 
ATOM   686  C  C   . GLU A  1 89  ? -8.84776  -7.78285  35.27867  1.000 31.58803  ? 115 GLU A C   1 
ATOM   687  O  O   . GLU A  1 89  ? -8.15522  -7.38121  34.33400  1.000 31.27067  ? 115 GLU A O   1 
ATOM   688  C  CB  . GLU A  1 89  ? -10.06146 -6.28284  36.89398  1.000 39.61513  ? 115 GLU A CB  1 
ATOM   689  C  CG  . GLU A  1 89  ? -9.43144  -4.91498  36.70905  1.000 43.57545  ? 115 GLU A CG  1 
ATOM   690  C  CD  . GLU A  1 89  ? -9.55762  -4.05046  37.94874  1.000 47.89271  ? 115 GLU A CD  1 
ATOM   691  O  OE1 . GLU A  1 89  ? -9.51553  -4.60497  39.06724  1.000 49.52247  ? 115 GLU A OE1 1 
ATOM   692  O  OE2 . GLU A  1 89  ? -9.70174  -2.81800  37.80571  1.000 50.15316  ? 115 GLU A OE2 1 
ATOM   693  N  N   . LEU A  1 90  ? -8.47762  -8.81546  36.03987  1.000 28.04557  ? 116 LEU A N   1 
ATOM   694  C  CA  . LEU A  1 90  ? -7.25098  -9.54846  35.74613  1.000 25.88213  ? 116 LEU A CA  1 
ATOM   695  C  C   . LEU A  1 90  ? -7.34761  -10.28815 34.41691  1.000 25.90846  ? 116 LEU A C   1 
ATOM   696  O  O   . LEU A  1 90  ? -6.33871  -10.43916 33.71486  1.000 25.15402  ? 116 LEU A O   1 
ATOM   697  C  CB  . LEU A  1 90  ? -6.94344  -10.51910 36.88568  1.000 25.11646  ? 116 LEU A CB  1 
ATOM   698  C  CG  . LEU A  1 90  ? -6.85809  -9.87540  38.27323  1.000 24.89892  ? 116 LEU A CG  1 
ATOM   699  C  CD1 . LEU A  1 90  ? -6.67051  -10.92683 39.35574  1.000 21.93595  ? 116 LEU A CD1 1 
ATOM   700  C  CD2 . LEU A  1 90  ? -5.73775  -8.84578  38.32193  1.000 24.12089  ? 116 LEU A CD2 1 
ATOM   701  N  N   . LEU A  1 91  ? -8.54807  -10.74824 34.05308  1.000 27.84396  ? 117 LEU A N   1 
ATOM   702  C  CA  . LEU A  1 91  ? -8.74058  -11.35436 32.73970  1.000 28.81767  ? 117 LEU A CA  1 
ATOM   703  C  C   . LEU A  1 91  ? -8.48225  -10.34451 31.62887  1.000 29.35041  ? 117 LEU A C   1 
ATOM   704  O  O   . LEU A  1 91  ? -7.82096  -10.66093 30.63383  1.000 27.24779  ? 117 LEU A O   1 
ATOM   705  C  CB  . LEU A  1 91  ? -10.15352 -11.92657 32.62526  1.000 23.90193  ? 117 LEU A CB  1 
ATOM   706  C  CG  . LEU A  1 91  ? -10.39396 -13.31849 33.21295  1.000 26.30962  ? 117 LEU A CG  1 
ATOM   707  C  CD1 . LEU A  1 91  ? -11.86370 -13.69635 33.10506  1.000 26.51491  ? 117 LEU A CD1 1 
ATOM   708  C  CD2 . LEU A  1 91  ? -9.51948  -14.35399 32.52436  1.000 23.43454  ? 117 LEU A CD2 1 
ATOM   709  N  N   . LYS A  1 92  ? -8.99881  -9.12189  31.78075  1.000 30.77565  ? 118 LYS A N   1 
ATOM   710  C  CA  . LYS A  1 92  ? -8.71261  -8.07059  30.80972  1.000 33.67129  ? 118 LYS A CA  1 
ATOM   711  C  C   . LYS A  1 92  ? -7.22271  -7.76145  30.76215  1.000 34.59274  ? 118 LYS A C   1 
ATOM   712  O  O   . LYS A  1 92  ? -6.67354  -7.47164  29.69251  1.000 35.00153  ? 118 LYS A O   1 
ATOM   713  C  CB  . LYS A  1 92  ? -9.50640  -6.80805  31.14880  1.000 35.07401  ? 118 LYS A CB  1 
ATOM   714  C  CG  . LYS A  1 92  ? -11.00692 -6.92551  30.93526  1.000 38.81467  ? 118 LYS A CG  1 
ATOM   715  C  CD  . LYS A  1 92  ? -11.67357 -5.55929  30.94220  1.000 43.14147  ? 118 LYS A CD  1 
ATOM   716  C  CE  . LYS A  1 92  ? -13.16794 -5.66928  30.68100  1.000 47.48178  ? 118 LYS A CE  1 
ATOM   717  N  NZ  . LYS A  1 92  ? -13.90706 -6.18004  31.86911  1.000 48.25577  ? 118 LYS A NZ  1 
ATOM   718  N  N   . LEU A  1 93  ? -6.55346  -7.81292  31.91616  1.000 34.24706  ? 119 LEU A N   1 
ATOM   719  C  CA  . LEU A  1 93  ? -5.11773  -7.54747  31.94539  1.000 35.01063  ? 119 LEU A CA  1 
ATOM   720  C  C   . LEU A  1 93  ? -4.33874  -8.60779  31.17288  1.000 34.97389  ? 119 LEU A C   1 
ATOM   721  O  O   . LEU A  1 93  ? -3.43854  -8.27680  30.39158  1.000 34.15442  ? 119 LEU A O   1 
ATOM   722  C  CB  . LEU A  1 93  ? -4.62376  -7.46433  33.38988  1.000 34.23744  ? 119 LEU A CB  1 
ATOM   723  C  CG  . LEU A  1 93  ? -4.83934  -6.12319  34.09447  1.000 36.72052  ? 119 LEU A CG  1 
ATOM   724  C  CD1 . LEU A  1 93  ? -4.36891  -6.18918  35.54016  1.000 35.62105  ? 119 LEU A CD1 1 
ATOM   725  C  CD2 . LEU A  1 93  ? -4.13036  -5.00470  33.34472  1.000 36.75460  ? 119 LEU A CD2 1 
ATOM   726  N  N   . VAL A  1 94  ? -4.66846  -9.88619  31.37537  1.000 34.66469  ? 120 VAL A N   1 
ATOM   727  C  CA  . VAL A  1 94  ? -3.94602  -10.95061 30.68053  1.000 35.83712  ? 120 VAL A CA  1 
ATOM   728  C  C   . VAL A  1 94  ? -4.37530  -11.09940 29.22868  1.000 33.47701  ? 120 VAL A C   1 
ATOM   729  O  O   . VAL A  1 94  ? -3.64468  -11.70981 28.43739  1.000 33.38231  ? 120 VAL A O   1 
ATOM   730  C  CB  . VAL A  1 94  ? -4.11493  -12.31244 31.37091  1.000 37.62100  ? 120 VAL A CB  1 
ATOM   731  C  CG1 . VAL A  1 94  ? -3.65416  -12.23568 32.79670  1.000 37.92328  ? 120 VAL A CG1 1 
ATOM   732  C  CG2 . VAL A  1 94  ? -5.55658  -12.77996 31.29515  1.000 38.47833  ? 120 VAL A CG2 1 
ATOM   733  N  N   . ALA A  1 95  ? -5.54485  -10.57335 28.85559  1.000 34.45091  ? 121 ALA A N   1 
ATOM   734  C  CA  . ALA A  1 95  ? -5.96229  -10.62366 27.46109  1.000 35.48473  ? 121 ALA A CA  1 
ATOM   735  C  C   . ALA A  1 95  ? -5.01261  -9.85568  26.55366  1.000 36.67638  ? 121 ALA A C   1 
ATOM   736  O  O   . ALA A  1 95  ? -4.99855  -10.09687 25.34204  1.000 36.35701  ? 121 ALA A O   1 
ATOM   737  C  CB  . ALA A  1 95  ? -7.38323  -10.08089 27.32045  1.000 34.68580  ? 121 ALA A CB  1 
ATOM   738  N  N   . LYS A  1 96  ? -4.21874  -8.93795  27.11144  1.000 36.18450  ? 122 LYS A N   1 
ATOM   739  C  CA  . LYS A  1 96  ? -3.23045  -8.23044  26.30674  1.000 40.34644  ? 122 LYS A CA  1 
ATOM   740  C  C   . LYS A  1 96  ? -2.10135  -9.15730  25.87269  1.000 41.58205  ? 122 LYS A C   1 
ATOM   741  O  O   . LYS A  1 96  ? -1.45146  -8.90420  24.85214  1.000 43.66415  ? 122 LYS A O   1 
ATOM   742  C  CB  . LYS A  1 96  ? -2.68900  -7.03162  27.08570  1.000 42.17557  ? 122 LYS A CB  1 
ATOM   743  C  CG  . LYS A  1 96  ? -3.74802  -5.97199  27.37161  1.000 44.69923  ? 122 LYS A CG  1 
ATOM   744  C  CD  . LYS A  1 96  ? -3.52647  -5.29337  28.71538  1.000 46.45586  ? 122 LYS A CD  1 
ATOM   745  C  CE  . LYS A  1 96  ? -2.50748  -4.16802  28.62096  1.000 47.34409  ? 122 LYS A CE  1 
ATOM   746  N  NZ  . LYS A  1 96  ? -2.42627  -3.41824  29.90698  1.000 45.88597  ? 122 LYS A NZ  1 
ATOM   747  N  N   . HIS A  1 97  ? -1.85340  -10.22750 26.62917  1.000 40.97154  ? 123 HIS A N   1 
ATOM   748  C  CA  . HIS A  1 97  ? -0.94908  -11.28938 26.20768  1.000 40.43175  ? 123 HIS A CA  1 
ATOM   749  C  C   . HIS A  1 97  ? -1.66954  -12.42891 25.50130  1.000 38.41118  ? 123 HIS A C   1 
ATOM   750  O  O   . HIS A  1 97  ? -1.01519  -13.24372 24.84169  1.000 36.98502  ? 123 HIS A O   1 
ATOM   751  C  CB  . HIS A  1 97  ? -0.18882  -11.86204 27.41038  1.000 40.19347  ? 123 HIS A CB  1 
ATOM   752  C  CG  . HIS A  1 97  ? 0.58298   -10.84216 28.18670  1.000 41.64445  ? 123 HIS A CG  1 
ATOM   753  N  ND1 . HIS A  1 97  ? 1.62621   -10.12484 27.64265  1.000 42.58548  ? 123 HIS A ND1 1 
ATOM   754  C  CD2 . HIS A  1 97  ? 0.47252   -10.43017 29.47174  1.000 41.41255  ? 123 HIS A CD2 1 
ATOM   755  C  CE1 . HIS A  1 97  ? 2.12017   -9.30918  28.55683  1.000 42.37567  ? 123 HIS A CE1 1 
ATOM   756  N  NE2 . HIS A  1 97  ? 1.43815   -9.47498  29.67568  1.000 41.26571  ? 123 HIS A NE2 1 
ATOM   757  N  N   . ASP A  1 98  ? -2.99329  -12.50309 25.62469  1.000 39.20975  ? 124 ASP A N   1 
ATOM   758  C  CA  . ASP A  1 98  ? -3.76499  -13.62772 25.09752  1.000 40.44308  ? 124 ASP A CA  1 
ATOM   759  C  C   . ASP A  1 98  ? -5.15633  -13.12100 24.76355  1.000 41.24916  ? 124 ASP A C   1 
ATOM   760  O  O   . ASP A  1 98  ? -6.07964  -13.19941 25.58709  1.000 39.01766  ? 124 ASP A O   1 
ATOM   761  C  CB  . ASP A  1 98  ? -3.82144  -14.77996 26.09977  1.000 41.35668  ? 124 ASP A CB  1 
ATOM   762  C  CG  . ASP A  1 98  ? -4.70120  -15.92235 25.63621  1.000 43.45438  ? 124 ASP A CG  1 
ATOM   763  O  OD1 . ASP A  1 98  ? -4.70085  -16.22745 24.42535  1.000 44.60689  ? 124 ASP A OD1 1 
ATOM   764  O  OD2 . ASP A  1 98  ? -5.38587  -16.52376 26.49074  1.000 43.30159  ? 124 ASP A OD2 1 
ATOM   765  N  N   . PRO A  1 99  ? -5.34828  -12.58081 23.55797  1.000 44.56547  ? 125 PRO A N   1 
ATOM   766  C  CA  . PRO A  1 99  ? -6.62797  -11.94233 23.22387  1.000 45.04273  ? 125 PRO A CA  1 
ATOM   767  C  C   . PRO A  1 99  ? -7.80247  -12.89851 23.37516  1.000 45.11894  ? 125 PRO A C   1 
ATOM   768  O  O   . PRO A  1 99  ? -7.74084  -14.06078 22.96783  1.000 43.93975  ? 125 PRO A O   1 
ATOM   769  C  CB  . PRO A  1 99  ? -6.44030  -11.50443 21.76521  1.000 48.60423  ? 125 PRO A CB  1 
ATOM   770  C  CG  . PRO A  1 99  ? -5.26526  -12.28941 21.26180  1.000 49.29312  ? 125 PRO A CG  1 
ATOM   771  C  CD  . PRO A  1 99  ? -4.38298  -12.50035 22.44901  1.000 46.52813  ? 125 PRO A CD  1 
ATOM   772  N  N   . ASP A  1 100 ? -8.87384  -12.38878 23.98625  1.000 46.58875  ? 126 ASP A N   1 
ATOM   773  C  CA  . ASP A  1 100 ? -10.09826 -13.13546 24.27171  1.000 48.41502  ? 126 ASP A CA  1 
ATOM   774  C  C   . ASP A  1 100 ? -9.86248  -14.30943 25.21843  1.000 46.42327  ? 126 ASP A C   1 
ATOM   775  O  O   . ASP A  1 100 ? -10.68938 -15.22567 25.28271  1.000 47.86113  ? 126 ASP A O   1 
ATOM   776  C  CB  . ASP A  1 100 ? -10.77068 -13.62225 22.98151  1.000 53.79367  ? 126 ASP A CB  1 
ATOM   777  C  CG  . ASP A  1 100 ? -11.10131 -12.48618 22.03340  1.000 61.07063  ? 126 ASP A CG  1 
ATOM   778  O  OD1 . ASP A  1 100 ? -10.43009 -12.36721 20.98658  1.000 64.59495  ? 126 ASP A OD1 1 
ATOM   779  O  OD2 . ASP A  1 100 ? -12.03189 -11.71022 22.33702  1.000 65.69012  ? 126 ASP A OD2 1 
ATOM   780  N  N   . ASN A  1 101 ? -8.75442  -14.28605 25.96449  1.000 43.30748  ? 127 ASN A N   1 
ATOM   781  C  CA  . ASN A  1 101 ? -8.40945  -15.33827 26.92412  1.000 40.27376  ? 127 ASN A CA  1 
ATOM   782  C  C   . ASN A  1 101 ? -8.53928  -16.72103 26.28828  1.000 39.66911  ? 127 ASN A C   1 
ATOM   783  O  O   . ASN A  1 101 ? -9.20372  -17.61862 26.80997  1.000 40.78864  ? 127 ASN A O   1 
ATOM   784  C  CB  . ASN A  1 101 ? -9.26695  -15.22809 28.18604  1.000 39.10931  ? 127 ASN A CB  1 
ATOM   785  C  CG  . ASN A  1 101 ? -9.14605  -13.87269 28.85627  1.000 40.14311  ? 127 ASN A CG  1 
ATOM   786  O  OD1 . ASN A  1 101 ? -10.14762 -13.24598 29.20100  1.000 42.26034  ? 127 ASN A OD1 1 
ATOM   787  N  ND2 . ASN A  1 101 ? -7.91472  -13.41349 29.04471  1.000 38.66638  ? 127 ASN A ND2 1 
ATOM   788  N  N   . LYS A  1 102 ? -7.88202  -16.88658 25.14046  1.000 37.95794  ? 128 LYS A N   1 
ATOM   789  C  CA  . LYS A  1 102 ? -8.13905  -18.04441 24.29210  1.000 39.33725  ? 128 LYS A CA  1 
ATOM   790  C  C   . LYS A  1 102 ? -7.33401  -19.26646 24.72014  1.000 37.24316  ? 128 LYS A C   1 
ATOM   791  O  O   . LYS A  1 102 ? -7.87203  -20.37837 24.76717  1.000 39.40097  ? 128 LYS A O   1 
ATOM   792  C  CB  . LYS A  1 102 ? -7.83606  -17.68916 22.83700  1.000 40.87655  ? 128 LYS A CB  1 
ATOM   793  C  CG  . LYS A  1 102 ? -8.17990  -18.77293 21.83782  1.000 43.37774  ? 128 LYS A CG  1 
ATOM   794  C  CD  . LYS A  1 102 ? -7.24145  -18.71350 20.64938  1.000 45.09371  ? 128 LYS A CD  1 
ATOM   795  C  CE  . LYS A  1 102 ? -7.99854  -18.50397 19.35404  1.000 47.54970  ? 128 LYS A CE  1 
ATOM   796  N  NZ  . LYS A  1 102 ? -7.12268  -18.68650 18.16293  1.000 47.31867  ? 128 LYS A NZ  1 
ATOM   797  N  N   . PHE A  1 103 ? -6.05120  -19.08792 25.03069  1.000 34.08603  ? 129 PHE A N   1 
ATOM   798  C  CA  . PHE A  1 103 ? -5.16746  -20.21569 25.30006  1.000 32.55154  ? 129 PHE A CA  1 
ATOM   799  C  C   . PHE A  1 103 ? -4.87344  -20.43160 26.77667  1.000 30.02355  ? 129 PHE A C   1 
ATOM   800  O  O   . PHE A  1 103 ? -4.59455  -21.56628 27.17748  1.000 28.77323  ? 129 PHE A O   1 
ATOM   801  C  CB  . PHE A  1 103 ? -3.83205  -20.03480 24.56810  1.000 33.29153  ? 129 PHE A CB  1 
ATOM   802  C  CG  . PHE A  1 103 ? -3.93510  -20.12360 23.07306  1.000 38.52035  ? 129 PHE A CG  1 
ATOM   803  C  CD1 . PHE A  1 103 ? -4.20791  -21.33160 22.45338  1.000 40.27488  ? 129 PHE A CD1 1 
ATOM   804  C  CD2 . PHE A  1 103 ? -3.73781  -19.00161 22.28556  1.000 41.39016  ? 129 PHE A CD2 1 
ATOM   805  C  CE1 . PHE A  1 103 ? -4.29534  -21.41615 21.07615  1.000 43.00472  ? 129 PHE A CE1 1 
ATOM   806  C  CE2 . PHE A  1 103 ? -3.82087  -19.07955 20.90754  1.000 43.78117  ? 129 PHE A CE2 1 
ATOM   807  C  CZ  . PHE A  1 103 ? -4.10142  -20.28857 20.30229  1.000 44.18276  ? 129 PHE A CZ  1 
ATOM   808  N  N   . ALA A  1 104 ? -4.92347  -19.38437 27.59419  1.000 30.19880  ? 130 ALA A N   1 
ATOM   809  C  CA  . ALA A  1 104 ? -4.35314  -19.41691 28.93281  1.000 28.90421  ? 130 ALA A CA  1 
ATOM   810  C  C   . ALA A  1 104 ? -5.41517  -19.18773 29.99865  1.000 27.75174  ? 130 ALA A C   1 
ATOM   811  O  O   . ALA A  1 104 ? -6.32458  -18.37040 29.82211  1.000 26.46650  ? 130 ALA A O   1 
ATOM   812  C  CB  . ALA A  1 104 ? -3.25260  -18.36315 29.07154  1.000 22.22329  ? 130 ALA A CB  1 
ATOM   813  N  N   . MET A  1 105 ? -5.28620  -19.91366 31.11015  1.000 26.88454  ? 131 MET A N   1 
ATOM   814  C  CA  . MET A  1 105 ? -6.07077  -19.65883 32.30936  1.000 26.44623  ? 131 MET A CA  1 
ATOM   815  C  C   . MET A  1 105 ? -5.15966  -19.04939 33.36181  1.000 24.00095  ? 131 MET A C   1 
ATOM   816  O  O   . MET A  1 105 ? -4.19301  -19.70415 33.77870  1.000 22.09013  ? 131 MET A O   1 
ATOM   817  C  CB  . MET A  1 105 ? -6.70610  -20.94535 32.83489  1.000 28.72333  ? 131 MET A CB  1 
ATOM   818  C  CG  . MET A  1 105 ? -7.66671  -20.73187 33.99568  1.000 32.39481  ? 131 MET A CG  1 
ATOM   819  S  SD  . MET A  1 105 ? -7.97781  -22.23805 34.93654  1.000 36.07307  ? 131 MET A SD  1 
ATOM   820  C  CE  . MET A  1 105 ? -6.46025  -22.37316 35.87855  1.000 34.69215  ? 131 MET A CE  1 
ATOM   821  N  N   . PRO A  1 106 ? -5.40450  -17.81924 33.80882  1.000 24.35172  ? 132 PRO A N   1 
ATOM   822  C  CA  . PRO A  1 106 ? -4.49210  -17.19322 34.77620  1.000 22.11847  ? 132 PRO A CA  1 
ATOM   823  C  C   . PRO A  1 106 ? -4.48777  -17.94667 36.09945  1.000 21.05761  ? 132 PRO A C   1 
ATOM   824  O  O   . PRO A  1 106 ? -5.54035  -18.26590 36.65637  1.000 19.38734  ? 132 PRO A O   1 
ATOM   825  C  CB  . PRO A  1 106 ? -5.05422  -15.77478 34.92691  1.000 19.41414  ? 132 PRO A CB  1 
ATOM   826  C  CG  . PRO A  1 106 ? -6.48784  -15.88619 34.51466  1.000 20.43870  ? 132 PRO A CG  1 
ATOM   827  C  CD  . PRO A  1 106 ? -6.52616  -16.93696 33.44571  1.000 21.06340  ? 132 PRO A CD  1 
ATOM   828  N  N   . TYR A  1 107 ? -3.28477  -18.22941 36.60133  1.000 19.89847  ? 133 TYR A N   1 
ATOM   829  C  CA  . TYR A  1 107 ? -3.09339  -19.04054 37.79833  1.000 19.47786  ? 133 TYR A CA  1 
ATOM   830  C  C   . TYR A  1 107 ? -2.70288  -18.16277 38.97985  1.000 20.18422  ? 133 TYR A C   1 
ATOM   831  O  O   . TYR A  1 107 ? -3.49503  -17.98972 39.91031  1.000 19.93096  ? 133 TYR A O   1 
ATOM   832  C  CB  . TYR A  1 107 ? -2.03525  -20.10756 37.50324  1.000 18.79202  ? 133 TYR A CB  1 
ATOM   833  C  CG  . TYR A  1 107 ? -1.68140  -21.02754 38.64802  1.000 20.52711  ? 133 TYR A CG  1 
ATOM   834  C  CD1 . TYR A  1 107 ? -2.64505  -21.81816 39.25983  1.000 21.77527  ? 133 TYR A CD1 1 
ATOM   835  C  CD2 . TYR A  1 107 ? -0.37024  -21.12839 39.09472  1.000 19.20931  ? 133 TYR A CD2 1 
ATOM   836  C  CE1 . TYR A  1 107 ? -2.31315  -22.67014 40.29951  1.000 21.61880  ? 133 TYR A CE1 1 
ATOM   837  C  CE2 . TYR A  1 107 ? -0.02998  -21.97470 40.12978  1.000 19.02022  ? 133 TYR A CE2 1 
ATOM   838  C  CZ  . TYR A  1 107 ? -1.00323  -22.74298 40.72896  1.000 19.54528  ? 133 TYR A CZ  1 
ATOM   839  O  OH  . TYR A  1 107 ? -0.66067  -23.58751 41.76051  1.000 19.40623  ? 133 TYR A OH  1 
ATOM   840  N  N   . MET A  1 108 ? -1.49940  -17.59279 38.96798  1.000 19.60645  ? 134 MET A N   1 
ATOM   841  C  CA  . MET A  1 108 ? -1.04589  -16.64792 39.97714  1.000 19.30586  ? 134 MET A CA  1 
ATOM   842  C  C   . MET A  1 108 ? -0.45918  -15.42877 39.27853  1.000 20.80951  ? 134 MET A C   1 
ATOM   843  O  O   . MET A  1 108 ? -0.17835  -15.44986 38.07679  1.000 22.22197  ? 134 MET A O   1 
ATOM   844  C  CB  . MET A  1 108 ? -0.00510  -17.27770 40.91415  1.000 16.61537  ? 134 MET A CB  1 
ATOM   845  C  CG  . MET A  1 108 ? -0.49823  -18.50383 41.66312  1.000 18.51931  ? 134 MET A CG  1 
ATOM   846  S  SD  . MET A  1 108 ? -1.64156  -18.09577 42.99305  1.000 18.85294  ? 134 MET A SD  1 
ATOM   847  C  CE  . MET A  1 108 ? -2.54294  -19.63386 43.14411  1.000 18.52317  ? 134 MET A CE  1 
ATOM   848  N  N   . TRP A  1 109 ? -0.27206  -14.35394 40.04190  1.000 17.74241  ? 135 TRP A N   1 
ATOM   849  C  CA  . TRP A  1 109 ? 0.31456   -13.14119 39.49142  1.000 18.49856  ? 135 TRP A CA  1 
ATOM   850  C  C   . TRP A  1 109 ? 1.07936   -12.40395 40.57948  1.000 18.94126  ? 135 TRP A C   1 
ATOM   851  O  O   . TRP A  1 109 ? 0.87133   -12.62612 41.77474  1.000 19.02060  ? 135 TRP A O   1 
ATOM   852  C  CB  . TRP A  1 109 ? -0.74852  -12.22612 38.86848  1.000 19.07475  ? 135 TRP A CB  1 
ATOM   853  C  CG  . TRP A  1 109 ? -1.84001  -11.79515 39.80584  1.000 19.24840  ? 135 TRP A CG  1 
ATOM   854  C  CD1 . TRP A  1 109 ? -2.89920  -12.54327 40.23221  1.000 19.26734  ? 135 TRP A CD1 1 
ATOM   855  C  CD2 . TRP A  1 109 ? -1.99014  -10.50575 40.41340  1.000 19.33623  ? 135 TRP A CD2 1 
ATOM   856  N  NE1 . TRP A  1 109 ? -3.69310  -11.80349 41.07560  1.000 18.63721  ? 135 TRP A NE1 1 
ATOM   857  C  CE2 . TRP A  1 109 ? -3.15688  -10.54900 41.20273  1.000 20.48719  ? 135 TRP A CE2 1 
ATOM   858  C  CE3 . TRP A  1 109 ? -1.24888  -9.32088  40.36986  1.000 20.44158  ? 135 TRP A CE3 1 
ATOM   859  C  CZ2 . TRP A  1 109 ? -3.59842  -9.45403  41.94274  1.000 23.05773  ? 135 TRP A CZ2 1 
ATOM   860  C  CZ3 . TRP A  1 109 ? -1.68877  -8.23513  41.10509  1.000 22.63365  ? 135 TRP A CZ3 1 
ATOM   861  C  CH2 . TRP A  1 109 ? -2.85218  -8.30921  41.88131  1.000 23.98094  ? 135 TRP A CH2 1 
ATOM   862  N  N   . ALA A  1 110 ? 1.97893   -11.52505 40.14142  1.000 19.43612  ? 136 ALA A N   1 
ATOM   863  C  CA  . ALA A  1 110 ? 2.76101   -10.68335 41.03549  1.000 18.34317  ? 136 ALA A CA  1 
ATOM   864  C  C   . ALA A  1 110 ? 3.04192   -9.36499  40.32401  1.000 20.35651  ? 136 ALA A C   1 
ATOM   865  O  O   . ALA A  1 110 ? 2.65230   -9.16496  39.16987  1.000 21.35397  ? 136 ALA A O   1 
ATOM   866  C  CB  . ALA A  1 110 ? 4.05088   -11.38497 41.47150  1.000 17.75395  ? 136 ALA A CB  1 
ATOM   867  N  N   . THR A  1 111 ? 3.72493   -8.45824  41.02001  1.000 19.76855  ? 137 THR A N   1 
ATOM   868  C  CA  . THR A  1 111 ? 3.95062   -7.11279  40.51447  1.000 21.83597  ? 137 THR A CA  1 
ATOM   869  C  C   . THR A  1 111 ? 5.42223   -6.73722  40.62032  1.000 21.21601  ? 137 THR A C   1 
ATOM   870  O  O   . THR A  1 111 ? 6.20838   -7.38265  41.31905  1.000 19.47489  ? 137 THR A O   1 
ATOM   871  C  CB  . THR A  1 111 ? 3.11087   -6.07117  41.27158  1.000 23.92520  ? 137 THR A CB  1 
ATOM   872  O  OG1 . THR A  1 111 ? 3.43738   -6.11430  42.66646  1.000 24.46766  ? 137 THR A OG1 1 
ATOM   873  C  CG2 . THR A  1 111 ? 1.62334   -6.34005  41.09168  1.000 25.14338  ? 137 THR A CG2 1 
ATOM   874  N  N   . THR A  1 112 ? 5.77974   -5.67308  39.90406  1.000 20.90992  ? 138 THR A N   1 
ATOM   875  C  CA  . THR A  1 112 ? 7.08319   -5.02369  40.02258  1.000 21.04387  ? 138 THR A CA  1 
ATOM   876  C  C   . THR A  1 112 ? 6.87713   -3.77793  40.87759  1.000 19.21044  ? 138 THR A C   1 
ATOM   877  O  O   . THR A  1 112 ? 6.36858   -2.76142  40.39766  1.000 20.71549  ? 138 THR A O   1 
ATOM   878  C  CB  . THR A  1 112 ? 7.65026   -4.67330  38.65002  1.000 22.50405  ? 138 THR A CB  1 
ATOM   879  O  OG1 . THR A  1 112 ? 7.81758   -5.86828  37.87766  1.000 21.44103  ? 138 THR A OG1 1 
ATOM   880  C  CG2 . THR A  1 112 ? 8.99439   -3.97033  38.78838  1.000 22.77561  ? 138 THR A CG2 1 
ATOM   881  N  N   . GLY A  1 113 ? 7.26275   -3.85885  42.14973  1.000 17.15569  ? 139 GLY A N   1 
ATOM   882  C  CA  . GLY A  1 113 ? 7.00263   -2.80340  43.10192  1.000 16.46427  ? 139 GLY A CA  1 
ATOM   883  C  C   . GLY A  1 113 ? 8.27549   -2.35307  43.79470  1.000 17.60315  ? 139 GLY A C   1 
ATOM   884  O  O   . GLY A  1 113 ? 9.38429   -2.46793  43.25652  1.000 18.20186  ? 139 GLY A O   1 
ATOM   885  N  N   . ILE A  1 114 ? 8.10422   -1.83816  45.01105  1.000 15.28301  ? 140 ILE A N   1 
ATOM   886  C  CA  . ILE A  1 114 ? 9.20623   -1.27177  45.78225  1.000 17.49056  ? 140 ILE A CA  1 
ATOM   887  C  C   . ILE A  1 114 ? 9.47484   -2.16768  46.98278  1.000 17.77357  ? 140 ILE A C   1 
ATOM   888  O  O   . ILE A  1 114 ? 8.58655   -2.38471  47.81463  1.000 18.05899  ? 140 ILE A O   1 
ATOM   889  C  CB  . ILE A  1 114 ? 8.90438   0.16457   46.23588  1.000 17.98499  ? 140 ILE A CB  1 
ATOM   890  C  CG1 . ILE A  1 114 ? 8.61947   1.06177   45.03112  1.000 19.53591  ? 140 ILE A CG1 1 
ATOM   891  C  CG2 . ILE A  1 114 ? 10.06328  0.71740   47.05135  1.000 18.67861  ? 140 ILE A CG2 1 
ATOM   892  C  CD1 . ILE A  1 114 ? 8.26440   2.48718   45.40502  1.000 20.14940  ? 140 ILE A CD1 1 
ATOM   893  N  N   . GLY A  1 115 ? 10.69578  -2.68384  47.07600  1.000 16.88430  ? 141 GLY A N   1 
ATOM   894  C  CA  . GLY A  1 115 ? 11.16869  -3.34364  48.28194  1.000 18.64398  ? 141 GLY A CA  1 
ATOM   895  C  C   . GLY A  1 115 ? 12.02292  -2.36475  49.07533  1.000 20.01121  ? 141 GLY A C   1 
ATOM   896  O  O   . GLY A  1 115 ? 12.79746  -1.60444  48.50051  1.000 18.34021  ? 141 GLY A O   1 
ATOM   897  N  N   . TYR A  1 116 ? 11.85786  -2.37294  50.39399  1.000 20.82062  ? 142 TYR A N   1 
ATOM   898  C  CA  . TYR A  1 116 ? 12.53667  -1.34606  51.17356  1.000 21.48120  ? 142 TYR A CA  1 
ATOM   899  C  C   . TYR A  1 116 ? 12.74049  -1.79676  52.61186  1.000 22.52534  ? 142 TYR A C   1 
ATOM   900  O  O   . TYR A  1 116 ? 12.01457  -2.64638  53.13617  1.000 21.60771  ? 142 TYR A O   1 
ATOM   901  C  CB  . TYR A  1 116 ? 11.76735  -0.01885  51.13412  1.000 23.01996  ? 142 TYR A CB  1 
ATOM   902  C  CG  . TYR A  1 116 ? 10.41734  -0.05629  51.81481  1.000 23.27220  ? 142 TYR A CG  1 
ATOM   903  C  CD1 . TYR A  1 116 ? 10.26416  0.38737   53.12183  1.000 24.51113  ? 142 TYR A CD1 1 
ATOM   904  C  CD2 . TYR A  1 116 ? 9.29466   -0.52704  51.14704  1.000 23.71082  ? 142 TYR A CD2 1 
ATOM   905  C  CE1 . TYR A  1 116 ? 9.03176   0.35793   53.74705  1.000 25.71083  ? 142 TYR A CE1 1 
ATOM   906  C  CE2 . TYR A  1 116 ? 8.05790   -0.56016  51.76328  1.000 25.47691  ? 142 TYR A CE2 1 
ATOM   907  C  CZ  . TYR A  1 116 ? 7.93228   -0.11658  53.06298  1.000 26.35551  ? 142 TYR A CZ  1 
ATOM   908  O  OH  . TYR A  1 116 ? 6.70303   -0.14797  53.68062  1.000 27.08214  ? 142 TYR A OH  1 
ATOM   909  N  N   . ASN A  1 117 ? 13.75085  -1.19752  53.23874  1.000 22.66482  ? 143 ASN A N   1 
ATOM   910  C  CA  . ASN A  1 117 ? 14.02610  -1.36852  54.65998  1.000 22.95904  ? 143 ASN A CA  1 
ATOM   911  C  C   . ASN A  1 117 ? 13.15061  -0.38244  55.42501  1.000 22.71647  ? 143 ASN A C   1 
ATOM   912  O  O   . ASN A  1 117 ? 13.32433  0.83396   55.30243  1.000 21.10984  ? 143 ASN A O   1 
ATOM   913  C  CB  . ASN A  1 117 ? 15.50938  -1.13814  54.94256  1.000 25.17123  ? 143 ASN A CB  1 
ATOM   914  C  CG  . ASN A  1 117 ? 15.90062  -1.48398  56.36719  1.000 26.86191  ? 143 ASN A CG  1 
ATOM   915  O  OD1 . ASN A  1 117 ? 15.33145  -0.96573  57.32750  1.000 27.48339  ? 143 ASN A OD1 1 
ATOM   916  N  ND2 . ASN A  1 117 ? 16.88808  -2.36037  56.50916  1.000 28.16932  ? 143 ASN A ND2 1 
ATOM   917  N  N   . VAL A  1 118 ? 12.20956  -0.90850  56.21197  1.000 23.95949  ? 144 VAL A N   1 
ATOM   918  C  CA  . VAL A  1 118 ? 11.24572  -0.05730  56.90837  1.000 25.94758  ? 144 VAL A CA  1 
ATOM   919  C  C   . VAL A  1 118 ? 11.96178  0.92265   57.83085  1.000 27.59543  ? 144 VAL A C   1 
ATOM   920  O  O   . VAL A  1 118 ? 11.70869  2.13474   57.80007  1.000 27.27702  ? 144 VAL A O   1 
ATOM   921  C  CB  . VAL A  1 118 ? 10.23598  -0.92173  57.68517  1.000 27.28469  ? 144 VAL A CB  1 
ATOM   922  C  CG1 . VAL A  1 118 ? 9.28590   -0.04389  58.48417  1.000 29.56945  ? 144 VAL A CG1 1 
ATOM   923  C  CG2 . VAL A  1 118 ? 9.46845   -1.82653  56.73567  1.000 24.64213  ? 144 VAL A CG2 1 
ATOM   924  N  N   . ASP A  1 119 ? 12.87794  0.41095   58.65592  1.000 28.56409  ? 145 ASP A N   1 
ATOM   925  C  CA  . ASP A  1 119 ? 13.49487  1.23358   59.69151  1.000 32.59678  ? 145 ASP A CA  1 
ATOM   926  C  C   . ASP A  1 119 ? 14.37048  2.32682   59.09041  1.000 31.77247  ? 145 ASP A C   1 
ATOM   927  O  O   . ASP A  1 119 ? 14.28310  3.49110   59.49113  1.000 32.57881  ? 145 ASP A O   1 
ATOM   928  C  CB  . ASP A  1 119 ? 14.30109  0.35095   60.64350  1.000 36.17823  ? 145 ASP A CB  1 
ATOM   929  C  CG  . ASP A  1 119 ? 13.44642  -0.70397  61.31863  1.000 40.59488  ? 145 ASP A CG  1 
ATOM   930  O  OD1 . ASP A  1 119 ? 12.53511  -0.32881  62.08577  1.000 42.94954  ? 145 ASP A OD1 1 
ATOM   931  O  OD2 . ASP A  1 119 ? 13.68059  -1.90718  61.07824  1.000 41.79289  ? 145 ASP A OD2 1 
ATOM   932  N  N   . LYS A  1 120 ? 15.21585  1.97679   58.11961  1.000 31.38287  ? 146 LYS A N   1 
ATOM   933  C  CA  . LYS A  1 120 ? 16.10608  2.97421   57.53147  1.000 33.04549  ? 146 LYS A CA  1 
ATOM   934  C  C   . LYS A  1 120 ? 15.32763  4.01685   56.73519  1.000 30.48226  ? 146 LYS A C   1 
ATOM   935  O  O   . LYS A  1 120 ? 15.64690  5.21379   56.78533  1.000 31.00975  ? 146 LYS A O   1 
ATOM   936  C  CB  . LYS A  1 120 ? 17.14720  2.28607   56.65140  1.000 35.83134  ? 146 LYS A CB  1 
ATOM   937  C  CG  . LYS A  1 120 ? 17.90470  1.16799   57.35248  1.000 41.73339  ? 146 LYS A CG  1 
ATOM   938  C  CD  . LYS A  1 120 ? 19.38277  1.49732   57.48630  1.000 47.27458  ? 146 LYS A CD  1 
ATOM   939  C  CE  . LYS A  1 120 ? 20.18601  0.27203   57.89299  1.000 50.64104  ? 146 LYS A CE  1 
ATOM   940  N  NZ  . LYS A  1 120 ? 21.64756  0.55376   57.94122  1.000 52.91466  ? 146 LYS A NZ  1 
ATOM   941  N  N   . VAL A  1 121 ? 14.30183  3.58290   55.99833  1.000 28.55979  ? 147 VAL A N   1 
ATOM   942  C  CA  . VAL A  1 121 ? 13.48387  4.52176   55.23441  1.000 28.45257  ? 147 VAL A CA  1 
ATOM   943  C  C   . VAL A  1 121 ? 12.78163  5.49538   56.17181  1.000 31.23526  ? 147 VAL A C   1 
ATOM   944  O  O   . VAL A  1 121 ? 12.78333  6.71091   55.94606  1.000 28.75231  ? 147 VAL A O   1 
ATOM   945  C  CB  . VAL A  1 121 ? 12.47823  3.76614   54.34676  1.000 26.15230  ? 147 VAL A CB  1 
ATOM   946  C  CG1 . VAL A  1 121 ? 11.32808  4.67894   53.94640  1.000 25.43740  ? 147 VAL A CG1 1 
ATOM   947  C  CG2 . VAL A  1 121 ? 13.17297  3.21321   53.11218  1.000 24.69829  ? 147 VAL A CG2 1 
ATOM   948  N  N   . LYS A  1 122 ? 12.17728  4.97919   57.24574  1.000 33.71333  ? 148 LYS A N   1 
ATOM   949  C  CA  . LYS A  1 122 ? 11.48883  5.86244   58.17996  1.000 37.15750  ? 148 LYS A CA  1 
ATOM   950  C  C   . LYS A  1 122 ? 12.45535  6.66336   59.04313  1.000 38.21007  ? 148 LYS A C   1 
ATOM   951  O  O   . LYS A  1 122 ? 12.03787  7.63825   59.67569  1.000 37.97750  ? 148 LYS A O   1 
ATOM   952  C  CB  . LYS A  1 122 ? 10.53183  5.06015   59.06185  1.000 41.31601  ? 148 LYS A CB  1 
ATOM   953  C  CG  . LYS A  1 122 ? 9.15924   4.86527   58.43699  1.000 45.50023  ? 148 LYS A CG  1 
ATOM   954  C  CD  . LYS A  1 122 ? 8.09369   4.60305   59.48743  1.000 50.00278  ? 148 LYS A CD  1 
ATOM   955  C  CE  . LYS A  1 122 ? 7.95671   3.11845   59.77353  1.000 51.31329  ? 148 LYS A CE  1 
ATOM   956  N  NZ  . LYS A  1 122 ? 6.54927   2.65657   59.62543  1.000 51.48406  ? 148 LYS A NZ  1 
ATOM   957  N  N   . ALA A  1 123 ? 13.73024  6.27537   59.08983  1.000 38.78124  ? 149 ALA A N   1 
ATOM   958  C  CA  . ALA A  1 123 ? 14.71814  7.07978   59.79699  1.000 41.40979  ? 149 ALA A CA  1 
ATOM   959  C  C   . ALA A  1 123 ? 15.18816  8.25373   58.94891  1.000 41.13276  ? 149 ALA A C   1 
ATOM   960  O  O   . ALA A  1 123 ? 15.37814  9.35987   59.46676  1.000 41.93878  ? 149 ALA A O   1 
ATOM   961  C  CB  . ALA A  1 123 ? 15.90642  6.21076   60.21056  1.000 43.68175  ? 149 ALA A CB  1 
ATOM   962  N  N   . VAL A  1 124 ? 15.38063  8.03429   57.64434  1.000 39.54707  ? 150 VAL A N   1 
ATOM   963  C  CA  . VAL A  1 124 ? 15.83496  9.11417   56.76844  1.000 40.50070  ? 150 VAL A CA  1 
ATOM   964  C  C   . VAL A  1 124 ? 14.69302  9.91068   56.15143  1.000 40.50831  ? 150 VAL A C   1 
ATOM   965  O  O   . VAL A  1 124 ? 14.95034  10.93070  55.49311  1.000 40.15686  ? 150 VAL A O   1 
ATOM   966  C  CB  . VAL A  1 124 ? 16.73183  8.58131   55.63435  1.000 40.56329  ? 150 VAL A CB  1 
ATOM   967  C  CG1 . VAL A  1 124 ? 17.90515  7.80513   56.20649  1.000 41.41585  ? 150 VAL A CG1 1 
ATOM   968  C  CG2 . VAL A  1 124 ? 15.92276  7.71813   54.69007  1.000 40.10502  ? 150 VAL A CG2 1 
ATOM   969  N  N   . LEU A  1 125 ? 13.44226  9.48701   56.34003  1.000 40.38797  ? 151 LEU A N   1 
ATOM   970  C  CA  . LEU A  1 125 ? 12.30998  10.18698  55.75052  1.000 39.43343  ? 151 LEU A CA  1 
ATOM   971  C  C   . LEU A  1 125 ? 11.13699  10.36529  56.70403  1.000 41.33163  ? 151 LEU A C   1 
ATOM   972  O  O   . LEU A  1 125 ? 10.14701  10.99559  56.31816  1.000 39.73953  ? 151 LEU A O   1 
ATOM   973  C  CB  . LEU A  1 125 ? 11.82747  9.45374   54.48690  1.000 36.80689  ? 151 LEU A CB  1 
ATOM   974  C  CG  . LEU A  1 125 ? 12.66037  9.65726   53.21920  1.000 34.57390  ? 151 LEU A CG  1 
ATOM   975  C  CD1 . LEU A  1 125 ? 12.12577  8.80365   52.08043  1.000 31.80411  ? 151 LEU A CD1 1 
ATOM   976  C  CD2 . LEU A  1 125 ? 12.68690  11.12493  52.82365  1.000 34.97005  ? 151 LEU A CD2 1 
ATOM   977  N  N   . GLY A  1 126 ? 11.20678  9.83318   57.92136  1.000 42.28680  ? 152 GLY A N   1 
ATOM   978  C  CA  . GLY A  1 126 ? 10.16629  10.02704  58.90738  1.000 41.87177  ? 152 GLY A CA  1 
ATOM   979  C  C   . GLY A  1 126 ? 9.06136   8.98914   58.82101  1.000 41.42025  ? 152 GLY A C   1 
ATOM   980  O  O   . GLY A  1 126 ? 9.01039   8.14524   57.92276  1.000 40.22454  ? 152 GLY A O   1 
ATOM   981  N  N   . GLU A  1 127 ? 8.15164   9.06363   59.79648  1.000 43.09962  ? 153 GLU A N   1 
ATOM   982  C  CA  . GLU A  1 127 ? 6.97463   8.20227   59.79444  1.000 44.39267  ? 153 GLU A CA  1 
ATOM   983  C  C   . GLU A  1 127 ? 6.05680   8.49067   58.61422  1.000 40.56400  ? 153 GLU A C   1 
ATOM   984  O  O   . GLU A  1 127 ? 5.19620   7.66350   58.29408  1.000 40.36882  ? 153 GLU A O   1 
ATOM   985  C  CB  . GLU A  1 127 ? 6.20233   8.36865   61.10621  1.000 49.04545  ? 153 GLU A CB  1 
ATOM   986  C  CG  . GLU A  1 127 ? 5.33581   7.17793   61.49097  1.000 50.90690  ? 153 GLU A CG  1 
ATOM   987  C  CD  . GLU A  1 127 ? 6.13063   6.05539   62.12827  1.000 52.56597  ? 153 GLU A CD  1 
ATOM   988  O  OE1 . GLU A  1 127 ? 7.18697   6.34070   62.73116  1.000 53.74893  ? 153 GLU A OE1 1 
ATOM   989  O  OE2 . GLU A  1 127 ? 5.69668   4.88809   62.03006  1.000 51.86052  ? 153 GLU A OE2 1 
ATOM   990  N  N   . ASN A  1 128 ? 6.22097   9.64119   57.96422  1.000 38.84458  ? 154 ASN A N   1 
ATOM   991  C  CA  . ASN A  1 128 ? 5.39961   10.04181  56.83116  1.000 39.92007  ? 154 ASN A CA  1 
ATOM   992  C  C   . ASN A  1 128 ? 5.98470   9.61590   55.49215  1.000 37.96965  ? 154 ASN A C   1 
ATOM   993  O  O   . ASN A  1 128 ? 5.49648   10.06889  54.45138  1.000 38.94787  ? 154 ASN A O   1 
ATOM   994  C  CB  . ASN A  1 128 ? 5.20469   11.55955  56.83387  1.000 43.00011  ? 154 ASN A CB  1 
ATOM   995  C  CG  . ASN A  1 128 ? 4.33636   12.03210  57.97388  1.000 47.54043  ? 154 ASN A CG  1 
ATOM   996  O  OD1 . ASN A  1 128 ? 3.43755   11.31933  58.41981  1.000 50.08147  ? 154 ASN A OD1 1 
ATOM   997  N  ND2 . ASN A  1 128 ? 4.60237   13.23994  58.45955  1.000 49.51458  ? 154 ASN A ND2 1 
ATOM   998  N  N   . ALA A  1 129 ? 7.01364   8.77242   55.49636  1.000 36.21693  ? 155 ALA A N   1 
ATOM   999  C  CA  . ALA A  1 129 ? 7.67942   8.38275   54.26338  1.000 32.85931  ? 155 ALA A CA  1 
ATOM   1000 C  C   . ALA A  1 129 ? 6.66594   7.80225   53.27885  1.000 28.98228  ? 155 ALA A C   1 
ATOM   1001 O  O   . ALA A  1 129 ? 5.90806   6.89130   53.64178  1.000 24.86339  ? 155 ALA A O   1 
ATOM   1002 C  CB  . ALA A  1 129 ? 8.78037   7.36087   54.54922  1.000 31.57914  ? 155 ALA A CB  1 
ATOM   1003 N  N   . PRO A  1 130 ? 6.61480   8.29941   52.04184  1.000 29.57599  ? 156 PRO A N   1 
ATOM   1004 C  CA  . PRO A  1 130 ? 5.61413   7.82637   51.06767  1.000 27.48815  ? 156 PRO A CA  1 
ATOM   1005 C  C   . PRO A  1 130 ? 5.94220   6.43949   50.52360  1.000 24.58282  ? 156 PRO A C   1 
ATOM   1006 O  O   . PRO A  1 130 ? 6.19872   6.24950   49.33045  1.000 23.05491  ? 156 PRO A O   1 
ATOM   1007 C  CB  . PRO A  1 130 ? 5.67312   8.91380   49.98693  1.000 27.46011  ? 156 PRO A CB  1 
ATOM   1008 C  CG  . PRO A  1 130 ? 7.07990   9.39978   50.03154  1.000 29.45698  ? 156 PRO A CG  1 
ATOM   1009 C  CD  . PRO A  1 130 ? 7.50802   9.32420   51.47311  1.000 30.16730  ? 156 PRO A CD  1 
ATOM   1010 N  N   . VAL A  1 131 ? 5.92686   5.44372   51.41407  1.000 23.65267  ? 157 VAL A N   1 
ATOM   1011 C  CA  . VAL A  1 131 ? 6.19820   4.06694   51.01605  1.000 24.15927  ? 157 VAL A CA  1 
ATOM   1012 C  C   . VAL A  1 131 ? 5.09068   3.47167   50.16350  1.000 25.48880  ? 157 VAL A C   1 
ATOM   1013 O  O   . VAL A  1 131 ? 5.27618   2.39249   49.59165  1.000 27.03653  ? 157 VAL A O   1 
ATOM   1014 C  CB  . VAL A  1 131 ? 6.42721   3.17967   52.25669  1.000 23.40090  ? 157 VAL A CB  1 
ATOM   1015 C  CG1 . VAL A  1 131 ? 7.61336   3.68854   53.06031  1.000 22.70105  ? 157 VAL A CG1 1 
ATOM   1016 C  CG2 . VAL A  1 131 ? 5.17215   3.13556   53.11676  1.000 22.36694  ? 157 VAL A CG2 1 
ATOM   1017 N  N   . ASP A  1 132 ? 3.94469   4.14507   50.06408  1.000 25.26002  ? 158 ASP A N   1 
ATOM   1018 C  CA  . ASP A  1 132 ? 2.82597   3.68953   49.25179  1.000 24.11112  ? 158 ASP A CA  1 
ATOM   1019 C  C   . ASP A  1 132 ? 2.77763   4.37632   47.89154  1.000 22.38521  ? 158 ASP A C   1 
ATOM   1020 O  O   . ASP A  1 132 ? 1.72287   4.39148   47.24774  1.000 22.66469  ? 158 ASP A O   1 
ATOM   1021 C  CB  . ASP A  1 132 ? 1.50991   3.91058   49.99839  1.000 25.43241  ? 158 ASP A CB  1 
ATOM   1022 C  CG  . ASP A  1 132 ? 1.22822   5.37886   50.26361  1.000 26.60986  ? 158 ASP A CG  1 
ATOM   1023 O  OD1 . ASP A  1 132 ? 2.17164   6.19536   50.19218  1.000 26.69193  ? 158 ASP A OD1 1 
ATOM   1024 O  OD2 . ASP A  1 132 ? 0.05933   5.71738   50.54143  1.000 28.78194  ? 158 ASP A OD2 1 
ATOM   1025 N  N   . SER A  1 133 ? 3.89348   4.94582   47.44343  1.000 21.50457  ? 159 SER A N   1 
ATOM   1026 C  CA  . SER A  1 133 ? 3.91447   5.70205   46.20187  1.000 23.29790  ? 159 SER A CA  1 
ATOM   1027 C  C   . SER A  1 133 ? 5.29445   5.60142   45.57159  1.000 25.42919  ? 159 SER A C   1 
ATOM   1028 O  O   . SER A  1 133 ? 6.30610   5.49471   46.27051  1.000 26.70543  ? 159 SER A O   1 
ATOM   1029 C  CB  . SER A  1 133 ? 3.54711   7.17192   46.43882  1.000 23.50467  ? 159 SER A CB  1 
ATOM   1030 O  OG  . SER A  1 133 ? 4.02227   7.99484   45.38780  1.000 23.29921  ? 159 SER A OG  1 
ATOM   1031 N  N   . TRP A  1 134 ? 5.32467   5.64386   44.23625  1.000 24.68503  ? 160 TRP A N   1 
ATOM   1032 C  CA  . TRP A  1 134 ? 6.59693   5.67770   43.52397  1.000 22.86403  ? 160 TRP A CA  1 
ATOM   1033 C  C   . TRP A  1 134 ? 7.39431   6.93539   43.84538  1.000 22.47997  ? 160 TRP A C   1 
ATOM   1034 O  O   . TRP A  1 134 ? 8.59682   6.98290   43.55930  1.000 24.45863  ? 160 TRP A O   1 
ATOM   1035 C  CB  . TRP A  1 134 ? 6.36030   5.56820   42.01478  1.000 21.45389  ? 160 TRP A CB  1 
ATOM   1036 C  CG  . TRP A  1 134 ? 5.92329   4.19896   41.57303  1.000 21.23441  ? 160 TRP A CG  1 
ATOM   1037 C  CD1 . TRP A  1 134 ? 4.67133   3.82574   41.17603  1.000 22.71263  ? 160 TRP A CD1 1 
ATOM   1038 C  CD2 . TRP A  1 134 ? 6.73880   3.02226   41.48354  1.000 19.68499  ? 160 TRP A CD2 1 
ATOM   1039 N  NE1 . TRP A  1 134 ? 4.65651   2.49082   40.84702  1.000 16.77266  ? 160 TRP A NE1 1 
ATOM   1040 C  CE2 . TRP A  1 134 ? 5.91339   1.97526   41.02581  1.000 20.38090  ? 160 TRP A CE2 1 
ATOM   1041 C  CE3 . TRP A  1 134 ? 8.08594   2.75303   41.74542  1.000 19.51873  ? 160 TRP A CE3 1 
ATOM   1042 C  CZ2 . TRP A  1 134 ? 6.39020   0.67927   40.82848  1.000 20.85190  ? 160 TRP A CZ2 1 
ATOM   1043 C  CZ3 . TRP A  1 134 ? 8.55776   1.46658   41.54530  1.000 17.81906  ? 160 TRP A CZ3 1 
ATOM   1044 C  CH2 . TRP A  1 134 ? 7.71193   0.44646   41.09205  1.000 15.74347  ? 160 TRP A CH2 1 
ATOM   1045 N  N   . ASP A  1 135 ? 6.74905   7.94839   44.43836  1.000 21.60343  ? 161 ASP A N   1 
ATOM   1046 C  CA  . ASP A  1 135 ? 7.45871   9.12758   44.92739  1.000 22.85927  ? 161 ASP A CA  1 
ATOM   1047 C  C   . ASP A  1 135 ? 8.64191   8.75231   45.80741  1.000 21.83667  ? 161 ASP A C   1 
ATOM   1048 O  O   . ASP A  1 135 ? 9.64190   9.47803   45.84793  1.000 22.35889  ? 161 ASP A O   1 
ATOM   1049 C  CB  . ASP A  1 135 ? 6.50492   10.02743  45.71829  1.000 25.15507  ? 161 ASP A CB  1 
ATOM   1050 C  CG  . ASP A  1 135 ? 5.49937   10.73832  44.83677  1.000 28.41196  ? 161 ASP A CG  1 
ATOM   1051 O  OD1 . ASP A  1 135 ? 5.70383   10.77717  43.60661  1.000 29.55865  ? 161 ASP A OD1 1 
ATOM   1052 O  OD2 . ASP A  1 135 ? 4.50150   11.26005  45.37848  1.000 30.20574  ? 161 ASP A OD2 1 
ATOM   1053 N  N   . LEU A  1 136 ? 8.54175   7.62974   46.52452  1.000 18.62978  ? 162 LEU A N   1 
ATOM   1054 C  CA  . LEU A  1 136 ? 9.62670   7.19750   47.39782  1.000 23.23781  ? 162 LEU A CA  1 
ATOM   1055 C  C   . LEU A  1 136 ? 10.92366  6.98710   46.62902  1.000 24.94502  ? 162 LEU A C   1 
ATOM   1056 O  O   . LEU A  1 136 ? 12.00834  7.25029   47.16123  1.000 24.45837  ? 162 LEU A O   1 
ATOM   1057 C  CB  . LEU A  1 136 ? 9.23053   5.91008   48.12143  1.000 22.55976  ? 162 LEU A CB  1 
ATOM   1058 C  CG  . LEU A  1 136 ? 10.21270  5.37238   49.16354  1.000 23.00853  ? 162 LEU A CG  1 
ATOM   1059 C  CD1 . LEU A  1 136 ? 10.13997  6.19460   50.44005  1.000 21.66148  ? 162 LEU A CD1 1 
ATOM   1060 C  CD2 . LEU A  1 136 ? 9.94697   3.90199   49.44772  1.000 22.09316  ? 162 LEU A CD2 1 
ATOM   1061 N  N   . ILE A  1 137 ? 10.83806  6.52766   45.38250  1.000 24.39337  ? 163 ILE A N   1 
ATOM   1062 C  CA  . ILE A  1 137 ? 12.02339  6.17509   44.60916  1.000 26.72609  ? 163 ILE A CA  1 
ATOM   1063 C  C   . ILE A  1 137 ? 12.13216  6.93878   43.29812  1.000 26.93775  ? 163 ILE A C   1 
ATOM   1064 O  O   . ILE A  1 137 ? 13.21315  6.93572   42.68898  1.000 28.86118  ? 163 ILE A O   1 
ATOM   1065 C  CB  . ILE A  1 137 ? 12.08606  4.65392   44.34259  1.000 28.67151  ? 163 ILE A CB  1 
ATOM   1066 C  CG1 . ILE A  1 137 ? 13.53588  4.19187   44.17826  1.000 31.27838  ? 163 ILE A CG1 1 
ATOM   1067 C  CG2 . ILE A  1 137 ? 11.25356  4.28319   43.12205  1.000 28.72363  ? 163 ILE A CG2 1 
ATOM   1068 C  CD1 . ILE A  1 137 ? 13.69150  2.68948   44.08430  1.000 31.70715  ? 163 ILE A CD1 1 
ATOM   1069 N  N   . LEU A  1 138 ? 11.07048  7.60259   42.84264  1.000 26.27377  ? 164 LEU A N   1 
ATOM   1070 C  CA  . LEU A  1 138 ? 11.09035  8.30853   41.56894  1.000 25.26388  ? 164 LEU A CA  1 
ATOM   1071 C  C   . LEU A  1 138 ? 11.06800  9.82339   41.71856  1.000 26.17451  ? 164 LEU A C   1 
ATOM   1072 O  O   . LEU A  1 138 ? 11.02207  10.53035  40.70595  1.000 24.63636  ? 164 LEU A O   1 
ATOM   1073 C  CB  . LEU A  1 138 ? 9.91656   7.85208   40.69462  1.000 18.79464  ? 164 LEU A CB  1 
ATOM   1074 C  CG  . LEU A  1 138 ? 9.99400   6.39504   40.23047  1.000 18.18403  ? 164 LEU A CG  1 
ATOM   1075 C  CD1 . LEU A  1 138 ? 8.94716   6.10474   39.17251  1.000 18.26009  ? 164 LEU A CD1 1 
ATOM   1076 C  CD2 . LEU A  1 138 ? 11.38539  6.06508   39.71070  1.000 18.27157  ? 164 LEU A CD2 1 
ATOM   1077 N  N   . LYS A  1 139 ? 11.09495  10.34189  42.94651  1.000 27.09771  ? 165 LYS A N   1 
ATOM   1078 C  CA  . LYS A  1 139 ? 11.25198  11.77108  43.16881  1.000 29.90500  ? 165 LYS A CA  1 
ATOM   1079 C  C   . LYS A  1 139 ? 12.69072  12.05161  43.56461  1.000 27.71137  ? 165 LYS A C   1 
ATOM   1080 O  O   . LYS A  1 139 ? 13.16513  11.48816  44.56403  1.000 26.73280  ? 165 LYS A O   1 
ATOM   1081 C  CB  . LYS A  1 139 ? 10.29796  12.26295  44.25202  1.000 33.62513  ? 165 LYS A CB  1 
ATOM   1082 C  CG  . LYS A  1 139 ? 9.08170   13.00451  43.71391  1.000 37.30650  ? 165 LYS A CG  1 
ATOM   1083 C  CD  . LYS A  1 139 ? 8.08648   13.32839  44.81787  1.000 40.27777  ? 165 LYS A CD  1 
ATOM   1084 C  CE  . LYS A  1 139 ? 8.50719   14.55978  45.60327  1.000 44.43265  ? 165 LYS A CE  1 
ATOM   1085 N  NZ  . LYS A  1 139 ? 8.21131   15.81954  44.86381  1.000 46.75534  ? 165 LYS A NZ  1 
ATOM   1086 N  N   . PRO A  1 140 ? 13.41954  12.88993  42.82194  1.000 28.92989  ? 166 PRO A N   1 
ATOM   1087 C  CA  . PRO A  1 140 ? 14.84105  13.10795  43.14245  1.000 30.01688  ? 166 PRO A CA  1 
ATOM   1088 C  C   . PRO A  1 140 ? 15.08092  13.60490  44.55645  1.000 30.48067  ? 166 PRO A C   1 
ATOM   1089 O  O   . PRO A  1 140 ? 16.11911  13.28131  45.14783  1.000 29.24054  ? 166 PRO A O   1 
ATOM   1090 C  CB  . PRO A  1 140 ? 15.27687  14.14697  42.09933  1.000 32.49120  ? 166 PRO A CB  1 
ATOM   1091 C  CG  . PRO A  1 140 ? 14.31421  13.97914  40.97041  1.000 32.43772  ? 166 PRO A CG  1 
ATOM   1092 C  CD  . PRO A  1 140 ? 13.00633  13.60265  41.60132  1.000 30.19777  ? 166 PRO A CD  1 
ATOM   1093 N  N   . GLU A  1 141 ? 14.14564  14.37257  45.12121  1.000 31.77109  ? 167 GLU A N   1 
ATOM   1094 C  CA  . GLU A  1 141 ? 14.33138  14.90642  46.46651  1.000 35.54339  ? 167 GLU A CA  1 
ATOM   1095 C  C   . GLU A  1 141 ? 14.37313  13.80191  47.51583  1.000 33.44739  ? 167 GLU A C   1 
ATOM   1096 O  O   . GLU A  1 141 ? 15.07178  13.93765  48.52665  1.000 34.90956  ? 167 GLU A O   1 
ATOM   1097 C  CB  . GLU A  1 141 ? 13.22256  15.90921  46.78937  1.000 40.26286  ? 167 GLU A CB  1 
ATOM   1098 C  CG  . GLU A  1 141 ? 13.02718  16.98556  45.72808  1.000 47.37304  ? 167 GLU A CG  1 
ATOM   1099 C  CD  . GLU A  1 141 ? 12.07382  16.56170  44.62629  1.000 51.85756  ? 167 GLU A CD  1 
ATOM   1100 O  OE1 . GLU A  1 141 ? 10.84585  16.63681  44.83853  1.000 55.31056  ? 167 GLU A OE1 1 
ATOM   1101 O  OE2 . GLU A  1 141 ? 12.55305  16.15188  43.54862  1.000 54.60672  ? 167 GLU A OE2 1 
ATOM   1102 N  N   . ASN A  1 142 ? 13.63935  12.70842  47.29935  1.000 31.47450  ? 168 ASN A N   1 
ATOM   1103 C  CA  . ASN A  1 142 ? 13.68633  11.58622  48.22973  1.000 31.55258  ? 168 ASN A CA  1 
ATOM   1104 C  C   . ASN A  1 142 ? 14.86239  10.66135  47.94358  1.000 32.18947  ? 168 ASN A C   1 
ATOM   1105 O  O   . ASN A  1 142 ? 15.45216  10.10264  48.87761  1.000 21.30922  ? 168 ASN A O   1 
ATOM   1106 C  CB  . ASN A  1 142 ? 12.37363  10.80238  48.17547  1.000 29.75571  ? 168 ASN A CB  1 
ATOM   1107 C  CG  . ASN A  1 142 ? 11.19817  11.59596  48.71290  1.000 29.12638  ? 168 ASN A CG  1 
ATOM   1108 O  OD1 . ASN A  1 142 ? 11.32706  12.33378  49.69046  1.000 30.06487  ? 168 ASN A OD1 1 
ATOM   1109 N  ND2 . ASN A  1 142 ? 10.04228  11.44673  48.07581  1.000 25.90487  ? 168 ASN A ND2 1 
ATOM   1110 N  N   . LEU A  1 143 ? 15.21890  10.48942  46.66858  1.000 32.37817  ? 169 LEU A N   1 
ATOM   1111 C  CA  . LEU A  1 143 ? 16.37384  9.66384   46.33883  1.000 32.00866  ? 169 LEU A CA  1 
ATOM   1112 C  C   . LEU A  1 143 ? 17.66807  10.28831  46.84273  1.000 33.74052  ? 169 LEU A C   1 
ATOM   1113 O  O   . LEU A  1 143 ? 18.60826  9.56425   47.18468  1.000 34.75603  ? 169 LEU A O   1 
ATOM   1114 C  CB  . LEU A  1 143 ? 16.44260  9.42702   44.83042  1.000 28.41373  ? 169 LEU A CB  1 
ATOM   1115 C  CG  . LEU A  1 143 ? 16.71977  7.97982   44.41881  1.000 23.66470  ? 169 LEU A CG  1 
ATOM   1116 C  CD1 . LEU A  1 143 ? 15.67172  7.05099   45.01034  1.000 20.79914  ? 169 LEU A CD1 1 
ATOM   1117 C  CD2 . LEU A  1 143 ? 16.76898  7.84294   42.90557  1.000 21.87670  ? 169 LEU A CD2 1 
ATOM   1118 N  N   . GLU A  1 144 ? 17.73383  11.62062  46.91084  1.000 35.28645  ? 170 GLU A N   1 
ATOM   1119 C  CA  . GLU A  1 144 ? 18.91179  12.26657  47.48232  1.000 36.36891  ? 170 GLU A CA  1 
ATOM   1120 C  C   . GLU A  1 144 ? 19.09236  11.88544  48.94640  1.000 34.37317  ? 170 GLU A C   1 
ATOM   1121 O  O   . GLU A  1 144 ? 20.21608  11.63324  49.39697  1.000 35.01780  ? 170 GLU A O   1 
ATOM   1122 C  CB  . GLU A  1 144 ? 18.80692  13.78392  47.33456  1.000 40.76633  ? 170 GLU A CB  1 
ATOM   1123 C  CG  . GLU A  1 144 ? 19.05986  14.29007  45.92734  1.000 44.83780  ? 170 GLU A CG  1 
ATOM   1124 C  CD  . GLU A  1 144 ? 18.35189  15.60014  45.64604  1.000 47.99481  ? 170 GLU A CD  1 
ATOM   1125 O  OE1 . GLU A  1 144 ? 17.91827  16.26260  46.61245  1.000 48.89464  ? 170 GLU A OE1 1 
ATOM   1126 O  OE2 . GLU A  1 144 ? 18.22296  15.96403  44.45808  1.000 48.99913  ? 170 GLU A OE2 1 
ATOM   1127 N  N   . LYS A  1 145 ? 17.99621  11.83572  49.70462  1.000 33.30307  ? 171 LYS A N   1 
ATOM   1128 C  CA  . LYS A  1 145 ? 18.06666  11.45073  51.10771  1.000 33.83921  ? 171 LYS A CA  1 
ATOM   1129 C  C   . LYS A  1 145 ? 18.22733  9.94820   51.29541  1.000 33.61482  ? 171 LYS A C   1 
ATOM   1130 O  O   . LYS A  1 145 ? 18.70837  9.51714   52.34878  1.000 33.83034  ? 171 LYS A O   1 
ATOM   1131 C  CB  . LYS A  1 145 ? 16.81712  11.93581  51.84637  1.000 34.42389  ? 171 LYS A CB  1 
ATOM   1132 C  CG  . LYS A  1 145 ? 16.58032  13.43418  51.73205  1.000 37.22922  ? 171 LYS A CG  1 
ATOM   1133 C  CD  . LYS A  1 145 ? 15.24024  13.83687  52.32558  1.000 39.46504  ? 171 LYS A CD  1 
ATOM   1134 C  CE  . LYS A  1 145 ? 15.00929  15.33370  52.19179  1.000 42.55276  ? 171 LYS A CE  1 
ATOM   1135 N  NZ  . LYS A  1 145 ? 15.13014  15.78932  50.77886  1.000 44.76314  ? 171 LYS A NZ  1 
ATOM   1136 N  N   . LEU A  1 146 ? 17.83105  9.14660   50.30796  1.000 32.73784  ? 172 LEU A N   1 
ATOM   1137 C  CA  . LEU A  1 146 ? 17.98271  7.69877   50.39064  1.000 32.44057  ? 172 LEU A CA  1 
ATOM   1138 C  C   . LEU A  1 146 ? 19.31013  7.19043   49.83658  1.000 33.33272  ? 172 LEU A C   1 
ATOM   1139 O  O   . LEU A  1 146 ? 19.63444  6.01575   50.04258  1.000 33.18131  ? 172 LEU A O   1 
ATOM   1140 C  CB  . LEU A  1 146 ? 16.83387  7.00585   49.64977  1.000 30.71729  ? 172 LEU A CB  1 
ATOM   1141 C  CG  . LEU A  1 146 ? 15.48009  6.96667   50.35850  1.000 29.87790  ? 172 LEU A CG  1 
ATOM   1142 C  CD1 . LEU A  1 146 ? 14.39019  6.50861   49.40332  1.000 27.15692  ? 172 LEU A CD1 1 
ATOM   1143 C  CD2 . LEU A  1 146 ? 15.54828  6.05278   51.56779  1.000 29.55320  ? 172 LEU A CD2 1 
ATOM   1144 N  N   . LYS A  1 147 ? 20.07299  8.03627   49.13698  1.000 34.12945  ? 173 LYS A N   1 
ATOM   1145 C  CA  . LYS A  1 147 ? 21.29475  7.57779   48.47859  1.000 35.43161  ? 173 LYS A CA  1 
ATOM   1146 C  C   . LYS A  1 147 ? 22.27757  6.95279   49.46233  1.000 36.35052  ? 173 LYS A C   1 
ATOM   1147 O  O   . LYS A  1 147 ? 22.95390  5.97103   49.13231  1.000 36.57101  ? 173 LYS A O   1 
ATOM   1148 C  CB  . LYS A  1 147 ? 21.95523  8.74261   47.73927  1.000 38.76135  ? 173 LYS A CB  1 
ATOM   1149 C  CG  . LYS A  1 147 ? 23.24788  8.37318   47.02474  1.000 40.07078  ? 173 LYS A CG  1 
ATOM   1150 C  CD  . LYS A  1 147 ? 24.09939  9.59994   46.74049  1.000 41.87194  ? 173 LYS A CD  1 
ATOM   1151 C  CE  . LYS A  1 147 ? 25.43304  9.21133   46.12125  1.000 43.71861  ? 173 LYS A CE  1 
ATOM   1152 N  NZ  . LYS A  1 147 ? 26.16358  8.21055   46.94925  1.000 43.52512  ? 173 LYS A NZ  1 
ATOM   1153 N  N   . SER A  1 148 ? 22.37188  7.50324   50.67474  1.000 35.96603  ? 174 SER A N   1 
ATOM   1154 C  CA  . SER A  1 148 ? 23.39586  7.04560   51.60952  1.000 36.95896  ? 174 SER A CA  1 
ATOM   1155 C  C   . SER A  1 148 ? 23.15513  5.60531   52.04933  1.000 36.02760  ? 174 SER A C   1 
ATOM   1156 O  O   . SER A  1 148 ? 24.11082  4.84327   52.23844  1.000 37.99847  ? 174 SER A O   1 
ATOM   1157 C  CB  . SER A  1 148 ? 23.45567  7.97485   52.82187  1.000 38.84498  ? 174 SER A CB  1 
ATOM   1158 O  OG  . SER A  1 148 ? 22.63950  7.49447   53.87522  1.000 40.16706  ? 174 SER A OG  1 
ATOM   1159 N  N   . CYS A  1 149 ? 21.89398  5.20793   52.21222  1.000 33.17697  ? 175 CYS A N   1 
ATOM   1160 C  CA  A CYS A  1 149 ? 21.59098  3.85422   52.66232  0.578 33.38969  ? 175 CYS A CA  1 
ATOM   1161 C  CA  B CYS A  1 149 ? 21.55090  3.86620   52.65775  0.422 33.35754  ? 175 CYS A CA  1 
ATOM   1162 C  C   . CYS A  1 149 ? 21.47391  2.85505   51.51927  1.000 30.73768  ? 175 CYS A C   1 
ATOM   1163 O  O   . CYS A  1 149 ? 21.28708  1.66231   51.78181  1.000 30.03460  ? 175 CYS A O   1 
ATOM   1164 C  CB  A CYS A  1 149 ? 20.30722  3.82859   53.50888  0.578 33.64846  ? 175 CYS A CB  1 
ATOM   1165 C  CB  B CYS A  1 149 ? 20.21913  3.90093   53.41200  0.422 33.55949  ? 175 CYS A CB  1 
ATOM   1166 S  SG  A CYS A  1 149 ? 18.78279  4.42735   52.72994  0.578 33.04070  ? 175 CYS A SG  1 
ATOM   1167 S  SG  B CYS A  1 149 ? 20.32547  4.60247   55.07483  0.422 36.22739  ? 175 CYS A SG  1 
ATOM   1168 N  N   . GLY A  1 150 ? 21.59309  3.29875   50.26897  1.000 29.87606  ? 176 GLY A N   1 
ATOM   1169 C  CA  . GLY A  1 150 ? 21.62446  2.37838   49.14736  1.000 27.49778  ? 176 GLY A CA  1 
ATOM   1170 C  C   . GLY A  1 150 ? 20.35153  2.26859   48.33232  1.000 25.60943  ? 176 GLY A C   1 
ATOM   1171 O  O   . GLY A  1 150 ? 19.31595  1.82245   48.83498  1.000 23.97018  ? 176 GLY A O   1 
ATOM   1172 N  N   . VAL A  1 151 ? 20.42672  2.65643   47.06074  1.000 24.47781  ? 177 VAL A N   1 
ATOM   1173 C  CA  . VAL A  1 151 ? 19.31393  2.55903   46.12347  1.000 23.54722  ? 177 VAL A CA  1 
ATOM   1174 C  C   . VAL A  1 151 ? 19.74837  1.67823   44.96081  1.000 24.05494  ? 177 VAL A C   1 
ATOM   1175 O  O   . VAL A  1 151 ? 20.84723  1.85370   44.42135  1.000 26.00493  ? 177 VAL A O   1 
ATOM   1176 C  CB  . VAL A  1 151 ? 18.87273  3.94414   45.61470  1.000 24.29450  ? 177 VAL A CB  1 
ATOM   1177 C  CG1 . VAL A  1 151 ? 17.61439  3.82232   44.76528  1.000 22.95599  ? 177 VAL A CG1 1 
ATOM   1178 C  CG2 . VAL A  1 151 ? 18.66027  4.90349   46.77802  1.000 23.53138  ? 177 VAL A CG2 1 
ATOM   1179 N  N   . SER A  1 152 ? 18.88917  0.73828   44.57271  1.000 21.70889  ? 178 SER A N   1 
ATOM   1180 C  CA  . SER A  1 152 ? 19.16418  -0.13604  43.44365  1.000 24.06216  ? 178 SER A CA  1 
ATOM   1181 C  C   . SER A  1 152 ? 17.95270  -0.19201  42.52477  1.000 23.03085  ? 178 SER A C   1 
ATOM   1182 O  O   . SER A  1 152 ? 16.80446  -0.13225  42.97344  1.000 23.64728  ? 178 SER A O   1 
ATOM   1183 C  CB  . SER A  1 152 ? 19.53869  -1.55530  43.89842  1.000 26.38590  ? 178 SER A CB  1 
ATOM   1184 O  OG  . SER A  1 152 ? 18.38696  -2.32393  44.19058  1.000 28.01352  ? 178 SER A OG  1 
ATOM   1185 N  N   . PHE A  1 153 ? 18.22593  -0.29607  41.22801  1.000 20.29810  ? 179 PHE A N   1 
ATOM   1186 C  CA  . PHE A  1 153 ? 17.20259  -0.45460  40.20771  1.000 17.47708  ? 179 PHE A CA  1 
ATOM   1187 C  C   . PHE A  1 153 ? 17.38937  -1.79690  39.51531  1.000 19.63211  ? 179 PHE A C   1 
ATOM   1188 O  O   . PHE A  1 153 ? 18.49987  -2.33346  39.46005  1.000 17.80936  ? 179 PHE A O   1 
ATOM   1189 C  CB  . PHE A  1 153 ? 17.26468  0.67043   39.16216  1.000 18.55059  ? 179 PHE A CB  1 
ATOM   1190 C  CG  . PHE A  1 153 ? 16.51653  1.91704   39.55091  1.000 19.45509  ? 179 PHE A CG  1 
ATOM   1191 C  CD1 . PHE A  1 153 ? 16.39919  2.29466   40.87773  1.000 19.88560  ? 179 PHE A CD1 1 
ATOM   1192 C  CD2 . PHE A  1 153 ? 15.93491  2.71568   38.57948  1.000 21.09753  ? 179 PHE A CD2 1 
ATOM   1193 C  CE1 . PHE A  1 153 ? 15.71416  3.44362   41.22829  1.000 20.39301  ? 179 PHE A CE1 1 
ATOM   1194 C  CE2 . PHE A  1 153 ? 15.24791  3.86495   38.92311  1.000 20.30119  ? 179 PHE A CE2 1 
ATOM   1195 C  CZ  . PHE A  1 153 ? 15.13689  4.22925   40.24882  1.000 19.87092  ? 179 PHE A CZ  1 
ATOM   1196 N  N   . LEU A  1 154 ? 16.29394  -2.34031  38.99133  1.000 19.43616  ? 180 LEU A N   1 
ATOM   1197 C  CA  . LEU A  1 154 ? 16.39149  -3.53838  38.17132  1.000 19.55430  ? 180 LEU A CA  1 
ATOM   1198 C  C   . LEU A  1 154 ? 17.17102  -3.23854  36.89725  1.000 21.30948  ? 180 LEU A C   1 
ATOM   1199 O  O   . LEU A  1 154 ? 17.14916  -2.11967  36.37741  1.000 20.21473  ? 180 LEU A O   1 
ATOM   1200 C  CB  . LEU A  1 154 ? 15.00072  -4.06344  37.80776  1.000 17.36235  ? 180 LEU A CB  1 
ATOM   1201 C  CG  . LEU A  1 154 ? 14.10725  -4.65120  38.89979  1.000 16.82821  ? 180 LEU A CG  1 
ATOM   1202 C  CD1 . LEU A  1 154 ? 12.72773  -4.96089  38.33549  1.000 17.03440  ? 180 LEU A CD1 1 
ATOM   1203 C  CD2 . LEU A  1 154 ? 14.73486  -5.89947  39.49824  1.000 16.12290  ? 180 LEU A CD2 1 
ATOM   1204 N  N   . ASP A  1 155 ? 17.87285  -4.25003  36.39655  1.000 21.58314  ? 181 ASP A N   1 
ATOM   1205 C  CA  . ASP A  1 155 ? 18.48092  -4.16783  35.06948  1.000 23.95756  ? 181 ASP A CA  1 
ATOM   1206 C  C   . ASP A  1 155 ? 17.49821  -4.63827  34.00161  1.000 24.09525  ? 181 ASP A C   1 
ATOM   1207 O  O   . ASP A  1 155 ? 17.79932  -5.48916  33.16631  1.000 24.83371  ? 181 ASP A O   1 
ATOM   1208 C  CB  . ASP A  1 155 ? 19.77360  -4.97386  35.02634  1.000 25.46911  ? 181 ASP A CB  1 
ATOM   1209 C  CG  . ASP A  1 155 ? 20.62845  -4.63793  33.81610  1.000 26.00907  ? 181 ASP A CG  1 
ATOM   1210 O  OD1 . ASP A  1 155 ? 20.46245  -3.53243  33.25898  1.000 25.23707  ? 181 ASP A OD1 1 
ATOM   1211 O  OD2 . ASP A  1 155 ? 21.46292  -5.47891  33.41997  1.000 26.30271  ? 181 ASP A OD2 1 
ATOM   1212 N  N   . ALA A  1 156 ? 16.29043  -4.07745  34.04540  1.000 23.05771  ? 182 ALA A N   1 
ATOM   1213 C  CA  . ALA A  1 156 ? 15.20299  -4.43623  33.13776  1.000 21.19155  ? 182 ALA A CA  1 
ATOM   1214 C  C   . ALA A  1 156 ? 14.68124  -3.15508  32.50353  1.000 19.62379  ? 182 ALA A C   1 
ATOM   1215 O  O   . ALA A  1 156 ? 13.78982  -2.49434  33.05468  1.000 20.36604  ? 182 ALA A O   1 
ATOM   1216 C  CB  . ALA A  1 156 ? 14.09530  -5.18724  33.87325  1.000 19.66068  ? 182 ALA A CB  1 
ATOM   1217 N  N   . PRO A  1 157 ? 15.21540  -2.77169  31.33994  1.000 20.51819  ? 183 PRO A N   1 
ATOM   1218 C  CA  . PRO A  1 157 ? 14.80777  -1.49000  30.73714  1.000 21.48344  ? 183 PRO A CA  1 
ATOM   1219 C  C   . PRO A  1 157 ? 13.32723  -1.40704  30.41445  1.000 23.43387  ? 183 PRO A C   1 
ATOM   1220 O  O   . PRO A  1 157 ? 12.72598  -0.33960  30.57625  1.000 24.78051  ? 183 PRO A O   1 
ATOM   1221 C  CB  . PRO A  1 157 ? 15.66768  -1.41480  29.46675  1.000 22.19249  ? 183 PRO A CB  1 
ATOM   1222 C  CG  . PRO A  1 157 ? 16.07289  -2.83272  29.18784  1.000 22.55903  ? 183 PRO A CG  1 
ATOM   1223 C  CD  . PRO A  1 157 ? 16.22920  -3.46791  30.53184  1.000 21.46417  ? 183 PRO A CD  1 
ATOM   1224 N  N   . GLU A  1 158 ? 12.71849  -2.50480  29.96498  1.000 23.19977  ? 184 GLU A N   1 
ATOM   1225 C  CA  A GLU A  1 158 ? 11.30214  -2.47612  29.61248  0.490 25.49909  ? 184 GLU A CA  1 
ATOM   1226 C  CA  B GLU A  1 158 ? 11.30330  -2.47102  29.61127  0.510 25.49282  ? 184 GLU A CA  1 
ATOM   1227 C  C   . GLU A  1 158 ? 10.44029  -2.16892  30.83127  1.000 23.25263  ? 184 GLU A C   1 
ATOM   1228 O  O   . GLU A  1 158 ? 9.60392   -1.25656  30.80481  1.000 21.99360  ? 184 GLU A O   1 
ATOM   1229 C  CB  A GLU A  1 158 ? 10.89354  -3.80927  28.98296  0.490 26.73429  ? 184 GLU A CB  1 
ATOM   1230 C  CB  B GLU A  1 158 ? 10.89787  -3.79680  28.96442  0.510 26.75554  ? 184 GLU A CB  1 
ATOM   1231 C  CG  A GLU A  1 158 ? 11.52704  -4.08454  27.62571  0.490 29.87161  ? 184 GLU A CG  1 
ATOM   1232 C  CG  B GLU A  1 158 ? 11.78319  -4.19580  27.78980  0.510 30.49556  ? 184 GLU A CG  1 
ATOM   1233 C  CD  A GLU A  1 158 ? 12.94385  -4.61756  27.73307  0.490 30.82245  ? 184 GLU A CD  1 
ATOM   1234 C  CD  B GLU A  1 158 ? 11.32216  -5.46730  27.10139  0.510 30.76901  ? 184 GLU A CD  1 
ATOM   1235 O  OE1 A GLU A  1 158 ? 13.68992  -4.53301  26.73527  0.490 32.50440  ? 184 GLU A OE1 1 
ATOM   1236 O  OE1 B GLU A  1 158 ? 10.56530  -6.24347  27.71952  0.510 30.88572  ? 184 GLU A OE1 1 
ATOM   1237 O  OE2 A GLU A  1 158 ? 13.31275  -5.11916  28.81534  0.490 32.02058  ? 184 GLU A OE2 1 
ATOM   1238 O  OE2 B GLU A  1 158 ? 11.71978  -5.69085  25.93833  0.510 33.64234  ? 184 GLU A OE2 1 
ATOM   1239 N  N   . GLU A  1 159 ? 10.64130  -2.91807  31.91822  1.000 22.31146  ? 185 GLU A N   1 
ATOM   1240 C  CA  . GLU A  1 159 ? 9.84114   -2.71773  33.12222  1.000 22.22658  ? 185 GLU A CA  1 
ATOM   1241 C  C   . GLU A  1 159 ? 10.09975  -1.35219  33.74875  1.000 22.54659  ? 185 GLU A C   1 
ATOM   1242 O  O   . GLU A  1 159 ? 9.15629   -0.66327  34.15373  1.000 23.05880  ? 185 GLU A O   1 
ATOM   1243 C  CB  . GLU A  1 159 ? 10.12740  -3.83217  34.12716  1.000 22.71118  ? 185 GLU A CB  1 
ATOM   1244 C  CG  . GLU A  1 159 ? 10.17602  -5.21708  33.50482  1.000 26.26850  ? 185 GLU A CG  1 
ATOM   1245 C  CD  . GLU A  1 159 ? 9.87876   -6.31582  34.50296  1.000 27.73827  ? 185 GLU A CD  1 
ATOM   1246 O  OE1 . GLU A  1 159 ? 9.55711   -5.99402  35.66726  1.000 26.93274  ? 185 GLU A OE1 1 
ATOM   1247 O  OE2 . GLU A  1 159 ? 9.96189   -7.50199  34.12086  1.000 28.04200  ? 185 GLU A OE2 1 
ATOM   1248 N  N   . VAL A  1 160 ? 11.36701  -0.94301  33.84146  1.000 21.39777  ? 186 VAL A N   1 
ATOM   1249 C  CA  . VAL A  1 160 ? 11.67899  0.34308   34.45820  1.000 21.73783  ? 186 VAL A CA  1 
ATOM   1250 C  C   . VAL A  1 160 ? 11.10753  1.48650   33.62997  1.000 22.01481  ? 186 VAL A C   1 
ATOM   1251 O  O   . VAL A  1 160 ? 10.54777  2.44506   34.17671  1.000 18.84131  ? 186 VAL A O   1 
ATOM   1252 C  CB  . VAL A  1 160 ? 13.19839  0.49058   34.66396  1.000 23.29099  ? 186 VAL A CB  1 
ATOM   1253 C  CG1 . VAL A  1 160 ? 13.53299  1.88786   35.16591  1.000 21.51052  ? 186 VAL A CG1 1 
ATOM   1254 C  CG2 . VAL A  1 160 ? 13.70763  -0.56046  35.63726  1.000 24.51468  ? 186 VAL A CG2 1 
ATOM   1255 N  N   . PHE A  1 161 ? 11.22355  1.40008   32.30226  1.000 21.59166  ? 187 PHE A N   1 
ATOM   1256 C  CA  . PHE A  1 161 ? 10.69631  2.45620   31.44582  1.000 21.27257  ? 187 PHE A CA  1 
ATOM   1257 C  C   . PHE A  1 161 ? 9.17512   2.51277   31.50566  1.000 23.01072  ? 187 PHE A C   1 
ATOM   1258 O  O   . PHE A  1 161 ? 8.59358   3.60336   31.50346  1.000 24.08074  ? 187 PHE A O   1 
ATOM   1259 C  CB  . PHE A  1 161 ? 11.17266  2.25978   30.00640  1.000 21.84694  ? 187 PHE A CB  1 
ATOM   1260 C  CG  . PHE A  1 161 ? 12.38511  3.07318   29.65531  1.000 24.03478  ? 187 PHE A CG  1 
ATOM   1261 C  CD1 . PHE A  1 161 ? 12.30916  4.45421   29.56784  1.000 25.10827  ? 187 PHE A CD1 1 
ATOM   1262 C  CD2 . PHE A  1 161 ? 13.60282  2.45809   29.41852  1.000 26.56987  ? 187 PHE A CD2 1 
ATOM   1263 C  CE1 . PHE A  1 161 ? 13.42632  5.20590   29.24783  1.000 24.53111  ? 187 PHE A CE1 1 
ATOM   1264 C  CE2 . PHE A  1 161 ? 14.72214  3.20354   29.09792  1.000 26.41400  ? 187 PHE A CE2 1 
ATOM   1265 C  CZ  . PHE A  1 161 ? 14.63356  4.57864   29.01338  1.000 24.88390  ? 187 PHE A CZ  1 
ATOM   1266 N  N   . ALA A  1 162 ? 8.50984   1.35442   31.56533  1.000 22.13709  ? 188 ALA A N   1 
ATOM   1267 C  CA  . ALA A  1 162 ? 7.05799   1.35773   31.71554  1.000 21.78530  ? 188 ALA A CA  1 
ATOM   1268 C  C   . ALA A  1 162 ? 6.64748   1.96678   33.05012  1.000 22.17783  ? 188 ALA A C   1 
ATOM   1269 O  O   . ALA A  1 162 ? 5.68655   2.74393   33.11890  1.000 21.26415  ? 188 ALA A O   1 
ATOM   1270 C  CB  . ALA A  1 162 ? 6.51027   -0.06261  31.57924  1.000 20.16394  ? 188 ALA A CB  1 
ATOM   1271 N  N   . THR A  1 163 ? 7.37194   1.63116   34.12134  1.000 22.65974  ? 189 THR A N   1 
ATOM   1272 C  CA  . THR A  1 163 ? 7.08417   2.21196   35.42854  1.000 22.23524  ? 189 THR A CA  1 
ATOM   1273 C  C   . THR A  1 163 ? 7.25646   3.72611   35.41038  1.000 24.98447  ? 189 THR A C   1 
ATOM   1274 O  O   . THR A  1 163 ? 6.42560   4.46058   35.95780  1.000 18.76298  ? 189 THR A O   1 
ATOM   1275 C  CB  . THR A  1 163 ? 7.98954   1.58105   36.48665  1.000 19.89148  ? 189 THR A CB  1 
ATOM   1276 O  OG1 . THR A  1 163 ? 7.82392   0.15731   36.46993  1.000 19.14993  ? 189 THR A OG1 1 
ATOM   1277 C  CG2 . THR A  1 163 ? 7.65093   2.11239   37.86887  1.000 17.01575  ? 189 THR A CG2 1 
ATOM   1278 N  N   . VAL A  1 164 ? 8.32117   4.21222   34.76880  1.000 19.12711  ? 190 VAL A N   1 
ATOM   1279 C  CA  . VAL A  1 164 ? 8.56247   5.65135   34.71256  1.000 19.80074  ? 190 VAL A CA  1 
ATOM   1280 C  C   . VAL A  1 164 ? 7.49542   6.34449   33.87092  1.000 24.94882  ? 190 VAL A C   1 
ATOM   1281 O  O   . VAL A  1 164 ? 7.00267   7.42058   34.23325  1.000 25.09794  ? 190 VAL A O   1 
ATOM   1282 C  CB  . VAL A  1 164 ? 9.98077   5.93283   34.18304  1.000 20.26496  ? 190 VAL A CB  1 
ATOM   1283 C  CG1 . VAL A  1 164 ? 10.14440  7.40768   33.84474  1.000 21.19829  ? 190 VAL A CG1 1 
ATOM   1284 C  CG2 . VAL A  1 164 ? 11.02151  5.50084   35.20547  1.000 19.61799  ? 190 VAL A CG2 1 
ATOM   1285 N  N   . LEU A  1 165 ? 7.11604   5.74081   32.74038  1.000 24.44664  ? 191 LEU A N   1 
ATOM   1286 C  CA  . LEU A  1 165 ? 6.07909   6.32751   31.89740  1.000 24.93221  ? 191 LEU A CA  1 
ATOM   1287 C  C   . LEU A  1 165 ? 4.74714   6.39876   32.63275  1.000 25.59599  ? 191 LEU A C   1 
ATOM   1288 O  O   . LEU A  1 165 ? 4.01393   7.38710   32.50972  1.000 25.67312  ? 191 LEU A O   1 
ATOM   1289 C  CB  . LEU A  1 165 ? 5.93456   5.52389   30.60479  1.000 24.38062  ? 191 LEU A CB  1 
ATOM   1290 C  CG  . LEU A  1 165 ? 6.99830   5.73590   29.52528  1.000 25.56383  ? 191 LEU A CG  1 
ATOM   1291 C  CD1 . LEU A  1 165 ? 6.70623   4.86783   28.30897  1.000 27.20344  ? 191 LEU A CD1 1 
ATOM   1292 C  CD2 . LEU A  1 165 ? 7.08802   7.20165   29.13308  1.000 25.91277  ? 191 LEU A CD2 1 
ATOM   1293 N  N   . ASN A  1 166 ? 4.41503   5.35822   33.40176  1.000 25.73422  ? 192 ASN A N   1 
ATOM   1294 C  CA  . ASN A  1 166 ? 3.20069   5.40107   34.21008  1.000 27.46721  ? 192 ASN A CA  1 
ATOM   1295 C  C   . ASN A  1 166 ? 3.29873   6.46877   35.29276  1.000 27.12170  ? 192 ASN A C   1 
ATOM   1296 O  O   . ASN A  1 166 ? 2.32030   7.17059   35.57507  1.000 27.39466  ? 192 ASN A O   1 
ATOM   1297 C  CB  . ASN A  1 166 ? 2.93425   4.03072   34.83140  1.000 28.44088  ? 192 ASN A CB  1 
ATOM   1298 C  CG  . ASN A  1 166 ? 1.68724   4.01536   35.69275  1.000 28.85234  ? 192 ASN A CG  1 
ATOM   1299 O  OD1 . ASN A  1 166 ? 0.56689   4.05679   35.18421  1.000 28.79992  ? 192 ASN A OD1 1 
ATOM   1300 N  ND2 . ASN A  1 166 ? 1.87615   3.95880   37.00672  1.000 27.53405  ? 192 ASN A ND2 1 
ATOM   1301 N  N   . TYR A  1 167 ? 4.47554   6.60696   35.90884  1.000 26.68198  ? 193 TYR A N   1 
ATOM   1302 C  CA  . TYR A  1 167 ? 4.66256   7.62237   36.93908  1.000 26.86134  ? 193 TYR A CA  1 
ATOM   1303 C  C   . TYR A  1 167 ? 4.50942   9.02907   36.37782  1.000 26.93718  ? 193 TYR A C   1 
ATOM   1304 O  O   . TYR A  1 167 ? 4.02191   9.92580   37.07536  1.000 24.76629  ? 193 TYR A O   1 
ATOM   1305 C  CB  . TYR A  1 167 ? 6.03661   7.45488   37.58588  1.000 26.60449  ? 193 TYR A CB  1 
ATOM   1306 C  CG  . TYR A  1 167 ? 6.36093   8.48843   38.63954  1.000 27.33242  ? 193 TYR A CG  1 
ATOM   1307 C  CD1 . TYR A  1 167 ? 5.76607   8.44018   39.89244  1.000 29.06351  ? 193 TYR A CD1 1 
ATOM   1308 C  CD2 . TYR A  1 167 ? 7.26910   9.50744   38.38377  1.000 28.85211  ? 193 TYR A CD2 1 
ATOM   1309 C  CE1 . TYR A  1 167 ? 6.06243   9.37987   40.85994  1.000 31.35444  ? 193 TYR A CE1 1 
ATOM   1310 C  CE2 . TYR A  1 167 ? 7.57171   10.45289  39.34495  1.000 31.94828  ? 193 TYR A CE2 1 
ATOM   1311 C  CZ  . TYR A  1 167 ? 6.96562   10.38398  40.58144  1.000 33.46556  ? 193 TYR A CZ  1 
ATOM   1312 O  OH  . TYR A  1 167 ? 7.26322   11.32222  41.54292  1.000 36.42898  ? 193 TYR A OH  1 
ATOM   1313 N  N   . LEU A  1 168 ? 4.91594   9.24266   35.12860  1.000 29.37091  ? 194 LEU A N   1 
ATOM   1314 C  CA  . LEU A  1 168 ? 4.80768   10.55060  34.49516  1.000 31.32235  ? 194 LEU A CA  1 
ATOM   1315 C  C   . LEU A  1 168 ? 3.43402   10.80514  33.88370  1.000 33.32397  ? 194 LEU A C   1 
ATOM   1316 O  O   . LEU A  1 168 ? 3.25199   11.82721  33.21310  1.000 36.13221  ? 194 LEU A O   1 
ATOM   1317 C  CB  . LEU A  1 168 ? 5.88961   10.70669  33.42335  1.000 32.35063  ? 194 LEU A CB  1 
ATOM   1318 C  CG  . LEU A  1 168 ? 7.33499   10.66052  33.92293  1.000 32.98539  ? 194 LEU A CG  1 
ATOM   1319 C  CD1 . LEU A  1 168 ? 8.30907   10.93784  32.78775  1.000 33.85950  ? 194 LEU A CD1 1 
ATOM   1320 C  CD2 . LEU A  1 168 ? 7.54205   11.63945  35.06848  1.000 32.44066  ? 194 LEU A CD2 1 
ATOM   1321 N  N   . GLY A  1 169 ? 2.47072   9.91068   34.09702  1.000 33.14583  ? 195 GLY A N   1 
ATOM   1322 C  CA  . GLY A  1 169 ? 1.13664   10.08059  33.56321  1.000 35.92911  ? 195 GLY A CA  1 
ATOM   1323 C  C   . GLY A  1 169 ? 0.96072   9.67714   32.11622  1.000 38.16014  ? 195 GLY A C   1 
ATOM   1324 O  O   . GLY A  1 169 ? -0.14834  9.81608   31.58419  1.000 40.19814  ? 195 GLY A O   1 
ATOM   1325 N  N   . LYS A  1 170 ? 2.00851   9.18377   31.46176  1.000 37.09062  ? 196 LYS A N   1 
ATOM   1326 C  CA  . LYS A  1 170 ? 1.91934   8.78449   30.06729  1.000 36.50219  ? 196 LYS A CA  1 
ATOM   1327 C  C   . LYS A  1 170 ? 1.39734   7.35316   29.96045  1.000 35.44288  ? 196 LYS A C   1 
ATOM   1328 O  O   . LYS A  1 170 ? 1.13012   6.68013   30.96006  1.000 35.28688  ? 196 LYS A O   1 
ATOM   1329 C  CB  . LYS A  1 170 ? 3.28065   8.92016   29.38897  1.000 35.21836  ? 196 LYS A CB  1 
ATOM   1330 C  CG  . LYS A  1 170 ? 4.13354   10.05758  29.92589  1.000 35.29207  ? 196 LYS A CG  1 
ATOM   1331 C  CD  . LYS A  1 170 ? 3.82043   11.36403  29.21827  1.000 37.31331  ? 196 LYS A CD  1 
ATOM   1332 C  CE  . LYS A  1 170 ? 4.91192   11.72495  28.22512  1.000 39.34996  ? 196 LYS A CE  1 
ATOM   1333 N  NZ  . LYS A  1 170 ? 4.63781   13.02012  27.54476  1.000 41.84736  ? 196 LYS A NZ  1 
ATOM   1334 N  N   . ASP A  1 171 ? 1.24445   6.88630   28.72980  1.000 35.19521  ? 197 ASP A N   1 
ATOM   1335 C  CA  . ASP A  1 171 ? 0.86232   5.50077   28.48634  1.000 33.94249  ? 197 ASP A CA  1 
ATOM   1336 C  C   . ASP A  1 171 ? 1.99076   4.58843   28.94875  1.000 30.72343  ? 197 ASP A C   1 
ATOM   1337 O  O   . ASP A  1 171 ? 3.11083   4.69923   28.43229  1.000 29.40348  ? 197 ASP A O   1 
ATOM   1338 C  CB  . ASP A  1 171 ? 0.56628   5.29056   27.00116  1.000 36.03846  ? 197 ASP A CB  1 
ATOM   1339 C  CG  . ASP A  1 171 ? -0.01899  3.91928   26.70097  1.000 37.71230  ? 197 ASP A CG  1 
ATOM   1340 O  OD1 . ASP A  1 171 ? -0.23487  3.13005   27.64326  1.000 37.14959  ? 197 ASP A OD1 1 
ATOM   1341 O  OD2 . ASP A  1 171 ? -0.26834  3.63136   25.51140  1.000 40.24031  ? 197 ASP A OD2 1 
ATOM   1342 N  N   . PRO A  1 172 ? 1.75679   3.69602   29.91616  1.000 30.10028  ? 198 PRO A N   1 
ATOM   1343 C  CA  . PRO A  1 172 ? 2.84167   2.81600   30.38680  1.000 28.68333  ? 198 PRO A CA  1 
ATOM   1344 C  C   . PRO A  1 172 ? 3.51246   2.02035   29.28006  1.000 28.12067  ? 198 PRO A C   1 
ATOM   1345 O  O   . PRO A  1 172 ? 4.68928   1.65923   29.41167  1.000 26.50698  ? 198 PRO A O   1 
ATOM   1346 C  CB  . PRO A  1 172 ? 2.13058   1.89897   31.39098  1.000 28.80717  ? 198 PRO A CB  1 
ATOM   1347 C  CG  . PRO A  1 172 ? 0.96487   2.69817   31.86716  1.000 29.28401  ? 198 PRO A CG  1 
ATOM   1348 C  CD  . PRO A  1 172 ? 0.51545   3.51088   30.68787  1.000 30.17338  ? 198 PRO A CD  1 
ATOM   1349 N  N   . ASN A  1 173 ? 2.80143   1.73308   28.19211  1.000 29.01431  ? 199 ASN A N   1 
ATOM   1350 C  CA  . ASN A  1 173 ? 3.41975   1.11538   27.02759  1.000 30.47478  ? 199 ASN A CA  1 
ATOM   1351 C  C   . ASN A  1 173 ? 3.28797   2.03517   25.82231  1.000 30.37865  ? 199 ASN A C   1 
ATOM   1352 O  O   . ASN A  1 173 ? 2.73253   1.64144   24.79074  1.000 32.51937  ? 199 ASN A O   1 
ATOM   1353 C  CB  . ASN A  1 173 ? 2.78324   -0.23729  26.72618  1.000 31.36725  ? 199 ASN A CB  1 
ATOM   1354 C  CG  . ASN A  1 173 ? 2.90835   -1.21517  27.87308  1.000 32.60977  ? 199 ASN A CG  1 
ATOM   1355 O  OD1 . ASN A  1 173 ? 3.93520   -1.87318  28.03280  1.000 34.21936  ? 199 ASN A OD1 1 
ATOM   1356 N  ND2 . ASN A  1 173 ? 1.85477   -1.32322  28.67639  1.000 32.46405  ? 199 ASN A ND2 1 
ATOM   1357 N  N   . SER A  1 174 ? 3.78213   3.26416   25.95161  1.000 28.57282  ? 200 SER A N   1 
ATOM   1358 C  CA  . SER A  1 174 ? 3.71181   4.21721   24.85376  1.000 29.36976  ? 200 SER A CA  1 
ATOM   1359 C  C   . SER A  1 174 ? 4.44570   3.67969   23.63244  1.000 31.25332  ? 200 SER A C   1 
ATOM   1360 O  O   . SER A  1 174 ? 5.47705   3.01202   23.74898  1.000 28.84482  ? 200 SER A O   1 
ATOM   1361 C  CB  . SER A  1 174 ? 4.30938   5.55938   25.27878  1.000 28.90231  ? 200 SER A CB  1 
ATOM   1362 O  OG  . SER A  1 174 ? 4.51268   6.40601   24.16051  1.000 31.45698  ? 200 SER A OG  1 
ATOM   1363 N  N   . THR A  1 175 ? 3.89544   3.96267   22.45376  1.000 33.43430  ? 201 THR A N   1 
ATOM   1364 C  CA  . THR A  1 175 ? 4.50985   3.58369   21.19027  1.000 36.02208  ? 201 THR A CA  1 
ATOM   1365 C  C   . THR A  1 175 ? 5.26017   4.73967   20.54311  1.000 39.09274  ? 201 THR A C   1 
ATOM   1366 O  O   . THR A  1 175 ? 5.70239   4.61708   19.39663  1.000 34.36694  ? 201 THR A O   1 
ATOM   1367 C  CB  . THR A  1 175 ? 3.45155   3.04132   20.22685  1.000 36.90257  ? 201 THR A CB  1 
ATOM   1368 O  OG1 . THR A  1 175 ? 2.40391   4.00681   20.07041  1.000 37.39853  ? 201 THR A OG1 1 
ATOM   1369 C  CG2 . THR A  1 175 ? 2.86346   1.74257   20.76019  1.000 33.89321  ? 201 THR A CG2 1 
ATOM   1370 N  N   . LYS A  1 176 ? 5.41108   5.85501   21.25068  1.000 39.11211  ? 202 LYS A N   1 
ATOM   1371 C  CA  . LYS A  1 176 ? 6.12453   7.02113   20.74957  1.000 39.15538  ? 202 LYS A CA  1 
ATOM   1372 C  C   . LYS A  1 176 ? 7.54088   7.00603   21.31076  1.000 35.34400  ? 202 LYS A C   1 
ATOM   1373 O  O   . LYS A  1 176 ? 7.72786   6.97299   22.53225  1.000 33.94577  ? 202 LYS A O   1 
ATOM   1374 C  CB  . LYS A  1 176 ? 5.39841   8.30819   21.13980  1.000 41.09115  ? 202 LYS A CB  1 
ATOM   1375 C  CG  . LYS A  1 176 ? 3.88503   8.16514   21.19143  1.000 43.36331  ? 202 LYS A CG  1 
ATOM   1376 C  CD  . LYS A  1 176 ? 3.18852   9.50843   21.05174  1.000 47.85810  ? 202 LYS A CD  1 
ATOM   1377 C  CE  . LYS A  1 176 ? 1.69025   9.37358   21.27279  1.000 50.15814  ? 202 LYS A CE  1 
ATOM   1378 N  NZ  . LYS A  1 176 ? 1.14041   8.15850   20.60914  1.000 51.35384  ? 202 LYS A NZ  1 
ATOM   1379 N  N   . ALA A  1 177 ? 8.53383   7.02598   20.41761  1.000 34.08264  ? 203 ALA A N   1 
ATOM   1380 C  CA  . ALA A  1 177 ? 9.92487   6.97888   20.85622  1.000 34.59432  ? 203 ALA A CA  1 
ATOM   1381 C  C   . ALA A  1 177 ? 10.31182  8.22355   21.64338  1.000 37.16260  ? 203 ALA A C   1 
ATOM   1382 O  O   . ALA A  1 177 ? 11.20240  8.16213   22.50111  1.000 36.29164  ? 203 ALA A O   1 
ATOM   1383 C  CB  . ALA A  1 177 ? 10.84966  6.80538   19.65125  1.000 35.17710  ? 203 ALA A CB  1 
ATOM   1384 N  N   . ASP A  1 178 ? 9.66143   9.35739   21.36328  1.000 38.91465  ? 204 ASP A N   1 
ATOM   1385 C  CA  . ASP A  1 178 ? 9.97449   10.59292  22.07347  1.000 39.74778  ? 204 ASP A CA  1 
ATOM   1386 C  C   . ASP A  1 178 ? 9.69627   10.47062  23.56508  1.000 35.70670  ? 204 ASP A C   1 
ATOM   1387 O  O   . ASP A  1 178 ? 10.37787  11.10766  24.37575  1.000 34.87748  ? 204 ASP A O   1 
ATOM   1388 C  CB  . ASP A  1 178 ? 9.17881   11.75611  21.48049  1.000 43.20071  ? 204 ASP A CB  1 
ATOM   1389 C  CG  . ASP A  1 178 ? 9.79471   12.29341  20.20348  1.000 49.80819  ? 204 ASP A CG  1 
ATOM   1390 O  OD1 . ASP A  1 178 ? 10.80582  11.72309  19.74224  1.000 51.81804  ? 204 ASP A OD1 1 
ATOM   1391 O  OD2 . ASP A  1 178 ? 9.26794   13.28824  19.66161  1.000 52.74102  ? 204 ASP A OD2 1 
ATOM   1392 N  N   . ASP A  1 179 ? 8.70107   9.66522   23.94623  1.000 34.27217  ? 205 ASP A N   1 
ATOM   1393 C  CA  . ASP A  1 179 ? 8.43502   9.44213   25.36318  1.000 33.50836  ? 205 ASP A CA  1 
ATOM   1394 C  C   . ASP A  1 179 ? 9.60707   8.75439   26.04831  1.000 34.12491  ? 205 ASP A C   1 
ATOM   1395 O  O   . ASP A  1 179 ? 9.88180   9.01843   27.22457  1.000 33.09446  ? 205 ASP A O   1 
ATOM   1396 C  CB  . ASP A  1 179 ? 7.16269   8.61197   25.53761  1.000 32.62170  ? 205 ASP A CB  1 
ATOM   1397 C  CG  . ASP A  1 179 ? 5.90408   9.40720   25.25755  1.000 35.04027  ? 205 ASP A CG  1 
ATOM   1398 O  OD1 . ASP A  1 179 ? 5.96481   10.65325  25.30262  1.000 37.12670  ? 205 ASP A OD1 1 
ATOM   1399 O  OD2 . ASP A  1 179 ? 4.85261   8.78612   24.99539  1.000 35.87430  ? 205 ASP A OD2 1 
ATOM   1400 N  N   . TYR A  1 180 ? 10.30995  7.87619   25.33201  1.000 34.15177  ? 206 TYR A N   1 
ATOM   1401 C  CA  . TYR A  1 180 ? 11.43559  7.16171   25.92202  1.000 33.20939  ? 206 TYR A CA  1 
ATOM   1402 C  C   . TYR A  1 180 ? 12.70316  8.00747   25.89822  1.000 33.85568  ? 206 TYR A C   1 
ATOM   1403 O  O   . TYR A  1 180 ? 13.38807  8.13963   26.91840  1.000 34.07437  ? 206 TYR A O   1 
ATOM   1404 C  CB  . TYR A  1 180 ? 11.65406  5.83544   25.19090  1.000 27.81440  ? 206 TYR A CB  1 
ATOM   1405 C  CG  . TYR A  1 180 ? 10.48328  4.88463   25.30120  1.000 27.08245  ? 206 TYR A CG  1 
ATOM   1406 C  CD1 . TYR A  1 180 ? 10.43886  3.91926   26.29892  1.000 25.58707  ? 206 TYR A CD1 1 
ATOM   1407 C  CD2 . TYR A  1 180 ? 9.41983   4.95537   24.41075  1.000 28.01921  ? 206 TYR A CD2 1 
ATOM   1408 C  CE1 . TYR A  1 180 ? 9.36896   3.04995   26.40507  1.000 25.01793  ? 206 TYR A CE1 1 
ATOM   1409 C  CE2 . TYR A  1 180 ? 8.34608   4.09133   24.50930  1.000 29.40114  ? 206 TYR A CE2 1 
ATOM   1410 C  CZ  . TYR A  1 180 ? 8.32554   3.14058   25.50728  1.000 25.95095  ? 206 TYR A CZ  1 
ATOM   1411 O  OH  . TYR A  1 180 ? 7.25759   2.27884   25.60724  1.000 25.49744  ? 206 TYR A OH  1 
ATOM   1412 N  N   . THR A  1 181 ? 13.02874  8.59317   24.74322  1.000 33.74684  ? 207 THR A N   1 
ATOM   1413 C  CA  . THR A  1 181 ? 14.23337  9.41083   24.64896  1.000 34.52694  ? 207 THR A CA  1 
ATOM   1414 C  C   . THR A  1 181 ? 14.08719  10.74737  25.36412  1.000 33.36859  ? 207 THR A C   1 
ATOM   1415 O  O   . THR A  1 181 ? 15.09912  11.34498  25.74570  1.000 33.54515  ? 207 THR A O   1 
ATOM   1416 C  CB  . THR A  1 181 ? 14.60505  9.65562   23.18439  1.000 38.81137  ? 207 THR A CB  1 
ATOM   1417 O  OG1 . THR A  1 181 ? 13.47981  10.20301  22.48539  1.000 41.06376  ? 207 THR A OG1 1 
ATOM   1418 C  CG2 . THR A  1 181 ? 15.03300  8.35826   22.51693  1.000 38.40161  ? 207 THR A CG2 1 
ATOM   1419 N  N   . GLY A  1 182 ? 12.86149  11.22449  25.56003  1.000 32.50935  ? 208 GLY A N   1 
ATOM   1420 C  CA  . GLY A  1 182 ? 12.63772  12.52115  26.15085  1.000 33.57249  ? 208 GLY A CA  1 
ATOM   1421 C  C   . GLY A  1 182 ? 12.45901  12.48103  27.65537  1.000 32.03704  ? 208 GLY A C   1 
ATOM   1422 O  O   . GLY A  1 182 ? 13.41766  12.31295  28.41568  1.000 32.33183  ? 208 GLY A O   1 
ATOM   1423 N  N   . PRO A  1 183 ? 11.21108  12.62913  28.11202  1.000 31.19716  ? 209 PRO A N   1 
ATOM   1424 C  CA  . PRO A  1 183 ? 10.97773  12.82758  29.55522  1.000 29.79088  ? 209 PRO A CA  1 
ATOM   1425 C  C   . PRO A  1 183 ? 11.38951  11.64960  30.42420  1.000 29.27399  ? 209 PRO A C   1 
ATOM   1426 O  O   . PRO A  1 183 ? 11.90615  11.85949  31.52999  1.000 29.37943  ? 209 PRO A O   1 
ATOM   1427 C  CB  . PRO A  1 183 ? 9.46522   13.08738  29.62874  1.000 30.06605  ? 209 PRO A CB  1 
ATOM   1428 C  CG  . PRO A  1 183 ? 8.90749   12.51405  28.36471  1.000 31.64802  ? 209 PRO A CG  1 
ATOM   1429 C  CD  . PRO A  1 183 ? 9.96716   12.69853  27.32773  1.000 32.43767  ? 209 PRO A CD  1 
ATOM   1430 N  N   . ALA A  1 184 ? 11.16566  10.41481  29.96877  1.000 28.79753  ? 210 ALA A N   1 
ATOM   1431 C  CA  . ALA A  1 184 ? 11.56272  9.25607   30.76391  1.000 24.43878  ? 210 ALA A CA  1 
ATOM   1432 C  C   . ALA A  1 184 ? 13.07378  9.22086   30.95607  1.000 24.51889  ? 210 ALA A C   1 
ATOM   1433 O  O   . ALA A  1 184 ? 13.56798  9.01921   32.07316  1.000 23.69203  ? 210 ALA A O   1 
ATOM   1434 C  CB  . ALA A  1 184 ? 11.06880  7.96917   30.10250  1.000 24.18353  ? 210 ALA A CB  1 
ATOM   1435 N  N   . THR A  1 185 ? 13.82403  9.42221   29.86971  1.000 26.82478  ? 211 THR A N   1 
ATOM   1436 C  CA  . THR A  1 185 ? 15.27751  9.49578   29.96960  1.000 29.39757  ? 211 THR A CA  1 
ATOM   1437 C  C   . THR A  1 185 ? 15.70793  10.67433  30.83438  1.000 30.56278  ? 211 THR A C   1 
ATOM   1438 O  O   . THR A  1 185 ? 16.66429  10.56617  31.61000  1.000 31.98888  ? 211 THR A O   1 
ATOM   1439 C  CB  . THR A  1 185 ? 15.89204  9.59478   28.57087  1.000 32.69102  ? 211 THR A CB  1 
ATOM   1440 O  OG1 . THR A  1 185 ? 15.76985  8.33221   27.90416  1.000 31.87607  ? 211 THR A OG1 1 
ATOM   1441 C  CG2 . THR A  1 185 ? 17.36461  9.97952   28.64455  1.000 34.05641  ? 211 THR A CG2 1 
ATOM   1442 N  N   . ASP A  1 186 ? 15.00356  11.80450  30.72497  1.000 30.26506  ? 212 ASP A N   1 
ATOM   1443 C  CA  . ASP A  1 186 ? 15.32585  12.96852  31.54654  1.000 29.93712  ? 212 ASP A CA  1 
ATOM   1444 C  C   . ASP A  1 186 ? 15.22204  12.63800  33.03106  1.000 28.75719  ? 212 ASP A C   1 
ATOM   1445 O  O   . ASP A  1 186 ? 16.15225  12.89648  33.80564  1.000 28.76816  ? 212 ASP A O   1 
ATOM   1446 C  CB  . ASP A  1 186 ? 14.40026  14.13437  31.19185  1.000 31.20045  ? 212 ASP A CB  1 
ATOM   1447 C  CG  . ASP A  1 186 ? 14.67998  14.70771  29.81538  1.000 35.10860  ? 212 ASP A CG  1 
ATOM   1448 O  OD1 . ASP A  1 186 ? 15.82227  14.56747  29.33033  1.000 36.22573  ? 212 ASP A OD1 1 
ATOM   1449 O  OD2 . ASP A  1 186 ? 13.75546  15.29929  29.21762  1.000 35.23960  ? 212 ASP A OD2 1 
ATOM   1450 N  N   . LEU A  1 187 ? 14.09373  12.05514  33.44481  1.000 27.55117  ? 213 LEU A N   1 
ATOM   1451 C  CA  . LEU A  1 187 ? 13.91056  11.72553  34.85489  1.000 26.82206  ? 213 LEU A CA  1 
ATOM   1452 C  C   . LEU A  1 187 ? 14.89194  10.65095  35.30758  1.000 28.23327  ? 213 LEU A C   1 
ATOM   1453 O  O   . LEU A  1 187 ? 15.42407  10.71928  36.42339  1.000 30.04384  ? 213 LEU A O   1 
ATOM   1454 C  CB  . LEU A  1 187 ? 12.47281  11.27681  35.11323  1.000 24.84569  ? 213 LEU A CB  1 
ATOM   1455 C  CG  . LEU A  1 187 ? 12.18915  10.86699  36.56090  1.000 21.94991  ? 213 LEU A CG  1 
ATOM   1456 C  CD1 . LEU A  1 187 ? 12.44427  12.03539  37.50578  1.000 22.31025  ? 213 LEU A CD1 1 
ATOM   1457 C  CD2 . LEU A  1 187 ? 10.77085  10.33989  36.71769  1.000 21.40890  ? 213 LEU A CD2 1 
ATOM   1458 N  N   . LEU A  1 188 ? 15.14838  9.65024   34.46031  1.000 26.12956  ? 214 LEU A N   1 
ATOM   1459 C  CA  . LEU A  1 188 ? 16.07830  8.59530   34.84784  1.000 25.02197  ? 214 LEU A CA  1 
ATOM   1460 C  C   . LEU A  1 188 ? 17.48834  9.14336   35.03005  1.000 27.30121  ? 214 LEU A C   1 
ATOM   1461 O  O   . LEU A  1 188 ? 18.19570  8.75419   35.96530  1.000 26.94112  ? 214 LEU A O   1 
ATOM   1462 C  CB  . LEU A  1 188 ? 16.05951  7.46958   33.81491  1.000 23.37920  ? 214 LEU A CB  1 
ATOM   1463 C  CG  . LEU A  1 188 ? 14.87892  6.50247   33.93487  1.000 23.15918  ? 214 LEU A CG  1 
ATOM   1464 C  CD1 . LEU A  1 188 ? 14.81259  5.57183   32.73268  1.000 23.26901  ? 214 LEU A CD1 1 
ATOM   1465 C  CD2 . LEU A  1 188 ? 14.96357  5.70841   35.23081  1.000 21.63676  ? 214 LEU A CD2 1 
ATOM   1466 N  N   . LEU A  1 189 ? 17.91008  10.06375  34.15967  1.000 27.35403  ? 215 LEU A N   1 
ATOM   1467 C  CA  . LEU A  1 189 ? 19.22969  10.66453  34.31338  1.000 29.68126  ? 215 LEU A CA  1 
ATOM   1468 C  C   . LEU A  1 189 ? 19.27854  11.60727  35.50795  1.000 30.99969  ? 215 LEU A C   1 
ATOM   1469 O  O   . LEU A  1 189 ? 20.33309  11.75315  36.13665  1.000 33.67990  ? 215 LEU A O   1 
ATOM   1470 C  CB  . LEU A  1 189 ? 19.62653  11.39793  33.03271  1.000 32.03408  ? 215 LEU A CB  1 
ATOM   1471 C  CG  . LEU A  1 189 ? 20.10252  10.49655  31.89088  1.000 34.56946  ? 215 LEU A CG  1 
ATOM   1472 C  CD1 . LEU A  1 189 ? 20.33242  11.30196  30.62074  1.000 36.99622  ? 215 LEU A CD1 1 
ATOM   1473 C  CD2 . LEU A  1 189 ? 21.36314  9.74394   32.29113  1.000 33.94485  ? 215 LEU A CD2 1 
ATOM   1474 N  N   . LYS A  1 190 ? 18.15700  12.25447  35.83514  1.000 30.34124  ? 216 LYS A N   1 
ATOM   1475 C  CA  . LYS A  1 190 ? 18.10719  13.06154  37.04932  1.000 32.56507  ? 216 LYS A CA  1 
ATOM   1476 C  C   . LYS A  1 190 ? 18.23053  12.19738  38.29849  1.000 31.01331  ? 216 LYS A C   1 
ATOM   1477 O  O   . LYS A  1 190 ? 18.82575  12.62735  39.29316  1.000 30.62609  ? 216 LYS A O   1 
ATOM   1478 C  CB  . LYS A  1 190 ? 16.81119  13.87227  37.08750  1.000 35.65322  ? 216 LYS A CB  1 
ATOM   1479 C  CG  . LYS A  1 190 ? 16.80069  14.98737  38.12032  1.000 38.46285  ? 216 LYS A CG  1 
ATOM   1480 C  CD  . LYS A  1 190 ? 15.69606  15.99300  37.83275  1.000 39.56602  ? 216 LYS A CD  1 
ATOM   1481 C  CE  . LYS A  1 190 ? 15.84689  16.59732  36.44568  1.000 40.49124  ? 216 LYS A CE  1 
ATOM   1482 N  NZ  . LYS A  1 190 ? 14.76010  17.56887  36.13984  1.000 40.78486  ? 216 LYS A NZ  1 
ATOM   1483 N  N   . LEU A  1 191 ? 17.67678  10.98331  38.26502  1.000 29.72696  ? 217 LEU A N   1 
ATOM   1484 C  CA  . LEU A  1 191 ? 17.75615  10.07807  39.40700  1.000 28.25869  ? 217 LEU A CA  1 
ATOM   1485 C  C   . LEU A  1 191 ? 19.07420  9.31491   39.47454  1.000 30.14978  ? 217 LEU A C   1 
ATOM   1486 O  O   . LEU A  1 191 ? 19.45566  8.86629   40.56121  1.000 29.68191  ? 217 LEU A O   1 
ATOM   1487 C  CB  . LEU A  1 191 ? 16.60257  9.07274   39.36657  1.000 25.13931  ? 217 LEU A CB  1 
ATOM   1488 C  CG  . LEU A  1 191 ? 15.17394  9.60739   39.46970  1.000 23.59948  ? 217 LEU A CG  1 
ATOM   1489 C  CD1 . LEU A  1 191 ? 14.17406  8.49304   39.20261  1.000 20.07945  ? 217 LEU A CD1 1 
ATOM   1490 C  CD2 . LEU A  1 191 ? 14.92885  10.23512  40.83102  1.000 22.16203  ? 217 LEU A CD2 1 
ATOM   1491 N  N   . ARG A  1 192 ? 19.76489  9.15993   38.34343  1.000 31.92731  ? 218 ARG A N   1 
ATOM   1492 C  CA  . ARG A  1 192 ? 20.95407  8.31031   38.25743  1.000 32.00275  ? 218 ARG A CA  1 
ATOM   1493 C  C   . ARG A  1 192 ? 22.01763  8.57795   39.31894  1.000 32.62501  ? 218 ARG A C   1 
ATOM   1494 O  O   . ARG A  1 192 ? 22.53099  7.60378   39.89251  1.000 32.62855  ? 218 ARG A O   1 
ATOM   1495 C  CB  . ARG A  1 192 ? 21.55052  8.43832   36.84815  1.000 34.88437  ? 218 ARG A CB  1 
ATOM   1496 C  CG  . ARG A  1 192 ? 22.85125  7.67897   36.65159  1.000 37.04810  ? 218 ARG A CG  1 
ATOM   1497 C  CD  . ARG A  1 192 ? 22.64062  6.18451   36.81948  1.000 39.74050  ? 218 ARG A CD  1 
ATOM   1498 N  NE  . ARG A  1 192 ? 23.89219  5.43739   36.73724  1.000 43.32067  ? 218 ARG A NE  1 
ATOM   1499 C  CZ  . ARG A  1 192 ? 24.59008  5.03058   37.79274  1.000 45.05597  ? 218 ARG A CZ  1 
ATOM   1500 N  NH1 . ARG A  1 192 ? 24.16146  5.30071   39.01835  1.000 44.73220  ? 218 ARG A NH1 1 
ATOM   1501 N  NH2 . ARG A  1 192 ? 25.71764  4.35373   37.62355  1.000 46.19327  ? 218 ARG A NH2 1 
ATOM   1502 N  N   . PRO A  1 193 ? 22.40883  9.82341   39.62240  1.000 33.62271  ? 219 PRO A N   1 
ATOM   1503 C  CA  . PRO A  1 193 ? 23.49167  10.02664  40.60366  1.000 32.48264  ? 219 PRO A CA  1 
ATOM   1504 C  C   . PRO A  1 193 ? 23.20382  9.45915   41.98754  1.000 30.02134  ? 219 PRO A C   1 
ATOM   1505 O  O   . PRO A  1 193 ? 24.13761  9.35112   42.79260  1.000 28.31583  ? 219 PRO A O   1 
ATOM   1506 C  CB  . PRO A  1 193 ? 23.63957  11.55322  40.65427  1.000 34.49097  ? 219 PRO A CB  1 
ATOM   1507 C  CG  . PRO A  1 193 ? 23.14172  12.01629  39.33774  1.000 35.59380  ? 219 PRO A CG  1 
ATOM   1508 C  CD  . PRO A  1 193 ? 21.99966  11.10252  39.01148  1.000 34.55209  ? 219 PRO A CD  1 
ATOM   1509 N  N   . ASN A  1 194 ? 21.95932  9.09054   42.28912  1.000 29.96760  ? 220 ASN A N   1 
ATOM   1510 C  CA  . ASN A  1 194 ? 21.60660  8.54391   43.59187  1.000 28.68324  ? 220 ASN A CA  1 
ATOM   1511 C  C   . ASN A  1 194 ? 21.45157  7.02855   43.58864  1.000 27.25363  ? 220 ASN A C   1 
ATOM   1512 O  O   . ASN A  1 194 ? 21.25318  6.44172   44.65764  1.000 26.97626  ? 220 ASN A O   1 
ATOM   1513 C  CB  . ASN A  1 194 ? 20.30839  9.18533   44.09762  1.000 29.19740  ? 220 ASN A CB  1 
ATOM   1514 C  CG  . ASN A  1 194 ? 20.43751  10.68263  44.29202  1.000 32.46906  ? 220 ASN A CG  1 
ATOM   1515 O  OD1 . ASN A  1 194 ? 21.28690  11.15062  45.04997  1.000 35.44814  ? 220 ASN A OD1 1 
ATOM   1516 N  ND2 . ASN A  1 194 ? 19.59657  11.44369  43.60170  1.000 33.32465  ? 220 ASN A ND2 1 
ATOM   1517 N  N   . ILE A  1 195 ? 21.53815  6.38613   42.42869  1.000 26.42876  ? 221 ILE A N   1 
ATOM   1518 C  CA  . ILE A  1 195 ? 21.37438  4.94111   42.31972  1.000 24.97264  ? 221 ILE A CA  1 
ATOM   1519 C  C   . ILE A  1 195 ? 22.74392  4.28222   42.40626  1.000 26.36193  ? 221 ILE A C   1 
ATOM   1520 O  O   . ILE A  1 195 ? 23.67142  4.65657   41.67796  1.000 25.76366  ? 221 ILE A O   1 
ATOM   1521 C  CB  . ILE A  1 195 ? 20.66340  4.56826   41.00871  1.000 25.71357  ? 221 ILE A CB  1 
ATOM   1522 C  CG1 . ILE A  1 195 ? 19.35202  5.34627   40.87775  1.000 24.89341  ? 221 ILE A CG1 1 
ATOM   1523 C  CG2 . ILE A  1 195 ? 20.41065  3.06909   40.94604  1.000 27.09530  ? 221 ILE A CG2 1 
ATOM   1524 C  CD1 . ILE A  1 195 ? 18.70652  5.23458   39.51496  1.000 23.93841  ? 221 ILE A CD1 1 
ATOM   1525 N  N   . ARG A  1 196 ? 22.87274  3.29355   43.29402  1.000 25.43019  ? 222 ARG A N   1 
ATOM   1526 C  CA  . ARG A  1 196 ? 24.16368  2.64169   43.48630  1.000 27.55030  ? 222 ARG A CA  1 
ATOM   1527 C  C   . ARG A  1 196 ? 24.48902  1.69142   42.33864  1.000 28.12556  ? 222 ARG A C   1 
ATOM   1528 O  O   . ARG A  1 196 ? 25.61082  1.69863   41.82006  1.000 30.75503  ? 222 ARG A O   1 
ATOM   1529 C  CB  . ARG A  1 196 ? 24.19167  1.89651   44.82257  1.000 28.50104  ? 222 ARG A CB  1 
ATOM   1530 C  CG  . ARG A  1 196 ? 25.53430  1.24222   45.11928  1.000 29.51137  ? 222 ARG A CG  1 
ATOM   1531 C  CD  . ARG A  1 196 ? 25.52616  0.51204   46.45059  1.000 29.27401  ? 222 ARG A CD  1 
ATOM   1532 N  NE  . ARG A  1 196 ? 25.38420  1.42909   47.57691  1.000 29.80237  ? 222 ARG A NE  1 
ATOM   1533 C  CZ  . ARG A  1 196 ? 25.11442  1.04548   48.81989  1.000 29.08971  ? 222 ARG A CZ  1 
ATOM   1534 N  NH1 . ARG A  1 196 ? 24.95934  -0.24216  49.09873  1.000 27.43816  ? 222 ARG A NH1 1 
ATOM   1535 N  NH2 . ARG A  1 196 ? 25.00154  1.94801   49.78460  1.000 28.26094  ? 222 ARG A NH2 1 
ATOM   1536 N  N   . TYR A  1 197 ? 23.52979  0.86224   41.93126  1.000 26.20515  ? 223 TYR A N   1 
ATOM   1537 C  CA  . TYR A  1 197 ? 23.77746  -0.06601  40.83662  1.000 26.96012  ? 223 TYR A CA  1 
ATOM   1538 C  C   . TYR A  1 197 ? 22.46073  -0.45726  40.18302  1.000 28.25954  ? 223 TYR A C   1 
ATOM   1539 O  O   . TYR A  1 197 ? 21.37898  -0.25191  40.74024  1.000 29.06752  ? 223 TYR A O   1 
ATOM   1540 C  CB  . TYR A  1 197 ? 24.53845  -1.31295  41.31177  1.000 27.85322  ? 223 TYR A CB  1 
ATOM   1541 C  CG  . TYR A  1 197 ? 23.85145  -2.11999  42.39693  1.000 26.47987  ? 223 TYR A CG  1 
ATOM   1542 C  CD1 . TYR A  1 197 ? 22.85326  -3.03715  42.08644  1.000 25.04062  ? 223 TYR A CD1 1 
ATOM   1543 C  CD2 . TYR A  1 197 ? 24.21847  -1.98085  43.72934  1.000 26.87516  ? 223 TYR A CD2 1 
ATOM   1544 C  CE1 . TYR A  1 197 ? 22.23079  -3.78007  43.07272  1.000 24.75704  ? 223 TYR A CE1 1 
ATOM   1545 C  CE2 . TYR A  1 197 ? 23.60189  -2.72160  44.72297  1.000 25.83097  ? 223 TYR A CE2 1 
ATOM   1546 C  CZ  . TYR A  1 197 ? 22.60922  -3.61887  44.38818  1.000 25.62703  ? 223 TYR A CZ  1 
ATOM   1547 O  OH  . TYR A  1 197 ? 21.99240  -4.35806  45.37146  1.000 26.11744  ? 223 TYR A OH  1 
ATOM   1548 N  N   . PHE A  1 198 ? 22.57740  -1.02426  38.98337  1.000 27.71710  ? 224 PHE A N   1 
ATOM   1549 C  CA  . PHE A  1 198 ? 21.45160  -1.56103  38.22645  1.000 27.57245  ? 224 PHE A CA  1 
ATOM   1550 C  C   . PHE A  1 198 ? 21.64371  -3.06955  38.11981  1.000 28.82811  ? 224 PHE A C   1 
ATOM   1551 O  O   . PHE A  1 198 ? 22.50669  -3.53838  37.36971  1.000 29.67995  ? 224 PHE A O   1 
ATOM   1552 C  CB  . PHE A  1 198 ? 21.36067  -0.92220  36.84112  1.000 26.44895  ? 224 PHE A CB  1 
ATOM   1553 C  CG  . PHE A  1 198 ? 20.95088  0.52464   36.85880  1.000 25.33451  ? 224 PHE A CG  1 
ATOM   1554 C  CD1 . PHE A  1 198 ? 19.64732  0.89320   36.56862  1.000 24.84146  ? 224 PHE A CD1 1 
ATOM   1555 C  CD2 . PHE A  1 198 ? 21.87140  1.51628   37.15172  1.000 26.17877  ? 224 PHE A CD2 1 
ATOM   1556 C  CE1 . PHE A  1 198 ? 19.26794  2.22323   36.57862  1.000 23.59195  ? 224 PHE A CE1 1 
ATOM   1557 C  CE2 . PHE A  1 198 ? 21.49886  2.84673   37.16379  1.000 25.83952  ? 224 PHE A CE2 1 
ATOM   1558 C  CZ  . PHE A  1 198 ? 20.19583  3.20093   36.87661  1.000 25.86419  ? 224 PHE A CZ  1 
ATOM   1559 N  N   . HIS A  1 199 ? 20.84620  -3.82551  38.87163  1.000 27.69636  ? 225 HIS A N   1 
ATOM   1560 C  CA  . HIS A  1 199 ? 20.94513  -5.27728  38.87438  1.000 27.39203  ? 225 HIS A CA  1 
ATOM   1561 C  C   . HIS A  1 199 ? 19.59844  -5.86256  39.27290  1.000 26.26381  ? 225 HIS A C   1 
ATOM   1562 O  O   . HIS A  1 199 ? 18.86230  -5.27589  40.07067  1.000 28.06765  ? 225 HIS A O   1 
ATOM   1563 C  CB  . HIS A  1 199 ? 22.04692  -5.76356  39.82421  1.000 29.05398  ? 225 HIS A CB  1 
ATOM   1564 C  CG  . HIS A  1 199 ? 22.62422  -7.09356  39.45131  1.000 30.31968  ? 225 HIS A CG  1 
ATOM   1565 N  ND1 . HIS A  1 199 ? 22.04407  -8.28775  39.82149  1.000 30.05042  ? 225 HIS A ND1 1 
ATOM   1566 C  CD2 . HIS A  1 199 ? 23.73185  -7.41739  38.74275  1.000 31.50204  ? 225 HIS A CD2 1 
ATOM   1567 C  CE1 . HIS A  1 199 ? 22.76871  -9.28980  39.35629  1.000 30.80854  ? 225 HIS A CE1 1 
ATOM   1568 N  NE2 . HIS A  1 199 ? 23.79847  -8.78885  38.69813  1.000 32.07987  ? 225 HIS A NE2 1 
ATOM   1569 N  N   . SER A  1 200 ? 19.28503  -7.03099  38.71166  1.000 25.64775  ? 226 SER A N   1 
ATOM   1570 C  CA  . SER A  1 200 ? 17.98958  -7.66942  38.90731  1.000 26.83909  ? 226 SER A CA  1 
ATOM   1571 C  C   . SER A  1 200 ? 18.06276  -8.89725  39.81134  1.000 24.17472  ? 226 SER A C   1 
ATOM   1572 O  O   . SER A  1 200 ? 17.13622  -9.71393  39.80978  1.000 24.47842  ? 226 SER A O   1 
ATOM   1573 C  CB  . SER A  1 200 ? 17.37890  -8.04805  37.55702  1.000 29.91726  ? 226 SER A CB  1 
ATOM   1574 O  OG  . SER A  1 200 ? 17.44877  -6.97097  36.63927  1.000 30.98133  ? 226 SER A OG  1 
ATOM   1575 N  N   . SER A  1 201 ? 19.13651  -9.04745  40.58885  1.000 24.06090  ? 227 SER A N   1 
ATOM   1576 C  CA  . SER A  1 201 ? 19.24375  -10.20118 41.47687  1.000 24.60406  ? 227 SER A CA  1 
ATOM   1577 C  C   . SER A  1 201 ? 20.03343  -9.88736  42.74462  1.000 26.04994  ? 227 SER A C   1 
ATOM   1578 O  O   . SER A  1 201 ? 19.74620  -10.44384 43.80951  1.000 27.00783  ? 227 SER A O   1 
ATOM   1579 C  CB  . SER A  1 201 ? 19.88001  -11.38240 40.73850  1.000 23.45703  ? 227 SER A CB  1 
ATOM   1580 O  OG  . SER A  1 201 ? 21.28169  -11.41588 40.93494  1.000 25.99128  ? 227 SER A OG  1 
ATOM   1581 N  N   . GLN A  1 202 ? 21.02870  -9.00135  42.64426  1.000 26.41314  ? 228 GLN A N   1 
ATOM   1582 C  CA  . GLN A  1 202 ? 21.85356  -8.67400  43.80542  1.000 27.89464  ? 228 GLN A CA  1 
ATOM   1583 C  C   . GLN A  1 202 ? 21.04156  -7.99052  44.89987  1.000 26.11831  ? 228 GLN A C   1 
ATOM   1584 O  O   . GLN A  1 202 ? 21.36634  -8.11159  46.09298  1.000 27.12386  ? 228 GLN A O   1 
ATOM   1585 C  CB  . GLN A  1 202 ? 23.02215  -7.78649  43.37283  1.000 31.57231  ? 228 GLN A CB  1 
ATOM   1586 C  CG  . GLN A  1 202 ? 24.11736  -7.62322  44.41441  1.000 36.86113  ? 228 GLN A CG  1 
ATOM   1587 C  CD  . GLN A  1 202 ? 25.25617  -6.74596  43.92643  1.000 41.15039  ? 228 GLN A CD  1 
ATOM   1588 O  OE1 . GLN A  1 202 ? 25.52492  -6.66650  42.72715  1.000 41.48200  ? 228 GLN A OE1 1 
ATOM   1589 N  NE2 . GLN A  1 202 ? 25.93015  -6.07945  44.85653  1.000 43.26456  ? 228 GLN A NE2 1 
ATOM   1590 N  N   . TYR A  1 203 ? 19.97776  -7.28004  44.51729  1.000 23.94045  ? 229 TYR A N   1 
ATOM   1591 C  CA  . TYR A  1 203 ? 19.18961  -6.54346  45.49443  1.000 24.39737  ? 229 TYR A CA  1 
ATOM   1592 C  C   . TYR A  1 203 ? 18.48900  -7.45890  46.48729  1.000 21.14323  ? 229 TYR A C   1 
ATOM   1593 O  O   . TYR A  1 203 ? 18.17120  -7.00991  47.58724  1.000 22.93447  ? 229 TYR A O   1 
ATOM   1594 C  CB  . TYR A  1 203 ? 18.17134  -5.64357  44.79069  1.000 23.33200  ? 229 TYR A CB  1 
ATOM   1595 C  CG  . TYR A  1 203 ? 17.01063  -6.36814  44.14716  1.000 21.30964  ? 229 TYR A CG  1 
ATOM   1596 C  CD1 . TYR A  1 203 ? 15.77747  -6.44828  44.78282  1.000 19.23981  ? 229 TYR A CD1 1 
ATOM   1597 C  CD2 . TYR A  1 203 ? 17.14127  -6.95302  42.89492  1.000 20.67400  ? 229 TYR A CD2 1 
ATOM   1598 C  CE1 . TYR A  1 203 ? 14.71064  -7.10221  44.19357  1.000 20.79003  ? 229 TYR A CE1 1 
ATOM   1599 C  CE2 . TYR A  1 203 ? 16.08137  -7.60820  42.29818  1.000 19.58582  ? 229 TYR A CE2 1 
ATOM   1600 C  CZ  . TYR A  1 203 ? 14.86896  -7.67940  42.95033  1.000 19.17563  ? 229 TYR A CZ  1 
ATOM   1601 O  OH  . TYR A  1 203 ? 13.81369  -8.32918  42.35378  1.000 17.35144  ? 229 TYR A OH  1 
ATOM   1602 N  N   . ILE A  1 204 ? 18.28161  -8.73327  46.14981  1.000 19.55286  ? 230 ILE A N   1 
ATOM   1603 C  CA  . ILE A  1 204 ? 17.68039  -9.66797  47.10204  1.000 21.81689  ? 230 ILE A CA  1 
ATOM   1604 C  C   . ILE A  1 204 ? 18.55200  -9.78759  48.34823  1.000 23.27600  ? 230 ILE A C   1 
ATOM   1605 O  O   . ILE A  1 204 ? 18.13310  -9.45073  49.46447  1.000 23.38837  ? 230 ILE A O   1 
ATOM   1606 C  CB  . ILE A  1 204 ? 17.45739  -11.04100 46.44423  1.000 21.51362  ? 230 ILE A CB  1 
ATOM   1607 C  CG1 . ILE A  1 204 ? 16.65646  -10.89378 45.14991  1.000 19.91655  ? 230 ILE A CG1 1 
ATOM   1608 C  CG2 . ILE A  1 204 ? 16.75342  -11.98512 47.40854  1.000 20.06097  ? 230 ILE A CG2 1 
ATOM   1609 C  CD1 . ILE A  1 204 ? 16.54542  -12.17778 44.35685  1.000 19.81818  ? 230 ILE A CD1 1 
ATOM   1610 N  N   . ASN A  1 205 ? 19.78393  -10.27132 48.17165  1.000 24.63817  ? 231 ASN A N   1 
ATOM   1611 C  CA  . ASN A  1 205 ? 20.68348  -10.41918 49.30926  1.000 25.87474  ? 231 ASN A CA  1 
ATOM   1612 C  C   . ASN A  1 205 ? 21.05689  -9.07143  49.90916  1.000 27.45882  ? 231 ASN A C   1 
ATOM   1613 O  O   . ASN A  1 205 ? 21.25780  -8.97419  51.12628  1.000 28.11258  ? 231 ASN A O   1 
ATOM   1614 C  CB  . ASN A  1 205 ? 21.94202  -11.18253 48.89778  1.000 24.85637  ? 231 ASN A CB  1 
ATOM   1615 C  CG  . ASN A  1 205 ? 22.62067  -11.86049 50.07352  1.000 29.29544  ? 231 ASN A CG  1 
ATOM   1616 O  OD1 . ASN A  1 205 ? 21.96905  -12.51524 50.88819  1.000 28.17650  ? 231 ASN A OD1 1 
ATOM   1617 N  ND2 . ASN A  1 205 ? 23.93616  -11.70296 50.16978  1.000 31.12524  ? 231 ASN A ND2 1 
ATOM   1618 N  N   . ASP A  1 206 ? 21.14662  -8.02103  49.08616  1.000 27.03290  ? 232 ASP A N   1 
ATOM   1619 C  CA  . ASP A  1 206 ? 21.48777  -6.71489  49.64138  1.000 25.99688  ? 232 ASP A CA  1 
ATOM   1620 C  C   . ASP A  1 206 ? 20.37171  -6.16250  50.52487  1.000 26.66149  ? 232 ASP A C   1 
ATOM   1621 O  O   . ASP A  1 206 ? 20.65234  -5.47971  51.51644  1.000 27.17546  ? 232 ASP A O   1 
ATOM   1622 C  CB  . ASP A  1 206 ? 21.82980  -5.74189  48.51675  1.000 27.12697  ? 232 ASP A CB  1 
ATOM   1623 C  CG  . ASP A  1 206 ? 23.25885  -5.89745  48.03305  1.000 28.93978  ? 232 ASP A CG  1 
ATOM   1624 O  OD1 . ASP A  1 206 ? 23.97298  -6.77406  48.56502  1.000 29.78216  ? 232 ASP A OD1 1 
ATOM   1625 O  OD2 . ASP A  1 206 ? 23.67013  -5.14362  47.12656  1.000 29.71869  ? 232 ASP A OD2 1 
ATOM   1626 N  N   . LEU A  1 207 ? 19.10958  -6.44877  50.19326  1.000 25.51822  ? 233 LEU A N   1 
ATOM   1627 C  CA  . LEU A  1 207 ? 18.00512  -6.09361  51.07613  1.000 24.96962  ? 233 LEU A CA  1 
ATOM   1628 C  C   . LEU A  1 207 ? 18.00775  -6.96317  52.32336  1.000 24.61593  ? 233 LEU A C   1 
ATOM   1629 O  O   . LEU A  1 207 ? 17.74845  -6.47475  53.42962  1.000 26.54680  ? 233 LEU A O   1 
ATOM   1630 C  CB  . LEU A  1 207 ? 16.67324  -6.24051  50.33811  1.000 21.85628  ? 233 LEU A CB  1 
ATOM   1631 C  CG  . LEU A  1 207 ? 16.19379  -5.11871  49.41658  1.000 21.07419  ? 233 LEU A CG  1 
ATOM   1632 C  CD1 . LEU A  1 207 ? 15.01377  -5.59724  48.58105  1.000 19.56298  ? 233 LEU A CD1 1 
ATOM   1633 C  CD2 . LEU A  1 207 ? 15.81591  -3.88675  50.21980  1.000 19.85131  ? 233 LEU A CD2 1 
ATOM   1634 N  N   . ALA A  1 208 ? 18.29437  -8.25782  52.16023  1.000 23.09130  ? 234 ALA A N   1 
ATOM   1635 C  CA  . ALA A  1 208 ? 18.29589  -9.16358  53.30455  1.000 22.68643  ? 234 ALA A CA  1 
ATOM   1636 C  C   . ALA A  1 208 ? 19.36011  -8.77317  54.32375  1.000 24.22725  ? 234 ALA A C   1 
ATOM   1637 O  O   . ALA A  1 208 ? 19.15234  -8.91772  55.53434  1.000 25.05370  ? 234 ALA A O   1 
ATOM   1638 C  CB  . ALA A  1 208 ? 18.50529  -10.60276 52.83474  1.000 19.97324  ? 234 ALA A CB  1 
ATOM   1639 N  N   . ASN A  1 209 ? 20.50356  -8.27177  53.85701  1.000 24.45430  ? 235 ASN A N   1 
ATOM   1640 C  CA  . ASN A  1 209 ? 21.60565  -7.92964  54.74695  1.000 26.99236  ? 235 ASN A CA  1 
ATOM   1641 C  C   . ASN A  1 209 ? 21.58989  -6.47638  55.20483  1.000 26.65112  ? 235 ASN A C   1 
ATOM   1642 O  O   . ASN A  1 209 ? 22.40069  -6.10675  56.06108  1.000 27.01459  ? 235 ASN A O   1 
ATOM   1643 C  CB  . ASN A  1 209 ? 22.94486  -8.23124  54.06646  1.000 29.67623  ? 235 ASN A CB  1 
ATOM   1644 C  CG  . ASN A  1 209 ? 23.23004  -9.71647  53.98002  1.000 32.67170  ? 235 ASN A CG  1 
ATOM   1645 O  OD1 . ASN A  1 209 ? 22.84724  -10.48514 54.86215  1.000 32.82118  ? 235 ASN A OD1 1 
ATOM   1646 N  ND2 . ASN A  1 209 ? 23.90567  -10.12917 52.91368  1.000 33.75033  ? 235 ASN A ND2 1 
ATOM   1647 N  N   . GLY A  1 210 ? 20.69854  -5.64847  54.66574  1.000 26.06687  ? 236 GLY A N   1 
ATOM   1648 C  CA  . GLY A  1 210 ? 20.63536  -4.25152  55.03579  1.000 26.59813  ? 236 GLY A CA  1 
ATOM   1649 C  C   . GLY A  1 210 ? 21.57285  -3.34038  54.27524  1.000 28.16280  ? 236 GLY A C   1 
ATOM   1650 O  O   . GLY A  1 210 ? 21.64211  -2.14630  54.59431  1.000 27.62844  ? 236 GLY A O   1 
ATOM   1651 N  N   . ASP A  1 211 ? 22.29707  -3.85977  53.28237  1.000 29.45731  ? 237 ASP A N   1 
ATOM   1652 C  CA  . ASP A  1 211 ? 23.20709  -3.03544  52.49792  1.000 31.61954  ? 237 ASP A CA  1 
ATOM   1653 C  C   . ASP A  1 211 ? 22.47705  -2.14289  51.50301  1.000 30.50370  ? 237 ASP A C   1 
ATOM   1654 O  O   . ASP A  1 211 ? 23.03270  -1.12244  51.08226  1.000 31.32564  ? 237 ASP A O   1 
ATOM   1655 C  CB  . ASP A  1 211 ? 24.21480  -3.92419  51.76548  1.000 31.44037  ? 237 ASP A CB  1 
ATOM   1656 C  CG  . ASP A  1 211 ? 25.05380  -4.75733  52.71717  1.000 35.40295  ? 237 ASP A CG  1 
ATOM   1657 O  OD1 . ASP A  1 211 ? 25.56021  -4.19699  53.71225  1.000 37.11109  ? 237 ASP A OD1 1 
ATOM   1658 O  OD2 . ASP A  1 211 ? 25.20312  -5.97309  52.47440  1.000 36.64096  ? 237 ASP A OD2 1 
ATOM   1659 N  N   . ILE A  1 212 ? 21.25575  -2.50502  51.11846  1.000 29.87070  ? 238 ILE A N   1 
ATOM   1660 C  CA  . ILE A  1 212 ? 20.39293  -1.67344  50.28885  1.000 28.34690  ? 238 ILE A CA  1 
ATOM   1661 C  C   . ILE A  1 212 ? 19.09637  -1.44522  51.05232  1.000 26.49165  ? 238 ILE A C   1 
ATOM   1662 O  O   . ILE A  1 212 ? 18.54383  -2.37871  51.64494  1.000 26.96027  ? 238 ILE A O   1 
ATOM   1663 C  CB  . ILE A  1 212 ? 20.12331  -2.31898  48.91248  1.000 27.84711  ? 238 ILE A CB  1 
ATOM   1664 C  CG1 . ILE A  1 212 ? 21.38933  -2.29755  48.05262  1.000 28.18321  ? 238 ILE A CG1 1 
ATOM   1665 C  CG2 . ILE A  1 212 ? 18.98805  -1.61016  48.19170  1.000 28.78207  ? 238 ILE A CG2 1 
ATOM   1666 C  CD1 . ILE A  1 212 ? 21.89267  -0.91291  47.72750  1.000 28.56946  ? 238 ILE A CD1 1 
ATOM   1667 N  N   . CYS A  1 213 ? 18.61389  -0.20125  51.04382  1.000 26.57858  ? 239 CYS A N   1 
ATOM   1668 C  CA  A CYS A  1 213 ? 17.44875  0.22024   51.81105  0.660 26.72021  ? 239 CYS A CA  1 
ATOM   1669 C  CA  B CYS A  1 213 ? 17.42516  0.12694   51.81177  0.340 26.56211  ? 239 CYS A CA  1 
ATOM   1670 C  C   . CYS A  1 213 ? 16.20761  0.45957   50.96259  1.000 23.85102  ? 239 CYS A C   1 
ATOM   1671 O  O   . CYS A  1 213 ? 15.11224  0.58729   51.51920  1.000 20.39465  ? 239 CYS A O   1 
ATOM   1672 C  CB  A CYS A  1 213 ? 17.76542  1.51109   52.58642  0.660 28.61178  ? 239 CYS A CB  1 
ATOM   1673 C  CB  B CYS A  1 213 ? 17.72733  1.28289   52.77159  0.340 28.81210  ? 239 CYS A CB  1 
ATOM   1674 S  SG  A CYS A  1 213 ? 18.15122  2.92532   51.51045  0.660 30.09127  ? 239 CYS A SG  1 
ATOM   1675 S  SG  B CYS A  1 213 ? 18.94747  0.80948   54.01497  0.340 30.34808  ? 239 CYS A SG  1 
ATOM   1676 N  N   . VAL A  1 214 ? 16.35233  0.56221   49.64439  1.000 22.86105  ? 240 VAL A N   1 
ATOM   1677 C  CA  . VAL A  1 214 ? 15.21645  0.76642   48.74990  1.000 23.74992  ? 240 VAL A CA  1 
ATOM   1678 C  C   . VAL A  1 214 ? 15.60652  0.25544   47.36980  1.000 23.62336  ? 240 VAL A C   1 
ATOM   1679 O  O   . VAL A  1 214 ? 16.74660  0.42688   46.92778  1.000 23.22483  ? 240 VAL A O   1 
ATOM   1680 C  CB  . VAL A  1 214 ? 14.76976  2.24627   48.71491  1.000 26.36550  ? 240 VAL A CB  1 
ATOM   1681 C  CG1 . VAL A  1 214 ? 15.87660  3.13575   48.18240  1.000 27.77849  ? 240 VAL A CG1 1 
ATOM   1682 C  CG2 . VAL A  1 214 ? 13.50009  2.40615   47.88840  1.000 26.16124  ? 240 VAL A CG2 1 
ATOM   1683 N  N   . ALA A  1 215 ? 14.65699  -0.38880  46.69487  1.000 23.30797  ? 241 ALA A N   1 
ATOM   1684 C  CA  . ALA A  1 215 ? 14.95111  -1.05793  45.43839  1.000 21.98664  ? 241 ALA A CA  1 
ATOM   1685 C  C   . ALA A  1 215 ? 13.66860  -1.25579  44.64446  1.000 20.16862  ? 241 ALA A C   1 
ATOM   1686 O  O   . ALA A  1 215 ? 12.60486  -1.50752  45.21848  1.000 20.98413  ? 241 ALA A O   1 
ATOM   1687 C  CB  . ALA A  1 215 ? 15.62712  -2.41165  45.68435  1.000 21.80754  ? 241 ALA A CB  1 
ATOM   1688 N  N   . ILE A  1 216 ? 13.77903  -1.12453  43.32649  1.000 18.32004  ? 242 ILE A N   1 
ATOM   1689 C  CA  . ILE A  1 216 ? 12.74736  -1.61218  42.41901  1.000 18.38341  ? 242 ILE A CA  1 
ATOM   1690 C  C   . ILE A  1 216 ? 12.92380  -3.11899  42.30687  1.000 18.42106  ? 242 ILE A C   1 
ATOM   1691 O  O   . ILE A  1 216 ? 14.00487  -3.59842  41.94993  1.000 18.41569  ? 242 ILE A O   1 
ATOM   1692 C  CB  . ILE A  1 216 ? 12.84898  -0.94089  41.04250  1.000 15.85542  ? 242 ILE A CB  1 
ATOM   1693 C  CG1 . ILE A  1 216 ? 12.75773  0.57962   41.17455  1.000 16.21884  ? 242 ILE A CG1 1 
ATOM   1694 C  CG2 . ILE A  1 216 ? 11.76542  -1.46885  40.11357  1.000 15.66600  ? 242 ILE A CG2 1 
ATOM   1695 C  CD1 . ILE A  1 216 ? 12.84044  1.30798   39.85069  1.000 16.67352  ? 242 ILE A CD1 1 
ATOM   1696 N  N   . GLY A  1 217 ? 11.87584  -3.87232  42.62472  1.000 18.67395  ? 243 GLY A N   1 
ATOM   1697 C  CA  . GLY A  1 217 ? 12.01624  -5.31448  42.66811  1.000 17.23958  ? 243 GLY A CA  1 
ATOM   1698 C  C   . GLY A  1 217 ? 10.73173  -6.04543  42.35152  1.000 19.00541  ? 243 GLY A C   1 
ATOM   1699 O  O   . GLY A  1 217 ? 9.62485   -5.51969  42.51466  1.000 19.69754  ? 243 GLY A O   1 
ATOM   1700 N  N   . TRP A  1 218 ? 10.90160  -7.28193  41.89309  1.000 18.89290  ? 244 TRP A N   1 
ATOM   1701 C  CA  . TRP A  1 218 ? 9.78135   -8.19025  41.71664  1.000 18.92228  ? 244 TRP A CA  1 
ATOM   1702 C  C   . TRP A  1 218 ? 9.34137   -8.72255  43.07428  1.000 20.45498  ? 244 TRP A C   1 
ATOM   1703 O  O   . TRP A  1 218 ? 10.17061  -8.98506  43.95046  1.000 20.72931  ? 244 TRP A O   1 
ATOM   1704 C  CB  . TRP A  1 218 ? 10.17029  -9.33561  40.78086  1.000 18.63273  ? 244 TRP A CB  1 
ATOM   1705 C  CG  . TRP A  1 218 ? 10.48785  -8.86710  39.38839  1.000 19.88681  ? 244 TRP A CG  1 
ATOM   1706 C  CD1 . TRP A  1 218 ? 9.64442   -8.22257  38.53147  1.000 20.84345  ? 244 TRP A CD1 1 
ATOM   1707 C  CD2 . TRP A  1 218 ? 11.73900  -8.99468  38.69791  1.000 21.64061  ? 244 TRP A CD2 1 
ATOM   1708 N  NE1 . TRP A  1 218 ? 10.28829  -7.94573  37.35000  1.000 22.63741  ? 244 TRP A NE1 1 
ATOM   1709 C  CE2 . TRP A  1 218 ? 11.57520  -8.40915  37.42613  1.000 22.38505  ? 244 TRP A CE2 1 
ATOM   1710 C  CE3 . TRP A  1 218 ? 12.97936  -9.54930  39.02991  1.000 20.74072  ? 244 TRP A CE3 1 
ATOM   1711 C  CZ2 . TRP A  1 218 ? 12.60434  -8.36226  36.48648  1.000 22.21239  ? 244 TRP A CZ2 1 
ATOM   1712 C  CZ3 . TRP A  1 218 ? 14.00036  -9.50098  38.09512  1.000 20.95733  ? 244 TRP A CZ3 1 
ATOM   1713 C  CH2 . TRP A  1 218 ? 13.80599  -8.91199  36.83912  1.000 21.01923  ? 244 TRP A CH2 1 
ATOM   1714 N  N   . ALA A  1 219 ? 8.02396   -8.87423  43.24157  1.000 20.40936  ? 245 ALA A N   1 
ATOM   1715 C  CA  . ALA A  1 219 ? 7.45763   -9.15937  44.55830  1.000 20.55490  ? 245 ALA A CA  1 
ATOM   1716 C  C   . ALA A  1 219 ? 8.05535   -10.41837 45.17528  1.000 22.10344  ? 245 ALA A C   1 
ATOM   1717 O  O   . ALA A  1 219 ? 8.37169   -10.44046 46.37168  1.000 23.04798  ? 245 ALA A O   1 
ATOM   1718 C  CB  . ALA A  1 219 ? 5.93811   -9.28633  44.45495  1.000 19.42087  ? 245 ALA A CB  1 
ATOM   1719 N  N   . GLY A  1 220 ? 8.21171   -11.47777 44.37840  1.000 21.52737  ? 246 GLY A N   1 
ATOM   1720 C  CA  . GLY A  1 220 ? 8.75914   -12.71527 44.91111  1.000 20.39173  ? 246 GLY A CA  1 
ATOM   1721 C  C   . GLY A  1 220 ? 10.16486  -12.54800 45.45430  1.000 18.69968  ? 246 GLY A C   1 
ATOM   1722 O  O   . GLY A  1 220 ? 10.50302  -13.09480 46.50681  1.000 20.85552  ? 246 GLY A O   1 
ATOM   1723 N  N   . ASP A  1 221 ? 10.99890  -11.77788 44.75117  1.000 16.87727  ? 247 ASP A N   1 
ATOM   1724 C  CA  . ASP A  1 221 ? 12.35960  -11.53773 45.22081  1.000 18.88909  ? 247 ASP A CA  1 
ATOM   1725 C  C   . ASP A  1 221 ? 12.36346  -10.78371 46.54527  1.000 18.88843  ? 247 ASP A C   1 
ATOM   1726 O  O   . ASP A  1 221 ? 13.14726  -11.10134 47.44868  1.000 19.91287  ? 247 ASP A O   1 
ATOM   1727 C  CB  . ASP A  1 221 ? 13.14715  -10.76136 44.16715  1.000 20.23571  ? 247 ASP A CB  1 
ATOM   1728 C  CG  . ASP A  1 221 ? 13.28706  -11.52001 42.86252  1.000 24.92876  ? 247 ASP A CG  1 
ATOM   1729 O  OD1 . ASP A  1 221 ? 12.93595  -12.71822 42.82529  1.000 24.55556  ? 247 ASP A OD1 1 
ATOM   1730 O  OD2 . ASP A  1 221 ? 13.74872  -10.91449 41.87162  1.000 25.78782  ? 247 ASP A OD2 1 
ATOM   1731 N  N   . VAL A  1 222 ? 11.49076  -9.78294  46.68178  1.000 18.01038  ? 248 VAL A N   1 
ATOM   1732 C  CA  . VAL A  1 222 ? 11.45725  -8.99558  47.91040  1.000 19.03049  ? 248 VAL A CA  1 
ATOM   1733 C  C   . VAL A  1 222 ? 10.95009  -9.83870  49.07317  1.000 22.17555  ? 248 VAL A C   1 
ATOM   1734 O  O   . VAL A  1 222 ? 11.46107  -9.74234  50.19655  1.000 24.39131  ? 248 VAL A O   1 
ATOM   1735 C  CB  . VAL A  1 222 ? 10.60507  -7.72938  47.71369  1.000 16.56953  ? 248 VAL A CB  1 
ATOM   1736 C  CG1 . VAL A  1 222 ? 10.58548  -6.90307  48.99086  1.000 15.55394  ? 248 VAL A CG1 1 
ATOM   1737 C  CG2 . VAL A  1 222 ? 11.13865  -6.90840  46.55147  1.000 17.07242  ? 248 VAL A CG2 1 
ATOM   1738 N  N   . TRP A  1 223 ? 9.93815   -10.67592 48.82997  1.000 22.35709  ? 249 TRP A N   1 
ATOM   1739 C  CA  . TRP A  1 223 ? 9.46338   -11.55979 49.88925  1.000 24.55097  ? 249 TRP A CA  1 
ATOM   1740 C  C   . TRP A  1 223 ? 10.53575  -12.56890 50.27832  1.000 26.97937  ? 249 TRP A C   1 
ATOM   1741 O  O   . TRP A  1 223 ? 10.68968  -12.89560 51.46086  1.000 29.91890  ? 249 TRP A O   1 
ATOM   1742 C  CB  . TRP A  1 223 ? 8.17901   -12.27107 49.46042  1.000 24.55605  ? 249 TRP A CB  1 
ATOM   1743 C  CG  . TRP A  1 223 ? 6.99767   -11.35726 49.26398  1.000 25.28206  ? 249 TRP A CG  1 
ATOM   1744 C  CD1 . TRP A  1 223 ? 6.16363   -11.32428 48.18441  1.000 26.06923  ? 249 TRP A CD1 1 
ATOM   1745 C  CD2 . TRP A  1 223 ? 6.51581   -10.35309 50.17152  1.000 27.05282  ? 249 TRP A CD2 1 
ATOM   1746 N  NE1 . TRP A  1 223 ? 5.19803   -10.36323 48.35869  1.000 27.21968  ? 249 TRP A NE1 1 
ATOM   1747 C  CE2 . TRP A  1 223 ? 5.39120   -9.75311  49.56985  1.000 26.25028  ? 249 TRP A CE2 1 
ATOM   1748 C  CE3 . TRP A  1 223 ? 6.92560   -9.90347  51.43174  1.000 29.57378  ? 249 TRP A CE3 1 
ATOM   1749 C  CZ2 . TRP A  1 223 ? 4.67365   -8.72837  50.18290  1.000 27.26892  ? 249 TRP A CZ2 1 
ATOM   1750 C  CZ3 . TRP A  1 223 ? 6.21189   -8.88518  52.03793  1.000 32.05941  ? 249 TRP A CZ3 1 
ATOM   1751 C  CH2 . TRP A  1 223 ? 5.09853   -8.30968  51.41342  1.000 31.28784  ? 249 TRP A CH2 1 
ATOM   1752 N  N   . GLN A  1 224 ? 11.29930  -13.06160 49.29845  1.000 26.11859  ? 250 GLN A N   1 
ATOM   1753 C  CA  . GLN A  1 224 ? 12.40996  -13.95589 49.60698  1.000 27.46905  ? 250 GLN A CA  1 
ATOM   1754 C  C   . GLN A  1 224 ? 13.45559  -13.25796 50.46709  1.000 26.41514  ? 250 GLN A C   1 
ATOM   1755 O  O   . GLN A  1 224 ? 13.97528  -13.84478 51.42189  1.000 24.31959  ? 250 GLN A O   1 
ATOM   1756 C  CB  . GLN A  1 224 ? 13.03958  -14.47607 48.31480  1.000 30.96375  ? 250 GLN A CB  1 
ATOM   1757 C  CG  . GLN A  1 224 ? 14.15743  -15.48300 48.52988  1.000 35.98191  ? 250 GLN A CG  1 
ATOM   1758 C  CD  . GLN A  1 224 ? 14.78676  -15.94319 47.22900  1.000 39.80349  ? 250 GLN A CD  1 
ATOM   1759 O  OE1 . GLN A  1 224 ? 15.13291  -15.13083 46.37086  1.000 40.09945  ? 250 GLN A OE1 1 
ATOM   1760 N  NE2 . GLN A  1 224 ? 14.93760  -17.25349 47.07644  1.000 41.60103  ? 250 GLN A NE2 1 
ATOM   1761 N  N   . ALA A  1 225 ? 13.77148  -12.00039 50.14733  1.000 25.19506  ? 251 ALA A N   1 
ATOM   1762 C  CA  . ALA A  1 225 ? 14.74942  -11.25797 50.93933  1.000 24.37598  ? 251 ALA A CA  1 
ATOM   1763 C  C   . ALA A  1 225 ? 14.25237  -11.02910 52.36242  1.000 24.92554  ? 251 ALA A C   1 
ATOM   1764 O  O   . ALA A  1 225 ? 15.00914  -11.19049 53.33024  1.000 26.48102  ? 251 ALA A O   1 
ATOM   1765 C  CB  . ALA A  1 225 ? 15.06847  -9.92477  50.26325  1.000 20.39244  ? 251 ALA A CB  1 
ATOM   1766 N  N   . SER A  1 226 ? 12.98019  -10.65087 52.50859  1.000 24.92720  ? 252 SER A N   1 
ATOM   1767 C  CA  . SER A  1 226 ? 12.42592  -10.41595 53.83825  1.000 25.73002  ? 252 SER A CA  1 
ATOM   1768 C  C   . SER A  1 226 ? 12.39759  -11.70117 54.65739  1.000 23.81435  ? 252 SER A C   1 
ATOM   1769 O  O   . SER A  1 226 ? 12.72072  -11.69333 55.85193  1.000 23.08985  ? 252 SER A O   1 
ATOM   1770 C  CB  . SER A  1 226 ? 11.02459  -9.81478  53.72247  1.000 26.94650  ? 252 SER A CB  1 
ATOM   1771 O  OG  . SER A  1 226 ? 10.21900  -10.16632 54.83333  1.000 31.27122  ? 252 SER A OG  1 
ATOM   1772 N  N   . ASN A  1 227 ? 12.02979  -12.82169 54.02837  1.000 23.75151  ? 253 ASN A N   1 
ATOM   1773 C  CA  . ASN A  1 227 ? 12.01769  -14.09611 54.73719  1.000 24.13291  ? 253 ASN A CA  1 
ATOM   1774 C  C   . ASN A  1 227 ? 13.42596  -14.55852 55.08589  1.000 24.62632  ? 253 ASN A C   1 
ATOM   1775 O  O   . ASN A  1 227 ? 13.62802  -15.17396 56.13697  1.000 25.95596  ? 253 ASN A O   1 
ATOM   1776 C  CB  . ASN A  1 227 ? 11.29773  -15.15447 53.90239  1.000 24.65739  ? 253 ASN A CB  1 
ATOM   1777 C  CG  . ASN A  1 227 ? 9.79619   -14.94443 53.86771  1.000 25.63810  ? 253 ASN A CG  1 
ATOM   1778 O  OD1 . ASN A  1 227 ? 9.22952   -14.29406 54.74530  1.000 28.36061  ? 253 ASN A OD1 1 
ATOM   1779 N  ND2 . ASN A  1 227 ? 9.14353   -15.49521 52.85064  1.000 23.30929  ? 253 ASN A ND2 1 
ATOM   1780 N  N   . ARG A  1 228 ? 14.40824  -14.26971 54.22812  1.000 23.50444  ? 254 ARG A N   1 
ATOM   1781 C  CA  . ARG A  1 228 ? 15.79489  -14.58338 54.55542  1.000 24.31088  ? 254 ARG A CA  1 
ATOM   1782 C  C   . ARG A  1 228 ? 16.26180  -13.78485 55.76439  1.000 26.11810  ? 254 ARG A C   1 
ATOM   1783 O  O   . ARG A  1 228 ? 16.92269  -14.32532 56.66101  1.000 26.06162  ? 254 ARG A O   1 
ATOM   1784 C  CB  . ARG A  1 228 ? 16.68952  -14.30559 53.34695  1.000 24.21672  ? 254 ARG A CB  1 
ATOM   1785 C  CG  . ARG A  1 228 ? 18.15129  -14.67577 53.54087  1.000 28.43202  ? 254 ARG A CG  1 
ATOM   1786 C  CD  . ARG A  1 228 ? 18.93706  -14.48589 52.25040  1.000 29.76303  ? 254 ARG A CD  1 
ATOM   1787 N  NE  . ARG A  1 228 ? 18.40810  -15.30562 51.16334  1.000 30.07641  ? 254 ARG A NE  1 
ATOM   1788 C  CZ  . ARG A  1 228 ? 18.61479  -15.06210 49.87250  1.000 31.43346  ? 254 ARG A CZ  1 
ATOM   1789 N  NH1 . ARG A  1 228 ? 19.34103  -14.01667 49.49941  1.000 31.08240  ? 254 ARG A NH1 1 
ATOM   1790 N  NH2 . ARG A  1 228 ? 18.09349  -15.86352 48.95272  1.000 29.68475  ? 254 ARG A NH2 1 
ATOM   1791 N  N   . ALA A  1 229 ? 15.92293  -12.49347 55.80538  1.000 26.76675  ? 255 ALA A N   1 
ATOM   1792 C  CA  . ALA A  1 229 ? 16.25773  -11.67887 56.96893  1.000 28.60419  ? 255 ALA A CA  1 
ATOM   1793 C  C   . ALA A  1 229 ? 15.59014  -12.21784 58.22855  1.000 30.53791  ? 255 ALA A C   1 
ATOM   1794 O  O   . ALA A  1 229 ? 16.22191  -12.29825 59.28878  1.000 24.31400  ? 255 ALA A O   1 
ATOM   1795 C  CB  . ALA A  1 229 ? 15.85578  -10.22415 56.72707  1.000 27.95021  ? 255 ALA A CB  1 
ATOM   1796 N  N   . LYS A  1 230 ? 14.31378  -12.59933 58.12918  1.000 30.45667  ? 256 LYS A N   1 
ATOM   1797 C  CA  . LYS A  1 230 ? 13.60629  -13.14228 59.28672  1.000 30.74044  ? 256 LYS A CA  1 
ATOM   1798 C  C   . LYS A  1 230 ? 14.25114  -14.43648 59.77104  1.000 30.01052  ? 256 LYS A C   1 
ATOM   1799 O  O   . LYS A  1 230 ? 14.45012  -14.63280 60.97621  1.000 29.09348  ? 256 LYS A O   1 
ATOM   1800 C  CB  . LYS A  1 230 ? 12.13467  -13.37368 58.94148  1.000 31.26736  ? 256 LYS A CB  1 
ATOM   1801 C  CG  . LYS A  1 230 ? 11.32121  -12.10275 58.76774  1.000 31.49748  ? 256 LYS A CG  1 
ATOM   1802 C  CD  . LYS A  1 230 ? 9.84703   -12.42369 58.58276  1.000 33.15604  ? 256 LYS A CD  1 
ATOM   1803 C  CE  . LYS A  1 230 ? 9.01627   -11.15870 58.44578  1.000 34.36392  ? 256 LYS A CE  1 
ATOM   1804 N  NZ  . LYS A  1 230 ? 7.56067   -11.46247 58.37162  1.000 35.39312  ? 256 LYS A NZ  1 
ATOM   1805 N  N   . GLU A  1 231 ? 14.58221  -15.33522 58.83953  1.000 26.96621  ? 257 GLU A N   1 
ATOM   1806 C  CA  . GLU A  1 231 ? 15.20249  -16.60319 59.20916  1.000 29.89435  ? 257 GLU A CA  1 
ATOM   1807 C  C   . GLU A  1 231 ? 16.56667  -16.38395 59.84844  1.000 31.39121  ? 257 GLU A C   1 
ATOM   1808 O  O   . GLU A  1 231 ? 16.93801  -17.08903 60.79411  1.000 33.48119  ? 257 GLU A O   1 
ATOM   1809 C  CB  . GLU A  1 231 ? 15.32445  -17.50283 57.97823  1.000 32.65933  ? 257 GLU A CB  1 
ATOM   1810 C  CG  . GLU A  1 231 ? 15.41369  -18.98949 58.28862  1.000 38.58251  ? 257 GLU A CG  1 
ATOM   1811 C  CD  . GLU A  1 231 ? 16.81959  -19.43171 58.64351  1.000 43.32852  ? 257 GLU A CD  1 
ATOM   1812 O  OE1 . GLU A  1 231 ? 17.78316  -18.79497 58.16771  1.000 44.69321  ? 257 GLU A OE1 1 
ATOM   1813 O  OE2 . GLU A  1 231 ? 16.96097  -20.41791 59.39662  1.000 46.09191  ? 257 GLU A OE2 1 
ATOM   1814 N  N   . ALA A  1 232 ? 17.32877  -15.41027 59.34672  1.000 32.11478  ? 258 ALA A N   1 
ATOM   1815 C  CA  . ALA A  1 232 ? 18.63547  -15.11761 59.92099  1.000 33.97332  ? 258 ALA A CA  1 
ATOM   1816 C  C   . ALA A  1 232 ? 18.54620  -14.43798 61.28107  1.000 34.89384  ? 258 ALA A C   1 
ATOM   1817 O  O   . ALA A  1 232 ? 19.55891  -14.38011 61.98777  1.000 35.18362  ? 258 ALA A O   1 
ATOM   1818 C  CB  . ALA A  1 232 ? 19.44612  -14.24531 58.96092  1.000 25.89520  ? 258 ALA A CB  1 
ATOM   1819 N  N   . LYS A  1 233 ? 17.36928  -13.93278 61.66098  1.000 33.81930  ? 259 LYS A N   1 
ATOM   1820 C  CA  . LYS A  1 233 ? 17.17766  -13.19993 62.91472  1.000 32.80089  ? 259 LYS A CA  1 
ATOM   1821 C  C   . LYS A  1 233 ? 18.13193  -12.01384 63.02796  1.000 31.54040  ? 259 LYS A C   1 
ATOM   1822 O  O   . LYS A  1 233 ? 18.58775  -11.67178 64.12186  1.000 31.70652  ? 259 LYS A O   1 
ATOM   1823 C  CB  . LYS A  1 233 ? 17.32406  -14.11892 64.13254  1.000 34.17251  ? 259 LYS A CB  1 
ATOM   1824 C  CG  . LYS A  1 233 ? 16.37405  -15.30662 64.14708  1.000 35.52923  ? 259 LYS A CG  1 
ATOM   1825 C  CD  . LYS A  1 233 ? 16.63115  -16.19463 65.35642  1.000 39.85274  ? 259 LYS A CD  1 
ATOM   1826 C  CE  . LYS A  1 233 ? 15.94641  -17.54587 65.21351  1.000 43.03965  ? 259 LYS A CE  1 
ATOM   1827 N  NZ  . LYS A  1 233 ? 14.77505  -17.68242 66.12398  1.000 45.40766  ? 259 LYS A NZ  1 
ATOM   1828 N  N   . ASN A  1 234 ? 18.44075  -11.37622 61.89797  1.000 30.10674  ? 260 ASN A N   1 
ATOM   1829 C  CA  . ASN A  1 234 ? 19.37312  -10.25647 61.88598  1.000 30.38530  ? 260 ASN A CA  1 
ATOM   1830 C  C   . ASN A  1 234 ? 18.71865  -8.92813  62.24137  1.000 30.24962  ? 260 ASN A C   1 
ATOM   1831 O  O   . ASN A  1 234 ? 19.43003  -7.92925  62.39472  1.000 29.59258  ? 260 ASN A O   1 
ATOM   1832 C  CB  . ASN A  1 234 ? 20.04756  -10.14620 60.51457  1.000 28.30094  ? 260 ASN A CB  1 
ATOM   1833 C  CG  . ASN A  1 234 ? 19.04934  -10.02626 59.37642  1.000 28.26600  ? 260 ASN A CG  1 
ATOM   1834 O  OD1 . ASN A  1 234 ? 17.84297  -9.91643  59.59691  1.000 28.22177  ? 260 ASN A OD1 1 
ATOM   1835 N  ND2 . ASN A  1 234 ? 19.55266  -10.04466 58.14770  1.000 28.62226  ? 260 ASN A ND2 1 
ATOM   1836 N  N   . GLY A  1 235 ? 17.39521  -8.88862  62.37320  1.000 27.69199  ? 261 GLY A N   1 
ATOM   1837 C  CA  . GLY A  1 235 ? 16.70912  -7.65972  62.70958  1.000 32.37460  ? 261 GLY A CA  1 
ATOM   1838 C  C   . GLY A  1 235 ? 16.46618  -6.71865  61.55325  1.000 31.74567  ? 261 GLY A C   1 
ATOM   1839 O  O   . GLY A  1 235 ? 16.09876  -5.56145  61.78619  1.000 31.69652  ? 261 GLY A O   1 
ATOM   1840 N  N   . VAL A  1 236 ? 16.66111  -7.16934  60.31839  1.000 30.77441  ? 262 VAL A N   1 
ATOM   1841 C  CA  . VAL A  1 236 ? 16.40958  -6.34854  59.13934  1.000 28.76154  ? 262 VAL A CA  1 
ATOM   1842 C  C   . VAL A  1 236 ? 14.95755  -6.54205  58.72261  1.000 27.64330  ? 262 VAL A C   1 
ATOM   1843 O  O   . VAL A  1 236 ? 14.52388  -7.66810  58.45565  1.000 26.47005  ? 262 VAL A O   1 
ATOM   1844 C  CB  . VAL A  1 236 ? 17.36693  -6.70905  57.99397  1.000 27.42617  ? 262 VAL A CB  1 
ATOM   1845 C  CG1 . VAL A  1 236 ? 17.01607  -5.91789  56.74220  1.000 27.30716  ? 262 VAL A CG1 1 
ATOM   1846 C  CG2 . VAL A  1 236 ? 18.80869  -6.45155  58.40839  1.000 24.12819  ? 262 VAL A CG2 1 
ATOM   1847 N  N   . ASN A  1 237 ? 14.20584  -5.44511  58.66666  1.000 26.81695  ? 263 ASN A N   1 
ATOM   1848 C  CA  . ASN A  1 237 ? 12.78179  -5.47694  58.33948  1.000 28.23044  ? 263 ASN A CA  1 
ATOM   1849 C  C   . ASN A  1 237 ? 12.60826  -5.01518  56.89635  1.000 27.25269  ? 263 ASN A C   1 
ATOM   1850 O  O   . ASN A  1 237 ? 12.69077  -3.82052  56.59938  1.000 25.78021  ? 263 ASN A O   1 
ATOM   1851 C  CB  . ASN A  1 237 ? 11.98743  -4.60588  59.30679  1.000 31.13578  ? 263 ASN A CB  1 
ATOM   1852 C  CG  . ASN A  1 237 ? 11.96623  -5.16985  60.71353  1.000 34.83670  ? 263 ASN A CG  1 
ATOM   1853 O  OD1 . ASN A  1 237 ? 11.70639  -6.35628  60.91455  1.000 35.98256  ? 263 ASN A OD1 1 
ATOM   1854 N  ND2 . ASN A  1 237 ? 12.24295  -4.32051  61.69671  1.000 35.47192  ? 263 ASN A ND2 1 
ATOM   1855 N  N   . VAL A  1 238 ? 12.36262  -5.96761  56.00055  1.000 26.70109  ? 264 VAL A N   1 
ATOM   1856 C  CA  . VAL A  1 238 ? 12.16647  -5.69242  54.58209  1.000 27.65900  ? 264 VAL A CA  1 
ATOM   1857 C  C   . VAL A  1 238 ? 10.68388  -5.81691  54.26486  1.000 26.16745  ? 264 VAL A C   1 
ATOM   1858 O  O   . VAL A  1 238 ? 10.03963  -6.80235  54.64595  1.000 27.18166  ? 264 VAL A O   1 
ATOM   1859 C  CB  . VAL A  1 238 ? 12.99703  -6.64818  53.70802  1.000 28.90284  ? 264 VAL A CB  1 
ATOM   1860 C  CG1 . VAL A  1 238 ? 12.69710  -6.41772  52.23315  1.000 26.60838  ? 264 VAL A CG1 1 
ATOM   1861 C  CG2 . VAL A  1 238 ? 14.48018  -6.47322  53.99002  1.000 31.91577  ? 264 VAL A CG2 1 
ATOM   1862 N  N   . SER A  1 239 ? 10.14091  -4.82055  53.57031  1.000 24.93634  ? 265 SER A N   1 
ATOM   1863 C  CA  A SER A  1 239 ? 8.74285   -4.81972  53.17154  0.571 24.19215  ? 265 SER A CA  1 
ATOM   1864 C  CA  B SER A  1 239 ? 8.74246   -4.81603  53.17219  0.429 24.21365  ? 265 SER A CA  1 
ATOM   1865 C  C   . SER A  1 239 ? 8.63971   -4.56597  51.67451  1.000 22.83819  ? 265 SER A C   1 
ATOM   1866 O  O   . SER A  1 239 ? 9.56261   -4.04243  51.04448  1.000 22.40809  ? 265 SER A O   1 
ATOM   1867 C  CB  A SER A  1 239 ? 7.93440   -3.76545  53.94039  0.571 24.91770  ? 265 SER A CB  1 
ATOM   1868 C  CB  B SER A  1 239 ? 7.93862   -3.75587  53.93878  0.429 24.94583  ? 265 SER A CB  1 
ATOM   1869 O  OG  A SER A  1 239 ? 6.54648   -3.91363  53.69598  0.571 25.43650  ? 265 SER A OG  1 
ATOM   1870 O  OG  B SER A  1 239 ? 7.69401   -4.16579  55.27279  0.429 26.34377  ? 265 SER A OG  1 
ATOM   1871 N  N   . PHE A  1 240 ? 7.49828   -4.95223  51.11109  1.000 23.16984  ? 266 PHE A N   1 
ATOM   1872 C  CA  . PHE A  1 240 ? 7.20646   -4.77224  49.69712  1.000 22.29173  ? 266 PHE A CA  1 
ATOM   1873 C  C   . PHE A  1 240 ? 5.91866   -3.97704  49.55076  1.000 23.64394  ? 266 PHE A C   1 
ATOM   1874 O  O   . PHE A  1 240 ? 4.95516   -4.19590  50.29235  1.000 27.24385  ? 266 PHE A O   1 
ATOM   1875 C  CB  . PHE A  1 240 ? 7.07513   -6.11839  48.97796  1.000 23.18711  ? 266 PHE A CB  1 
ATOM   1876 C  CG  . PHE A  1 240 ? 6.71218   -5.99721  47.52475  1.000 23.62356  ? 266 PHE A CG  1 
ATOM   1877 C  CD1 . PHE A  1 240 ? 7.67504   -5.68413  46.57949  1.000 22.32320  ? 266 PHE A CD1 1 
ATOM   1878 C  CD2 . PHE A  1 240 ? 5.40722   -6.19694  47.10433  1.000 25.49463  ? 266 PHE A CD2 1 
ATOM   1879 C  CE1 . PHE A  1 240 ? 7.34328   -5.57281  45.24207  1.000 23.44467  ? 266 PHE A CE1 1 
ATOM   1880 C  CE2 . PHE A  1 240 ? 5.06832   -6.08525  45.76827  1.000 25.34511  ? 266 PHE A CE2 1 
ATOM   1881 C  CZ  . PHE A  1 240 ? 6.03788   -5.77265  44.83592  1.000 23.67818  ? 266 PHE A CZ  1 
ATOM   1882 N  N   . SER A  1 241 ? 5.90311   -3.05524  48.59231  1.000 21.31920  ? 267 SER A N   1 
ATOM   1883 C  CA  . SER A  1 241 ? 4.74875   -2.19335  48.39340  1.000 22.99966  ? 267 SER A CA  1 
ATOM   1884 C  C   . SER A  1 241 ? 4.42780   -2.08949  46.91134  1.000 25.29028  ? 267 SER A C   1 
ATOM   1885 O  O   . SER A  1 241 ? 5.32540   -1.88830  46.08189  1.000 25.46251  ? 267 SER A O   1 
ATOM   1886 C  CB  . SER A  1 241 ? 4.98767   -0.79814  48.98072  1.000 22.60858  ? 267 SER A CB  1 
ATOM   1887 O  OG  . SER A  1 241 ? 4.25081   0.18658   48.27614  1.000 20.72428  ? 267 SER A OG  1 
ATOM   1888 N  N   . ILE A  1 242 ? 3.14530   -2.25042  46.59666  1.000 25.79544  ? 268 ILE A N   1 
ATOM   1889 C  CA  . ILE A  1 242 ? 2.58057   -1.95336  45.28436  1.000 22.54646  ? 268 ILE A CA  1 
ATOM   1890 C  C   . ILE A  1 242 ? 2.04798   -0.52723  45.35088  1.000 21.17172  ? 268 ILE A C   1 
ATOM   1891 O  O   . ILE A  1 242 ? 0.98873   -0.29342  45.95173  1.000 22.84624  ? 268 ILE A O   1 
ATOM   1892 C  CB  . ILE A  1 242 ? 1.47527   -2.95265  44.90858  1.000 21.18799  ? 268 ILE A CB  1 
ATOM   1893 C  CG1 . ILE A  1 242 ? 1.93016   -4.38592  45.19554  1.000 21.81994  ? 268 ILE A CG1 1 
ATOM   1894 C  CG2 . ILE A  1 242 ? 1.07923   -2.79051  43.44830  1.000 21.11918  ? 268 ILE A CG2 1 
ATOM   1895 C  CD1 . ILE A  1 242 ? 0.85923   -5.42950  44.95473  1.000 23.55877  ? 268 ILE A CD1 1 
ATOM   1896 N  N   . PRO A  1 243 ? 2.74304   0.44835   44.76659  1.000 20.72578  ? 269 PRO A N   1 
ATOM   1897 C  CA  . PRO A  1 243 ? 2.37980   1.85422   44.98285  1.000 23.01421  ? 269 PRO A CA  1 
ATOM   1898 C  C   . PRO A  1 243 ? 0.98608   2.18647   44.46785  1.000 22.85065  ? 269 PRO A C   1 
ATOM   1899 O  O   . PRO A  1 243 ? 0.40194   1.47243   43.64996  1.000 24.38314  ? 269 PRO A O   1 
ATOM   1900 C  CB  . PRO A  1 243 ? 3.45795   2.62067   44.20673  1.000 23.19595  ? 269 PRO A CB  1 
ATOM   1901 C  CG  . PRO A  1 243 ? 4.60922   1.66519   44.12623  1.000 21.41949  ? 269 PRO A CG  1 
ATOM   1902 C  CD  . PRO A  1 243 ? 3.97917   0.31379   43.97944  1.000 19.81156  ? 269 PRO A CD  1 
ATOM   1903 N  N   . LYS A  1 244 ? 0.45712   3.30805   44.96613  1.000 22.72739  ? 270 LYS A N   1 
ATOM   1904 C  CA  . LYS A  1 244 ? -0.91598  3.69756   44.66720  1.000 25.68632  ? 270 LYS A CA  1 
ATOM   1905 C  C   . LYS A  1 244 ? -1.09972  4.15408   43.22597  1.000 25.21042  ? 270 LYS A C   1 
ATOM   1906 O  O   . LYS A  1 244 ? -2.22483  4.10992   42.71738  1.000 25.19213  ? 270 LYS A O   1 
ATOM   1907 C  CB  . LYS A  1 244 ? -1.36823  4.80284   45.62388  1.000 27.83059  ? 270 LYS A CB  1 
ATOM   1908 C  CG  . LYS A  1 244 ? -0.62134  6.11937   45.46708  1.000 30.02130  ? 270 LYS A CG  1 
ATOM   1909 C  CD  . LYS A  1 244 ? -0.59156  6.89032   46.77921  1.000 33.41417  ? 270 LYS A CD  1 
ATOM   1910 C  CE  . LYS A  1 244 ? -0.55228  8.39351   46.54551  1.000 35.22776  ? 270 LYS A CE  1 
ATOM   1911 N  NZ  . LYS A  1 244 ? 0.30505   8.76206   45.38614  1.000 36.67225  ? 270 LYS A NZ  1 
ATOM   1912 N  N   . GLU A  1 245 ? -0.03290  4.59268   42.55918  1.000 24.81654  ? 271 GLU A N   1 
ATOM   1913 C  CA  . GLU A  1 245 ? -0.12101  4.99634   41.16123  1.000 25.03192  ? 271 GLU A CA  1 
ATOM   1914 C  C   . GLU A  1 245 ? -0.22024  3.81226   40.21000  1.000 24.01280  ? 271 GLU A C   1 
ATOM   1915 O  O   . GLU A  1 245 ? -0.34718  4.02010   38.99843  1.000 26.27046  ? 271 GLU A O   1 
ATOM   1916 C  CB  . GLU A  1 245 ? 1.08819   5.85561   40.77868  1.000 25.53018  ? 271 GLU A CB  1 
ATOM   1917 C  CG  . GLU A  1 245 ? 1.23363   7.13406   41.58720  1.000 26.26932  ? 271 GLU A CG  1 
ATOM   1918 C  CD  . GLU A  1 245 ? 2.12462   6.95949   42.80161  1.000 28.39230  ? 271 GLU A CD  1 
ATOM   1919 O  OE1 . GLU A  1 245 ? 2.65964   5.84787   42.99622  1.000 27.73052  ? 271 GLU A OE1 1 
ATOM   1920 O  OE2 . GLU A  1 245 ? 2.29035   7.93615   43.56192  1.000 29.77346  ? 271 GLU A OE2 1 
ATOM   1921 N  N   . GLY A  1 246 ? -0.16885  2.58825   40.72201  1.000 23.71836  ? 272 GLY A N   1 
ATOM   1922 C  CA  . GLY A  1 246 ? -0.17561  1.40031   39.89236  1.000 23.34244  ? 272 GLY A CA  1 
ATOM   1923 C  C   . GLY A  1 246 ? 1.20615   0.78886   39.77952  1.000 23.80645  ? 272 GLY A C   1 
ATOM   1924 O  O   . GLY A  1 246 ? 2.20654   1.31339   40.27908  1.000 23.79936  ? 272 GLY A O   1 
ATOM   1925 N  N   . ALA A  1 247 ? 1.24804   -0.35481  39.10167  1.000 23.54814  ? 273 ALA A N   1 
ATOM   1926 C  CA  . ALA A  1 247 ? 2.49593   -1.07548  38.89949  1.000 23.34256  ? 273 ALA A CA  1 
ATOM   1927 C  C   . ALA A  1 247 ? 2.30580   -2.07236  37.76858  1.000 22.90486  ? 273 ALA A C   1 
ATOM   1928 O  O   . ALA A  1 247 ? 1.17917   -2.40316  37.39062  1.000 21.46823  ? 273 ALA A O   1 
ATOM   1929 C  CB  . ALA A  1 247 ? 2.94991   -1.79087  40.17681  1.000 23.24128  ? 273 ALA A CB  1 
ATOM   1930 N  N   . MET A  1 248 ? 3.42639   -2.54400  37.23007  1.000 23.43679  ? 274 MET A N   1 
ATOM   1931 C  CA  . MET A  1 248 ? 3.37649   -3.57873  36.20856  1.000 25.07206  ? 274 MET A CA  1 
ATOM   1932 C  C   . MET A  1 248 ? 3.05396   -4.92172  36.84855  1.000 24.29064  ? 274 MET A C   1 
ATOM   1933 O  O   . MET A  1 248 ? 3.66383   -5.30687  37.85046  1.000 21.91030  ? 274 MET A O   1 
ATOM   1934 C  CB  . MET A  1 248 ? 4.70291   -3.65992  35.45608  1.000 28.46991  ? 274 MET A CB  1 
ATOM   1935 C  CG  . MET A  1 248 ? 4.69358   -4.67084  34.31772  1.000 32.14576  ? 274 MET A CG  1 
ATOM   1936 S  SD  . MET A  1 248 ? 6.34296   -5.10335  33.73592  1.000 35.99152  ? 274 MET A SD  1 
ATOM   1937 C  CE  . MET A  1 248 ? 6.43434   -6.82321  34.22970  1.000 34.40779  ? 274 MET A CE  1 
ATOM   1938 N  N   . ALA A  1 249 ? 2.09033   -5.63118  36.27257  1.000 24.59662  ? 275 ALA A N   1 
ATOM   1939 C  CA  . ALA A  1 249 ? 1.71186   -6.95682  36.73164  1.000 21.21972  ? 275 ALA A CA  1 
ATOM   1940 C  C   . ALA A  1 249 ? 2.13535   -8.00034  35.70694  1.000 21.49796  ? 275 ALA A C   1 
ATOM   1941 O  O   . ALA A  1 249 ? 2.12269   -7.75029  34.49850  1.000 21.40079  ? 275 ALA A O   1 
ATOM   1942 C  CB  . ALA A  1 249 ? 0.20296   -7.04786  36.97873  1.000 17.21005  ? 275 ALA A CB  1 
ATOM   1943 N  N   . PHE A  1 250 ? 2.52390   -9.17198  36.20353  1.000 21.60127  ? 276 PHE A N   1 
ATOM   1944 C  CA  . PHE A  1 250 ? 2.88791   -10.29223 35.35031  1.000 23.48933  ? 276 PHE A CA  1 
ATOM   1945 C  C   . PHE A  1 250 ? 2.22880   -11.55112 35.89073  1.000 22.14874  ? 276 PHE A C   1 
ATOM   1946 O  O   . PHE A  1 250 ? 2.06955   -11.71585 37.10324  1.000 21.35521  ? 276 PHE A O   1 
ATOM   1947 C  CB  . PHE A  1 250 ? 4.40967   -10.47615 35.25759  1.000 24.58434  ? 276 PHE A CB  1 
ATOM   1948 C  CG  . PHE A  1 250 ? 5.11793   -10.37995 36.57719  1.000 26.28441  ? 276 PHE A CG  1 
ATOM   1949 C  CD1 . PHE A  1 250 ? 5.34435   -11.51336 37.33968  1.000 26.00536  ? 276 PHE A CD1 1 
ATOM   1950 C  CD2 . PHE A  1 250 ? 5.56893   -9.15825  37.04975  1.000 26.23244  ? 276 PHE A CD2 1 
ATOM   1951 C  CE1 . PHE A  1 250 ? 6.00091   -11.43002 38.55144  1.000 27.04552  ? 276 PHE A CE1 1 
ATOM   1952 C  CE2 . PHE A  1 250 ? 6.22416   -9.06751  38.26164  1.000 26.90785  ? 276 PHE A CE2 1 
ATOM   1953 C  CZ  . PHE A  1 250 ? 6.44073   -10.20494 39.01417  1.000 28.39021  ? 276 PHE A CZ  1 
ATOM   1954 N  N   . PHE A  1 251 ? 1.84809   -12.43931 34.97812  1.000 21.60285  ? 277 PHE A N   1 
ATOM   1955 C  CA  . PHE A  1 251 ? 1.00592   -13.58000 35.30132  1.000 22.53274  ? 277 PHE A CA  1 
ATOM   1956 C  C   . PHE A  1 251 ? 1.67805   -14.88423 34.90463  1.000 23.46308  ? 277 PHE A C   1 
ATOM   1957 O  O   . PHE A  1 251 ? 2.35339   -14.96210 33.87330  1.000 24.65823  ? 277 PHE A O   1 
ATOM   1958 C  CB  . PHE A  1 251 ? -0.34688  -13.49023 34.58695  1.000 23.92673  ? 277 PHE A CB  1 
ATOM   1959 C  CG  . PHE A  1 251 ? -1.19216  -12.32961 35.01800  1.000 24.72466  ? 277 PHE A CG  1 
ATOM   1960 C  CD1 . PHE A  1 251 ? -2.27614  -12.52227 35.85948  1.000 26.85108  ? 277 PHE A CD1 1 
ATOM   1961 C  CD2 . PHE A  1 251 ? -0.91881  -11.04894 34.56558  1.000 24.15353  ? 277 PHE A CD2 1 
ATOM   1962 C  CE1 . PHE A  1 251 ? -3.06614  -11.45691 36.25049  1.000 26.47381  ? 277 PHE A CE1 1 
ATOM   1963 C  CE2 . PHE A  1 251 ? -1.70315  -9.98027  34.95231  1.000 25.26746  ? 277 PHE A CE2 1 
ATOM   1964 C  CZ  . PHE A  1 251 ? -2.77840  -10.18343 35.79641  1.000 27.23184  ? 277 PHE A CZ  1 
ATOM   1965 N  N   . ASP A  1 252 ? 1.48183   -15.90446 35.73095  1.000 21.12905  ? 278 ASP A N   1 
ATOM   1966 C  CA  . ASP A  1 252 ? 1.69385   -17.28575 35.33356  1.000 21.93695  ? 278 ASP A CA  1 
ATOM   1967 C  C   . ASP A  1 252 ? 0.34713   -17.87276 34.93505  1.000 21.86830  ? 278 ASP A C   1 
ATOM   1968 O  O   . ASP A  1 252 ? -0.68664  -17.53339 35.51896  1.000 20.14588  ? 278 ASP A O   1 
ATOM   1969 C  CB  . ASP A  1 252 ? 2.32755   -18.09923 36.46338  1.000 25.07736  ? 278 ASP A CB  1 
ATOM   1970 C  CG  . ASP A  1 252 ? 3.81360   -17.82910 36.61013  1.000 27.67037  ? 278 ASP A CG  1 
ATOM   1971 O  OD1 . ASP A  1 252 ? 4.49071   -17.64959 35.57514  1.000 29.08957  ? 278 ASP A OD1 1 
ATOM   1972 O  OD2 . ASP A  1 252 ? 4.30478   -17.79289 37.75771  1.000 28.44341  ? 278 ASP A OD2 1 
ATOM   1973 N  N   . VAL A  1 253 ? 0.35215   -18.72557 33.91654  1.000 22.68388  ? 279 VAL A N   1 
ATOM   1974 C  CA  . VAL A  1 253 ? -0.88735  -19.23490 33.34916  1.000 23.28614  ? 279 VAL A CA  1 
ATOM   1975 C  C   . VAL A  1 253 ? -0.78450  -20.73943 33.16251  1.000 23.51669  ? 279 VAL A C   1 
ATOM   1976 O  O   . VAL A  1 253 ? 0.29673   -21.28593 32.92625  1.000 24.08608  ? 279 VAL A O   1 
ATOM   1977 C  CB  . VAL A  1 253 ? -1.23021  -18.55193 32.00516  1.000 25.18170  ? 279 VAL A CB  1 
ATOM   1978 C  CG1 . VAL A  1 253 ? -1.39623  -17.05065 32.18768  1.000 24.04723  ? 279 VAL A CG1 1 
ATOM   1979 C  CG2 . VAL A  1 253 ? -0.16174  -18.85199 30.96341  1.000 26.76570  ? 279 VAL A CG2 1 
ATOM   1980 N  N   . PHE A  1 254 ? -1.92566  -21.40990 33.28312  1.000 22.60324  ? 280 PHE A N   1 
ATOM   1981 C  CA  . PHE A  1 254 ? -2.05357  -22.79993 32.87790  1.000 23.56233  ? 280 PHE A CA  1 
ATOM   1982 C  C   . PHE A  1 254 ? -2.45921  -22.84101 31.41092  1.000 25.31961  ? 280 PHE A C   1 
ATOM   1983 O  O   . PHE A  1 254 ? -3.36693  -22.11413 30.98960  1.000 26.34438  ? 280 PHE A O   1 
ATOM   1984 C  CB  . PHE A  1 254 ? -3.08240  -23.53154 33.74068  1.000 24.24421  ? 280 PHE A CB  1 
ATOM   1985 C  CG  . PHE A  1 254 ? -2.47424  -24.38237 34.82024  1.000 22.93747  ? 280 PHE A CG  1 
ATOM   1986 C  CD1 . PHE A  1 254 ? -2.26679  -25.73741 34.61882  1.000 22.02108  ? 280 PHE A CD1 1 
ATOM   1987 C  CD2 . PHE A  1 254 ? -2.11220  -23.82792 36.03676  1.000 19.32613  ? 280 PHE A CD2 1 
ATOM   1988 C  CE1 . PHE A  1 254 ? -1.70780  -26.52403 35.61046  1.000 20.37558  ? 280 PHE A CE1 1 
ATOM   1989 C  CE2 . PHE A  1 254 ? -1.55263  -24.60857 37.03187  1.000 26.07209  ? 280 PHE A CE2 1 
ATOM   1990 C  CZ  . PHE A  1 254 ? -1.35075  -25.95805 36.81881  1.000 19.59800  ? 280 PHE A CZ  1 
ATOM   1991 N  N   . ALA A  1 255 ? -1.77306  -23.67617 30.63533  1.000 24.55536  ? 281 ALA A N   1 
ATOM   1992 C  CA  . ALA A  1 255 ? -2.02680  -23.79537 29.20900  1.000 24.97597  ? 281 ALA A CA  1 
ATOM   1993 C  C   . ALA A  1 255 ? -1.93868  -25.25845 28.80583  1.000 25.71281  ? 281 ALA A C   1 
ATOM   1994 O  O   . ALA A  1 255 ? -1.26225  -26.05939 29.45645  1.000 26.52377  ? 281 ALA A O   1 
ATOM   1995 C  CB  . ALA A  1 255 ? -1.03943  -22.95717 28.38579  1.000 23.78294  ? 281 ALA A CB  1 
ATOM   1996 N  N   . MET A  1 256 ? -2.63257  -25.59883 27.72263  1.000 26.96367  ? 282 MET A N   1 
ATOM   1997 C  CA  . MET A  1 256 ? -2.69149  -26.96947 27.23940  1.000 27.54062  ? 282 MET A CA  1 
ATOM   1998 C  C   . MET A  1 256 ? -1.94613  -27.07878 25.91980  1.000 30.46278  ? 282 MET A C   1 
ATOM   1999 O  O   . MET A  1 256 ? -2.34514  -26.43316 24.93845  1.000 29.65802  ? 282 MET A O   1 
ATOM   2000 C  CB  . MET A  1 256 ? -4.14271  -27.41381 27.07119  1.000 27.04071  ? 282 MET A CB  1 
ATOM   2001 C  CG  . MET A  1 256 ? -4.31131  -28.87996 26.71506  1.000 30.23350  ? 282 MET A CG  1 
ATOM   2002 S  SD  . MET A  1 256 ? -6.03704  -29.31062 26.42626  1.000 31.07876  ? 282 MET A SD  1 
ATOM   2003 C  CE  . MET A  1 256 ? -6.79986  -28.63870 27.90258  1.000 28.80986  ? 282 MET A CE  1 
ATOM   2004 N  N   . PRO A  1 257 ? -0.86758  -27.85947 25.84780  1.000 31.60461  ? 283 PRO A N   1 
ATOM   2005 C  CA  . PRO A  1 257 ? -0.17242  -28.03669 24.56839  1.000 33.04067  ? 283 PRO A CA  1 
ATOM   2006 C  C   . PRO A  1 257 ? -1.09452  -28.64044 23.52006  1.000 36.34829  ? 283 PRO A C   1 
ATOM   2007 O  O   . PRO A  1 257 ? -2.03605  -29.37221 23.83441  1.000 37.68425  ? 283 PRO A O   1 
ATOM   2008 C  CB  . PRO A  1 257 ? 0.98110   -28.98502 24.91743  1.000 31.48845  ? 283 PRO A CB  1 
ATOM   2009 C  CG  . PRO A  1 257 ? 1.18192   -28.81203 26.38997  1.000 29.14614  ? 283 PRO A CG  1 
ATOM   2010 C  CD  . PRO A  1 257 ? -0.18388  -28.55366 26.95163  1.000 29.74682  ? 283 PRO A CD  1 
ATOM   2011 N  N   . ALA A  1 258 ? -0.80877  -28.31956 22.25527  1.000 38.05838  ? 284 ALA A N   1 
ATOM   2012 C  CA  . ALA A  1 258 ? -1.69503  -28.72076 21.16739  1.000 39.66174  ? 284 ALA A CA  1 
ATOM   2013 C  C   . ALA A  1 258 ? -1.79910  -30.23474 21.04274  1.000 40.77577  ? 284 ALA A C   1 
ATOM   2014 O  O   . ALA A  1 258 ? -2.86279  -30.75438 20.68607  1.000 42.93824  ? 284 ALA A O   1 
ATOM   2015 C  CB  . ALA A  1 258 ? -1.21471  -28.11344 19.84931  1.000 41.33590  ? 284 ALA A CB  1 
ATOM   2016 N  N   . ASP A  1 259 ? -0.71773  -30.95891 21.33246  1.000 40.70284  ? 285 ASP A N   1 
ATOM   2017 C  CA  . ASP A  1 259 ? -0.68471  -32.40881 21.18533  1.000 43.78033  ? 285 ASP A CA  1 
ATOM   2018 C  C   . ASP A  1 259 ? -0.94368  -33.13681 22.50117  1.000 42.41201  ? 285 ASP A C   1 
ATOM   2019 O  O   . ASP A  1 259 ? -0.49832  -34.27658 22.67661  1.000 41.66915  ? 285 ASP A O   1 
ATOM   2020 C  CB  . ASP A  1 259 ? 0.65114   -32.84882 20.58695  1.000 46.36497  ? 285 ASP A CB  1 
ATOM   2021 C  CG  . ASP A  1 259 ? 1.83672   -32.44723 21.44312  1.000 47.32486  ? 285 ASP A CG  1 
ATOM   2022 O  OD1 . ASP A  1 259 ? 1.65021   -31.68681 22.41714  1.000 45.67846  ? 285 ASP A OD1 1 
ATOM   2023 O  OD2 . ASP A  1 259 ? 2.96007   -32.89569 21.13904  1.000 48.48787  ? 285 ASP A OD2 1 
ATOM   2024 N  N   . ALA A  1 260 ? -1.65303  -32.49949 23.43076  1.000 40.79009  ? 286 ALA A N   1 
ATOM   2025 C  CA  . ALA A  1 260 ? -1.98149  -33.14677 24.69361  1.000 39.25384  ? 286 ALA A CA  1 
ATOM   2026 C  C   . ALA A  1 260 ? -2.89584  -34.34067 24.45166  1.000 39.94451  ? 286 ALA A C   1 
ATOM   2027 O  O   . ALA A  1 260 ? -3.88954  -34.24149 23.72605  1.000 32.92076  ? 286 ALA A O   1 
ATOM   2028 C  CB  . ALA A  1 260 ? -2.64633  -32.15005 25.64270  1.000 38.06266  ? 286 ALA A CB  1 
ATOM   2029 N  N   . LYS A  1 261 ? -2.55454  -35.47449 25.06329  1.000 39.59253  ? 287 LYS A N   1 
ATOM   2030 C  CA  . LYS A  1 261 ? -3.29774  -36.70964 24.85369  1.000 41.14803  ? 287 LYS A CA  1 
ATOM   2031 C  C   . LYS A  1 261 ? -4.43869  -36.90183 25.84268  1.000 38.63429  ? 287 LYS A C   1 
ATOM   2032 O  O   . LYS A  1 261 ? -5.37204  -37.65775 25.54855  1.000 36.16811  ? 287 LYS A O   1 
ATOM   2033 C  CB  . LYS A  1 261 ? -2.35316  -37.91322 24.93541  1.000 42.95727  ? 287 LYS A CB  1 
ATOM   2034 C  CG  . LYS A  1 261 ? -1.10922  -37.78658 24.07056  1.000 45.34024  ? 287 LYS A CG  1 
ATOM   2035 C  CD  . LYS A  1 261 ? -1.45271  -37.85847 22.59098  1.000 49.56277  ? 287 LYS A CD  1 
ATOM   2036 C  CE  . LYS A  1 261 ? -0.24586  -37.52582 21.72730  1.000 51.08271  ? 287 LYS A CE  1 
ATOM   2037 N  NZ  . LYS A  1 261 ? -0.52602  -36.40621 20.78590  1.000 51.13653  ? 287 LYS A NZ  1 
ATOM   2038 N  N   . ASN A  1 262 ? -4.39015  -36.24507 26.99590  1.000 37.35260  ? 288 ASN A N   1 
ATOM   2039 C  CA  . ASN A  1 262 ? -5.41206  -36.37402 28.03221  1.000 39.50338  ? 288 ASN A CA  1 
ATOM   2040 C  C   . ASN A  1 262 ? -6.09871  -35.02241 28.21270  1.000 41.45688  ? 288 ASN A C   1 
ATOM   2041 O  O   . ASN A  1 262 ? -5.95209  -34.36810 29.24940  1.000 39.10224  ? 288 ASN A O   1 
ATOM   2042 C  CB  . ASN A  1 262 ? -4.79422  -36.87214 29.34145  1.000 39.85138  ? 288 ASN A CB  1 
ATOM   2043 C  CG  . ASN A  1 262 ? -3.89524  -38.07575 29.14074  1.000 39.87944  ? 288 ASN A CG  1 
ATOM   2044 O  OD1 . ASN A  1 262 ? -4.36852  -39.18225 28.88037  1.000 38.54856  ? 288 ASN A OD1 1 
ATOM   2045 N  ND2 . ASN A  1 262 ? -2.58945  -37.86585 29.26330  1.000 38.11917  ? 288 ASN A ND2 1 
ATOM   2046 N  N   . LYS A  1 263 ? -6.85766  -34.60777 27.19630  1.000 42.78583  ? 289 LYS A N   1 
ATOM   2047 C  CA  . LYS A  1 263 ? -7.51592  -33.30700 27.25402  1.000 42.68311  ? 289 LYS A CA  1 
ATOM   2048 C  C   . LYS A  1 263 ? -8.67793  -33.31488 28.24056  1.000 44.11334  ? 289 LYS A C   1 
ATOM   2049 O  O   . LYS A  1 263 ? -8.92814  -32.31175 28.91784  1.000 44.79971  ? 289 LYS A O   1 
ATOM   2050 C  CB  . LYS A  1 263 ? -7.98762  -32.89866 25.85873  1.000 43.15447  ? 289 LYS A CB  1 
ATOM   2051 C  CG  . LYS A  1 263 ? -6.84898  -32.59143 24.89745  1.000 44.48621  ? 289 LYS A CG  1 
ATOM   2052 C  CD  . LYS A  1 263 ? -7.33849  -31.85665 23.66064  1.000 47.67418  ? 289 LYS A CD  1 
ATOM   2053 C  CE  . LYS A  1 263 ? -6.18188  -31.21210 22.91197  1.000 48.12318  ? 289 LYS A CE  1 
ATOM   2054 N  NZ  . LYS A  1 263 ? -5.19609  -32.21948 22.43049  1.000 48.31113  ? 289 LYS A NZ  1 
ATOM   2055 N  N   . ASP A  1 264 ? -9.39473  -34.43694 28.33922  1.000 44.43181  ? 290 ASP A N   1 
ATOM   2056 C  CA  . ASP A  1 264 ? -10.50329 -34.53621 29.28531  1.000 44.55795  ? 290 ASP A CA  1 
ATOM   2057 C  C   . ASP A  1 264 ? -10.01659 -34.36283 30.72024  1.000 41.42501  ? 290 ASP A C   1 
ATOM   2058 O  O   . ASP A  1 264 ? -10.57346 -33.56934 31.49181  1.000 41.63387  ? 290 ASP A O   1 
ATOM   2059 C  CB  . ASP A  1 264 ? -11.20844 -35.88250 29.11083  1.000 48.25700  ? 290 ASP A CB  1 
ATOM   2060 C  CG  . ASP A  1 264 ? -12.64132 -35.86115 29.60065  1.000 51.01999  ? 290 ASP A CG  1 
ATOM   2061 O  OD1 . ASP A  1 264 ? -13.54002 -35.52444 28.80131  1.000 53.20312  ? 290 ASP A OD1 1 
ATOM   2062 O  OD2 . ASP A  1 264 ? -12.86925 -36.18564 30.78491  1.000 51.43482  ? 290 ASP A OD2 1 
ATOM   2063 N  N   . GLU A  1 265 ? -8.96765  -35.10038 31.09245  1.000 38.55191  ? 291 GLU A N   1 
ATOM   2064 C  CA  . GLU A  1 265 ? -8.40844  -34.98745 32.43437  1.000 34.98920  ? 291 GLU A CA  1 
ATOM   2065 C  C   . GLU A  1 265 ? -7.81775  -33.60365 32.67970  1.000 29.37644  ? 291 GLU A C   1 
ATOM   2066 O  O   . GLU A  1 265 ? -7.90146  -33.08177 33.79860  1.000 29.28083  ? 291 GLU A O   1 
ATOM   2067 C  CB  . GLU A  1 265 ? -7.34899  -36.07199 32.64471  1.000 36.66268  ? 291 GLU A CB  1 
ATOM   2068 C  CG  . GLU A  1 265 ? -7.89260  -37.49855 32.61045  1.000 39.85891  ? 291 GLU A CG  1 
ATOM   2069 C  CD  . GLU A  1 265 ? -8.07848  -38.03809 31.19879  1.000 43.01295  ? 291 GLU A CD  1 
ATOM   2070 O  OE1 . GLU A  1 265 ? -7.90719  -37.26706 30.23109  1.000 43.69122  ? 291 GLU A OE1 1 
ATOM   2071 O  OE2 . GLU A  1 265 ? -8.39748  -39.23779 31.05805  1.000 44.56640  ? 291 GLU A OE2 1 
ATOM   2072 N  N   . ALA A  1 266 ? -7.23004  -32.99087 31.64879  1.000 27.78214  ? 292 ALA A N   1 
ATOM   2073 C  CA  . ALA A  1 266 ? -6.69727  -31.64017 31.79663  1.000 28.11171  ? 292 ALA A CA  1 
ATOM   2074 C  C   . ALA A  1 266 ? -7.80933  -30.63332 32.06693  1.000 30.27383  ? 292 ALA A C   1 
ATOM   2075 O  O   . ALA A  1 266 ? -7.65602  -29.74084 32.90973  1.000 30.64342  ? 292 ALA A O   1 
ATOM   2076 C  CB  . ALA A  1 266 ? -5.90725  -31.24901 30.54817  1.000 27.11963  ? 292 ALA A CB  1 
ATOM   2077 N  N   . TYR A  1 267 ? -8.93595  -30.75845 31.36077  1.000 29.35875  ? 293 TYR A N   1 
ATOM   2078 C  CA  . TYR A  1 267 ? -10.06886 -29.87626 31.62106  1.000 29.46314  ? 293 TYR A CA  1 
ATOM   2079 C  C   . TYR A  1 267 ? -10.63871 -30.11345 33.01322  1.000 30.14686  ? 293 TYR A C   1 
ATOM   2080 O  O   . TYR A  1 267 ? -11.05099 -29.16425 33.69213  1.000 30.78640  ? 293 TYR A O   1 
ATOM   2081 C  CB  . TYR A  1 267 ? -11.14666 -30.07183 30.55494  1.000 30.69682  ? 293 TYR A CB  1 
ATOM   2082 C  CG  . TYR A  1 267 ? -10.85123 -29.35327 29.25904  1.000 31.80209  ? 293 TYR A CG  1 
ATOM   2083 C  CD1 . TYR A  1 267 ? -10.66254 -27.97792 29.23413  1.000 31.81133  ? 293 TYR A CD1 1 
ATOM   2084 C  CD2 . TYR A  1 267 ? -10.75979 -30.04873 28.06098  1.000 32.20119  ? 293 TYR A CD2 1 
ATOM   2085 C  CE1 . TYR A  1 267 ? -10.38907 -27.31581 28.05267  1.000 33.65656  ? 293 TYR A CE1 1 
ATOM   2086 C  CE2 . TYR A  1 267 ? -10.48607 -29.39596 26.87486  1.000 33.95868  ? 293 TYR A CE2 1 
ATOM   2087 C  CZ  . TYR A  1 267 ? -10.30240 -28.02967 26.87640  1.000 35.17231  ? 293 TYR A CZ  1 
ATOM   2088 O  OH  . TYR A  1 267 ? -10.03017 -27.37464 25.69802  1.000 37.72857  ? 293 TYR A OH  1 
ATOM   2089 N  N   . GLN A  1 268 ? -10.66507 -31.37318 33.45681  1.000 30.27442  ? 294 GLN A N   1 
ATOM   2090 C  CA  . GLN A  1 268 ? -11.08998 -31.65852 34.82420  1.000 32.92510  ? 294 GLN A CA  1 
ATOM   2091 C  C   . GLN A  1 268 ? -10.18749 -30.96361 35.83741  1.000 33.30051  ? 294 GLN A C   1 
ATOM   2092 O  O   . GLN A  1 268 ? -10.67183 -30.36559 36.80596  1.000 34.75327  ? 294 GLN A O   1 
ATOM   2093 C  CB  . GLN A  1 268 ? -11.10788 -33.16686 35.06909  1.000 35.13494  ? 294 GLN A CB  1 
ATOM   2094 C  CG  . GLN A  1 268 ? -12.21485 -33.90592 34.33667  1.000 37.61779  ? 294 GLN A CG  1 
ATOM   2095 C  CD  . GLN A  1 268 ? -12.37801 -35.33262 34.82218  1.000 39.74821  ? 294 GLN A CD  1 
ATOM   2096 O  OE1 . GLN A  1 268 ? -12.29156 -36.28032 34.04171  1.000 42.25094  ? 294 GLN A OE1 1 
ATOM   2097 N  NE2 . GLN A  1 268 ? -12.61618 -35.49230 36.11895  1.000 39.04004  ? 294 GLN A NE2 1 
ATOM   2098 N  N   . PHE A  1 269 ? -8.87065  -31.02069 35.62340  1.000 32.80527  ? 295 PHE A N   1 
ATOM   2099 C  CA  . PHE A  1 269 ? -7.94458  -30.37110 36.54831  1.000 30.28555  ? 295 PHE A CA  1 
ATOM   2100 C  C   . PHE A  1 269 ? -8.09289  -28.85449 36.51510  1.000 28.29224  ? 295 PHE A C   1 
ATOM   2101 O  O   . PHE A  1 269 ? -7.98711  -28.19213 37.55395  1.000 28.31393  ? 295 PHE A O   1 
ATOM   2102 C  CB  . PHE A  1 269 ? -6.50598  -30.76961 36.22675  1.000 30.69426  ? 295 PHE A CB  1 
ATOM   2103 C  CG  . PHE A  1 269 ? -5.52079  -30.39160 37.29615  1.000 30.18890  ? 295 PHE A CG  1 
ATOM   2104 C  CD1 . PHE A  1 269 ? -5.39905  -31.15520 38.44532  1.000 30.60889  ? 295 PHE A CD1 1 
ATOM   2105 C  CD2 . PHE A  1 269 ? -4.72014  -29.27041 37.15464  1.000 29.00362  ? 295 PHE A CD2 1 
ATOM   2106 C  CE1 . PHE A  1 269 ? -4.49515  -30.80956 39.43196  1.000 29.53499  ? 295 PHE A CE1 1 
ATOM   2107 C  CE2 . PHE A  1 269 ? -3.81417  -28.91944 38.13792  1.000 29.04535  ? 295 PHE A CE2 1 
ATOM   2108 C  CZ  . PHE A  1 269 ? -3.70178  -29.69020 39.27798  1.000 29.13715  ? 295 PHE A CZ  1 
ATOM   2109 N  N   . LEU A  1 270 ? -8.32874  -28.28387 35.33218  1.000 26.88499  ? 296 LEU A N   1 
ATOM   2110 C  CA  . LEU A  1 270 ? -8.52466  -26.83972 35.24421  1.000 25.40954  ? 296 LEU A CA  1 
ATOM   2111 C  C   . LEU A  1 270 ? -9.78998  -26.41196 35.97904  1.000 26.30113  ? 296 LEU A C   1 
ATOM   2112 O  O   . LEU A  1 270 ? -9.79375  -25.39815 36.68944  1.000 25.39793  ? 296 LEU A O   1 
ATOM   2113 C  CB  . LEU A  1 270 ? -8.57318  -26.40307 33.78026  1.000 25.63772  ? 296 LEU A CB  1 
ATOM   2114 C  CG  . LEU A  1 270 ? -7.25901  -26.51913 33.00528  1.000 25.37558  ? 296 LEU A CG  1 
ATOM   2115 C  CD1 . LEU A  1 270 ? -7.46492  -26.18661 31.53465  1.000 24.85725  ? 296 LEU A CD1 1 
ATOM   2116 C  CD2 . LEU A  1 270 ? -6.19318  -25.62458 33.61965  1.000 25.46116  ? 296 LEU A CD2 1 
ATOM   2117 N  N   . ASN A  1 271 ? -10.87431 -27.17733 35.82590  1.000 28.22722  ? 297 ASN A N   1 
ATOM   2118 C  CA  . ASN A  1 271 ? -12.09342 -26.88754 36.57490  1.000 31.14645  ? 297 ASN A CA  1 
ATOM   2119 C  C   . ASN A  1 271 ? -11.86219 -27.02760 38.07384  1.000 30.59436  ? 297 ASN A C   1 
ATOM   2120 O  O   . ASN A  1 271 ? -12.41003 -26.25573 38.87029  1.000 31.67041  ? 297 ASN A O   1 
ATOM   2121 C  CB  . ASN A  1 271 ? -13.22214 -27.81096 36.11981  1.000 34.44169  ? 297 ASN A CB  1 
ATOM   2122 C  CG  . ASN A  1 271 ? -14.24482 -27.09907 35.26279  1.000 37.92987  ? 297 ASN A CG  1 
ATOM   2123 O  OD1 . ASN A  1 271 ? -14.80638 -26.07907 35.66318  1.000 38.37428  ? 297 ASN A OD1 1 
ATOM   2124 N  ND2 . ASN A  1 271 ? -14.49342 -27.63426 34.07401  1.000 40.76405  ? 297 ASN A ND2 1 
ATOM   2125 N  N   . TYR A  1 272 ? -11.05765 -28.01503 38.47530  1.000 29.08052  ? 298 TYR A N   1 
ATOM   2126 C  CA  . TYR A  1 272 ? -10.69847 -28.16124 39.88223  1.000 28.70120  ? 298 TYR A CA  1 
ATOM   2127 C  C   . TYR A  1 272 ? -9.95268  -26.93243 40.38818  1.000 28.32856  ? 298 TYR A C   1 
ATOM   2128 O  O   . TYR A  1 272 ? -10.20501 -26.45480 41.50072  1.000 26.94395  ? 298 TYR A O   1 
ATOM   2129 C  CB  . TYR A  1 272 ? -9.85475  -29.42315 40.06650  1.000 29.26861  ? 298 TYR A CB  1 
ATOM   2130 C  CG  . TYR A  1 272 ? -9.46734  -29.72379 41.49558  1.000 29.07660  ? 298 TYR A CG  1 
ATOM   2131 C  CD1 . TYR A  1 272 ? -10.37068 -30.31070 42.37155  1.000 29.47484  ? 298 TYR A CD1 1 
ATOM   2132 C  CD2 . TYR A  1 272 ? -8.19225  -29.43498 41.96463  1.000 28.90840  ? 298 TYR A CD2 1 
ATOM   2133 C  CE1 . TYR A  1 272 ? -10.01828 -30.59318 43.67743  1.000 30.26623  ? 298 TYR A CE1 1 
ATOM   2134 C  CE2 . TYR A  1 272 ? -7.83057  -29.71400 43.26837  1.000 28.81601  ? 298 TYR A CE2 1 
ATOM   2135 C  CZ  . TYR A  1 272 ? -8.74723  -30.29238 44.11975  1.000 31.60997  ? 298 TYR A CZ  1 
ATOM   2136 O  OH  . TYR A  1 272 ? -8.39126  -30.56995 45.41879  1.000 33.72083  ? 298 TYR A OH  1 
ATOM   2137 N  N   . LEU A  1 273 ? -9.02931  -26.40742 39.57973  1.000 27.66884  ? 299 LEU A N   1 
ATOM   2138 C  CA  . LEU A  1 273 ? -8.30469  -25.19850 39.95884  1.000 25.90501  ? 299 LEU A CA  1 
ATOM   2139 C  C   . LEU A  1 273 ? -9.22023  -23.98224 39.99903  1.000 28.64784  ? 299 LEU A C   1 
ATOM   2140 O  O   . LEU A  1 273 ? -8.95634  -23.03368 40.74746  1.000 29.02164  ? 299 LEU A O   1 
ATOM   2141 C  CB  . LEU A  1 273 ? -7.14678  -24.94977 38.99308  1.000 25.84293  ? 299 LEU A CB  1 
ATOM   2142 C  CG  . LEU A  1 273 ? -5.92144  -25.85166 39.13708  1.000 25.96900  ? 299 LEU A CG  1 
ATOM   2143 C  CD1 . LEU A  1 273 ? -4.86225  -25.47019 38.11556  1.000 24.85404  ? 299 LEU A CD1 1 
ATOM   2144 C  CD2 . LEU A  1 273 ? -5.36447  -25.77528 40.54989  1.000 25.99329  ? 299 LEU A CD2 1 
ATOM   2145 N  N   . LEU A  1 274 ? -10.28984 -23.98463 39.20124  1.000 29.56372  ? 300 LEU A N   1 
ATOM   2146 C  CA  . LEU A  1 274 ? -11.23382 -22.87370 39.21899  1.000 29.56210  ? 300 LEU A CA  1 
ATOM   2147 C  C   . LEU A  1 274 ? -12.09895 -22.84986 40.47309  1.000 29.85413  ? 300 LEU A C   1 
ATOM   2148 O  O   . LEU A  1 274 ? -12.78977 -21.85166 40.70483  1.000 30.83067  ? 300 LEU A O   1 
ATOM   2149 C  CB  . LEU A  1 274 ? -12.12406 -22.91958 37.97640  1.000 30.47260  ? 300 LEU A CB  1 
ATOM   2150 C  CG  . LEU A  1 274 ? -11.47599 -22.42020 36.68374  1.000 29.90654  ? 300 LEU A CG  1 
ATOM   2151 C  CD1 . LEU A  1 274 ? -12.33810 -22.76392 35.47974  1.000 31.00856  ? 300 LEU A CD1 1 
ATOM   2152 C  CD2 . LEU A  1 274 ? -11.22047 -20.92199 36.75665  1.000 29.21428  ? 300 LEU A CD2 1 
ATOM   2153 N  N   . ARG A  1 275 ? -12.08488 -23.90915 41.27483  1.000 28.90567  ? 301 ARG A N   1 
ATOM   2154 C  CA  . ARG A  1 275 ? -12.81672 -23.89710 42.53598  1.000 29.15578  ? 301 ARG A CA  1 
ATOM   2155 C  C   . ARG A  1 275 ? -12.19885 -22.86697 43.47498  1.000 24.64356  ? 301 ARG A C   1 
ATOM   2156 O  O   . ARG A  1 275 ? -10.96997 -22.81496 43.60512  1.000 25.01743  ? 301 ARG A O   1 
ATOM   2157 C  CB  . ARG A  1 275 ? -12.79712 -25.27733 43.18796  1.000 30.20447  ? 301 ARG A CB  1 
ATOM   2158 C  CG  . ARG A  1 275 ? -13.61716 -26.33295 42.46814  1.000 32.45319  ? 301 ARG A CG  1 
ATOM   2159 C  CD  . ARG A  1 275 ? -13.71708 -27.59513 43.30806  1.000 33.18065  ? 301 ARG A CD  1 
ATOM   2160 N  NE  . ARG A  1 275 ? -14.04060 -28.77130 42.50706  1.000 35.84966  ? 301 ARG A NE  1 
ATOM   2161 C  CZ  . ARG A  1 275 ? -13.94557 -30.02103 42.94883  1.000 37.39733  ? 301 ARG A CZ  1 
ATOM   2162 N  NH1 . ARG A  1 275 ? -14.26023 -31.03438 42.15363  1.000 38.64816  ? 301 ARG A NH1 1 
ATOM   2163 N  NH2 . ARG A  1 275 ? -13.53264 -30.25792 44.18663  1.000 36.08062  ? 301 ARG A NH2 1 
ATOM   2164 N  N   . PRO A  1 276 ? -13.00546 -22.03394 44.13905  1.000 26.68109  ? 302 PRO A N   1 
ATOM   2165 C  CA  . PRO A  1 276 ? -12.42226 -20.99363 45.00485  1.000 26.92588  ? 302 PRO A CA  1 
ATOM   2166 C  C   . PRO A  1 276 ? -11.56979 -21.54631 46.13473  1.000 27.91995  ? 302 PRO A C   1 
ATOM   2167 O  O   . PRO A  1 276 ? -10.47257 -21.03005 46.38380  1.000 28.34546  ? 302 PRO A O   1 
ATOM   2168 C  CB  . PRO A  1 276 ? -13.65906 -20.25142 45.53296  1.000 27.64484  ? 302 PRO A CB  1 
ATOM   2169 C  CG  . PRO A  1 276 ? -14.72312 -20.51641 44.51674  1.000 28.75559  ? 302 PRO A CG  1 
ATOM   2170 C  CD  . PRO A  1 276 ? -14.46876 -21.91168 44.03114  1.000 27.90706  ? 302 PRO A CD  1 
ATOM   2171 N  N   . ASP A  1 277 ? -12.03766 -22.59243 46.82059  1.000 28.54009  ? 303 ASP A N   1 
ATOM   2172 C  CA  . ASP A  1 277 ? -11.29206 -23.12322 47.95855  1.000 29.68503  ? 303 ASP A CA  1 
ATOM   2173 C  C   . ASP A  1 277 ? -9.95459  -23.71407 47.52617  1.000 27.63726  ? 303 ASP A C   1 
ATOM   2174 O  O   . ASP A  1 277 ? -8.94885  -23.55998 48.22829  1.000 28.39521  ? 303 ASP A O   1 
ATOM   2175 C  CB  . ASP A  1 277 ? -12.13331 -24.16619 48.69546  1.000 32.31922  ? 303 ASP A CB  1 
ATOM   2176 C  CG  . ASP A  1 277 ? -12.62784 -25.27076 47.78150  1.000 34.45626  ? 303 ASP A CG  1 
ATOM   2177 O  OD1 . ASP A  1 277 ? -12.09741 -26.39819 47.86817  1.000 34.69940  ? 303 ASP A OD1 1 
ATOM   2178 O  OD2 . ASP A  1 277 ? -13.54815 -25.01188 46.97746  1.000 35.47437  ? 303 ASP A OD2 1 
ATOM   2179 N  N   . VAL A  1 278 ? -9.91923  -24.37139 46.36458  1.000 27.57481  ? 304 VAL A N   1 
ATOM   2180 C  CA  . VAL A  1 278 ? -8.68714  -24.99600 45.88042  1.000 25.04187  ? 304 VAL A CA  1 
ATOM   2181 C  C   . VAL A  1 278 ? -7.59733  -23.94679 45.68648  1.000 22.42006  ? 304 VAL A C   1 
ATOM   2182 O  O   . VAL A  1 278 ? -6.51429  -24.01540 46.28741  1.000 23.29277  ? 304 VAL A O   1 
ATOM   2183 C  CB  . VAL A  1 278 ? -8.95682  -25.76460 44.57434  1.000 25.60942  ? 304 VAL A CB  1 
ATOM   2184 C  CG1 . VAL A  1 278 ? -7.65141  -26.23675 43.95087  1.000 26.19662  ? 304 VAL A CG1 1 
ATOM   2185 C  CG2 . VAL A  1 278 ? -9.89505  -26.93524 44.82477  1.000 28.24069  ? 304 VAL A CG2 1 
ATOM   2186 N  N   . VAL A  1 279 ? -7.87165  -22.95715 44.83583  1.000 22.11244  ? 305 VAL A N   1 
ATOM   2187 C  CA  . VAL A  1 279 ? -6.85324  -21.96637 44.51680  1.000 21.50398  ? 305 VAL A CA  1 
ATOM   2188 C  C   . VAL A  1 279 ? -6.59129  -21.05675 45.71260  1.000 22.15481  ? 305 VAL A C   1 
ATOM   2189 O  O   . VAL A  1 279 ? -5.48651  -20.52235 45.86051  1.000 22.25228  ? 305 VAL A O   1 
ATOM   2190 C  CB  . VAL A  1 279 ? -7.26069  -21.18095 43.25481  1.000 20.76394  ? 305 VAL A CB  1 
ATOM   2191 C  CG1 . VAL A  1 279 ? -8.39841  -20.22220 43.55098  1.000 20.96529  ? 305 VAL A CG1 1 
ATOM   2192 C  CG2 . VAL A  1 279 ? -6.06510  -20.45751 42.66513  1.000 20.37429  ? 305 VAL A CG2 1 
ATOM   2193 N  N   . ALA A  1 280 ? -7.57142  -20.89667 46.60762  1.000 23.32581  ? 306 ALA A N   1 
ATOM   2194 C  CA  . ALA A  1 280 ? -7.32467  -20.14081 47.83200  1.000 23.99858  ? 306 ALA A CA  1 
ATOM   2195 C  C   . ALA A  1 280 ? -6.33474  -20.86556 48.73730  1.000 23.37209  ? 306 ALA A C   1 
ATOM   2196 O  O   . ALA A  1 280 ? -5.44295  -20.23809 49.31855  1.000 23.61373  ? 306 ALA A O   1 
ATOM   2197 C  CB  . ALA A  1 280 ? -8.64002  -19.88398 48.56588  1.000 25.12012  ? 306 ALA A CB  1 
ATOM   2198 N  N   . HIS A  1 281 ? -6.47753  -22.18690 48.86892  1.000 23.98046  ? 307 HIS A N   1 
ATOM   2199 C  CA  . HIS A  1 281 ? -5.49989  -22.98096 49.60824  1.000 25.44908  ? 307 HIS A CA  1 
ATOM   2200 C  C   . HIS A  1 281 ? -4.11853  -22.88219 48.96899  1.000 24.69522  ? 307 HIS A C   1 
ATOM   2201 O  O   . HIS A  1 281 ? -3.10034  -22.73903 49.66703  1.000 25.13648  ? 307 HIS A O   1 
ATOM   2202 C  CB  . HIS A  1 281 ? -5.97706  -24.43375 49.66463  1.000 29.06172  ? 307 HIS A CB  1 
ATOM   2203 C  CG  . HIS A  1 281 ? -5.10485  -25.33786 50.47754  1.000 32.90606  ? 307 HIS A CG  1 
ATOM   2204 N  ND1 . HIS A  1 281 ? -4.78590  -25.08276 51.79374  1.000 34.37119  ? 307 HIS A ND1 1 
ATOM   2205 C  CD2 . HIS A  1 281 ? -4.50248  -26.50959 50.16468  1.000 33.56936  ? 307 HIS A CD2 1 
ATOM   2206 C  CE1 . HIS A  1 281 ? -4.01569  -26.05300 52.25337  1.000 34.69550  ? 307 HIS A CE1 1 
ATOM   2207 N  NE2 . HIS A  1 281 ? -3.82737  -26.93054 51.28426  1.000 33.58981  ? 307 HIS A NE2 1 
ATOM   2208 N  N   . ILE A  1 282 ? -4.06693  -22.94549 47.63624  1.000 23.40365  ? 308 ILE A N   1 
ATOM   2209 C  CA  . ILE A  1 282 ? -2.78761  -22.81097 46.94097  1.000 21.23744  ? 308 ILE A CA  1 
ATOM   2210 C  C   . ILE A  1 282 ? -2.14858  -21.46257 47.25683  1.000 20.86271  ? 308 ILE A C   1 
ATOM   2211 O  O   . ILE A  1 282 ? -0.94595  -21.37488 47.52916  1.000 21.40074  ? 308 ILE A O   1 
ATOM   2212 C  CB  . ILE A  1 282 ? -2.96758  -23.00438 45.42560  1.000 19.00060  ? 308 ILE A CB  1 
ATOM   2213 C  CG1 . ILE A  1 282 ? -3.48490  -24.40991 45.12023  1.000 19.67244  ? 308 ILE A CG1 1 
ATOM   2214 C  CG2 . ILE A  1 282 ? -1.65036  -22.76175 44.70799  1.000 18.22504  ? 308 ILE A CG2 1 
ATOM   2215 C  CD1 . ILE A  1 282 ? -3.62160  -24.69243 43.64065  1.000 19.57890  ? 308 ILE A CD1 1 
ATOM   2216 N  N   . SER A  1 283 ? -2.94461  -20.39055 47.21923  1.000 20.82485  ? 309 SER A N   1 
ATOM   2217 C  CA  . SER A  1 283 ? -2.41945  -19.06291 47.52663  1.000 20.20026  ? 309 SER A CA  1 
ATOM   2218 C  C   . SER A  1 283 ? -1.96508  -18.97058 48.97749  1.000 21.77360  ? 309 SER A C   1 
ATOM   2219 O  O   . SER A  1 283 ? -0.97884  -18.29019 49.28599  1.000 20.27088  ? 309 SER A O   1 
ATOM   2220 C  CB  . SER A  1 283 ? -3.47497  -17.99844 47.22787  1.000 20.37289  ? 309 SER A CB  1 
ATOM   2221 O  OG  . SER A  1 283 ? -3.47974  -17.65618 45.85277  1.000 20.73787  ? 309 SER A OG  1 
ATOM   2222 N  N   . ASP A  1 284 ? -2.68131  -19.63993 49.88361  1.000 23.17137  ? 310 ASP A N   1 
ATOM   2223 C  CA  . ASP A  1 284 ? -2.25648  -19.68663 51.27806  1.000 27.13467  ? 310 ASP A CA  1 
ATOM   2224 C  C   . ASP A  1 284 ? -0.88126  -20.32415 51.40628  1.000 30.17177  ? 310 ASP A C   1 
ATOM   2225 O  O   . ASP A  1 284 ? -0.07398  -19.91640 52.24990  1.000 31.15607  ? 310 ASP A O   1 
ATOM   2226 C  CB  . ASP A  1 284 ? -3.27708  -20.45732 52.11625  1.000 28.09199  ? 310 ASP A CB  1 
ATOM   2227 C  CG  . ASP A  1 284 ? -4.58830  -19.71667 52.26529  1.000 29.68591  ? 310 ASP A CG  1 
ATOM   2228 O  OD1 . ASP A  1 284 ? -4.59907  -18.48210 52.08152  1.000 30.33481  ? 310 ASP A OD1 1 
ATOM   2229 O  OD2 . ASP A  1 284 ? -5.60854  -20.37029 52.56743  1.000 32.89388  ? 310 ASP A OD2 1 
ATOM   2230 N  N   . HIS A  1 285 ? -0.59758  -21.33200 50.57987  1.000 30.80859  ? 311 HIS A N   1 
ATOM   2231 C  CA  . HIS A  1 285 ? 0.71118   -21.97702 50.66850  1.000 30.94809  ? 311 HIS A CA  1 
ATOM   2232 C  C   . HIS A  1 285 ? 1.80696   -21.15092 49.99535  1.000 28.70676  ? 311 HIS A C   1 
ATOM   2233 O  O   . HIS A  1 285 ? 2.87246   -20.92900 50.58132  1.000 27.78019  ? 311 HIS A O   1 
ATOM   2234 C  CB  . HIS A  1 285 ? 0.66826   -23.37858 50.06141  1.000 35.61189  ? 311 HIS A CB  1 
ATOM   2235 C  CG  . HIS A  1 285 ? 2.00070   -24.06169 50.05037  1.000 39.40183  ? 311 HIS A CG  1 
ATOM   2236 N  ND1 . HIS A  1 285 ? 2.59038   -24.55926 51.19269  1.000 41.04267  ? 311 HIS A ND1 1 
ATOM   2237 C  CD2 . HIS A  1 285 ? 2.86677   -24.31317 49.04027  1.000 39.61657  ? 311 HIS A CD2 1 
ATOM   2238 C  CE1 . HIS A  1 285 ? 3.75797   -25.09556 50.88560  1.000 40.83242  ? 311 HIS A CE1 1 
ATOM   2239 N  NE2 . HIS A  1 285 ? 3.94936   -24.95995 49.58570  1.000 40.54603  ? 311 HIS A NE2 1 
ATOM   2240 N  N   . VAL A  1 286 ? 1.56860   -20.69090 48.76160  1.000 26.84051  ? 312 VAL A N   1 
ATOM   2241 C  CA  . VAL A  1 286 ? 2.63187   -20.08825 47.95584  1.000 24.02534  ? 312 VAL A CA  1 
ATOM   2242 C  C   . VAL A  1 286 ? 2.78773   -18.58862 48.16779  1.000 23.40414  ? 312 VAL A C   1 
ATOM   2243 O  O   . VAL A  1 286 ? 3.76596   -18.00681 47.67201  1.000 19.96266  ? 312 VAL A O   1 
ATOM   2244 C  CB  . VAL A  1 286 ? 2.40744   -20.35056 46.45258  1.000 23.27509  ? 312 VAL A CB  1 
ATOM   2245 C  CG1 . VAL A  1 286 ? 2.21035   -21.83748 46.19526  1.000 22.06635  ? 312 VAL A CG1 1 
ATOM   2246 C  CG2 . VAL A  1 286 ? 1.22041   -19.54744 45.94020  1.000 23.33521  ? 312 VAL A CG2 1 
ATOM   2247 N  N   . PHE A  1 287 ? 1.85951   -17.94425 48.87821  1.000 24.77528  ? 313 PHE A N   1 
ATOM   2248 C  CA  . PHE A  1 287 ? 1.92994   -16.50824 49.16552  1.000 25.92208  ? 313 PHE A CA  1 
ATOM   2249 C  C   . PHE A  1 287 ? 1.94042   -15.67611 47.88370  1.000 24.29046  ? 313 PHE A C   1 
ATOM   2250 O  O   . PHE A  1 287 ? 2.66740   -14.68687 47.76580  1.000 22.93128  ? 313 PHE A O   1 
ATOM   2251 C  CB  . PHE A  1 287 ? 3.13783   -16.17562 50.04501  1.000 29.19328  ? 313 PHE A CB  1 
ATOM   2252 C  CG  . PHE A  1 287 ? 2.91238   -16.44521 51.50404  1.000 34.07516  ? 313 PHE A CG  1 
ATOM   2253 C  CD1 . PHE A  1 287 ? 2.52158   -15.42723 52.35775  1.000 34.95126  ? 313 PHE A CD1 1 
ATOM   2254 C  CD2 . PHE A  1 287 ? 3.08258   -17.71896 52.02086  1.000 36.40985  ? 313 PHE A CD2 1 
ATOM   2255 C  CE1 . PHE A  1 287 ? 2.30962   -15.67331 53.70118  1.000 36.18332  ? 313 PHE A CE1 1 
ATOM   2256 C  CE2 . PHE A  1 287 ? 2.87222   -17.97166 53.36324  1.000 36.71592  ? 313 PHE A CE2 1 
ATOM   2257 C  CZ  . PHE A  1 287 ? 2.48508   -16.94732 54.20423  1.000 37.34517  ? 313 PHE A CZ  1 
ATOM   2258 N  N   . TYR A  1 288 ? 1.12688   -16.08539 46.91461  1.000 24.42531  ? 314 TYR A N   1 
ATOM   2259 C  CA  . TYR A  1 288 ? 0.87218   -15.31785 45.70617  1.000 21.99721  ? 314 TYR A CA  1 
ATOM   2260 C  C   . TYR A  1 288 ? -0.62375  -15.07053 45.58104  1.000 19.11490  ? 314 TYR A C   1 
ATOM   2261 O  O   . TYR A  1 288 ? -1.44031  -15.91755 45.95359  1.000 19.97369  ? 314 TYR A O   1 
ATOM   2262 C  CB  . TYR A  1 288 ? 1.36768   -16.04631 44.44906  1.000 28.15927  ? 314 TYR A CB  1 
ATOM   2263 C  CG  . TYR A  1 288 ? 2.84581   -15.90520 44.16430  1.000 33.97422  ? 314 TYR A CG  1 
ATOM   2264 C  CD1 . TYR A  1 288 ? 3.30948   -14.97663 43.24068  1.000 36.30510  ? 314 TYR A CD1 1 
ATOM   2265 C  CD2 . TYR A  1 288 ? 3.77525   -16.71717 44.79955  1.000 35.27539  ? 314 TYR A CD2 1 
ATOM   2266 C  CE1 . TYR A  1 288 ? 4.65990   -14.85120 42.96957  1.000 38.05908  ? 314 TYR A CE1 1 
ATOM   2267 C  CE2 . TYR A  1 288 ? 5.12596   -16.59967 44.53527  1.000 37.14412  ? 314 TYR A CE2 1 
ATOM   2268 C  CZ  . TYR A  1 288 ? 5.56301   -15.66554 43.62012  1.000 38.87411  ? 314 TYR A CZ  1 
ATOM   2269 O  OH  . TYR A  1 288 ? 6.90849   -15.54752 43.35564  1.000 39.67419  ? 314 TYR A OH  1 
ATOM   2270 N  N   . ALA A  1 289 ? -0.98232  -13.90504 45.05435  1.000 16.13081  ? 315 ALA A N   1 
ATOM   2271 C  CA  . ALA A  1 289 ? -2.38105  -13.64176 44.75546  1.000 16.63964  ? 315 ALA A CA  1 
ATOM   2272 C  C   . ALA A  1 289 ? -2.80038  -14.41878 43.51545  1.000 17.88504  ? 315 ALA A C   1 
ATOM   2273 O  O   . ALA A  1 289 ? -2.07991  -14.45805 42.51425  1.000 16.88589  ? 315 ALA A O   1 
ATOM   2274 C  CB  . ALA A  1 289 ? -2.61670  -12.14717 44.54663  1.000 17.74381  ? 315 ALA A CB  1 
ATOM   2275 N  N   . ASN A  1 290 ? -3.96353  -15.05405 43.59002  1.000 20.17459  ? 316 ASN A N   1 
ATOM   2276 C  CA  . ASN A  1 290 ? -4.50114  -15.76602 42.44371  1.000 21.61308  ? 316 ASN A CA  1 
ATOM   2277 C  C   . ASN A  1 290 ? -5.46950  -14.87116 41.67475  1.000 21.93678  ? 316 ASN A C   1 
ATOM   2278 O  O   . ASN A  1 290 ? -5.84609  -13.78595 42.12193  1.000 23.06908  ? 316 ASN A O   1 
ATOM   2279 C  CB  . ASN A  1 290 ? -5.18574  -17.06047 42.88361  1.000 18.25173  ? 316 ASN A CB  1 
ATOM   2280 C  CG  . ASN A  1 290 ? -6.36934  -16.81859 43.79924  1.000 18.99710  ? 316 ASN A CG  1 
ATOM   2281 O  OD1 . ASN A  1 290 ? -7.44975  -16.43884 43.34916  1.000 20.61505  ? 316 ASN A OD1 1 
ATOM   2282 N  ND2 . ASN A  1 290 ? -6.17416  -17.05015 45.09264  1.000 19.11443  ? 316 ASN A ND2 1 
ATOM   2283 N  N   . ALA A  1 291 ? -5.87136  -15.34047 40.49664  1.000 20.09793  ? 317 ALA A N   1 
ATOM   2284 C  CA  . ALA A  1 291 ? -6.75103  -14.58328 39.61806  1.000 20.29356  ? 317 ALA A CA  1 
ATOM   2285 C  C   . ALA A  1 291 ? -8.22268  -14.93088 39.80571  1.000 21.44840  ? 317 ALA A C   1 
ATOM   2286 O  O   . ALA A  1 291 ? -9.04727  -14.55102 38.96821  1.000 21.76663  ? 317 ALA A O   1 
ATOM   2287 C  CB  . ALA A  1 291 ? -6.34837  -14.80013 38.15772  1.000 21.77157  ? 317 ALA A CB  1 
ATOM   2288 N  N   . ASN A  1 292 ? -8.57022  -15.63450 40.88027  1.000 22.83278  ? 318 ASN A N   1 
ATOM   2289 C  CA  . ASN A  1 292 ? -9.94332  -16.05084 41.14433  1.000 25.61194  ? 318 ASN A CA  1 
ATOM   2290 C  C   . ASN A  1 292 ? -10.55707 -15.08454 42.15215  1.000 27.93373  ? 318 ASN A C   1 
ATOM   2291 O  O   . ASN A  1 292 ? -10.15829 -15.06013 43.32138  1.000 26.94995  ? 318 ASN A O   1 
ATOM   2292 C  CB  . ASN A  1 292 ? -9.97993  -17.48842 41.65921  1.000 24.90949  ? 318 ASN A CB  1 
ATOM   2293 C  CG  . ASN A  1 292 ? -11.36185 -18.10423 41.57804  1.000 25.21943  ? 318 ASN A CG  1 
ATOM   2294 O  OD1 . ASN A  1 292 ? -12.32743 -17.56816 42.12067  1.000 23.48603  ? 318 ASN A OD1 1 
ATOM   2295 N  ND2 . ASN A  1 292 ? -11.46311 -19.23922 40.89509  1.000 25.41017  ? 318 ASN A ND2 1 
ATOM   2296 N  N   . LYS A  1 293 ? -11.52805 -14.28968 41.69553  1.000 29.75822  ? 319 LYS A N   1 
ATOM   2297 C  CA  . LYS A  1 293 ? -12.16996 -13.31722 42.57512  1.000 31.55522  ? 319 LYS A CA  1 
ATOM   2298 C  C   . LYS A  1 293 ? -12.95710 -14.00946 43.68132  1.000 32.32850  ? 319 LYS A C   1 
ATOM   2299 O  O   . LYS A  1 293 ? -12.83716 -13.65178 44.85980  1.000 32.80821  ? 319 LYS A O   1 
ATOM   2300 C  CB  . LYS A  1 293 ? -13.07944 -12.39602 41.76150  1.000 34.57529  ? 319 LYS A CB  1 
ATOM   2301 C  CG  . LYS A  1 293 ? -13.85683 -11.39205 42.59896  1.000 39.04701  ? 319 LYS A CG  1 
ATOM   2302 C  CD  . LYS A  1 293 ? -14.10777 -10.10491 41.82953  1.000 42.30441  ? 319 LYS A CD  1 
ATOM   2303 C  CE  . LYS A  1 293 ? -14.43143 -8.95408  42.76894  1.000 44.75062  ? 319 LYS A CE  1 
ATOM   2304 N  NZ  . LYS A  1 293 ? -14.05529 -7.63713  42.18369  1.000 45.31132  ? 319 LYS A NZ  1 
ATOM   2305 N  N   . ALA A  1 294 ? -13.76191 -15.01322 43.31983  1.000 32.61047  ? 320 ALA A N   1 
ATOM   2306 C  CA  . ALA A  1 294 ? -14.57130 -15.72338 44.30433  1.000 34.39317  ? 320 ALA A CA  1 
ATOM   2307 C  C   . ALA A  1 294 ? -13.72713 -16.37519 45.39077  1.000 32.29790  ? 320 ALA A C   1 
ATOM   2308 O  O   . ALA A  1 294 ? -14.24072 -16.64309 46.48248  1.000 32.04151  ? 320 ALA A O   1 
ATOM   2309 C  CB  . ALA A  1 294 ? -15.43207 -16.78141 43.61156  1.000 35.73300  ? 320 ALA A CB  1 
ATOM   2310 N  N   . ALA A  1 295 ? -12.44635 -16.63044 45.12027  1.000 29.85438  ? 321 ALA A N   1 
ATOM   2311 C  CA  . ALA A  1 295 ? -11.56986 -17.24551 46.10691  1.000 28.63534  ? 321 ALA A CA  1 
ATOM   2312 C  C   . ALA A  1 295 ? -11.00433 -16.24614 47.10478  1.000 28.79527  ? 321 ALA A C   1 
ATOM   2313 O  O   . ALA A  1 295 ? -10.48578 -16.66462 48.14564  1.000 30.04763  ? 321 ALA A O   1 
ATOM   2314 C  CB  . ALA A  1 295 ? -10.41580 -17.96437 45.40904  1.000 25.96067  ? 321 ALA A CB  1 
ATOM   2315 N  N   . THR A  1 296 ? -11.09186 -14.94647 46.81340  1.000 27.59558  ? 322 THR A N   1 
ATOM   2316 C  CA  . THR A  1 296 ? -10.45446 -13.94699 47.67030  1.000 28.07454  ? 322 THR A CA  1 
ATOM   2317 C  C   . THR A  1 296 ? -10.91105 -14.01725 49.12426  1.000 30.12140  ? 322 THR A C   1 
ATOM   2318 O  O   . THR A  1 296 ? -10.04268 -14.03014 50.01424  1.000 30.12831  ? 322 THR A O   1 
ATOM   2319 C  CB  . THR A  1 296 ? -10.67117 -12.54830 47.08060  1.000 25.84690  ? 322 THR A CB  1 
ATOM   2320 O  OG1 . THR A  1 296 ? -9.96465  -12.43870 45.83928  1.000 23.77767  ? 322 THR A OG1 1 
ATOM   2321 C  CG2 . THR A  1 296 ? -10.16407 -11.48017 48.03831  1.000 25.34425  ? 322 THR A CG2 1 
ATOM   2322 N  N   . PRO A  1 297 ? -12.20973 -14.07342 49.44870  1.000 30.35554  ? 323 PRO A N   1 
ATOM   2323 C  CA  . PRO A  1 297 ? -12.59078 -14.15331 50.87007  1.000 29.77078  ? 323 PRO A CA  1 
ATOM   2324 C  C   . PRO A  1 297 ? -12.13921 -15.43436 51.54846  1.000 28.82977  ? 323 PRO A C   1 
ATOM   2325 O  O   . PRO A  1 297 ? -12.05408 -15.46770 52.78263  1.000 27.53553  ? 323 PRO A O   1 
ATOM   2326 C  CB  . PRO A  1 297 ? -14.12359 -14.05069 50.83626  1.000 32.63186  ? 323 PRO A CB  1 
ATOM   2327 C  CG  . PRO A  1 297 ? -14.45324 -13.50058 49.48932  1.000 33.47370  ? 323 PRO A CG  1 
ATOM   2328 C  CD  . PRO A  1 297 ? -13.40052 -14.03744 48.58084  1.000 30.96736  ? 323 PRO A CD  1 
ATOM   2329 N  N   . LEU A  1 298 ? -11.84549 -16.48653 50.78684  1.000 28.17416  ? 324 LEU A N   1 
ATOM   2330 C  CA  . LEU A  1 298 ? -11.40183 -17.75385 51.35021  1.000 26.13990  ? 324 LEU A CA  1 
ATOM   2331 C  C   . LEU A  1 298 ? -9.90213  -17.79330 51.61387  1.000 26.27042  ? 324 LEU A C   1 
ATOM   2332 O  O   . LEU A  1 298 ? -9.43768  -18.68733 52.33032  1.000 28.06759  ? 324 LEU A O   1 
ATOM   2333 C  CB  . LEU A  1 298 ? -11.78860 -18.90968 50.41846  1.000 25.53272  ? 324 LEU A CB  1 
ATOM   2334 C  CG  . LEU A  1 298 ? -13.15484 -19.57463 50.62710  1.000 30.76349  ? 324 LEU A CG  1 
ATOM   2335 C  CD1 . LEU A  1 298 ? -14.27831 -18.55201 50.73787  1.000 31.33471  ? 324 LEU A CD1 1 
ATOM   2336 C  CD2 . LEU A  1 298 ? -13.44629 -20.56158 49.50732  1.000 32.10589  ? 324 LEU A CD2 1 
ATOM   2337 N  N   . VAL A  1 299 ? -9.13851  -16.85515 51.05079  1.000 24.76989  ? 325 VAL A N   1 
ATOM   2338 C  CA  . VAL A  1 299 ? -7.70631  -16.79509 51.30760  1.000 25.87442  ? 325 VAL A CA  1 
ATOM   2339 C  C   . VAL A  1 299 ? -7.46715  -16.42070 52.76644  1.000 28.09463  ? 325 VAL A C   1 
ATOM   2340 O  O   . VAL A  1 299 ? -8.23884  -15.66593 53.37446  1.000 29.04298  ? 325 VAL A O   1 
ATOM   2341 C  CB  . VAL A  1 299 ? -7.03705  -15.79230 50.34782  1.000 25.84134  ? 325 VAL A CB  1 
ATOM   2342 C  CG1 . VAL A  1 299 ? -5.53897  -15.69119 50.60687  1.000 25.29975  ? 325 VAL A CG1 1 
ATOM   2343 C  CG2 . VAL A  1 299 ? -7.30431  -16.18460 48.90066  1.000 20.87039  ? 325 VAL A CG2 1 
ATOM   2344 N  N   . SER A  1 300 ? -6.39838  -16.97371 53.34160  1.000 27.84158  ? 326 SER A N   1 
ATOM   2345 C  CA  . SER A  1 300 ? -6.03625  -16.67249 54.71994  1.000 28.96603  ? 326 SER A CA  1 
ATOM   2346 C  C   . SER A  1 300 ? -5.88750  -15.17025 54.92362  1.000 30.33056  ? 326 SER A C   1 
ATOM   2347 O  O   . SER A  1 300 ? -5.46898  -14.43729 54.02294  1.000 32.69681  ? 326 SER A O   1 
ATOM   2348 C  CB  . SER A  1 300 ? -4.73005  -17.37712 55.09075  1.000 30.32649  ? 326 SER A CB  1 
ATOM   2349 O  OG  . SER A  1 300 ? -3.60809  -16.62008 54.66630  1.000 32.77415  ? 326 SER A OG  1 
ATOM   2350 N  N   . ALA A  1 301 ? -6.24481  -14.71145 56.12659  1.000 31.37833  ? 327 ALA A N   1 
ATOM   2351 C  CA  . ALA A  1 301 ? -6.08775  -13.30192 56.46601  1.000 32.95768  ? 327 ALA A CA  1 
ATOM   2352 C  C   . ALA A  1 301 ? -4.63143  -12.86232 56.41839  1.000 33.04674  ? 327 ALA A C   1 
ATOM   2353 O  O   . ALA A  1 301 ? -4.35844  -11.67234 56.22623  1.000 32.69585  ? 327 ALA A O   1 
ATOM   2354 C  CB  . ALA A  1 301 ? -6.67216  -13.02480 57.85168  1.000 35.18280  ? 327 ALA A CB  1 
ATOM   2355 N  N   . GLU A  1 302 ? -3.69255  -13.79613 56.58839  1.000 33.54021  ? 328 GLU A N   1 
ATOM   2356 C  CA  . GLU A  1 302 ? -2.27737  -13.45561 56.48666  1.000 34.67287  ? 328 GLU A CA  1 
ATOM   2357 C  C   . GLU A  1 302 ? -1.91897  -13.00044 55.07698  1.000 29.75511  ? 328 GLU A C   1 
ATOM   2358 O  O   . GLU A  1 302 ? -1.13363  -12.06166 54.89918  1.000 29.63043  ? 328 GLU A O   1 
ATOM   2359 C  CB  . GLU A  1 302 ? -1.42565  -14.65617 56.89800  1.000 39.22852  ? 328 GLU A CB  1 
ATOM   2360 C  CG  . GLU A  1 302 ? 0.06211   -14.37302 57.00436  1.000 43.11766  ? 328 GLU A CG  1 
ATOM   2361 C  CD  . GLU A  1 302 ? 0.87018   -15.63379 57.24680  1.000 47.90052  ? 328 GLU A CD  1 
ATOM   2362 O  OE1 . GLU A  1 302 ? 0.30963   -16.73835 57.08268  1.000 49.17501  ? 328 GLU A OE1 1 
ATOM   2363 O  OE2 . GLU A  1 302 ? 2.06235   -15.52258 57.60331  1.000 50.21554  ? 328 GLU A OE2 1 
ATOM   2364 N  N   . VAL A  1 303 ? -2.49013  -13.64695 54.06448  1.000 27.48687  ? 329 VAL A N   1 
ATOM   2365 C  CA  . VAL A  1 303 ? -2.20301  -13.29845 52.67611  1.000 24.70576  ? 329 VAL A CA  1 
ATOM   2366 C  C   . VAL A  1 303 ? -3.22320  -12.30887 52.12606  1.000 24.14707  ? 329 VAL A C   1 
ATOM   2367 O  O   . VAL A  1 303 ? -2.86038  -11.36666 51.41777  1.000 22.42823  ? 329 VAL A O   1 
ATOM   2368 C  CB  . VAL A  1 303 ? -2.14323  -14.57902 51.81861  1.000 26.28548  ? 329 VAL A CB  1 
ATOM   2369 C  CG1 . VAL A  1 303 ? -1.89240  -14.23360 50.35660  1.000 24.85651  ? 329 VAL A CG1 1 
ATOM   2370 C  CG2 . VAL A  1 303 ? -1.07182  -15.52140 52.34331  1.000 27.41241  ? 329 VAL A CG2 1 
ATOM   2371 N  N   . ARG A  1 304 ? -4.50474  -12.50207 52.44890  1.000 25.90964  ? 330 ARG A N   1 
ATOM   2372 C  CA  . ARG A  1 304 ? -5.55310  -11.66127 51.87731  1.000 25.73861  ? 330 ARG A CA  1 
ATOM   2373 C  C   . ARG A  1 304 ? -5.41941  -10.21098 52.32881  1.000 25.92191  ? 330 ARG A C   1 
ATOM   2374 O  O   . ARG A  1 304 ? -5.65444  -9.28478  51.54321  1.000 25.17929  ? 330 ARG A O   1 
ATOM   2375 C  CB  . ARG A  1 304 ? -6.92770  -12.21891 52.25179  1.000 26.73275  ? 330 ARG A CB  1 
ATOM   2376 C  CG  . ARG A  1 304 ? -8.06916  -11.22260 52.13144  1.000 31.08134  ? 330 ARG A CG  1 
ATOM   2377 C  CD  . ARG A  1 304 ? -9.42111  -11.89442 52.32206  1.000 35.21197  ? 330 ARG A CD  1 
ATOM   2378 N  NE  . ARG A  1 304 ? -9.37043  -12.97195 53.30625  1.000 36.70657  ? 330 ARG A NE  1 
ATOM   2379 C  CZ  . ARG A  1 304 ? -9.51777  -12.79676 54.61537  1.000 37.88009  ? 330 ARG A CZ  1 
ATOM   2380 N  NH1 . ARG A  1 304 ? -9.72661  -11.58227 55.10474  1.000 38.56366  ? 330 ARG A NH1 1 
ATOM   2381 N  NH2 . ARG A  1 304 ? -9.45723  -13.83656 55.43626  1.000 38.67891  ? 330 ARG A NH2 1 
ATOM   2382 N  N   . GLU A  1 305 ? -5.03544  -9.99109  53.58327  1.000 25.95513  ? 331 GLU A N   1 
ATOM   2383 C  CA  . GLU A  1 305 ? -4.94994  -8.64566  54.13495  1.000 29.53821  ? 331 GLU A CA  1 
ATOM   2384 C  C   . GLU A  1 305 ? -3.58158  -8.00323  53.94310  1.000 27.55547  ? 331 GLU A C   1 
ATOM   2385 O  O   . GLU A  1 305 ? -3.36295  -6.89171  54.43488  1.000 27.26434  ? 331 GLU A O   1 
ATOM   2386 C  CB  . GLU A  1 305 ? -5.31320  -8.66564  55.62246  1.000 35.32921  ? 331 GLU A CB  1 
ATOM   2387 C  CG  . GLU A  1 305 ? -6.75742  -9.06313  55.88674  1.000 41.35570  ? 331 GLU A CG  1 
ATOM   2388 C  CD  . GLU A  1 305 ? -7.15897  -8.88425  57.33561  1.000 47.64503  ? 331 GLU A CD  1 
ATOM   2389 O  OE1 . GLU A  1 305 ? -6.29347  -9.05563  58.21928  1.000 49.72827  ? 331 GLU A OE1 1 
ATOM   2390 O  OE2 . GLU A  1 305 ? -8.34096  -8.57052  57.59062  1.000 50.97888  ? 331 GLU A OE2 1 
ATOM   2391 N  N   . ASN A  1 306 ? -2.66223  -8.66728  53.24601  1.000 24.69286  ? 332 ASN A N   1 
ATOM   2392 C  CA  . ASN A  1 306 ? -1.37292  -8.07902  52.90617  1.000 24.25854  ? 332 ASN A CA  1 
ATOM   2393 C  C   . ASN A  1 306 ? -1.54591  -7.18228  51.68573  1.000 24.71971  ? 332 ASN A C   1 
ATOM   2394 O  O   . ASN A  1 306 ? -1.78115  -7.68310  50.57856  1.000 22.55181  ? 332 ASN A O   1 
ATOM   2395 C  CB  . ASN A  1 306 ? -0.33489  -9.17289  52.63773  1.000 24.61712  ? 332 ASN A CB  1 
ATOM   2396 C  CG  . ASN A  1 306 ? 1.08689   -8.63564  52.56176  1.000 25.44048  ? 332 ASN A CG  1 
ATOM   2397 O  OD1 . ASN A  1 306 ? 1.31469   -7.47686  52.21189  1.000 26.22136  ? 332 ASN A OD1 1 
ATOM   2398 N  ND2 . ASN A  1 306 ? 2.05344   -9.48601  52.88778  1.000 25.05388  ? 332 ASN A ND2 1 
ATOM   2399 N  N   . PRO A  1 307 ? -1.43876  -5.85990  51.84077  1.000 26.27786  ? 333 PRO A N   1 
ATOM   2400 C  CA  . PRO A  1 307 ? -1.63138  -4.97166  50.68291  1.000 25.85516  ? 333 PRO A CA  1 
ATOM   2401 C  C   . PRO A  1 307 ? -0.57261  -5.14154  49.61022  1.000 25.13211  ? 333 PRO A C   1 
ATOM   2402 O  O   . PRO A  1 307 ? -0.82401  -4.78574  48.45234  1.000 24.31527  ? 333 PRO A O   1 
ATOM   2403 C  CB  . PRO A  1 307 ? -1.58478  -3.56930  51.30451  1.000 27.10907  ? 333 PRO A CB  1 
ATOM   2404 C  CG  . PRO A  1 307 ? -0.77011  -3.73836  52.54124  1.000 27.55240  ? 333 PRO A CG  1 
ATOM   2405 C  CD  . PRO A  1 307 ? -1.09247  -5.11240  53.06195  1.000 27.97066  ? 333 PRO A CD  1 
ATOM   2406 N  N   . GLY A  1 308 ? 0.60050   -5.66958  49.95484  1.000 26.15142  ? 334 GLY A N   1 
ATOM   2407 C  CA  . GLY A  1 308 ? 1.62745   -5.98384  48.98512  1.000 24.41019  ? 334 GLY A CA  1 
ATOM   2408 C  C   . GLY A  1 308 ? 1.39221   -7.24678  48.19299  1.000 25.28492  ? 334 GLY A C   1 
ATOM   2409 O  O   . GLY A  1 308 ? 2.16290   -7.55131  47.27861  1.000 26.00155  ? 334 GLY A O   1 
ATOM   2410 N  N   . ILE A  1 309 ? 0.34594   -8.00288  48.52776  1.000 26.26329  ? 335 ILE A N   1 
ATOM   2411 C  CA  . ILE A  1 309 ? -0.05678  -9.18874  47.78255  1.000 25.74870  ? 335 ILE A CA  1 
ATOM   2412 C  C   . ILE A  1 309 ? -1.44432  -9.01491  47.17579  1.000 26.93176  ? 335 ILE A C   1 
ATOM   2413 O  O   . ILE A  1 309 ? -1.64679  -9.24937  45.98064  1.000 25.23566  ? 335 ILE A O   1 
ATOM   2414 C  CB  . ILE A  1 309 ? -0.00277  -10.45521 48.66651  1.000 24.50891  ? 335 ILE A CB  1 
ATOM   2415 C  CG1 . ILE A  1 309 ? 1.37722   -10.59820 49.31166  1.000 23.73716  ? 335 ILE A CG1 1 
ATOM   2416 C  CG2 . ILE A  1 309 ? -0.34640  -11.69378 47.85083  1.000 21.38782  ? 335 ILE A CG2 1 
ATOM   2417 C  CD1 . ILE A  1 309 ? 1.50054   -11.79429 50.23005  1.000 22.18721  ? 335 ILE A CD1 1 
ATOM   2418 N  N   . TYR A  1 310 ? -2.41570  -8.59707  47.98911  1.000 27.31885  ? 336 TYR A N   1 
ATOM   2419 C  CA  . TYR A  1 310 ? -3.77109  -8.30770  47.52938  1.000 25.16036  ? 336 TYR A CA  1 
ATOM   2420 C  C   . TYR A  1 310 ? -4.02357  -6.81245  47.66985  1.000 25.16024  ? 336 TYR A C   1 
ATOM   2421 O  O   . TYR A  1 310 ? -4.52539  -6.35497  48.70735  1.000 26.69794  ? 336 TYR A O   1 
ATOM   2422 C  CB  . TYR A  1 310 ? -4.80317  -9.11500  48.32049  1.000 25.03238  ? 336 TYR A CB  1 
ATOM   2423 C  CG  . TYR A  1 310 ? -5.03866  -10.50080 47.76146  1.000 23.82193  ? 336 TYR A CG  1 
ATOM   2424 C  CD1 . TYR A  1 310 ? -6.08896  -10.74886 46.88724  1.000 23.84094  ? 336 TYR A CD1 1 
ATOM   2425 C  CD2 . TYR A  1 310 ? -4.20635  -11.55886 48.10193  1.000 20.78765  ? 336 TYR A CD2 1 
ATOM   2426 C  CE1 . TYR A  1 310 ? -6.30535  -12.01236 46.36936  1.000 23.19057  ? 336 TYR A CE1 1 
ATOM   2427 C  CE2 . TYR A  1 310 ? -4.41594  -12.82653 47.59052  1.000 21.44036  ? 336 TYR A CE2 1 
ATOM   2428 C  CZ  . TYR A  1 310 ? -5.46620  -13.04711 46.72404  1.000 22.43119  ? 336 TYR A CZ  1 
ATOM   2429 O  OH  . TYR A  1 310 ? -5.67934  -14.30622 46.21079  1.000 22.64978  ? 336 TYR A OH  1 
ATOM   2430 N  N   . PRO A  1 311 ? -3.69242  -6.01018  46.66283  1.000 24.68313  ? 337 PRO A N   1 
ATOM   2431 C  CA  . PRO A  1 311 ? -3.85142  -4.55794  46.77890  1.000 27.13489  ? 337 PRO A CA  1 
ATOM   2432 C  C   . PRO A  1 311 ? -5.31471  -4.16163  46.71259  1.000 29.43258  ? 337 PRO A C   1 
ATOM   2433 O  O   . PRO A  1 311 ? -6.15607  -4.93716  46.23432  1.000 28.31193  ? 337 PRO A O   1 
ATOM   2434 C  CB  . PRO A  1 311 ? -3.07224  -4.02409  45.56783  1.000 27.49515  ? 337 PRO A CB  1 
ATOM   2435 C  CG  . PRO A  1 311 ? -3.15098  -5.12562  44.56900  1.000 25.81245  ? 337 PRO A CG  1 
ATOM   2436 C  CD  . PRO A  1 311 ? -3.12867  -6.40629  45.36033  1.000 26.06108  ? 337 PRO A CD  1 
ATOM   2437 N  N   . PRO A  1 312 ? -5.66061  -2.96629  47.18548  1.000 31.68141  ? 338 PRO A N   1 
ATOM   2438 C  CA  . PRO A  1 312 ? -7.05592  -2.51678  47.11656  1.000 33.72356  ? 338 PRO A CA  1 
ATOM   2439 C  C   . PRO A  1 312 ? -7.48845  -2.25589  45.68028  1.000 36.25116  ? 338 PRO A C   1 
ATOM   2440 O  O   . PRO A  1 312 ? -6.69182  -2.26193  44.73956  1.000 37.09851  ? 338 PRO A O   1 
ATOM   2441 C  CB  . PRO A  1 312 ? -7.06206  -1.23107  47.94920  1.000 34.76449  ? 338 PRO A CB  1 
ATOM   2442 C  CG  . PRO A  1 312 ? -5.64320  -0.76644  47.94373  1.000 32.52711  ? 338 PRO A CG  1 
ATOM   2443 C  CD  . PRO A  1 312 ? -4.80255  -2.00606  47.90070  1.000 32.34254  ? 338 PRO A CD  1 
ATOM   2444 N  N   . ALA A  1 313 ? -8.79304  -2.01212  45.52800  1.000 38.74425  ? 339 ALA A N   1 
ATOM   2445 C  CA  . ALA A  1 313 ? -9.38117  -1.89197  44.19684  1.000 40.00409  ? 339 ALA A CA  1 
ATOM   2446 C  C   . ALA A  1 313 ? -8.83127  -0.68683  43.44331  1.000 40.43766  ? 339 ALA A C   1 
ATOM   2447 O  O   . ALA A  1 313 ? -8.63636  -0.74666  42.22314  1.000 40.39510  ? 339 ALA A O   1 
ATOM   2448 C  CB  . ALA A  1 313 ? -10.90351 -1.80663  44.30397  1.000 41.30083  ? 339 ALA A CB  1 
ATOM   2449 N  N   . ASP A  1 314 ? -8.58101  0.41978   44.14842  1.000 40.34848  ? 340 ASP A N   1 
ATOM   2450 C  CA  . ASP A  1 314 ? -8.06750  1.61143   43.48023  1.000 42.43253  ? 340 ASP A CA  1 
ATOM   2451 C  C   . ASP A  1 314 ? -6.66729  1.38445   42.92435  1.000 39.15603  ? 340 ASP A C   1 
ATOM   2452 O  O   . ASP A  1 314 ? -6.29779  1.99259   41.91329  1.000 38.19275  ? 340 ASP A O   1 
ATOM   2453 C  CB  . ASP A  1 314 ? -8.07740  2.80254   44.43937  1.000 46.22777  ? 340 ASP A CB  1 
ATOM   2454 C  CG  . ASP A  1 314 ? -7.13564  2.61663   45.61102  1.000 49.88202  ? 340 ASP A CG  1 
ATOM   2455 O  OD1 . ASP A  1 314 ? -6.59233  3.62733   46.10528  1.000 51.64252  ? 340 ASP A OD1 1 
ATOM   2456 O  OD2 . ASP A  1 314 ? -6.93928  1.46051   46.03834  1.000 51.53939  ? 340 ASP A OD2 1 
ATOM   2457 N  N   . VAL A  1 315 ? -5.87981  0.51775   43.56233  1.000 35.59861  ? 341 VAL A N   1 
ATOM   2458 C  CA  . VAL A  1 315 ? -4.56709  0.17454   43.02667  1.000 30.06769  ? 341 VAL A CA  1 
ATOM   2459 C  C   . VAL A  1 315 ? -4.69880  -0.83360  41.89289  1.000 29.06308  ? 341 VAL A C   1 
ATOM   2460 O  O   . VAL A  1 315 ? -4.01303  -0.72634  40.86983  1.000 27.66673  ? 341 VAL A O   1 
ATOM   2461 C  CB  . VAL A  1 315 ? -3.65543  -0.34989  44.15083  1.000 25.50898  ? 341 VAL A CB  1 
ATOM   2462 C  CG1 . VAL A  1 315 ? -2.31724  -0.80442  43.58581  1.000 22.84304  ? 341 VAL A CG1 1 
ATOM   2463 C  CG2 . VAL A  1 315 ? -3.45497  0.72121   45.20870  1.000 26.52281  ? 341 VAL A CG2 1 
ATOM   2464 N  N   . ARG A  1 316 ? -5.58396  -1.82234  42.05372  1.000 29.23408  ? 342 ARG A N   1 
ATOM   2465 C  CA  . ARG A  1 316 ? -5.78911  -2.81880  41.00756  1.000 29.93414  ? 342 ARG A CA  1 
ATOM   2466 C  C   . ARG A  1 316 ? -6.27477  -2.18167  39.71323  1.000 29.29432  ? 342 ARG A C   1 
ATOM   2467 O  O   . ARG A  1 316 ? -5.93981  -2.65898  38.62287  1.000 28.06864  ? 342 ARG A O   1 
ATOM   2468 C  CB  . ARG A  1 316 ? -6.78509  -3.87759  41.48049  1.000 32.99164  ? 342 ARG A CB  1 
ATOM   2469 C  CG  . ARG A  1 316 ? -6.25824  -4.78116  42.58092  1.000 35.18529  ? 342 ARG A CG  1 
ATOM   2470 C  CD  . ARG A  1 316 ? -7.39255  -5.51044  43.27950  1.000 38.44137  ? 342 ARG A CD  1 
ATOM   2471 N  NE  . ARG A  1 316 ? -6.91953  -6.67630  44.01927  1.000 38.89644  ? 342 ARG A NE  1 
ATOM   2472 C  CZ  . ARG A  1 316 ? -6.94158  -7.91765  43.54580  1.000 39.51550  ? 342 ARG A CZ  1 
ATOM   2473 N  NH1 . ARG A  1 316 ? -6.49091  -8.92069  44.28613  1.000 38.44459  ? 342 ARG A NH1 1 
ATOM   2474 N  NH2 . ARG A  1 316 ? -7.41511  -8.15668  42.33063  1.000 40.77881  ? 342 ARG A NH2 1 
ATOM   2475 N  N   . ALA A  1 317 ? -7.05868  -1.10489  39.81072  1.000 29.17147  ? 343 ALA A N   1 
ATOM   2476 C  CA  . ALA A  1 317 ? -7.53117  -0.41492  38.61704  1.000 29.83452  ? 343 ALA A CA  1 
ATOM   2477 C  C   . ALA A  1 317 ? -6.40854  0.30174   37.87947  1.000 31.02318  ? 343 ALA A C   1 
ATOM   2478 O  O   . ALA A  1 317 ? -6.58988  0.67803   36.71660  1.000 32.12708  ? 343 ALA A O   1 
ATOM   2479 C  CB  . ALA A  1 317 ? -8.63108  0.58192   38.98511  1.000 30.26634  ? 343 ALA A CB  1 
ATOM   2480 N  N   . LYS A  1 318 ? -5.25864  0.49852   38.52350  1.000 30.16722  ? 344 LYS A N   1 
ATOM   2481 C  CA  . LYS A  1 318 ? -4.11849  1.16232   37.90635  1.000 28.53847  ? 344 LYS A CA  1 
ATOM   2482 C  C   . LYS A  1 318 ? -3.00735  0.18955   37.53189  1.000 25.15630  ? 344 LYS A C   1 
ATOM   2483 O  O   . LYS A  1 318 ? -1.92310  0.62629   37.13160  1.000 24.11645  ? 344 LYS A O   1 
ATOM   2484 C  CB  . LYS A  1 318 ? -3.57822  2.25332   38.83364  1.000 28.29123  ? 344 LYS A CB  1 
ATOM   2485 C  CG  . LYS A  1 318 ? -4.53322  3.42127   39.02663  1.000 30.68880  ? 344 LYS A CG  1 
ATOM   2486 C  CD  . LYS A  1 318 ? -3.89836  4.53115   39.84705  1.000 32.50621  ? 344 LYS A CD  1 
ATOM   2487 C  CE  . LYS A  1 318 ? -4.85021  5.70512   40.01393  1.000 34.42190  ? 344 LYS A CE  1 
ATOM   2488 N  NZ  . LYS A  1 318 ? -6.09635  5.31447   40.72971  1.000 34.85016  ? 344 LYS A NZ  1 
ATOM   2489 N  N   . LEU A  1 319 ? -3.24658  -1.11354  37.65414  1.000 24.34479  ? 345 LEU A N   1 
ATOM   2490 C  CA  . LEU A  1 319 ? -2.26765  -2.09519  37.21805  1.000 22.86266  ? 345 LEU A CA  1 
ATOM   2491 C  C   . LEU A  1 319 ? -2.22291  -2.15682  35.69369  1.000 24.57007  ? 345 LEU A C   1 
ATOM   2492 O  O   . LEU A  1 319 ? -3.17622  -1.79235  34.99982  1.000 23.87295  ? 345 LEU A O   1 
ATOM   2493 C  CB  . LEU A  1 319 ? -2.59476  -3.47548  37.78909  1.000 21.61511  ? 345 LEU A CB  1 
ATOM   2494 C  CG  . LEU A  1 319 ? -2.37121  -3.68000  39.28888  1.000 21.02198  ? 345 LEU A CG  1 
ATOM   2495 C  CD1 . LEU A  1 319 ? -2.87916  -5.04590  39.72431  1.000 19.82677  ? 345 LEU A CD1 1 
ATOM   2496 C  CD2 . LEU A  1 319 ? -0.90231  -3.51423  39.64299  1.000 19.97890  ? 345 LEU A CD2 1 
ATOM   2497 N  N   . PHE A  1 320 ? -1.09100  -2.62445  35.17292  1.000 25.02691  ? 346 PHE A N   1 
ATOM   2498 C  CA  . PHE A  1 320 ? -0.91184  -2.74100  33.73388  1.000 26.08470  ? 346 PHE A CA  1 
ATOM   2499 C  C   . PHE A  1 320 ? 0.08186   -3.85459  33.44363  1.000 23.94296  ? 346 PHE A C   1 
ATOM   2500 O  O   . PHE A  1 320 ? 0.89413   -4.22697  34.29359  1.000 20.87109  ? 346 PHE A O   1 
ATOM   2501 C  CB  . PHE A  1 320 ? -0.43762  -1.41867  33.11261  1.000 28.55356  ? 346 PHE A CB  1 
ATOM   2502 C  CG  . PHE A  1 320 ? 0.89333   -0.94162  33.62991  1.000 29.68731  ? 346 PHE A CG  1 
ATOM   2503 C  CD1 . PHE A  1 320 ? 2.07316   -1.31737  33.00550  1.000 29.49749  ? 346 PHE A CD1 1 
ATOM   2504 C  CD2 . PHE A  1 320 ? 0.96321   -0.11073  34.73588  1.000 29.59238  ? 346 PHE A CD2 1 
ATOM   2505 C  CE1 . PHE A  1 320 ? 3.29562   -0.87891  33.47844  1.000 29.91630  ? 346 PHE A CE1 1 
ATOM   2506 C  CE2 . PHE A  1 320 ? 2.18344   0.33147   35.21353  1.000 29.77421  ? 346 PHE A CE2 1 
ATOM   2507 C  CZ  . PHE A  1 320 ? 3.35065   -0.05301  34.58356  1.000 29.98357  ? 346 PHE A CZ  1 
ATOM   2508 N  N   . THR A  1 321 ? 0.00429   -4.38557  32.22879  1.000 25.24294  ? 347 THR A N   1 
ATOM   2509 C  CA  . THR A  1 321 ? 0.94046   -5.38884  31.75018  1.000 28.80444  ? 347 THR A CA  1 
ATOM   2510 C  C   . THR A  1 321 ? 1.80837   -4.79770  30.64636  1.000 30.14226  ? 347 THR A C   1 
ATOM   2511 O  O   . THR A  1 321 ? 1.50053   -3.74750  30.07645  1.000 31.27037  ? 347 THR A O   1 
ATOM   2512 C  CB  . THR A  1 321 ? 0.20838   -6.63471  31.23736  1.000 31.85502  ? 347 THR A CB  1 
ATOM   2513 O  OG1 . THR A  1 321 ? -0.79798  -6.24841  30.29487  1.000 33.35737  ? 347 THR A OG1 1 
ATOM   2514 C  CG2 . THR A  1 321 ? -0.44585  -7.37875  32.38998  1.000 32.40875  ? 347 THR A CG2 1 
ATOM   2515 N  N   . LEU A  1 322 ? 2.90518   -5.48876  30.35020  1.000 30.92532  ? 348 LEU A N   1 
ATOM   2516 C  CA  . LEU A  1 322 ? 3.89024   -5.01558  29.38332  1.000 35.63342  ? 348 LEU A CA  1 
ATOM   2517 C  C   . LEU A  1 322 ? 3.48979   -5.48485  27.98885  1.000 38.37640  ? 348 LEU A C   1 
ATOM   2518 O  O   . LEU A  1 322 ? 3.50547   -6.68667  27.70437  1.000 37.67404  ? 348 LEU A O   1 
ATOM   2519 C  CB  . LEU A  1 322 ? 5.28084   -5.52308  29.75428  1.000 36.54591  ? 348 LEU A CB  1 
ATOM   2520 C  CG  . LEU A  1 322 ? 6.46617   -4.88726  29.02908  1.000 39.28983  ? 348 LEU A CG  1 
ATOM   2521 C  CD1 . LEU A  1 322 ? 6.83919   -3.56038  29.67228  1.000 39.47807  ? 348 LEU A CD1 1 
ATOM   2522 C  CD2 . LEU A  1 322 ? 7.65263   -5.83581  29.02046  1.000 39.05226  ? 348 LEU A CD2 1 
ATOM   2523 N  N   . LYS A  1 323 ? 3.13090   -4.54348  27.11854  1.000 40.73012  ? 349 LYS A N   1 
ATOM   2524 C  CA  . LYS A  1 323 ? 2.83863   -4.89535  25.73730  1.000 44.05690  ? 349 LYS A CA  1 
ATOM   2525 C  C   . LYS A  1 323 ? 4.13673   -5.09664  24.96396  1.000 41.84996  ? 349 LYS A C   1 
ATOM   2526 O  O   . LYS A  1 323 ? 5.15128   -4.44282  25.22493  1.000 40.29651  ? 349 LYS A O   1 
ATOM   2527 C  CB  . LYS A  1 323 ? 1.99873   -3.81749  25.04239  1.000 50.28201  ? 349 LYS A CB  1 
ATOM   2528 C  CG  . LYS A  1 323 ? 0.68940   -3.42872  25.72732  1.000 53.78333  ? 349 LYS A CG  1 
ATOM   2529 C  CD  . LYS A  1 323 ? 0.32132   -1.99625  25.35632  1.000 57.30490  ? 349 LYS A CD  1 
ATOM   2530 C  CE  . LYS A  1 323 ? -1.04143  -1.57480  25.87136  1.000 59.26474  ? 349 LYS A CE  1 
ATOM   2531 N  NZ  . LYS A  1 323 ? -1.58039  -0.42150  25.08842  1.000 63.64229  ? 349 LYS A NZ  1 
ATOM   2532 N  N   . VAL A  1 324 ? 4.09614   -6.01916  24.00369  1.000 42.35992  ? 350 VAL A N   1 
ATOM   2533 C  CA  . VAL A  1 324 ? 5.23743   -6.23847  23.12464  1.000 43.06373  ? 350 VAL A CA  1 
ATOM   2534 C  C   . VAL A  1 324 ? 5.37772   -5.04803  22.18780  1.000 46.32588  ? 350 VAL A C   1 
ATOM   2535 O  O   . VAL A  1 324 ? 4.41680   -4.64876  21.51710  1.000 48.19815  ? 350 VAL A O   1 
ATOM   2536 C  CB  . VAL A  1 324 ? 5.07111   -7.55030  22.34471  1.000 43.05823  ? 350 VAL A CB  1 
ATOM   2537 C  CG1 . VAL A  1 324 ? 6.17597   -7.69841  21.31277  1.000 43.77364  ? 350 VAL A CG1 1 
ATOM   2538 C  CG2 . VAL A  1 324 ? 5.06228   -8.73299  23.30137  1.000 40.61239  ? 350 VAL A CG2 1 
ATOM   2539 N  N   . GLN A  1 325 ? 6.57340   -4.47097  22.14161  1.000 48.96800  ? 351 GLN A N   1 
ATOM   2540 C  CA  . GLN A  1 325 ? 6.81211   -3.24790  21.39275  1.000 54.35271  ? 351 GLN A CA  1 
ATOM   2541 C  C   . GLN A  1 325 ? 7.39369   -3.54649  20.01752  1.000 64.18986  ? 351 GLN A C   1 
ATOM   2542 O  O   . GLN A  1 325 ? 8.05357   -4.56676  19.80213  1.000 64.76875  ? 351 GLN A O   1 
ATOM   2543 C  CB  . GLN A  1 325 ? 7.75348   -2.31317  22.15520  1.000 50.20030  ? 351 GLN A CB  1 
ATOM   2544 C  CG  . GLN A  1 325 ? 7.11182   -1.61649  23.34315  1.000 45.19298  ? 351 GLN A CG  1 
ATOM   2545 C  CD  . GLN A  1 325 ? 6.06608   -0.59474  22.93514  1.000 42.91962  ? 351 GLN A CD  1 
ATOM   2546 O  OE1 . GLN A  1 325 ? 6.04752   -0.12340  21.79744  1.000 43.50178  ? 351 GLN A OE1 1 
ATOM   2547 N  NE2 . GLN A  1 325 ? 5.18706   -0.24737  23.86764  1.000 39.68917  ? 351 GLN A NE2 1 
ATOM   2548 N  N   . ASP A  1 326 ? 7.13249   -2.63385  19.08774  1.000 70.89089  ? 352 ASP A N   1 
ATOM   2549 C  CA  . ASP A  1 326 ? 7.69948   -2.72009  17.75568  1.000 76.38010  ? 352 ASP A CA  1 
ATOM   2550 C  C   . ASP A  1 326 ? 9.21458   -2.51196  17.82020  1.000 75.31500  ? 352 ASP A C   1 
ATOM   2551 O  O   . ASP A  1 326 ? 9.71084   -1.80004  18.69675  1.000 75.38128  ? 352 ASP A O   1 
ATOM   2552 C  CB  . ASP A  1 326 ? 7.03716   -1.68234  16.85041  1.000 82.60882  ? 352 ASP A CB  1 
ATOM   2553 C  CG  . ASP A  1 326 ? 7.86221   -1.34931  15.63267  1.000 90.76850  ? 352 ASP A CG  1 
ATOM   2554 O  OD1 . ASP A  1 326 ? 7.94814   -2.18848  14.71072  1.000 94.78741  ? 352 ASP A OD1 1 
ATOM   2555 O  OD2 . ASP A  1 326 ? 8.41997   -0.23736  15.59971  1.000 94.25285  ? 352 ASP A OD2 1 
ATOM   2556 N  N   . PRO A  1 327 ? 9.97142   -3.15285  16.92047  1.000 73.32478  ? 353 PRO A N   1 
ATOM   2557 C  CA  . PRO A  1 327 ? 11.44297  -3.12389  17.02651  1.000 70.76767  ? 353 PRO A CA  1 
ATOM   2558 C  C   . PRO A  1 327 ? 12.07555  -1.74652  17.19558  1.000 67.73990  ? 353 PRO A C   1 
ATOM   2559 O  O   . PRO A  1 327 ? 13.04362  -1.63496  17.95765  1.000 66.75987  ? 353 PRO A O   1 
ATOM   2560 C  CB  . PRO A  1 327 ? 11.87779  -3.78913  15.71609  1.000 73.25187  ? 353 PRO A CB  1 
ATOM   2561 C  CG  . PRO A  1 327 ? 10.80180  -4.79064  15.45518  1.000 74.66914  ? 353 PRO A CG  1 
ATOM   2562 C  CD  . PRO A  1 327 ? 9.51402   -4.18143  15.96755  1.000 74.86317  ? 353 PRO A CD  1 
ATOM   2563 N  N   . LYS A  1 328 ? 11.58852  -0.70215  16.51454  1.000 64.99103  ? 354 LYS A N   1 
ATOM   2564 C  CA  . LYS A  1 328 ? 12.19441  0.61664   16.70011  1.000 62.30746  ? 354 LYS A CA  1 
ATOM   2565 C  C   . LYS A  1 328 ? 12.10178  1.06259   18.15440  1.000 55.67391  ? 354 LYS A C   1 
ATOM   2566 O  O   . LYS A  1 328 ? 13.05693  1.63002   18.70271  1.000 53.39788  ? 354 LYS A O   1 
ATOM   2567 C  CB  . LYS A  1 328 ? 11.54378  1.66154   15.78930  1.000 64.85018  ? 354 LYS A CB  1 
ATOM   2568 C  CG  . LYS A  1 328 ? 10.94516  1.14816   14.49196  1.000 67.14863  ? 354 LYS A CG  1 
ATOM   2569 C  CD  . LYS A  1 328 ? 9.82490   2.07995   14.03680  1.000 67.69960  ? 354 LYS A CD  1 
ATOM   2570 C  CE  . LYS A  1 328 ? 9.14815   1.58914   12.76907  1.000 68.57733  ? 354 LYS A CE  1 
ATOM   2571 N  NZ  . LYS A  1 328 ? 7.74103   2.07286   12.68504  1.000 68.28513  ? 354 LYS A NZ  1 
ATOM   2572 N  N   . ILE A  1 329 ? 10.95680  0.81512   18.79427  1.000 53.34774  ? 355 ILE A N   1 
ATOM   2573 C  CA  . ILE A  1 329 ? 10.81399  1.13855   20.21000  1.000 50.56509  ? 355 ILE A CA  1 
ATOM   2574 C  C   . ILE A  1 329 ? 11.80258  0.32944   21.03873  1.000 51.69424  ? 355 ILE A C   1 
ATOM   2575 O  O   . ILE A  1 329 ? 12.36827  0.82944   22.01614  1.000 51.35416  ? 355 ILE A O   1 
ATOM   2576 C  CB  . ILE A  1 329 ? 9.36028   0.91114   20.66736  1.000 47.84919  ? 355 ILE A CB  1 
ATOM   2577 C  CG1 . ILE A  1 329 ? 8.40603   1.79849   19.86502  1.000 47.65333  ? 355 ILE A CG1 1 
ATOM   2578 C  CG2 . ILE A  1 329 ? 9.20826   1.19362   22.15652  1.000 45.34749  ? 355 ILE A CG2 1 
ATOM   2579 C  CD1 . ILE A  1 329 ? 8.73134   3.27747   19.94372  1.000 47.43459  ? 355 ILE A CD1 1 
ATOM   2580 N  N   . ASP A  1 330 ? 12.04645  -0.92382  20.64751  1.000 53.21403  ? 356 ASP A N   1 
ATOM   2581 C  CA  . ASP A  1 330 ? 12.99681  -1.75534  21.37960  1.000 54.85685  ? 356 ASP A CA  1 
ATOM   2582 C  C   . ASP A  1 330 ? 14.40737  -1.18381  21.28933  1.000 55.15257  ? 356 ASP A C   1 
ATOM   2583 O  O   . ASP A  1 330 ? 15.12341  -1.11339  22.29726  1.000 54.49941  ? 356 ASP A O   1 
ATOM   2584 C  CB  . ASP A  1 330 ? 12.95554  -3.18836  20.84366  1.000 59.45718  ? 356 ASP A CB  1 
ATOM   2585 C  CG  . ASP A  1 330 ? 13.37572  -4.21672  21.87810  1.000 64.01808  ? 356 ASP A CG  1 
ATOM   2586 O  OD1 . ASP A  1 330 ? 12.51491  -4.66822  22.66365  1.000 66.93388  ? 356 ASP A OD1 1 
ATOM   2587 O  OD2 . ASP A  1 330 ? 14.56797  -4.58449  21.89416  1.000 67.36734  ? 356 ASP A OD2 1 
ATOM   2588 N  N   . ARG A  1 331 ? 14.81630  -0.75179  20.09031  1.000 55.19021  ? 357 ARG A N   1 
ATOM   2589 C  CA  . ARG A  1 331 ? 16.15202  -0.18590  19.92155  1.000 54.70978  ? 357 ARG A CA  1 
ATOM   2590 C  C   . ARG A  1 331 ? 16.28626  1.11400   20.69912  1.000 51.00100  ? 357 ARG A C   1 
ATOM   2591 O  O   . ARG A  1 331 ? 17.29337  1.33320   21.38538  1.000 50.04438  ? 357 ARG A O   1 
ATOM   2592 C  CB  . ARG A  1 331 ? 16.44393  0.06200   18.43948  1.000 59.53554  ? 357 ARG A CB  1 
ATOM   2593 C  CG  . ARG A  1 331 ? 17.07457  -1.11309  17.70967  1.000 62.54813  ? 357 ARG A CG  1 
ATOM   2594 C  CD  . ARG A  1 331 ? 15.98218  -1.95729  17.10413  1.000 63.34851  ? 357 ARG A CD  1 
ATOM   2595 N  NE  . ARG A  1 331 ? 16.43213  -3.27164  16.66412  1.000 64.26492  ? 357 ARG A NE  1 
ATOM   2596 C  CZ  . ARG A  1 331 ? 15.95811  -4.41072  17.16248  1.000 63.01731  ? 357 ARG A CZ  1 
ATOM   2597 N  NH1 . ARG A  1 331 ? 16.41078  -5.57645  16.70987  1.000 62.98294  ? 357 ARG A NH1 1 
ATOM   2598 N  NH2 . ARG A  1 331 ? 15.01938  -4.38145  18.11062  1.000 61.58453  ? 357 ARG A NH2 1 
ATOM   2599 N  N   . VAL A  1 332 ? 15.28185  1.99088   20.58943  1.000 48.47910  ? 358 VAL A N   1 
ATOM   2600 C  CA  . VAL A  1 332 ? 15.29939  3.25354   21.32342  1.000 45.24186  ? 358 VAL A CA  1 
ATOM   2601 C  C   . VAL A  1 332 ? 15.39518  2.99294   22.82083  1.000 40.11163  ? 358 VAL A C   1 
ATOM   2602 O  O   . VAL A  1 332 ? 16.17871  3.63501   23.53196  1.000 39.83471  ? 358 VAL A O   1 
ATOM   2603 C  CB  . VAL A  1 332 ? 14.05483  4.08860   20.96358  1.000 45.71741  ? 358 VAL A CB  1 
ATOM   2604 C  CG1 . VAL A  1 332 ? 13.67291  5.02295   22.10068  1.000 44.70815  ? 358 VAL A CG1 1 
ATOM   2605 C  CG2 . VAL A  1 332 ? 14.29091  4.86331   19.67501  1.000 47.15163  ? 358 VAL A CG2 1 
ATOM   2606 N  N   . ARG A  1 333 ? 14.62286  2.02257   23.31362  1.000 37.39612  ? 359 ARG A N   1 
ATOM   2607 C  CA  . ARG A  1 333 ? 14.64671  1.67602   24.72819  1.000 37.19229  ? 359 ARG A CA  1 
ATOM   2608 C  C   . ARG A  1 333 ? 16.02134  1.17948   25.15383  1.000 38.43055  ? 359 ARG A C   1 
ATOM   2609 O  O   . ARG A  1 333 ? 16.53848  1.58711   26.19959  1.000 39.12189  ? 359 ARG A O   1 
ATOM   2610 C  CB  . ARG A  1 333 ? 13.58010  0.61711   25.00632  1.000 35.22177  ? 359 ARG A CB  1 
ATOM   2611 C  CG  . ARG A  1 333 ? 13.09333  0.55474   26.43779  1.000 33.99366  ? 359 ARG A CG  1 
ATOM   2612 C  CD  . ARG A  1 333 ? 11.66023  0.04839   26.48740  1.000 34.45346  ? 359 ARG A CD  1 
ATOM   2613 N  NE  . ARG A  1 333 ? 11.43359  -1.04421  25.54449  1.000 35.09444  ? 359 ARG A NE  1 
ATOM   2614 C  CZ  . ARG A  1 333 ? 10.28739  -1.70770  25.42935  1.000 35.18858  ? 359 ARG A CZ  1 
ATOM   2615 N  NH1 . ARG A  1 333 ? 9.25572   -1.39424  26.20124  1.000 31.44991  ? 359 ARG A NH1 1 
ATOM   2616 N  NH2 . ARG A  1 333 ? 10.17312  -2.68906  24.54442  1.000 38.46469  ? 359 ARG A NH2 1 
ATOM   2617 N  N   . THR A  1 334 ? 16.63432  0.30577   24.35111  1.000 38.61815  ? 360 THR A N   1 
ATOM   2618 C  CA  . THR A  1 334 ? 17.93369  -0.24561  24.72458  1.000 38.52768  ? 360 THR A CA  1 
ATOM   2619 C  C   . THR A  1 334 ? 19.01480  0.83009   24.73647  1.000 38.69853  ? 360 THR A C   1 
ATOM   2620 O  O   . THR A  1 334 ? 19.83096  0.88583   25.66616  1.000 37.95605  ? 360 THR A O   1 
ATOM   2621 C  CB  . THR A  1 334 ? 18.31477  -1.38555  23.78018  1.000 39.92026  ? 360 THR A CB  1 
ATOM   2622 O  OG1 . THR A  1 334 ? 17.25484  -2.34985  23.74539  1.000 40.05021  ? 360 THR A OG1 1 
ATOM   2623 C  CG2 . THR A  1 334 ? 19.59102  -2.06547  24.25280  1.000 38.82606  ? 360 THR A CG2 1 
ATOM   2624 N  N   . ARG A  1 335 ? 19.03275  1.70453   23.72546  1.000 40.05347  ? 361 ARG A N   1 
ATOM   2625 C  CA  . ARG A  1 335 ? 20.05230  2.75095   23.70416  1.000 41.09937  ? 361 ARG A CA  1 
ATOM   2626 C  C   . ARG A  1 335 ? 19.82514  3.76766   24.81760  1.000 37.80022  ? 361 ARG A C   1 
ATOM   2627 O  O   . ARG A  1 335 ? 20.78693  4.25959   25.42145  1.000 35.94903  ? 361 ARG A O   1 
ATOM   2628 C  CB  . ARG A  1 335 ? 20.09498  3.44911   22.34431  1.000 47.17488  ? 361 ARG A CB  1 
ATOM   2629 C  CG  . ARG A  1 335 ? 21.27184  4.41576   22.22494  1.000 51.11658  ? 361 ARG A CG  1 
ATOM   2630 C  CD  . ARG A  1 335 ? 21.42959  5.00851   20.83375  1.000 55.97747  ? 361 ARG A CD  1 
ATOM   2631 N  NE  . ARG A  1 335 ? 21.96656  6.36679   20.89456  1.000 58.83869  ? 361 ARG A NE  1 
ATOM   2632 C  CZ  . ARG A  1 335 ? 23.22125  6.69272   20.59692  1.000 61.66529  ? 361 ARG A CZ  1 
ATOM   2633 N  NH1 . ARG A  1 335 ? 24.08100  5.75748   20.21582  1.000 63.65672  ? 361 ARG A NH1 1 
ATOM   2634 N  NH2 . ARG A  1 335 ? 23.61888  7.95532   20.68365  1.000 61.02896  ? 361 ARG A NH2 1 
ATOM   2635 N  N   . ALA A  1 336 ? 18.56272  4.08702   25.11722  1.000 36.74645  ? 362 ALA A N   1 
ATOM   2636 C  CA  . ALA A  1 336 ? 18.28164  5.00046   26.21830  1.000 35.04900  ? 362 ALA A CA  1 
ATOM   2637 C  C   . ALA A  1 336 ? 18.69116  4.39275   27.55343  1.000 34.87796  ? 362 ALA A C   1 
ATOM   2638 O  O   . ALA A  1 336 ? 19.21256  5.09417   28.42631  1.000 36.97961  ? 362 ALA A O   1 
ATOM   2639 C  CB  . ALA A  1 336 ? 16.79987  5.37354   26.22432  1.000 34.22596  ? 362 ALA A CB  1 
ATOM   2640 N  N   . TRP A  1 337 ? 18.47563  3.08665   27.72620  1.000 32.58876  ? 363 TRP A N   1 
ATOM   2641 C  CA  . TRP A  1 337 ? 18.90653  2.41754   28.94910  1.000 30.71356  ? 363 TRP A CA  1 
ATOM   2642 C  C   . TRP A  1 337 ? 20.42587  2.40344   29.06157  1.000 32.72473  ? 363 TRP A C   1 
ATOM   2643 O  O   . TRP A  1 337 ? 20.97564  2.57124   30.15746  1.000 32.88352  ? 363 TRP A O   1 
ATOM   2644 C  CB  . TRP A  1 337 ? 18.34588  0.99665   28.98154  1.000 28.85609  ? 363 TRP A CB  1 
ATOM   2645 C  CG  . TRP A  1 337 ? 18.42884  0.31877   30.31573  1.000 27.96779  ? 363 TRP A CG  1 
ATOM   2646 C  CD1 . TRP A  1 337 ? 19.13557  -0.80854  30.61670  1.000 26.87061  ? 363 TRP A CD1 1 
ATOM   2647 C  CD2 . TRP A  1 337 ? 17.76452  0.71009   31.52443  1.000 24.82895  ? 363 TRP A CD2 1 
ATOM   2648 N  NE1 . TRP A  1 337 ? 18.95860  -1.14010  31.93732  1.000 24.90714  ? 363 TRP A NE1 1 
ATOM   2649 C  CE2 . TRP A  1 337 ? 18.12253  -0.22311  32.51770  1.000 23.78403  ? 363 TRP A CE2 1 
ATOM   2650 C  CE3 . TRP A  1 337 ? 16.90641  1.76052   31.86399  1.000 25.57569  ? 363 TRP A CE3 1 
ATOM   2651 C  CZ2 . TRP A  1 337 ? 17.65310  -0.13795  33.82729  1.000 21.65939  ? 363 TRP A CZ2 1 
ATOM   2652 C  CZ3 . TRP A  1 337 ? 16.44215  1.84392   33.16474  1.000 24.62246  ? 363 TRP A CZ3 1 
ATOM   2653 C  CH2 . TRP A  1 337 ? 16.81605  0.89970   34.13010  1.000 22.71808  ? 363 TRP A CH2 1 
ATOM   2654 N  N   . THR A  1 338 ? 21.12025  2.20210   27.93807  1.000 34.13184  ? 364 THR A N   1 
ATOM   2655 C  CA  . THR A  1 338 ? 22.57836  2.27618   27.94887  1.000 34.01567  ? 364 THR A CA  1 
ATOM   2656 C  C   . THR A  1 338 ? 23.05337  3.67380   28.32910  1.000 33.07366  ? 364 THR A C   1 
ATOM   2657 O  O   . THR A  1 338 ? 24.02244  3.82659   29.08255  1.000 32.79321  ? 364 THR A O   1 
ATOM   2658 C  CB  . THR A  1 338 ? 23.13655  1.87299   26.58342  1.000 36.40742  ? 364 THR A CB  1 
ATOM   2659 O  OG1 . THR A  1 338 ? 22.67522  0.55904   26.24585  1.000 37.66448  ? 364 THR A OG1 1 
ATOM   2660 C  CG2 . THR A  1 338 ? 24.65915  1.87895   26.60364  1.000 37.08333  ? 364 THR A CG2 1 
ATOM   2661 N  N   . LYS A  1 339 ? 22.37896  4.70666   27.81810  1.000 33.16602  ? 365 LYS A N   1 
ATOM   2662 C  CA  . LYS A  1 339 ? 22.73100  6.07712   28.17955  1.000 34.73287  ? 365 LYS A CA  1 
ATOM   2663 C  C   . LYS A  1 339 ? 22.46478  6.34623   29.65694  1.000 36.92481  ? 365 LYS A C   1 
ATOM   2664 O  O   . LYS A  1 339 ? 23.23715  7.05289   30.31553  1.000 38.37373  ? 365 LYS A O   1 
ATOM   2665 C  CB  . LYS A  1 339 ? 21.95476  7.06181   27.30396  1.000 34.96046  ? 365 LYS A CB  1 
ATOM   2666 C  CG  . LYS A  1 339 ? 22.13595  8.52496   27.68124  1.000 34.65583  ? 365 LYS A CG  1 
ATOM   2667 C  CD  . LYS A  1 339 ? 21.40771  9.43502   26.70366  1.000 35.66125  ? 365 LYS A CD  1 
ATOM   2668 C  CE  . LYS A  1 339 ? 21.72796  10.89814  26.96028  1.000 36.76137  ? 365 LYS A CE  1 
ATOM   2669 N  NZ  . LYS A  1 339 ? 21.83248  11.67133  25.69196  1.000 34.38494  ? 365 LYS A NZ  1 
ATOM   2670 N  N   . VAL A  1 340 ? 21.37787  5.78814   30.19355  1.000 37.81278  ? 366 VAL A N   1 
ATOM   2671 C  CA  . VAL A  1 340 ? 21.03402  6.01259   31.59465  1.000 36.26490  ? 366 VAL A CA  1 
ATOM   2672 C  C   . VAL A  1 340 ? 22.03477  5.32088   32.51292  1.000 36.41931  ? 366 VAL A C   1 
ATOM   2673 O  O   . VAL A  1 340 ? 22.46306  5.88783   33.52563  1.000 35.28581  ? 366 VAL A O   1 
ATOM   2674 C  CB  . VAL A  1 340 ? 19.59221  5.54427   31.86921  1.000 33.48138  ? 366 VAL A CB  1 
ATOM   2675 C  CG1 . VAL A  1 340 ? 19.33426  5.44132   33.36644  1.000 32.38329  ? 366 VAL A CG1 1 
ATOM   2676 C  CG2 . VAL A  1 340 ? 18.59426  6.49183   31.22328  1.000 33.10385  ? 366 VAL A CG2 1 
ATOM   2677 N  N   . LYS A  1 341 ? 22.43321  4.09347   32.17292  1.000 38.88119  ? 367 LYS A N   1 
ATOM   2678 C  CA  . LYS A  1 341 ? 23.31379  3.32312   33.04398  1.000 42.32266  ? 367 LYS A CA  1 
ATOM   2679 C  C   . LYS A  1 341 ? 24.75129  3.82875   33.04970  1.000 48.93832  ? 367 LYS A C   1 
ATOM   2680 O  O   . LYS A  1 341 ? 25.53203  3.40152   33.90716  1.000 50.64457  ? 367 LYS A O   1 
ATOM   2681 C  CB  . LYS A  1 341 ? 23.29075  1.84866   32.63775  1.000 40.26399  ? 367 LYS A CB  1 
ATOM   2682 C  CG  . LYS A  1 341 ? 22.46678  0.96970   33.56355  1.000 37.39702  ? 367 LYS A CG  1 
ATOM   2683 C  CD  . LYS A  1 341 ? 21.97123  -0.27831  32.85291  1.000 34.97800  ? 367 LYS A CD  1 
ATOM   2684 C  CE  . LYS A  1 341 ? 23.10855  -1.03377  32.18831  1.000 34.20820  ? 367 LYS A CE  1 
ATOM   2685 N  NZ  . LYS A  1 341 ? 22.66048  -2.35669  31.67296  1.000 34.36590  ? 367 LYS A NZ  1 
ATOM   2686 N  N   . SER A  1 342 ? 25.12093  4.72160   32.12968  1.000 52.78147  ? 368 SER A N   1 
ATOM   2687 C  CA  . SER A  1 342 ? 26.49591  5.20299   32.06330  1.000 57.10867  ? 368 SER A CA  1 
ATOM   2688 C  C   . SER A  1 342 ? 26.84551  6.16981   33.18728  1.000 59.99421  ? 368 SER A C   1 
ATOM   2689 O  O   . SER A  1 342 ? 28.02205  6.51830   33.33334  1.000 61.94236  ? 368 SER A O   1 
ATOM   2690 C  CB  . SER A  1 342 ? 26.75215  5.87320   30.71256  1.000 57.83564  ? 368 SER A CB  1 
ATOM   2691 O  OG  . SER A  1 342 ? 26.88706  4.90992   29.68276  1.000 58.54679  ? 368 SER A OG  1 
ATOM   2692 N  N   . GLY A  1 343 ? 25.86921  6.60784   33.97566  1.000 60.43609  ? 369 GLY A N   1 
ATOM   2693 C  CA  . GLY A  1 343 ? 26.12443  7.53793   35.06015  1.000 62.10254  ? 369 GLY A CA  1 
ATOM   2694 C  C   . GLY A  1 343 ? 26.92366  6.93761   36.20038  1.000 63.38246  ? 369 GLY A C   1 
ATOM   2695 O  O   . GLY A  1 343 ? 26.91808  7.45727   37.31659  1.000 64.18270  ? 369 GLY A O   1 
ATOM   2696 N  N   . GLN B  1 3   ? -24.29617 13.14759  76.04324  1.000 82.04076  ? 29  GLN B N   1 
ATOM   2697 C  CA  . GLN B  1 3   ? -23.74789 13.04982  77.39099  1.000 81.51079  ? 29  GLN B CA  1 
ATOM   2698 C  C   . GLN B  1 3   ? -23.60246 11.59168  77.80810  1.000 76.77956  ? 29  GLN B C   1 
ATOM   2699 O  O   . GLN B  1 3   ? -23.05138 11.28162  78.86539  1.000 76.88405  ? 29  GLN B O   1 
ATOM   2700 C  CB  . GLN B  1 3   ? -24.63771 13.79394  78.38725  1.000 85.23858  ? 29  GLN B CB  1 
ATOM   2701 C  CG  . GLN B  1 3   ? -25.18629 15.11749  77.87136  1.000 87.94191  ? 29  GLN B CG  1 
ATOM   2702 C  CD  . GLN B  1 3   ? -26.66610 15.04621  77.54550  1.000 89.19821  ? 29  GLN B CD  1 
ATOM   2703 O  OE1 . GLN B  1 3   ? -27.45708 14.50728  78.31947  1.000 90.43420  ? 29  GLN B OE1 1 
ATOM   2704 N  NE2 . GLN B  1 3   ? -27.04806 15.59249  76.39673  1.000 88.63927  ? 29  GLN B NE2 1 
ATOM   2705 N  N   . LYS B  1 4   ? -24.09422 10.69935  76.95569  1.000 73.06410  ? 30  LYS B N   1 
ATOM   2706 C  CA  . LYS B  1 4   ? -24.14440 9.28193   77.27632  1.000 70.17363  ? 30  LYS B CA  1 
ATOM   2707 C  C   . LYS B  1 4   ? -22.75327 8.67197   77.10021  1.000 64.52454  ? 30  LYS B C   1 
ATOM   2708 O  O   . LYS B  1 4   ? -22.14589 8.78815   76.02912  1.000 63.46596  ? 30  LYS B O   1 
ATOM   2709 C  CB  . LYS B  1 4   ? -25.16773 8.58828   76.37487  1.000 72.16933  ? 30  LYS B CB  1 
ATOM   2710 C  CG  . LYS B  1 4   ? -26.52140 8.36490   77.04803  1.000 75.37185  ? 30  LYS B CG  1 
ATOM   2711 C  CD  . LYS B  1 4   ? -27.29478 7.20952   76.42525  1.000 76.11856  ? 30  LYS B CD  1 
ATOM   2712 C  CE  . LYS B  1 4   ? -27.81249 7.49887   75.02708  1.000 76.44195  ? 30  LYS B CE  1 
ATOM   2713 N  NZ  . LYS B  1 4   ? -29.20212 6.97616   74.86130  1.000 77.09783  ? 30  LYS B NZ  1 
ATOM   2714 N  N   . THR B  1 5   ? -22.23147 8.05468   78.15991  1.000 60.85413  ? 31  THR B N   1 
ATOM   2715 C  CA  . THR B  1 5   ? -20.91429 7.42905   78.13623  1.000 57.49637  ? 31  THR B CA  1 
ATOM   2716 C  C   . THR B  1 5   ? -21.02745 5.95055   78.48870  1.000 54.61986  ? 31  THR B C   1 
ATOM   2717 O  O   . THR B  1 5   ? -22.08867 5.45886   78.87686  1.000 55.10796  ? 31  THR B O   1 
ATOM   2718 C  CB  . THR B  1 5   ? -19.93623 8.12059   79.09918  1.000 58.09077  ? 31  THR B CB  1 
ATOM   2719 O  OG1 . THR B  1 5   ? -20.08491 7.57322   80.41391  1.000 58.46135  ? 31  THR B OG1 1 
ATOM   2720 C  CG2 . THR B  1 5   ? -20.17825 9.61685   79.14060  1.000 58.58251  ? 31  THR B CG2 1 
ATOM   2721 N  N   . LEU B  1 6   ? -19.90718 5.24136   78.34778  1.000 50.96641  ? 32  LEU B N   1 
ATOM   2722 C  CA  . LEU B  1 6   ? -19.85724 3.80839   78.61729  1.000 49.68904  ? 32  LEU B CA  1 
ATOM   2723 C  C   . LEU B  1 6   ? -18.42586 3.42631   78.96371  1.000 50.67996  ? 32  LEU B C   1 
ATOM   2724 O  O   . LEU B  1 6   ? -17.49314 3.81532   78.25470  1.000 52.25188  ? 32  LEU B O   1 
ATOM   2725 C  CB  . LEU B  1 6   ? -20.35003 2.99954   77.40953  1.000 47.28935  ? 32  LEU B CB  1 
ATOM   2726 C  CG  . LEU B  1 6   ? -20.42411 1.47999   77.57292  1.000 45.09568  ? 32  LEU B CG  1 
ATOM   2727 C  CD1 . LEU B  1 6   ? -21.38492 1.11121   78.68845  1.000 45.10654  ? 32  LEU B CD1 1 
ATOM   2728 C  CD2 . LEU B  1 6   ? -20.83848 0.82503   76.26571  1.000 44.04290  ? 32  LEU B CD2 1 
ATOM   2729 N  N   . HIS B  1 7   ? -18.25553 2.66975   80.04658  1.000 49.92181  ? 33  HIS B N   1 
ATOM   2730 C  CA  . HIS B  1 7   ? -16.94165 2.25334   80.52448  1.000 50.12398  ? 33  HIS B CA  1 
ATOM   2731 C  C   . HIS B  1 7   ? -16.84506 0.73775   80.43671  1.000 49.21246  ? 33  HIS B C   1 
ATOM   2732 O  O   . HIS B  1 7   ? -17.64637 0.02539   81.05125  1.000 47.89127  ? 33  HIS B O   1 
ATOM   2733 C  CB  . HIS B  1 7   ? -16.70240 2.73051   81.95842  1.000 52.54788  ? 33  HIS B CB  1 
ATOM   2734 C  CG  . HIS B  1 7   ? -16.45915 4.20313   82.06972  1.000 54.64217  ? 33  HIS B CG  1 
ATOM   2735 N  ND1 . HIS B  1 7   ? -17.43345 5.14031   81.80109  1.000 55.46590  ? 33  HIS B ND1 1 
ATOM   2736 C  CD2 . HIS B  1 7   ? -15.35162 4.90068   82.41627  1.000 55.76540  ? 33  HIS B CD2 1 
ATOM   2737 C  CE1 . HIS B  1 7   ? -16.93722 6.35165   81.97874  1.000 56.67614  ? 33  HIS B CE1 1 
ATOM   2738 N  NE2 . HIS B  1 7   ? -15.67576 6.23420   82.35247  1.000 56.59462  ? 33  HIS B NE2 1 
ATOM   2739 N  N   . ILE B  1 8   ? -15.86594 0.25013   79.67792  1.000 48.65526  ? 34  ILE B N   1 
ATOM   2740 C  CA  . ILE B  1 8   ? -15.68943 -1.17397  79.42032  1.000 46.47775  ? 34  ILE B CA  1 
ATOM   2741 C  C   . ILE B  1 8   ? -14.28563 -1.57512  79.85091  1.000 45.34079  ? 34  ILE B C   1 
ATOM   2742 O  O   . ILE B  1 8   ? -13.31277 -0.87531  79.54579  1.000 44.73254  ? 34  ILE B O   1 
ATOM   2743 C  CB  . ILE B  1 8   ? -15.92520 -1.51318  77.93629  1.000 44.38817  ? 34  ILE B CB  1 
ATOM   2744 C  CG1 . ILE B  1 8   ? -17.34190 -1.11472  77.51794  1.000 44.56201  ? 34  ILE B CG1 1 
ATOM   2745 C  CG2 . ILE B  1 8   ? -15.68995 -2.99393  77.67692  1.000 42.57019  ? 34  ILE B CG2 1 
ATOM   2746 C  CD1 . ILE B  1 8   ? -17.58669 -1.20256  76.02764  1.000 43.31214  ? 34  ILE B CD1 1 
ATOM   2747 N  N   . TYR B  1 9   ? -14.18487 -2.69823  80.55955  1.000 45.53747  ? 35  TYR B N   1 
ATOM   2748 C  CA  . TYR B  1 9   ? -12.90967 -3.26710  80.98547  1.000 47.56612  ? 35  TYR B CA  1 
ATOM   2749 C  C   . TYR B  1 9   ? -12.78413 -4.64879  80.35669  1.000 47.24722  ? 35  TYR B C   1 
ATOM   2750 O  O   . TYR B  1 9   ? -13.54015 -5.56347  80.70235  1.000 46.80516  ? 35  TYR B O   1 
ATOM   2751 C  CB  . TYR B  1 9   ? -12.82240 -3.33988  82.50940  1.000 49.56622  ? 35  TYR B CB  1 
ATOM   2752 C  CG  . TYR B  1 9   ? -11.42073 -3.18759  83.05724  1.000 51.93851  ? 35  TYR B CG  1 
ATOM   2753 C  CD1 . TYR B  1 9   ? -10.54862 -2.24033  82.53747  1.000 53.22985  ? 35  TYR B CD1 1 
ATOM   2754 C  CD2 . TYR B  1 9   ? -10.97296 -3.98612  84.10094  1.000 52.46749  ? 35  TYR B CD2 1 
ATOM   2755 C  CE1 . TYR B  1 9   ? -9.26719  -2.09787  83.03894  1.000 54.74107  ? 35  TYR B CE1 1 
ATOM   2756 C  CE2 . TYR B  1 9   ? -9.69607  -3.85028  84.60988  1.000 54.28971  ? 35  TYR B CE2 1 
ATOM   2757 C  CZ  . TYR B  1 9   ? -8.84695  -2.90582  84.07530  1.000 55.89903  ? 35  TYR B CZ  1 
ATOM   2758 O  OH  . TYR B  1 9   ? -7.57374  -2.76957  84.57968  1.000 56.94258  ? 35  TYR B OH  1 
ATOM   2759 N  N   . ASN B  1 10  ? -11.83387 -4.79972  79.43585  1.000 46.87614  ? 36  ASN B N   1 
ATOM   2760 C  CA  . ASN B  1 10  ? -11.68476 -6.02705  78.66822  1.000 47.01848  ? 36  ASN B CA  1 
ATOM   2761 C  C   . ASN B  1 10  ? -10.20468 -6.35326  78.51638  1.000 47.78144  ? 36  ASN B C   1 
ATOM   2762 O  O   . ASN B  1 10  ? -9.32928  -5.54396  78.83258  1.000 39.92696  ? 36  ASN B O   1 
ATOM   2763 C  CB  . ASN B  1 10  ? -12.35854 -5.90459  77.29284  1.000 45.22645  ? 36  ASN B CB  1 
ATOM   2764 C  CG  . ASN B  1 10  ? -12.47491 -7.23680  76.57436  1.000 41.36990  ? 36  ASN B CG  1 
ATOM   2765 O  OD1 . ASN B  1 10  ? -12.39111 -8.29809  77.19253  1.000 40.73187  ? 36  ASN B OD1 1 
ATOM   2766 N  ND2 . ASN B  1 10  ? -12.66048 -7.18645  75.26065  1.000 38.85010  ? 36  ASN B ND2 1 
ATOM   2767 N  N   . TRP B  1 11  ? -9.93425  -7.56495  78.03861  1.000 47.75801  ? 37  TRP B N   1 
ATOM   2768 C  CA  . TRP B  1 11  ? -8.57849  -7.98338  77.72636  1.000 48.82862  ? 37  TRP B CA  1 
ATOM   2769 C  C   . TRP B  1 11  ? -8.02959  -7.19239  76.54237  1.000 47.38405  ? 37  TRP B C   1 
ATOM   2770 O  O   . TRP B  1 11  ? -8.77305  -6.60696  75.74971  1.000 45.25642  ? 37  TRP B O   1 
ATOM   2771 C  CB  . TRP B  1 11  ? -8.54457  -9.47611  77.40501  1.000 50.78420  ? 37  TRP B CB  1 
ATOM   2772 C  CG  . TRP B  1 11  ? -8.78770  -10.35073 78.58718  1.000 53.97587  ? 37  TRP B CG  1 
ATOM   2773 C  CD1 . TRP B  1 11  ? -9.99599  -10.70540 79.10965  1.000 55.93872  ? 37  TRP B CD1 1 
ATOM   2774 C  CD2 . TRP B  1 11  ? -7.79654  -11.00475 79.38525  1.000 56.23152  ? 37  TRP B CD2 1 
ATOM   2775 N  NE1 . TRP B  1 11  ? -9.81856  -11.53036 80.19382  1.000 58.01470  ? 37  TRP B NE1 1 
ATOM   2776 C  CE2 . TRP B  1 11  ? -8.47646  -11.73156 80.38208  1.000 58.16240  ? 37  TRP B CE2 1 
ATOM   2777 C  CE3 . TRP B  1 11  ? -6.39982  -11.04267 79.35646  1.000 57.36919  ? 37  TRP B CE3 1 
ATOM   2778 C  CZ2 . TRP B  1 11  ? -7.80771  -12.48581 81.34174  1.000 58.64628  ? 37  TRP B CZ2 1 
ATOM   2779 C  CZ3 . TRP B  1 11  ? -5.73896  -11.79511 80.30529  1.000 58.76740  ? 37  TRP B CZ3 1 
ATOM   2780 C  CH2 . TRP B  1 11  ? -6.44242  -12.50540 81.28712  1.000 58.88655  ? 37  TRP B CH2 1 
ATOM   2781 N  N   . SER B  1 12  ? -6.70418  -7.18568  76.42655  1.000 48.40646  ? 38  SER B N   1 
ATOM   2782 C  CA  . SER B  1 12  ? -6.06149  -6.56145  75.27914  1.000 49.12126  ? 38  SER B CA  1 
ATOM   2783 C  C   . SER B  1 12  ? -6.25075  -7.41816  74.03656  1.000 46.66778  ? 38  SER B C   1 
ATOM   2784 O  O   . SER B  1 12  ? -6.11574  -8.64417  74.08257  1.000 45.61371  ? 38  SER B O   1 
ATOM   2785 C  CB  . SER B  1 12  ? -4.57186  -6.34566  75.54800  1.000 52.18513  ? 38  SER B CB  1 
ATOM   2786 O  OG  . SER B  1 12  ? -4.32166  -5.04166  76.04299  1.000 54.39489  ? 38  SER B OG  1 
ATOM   2787 N  N   . ASP B  1 13  ? -6.57614  -6.75959  72.92283  1.000 46.60907  ? 39  ASP B N   1 
ATOM   2788 C  CA  . ASP B  1 13  ? -6.74748  -7.42645  71.63210  1.000 46.80152  ? 39  ASP B CA  1 
ATOM   2789 C  C   . ASP B  1 13  ? -7.80496  -8.52667  71.71176  1.000 46.98849  ? 39  ASP B C   1 
ATOM   2790 O  O   . ASP B  1 13  ? -7.67778  -9.58511  71.09312  1.000 48.11188  ? 39  ASP B O   1 
ATOM   2791 C  CB  . ASP B  1 13  ? -5.41462  -7.98040  71.12106  1.000 47.90959  ? 39  ASP B CB  1 
ATOM   2792 C  CG  . ASP B  1 13  ? -5.43504  -8.27493  69.63563  1.000 49.19071  ? 39  ASP B CG  1 
ATOM   2793 O  OD1 . ASP B  1 13  ? -5.82981  -7.38304  68.85537  1.000 49.50189  ? 39  ASP B OD1 1 
ATOM   2794 O  OD2 . ASP B  1 13  ? -5.05507  -9.40031  69.24999  1.000 50.01383  ? 39  ASP B OD2 1 
ATOM   2795 N  N   . TYR B  1 14  ? -8.85722  -8.27957  72.49172  1.000 46.24898  ? 40  TYR B N   1 
ATOM   2796 C  CA  . TYR B  1 14  ? -9.97170  -9.20937  72.62450  1.000 44.33277  ? 40  TYR B CA  1 
ATOM   2797 C  C   . TYR B  1 14  ? -11.23817 -8.66373  71.97243  1.000 41.38759  ? 40  TYR B C   1 
ATOM   2798 O  O   . TYR B  1 14  ? -12.35295 -8.99974  72.37972  1.000 38.91888  ? 40  TYR B O   1 
ATOM   2799 C  CB  . TYR B  1 14  ? -10.22624 -9.54307  74.09293  1.000 44.41153  ? 40  TYR B CB  1 
ATOM   2800 C  CG  . TYR B  1 14  ? -10.77397 -10.93560 74.30452  1.000 41.99113  ? 40  TYR B CG  1 
ATOM   2801 C  CD1 . TYR B  1 14  ? -10.33002 -12.00006 73.53022  1.000 39.39182  ? 40  TYR B CD1 1 
ATOM   2802 C  CD2 . TYR B  1 14  ? -11.73340 -11.18702 75.27611  1.000 39.70492  ? 40  TYR B CD2 1 
ATOM   2803 C  CE1 . TYR B  1 14  ? -10.82625 -13.27564 73.71720  1.000 38.23215  ? 40  TYR B CE1 1 
ATOM   2804 C  CE2 . TYR B  1 14  ? -12.23559 -12.45955 75.47068  1.000 38.79350  ? 40  TYR B CE2 1 
ATOM   2805 C  CZ  . TYR B  1 14  ? -11.77846 -13.49975 74.68873  1.000 38.81955  ? 40  TYR B CZ  1 
ATOM   2806 O  OH  . TYR B  1 14  ? -12.27486 -14.76904 74.87875  1.000 38.96794  ? 40  TYR B OH  1 
ATOM   2807 N  N   . ILE B  1 15  ? -11.07157 -7.81690  70.95769  1.000 41.16309  ? 41  ILE B N   1 
ATOM   2808 C  CA  . ILE B  1 15  ? -12.19121 -7.23577  70.22951  1.000 39.26629  ? 41  ILE B CA  1 
ATOM   2809 C  C   . ILE B  1 15  ? -11.66342 -6.78370  68.87784  1.000 39.24715  ? 41  ILE B C   1 
ATOM   2810 O  O   . ILE B  1 15  ? -10.46788 -6.51947  68.72068  1.000 39.52022  ? 41  ILE B O   1 
ATOM   2811 C  CB  . ILE B  1 15  ? -12.83585 -6.07065  71.02508  1.000 38.24980  ? 41  ILE B CB  1 
ATOM   2812 C  CG1 . ILE B  1 15  ? -14.27581 -5.83008  70.56606  1.000 38.45373  ? 41  ILE B CG1 1 
ATOM   2813 C  CG2 . ILE B  1 15  ? -12.00438 -4.80144  70.89867  1.000 38.02381  ? 41  ILE B CG2 1 
ATOM   2814 C  CD1 . ILE B  1 15  ? -15.02703 -4.82817  71.41818  1.000 39.03098  ? 41  ILE B CD1 1 
ATOM   2815 N  N   . ALA B  1 16  ? -12.55414 -6.71720  67.89214  1.000 39.13303  ? 42  ALA B N   1 
ATOM   2816 C  CA  . ALA B  1 16  ? -12.15323 -6.26459  66.57204  1.000 42.96581  ? 42  ALA B CA  1 
ATOM   2817 C  C   . ALA B  1 16  ? -11.72279 -4.79840  66.63100  1.000 47.41824  ? 42  ALA B C   1 
ATOM   2818 O  O   . ALA B  1 16  ? -12.22993 -4.02695  67.45052  1.000 48.69020  ? 42  ALA B O   1 
ATOM   2819 C  CB  . ALA B  1 16  ? -13.29274 -6.44334  65.57271  1.000 42.18193  ? 42  ALA B CB  1 
ATOM   2820 N  N   . PRO B  1 17  ? -10.78063 -4.39144  65.77555  1.000 47.04105  ? 43  PRO B N   1 
ATOM   2821 C  CA  . PRO B  1 17  ? -10.22300 -3.03245  65.88874  1.000 46.98924  ? 43  PRO B CA  1 
ATOM   2822 C  C   . PRO B  1 17  ? -11.24016 -1.92005  65.69554  1.000 46.45913  ? 43  PRO B C   1 
ATOM   2823 O  O   . PRO B  1 17  ? -10.99677 -0.79884  66.15858  1.000 47.38464  ? 43  PRO B O   1 
ATOM   2824 C  CB  . PRO B  1 17  ? -9.15087  -3.00105  64.78941  1.000 46.51237  ? 43  PRO B CB  1 
ATOM   2825 C  CG  . PRO B  1 17  ? -8.82064  -4.43636  64.53201  1.000 46.43144  ? 43  PRO B CG  1 
ATOM   2826 C  CD  . PRO B  1 17  ? -10.10262 -5.18114  64.73362  1.000 46.55510  ? 43  PRO B CD  1 
ATOM   2827 N  N   . ASP B  1 18  ? -12.36863 -2.18420  65.03786  1.000 45.59724  ? 44  ASP B N   1 
ATOM   2828 C  CA  . ASP B  1 18  ? -13.33476 -1.14352  64.70939  1.000 45.13473  ? 44  ASP B CA  1 
ATOM   2829 C  C   . ASP B  1 18  ? -14.67924 -1.33125  65.40249  1.000 42.87850  ? 44  ASP B C   1 
ATOM   2830 O  O   . ASP B  1 18  ? -15.64642 -0.65339  65.04184  1.000 44.75302  ? 44  ASP B O   1 
ATOM   2831 C  CB  . ASP B  1 18  ? -13.53865 -1.07618  63.19443  1.000 46.29573  ? 44  ASP B CB  1 
ATOM   2832 C  CG  . ASP B  1 18  ? -14.14491 -2.34660  62.63241  1.000 47.30731  ? 44  ASP B CG  1 
ATOM   2833 O  OD1 . ASP B  1 18  ? -13.88207 -3.43112  63.19389  1.000 47.71801  ? 44  ASP B OD1 1 
ATOM   2834 O  OD2 . ASP B  1 18  ? -14.88647 -2.26061  61.63086  1.000 47.79697  ? 44  ASP B OD2 1 
ATOM   2835 N  N   . THR B  1 19  ? -14.76832 -2.22730  66.38747  1.000 40.33183  ? 45  THR B N   1 
ATOM   2836 C  CA  . THR B  1 19  ? -16.04574 -2.46169  67.05595  1.000 41.03268  ? 45  THR B CA  1 
ATOM   2837 C  C   . THR B  1 19  ? -16.48719 -1.23753  67.84924  1.000 42.23819  ? 45  THR B C   1 
ATOM   2838 O  O   . THR B  1 19  ? -17.60409 -0.73502  67.66742  1.000 41.48642  ? 45  THR B O   1 
ATOM   2839 C  CB  . THR B  1 19  ? -15.94748 -3.67991  67.97440  1.000 39.61140  ? 45  THR B CB  1 
ATOM   2840 O  OG1 . THR B  1 19  ? -15.21101 -4.71765  67.31990  1.000 39.89902  ? 45  THR B OG1 1 
ATOM   2841 C  CG2 . THR B  1 19  ? -17.33496 -4.19605  68.32360  1.000 38.49828  ? 45  THR B CG2 1 
ATOM   2842 N  N   . VAL B  1 20  ? -15.61987 -0.74677  68.73856  1.000 41.86545  ? 46  VAL B N   1 
ATOM   2843 C  CA  . VAL B  1 20  ? -15.98373 0.37405   69.60100  1.000 43.00542  ? 46  VAL B CA  1 
ATOM   2844 C  C   . VAL B  1 20  ? -16.22900 1.62974   68.77458  1.000 43.49348  ? 46  VAL B C   1 
ATOM   2845 O  O   . VAL B  1 20  ? -17.15379 2.40136   69.05351  1.000 45.98816  ? 46  VAL B O   1 
ATOM   2846 C  CB  . VAL B  1 20  ? -14.89721 0.59830   70.66980  1.000 39.11455  ? 46  VAL B CB  1 
ATOM   2847 C  CG1 . VAL B  1 20  ? -15.16461 1.87837   71.44638  1.000 43.86257  ? 46  VAL B CG1 1 
ATOM   2848 C  CG2 . VAL B  1 20  ? -14.82854 -0.59353  71.61073  1.000 38.82571  ? 46  VAL B CG2 1 
ATOM   2849 N  N   . ALA B  1 21  ? -15.41308 1.85198   67.74124  1.000 41.39306  ? 47  ALA B N   1 
ATOM   2850 C  CA  . ALA B  1 21  ? -15.59231 3.03369   66.90296  1.000 41.68706  ? 47  ALA B CA  1 
ATOM   2851 C  C   . ALA B  1 21  ? -16.92012 2.98743   66.15664  1.000 41.20790  ? 47  ALA B C   1 
ATOM   2852 O  O   . ALA B  1 21  ? -17.62667 3.99913   66.06774  1.000 41.13053  ? 47  ALA B O   1 
ATOM   2853 C  CB  . ALA B  1 21  ? -14.42777 3.16424   65.92243  1.000 42.95437  ? 47  ALA B CB  1 
ATOM   2854 N  N   . ASN B  1 22  ? -17.28002 1.81946   65.61824  1.000 40.41088  ? 48  ASN B N   1 
ATOM   2855 C  CA  . ASN B  1 22  ? -18.56004 1.68736   64.92939  1.000 41.19977  ? 48  ASN B CA  1 
ATOM   2856 C  C   . ASN B  1 22  ? -19.72659 1.86767   65.89274  1.000 42.19728  ? 48  ASN B C   1 
ATOM   2857 O  O   . ASN B  1 22  ? -20.72864 2.50838   65.55037  1.000 41.30127  ? 48  ASN B O   1 
ATOM   2858 C  CB  . ASN B  1 22  ? -18.64280 0.33028   64.23124  1.000 41.56147  ? 48  ASN B CB  1 
ATOM   2859 C  CG  . ASN B  1 22  ? -17.73973 0.24407   63.01692  1.000 42.28406  ? 48  ASN B CG  1 
ATOM   2860 O  OD1 . ASN B  1 22  ? -17.27827 1.26109   62.49933  1.000 42.47407  ? 48  ASN B OD1 1 
ATOM   2861 N  ND2 . ASN B  1 22  ? -17.48396 -0.97439  62.55436  1.000 42.10408  ? 48  ASN B ND2 1 
ATOM   2862 N  N   . PHE B  1 23  ? -19.61328 1.31303   67.10322  1.000 43.32279  ? 49  PHE B N   1 
ATOM   2863 C  CA  . PHE B  1 23  ? -20.66426 1.49454   68.10012  1.000 44.75546  ? 49  PHE B CA  1 
ATOM   2864 C  C   . PHE B  1 23  ? -20.82716 2.96519   68.46649  1.000 48.14102  ? 49  PHE B C   1 
ATOM   2865 O  O   . PHE B  1 23  ? -21.95373 3.46536   68.57641  1.000 50.33450  ? 49  PHE B O   1 
ATOM   2866 C  CB  . PHE B  1 23  ? -20.35418 0.65836   69.34270  1.000 43.73052  ? 49  PHE B CB  1 
ATOM   2867 C  CG  . PHE B  1 23  ? -21.33089 0.85349   70.46719  1.000 42.94261  ? 49  PHE B CG  1 
ATOM   2868 C  CD1 . PHE B  1 23  ? -22.55743 0.21041   70.45603  1.000 42.56267  ? 49  PHE B CD1 1 
ATOM   2869 C  CD2 . PHE B  1 23  ? -21.01997 1.67413   71.53916  1.000 45.17247  ? 49  PHE B CD2 1 
ATOM   2870 C  CE1 . PHE B  1 23  ? -23.45793 0.38586   71.48992  1.000 43.44138  ? 49  PHE B CE1 1 
ATOM   2871 C  CE2 . PHE B  1 23  ? -21.91681 1.85387   72.57632  1.000 45.38903  ? 49  PHE B CE2 1 
ATOM   2872 C  CZ  . PHE B  1 23  ? -23.13677 1.20822   72.55139  1.000 44.34517  ? 49  PHE B CZ  1 
ATOM   2873 N  N   . GLU B  1 24  ? -19.71045 3.67343   68.65778  1.000 49.26436  ? 50  GLU B N   1 
ATOM   2874 C  CA  . GLU B  1 24  ? -19.77251 5.09771   68.96928  1.000 49.40124  ? 50  GLU B CA  1 
ATOM   2875 C  C   . GLU B  1 24  ? -20.39819 5.88324   67.82615  1.000 50.30955  ? 50  GLU B C   1 
ATOM   2876 O  O   . GLU B  1 24  ? -21.21525 6.78322   68.05435  1.000 51.24599  ? 50  GLU B O   1 
ATOM   2877 C  CB  . GLU B  1 24  ? -18.37238 5.63336   69.27106  1.000 49.09496  ? 50  GLU B CB  1 
ATOM   2878 C  CG  . GLU B  1 24  ? -17.76368 5.13258   70.56827  1.000 49.36096  ? 50  GLU B CG  1 
ATOM   2879 C  CD  . GLU B  1 24  ? -16.34280 5.62484   70.76699  1.000 50.87725  ? 50  GLU B CD  1 
ATOM   2880 O  OE1 . GLU B  1 24  ? -15.62717 5.79980   69.75802  1.000 51.16817  ? 50  GLU B OE1 1 
ATOM   2881 O  OE2 . GLU B  1 24  ? -15.94121 5.83779   71.93020  1.000 51.72071  ? 50  GLU B OE2 1 
ATOM   2882 N  N   . LYS B  1 25  ? -20.02336 5.55933   66.58651  1.000 49.31830  ? 51  LYS B N   1 
ATOM   2883 C  CA  . LYS B  1 25  ? -20.56668 6.28084   65.44204  1.000 48.94414  ? 51  LYS B CA  1 
ATOM   2884 C  C   . LYS B  1 25  ? -22.06161 6.03200   65.28940  1.000 46.73546  ? 51  LYS B C   1 
ATOM   2885 O  O   . LYS B  1 25  ? -22.81024 6.94127   64.91564  1.000 46.73120  ? 51  LYS B O   1 
ATOM   2886 C  CB  . LYS B  1 25  ? -19.82008 5.88441   64.16854  1.000 51.00344  ? 51  LYS B CB  1 
ATOM   2887 C  CG  . LYS B  1 25  ? -18.82637 6.92934   63.68512  1.000 52.52415  ? 51  LYS B CG  1 
ATOM   2888 C  CD  . LYS B  1 25  ? -18.33067 6.61723   62.28225  1.000 53.27652  ? 51  LYS B CD  1 
ATOM   2889 C  CE  . LYS B  1 25  ? -17.12002 5.69828   62.31535  1.000 53.23239  ? 51  LYS B CE  1 
ATOM   2890 N  NZ  . LYS B  1 25  ? -15.90861 6.39383   62.83117  1.000 53.86679  ? 51  LYS B NZ  1 
ATOM   2891 N  N   . GLU B  1 26  ? -22.51968 4.81340   65.58408  1.000 45.25003  ? 52  GLU B N   1 
ATOM   2892 C  CA  . GLU B  1 26  ? -23.93869 4.51512   65.42101  1.000 44.68108  ? 52  GLU B CA  1 
ATOM   2893 C  C   . GLU B  1 26  ? -24.77924 5.10381   66.54860  1.000 45.10359  ? 52  GLU B C   1 
ATOM   2894 O  O   . GLU B  1 26  ? -25.84523 5.67574   66.29463  1.000 45.90584  ? 52  GLU B O   1 
ATOM   2895 C  CB  . GLU B  1 26  ? -24.16145 3.00460   65.33773  1.000 43.92119  ? 52  GLU B CB  1 
ATOM   2896 C  CG  . GLU B  1 26  ? -25.62994 2.61912   65.21007  1.000 44.95600  ? 52  GLU B CG  1 
ATOM   2897 C  CD  . GLU B  1 26  ? -25.85512 1.12045   65.23156  1.000 46.38673  ? 52  GLU B CD  1 
ATOM   2898 O  OE1 . GLU B  1 26  ? -24.90415 0.36756   64.93797  1.000 47.03849  ? 52  GLU B OE1 1 
ATOM   2899 O  OE2 . GLU B  1 26  ? -26.98799 0.69521   65.54131  1.000 47.88880  ? 52  GLU B OE2 1 
ATOM   2900 N  N   . THR B  1 27  ? -24.32211 4.97873   67.79533  1.000 45.50939  ? 53  THR B N   1 
ATOM   2901 C  CA  . THR B  1 27  ? -25.13872 5.35073   68.94355  1.000 46.69618  ? 53  THR B CA  1 
ATOM   2902 C  C   . THR B  1 27  ? -24.86577 6.75334   69.46929  1.000 49.39016  ? 53  THR B C   1 
ATOM   2903 O  O   . THR B  1 27  ? -25.72799 7.31576   70.15341  1.000 51.96688  ? 53  THR B O   1 
ATOM   2904 C  CB  . THR B  1 27  ? -24.93143 4.35079   70.08750  1.000 45.04922  ? 53  THR B CB  1 
ATOM   2905 O  OG1 . THR B  1 27  ? -23.59162 4.46165   70.58297  1.000 44.05562  ? 53  THR B OG1 1 
ATOM   2906 C  CG2 . THR B  1 27  ? -25.17019 2.93051   69.60154  1.000 40.76282  ? 53  THR B CG2 1 
ATOM   2907 N  N   . GLY B  1 28  ? -23.70316 7.32997   69.17412  1.000 48.45433  ? 54  GLY B N   1 
ATOM   2908 C  CA  . GLY B  1 28  ? -23.32479 8.60161   69.75202  1.000 47.77460  ? 54  GLY B CA  1 
ATOM   2909 C  C   . GLY B  1 28  ? -22.77748 8.52077   71.15955  1.000 49.52174  ? 54  GLY B C   1 
ATOM   2910 O  O   . GLY B  1 28  ? -22.42248 9.56051   71.72983  1.000 50.61332  ? 54  GLY B O   1 
ATOM   2911 N  N   . ILE B  1 29  ? -22.69871 7.32191   71.73783  1.000 49.03143  ? 55  ILE B N   1 
ATOM   2912 C  CA  . ILE B  1 29  ? -22.16179 7.15758   73.08126  1.000 50.11879  ? 55  ILE B CA  1 
ATOM   2913 C  C   . ILE B  1 29  ? -20.64741 7.31319   73.04910  1.000 51.55728  ? 55  ILE B C   1 
ATOM   2914 O  O   . ILE B  1 29  ? -19.97595 6.85112   72.11673  1.000 50.16993  ? 55  ILE B O   1 
ATOM   2915 C  CB  . ILE B  1 29  ? -22.57066 5.78526   73.64430  1.000 49.41838  ? 55  ILE B CB  1 
ATOM   2916 C  CG1 . ILE B  1 29  ? -24.09171 5.62230   73.59553  1.000 50.66308  ? 55  ILE B CG1 1 
ATOM   2917 C  CG2 . ILE B  1 29  ? -22.05272 5.60186   75.06364  1.000 48.43882  ? 55  ILE B CG2 1 
ATOM   2918 C  CD1 . ILE B  1 29  ? -24.56666 4.22137   73.91215  1.000 50.82023  ? 55  ILE B CD1 1 
ATOM   2919 N  N   . LYS B  1 30  ? -20.10030 7.97433   74.06739  1.000 52.31998  ? 56  LYS B N   1 
ATOM   2920 C  CA  . LYS B  1 30  ? -18.65569 8.11068   74.22539  1.000 53.85616  ? 56  LYS B CA  1 
ATOM   2921 C  C   . LYS B  1 30  ? -18.15308 6.94422   75.06516  1.000 51.48414  ? 56  LYS B C   1 
ATOM   2922 O  O   . LYS B  1 30  ? -18.37824 6.90145   76.27839  1.000 51.61479  ? 56  LYS B O   1 
ATOM   2923 C  CB  . LYS B  1 30  ? -18.30477 9.44318   74.87842  1.000 57.91105  ? 56  LYS B CB  1 
ATOM   2924 C  CG  . LYS B  1 30  ? -18.43761 10.62878  73.94953  1.000 60.69084  ? 56  LYS B CG  1 
ATOM   2925 C  CD  . LYS B  1 30  ? -19.73981 11.35914  74.21965  1.000 62.51670  ? 56  LYS B CD  1 
ATOM   2926 C  CE  . LYS B  1 30  ? -20.15390 12.20225  73.03385  1.000 62.83204  ? 56  LYS B CE  1 
ATOM   2927 N  NZ  . LYS B  1 30  ? -20.40374 11.38564  71.81959  1.000 61.82871  ? 56  LYS B NZ  1 
ATOM   2928 N  N   . VAL B  1 31  ? -17.46620 6.00532   74.42482  1.000 49.59058  ? 57  VAL B N   1 
ATOM   2929 C  CA  . VAL B  1 31  ? -16.99740 4.78979   75.07806  1.000 48.06948  ? 57  VAL B CA  1 
ATOM   2930 C  C   . VAL B  1 31  ? -15.54534 4.98746   75.49045  1.000 49.22001  ? 57  VAL B C   1 
ATOM   2931 O  O   . VAL B  1 31  ? -14.66975 5.17989   74.63743  1.000 49.73901  ? 57  VAL B O   1 
ATOM   2932 C  CB  . VAL B  1 31  ? -17.14800 3.56687   74.15995  1.000 44.78310  ? 57  VAL B CB  1 
ATOM   2933 C  CG1 . VAL B  1 31  ? -16.66609 2.31096   74.87030  1.000 42.71794  ? 57  VAL B CG1 1 
ATOM   2934 C  CG2 . VAL B  1 31  ? -18.59408 3.41502   73.71230  1.000 44.13694  ? 57  VAL B CG2 1 
ATOM   2935 N  N   . VAL B  1 32  ? -15.29185 4.94886   76.79585  1.000 48.80949  ? 58  VAL B N   1 
ATOM   2936 C  CA  . VAL B  1 32  ? -13.93495 4.92916   77.32951  1.000 48.66184  ? 58  VAL B CA  1 
ATOM   2937 C  C   . VAL B  1 32  ? -13.56284 3.46774   77.54649  1.000 47.23809  ? 58  VAL B C   1 
ATOM   2938 O  O   . VAL B  1 32  ? -14.08201 2.81254   78.45321  1.000 43.40950  ? 58  VAL B O   1 
ATOM   2939 C  CB  . VAL B  1 32  ? -13.82173 5.73833   78.62600  1.000 50.75374  ? 58  VAL B CB  1 
ATOM   2940 C  CG1 . VAL B  1 32  ? -12.35895 5.97071   78.97907  1.000 51.19723  ? 58  VAL B CG1 1 
ATOM   2941 C  CG2 . VAL B  1 32  ? -14.55534 7.06305   78.48303  1.000 50.89583  ? 58  VAL B CG2 1 
ATOM   2942 N  N   . TYR B  1 33  ? -12.66590 2.95594   76.70756  1.000 48.72430  ? 59  TYR B N   1 
ATOM   2943 C  CA  . TYR B  1 33  ? -12.36580 1.52550   76.63513  1.000 48.59264  ? 59  TYR B CA  1 
ATOM   2944 C  C   . TYR B  1 33  ? -11.03213 1.26686   77.33266  1.000 51.25020  ? 59  TYR B C   1 
ATOM   2945 O  O   . TYR B  1 33  ? -9.97032  1.26697   76.70788  1.000 52.53847  ? 59  TYR B O   1 
ATOM   2946 C  CB  . TYR B  1 33  ? -12.34564 1.07038   75.17912  1.000 47.11891  ? 59  TYR B CB  1 
ATOM   2947 C  CG  . TYR B  1 33  ? -12.30365 -0.42572  74.97032  1.000 45.43145  ? 59  TYR B CG  1 
ATOM   2948 C  CD1 . TYR B  1 33  ? -13.46623 -1.18519  74.99640  1.000 43.94869  ? 59  TYR B CD1 1 
ATOM   2949 C  CD2 . TYR B  1 33  ? -11.10310 -1.07413  74.71970  1.000 45.88052  ? 59  TYR B CD2 1 
ATOM   2950 C  CE1 . TYR B  1 33  ? -13.43074 -2.55402  74.79499  1.000 43.48781  ? 59  TYR B CE1 1 
ATOM   2951 C  CE2 . TYR B  1 33  ? -11.05657 -2.43983  74.51679  1.000 45.10502  ? 59  TYR B CE2 1 
ATOM   2952 C  CZ  . TYR B  1 33  ? -12.22273 -3.17531  74.55536  1.000 43.57119  ? 59  TYR B CZ  1 
ATOM   2953 O  OH  . TYR B  1 33  ? -12.17835 -4.53505  74.35305  1.000 38.23445  ? 59  TYR B OH  1 
ATOM   2954 N  N   . ASP B  1 34  ? -11.08966 1.05008   78.64429  1.000 52.14292  ? 60  ASP B N   1 
ATOM   2955 C  CA  . ASP B  1 34  ? -9.89978  0.68021   79.39312  1.000 53.52229  ? 60  ASP B CA  1 
ATOM   2956 C  C   . ASP B  1 34  ? -9.59881  -0.80223  79.19938  1.000 51.42643  ? 60  ASP B C   1 
ATOM   2957 O  O   . ASP B  1 34  ? -10.44979 -1.58520  78.76845  1.000 49.71395  ? 60  ASP B O   1 
ATOM   2958 C  CB  . ASP B  1 34  ? -10.07154 1.00242   80.87718  1.000 55.67547  ? 60  ASP B CB  1 
ATOM   2959 C  CG  . ASP B  1 34  ? -10.08224 2.49356   81.14890  1.000 58.22886  ? 60  ASP B CG  1 
ATOM   2960 O  OD1 . ASP B  1 34  ? -9.31613  3.22497   80.48613  1.000 59.15600  ? 60  ASP B OD1 1 
ATOM   2961 O  OD2 . ASP B  1 34  ? -10.85480 2.93505   82.02464  1.000 59.59319  ? 60  ASP B OD2 1 
ATOM   2962 N  N   . VAL B  1 35  ? -8.36709  -1.18770  79.52787  1.000 52.06057  ? 61  VAL B N   1 
ATOM   2963 C  CA  . VAL B  1 35  ? -7.88471  -2.52148  79.19922  1.000 51.50405  ? 61  VAL B CA  1 
ATOM   2964 C  C   . VAL B  1 35  ? -6.94652  -3.01125  80.29463  1.000 52.19941  ? 61  VAL B C   1 
ATOM   2965 O  O   . VAL B  1 35  ? -6.21311  -2.23173  80.90930  1.000 52.98772  ? 61  VAL B O   1 
ATOM   2966 C  CB  . VAL B  1 35  ? -7.19858  -2.52706  77.81137  1.000 52.66261  ? 61  VAL B CB  1 
ATOM   2967 C  CG1 . VAL B  1 35  ? -5.85472  -1.80808  77.85645  1.000 52.66445  ? 61  VAL B CG1 1 
ATOM   2968 C  CG2 . VAL B  1 35  ? -7.04175  -3.93574  77.30930  1.000 52.74497  ? 61  VAL B CG2 1 
ATOM   2969 N  N   . PHE B  1 36  ? -6.99203  -4.31730  80.54595  1.000 53.88660  ? 62  PHE B N   1 
ATOM   2970 C  CA  . PHE B  1 36  ? -6.08692  -5.00565  81.45425  1.000 58.93656  ? 62  PHE B CA  1 
ATOM   2971 C  C   . PHE B  1 36  ? -5.37941  -6.12306  80.69743  1.000 63.65524  ? 62  PHE B C   1 
ATOM   2972 O  O   . PHE B  1 36  ? -5.76712  -6.49206  79.58608  1.000 64.11395  ? 62  PHE B O   1 
ATOM   2973 C  CB  . PHE B  1 36  ? -6.83557  -5.56535  82.67198  1.000 58.34186  ? 62  PHE B CB  1 
ATOM   2974 C  CG  . PHE B  1 36  ? -7.93838  -6.52663  82.32190  1.000 55.65380  ? 62  PHE B CG  1 
ATOM   2975 C  CD1 . PHE B  1 36  ? -7.69174  -7.88720  82.23733  1.000 53.69233  ? 62  PHE B CD1 1 
ATOM   2976 C  CD2 . PHE B  1 36  ? -9.22298  -6.06957  82.08217  1.000 54.11932  ? 62  PHE B CD2 1 
ATOM   2977 C  CE1 . PHE B  1 36  ? -8.70505  -8.77070  81.91810  1.000 51.70530  ? 62  PHE B CE1 1 
ATOM   2978 C  CE2 . PHE B  1 36  ? -10.24028 -6.94872  81.76622  1.000 51.74629  ? 62  PHE B CE2 1 
ATOM   2979 C  CZ  . PHE B  1 36  ? -9.98032  -8.30022  81.68046  1.000 50.87221  ? 62  PHE B CZ  1 
ATOM   2980 N  N   . ASP B  1 37  ? -4.33198  -6.67677  81.31091  1.000 66.29252  ? 63  ASP B N   1 
ATOM   2981 C  CA  . ASP B  1 37  ? -3.48726  -7.64106  80.62265  1.000 69.07320  ? 63  ASP B CA  1 
ATOM   2982 C  C   . ASP B  1 37  ? -3.43284  -9.02345  81.26221  1.000 71.26925  ? 63  ASP B C   1 
ATOM   2983 O  O   . ASP B  1 37  ? -2.87289  -9.93709  80.64536  1.000 71.12730  ? 63  ASP B O   1 
ATOM   2984 C  CB  . ASP B  1 37  ? -2.05819  -7.09201  80.48145  1.000 71.30788  ? 63  ASP B CB  1 
ATOM   2985 C  CG  . ASP B  1 37  ? -1.91952  -6.13406  79.31014  1.000 73.80975  ? 63  ASP B CG  1 
ATOM   2986 O  OD1 . ASP B  1 37  ? -1.49399  -4.97939  79.52321  1.000 75.73474  ? 63  ASP B OD1 1 
ATOM   2987 O  OD2 . ASP B  1 37  ? -2.24839  -6.53655  78.17391  1.000 74.01032  ? 63  ASP B OD2 1 
ATOM   2988 N  N   . SER B  1 38  ? -3.98815  -9.21432  82.45861  1.000 74.42353  ? 64  SER B N   1 
ATOM   2989 C  CA  . SER B  1 38  ? -4.13420  -10.55611 83.01393  1.000 76.68199  ? 64  SER B CA  1 
ATOM   2990 C  C   . SER B  1 38  ? -5.15649  -10.53150 84.14284  1.000 78.46892  ? 64  SER B C   1 
ATOM   2991 O  O   . SER B  1 38  ? -5.54443  -9.47048  84.63801  1.000 79.74450  ? 64  SER B O   1 
ATOM   2992 C  CB  . SER B  1 38  ? -2.79511  -11.13505 83.48172  1.000 78.61187  ? 64  SER B CB  1 
ATOM   2993 O  OG  . SER B  1 38  ? -2.20845  -11.91093 82.44705  1.000 78.55399  ? 64  SER B OG  1 
ATOM   2994 N  N   . ASN B  1 39  ? -5.56531  -11.73738 84.55441  1.000 77.47617  ? 65  ASN B N   1 
ATOM   2995 C  CA  . ASN B  1 39  ? -6.77287  -11.91330 85.36049  1.000 79.52025  ? 65  ASN B CA  1 
ATOM   2996 C  C   . ASN B  1 39  ? -6.72142  -11.10780 86.65297  1.000 79.81508  ? 65  ASN B C   1 
ATOM   2997 O  O   . ASN B  1 39  ? -7.69503  -10.43413 87.01394  1.000 80.16943  ? 65  ASN B O   1 
ATOM   2998 C  CB  . ASN B  1 39  ? -6.97431  -13.39655 85.67736  1.000 81.35355  ? 65  ASN B CB  1 
ATOM   2999 C  CG  . ASN B  1 39  ? -7.00492  -14.26300 84.43589  1.000 84.48283  ? 65  ASN B CG  1 
ATOM   3000 O  OD1 . ASN B  1 39  ? -5.98076  -14.80345 84.01819  1.000 86.09507  ? 65  ASN B OD1 1 
ATOM   3001 N  ND2 . ASN B  1 39  ? -8.18550  -14.41450 83.84796  1.000 85.68798  ? 65  ASN B ND2 1 
ATOM   3002 N  N   . GLU B  1 40  ? -5.59043  -11.17068 87.36324  1.000 77.92717  ? 66  GLU B N   1 
ATOM   3003 C  CA  . GLU B  1 40  ? -5.51964  -10.63284 88.71990  1.000 76.68048  ? 66  GLU B CA  1 
ATOM   3004 C  C   . GLU B  1 40  ? -5.91956  -9.16356  88.76864  1.000 75.04790  ? 66  GLU B C   1 
ATOM   3005 O  O   . GLU B  1 40  ? -6.58966  -8.73107  89.71255  1.000 76.67882  ? 66  GLU B O   1 
ATOM   3006 C  CB  . GLU B  1 40  ? -4.11288  -10.82562 89.28775  1.000 77.83129  ? 66  GLU B CB  1 
ATOM   3007 C  CG  . GLU B  1 40  ? -3.55726  -12.23075 89.11443  1.000 77.52607  ? 66  GLU B CG  1 
ATOM   3008 C  CD  . GLU B  1 40  ? -2.81232  -12.40692 87.80586  1.000 78.10807  ? 66  GLU B CD  1 
ATOM   3009 O  OE1 . GLU B  1 40  ? -2.79541  -11.45472 86.99745  1.000 78.42736  ? 66  GLU B OE1 1 
ATOM   3010 O  OE2 . GLU B  1 40  ? -2.24583  -13.49753 87.58485  1.000 78.16243  ? 66  GLU B OE2 1 
ATOM   3011 N  N   . VAL B  1 41  ? -5.54059  -8.38787  87.75068  1.000 71.60664  ? 67  VAL B N   1 
ATOM   3012 C  CA  . VAL B  1 41  ? -5.87520  -6.96400  87.72504  1.000 70.51533  ? 67  VAL B CA  1 
ATOM   3013 C  C   . VAL B  1 41  ? -7.38680  -6.77181  87.79159  1.000 68.43548  ? 67  VAL B C   1 
ATOM   3014 O  O   . VAL B  1 41  ? -7.91380  -6.13634  88.71510  1.000 68.72568  ? 67  VAL B O   1 
ATOM   3015 C  CB  . VAL B  1 41  ? -5.27984  -6.29422  86.47402  1.000 70.10869  ? 67  VAL B CB  1 
ATOM   3016 C  CG1 . VAL B  1 41  ? -5.27102  -4.78178  86.63320  1.000 70.66851  ? 67  VAL B CG1 1 
ATOM   3017 C  CG2 . VAL B  1 41  ? -3.87583  -6.81875  86.20789  1.000 70.21605  ? 67  VAL B CG2 1 
ATOM   3018 N  N   . LEU B  1 42  ? -8.10315  -7.32647  86.80873  1.000 65.86851  ? 68  LEU B N   1 
ATOM   3019 C  CA  . LEU B  1 42  ? -9.55244  -7.16092  86.74880  1.000 63.24455  ? 68  LEU B CA  1 
ATOM   3020 C  C   . LEU B  1 42  ? -10.23749 -7.76838  87.96673  1.000 63.25052  ? 68  LEU B C   1 
ATOM   3021 O  O   . LEU B  1 42  ? -11.17798 -7.18098  88.51388  1.000 61.90421  ? 68  LEU B O   1 
ATOM   3022 C  CB  . LEU B  1 42  ? -10.09583 -7.78503  85.46287  1.000 60.37854  ? 68  LEU B CB  1 
ATOM   3023 C  CG  . LEU B  1 42  ? -11.58891 -8.12507  85.43645  1.000 57.52817  ? 68  LEU B CG  1 
ATOM   3024 C  CD1 . LEU B  1 42  ? -12.43167 -6.92334  85.03045  1.000 56.13954  ? 68  LEU B CD1 1 
ATOM   3025 C  CD2 . LEU B  1 42  ? -11.84985 -9.30642  84.51720  1.000 55.62840  ? 68  LEU B CD2 1 
ATOM   3026 N  N   . GLU B  1 43  ? -9.77409  -8.93779  88.41504  1.000 64.76936  ? 69  GLU B N   1 
ATOM   3027 C  CA  . GLU B  1 43  ? -10.44217 -9.61614  89.52218  1.000 68.06966  ? 69  GLU B CA  1 
ATOM   3028 C  C   . GLU B  1 43  ? -10.29653 -8.83484  90.82646  1.000 71.32420  ? 69  GLU B C   1 
ATOM   3029 O  O   . GLU B  1 43  ? -11.27569 -8.66208  91.56913  1.000 71.22256  ? 69  GLU B O   1 
ATOM   3030 C  CB  . GLU B  1 43  ? -9.89364  -11.03712 89.66119  1.000 67.97950  ? 69  GLU B CB  1 
ATOM   3031 C  CG  . GLU B  1 43  ? -10.26312 -11.94964 88.49010  1.000 66.96532  ? 69  GLU B CG  1 
ATOM   3032 C  CD  . GLU B  1 43  ? -9.71316  -13.35668 88.63613  1.000 67.39951  ? 69  GLU B CD  1 
ATOM   3033 O  OE1 . GLU B  1 43  ? -10.01680 -14.20725 87.77240  1.000 66.09393  ? 69  GLU B OE1 1 
ATOM   3034 O  OE2 . GLU B  1 43  ? -8.97631  -13.61206 89.61160  1.000 68.22929  ? 69  GLU B OE2 1 
ATOM   3035 N  N   . GLY B  1 44  ? -9.08877  -8.34588  91.12038  1.000 74.87650  ? 70  GLY B N   1 
ATOM   3036 C  CA  . GLY B  1 44  ? -8.90204  -7.53866  92.31324  1.000 75.74858  ? 70  GLY B CA  1 
ATOM   3037 C  C   . GLY B  1 44  ? -9.63251  -6.21324  92.23384  1.000 77.18319  ? 70  GLY B C   1 
ATOM   3038 O  O   . GLY B  1 44  ? -10.22281 -5.75955  93.22032  1.000 76.88297  ? 70  GLY B O   1 
ATOM   3039 N  N   . LYS B  1 45  ? -9.61962  -5.58046  91.05600  1.000 73.96552  ? 71  LYS B N   1 
ATOM   3040 C  CA  . LYS B  1 45  ? -10.37710 -4.34736  90.87938  1.000 73.33694  ? 71  LYS B CA  1 
ATOM   3041 C  C   . LYS B  1 45  ? -11.86328 -4.56664  91.14095  1.000 76.37428  ? 71  LYS B C   1 
ATOM   3042 O  O   . LYS B  1 45  ? -12.51219 -3.73847  91.78854  1.000 77.31354  ? 71  LYS B O   1 
ATOM   3043 C  CB  . LYS B  1 45  ? -10.15247 -3.79094  89.47203  1.000 70.49152  ? 71  LYS B CB  1 
ATOM   3044 C  CG  . LYS B  1 45  ? -8.86160  -3.00732  89.30921  1.000 69.72111  ? 71  LYS B CG  1 
ATOM   3045 C  CD  . LYS B  1 45  ? -8.48465  -2.86719  87.84462  1.000 68.45450  ? 71  LYS B CD  1 
ATOM   3046 C  CE  . LYS B  1 45  ? -8.18140  -1.42053  87.49084  1.000 69.65645  ? 71  LYS B CE  1 
ATOM   3047 N  NZ  . LYS B  1 45  ? -9.41046  -0.58226  87.44604  1.000 70.30081  ? 71  LYS B NZ  1 
ATOM   3048 N  N   . LEU B  1 46  ? -12.41808 -5.68422  90.66087  1.000 77.94560  ? 72  LEU B N   1 
ATOM   3049 C  CA  . LEU B  1 46  ? -13.85707 -5.90209  90.78915  1.000 80.70274  ? 72  LEU B CA  1 
ATOM   3050 C  C   . LEU B  1 46  ? -14.25353 -6.26551  92.21430  1.000 86.72567  ? 72  LEU B C   1 
ATOM   3051 O  O   . LEU B  1 46  ? -15.25510 -5.75637  92.72660  1.000 87.41877  ? 72  LEU B O   1 
ATOM   3052 C  CB  . LEU B  1 46  ? -14.33485 -6.97256  89.80624  1.000 77.19633  ? 72  LEU B CB  1 
ATOM   3053 C  CG  . LEU B  1 46  ? -14.62185 -6.48544  88.39088  1.000 75.61660  ? 72  LEU B CG  1 
ATOM   3054 C  CD1 . LEU B  1 46  ? -15.18634 -7.62127  87.56032  1.000 74.25434  ? 72  LEU B CD1 1 
ATOM   3055 C  CD2 . LEU B  1 46  ? -15.59602 -5.32078  88.44217  1.000 76.03931  ? 72  LEU B CD2 1 
ATOM   3056 N  N   . MET B  1 47  ? -13.49936 -7.15153  92.86903  1.000 91.03255  ? 73  MET B N   1 
ATOM   3057 C  CA  . MET B  1 47  ? -13.83728 -7.50497  94.24865  1.000 91.50952  ? 73  MET B CA  1 
ATOM   3058 C  C   . MET B  1 47  ? -13.46338 -6.40134  95.22996  1.000 91.14658  ? 73  MET B C   1 
ATOM   3059 O  O   . MET B  1 47  ? -13.86556 -6.44687  96.40539  1.000 92.89582  ? 73  MET B O   1 
ATOM   3060 C  CB  . MET B  1 47  ? -13.14192 -8.78341  94.67853  1.000 92.63473  ? 73  MET B CB  1 
ATOM   3061 C  CG  . MET B  1 47  ? -14.05710 -9.99628  94.59035  1.000 95.29707  ? 73  MET B CG  1 
ATOM   3062 S  SD  . MET B  1 47  ? -15.50643 -9.75911  95.67669  1.000 100.31504 ? 73  MET B SD  1 
ATOM   3063 C  CE  . MET B  1 47  ? -14.76550 -9.69720  97.30664  1.000 101.31096 ? 73  MET B CE  1 
ATOM   3064 N  N   . ALA B  1 48  ? -12.66732 -5.42791  94.78801  1.000 88.66254  ? 74  ALA B N   1 
ATOM   3065 C  CA  . ALA B  1 48  ? -12.65890 -4.16084  95.49076  1.000 88.45276  ? 74  ALA B CA  1 
ATOM   3066 C  C   . ALA B  1 48  ? -14.06884 -3.59504  95.39727  1.000 86.79379  ? 74  ALA B C   1 
ATOM   3067 O  O   . ALA B  1 48  ? -14.78302 -3.49973  96.40127  1.000 86.46111  ? 74  ALA B O   1 
ATOM   3068 C  CB  . ALA B  1 48  ? -11.62665 -3.23133  94.87806  1.000 88.86245  ? 74  ALA B CB  1 
ATOM   3069 N  N   . GLY B  1 49  ? -14.47781 -3.25232  94.18334  1.000 85.90570  ? 75  GLY B N   1 
ATOM   3070 C  CA  . GLY B  1 49  ? -15.76999 -2.65706  93.91326  1.000 85.10428  ? 75  GLY B CA  1 
ATOM   3071 C  C   . GLY B  1 49  ? -15.62403 -1.20457  93.50851  1.000 84.01698  ? 75  GLY B C   1 
ATOM   3072 O  O   . GLY B  1 49  ? -14.52241 -0.65896  93.43369  1.000 85.18627  ? 75  GLY B O   1 
ATOM   3073 N  N   . SER B  1 50  ? -16.77921 -0.59170  93.24372  1.000 79.79984  ? 76  SER B N   1 
ATOM   3074 C  CA  . SER B  1 50  ? -16.85540 0.80486   92.83257  1.000 77.37195  ? 76  SER B CA  1 
ATOM   3075 C  C   . SER B  1 50  ? -15.86796 1.09264   91.70777  1.000 72.81715  ? 76  SER B C   1 
ATOM   3076 O  O   . SER B  1 50  ? -15.20449 2.13508   91.70116  1.000 72.44837  ? 76  SER B O   1 
ATOM   3077 C  CB  . SER B  1 50  ? -16.59790 1.72332   94.02584  1.000 79.39102  ? 76  SER B CB  1 
ATOM   3078 O  OG  . SER B  1 50  ? -16.38329 3.05468   93.60238  1.000 80.04838  ? 76  SER B OG  1 
ATOM   3079 N  N   . THR B  1 51  ? -15.75814 0.16042   90.75825  1.000 68.91039  ? 77  THR B N   1 
ATOM   3080 C  CA  . THR B  1 51  ? -14.71985 0.23911   89.73859  1.000 64.23137  ? 77  THR B CA  1 
ATOM   3081 C  C   . THR B  1 51  ? -14.97882 1.33533   88.71594  1.000 62.03855  ? 77  THR B C   1 
ATOM   3082 O  O   . THR B  1 51  ? -14.05036 1.72892   88.00249  1.000 59.93133  ? 77  THR B O   1 
ATOM   3083 C  CB  . THR B  1 51  ? -14.59213 -1.10566  89.02706  1.000 60.70247  ? 77  THR B CB  1 
ATOM   3084 O  OG1 . THR B  1 51  ? -15.70268 -1.28141  88.13922  1.000 59.75946  ? 77  THR B OG1 1 
ATOM   3085 C  CG2 . THR B  1 51  ? -14.58461 -2.23508  90.03666  1.000 60.31975  ? 77  THR B CG2 1 
ATOM   3086 N  N   . GLY B  1 52  ? -16.20643 1.83872   88.63057  1.000 62.64887  ? 78  GLY B N   1 
ATOM   3087 C  CA  . GLY B  1 52  ? -16.54738 2.80335   87.60852  1.000 61.15276  ? 78  GLY B CA  1 
ATOM   3088 C  C   . GLY B  1 52  ? -16.81337 2.21185   86.24482  1.000 58.37616  ? 78  GLY B C   1 
ATOM   3089 O  O   . GLY B  1 52  ? -17.02409 2.96792   85.28976  1.000 56.10014  ? 78  GLY B O   1 
ATOM   3090 N  N   . PHE B  1 53  ? -16.80578 0.88841   86.11957  1.000 56.74594  ? 79  PHE B N   1 
ATOM   3091 C  CA  . PHE B  1 53  ? -17.08407 0.23216   84.85270  1.000 55.63465  ? 79  PHE B CA  1 
ATOM   3092 C  C   . PHE B  1 53  ? -18.57144 -0.06624  84.72738  1.000 54.72459  ? 79  PHE B C   1 
ATOM   3093 O  O   . PHE B  1 53  ? -19.26245 -0.31787  85.71818  1.000 55.27736  ? 79  PHE B O   1 
ATOM   3094 C  CB  . PHE B  1 53  ? -16.29334 -1.07197  84.71818  1.000 56.09780  ? 79  PHE B CB  1 
ATOM   3095 C  CG  . PHE B  1 53  ? -14.82320 -0.92917  84.98971  1.000 59.11296  ? 79  PHE B CG  1 
ATOM   3096 C  CD1 . PHE B  1 53  ? -14.12941 -1.93750  85.63747  1.000 60.00569  ? 79  PHE B CD1 1 
ATOM   3097 C  CD2 . PHE B  1 53  ? -14.13150 0.20146   84.58768  1.000 60.92366  ? 79  PHE B CD2 1 
ATOM   3098 C  CE1 . PHE B  1 53  ? -12.77962 -1.81574  85.89473  1.000 61.10904  ? 79  PHE B CE1 1 
ATOM   3099 C  CE2 . PHE B  1 53  ? -12.77756 0.32723   84.83860  1.000 61.76144  ? 79  PHE B CE2 1 
ATOM   3100 C  CZ  . PHE B  1 53  ? -12.10115 -0.68393  85.49183  1.000 61.69643  ? 79  PHE B CZ  1 
ATOM   3101 N  N   . ASP B  1 54  ? -19.06079 -0.03238  83.48927  1.000 53.85692  ? 80  ASP B N   1 
ATOM   3102 C  CA  . ASP B  1 54  ? -20.41616 -0.47045  83.19253  1.000 53.16123  ? 80  ASP B CA  1 
ATOM   3103 C  C   . ASP B  1 54  ? -20.46860 -1.87643  82.61520  1.000 50.01324  ? 80  ASP B C   1 
ATOM   3104 O  O   . ASP B  1 54  ? -21.50572 -2.53754  82.73040  1.000 48.57002  ? 80  ASP B O   1 
ATOM   3105 C  CB  . ASP B  1 54  ? -21.09209 0.49894   82.21564  1.000 54.85571  ? 80  ASP B CB  1 
ATOM   3106 C  CG  . ASP B  1 54  ? -21.14914 1.91704   82.74637  1.000 57.62000  ? 80  ASP B CG  1 
ATOM   3107 O  OD1 . ASP B  1 54  ? -20.23970 2.71071   82.42605  1.000 57.75585  ? 80  ASP B OD1 1 
ATOM   3108 O  OD2 . ASP B  1 54  ? -22.10401 2.23817   83.48452  1.000 59.30589  ? 80  ASP B OD2 1 
ATOM   3109 N  N   . LEU B  1 55  ? -19.38067 -2.34491  82.00630  1.000 49.45695  ? 81  LEU B N   1 
ATOM   3110 C  CA  . LEU B  1 55  ? -19.32039 -3.68417  81.43660  1.000 47.91465  ? 81  LEU B CA  1 
ATOM   3111 C  C   . LEU B  1 55  ? -17.91460 -4.23314  81.62066  1.000 48.05567  ? 81  LEU B C   1 
ATOM   3112 O  O   . LEU B  1 55  ? -16.93512 -3.54894  81.31056  1.000 48.45294  ? 81  LEU B O   1 
ATOM   3113 C  CB  . LEU B  1 55  ? -19.69526 -3.67418  79.94983  1.000 46.37647  ? 81  LEU B CB  1 
ATOM   3114 C  CG  . LEU B  1 55  ? -21.17004 -3.45299  79.60965  1.000 46.86627  ? 81  LEU B CG  1 
ATOM   3115 C  CD1 . LEU B  1 55  ? -21.35897 -3.28688  78.10959  1.000 47.08042  ? 81  LEU B CD1 1 
ATOM   3116 C  CD2 . LEU B  1 55  ? -22.01954 -4.59659  80.14034  1.000 46.57076  ? 81  LEU B CD2 1 
ATOM   3117 N  N   . VAL B  1 56  ? -17.82053 -5.46104  82.12518  1.000 48.18527  ? 82  VAL B N   1 
ATOM   3118 C  CA  . VAL B  1 56  ? -16.54526 -6.13853  82.31393  1.000 47.89184  ? 82  VAL B CA  1 
ATOM   3119 C  C   . VAL B  1 56  ? -16.63361 -7.52250  81.68944  1.000 47.62867  ? 82  VAL B C   1 
ATOM   3120 O  O   . VAL B  1 56  ? -17.71659 -8.10531  81.57524  1.000 48.29129  ? 82  VAL B O   1 
ATOM   3121 C  CB  . VAL B  1 56  ? -16.15317 -6.23851  83.80529  1.000 47.37229  ? 82  VAL B CB  1 
ATOM   3122 C  CG1 . VAL B  1 56  ? -15.85989 -4.85857  84.37143  1.000 47.74112  ? 82  VAL B CG1 1 
ATOM   3123 C  CG2 . VAL B  1 56  ? -17.25529 -6.92238  84.59887  1.000 47.90549  ? 82  VAL B CG2 1 
ATOM   3124 N  N   . VAL B  1 57  ? -15.48248 -8.04818  81.28070  1.000 46.94730  ? 83  VAL B N   1 
ATOM   3125 C  CA  . VAL B  1 57  ? -15.42083 -9.36716  80.65548  1.000 44.92547  ? 83  VAL B CA  1 
ATOM   3126 C  C   . VAL B  1 57  ? -14.55775 -10.29140 81.50635  1.000 46.23783  ? 83  VAL B C   1 
ATOM   3127 O  O   . VAL B  1 57  ? -13.38337 -10.51586 81.17841  1.000 47.94823  ? 83  VAL B O   1 
ATOM   3128 C  CB  . VAL B  1 57  ? -14.88040 -9.28300  79.21943  1.000 42.39108  ? 83  VAL B CB  1 
ATOM   3129 C  CG1 . VAL B  1 57  ? -15.14296 -10.58698 78.47485  1.000 41.19919  ? 83  VAL B CG1 1 
ATOM   3130 C  CG2 . VAL B  1 57  ? -15.49898 -8.10707  78.48818  1.000 42.09296  ? 83  VAL B CG2 1 
ATOM   3131 N  N   . PRO B  1 58  ? -15.08305 -10.84342 82.60151  1.000 46.01818  ? 84  PRO B N   1 
ATOM   3132 C  CA  . PRO B  1 58  ? -14.29280 -11.79162 83.39288  1.000 44.96442  ? 84  PRO B CA  1 
ATOM   3133 C  C   . PRO B  1 58  ? -14.50087 -13.22385 82.93339  1.000 42.40237  ? 84  PRO B C   1 
ATOM   3134 O  O   . PRO B  1 58  ? -15.28604 -13.47972 82.01504  1.000 42.28230  ? 84  PRO B O   1 
ATOM   3135 C  CB  . PRO B  1 58  ? -14.82516 -11.57377 84.81147  1.000 46.77714  ? 84  PRO B CB  1 
ATOM   3136 C  CG  . PRO B  1 58  ? -16.27514 -11.25001 84.58882  1.000 47.00558  ? 84  PRO B CG  1 
ATOM   3137 C  CD  . PRO B  1 58  ? -16.37633 -10.54648 83.24373  1.000 46.26718  ? 84  PRO B CD  1 
ATOM   3138 N  N   . SER B  1 59  ? -13.80328 -14.16366 83.56335  1.000 42.29476  ? 85  SER B N   1 
ATOM   3139 C  CA  . SER B  1 59  ? -14.04166 -15.57013 83.28974  1.000 43.15527  ? 85  SER B CA  1 
ATOM   3140 C  C   . SER B  1 59  ? -15.41423 -15.98233 83.81556  1.000 45.78254  ? 85  SER B C   1 
ATOM   3141 O  O   . SER B  1 59  ? -16.03249 -15.29082 84.62963  1.000 46.74170  ? 85  SER B O   1 
ATOM   3142 C  CB  . SER B  1 59  ? -12.95221 -16.43370 83.92569  1.000 42.77804  ? 85  SER B CB  1 
ATOM   3143 O  OG  . SER B  1 59  ? -12.53352 -15.89027 85.16558  1.000 42.59504  ? 85  SER B OG  1 
ATOM   3144 N  N   . ALA B  1 60  ? -15.89479 -17.12901 83.33191  1.000 46.49495  ? 86  ALA B N   1 
ATOM   3145 C  CA  . ALA B  1 60  ? -17.18330 -17.63297 83.79524  1.000 47.44770  ? 86  ALA B CA  1 
ATOM   3146 C  C   . ALA B  1 60  ? -17.08647 -18.16633 85.21979  1.000 52.19245  ? 86  ALA B C   1 
ATOM   3147 O  O   . ALA B  1 60  ? -18.00680 -17.97779 86.02594  1.000 55.36005  ? 86  ALA B O   1 
ATOM   3148 C  CB  . ALA B  1 60  ? -17.69546 -18.71621 82.84635  1.000 44.79370  ? 86  ALA B CB  1 
ATOM   3149 N  N   . SER B  1 61  ? -15.97215 -18.82354 85.55236  1.000 52.82652  ? 87  SER B N   1 
ATOM   3150 C  CA  . SER B  1 61  ? -15.82518 -19.40981 86.88075  1.000 55.89578  ? 87  SER B CA  1 
ATOM   3151 C  C   . SER B  1 61  ? -15.59464 -18.34960 87.95117  1.000 58.29343  ? 87  SER B C   1 
ATOM   3152 O  O   . SER B  1 61  ? -16.00772 -18.53645 89.09882  1.000 60.78380  ? 87  SER B O   1 
ATOM   3153 C  CB  . SER B  1 61  ? -14.68660 -20.42872 86.88238  1.000 55.54590  ? 87  SER B CB  1 
ATOM   3154 O  OG  . SER B  1 61  ? -14.84663 -21.36879 85.83369  1.000 54.11745  ? 87  SER B OG  1 
ATOM   3155 N  N   . PHE B  1 62  ? -14.94876 -17.23406 87.60551  1.000 59.65133  ? 88  PHE B N   1 
ATOM   3156 C  CA  . PHE B  1 62  ? -14.84135 -16.13011 88.55527  1.000 65.15181  ? 88  PHE B CA  1 
ATOM   3157 C  C   . PHE B  1 62  ? -16.21646 -15.55677 88.87817  1.000 67.30635  ? 88  PHE B C   1 
ATOM   3158 O  O   . PHE B  1 62  ? -16.53785 -15.29814 90.04703  1.000 68.38245  ? 88  PHE B O   1 
ATOM   3159 C  CB  . PHE B  1 62  ? -13.92084 -15.04764 87.99276  1.000 68.13291  ? 88  PHE B CB  1 
ATOM   3160 C  CG  . PHE B  1 62  ? -13.66025 -13.91607 88.94400  1.000 71.95687  ? 88  PHE B CG  1 
ATOM   3161 C  CD1 . PHE B  1 62  ? -12.87471 -14.10463 90.06856  1.000 73.96060  ? 88  PHE B CD1 1 
ATOM   3162 C  CD2 . PHE B  1 62  ? -14.19884 -12.66147 88.71117  1.000 72.96864  ? 88  PHE B CD2 1 
ATOM   3163 C  CE1 . PHE B  1 62  ? -12.63113 -13.06401 90.94388  1.000 75.34777  ? 88  PHE B CE1 1 
ATOM   3164 C  CE2 . PHE B  1 62  ? -13.96047 -11.61648 89.58286  1.000 74.70816  ? 88  PHE B CE2 1 
ATOM   3165 C  CZ  . PHE B  1 62  ? -13.17622 -11.81830 90.70161  1.000 75.60854  ? 88  PHE B CZ  1 
ATOM   3166 N  N   . LEU B  1 63  ? -17.04356 -15.35805 87.84848  1.000 67.64881  ? 89  LEU B N   1 
ATOM   3167 C  CA  . LEU B  1 63  ? -18.41773 -14.91869 88.06304  1.000 68.70545  ? 89  LEU B CA  1 
ATOM   3168 C  C   . LEU B  1 63  ? -19.19269 -15.92900 88.90032  1.000 70.21151  ? 89  LEU B C   1 
ATOM   3169 O  O   . LEU B  1 63  ? -20.02406 -15.54938 89.73373  1.000 71.31214  ? 89  LEU B O   1 
ATOM   3170 C  CB  . LEU B  1 63  ? -19.10081 -14.69073 86.71407  1.000 68.18718  ? 89  LEU B CB  1 
ATOM   3171 C  CG  . LEU B  1 63  ? -20.60083 -14.39904 86.69995  1.000 68.16976  ? 89  LEU B CG  1 
ATOM   3172 C  CD1 . LEU B  1 63  ? -20.89716 -13.19823 85.81743  1.000 67.71354  ? 89  LEU B CD1 1 
ATOM   3173 C  CD2 . LEU B  1 63  ? -21.37254 -15.61683 86.22324  1.000 67.66711  ? 89  LEU B CD2 1 
ATOM   3174 N  N   . GLU B  1 64  ? -18.93318 -17.22285 88.69207  1.000 70.54438  ? 90  GLU B N   1 
ATOM   3175 C  CA  . GLU B  1 64  ? -19.56141 -18.24567 89.52364  1.000 72.30370  ? 90  GLU B CA  1 
ATOM   3176 C  C   . GLU B  1 64  ? -19.12060 -18.12187 90.97768  1.000 72.85336  ? 90  GLU B C   1 
ATOM   3177 O  O   . GLU B  1 64  ? -19.93539 -18.25673 91.89810  1.000 72.81325  ? 90  GLU B O   1 
ATOM   3178 C  CB  . GLU B  1 64  ? -19.23080 -19.63653 88.98221  1.000 72.96386  ? 90  GLU B CB  1 
ATOM   3179 C  CG  . GLU B  1 64  ? -19.70636 -20.77761 89.86779  1.000 75.03376  ? 90  GLU B CG  1 
ATOM   3180 C  CD  . GLU B  1 64  ? -19.48650 -22.13733 89.23515  1.000 76.01458  ? 90  GLU B CD  1 
ATOM   3181 O  OE1 . GLU B  1 64  ? -18.84703 -22.20020 88.16407  1.000 75.76438  ? 90  GLU B OE1 1 
ATOM   3182 O  OE2 . GLU B  1 64  ? -19.95172 -23.14399 89.80961  1.000 76.85437  ? 90  GLU B OE2 1 
ATOM   3183 N  N   . ARG B  1 65  ? -17.83089 -17.86832 91.20235  1.000 72.77289  ? 91  ARG B N   1 
ATOM   3184 C  CA  . ARG B  1 65  ? -17.31362 -17.73200 92.55782  1.000 73.59119  ? 91  ARG B CA  1 
ATOM   3185 C  C   . ARG B  1 65  ? -17.82142 -16.47476 93.24886  1.000 75.00808  ? 91  ARG B C   1 
ATOM   3186 O  O   . ARG B  1 65  ? -17.87288 -16.44134 94.48299  1.000 76.31021  ? 91  ARG B O   1 
ATOM   3187 C  CB  . ARG B  1 65  ? -15.78411 -17.73529 92.54253  1.000 72.28603  ? 91  ARG B CB  1 
ATOM   3188 C  CG  . ARG B  1 65  ? -15.17215 -19.06894 92.14566  1.000 71.20212  ? 91  ARG B CG  1 
ATOM   3189 C  CD  . ARG B  1 65  ? -13.65237 -19.01006 92.14861  1.000 71.06698  ? 91  ARG B CD  1 
ATOM   3190 N  NE  . ARG B  1 65  ? -13.14976 -17.78084 92.75524  1.000 71.68675  ? 91  ARG B NE  1 
ATOM   3191 C  CZ  . ARG B  1 65  ? -12.38559 -16.89501 92.12494  1.000 71.58248  ? 91  ARG B CZ  1 
ATOM   3192 N  NH1 . ARG B  1 65  ? -12.03050 -17.10115 90.86405  1.000 70.15485  ? 91  ARG B NH1 1 
ATOM   3193 N  NH2 . ARG B  1 65  ? -11.97435 -15.80372 92.75611  1.000 72.90745  ? 91  ARG B NH2 1 
ATOM   3194 N  N   . GLN B  1 66  ? -18.19069 -15.44388 92.49215  1.000 74.53786  ? 92  GLN B N   1 
ATOM   3195 C  CA  . GLN B  1 66  ? -18.75099 -14.22115 93.05978  1.000 75.43764  ? 92  GLN B CA  1 
ATOM   3196 C  C   . GLN B  1 66  ? -20.24603 -14.09667 92.77287  1.000 75.18862  ? 92  GLN B C   1 
ATOM   3197 O  O   . GLN B  1 66  ? -20.75449 -13.00636 92.50566  1.000 75.65128  ? 92  GLN B O   1 
ATOM   3198 C  CB  . GLN B  1 66  ? -18.00156 -12.99460 92.54779  1.000 75.18682  ? 92  GLN B CB  1 
ATOM   3199 C  CG  . GLN B  1 66  ? -17.10569 -12.34769 93.59303  1.000 75.19122  ? 92  GLN B CG  1 
ATOM   3200 C  CD  . GLN B  1 66  ? -15.75680 -13.02845 93.70270  1.000 72.70937  ? 92  GLN B CD  1 
ATOM   3201 O  OE1 . GLN B  1 66  ? -15.16374 -13.41897 92.69867  1.000 70.84627  ? 92  GLN B OE1 1 
ATOM   3202 N  NE2 . GLN B  1 66  ? -15.26837 -13.18202 94.92815  1.000 73.21481  ? 92  GLN B NE2 1 
ATOM   3203 N  N   . LEU B  1 67  ? -20.97079 -15.21720 92.83968  1.000 74.15490  ? 93  LEU B N   1 
ATOM   3204 C  CA  . LEU B  1 67  ? -22.40694 -15.18438 92.57556  1.000 74.35031  ? 93  LEU B CA  1 
ATOM   3205 C  C   . LEU B  1 67  ? -23.16918 -14.52049 93.71625  1.000 75.88606  ? 93  LEU B C   1 
ATOM   3206 O  O   . LEU B  1 67  ? -24.10012 -13.74221 93.47732  1.000 76.83954  ? 93  LEU B O   1 
ATOM   3207 C  CB  . LEU B  1 67  ? -22.93370 -16.59993 92.33672  1.000 73.66207  ? 93  LEU B CB  1 
ATOM   3208 C  CG  . LEU B  1 67  ? -22.77979 -17.17843 90.92866  1.000 71.88319  ? 93  LEU B CG  1 
ATOM   3209 C  CD1 . LEU B  1 67  ? -23.09690 -18.66727 90.92372  1.000 71.77850  ? 93  LEU B CD1 1 
ATOM   3210 C  CD2 . LEU B  1 67  ? -23.65891 -16.43573 89.93513  1.000 71.61879  ? 93  LEU B CD2 1 
ATOM   3211 N  N   . THR B  1 68  ? -22.79434 -14.81634 94.96062  1.000 75.74461  ? 94  THR B N   1 
ATOM   3212 C  CA  . THR B  1 68  ? -23.47232 -14.26528 96.12574  1.000 76.08703  ? 94  THR B CA  1 
ATOM   3213 C  C   . THR B  1 68  ? -22.79733 -13.01858 96.68218  1.000 76.39776  ? 94  THR B C   1 
ATOM   3214 O  O   . THR B  1 68  ? -23.33396 -12.40933 97.61374  1.000 77.25539  ? 94  THR B O   1 
ATOM   3215 C  CB  . THR B  1 68  ? -23.56966 -15.32109 97.23523  1.000 75.64482  ? 94  THR B CB  1 
ATOM   3216 O  OG1 . THR B  1 68  ? -22.28108 -15.51037 97.83321  1.000 75.65926  ? 94  THR B OG1 1 
ATOM   3217 C  CG2 . THR B  1 68  ? -24.06089 -16.64531 96.66928  1.000 74.64797  ? 94  THR B CG2 1 
ATOM   3218 N  N   . ALA B  1 69  ? -21.64206 -12.62460 96.14062  1.000 75.48632  ? 95  ALA B N   1 
ATOM   3219 C  CA  . ALA B  1 69  ? -20.95477 -11.43876 96.63757  1.000 76.78483  ? 95  ALA B CA  1 
ATOM   3220 C  C   . ALA B  1 69  ? -21.67328 -10.15028 96.25946  1.000 77.38851  ? 95  ALA B C   1 
ATOM   3221 O  O   . ALA B  1 69  ? -21.44898 -9.11961  96.90284  1.000 80.00355  ? 95  ALA B O   1 
ATOM   3222 C  CB  . ALA B  1 69  ? -19.51710 -11.40581 96.11974  1.000 77.72328  ? 95  ALA B CB  1 
ATOM   3223 N  N   . GLY B  1 70  ? -22.52021 -10.18083 95.23391  1.000 74.25001  ? 96  GLY B N   1 
ATOM   3224 C  CA  . GLY B  1 70  ? -23.31404 -9.01701  94.88928  1.000 73.41442  ? 96  GLY B CA  1 
ATOM   3225 C  C   . GLY B  1 70  ? -22.55893 -7.90343  94.19952  1.000 72.23939  ? 96  GLY B C   1 
ATOM   3226 O  O   . GLY B  1 70  ? -22.89683 -6.72993  94.38486  1.000 73.31654  ? 96  GLY B O   1 
ATOM   3227 N  N   . VAL B  1 71  ? -21.54009 -8.23534  93.40770  1.000 71.41664  ? 97  VAL B N   1 
ATOM   3228 C  CA  . VAL B  1 71  ? -20.83342 -7.23236  92.61972  1.000 71.45347  ? 97  VAL B CA  1 
ATOM   3229 C  C   . VAL B  1 71  ? -21.39228 -7.12311  91.20221  1.000 70.41719  ? 97  VAL B C   1 
ATOM   3230 O  O   . VAL B  1 71  ? -21.20979 -6.08031  90.55567  1.000 70.05739  ? 97  VAL B O   1 
ATOM   3231 C  CB  . VAL B  1 71  ? -19.31724 -7.52732  92.58203  1.000 70.96389  ? 97  VAL B CB  1 
ATOM   3232 C  CG1 . VAL B  1 71  ? -19.02404 -8.76071  91.73854  1.000 69.19341  ? 97  VAL B CG1 1 
ATOM   3233 C  CG2 . VAL B  1 71  ? -18.53342 -6.31360  92.08568  1.000 71.29991  ? 97  VAL B CG2 1 
ATOM   3234 N  N   . PHE B  1 72  ? -22.08035 -8.14860  90.71135  1.000 69.45435  ? 98  PHE B N   1 
ATOM   3235 C  CA  . PHE B  1 72  ? -22.69092 -8.13470  89.39129  1.000 67.37301  ? 98  PHE B CA  1 
ATOM   3236 C  C   . PHE B  1 72  ? -24.19908 -7.94261  89.50139  1.000 66.76020  ? 98  PHE B C   1 
ATOM   3237 O  O   . PHE B  1 72  ? -24.80805 -8.17775  90.54829  1.000 67.47153  ? 98  PHE B O   1 
ATOM   3238 C  CB  . PHE B  1 72  ? -22.38868 -9.43337  88.63828  1.000 66.51476  ? 98  PHE B CB  1 
ATOM   3239 C  CG  . PHE B  1 72  ? -20.94493 -9.59782  88.26462  1.000 66.62213  ? 98  PHE B CG  1 
ATOM   3240 C  CD1 . PHE B  1 72  ? -20.31656 -10.82377 88.40592  1.000 65.91318  ? 98  PHE B CD1 1 
ATOM   3241 C  CD2 . PHE B  1 72  ? -20.21639 -8.52961  87.76862  1.000 67.22830  ? 98  PHE B CD2 1 
ATOM   3242 C  CE1 . PHE B  1 72  ? -18.98738 -10.98144 88.06222  1.000 65.43624  ? 98  PHE B CE1 1 
ATOM   3243 C  CE2 . PHE B  1 72  ? -18.88603 -8.68055  87.42294  1.000 66.47012  ? 98  PHE B CE2 1 
ATOM   3244 C  CZ  . PHE B  1 72  ? -18.27117 -9.90846  87.57013  1.000 65.62341  ? 98  PHE B CZ  1 
ATOM   3245 N  N   . GLN B  1 73  ? -24.79660 -7.51075  88.39402  1.000 64.25650  ? 99  GLN B N   1 
ATOM   3246 C  CA  . GLN B  1 73  ? -26.22834 -7.31344  88.22462  1.000 62.51239  ? 99  GLN B CA  1 
ATOM   3247 C  C   . GLN B  1 73  ? -26.82157 -8.41835  87.36228  1.000 58.79944  ? 99  GLN B C   1 
ATOM   3248 O  O   . GLN B  1 73  ? -26.19373 -8.84939  86.38866  1.000 55.63006  ? 99  GLN B O   1 
ATOM   3249 C  CB  . GLN B  1 73  ? -26.52055 -5.96544  87.56526  1.000 63.57525  ? 99  GLN B CB  1 
ATOM   3250 C  CG  . GLN B  1 73  ? -26.50976 -4.77950  88.50564  1.000 66.63127  ? 99  GLN B CG  1 
ATOM   3251 C  CD  . GLN B  1 73  ? -27.00159 -3.51487  87.83544  1.000 69.16458  ? 99  GLN B CD  1 
ATOM   3252 O  OE1 . GLN B  1 73  ? -28.06978 -3.50202  87.22800  1.000 69.90718  ? 99  GLN B OE1 1 
ATOM   3253 N  NE2 . GLN B  1 73  ? -26.22116 -2.44557  87.93522  1.000 70.39765  ? 99  GLN B NE2 1 
ATOM   3254 N  N   . PRO B  1 74  ? -28.01952 -8.90039  87.68737  1.000 58.78297  ? 100 PRO B N   1 
ATOM   3255 C  CA  . PRO B  1 74  ? -28.69798 -9.83482  86.78220  1.000 57.11550  ? 100 PRO B CA  1 
ATOM   3256 C  C   . PRO B  1 74  ? -29.09845 -9.13765  85.49120  1.000 55.48366  ? 100 PRO B C   1 
ATOM   3257 O  O   . PRO B  1 74  ? -29.55741 -7.99294  85.49734  1.000 55.00839  ? 100 PRO B O   1 
ATOM   3258 C  CB  . PRO B  1 74  ? -29.92345 -10.28912 87.58451  1.000 59.46343  ? 100 PRO B CB  1 
ATOM   3259 C  CG  . PRO B  1 74  ? -30.13147 -9.22211  88.60745  1.000 60.91936  ? 100 PRO B CG  1 
ATOM   3260 C  CD  . PRO B  1 74  ? -28.77199 -8.68354  88.93431  1.000 60.17111  ? 100 PRO B CD  1 
ATOM   3261 N  N   . LEU B  1 75  ? -28.91419 -9.83993  84.37647  1.000 53.99896  ? 101 LEU B N   1 
ATOM   3262 C  CA  . LEU B  1 75  ? -29.13078 -9.25297  83.05997  1.000 53.86780  ? 101 LEU B CA  1 
ATOM   3263 C  C   . LEU B  1 75  ? -30.61805 -9.24987  82.72690  1.000 55.46471  ? 101 LEU B C   1 
ATOM   3264 O  O   . LEU B  1 75  ? -31.25609 -10.30781 82.68901  1.000 55.63412  ? 101 LEU B O   1 
ATOM   3265 C  CB  . LEU B  1 75  ? -28.34025 -10.01840 82.00168  1.000 51.39790  ? 101 LEU B CB  1 
ATOM   3266 C  CG  . LEU B  1 75  ? -26.82718 -9.78981  82.01813  1.000 49.87959  ? 101 LEU B CG  1 
ATOM   3267 C  CD1 . LEU B  1 75  ? -26.14519 -10.60131 80.92779  1.000 47.91610  ? 101 LEU B CD1 1 
ATOM   3268 C  CD2 . LEU B  1 75  ? -26.50536 -8.30959  81.87329  1.000 49.71203  ? 101 LEU B CD2 1 
ATOM   3269 N  N   . ASP B  1 76  ? -31.16477 -8.06144  82.48283  1.000 56.21191  ? 102 ASP B N   1 
ATOM   3270 C  CA  . ASP B  1 76  ? -32.56872 -7.90457  82.10956  1.000 58.12895  ? 102 ASP B CA  1 
ATOM   3271 C  C   . ASP B  1 76  ? -32.76570 -8.44125  80.69834  1.000 57.18973  ? 102 ASP B C   1 
ATOM   3272 O  O   . ASP B  1 76  ? -32.50343 -7.74706  79.71394  1.000 57.12718  ? 102 ASP B O   1 
ATOM   3273 C  CB  . ASP B  1 76  ? -32.98059 -6.43955  82.20271  1.000 61.06764  ? 102 ASP B CB  1 
ATOM   3274 C  CG  . ASP B  1 76  ? -34.48279 -6.24452  82.10494  1.000 64.98587  ? 102 ASP B CG  1 
ATOM   3275 O  OD1 . ASP B  1 76  ? -35.20994 -7.24554  81.93241  1.000 65.99896  ? 102 ASP B OD1 1 
ATOM   3276 O  OD2 . ASP B  1 76  ? -34.93681 -5.08439  82.19550  1.000 66.81330  ? 102 ASP B OD2 1 
ATOM   3277 N  N   . LYS B  1 77  ? -33.23846 -9.68635  80.59516  1.000 56.23719  ? 103 LYS B N   1 
ATOM   3278 C  CA  . LYS B  1 77  ? -33.48317 -10.28792 79.28883  1.000 55.45982  ? 103 LYS B CA  1 
ATOM   3279 C  C   . LYS B  1 77  ? -34.54750 -9.54031  78.49697  1.000 56.83867  ? 103 LYS B C   1 
ATOM   3280 O  O   . LYS B  1 77  ? -34.59107 -9.66587  77.26812  1.000 56.69576  ? 103 LYS B O   1 
ATOM   3281 C  CB  . LYS B  1 77  ? -33.89046 -11.75277 79.45302  1.000 55.10633  ? 103 LYS B CB  1 
ATOM   3282 C  CG  . LYS B  1 77  ? -32.84711 -12.61235 80.14462  1.000 53.97407  ? 103 LYS B CG  1 
ATOM   3283 C  CD  . LYS B  1 77  ? -31.54771 -12.64826 79.35563  1.000 51.61122  ? 103 LYS B CD  1 
ATOM   3284 C  CE  . LYS B  1 77  ? -30.39579 -13.13527 80.21742  1.000 51.74729  ? 103 LYS B CE  1 
ATOM   3285 N  NZ  . LYS B  1 77  ? -30.65999 -14.48664 80.78574  1.000 53.06258  ? 103 LYS B NZ  1 
ATOM   3286 N  N   . SER B  1 78  ? -35.40435 -8.76835  79.17038  1.000 56.90981  ? 104 SER B N   1 
ATOM   3287 C  CA  . SER B  1 78  ? -36.39752 -7.96373  78.47026  1.000 56.81970  ? 104 SER B CA  1 
ATOM   3288 C  C   . SER B  1 78  ? -35.76055 -6.92006  77.56183  1.000 57.23438  ? 104 SER B C   1 
ATOM   3289 O  O   . SER B  1 78  ? -36.40310 -6.47151  76.60671  1.000 59.15680  ? 104 SER B O   1 
ATOM   3290 C  CB  . SER B  1 78  ? -37.32379 -7.28641  79.48138  1.000 55.26986  ? 104 SER B CB  1 
ATOM   3291 O  OG  . SER B  1 78  ? -37.76529 -6.02670  79.00717  1.000 55.06618  ? 104 SER B OG  1 
ATOM   3292 N  N   . LYS B  1 79  ? -34.51852 -6.52493  77.83257  1.000 55.08009  ? 105 LYS B N   1 
ATOM   3293 C  CA  . LYS B  1 79  ? -33.82390 -5.52415  77.03504  1.000 52.12094  ? 105 LYS B CA  1 
ATOM   3294 C  C   . LYS B  1 79  ? -32.81639 -6.13035  76.06655  1.000 48.08789  ? 105 LYS B C   1 
ATOM   3295 O  O   . LYS B  1 79  ? -32.10460 -5.38402  75.38693  1.000 45.84316  ? 105 LYS B O   1 
ATOM   3296 C  CB  . LYS B  1 79  ? -33.12625 -4.51799  77.95503  1.000 52.92378  ? 105 LYS B CB  1 
ATOM   3297 C  CG  . LYS B  1 79  ? -33.99215 -4.07159  79.12452  1.000 56.34914  ? 105 LYS B CG  1 
ATOM   3298 C  CD  . LYS B  1 79  ? -33.24378 -3.13002  80.05208  1.000 58.76189  ? 105 LYS B CD  1 
ATOM   3299 C  CE  . LYS B  1 79  ? -33.07350 -1.75650  79.42722  1.000 60.31514  ? 105 LYS B CE  1 
ATOM   3300 N  NZ  . LYS B  1 79  ? -32.33578 -0.82945  80.32894  1.000 61.59465  ? 105 LYS B NZ  1 
ATOM   3301 N  N   . LEU B  1 80  ? -32.73762 -7.46049  75.98875  1.000 46.94019  ? 106 LEU B N   1 
ATOM   3302 C  CA  . LEU B  1 80  ? -31.90358 -8.16685  75.01755  1.000 45.50182  ? 106 LEU B CA  1 
ATOM   3303 C  C   . LEU B  1 80  ? -32.81203 -8.97462  74.09567  1.000 44.86570  ? 106 LEU B C   1 
ATOM   3304 O  O   . LEU B  1 80  ? -32.89497 -10.20485 74.21265  1.000 46.39767  ? 106 LEU B O   1 
ATOM   3305 C  CB  . LEU B  1 80  ? -30.88927 -9.08489  75.69876  1.000 43.89138  ? 106 LEU B CB  1 
ATOM   3306 C  CG  . LEU B  1 80  ? -29.65181 -8.50171  76.38676  1.000 46.20154  ? 106 LEU B CG  1 
ATOM   3307 C  CD1 . LEU B  1 80  ? -29.06309 -7.34393  75.59580  1.000 46.92899  ? 106 LEU B CD1 1 
ATOM   3308 C  CD2 . LEU B  1 80  ? -29.96700 -8.08760  77.81018  1.000 48.45512  ? 106 LEU B CD2 1 
ATOM   3309 N  N   . PRO B  1 81  ? -33.50646 -8.31527  73.16449  1.000 44.71721  ? 107 PRO B N   1 
ATOM   3310 C  CA  . PRO B  1 81  ? -34.46745 -9.04916  72.32423  1.000 47.22602  ? 107 PRO B CA  1 
ATOM   3311 C  C   . PRO B  1 81  ? -33.82057 -10.08186 71.41858  1.000 49.66651  ? 107 PRO B C   1 
ATOM   3312 O  O   . PRO B  1 81  ? -34.46583 -11.08138 71.07756  1.000 51.40705  ? 107 PRO B O   1 
ATOM   3313 C  CB  . PRO B  1 81  ? -35.14719 -7.93446  71.51697  1.000 47.66074  ? 107 PRO B CB  1 
ATOM   3314 C  CG  . PRO B  1 81  ? -34.15518 -6.82352  71.50016  1.000 46.51478  ? 107 PRO B CG  1 
ATOM   3315 C  CD  . PRO B  1 81  ? -33.44935 -6.88420  72.82123  1.000 44.59619  ? 107 PRO B CD  1 
ATOM   3316 N  N   . GLU B  1 82  ? -32.56525 -9.87749  71.01932  1.000 49.23821  ? 108 GLU B N   1 
ATOM   3317 C  CA  . GLU B  1 82  ? -31.86097 -10.81050 70.15128  1.000 49.41231  ? 108 GLU B CA  1 
ATOM   3318 C  C   . GLU B  1 82  ? -31.10173 -11.88074 70.92960  1.000 48.05969  ? 108 GLU B C   1 
ATOM   3319 O  O   . GLU B  1 82  ? -30.19898 -12.51807 70.37197  1.000 46.39184  ? 108 GLU B O   1 
ATOM   3320 C  CB  . GLU B  1 82  ? -30.90893 -10.05041 69.22548  1.000 51.81120  ? 108 GLU B CB  1 
ATOM   3321 C  CG  . GLU B  1 82  ? -31.60481 -9.01891  68.35324  1.000 55.33453  ? 108 GLU B CG  1 
ATOM   3322 C  CD  . GLU B  1 82  ? -32.83603 -9.57719  67.66494  1.000 60.48043  ? 108 GLU B CD  1 
ATOM   3323 O  OE1 . GLU B  1 82  ? -32.71373 -10.60498 66.96553  1.000 62.06447  ? 108 GLU B OE1 1 
ATOM   3324 O  OE2 . GLU B  1 82  ? -33.92797 -8.99243  67.82963  1.000 62.60761  ? 108 GLU B OE2 1 
ATOM   3325 N  N   . TRP B  1 83  ? -31.45696 -12.09569 72.20041  1.000 48.84708  ? 109 TRP B N   1 
ATOM   3326 C  CA  . TRP B  1 83  ? -30.80654 -13.12931 73.00073  1.000 49.45588  ? 109 TRP B CA  1 
ATOM   3327 C  C   . TRP B  1 83  ? -30.95607 -14.50762 72.36959  1.000 48.19458  ? 109 TRP B C   1 
ATOM   3328 O  O   . TRP B  1 83  ? -30.12363 -15.39156 72.60412  1.000 46.86168  ? 109 TRP B O   1 
ATOM   3329 C  CB  . TRP B  1 83  ? -31.38265 -13.12517 74.41829  1.000 50.60248  ? 109 TRP B CB  1 
ATOM   3330 C  CG  . TRP B  1 83  ? -30.68779 -14.05026 75.37340  1.000 50.50785  ? 109 TRP B CG  1 
ATOM   3331 C  CD1 . TRP B  1 83  ? -30.96949 -15.36790 75.59025  1.000 49.87752  ? 109 TRP B CD1 1 
ATOM   3332 C  CD2 . TRP B  1 83  ? -29.60373 -13.72262 76.25146  1.000 51.11888  ? 109 TRP B CD2 1 
ATOM   3333 N  NE1 . TRP B  1 83  ? -30.12468 -15.88232 76.54360  1.000 49.54561  ? 109 TRP B NE1 1 
ATOM   3334 C  CE2 . TRP B  1 83  ? -29.27676 -14.89245 76.96565  1.000 50.59888  ? 109 TRP B CE2 1 
ATOM   3335 C  CE3 . TRP B  1 83  ? -28.87601 -12.55476 76.50052  1.000 52.15210  ? 109 TRP B CE3 1 
ATOM   3336 C  CZ2 . TRP B  1 83  ? -28.25430 -14.92844 77.91136  1.000 52.78971  ? 109 TRP B CZ2 1 
ATOM   3337 C  CZ3 . TRP B  1 83  ? -27.86140 -12.59255 77.44003  1.000 53.01612  ? 109 TRP B CZ3 1 
ATOM   3338 C  CH2 . TRP B  1 83  ? -27.55982 -13.77112 78.13349  1.000 53.60046  ? 109 TRP B CH2 1 
ATOM   3339 N  N   . LYS B  1 84  ? -31.99937 -14.70662 71.56013  1.000 47.23559  ? 110 LYS B N   1 
ATOM   3340 C  CA  . LYS B  1 84  ? -32.20356 -15.97698 70.87507  1.000 45.97600  ? 110 LYS B CA  1 
ATOM   3341 C  C   . LYS B  1 84  ? -31.11307 -16.28207 69.85634  1.000 45.11305  ? 110 LYS B C   1 
ATOM   3342 O  O   . LYS B  1 84  ? -31.07060 -17.40512 69.34120  1.000 45.70249  ? 110 LYS B O   1 
ATOM   3343 C  CB  . LYS B  1 84  ? -33.56964 -15.98283 70.18517  1.000 47.69940  ? 110 LYS B CB  1 
ATOM   3344 C  CG  . LYS B  1 84  ? -33.76377 -14.84699 69.19333  1.000 49.27912  ? 110 LYS B CG  1 
ATOM   3345 C  CD  . LYS B  1 84  ? -35.15958 -14.86482 68.59232  1.000 52.19619  ? 110 LYS B CD  1 
ATOM   3346 C  CE  . LYS B  1 84  ? -35.38966 -13.65370 67.70178  1.000 52.96361  ? 110 LYS B CE  1 
ATOM   3347 N  NZ  . LYS B  1 84  ? -36.75611 -13.64662 67.10991  1.000 54.01042  ? 110 LYS B NZ  1 
ATOM   3348 N  N   . ASN B  1 85  ? -30.23918 -15.31921 69.54750  1.000 43.69938  ? 111 ASN B N   1 
ATOM   3349 C  CA  . ASN B  1 85  ? -29.13907 -15.59548 68.62969  1.000 40.85143  ? 111 ASN B CA  1 
ATOM   3350 C  C   . ASN B  1 85  ? -28.11275 -16.53519 69.24891  1.000 40.14921  ? 111 ASN B C   1 
ATOM   3351 O  O   . ASN B  1 85  ? -27.41129 -17.24870 68.52292  1.000 39.60838  ? 111 ASN B O   1 
ATOM   3352 C  CB  . ASN B  1 85  ? -28.46655 -14.29114 68.20073  1.000 39.13103  ? 111 ASN B CB  1 
ATOM   3353 C  CG  . ASN B  1 85  ? -29.32945 -13.47019 67.26300  1.000 40.78078  ? 111 ASN B CG  1 
ATOM   3354 O  OD1 . ASN B  1 85  ? -30.33470 -13.95321 66.74244  1.000 37.77305  ? 111 ASN B OD1 1 
ATOM   3355 N  ND2 . ASN B  1 85  ? -28.93739 -12.22115 67.03995  1.000 37.25759  ? 111 ASN B ND2 1 
ATOM   3356 N  N   . LEU B  1 86  ? -28.01142 -16.55180 70.57541  1.000 40.07146  ? 112 LEU B N   1 
ATOM   3357 C  CA  . LEU B  1 86  ? -27.02932 -17.39371 71.24340  1.000 39.17286  ? 112 LEU B CA  1 
ATOM   3358 C  C   . LEU B  1 86  ? -27.39560 -18.86613 71.10299  1.000 41.01132  ? 112 LEU B C   1 
ATOM   3359 O  O   . LEU B  1 86  ? -28.57236 -19.23735 71.13126  1.000 42.77237  ? 112 LEU B O   1 
ATOM   3360 C  CB  . LEU B  1 86  ? -26.92501 -17.01645 72.72079  1.000 37.93923  ? 112 LEU B CB  1 
ATOM   3361 C  CG  . LEU B  1 86  ? -26.44929 -15.59540 73.02965  1.000 38.25989  ? 112 LEU B CG  1 
ATOM   3362 C  CD1 . LEU B  1 86  ? -26.53648 -15.31227 74.52262  1.000 38.48368  ? 112 LEU B CD1 1 
ATOM   3363 C  CD2 . LEU B  1 86  ? -25.03173 -15.37907 72.52089  1.000 38.10476  ? 112 LEU B CD2 1 
ATOM   3364 N  N   . ASP B  1 87  ? -26.37809 -19.70427 70.95073  1.000 42.73935  ? 113 ASP B N   1 
ATOM   3365 C  CA  . ASP B  1 87  ? -26.60880 -21.13526 70.79757  1.000 47.40164  ? 113 ASP B CA  1 
ATOM   3366 C  C   . ASP B  1 87  ? -27.06334 -21.73188 72.12548  1.000 49.91956  ? 113 ASP B C   1 
ATOM   3367 O  O   . ASP B  1 87  ? -26.40324 -21.52404 73.15049  1.000 49.70903  ? 113 ASP B O   1 
ATOM   3368 C  CB  . ASP B  1 87  ? -25.34142 -21.83079 70.30632  1.000 49.76663  ? 113 ASP B CB  1 
ATOM   3369 C  CG  . ASP B  1 87  ? -25.58628 -23.27201 69.90837  1.000 53.01675  ? 113 ASP B CG  1 
ATOM   3370 O  OD1 . ASP B  1 87  ? -25.73891 -23.54164 68.69885  1.000 54.42104  ? 113 ASP B OD1 1 
ATOM   3371 O  OD2 . ASP B  1 87  ? -25.62629 -24.13693 70.80614  1.000 54.74340  ? 113 ASP B OD2 1 
ATOM   3372 N  N   . PRO B  1 88  ? -28.17548 -22.47270 72.15193  1.000 52.92853  ? 114 PRO B N   1 
ATOM   3373 C  CA  . PRO B  1 88  ? -28.67307 -22.99423 73.43601  1.000 54.99257  ? 114 PRO B CA  1 
ATOM   3374 C  C   . PRO B  1 88  ? -27.74621 -24.00803 74.08501  1.000 57.25922  ? 114 PRO B C   1 
ATOM   3375 O  O   . PRO B  1 88  ? -27.70833 -24.08568 75.31879  1.000 57.78003  ? 114 PRO B O   1 
ATOM   3376 C  CB  . PRO B  1 88  ? -30.02436 -23.62110 73.06157  1.000 54.95295  ? 114 PRO B CB  1 
ATOM   3377 C  CG  . PRO B  1 88  ? -29.92951 -23.89186 71.59253  1.000 54.32572  ? 114 PRO B CG  1 
ATOM   3378 C  CD  . PRO B  1 88  ? -29.07001 -22.80168 71.02960  1.000 53.54708  ? 114 PRO B CD  1 
ATOM   3379 N  N   . GLU B  1 89  ? -26.99992 -24.78709 73.29896  1.000 58.65181  ? 115 GLU B N   1 
ATOM   3380 C  CA  . GLU B  1 89  ? -26.05903 -25.74329 73.87725  1.000 59.22129  ? 115 GLU B CA  1 
ATOM   3381 C  C   . GLU B  1 89  ? -24.97892 -25.02685 74.68159  1.000 57.92418  ? 115 GLU B C   1 
ATOM   3382 O  O   . GLU B  1 89  ? -24.73747 -25.34743 75.85353  1.000 59.20691  ? 115 GLU B O   1 
ATOM   3383 C  CB  . GLU B  1 89  ? -25.43834 -26.59174 72.76603  1.000 61.60601  ? 115 GLU B CB  1 
ATOM   3384 C  CG  . GLU B  1 89  ? -25.17144 -28.03972 73.13437  1.000 64.75058  ? 115 GLU B CG  1 
ATOM   3385 C  CD  . GLU B  1 89  ? -24.56895 -28.82294 71.98210  1.000 66.24999  ? 115 GLU B CD  1 
ATOM   3386 O  OE1 . GLU B  1 89  ? -23.93116 -28.19841 71.10834  1.000 66.45005  ? 115 GLU B OE1 1 
ATOM   3387 O  OE2 . GLU B  1 89  ? -24.73269 -30.06068 71.94797  1.000 67.81214  ? 115 GLU B OE2 1 
ATOM   3388 N  N   . LEU B  1 90  ? -24.31965 -24.04329 74.06415  1.000 56.67320  ? 116 LEU B N   1 
ATOM   3389 C  CA  . LEU B  1 90  ? -23.33385 -23.24548 74.78408  1.000 55.53518  ? 116 LEU B CA  1 
ATOM   3390 C  C   . LEU B  1 90  ? -23.97956 -22.45517 75.91372  1.000 54.15748  ? 116 LEU B C   1 
ATOM   3391 O  O   . LEU B  1 90  ? -23.34461 -22.21586 76.94914  1.000 54.72684  ? 116 LEU B O   1 
ATOM   3392 C  CB  . LEU B  1 90  ? -22.61649 -22.30673 73.81389  1.000 55.89884  ? 116 LEU B CB  1 
ATOM   3393 C  CG  . LEU B  1 90  ? -22.01178 -22.96963 72.57398  1.000 55.30935  ? 116 LEU B CG  1 
ATOM   3394 C  CD1 . LEU B  1 90  ? -21.52312 -21.92297 71.58450  1.000 54.99706  ? 116 LEU B CD1 1 
ATOM   3395 C  CD2 . LEU B  1 90  ? -20.88263 -23.91071 72.96556  1.000 53.79410  ? 116 LEU B CD2 1 
ATOM   3396 N  N   . LEU B  1 91  ? -25.23954 -22.04794 75.73676  1.000 52.82250  ? 117 LEU B N   1 
ATOM   3397 C  CA  . LEU B  1 91  ? -25.94941 -21.36171 76.81007  1.000 51.53295  ? 117 LEU B CA  1 
ATOM   3398 C  C   . LEU B  1 91  ? -26.06216 -22.24690 78.04365  1.000 50.48005  ? 117 LEU B C   1 
ATOM   3399 O  O   . LEU B  1 91  ? -25.79361 -21.79791 79.16102  1.000 49.93272  ? 117 LEU B O   1 
ATOM   3400 C  CB  . LEU B  1 91  ? -27.33237 -20.92068 76.33206  1.000 51.99763  ? 117 LEU B CB  1 
ATOM   3401 C  CG  . LEU B  1 91  ? -27.40703 -19.51849 75.72448  1.000 51.75657  ? 117 LEU B CG  1 
ATOM   3402 C  CD1 . LEU B  1 91  ? -28.73638 -19.30874 75.01994  1.000 51.47648  ? 117 LEU B CD1 1 
ATOM   3403 C  CD2 . LEU B  1 91  ? -27.18611 -18.45587 76.79087  1.000 52.33424  ? 117 LEU B CD2 1 
ATOM   3404 N  N   . LYS B  1 92  ? -26.43780 -23.51524 77.85922  1.000 50.29098  ? 118 LYS B N   1 
ATOM   3405 C  CA  . LYS B  1 92  ? -26.47165 -24.44806 78.98308  1.000 52.31574  ? 118 LYS B CA  1 
ATOM   3406 C  C   . LYS B  1 92  ? -25.07551 -24.67512 79.55099  1.000 54.40914  ? 118 LYS B C   1 
ATOM   3407 O  O   . LYS B  1 92  ? -24.89592 -24.75237 80.77616  1.000 56.23098  ? 118 LYS B O   1 
ATOM   3408 C  CB  . LYS B  1 92  ? -27.08790 -25.77745 78.54549  1.000 51.39456  ? 118 LYS B CB  1 
ATOM   3409 C  CG  . LYS B  1 92  ? -28.50074 -25.67111 77.99804  1.000 51.50185  ? 118 LYS B CG  1 
ATOM   3410 C  CD  . LYS B  1 92  ? -29.06369 -27.04717 77.67819  1.000 53.42007  ? 118 LYS B CD  1 
ATOM   3411 C  CE  . LYS B  1 92  ? -30.51249 -26.96482 77.22572  1.000 56.17532  ? 118 LYS B CE  1 
ATOM   3412 N  NZ  . LYS B  1 92  ? -30.62668 -26.56202 75.79629  1.000 56.82230  ? 118 LYS B NZ  1 
ATOM   3413 N  N   . LEU B  1 93  ? -24.07555 -24.79208 78.67057  1.000 54.21710  ? 119 LEU B N   1 
ATOM   3414 C  CA  . LEU B  1 93  ? -22.70104 -24.99989 79.11929  1.000 53.27820  ? 119 LEU B CA  1 
ATOM   3415 C  C   . LEU B  1 93  ? -22.26731 -23.91311 80.09650  1.000 53.94115  ? 119 LEU B C   1 
ATOM   3416 O  O   . LEU B  1 93  ? -21.70666 -24.20387 81.16016  1.000 53.73963  ? 119 LEU B O   1 
ATOM   3417 C  CB  . LEU B  1 93  ? -21.75533 -25.04904 77.91748  1.000 53.60763  ? 119 LEU B CB  1 
ATOM   3418 C  CG  . LEU B  1 93  ? -21.58843 -26.39943 77.21897  1.000 53.06410  ? 119 LEU B CG  1 
ATOM   3419 C  CD1 . LEU B  1 93  ? -20.49426 -26.32206 76.16588  1.000 51.98609  ? 119 LEU B CD1 1 
ATOM   3420 C  CD2 . LEU B  1 93  ? -21.28466 -27.49229 78.23062  1.000 52.68219  ? 119 LEU B CD2 1 
ATOM   3421 N  N   . VAL B  1 94  ? -22.52414 -22.64845 79.74999  1.000 54.50227  ? 120 VAL B N   1 
ATOM   3422 C  CA  . VAL B  1 94  ? -22.17046 -21.56039 80.66115  1.000 56.07140  ? 120 VAL B CA  1 
ATOM   3423 C  C   . VAL B  1 94  ? -23.15391 -21.48016 81.82118  1.000 57.66928  ? 120 VAL B C   1 
ATOM   3424 O  O   . VAL B  1 94  ? -22.81300 -20.97311 82.89806  1.000 58.89701  ? 120 VAL B O   1 
ATOM   3425 C  CB  . VAL B  1 94  ? -22.09594 -20.21368 79.92247  1.000 56.07406  ? 120 VAL B CB  1 
ATOM   3426 C  CG1 . VAL B  1 94  ? -21.25874 -19.21833 80.71932  1.000 56.77151  ? 120 VAL B CG1 1 
ATOM   3427 C  CG2 . VAL B  1 94  ? -21.51933 -20.39551 78.54261  1.000 55.51316  ? 120 VAL B CG2 1 
ATOM   3428 N  N   . ALA B  1 95  ? -24.38525 -21.96221 81.62810  1.000 60.00992  ? 121 ALA B N   1 
ATOM   3429 C  CA  . ALA B  1 95  ? -25.35153 -21.97554 82.71744  1.000 63.57212  ? 121 ALA B CA  1 
ATOM   3430 C  C   . ALA B  1 95  ? -24.90942 -22.90285 83.83479  1.000 65.99962  ? 121 ALA B C   1 
ATOM   3431 O  O   . ALA B  1 95  ? -25.30401 -22.71239 84.99016  1.000 68.01356  ? 121 ALA B O   1 
ATOM   3432 C  CB  . ALA B  1 95  ? -26.72683 -22.38120 82.19440  1.000 64.26252  ? 121 ALA B CB  1 
ATOM   3433 N  N   . LYS B  1 96  ? -24.09567 -23.91087 83.51159  1.000 64.39180  ? 122 LYS B N   1 
ATOM   3434 C  CA  . LYS B  1 96  ? -23.45744 -24.70105 84.55878  1.000 65.07874  ? 122 LYS B CA  1 
ATOM   3435 C  C   . LYS B  1 96  ? -22.59745 -23.84037 85.47880  1.000 63.78394  ? 122 LYS B C   1 
ATOM   3436 O  O   . LYS B  1 96  ? -22.36736 -24.22258 86.63144  1.000 65.08279  ? 122 LYS B O   1 
ATOM   3437 C  CB  . LYS B  1 96  ? -22.61588 -25.81814 83.93922  1.000 66.15320  ? 122 LYS B CB  1 
ATOM   3438 C  CG  . LYS B  1 96  ? -23.39561 -26.72332 83.00178  1.000 69.22958  ? 122 LYS B CG  1 
ATOM   3439 C  CD  . LYS B  1 96  ? -24.07634 -27.85492 83.75738  1.000 72.88194  ? 122 LYS B CD  1 
ATOM   3440 C  CE  . LYS B  1 96  ? -23.97329 -29.16712 82.99538  1.000 74.26485  ? 122 LYS B CE  1 
ATOM   3441 N  NZ  . LYS B  1 96  ? -24.70466 -30.27162 83.67449  1.000 75.77761  ? 122 LYS B NZ  1 
ATOM   3442 N  N   . HIS B  1 97  ? -22.11914 -22.69177 84.99713  1.000 62.59871  ? 123 HIS B N   1 
ATOM   3443 C  CA  . HIS B  1 97  ? -21.42300 -21.71715 85.82890  1.000 62.71839  ? 123 HIS B CA  1 
ATOM   3444 C  C   . HIS B  1 97  ? -22.33135 -20.60591 86.33284  1.000 63.13123  ? 123 HIS B C   1 
ATOM   3445 O  O   . HIS B  1 97  ? -22.13781 -20.12119 87.45251  1.000 63.74405  ? 123 HIS B O   1 
ATOM   3446 C  CB  . HIS B  1 97  ? -20.26273 -21.08119 85.05450  1.000 62.86726  ? 123 HIS B CB  1 
ATOM   3447 C  CG  . HIS B  1 97  ? -19.17219 -22.04003 84.69450  1.000 61.44940  ? 123 HIS B CG  1 
ATOM   3448 N  ND1 . HIS B  1 97  ? -18.04638 -22.21123 85.47082  1.000 61.12156  ? 123 HIS B ND1 1 
ATOM   3449 C  CD2 . HIS B  1 97  ? -19.02850 -22.87023 83.63475  1.000 60.45582  ? 123 HIS B CD2 1 
ATOM   3450 C  CE1 . HIS B  1 97  ? -17.25922 -23.11061 84.90840  1.000 60.56771  ? 123 HIS B CE1 1 
ATOM   3451 N  NE2 . HIS B  1 97  ? -17.83156 -23.52539 83.79275  1.000 60.15085  ? 123 HIS B NE2 1 
ATOM   3452 N  N   . ASP B  1 98  ? -23.30814 -20.18986 85.53049  1.000 62.08247  ? 124 ASP B N   1 
ATOM   3453 C  CA  . ASP B  1 98  ? -24.21588 -19.09671 85.87434  1.000 62.41388  ? 124 ASP B CA  1 
ATOM   3454 C  C   . ASP B  1 98  ? -25.64586 -19.59133 85.70203  1.000 62.05330  ? 124 ASP B C   1 
ATOM   3455 O  O   . ASP B  1 98  ? -26.17515 -19.58136 84.57657  1.000 59.61938  ? 124 ASP B O   1 
ATOM   3456 C  CB  . ASP B  1 98  ? -23.94734 -17.87307 85.00564  1.000 64.03180  ? 124 ASP B CB  1 
ATOM   3457 C  CG  . ASP B  1 98  ? -24.95532 -16.76436 85.22674  1.000 67.53730  ? 124 ASP B CG  1 
ATOM   3458 O  OD1 . ASP B  1 98  ? -25.25412 -16.45456 86.39855  1.000 70.11498  ? 124 ASP B OD1 1 
ATOM   3459 O  OD2 . ASP B  1 98  ? -25.44129 -16.19535 84.22703  1.000 68.53053  ? 124 ASP B OD2 1 
ATOM   3460 N  N   . PRO B  1 99  ? -26.30207 -20.01871 86.78205  1.000 64.76940  ? 125 PRO B N   1 
ATOM   3461 C  CA  . PRO B  1 99  ? -27.61329 -20.66748 86.64452  1.000 65.80217  ? 125 PRO B CA  1 
ATOM   3462 C  C   . PRO B  1 99  ? -28.63980 -19.75129 85.99448  1.000 66.87291  ? 125 PRO B C   1 
ATOM   3463 O  O   . PRO B  1 99  ? -28.72673 -18.56100 86.30479  1.000 67.42487  ? 125 PRO B O   1 
ATOM   3464 C  CB  . PRO B  1 99  ? -27.99672 -21.00603 88.09040  1.000 67.72398  ? 125 PRO B CB  1 
ATOM   3465 C  CG  . PRO B  1 99  ? -27.16107 -20.10069 88.93680  1.000 67.98720  ? 125 PRO B CG  1 
ATOM   3466 C  CD  . PRO B  1 99  ? -25.88047 -19.90679 88.18783  1.000 65.68623  ? 125 PRO B CD  1 
ATOM   3467 N  N   . ASP B  1 100 ? -29.41199 -20.32641 85.07292  1.000 66.59182  ? 126 ASP B N   1 
ATOM   3468 C  CA  . ASP B  1 100 ? -30.43909 -19.64397 84.29015  1.000 68.88936  ? 126 ASP B CA  1 
ATOM   3469 C  C   . ASP B  1 100 ? -29.88211 -18.50072 83.44959  1.000 65.80674  ? 126 ASP B C   1 
ATOM   3470 O  O   . ASP B  1 100 ? -30.65775 -17.68393 82.93731  1.000 66.53823  ? 126 ASP B O   1 
ATOM   3471 C  CB  . ASP B  1 100 ? -31.57865 -19.13095 85.18205  1.000 74.29544  ? 126 ASP B CB  1 
ATOM   3472 C  CG  . ASP B  1 100 ? -32.92589 -19.16632 84.48477  1.000 79.22824  ? 126 ASP B CG  1 
ATOM   3473 O  OD1 . ASP B  1 100 ? -33.35331 -18.11787 83.95781  1.000 80.92582  ? 126 ASP B OD1 1 
ATOM   3474 O  OD2 . ASP B  1 100 ? -33.55613 -20.24497 84.46022  1.000 81.06605  ? 126 ASP B OD2 1 
ATOM   3475 N  N   . ASN B  1 101 ? -28.55930 -18.42838 83.28897  1.000 63.37036  ? 127 ASN B N   1 
ATOM   3476 C  CA  . ASN B  1 101 ? -27.90387 -17.39929 82.48106  1.000 61.07344  ? 127 ASN B CA  1 
ATOM   3477 C  C   . ASN B  1 101 ? -28.33272 -15.99824 82.91418  1.000 61.20298  ? 127 ASN B C   1 
ATOM   3478 O  O   . ASN B  1 101 ? -28.74705 -15.16933 82.10191  1.000 61.54219  ? 127 ASN B O   1 
ATOM   3479 C  CB  . ASN B  1 101 ? -28.18222 -17.61445 80.99138  1.000 60.33980  ? 127 ASN B CB  1 
ATOM   3480 C  CG  . ASN B  1 101 ? -27.58391 -18.90260 80.46306  1.000 57.96421  ? 127 ASN B CG  1 
ATOM   3481 O  OD1 . ASN B  1 101 ? -28.29652 -19.76794 79.95261  1.000 56.87643  ? 127 ASN B OD1 1 
ATOM   3482 N  ND2 . ASN B  1 101 ? -26.26736 -19.03385 80.57599  1.000 55.88296  ? 127 ASN B ND2 1 
ATOM   3483 N  N   . LYS B  1 102 ? -28.22443 -15.72709 84.21440  1.000 60.19557  ? 128 LYS B N   1 
ATOM   3484 C  CA  . LYS B  1 102 ? -28.77433 -14.48432 84.74124  1.000 60.94529  ? 128 LYS B CA  1 
ATOM   3485 C  C   . LYS B  1 102 ? -27.76979 -13.34055 84.77901  1.000 59.29598  ? 128 LYS B C   1 
ATOM   3486 O  O   . LYS B  1 102 ? -28.16733 -12.17852 84.63418  1.000 59.77346  ? 128 LYS B O   1 
ATOM   3487 C  CB  . LYS B  1 102 ? -29.35121 -14.71015 86.14428  1.000 63.33021  ? 128 LYS B CB  1 
ATOM   3488 C  CG  . LYS B  1 102 ? -30.69548 -15.45352 86.17252  1.000 66.07670  ? 128 LYS B CG  1 
ATOM   3489 C  CD  . LYS B  1 102 ? -31.55798 -15.22564 84.91798  1.000 67.61367  ? 128 LYS B CD  1 
ATOM   3490 C  CE  . LYS B  1 102 ? -32.03766 -13.78005 84.73678  1.000 68.35427  ? 128 LYS B CE  1 
ATOM   3491 N  NZ  . LYS B  1 102 ? -32.85336 -13.63846 83.49580  1.000 68.05319  ? 128 LYS B NZ  1 
ATOM   3492 N  N   . PHE B  1 103 ? -26.48022 -13.62802 84.96019  1.000 57.35648  ? 129 PHE B N   1 
ATOM   3493 C  CA  . PHE B  1 103 ? -25.48659 -12.57274 85.09084  1.000 56.10060  ? 129 PHE B CA  1 
ATOM   3494 C  C   . PHE B  1 103 ? -24.55620 -12.44055 83.89551  1.000 51.83994  ? 129 PHE B C   1 
ATOM   3495 O  O   . PHE B  1 103 ? -23.97704 -11.36665 83.70584  1.000 51.98849  ? 129 PHE B O   1 
ATOM   3496 C  CB  . PHE B  1 103 ? -24.63269 -12.79688 86.34832  1.000 57.41062  ? 129 PHE B CB  1 
ATOM   3497 C  CG  . PHE B  1 103 ? -25.40095 -12.68280 87.63315  1.000 58.42217  ? 129 PHE B CG  1 
ATOM   3498 C  CD1 . PHE B  1 103 ? -26.00608 -13.79527 88.19289  1.000 59.09604  ? 129 PHE B CD1 1 
ATOM   3499 C  CD2 . PHE B  1 103 ? -25.51713 -11.46446 88.28208  1.000 60.35629  ? 129 PHE B CD2 1 
ATOM   3500 C  CE1 . PHE B  1 103 ? -26.71415 -13.69637 89.37514  1.000 61.22854  ? 129 PHE B CE1 1 
ATOM   3501 C  CE2 . PHE B  1 103 ? -26.22472 -11.35854 89.46620  1.000 62.39762  ? 129 PHE B CE2 1 
ATOM   3502 C  CZ  . PHE B  1 103 ? -26.82369 -12.47661 90.01275  1.000 62.66272  ? 129 PHE B CZ  1 
ATOM   3503 N  N   . ALA B  1 104 ? -24.40712 -13.48381 83.08496  1.000 49.14703  ? 130 ALA B N   1 
ATOM   3504 C  CA  . ALA B  1 104 ? -23.34472 -13.55442 82.09373  1.000 46.84606  ? 130 ALA B CA  1 
ATOM   3505 C  C   . ALA B  1 104 ? -23.90887 -13.73474 80.69214  1.000 46.05180  ? 130 ALA B C   1 
ATOM   3506 O  O   . ALA B  1 104 ? -24.83983 -14.51871 80.48091  1.000 46.53263  ? 130 ALA B O   1 
ATOM   3507 C  CB  . ALA B  1 104 ? -22.38877 -14.70606 82.41364  1.000 46.29224  ? 130 ALA B CB  1 
ATOM   3508 N  N   . MET B  1 105 ? -23.33360 -13.00506 79.73551  1.000 45.15999  ? 131 MET B N   1 
ATOM   3509 C  CA  . MET B  1 105 ? -23.58841 -13.24214 78.32063  1.000 42.46591  ? 131 MET B CA  1 
ATOM   3510 C  C   . MET B  1 105 ? -22.33368 -13.82677 77.69287  1.000 40.14848  ? 131 MET B C   1 
ATOM   3511 O  O   . MET B  1 105 ? -21.29882 -13.14571 77.66085  1.000 37.19746  ? 131 MET B O   1 
ATOM   3512 C  CB  . MET B  1 105 ? -23.99117 -11.95363 77.60523  1.000 43.13515  ? 131 MET B CB  1 
ATOM   3513 C  CG  . MET B  1 105 ? -24.07019 -12.09621 76.09197  1.000 43.78166  ? 131 MET B CG  1 
ATOM   3514 S  SD  . MET B  1 105 ? -24.22042 -10.51994 75.22889  1.000 45.20321  ? 131 MET B SD  1 
ATOM   3515 C  CE  . MET B  1 105 ? -25.85578 -10.00883 75.74778  1.000 46.67663  ? 131 MET B CE  1 
ATOM   3516 N  N   . PRO B  1 106 ? -22.36409 -15.06330 77.19552  1.000 39.42122  ? 132 PRO B N   1 
ATOM   3517 C  CA  . PRO B  1 106 ? -21.13206 -15.68654 76.68774  1.000 41.20446  ? 132 PRO B CA  1 
ATOM   3518 C  C   . PRO B  1 106 ? -20.59500 -14.94759 75.46892  1.000 41.85465  ? 132 PRO B C   1 
ATOM   3519 O  O   . PRO B  1 106 ? -21.30979 -14.73390 74.48738  1.000 41.13869  ? 132 PRO B O   1 
ATOM   3520 C  CB  . PRO B  1 106 ? -21.57177 -17.11383 76.34021  1.000 43.59246  ? 132 PRO B CB  1 
ATOM   3521 C  CG  . PRO B  1 106 ? -23.05304 -17.02228 76.14786  1.000 45.12653  ? 132 PRO B CG  1 
ATOM   3522 C  CD  . PRO B  1 106 ? -23.52919 -15.95713 77.08749  1.000 37.15394  ? 132 PRO B CD  1 
ATOM   3523 N  N   . TYR B  1 107 ? -19.32122 -14.55858 75.54303  1.000 41.87949  ? 133 TYR B N   1 
ATOM   3524 C  CA  . TYR B  1 107 ? -18.66290 -13.76011 74.51877  1.000 41.47316  ? 133 TYR B CA  1 
ATOM   3525 C  C   . TYR B  1 107 ? -17.89268 -14.66193 73.56252  1.000 39.84225  ? 133 TYR B C   1 
ATOM   3526 O  O   . TYR B  1 107 ? -18.28411 -14.83001 72.40302  1.000 40.79633  ? 133 TYR B O   1 
ATOM   3527 C  CB  . TYR B  1 107 ? -17.73655 -12.74649 75.19560  1.000 43.40987  ? 133 TYR B CB  1 
ATOM   3528 C  CG  . TYR B  1 107 ? -17.00535 -11.79486 74.27964  1.000 44.82942  ? 133 TYR B CG  1 
ATOM   3529 C  CD1 . TYR B  1 107 ? -17.69446 -10.97217 73.39873  1.000 45.83510  ? 133 TYR B CD1 1 
ATOM   3530 C  CD2 . TYR B  1 107 ? -15.62115 -11.69480 74.32411  1.000 35.58122  ? 133 TYR B CD2 1 
ATOM   3531 C  CE1 . TYR B  1 107 ? -17.02088 -10.09024 72.57365  1.000 35.60189  ? 133 TYR B CE1 1 
ATOM   3532 C  CE2 . TYR B  1 107 ? -14.94124 -10.81953 73.50540  1.000 35.60186  ? 133 TYR B CE2 1 
ATOM   3533 C  CZ  . TYR B  1 107 ? -15.64406 -10.01975 72.63258  1.000 35.60288  ? 133 TYR B CZ  1 
ATOM   3534 O  OH  . TYR B  1 107 ? -14.96328 -9.14583  71.81925  1.000 35.68422  ? 133 TYR B OH  1 
ATOM   3535 N  N   . MET B  1 108 ? -16.79896 -15.24773 74.04450  1.000 38.66493  ? 134 MET B N   1 
ATOM   3536 C  CA  . MET B  1 108 ? -16.01005 -16.21364 73.29462  1.000 39.45296  ? 134 MET B CA  1 
ATOM   3537 C  C   . MET B  1 108 ? -15.75297 -17.42944 74.17500  1.000 42.25431  ? 134 MET B C   1 
ATOM   3538 O  O   . MET B  1 108 ? -16.03912 -17.42596 75.37556  1.000 44.66753  ? 134 MET B O   1 
ATOM   3539 C  CB  . MET B  1 108 ? -14.68081 -15.61038 72.81789  1.000 36.99050  ? 134 MET B CB  1 
ATOM   3540 C  CG  . MET B  1 108 ? -14.82555 -14.32948 72.01393  1.000 35.41830  ? 134 MET B CG  1 
ATOM   3541 S  SD  . MET B  1 108 ? -15.29217 -14.62547 70.29862  1.000 36.93635  ? 134 MET B SD  1 
ATOM   3542 C  CE  . MET B  1 108 ? -16.18077 -13.11663 69.92858  1.000 37.15167  ? 134 MET B CE  1 
ATOM   3543 N  N   . TRP B  1 109 ? -15.20586 -18.48098 73.56919  1.000 42.37861  ? 135 TRP B N   1 
ATOM   3544 C  CA  . TRP B  1 109 ? -14.88154 -19.68324 74.32359  1.000 44.30450  ? 135 TRP B CA  1 
ATOM   3545 C  C   . TRP B  1 109 ? -13.77884 -20.45193 73.61305  1.000 45.93242  ? 135 TRP B C   1 
ATOM   3546 O  O   . TRP B  1 109 ? -13.60389 -20.33508 72.39789  1.000 45.77901  ? 135 TRP B O   1 
ATOM   3547 C  CB  . TRP B  1 109 ? -16.10919 -20.58025 74.52147  1.000 41.43165  ? 135 TRP B CB  1 
ATOM   3548 C  CG  . TRP B  1 109 ? -16.80758 -20.98440 73.25837  1.000 39.21567  ? 135 TRP B CG  1 
ATOM   3549 C  CD1 . TRP B  1 109 ? -17.65354 -20.22060 72.50806  1.000 37.90616  ? 135 TRP B CD1 1 
ATOM   3550 C  CD2 . TRP B  1 109 ? -16.73782 -22.26067 72.60922  1.000 38.70896  ? 135 TRP B CD2 1 
ATOM   3551 N  NE1 . TRP B  1 109 ? -18.10584 -20.93755 71.42651  1.000 36.27760  ? 135 TRP B NE1 1 
ATOM   3552 C  CE2 . TRP B  1 109 ? -17.55890 -22.19310 71.46590  1.000 37.11804  ? 135 TRP B CE2 1 
ATOM   3553 C  CE3 . TRP B  1 109 ? -16.05652 -23.45143 72.88083  1.000 37.26810  ? 135 TRP B CE3 1 
ATOM   3554 C  CZ2 . TRP B  1 109 ? -17.71719 -23.27006 70.59550  1.000 37.41330  ? 135 TRP B CZ2 1 
ATOM   3555 C  CZ3 . TRP B  1 109 ? -16.21523 -24.51945 72.01549  1.000 36.12187  ? 135 TRP B CZ3 1 
ATOM   3556 C  CH2 . TRP B  1 109 ? -17.03850 -24.42133 70.88701  1.000 37.11033  ? 135 TRP B CH2 1 
ATOM   3557 N  N   . ALA B  1 110 ? -13.03725 -21.23583 74.39495  1.000 46.67668  ? 136 ALA B N   1 
ATOM   3558 C  CA  . ALA B  1 110 ? -11.99131 -22.11016 73.88651  1.000 47.91092  ? 136 ALA B CA  1 
ATOM   3559 C  C   . ALA B  1 110 ? -12.06785 -23.43314 74.63819  1.000 50.00386  ? 136 ALA B C   1 
ATOM   3560 O  O   . ALA B  1 110 ? -12.89870 -23.61380 75.53396  1.000 51.42028  ? 136 ALA B O   1 
ATOM   3561 C  CB  . ALA B  1 110 ? -10.60806 -21.46259 74.02021  1.000 46.42595  ? 136 ALA B CB  1 
ATOM   3562 N  N   . THR B  1 111 ? -11.19586 -24.36986 74.27089  1.000 50.41688  ? 137 THR B N   1 
ATOM   3563 C  CA  . THR B  1 111 ? -11.20305 -25.70259 74.85507  1.000 50.05961  ? 137 THR B CA  1 
ATOM   3564 C  C   . THR B  1 111 ? -9.79576  -26.10686 75.27097  1.000 50.17487  ? 137 THR B C   1 
ATOM   3565 O  O   . THR B  1 111 ? -8.80125  -25.50145 74.86251  1.000 50.58885  ? 137 THR B O   1 
ATOM   3566 C  CB  . THR B  1 111 ? -11.76456 -26.75157 73.88156  1.000 48.75246  ? 137 THR B CB  1 
ATOM   3567 O  OG1 . THR B  1 111 ? -10.95709 -26.78808 72.69844  1.000 48.31317  ? 137 THR B OG1 1 
ATOM   3568 C  CG2 . THR B  1 111 ? -13.20289 -26.42712 73.50547  1.000 48.24873  ? 137 THR B CG2 1 
ATOM   3569 N  N   . THR B  1 112 ? -9.73064  -27.14908 76.09713  1.000 48.99243  ? 138 THR B N   1 
ATOM   3570 C  CA  . THR B  1 112 ? -8.47174  -27.76962 76.50344  1.000 47.98259  ? 138 THR B CA  1 
ATOM   3571 C  C   . THR B  1 112 ? -8.28903  -29.01974 75.64906  1.000 46.41520  ? 138 THR B C   1 
ATOM   3572 O  O   . THR B  1 112 ? -8.92735  -30.04801 75.88999  1.000 45.48019  ? 138 THR B O   1 
ATOM   3573 C  CB  . THR B  1 112 ? -8.47946  -28.10171 77.99257  1.000 48.76663  ? 138 THR B CB  1 
ATOM   3574 O  OG1 . THR B  1 112 ? -8.89529  -26.95281 78.74206  1.000 48.71245  ? 138 THR B OG1 1 
ATOM   3575 C  CG2 . THR B  1 112 ? -7.09220  -28.52195 78.45107  1.000 48.20304  ? 138 THR B CG2 1 
ATOM   3576 N  N   . GLY B  1 113 ? -7.42103  -28.92748 74.64321  1.000 46.39418  ? 139 GLY B N   1 
ATOM   3577 C  CA  . GLY B  1 113 ? -7.24236  -29.98382 73.67391  1.000 47.87965  ? 139 GLY B CA  1 
ATOM   3578 C  C   . GLY B  1 113 ? -5.78568  -30.39485 73.56923  1.000 49.85896  ? 139 GLY B C   1 
ATOM   3579 O  O   . GLY B  1 113 ? -5.00622  -30.26945 74.52006  1.000 49.42279  ? 139 GLY B O   1 
ATOM   3580 N  N   . ILE B  1 114 ? -5.42050  -30.88208 72.38467  1.000 50.20333  ? 140 ILE B N   1 
ATOM   3581 C  CA  . ILE B  1 114 ? -4.09630  -31.44694 72.14587  1.000 50.62211  ? 140 ILE B CA  1 
ATOM   3582 C  C   . ILE B  1 114 ? -3.37412  -30.60331 71.10501  1.000 53.35690  ? 140 ILE B C   1 
ATOM   3583 O  O   . ILE B  1 114 ? -3.85573  -30.45585 69.97607  1.000 54.04976  ? 140 ILE B O   1 
ATOM   3584 C  CB  . ILE B  1 114 ? -4.17404  -32.91101 71.68765  1.000 49.09283  ? 140 ILE B CB  1 
ATOM   3585 C  CG1 . ILE B  1 114 ? -4.96773  -33.75090 72.68989  1.000 47.22527  ? 140 ILE B CG1 1 
ATOM   3586 C  CG2 . ILE B  1 114 ? -2.77781  -33.47552 71.51103  1.000 50.11664  ? 140 ILE B CG2 1 
ATOM   3587 C  CD1 . ILE B  1 114 ? -5.05490  -35.21546 72.31737  1.000 46.40207  ? 140 ILE B CD1 1 
ATOM   3588 N  N   . GLY B  1 115 ? -2.21918  -30.05896 71.48023  1.000 54.60970  ? 141 GLY B N   1 
ATOM   3589 C  CA  . GLY B  1 115 ? -1.30378  -29.47669 70.51237  1.000 54.38820  ? 141 GLY B CA  1 
ATOM   3590 C  C   . GLY B  1 115 ? -0.27304  -30.52106 70.11734  1.000 55.23143  ? 141 GLY B C   1 
ATOM   3591 O  O   . GLY B  1 115 ? 0.14801   -31.33214 70.93598  1.000 55.85296  ? 141 GLY B O   1 
ATOM   3592 N  N   . TYR B  1 116 ? 0.11990   -30.50282 68.84761  1.000 55.00438  ? 142 TYR B N   1 
ATOM   3593 C  CA  . TYR B  1 116 ? 0.94786   -31.59854 68.36167  1.000 56.19508  ? 142 TYR B CA  1 
ATOM   3594 C  C   . TYR B  1 116 ? 1.72667   -31.18414 67.12280  1.000 55.09867  ? 142 TYR B C   1 
ATOM   3595 O  O   . TYR B  1 116 ? 1.36683   -30.23661 66.41693  1.000 53.79755  ? 142 TYR B O   1 
ATOM   3596 C  CB  . TYR B  1 116 ? 0.10451   -32.84091 68.05325  1.000 58.70483  ? 142 TYR B CB  1 
ATOM   3597 C  CG  . TYR B  1 116 ? -0.81424  -32.66018 66.86928  1.000 60.40397  ? 142 TYR B CG  1 
ATOM   3598 C  CD1 . TYR B  1 116 ? -1.98082  -31.91570 66.97946  1.000 60.21812  ? 142 TYR B CD1 1 
ATOM   3599 C  CD2 . TYR B  1 116 ? -0.50448  -33.21523 65.63557  1.000 62.01324  ? 142 TYR B CD2 1 
ATOM   3600 C  CE1 . TYR B  1 116 ? -2.81997  -31.74070 65.89987  1.000 60.85436  ? 142 TYR B CE1 1 
ATOM   3601 C  CE2 . TYR B  1 116 ? -1.33632  -33.04310 64.54707  1.000 62.42290  ? 142 TYR B CE2 1 
ATOM   3602 C  CZ  . TYR B  1 116 ? -2.49236  -32.30393 64.68478  1.000 61.82317  ? 142 TYR B CZ  1 
ATOM   3603 O  OH  . TYR B  1 116 ? -3.32607  -32.13306 63.60470  1.000 62.12076  ? 142 TYR B OH  1 
ATOM   3604 N  N   . ASN B  1 117 ? 2.79936   -31.93376 66.87131  1.000 55.65435  ? 143 ASN B N   1 
ATOM   3605 C  CA  . ASN B  1 117 ? 3.61684   -31.81129 65.67129  1.000 56.40885  ? 143 ASN B CA  1 
ATOM   3606 C  C   . ASN B  1 117 ? 3.15305   -32.85217 64.65912  1.000 57.06799  ? 143 ASN B C   1 
ATOM   3607 O  O   . ASN B  1 117 ? 3.28805   -34.05255 64.90018  1.000 57.07274  ? 143 ASN B O   1 
ATOM   3608 C  CB  . ASN B  1 117 ? 5.09389   -32.02263 66.00168  1.000 56.83477  ? 143 ASN B CB  1 
ATOM   3609 C  CG  . ASN B  1 117 ? 5.99611   -31.82439 64.79989  1.000 55.83512  ? 143 ASN B CG  1 
ATOM   3610 O  OD1 . ASN B  1 117 ? 6.14135   -32.71707 63.96454  1.000 54.72623  ? 143 ASN B OD1 1 
ATOM   3611 N  ND2 . ASN B  1 117 ? 6.63665   -30.66492 64.72604  1.000 55.27980  ? 143 ASN B ND2 1 
ATOM   3612 N  N   . VAL B  1 118 ? 2.62031   -32.39450 63.52679  1.000 56.74942  ? 144 VAL B N   1 
ATOM   3613 C  CA  . VAL B  1 118 ? 2.08621   -33.31236 62.51939  1.000 57.89134  ? 144 VAL B CA  1 
ATOM   3614 C  C   . VAL B  1 118 ? 3.17203   -34.27272 62.03564  1.000 59.39413  ? 144 VAL B C   1 
ATOM   3615 O  O   . VAL B  1 118 ? 3.05102   -35.50851 62.15977  1.000 60.41966  ? 144 VAL B O   1 
ATOM   3616 C  CB  . VAL B  1 118 ? 1.47325   -32.50714 61.35711  1.000 58.68281  ? 144 VAL B CB  1 
ATOM   3617 C  CG1 . VAL B  1 118 ? 0.58611   -33.38037 60.50002  1.000 59.05429  ? 144 VAL B CG1 1 
ATOM   3618 C  CG2 . VAL B  1 118 ? 0.68147   -31.31736 61.90332  1.000 58.05062  ? 144 VAL B CG2 1 
ATOM   3619 N  N   . ASP B  1 119 ? 4.26066   -33.70589 61.49972  1.000 59.95788  ? 145 ASP B N   1 
ATOM   3620 C  CA  . ASP B  1 119 ? 5.31835   -34.49737 60.87754  1.000 61.96790  ? 145 ASP B CA  1 
ATOM   3621 C  C   . ASP B  1 119 ? 5.86215   -35.55209 61.83394  1.000 61.50077  ? 145 ASP B C   1 
ATOM   3622 O  O   . ASP B  1 119 ? 5.87216   -36.74734 61.51550  1.000 61.67187  ? 145 ASP B O   1 
ATOM   3623 C  CB  . ASP B  1 119 ? 6.44755   -33.58050 60.39171  1.000 64.56433  ? 145 ASP B CB  1 
ATOM   3624 C  CG  . ASP B  1 119 ? 5.94108   -32.24742 59.85714  1.000 65.57596  ? 145 ASP B CG  1 
ATOM   3625 O  OD1 . ASP B  1 119 ? 6.22076   -31.20366 60.48518  1.000 65.46768  ? 145 ASP B OD1 1 
ATOM   3626 O  OD2 . ASP B  1 119 ? 5.26370   -32.24240 58.80789  1.000 66.06140  ? 145 ASP B OD2 1 
ATOM   3627 N  N   . LYS B  1 120 ? 6.30948   -35.12829 63.01861  1.000 60.83185  ? 146 LYS B N   1 
ATOM   3628 C  CA  . LYS B  1 120 ? 6.91495   -36.06936 63.95584  1.000 62.20623  ? 146 LYS B CA  1 
ATOM   3629 C  C   . LYS B  1 120 ? 5.90210   -37.09129 64.46425  1.000 61.34515  ? 146 LYS B C   1 
ATOM   3630 O  O   . LYS B  1 120 ? 6.22459   -38.28187 64.57525  1.000 60.17529  ? 146 LYS B O   1 
ATOM   3631 C  CB  . LYS B  1 120 ? 7.55368   -35.31665 65.12500  1.000 62.94689  ? 146 LYS B CB  1 
ATOM   3632 C  CG  . LYS B  1 120 ? 8.76446   -34.46994 64.76272  1.000 65.61386  ? 146 LYS B CG  1 
ATOM   3633 C  CD  . LYS B  1 120 ? 9.64029   -34.21966 65.98521  1.000 67.34108  ? 146 LYS B CD  1 
ATOM   3634 C  CE  . LYS B  1 120 ? 9.46687   -32.80329 66.51342  1.000 67.36620  ? 146 LYS B CE  1 
ATOM   3635 N  NZ  . LYS B  1 120 ? 10.61097  -32.37675 67.36739  1.000 68.58190  ? 146 LYS B NZ  1 
ATOM   3636 N  N   . VAL B  1 121 ? 4.67767   -36.65202 64.77881  1.000 61.82023  ? 147 VAL B N   1 
ATOM   3637 C  CA  . VAL B  1 121 ? 3.68688   -37.56780 65.34285  1.000 63.82456  ? 147 VAL B CA  1 
ATOM   3638 C  C   . VAL B  1 121 ? 3.44933   -38.74228 64.40869  1.000 69.28211  ? 147 VAL B C   1 
ATOM   3639 O  O   . VAL B  1 121 ? 3.50172   -39.90512 64.83504  1.000 71.06657  ? 147 VAL B O   1 
ATOM   3640 C  CB  . VAL B  1 121 ? 2.37342   -36.83545 65.67566  1.000 60.77134  ? 147 VAL B CB  1 
ATOM   3641 C  CG1 . VAL B  1 121 ? 1.23078   -37.82210 65.76321  1.000 60.21951  ? 147 VAL B CG1 1 
ATOM   3642 C  CG2 . VAL B  1 121 ? 2.47526   -36.12932 67.01900  1.000 58.90711  ? 147 VAL B CG2 1 
ATOM   3643 N  N   . LYS B  1 122 ? 3.20072   -38.46549 63.11839  1.000 72.09909  ? 148 LYS B N   1 
ATOM   3644 C  CA  . LYS B  1 122 ? 2.90279   -39.59245 62.23919  1.000 75.08899  ? 148 LYS B CA  1 
ATOM   3645 C  C   . LYS B  1 122 ? 4.14682   -40.18593 61.57060  1.000 73.73600  ? 148 LYS B C   1 
ATOM   3646 O  O   . LYS B  1 122 ? 4.04594   -41.23389 60.91128  1.000 72.12694  ? 148 LYS B O   1 
ATOM   3647 C  CB  . LYS B  1 122 ? 1.84829   -39.21447 61.18169  1.000 79.01432  ? 148 LYS B CB  1 
ATOM   3648 C  CG  . LYS B  1 122 ? 2.16086   -38.21670 60.06770  1.000 81.98453  ? 148 LYS B CG  1 
ATOM   3649 C  CD  . LYS B  1 122 ? 1.27915   -38.54701 58.87291  1.000 84.62751  ? 148 LYS B CD  1 
ATOM   3650 C  CE  . LYS B  1 122 ? -0.06129  -39.14283 59.29781  1.000 85.77979  ? 148 LYS B CE  1 
ATOM   3651 N  NZ  . LYS B  1 122 ? -0.99564  -38.30121 60.12211  1.000 85.47191  ? 148 LYS B NZ  1 
ATOM   3652 N  N   . ALA B  1 123 ? 5.32595   -39.58074 61.76211  1.000 73.30237  ? 149 ALA B N   1 
ATOM   3653 C  CA  . ALA B  1 123 ? 6.56015   -40.30385 61.49279  1.000 73.94404  ? 149 ALA B CA  1 
ATOM   3654 C  C   . ALA B  1 123 ? 6.81549   -41.34509 62.56833  1.000 70.62122  ? 149 ALA B C   1 
ATOM   3655 O  O   . ALA B  1 123 ? 7.49683   -42.34238 62.31634  1.000 69.90298  ? 149 ALA B O   1 
ATOM   3656 C  CB  . ALA B  1 123 ? 7.72768   -39.32725 61.41192  1.000 77.93349  ? 149 ALA B CB  1 
ATOM   3657 N  N   . VAL B  1 124 ? 6.30332   -41.11132 63.77441  1.000 67.51566  ? 150 VAL B N   1 
ATOM   3658 C  CA  . VAL B  1 124 ? 6.44178   -42.06964 64.86821  1.000 66.18442  ? 150 VAL B CA  1 
ATOM   3659 C  C   . VAL B  1 124 ? 5.31412   -43.10288 64.87001  1.000 68.29917  ? 150 VAL B C   1 
ATOM   3660 O  O   . VAL B  1 124 ? 5.54248   -44.27818 65.17244  1.000 68.97160  ? 150 VAL B O   1 
ATOM   3661 C  CB  . VAL B  1 124 ? 6.51559   -41.30069 66.20252  1.000 62.70669  ? 150 VAL B CB  1 
ATOM   3662 C  CG1 . VAL B  1 124 ? 6.43749   -42.24573 67.37391  1.000 61.65470  ? 150 VAL B CG1 1 
ATOM   3663 C  CG2 . VAL B  1 124 ? 7.78788   -40.47191 66.25560  1.000 62.83755  ? 150 VAL B CG2 1 
ATOM   3664 N  N   . LEU B  1 125 ? 4.08736   -42.70867 64.51365  1.000 70.03508  ? 151 LEU B N   1 
ATOM   3665 C  CA  . LEU B  1 125 ? 2.92234   -43.56439 64.72163  1.000 72.53822  ? 151 LEU B CA  1 
ATOM   3666 C  C   . LEU B  1 125 ? 2.17153   -43.89372 63.43486  1.000 76.64245  ? 151 LEU B C   1 
ATOM   3667 O  O   . LEU B  1 125 ? 0.96601   -44.15927 63.48170  1.000 75.17887  ? 151 LEU B O   1 
ATOM   3668 C  CB  . LEU B  1 125 ? 1.96857   -42.92296 65.72934  1.000 71.02198  ? 151 LEU B CB  1 
ATOM   3669 C  CG  . LEU B  1 125 ? 1.95026   -43.55387 67.12213  1.000 72.74186  ? 151 LEU B CG  1 
ATOM   3670 C  CD1 . LEU B  1 125 ? 1.11203   -42.71577 68.07394  1.000 73.71979  ? 151 LEU B CD1 1 
ATOM   3671 C  CD2 . LEU B  1 125 ? 1.43442   -44.98038 67.05746  1.000 74.07430  ? 151 LEU B CD2 1 
ATOM   3672 N  N   . GLY B  1 126 ? 2.85317   -43.91246 62.29380  1.000 82.93300  ? 152 GLY B N   1 
ATOM   3673 C  CA  . GLY B  1 126 ? 2.21856   -44.32913 61.05756  1.000 87.34271  ? 152 GLY B CA  1 
ATOM   3674 C  C   . GLY B  1 126 ? 1.23203   -43.33057 60.48695  1.000 88.64843  ? 152 GLY B C   1 
ATOM   3675 O  O   . GLY B  1 126 ? 0.82687   -42.38172 61.16543  1.000 87.87580  ? 152 GLY B O   1 
ATOM   3676 N  N   . GLU B  1 127 ? 0.82370   -43.54667 59.23777  1.000 88.83609  ? 153 GLU B N   1 
ATOM   3677 C  CA  . GLU B  1 127 ? -0.01313  -42.59487 58.51718  1.000 90.26678  ? 153 GLU B CA  1 
ATOM   3678 C  C   . GLU B  1 127 ? -1.49093  -42.67752 58.89239  1.000 92.45995  ? 153 GLU B C   1 
ATOM   3679 O  O   . GLU B  1 127 ? -2.32713  -42.11688 58.17522  1.000 92.83779  ? 153 GLU B O   1 
ATOM   3680 C  CB  . GLU B  1 127 ? 0.15282   -42.78716 57.00734  1.000 91.27541  ? 153 GLU B CB  1 
ATOM   3681 C  CG  . GLU B  1 127 ? 0.23470   -41.47888 56.23665  1.000 92.20174  ? 153 GLU B CG  1 
ATOM   3682 C  CD  . GLU B  1 127 ? 1.07733   -41.58482 54.98203  1.000 95.04491  ? 153 GLU B CD  1 
ATOM   3683 O  OE1 . GLU B  1 127 ? 2.00587   -40.76506 54.82014  1.000 95.87394  ? 153 GLU B OE1 1 
ATOM   3684 O  OE2 . GLU B  1 127 ? 0.80992   -42.48291 54.15660  1.000 96.64738  ? 153 GLU B OE2 1 
ATOM   3685 N  N   . ASN B  1 128 ? -1.83211  -43.35139 59.98678  1.000 95.03571  ? 154 ASN B N   1 
ATOM   3686 C  CA  . ASN B  1 128 ? -3.19659  -43.39972 60.49930  1.000 94.85026  ? 154 ASN B CA  1 
ATOM   3687 C  C   . ASN B  1 128 ? -3.21136  -43.09573 61.98944  1.000 92.67469  ? 154 ASN B C   1 
ATOM   3688 O  O   . ASN B  1 128 ? -3.92036  -43.73802 62.77007  1.000 97.13949  ? 154 ASN B O   1 
ATOM   3689 C  CB  . ASN B  1 128 ? -3.84521  -44.75220 60.21449  1.000 97.21696  ? 154 ASN B CB  1 
ATOM   3690 C  CG  . ASN B  1 128 ? -4.26865  -44.90128 58.76675  1.000 99.35339  ? 154 ASN B CG  1 
ATOM   3691 O  OD1 . ASN B  1 128 ? -4.83254  -43.98079 58.17469  1.000 99.85283  ? 154 ASN B OD1 1 
ATOM   3692 N  ND2 . ASN B  1 128 ? -4.00078  -46.06626 58.18908  1.000 101.21423 ? 154 ASN B ND2 1 
ATOM   3693 N  N   . ALA B  1 129 ? -2.42724  -42.10640 62.39984  1.000 85.48766  ? 155 ALA B N   1 
ATOM   3694 C  CA  . ALA B  1 129 ? -2.31105  -41.77471 63.81444  1.000 80.70135  ? 155 ALA B CA  1 
ATOM   3695 C  C   . ALA B  1 129 ? -3.62068  -41.18556 64.32745  1.000 75.26927  ? 155 ALA B C   1 
ATOM   3696 O  O   . ALA B  1 129 ? -4.16283  -40.26146 63.70972  1.000 74.75976  ? 155 ALA B O   1 
ATOM   3697 C  CB  . ALA B  1 129 ? -1.16562  -40.79007 64.03445  1.000 80.23562  ? 155 ALA B CB  1 
ATOM   3698 N  N   . PRO B  1 130 ? -4.16009  -41.68621 65.44345  1.000 71.60062  ? 156 PRO B N   1 
ATOM   3699 C  CA  . PRO B  1 130 ? -5.42575  -41.14619 65.95972  1.000 67.55256  ? 156 PRO B CA  1 
ATOM   3700 C  C   . PRO B  1 130 ? -5.25101  -39.77656 66.59445  1.000 63.20647  ? 156 PRO B C   1 
ATOM   3701 O  O   . PRO B  1 130 ? -5.21464  -39.65284 67.82263  1.000 64.65412  ? 156 PRO B O   1 
ATOM   3702 C  CB  . PRO B  1 130 ? -5.86310  -42.19218 66.99747  1.000 69.34799  ? 156 PRO B CB  1 
ATOM   3703 C  CG  . PRO B  1 130 ? -4.94850  -43.37787 66.79697  1.000 71.06027  ? 156 PRO B CG  1 
ATOM   3704 C  CD  . PRO B  1 130 ? -3.67944  -42.81867 66.24808  1.000 71.24555  ? 156 PRO B CD  1 
ATOM   3705 N  N   . VAL B  1 131 ? -5.14730  -38.73820 65.76351  1.000 57.39242  ? 157 VAL B N   1 
ATOM   3706 C  CA  . VAL B  1 131 ? -4.92130  -37.39308 66.28015  1.000 57.53748  ? 157 VAL B CA  1 
ATOM   3707 C  C   . VAL B  1 131 ? -6.21847  -36.71955 66.71563  1.000 56.38590  ? 157 VAL B C   1 
ATOM   3708 O  O   . VAL B  1 131 ? -6.18976  -35.83327 67.57928  1.000 57.74631  ? 157 VAL B O   1 
ATOM   3709 C  CB  . VAL B  1 131 ? -4.18323  -36.54560 65.23026  1.000 59.14106  ? 157 VAL B CB  1 
ATOM   3710 C  CG1 . VAL B  1 131 ? -3.77008  -35.21005 65.81622  1.000 59.73416  ? 157 VAL B CG1 1 
ATOM   3711 C  CG2 . VAL B  1 131 ? -2.96570  -37.29723 64.71131  1.000 58.94705  ? 157 VAL B CG2 1 
ATOM   3712 N  N   . ASP B  1 132 ? -7.35982  -37.12024 66.15602  1.000 54.83984  ? 158 ASP B N   1 
ATOM   3713 C  CA  . ASP B  1 132 ? -8.65521  -36.62762 66.60712  1.000 52.79973  ? 158 ASP B CA  1 
ATOM   3714 C  C   . ASP B  1 132 ? -9.16679  -37.36452 67.84018  1.000 50.37310  ? 158 ASP B C   1 
ATOM   3715 O  O   . ASP B  1 132 ? -10.36822 -37.31320 68.12927  1.000 49.42679  ? 158 ASP B O   1 
ATOM   3716 C  CB  . ASP B  1 132 ? -9.68301  -36.72770 65.47661  1.000 53.41955  ? 158 ASP B CB  1 
ATOM   3717 C  CG  . ASP B  1 132 ? -9.88506  -38.15206 64.99484  1.000 54.73190  ? 158 ASP B CG  1 
ATOM   3718 O  OD1 . ASP B  1 132 ? -9.06056  -39.02484 65.33935  1.000 55.95566  ? 158 ASP B OD1 1 
ATOM   3719 O  OD2 . ASP B  1 132 ? -10.87368 -38.40023 64.27366  1.000 56.31541  ? 158 ASP B OD2 1 
ATOM   3720 N  N   . SER B  1 133 ? -8.28292  -38.04582 68.56509  1.000 48.71791  ? 159 SER B N   1 
ATOM   3721 C  CA  . SER B  1 133 ? -8.65352  -38.86329 69.70856  1.000 45.57425  ? 159 SER B CA  1 
ATOM   3722 C  C   . SER B  1 133 ? -7.74323  -38.54921 70.88549  1.000 44.88197  ? 159 SER B C   1 
ATOM   3723 O  O   . SER B  1 133 ? -6.60955  -38.09332 70.71082  1.000 45.06163  ? 159 SER B O   1 
ATOM   3724 C  CB  . SER B  1 133 ? -8.56444  -40.36016 69.37390  1.000 45.49557  ? 159 SER B CB  1 
ATOM   3725 O  OG  . SER B  1 133 ? -9.30031  -41.14111 70.29791  1.000 45.55987  ? 159 SER B OG  1 
ATOM   3726 N  N   . TRP B  1 134 ? -8.25333  -38.79621 72.09376  1.000 43.09212  ? 160 TRP B N   1 
ATOM   3727 C  CA  . TRP B  1 134 ? -7.40835  -38.70973 73.27734  1.000 42.79885  ? 160 TRP B CA  1 
ATOM   3728 C  C   . TRP B  1 134 ? -6.44799  -39.88606 73.38381  1.000 45.07648  ? 160 TRP B C   1 
ATOM   3729 O  O   . TRP B  1 134 ? -5.48425  -39.81034 74.15497  1.000 46.93555  ? 160 TRP B O   1 
ATOM   3730 C  CB  . TRP B  1 134 ? -8.26872  -38.61093 74.53964  1.000 41.57995  ? 160 TRP B CB  1 
ATOM   3731 C  CG  . TRP B  1 134 ? -8.80763  -37.22987 74.78429  1.000 39.13058  ? 160 TRP B CG  1 
ATOM   3732 C  CD1 . TRP B  1 134 ? -10.10394 -36.82151 74.66205  1.000 38.56083  ? 160 TRP B CD1 1 
ATOM   3733 C  CD2 . TRP B  1 134 ? -8.05976  -36.07403 75.18356  1.000 37.51155  ? 160 TRP B CD2 1 
ATOM   3734 N  NE1 . TRP B  1 134 ? -10.21031 -35.48505 74.96410  1.000 37.48386  ? 160 TRP B NE1 1 
ATOM   3735 C  CE2 . TRP B  1 134 ? -8.96947  -35.00326 75.28879  1.000 36.91928  ? 160 TRP B CE2 1 
ATOM   3736 C  CE3 . TRP B  1 134 ? -6.71047  -35.84197 75.46562  1.000 36.69596  ? 160 TRP B CE3 1 
ATOM   3737 C  CZ2 . TRP B  1 134 ? -8.57227  -33.71945 75.65886  1.000 36.05744  ? 160 TRP B CZ2 1 
ATOM   3738 C  CZ3 . TRP B  1 134 ? -6.31864  -34.56810 75.83629  1.000 35.82975  ? 160 TRP B CZ3 1 
ATOM   3739 C  CH2 . TRP B  1 134 ? -7.24587  -33.52335 75.92932  1.000 35.66745  ? 160 TRP B CH2 1 
ATOM   3740 N  N   . ASP B  1 135 ? -6.68135  -40.95938 72.62068  1.000 46.36100  ? 161 ASP B N   1 
ATOM   3741 C  CA  . ASP B  1 135 ? -5.71056  -42.04302 72.51929  1.000 47.91092  ? 161 ASP B CA  1 
ATOM   3742 C  C   . ASP B  1 135 ? -4.35726  -41.54964 72.02883  1.000 48.96325  ? 161 ASP B C   1 
ATOM   3743 O  O   . ASP B  1 135 ? -3.34942  -42.23793 72.22315  1.000 48.89806  ? 161 ASP B O   1 
ATOM   3744 C  CB  . ASP B  1 135 ? -6.23035  -43.13276 71.57944  1.000 49.64565  ? 161 ASP B CB  1 
ATOM   3745 C  CG  . ASP B  1 135 ? -7.62652  -43.59851 71.93921  1.000 51.62406  ? 161 ASP B CG  1 
ATOM   3746 O  OD1 . ASP B  1 135 ? -8.45514  -43.75670 71.01842  1.000 52.94368  ? 161 ASP B OD1 1 
ATOM   3747 O  OD2 . ASP B  1 135 ? -7.89453  -43.81201 73.13976  1.000 52.76875  ? 161 ASP B OD2 1 
ATOM   3748 N  N   . LEU B  1 136 ? -4.31888  -40.37946 71.38571  1.000 49.82497  ? 162 LEU B N   1 
ATOM   3749 C  CA  . LEU B  1 136 ? -3.05088  -39.77764 70.99120  1.000 50.72542  ? 162 LEU B CA  1 
ATOM   3750 C  C   . LEU B  1 136 ? -2.15014  -39.52520 72.19262  1.000 52.72983  ? 162 LEU B C   1 
ATOM   3751 O  O   . LEU B  1 136 ? -0.92168  -39.60299 72.07401  1.000 53.85626  ? 162 LEU B O   1 
ATOM   3752 C  CB  . LEU B  1 136 ? -3.31292  -38.47197 70.23807  1.000 50.36179  ? 162 LEU B CB  1 
ATOM   3753 C  CG  . LEU B  1 136 ? -2.11819  -37.60500 69.83566  1.000 51.79003  ? 162 LEU B CG  1 
ATOM   3754 C  CD1 . LEU B  1 136 ? -1.24941  -38.32104 68.81836  1.000 51.37361  ? 162 LEU B CD1 1 
ATOM   3755 C  CD2 . LEU B  1 136 ? -2.59459  -36.27203 69.28572  1.000 53.06119  ? 162 LEU B CD2 1 
ATOM   3756 N  N   . ILE B  1 137 ? -2.73426  -39.23948 73.35512  1.000 51.97162  ? 163 ILE B N   1 
ATOM   3757 C  CA  . ILE B  1 137 ? -1.94550  -38.87048 74.52692  1.000 53.51011  ? 163 ILE B CA  1 
ATOM   3758 C  C   . ILE B  1 137 ? -2.28495  -39.68028 75.76861  1.000 53.33289  ? 163 ILE B C   1 
ATOM   3759 O  O   . ILE B  1 137 ? -1.45645  -39.75447 76.69559  1.000 54.13268  ? 163 ILE B O   1 
ATOM   3760 C  CB  . ILE B  1 137 ? -2.09536  -37.35829 74.81472  1.000 54.95036  ? 163 ILE B CB  1 
ATOM   3761 C  CG1 . ILE B  1 137 ? -0.94629  -36.85139 75.68743  1.000 56.44870  ? 163 ILE B CG1 1 
ATOM   3762 C  CG2 . ILE B  1 137 ? -3.43364  -37.06282 75.46481  1.000 55.01387  ? 163 ILE B CG2 1 
ATOM   3763 C  CD1 . ILE B  1 137 ? 0.27699   -36.45377 74.90832  1.000 55.71742  ? 163 ILE B CD1 1 
ATOM   3764 N  N   . LEU B  1 138 ? -3.45171  -40.31715 75.85708  1.000 51.75002  ? 164 LEU B N   1 
ATOM   3765 C  CA  . LEU B  1 138 ? -3.84713  -41.03274 77.06183  1.000 49.96988  ? 164 LEU B CA  1 
ATOM   3766 C  C   . LEU B  1 138 ? -3.73962  -42.54486 76.92660  1.000 50.61995  ? 164 LEU B C   1 
ATOM   3767 O  O   . LEU B  1 138 ? -4.12075  -43.26431 77.85619  1.000 52.30539  ? 164 LEU B O   1 
ATOM   3768 C  CB  . LEU B  1 138 ? -5.27323  -40.64033 77.46338  1.000 47.82092  ? 164 LEU B CB  1 
ATOM   3769 C  CG  . LEU B  1 138 ? -5.44602  -39.15496 77.79330  1.000 47.42459  ? 164 LEU B CG  1 
ATOM   3770 C  CD1 . LEU B  1 138 ? -6.78988  -38.89198 78.44957  1.000 47.34523  ? 164 LEU B CD1 1 
ATOM   3771 C  CD2 . LEU B  1 138 ? -4.30895  -38.65876 78.67695  1.000 47.53834  ? 164 LEU B CD2 1 
ATOM   3772 N  N   . LYS B  1 139 ? -3.23614  -43.04688 75.80004  1.000 50.78794  ? 165 LYS B N   1 
ATOM   3773 C  CA  . LYS B  1 139 ? -2.90901  -44.46300 75.69628  1.000 51.25276  ? 165 LYS B CA  1 
ATOM   3774 C  C   . LYS B  1 139 ? -1.42564  -44.65719 75.95491  1.000 49.76973  ? 165 LYS B C   1 
ATOM   3775 O  O   . LYS B  1 139 ? -0.60210  -44.00251 75.29911  1.000 48.68642  ? 165 LYS B O   1 
ATOM   3776 C  CB  . LYS B  1 139 ? -3.26838  -45.00775 74.31615  1.000 53.61843  ? 165 LYS B CB  1 
ATOM   3777 C  CG  . LYS B  1 139 ? -4.69563  -45.51927 74.19663  1.000 54.95329  ? 165 LYS B CG  1 
ATOM   3778 C  CD  . LYS B  1 139 ? -4.78525  -46.69828 73.23715  1.000 55.78183  ? 165 LYS B CD  1 
ATOM   3779 C  CE  . LYS B  1 139 ? -4.83640  -48.02106 73.98774  1.000 56.59091  ? 165 LYS B CE  1 
ATOM   3780 N  NZ  . LYS B  1 139 ? -4.90283  -49.18807 73.06410  1.000 57.67654  ? 165 LYS B NZ  1 
ATOM   3781 N  N   . PRO B  1 140 ? -1.04004  -45.52096 76.89701  1.000 50.06242  ? 166 PRO B N   1 
ATOM   3782 C  CA  . PRO B  1 140 ? 0.39594   -45.71370 77.15899  1.000 51.33108  ? 166 PRO B CA  1 
ATOM   3783 C  C   . PRO B  1 140 ? 1.15520   -46.26683 75.96702  1.000 53.01701  ? 166 PRO B C   1 
ATOM   3784 O  O   . PRO B  1 140 ? 2.35141   -45.98545 75.82227  1.000 52.98289  ? 166 PRO B O   1 
ATOM   3785 C  CB  . PRO B  1 140 ? 0.41005   -46.69075 78.34434  1.000 51.27254  ? 166 PRO B CB  1 
ATOM   3786 C  CG  . PRO B  1 140 ? -0.93324  -47.35004 78.32160  1.000 51.64651  ? 166 PRO B CG  1 
ATOM   3787 C  CD  . PRO B  1 140 ? -1.88483  -46.32070 77.79891  1.000 50.15663  ? 166 PRO B CD  1 
ATOM   3788 N  N   . GLU B  1 141 ? 0.49074   -47.03517 75.09971  1.000 53.67705  ? 167 GLU B N   1 
ATOM   3789 C  CA  . GLU B  1 141 ? 1.16921   -47.61691 73.94594  1.000 55.10288  ? 167 GLU B CA  1 
ATOM   3790 C  C   . GLU B  1 141 ? 1.68324   -46.54541 72.99233  1.000 53.73828  ? 167 GLU B C   1 
ATOM   3791 O  O   . GLU B  1 141 ? 2.74259   -46.71825 72.37885  1.000 53.80263  ? 167 GLU B O   1 
ATOM   3792 C  CB  . GLU B  1 141 ? 0.22666   -48.57396 73.21330  1.000 58.18268  ? 167 GLU B CB  1 
ATOM   3793 C  CG  . GLU B  1 141 ? -0.19008  -49.79604 74.02475  1.000 60.78201  ? 167 GLU B CG  1 
ATOM   3794 C  CD  . GLU B  1 141 ? -1.33636  -49.51156 74.98030  1.000 61.84742  ? 167 GLU B CD  1 
ATOM   3795 O  OE1 . GLU B  1 141 ? -1.77640  -48.34527 75.05803  1.000 61.76651  ? 167 GLU B OE1 1 
ATOM   3796 O  OE2 . GLU B  1 141 ? -1.79894  -50.45656 75.65338  1.000 62.80359  ? 167 GLU B OE2 1 
ATOM   3797 N  N   . ASN B  1 142 ? 0.95504   -45.43754 72.85451  1.000 52.46924  ? 168 ASN B N   1 
ATOM   3798 C  CA  . ASN B  1 142 ? 1.38050   -44.34042 71.99325  1.000 53.15216  ? 168 ASN B CA  1 
ATOM   3799 C  C   . ASN B  1 142 ? 2.32686   -43.38224 72.70707  1.000 52.05199  ? 168 ASN B C   1 
ATOM   3800 O  O   . ASN B  1 142 ? 3.24580   -42.83380 72.08325  1.000 52.24695  ? 168 ASN B O   1 
ATOM   3801 C  CB  . ASN B  1 142 ? 0.15852   -43.57888 71.47328  1.000 53.42047  ? 168 ASN B CB  1 
ATOM   3802 C  CG  . ASN B  1 142 ? -0.77281  -44.45802 70.66006  1.000 53.98143  ? 168 ASN B CG  1 
ATOM   3803 O  OD1 . ASN B  1 142 ? -0.33330  -45.38639 69.98124  1.000 54.82517  ? 168 ASN B OD1 1 
ATOM   3804 N  ND2 . ASN B  1 142 ? -2.06748  -44.16913 70.72529  1.000 52.88626  ? 168 ASN B ND2 1 
ATOM   3805 N  N   . LEU B  1 143 ? 2.11513   -43.16670 74.00782  1.000 50.31192  ? 169 LEU B N   1 
ATOM   3806 C  CA  . LEU B  1 143 ? 3.02677   -42.32169 74.76884  1.000 50.37228  ? 169 LEU B CA  1 
ATOM   3807 C  C   . LEU B  1 143 ? 4.41858   -42.93317 74.84274  1.000 51.13028  ? 169 LEU B C   1 
ATOM   3808 O  O   . LEU B  1 143 ? 5.41597   -42.20485 74.82133  1.000 51.54471  ? 169 LEU B O   1 
ATOM   3809 C  CB  . LEU B  1 143 ? 2.47353   -42.07762 76.17285  1.000 49.04305  ? 169 LEU B CB  1 
ATOM   3810 C  CG  . LEU B  1 143 ? 2.45488   -40.61508 76.62154  1.000 47.11778  ? 169 LEU B CG  1 
ATOM   3811 C  CD1 . LEU B  1 143 ? 1.80015   -39.74497 75.56150  1.000 45.63261  ? 169 LEU B CD1 1 
ATOM   3812 C  CD2 . LEU B  1 143 ? 1.74558   -40.46237 77.95627  1.000 45.79220  ? 169 LEU B CD2 1 
ATOM   3813 N  N   . GLU B  1 144 ? 4.50939   -44.26400 74.91659  1.000 51.15053  ? 170 GLU B N   1 
ATOM   3814 C  CA  . GLU B  1 144 ? 5.81661   -44.91250 74.91899  1.000 51.21440  ? 170 GLU B CA  1 
ATOM   3815 C  C   . GLU B  1 144 ? 6.55941   -44.68216 73.60949  1.000 50.12585  ? 170 GLU B C   1 
ATOM   3816 O  O   . GLU B  1 144 ? 7.79141   -44.57930 73.60496  1.000 49.07142  ? 170 GLU B O   1 
ATOM   3817 C  CB  . GLU B  1 144 ? 5.66010   -46.40956 75.18526  1.000 53.12524  ? 170 GLU B CB  1 
ATOM   3818 C  CG  . GLU B  1 144 ? 5.35499   -46.75281 76.63443  1.000 55.93411  ? 170 GLU B CG  1 
ATOM   3819 C  CD  . GLU B  1 144 ? 4.66808   -48.09631 76.78338  1.000 58.49990  ? 170 GLU B CD  1 
ATOM   3820 O  OE1 . GLU B  1 144 ? 4.49982   -48.79649 75.76295  1.000 59.69690  ? 170 GLU B OE1 1 
ATOM   3821 O  OE2 . GLU B  1 144 ? 4.29083   -48.44971 77.92042  1.000 59.20265  ? 170 GLU B OE2 1 
ATOM   3822 N  N   . LYS B  1 145 ? 5.83382   -44.59553 72.49294  1.000 49.84870  ? 171 LYS B N   1 
ATOM   3823 C  CA  . LYS B  1 145 ? 6.47482   -44.33945 71.20872  1.000 51.00897  ? 171 LYS B CA  1 
ATOM   3824 C  C   . LYS B  1 145 ? 6.82266   -42.86846 71.02542  1.000 51.31303  ? 171 LYS B C   1 
ATOM   3825 O  O   . LYS B  1 145 ? 7.82843   -42.55095 70.38069  1.000 54.09343  ? 171 LYS B O   1 
ATOM   3826 C  CB  . LYS B  1 145 ? 5.57369   -44.80648 70.06393  1.000 49.40188  ? 171 LYS B CB  1 
ATOM   3827 C  CG  . LYS B  1 145 ? 5.55679   -46.31153 69.85918  1.000 50.87920  ? 171 LYS B CG  1 
ATOM   3828 C  CD  . LYS B  1 145 ? 4.25525   -46.76471 69.21999  1.000 52.73643  ? 171 LYS B CD  1 
ATOM   3829 C  CE  . LYS B  1 145 ? 4.11473   -48.27689 69.26804  1.000 55.48693  ? 171 LYS B CE  1 
ATOM   3830 N  NZ  . LYS B  1 145 ? 2.68695   -48.69874 69.26365  1.000 55.91418  ? 171 LYS B NZ  1 
ATOM   3831 N  N   . LEU B  1 146 ? 6.01453   -41.96481 71.57436  1.000 49.59485  ? 172 LEU B N   1 
ATOM   3832 C  CA  . LEU B  1 146 ? 6.25146   -40.53482 71.41501  1.000 49.04887  ? 172 LEU B CA  1 
ATOM   3833 C  C   . LEU B  1 146 ? 7.10893   -39.93122 72.52365  1.000 49.41258  ? 172 LEU B C   1 
ATOM   3834 O  O   . LEU B  1 146 ? 7.38594   -38.72766 72.48058  1.000 48.63358  ? 172 LEU B O   1 
ATOM   3835 C  CB  . LEU B  1 146 ? 4.91733   -39.78703 71.33421  1.000 47.96554  ? 172 LEU B CB  1 
ATOM   3836 C  CG  . LEU B  1 146 ? 4.10488   -40.04607 70.06422  1.000 48.53571  ? 172 LEU B CG  1 
ATOM   3837 C  CD1 . LEU B  1 146 ? 2.61353   -40.07045 70.36637  1.000 47.58763  ? 172 LEU B CD1 1 
ATOM   3838 C  CD2 . LEU B  1 146 ? 4.43082   -39.00999 68.99739  1.000 48.55231  ? 172 LEU B CD2 1 
ATOM   3839 N  N   . LYS B  1 147 ? 7.52327   -40.72831 73.51380  1.000 50.02211  ? 173 LYS B N   1 
ATOM   3840 C  CA  . LYS B  1 147 ? 8.36455   -40.21272 74.59192  1.000 50.71642  ? 173 LYS B CA  1 
ATOM   3841 C  C   . LYS B  1 147 ? 9.64041   -39.56457 74.06550  1.000 52.17317  ? 173 LYS B C   1 
ATOM   3842 O  O   . LYS B  1 147 ? 10.12526  -38.57977 74.63526  1.000 52.13953  ? 173 LYS B O   1 
ATOM   3843 C  CB  . LYS B  1 147 ? 8.70789   -41.34339 75.56472  1.000 51.61066  ? 173 LYS B CB  1 
ATOM   3844 C  CG  . LYS B  1 147 ? 9.58035   -40.92031 76.73640  1.000 52.31655  ? 173 LYS B CG  1 
ATOM   3845 C  CD  . LYS B  1 147 ? 10.05119  -42.12164 77.54293  1.000 54.12237  ? 173 LYS B CD  1 
ATOM   3846 C  CE  . LYS B  1 147 ? 10.96571  -43.01997 76.72349  1.000 56.36608  ? 173 LYS B CE  1 
ATOM   3847 N  NZ  . LYS B  1 147 ? 11.54385  -44.12210 77.54336  1.000 56.98782  ? 173 LYS B NZ  1 
ATOM   3848 N  N   . SER B  1 148 ? 10.19811  -40.10171 72.97729  1.000 53.66054  ? 174 SER B N   1 
ATOM   3849 C  CA  . SER B  1 148 ? 11.47392  -39.59956 72.47378  1.000 55.80370  ? 174 SER B CA  1 
ATOM   3850 C  C   . SER B  1 148 ? 11.36545  -38.15199 72.00771  1.000 55.19457  ? 174 SER B C   1 
ATOM   3851 O  O   . SER B  1 148 ? 12.23757  -37.32861 72.31049  1.000 55.27413  ? 174 SER B O   1 
ATOM   3852 C  CB  . SER B  1 148 ? 11.97628  -40.48772 71.33613  1.000 57.68933  ? 174 SER B CB  1 
ATOM   3853 O  OG  . SER B  1 148 ? 12.31277  -41.78086 71.80643  1.000 59.77628  ? 174 SER B OG  1 
ATOM   3854 N  N   . CYS B  1 149 ? 10.30339  -37.81800 71.27539  1.000 55.31697  ? 175 CYS B N   1 
ATOM   3855 C  CA  A CYS B  1 149 ? 10.14030  -36.46662 70.75124  0.417 55.67254  ? 175 CYS B CA  1 
ATOM   3856 C  CA  B CYS B  1 149 ? 10.13565  -36.47078 70.74877  0.583 55.65871  ? 175 CYS B CA  1 
ATOM   3857 C  C   . CYS B  1 149 ? 9.54707   -35.49896 71.76596  1.000 55.08725  ? 175 CYS B C   1 
ATOM   3858 O  O   . CYS B  1 149 ? 9.35945   -34.32356 71.43515  1.000 54.45973  ? 175 CYS B O   1 
ATOM   3859 C  CB  A CYS B  1 149 ? 9.27445   -36.48014 69.48505  0.417 55.79999  ? 175 CYS B CB  1 
ATOM   3860 C  CB  B CYS B  1 149 ? 9.26059   -36.51171 69.49433  0.583 55.76649  ? 175 CYS B CB  1 
ATOM   3861 S  SG  A CYS B  1 149 ? 7.63896   -37.24143 69.65124  0.417 55.40575  ? 175 CYS B SG  1 
ATOM   3862 S  SG  B CYS B  1 149 ? 9.97504   -37.42786 68.10862  0.583 57.04959  ? 175 CYS B SG  1 
ATOM   3863 N  N   . GLY B  1 150 ? 9.24868   -35.95281 72.98225  1.000 55.25848  ? 176 GLY B N   1 
ATOM   3864 C  CA  . GLY B  1 150 ? 8.77430   -35.05963 74.02324  1.000 55.00809  ? 176 GLY B CA  1 
ATOM   3865 C  C   . GLY B  1 150 ? 7.27122   -34.99616 74.20546  1.000 54.12930  ? 176 GLY B C   1 
ATOM   3866 O  O   . GLY B  1 150 ? 6.54108   -34.59266 73.29600  1.000 53.45659  ? 176 GLY B O   1 
ATOM   3867 N  N   . VAL B  1 151 ? 6.80039   -35.37703 75.39054  1.000 52.15155  ? 177 VAL B N   1 
ATOM   3868 C  CA  . VAL B  1 151 ? 5.38776   -35.32213 75.74803  1.000 51.68456  ? 177 VAL B CA  1 
ATOM   3869 C  C   . VAL B  1 151 ? 5.23664   -34.37766 76.93236  1.000 50.50132  ? 177 VAL B C   1 
ATOM   3870 O  O   . VAL B  1 151 ? 5.98737   -34.47718 77.90991  1.000 51.08788  ? 177 VAL B O   1 
ATOM   3871 C  CB  . VAL B  1 151 ? 4.83293   -36.71926 76.08313  1.000 52.37023  ? 177 VAL B CB  1 
ATOM   3872 C  CG1 . VAL B  1 151 ? 3.46325   -36.61143 76.73777  1.000 51.21545  ? 177 VAL B CG1 1 
ATOM   3873 C  CG2 . VAL B  1 151 ? 4.76618   -37.57727 74.82867  1.000 52.37313  ? 177 VAL B CG2 1 
ATOM   3874 N  N   . SER B  1 152 ? 4.27176   -33.46446 76.84441  1.000 49.38347  ? 178 SER B N   1 
ATOM   3875 C  CA  . SER B  1 152 ? 4.04661   -32.46136 77.87358  1.000 50.53923  ? 178 SER B CA  1 
ATOM   3876 C  C   . SER B  1 152 ? 2.60977   -32.51756 78.37603  1.000 47.09995  ? 178 SER B C   1 
ATOM   3877 O  O   . SER B  1 152 ? 1.67833   -32.81435 77.62225  1.000 44.95283  ? 178 SER B O   1 
ATOM   3878 C  CB  . SER B  1 152 ? 4.35452   -31.05335 77.35086  1.000 54.09576  ? 178 SER B CB  1 
ATOM   3879 O  OG  . SER B  1 152 ? 4.41107   -30.11513 78.41028  1.000 56.58642  ? 178 SER B OG  1 
ATOM   3880 N  N   . PHE B  1 153 ? 2.44402   -32.22490 79.66411  1.000 46.06817  ? 179 PHE B N   1 
ATOM   3881 C  CA  . PHE B  1 153 ? 1.14046   -32.15300 80.30552  1.000 44.85832  ? 179 PHE B CA  1 
ATOM   3882 C  C   . PHE B  1 153 ? 1.00638   -30.81136 81.01079  1.000 43.31416  ? 179 PHE B C   1 
ATOM   3883 O  O   . PHE B  1 153 ? 2.00084   -30.21041 81.42602  1.000 43.99393  ? 179 PHE B O   1 
ATOM   3884 C  CB  . PHE B  1 153 ? 0.94331   -33.28871 81.32280  1.000 46.62084  ? 179 PHE B CB  1 
ATOM   3885 C  CG  . PHE B  1 153 ? 0.25421   -34.50248 80.76473  1.000 45.77462  ? 179 PHE B CG  1 
ATOM   3886 C  CD1 . PHE B  1 153 ? 0.57636   -34.98788 79.50941  1.000 45.14051  ? 179 PHE B CD1 1 
ATOM   3887 C  CD2 . PHE B  1 153 ? -0.71041  -35.16580 81.50631  1.000 45.47096  ? 179 PHE B CD2 1 
ATOM   3888 C  CE1 . PHE B  1 153 ? -0.05495  -36.10669 79.00041  1.000 44.58533  ? 179 PHE B CE1 1 
ATOM   3889 C  CE2 . PHE B  1 153 ? -1.34515  -36.28538 81.00285  1.000 44.64911  ? 179 PHE B CE2 1 
ATOM   3890 C  CZ  . PHE B  1 153 ? -1.01671  -36.75631 79.74807  1.000 44.14389  ? 179 PHE B CZ  1 
ATOM   3891 N  N   . LEU B  1 154 ? -0.23187  -30.34476 81.14358  1.000 42.02010  ? 180 LEU B N   1 
ATOM   3892 C  CA  . LEU B  1 154 ? -0.48310  -29.11436 81.87882  1.000 41.14515  ? 180 LEU B CA  1 
ATOM   3893 C  C   . LEU B  1 154 ? -0.31494  -29.34223 83.37648  1.000 42.93694  ? 180 LEU B C   1 
ATOM   3894 O  O   . LEU B  1 154 ? -0.56539  -30.43354 83.89465  1.000 44.32015  ? 180 LEU B O   1 
ATOM   3895 C  CB  . LEU B  1 154 ? -1.89251  -28.59227 81.59703  1.000 39.84003  ? 180 LEU B CB  1 
ATOM   3896 C  CG  . LEU B  1 154 ? -2.22046  -28.11131 80.18392  1.000 38.72469  ? 180 LEU B CG  1 
ATOM   3897 C  CD1 . LEU B  1 154 ? -3.72169  -27.92959 80.01799  1.000 36.17315  ? 180 LEU B CD1 1 
ATOM   3898 C  CD2 . LEU B  1 154 ? -1.48374  -26.81986 79.86827  1.000 39.23535  ? 180 LEU B CD2 1 
ATOM   3899 N  N   . ASP B  1 155 ? 0.11518   -28.29518 84.07417  1.000 43.52450  ? 181 ASP B N   1 
ATOM   3900 C  CA  . ASP B  1 155 ? 0.16119   -28.31396 85.53616  1.000 44.21563  ? 181 ASP B CA  1 
ATOM   3901 C  C   . ASP B  1 155 ? -1.16447  -27.83969 86.12610  1.000 42.23633  ? 181 ASP B C   1 
ATOM   3902 O  O   . ASP B  1 155 ? -1.21441  -27.00383 87.02702  1.000 39.12209  ? 181 ASP B O   1 
ATOM   3903 C  CB  . ASP B  1 155 ? 1.32545   -27.46768 86.03867  1.000 46.01542  ? 181 ASP B CB  1 
ATOM   3904 C  CG  . ASP B  1 155 ? 1.65751   -27.73886 87.49604  1.000 48.93365  ? 181 ASP B CG  1 
ATOM   3905 O  OD1 . ASP B  1 155 ? 1.11006   -28.70914 88.06084  1.000 49.55821  ? 181 ASP B OD1 1 
ATOM   3906 O  OD2 . ASP B  1 155 ? 2.46324   -26.98219 88.07758  1.000 50.22543  ? 181 ASP B OD2 1 
ATOM   3907 N  N   . ALA B  1 156 ? -2.25892  -28.37870 85.59520  1.000 41.28826  ? 182 ALA B N   1 
ATOM   3908 C  CA  . ALA B  1 156 ? -3.61167  -28.04260 86.03905  1.000 40.98675  ? 182 ALA B CA  1 
ATOM   3909 C  C   . ALA B  1 156 ? -4.31708  -29.31760 86.47516  1.000 40.06612  ? 182 ALA B C   1 
ATOM   3910 O  O   . ALA B  1 156 ? -4.86866  -30.04482 85.62895  1.000 37.32273  ? 182 ALA B O   1 
ATOM   3911 C  CB  . ALA B  1 156 ? -4.39397  -27.34715 84.92622  1.000 37.34033  ? 182 ALA B CB  1 
ATOM   3912 N  N   . PRO B  1 157 ? -4.32773  -29.63402 87.77429  1.000 40.37900  ? 183 PRO B N   1 
ATOM   3913 C  CA  . PRO B  1 157 ? -4.93167  -30.90685 88.20783  1.000 40.95860  ? 183 PRO B CA  1 
ATOM   3914 C  C   . PRO B  1 157 ? -6.40954  -31.02561 87.88165  1.000 41.72329  ? 183 PRO B C   1 
ATOM   3915 O  O   . PRO B  1 157 ? -6.86038  -32.10453 87.48143  1.000 40.52678  ? 183 PRO B O   1 
ATOM   3916 C  CB  . PRO B  1 157 ? -4.68352  -30.91387 89.72419  1.000 41.15875  ? 183 PRO B CB  1 
ATOM   3917 C  CG  . PRO B  1 157 ? -4.42682  -29.48740 90.08606  1.000 42.06827  ? 183 PRO B CG  1 
ATOM   3918 C  CD  . PRO B  1 157 ? -3.75070  -28.87966 88.89892  1.000 41.52691  ? 183 PRO B CD  1 
ATOM   3919 N  N   . GLU B  1 158 ? -7.17801  -29.94578 88.03610  1.000 43.16148  ? 184 GLU B N   1 
ATOM   3920 C  CA  . GLU B  1 158 ? -8.61398  -30.01218 87.77853  1.000 45.01690  ? 184 GLU B CA  1 
ATOM   3921 C  C   . GLU B  1 158 ? -8.89908  -30.40483 86.33285  1.000 44.50644  ? 184 GLU B C   1 
ATOM   3922 O  O   . GLU B  1 158 ? -9.64177  -31.35951 86.06886  1.000 43.54785  ? 184 GLU B O   1 
ATOM   3923 C  CB  . GLU B  1 158 ? -9.26431  -28.66798 88.11067  1.000 46.88885  ? 184 GLU B CB  1 
ATOM   3924 C  CG  . GLU B  1 158 ? -9.31349  -28.34243 89.59710  1.000 49.20526  ? 184 GLU B CG  1 
ATOM   3925 C  CD  . GLU B  1 158 ? -8.04556  -27.67732 90.10145  1.000 52.67997  ? 184 GLU B CD  1 
ATOM   3926 O  OE1 . GLU B  1 158 ? -8.05300  -27.17646 91.24578  1.000 54.48721  ? 184 GLU B OE1 1 
ATOM   3927 O  OE2 . GLU B  1 158 ? -7.04214  -27.65459 89.35763  1.000 53.92158  ? 184 GLU B OE2 1 
ATOM   3928 N  N   . GLU B  1 159 ? -8.30171  -29.68343 85.38114  1.000 44.58180  ? 185 GLU B N   1 
ATOM   3929 C  CA  . GLU B  1 159 ? -8.58546  -29.92775 83.97055  1.000 43.79771  ? 185 GLU B CA  1 
ATOM   3930 C  C   . GLU B  1 159 ? -8.06745  -31.28916 83.52319  1.000 41.78929  ? 185 GLU B C   1 
ATOM   3931 O  O   . GLU B  1 159 ? -8.76695  -32.02125 82.81231  1.000 41.47798  ? 185 GLU B O   1 
ATOM   3932 C  CB  . GLU B  1 159 ? -7.97861  -28.81363 83.11912  1.000 45.38045  ? 185 GLU B CB  1 
ATOM   3933 C  CG  . GLU B  1 159 ? -8.16222  -27.42450 83.70824  1.000 46.14301  ? 185 GLU B CG  1 
ATOM   3934 C  CD  . GLU B  1 159 ? -8.10797  -26.33321 82.65910  1.000 46.42088  ? 185 GLU B CD  1 
ATOM   3935 O  OE1 . GLU B  1 159 ? -8.09405  -26.66475 81.45519  1.000 46.05728  ? 185 GLU B OE1 1 
ATOM   3936 O  OE2 . GLU B  1 159 ? -8.08279  -25.14347 83.03860  1.000 46.96588  ? 185 GLU B OE2 1 
ATOM   3937 N  N   . VAL B  1 160 ? -6.84722  -31.64772 83.92979  1.000 40.88028  ? 186 VAL B N   1 
ATOM   3938 C  CA  . VAL B  1 160 ? -6.28533  -32.93714 83.53571  1.000 40.47088  ? 186 VAL B CA  1 
ATOM   3939 C  C   . VAL B  1 160 ? -7.11132  -34.07925 84.11365  1.000 39.85154  ? 186 VAL B C   1 
ATOM   3940 O  O   . VAL B  1 160 ? -7.39813  -35.06581 83.42528  1.000 38.13148  ? 186 VAL B O   1 
ATOM   3941 C  CB  . VAL B  1 160 ? -4.80814  -33.03412 83.96075  1.000 40.87616  ? 186 VAL B CB  1 
ATOM   3942 C  CG1 . VAL B  1 160 ? -4.27376  -34.43369 83.69861  1.000 36.82343  ? 186 VAL B CG1 1 
ATOM   3943 C  CG2 . VAL B  1 160 ? -3.97495  -31.99999 83.22165  1.000 42.07204  ? 186 VAL B CG2 1 
ATOM   3944 N  N   . PHE B  1 161 ? -7.51279  -33.96340 85.38254  1.000 40.42818  ? 187 PHE B N   1 
ATOM   3945 C  CA  . PHE B  1 161 ? -8.30623  -35.01610 86.00736  1.000 38.96590  ? 187 PHE B CA  1 
ATOM   3946 C  C   . PHE B  1 161 ? -9.67530  -35.14164 85.35121  1.000 39.94503  ? 187 PHE B C   1 
ATOM   3947 O  O   . PHE B  1 161 ? -10.16476 -36.25750 85.13872  1.000 41.03694  ? 187 PHE B O   1 
ATOM   3948 C  CB  . PHE B  1 161 ? -8.45031  -34.74727 87.50547  1.000 38.82691  ? 187 PHE B CB  1 
ATOM   3949 C  CG  . PHE B  1 161 ? -7.42758  -35.45419 88.35142  1.000 40.80721  ? 187 PHE B CG  1 
ATOM   3950 C  CD1 . PHE B  1 161 ? -7.43488  -36.83484 88.46152  1.000 42.17451  ? 187 PHE B CD1 1 
ATOM   3951 C  CD2 . PHE B  1 161 ? -6.46274  -34.73789 89.04031  1.000 41.94694  ? 187 PHE B CD2 1 
ATOM   3952 C  CE1 . PHE B  1 161 ? -6.49660  -37.48787 89.24013  1.000 44.24630  ? 187 PHE B CE1 1 
ATOM   3953 C  CE2 . PHE B  1 161 ? -5.52214  -35.38420 89.82075  1.000 45.10751  ? 187 PHE B CE2 1 
ATOM   3954 C  CZ  . PHE B  1 161 ? -5.53910  -36.76083 89.92101  1.000 45.38220  ? 187 PHE B CZ  1 
ATOM   3955 N  N   . ALA B  1 162 ? -10.31102 -34.01197 85.02331  1.000 38.28308  ? 188 ALA B N   1 
ATOM   3956 C  CA  . ALA B  1 162 ? -11.59705 -34.07119 84.33639  1.000 38.24615  ? 188 ALA B CA  1 
ATOM   3957 C  C   . ALA B  1 162 ? -11.45198 -34.70432 82.95851  1.000 38.06166  ? 188 ALA B C   1 
ATOM   3958 O  O   . ALA B  1 162 ? -12.31279 -35.48282 82.52932  1.000 36.48856  ? 188 ALA B O   1 
ATOM   3959 C  CB  . ALA B  1 162 ? -12.20116 -32.67133 84.22823  1.000 37.81273  ? 188 ALA B CB  1 
ATOM   3960 N  N   . THR B  1 163 ? -10.35905 -34.39281 82.25647  1.000 36.60520  ? 189 THR B N   1 
ATOM   3961 C  CA  . THR B  1 163 ? -10.11049 -35.00935 80.95773  1.000 36.59104  ? 189 THR B CA  1 
ATOM   3962 C  C   . THR B  1 163 ? -9.91526  -36.51524 81.08798  1.000 36.48030  ? 189 THR B C   1 
ATOM   3963 O  O   . THR B  1 163 ? -10.45872 -37.28889 80.29211  1.000 36.18017  ? 189 THR B O   1 
ATOM   3964 C  CB  . THR B  1 163 ? -8.89105  -34.36538 80.29970  1.000 35.38788  ? 189 THR B CB  1 
ATOM   3965 O  OG1 . THR B  1 163 ? -9.11526  -32.95741 80.15431  1.000 35.21484  ? 189 THR B OG1 1 
ATOM   3966 C  CG2 . THR B  1 163 ? -8.63537  -34.98032 78.93406  1.000 47.53969  ? 189 THR B CG2 1 
ATOM   3967 N  N   . VAL B  1 164 ? -9.14483  -36.94976 82.08835  1.000 36.04120  ? 190 VAL B N   1 
ATOM   3968 C  CA  . VAL B  1 164 ? -8.94284  -38.38104 82.30834  1.000 36.31374  ? 190 VAL B CA  1 
ATOM   3969 C  C   . VAL B  1 164 ? -10.26674 -39.06800 82.61863  1.000 38.06657  ? 190 VAL B C   1 
ATOM   3970 O  O   . VAL B  1 164 ? -10.56571 -40.14435 82.08374  1.000 37.32830  ? 190 VAL B O   1 
ATOM   3971 C  CB  . VAL B  1 164 ? -7.90787  -38.61583 83.42597  1.000 39.21319  ? 190 VAL B CB  1 
ATOM   3972 C  CG1 . VAL B  1 164 ? -7.76350  -40.09976 83.70768  1.000 36.96947  ? 190 VAL B CG1 1 
ATOM   3973 C  CG2 . VAL B  1 164 ? -6.56065  -38.03106 83.03709  1.000 38.88910  ? 190 VAL B CG2 1 
ATOM   3974 N  N   . LEU B  1 165 ? -11.08204 -38.45626 83.48170  1.000 38.92942  ? 191 LEU B N   1 
ATOM   3975 C  CA  . LEU B  1 165 ? -12.35642 -39.06279 83.85359  1.000 39.82080  ? 191 LEU B CA  1 
ATOM   3976 C  C   . LEU B  1 165 ? -13.29696 -39.15421 82.65758  1.000 40.77746  ? 191 LEU B C   1 
ATOM   3977 O  O   . LEU B  1 165 ? -14.00410 -40.15513 82.48979  1.000 42.77975  ? 191 LEU B O   1 
ATOM   3978 C  CB  . LEU B  1 165 ? -13.00224 -38.26908 84.98883  1.000 37.22088  ? 191 LEU B CB  1 
ATOM   3979 C  CG  . LEU B  1 165 ? -12.32864 -38.39733 86.35778  1.000 37.61488  ? 191 LEU B CG  1 
ATOM   3980 C  CD1 . LEU B  1 165 ? -12.94517 -37.42821 87.35248  1.000 37.95470  ? 191 LEU B CD1 1 
ATOM   3981 C  CD2 . LEU B  1 165 ? -12.41510 -39.82593 86.87313  1.000 38.03714  ? 191 LEU B CD2 1 
ATOM   3982 N  N   . ASN B  1 166 ? -13.31984 -38.11974 81.81352  1.000 40.13902  ? 192 ASN B N   1 
ATOM   3983 C  CA  . ASN B  1 166 ? -14.13593 -38.17539 80.60489  1.000 41.33123  ? 192 ASN B CA  1 
ATOM   3984 C  C   . ASN B  1 166 ? -13.61623 -39.23211 79.63777  1.000 41.77604  ? 192 ASN B C   1 
ATOM   3985 O  O   . ASN B  1 166 ? -14.40315 -39.90101 78.95809  1.000 43.44863  ? 192 ASN B O   1 
ATOM   3986 C  CB  . ASN B  1 166 ? -14.17284 -36.80310 79.93281  1.000 39.84215  ? 192 ASN B CB  1 
ATOM   3987 C  CG  . ASN B  1 166 ? -15.03764 -36.78764 78.68708  1.000 41.81617  ? 192 ASN B CG  1 
ATOM   3988 O  OD1 . ASN B  1 166 ? -16.25113 -36.98145 78.75743  1.000 43.37261  ? 192 ASN B OD1 1 
ATOM   3989 N  ND2 . ASN B  1 166 ? -14.41519 -36.55579 77.53707  1.000 40.77584  ? 192 ASN B ND2 1 
ATOM   3990 N  N   . TYR B  1 167 ? -12.29359 -39.39840 79.56684  1.000 42.06489  ? 193 TYR B N   1 
ATOM   3991 C  CA  . TYR B  1 167 ? -11.71309 -40.40742 78.68756  1.000 42.67594  ? 193 TYR B CA  1 
ATOM   3992 C  C   . TYR B  1 167 ? -12.05415 -41.81488 79.15946  1.000 44.43479  ? 193 TYR B C   1 
ATOM   3993 O  O   . TYR B  1 167 ? -12.26700 -42.71612 78.33982  1.000 44.91340  ? 193 TYR B O   1 
ATOM   3994 C  CB  . TYR B  1 167 ? -10.19869 -40.21367 78.61140  1.000 43.30038  ? 193 TYR B CB  1 
ATOM   3995 C  CG  . TYR B  1 167 ? -9.46300  -41.28559 77.83980  1.000 44.12130  ? 193 TYR B CG  1 
ATOM   3996 C  CD1 . TYR B  1 167 ? -9.48854  -41.31051 76.45213  1.000 43.85940  ? 193 TYR B CD1 1 
ATOM   3997 C  CD2 . TYR B  1 167 ? -8.73093  -42.26459 78.49931  1.000 45.51865  ? 193 TYR B CD2 1 
ATOM   3998 C  CE1 . TYR B  1 167 ? -8.81252  -42.28414 75.74256  1.000 44.29206  ? 193 TYR B CE1 1 
ATOM   3999 C  CE2 . TYR B  1 167 ? -8.05178  -43.24302 77.79816  1.000 46.42577  ? 193 TYR B CE2 1 
ATOM   4000 C  CZ  . TYR B  1 167 ? -8.09611  -43.24785 76.42017  1.000 47.04302  ? 193 TYR B CZ  1 
ATOM   4001 O  OH  . TYR B  1 167 ? -7.42138  -44.21955 75.71749  1.000 49.44212  ? 193 TYR B OH  1 
ATOM   4002 N  N   . LEU B  1 168 ? -12.11342 -42.02308 80.47324  1.000 43.55445  ? 194 LEU B N   1 
ATOM   4003 C  CA  . LEU B  1 168 ? -12.44752 -43.32842 81.02876  1.000 45.38072  ? 194 LEU B CA  1 
ATOM   4004 C  C   . LEU B  1 168 ? -13.94887 -43.59484 81.06637  1.000 46.44776  ? 194 LEU B C   1 
ATOM   4005 O  O   . LEU B  1 168 ? -14.37050 -44.58972 81.66628  1.000 48.00466  ? 194 LEU B O   1 
ATOM   4006 C  CB  . LEU B  1 168 ? -11.85982 -43.46876 82.43548  1.000 48.10372  ? 194 LEU B CB  1 
ATOM   4007 C  CG  . LEU B  1 168 ? -10.34193 -43.64708 82.50523  1.000 49.60360  ? 194 LEU B CG  1 
ATOM   4008 C  CD1 . LEU B  1 168 ? -9.83040  -43.38281 83.91375  1.000 50.22615  ? 194 LEU B CD1 1 
ATOM   4009 C  CD2 . LEU B  1 168 ? -9.94327  -45.03839 82.03545  1.000 50.66576  ? 194 LEU B CD2 1 
ATOM   4010 N  N   . GLY B  1 169 ? -14.75914 -42.73929 80.44710  1.000 46.00363  ? 195 GLY B N   1 
ATOM   4011 C  CA  . GLY B  1 169 ? -16.19126 -42.94814 80.40338  1.000 46.77543  ? 195 GLY B CA  1 
ATOM   4012 C  C   . GLY B  1 169 ? -16.93341 -42.62933 81.68015  1.000 49.05125  ? 195 GLY B C   1 
ATOM   4013 O  O   . GLY B  1 169 ? -18.12289 -42.95102 81.78120  1.000 50.31836  ? 195 GLY B O   1 
ATOM   4014 N  N   . LYS B  1 170 ? -16.27768 -42.01048 82.65677  1.000 49.56789  ? 196 LYS B N   1 
ATOM   4015 C  CA  . LYS B  1 170 ? -16.90769 -41.65137 83.91519  1.000 50.92235  ? 196 LYS B CA  1 
ATOM   4016 C  C   . LYS B  1 170 ? -17.37264 -40.19704 83.86776  1.000 49.37803  ? 196 LYS B C   1 
ATOM   4017 O  O   . LYS B  1 170 ? -17.26049 -39.51094 82.84892  1.000 50.39754  ? 196 LYS B O   1 
ATOM   4018 C  CB  . LYS B  1 170 ? -15.94456 -41.89190 85.07977  1.000 53.20699  ? 196 LYS B CB  1 
ATOM   4019 C  CG  . LYS B  1 170 ? -15.16473 -43.19340 84.97540  1.000 56.15909  ? 196 LYS B CG  1 
ATOM   4020 C  CD  . LYS B  1 170 ? -14.40273 -43.49207 86.25641  1.000 58.94579  ? 196 LYS B CD  1 
ATOM   4021 C  CE  . LYS B  1 170 ? -15.34958 -43.82677 87.39689  1.000 62.19278  ? 196 LYS B CE  1 
ATOM   4022 N  NZ  . LYS B  1 170 ? -16.28597 -44.92933 87.04425  1.000 63.38428  ? 196 LYS B NZ  1 
ATOM   4023 N  N   . ASP B  1 171 ? -17.90475 -39.72739 84.98709  1.000 48.35724  ? 197 ASP B N   1 
ATOM   4024 C  CA  . ASP B  1 171 ? -18.37533 -38.34990 85.08608  1.000 47.68759  ? 197 ASP B CA  1 
ATOM   4025 C  C   . ASP B  1 171 ? -17.18616 -37.39826 85.05475  1.000 44.81144  ? 197 ASP B C   1 
ATOM   4026 O  O   . ASP B  1 171 ? -16.31847 -37.48035 85.93436  1.000 44.24180  ? 197 ASP B O   1 
ATOM   4027 C  CB  . ASP B  1 171 ? -19.18164 -38.16320 86.37047  1.000 51.04095  ? 197 ASP B CB  1 
ATOM   4028 C  CG  . ASP B  1 171 ? -19.79701 -36.77860 86.48567  1.000 52.24591  ? 197 ASP B CG  1 
ATOM   4029 O  OD1 . ASP B  1 171 ? -19.82961 -36.04510 85.47640  1.000 52.17001  ? 197 ASP B OD1 1 
ATOM   4030 O  OD2 . ASP B  1 171 ? -20.25326 -36.42398 87.59320  1.000 54.01267  ? 197 ASP B OD2 1 
ATOM   4031 N  N   . PRO B  1 172 ? -17.09491 -36.49666 84.07175  1.000 42.66543  ? 198 PRO B N   1 
ATOM   4032 C  CA  . PRO B  1 172 ? -15.95370 -35.56559 84.03845  1.000 40.98501  ? 198 PRO B CA  1 
ATOM   4033 C  C   . PRO B  1 172 ? -15.85328 -34.68918 85.27320  1.000 39.68940  ? 198 PRO B C   1 
ATOM   4034 O  O   . PRO B  1 172 ? -14.75208 -34.24272 85.61819  1.000 39.44563  ? 198 PRO B O   1 
ATOM   4035 C  CB  . PRO B  1 172 ? -16.21725 -34.73358 82.77473  1.000 41.34636  ? 198 PRO B CB  1 
ATOM   4036 C  CG  . PRO B  1 172 ? -17.11839 -35.58223 81.93697  1.000 42.18973  ? 198 PRO B CG  1 
ATOM   4037 C  CD  . PRO B  1 172 ? -17.97827 -36.33451 82.90504  1.000 41.27956  ? 198 PRO B CD  1 
ATOM   4038 N  N   . ASN B  1 173 ? -16.97043 -34.42530 85.94807  1.000 39.20554  ? 199 ASN B N   1 
ATOM   4039 C  CA  . ASN B  1 173 ? -16.95055 -33.67967 87.19911  1.000 39.21714  ? 199 ASN B CA  1 
ATOM   4040 C  C   . ASN B  1 173 ? -17.33644 -34.59670 88.35144  1.000 39.99040  ? 199 ASN B C   1 
ATOM   4041 O  O   . ASN B  1 173 ? -18.28524 -34.31398 89.09067  1.000 40.94590  ? 199 ASN B O   1 
ATOM   4042 C  CB  . ASN B  1 173 ? -17.89084 -32.47612 87.12431  1.000 40.35408  ? 199 ASN B CB  1 
ATOM   4043 C  CG  . ASN B  1 173 ? -17.39837 -31.41339 86.16213  1.000 41.03385  ? 199 ASN B CG  1 
ATOM   4044 O  OD1 . ASN B  1 173 ? -16.53137 -30.60707 86.50056  1.000 43.01357  ? 199 ASN B OD1 1 
ATOM   4045 N  ND2 . ASN B  1 173 ? -17.94665 -31.40998 84.95274  1.000 38.06465  ? 199 ASN B ND2 1 
ATOM   4046 N  N   . SER B  1 174 ? -16.60529 -35.69917 88.50187  1.000 39.39350  ? 200 SER B N   1 
ATOM   4047 C  CA  . SER B  1 174 ? -16.92093 -36.68118 89.52963  1.000 40.85161  ? 200 SER B CA  1 
ATOM   4048 C  C   . SER B  1 174 ? -16.82988 -36.06533 90.91963  1.000 42.96765  ? 200 SER B C   1 
ATOM   4049 O  O   . SER B  1 174 ? -15.94334 -35.25566 91.20531  1.000 43.07331  ? 200 SER B O   1 
ATOM   4050 C  CB  . SER B  1 174 ? -15.97277 -37.87620 89.42729  1.000 39.62698  ? 200 SER B CB  1 
ATOM   4051 O  OG  . SER B  1 174 ? -16.27824 -38.85339 90.40690  1.000 40.34050  ? 200 SER B OG  1 
ATOM   4052 N  N   . THR B  1 175 ? -17.76610 -36.45070 91.78473  1.000 41.36104  ? 201 THR B N   1 
ATOM   4053 C  CA  . THR B  1 175 ? -17.76537 -36.03767 93.18066  1.000 42.18752  ? 201 THR B CA  1 
ATOM   4054 C  C   . THR B  1 175 ? -17.33058 -37.16209 94.11089  1.000 43.74258  ? 201 THR B C   1 
ATOM   4055 O  O   . THR B  1 175 ? -17.36944 -36.99417 95.33397  1.000 43.51823  ? 201 THR B O   1 
ATOM   4056 C  CB  . THR B  1 175 ? -19.14877 -35.52106 93.58385  1.000 46.10339  ? 201 THR B CB  1 
ATOM   4057 O  OG1 . THR B  1 175 ? -20.14488 -36.48947 93.23344  1.000 47.58761  ? 201 THR B OG1 1 
ATOM   4058 C  CG2 . THR B  1 175 ? -19.45277 -34.20979 92.87353  1.000 42.60458  ? 201 THR B CG2 1 
ATOM   4059 N  N   . LYS B  1 176 ? -16.92183 -38.30249 93.56074  1.000 44.19712  ? 202 LYS B N   1 
ATOM   4060 C  CA  . LYS B  1 176 ? -16.39031 -39.40587 94.34952  1.000 45.31830  ? 202 LYS B CA  1 
ATOM   4061 C  C   . LYS B  1 176 ? -14.87054 -39.30130 94.38146  1.000 43.16368  ? 202 LYS B C   1 
ATOM   4062 O  O   . LYS B  1 176 ? -14.22329 -39.28991 93.32845  1.000 41.77125  ? 202 LYS B O   1 
ATOM   4063 C  CB  . LYS B  1 176 ? -16.82349 -40.75057 93.76670  1.000 49.06673  ? 202 LYS B CB  1 
ATOM   4064 C  CG  . LYS B  1 176 ? -18.31503 -40.86918 93.49632  1.000 53.14316  ? 202 LYS B CG  1 
ATOM   4065 C  CD  . LYS B  1 176 ? -18.72591 -42.32349 93.32185  1.000 56.92396  ? 202 LYS B CD  1 
ATOM   4066 C  CE  . LYS B  1 176 ? -18.70527 -43.06552 94.64909  1.000 60.51184  ? 202 LYS B CE  1 
ATOM   4067 N  NZ  . LYS B  1 176 ? -18.12715 -44.43164 94.51648  1.000 61.69131  ? 202 LYS B NZ  1 
ATOM   4068 N  N   . ALA B  1 177 ? -14.30408 -39.22300 95.58869  1.000 42.78755  ? 203 ALA B N   1 
ATOM   4069 C  CA  . ALA B  1 177 ? -12.85466 -39.11297 95.72015  1.000 42.47951  ? 203 ALA B CA  1 
ATOM   4070 C  C   . ALA B  1 177 ? -12.14602 -40.35784 95.20283  1.000 53.49648  ? 203 ALA B C   1 
ATOM   4071 O  O   . ALA B  1 177 ? -10.99369 -40.27787 94.75561  1.000 51.97734  ? 203 ALA B O   1 
ATOM   4072 C  CB  . ALA B  1 177 ? -12.47895 -38.85576 97.17976  1.000 48.42711  ? 203 ALA B CB  1 
ATOM   4073 N  N   . ASP B  1 178 ? -12.81569 -41.51242 95.25271  1.000 42.41984  ? 204 ASP B N   1 
ATOM   4074 C  CA  . ASP B  1 178 ? -12.19768 -42.74972 94.79053  1.000 49.62287  ? 204 ASP B CA  1 
ATOM   4075 C  C   . ASP B  1 178 ? -11.98135 -42.74351 93.28319  1.000 41.29891  ? 204 ASP B C   1 
ATOM   4076 O  O   . ASP B  1 178 ? -11.08522 -43.43440 92.78614  1.000 41.00043  ? 204 ASP B O   1 
ATOM   4077 C  CB  . ASP B  1 178 ? -13.05190 -43.94780 95.20300  1.000 50.10903  ? 204 ASP B CB  1 
ATOM   4078 C  CG  . ASP B  1 178 ? -12.94750 -44.25335 96.68453  1.000 50.87448  ? 204 ASP B CG  1 
ATOM   4079 O  OD1 . ASP B  1 178 ? -12.11764 -43.61591 97.36704  1.000 50.18241  ? 204 ASP B OD1 1 
ATOM   4080 O  OD2 . ASP B  1 178 ? -13.69447 -45.13025 97.16687  1.000 51.77362  ? 204 ASP B OD2 1 
ATOM   4081 N  N   . ASP B  1 179 ? -12.78674 -41.97980 92.54111  1.000 40.95581  ? 205 ASP B N   1 
ATOM   4082 C  CA  . ASP B  1 179 ? -12.55327 -41.85143 91.10709  1.000 40.17414  ? 205 ASP B CA  1 
ATOM   4083 C  C   . ASP B  1 179 ? -11.25696 -41.10660 90.82014  1.000 44.27673  ? 205 ASP B C   1 
ATOM   4084 O  O   . ASP B  1 179 ? -10.59501 -41.38028 89.81258  1.000 41.16681  ? 205 ASP B O   1 
ATOM   4085 C  CB  . ASP B  1 179 ? -13.73139 -41.14234 90.44034  1.000 39.99472  ? 205 ASP B CB  1 
ATOM   4086 C  CG  . ASP B  1 179 ? -14.95466 -42.02919 90.32412  1.000 43.91306  ? 205 ASP B CG  1 
ATOM   4087 O  OD1 . ASP B  1 179 ? -14.84111 -43.24065 90.60603  1.000 44.69818  ? 205 ASP B OD1 1 
ATOM   4088 O  OD2 . ASP B  1 179 ? -16.02916 -41.51601 89.94726  1.000 43.94699  ? 205 ASP B OD2 1 
ATOM   4089 N  N   . TYR B  1 180 ? -10.87757 -40.17065 91.69180  1.000 44.52834  ? 206 TYR B N   1 
ATOM   4090 C  CA  . TYR B  1 180 ? -9.62695  -39.44460 91.50885  1.000 39.63499  ? 206 TYR B CA  1 
ATOM   4091 C  C   . TYR B  1 180 ? -8.43734  -40.24145 92.02769  1.000 39.90350  ? 206 TYR B C   1 
ATOM   4092 O  O   . TYR B  1 180 ? -7.39440  -40.30190 91.36763  1.000 39.58841  ? 206 TYR B O   1 
ATOM   4093 C  CB  . TYR B  1 180 ? -9.70197  -38.08552 92.20410  1.000 39.86927  ? 206 TYR B CB  1 
ATOM   4094 C  CG  . TYR B  1 180 ? -10.78712 -37.18534 91.66174  1.000 39.62932  ? 206 TYR B CG  1 
ATOM   4095 C  CD1 . TYR B  1 180 ? -10.53751 -36.32832 90.59807  1.000 39.01607  ? 206 TYR B CD1 1 
ATOM   4096 C  CD2 . TYR B  1 180 ? -12.06228 -37.19446 92.21075  1.000 40.09817  ? 206 TYR B CD2 1 
ATOM   4097 C  CE1 . TYR B  1 180 ? -11.52679 -35.50395 90.09793  1.000 38.82783  ? 206 TYR B CE1 1 
ATOM   4098 C  CE2 . TYR B  1 180 ? -13.05735 -36.37509 91.71752  1.000 39.95720  ? 206 TYR B CE2 1 
ATOM   4099 C  CZ  . TYR B  1 180 ? -12.78496 -35.53166 90.66131  1.000 39.29661  ? 206 TYR B CZ  1 
ATOM   4100 O  OH  . TYR B  1 180 ? -13.77484 -34.71337 90.16744  1.000 39.18548  ? 206 TYR B OH  1 
ATOM   4101 N  N   . THR B  1 181 ? -8.57229  -40.86093 93.20181  1.000 40.56100  ? 207 THR B N   1 
ATOM   4102 C  CA  . THR B  1 181 ? -7.46653  -41.63054 93.75961  1.000 40.89175  ? 207 THR B CA  1 
ATOM   4103 C  C   . THR B  1 181 ? -7.32187  -43.00651 93.12252  1.000 42.05339  ? 207 THR B C   1 
ATOM   4104 O  O   . THR B  1 181 ? -6.27100  -43.63768 93.27929  1.000 40.92643  ? 207 THR B O   1 
ATOM   4105 C  CB  . THR B  1 181 ? -7.63317  -41.79044 95.27336  1.000 42.45454  ? 207 THR B CB  1 
ATOM   4106 O  OG1 . THR B  1 181 ? -8.96244  -42.23640 95.56808  1.000 42.03560  ? 207 THR B OG1 1 
ATOM   4107 C  CG2 . THR B  1 181 ? -7.37424  -40.46931 95.98227  1.000 45.39244  ? 207 THR B CG2 1 
ATOM   4108 N  N   . GLY B  1 182 ? -8.33790  -43.48005 92.40573  1.000 42.85122  ? 208 GLY B N   1 
ATOM   4109 C  CA  . GLY B  1 182 ? -8.32016  -44.81330 91.85372  1.000 43.73062  ? 208 GLY B CA  1 
ATOM   4110 C  C   . GLY B  1 182 ? -7.97299  -44.86054 90.37890  1.000 41.94780  ? 208 GLY B C   1 
ATOM   4111 O  O   . GLY B  1 182 ? -6.81038  -44.72406 89.98484  1.000 40.50784  ? 208 GLY B O   1 
ATOM   4112 N  N   . PRO B  1 183 ? -8.98971  -45.05670 89.53218  1.000 41.09336  ? 209 PRO B N   1 
ATOM   4113 C  CA  . PRO B  1 183 ? -8.71862  -45.29354 88.10080  1.000 41.58137  ? 209 PRO B CA  1 
ATOM   4114 C  C   . PRO B  1 183 ? -7.99757  -44.14981 87.40664  1.000 41.42145  ? 209 PRO B C   1 
ATOM   4115 O  O   . PRO B  1 183 ? -7.07123  -44.39646 86.62124  1.000 43.64568  ? 209 PRO B O   1 
ATOM   4116 C  CB  . PRO B  1 183 ? -10.12146 -45.51943 87.51426  1.000 40.45382  ? 209 PRO B CB  1 
ATOM   4117 C  CG  . PRO B  1 183 ? -11.06904 -44.93275 88.51923  1.000 40.47645  ? 209 PRO B CG  1 
ATOM   4118 C  CD  . PRO B  1 183 ? -10.42420 -45.13904 89.85009  1.000 41.36694  ? 209 PRO B CD  1 
ATOM   4119 N  N   . ALA B  1 184 ? -8.40277  -42.90346 87.66122  1.000 40.35187  ? 210 ALA B N   1 
ATOM   4120 C  CA  . ALA B  1 184 ? -7.72741  -41.76699 87.04176  1.000 41.62484  ? 210 ALA B CA  1 
ATOM   4121 C  C   . ALA B  1 184 ? -6.26520  -41.70818 87.46384  1.000 41.12411  ? 210 ALA B C   1 
ATOM   4122 O  O   . ALA B  1 184 ? -5.36993  -41.51337 86.63111  1.000 42.56327  ? 210 ALA B O   1 
ATOM   4123 C  CB  . ALA B  1 184 ? -8.44826  -40.46775 87.40161  1.000 41.49665  ? 210 ALA B CB  1 
ATOM   4124 N  N   . THR B  1 185 ? -6.00619  -41.88108 88.76187  1.000 41.25641  ? 211 THR B N   1 
ATOM   4125 C  CA  . THR B  1 185 ? -4.63111  -41.91452 89.24516  1.000 42.74798  ? 211 THR B CA  1 
ATOM   4126 C  C   . THR B  1 185 ? -3.86857  -43.08893 88.64488  1.000 43.25439  ? 211 THR B C   1 
ATOM   4127 O  O   . THR B  1 185 ? -2.68752  -42.96097 88.31060  1.000 44.02215  ? 211 THR B O   1 
ATOM   4128 C  CB  . THR B  1 185 ? -4.61429  -41.97721 90.77409  1.000 43.63366  ? 211 THR B CB  1 
ATOM   4129 O  OG1 . THR B  1 185 ? -5.12778  -40.74992 91.30633  1.000 42.73337  ? 211 THR B OG1 1 
ATOM   4130 C  CG2 . THR B  1 185 ? -3.19984  -42.18759 91.29479  1.000 44.42671  ? 211 THR B CG2 1 
ATOM   4131 N  N   . ASP B  1 186 ? -4.53359  -44.23482 88.47674  1.000 43.87688  ? 212 ASP B N   1 
ATOM   4132 C  CA  . ASP B  1 186 ? -3.87488  -45.39608 87.88324  1.000 44.64248  ? 212 ASP B CA  1 
ATOM   4133 C  C   . ASP B  1 186 ? -3.42524  -45.10458 86.45550  1.000 42.65419  ? 212 ASP B C   1 
ATOM   4134 O  O   . ASP B  1 186 ? -2.28109  -45.39139 86.07831  1.000 41.75893  ? 212 ASP B O   1 
ATOM   4135 C  CB  . ASP B  1 186 ? -4.81249  -46.60397 87.91521  1.000 46.93566  ? 212 ASP B CB  1 
ATOM   4136 C  CG  . ASP B  1 186 ? -5.04127  -47.12892 89.31910  1.000 50.29325  ? 212 ASP B CG  1 
ATOM   4137 O  OD1 . ASP B  1 186 ? -4.31115  -46.70707 90.24005  1.000 50.71487  ? 212 ASP B OD1 1 
ATOM   4138 O  OD2 . ASP B  1 186 ? -5.95356  -47.96274 89.50182  1.000 51.92183  ? 212 ASP B OD2 1 
ATOM   4139 N  N   . LEU B  1 187 ? -4.31590  -44.52917 85.64404  1.000 41.27544  ? 213 LEU B N   1 
ATOM   4140 C  CA  . LEU B  1 187 ? -3.94974  -44.21437 84.26608  1.000 42.21154  ? 213 LEU B CA  1 
ATOM   4141 C  C   . LEU B  1 187 ? -2.86489  -43.14461 84.21165  1.000 42.55938  ? 213 LEU B C   1 
ATOM   4142 O  O   . LEU B  1 187 ? -1.94054  -43.22976 83.39165  1.000 44.36054  ? 213 LEU B O   1 
ATOM   4143 C  CB  . LEU B  1 187 ? -5.18145  -43.77144 83.47673  1.000 40.32422  ? 213 LEU B CB  1 
ATOM   4144 C  CG  . LEU B  1 187 ? -4.92447  -43.41940 82.00888  1.000 40.15181  ? 213 LEU B CG  1 
ATOM   4145 C  CD1 . LEU B  1 187 ? -4.21364  -44.56266 81.29712  1.000 39.19068  ? 213 LEU B CD1 1 
ATOM   4146 C  CD2 . LEU B  1 187 ? -6.22222  -43.06630 81.29910  1.000 39.47051  ? 213 LEU B CD2 1 
ATOM   4147 N  N   . LEU B  1 188 ? -2.95285  -42.13200 85.07844  1.000 40.94237  ? 214 LEU B N   1 
ATOM   4148 C  CA  . LEU B  1 188 ? -1.92602  -41.09538 85.08774  1.000 41.00673  ? 214 LEU B CA  1 
ATOM   4149 C  C   . LEU B  1 188 ? -0.57345  -41.66311 85.50244  1.000 40.70833  ? 214 LEU B C   1 
ATOM   4150 O  O   . LEU B  1 188 ? 0.46691   -41.24369 84.98508  1.000 41.33269  ? 214 LEU B O   1 
ATOM   4151 C  CB  . LEU B  1 188 ? -2.34343  -39.94861 86.00729  1.000 42.39114  ? 214 LEU B CB  1 
ATOM   4152 C  CG  . LEU B  1 188 ? -3.36186  -38.98056 85.39906  1.000 42.52957  ? 214 LEU B CG  1 
ATOM   4153 C  CD1 . LEU B  1 188 ? -3.93961  -38.05749 86.46115  1.000 42.64181  ? 214 LEU B CD1 1 
ATOM   4154 C  CD2 . LEU B  1 188 ? -2.73457  -38.17985 84.26742  1.000 37.63711  ? 214 LEU B CD2 1 
ATOM   4155 N  N   . LEU B  1 189 ? -0.56726  -42.63315 86.42032  1.000 40.44900  ? 215 LEU B N   1 
ATOM   4156 C  CA  . LEU B  1 189 ? 0.68209   -43.28634 86.79731  1.000 42.06436  ? 215 LEU B CA  1 
ATOM   4157 C  C   . LEU B  1 189 ? 1.22540   -44.13075 85.65356  1.000 41.91178  ? 215 LEU B C   1 
ATOM   4158 O  O   . LEU B  1 189 ? 2.44301   -44.20020 85.45038  1.000 42.64257  ? 215 LEU B O   1 
ATOM   4159 C  CB  . LEU B  1 189 ? 0.47467   -44.14500 88.04626  1.000 43.17426  ? 215 LEU B CB  1 
ATOM   4160 C  CG  . LEU B  1 189 ? 0.20824   -43.41485 89.36400  1.000 44.65735  ? 215 LEU B CG  1 
ATOM   4161 C  CD1 . LEU B  1 189 ? -0.38801  -44.36800 90.38827  1.000 46.30432  ? 215 LEU B CD1 1 
ATOM   4162 C  CD2 . LEU B  1 189 ? 1.47537   -42.77060 89.90017  1.000 45.05686  ? 215 LEU B CD2 1 
ATOM   4163 N  N   . LYS B  1 190 ? 0.33768   -44.78993 84.90546  1.000 42.08615  ? 216 LYS B N   1 
ATOM   4164 C  CA  . LYS B  1 190 ? 0.77583   -45.53147 83.72659  1.000 42.50910  ? 216 LYS B CA  1 
ATOM   4165 C  C   . LYS B  1 190 ? 1.41922   -44.60418 82.70195  1.000 40.39133  ? 216 LYS B C   1 
ATOM   4166 O  O   . LYS B  1 190 ? 2.41330   -44.96544 82.06061  1.000 40.40721  ? 216 LYS B O   1 
ATOM   4167 C  CB  . LYS B  1 190 ? -0.40503  -46.27558 83.10231  1.000 45.96204  ? 216 LYS B CB  1 
ATOM   4168 C  CG  . LYS B  1 190 ? -0.65898  -47.65572 83.68150  1.000 50.06360  ? 216 LYS B CG  1 
ATOM   4169 C  CD  . LYS B  1 190 ? -2.01860  -48.18230 83.25116  1.000 53.25162  ? 216 LYS B CD  1 
ATOM   4170 C  CE  . LYS B  1 190 ? -2.07267  -49.69894 83.31762  1.000 56.95205  ? 216 LYS B CE  1 
ATOM   4171 N  NZ  . LYS B  1 190 ? -1.25987  -50.33007 82.24203  1.000 59.80236  ? 216 LYS B NZ  1 
ATOM   4172 N  N   . LEU B  1 191 ? 0.86708   -43.40093 82.53968  1.000 40.37440  ? 217 LEU B N   1 
ATOM   4173 C  CA  . LEU B  1 191 ? 1.36996   -42.46795 81.53646  1.000 39.37104  ? 217 LEU B CA  1 
ATOM   4174 C  C   . LEU B  1 191 ? 2.59273   -41.68189 81.99862  1.000 42.31991  ? 217 LEU B C   1 
ATOM   4175 O  O   . LEU B  1 191 ? 3.35811   -41.20787 81.15151  1.000 42.84553  ? 217 LEU B O   1 
ATOM   4176 C  CB  . LEU B  1 191 ? 0.26859   -41.48590 81.13324  1.000 38.70212  ? 217 LEU B CB  1 
ATOM   4177 C  CG  . LEU B  1 191 ? -1.02312  -42.07544 80.56539  1.000 39.36649  ? 217 LEU B CG  1 
ATOM   4178 C  CD1 . LEU B  1 191 ? -2.05252  -40.98033 80.35424  1.000 37.73623  ? 217 LEU B CD1 1 
ATOM   4179 C  CD2 . LEU B  1 191 ? -0.75883  -42.82379 79.26912  1.000 40.17636  ? 217 LEU B CD2 1 
ATOM   4180 N  N   . ARG B  1 192 ? 2.79017   -41.53547 83.30981  1.000 41.07789  ? 218 ARG B N   1 
ATOM   4181 C  CA  . ARG B  1 192 ? 3.83900   -40.65120 83.81501  1.000 41.00223  ? 218 ARG B CA  1 
ATOM   4182 C  C   . ARG B  1 192 ? 5.24600   -40.96628 83.31020  1.000 41.21625  ? 218 ARG B C   1 
ATOM   4183 O  O   . ARG B  1 192 ? 5.96926   -40.01113 82.97653  1.000 41.57830  ? 218 ARG B O   1 
ATOM   4184 C  CB  . ARG B  1 192 ? 3.80674   -40.65062 85.34973  1.000 43.24722  ? 218 ARG B CB  1 
ATOM   4185 C  CG  . ARG B  1 192 ? 4.14514   -39.30603 85.98050  1.000 45.91681  ? 218 ARG B CG  1 
ATOM   4186 C  CD  . ARG B  1 192 ? 5.64737   -39.08907 86.05429  1.000 48.80384  ? 218 ARG B CD  1 
ATOM   4187 N  NE  . ARG B  1 192 ? 5.99390   -37.72617 86.44498  1.000 52.05352  ? 218 ARG B NE  1 
ATOM   4188 C  CZ  . ARG B  1 192 ? 6.98214   -37.02420 85.89997  1.000 53.16568  ? 218 ARG B CZ  1 
ATOM   4189 N  NH1 . ARG B  1 192 ? 7.72175   -37.55672 84.93678  1.000 53.21902  ? 218 ARG B NH1 1 
ATOM   4190 N  NH2 . ARG B  1 192 ? 7.23044   -35.78964 86.31538  1.000 53.62217  ? 218 ARG B NH2 1 
ATOM   4191 N  N   . PRO B  1 193 ? 5.70783   -42.22219 83.24011  1.000 42.04347  ? 219 PRO B N   1 
ATOM   4192 C  CA  . PRO B  1 193 ? 7.09129   -42.46305 82.78812  1.000 43.49513  ? 219 PRO B CA  1 
ATOM   4193 C  C   . PRO B  1 193 ? 7.39356   -41.95052 81.38610  1.000 44.19274  ? 219 PRO B C   1 
ATOM   4194 O  O   . PRO B  1 193 ? 8.57000   -41.92806 81.00057  1.000 44.73988  ? 219 PRO B O   1 
ATOM   4195 C  CB  . PRO B  1 193 ? 7.22475   -43.99010 82.85792  1.000 44.13570  ? 219 PRO B CB  1 
ATOM   4196 C  CG  . PRO B  1 193 ? 6.23228   -44.40107 83.87828  1.000 42.74094  ? 219 PRO B CG  1 
ATOM   4197 C  CD  . PRO B  1 193 ? 5.07044   -43.47391 83.68983  1.000 42.21604  ? 219 PRO B CD  1 
ATOM   4198 N  N   . ASN B  1 194 ? 6.38649   -41.53597 80.61922  1.000 43.34399  ? 220 ASN B N   1 
ATOM   4199 C  CA  . ASN B  1 194 ? 6.59245   -41.02079 79.27378  1.000 45.23443  ? 220 ASN B CA  1 
ATOM   4200 C  C   . ASN B  1 194 ? 6.36207   -39.51967 79.16583  1.000 45.44697  ? 220 ASN B C   1 
ATOM   4201 O  O   . ASN B  1 194 ? 6.52755   -38.95937 78.07710  1.000 46.89690  ? 220 ASN B O   1 
ATOM   4202 C  CB  . ASN B  1 194 ? 5.68306   -41.75829 78.28463  1.000 44.78850  ? 220 ASN B CB  1 
ATOM   4203 C  CG  . ASN B  1 194 ? 5.85811   -43.26295 78.34660  1.000 46.82541  ? 220 ASN B CG  1 
ATOM   4204 O  OD1 . ASN B  1 194 ? 6.88535   -43.79752 77.92915  1.000 49.53584  ? 220 ASN B OD1 1 
ATOM   4205 N  ND2 . ASN B  1 194 ? 4.85454   -43.95448 78.87334  1.000 47.25785  ? 220 ASN B ND2 1 
ATOM   4206 N  N   . ILE B  1 195 ? 5.98856   -38.85524 80.25505  1.000 45.27902  ? 221 ILE B N   1 
ATOM   4207 C  CA  . ILE B  1 195 ? 5.78448   -37.41115 80.25686  1.000 45.82104  ? 221 ILE B CA  1 
ATOM   4208 C  C   . ILE B  1 195 ? 7.07159   -36.73737 80.71078  1.000 46.15398  ? 221 ILE B C   1 
ATOM   4209 O  O   . ILE B  1 195 ? 7.60776   -37.05614 81.77912  1.000 42.19497  ? 221 ILE B O   1 
ATOM   4210 C  CB  . ILE B  1 195 ? 4.60697   -37.02145 81.16550  1.000 46.07718  ? 221 ILE B CB  1 
ATOM   4211 C  CG1 . ILE B  1 195 ? 3.33892   -37.76835 80.74650  1.000 45.35858  ? 221 ILE B CG1 1 
ATOM   4212 C  CG2 . ILE B  1 195 ? 4.37977   -35.51676 81.12749  1.000 45.86837  ? 221 ILE B CG2 1 
ATOM   4213 C  CD1 . ILE B  1 195 ? 2.16912   -37.55660 81.68265  1.000 39.00989  ? 221 ILE B CD1 1 
ATOM   4214 N  N   . ARG B  1 196 ? 7.56923   -35.80081 79.90045  1.000 45.65138  ? 222 ARG B N   1 
ATOM   4215 C  CA  . ARG B  1 196 ? 8.83065   -35.14251 80.22508  1.000 46.25005  ? 222 ARG B CA  1 
ATOM   4216 C  C   . ARG B  1 196 ? 8.66688   -34.18106 81.39677  1.000 45.68898  ? 222 ARG B C   1 
ATOM   4217 O  O   . ARG B  1 196 ? 9.47851   -34.18219 82.32982  1.000 45.69048  ? 222 ARG B O   1 
ATOM   4218 C  CB  . ARG B  1 196 ? 9.37797   -34.41299 78.99743  1.000 46.31946  ? 222 ARG B CB  1 
ATOM   4219 C  CG  . ARG B  1 196 ? 10.77956  -33.85182 79.19335  1.000 47.54540  ? 222 ARG B CG  1 
ATOM   4220 C  CD  . ARG B  1 196 ? 11.28351  -33.14687 77.94344  1.000 45.01369  ? 222 ARG B CD  1 
ATOM   4221 N  NE  . ARG B  1 196 ? 11.57648  -34.08397 76.86257  1.000 48.09602  ? 222 ARG B NE  1 
ATOM   4222 C  CZ  . ARG B  1 196 ? 11.78558  -33.72566 75.59970  1.000 48.16646  ? 222 ARG B CZ  1 
ATOM   4223 N  NH1 . ARG B  1 196 ? 11.73342  -32.44662 75.25369  1.000 45.68459  ? 222 ARG B NH1 1 
ATOM   4224 N  NH2 . ARG B  1 196 ? 12.04649  -34.64642 74.68170  1.000 48.49673  ? 222 ARG B NH2 1 
ATOM   4225 N  N   . TYR B  1 197 ? 7.62518   -33.35219 81.36926  1.000 45.12337  ? 223 TYR B N   1 
ATOM   4226 C  CA  . TYR B  1 197 ? 7.40476   -32.39867 82.44782  1.000 46.78574  ? 223 TYR B CA  1 
ATOM   4227 C  C   . TYR B  1 197 ? 5.93245   -32.01942 82.49974  1.000 46.49059  ? 223 TYR B C   1 
ATOM   4228 O  O   . TYR B  1 197 ? 5.17136   -32.26590 81.56030  1.000 44.34273  ? 223 TYR B O   1 
ATOM   4229 C  CB  . TYR B  1 197 ? 8.27858   -31.14778 82.28303  1.000 48.59831  ? 223 TYR B CB  1 
ATOM   4230 C  CG  . TYR B  1 197 ? 8.06589   -30.39328 80.98679  1.000 49.98982  ? 223 TYR B CG  1 
ATOM   4231 C  CD1 . TYR B  1 197 ? 7.09501   -29.40387 80.88578  1.000 50.26775  ? 223 TYR B CD1 1 
ATOM   4232 C  CD2 . TYR B  1 197 ? 8.84410   -30.66231 79.86790  1.000 50.32032  ? 223 TYR B CD2 1 
ATOM   4233 C  CE1 . TYR B  1 197 ? 6.90054   -28.70997 79.70619  1.000 50.15476  ? 223 TYR B CE1 1 
ATOM   4234 C  CE2 . TYR B  1 197 ? 8.65664   -29.97292 78.68342  1.000 49.96534  ? 223 TYR B CE2 1 
ATOM   4235 C  CZ  . TYR B  1 197 ? 7.68334   -28.99834 78.60858  1.000 50.26588  ? 223 TYR B CZ  1 
ATOM   4236 O  OH  . TYR B  1 197 ? 7.49195   -28.30892 77.43297  1.000 49.73178  ? 223 TYR B OH  1 
ATOM   4237 N  N   . PHE B  1 198 ? 5.54664   -31.41450 83.62124  1.000 47.71476  ? 224 PHE B N   1 
ATOM   4238 C  CA  . PHE B  1 198 ? 4.20050   -30.88900 83.83934  1.000 48.41860  ? 224 PHE B CA  1 
ATOM   4239 C  C   . PHE B  1 198 ? 4.32339   -29.37617 83.99520  1.000 50.16931  ? 224 PHE B C   1 
ATOM   4240 O  O   . PHE B  1 198 ? 4.74505   -28.88932 85.04896  1.000 51.44321  ? 224 PHE B O   1 
ATOM   4241 C  CB  . PHE B  1 198 ? 3.55063   -31.51634 85.07209  1.000 48.55235  ? 224 PHE B CB  1 
ATOM   4242 C  CG  . PHE B  1 198 ? 3.29634   -32.99327 84.94973  1.000 47.71967  ? 224 PHE B CG  1 
ATOM   4243 C  CD1 . PHE B  1 198 ? 2.04539   -33.46614 84.59134  1.000 46.69214  ? 224 PHE B CD1 1 
ATOM   4244 C  CD2 . PHE B  1 198 ? 4.30248   -33.90886 85.21104  1.000 48.28362  ? 224 PHE B CD2 1 
ATOM   4245 C  CE1 . PHE B  1 198 ? 1.80494   -34.82397 84.48354  1.000 46.01674  ? 224 PHE B CE1 1 
ATOM   4246 C  CE2 . PHE B  1 198 ? 4.06842   -35.26772 85.10552  1.000 47.35956  ? 224 PHE B CE2 1 
ATOM   4247 C  CZ  . PHE B  1 198 ? 2.81834   -35.72539 84.74156  1.000 46.48670  ? 224 PHE B CZ  1 
ATOM   4248 N  N   . HIS B  1 199 ? 3.96243   -28.63025 82.95308  1.000 51.08424  ? 225 HIS B N   1 
ATOM   4249 C  CA  . HIS B  1 199 ? 4.02493   -27.17749 83.01482  1.000 53.54662  ? 225 HIS B CA  1 
ATOM   4250 C  C   . HIS B  1 199 ? 2.87501   -26.58664 82.21367  1.000 54.18200  ? 225 HIS B C   1 
ATOM   4251 O  O   . HIS B  1 199 ? 2.37873   -27.19909 81.26422  1.000 54.65594  ? 225 HIS B O   1 
ATOM   4252 C  CB  . HIS B  1 199 ? 5.36464   -26.64105 82.49781  1.000 55.35262  ? 225 HIS B CB  1 
ATOM   4253 C  CG  . HIS B  1 199 ? 5.76699   -25.33742 83.11413  1.000 56.78342  ? 225 HIS B CG  1 
ATOM   4254 N  ND1 . HIS B  1 199 ? 5.44145   -24.11889 82.55841  1.000 56.79597  ? 225 HIS B ND1 1 
ATOM   4255 C  CD2 . HIS B  1 199 ? 6.45915   -25.06204 84.24500  1.000 57.83785  ? 225 HIS B CD2 1 
ATOM   4256 C  CE1 . HIS B  1 199 ? 5.92072   -23.14923 83.31702  1.000 57.76023  ? 225 HIS B CE1 1 
ATOM   4257 N  NE2 . HIS B  1 199 ? 6.54219   -23.69460 84.34708  1.000 58.33730  ? 225 HIS B NE2 1 
ATOM   4258 N  N   . SER B  1 200 ? 2.46539   -25.38097 82.60305  1.000 54.28754  ? 226 SER B N   1 
ATOM   4259 C  CA  . SER B  1 200 ? 1.29905   -24.72533 82.03037  1.000 55.64395  ? 226 SER B CA  1 
ATOM   4260 C  C   . SER B  1 200 ? 1.64740   -23.63096 81.02927  1.000 56.95911  ? 226 SER B C   1 
ATOM   4261 O  O   . SER B  1 200 ? 0.73384   -23.02473 80.46066  1.000 55.68701  ? 226 SER B O   1 
ATOM   4262 C  CB  . SER B  1 200 ? 0.43025   -24.13430 83.14708  1.000 55.87589  ? 226 SER B CB  1 
ATOM   4263 O  OG  . SER B  1 200 ? -0.12365  -25.15260 83.96216  1.000 55.79846  ? 226 SER B OG  1 
ATOM   4264 N  N   . SER B  1 201 ? 2.93231   -23.35994 80.79305  1.000 59.73663  ? 227 SER B N   1 
ATOM   4265 C  CA  . SER B  1 201 ? 3.29373   -22.25093 79.91639  1.000 60.58377  ? 227 SER B CA  1 
ATOM   4266 C  C   . SER B  1 201 ? 4.57732   -22.50215 79.13193  1.000 63.13119  ? 227 SER B C   1 
ATOM   4267 O  O   . SER B  1 201 ? 4.85014   -21.80205 78.15358  1.000 63.54484  ? 227 SER B O   1 
ATOM   4268 C  CB  . SER B  1 201 ? 3.43016   -20.96055 80.72783  1.000 59.76906  ? 227 SER B CB  1 
ATOM   4269 O  OG  . SER B  1 201 ? 4.60239   -20.97827 81.52275  1.000 60.04486  ? 227 SER B OG  1 
ATOM   4270 N  N   . GLN B  1 202 ? 5.38225   -23.48018 79.54989  1.000 63.41241  ? 228 GLN B N   1 
ATOM   4271 C  CA  . GLN B  1 202 ? 6.60632   -23.78306 78.81478  1.000 64.41711  ? 228 GLN B CA  1 
ATOM   4272 C  C   . GLN B  1 202 ? 6.32503   -24.53279 77.51829  1.000 59.98351  ? 228 GLN B C   1 
ATOM   4273 O  O   . GLN B  1 202 ? 7.13722   -24.47317 76.58170  1.000 60.90689  ? 228 GLN B O   1 
ATOM   4274 C  CB  . GLN B  1 202 ? 7.55651   -24.59531 79.69832  1.000 68.59197  ? 228 GLN B CB  1 
ATOM   4275 C  CG  . GLN B  1 202 ? 8.97119   -24.72356 79.15615  1.000 73.35250  ? 228 GLN B CG  1 
ATOM   4276 C  CD  . GLN B  1 202 ? 9.84087   -25.62454 80.01072  1.000 76.40181  ? 228 GLN B CD  1 
ATOM   4277 O  OE1 . GLN B  1 202 ? 9.62437   -25.75442 81.21573  1.000 77.10867  ? 228 GLN B OE1 1 
ATOM   4278 N  NE2 . GLN B  1 202 ? 10.82970  -26.25628 79.38860  1.000 78.33341  ? 228 GLN B NE2 1 
ATOM   4279 N  N   . TYR B  1 203 ? 5.18195   -25.21737 77.43761  1.000 54.60113  ? 229 TYR B N   1 
ATOM   4280 C  CA  . TYR B  1 203 ? 4.91769   -26.07393 76.29007  1.000 52.25685  ? 229 TYR B CA  1 
ATOM   4281 C  C   . TYR B  1 203 ? 4.68028   -25.27168 75.01880  1.000 52.45211  ? 229 TYR B C   1 
ATOM   4282 O  O   . TYR B  1 203 ? 4.94556   -25.77579 73.92741  1.000 52.16412  ? 229 TYR B O   1 
ATOM   4283 C  CB  . TYR B  1 203 ? 3.73231   -26.99579 76.57678  1.000 49.96569  ? 229 TYR B CB  1 
ATOM   4284 C  CG  . TYR B  1 203 ? 2.38332   -26.31623 76.58593  1.000 47.04062  ? 229 TYR B CG  1 
ATOM   4285 C  CD1 . TYR B  1 203 ? 1.53510   -26.39927 75.48908  1.000 45.00516  ? 229 TYR B CD1 1 
ATOM   4286 C  CD2 . TYR B  1 203 ? 1.94977   -25.60659 77.69760  1.000 46.22193  ? 229 TYR B CD2 1 
ATOM   4287 C  CE1 . TYR B  1 203 ? 0.29636   -25.78637 75.49628  1.000 44.27813  ? 229 TYR B CE1 1 
ATOM   4288 C  CE2 . TYR B  1 203 ? 0.71415   -24.99044 77.71367  1.000 44.83808  ? 229 TYR B CE2 1 
ATOM   4289 C  CZ  . TYR B  1 203 ? -0.10799  -25.08396 76.61152  1.000 44.06625  ? 229 TYR B CZ  1 
ATOM   4290 O  OH  . TYR B  1 203 ? -1.33919  -24.47321 76.62699  1.000 44.37394  ? 229 TYR B OH  1 
ATOM   4291 N  N   . ILE B  1 204 ? 4.22003   -24.02359 75.12487  1.000 53.28307  ? 230 ILE B N   1 
ATOM   4292 C  CA  . ILE B  1 204 ? 4.03106   -23.21804 73.91987  1.000 54.56199  ? 230 ILE B CA  1 
ATOM   4293 C  C   . ILE B  1 204 ? 5.37497   -22.92418 73.26175  1.000 56.65474  ? 230 ILE B C   1 
ATOM   4294 O  O   . ILE B  1 204 ? 5.53761   -23.08412 72.04520  1.000 57.59086  ? 230 ILE B O   1 
ATOM   4295 C  CB  . ILE B  1 204 ? 3.25000   -21.92800 74.23737  1.000 54.36670  ? 230 ILE B CB  1 
ATOM   4296 C  CG1 . ILE B  1 204 ? 3.93131   -21.10836 75.33422  1.000 55.30657  ? 230 ILE B CG1 1 
ATOM   4297 C  CG2 . ILE B  1 204 ? 1.84744   -22.26843 74.66903  1.000 52.67551  ? 230 ILE B CG2 1 
ATOM   4298 C  CD1 . ILE B  1 204 ? 4.57771   -19.83397 74.83745  1.000 55.62787  ? 230 ILE B CD1 1 
ATOM   4299 N  N   . ASN B  1 205 ? 6.36513   -22.51720 74.06013  1.000 58.46568  ? 231 ASN B N   1 
ATOM   4300 C  CA  . ASN B  1 205 ? 7.69357   -22.25619 73.51899  1.000 61.17533  ? 231 ASN B CA  1 
ATOM   4301 C  C   . ASN B  1 205 ? 8.34870   -23.54175 73.03188  1.000 61.19820  ? 231 ASN B C   1 
ATOM   4302 O  O   . ASN B  1 205 ? 8.96140   -23.56505 71.95596  1.000 61.33629  ? 231 ASN B O   1 
ATOM   4303 C  CB  . ASN B  1 205 ? 8.56375   -21.57371 74.57484  1.000 63.86633  ? 231 ASN B CB  1 
ATOM   4304 C  CG  . ASN B  1 205 ? 9.59452   -20.64290 73.96900  1.000 69.18269  ? 231 ASN B CG  1 
ATOM   4305 O  OD1 . ASN B  1 205 ? 9.31194   -19.92293 73.01109  1.000 71.24686  ? 231 ASN B OD1 1 
ATOM   4306 N  ND2 . ASN B  1 205 ? 10.80029  -20.65380 74.52588  1.000 71.59687  ? 231 ASN B ND2 1 
ATOM   4307 N  N   . ASP B  1 206 ? 8.22092   -24.62640 73.80296  1.000 60.68421  ? 232 ASP B N   1 
ATOM   4308 C  CA  . ASP B  1 206 ? 8.81820   -25.88989 73.38480  1.000 60.86434  ? 232 ASP B CA  1 
ATOM   4309 C  C   . ASP B  1 206 ? 8.14150   -26.47585 72.14886  1.000 59.51624  ? 232 ASP B C   1 
ATOM   4310 O  O   . ASP B  1 206 ? 8.77239   -27.25195 71.42332  1.000 59.74525  ? 232 ASP B O   1 
ATOM   4311 C  CB  . ASP B  1 206 ? 8.78212   -26.88954 74.54044  1.000 61.21763  ? 232 ASP B CB  1 
ATOM   4312 C  CG  . ASP B  1 206 ? 9.59835   -26.42555 75.73287  1.000 61.88525  ? 232 ASP B CG  1 
ATOM   4313 O  OD1 . ASP B  1 206 ? 10.11587  -25.28894 75.69226  1.000 62.29628  ? 232 ASP B OD1 1 
ATOM   4314 O  OD2 . ASP B  1 206 ? 9.72562   -27.19494 76.70814  1.000 61.91038  ? 232 ASP B OD2 1 
ATOM   4315 N  N   . LEU B  1 207 ? 6.88056   -26.11990 71.89047  1.000 58.98035  ? 233 LEU B N   1 
ATOM   4316 C  CA  . LEU B  1 207 ? 6.20379   -26.54536 70.67196  1.000 59.23918  ? 233 LEU B CA  1 
ATOM   4317 C  C   . LEU B  1 207 ? 6.62006   -25.68990 69.48530  1.000 61.82104  ? 233 LEU B C   1 
ATOM   4318 O  O   . LEU B  1 207 ? 6.87082   -26.21578 68.39491  1.000 63.06961  ? 233 LEU B O   1 
ATOM   4319 C  CB  . LEU B  1 207 ? 4.68700   -26.47398 70.86116  1.000 56.06865  ? 233 LEU B CB  1 
ATOM   4320 C  CG  . LEU B  1 207 ? 3.96542   -27.68543 71.45288  1.000 53.65456  ? 233 LEU B CG  1 
ATOM   4321 C  CD1 . LEU B  1 207 ? 2.58048   -27.28718 71.93903  1.000 51.52469  ? 233 LEU B CD1 1 
ATOM   4322 C  CD2 . LEU B  1 207 ? 3.87602   -28.81261 70.43830  1.000 53.38207  ? 233 LEU B CD2 1 
ATOM   4323 N  N   . ALA B  1 208 ? 6.68954   -24.36928 69.67934  1.000 62.22116  ? 234 ALA B N   1 
ATOM   4324 C  CA  . ALA B  1 208 ? 7.13092   -23.48898 68.60350  1.000 65.15193  ? 234 ALA B CA  1 
ATOM   4325 C  C   . ALA B  1 208 ? 8.56275   -23.79305 68.18473  1.000 69.53133  ? 234 ALA B C   1 
ATOM   4326 O  O   . ALA B  1 208 ? 8.90358   -23.66829 67.00247  1.000 73.53063  ? 234 ALA B O   1 
ATOM   4327 C  CB  . ALA B  1 208 ? 6.99980   -22.02720 69.03067  1.000 64.88603  ? 234 ALA B CB  1 
ATOM   4328 N  N   . ASN B  1 209 ? 9.41219   -24.19704 69.13176  1.000 67.31417  ? 235 ASN B N   1 
ATOM   4329 C  CA  . ASN B  1 209 ? 10.78415  -24.55715 68.79739  1.000 66.89205  ? 235 ASN B CA  1 
ATOM   4330 C  C   . ASN B  1 209 ? 10.91857  -26.00211 68.33631  1.000 66.70378  ? 235 ASN B C   1 
ATOM   4331 O  O   . ASN B  1 209 ? 11.94926  -26.35862 67.75508  1.000 65.50521  ? 235 ASN B O   1 
ATOM   4332 C  CB  . ASN B  1 209 ? 11.70136  -24.31793 69.99856  1.000 66.72047  ? 235 ASN B CB  1 
ATOM   4333 C  CG  . ASN B  1 209 ? 12.00519  -22.84982 70.21583  1.000 66.27822  ? 235 ASN B CG  1 
ATOM   4334 O  OD1 . ASN B  1 209 ? 11.85878  -22.03266 69.30707  1.000 65.92335  ? 235 ASN B OD1 1 
ATOM   4335 N  ND2 . ASN B  1 209 ? 12.43408  -22.50707 71.42491  1.000 66.25836  ? 235 ASN B ND2 1 
ATOM   4336 N  N   . GLY B  1 210 ? 9.90934   -26.83440 68.57545  1.000 68.18484  ? 236 GLY B N   1 
ATOM   4337 C  CA  . GLY B  1 210 ? 9.97943   -28.23798 68.23126  1.000 68.99431  ? 236 GLY B CA  1 
ATOM   4338 C  C   . GLY B  1 210 ? 10.60464  -29.12591 69.28204  1.000 69.09605  ? 236 GLY B C   1 
ATOM   4339 O  O   . GLY B  1 210 ? 10.90315  -30.28929 68.98657  1.000 70.22266  ? 236 GLY B O   1 
ATOM   4340 N  N   . ASP B  1 211 ? 10.81064  -28.61886 70.50038  1.000 65.96528  ? 237 ASP B N   1 
ATOM   4341 C  CA  . ASP B  1 211 ? 11.44361  -29.42120 71.54182  1.000 67.90167  ? 237 ASP B CA  1 
ATOM   4342 C  C   . ASP B  1 211 ? 10.52922  -30.53718 72.03068  1.000 65.32375  ? 237 ASP B C   1 
ATOM   4343 O  O   . ASP B  1 211 ? 11.00845  -31.62659 72.36504  1.000 64.75073  ? 237 ASP B O   1 
ATOM   4344 C  CB  . ASP B  1 211 ? 11.86652  -28.52536 72.70544  1.000 71.06249  ? 237 ASP B CB  1 
ATOM   4345 C  CG  . ASP B  1 211 ? 12.93385  -27.52377 72.30862  1.000 75.86168  ? 237 ASP B CG  1 
ATOM   4346 O  OD1 . ASP B  1 211 ? 13.78429  -27.86593 71.45992  1.000 77.83258  ? 237 ASP B OD1 1 
ATOM   4347 O  OD2 . ASP B  1 211 ? 12.92149  -26.39439 72.84186  1.000 77.36107  ? 237 ASP B OD2 1 
ATOM   4348 N  N   . ILE B  1 212 ? 9.22415   -30.28973 72.08619  1.000 63.81287  ? 238 ILE B N   1 
ATOM   4349 C  CA  . ILE B  1 212 ? 8.24753   -31.31896 72.41334  1.000 62.89101  ? 238 ILE B CA  1 
ATOM   4350 C  C   . ILE B  1 212 ? 7.32130   -31.49533 71.21849  1.000 62.20929  ? 238 ILE B C   1 
ATOM   4351 O  O   . ILE B  1 212 ? 7.04027   -30.54764 70.47701  1.000 63.20697  ? 238 ILE B O   1 
ATOM   4352 C  CB  . ILE B  1 212 ? 7.45450   -30.98610 73.69585  1.000 61.39595  ? 238 ILE B CB  1 
ATOM   4353 C  CG1 . ILE B  1 212 ? 6.56352   -29.76554 73.47731  1.000 60.39488  ? 238 ILE B CG1 1 
ATOM   4354 C  CG2 . ILE B  1 212 ? 8.40174   -30.76012 74.86572  1.000 61.64017  ? 238 ILE B CG2 1 
ATOM   4355 C  CD1 . ILE B  1 212 ? 5.17176   -29.94940 73.99615  1.000 58.97020  ? 238 ILE B CD1 1 
ATOM   4356 N  N   . CYS B  1 213 ? 6.84926   -32.72694 71.03163  1.000 59.78274  ? 239 CYS B N   1 
ATOM   4357 C  CA  A CYS B  1 213 ? 6.06445   -33.06500 69.85215  0.831 57.69188  ? 239 CYS B CA  1 
ATOM   4358 C  CA  B CYS B  1 213 ? 6.06455   -33.09655 69.86102  0.169 57.84304  ? 239 CYS B CA  1 
ATOM   4359 C  C   . CYS B  1 213 ? 4.56270   -33.09018 70.10334  1.000 56.54895  ? 239 CYS B C   1 
ATOM   4360 O  O   . CYS B  1 213 ? 3.79417   -32.89222 69.15659  1.000 56.35075  ? 239 CYS B O   1 
ATOM   4361 C  CB  A CYS B  1 213 ? 6.50717   -34.42339 69.28624  0.831 57.57471  ? 239 CYS B CB  1 
ATOM   4362 C  CB  B CYS B  1 213 ? 6.48502   -34.48619 69.37744  0.169 57.71259  ? 239 CYS B CB  1 
ATOM   4363 S  SG  A CYS B  1 213 ? 6.45765   -35.79774 70.46194  0.831 56.51675  ? 239 CYS B SG  1 
ATOM   4364 S  SG  B CYS B  1 213 ? 5.61277   -35.08940 67.93045  0.169 57.96727  ? 239 CYS B SG  1 
ATOM   4365 N  N   . VAL B  1 214 ? 4.12140   -33.31120 71.34047  1.000 55.38391  ? 240 VAL B N   1 
ATOM   4366 C  CA  . VAL B  1 214 ? 2.69651   -33.36930 71.64265  1.000 53.97332  ? 240 VAL B CA  1 
ATOM   4367 C  C   . VAL B  1 214 ? 2.48477   -32.96242 73.09456  1.000 50.95999  ? 240 VAL B C   1 
ATOM   4368 O  O   . VAL B  1 214 ? 3.31976   -33.22976 73.96320  1.000 50.27740  ? 240 VAL B O   1 
ATOM   4369 C  CB  . VAL B  1 214 ? 2.11902   -34.77501 71.34163  1.000 56.34963  ? 240 VAL B CB  1 
ATOM   4370 C  CG1 . VAL B  1 214 ? 2.65580   -35.80531 72.32056  1.000 57.55024  ? 240 VAL B CG1 1 
ATOM   4371 C  CG2 . VAL B  1 214 ? 0.59897   -34.74775 71.35636  1.000 57.24298  ? 240 VAL B CG2 1 
ATOM   4372 N  N   . ALA B  1 215 ? 1.36025   -32.29613 73.34976  1.000 49.22648  ? 241 ALA B N   1 
ATOM   4373 C  CA  . ALA B  1 215 ? 1.07172   -31.75550 74.66919  1.000 49.48948  ? 241 ALA B CA  1 
ATOM   4374 C  C   . ALA B  1 215 ? -0.42460  -31.53049 74.81535  1.000 47.54226  ? 241 ALA B C   1 
ATOM   4375 O  O   . ALA B  1 215 ? -1.15271  -31.38083 73.83026  1.000 47.28521  ? 241 ALA B O   1 
ATOM   4376 C  CB  . ALA B  1 215 ? 1.82011   -30.44247 74.91343  1.000 50.17831  ? 241 ALA B CB  1 
ATOM   4377 N  N   . ILE B  1 216 ? -0.86832  -31.51176 76.06657  1.000 45.87049  ? 242 ILE B N   1 
ATOM   4378 C  CA  . ILE B  1 216 ? -2.19930  -31.03820 76.42084  1.000 45.18431  ? 242 ILE B CA  1 
ATOM   4379 C  C   . ILE B  1 216 ? -2.10686  -29.53721 76.64717  1.000 45.09162  ? 242 ILE B C   1 
ATOM   4380 O  O   . ILE B  1 216 ? -1.20544  -29.06394 77.34899  1.000 46.20641  ? 242 ILE B O   1 
ATOM   4381 C  CB  . ILE B  1 216 ? -2.72475  -31.75637 77.67482  1.000 44.85132  ? 242 ILE B CB  1 
ATOM   4382 C  CG1 . ILE B  1 216 ? -2.83413  -33.26103 77.42243  1.000 45.60084  ? 242 ILE B CG1 1 
ATOM   4383 C  CG2 . ILE B  1 216 ? -4.06902  -31.18160 78.09855  1.000 43.41800  ? 242 ILE B CG2 1 
ATOM   4384 C  CD1 . ILE B  1 216 ? -3.14160  -34.06486 78.66463  1.000 46.46705  ? 242 ILE B CD1 1 
ATOM   4385 N  N   . GLY B  1 217 ? -3.01987  -28.78157 76.04581  1.000 45.18499  ? 243 GLY B N   1 
ATOM   4386 C  CA  . GLY B  1 217 ? -2.93387  -27.33868 76.15613  1.000 46.49657  ? 243 GLY B CA  1 
ATOM   4387 C  C   . GLY B  1 217 ? -4.22901  -26.64186 75.81705  1.000 46.81037  ? 243 GLY B C   1 
ATOM   4388 O  O   . GLY B  1 217 ? -5.12840  -27.21141 75.18914  1.000 45.04947  ? 243 GLY B O   1 
ATOM   4389 N  N   . TRP B  1 218 ? -4.31009  -25.38719 76.24891  1.000 48.50326  ? 244 TRP B N   1 
ATOM   4390 C  CA  . TRP B  1 218 ? -5.42534  -24.52568 75.89743  1.000 49.41815  ? 244 TRP B CA  1 
ATOM   4391 C  C   . TRP B  1 218 ? -5.28374  -24.05576 74.45361  1.000 51.09141  ? 244 TRP B C   1 
ATOM   4392 O  O   . TRP B  1 218 ? -4.17975  -23.98987 73.90558  1.000 50.86989  ? 244 TRP B O   1 
ATOM   4393 C  CB  . TRP B  1 218 ? -5.49572  -23.33296 76.85239  1.000 50.03654  ? 244 TRP B CB  1 
ATOM   4394 C  CG  . TRP B  1 218 ? -5.72958  -23.73520 78.28511  1.000 51.21496  ? 244 TRP B CG  1 
ATOM   4395 C  CD1 . TRP B  1 218 ? -6.84041  -24.34317 78.79254  1.000 50.69837  ? 244 TRP B CD1 1 
ATOM   4396 C  CD2 . TRP B  1 218 ? -4.82870  -23.56352 79.38892  1.000 51.85544  ? 244 TRP B CD2 1 
ATOM   4397 N  NE1 . TRP B  1 218 ? -6.69044  -24.55769 80.14119  1.000 51.62778  ? 244 TRP B NE1 1 
ATOM   4398 C  CE2 . TRP B  1 218 ? -5.46435  -24.08840 80.53215  1.000 51.33255  ? 244 TRP B CE2 1 
ATOM   4399 C  CE3 . TRP B  1 218 ? -3.54879  -23.01605 79.52142  1.000 52.76659  ? 244 TRP B CE3 1 
ATOM   4400 C  CZ2 . TRP B  1 218 ? -4.86421  -24.08198 81.79041  1.000 51.81653  ? 244 TRP B CZ2 1 
ATOM   4401 C  CZ3 . TRP B  1 218 ? -2.95425  -23.01056 80.77234  1.000 53.16764  ? 244 TRP B CZ3 1 
ATOM   4402 C  CH2 . TRP B  1 218 ? -3.61222  -23.54011 81.88945  1.000 53.30152  ? 244 TRP B CH2 1 
ATOM   4403 N  N   . ALA B  1 219 ? -6.42240  -23.72840 73.83828  1.000 53.67501  ? 245 ALA B N   1 
ATOM   4404 C  CA  . ALA B  1 219 ? -6.44843  -23.46999 72.40039  1.000 54.21683  ? 245 ALA B CA  1 
ATOM   4405 C  C   . ALA B  1 219 ? -5.60808  -22.25203 72.03148  1.000 56.85691  ? 245 ALA B C   1 
ATOM   4406 O  O   . ALA B  1 219 ? -4.75804  -22.31937 71.13396  1.000 58.98510  ? 245 ALA B O   1 
ATOM   4407 C  CB  . ALA B  1 219 ? -7.89197  -23.29181 71.92996  1.000 53.77554  ? 245 ALA B CB  1 
ATOM   4408 N  N   . GLY B  1 220 ? -5.83937  -21.12486 72.70916  1.000 55.50032  ? 246 GLY B N   1 
ATOM   4409 C  CA  . GLY B  1 220 ? -5.12311  -19.90569 72.36695  1.000 55.70680  ? 246 GLY B CA  1 
ATOM   4410 C  C   . GLY B  1 220 ? -3.62148  -20.04105 72.52638  1.000 56.38089  ? 246 GLY B C   1 
ATOM   4411 O  O   . GLY B  1 220 ? -2.85065  -19.48465 71.74001  1.000 57.65983  ? 246 GLY B O   1 
ATOM   4412 N  N   . ASP B  1 221 ? -3.18677  -20.79049 73.54050  1.000 54.98488  ? 247 ASP B N   1 
ATOM   4413 C  CA  . ASP B  1 221 ? -1.76003  -21.01538 73.74545  1.000 53.21780  ? 247 ASP B CA  1 
ATOM   4414 C  C   . ASP B  1 221 ? -1.14263  -21.74317 72.55578  1.000 50.81797  ? 247 ASP B C   1 
ATOM   4415 O  O   . ASP B  1 221 ? -0.09484  -21.33757 72.03546  1.000 49.43458  ? 247 ASP B O   1 
ATOM   4416 C  CB  . ASP B  1 221 ? -1.54578  -21.80594 75.03553  1.000 54.49157  ? 247 ASP B CB  1 
ATOM   4417 C  CG  . ASP B  1 221 ? -1.67775  -20.94773 76.27788  1.000 55.61165  ? 247 ASP B CG  1 
ATOM   4418 O  OD1 . ASP B  1 221 ? -1.90231  -21.51253 77.36860  1.000 55.96478  ? 247 ASP B OD1 1 
ATOM   4419 O  OD2 . ASP B  1 221 ? -1.55652  -19.71046 76.16604  1.000 56.80777  ? 247 ASP B OD2 1 
ATOM   4420 N  N   . VAL B  1 222 ? -1.78955  -22.82036 72.10524  1.000 50.32653  ? 248 VAL B N   1 
ATOM   4421 C  CA  . VAL B  1 222 ? -1.27458  -23.58467 70.97363  1.000 50.92416  ? 248 VAL B CA  1 
ATOM   4422 C  C   . VAL B  1 222 ? -1.30020  -22.74461 69.70167  1.000 54.27548  ? 248 VAL B C   1 
ATOM   4423 O  O   . VAL B  1 222 ? -0.37829  -22.81148 68.87912  1.000 55.33542  ? 248 VAL B O   1 
ATOM   4424 C  CB  . VAL B  1 222 ? -2.07244  -24.89207 70.81161  1.000 48.67645  ? 248 VAL B CB  1 
ATOM   4425 C  CG1 . VAL B  1 222 ? -1.52841  -25.71350 69.65459  1.000 48.66283  ? 248 VAL B CG1 1 
ATOM   4426 C  CG2 . VAL B  1 222 ? -2.03874  -25.69730 72.10351  1.000 48.36882  ? 248 VAL B CG2 1 
ATOM   4427 N  N   . TRP B  1 223 ? -2.34480  -21.93088 69.52241  1.000 56.36037  ? 249 TRP B N   1 
ATOM   4428 C  CA  . TRP B  1 223 ? -2.42035  -21.09548 68.32639  1.000 58.69404  ? 249 TRP B CA  1 
ATOM   4429 C  C   . TRP B  1 223 ? -1.31827  -20.04126 68.31417  1.000 63.29575  ? 249 TRP B C   1 
ATOM   4430 O  O   . TRP B  1 223 ? -0.71366  -19.77588 67.26598  1.000 65.47257  ? 249 TRP B O   1 
ATOM   4431 C  CB  . TRP B  1 223 ? -3.79656  -20.43556 68.22565  1.000 56.21882  ? 249 TRP B CB  1 
ATOM   4432 C  CG  . TRP B  1 223 ? -4.93325  -21.39044 67.95676  1.000 53.01652  ? 249 TRP B CG  1 
ATOM   4433 C  CD1 . TRP B  1 223 ? -6.13530  -21.42840 68.60300  1.000 51.98271  ? 249 TRP B CD1 1 
ATOM   4434 C  CD2 . TRP B  1 223 ? -4.97867  -22.43266 66.96829  1.000 50.34462  ? 249 TRP B CD2 1 
ATOM   4435 N  NE1 . TRP B  1 223 ? -6.92178  -22.42850 68.08552  1.000 50.39869  ? 249 TRP B NE1 1 
ATOM   4436 C  CE2 . TRP B  1 223 ? -6.23618  -23.05935 67.08123  1.000 48.87494  ? 249 TRP B CE2 1 
ATOM   4437 C  CE3 . TRP B  1 223 ? -4.07969  -22.89671 66.00127  1.000 49.70336  ? 249 TRP B CE3 1 
ATOM   4438 C  CZ2 . TRP B  1 223 ? -6.61592  -24.12426 66.26657  1.000 47.07532  ? 249 TRP B CZ2 1 
ATOM   4439 C  CZ3 . TRP B  1 223 ? -4.45884  -23.95456 65.19497  1.000 48.47628  ? 249 TRP B CZ3 1 
ATOM   4440 C  CH2 . TRP B  1 223 ? -5.71568  -24.55590 65.33225  1.000 47.35556  ? 249 TRP B CH2 1 
ATOM   4441 N  N   . GLN B  1 224 ? -1.04313  -19.42581 69.46694  1.000 64.37252  ? 250 GLN B N   1 
ATOM   4442 C  CA  . GLN B  1 224 ? 0.04282   -18.45526 69.53085  1.000 68.05875  ? 250 GLN B CA  1 
ATOM   4443 C  C   . GLN B  1 224 ? 1.39576   -19.12364 69.32927  1.000 70.30656  ? 250 GLN B C   1 
ATOM   4444 O  O   . GLN B  1 224 ? 2.29001   -18.53181 68.71438  1.000 71.06716  ? 250 GLN B O   1 
ATOM   4445 C  CB  . GLN B  1 224 ? 0.00367   -17.70033 70.85934  1.000 70.10056  ? 250 GLN B CB  1 
ATOM   4446 C  CG  . GLN B  1 224 ? 0.69777   -16.34729 70.81293  1.000 74.03668  ? 250 GLN B CG  1 
ATOM   4447 C  CD  . GLN B  1 224 ? -0.14059  -15.23926 71.41869  1.000 78.02802  ? 250 GLN B CD  1 
ATOM   4448 O  OE1 . GLN B  1 224 ? -1.25311  -15.47452 71.88916  1.000 79.28181  ? 250 GLN B OE1 1 
ATOM   4449 N  NE2 . GLN B  1 224 ? 0.38433   -14.01882 71.39595  1.000 79.84609  ? 250 GLN B NE2 1 
ATOM   4450 N  N   . ALA B  1 225 ? 1.55935   -20.35756 69.81576  1.000 70.25577  ? 251 ALA B N   1 
ATOM   4451 C  CA  . ALA B  1 225 ? 2.77641   -21.10626 69.51610  1.000 71.82662  ? 251 ALA B CA  1 
ATOM   4452 C  C   . ALA B  1 225 ? 2.91598   -21.34610 68.01640  1.000 71.10612  ? 251 ALA B C   1 
ATOM   4453 O  O   . ALA B  1 225 ? 4.01498   -21.23311 67.45691  1.000 71.91352  ? 251 ALA B O   1 
ATOM   4454 C  CB  . ALA B  1 225 ? 2.77664   -22.43198 70.27627  1.000 73.56402  ? 251 ALA B CB  1 
ATOM   4455 N  N   . SER B  1 226 ? 1.80507   -21.66525 67.34657  1.000 69.24472  ? 252 SER B N   1 
ATOM   4456 C  CA  . SER B  1 226 ? 1.84765   -21.90621 65.90622  1.000 69.21708  ? 252 SER B CA  1 
ATOM   4457 C  C   . SER B  1 226 ? 2.21221   -20.63897 65.14320  1.000 69.74948  ? 252 SER B C   1 
ATOM   4458 O  O   . SER B  1 226 ? 2.99920   -20.68248 64.19103  1.000 70.57160  ? 252 SER B O   1 
ATOM   4459 C  CB  . SER B  1 226 ? 0.50392   -22.44611 65.41996  1.000 68.57207  ? 252 SER B CB  1 
ATOM   4460 O  OG  . SER B  1 226 ? -0.35117  -21.39143 65.01129  1.000 69.31898  ? 252 SER B OG  1 
ATOM   4461 N  N   . ASN B  1 227 ? 1.65953   -19.49544 65.55212  1.000 70.59360  ? 253 ASN B N   1 
ATOM   4462 C  CA  . ASN B  1 227 ? 2.00014   -18.24575 64.87604  1.000 72.67640  ? 253 ASN B CA  1 
ATOM   4463 C  C   . ASN B  1 227 ? 3.43652   -17.81943 65.16981  1.000 75.17678  ? 253 ASN B C   1 
ATOM   4464 O  O   . ASN B  1 227 ? 4.10205   -17.24355 64.29864  1.000 76.53672  ? 253 ASN B O   1 
ATOM   4465 C  CB  . ASN B  1 227 ? 1.00842   -17.15392 65.26951  1.000 72.41330  ? 253 ASN B CB  1 
ATOM   4466 C  CG  . ASN B  1 227 ? -0.39068  -17.43102 64.74775  1.000 71.88900  ? 253 ASN B CG  1 
ATOM   4467 O  OD1 . ASN B  1 227 ? -0.56672  -18.16728 63.77717  1.000 71.72700  ? 253 ASN B OD1 1 
ATOM   4468 N  ND2 . ASN B  1 227 ? -1.39379  -16.84904 65.39617  1.000 70.88165  ? 253 ASN B ND2 1 
ATOM   4469 N  N   . ARG B  1 228 ? 3.93837   -18.10976 66.37492  1.000 75.17299  ? 254 ARG B N   1 
ATOM   4470 C  CA  . ARG B  1 228 ? 5.33723   -17.82882 66.68294  1.000 76.34430  ? 254 ARG B CA  1 
ATOM   4471 C  C   . ARG B  1 228 ? 6.26928   -18.69130 65.84078  1.000 75.57342  ? 254 ARG B C   1 
ATOM   4472 O  O   . ARG B  1 228 ? 7.32503   -18.22431 65.39721  1.000 74.76679  ? 254 ARG B O   1 
ATOM   4473 C  CB  . ARG B  1 228 ? 5.59977   -18.04622 68.17313  1.000 77.60793  ? 254 ARG B CB  1 
ATOM   4474 C  CG  . ARG B  1 228 ? 7.02771   -17.75072 68.60244  1.000 81.04148  ? 254 ARG B CG  1 
ATOM   4475 C  CD  . ARG B  1 228 ? 7.22656   -18.00725 70.08748  1.000 83.47019  ? 254 ARG B CD  1 
ATOM   4476 N  NE  . ARG B  1 228 ? 6.34057   -17.18706 70.90881  1.000 84.72903  ? 254 ARG B NE  1 
ATOM   4477 C  CZ  . ARG B  1 228 ? 6.16283   -17.35752 72.21482  1.000 85.37050  ? 254 ARG B CZ  1 
ATOM   4478 N  NH1 . ARG B  1 228 ? 6.81278   -18.32065 72.85357  1.000 85.91914  ? 254 ARG B NH1 1 
ATOM   4479 N  NH2 . ARG B  1 228 ? 5.33637   -16.56460 72.88327  1.000 85.10712  ? 254 ARG B NH2 1 
ATOM   4480 N  N   . ALA B  1 229 ? 5.90015   -19.95510 65.61520  1.000 76.50771  ? 255 ALA B N   1 
ATOM   4481 C  CA  . ALA B  1 229 ? 6.67922   -20.79193 64.70804  1.000 78.33720  ? 255 ALA B CA  1 
ATOM   4482 C  C   . ALA B  1 229 ? 6.56539   -20.31074 63.26677  1.000 80.60116  ? 255 ALA B C   1 
ATOM   4483 O  O   . ALA B  1 229 ? 7.53085   -20.41752 62.50075  1.000 82.13841  ? 255 ALA B O   1 
ATOM   4484 C  CB  . ALA B  1 229 ? 6.23609   -22.25024 64.81887  1.000 78.46445  ? 255 ALA B CB  1 
ATOM   4485 N  N   . LYS B  1 230 ? 5.39958   -19.78437 62.88243  1.000 79.95342  ? 256 LYS B N   1 
ATOM   4486 C  CA  . LYS B  1 230 ? 5.23079   -19.24846 61.53623  1.000 81.14634  ? 256 LYS B CA  1 
ATOM   4487 C  C   . LYS B  1 230 ? 6.12783   -18.03936 61.30953  1.000 84.28175  ? 256 LYS B C   1 
ATOM   4488 O  O   . LYS B  1 230 ? 6.68410   -17.86615 60.21915  1.000 85.84256  ? 256 LYS B O   1 
ATOM   4489 C  CB  . LYS B  1 230 ? 3.76512   -18.88057 61.30239  1.000 79.23336  ? 256 LYS B CB  1 
ATOM   4490 C  CG  . LYS B  1 230 ? 3.06939   -19.70545 60.23655  1.000 79.36236  ? 256 LYS B CG  1 
ATOM   4491 C  CD  . LYS B  1 230 ? 1.62425   -19.98735 60.62896  1.000 78.47066  ? 256 LYS B CD  1 
ATOM   4492 C  CE  . LYS B  1 230 ? 0.98415   -21.01906 59.71015  1.000 77.99903  ? 256 LYS B CE  1 
ATOM   4493 N  NZ  . LYS B  1 230 ? -0.50203  -20.90245 59.71210  1.000 76.32916  ? 256 LYS B NZ  1 
ATOM   4494 N  N   . GLU B  1 231 ? 6.27299   -17.18967 62.32570  1.000 85.39907  ? 257 GLU B N   1 
ATOM   4495 C  CA  . GLU B  1 231 ? 7.12082   -16.00971 62.20818  1.000 88.23717  ? 257 GLU B CA  1 
ATOM   4496 C  C   . GLU B  1 231 ? 8.60786   -16.33662 62.32016  1.000 89.50722  ? 257 GLU B C   1 
ATOM   4497 O  O   . GLU B  1 231 ? 9.43786   -15.57185 61.81383  1.000 91.10718  ? 257 GLU B O   1 
ATOM   4498 C  CB  . GLU B  1 231 ? 6.72577   -14.97936 63.27531  1.000 89.97836  ? 257 GLU B CB  1 
ATOM   4499 C  CG  . GLU B  1 231 ? 7.49842   -13.66838 63.22849  1.000 92.43072  ? 257 GLU B CG  1 
ATOM   4500 C  CD  . GLU B  1 231 ? 6.91679   -12.67591 62.23906  1.000 93.57408  ? 257 GLU B CD  1 
ATOM   4501 O  OE1 . GLU B  1 231 ? 5.76451   -12.87489 61.80021  1.000 92.98451  ? 257 GLU B OE1 1 
ATOM   4502 O  OE2 . GLU B  1 231 ? 7.61321   -11.69468 61.90171  1.000 94.96478  ? 257 GLU B OE2 1 
ATOM   4503 N  N   . ALA B  1 232 ? 8.96162   -17.46199 62.94234  1.000 89.15671  ? 258 ALA B N   1 
ATOM   4504 C  CA  . ALA B  1 232 ? 10.35159  -17.78972 63.23516  1.000 88.66469  ? 258 ALA B CA  1 
ATOM   4505 C  C   . ALA B  1 232 ? 11.07295  -18.48945 62.09032  1.000 86.81146  ? 258 ALA B C   1 
ATOM   4506 O  O   . ALA B  1 232 ? 12.28834  -18.69427 62.18754  1.000 89.13231  ? 258 ALA B O   1 
ATOM   4507 C  CB  . ALA B  1 232 ? 10.43426  -18.66563 64.48948  1.000 88.29385  ? 258 ALA B CB  1 
ATOM   4508 N  N   . LYS B  1 233 ? 10.36124  -18.87093 61.02692  1.000 83.73512  ? 259 LYS B N   1 
ATOM   4509 C  CA  . LYS B  1 233 ? 10.96568  -19.46732 59.83228  1.000 82.96107  ? 259 LYS B CA  1 
ATOM   4510 C  C   . LYS B  1 233 ? 11.62164  -20.81550 60.12601  1.000 80.75823  ? 259 LYS B C   1 
ATOM   4511 O  O   . LYS B  1 233 ? 12.55705  -21.22232 59.43292  1.000 81.63673  ? 259 LYS B O   1 
ATOM   4512 C  CB  . LYS B  1 233 ? 11.98049  -18.51420 59.18902  1.000 85.36779  ? 259 LYS B CB  1 
ATOM   4513 C  CG  . LYS B  1 233 ? 11.43401  -17.68043 58.04252  1.000 84.67902  ? 259 LYS B CG  1 
ATOM   4514 C  CD  . LYS B  1 233 ? 11.13137  -18.53675 56.82466  1.000 82.95352  ? 259 LYS B CD  1 
ATOM   4515 C  CE  . LYS B  1 233 ? 12.25776  -18.45062 55.80630  1.000 82.15502  ? 259 LYS B CE  1 
ATOM   4516 N  NZ  . LYS B  1 233 ? 11.95863  -19.22352 54.57092  1.000 80.66003  ? 259 LYS B NZ  1 
ATOM   4517 N  N   . ASN B  1 234 ? 11.13732  -21.52965 61.14409  1.000 77.11542  ? 260 ASN B N   1 
ATOM   4518 C  CA  . ASN B  1 234 ? 11.72022  -22.81785 61.50184  1.000 74.82125  ? 260 ASN B CA  1 
ATOM   4519 C  C   . ASN B  1 234 ? 11.07777  -23.99519 60.77779  1.000 72.80104  ? 260 ASN B C   1 
ATOM   4520 O  O   . ASN B  1 234 ? 11.70200  -25.05826 60.68410  1.000 74.77090  ? 260 ASN B O   1 
ATOM   4521 C  CB  . ASN B  1 234 ? 11.63614  -23.04300 63.01661  1.000 73.34067  ? 260 ASN B CB  1 
ATOM   4522 C  CG  . ASN B  1 234 ? 10.26836  -22.72035 63.58336  1.000 70.33251  ? 260 ASN B CG  1 
ATOM   4523 O  OD1 . ASN B  1 234 ? 9.27992   -22.64989 62.85366  1.000 69.03500  ? 260 ASN B OD1 1 
ATOM   4524 N  ND2 . ASN B  1 234 ? 10.20458  -22.52638 64.89575  1.000 69.56849  ? 260 ASN B ND2 1 
ATOM   4525 N  N   . GLY B  1 235 ? 9.85570   -23.84143 60.27469  1.000 69.23213  ? 261 GLY B N   1 
ATOM   4526 C  CA  . GLY B  1 235 ? 9.23456   -24.86393 59.45714  1.000 68.07945  ? 261 GLY B CA  1 
ATOM   4527 C  C   . GLY B  1 235 ? 8.47562   -25.93985 60.20046  1.000 67.75743  ? 261 GLY B C   1 
ATOM   4528 O  O   . GLY B  1 235 ? 8.01171   -26.89445 59.56509  1.000 68.31166  ? 261 GLY B O   1 
ATOM   4529 N  N   . VAL B  1 236 ? 8.33606   -25.82711 61.51604  1.000 67.41303  ? 262 VAL B N   1 
ATOM   4530 C  CA  . VAL B  1 236 ? 7.57557   -26.79194 62.30142  1.000 66.72520  ? 262 VAL B CA  1 
ATOM   4531 C  C   . VAL B  1 236 ? 6.13716   -26.30115 62.40677  1.000 66.72488  ? 262 VAL B C   1 
ATOM   4532 O  O   . VAL B  1 236 ? 5.89061   -25.13982 62.75357  1.000 65.55400  ? 262 VAL B O   1 
ATOM   4533 C  CB  . VAL B  1 236 ? 8.20017   -26.98602 63.69393  1.000 65.12277  ? 262 VAL B CB  1 
ATOM   4534 C  CG1 . VAL B  1 236 ? 9.40952   -27.90931 63.60973  1.000 66.43824  ? 262 VAL B CG1 1 
ATOM   4535 C  CG2 . VAL B  1 236 ? 8.59256   -25.64937 64.29674  1.000 63.50386  ? 262 VAL B CG2 1 
ATOM   4536 N  N   . ASN B  1 237 ? 5.18437   -27.17392 62.08637  1.000 67.51835  ? 263 ASN B N   1 
ATOM   4537 C  CA  . ASN B  1 237 ? 3.76272   -26.85430 62.17493  1.000 69.50931  ? 263 ASN B CA  1 
ATOM   4538 C  C   . ASN B  1 237 ? 3.16955   -27.52850 63.40780  1.000 69.26101  ? 263 ASN B C   1 
ATOM   4539 O  O   . ASN B  1 237 ? 3.04058   -28.75384 63.45795  1.000 68.69715  ? 263 ASN B O   1 
ATOM   4540 C  CB  . ASN B  1 237 ? 3.02358   -27.23847 60.88688  1.000 72.52693  ? 263 ASN B CB  1 
ATOM   4541 C  CG  . ASN B  1 237 ? 3.34920   -28.64711 60.38593  1.000 78.60399  ? 263 ASN B CG  1 
ATOM   4542 O  OD1 . ASN B  1 237 ? 3.34489   -29.62856 61.13065  1.000 83.29653  ? 263 ASN B OD1 1 
ATOM   4543 N  ND2 . ASN B  1 237 ? 3.61708   -28.74248 59.09353  1.000 80.26525  ? 263 ASN B ND2 1 
ATOM   4544 N  N   . VAL B  1 238 ? 2.82887   -26.72977 64.40995  1.000 69.44108  ? 264 VAL B N   1 
ATOM   4545 C  CA  . VAL B  1 238 ? 2.07032   -27.21676 65.55471  1.000 70.13565  ? 264 VAL B CA  1 
ATOM   4546 C  C   . VAL B  1 238 ? 0.59247   -26.93832 65.31755  1.000 69.04779  ? 264 VAL B C   1 
ATOM   4547 O  O   . VAL B  1 238 ? 0.21314   -25.84936 64.86960  1.000 67.84183  ? 264 VAL B O   1 
ATOM   4548 C  CB  . VAL B  1 238 ? 2.56954   -26.58951 66.87041  1.000 71.77574  ? 264 VAL B CB  1 
ATOM   4549 C  CG1 . VAL B  1 238 ? 2.72407   -25.08420 66.74756  1.000 72.90129  ? 264 VAL B CG1 1 
ATOM   4550 C  CG2 . VAL B  1 238 ? 1.60652   -26.91939 68.00399  1.000 70.79345  ? 264 VAL B CG2 1 
ATOM   4551 N  N   . SER B  1 239 ? -0.23871  -27.93694 65.59627  1.000 68.44526  ? 265 SER B N   1 
ATOM   4552 C  CA  . SER B  1 239 ? -1.66727  -27.85902 65.35135  1.000 66.75125  ? 265 SER B CA  1 
ATOM   4553 C  C   . SER B  1 239 ? -2.41815  -28.21028 66.62506  1.000 63.94222  ? 265 SER B C   1 
ATOM   4554 O  O   . SER B  1 239 ? -1.88649  -28.86418 67.52553  1.000 63.14082  ? 265 SER B O   1 
ATOM   4555 C  CB  . SER B  1 239 ? -2.08762  -28.78568 64.20486  1.000 67.95997  ? 265 SER B CB  1 
ATOM   4556 O  OG  . SER B  1 239 ? -1.15583  -28.73278 63.13702  1.000 69.53336  ? 265 SER B OG  1 
ATOM   4557 N  N   . PHE B  1 240 ? -3.66730  -27.75938 66.68494  1.000 62.60346  ? 266 PHE B N   1 
ATOM   4558 C  CA  . PHE B  1 240 ? -4.52810  -27.94814 67.84143  1.000 60.86514  ? 266 PHE B CA  1 
ATOM   4559 C  C   . PHE B  1 240 ? -5.73364  -28.78990 67.44975  1.000 59.18951  ? 266 PHE B C   1 
ATOM   4560 O  O   . PHE B  1 240 ? -6.33864  -28.57356 66.39502  1.000 59.25240  ? 266 PHE B O   1 
ATOM   4561 C  CB  . PHE B  1 240 ? -4.98553  -26.60150 68.40897  1.000 59.76999  ? 266 PHE B CB  1 
ATOM   4562 C  CG  . PHE B  1 240 ? -5.87798  -26.72118 69.60990  1.000 58.53942  ? 266 PHE B CG  1 
ATOM   4563 C  CD1 . PHE B  1 240 ? -5.34604  -26.98848 70.86021  1.000 58.48575  ? 266 PHE B CD1 1 
ATOM   4564 C  CD2 . PHE B  1 240 ? -7.24867  -26.56214 69.48959  1.000 56.83873  ? 266 PHE B CD2 1 
ATOM   4565 C  CE1 . PHE B  1 240 ? -6.16462  -27.09726 71.96756  1.000 56.54152  ? 266 PHE B CE1 1 
ATOM   4566 C  CE2 . PHE B  1 240 ? -8.07235  -26.67065 70.59308  1.000 55.57265  ? 266 PHE B CE2 1 
ATOM   4567 C  CZ  . PHE B  1 240 ? -7.52972  -26.93835 71.83342  1.000 55.18763  ? 266 PHE B CZ  1 
ATOM   4568 N  N   . SER B  1 241 ? -6.08174  -29.74544 68.30826  1.000 57.60503  ? 267 SER B N   1 
ATOM   4569 C  CA  . SER B  1 241 ? -7.15759  -30.68902 68.04132  1.000 55.83553  ? 267 SER B CA  1 
ATOM   4570 C  C   . SER B  1 241 ? -8.07161  -30.79094 69.25251  1.000 55.69968  ? 267 SER B C   1 
ATOM   4571 O  O   . SER B  1 241 ? -7.59818  -30.94829 70.38572  1.000 56.46111  ? 267 SER B O   1 
ATOM   4572 C  CB  . SER B  1 241 ? -6.60274  -32.07463 67.68624  1.000 55.38618  ? 267 SER B CB  1 
ATOM   4573 O  OG  . SER B  1 241 ? -7.61242  -33.06578 67.77253  1.000 54.41870  ? 267 SER B OG  1 
ATOM   4574 N  N   . ILE B  1 242 ? -9.37366  -30.68460 69.00186  1.000 53.18196  ? 268 ILE B N   1 
ATOM   4575 C  CA  . ILE B  1 242 ? -10.40933 -30.99855 69.98341  1.000 50.63386  ? 268 ILE B CA  1 
ATOM   4576 C  C   . ILE B  1 242 ? -10.85509 -32.43067 69.72525  1.000 49.08819  ? 268 ILE B C   1 
ATOM   4577 O  O   . ILE B  1 242 ? -11.54374 -32.68538 68.72073  1.000 48.59069  ? 268 ILE B O   1 
ATOM   4578 C  CB  . ILE B  1 242 ? -11.58917 -30.02224 69.88767  1.000 48.91086  ? 268 ILE B CB  1 
ATOM   4579 C  CG1 . ILE B  1 242 ? -11.08901 -28.57567 69.87938  1.000 47.90789  ? 268 ILE B CG1 1 
ATOM   4580 C  CG2 . ILE B  1 242 ? -12.56507 -30.24919 71.03377  1.000 48.97456  ? 268 ILE B CG2 1 
ATOM   4581 C  CD1 . ILE B  1 242 ? -12.19034 -27.54686 69.72534  1.000 47.13479  ? 268 ILE B CD1 1 
ATOM   4582 N  N   . PRO B  1 243 ? -10.49297 -33.39351 70.57254  1.000 48.22910  ? 269 PRO B N   1 
ATOM   4583 C  CA  . PRO B  1 243 ? -10.71867 -34.80333 70.24193  1.000 48.36935  ? 269 PRO B CA  1 
ATOM   4584 C  C   . PRO B  1 243 ? -12.19671 -35.15752 70.17356  1.000 49.75434  ? 269 PRO B C   1 
ATOM   4585 O  O   . PRO B  1 243 ? -13.06898 -34.44194 70.67147  1.000 50.68963  ? 269 PRO B O   1 
ATOM   4586 C  CB  . PRO B  1 243 ? -10.02115 -35.55290 71.38341  1.000 49.16416  ? 269 PRO B CB  1 
ATOM   4587 C  CG  . PRO B  1 243 ? -9.04907  -34.56122 71.94956  1.000 49.24673  ? 269 PRO B CG  1 
ATOM   4588 C  CD  . PRO B  1 243 ? -9.73029  -33.23662 71.82171  1.000 48.35563  ? 269 PRO B CD  1 
ATOM   4589 N  N   . LYS B  1 244 ? -12.46275 -36.30302 69.53854  1.000 49.32811  ? 270 LYS B N   1 
ATOM   4590 C  CA  . LYS B  1 244 ? -13.83798 -36.72954 69.30130  1.000 50.72409  ? 270 LYS B CA  1 
ATOM   4591 C  C   . LYS B  1 244 ? -14.55468 -37.09668 70.59449  1.000 50.21929  ? 270 LYS B C   1 
ATOM   4592 O  O   . LYS B  1 244 ? -15.78126 -36.96827 70.67592  1.000 50.51141  ? 270 LYS B O   1 
ATOM   4593 C  CB  . LYS B  1 244 ? -13.85953 -37.91073 68.32953  1.000 51.52015  ? 270 LYS B CB  1 
ATOM   4594 C  CG  . LYS B  1 244 ? -13.16169 -39.15880 68.84893  1.000 53.61884  ? 270 LYS B CG  1 
ATOM   4595 C  CD  . LYS B  1 244 ? -12.75009 -40.08147 67.71345  1.000 56.30182  ? 270 LYS B CD  1 
ATOM   4596 C  CE  . LYS B  1 244 ? -12.22569 -41.40617 68.24430  1.000 58.04799  ? 270 LYS B CE  1 
ATOM   4597 N  NZ  . LYS B  1 244 ? -11.63555 -42.24436 67.16472  1.000 59.91475  ? 270 LYS B NZ  1 
ATOM   4598 N  N   . GLU B  1 245 ? -13.81906 -37.55157 71.60987  1.000 49.79996  ? 271 GLU B N   1 
ATOM   4599 C  CA  . GLU B  1 245 ? -14.43426 -37.91020 72.88283  1.000 49.80487  ? 271 GLU B CA  1 
ATOM   4600 C  C   . GLU B  1 245 ? -14.88707 -36.69837 73.68447  1.000 47.69330  ? 271 GLU B C   1 
ATOM   4601 O  O   . GLU B  1 245 ? -15.50161 -36.87444 74.74277  1.000 48.41108  ? 271 GLU B O   1 
ATOM   4602 C  CB  . GLU B  1 245 ? -13.46445 -38.74665 73.72093  1.000 52.03103  ? 271 GLU B CB  1 
ATOM   4603 C  CG  . GLU B  1 245 ? -13.00037 -40.02950 73.04948  1.000 54.38575  ? 271 GLU B CG  1 
ATOM   4604 C  CD  . GLU B  1 245 ? -11.71925 -39.84579 72.25841  1.000 55.80791  ? 271 GLU B CD  1 
ATOM   4605 O  OE1 . GLU B  1 245 ? -11.17857 -38.71973 72.25052  1.000 55.70468  ? 271 GLU B OE1 1 
ATOM   4606 O  OE2 . GLU B  1 245 ? -11.25161 -40.82882 71.64629  1.000 56.29495  ? 271 GLU B OE2 1 
ATOM   4607 N  N   . GLY B  1 246 ? -14.60707 -35.49051 73.21558  1.000 46.11269  ? 272 GLY B N   1 
ATOM   4608 C  CA  . GLY B  1 246 ? -14.96617 -34.27400 73.91523  1.000 45.42664  ? 272 GLY B CA  1 
ATOM   4609 C  C   . GLY B  1 246 ? -13.75278 -33.62059 74.55424  1.000 46.40293  ? 272 GLY B C   1 
ATOM   4610 O  O   . GLY B  1 246 ? -12.62920 -34.12317 74.49804  1.000 48.71139  ? 272 GLY B O   1 
ATOM   4611 N  N   . ALA B  1 247 ? -14.01117 -32.47123 75.17110  1.000 45.57723  ? 273 ALA B N   1 
ATOM   4612 C  CA  . ALA B  1 247 ? -12.96896 -31.71351 75.84659  1.000 45.34854  ? 273 ALA B CA  1 
ATOM   4613 C  C   . ALA B  1 247 ? -13.62586 -30.73547 76.80623  1.000 47.16428  ? 273 ALA B C   1 
ATOM   4614 O  O   . ALA B  1 247 ? -14.82556 -30.46138 76.71740  1.000 47.11128  ? 273 ALA B O   1 
ATOM   4615 C  CB  . ALA B  1 247 ? -12.07180 -30.97216 74.84949  1.000 45.17788  ? 273 ALA B CB  1 
ATOM   4616 N  N   . MET B  1 248 ? -12.82364 -30.21695 77.73145  1.000 47.72495  ? 274 MET B N   1 
ATOM   4617 C  CA  . MET B  1 248 ? -13.30195 -29.19217 78.64649  1.000 47.07763  ? 274 MET B CA  1 
ATOM   4618 C  C   . MET B  1 248 ? -13.37525 -27.85503 77.92267  1.000 45.22388  ? 274 MET B C   1 
ATOM   4619 O  O   . MET B  1 248 ? -12.42650 -27.45507 77.24102  1.000 41.99938  ? 274 MET B O   1 
ATOM   4620 C  CB  . MET B  1 248 ? -12.38963 -29.07839 79.86651  1.000 48.41157  ? 274 MET B CB  1 
ATOM   4621 C  CG  . MET B  1 248 ? -12.68404 -27.85329 80.71931  1.000 50.65106  ? 274 MET B CG  1 
ATOM   4622 S  SD  . MET B  1 248 ? -11.50650 -27.58302 82.05418  1.000 53.71247  ? 274 MET B SD  1 
ATOM   4623 C  CE  . MET B  1 248 ? -11.92757 -25.90744 82.52981  1.000 54.21428  ? 274 MET B CE  1 
ATOM   4624 N  N   . ALA B  1 249 ? -14.50328 -27.16873 78.06728  1.000 45.52961  ? 275 ALA B N   1 
ATOM   4625 C  CA  . ALA B  1 249 ? -14.70379 -25.85281 77.48250  1.000 44.53660  ? 275 ALA B CA  1 
ATOM   4626 C  C   . ALA B  1 249 ? -14.79918 -24.81079 78.58752  1.000 46.38706  ? 275 ALA B C   1 
ATOM   4627 O  O   . ALA B  1 249 ? -15.40134 -25.05779 79.63682  1.000 49.21869  ? 275 ALA B O   1 
ATOM   4628 C  CB  . ALA B  1 249 ? -15.96735 -25.81963 76.61836  1.000 42.23730  ? 275 ALA B CB  1 
ATOM   4629 N  N   . PHE B  1 250 ? -14.18922 -23.65276 78.35374  1.000 45.23865  ? 276 PHE B N   1 
ATOM   4630 C  CA  . PHE B  1 250 ? -14.28541 -22.52157 79.26181  1.000 45.38399  ? 276 PHE B CA  1 
ATOM   4631 C  C   . PHE B  1 250 ? -14.74679 -21.30338 78.47674  1.000 44.97019  ? 276 PHE B C   1 
ATOM   4632 O  O   . PHE B  1 250 ? -14.56083 -21.21665 77.26046  1.000 46.38274  ? 276 PHE B O   1 
ATOM   4633 C  CB  . PHE B  1 250 ? -12.95207 -22.23437 79.96735  1.000 47.31984  ? 276 PHE B CB  1 
ATOM   4634 C  CG  . PHE B  1 250 ? -11.76302 -22.25969 79.05342  1.000 48.90130  ? 276 PHE B CG  1 
ATOM   4635 C  CD1 . PHE B  1 250 ? -11.34407 -21.10792 78.40998  1.000 48.44700  ? 276 PHE B CD1 1 
ATOM   4636 C  CD2 . PHE B  1 250 ? -11.05878 -23.43371 78.84305  1.000 49.56440  ? 276 PHE B CD2 1 
ATOM   4637 C  CE1 . PHE B  1 250 ? -10.24879 -21.12740 77.57091  1.000 48.75347  ? 276 PHE B CE1 1 
ATOM   4638 C  CE2 . PHE B  1 250 ? -9.96325  -23.45928 78.00338  1.000 49.17631  ? 276 PHE B CE2 1 
ATOM   4639 C  CZ  . PHE B  1 250 ? -9.55688  -22.30424 77.36720  1.000 49.00506  ? 276 PHE B CZ  1 
ATOM   4640 N  N   . PHE B  1 251 ? -15.35593 -20.35796 79.18584  1.000 44.18106  ? 277 PHE B N   1 
ATOM   4641 C  CA  . PHE B  1 251 ? -16.02001 -19.23123 78.55019  1.000 44.78770  ? 277 PHE B CA  1 
ATOM   4642 C  C   . PHE B  1 251 ? -15.58433 -17.91823 79.17807  1.000 46.38987  ? 277 PHE B C   1 
ATOM   4643 O  O   . PHE B  1 251 ? -15.48212 -17.80480 80.40337  1.000 50.24344  ? 277 PHE B O   1 
ATOM   4644 C  CB  . PHE B  1 251 ? -17.54627 -19.34951 78.65833  1.000 44.68965  ? 277 PHE B CB  1 
ATOM   4645 C  CG  . PHE B  1 251 ? -18.12933 -20.47453 77.85625  1.000 44.63937  ? 277 PHE B CG  1 
ATOM   4646 C  CD1 . PHE B  1 251 ? -18.71271 -20.23226 76.62470  1.000 44.75928  ? 277 PHE B CD1 1 
ATOM   4647 C  CD2 . PHE B  1 251 ? -18.10977 -21.77192 78.34029  1.000 45.43667  ? 277 PHE B CD2 1 
ATOM   4648 C  CE1 . PHE B  1 251 ? -19.25617 -21.26506 75.88451  1.000 45.85151  ? 277 PHE B CE1 1 
ATOM   4649 C  CE2 . PHE B  1 251 ? -18.65066 -22.80884 77.60552  1.000 46.27593  ? 277 PHE B CE2 1 
ATOM   4650 C  CZ  . PHE B  1 251 ? -19.22473 -22.55516 76.37579  1.000 46.60397  ? 277 PHE B CZ  1 
ATOM   4651 N  N   . ASP B  1 252 ? -15.32696 -16.93200 78.32595  1.000 44.29137  ? 278 ASP B N   1 
ATOM   4652 C  CA  . ASP B  1 252 ? -15.31627 -15.53924 78.73937  1.000 43.12077  ? 278 ASP B CA  1 
ATOM   4653 C  C   . ASP B  1 252 ? -16.71283 -14.97223 78.52626  1.000 42.53494  ? 278 ASP B C   1 
ATOM   4654 O  O   . ASP B  1 252 ? -17.40110 -15.33126 77.56665  1.000 43.11137  ? 278 ASP B O   1 
ATOM   4655 C  CB  . ASP B  1 252 ? -14.28175 -14.73635 77.94912  1.000 42.88448  ? 278 ASP B CB  1 
ATOM   4656 C  CG  . ASP B  1 252 ? -12.85730 -15.04302 78.37404  1.000 43.79439  ? 278 ASP B CG  1 
ATOM   4657 O  OD1 . ASP B  1 252 ? -12.64931 -15.39649 79.55417  1.000 43.38795  ? 278 ASP B OD1 1 
ATOM   4658 O  OD2 . ASP B  1 252 ? -11.94473 -14.92837 77.52886  1.000 43.88806  ? 278 ASP B OD2 1 
ATOM   4659 N  N   . VAL B  1 253 ? -17.14524 -14.10696 79.43890  1.000 40.82740  ? 279 VAL B N   1 
ATOM   4660 C  CA  . VAL B  1 253 ? -18.50986 -13.59863 79.41510  1.000 40.19794  ? 279 VAL B CA  1 
ATOM   4661 C  C   . VAL B  1 253 ? -18.50582 -12.09880 79.66388  1.000 37.68718  ? 279 VAL B C   1 
ATOM   4662 O  O   . VAL B  1 253 ? -17.64841 -11.56630 80.37400  1.000 47.42098  ? 279 VAL B O   1 
ATOM   4663 C  CB  . VAL B  1 253 ? -19.41012 -14.30759 80.45329  1.000 41.72947  ? 279 VAL B CB  1 
ATOM   4664 C  CG1 . VAL B  1 253 ? -19.55008 -15.78887 80.12927  1.000 42.00343  ? 279 VAL B CG1 1 
ATOM   4665 C  CG2 . VAL B  1 253 ? -18.85594 -14.11511 81.85749  1.000 42.03621  ? 279 VAL B CG2 1 
ATOM   4666 N  N   . PHE B  1 254 ? -19.47563 -11.41924 79.06082  1.000 37.79865  ? 280 PHE B N   1 
ATOM   4667 C  CA  . PHE B  1 254 ? -19.76652 -10.03124 79.37707  1.000 40.89927  ? 280 PHE B CA  1 
ATOM   4668 C  C   . PHE B  1 254 ? -20.72656 -9.97428  80.55761  1.000 42.90097  ? 280 PHE B C   1 
ATOM   4669 O  O   . PHE B  1 254 ? -21.69250 -10.74248 80.62782  1.000 42.74272  ? 280 PHE B O   1 
ATOM   4670 C  CB  . PHE B  1 254 ? -20.37449 -9.31187  78.17147  1.000 41.03161  ? 280 PHE B CB  1 
ATOM   4671 C  CG  . PHE B  1 254 ? -19.37891 -8.52623  77.36386  1.000 41.28150  ? 280 PHE B CG  1 
ATOM   4672 C  CD1 . PHE B  1 254 ? -19.25864 -7.15601  77.53080  1.000 41.18067  ? 280 PHE B CD1 1 
ATOM   4673 C  CD2 . PHE B  1 254 ? -18.56997 -9.15566  76.43232  1.000 37.22466  ? 280 PHE B CD2 1 
ATOM   4674 C  CE1 . PHE B  1 254 ? -18.34632 -6.42903  76.78761  1.000 40.60052  ? 280 PHE B CE1 1 
ATOM   4675 C  CE2 . PHE B  1 254 ? -17.65563 -8.43409  75.68619  1.000 37.07090  ? 280 PHE B CE2 1 
ATOM   4676 C  CZ  . PHE B  1 254 ? -17.54499 -7.06899  75.86293  1.000 40.06852  ? 280 PHE B CZ  1 
ATOM   4677 N  N   . ALA B  1 255 ? -20.44473 -9.06631  81.48931  1.000 43.68293  ? 281 ALA B N   1 
ATOM   4678 C  CA  . ALA B  1 255 ? -21.27531 -8.87627  82.66818  1.000 45.09253  ? 281 ALA B CA  1 
ATOM   4679 C  C   . ALA B  1 255 ? -21.14935 -7.42994  83.12064  1.000 45.97062  ? 281 ALA B C   1 
ATOM   4680 O  O   . ALA B  1 255 ? -20.18033 -6.74015  82.79306  1.000 45.33092  ? 281 ALA B O   1 
ATOM   4681 C  CB  . ALA B  1 255 ? -20.88258 -9.83510  83.79867  1.000 45.01630  ? 281 ALA B CB  1 
ATOM   4682 N  N   . MET B  1 256 ? -22.14380 -6.97308  83.88078  1.000 48.32655  ? 282 MET B N   1 
ATOM   4683 C  CA  . MET B  1 256 ? -22.13751 -5.58919  84.31620  1.000 52.10310  ? 282 MET B CA  1 
ATOM   4684 C  C   . MET B  1 256 ? -22.02136 -5.49606  85.83353  1.000 53.92980  ? 282 MET B C   1 
ATOM   4685 O  O   . MET B  1 256 ? -22.63833 -6.28759  86.55581  1.000 53.18407  ? 282 MET B O   1 
ATOM   4686 C  CB  . MET B  1 256 ? -23.40353 -4.85194  83.84358  1.000 54.67659  ? 282 MET B CB  1 
ATOM   4687 C  CG  . MET B  1 256 ? -24.70449 -5.32853  84.46621  1.000 57.54948  ? 282 MET B CG  1 
ATOM   4688 S  SD  . MET B  1 256 ? -26.13975 -4.49172  83.76493  1.000 60.93239  ? 282 MET B SD  1 
ATOM   4689 C  CE  . MET B  1 256 ? -25.48237 -2.84453  83.51053  1.000 61.37245  ? 282 MET B CE  1 
ATOM   4690 N  N   . PRO B  1 257 ? -21.22239 -4.56122  86.34192  1.000 55.68588  ? 283 PRO B N   1 
ATOM   4691 C  CA  . PRO B  1 257 ? -21.10092 -4.40074  87.79413  1.000 57.18210  ? 283 PRO B CA  1 
ATOM   4692 C  C   . PRO B  1 257 ? -22.39643 -3.90033  88.41494  1.000 58.37354  ? 283 PRO B C   1 
ATOM   4693 O  O   . PRO B  1 257 ? -23.26851 -3.33853  87.74851  1.000 57.29965  ? 283 PRO B O   1 
ATOM   4694 C  CB  . PRO B  1 257 ? -19.97730 -3.36840  87.94785  1.000 57.50424  ? 283 PRO B CB  1 
ATOM   4695 C  CG  . PRO B  1 257 ? -19.22323 -3.42653  86.65268  1.000 56.23366  ? 283 PRO B CG  1 
ATOM   4696 C  CD  . PRO B  1 257 ? -20.25748 -3.72383  85.61077  1.000 55.48999  ? 283 PRO B CD  1 
ATOM   4697 N  N   . ALA B  1 258 ? -22.50666 -4.11223  89.72885  1.000 61.55752  ? 284 ALA B N   1 
ATOM   4698 C  CA  . ALA B  1 258 ? -23.72063 -3.74591  90.44878  1.000 64.22201  ? 284 ALA B CA  1 
ATOM   4699 C  C   . ALA B  1 258 ? -23.91625 -2.23860  90.54248  1.000 66.06014  ? 284 ALA B C   1 
ATOM   4700 O  O   . ALA B  1 258 ? -25.05571 -1.78364  90.68857  1.000 67.15410  ? 284 ALA B O   1 
ATOM   4701 C  CB  . ALA B  1 258 ? -23.70520 -4.35569  91.85125  1.000 65.71287  ? 284 ALA B CB  1 
ATOM   4702 N  N   . ASP B  1 259 ? -22.83964 -1.45633  90.46145  1.000 66.11383  ? 285 ASP B N   1 
ATOM   4703 C  CA  . ASP B  1 259 ? -22.90961 -0.00431  90.56693  1.000 68.15626  ? 285 ASP B CA  1 
ATOM   4704 C  C   . ASP B  1 259 ? -22.76155 0.68286   89.21346  1.000 65.92504  ? 285 ASP B C   1 
ATOM   4705 O  O   . ASP B  1 259 ? -22.19036 1.77595   89.13170  1.000 65.66759  ? 285 ASP B O   1 
ATOM   4706 C  CB  . ASP B  1 259 ? -21.84578 0.50369   91.53936  1.000 71.95326  ? 285 ASP B CB  1 
ATOM   4707 C  CG  . ASP B  1 259 ? -20.43995 0.14467   91.10233  1.000 75.40852  ? 285 ASP B CG  1 
ATOM   4708 O  OD1 . ASP B  1 259 ? -19.63916 1.06974   90.85169  1.000 78.54895  ? 285 ASP B OD1 1 
ATOM   4709 O  OD2 . ASP B  1 259 ? -20.13587 -1.06315  91.00555  1.000 77.03440  ? 285 ASP B OD2 1 
ATOM   4710 N  N   . ALA B  1 260 ? -23.26879 0.06342   88.14998  1.000 64.69967  ? 286 ALA B N   1 
ATOM   4711 C  CA  . ALA B  1 260 ? -23.12336 0.62198   86.81282  1.000 63.98243  ? 286 ALA B CA  1 
ATOM   4712 C  C   . ALA B  1 260 ? -23.90035 1.92650   86.69036  1.000 64.60186  ? 286 ALA B C   1 
ATOM   4713 O  O   . ALA B  1 260 ? -25.07702 2.00091   87.05706  1.000 66.56873  ? 286 ALA B O   1 
ATOM   4714 C  CB  . ALA B  1 260 ? -23.60262 -0.38058  85.76473  1.000 64.24370  ? 286 ALA B CB  1 
ATOM   4715 N  N   . LYS B  1 261 ? -23.23534 2.95890   86.17168  1.000 63.62339  ? 287 LYS B N   1 
ATOM   4716 C  CA  . LYS B  1 261 ? -23.88485 4.25338   86.00251  1.000 64.58620  ? 287 LYS B CA  1 
ATOM   4717 C  C   . LYS B  1 261 ? -24.69347 4.31084   84.71306  1.000 65.18869  ? 287 LYS B C   1 
ATOM   4718 O  O   . LYS B  1 261 ? -25.76006 4.93535   84.67069  1.000 65.75379  ? 287 LYS B O   1 
ATOM   4719 C  CB  . LYS B  1 261 ? -22.84094 5.36862   86.01684  1.000 64.81760  ? 287 LYS B CB  1 
ATOM   4720 C  CG  . LYS B  1 261 ? -22.11508 5.53516   87.34647  1.000 66.61604  ? 287 LYS B CG  1 
ATOM   4721 C  CD  . LYS B  1 261 ? -22.53980 6.81088   88.06035  1.000 67.86575  ? 287 LYS B CD  1 
ATOM   4722 C  CE  . LYS B  1 261 ? -22.64230 6.59943   89.56227  1.000 68.00675  ? 287 LYS B CE  1 
ATOM   4723 N  NZ  . LYS B  1 261 ? -21.49987 5.79844   90.08177  1.000 67.33487  ? 287 LYS B NZ  1 
ATOM   4724 N  N   . ASN B  1 262 ? -24.20757 3.66549   83.65734  1.000 64.92778  ? 288 ASN B N   1 
ATOM   4725 C  CA  . ASN B  1 262 ? -24.83264 3.71911   82.33908  1.000 66.13649  ? 288 ASN B CA  1 
ATOM   4726 C  C   . ASN B  1 262 ? -25.37417 2.33191   82.00957  1.000 66.95979  ? 288 ASN B C   1 
ATOM   4727 O  O   . ASN B  1 262 ? -24.76479 1.56663   81.25425  1.000 65.06065  ? 288 ASN B O   1 
ATOM   4728 C  CB  . ASN B  1 262 ? -23.82771 4.22184   81.30657  1.000 65.50926  ? 288 ASN B CB  1 
ATOM   4729 C  CG  . ASN B  1 262 ? -23.01318 5.39664   81.81754  1.000 65.94500  ? 288 ASN B CG  1 
ATOM   4730 O  OD1 . ASN B  1 262 ? -23.48676 6.53272   81.82894  1.000 66.39619  ? 288 ASN B OD1 1 
ATOM   4731 N  ND2 . ASN B  1 262 ? -21.78092 5.12996   82.23654  1.000 65.83449  ? 288 ASN B ND2 1 
ATOM   4732 N  N   . LYS B  1 263 ? -26.53399 2.01269   82.59236  1.000 69.31700  ? 289 LYS B N   1 
ATOM   4733 C  CA  . LYS B  1 263 ? -27.16226 0.72266   82.34351  1.000 69.71407  ? 289 LYS B CA  1 
ATOM   4734 C  C   . LYS B  1 263 ? -27.73941 0.64425   80.93534  1.000 68.62072  ? 289 LYS B C   1 
ATOM   4735 O  O   . LYS B  1 263 ? -27.59190 -0.38420  80.26183  1.000 67.99997  ? 289 LYS B O   1 
ATOM   4736 C  CB  . LYS B  1 263 ? -28.23952 0.46802   83.41078  1.000 72.16719  ? 289 LYS B CB  1 
ATOM   4737 C  CG  . LYS B  1 263 ? -28.74732 -0.95159  83.51016  1.000 72.21822  ? 289 LYS B CG  1 
ATOM   4738 C  CD  . LYS B  1 263 ? -29.20717 -1.24534  84.94283  1.000 73.75708  ? 289 LYS B CD  1 
ATOM   4739 C  CE  . LYS B  1 263 ? -30.00724 -2.54124  85.03255  1.000 73.66316  ? 289 LYS B CE  1 
ATOM   4740 N  NZ  . LYS B  1 263 ? -31.09945 -2.64315  84.01924  1.000 73.23675  ? 289 LYS B NZ  1 
ATOM   4741 N  N   . ASP B  1 264 ? -28.41432 1.70628   80.48988  1.000 67.50933  ? 290 ASP B N   1 
ATOM   4742 C  CA  . ASP B  1 264 ? -29.02843 1.70509   79.16275  1.000 65.68129  ? 290 ASP B CA  1 
ATOM   4743 C  C   . ASP B  1 264 ? -27.98248 1.56730   78.06235  1.000 62.29570  ? 290 ASP B C   1 
ATOM   4744 O  O   . ASP B  1 264 ? -28.17554 0.80603   77.10759  1.000 61.51563  ? 290 ASP B O   1 
ATOM   4745 C  CB  . ASP B  1 264 ? -29.85087 2.98540   78.96560  1.000 67.86904  ? 290 ASP B CB  1 
ATOM   4746 C  CG  . ASP B  1 264 ? -30.97845 2.81841   77.96927  1.000 70.28879  ? 290 ASP B CG  1 
ATOM   4747 O  OD1 . ASP B  1 264 ? -32.07472 2.38373   78.38058  1.000 71.80830  ? 290 ASP B OD1 1 
ATOM   4748 O  OD2 . ASP B  1 264 ? -30.77653 3.11220   76.76923  1.000 70.11923  ? 290 ASP B OD2 1 
ATOM   4749 N  N   . GLU B  1 265 ? -26.86667 2.29305   78.18500  1.000 60.42146  ? 291 GLU B N   1 
ATOM   4750 C  CA  . GLU B  1 265 ? -25.77059 2.18023   77.22610  1.000 58.11929  ? 291 GLU B CA  1 
ATOM   4751 C  C   . GLU B  1 265 ? -25.13212 0.80151   77.27570  1.000 54.19832  ? 291 GLU B C   1 
ATOM   4752 O  O   . GLU B  1 265 ? -24.72565 0.25833   76.24082  1.000 53.10280  ? 291 GLU B O   1 
ATOM   4753 C  CB  . GLU B  1 265 ? -24.71069 3.23685   77.51585  1.000 59.64797  ? 291 GLU B CB  1 
ATOM   4754 C  CG  . GLU B  1 265 ? -25.21272 4.66793   77.49409  1.000 62.08869  ? 291 GLU B CG  1 
ATOM   4755 C  CD  . GLU B  1 265 ? -25.85873 5.09083   78.80146  1.000 64.93881  ? 291 GLU B CD  1 
ATOM   4756 O  OE1 . GLU B  1 265 ? -25.58463 6.21858   79.25943  1.000 66.11348  ? 291 GLU B OE1 1 
ATOM   4757 O  OE2 . GLU B  1 265 ? -26.64229 4.30317   79.37121  1.000 65.39513  ? 291 GLU B OE2 1 
ATOM   4758 N  N   . ALA B  1 266 ? -25.01360 0.23024   78.47657  1.000 51.80573  ? 292 ALA B N   1 
ATOM   4759 C  CA  . ALA B  1 266 ? -24.49889 -1.12656  78.59875  1.000 48.72896  ? 292 ALA B CA  1 
ATOM   4760 C  C   . ALA B  1 266 ? -25.38279 -2.11140  77.84790  1.000 48.29794  ? 292 ALA B C   1 
ATOM   4761 O  O   . ALA B  1 266 ? -24.88105 -2.97419  77.12082  1.000 46.93492  ? 292 ALA B O   1 
ATOM   4762 C  CB  . ALA B  1 266 ? -24.38469 -1.50944  80.07266  1.000 48.32665  ? 292 ALA B CB  1 
ATOM   4763 N  N   . TYR B  1 267 ? -26.70410 -1.98817  77.99586  1.000 47.08830  ? 293 TYR B N   1 
ATOM   4764 C  CA  . TYR B  1 267 ? -27.60445 -2.88638  77.27865  1.000 46.52889  ? 293 TYR B CA  1 
ATOM   4765 C  C   . TYR B  1 267 ? -27.55591 -2.63395  75.77600  1.000 46.17012  ? 293 TYR B C   1 
ATOM   4766 O  O   . TYR B  1 267 ? -27.67056 -3.57413  74.97940  1.000 47.20592  ? 293 TYR B O   1 
ATOM   4767 C  CB  . TYR B  1 267 ? -29.02872 -2.74148  77.81254  1.000 46.12865  ? 293 TYR B CB  1 
ATOM   4768 C  CG  . TYR B  1 267 ? -29.25883 -3.52632  79.08038  1.000 46.23593  ? 293 TYR B CG  1 
ATOM   4769 C  CD1 . TYR B  1 267 ? -29.23857 -4.91312  79.07414  1.000 46.08717  ? 293 TYR B CD1 1 
ATOM   4770 C  CD2 . TYR B  1 267 ? -29.47781 -2.88274  80.28589  1.000 47.26787  ? 293 TYR B CD2 1 
ATOM   4771 C  CE1 . TYR B  1 267 ? -29.43964 -5.63662  80.23414  1.000 46.84231  ? 293 TYR B CE1 1 
ATOM   4772 C  CE2 . TYR B  1 267 ? -29.67882 -3.59718  81.44796  1.000 47.80803  ? 293 TYR B CE2 1 
ATOM   4773 C  CZ  . TYR B  1 267 ? -29.66009 -4.97203  81.41846  1.000 47.67393  ? 293 TYR B CZ  1 
ATOM   4774 O  OH  . TYR B  1 267 ? -29.86190 -5.68020  82.58073  1.000 46.05492  ? 293 TYR B OH  1 
ATOM   4775 N  N   . GLN B  1 268 ? -27.38397 -1.37238  75.37057  1.000 44.73138  ? 294 GLN B N   1 
ATOM   4776 C  CA  . GLN B  1 268 ? -27.18356 -1.07140  73.95622  1.000 45.33246  ? 294 GLN B CA  1 
ATOM   4777 C  C   . GLN B  1 268 ? -25.95208 -1.78579  73.41560  1.000 43.33715  ? 294 GLN B C   1 
ATOM   4778 O  O   . GLN B  1 268 ? -25.98665 -2.36229  72.32300  1.000 42.32519  ? 294 GLN B O   1 
ATOM   4779 C  CB  . GLN B  1 268 ? -27.05118 0.43756   73.74893  1.000 47.04021  ? 294 GLN B CB  1 
ATOM   4780 C  CG  . GLN B  1 268 ? -28.34924 1.21868   73.86099  1.000 49.12757  ? 294 GLN B CG  1 
ATOM   4781 C  CD  . GLN B  1 268 ? -28.19710 2.66153   73.41160  1.000 50.69636  ? 294 GLN B CD  1 
ATOM   4782 O  OE1 . GLN B  1 268 ? -27.85958 2.93340   72.25889  1.000 50.11625  ? 294 GLN B OE1 1 
ATOM   4783 N  NE2 . GLN B  1 268 ? -28.44196 3.59457   74.32439  1.000 52.62632  ? 294 GLN B NE2 1 
ATOM   4784 N  N   . PHE B  1 269 ? -24.85465 -1.76084  74.17397  1.000 43.19490  ? 295 PHE B N   1 
ATOM   4785 C  CA  . PHE B  1 269 ? -23.63124 -2.42999  73.74221  1.000 43.47991  ? 295 PHE B CA  1 
ATOM   4786 C  C   . PHE B  1 269 ? -23.81186 -3.94225  73.69637  1.000 43.59279  ? 295 PHE B C   1 
ATOM   4787 O  O   . PHE B  1 269 ? -23.29097 -4.60847  72.79441  1.000 38.34652  ? 295 PHE B O   1 
ATOM   4788 C  CB  . PHE B  1 269 ? -22.47568 -2.05768  74.66984  1.000 39.84493  ? 295 PHE B CB  1 
ATOM   4789 C  CG  . PHE B  1 269 ? -21.12441 -2.43152  74.13429  1.000 39.17945  ? 295 PHE B CG  1 
ATOM   4790 C  CD1 . PHE B  1 269 ? -20.50098 -1.64363  73.18184  1.000 39.03770  ? 295 PHE B CD1 1 
ATOM   4791 C  CD2 . PHE B  1 269 ? -20.47910 -3.57282  74.58062  1.000 38.77998  ? 295 PHE B CD2 1 
ATOM   4792 C  CE1 . PHE B  1 269 ? -19.25726 -1.98484  72.68589  1.000 39.35985  ? 295 PHE B CE1 1 
ATOM   4793 C  CE2 . PHE B  1 269 ? -19.23566 -3.92003  74.08871  1.000 38.27620  ? 295 PHE B CE2 1 
ATOM   4794 C  CZ  . PHE B  1 269 ? -18.62390 -3.12509  73.13966  1.000 38.46003  ? 295 PHE B CZ  1 
ATOM   4795 N  N   . LEU B  1 270 ? -24.54257 -4.50351  74.66164  1.000 42.98918  ? 296 LEU B N   1 
ATOM   4796 C  CA  . LEU B  1 270 ? -24.78958 -5.94321  74.64502  1.000 41.20856  ? 296 LEU B CA  1 
ATOM   4797 C  C   . LEU B  1 270 ? -25.62695 -6.34761  73.43706  1.000 40.18636  ? 296 LEU B C   1 
ATOM   4798 O  O   . LEU B  1 270 ? -25.34524 -7.36529  72.79260  1.000 38.13813  ? 296 LEU B O   1 
ATOM   4799 C  CB  . LEU B  1 270 ? -25.46347 -6.38633  75.94442  1.000 41.77245  ? 296 LEU B CB  1 
ATOM   4800 C  CG  . LEU B  1 270 ? -24.76075 -6.00672  77.24861  1.000 42.22146  ? 296 LEU B CG  1 
ATOM   4801 C  CD1 . LEU B  1 270 ? -25.48732 -6.59054  78.45158  1.000 43.20679  ? 296 LEU B CD1 1 
ATOM   4802 C  CD2 . LEU B  1 270 ? -23.30307 -6.44191  77.22338  1.000 39.54832  ? 296 LEU B CD2 1 
ATOM   4803 N  N   . ASN B  1 271 ? -26.65447 -5.56117  73.10829  1.000 40.80178  ? 297 ASN B N   1 
ATOM   4804 C  CA  . ASN B  1 271 ? -27.44577 -5.85300  71.91738  1.000 41.78514  ? 297 ASN B CA  1 
ATOM   4805 C  C   . ASN B  1 271 ? -26.63136 -5.66444  70.64411  1.000 40.54632  ? 297 ASN B C   1 
ATOM   4806 O  O   . ASN B  1 271 ? -26.82643 -6.40114  69.67052  1.000 39.89591  ? 297 ASN B O   1 
ATOM   4807 C  CB  . ASN B  1 271 ? -28.69665 -4.97628  71.88311  1.000 44.29304  ? 297 ASN B CB  1 
ATOM   4808 C  CG  . ASN B  1 271 ? -29.92765 -5.70264  72.38467  1.000 47.24159  ? 297 ASN B CG  1 
ATOM   4809 O  OD1 . ASN B  1 271 ? -30.39018 -6.66268  71.76683  1.000 49.24544  ? 297 ASN B OD1 1 
ATOM   4810 N  ND2 . ASN B  1 271 ? -30.46956 -5.24433  73.50623  1.000 47.48588  ? 297 ASN B ND2 1 
ATOM   4811 N  N   . TYR B  1 272 ? -25.72577 -4.68353  70.63067  1.000 40.39152  ? 298 TYR B N   1 
ATOM   4812 C  CA  . TYR B  1 272 ? -24.81525 -4.52091  69.50256  1.000 39.80916  ? 298 TYR B CA  1 
ATOM   4813 C  C   . TYR B  1 272 ? -23.92986 -5.74881  69.33515  1.000 38.33340  ? 298 TYR B C   1 
ATOM   4814 O  O   . TYR B  1 272 ? -23.69560 -6.20956  68.21156  1.000 37.29436  ? 298 TYR B O   1 
ATOM   4815 C  CB  . TYR B  1 272 ? -23.96878 -3.26331  69.70473  1.000 40.55273  ? 298 TYR B CB  1 
ATOM   4816 C  CG  . TYR B  1 272 ? -22.96337 -2.99356  68.60994  1.000 40.99223  ? 298 TYR B CG  1 
ATOM   4817 C  CD1 . TYR B  1 272 ? -23.37498 -2.62091  67.33763  1.000 41.58487  ? 298 TYR B CD1 1 
ATOM   4818 C  CD2 . TYR B  1 272 ? -21.60044 -3.09963  68.85322  1.000 42.10371  ? 298 TYR B CD2 1 
ATOM   4819 C  CE1 . TYR B  1 272 ? -22.45682 -2.36791  66.33598  1.000 42.09243  ? 298 TYR B CE1 1 
ATOM   4820 C  CE2 . TYR B  1 272 ? -20.67573 -2.84901  67.85877  1.000 42.12318  ? 298 TYR B CE2 1 
ATOM   4821 C  CZ  . TYR B  1 272 ? -21.10910 -2.48416  66.60284  1.000 42.84407  ? 298 TYR B CZ  1 
ATOM   4822 O  OH  . TYR B  1 272 ? -20.19001 -2.23447  65.61085  1.000 45.61641  ? 298 TYR B OH  1 
ATOM   4823 N  N   . LEU B  1 273 ? -23.43174 -6.29329  70.44698  1.000 37.11831  ? 299 LEU B N   1 
ATOM   4824 C  CA  . LEU B  1 273 ? -22.63939 -7.51602  70.40029  1.000 36.56671  ? 299 LEU B CA  1 
ATOM   4825 C  C   . LEU B  1 273 ? -23.47444 -8.73180  70.02439  1.000 36.38394  ? 299 LEU B C   1 
ATOM   4826 O  O   . LEU B  1 273 ? -22.91997 -9.71964  69.53125  1.000 35.90717  ? 299 LEU B O   1 
ATOM   4827 C  CB  . LEU B  1 273 ? -21.95833 -7.75768  71.74798  1.000 36.70039  ? 299 LEU B CB  1 
ATOM   4828 C  CG  . LEU B  1 273 ? -20.74693 -6.88308  72.06909  1.000 36.80513  ? 299 LEU B CG  1 
ATOM   4829 C  CD1 . LEU B  1 273 ? -20.03986 -7.39996  73.30809  1.000 60.61316  ? 299 LEU B CD1 1 
ATOM   4830 C  CD2 . LEU B  1 273 ? -19.79386 -6.83008  70.88808  1.000 41.57043  ? 299 LEU B CD2 1 
ATOM   4831 N  N   . LEU B  1 274 ? -24.78691 -8.68895  70.25590  1.000 36.84536  ? 300 LEU B N   1 
ATOM   4832 C  CA  . LEU B  1 274 ? -25.65598 -9.79201  69.86738  1.000 36.81101  ? 300 LEU B CA  1 
ATOM   4833 C  C   . LEU B  1 274 ? -25.94773 -9.82255  68.37227  1.000 45.37807  ? 300 LEU B C   1 
ATOM   4834 O  O   . LEU B  1 274 ? -26.46678 -10.83171 67.88233  1.000 44.56762  ? 300 LEU B O   1 
ATOM   4835 C  CB  . LEU B  1 274 ? -26.97094 -9.72834  70.64725  1.000 42.56447  ? 300 LEU B CB  1 
ATOM   4836 C  CG  . LEU B  1 274 ? -26.91387 -10.28331 72.07184  1.000 42.77146  ? 300 LEU B CG  1 
ATOM   4837 C  CD1 . LEU B  1 274 ? -28.22223 -10.03004 72.80429  1.000 38.72006  ? 300 LEU B CD1 1 
ATOM   4838 C  CD2 . LEU B  1 274 ? -26.57996 -11.76783 72.05432  1.000 41.75909  ? 300 LEU B CD2 1 
ATOM   4839 N  N   . ARG B  1 275 ? -25.63791 -8.75587  67.64393  1.000 36.55065  ? 301 ARG B N   1 
ATOM   4840 C  CA  . ARG B  1 275 ? -25.79635 -8.77564  66.19476  1.000 40.34625  ? 301 ARG B CA  1 
ATOM   4841 C  C   . ARG B  1 275 ? -24.82524 -9.78533  65.59274  1.000 39.92128  ? 301 ARG B C   1 
ATOM   4842 O  O   . ARG B  1 275 ? -23.64416 -9.79488  65.96003  1.000 38.90496  ? 301 ARG B O   1 
ATOM   4843 C  CB  . ARG B  1 275 ? -25.55302 -7.38906  65.60332  1.000 39.61312  ? 301 ARG B CB  1 
ATOM   4844 C  CG  . ARG B  1 275 ? -26.44734 -6.29940  66.17106  1.000 42.38220  ? 301 ARG B CG  1 
ATOM   4845 C  CD  . ARG B  1 275 ? -26.19123 -4.96982  65.47915  1.000 44.64100  ? 301 ARG B CD  1 
ATOM   4846 N  NE  . ARG B  1 275 ? -26.78587 -3.84873  66.20103  1.000 46.70035  ? 301 ARG B NE  1 
ATOM   4847 C  CZ  . ARG B  1 275 ? -26.68172 -2.57884  65.82284  1.000 46.17900  ? 301 ARG B CZ  1 
ATOM   4848 N  NH1 . ARG B  1 275 ? -27.25486 -1.62174  66.53973  1.000 46.73836  ? 301 ARG B NH1 1 
ATOM   4849 N  NH2 . ARG B  1 275 ? -26.00292 -2.26517  64.72771  1.000 44.77717  ? 301 ARG B NH2 1 
ATOM   4850 N  N   . PRO B  1 276 ? -25.27839 -10.65047 64.68092  1.000 40.25209  ? 302 PRO B N   1 
ATOM   4851 C  CA  . PRO B  1 276 ? -24.38285 -11.70166 64.16580  1.000 39.81055  ? 302 PRO B CA  1 
ATOM   4852 C  C   . PRO B  1 276 ? -23.14073 -11.16904 63.47121  1.000 39.09803  ? 302 PRO B C   1 
ATOM   4853 O  O   . PRO B  1 276 ? -22.04523 -11.70485 63.68235  1.000 41.98473  ? 302 PRO B O   1 
ATOM   4854 C  CB  . PRO B  1 276 ? -25.28770 -12.47831 63.19833  1.000 35.48612  ? 302 PRO B CB  1 
ATOM   4855 C  CG  . PRO B  1 276 ? -26.67495 -12.22580 63.69676  1.000 35.98174  ? 302 PRO B CG  1 
ATOM   4856 C  CD  . PRO B  1 276 ? -26.66078 -10.81345 64.20075  1.000 36.15350  ? 302 PRO B CD  1 
ATOM   4857 N  N   . ASP B  1 277 ? -23.27547 -10.12230 62.65293  1.000 36.98699  ? 303 ASP B N   1 
ATOM   4858 C  CA  . ASP B  1 277 ? -22.13259 -9.63859  61.88305  1.000 38.36029  ? 303 ASP B CA  1 
ATOM   4859 C  C   . ASP B  1 277 ? -21.05327 -9.05219  62.78730  1.000 37.92827  ? 303 ASP B C   1 
ATOM   4860 O  O   . ASP B  1 277 ? -19.85787 -9.25022  62.54114  1.000 34.90282  ? 303 ASP B O   1 
ATOM   4861 C  CB  . ASP B  1 277 ? -22.59313 -8.61067  60.84796  1.000 39.69713  ? 303 ASP B CB  1 
ATOM   4862 C  CG  . ASP B  1 277 ? -23.24148 -7.39470  61.47851  1.000 41.34012  ? 303 ASP B CG  1 
ATOM   4863 O  OD1 . ASP B  1 277 ? -22.65251 -6.29664  61.39398  1.000 42.21921  ? 303 ASP B OD1 1 
ATOM   4864 O  OD2 . ASP B  1 277 ? -24.33918 -7.53646  62.05776  1.000 41.71563  ? 303 ASP B OD2 1 
ATOM   4865 N  N   . VAL B  1 278 ? -21.45260 -8.35086  63.85079  1.000 38.80459  ? 304 VAL B N   1 
ATOM   4866 C  CA  . VAL B  1 278 ? -20.47931 -7.72288  64.74358  1.000 39.17010  ? 304 VAL B CA  1 
ATOM   4867 C  C   . VAL B  1 278 ? -19.63043 -8.78172  65.43890  1.000 35.01463  ? 304 VAL B C   1 
ATOM   4868 O  O   . VAL B  1 278 ? -18.39191 -8.74257  65.40109  1.000 38.39771  ? 304 VAL B O   1 
ATOM   4869 C  CB  . VAL B  1 278 ? -21.19709 -6.81995  65.76314  1.000 40.46458  ? 304 VAL B CB  1 
ATOM   4870 C  CG1 . VAL B  1 278 ? -20.20252 -6.24287  66.75820  1.000 35.80547  ? 304 VAL B CG1 1 
ATOM   4871 C  CG2 . VAL B  1 278 ? -21.95881 -5.71215  65.04906  1.000 38.96428  ? 304 VAL B CG2 1 
ATOM   4872 N  N   . VAL B  1 279 ? -20.28641 -9.74534  66.08801  1.000 34.92885  ? 305 VAL B N   1 
ATOM   4873 C  CA  . VAL B  1 279 ? -19.54865 -10.76321 66.82601  1.000 34.71108  ? 305 VAL B CA  1 
ATOM   4874 C  C   . VAL B  1 279 ? -18.80593 -11.69353 65.87216  1.000 34.42815  ? 305 VAL B C   1 
ATOM   4875 O  O   . VAL B  1 279 ? -17.74967 -12.23371 66.22169  1.000 36.27890  ? 305 VAL B O   1 
ATOM   4876 C  CB  . VAL B  1 279 ? -20.50021 -11.52128 67.77336  1.000 34.78780  ? 305 VAL B CB  1 
ATOM   4877 C  CG1 . VAL B  1 279 ? -21.43402 -12.42629 66.99847  1.000 34.72364  ? 305 VAL B CG1 1 
ATOM   4878 C  CG2 . VAL B  1 279 ? -19.71149 -12.31199 68.80354  1.000 34.66237  ? 305 VAL B CG2 1 
ATOM   4879 N  N   . ALA B  1 280 ? -19.30413 -11.86004 64.64283  1.000 34.41473  ? 306 ALA B N   1 
ATOM   4880 C  CA  . ALA B  1 280 ? -18.56601 -12.63994 63.65378  1.000 34.28272  ? 306 ALA B CA  1 
ATOM   4881 C  C   . ALA B  1 280 ? -17.28617 -11.92691 63.23173  1.000 34.37629  ? 306 ALA B C   1 
ATOM   4882 O  O   . ALA B  1 280 ? -16.24219 -12.56497 63.05626  1.000 34.33451  ? 306 ALA B O   1 
ATOM   4883 C  CB  . ALA B  1 280 ? -19.45065 -12.92354 62.44052  1.000 45.33591  ? 306 ALA B CB  1 
ATOM   4884 N  N   . HIS B  1 281 ? -17.34821 -10.60404 63.06017  1.000 34.58674  ? 307 HIS B N   1 
ATOM   4885 C  CA  . HIS B  1 281 ? -16.14300 -9.82996  62.77645  1.000 34.79153  ? 307 HIS B CA  1 
ATOM   4886 C  C   . HIS B  1 281 ? -15.14906 -9.92574  63.92904  1.000 34.80067  ? 307 HIS B C   1 
ATOM   4887 O  O   . HIS B  1 281 ? -13.93431 -10.06603 63.71373  1.000 36.21114  ? 307 HIS B O   1 
ATOM   4888 C  CB  . HIS B  1 281 ? -16.52747 -8.37457  62.50584  1.000 35.06622  ? 307 HIS B CB  1 
ATOM   4889 C  CG  . HIS B  1 281 ? -15.39446 -7.52107  62.03041  1.000 40.44297  ? 307 HIS B CG  1 
ATOM   4890 N  ND1 . HIS B  1 281 ? -14.67170 -7.80741  60.89257  1.000 40.65065  ? 307 HIS B ND1 1 
ATOM   4891 C  CD2 . HIS B  1 281 ? -14.87023 -6.37782  62.53152  1.000 40.76857  ? 307 HIS B CD2 1 
ATOM   4892 C  CE1 . HIS B  1 281 ? -13.74504 -6.88210  60.71818  1.000 41.81244  ? 307 HIS B CE1 1 
ATOM   4893 N  NE2 . HIS B  1 281 ? -13.84388 -6.00328  61.69932  1.000 41.53593  ? 307 HIS B NE2 1 
ATOM   4894 N  N   . ILE B  1 282 ? -15.65178 -9.85943  65.16443  1.000 34.75197  ? 308 ILE B N   1 
ATOM   4895 C  CA  . ILE B  1 282 ? -14.77849 -10.02492 66.32442  1.000 34.80928  ? 308 ILE B CA  1 
ATOM   4896 C  C   . ILE B  1 282 ? -14.10903 -11.39370 66.29793  1.000 34.59287  ? 308 ILE B C   1 
ATOM   4897 O  O   . ILE B  1 282 ? -12.91402 -11.52134 66.58957  1.000 34.73125  ? 308 ILE B O   1 
ATOM   4898 C  CB  . ILE B  1 282 ? -15.56150 -9.81015  67.63157  1.000 34.87482  ? 308 ILE B CB  1 
ATOM   4899 C  CG1 . ILE B  1 282 ? -16.18052 -8.41359  67.66617  1.000 35.19336  ? 308 ILE B CG1 1 
ATOM   4900 C  CG2 . ILE B  1 282 ? -14.64428 -10.00481 68.82336  1.000 34.99933  ? 308 ILE B CG2 1 
ATOM   4901 C  CD1 . ILE B  1 282 ? -17.03278 -8.16194  68.88773  1.000 39.07839  ? 308 ILE B CD1 1 
ATOM   4902 N  N   . SER B  1 283 ? -14.86914 -12.43889 65.95966  1.000 34.97879  ? 309 SER B N   1 
ATOM   4903 C  CA  . SER B  1 283 ? -14.28926 -13.77554 65.86209  1.000 34.85622  ? 309 SER B CA  1 
ATOM   4904 C  C   . SER B  1 283 ? -13.22801 -13.83666 64.77075  1.000 35.14344  ? 309 SER B C   1 
ATOM   4905 O  O   . SER B  1 283 ? -12.18623 -14.48200 64.94097  1.000 34.41486  ? 309 SER B O   1 
ATOM   4906 C  CB  . SER B  1 283 ? -15.38813 -14.80644 65.60223  1.000 35.27877  ? 309 SER B CB  1 
ATOM   4907 O  OG  . SER B  1 283 ? -15.86293 -15.36207 66.81600  1.000 35.91933  ? 309 SER B OG  1 
ATOM   4908 N  N   . ASP B  1 284 ? -13.48136 -13.17521 63.63944  1.000 34.73046  ? 310 ASP B N   1 
ATOM   4909 C  CA  . ASP B  1 284 ? -12.48576 -13.11397 62.57421  1.000 37.45281  ? 310 ASP B CA  1 
ATOM   4910 C  C   . ASP B  1 284 ? -11.19186 -12.48376 63.06968  1.000 37.47759  ? 310 ASP B C   1 
ATOM   4911 O  O   . ASP B  1 284 ? -10.09613 -12.90432 62.67910  1.000 37.48377  ? 310 ASP B O   1 
ATOM   4912 C  CB  . ASP B  1 284 ? -13.03271 -12.32858 61.38159  1.000 37.32898  ? 310 ASP B CB  1 
ATOM   4913 C  CG  . ASP B  1 284 ? -14.15559 -13.05226 60.67114  1.000 38.88952  ? 310 ASP B CG  1 
ATOM   4914 O  OD1 . ASP B  1 284 ? -14.17648 -14.29944 60.70753  1.000 39.89192  ? 310 ASP B OD1 1 
ATOM   4915 O  OD2 . ASP B  1 284 ? -15.01559 -12.37280 60.07352  1.000 40.65833  ? 310 ASP B OD2 1 
ATOM   4916 N  N   . HIS B  1 285 ? -11.29845 -11.46983 63.92900  1.000 37.58132  ? 311 HIS B N   1 
ATOM   4917 C  CA  . HIS B  1 285 ? -10.08845 -10.81537 64.42134  1.000 36.87978  ? 311 HIS B CA  1 
ATOM   4918 C  C   . HIS B  1 285 ? -9.36859  -11.65821 65.47246  1.000 36.73312  ? 311 HIS B C   1 
ATOM   4919 O  O   . HIS B  1 285 ? -8.15360  -11.86674 65.38320  1.000 35.90764  ? 311 HIS B O   1 
ATOM   4920 C  CB  . HIS B  1 285 ? -10.41549 -9.43463  64.99021  1.000 38.94010  ? 311 HIS B CB  1 
ATOM   4921 C  CG  . HIS B  1 285 ? -9.21456  -8.70042  65.50180  1.000 40.30740  ? 311 HIS B CG  1 
ATOM   4922 N  ND1 . HIS B  1 285 ? -8.19857  -8.26981  64.67557  1.000 41.66114  ? 311 HIS B ND1 1 
ATOM   4923 C  CD2 . HIS B  1 285 ? -8.86043  -8.33229  66.75594  1.000 40.47469  ? 311 HIS B CD2 1 
ATOM   4924 C  CE1 . HIS B  1 285 ? -7.27365  -7.66274  65.39769  1.000 42.03910  ? 311 HIS B CE1 1 
ATOM   4925 N  NE2 . HIS B  1 285 ? -7.65116  -7.68677  66.66329  1.000 41.22806  ? 311 HIS B NE2 1 
ATOM   4926 N  N   . VAL B  1 286 ? -10.09941 -12.14986 66.47892  1.000 36.82827  ? 312 VAL B N   1 
ATOM   4927 C  CA  . VAL B  1 286 ? -9.46828  -12.77790 67.64039  1.000 37.11059  ? 312 VAL B CA  1 
ATOM   4928 C  C   . VAL B  1 286 ? -9.21487  -14.26916 67.46858  1.000 36.51225  ? 312 VAL B C   1 
ATOM   4929 O  O   . VAL B  1 286 ? -8.48121  -14.85497 68.28102  1.000 35.26101  ? 312 VAL B O   1 
ATOM   4930 C  CB  . VAL B  1 286 ? -10.31438 -12.56557 68.91235  1.000 37.45595  ? 312 VAL B CB  1 
ATOM   4931 C  CG1 . VAL B  1 286 ? -10.67810 -11.09735 69.06896  1.000 38.41926  ? 312 VAL B CG1 1 
ATOM   4932 C  CG2 . VAL B  1 286 ? -11.56461 -13.43199 68.87393  1.000 35.80393  ? 312 VAL B CG2 1 
ATOM   4933 N  N   . PHE B  1 287 ? -9.79383  -14.90093 66.44535  1.000 37.03276  ? 313 PHE B N   1 
ATOM   4934 C  CA  . PHE B  1 287 ? -9.64015  -16.33867 66.20533  1.000 38.54737  ? 313 PHE B CA  1 
ATOM   4935 C  C   . PHE B  1 287 ? -10.15202 -17.16024 67.38765  1.000 41.37879  ? 313 PHE B C   1 
ATOM   4936 O  O   . PHE B  1 287 ? -9.51792  -18.12347 67.82414  1.000 42.32781  ? 313 PHE B O   1 
ATOM   4937 C  CB  . PHE B  1 287 ? -8.18996  -16.69850 65.87202  1.000 40.27035  ? 313 PHE B CB  1 
ATOM   4938 C  CG  . PHE B  1 287 ? -7.81532  -16.42798 64.44360  1.000 42.46923  ? 313 PHE B CG  1 
ATOM   4939 C  CD1 . PHE B  1 287 ? -7.62538  -17.47140 63.55331  1.000 42.63224  ? 313 PHE B CD1 1 
ATOM   4940 C  CD2 . PHE B  1 287 ? -7.66156  -15.12922 63.98900  1.000 43.73271  ? 313 PHE B CD2 1 
ATOM   4941 C  CE1 . PHE B  1 287 ? -7.28400  -17.22459 62.23762  1.000 43.05463  ? 313 PHE B CE1 1 
ATOM   4942 C  CE2 . PHE B  1 287 ? -7.32031  -14.87549 62.67440  1.000 44.52466  ? 313 PHE B CE2 1 
ATOM   4943 C  CZ  . PHE B  1 287 ? -7.13134  -15.92443 61.79763  1.000 43.95305  ? 313 PHE B CZ  1 
ATOM   4944 N  N   . TYR B  1 288 ? -11.30973 -16.76719 67.91276  1.000 41.82667  ? 314 TYR B N   1 
ATOM   4945 C  CA  . TYR B  1 288 ? -12.03557 -17.53691 68.91028  1.000 42.85838  ? 314 TYR B CA  1 
ATOM   4946 C  C   . TYR B  1 288 ? -13.45329 -17.76771 68.41136  1.000 40.82651  ? 314 TYR B C   1 
ATOM   4947 O  O   . TYR B  1 288 ? -14.01983 -16.93298 67.70095  1.000 39.92402  ? 314 TYR B O   1 
ATOM   4948 C  CB  . TYR B  1 288 ? -12.08598 -16.82428 70.27236  1.000 46.25673  ? 314 TYR B CB  1 
ATOM   4949 C  CG  . TYR B  1 288 ? -10.81022 -16.90006 71.08137  1.000 49.91978  ? 314 TYR B CG  1 
ATOM   4950 C  CD1 . TYR B  1 288 ? -10.65670 -17.84707 72.08602  1.000 51.97812  ? 314 TYR B CD1 1 
ATOM   4951 C  CD2 . TYR B  1 288 ? -9.76860  -16.01144 70.85541  1.000 51.74586  ? 314 TYR B CD2 1 
ATOM   4952 C  CE1 . TYR B  1 288 ? -9.49550  -17.91459 72.83316  1.000 53.48238  ? 314 TYR B CE1 1 
ATOM   4953 C  CE2 . TYR B  1 288 ? -8.60361  -16.07107 71.59681  1.000 53.92186  ? 314 TYR B CE2 1 
ATOM   4954 C  CZ  . TYR B  1 288 ? -8.47249  -17.02395 72.58420  1.000 54.83680  ? 314 TYR B CZ  1 
ATOM   4955 O  OH  . TYR B  1 288 ? -7.31386  -17.08506 73.32405  1.000 56.04397  ? 314 TYR B OH  1 
ATOM   4956 N  N   . ALA B  1 289 ? -14.02337 -18.90867 68.78415  1.000 40.95825  ? 315 ALA B N   1 
ATOM   4957 C  CA  . ALA B  1 289 ? -15.41446 -19.18732 68.46148  1.000 39.36902  ? 315 ALA B CA  1 
ATOM   4958 C  C   . ALA B  1 289 ? -16.32085 -18.42106 69.41439  1.000 39.46694  ? 315 ALA B C   1 
ATOM   4959 O  O   . ALA B  1 289 ? -16.09031 -18.40734 70.62740  1.000 40.87088  ? 315 ALA B O   1 
ATOM   4960 C  CB  . ALA B  1 289 ? -15.70052 -20.68584 68.54364  1.000 33.51950  ? 315 ALA B CB  1 
ATOM   4961 N  N   . ASN B  1 290 ? -17.34123 -17.77307 68.86511  1.000 37.09359  ? 316 ASN B N   1 
ATOM   4962 C  CA  . ASN B  1 290 ? -18.30761 -17.05768 69.68022  1.000 35.85358  ? 316 ASN B CA  1 
ATOM   4963 C  C   . ASN B  1 290 ? -19.47243 -17.97458 70.04582  1.000 35.13396  ? 316 ASN B C   1 
ATOM   4964 O  O   . ASN B  1 290 ? -19.59040 -19.10212 69.56132  1.000 35.82324  ? 316 ASN B O   1 
ATOM   4965 C  CB  . ASN B  1 290 ? -18.80684 -15.80856 68.95217  1.000 35.55425  ? 316 ASN B CB  1 
ATOM   4966 C  CG  . ASN B  1 290 ? -19.47540 -16.12897 67.62925  1.000 35.98015  ? 316 ASN B CG  1 
ATOM   4967 O  OD1 . ASN B  1 290 ? -20.59134 -16.64704 67.59290  1.000 35.58855  ? 316 ASN B OD1 1 
ATOM   4968 N  ND2 . ASN B  1 290 ? -18.79532 -15.81598 66.53163  1.000 36.35831  ? 316 ASN B ND2 1 
ATOM   4969 N  N   . ALA B  1 291 ? -20.34282 -17.47427 70.92112  1.000 35.84820  ? 317 ALA B N   1 
ATOM   4970 C  CA  . ALA B  1 291 ? -21.50988 -18.21789 71.37244  1.000 36.54747  ? 317 ALA B CA  1 
ATOM   4971 C  C   . ALA B  1 291 ? -22.77722 -17.82214 70.62432  1.000 37.57567  ? 317 ALA B C   1 
ATOM   4972 O  O   . ALA B  1 291 ? -23.88293 -18.11486 71.09125  1.000 39.83596  ? 317 ALA B O   1 
ATOM   4973 C  CB  . ALA B  1 291 ? -21.70256 -18.03378 72.87711  1.000 35.03942  ? 317 ALA B CB  1 
ATOM   4974 N  N   . ASN B  1 292 ? -22.63867 -17.16766 69.47396  1.000 36.84794  ? 318 ASN B N   1 
ATOM   4975 C  CA  . ASN B  1 292 ? -23.77263 -16.72469 68.67066  1.000 37.05219  ? 318 ASN B CA  1 
ATOM   4976 C  C   . ASN B  1 292 ? -23.97809 -17.72311 67.53643  1.000 37.02378  ? 318 ASN B C   1 
ATOM   4977 O  O   . ASN B  1 292 ? -23.13204 -17.84137 66.64393  1.000 34.63560  ? 318 ASN B O   1 
ATOM   4978 C  CB  . ASN B  1 292 ? -23.53273 -15.31561 68.13226  1.000 37.60197  ? 318 ASN B CB  1 
ATOM   4979 C  CG  . ASN B  1 292 ? -24.79989 -14.66140 67.61953  1.000 37.13334  ? 318 ASN B CG  1 
ATOM   4980 O  OD1 . ASN B  1 292 ? -25.42551 -15.14532 66.67604  1.000 37.45589  ? 318 ASN B OD1 1 
ATOM   4981 N  ND2 . ASN B  1 292 ? -25.18284 -13.55032 68.23817  1.000 36.83336  ? 318 ASN B ND2 1 
ATOM   4982 N  N   . LYS B  1 293 ? -25.10273 -18.44223 67.57309  1.000 37.30525  ? 319 LYS B N   1 
ATOM   4983 C  CA  . LYS B  1 293 ? -25.36969 -19.43947 66.54136  1.000 38.82128  ? 319 LYS B CA  1 
ATOM   4984 C  C   . LYS B  1 293 ? -25.67126 -18.78249 65.19995  1.000 37.64747  ? 319 LYS B C   1 
ATOM   4985 O  O   . LYS B  1 293 ? -25.29182 -19.30754 64.14659  1.000 36.85137  ? 319 LYS B O   1 
ATOM   4986 C  CB  . LYS B  1 293 ? -26.52593 -20.34464 66.96710  1.000 41.88869  ? 319 LYS B CB  1 
ATOM   4987 C  CG  . LYS B  1 293 ? -26.78512 -21.49831 66.00942  1.000 45.21814  ? 319 LYS B CG  1 
ATOM   4988 C  CD  . LYS B  1 293 ? -28.13593 -22.14745 66.25970  1.000 49.24387  ? 319 LYS B CD  1 
ATOM   4989 C  CE  . LYS B  1 293 ? -28.39103 -23.27547 65.27279  1.000 50.71913  ? 319 LYS B CE  1 
ATOM   4990 N  NZ  . LYS B  1 293 ? -29.74950 -23.86364 65.43102  1.000 52.44570  ? 319 LYS B NZ  1 
ATOM   4991 N  N   . ALA B  1 294 ? -26.34879 -17.63208 65.21671  1.000 37.09022  ? 320 ALA B N   1 
ATOM   4992 C  CA  . ALA B  1 294 ? -26.67959 -16.94398 63.97474  1.000 38.04004  ? 320 ALA B CA  1 
ATOM   4993 C  C   . ALA B  1 294 ? -25.45634 -16.33869 63.29947  1.000 38.87721  ? 320 ALA B C   1 
ATOM   4994 O  O   . ALA B  1 294 ? -25.50807 -16.04589 62.10042  1.000 38.74898  ? 320 ALA B O   1 
ATOM   4995 C  CB  . ALA B  1 294 ? -27.71742 -15.85229 64.23791  1.000 36.21053  ? 320 ALA B CB  1 
ATOM   4996 N  N   . ALA B  1 295 ? -24.36181 -16.15197 64.03386  1.000 39.14832  ? 321 ALA B N   1 
ATOM   4997 C  CA  . ALA B  1 295 ? -23.17148 -15.50236 63.50418  1.000 38.30392  ? 321 ALA B CA  1 
ATOM   4998 C  C   . ALA B  1 295 ? -22.22417 -16.45536 62.79041  1.000 38.47567  ? 321 ALA B C   1 
ATOM   4999 O  O   . ALA B  1 295 ? -21.31992 -15.98807 62.08967  1.000 39.07911  ? 321 ALA B O   1 
ATOM   5000 C  CB  . ALA B  1 295 ? -22.41207 -14.80116 64.63122  1.000 36.46701  ? 321 ALA B CB  1 
ATOM   5001 N  N   . THR B  1 296 ? -22.40586 -17.76611 62.95021  1.000 40.04362  ? 322 THR B N   1 
ATOM   5002 C  CA  . THR B  1 296 ? -21.45703 -18.72555 62.38631  1.000 41.31185  ? 322 THR B CA  1 
ATOM   5003 C  C   . THR B  1 296 ? -21.31823 -18.62311 60.87040  1.000 41.59658  ? 322 THR B C   1 
ATOM   5004 O  O   . THR B  1 296 ? -20.17400 -18.59764 60.38407  1.000 41.18015  ? 322 THR B O   1 
ATOM   5005 C  CB  . THR B  1 296 ? -21.84509 -20.14385 62.81913  1.000 42.76415  ? 322 THR B CB  1 
ATOM   5006 O  OG1 . THR B  1 296 ? -21.75751 -20.24859 64.24594  1.000 34.34218  ? 322 THR B OG1 1 
ATOM   5007 C  CG2 . THR B  1 296 ? -20.91872 -21.16885 62.18446  1.000 34.44949  ? 322 THR B CG2 1 
ATOM   5008 N  N   . PRO B  1 297 ? -22.39216 -18.56042 60.07151  1.000 41.30834  ? 323 PRO B N   1 
ATOM   5009 C  CA  . PRO B  1 297 ? -22.19766 -18.45735 58.61375  1.000 39.98662  ? 323 PRO B CA  1 
ATOM   5010 C  C   . PRO B  1 297 ? -21.46438 -17.19916 58.18336  1.000 38.44103  ? 323 PRO B C   1 
ATOM   5011 O  O   . PRO B  1 297 ? -20.88808 -17.18041 57.08863  1.000 37.34067  ? 323 PRO B O   1 
ATOM   5012 C  CB  . PRO B  1 297 ? -23.63038 -18.48287 58.06040  1.000 40.17020  ? 323 PRO B CB  1 
ATOM   5013 C  CG  . PRO B  1 297 ? -24.45144 -19.09118 59.13956  1.000 40.88252  ? 323 PRO B CG  1 
ATOM   5014 C  CD  . PRO B  1 297 ? -23.82482 -18.63145 60.41392  1.000 41.53092  ? 323 PRO B CD  1 
ATOM   5015 N  N   . LEU B  1 298 ? -21.46167 -16.15262 59.00678  1.000 39.48507  ? 324 LEU B N   1 
ATOM   5016 C  CA  . LEU B  1 298 ? -20.80418 -14.89752 58.67110  1.000 37.89947  ? 324 LEU B CA  1 
ATOM   5017 C  C   . LEU B  1 298 ? -19.33198 -14.87049 59.06076  1.000 35.51456  ? 324 LEU B C   1 
ATOM   5018 O  O   . LEU B  1 298 ? -18.60299 -13.98475 58.60132  1.000 34.79610  ? 324 LEU B O   1 
ATOM   5019 C  CB  . LEU B  1 298 ? -21.53132 -13.72406 59.34038  1.000 39.45854  ? 324 LEU B CB  1 
ATOM   5020 C  CG  . LEU B  1 298 ? -22.90360 -13.32940 58.78287  1.000 42.28442  ? 324 LEU B CG  1 
ATOM   5021 C  CD1 . LEU B  1 298 ? -24.00896 -14.24984 59.28640  1.000 43.17302  ? 324 LEU B CD1 1 
ATOM   5022 C  CD2 . LEU B  1 298 ? -23.21942 -11.88196 59.12244  1.000 43.52995  ? 324 LEU B CD2 1 
ATOM   5023 N  N   . VAL B  1 299 ? -18.88073 -15.80669 59.89701  1.000 35.22215  ? 325 VAL B N   1 
ATOM   5024 C  CA  . VAL B  1 299 ? -17.46871 -15.88267 60.24717  1.000 34.39483  ? 325 VAL B CA  1 
ATOM   5025 C  C   . VAL B  1 299 ? -16.67464 -16.34574 59.03342  1.000 34.66176  ? 325 VAL B C   1 
ATOM   5026 O  O   . VAL B  1 299 ? -17.12176 -17.21403 58.27086  1.000 34.82864  ? 325 VAL B O   1 
ATOM   5027 C  CB  . VAL B  1 299 ? -17.26472 -16.82558 61.44652  1.000 35.70866  ? 325 VAL B CB  1 
ATOM   5028 C  CG1 . VAL B  1 299 ? -15.79988 -16.87825 61.85062  1.000 34.14011  ? 325 VAL B CG1 1 
ATOM   5029 C  CG2 . VAL B  1 299 ? -18.12750 -16.38798 62.62066  1.000 34.03300  ? 325 VAL B CG2 1 
ATOM   5030 N  N   . SER B  1 300 ? -15.49425 -15.75719 58.84094  1.000 34.81153  ? 326 SER B N   1 
ATOM   5031 C  CA  . SER B  1 300 ? -14.65493 -16.11038 57.70354  1.000 35.20848  ? 326 SER B CA  1 
ATOM   5032 C  C   . SER B  1 300 ? -14.31600 -17.59674 57.72456  1.000 35.24373  ? 326 SER B C   1 
ATOM   5033 O  O   . SER B  1 300 ? -14.20814 -18.21897 58.78496  1.000 37.40080  ? 326 SER B O   1 
ATOM   5034 C  CB  . SER B  1 300 ? -13.37177 -15.27801 57.70565  1.000 37.54961  ? 326 SER B CB  1 
ATOM   5035 O  OG  . SER B  1 300 ? -12.46536 -15.73556 58.69430  1.000 40.46244  ? 326 SER B OG  1 
ATOM   5036 N  N   . ALA B  1 301 ? -14.15009 -18.16475 56.52645  1.000 35.67316  ? 327 ALA B N   1 
ATOM   5037 C  CA  . ALA B  1 301 ? -13.93564 -19.60336 56.40395  1.000 37.37929  ? 327 ALA B CA  1 
ATOM   5038 C  C   . ALA B  1 301 ? -12.67524 -20.05568 57.12815  1.000 37.97314  ? 327 ALA B C   1 
ATOM   5039 O  O   . ALA B  1 301 ? -12.61622 -21.18994 57.61626  1.000 37.80862  ? 327 ALA B O   1 
ATOM   5040 C  CB  . ALA B  1 301 ? -13.87003 -20.00016 54.92918  1.000 37.21369  ? 327 ALA B CB  1 
ATOM   5041 N  N   . GLU B  1 302 ? -11.66161 -19.18972 57.20982  1.000 38.25517  ? 328 GLU B N   1 
ATOM   5042 C  CA  . GLU B  1 302 ? -10.43354 -19.55239 57.90989  1.000 39.78146  ? 328 GLU B CA  1 
ATOM   5043 C  C   . GLU B  1 302 ? -10.69681 -19.87927 59.37373  1.000 39.34765  ? 328 GLU B C   1 
ATOM   5044 O  O   . GLU B  1 302 ? -10.02390 -20.74257 59.94789  1.000 41.78392  ? 328 GLU B O   1 
ATOM   5045 C  CB  . GLU B  1 302 ? -9.41075  -18.42248 57.79009  1.000 40.60304  ? 328 GLU B CB  1 
ATOM   5046 C  CG  . GLU B  1 302 ? -8.02584  -18.77517 58.30424  1.000 41.05358  ? 328 GLU B CG  1 
ATOM   5047 C  CD  . GLU B  1 302 ? -7.07734  -17.59415 58.27167  1.000 37.14610  ? 328 GLU B CD  1 
ATOM   5048 O  OE1 . GLU B  1 302 ? -7.52971  -16.47679 57.94435  1.000 44.47568  ? 328 GLU B OE1 1 
ATOM   5049 O  OE2 . GLU B  1 302 ? -5.88014  -17.78286 58.57238  1.000 37.57054  ? 328 GLU B OE2 1 
ATOM   5050 N  N   . VAL B  1 303 ? -11.66882 -19.21221 59.98774  1.000 35.09040  ? 329 VAL B N   1 
ATOM   5051 C  CA  . VAL B  1 303 ? -12.02796 -19.49179 61.37410  1.000 37.62279  ? 329 VAL B CA  1 
ATOM   5052 C  C   . VAL B  1 303 ? -13.19259 -20.47023 61.45943  1.000 37.36282  ? 329 VAL B C   1 
ATOM   5053 O  O   . VAL B  1 303 ? -13.18688 -21.37822 62.29400  1.000 37.29242  ? 329 VAL B O   1 
ATOM   5054 C  CB  . VAL B  1 303 ? -12.34516 -18.17203 62.10701  1.000 37.26993  ? 329 VAL B CB  1 
ATOM   5055 C  CG1 . VAL B  1 303 ? -12.81176 -18.44679 63.53083  1.000 34.13523  ? 329 VAL B CG1 1 
ATOM   5056 C  CG2 . VAL B  1 303 ? -11.13153 -17.25688 62.10188  1.000 34.76313  ? 329 VAL B CG2 1 
ATOM   5057 N  N   . ARG B  1 304 ? -14.19147 -20.30591 60.59016  1.000 36.98485  ? 330 ARG B N   1 
ATOM   5058 C  CA  . ARG B  1 304 ? -15.39635 -21.12635 60.66482  1.000 36.77789  ? 330 ARG B CA  1 
ATOM   5059 C  C   . ARG B  1 304 ? -15.10521 -22.58861 60.34553  1.000 38.27254  ? 330 ARG B C   1 
ATOM   5060 O  O   . ARG B  1 304 ? -15.69501 -23.49054 60.95280  1.000 36.83082  ? 330 ARG B O   1 
ATOM   5061 C  CB  . ARG B  1 304 ? -16.45784 -20.57080 59.71420  1.000 36.65274  ? 330 ARG B CB  1 
ATOM   5062 C  CG  . ARG B  1 304 ? -17.76137 -21.34952 59.69668  1.000 37.84107  ? 330 ARG B CG  1 
ATOM   5063 C  CD  . ARG B  1 304 ? -18.67895 -20.85794 58.58745  1.000 40.83279  ? 330 ARG B CD  1 
ATOM   5064 N  NE  . ARG B  1 304 ? -18.18704 -21.22364 57.26175  1.000 43.91132  ? 330 ARG B NE  1 
ATOM   5065 C  CZ  . ARG B  1 304 ? -17.84693 -20.34740 56.32192  1.000 46.55351  ? 330 ARG B CZ  1 
ATOM   5066 N  NH1 . ARG B  1 304 ? -17.94348 -19.04658 56.55852  1.000 46.85017  ? 330 ARG B NH1 1 
ATOM   5067 N  NH2 . ARG B  1 304 ? -17.41025 -20.77134 55.14400  1.000 48.45652  ? 330 ARG B NH2 1 
ATOM   5068 N  N   . GLU B  1 305 ? -14.20009 -22.84568 59.40307  1.000 39.10287  ? 331 GLU B N   1 
ATOM   5069 C  CA  . GLU B  1 305 ? -13.92981 -24.19692 58.93227  1.000 41.40033  ? 331 GLU B CA  1 
ATOM   5070 C  C   . GLU B  1 305 ? -12.73345 -24.84136 59.62242  1.000 40.59342  ? 331 GLU B C   1 
ATOM   5071 O  O   . GLU B  1 305 ? -12.29501 -25.91628 59.20127  1.000 41.57007  ? 331 GLU B O   1 
ATOM   5072 C  CB  . GLU B  1 305 ? -13.72548 -24.19172 57.41657  1.000 45.59404  ? 331 GLU B CB  1 
ATOM   5073 C  CG  . GLU B  1 305 ? -14.80243 -23.42738 56.66349  1.000 50.89651  ? 331 GLU B CG  1 
ATOM   5074 C  CD  . GLU B  1 305 ? -15.29570 -24.16733 55.43751  1.000 58.00622  ? 331 GLU B CD  1 
ATOM   5075 O  OE1 . GLU B  1 305 ? -14.81469 -25.29251 55.18725  1.000 61.01960  ? 331 GLU B OE1 1 
ATOM   5076 O  OE2 . GLU B  1 305 ? -16.16827 -23.62547 54.72644  1.000 60.76474  ? 331 GLU B OE2 1 
ATOM   5077 N  N   . ASN B  1 306 ? -12.19443 -24.21349 60.66470  1.000 38.73683  ? 332 ASN B N   1 
ATOM   5078 C  CA  . ASN B  1 306 ? -11.15762 -24.84379 61.47116  1.000 38.88504  ? 332 ASN B CA  1 
ATOM   5079 C  C   . ASN B  1 306 ? -11.82835 -25.72296 62.51951  1.000 37.99708  ? 332 ASN B C   1 
ATOM   5080 O  O   . ASN B  1 306 ? -12.51466 -25.20844 63.41226  1.000 37.10405  ? 332 ASN B O   1 
ATOM   5081 C  CB  . ASN B  1 306 ? -10.25973 -23.79297 62.13082  1.000 38.14793  ? 332 ASN B CB  1 
ATOM   5082 C  CG  . ASN B  1 306 ? -9.00196  -24.39200 62.74597  1.000 38.83134  ? 332 ASN B CG  1 
ATOM   5083 O  OD1 . ASN B  1 306 ? -9.01748  -25.50381 63.27489  1.000 40.02615  ? 332 ASN B OD1 1 
ATOM   5084 N  ND2 . ASN B  1 306 ? -7.90335  -23.64897 62.67910  1.000 38.61381  ? 332 ASN B ND2 1 
ATOM   5085 N  N   . PRO B  1 307 ? -11.66315 -27.04617 62.44412  1.000 37.64935  ? 333 PRO B N   1 
ATOM   5086 C  CA  . PRO B  1 307 ? -12.31011 -27.91598 63.44000  1.000 37.94166  ? 333 PRO B CA  1 
ATOM   5087 C  C   . PRO B  1 307 ? -11.80386 -27.68753 64.85145  1.000 38.44792  ? 333 PRO B C   1 
ATOM   5088 O  O   . PRO B  1 307 ? -12.55756 -27.89120 65.81145  1.000 40.65643  ? 333 PRO B O   1 
ATOM   5089 C  CB  . PRO B  1 307 ? -11.98068 -29.32831 62.93698  1.000 37.87961  ? 333 PRO B CB  1 
ATOM   5090 C  CG  . PRO B  1 307 ? -10.74028 -29.15966 62.12389  1.000 37.99829  ? 333 PRO B CG  1 
ATOM   5091 C  CD  . PRO B  1 307 ? -10.85363 -27.80897 61.47869  1.000 37.29420  ? 333 PRO B CD  1 
ATOM   5092 N  N   . GLY B  1 308 ? -10.55085 -27.26327 65.00824  1.000 39.04233  ? 334 GLY B N   1 
ATOM   5093 C  CA  . GLY B  1 308 ? -10.02074 -26.92022 66.31301  1.000 40.74298  ? 334 GLY B CA  1 
ATOM   5094 C  C   . GLY B  1 308 ? -10.55913 -25.63716 66.90496  1.000 42.09497  ? 334 GLY B C   1 
ATOM   5095 O  O   . GLY B  1 308 ? -10.18239 -25.28475 68.02652  1.000 43.83790  ? 334 GLY B O   1 
ATOM   5096 N  N   . ILE B  1 309 ? -11.42321 -24.92470 66.18030  1.000 41.87973  ? 335 ILE B N   1 
ATOM   5097 C  CA  . ILE B  1 309 ? -12.06751 -23.71071 66.66593  1.000 41.27754  ? 335 ILE B CA  1 
ATOM   5098 C  C   . ILE B  1 309 ? -13.58492 -23.85227 66.66669  1.000 39.36116  ? 335 ILE B C   1 
ATOM   5099 O  O   . ILE B  1 309 ? -14.24259 -23.61504 67.68429  1.000 38.26152  ? 335 ILE B O   1 
ATOM   5100 C  CB  . ILE B  1 309 ? -11.63606 -22.47678 65.84235  1.000 42.73015  ? 335 ILE B CB  1 
ATOM   5101 C  CG1 . ILE B  1 309 ? -10.12463 -22.26613 65.94710  1.000 43.37008  ? 335 ILE B CG1 1 
ATOM   5102 C  CG2 . ILE B  1 309 ? -12.38745 -21.23764 66.30337  1.000 42.20139  ? 335 ILE B CG2 1 
ATOM   5103 C  CD1 . ILE B  1 309 ? -9.60146  -21.16007 65.05842  1.000 44.28492  ? 335 ILE B CD1 1 
ATOM   5104 N  N   . TYR B  1 310 ? -14.15894 -24.23721 65.52958  1.000 39.52776  ? 336 TYR B N   1 
ATOM   5105 C  CA  . TYR B  1 310 ? -15.58694 -24.50581 65.42906  1.000 38.90694  ? 336 TYR B CA  1 
ATOM   5106 C  C   . TYR B  1 310 ? -15.79786 -26.00055 65.22237  1.000 39.00417  ? 336 TYR B C   1 
ATOM   5107 O  O   . TYR B  1 310 ? -15.92993 -26.45823 64.08010  1.000 39.66222  ? 336 TYR B O   1 
ATOM   5108 C  CB  . TYR B  1 310 ? -16.21273 -23.70297 64.28643  1.000 37.94827  ? 336 TYR B CB  1 
ATOM   5109 C  CG  . TYR B  1 310 ? -16.64364 -22.30878 64.68533  1.000 36.86791  ? 336 TYR B CG  1 
ATOM   5110 C  CD1 . TYR B  1 310 ? -17.93569 -22.06083 65.12923  1.000 35.77830  ? 336 TYR B CD1 1 
ATOM   5111 C  CD2 . TYR B  1 310 ? -15.75694 -21.24212 64.62356  1.000 35.84048  ? 336 TYR B CD2 1 
ATOM   5112 C  CE1 . TYR B  1 310 ? -18.33394 -20.79055 65.49838  1.000 34.95430  ? 336 TYR B CE1 1 
ATOM   5113 C  CE2 . TYR B  1 310 ? -16.14608 -19.96689 64.99019  1.000 34.88524  ? 336 TYR B CE2 1 
ATOM   5114 C  CZ  . TYR B  1 310 ? -17.43567 -19.74723 65.42687  1.000 35.87543  ? 336 TYR B CZ  1 
ATOM   5115 O  OH  . TYR B  1 310 ? -17.82939 -18.48011 65.79307  1.000 36.18611  ? 336 TYR B OH  1 
ATOM   5116 N  N   . PRO B  1 311 ? -15.83391 -26.78817 66.29314  1.000 39.31634  ? 337 PRO B N   1 
ATOM   5117 C  CA  . PRO B  1 311 ? -15.91319 -28.24446 66.14695  1.000 39.87875  ? 337 PRO B CA  1 
ATOM   5118 C  C   . PRO B  1 311 ? -17.26285 -28.66674 65.59742  1.000 41.70315  ? 337 PRO B C   1 
ATOM   5119 O  O   . PRO B  1 311 ? -18.24869 -27.92096 65.70316  1.000 41.70360  ? 337 PRO B O   1 
ATOM   5120 C  CB  . PRO B  1 311 ? -15.71060 -28.75267 67.58236  1.000 38.91886  ? 337 PRO B CB  1 
ATOM   5121 C  CG  . PRO B  1 311 ? -16.18445 -27.63324 68.44066  1.000 37.97907  ? 337 PRO B CG  1 
ATOM   5122 C  CD  . PRO B  1 311 ? -15.83004 -26.37071 67.70612  1.000 38.77025  ? 337 PRO B CD  1 
ATOM   5123 N  N   . PRO B  1 312 ? -17.34872 -29.85844 64.99701  1.000 43.78912  ? 338 PRO B N   1 
ATOM   5124 C  CA  . PRO B  1 312 ? -18.64345 -30.34173 64.49612  1.000 46.61668  ? 338 PRO B CA  1 
ATOM   5125 C  C   . PRO B  1 312 ? -19.64067 -30.61034 65.61363  1.000 52.27643  ? 338 PRO B C   1 
ATOM   5126 O  O   . PRO B  1 312 ? -19.32053 -30.45496 66.79662  1.000 53.65670  ? 338 PRO B O   1 
ATOM   5127 C  CB  . PRO B  1 312 ? -18.27362 -31.62870 63.74580  1.000 46.22010  ? 338 PRO B CB  1 
ATOM   5128 C  CG  . PRO B  1 312 ? -16.95771 -32.04594 64.31820  1.000 45.84808  ? 338 PRO B CG  1 
ATOM   5129 C  CD  . PRO B  1 312 ? -16.24589 -30.77887 64.67253  1.000 43.88868  ? 338 PRO B CD  1 
ATOM   5130 N  N   . ALA B  1 313 ? -20.85530 -31.02400 65.24427  1.000 54.94306  ? 339 ALA B N   1 
ATOM   5131 C  CA  . ALA B  1 313 ? -21.92415 -31.16120 66.22927  1.000 57.10016  ? 339 ALA B CA  1 
ATOM   5132 C  C   . ALA B  1 313 ? -21.68575 -32.34363 67.16153  1.000 59.76055  ? 339 ALA B C   1 
ATOM   5133 O  O   . ALA B  1 313 ? -22.00686 -32.27252 68.35422  1.000 61.35515  ? 339 ALA B O   1 
ATOM   5134 C  CB  . ALA B  1 313 ? -23.27174 -31.29839 65.52194  1.000 57.50955  ? 339 ALA B CB  1 
ATOM   5135 N  N   . ASP B  1 314 ? -21.12996 -33.44057 66.63992  1.000 62.20335  ? 340 ASP B N   1 
ATOM   5136 C  CA  . ASP B  1 314 ? -20.90980 -34.61963 67.47289  1.000 64.87223  ? 340 ASP B CA  1 
ATOM   5137 C  C   . ASP B  1 314 ? -19.89547 -34.33750 68.57473  1.000 62.16358  ? 340 ASP B C   1 
ATOM   5138 O  O   . ASP B  1 314 ? -20.04447 -34.81802 69.70450  1.000 62.62350  ? 340 ASP B O   1 
ATOM   5139 C  CB  . ASP B  1 314 ? -20.45697 -35.79860 66.61036  1.000 71.00310  ? 340 ASP B CB  1 
ATOM   5140 C  CG  . ASP B  1 314 ? -19.24676 -35.46965 65.75728  1.000 76.01065  ? 340 ASP B CG  1 
ATOM   5141 O  OD1 . ASP B  1 314 ? -18.81149 -34.29916 65.76085  1.000 78.81884  ? 340 ASP B OD1 1 
ATOM   5142 O  OD2 . ASP B  1 314 ? -18.72849 -36.38487 65.08358  1.000 78.72914  ? 340 ASP B OD2 1 
ATOM   5143 N  N   . VAL B  1 315 ? -18.85786 -33.55902 68.26572  1.000 59.92101  ? 341 VAL B N   1 
ATOM   5144 C  CA  . VAL B  1 315 ? -17.88158 -33.18938 69.28404  1.000 56.01926  ? 341 VAL B CA  1 
ATOM   5145 C  C   . VAL B  1 315 ? -18.45545 -32.13504 70.22522  1.000 55.40338  ? 341 VAL B C   1 
ATOM   5146 O  O   . VAL B  1 315 ? -18.16445 -32.14621 71.42772  1.000 54.85682  ? 341 VAL B O   1 
ATOM   5147 C  CB  . VAL B  1 315 ? -16.57975 -32.71081 68.61735  1.000 53.41001  ? 341 VAL B CB  1 
ATOM   5148 C  CG1 . VAL B  1 315 ? -15.59464 -32.19650 69.65677  1.000 52.86314  ? 341 VAL B CG1 1 
ATOM   5149 C  CG2 . VAL B  1 315 ? -15.96051 -33.83615 67.80182  1.000 52.35857  ? 341 VAL B CG2 1 
ATOM   5150 N  N   . ARG B  1 316 ? -19.28133 -31.22149 69.70664  1.000 54.18970  ? 342 ARG B N   1 
ATOM   5151 C  CA  . ARG B  1 316 ? -19.92020 -30.22806 70.56342  1.000 53.44335  ? 342 ARG B CA  1 
ATOM   5152 C  C   . ARG B  1 316 ? -20.85072 -30.87897 71.57639  1.000 51.46058  ? 342 ARG B C   1 
ATOM   5153 O  O   . ARG B  1 316 ? -20.99664 -30.37836 72.69759  1.000 50.52460  ? 342 ARG B O   1 
ATOM   5154 C  CB  . ARG B  1 316 ? -20.69069 -29.21800 69.71383  1.000 54.49611  ? 342 ARG B CB  1 
ATOM   5155 C  CG  . ARG B  1 316 ? -19.91457 -27.95371 69.40234  1.000 56.18850  ? 342 ARG B CG  1 
ATOM   5156 C  CD  . ARG B  1 316 ? -20.82512 -26.86879 68.85774  1.000 58.55289  ? 342 ARG B CD  1 
ATOM   5157 N  NE  . ARG B  1 316 ? -20.11452 -25.97863 67.94673  1.000 60.16527  ? 342 ARG B NE  1 
ATOM   5158 C  CZ  . ARG B  1 316 ? -20.05080 -24.66018 68.09304  1.000 60.48742  ? 342 ARG B CZ  1 
ATOM   5159 N  NH1 . ARG B  1 316 ? -19.38109 -23.92626 67.21689  1.000 60.42831  ? 342 ARG B NH1 1 
ATOM   5160 N  NH2 . ARG B  1 316 ? -20.65256 -24.07600 69.11949  1.000 61.12262  ? 342 ARG B NH2 1 
ATOM   5161 N  N   . ALA B  1 317 ? -21.48547 -31.99219 71.20327  1.000 51.54848  ? 343 ALA B N   1 
ATOM   5162 C  CA  . ALA B  1 317 ? -22.37010 -32.69200 72.12601  1.000 52.22353  ? 343 ALA B CA  1 
ATOM   5163 C  C   . ALA B  1 317 ? -21.61975 -33.30670 73.30067  1.000 51.56094  ? 343 ALA B C   1 
ATOM   5164 O  O   . ALA B  1 317 ? -22.24414 -33.62398 74.31862  1.000 51.72569  ? 343 ALA B O   1 
ATOM   5165 C  CB  . ALA B  1 317 ? -23.15077 -33.77810 71.38455  1.000 53.05708  ? 343 ALA B CB  1 
ATOM   5166 N  N   . LYS B  1 318 ? -20.30243 -33.47619 73.19024  1.000 49.64511  ? 344 LYS B N   1 
ATOM   5167 C  CA  . LYS B  1 318 ? -19.51202 -34.10979 74.23558  1.000 48.34735  ? 344 LYS B CA  1 
ATOM   5168 C  C   . LYS B  1 318 ? -18.64273 -33.12929 75.00768  1.000 47.75733  ? 344 LYS B C   1 
ATOM   5169 O  O   . LYS B  1 318 ? -17.85014 -33.55993 75.85261  1.000 49.76047  ? 344 LYS B O   1 
ATOM   5170 C  CB  . LYS B  1 318 ? -18.63335 -35.21128 73.63652  1.000 46.78140  ? 344 LYS B CB  1 
ATOM   5171 C  CG  . LYS B  1 318 ? -19.43239 -36.32015 72.98679  1.000 47.26630  ? 344 LYS B CG  1 
ATOM   5172 C  CD  . LYS B  1 318 ? -18.54073 -37.29783 72.25165  1.000 48.59748  ? 344 LYS B CD  1 
ATOM   5173 C  CE  . LYS B  1 318 ? -19.37342 -38.25522 71.42177  1.000 50.92243  ? 344 LYS B CE  1 
ATOM   5174 N  NZ  . LYS B  1 318 ? -18.55299 -39.03082 70.45363  1.000 52.67344  ? 344 LYS B NZ  1 
ATOM   5175 N  N   . LEU B  1 319 ? -18.75485 -31.83240 74.73658  1.000 45.45216  ? 345 LEU B N   1 
ATOM   5176 C  CA  . LEU B  1 319 ? -18.02264 -30.85139 75.51893  1.000 44.36883  ? 345 LEU B CA  1 
ATOM   5177 C  C   . LEU B  1 319 ? -18.58606 -30.77646 76.93561  1.000 45.29792  ? 345 LEU B C   1 
ATOM   5178 O  O   . LEU B  1 319 ? -19.72126 -31.17813 77.20740  1.000 44.46969  ? 345 LEU B O   1 
ATOM   5179 C  CB  . LEU B  1 319 ? -18.08438 -29.47380 74.85797  1.000 44.01868  ? 345 LEU B CB  1 
ATOM   5180 C  CG  . LEU B  1 319 ? -17.56663 -29.35324 73.42344  1.000 43.99157  ? 345 LEU B CG  1 
ATOM   5181 C  CD1 . LEU B  1 319 ? -17.79670 -27.94661 72.89222  1.000 43.77780  ? 345 LEU B CD1 1 
ATOM   5182 C  CD2 . LEU B  1 319 ? -16.09393 -29.72185 73.34815  1.000 44.80083  ? 345 LEU B CD2 1 
ATOM   5183 N  N   . PHE B  1 320 ? -17.76904 -30.25545 77.84732  1.000 44.84720  ? 346 PHE B N   1 
ATOM   5184 C  CA  . PHE B  1 320 ? -18.18315 -30.08656 79.23122  1.000 44.01909  ? 346 PHE B CA  1 
ATOM   5185 C  C   . PHE B  1 320 ? -17.41567 -28.92218 79.83643  1.000 44.02416  ? 346 PHE B C   1 
ATOM   5186 O  O   . PHE B  1 320 ? -16.38004 -28.49779 79.31848  1.000 44.89703  ? 346 PHE B O   1 
ATOM   5187 C  CB  . PHE B  1 320 ? -17.95981 -31.36445 80.05266  1.000 42.95805  ? 346 PHE B CB  1 
ATOM   5188 C  CG  . PHE B  1 320 ? -16.52450 -31.81394 80.10464  1.000 43.16194  ? 346 PHE B CG  1 
ATOM   5189 C  CD1 . PHE B  1 320 ? -15.68841 -31.39484 81.12739  1.000 43.95034  ? 346 PHE B CD1 1 
ATOM   5190 C  CD2 . PHE B  1 320 ? -16.01385 -32.66101 79.13482  1.000 43.31318  ? 346 PHE B CD2 1 
ATOM   5191 C  CE1 . PHE B  1 320 ? -14.37020 -31.80675 81.17815  1.000 44.49499  ? 346 PHE B CE1 1 
ATOM   5192 C  CE2 . PHE B  1 320 ? -14.69628 -33.07667 79.18040  1.000 43.13263  ? 346 PHE B CE2 1 
ATOM   5193 C  CZ  . PHE B  1 320 ? -13.87379 -32.64904 80.20367  1.000 43.97322  ? 346 PHE B CZ  1 
ATOM   5194 N  N   . THR B  1 321 ? -17.94122 -28.40697 80.94206  1.000 43.81447  ? 347 THR B N   1 
ATOM   5195 C  CA  . THR B  1 321 ? -17.29403 -27.35054 81.70068  1.000 44.76196  ? 347 THR B CA  1 
ATOM   5196 C  C   . THR B  1 321 ? -16.92983 -27.87099 83.08487  1.000 46.50605  ? 347 THR B C   1 
ATOM   5197 O  O   . THR B  1 321 ? -17.50657 -28.84429 83.57762  1.000 46.00649  ? 347 THR B O   1 
ATOM   5198 C  CB  . THR B  1 321 ? -18.19302 -26.11298 81.82299  1.000 45.57410  ? 347 THR B CB  1 
ATOM   5199 O  OG1 . THR B  1 321 ? -19.43106 -26.47788 82.44265  1.000 46.97172  ? 347 THR B OG1 1 
ATOM   5200 C  CG2 . THR B  1 321 ? -18.47971 -25.52032 80.45215  1.000 46.39655  ? 347 THR B CG2 1 
ATOM   5201 N  N   . LEU B  1 322 ? -15.95798 -27.21068 83.70867  1.000 47.37552  ? 348 LEU B N   1 
ATOM   5202 C  CA  . LEU B  1 322 ? -15.47363 -27.62383 85.01948  1.000 47.53689  ? 348 LEU B CA  1 
ATOM   5203 C  C   . LEU B  1 322 ? -16.39245 -27.07582 86.10457  1.000 49.80973  ? 348 LEU B C   1 
ATOM   5204 O  O   . LEU B  1 322 ? -16.53911 -25.85685 86.24621  1.000 50.39121  ? 348 LEU B O   1 
ATOM   5205 C  CB  . LEU B  1 322 ? -14.04103 -27.14238 85.23243  1.000 45.99811  ? 348 LEU B CB  1 
ATOM   5206 C  CG  . LEU B  1 322 ? -13.36726 -27.56310 86.53961  1.000 46.69587  ? 348 LEU B CG  1 
ATOM   5207 C  CD1 . LEU B  1 322 ? -13.02598 -29.04638 86.52158  1.000 46.45404  ? 348 LEU B CD1 1 
ATOM   5208 C  CD2 . LEU B  1 322 ? -12.12472 -26.72453 86.79263  1.000 46.04683  ? 348 LEU B CD2 1 
ATOM   5209 N  N   . LYS B  1 323 ? -17.00752 -27.97320 86.86758  1.000 51.12949  ? 349 LYS B N   1 
ATOM   5210 C  CA  . LYS B  1 323 ? -17.88027 -27.58694 87.96460  1.000 52.42988  ? 349 LYS B CA  1 
ATOM   5211 C  C   . LYS B  1 323 ? -17.07148 -27.37647 89.23871  1.000 49.74487  ? 349 LYS B C   1 
ATOM   5212 O  O   . LYS B  1 323 ? -16.02221 -27.99310 89.44205  1.000 48.97019  ? 349 LYS B O   1 
ATOM   5213 C  CB  . LYS B  1 323 ? -18.95831 -28.64791 88.19755  1.000 56.90649  ? 349 LYS B CB  1 
ATOM   5214 C  CG  . LYS B  1 323 ? -20.31988 -28.28735 87.62041  1.000 60.32186  ? 349 LYS B CG  1 
ATOM   5215 C  CD  . LYS B  1 323 ? -20.94363 -29.46308 86.88122  1.000 62.49469  ? 349 LYS B CD  1 
ATOM   5216 C  CE  . LYS B  1 323 ? -21.19096 -30.63899 87.81393  1.000 64.85628  ? 349 LYS B CE  1 
ATOM   5217 N  NZ  . LYS B  1 323 ? -21.78299 -31.80406 87.09870  1.000 65.06519  ? 349 LYS B NZ  1 
ATOM   5218 N  N   . VAL B  1 324 ? -17.57006 -26.49106 90.09580  1.000 49.68072  ? 350 VAL B N   1 
ATOM   5219 C  CA  . VAL B  1 324 ? -16.92008 -26.21259 91.37165  1.000 50.72579  ? 350 VAL B CA  1 
ATOM   5220 C  C   . VAL B  1 324 ? -17.20761 -27.35778 92.33234  1.000 50.33916  ? 350 VAL B C   1 
ATOM   5221 O  O   . VAL B  1 324 ? -18.36298 -27.76202 92.51041  1.000 51.96274  ? 350 VAL B O   1 
ATOM   5222 C  CB  . VAL B  1 324 ? -17.39616 -24.86887 91.94525  1.000 51.95998  ? 350 VAL B CB  1 
ATOM   5223 C  CG1 . VAL B  1 324 ? -16.88302 -24.68480 93.36696  1.000 52.44583  ? 350 VAL B CG1 1 
ATOM   5224 C  CG2 . VAL B  1 324 ? -16.93441 -23.72426 91.05766  1.000 50.96066  ? 350 VAL B CG2 1 
ATOM   5225 N  N   . GLN B  1 325 ? -16.15783 -27.88272 92.95275  1.000 48.85539  ? 351 GLN B N   1 
ATOM   5226 C  CA  . GLN B  1 325 ? -16.25950 -29.03888 93.82838  1.000 48.35924  ? 351 GLN B CA  1 
ATOM   5227 C  C   . GLN B  1 325 ? -16.27844 -28.62035 95.29314  1.000 48.72655  ? 351 GLN B C   1 
ATOM   5228 O  O   . GLN B  1 325 ? -15.91825 -27.49677 95.65327  1.000 48.11852  ? 351 GLN B O   1 
ATOM   5229 C  CB  . GLN B  1 325 ? -15.09357 -30.00265 93.58771  1.000 47.65836  ? 351 GLN B CB  1 
ATOM   5230 C  CG  . GLN B  1 325 ? -15.07635 -30.63964 92.21129  1.000 45.48643  ? 351 GLN B CG  1 
ATOM   5231 C  CD  . GLN B  1 325 ? -16.04386 -31.79994 92.09265  1.000 44.68974  ? 351 GLN B CD  1 
ATOM   5232 O  OE1 . GLN B  1 325 ? -16.66905 -32.20664 93.07249  1.000 44.93822  ? 351 GLN B OE1 1 
ATOM   5233 N  NE2 . GLN B  1 325 ? -16.16991 -32.34239 90.88763  1.000 43.28800  ? 351 GLN B NE2 1 
ATOM   5234 N  N   . ASP B  1 326 ? -16.71658 -29.55179 96.13638  1.000 48.77677  ? 352 ASP B N   1 
ATOM   5235 C  CA  . ASP B  1 326 ? -16.54858 -29.40423 97.57078  1.000 48.05468  ? 352 ASP B CA  1 
ATOM   5236 C  C   . ASP B  1 326 ? -15.05768 -29.30616 97.89471  1.000 47.27493  ? 352 ASP B C   1 
ATOM   5237 O  O   . ASP B  1 326 ? -14.22960 -29.92793 97.22178  1.000 46.27920  ? 352 ASP B O   1 
ATOM   5238 C  CB  . ASP B  1 326 ? -17.18115 -30.59227 98.29767  1.000 47.86519  ? 352 ASP B CB  1 
ATOM   5239 C  CG  . ASP B  1 326 ? -17.23953 -30.40433 99.80296  1.000 49.25480  ? 352 ASP B CG  1 
ATOM   5240 O  OD1 . ASP B  1 326 ? -16.19298 -30.55485 100.46826 1.000 48.73858  ? 352 ASP B OD1 1 
ATOM   5241 O  OD2 . ASP B  1 326 ? -18.33712 -30.11193 100.32296 1.000 50.07255  ? 352 ASP B OD2 1 
ATOM   5242 N  N   . PRO B  1 327 ? -14.68367 -28.50868 98.89993  1.000 48.23238  ? 353 PRO B N   1 
ATOM   5243 C  CA  . PRO B  1 327 ? -13.25603 -28.39103 99.24689  1.000 47.48879  ? 353 PRO B CA  1 
ATOM   5244 C  C   . PRO B  1 327 ? -12.58017 -29.72126 99.54290  1.000 46.35859  ? 353 PRO B C   1 
ATOM   5245 O  O   . PRO B  1 327 ? -11.36748 -29.84971 99.32465  1.000 45.81413  ? 353 PRO B O   1 
ATOM   5246 C  CB  . PRO B  1 327 ? -13.27753 -27.47914 100.48009 1.000 48.55594  ? 353 PRO B CB  1 
ATOM   5247 C  CG  . PRO B  1 327 ? -14.50001 -26.64442 100.29878 1.000 48.92778  ? 353 PRO B CG  1 
ATOM   5248 C  CD  . PRO B  1 327 ? -15.51448 -27.53205 99.62715  1.000 49.29863  ? 353 PRO B CD  1 
ATOM   5249 N  N   . LYS B  1 328 ? -13.32530 -30.71420 100.03541 1.000 46.75680  ? 354 LYS B N   1 
ATOM   5250 C  CA  . LYS B  1 328 ? -12.74881 -32.03708 100.25878 1.000 46.65698  ? 354 LYS B CA  1 
ATOM   5251 C  C   . LYS B  1 328 ? -12.22939 -32.63138 98.95429  1.000 45.56658  ? 354 LYS B C   1 
ATOM   5252 O  O   . LYS B  1 328 ? -11.10921 -33.15759 98.89500  1.000 45.66104  ? 354 LYS B O   1 
ATOM   5253 C  CB  . LYS B  1 328 ? -13.79154 -32.95896 100.89314 1.000 47.20580  ? 354 LYS B CB  1 
ATOM   5254 C  CG  . LYS B  1 328 ? -14.09132 -32.66319 102.35466 1.000 49.25894  ? 354 LYS B CG  1 
ATOM   5255 C  CD  . LYS B  1 328 ? -15.31086 -33.43947 102.83078 1.000 50.75537  ? 354 LYS B CD  1 
ATOM   5256 C  CE  . LYS B  1 328 ? -15.28833 -33.64885 104.33784 1.000 54.41728  ? 354 LYS B CE  1 
ATOM   5257 N  NZ  . LYS B  1 328 ? -15.11606 -32.37088 105.08292 1.000 56.52126  ? 354 LYS B NZ  1 
ATOM   5258 N  N   . ILE B  1 329 ? -13.03798 -32.55289 97.89411  1.000 44.06231  ? 355 ILE B N   1 
ATOM   5259 C  CA  . ILE B  1 329 ? -12.61289 -33.04550 96.58752  1.000 48.04893  ? 355 ILE B CA  1 
ATOM   5260 C  C   . ILE B  1 329 ? -11.40715 -32.25936 96.09054  1.000 42.44247  ? 355 ILE B C   1 
ATOM   5261 O  O   . ILE B  1 329 ? -10.50968 -32.81450 95.44813  1.000 41.84664  ? 355 ILE B O   1 
ATOM   5262 C  CB  . ILE B  1 329 ? -13.78429 -32.98615 95.58827  1.000 47.74005  ? 355 ILE B CB  1 
ATOM   5263 C  CG1 . ILE B  1 329 ? -14.94331 -33.85924 96.07329  1.000 48.46095  ? 355 ILE B CG1 1 
ATOM   5264 C  CG2 . ILE B  1 329 ? -13.33596 -33.42379 94.20028  1.000 41.45183  ? 355 ILE B CG2 1 
ATOM   5265 C  CD1 . ILE B  1 329 ? -14.56465 -35.30655 96.29504  1.000 43.17248  ? 355 ILE B CD1 1 
ATOM   5266 N  N   . ASP B  1 330 ? -11.35590 -30.96041 96.39533  1.000 47.92117  ? 356 ASP B N   1 
ATOM   5267 C  CA  . ASP B  1 330 ? -10.22089 -30.14322 95.97410  1.000 46.64358  ? 356 ASP B CA  1 
ATOM   5268 C  C   . ASP B  1 330 ? -8.93167  -30.60347 96.64603  1.000 45.97010  ? 356 ASP B C   1 
ATOM   5269 O  O   . ASP B  1 330 ? -7.88623  -30.72713 95.99518  1.000 44.05375  ? 356 ASP B O   1 
ATOM   5270 C  CB  . ASP B  1 330 ? -10.49397 -28.67022 96.28112  1.000 46.80607  ? 356 ASP B CB  1 
ATOM   5271 C  CG  . ASP B  1 330 ? -11.50718 -28.05611 95.33547  1.000 47.70980  ? 356 ASP B CG  1 
ATOM   5272 O  OD1 . ASP B  1 330 ? -11.44247 -28.34691 94.12276  1.000 47.08745  ? 356 ASP B OD1 1 
ATOM   5273 O  OD2 . ASP B  1 330 ? -12.36810 -27.28212 95.80448  1.000 48.86809  ? 356 ASP B OD2 1 
ATOM   5274 N  N   . ARG B  1 331 ? -8.98702  -30.85942 97.95587  1.000 46.90127  ? 357 ARG B N   1 
ATOM   5275 C  CA  . ARG B  1 331 ? -7.80242  -31.34165 98.66128  1.000 44.11004  ? 357 ARG B CA  1 
ATOM   5276 C  C   . ARG B  1 331 ? -7.38177  -32.71664 98.15504  1.000 43.56287  ? 357 ARG B C   1 
ATOM   5277 O  O   . ARG B  1 331 ? -6.18375  -32.98449 97.97446  1.000 43.42065  ? 357 ARG B O   1 
ATOM   5278 C  CB  . ARG B  1 331 ? -8.06666  -31.37934 100.16675 1.000 45.29685  ? 357 ARG B CB  1 
ATOM   5279 C  CG  . ARG B  1 331 ? -8.51599  -30.04988 100.75231 1.000 52.43660  ? 357 ARG B CG  1 
ATOM   5280 C  CD  . ARG B  1 331 ? -8.85779  -30.17807 102.22864 1.000 53.03173  ? 357 ARG B CD  1 
ATOM   5281 N  NE  . ARG B  1 331 ? -9.77409  -31.28520 102.48648 1.000 53.23664  ? 357 ARG B NE  1 
ATOM   5282 C  CZ  . ARG B  1 331 ? -10.28381 -31.57027 103.68039 1.000 53.69547  ? 357 ARG B CZ  1 
ATOM   5283 N  NH1 . ARG B  1 331 ? -11.10934 -32.59783 103.82278 1.000 52.37945  ? 357 ARG B NH1 1 
ATOM   5284 N  NH2 . ARG B  1 331 ? -9.96807  -30.82819 104.73326 1.000 55.76428  ? 357 ARG B NH2 1 
ATOM   5285 N  N   . VAL B  1 332 ? -8.35587  -33.60245 97.92320  1.000 43.34463  ? 358 VAL B N   1 
ATOM   5286 C  CA  . VAL B  1 332 ? -8.04872  -34.92225 97.37650  1.000 42.86028  ? 358 VAL B CA  1 
ATOM   5287 C  C   . VAL B  1 332 ? -7.36129  -34.79120 96.02286  1.000 41.94754  ? 358 VAL B C   1 
ATOM   5288 O  O   . VAL B  1 332 ? -6.36575  -35.47306 95.74536  1.000 41.76412  ? 358 VAL B O   1 
ATOM   5289 C  CB  . VAL B  1 332 ? -9.32984  -35.77251 97.28156  1.000 42.85130  ? 358 VAL B CB  1 
ATOM   5290 C  CG1 . VAL B  1 332 ? -9.07448  -37.03526 96.47234  1.000 42.27397  ? 358 VAL B CG1 1 
ATOM   5291 C  CG2 . VAL B  1 332 ? -9.84196  -36.12067 98.67040  1.000 43.89004  ? 358 VAL B CG2 1 
ATOM   5292 N  N   . ARG B  1 333 ? -7.87559  -33.90520 95.16516  1.000 41.44390  ? 359 ARG B N   1 
ATOM   5293 C  CA  . ARG B  1 333 ? -7.29033  -33.70817 93.84363  1.000 40.65243  ? 359 ARG B CA  1 
ATOM   5294 C  C   . ARG B  1 333 ? -5.87268  -33.16457 93.94109  1.000 40.81522  ? 359 ARG B C   1 
ATOM   5295 O  O   . ARG B  1 333 ? -4.98281  -33.60109 93.20348  1.000 43.01536  ? 359 ARG B O   1 
ATOM   5296 C  CB  . ARG B  1 333 ? -8.16394  -32.76156 93.01978  1.000 41.23352  ? 359 ARG B CB  1 
ATOM   5297 C  CG  . ARG B  1 333 ? -9.19614  -33.45496 92.15041  1.000 42.96925  ? 359 ARG B CG  1 
ATOM   5298 C  CD  . ARG B  1 333 ? -9.79681  -32.49242 91.13660  1.000 42.91940  ? 359 ARG B CD  1 
ATOM   5299 N  NE  . ARG B  1 333 ? -10.38439 -31.31852 91.77611  1.000 45.01157  ? 359 ARG B NE  1 
ATOM   5300 C  CZ  . ARG B  1 333 ? -11.32583 -30.55961 91.22435  1.000 46.45057  ? 359 ARG B CZ  1 
ATOM   5301 N  NH1 . ARG B  1 333 ? -11.79002 -30.84859 90.01622  1.000 38.79902  ? 359 ARG B NH1 1 
ATOM   5302 N  NH2 . ARG B  1 333 ? -11.80200 -29.50902 91.87857  1.000 39.94955  ? 359 ARG B NH2 1 
ATOM   5303 N  N   . THR B  1 334 ? -5.64456  -32.20343 94.83926  1.000 41.44780  ? 360 THR B N   1 
ATOM   5304 C  CA  . THR B  1 334 ? -4.30469  -31.64321 94.98900  1.000 41.75217  ? 360 THR B CA  1 
ATOM   5305 C  C   . THR B  1 334 ? -3.31205  -32.70684 95.44474  1.000 42.07715  ? 360 THR B C   1 
ATOM   5306 O  O   . THR B  1 334 ? -2.20303  -32.80947 94.90014  1.000 41.95999  ? 360 THR B O   1 
ATOM   5307 C  CB  . THR B  1 334 ? -4.33087  -30.47147 95.97127  1.000 42.52180  ? 360 THR B CB  1 
ATOM   5308 O  OG1 . THR B  1 334 ? -5.09099  -29.39435 95.40926  1.000 45.73382  ? 360 THR B OG1 1 
ATOM   5309 C  CG2 . THR B  1 334 ? -2.91839  -29.98489 96.26349  1.000 43.02432  ? 360 THR B CG2 1 
ATOM   5310 N  N   . ARG B  1 335 ? -3.69853  -33.52153 96.43184  1.000 42.55484  ? 361 ARG B N   1 
ATOM   5311 C  CA  . ARG B  1 335 ? -2.79961  -34.57327 96.90056  1.000 43.77735  ? 361 ARG B CA  1 
ATOM   5312 C  C   . ARG B  1 335 ? -2.53591  -35.60665 95.80932  1.000 42.22154  ? 361 ARG B C   1 
ATOM   5313 O  O   . ARG B  1 335 ? -1.39299  -36.04560 95.62133  1.000 42.32977  ? 361 ARG B O   1 
ATOM   5314 C  CB  . ARG B  1 335 ? -3.37214  -35.24381 98.14890  1.000 43.58239  ? 361 ARG B CB  1 
ATOM   5315 C  CG  . ARG B  1 335 ? -2.53329  -36.40848 98.65444  1.000 55.56799  ? 361 ARG B CG  1 
ATOM   5316 C  CD  . ARG B  1 335 ? -2.16278  -36.23552 100.11803 1.000 57.15612  ? 361 ARG B CD  1 
ATOM   5317 N  NE  . ARG B  1 335 ? -1.40419  -37.37400 100.62977 1.000 57.45980  ? 361 ARG B NE  1 
ATOM   5318 C  CZ  . ARG B  1 335 ? -0.09309  -37.36231 100.84984 1.000 57.36584  ? 361 ARG B CZ  1 
ATOM   5319 N  NH1 . ARG B  1 335 ? 0.61400   -36.26736 100.60502 1.000 56.92952  ? 361 ARG B NH1 1 
ATOM   5320 N  NH2 . ARG B  1 335 ? 0.51213   -38.44602 101.31731 1.000 57.52725  ? 361 ARG B NH2 1 
ATOM   5321 N  N   . ALA B  1 336 ? -3.57868  -36.00289 95.07286  1.000 41.60535  ? 362 ALA B N   1 
ATOM   5322 C  CA  . ALA B  1 336 ? -3.39795  -36.98527 94.00822  1.000 47.25768  ? 362 ALA B CA  1 
ATOM   5323 C  C   . ALA B  1 336 ? -2.51052  -36.44007 92.89595  1.000 45.70003  ? 362 ALA B C   1 
ATOM   5324 O  O   . ALA B  1 336 ? -1.70444  -37.17695 92.31678  1.000 40.54046  ? 362 ALA B O   1 
ATOM   5325 C  CB  . ALA B  1 336 ? -4.75565  -37.41332 93.45241  1.000 40.56530  ? 362 ALA B CB  1 
ATOM   5326 N  N   . TRP B  1 337 ? -2.63850  -35.14801 92.58779  1.000 45.11108  ? 363 TRP B N   1 
ATOM   5327 C  CA  . TRP B  1 337 ? -1.78902  -34.53956 91.57007  1.000 44.19514  ? 363 TRP B CA  1 
ATOM   5328 C  C   . TRP B  1 337 ? -0.33839  -34.48332 92.02878  1.000 45.63829  ? 363 TRP B C   1 
ATOM   5329 O  O   . TRP B  1 337 ? 0.57938   -34.74400 91.24002  1.000 45.57767  ? 363 TRP B O   1 
ATOM   5330 C  CB  . TRP B  1 337 ? -2.30469  -33.14104 91.23448  1.000 39.98161  ? 363 TRP B CB  1 
ATOM   5331 C  CG  . TRP B  1 337 ? -1.71073  -32.54511 89.99524  1.000 47.85546  ? 363 TRP B CG  1 
ATOM   5332 C  CD1 . TRP B  1 337 ? -0.96250  -31.40744 89.91221  1.000 46.25505  ? 363 TRP B CD1 1 
ATOM   5333 C  CD2 . TRP B  1 337 ? -1.82689  -33.04727 88.65795  1.000 39.01109  ? 363 TRP B CD2 1 
ATOM   5334 N  NE1 . TRP B  1 337 ? -0.60182  -31.17177 88.60773  1.000 43.13140  ? 363 TRP B NE1 1 
ATOM   5335 C  CE2 . TRP B  1 337 ? -1.11863  -32.16476 87.81810  1.000 40.17029  ? 363 TRP B CE2 1 
ATOM   5336 C  CE3 . TRP B  1 337 ? -2.45746  -34.15856 88.09002  1.000 38.60044  ? 363 TRP B CE3 1 
ATOM   5337 C  CZ2 . TRP B  1 337 ? -1.02351  -32.35867 86.44201  1.000 39.82760  ? 363 TRP B CZ2 1 
ATOM   5338 C  CZ3 . TRP B  1 337 ? -2.36159  -34.34924 86.72370  1.000 38.15891  ? 363 TRP B CZ3 1 
ATOM   5339 C  CH2 . TRP B  1 337 ? -1.65020  -33.45394 85.91530  1.000 39.54506  ? 363 TRP B CH2 1 
ATOM   5340 N  N   . THR B  1 338 ? -0.11201  -34.14201 93.30088  1.000 46.80755  ? 364 THR B N   1 
ATOM   5341 C  CA  . THR B  1 338 ? 1.24527   -34.17279 93.83724  1.000 47.79321  ? 364 THR B CA  1 
ATOM   5342 C  C   . THR B  1 338 ? 1.82875   -35.57912 93.76532  1.000 46.70724  ? 364 THR B C   1 
ATOM   5343 O  O   . THR B  1 338 ? 3.01803   -35.75355 93.47256  1.000 45.11864  ? 364 THR B O   1 
ATOM   5344 C  CB  . THR B  1 338 ? 1.25601   -33.65914 95.27751  1.000 50.31973  ? 364 THR B CB  1 
ATOM   5345 O  OG1 . THR B  1 338 ? 0.68666   -32.34504 95.32138  1.000 52.61408  ? 364 THR B OG1 1 
ATOM   5346 C  CG2 . THR B  1 338 ? 2.67873   -33.60332 95.81512  1.000 51.35405  ? 364 THR B CG2 1 
ATOM   5347 N  N   . LYS B  1 339 ? 1.00198   -36.59602 94.02041  1.000 47.32496  ? 365 LYS B N   1 
ATOM   5348 C  CA  . LYS B  1 339 ? 1.46935   -37.97600 93.91469  1.000 50.05599  ? 365 LYS B CA  1 
ATOM   5349 C  C   . LYS B  1 339 ? 1.82823   -38.32895 92.47456  1.000 51.10541  ? 365 LYS B C   1 
ATOM   5350 O  O   . LYS B  1 339 ? 2.87011   -38.94308 92.21552  1.000 51.79133  ? 365 LYS B O   1 
ATOM   5351 C  CB  . LYS B  1 339 ? 0.40515   -38.93284 94.45303  1.000 51.49659  ? 365 LYS B CB  1 
ATOM   5352 C  CG  . LYS B  1 339 ? 0.72388   -40.40492 94.23430  1.000 52.68756  ? 365 LYS B CG  1 
ATOM   5353 C  CD  . LYS B  1 339 ? -0.37464  -41.29589 94.79434  1.000 53.22934  ? 365 LYS B CD  1 
ATOM   5354 C  CE  . LYS B  1 339 ? 0.01430   -42.76467 94.73313  1.000 53.64791  ? 365 LYS B CE  1 
ATOM   5355 N  NZ  . LYS B  1 339 ? -0.58919  -43.54269 95.85136  1.000 54.82966  ? 365 LYS B NZ  1 
ATOM   5356 N  N   . VAL B  1 340 ? 0.97121   -37.94944 91.52363  1.000 51.19369  ? 366 VAL B N   1 
ATOM   5357 C  CA  . VAL B  1 340 ? 1.21795   -38.27039 90.11916  1.000 51.62979  ? 366 VAL B CA  1 
ATOM   5358 C  C   . VAL B  1 340 ? 2.49111   -37.59114 89.62909  1.000 53.68927  ? 366 VAL B C   1 
ATOM   5359 O  O   . VAL B  1 340 ? 3.29170   -38.19053 88.90050  1.000 53.64094  ? 366 VAL B O   1 
ATOM   5360 C  CB  . VAL B  1 340 ? -0.00041  -37.88176 89.25942  1.000 50.45425  ? 366 VAL B CB  1 
ATOM   5361 C  CG1 . VAL B  1 340 ? 0.34536   -37.94481 87.77920  1.000 49.98304  ? 366 VAL B CG1 1 
ATOM   5362 C  CG2 . VAL B  1 340 ? -1.17858  -38.79119 89.56722  1.000 50.58323  ? 366 VAL B CG2 1 
ATOM   5363 N  N   . LYS B  1 341 ? 2.70845   -36.33705 90.03042  1.000 55.17714  ? 367 LYS B N   1 
ATOM   5364 C  CA  . LYS B  1 341 ? 3.88270   -35.60249 89.57384  1.000 55.14917  ? 367 LYS B CA  1 
ATOM   5365 C  C   . LYS B  1 341 ? 5.17697   -36.07769 90.22210  1.000 59.93549  ? 367 LYS B C   1 
ATOM   5366 O  O   . LYS B  1 341 ? 6.25233   -35.62914 89.81068  1.000 61.65766  ? 367 LYS B O   1 
ATOM   5367 C  CB  . LYS B  1 341 ? 3.69844   -34.10669 89.83311  1.000 53.27852  ? 367 LYS B CB  1 
ATOM   5368 C  CG  . LYS B  1 341 ? 3.20590   -33.32828 88.62442  1.000 51.59364  ? 367 LYS B CG  1 
ATOM   5369 C  CD  . LYS B  1 341 ? 2.52930   -32.03237 89.03605  1.000 50.72918  ? 367 LYS B CD  1 
ATOM   5370 C  CE  . LYS B  1 341 ? 3.42537   -31.19642 89.93421  1.000 51.88009  ? 367 LYS B CE  1 
ATOM   5371 N  NZ  . LYS B  1 341 ? 2.73675   -29.96371 90.40647  1.000 52.47374  ? 367 LYS B NZ  1 
ATOM   5372 N  N   . SER B  1 342 ? 5.10705   -36.96729 91.21093  1.000 61.63702  ? 368 SER B N   1 
ATOM   5373 C  CA  . SER B  1 342 ? 6.29972   -37.44237 91.90131  1.000 64.95684  ? 368 SER B CA  1 
ATOM   5374 C  C   . SER B  1 342 ? 7.03245   -38.54361 91.14525  1.000 66.54961  ? 368 SER B C   1 
ATOM   5375 O  O   . SER B  1 342 ? 8.03636   -39.05511 91.65291  1.000 66.88373  ? 368 SER B O   1 
ATOM   5376 C  CB  . SER B  1 342 ? 5.93242   -37.94001 93.30244  1.000 65.19172  ? 368 SER B CB  1 
ATOM   5377 O  OG  . SER B  1 342 ? 5.41619   -39.25911 93.25756  1.000 65.13637  ? 368 SER B OG  1 
ATOM   5378 N  N   . GLY B  1 343 ? 6.56632   -38.91948 89.95886  1.000 67.47420  ? 369 GLY B N   1 
ATOM   5379 C  CA  . GLY B  1 343 ? 7.21392   -39.96244 89.18502  1.000 68.66472  ? 369 GLY B CA  1 
ATOM   5380 C  C   . GLY B  1 343 ? 8.33140   -39.44752 88.29891  1.000 69.66436  ? 369 GLY B C   1 
ATOM   5381 O  O   . GLY B  1 343 ? 9.48174   -39.34906 88.72631  1.000 70.45191  ? 369 GLY B O   1 
HETATM 5382 C  C1  . PGE C  2 .   ? 11.07664  -15.90217 44.27731  1.000 52.18171  ? 401 PGE A C1  1 
HETATM 5383 O  O1  . PGE C  2 .   ? 11.69087  -16.67361 45.30054  1.000 52.24048  ? 401 PGE A O1  1 
HETATM 5384 C  C2  . PGE C  2 .   ? 11.17121  -16.66140 42.96966  1.000 53.32263  ? 401 PGE A C2  1 
HETATM 5385 O  O2  . PGE C  2 .   ? 11.01228  -15.75864 41.89437  1.000 53.95743  ? 401 PGE A O2  1 
HETATM 5386 C  C3  . PGE C  2 .   ? 10.74527  -16.39657 40.66221  1.000 53.47628  ? 401 PGE A C3  1 
HETATM 5387 C  C4  . PGE C  2 .   ? 11.03791  -15.42468 39.53657  1.000 52.46184  ? 401 PGE A C4  1 
HETATM 5388 O  O4  . PGE C  2 .   ? 10.39740  -15.18239 34.86796  1.000 51.86213  ? 401 PGE A O4  1 
HETATM 5389 C  C6  . PGE C  2 .   ? 9.76327   -15.45131 36.11092  1.000 51.88402  ? 401 PGE A C6  1 
HETATM 5390 C  C5  . PGE C  2 .   ? 10.82310  -15.55193 37.18864  1.000 52.21405  ? 401 PGE A C5  1 
HETATM 5391 O  O3  . PGE C  2 .   ? 10.19574  -15.72485 38.44264  1.000 52.34342  ? 401 PGE A O3  1 
HETATM 5392 C  C1  . PEG D  3 .   ? -14.01189 -5.13819  36.90337  1.000 66.09911  ? 402 PEG A C1  1 
HETATM 5393 O  O1  . PEG D  3 .   ? -15.34803 -5.49174  37.13345  1.000 65.54523  ? 402 PEG A O1  1 
HETATM 5394 C  C2  . PEG D  3 .   ? -13.69361 -5.28798  35.41749  1.000 66.48381  ? 402 PEG A C2  1 
HETATM 5395 O  O2  . PEG D  3 .   ? -12.44826 -4.71050  35.14769  1.000 67.01484  ? 402 PEG A O2  1 
HETATM 5396 C  C3  . PEG D  3 .   ? -12.45956 -3.81935  34.06930  1.000 67.37416  ? 402 PEG A C3  1 
HETATM 5397 C  C4  . PEG D  3 .   ? -11.04893 -3.28430  33.83192  1.000 67.61682  ? 402 PEG A C4  1 
HETATM 5398 O  O4  . PEG D  3 .   ? -10.17506 -4.35332  33.59335  1.000 68.01128  ? 402 PEG A O4  1 
HETATM 5399 C  C1  . PEG E  3 .   ? -1.24944  0.21381   29.90900  1.000 59.01850  ? 403 PEG A C1  1 
HETATM 5400 O  O1  . PEG E  3 .   ? -1.39410  0.69804   28.60213  1.000 58.63866  ? 403 PEG A O1  1 
HETATM 5401 C  C2  . PEG E  3 .   ? -2.56003  0.39337   30.67290  1.000 58.65409  ? 403 PEG A C2  1 
HETATM 5402 O  O2  . PEG E  3 .   ? -2.53359  1.60206   31.37738  1.000 59.14370  ? 403 PEG A O2  1 
HETATM 5403 C  C3  . PEG E  3 .   ? -2.65201  1.44718   32.76308  1.000 59.64382  ? 403 PEG A C3  1 
HETATM 5404 C  C4  . PEG E  3 .   ? -2.31632  2.76436   33.45859  1.000 60.54203  ? 403 PEG A C4  1 
HETATM 5405 O  O4  . PEG E  3 .   ? -2.12955  2.53531   34.82866  1.000 60.78719  ? 403 PEG A O4  1 
HETATM 5406 C  C1  . EDO F  4 .   ? 0.95872   -10.82578 44.53981  1.000 31.50598  ? 404 EDO A C1  1 
HETATM 5407 O  O1  . EDO F  4 .   ? 1.09719   -12.19736 44.15160  1.000 29.06927  ? 404 EDO A O1  1 
HETATM 5408 C  C2  . EDO F  4 .   ? 0.14032   -10.08062 43.49363  1.000 31.56438  ? 404 EDO A C2  1 
HETATM 5409 O  O2  . EDO F  4 .   ? 0.00410   -8.70768  43.87295  1.000 32.56399  ? 404 EDO A O2  1 
HETATM 5410 C  C1  . EDO G  4 .   ? 7.17956   -38.52297 33.66809  1.000 66.78365  ? 405 EDO A C1  1 
HETATM 5411 O  O1  . EDO G  4 .   ? 8.15701   -38.02911 34.59104  1.000 66.53561  ? 405 EDO A O1  1 
HETATM 5412 C  C2  . EDO G  4 .   ? 7.75735   -38.51528 32.25907  1.000 67.21767  ? 405 EDO A C2  1 
HETATM 5413 O  O2  . EDO G  4 .   ? 6.79301   -39.05492 31.34816  1.000 67.80334  ? 405 EDO A O2  1 
HETATM 5414 C  C1  . EDO H  4 .   ? 1.16385   -35.69925 49.35173  1.000 62.58718  ? 406 EDO A C1  1 
HETATM 5415 O  O1  . EDO H  4 .   ? -0.15703  -35.15853 49.46908  1.000 62.80636  ? 406 EDO A O1  1 
HETATM 5416 C  C2  . EDO H  4 .   ? 1.17890   -36.77894 48.27599  1.000 62.02015  ? 406 EDO A C2  1 
HETATM 5417 O  O2  . EDO H  4 .   ? 0.30378   -37.84649 48.65720  1.000 61.30459  ? 406 EDO A O2  1 
HETATM 5418 C  C1  . EDO I  4 .   ? 4.98145   -11.84293 32.00208  1.000 40.77842  ? 407 EDO A C1  1 
HETATM 5419 O  O1  . EDO I  4 .   ? 5.98380   -12.63872 32.64479  1.000 42.89234  ? 407 EDO A O1  1 
HETATM 5420 C  C2  . EDO I  4 .   ? 3.62636   -12.52298 32.14532  1.000 37.21634  ? 407 EDO A C2  1 
HETATM 5421 O  O2  . EDO I  4 .   ? 2.58971   -11.61974 31.74397  1.000 34.50937  ? 407 EDO A O2  1 
HETATM 5422 C  C1  . EDO J  4 .   ? -16.41907 -13.96882 40.57763  1.000 53.90111  ? 408 EDO A C1  1 
HETATM 5423 O  O1  . EDO J  4 .   ? -17.20705 -13.96816 41.77343  1.000 54.07850  ? 408 EDO A O1  1 
HETATM 5424 C  C2  . EDO J  4 .   ? -16.31055 -12.54696 40.03992  1.000 53.33584  ? 408 EDO A C2  1 
HETATM 5425 O  O2  . EDO J  4 .   ? -15.49996 -12.54270 38.85951  1.000 52.58055  ? 408 EDO A O2  1 
HETATM 5426 C  C1  . EDO K  4 .   ? -11.49334 -5.30611  43.41331  1.000 65.28511  ? 409 EDO A C1  1 
HETATM 5427 O  O1  . EDO K  4 .   ? -10.55260 -5.84532  44.34875  1.000 64.79261  ? 409 EDO A O1  1 
HETATM 5428 C  C2  . EDO K  4 .   ? -10.81215 -5.10848  42.06428  1.000 65.24568  ? 409 EDO A C2  1 
HETATM 5429 O  O2  . EDO K  4 .   ? -11.70095 -4.42516  41.17327  1.000 64.99507  ? 409 EDO A O2  1 
HETATM 5430 C  C1  . EDO L  4 .   ? 16.90023  -6.98612  30.05929  1.000 53.89716  ? 410 EDO A C1  1 
HETATM 5431 O  O1  . EDO L  4 .   ? 16.47961  -6.41563  28.81451  1.000 53.41079  ? 410 EDO A O1  1 
HETATM 5432 C  C2  . EDO L  4 .   ? 18.41497  -6.87054  30.18727  1.000 53.92159  ? 410 EDO A C2  1 
HETATM 5433 O  O2  . EDO L  4 .   ? 18.79756  -5.49072  30.15629  1.000 53.25819  ? 410 EDO A O2  1 
HETATM 5434 C  C1  . EDO M  4 .   ? -2.61150  2.01917   49.28394  1.000 51.24606  ? 411 EDO A C1  1 
HETATM 5435 O  O1  . EDO M  4 .   ? -2.66259  3.00965   48.25071  1.000 52.23222  ? 411 EDO A O1  1 
HETATM 5436 C  C2  . EDO M  4 .   ? -2.36749  0.65075   48.65997  1.000 49.82695  ? 411 EDO A C2  1 
HETATM 5437 O  O2  . EDO M  4 .   ? -2.33265  -0.35107  49.68213  1.000 48.98808  ? 411 EDO A O2  1 
HETATM 5438 C  C1  . EDO N  4 .   ? 26.48513  0.62592   38.45639  1.000 57.67253  ? 412 EDO A C1  1 
HETATM 5439 O  O1  . EDO N  4 .   ? 26.96124  1.93019   38.10551  1.000 58.39666  ? 412 EDO A O1  1 
HETATM 5440 C  C2  . EDO N  4 .   ? 25.59898  0.08987   37.33803  1.000 56.17497  ? 412 EDO A C2  1 
HETATM 5441 O  O2  . EDO N  4 .   ? 25.05693  -1.17808  37.72442  1.000 54.16766  ? 412 EDO A O2  1 
HETATM 5442 C  C1  . EDO O  4 .   ? -12.54369 -10.59858 30.14916  1.000 57.78155  ? 413 EDO A C1  1 
HETATM 5443 O  O1  . EDO O  4 .   ? -13.22860 -9.52446  30.80395  1.000 57.89765  ? 413 EDO A O1  1 
HETATM 5444 C  C2  . EDO O  4 .   ? -11.46180 -10.03008 29.23883  1.000 57.09596  ? 413 EDO A C2  1 
HETATM 5445 O  O2  . EDO O  4 .   ? -10.71318 -11.09803 28.64888  1.000 56.88725  ? 413 EDO A O2  1 
HETATM 5446 C  C1  . EDO P  4 .   ? -10.03494 -8.13853  25.75368  1.000 56.93419  ? 414 EDO A C1  1 
HETATM 5447 O  O1  . EDO P  4 .   ? -11.26992 -8.41734  26.42205  1.000 56.91854  ? 414 EDO A O1  1 
HETATM 5448 C  C2  . EDO P  4 .   ? -9.79269  -9.18956  24.67693  1.000 57.09304  ? 414 EDO A C2  1 
HETATM 5449 O  O2  . EDO P  4 .   ? -8.50641  -8.97762  24.08381  1.000 57.24039  ? 414 EDO A O2  1 
HETATM 5450 CL CL  . CL  Q  5 .   ? 7.62377   -18.58147 39.24761  1.000 53.04709  ? 415 CL  A CL  1 
HETATM 5451 CL CL  . CL  R  5 .   ? 8.65160   -10.46645 34.99744  1.000 84.92274  ? 416 CL  A CL  1 
HETATM 5452 C  C1  . PEG S  3 .   ? -7.96421  -16.73704 80.75733  1.000 68.96552  ? 401 PEG B C1  1 
HETATM 5453 O  O1  . PEG S  3 .   ? -8.34383  -16.63334 82.10190  1.000 67.96533  ? 401 PEG B O1  1 
HETATM 5454 C  C2  . PEG S  3 .   ? -6.44061  -16.72471 80.65565  1.000 69.06937  ? 401 PEG B C2  1 
HETATM 5455 O  O2  . PEG S  3 .   ? -6.06162  -16.95210 79.32835  1.000 68.70896  ? 401 PEG B O2  1 
HETATM 5456 C  C3  . PEG S  3 .   ? -4.71840  -16.66488 79.06317  1.000 68.28326  ? 401 PEG B C3  1 
HETATM 5457 C  C4  . PEG S  3 .   ? -4.44559  -16.83918 77.57080  1.000 67.94066  ? 401 PEG B C4  1 
HETATM 5458 O  O4  . PEG S  3 .   ? -4.64204  -18.17873 77.21070  1.000 67.77374  ? 401 PEG B O4  1 
HETATM 5459 C  C1  . PEG T  3 .   ? -6.15321  -20.35891 80.19088  1.000 71.37707  ? 402 PEG B C1  1 
HETATM 5460 O  O1  . PEG T  3 .   ? -4.94101  -19.93249 79.63269  1.000 71.13898  ? 402 PEG B O1  1 
HETATM 5461 C  C2  . PEG T  3 .   ? -6.03621  -20.36961 81.71356  1.000 71.99518  ? 402 PEG B C2  1 
HETATM 5462 O  O2  . PEG T  3 .   ? -7.31471  -20.41994 82.27966  1.000 72.04815  ? 402 PEG B O2  1 
HETATM 5463 C  C3  . PEG T  3 .   ? -7.48531  -19.55762 83.36814  1.000 70.95041  ? 402 PEG B C3  1 
HETATM 5464 C  C4  . PEG T  3 .   ? -8.93848  -19.60647 83.83467  1.000 70.46318  ? 402 PEG B C4  1 
HETATM 5465 O  O4  . PEG T  3 .   ? -9.11271  -18.72644 84.91078  1.000 70.28225  ? 402 PEG B O4  1 
HETATM 5466 C  C1  . PEG U  3 .   ? -22.51820 -2.94028  62.14679  1.000 68.93726  ? 403 PEG B C1  1 
HETATM 5467 O  O1  . PEG U  3 .   ? -23.63035 -3.31259  62.91362  1.000 68.21033  ? 403 PEG B O1  1 
HETATM 5468 C  C2  . PEG U  3 .   ? -21.83740 -1.73223  62.78654  1.000 69.39027  ? 403 PEG B C2  1 
HETATM 5469 O  O2  . PEG U  3 .   ? -22.74200 -0.66677  62.84724  1.000 70.58359  ? 403 PEG B O2  1 
HETATM 5470 C  C3  . PEG U  3 .   ? -22.17204 0.54288   63.25860  1.000 71.11298  ? 403 PEG B C3  1 
HETATM 5471 C  C4  . PEG U  3 .   ? -21.41910 1.18148   62.09383  1.000 71.50321  ? 403 PEG B C4  1 
HETATM 5472 O  O4  . PEG U  3 .   ? -21.03204 2.47983   62.45122  1.000 71.14594  ? 403 PEG B O4  1 
HETATM 5473 C  C1  . PEG V  3 .   ? -15.69432 -16.07734 53.58739  1.000 56.27563  ? 404 PEG B C1  1 
HETATM 5474 O  O1  . PEG V  3 .   ? -14.51450 -16.57235 54.15812  1.000 54.52621  ? 404 PEG B O1  1 
HETATM 5475 C  C2  . PEG V  3 .   ? -16.40562 -15.16949 54.58872  1.000 57.94789  ? 404 PEG B C2  1 
HETATM 5476 O  O2  . PEG V  3 .   ? -15.51572 -14.19407 55.05226  1.000 58.77168  ? 404 PEG B O2  1 
HETATM 5477 C  C3  . PEG V  3 .   ? -16.10009 -13.25099 55.90530  1.000 59.18996  ? 404 PEG B C3  1 
HETATM 5478 C  C4  . PEG V  3 .   ? -15.02552 -12.29578 56.42024  1.000 59.65478  ? 404 PEG B C4  1 
HETATM 5479 O  O4  . PEG V  3 .   ? -15.55121 -11.51668 57.45913  1.000 60.33751  ? 404 PEG B O4  1 
HETATM 5480 C  C1  . EDO W  4 .   ? -12.29069 -23.36939 70.50685  1.000 78.04320  ? 405 EDO B C1  1 
HETATM 5481 O  O1  . EDO W  4 .   ? -13.29441 -24.31222 70.11401  1.000 78.50854  ? 405 EDO B O1  1 
HETATM 5482 C  C2  . EDO W  4 .   ? -12.61227 -22.00502 69.90923  1.000 76.95228  ? 405 EDO B C2  1 
HETATM 5483 O  O2  . EDO W  4 .   ? -11.76273 -21.00815 70.48808  1.000 76.39678  ? 405 EDO B O2  1 
HETATM 5484 C  C1  . EDO X  4 .   ? -32.46655 -22.85276 67.61670  1.000 55.72797  ? 406 EDO B C1  1 
HETATM 5485 O  O1  . EDO X  4 .   ? -31.25493 -22.21699 68.03910  1.000 55.16791  ? 406 EDO B O1  1 
HETATM 5486 C  C2  . EDO X  4 .   ? -32.74284 -22.50331 66.15916  1.000 56.13126  ? 406 EDO B C2  1 
HETATM 5487 O  O2  . EDO X  4 .   ? -32.91343 -21.08728 66.03060  1.000 56.30631  ? 406 EDO B O2  1 
HETATM 5488 C  C1  . EDO Y  4 .   ? -22.63313 -23.15403 66.19446  1.000 45.33050  ? 407 EDO B C1  1 
HETATM 5489 O  O1  . EDO Y  4 .   ? -22.86150 -22.27283 65.08970  1.000 44.82247  ? 407 EDO B O1  1 
HETATM 5490 C  C2  . EDO Y  4 .   ? -23.01716 -22.45307 67.49173  1.000 44.40405  ? 407 EDO B C2  1 
HETATM 5491 O  O2  . EDO Y  4 .   ? -22.10894 -21.37651 67.74894  1.000 44.10341  ? 407 EDO B O2  1 
HETATM 5492 C  C1  . EDO Z  4 .   ? -7.87824  -18.03814 76.86157  1.000 66.30010  ? 408 EDO B C1  1 
HETATM 5493 O  O1  . EDO Z  4 .   ? -9.18014  -17.50143 77.12158  1.000 67.09846  ? 408 EDO B O1  1 
HETATM 5494 C  C2  . EDO Z  4 .   ? -7.97782  -19.14733 75.82126  1.000 64.84339  ? 408 EDO B C2  1 
HETATM 5495 O  O2  . EDO Z  4 .   ? -6.71956  -19.82310 75.71808  1.000 64.11988  ? 408 EDO B O2  1 
HETATM 5496 CL CL  . CL  AA 5 .   ? -8.44526  -14.38415 77.77381  1.000 105.44373 ? 409 CL  B CL  1 
HETATM 5497 O  O   . HOH BA 6 .   ? 12.97686  -5.68921  30.90357  1.000 17.71673  ? 501 HOH A O   1 
HETATM 5498 O  O   . HOH BA 6 .   ? -9.65365  -10.40147 42.37315  1.000 25.94728  ? 502 HOH A O   1 
HETATM 5499 O  O   . HOH BA 6 .   ? -11.72230 -33.06791 46.71109  1.000 36.75629  ? 503 HOH A O   1 
HETATM 5500 O  O   . HOH BA 6 .   ? 9.02597   -35.53051 33.05066  1.000 39.71381  ? 504 HOH A O   1 
HETATM 5501 O  O   . HOH BA 6 .   ? 24.65338  -7.72959  51.05939  1.000 31.31624  ? 505 HOH A O   1 
HETATM 5502 O  O   . HOH BA 6 .   ? 11.64284  -8.42020  32.77488  1.000 43.99226  ? 506 HOH A O   1 
HETATM 5503 O  O   . HOH BA 6 .   ? 7.59304   -17.41180 42.07455  1.000 26.94113  ? 507 HOH A O   1 
HETATM 5504 O  O   . HOH BA 6 .   ? -8.40140  -7.01653  40.49713  1.000 40.29109  ? 508 HOH A O   1 
HETATM 5505 O  O   . HOH BA 6 .   ? 7.50242   -4.12501  25.32307  1.000 33.06506  ? 509 HOH A O   1 
HETATM 5506 O  O   . HOH BA 6 .   ? 5.35565   -5.99170  53.59032  1.000 40.31616  ? 510 HOH A O   1 
HETATM 5507 O  O   . HOH BA 6 .   ? 8.35311   12.29622  57.23610  1.000 38.30118  ? 511 HOH A O   1 
HETATM 5508 O  O   . HOH BA 6 .   ? -3.68519  -23.40719 25.91097  1.000 29.95874  ? 512 HOH A O   1 
HETATM 5509 O  O   . HOH BA 6 .   ? -5.09004  -15.79581 22.08128  1.000 34.07578  ? 513 HOH A O   1 
HETATM 5510 O  O   . HOH BA 6 .   ? 23.193    -11.996   42.311    1.000 30.98078  ? 514 HOH A O   1 
HETATM 5511 O  O   . HOH BA 6 .   ? 2.78864   -8.17451  43.88649  1.000 24.01403  ? 515 HOH A O   1 
HETATM 5512 O  O   . HOH BA 6 .   ? -7.95300  -20.92182 51.89445  1.000 25.99390  ? 516 HOH A O   1 
HETATM 5513 O  O   . HOH BA 6 .   ? 13.35082  -3.01853  24.77135  1.000 36.61502  ? 517 HOH A O   1 
HETATM 5514 O  O   . HOH BA 6 .   ? 9.40692   12.07899  51.27877  1.000 32.98561  ? 518 HOH A O   1 
HETATM 5515 O  O   . HOH BA 6 .   ? 3.35378   -16.92619 17.65646  1.000 49.90985  ? 519 HOH A O   1 
HETATM 5516 O  O   . HOH BA 6 .   ? 4.67376   -27.19530 42.07607  1.000 21.07675  ? 520 HOH A O   1 
HETATM 5517 O  O   . HOH BA 6 .   ? -5.51432  -23.18088 53.29537  1.000 33.69573  ? 521 HOH A O   1 
HETATM 5518 O  O   . HOH BA 6 .   ? 22.48564  0.49746   53.68532  1.000 32.83416  ? 522 HOH A O   1 
HETATM 5519 O  O   . HOH BA 6 .   ? 25.33061  4.17389   48.60066  1.000 30.34408  ? 523 HOH A O   1 
HETATM 5520 O  O   . HOH BA 6 .   ? 13.78322  4.07386   61.92985  1.000 30.46232  ? 524 HOH A O   1 
HETATM 5521 O  O   . HOH BA 6 .   ? 18.88161  14.23279  42.68767  1.000 53.15545  ? 525 HOH A O   1 
HETATM 5522 O  O   . HOH BA 6 .   ? -16.72872 -20.99767 30.48138  1.000 41.40074  ? 526 HOH A O   1 
HETATM 5523 O  O   . HOH BA 6 .   ? -5.86626  -40.83081 30.17995  1.000 29.84852  ? 527 HOH A O   1 
HETATM 5524 O  O   . HOH BA 6 .   ? 9.12205   -0.15997  28.46337  1.000 16.42249  ? 528 HOH A O   1 
HETATM 5525 O  O   . HOH BA 6 .   ? -10.45516 -20.44899 24.09424  1.000 49.92564  ? 529 HOH A O   1 
HETATM 5526 O  O   . HOH BA 6 .   ? 15.94725  -11.98282 40.16653  1.000 23.39678  ? 530 HOH A O   1 
HETATM 5527 O  O   . HOH BA 6 .   ? 15.04780  -2.93150  59.13061  1.000 23.05419  ? 531 HOH A O   1 
HETATM 5528 O  O   . HOH BA 6 .   ? -8.11465  -14.47295 45.30847  1.000 22.48713  ? 532 HOH A O   1 
HETATM 5529 O  O   . HOH BA 6 .   ? 12.82173  9.86888   19.98265  1.000 33.36253  ? 533 HOH A O   1 
HETATM 5530 O  O   . HOH BA 6 .   ? -4.92569  -6.78879  51.31856  1.000 29.39401  ? 534 HOH A O   1 
HETATM 5531 O  O   . HOH BA 6 .   ? 21.26468  6.89295   56.02109  1.000 59.10534  ? 535 HOH A O   1 
HETATM 5532 O  O   . HOH BA 6 .   ? 12.91929  -1.38593  64.46160  1.000 39.02368  ? 536 HOH A O   1 
HETATM 5533 O  O   . HOH BA 6 .   ? -5.44920  -26.85852 46.69571  1.000 30.69725  ? 537 HOH A O   1 
HETATM 5534 O  O   . HOH BA 6 .   ? 2.75248   -3.31805  51.47511  1.000 22.99992  ? 538 HOH A O   1 
HETATM 5535 O  O   . HOH BA 6 .   ? 5.97036   -1.47942  26.37839  1.000 30.91516  ? 539 HOH A O   1 
HETATM 5536 O  O   . HOH BA 6 .   ? -10.50305 -2.09082  40.72967  1.000 38.77724  ? 540 HOH A O   1 
HETATM 5537 O  O   . HOH BA 6 .   ? -6.08866  -15.77866 29.25448  1.000 29.55635  ? 541 HOH A O   1 
HETATM 5538 O  O   . HOH BA 6 .   ? 14.608    -18.782   35.034    1.000 39.68865  ? 542 HOH A O   1 
HETATM 5539 O  O   . HOH BA 6 .   ? 2.72679   5.92461   18.22521  1.000 44.38192  ? 543 HOH A O   1 
HETATM 5540 O  O   . HOH BA 6 .   ? -6.28524  -18.35246 39.23169  1.000 28.28385  ? 544 HOH A O   1 
HETATM 5541 O  O   . HOH BA 6 .   ? 15.13503  -11.09680 61.43476  1.000 33.27567  ? 545 HOH A O   1 
HETATM 5542 O  O   . HOH BA 6 .   ? 0.00906   -30.99742 45.43922  1.000 27.63458  ? 546 HOH A O   1 
HETATM 5543 O  O   . HOH BA 6 .   ? 5.76664   -19.63922 34.28468  1.000 47.44848  ? 547 HOH A O   1 
HETATM 5544 O  O   . HOH BA 6 .   ? 17.51451  -3.57320  53.83102  1.000 16.49412  ? 548 HOH A O   1 
HETATM 5545 O  O   . HOH BA 6 .   ? 2.29413   8.54132   25.80883  1.000 56.71274  ? 549 HOH A O   1 
HETATM 5546 O  O   . HOH BA 6 .   ? -1.414    6.095     37.636    1.000 38.66712  ? 550 HOH A O   1 
HETATM 5547 O  O   . HOH BA 6 .   ? 5.86823   -1.47513  38.07290  1.000 14.83061  ? 551 HOH A O   1 
HETATM 5548 O  O   . HOH BA 6 .   ? 15.477    -4.840    64.325    1.000 30.40850  ? 552 HOH A O   1 
HETATM 5549 O  O   . HOH BA 6 .   ? -9.23839  -22.76948 50.80649  1.000 29.10892  ? 553 HOH A O   1 
HETATM 5550 O  O   . HOH BA 6 .   ? 6.70549   0.73727   27.84684  1.000 26.63135  ? 554 HOH A O   1 
HETATM 5551 O  O   . HOH BA 6 .   ? 22.26618  4.53710   46.38070  1.000 17.97923  ? 555 HOH A O   1 
HETATM 5552 O  O   . HOH BA 6 .   ? 7.99845   -11.70940 55.10863  1.000 40.88803  ? 556 HOH A O   1 
HETATM 5553 O  O   . HOH BA 6 .   ? 2.673     9.289     39.350    1.000 36.49239  ? 557 HOH A O   1 
HETATM 5554 O  O   . HOH BA 6 .   ? 4.04696   -30.84967 23.39734  1.000 38.74713  ? 558 HOH A O   1 
HETATM 5555 O  O   . HOH BA 6 .   ? 17.59697  15.18993  33.45971  1.000 31.09180  ? 559 HOH A O   1 
HETATM 5556 O  O   . HOH BA 6 .   ? -4.70328  4.66268   43.75381  1.000 23.53561  ? 560 HOH A O   1 
HETATM 5557 O  O   . HOH BA 6 .   ? 10.93944  14.16283  32.66647  1.000 34.49038  ? 561 HOH A O   1 
HETATM 5558 O  O   . HOH BA 6 .   ? 21.42925  -11.59398 45.64760  1.000 29.70758  ? 562 HOH A O   1 
HETATM 5559 O  O   . HOH BA 6 .   ? 10.42018  -33.58839 29.99401  1.000 40.37569  ? 563 HOH A O   1 
HETATM 5560 O  O   . HOH BA 6 .   ? -13.64470 -33.83706 38.06031  1.000 46.58458  ? 564 HOH A O   1 
HETATM 5561 O  O   . HOH BA 6 .   ? 18.150    -17.913   52.004    1.000 49.84017  ? 565 HOH A O   1 
HETATM 5562 O  O   . HOH BA 6 .   ? -3.232    -23.965   18.167    1.000 37.86334  ? 566 HOH A O   1 
HETATM 5563 O  O   . HOH BA 6 .   ? -10.19271 -9.84645  44.92385  1.000 32.90276  ? 567 HOH A O   1 
HETATM 5564 O  O   . HOH BA 6 .   ? -7.02154  -28.89492 47.13633  1.000 32.22608  ? 568 HOH A O   1 
HETATM 5565 O  O   . HOH BA 6 .   ? 16.75661  -3.39357  42.10089  1.000 23.93863  ? 569 HOH A O   1 
HETATM 5566 O  O   . HOH BA 6 .   ? -0.231    6.254     33.331    1.000 34.20750  ? 570 HOH A O   1 
HETATM 5567 O  O   . HOH BA 6 .   ? -12.67525 -28.92607 46.90075  1.000 37.71590  ? 571 HOH A O   1 
HETATM 5568 O  O   . HOH BA 6 .   ? 0.47795   1.79254   47.70776  1.000 30.80753  ? 572 HOH A O   1 
HETATM 5569 O  O   . HOH BA 6 .   ? -1.48950  -18.42438 54.89099  1.000 39.80546  ? 573 HOH A O   1 
HETATM 5570 O  O   . HOH BA 6 .   ? 1.73984   -11.97777 54.11603  1.000 32.21508  ? 574 HOH A O   1 
HETATM 5571 O  O   . HOH BA 6 .   ? 18.553    14.013    29.069    1.000 38.60763  ? 575 HOH A O   1 
HETATM 5572 O  O   . HOH BA 6 .   ? 4.50219   3.72854   37.96586  1.000 28.73252  ? 576 HOH A O   1 
HETATM 5573 O  O   . HOH BA 6 .   ? 3.22382   -7.88161  31.91433  1.000 29.97670  ? 577 HOH A O   1 
HETATM 5574 O  O   . HOH BA 6 .   ? -7.94046  -8.68896  50.01735  1.000 31.58732  ? 578 HOH A O   1 
HETATM 5575 O  O   . HOH BA 6 .   ? 21.40271  10.17551  51.48976  1.000 36.69227  ? 579 HOH A O   1 
HETATM 5576 O  O   . HOH BA 6 .   ? 29.550    8.395     37.736    1.000 35.20147  ? 580 HOH A O   1 
HETATM 5577 O  O   . HOH BA 6 .   ? 12.69374  -30.56837 35.16709  1.000 35.27235  ? 581 HOH A O   1 
HETATM 5578 O  O   . HOH BA 6 .   ? 1.81078   8.87374   49.33191  1.000 29.89194  ? 582 HOH A O   1 
HETATM 5579 O  O   . HOH BA 6 .   ? -4.15090  4.35478   35.66218  1.000 46.93349  ? 583 HOH A O   1 
HETATM 5580 O  O   . HOH BA 6 .   ? 6.48706   -18.84443 47.49222  1.000 36.88178  ? 584 HOH A O   1 
HETATM 5581 O  O   . HOH BA 6 .   ? 2.47967   -5.04883  53.17076  1.000 25.30542  ? 585 HOH A O   1 
HETATM 5582 O  O   . HOH BA 6 .   ? -10.32329 -20.25841 54.54965  1.000 45.70626  ? 586 HOH A O   1 
HETATM 5583 O  O   . HOH BA 6 .   ? 9.13356   -5.52333  57.34168  1.000 35.34436  ? 587 HOH A O   1 
HETATM 5584 O  O   . HOH BA 6 .   ? 10.78549  -13.23385 32.80023  1.000 60.87197  ? 588 HOH A O   1 
HETATM 5585 O  O   . HOH BA 6 .   ? 21.53583  -12.80158 53.79011  1.000 27.52575  ? 589 HOH A O   1 
HETATM 5586 O  O   . HOH BA 6 .   ? 14.34899  -15.42454 43.61944  1.000 43.99780  ? 590 HOH A O   1 
HETATM 5587 O  O   . HOH BA 6 .   ? 18.56162  -16.77668 56.27105  1.000 37.96216  ? 591 HOH A O   1 
HETATM 5588 O  O   . HOH BA 6 .   ? 12.29848  -8.76161  56.99598  1.000 22.01139  ? 592 HOH A O   1 
HETATM 5589 O  O   . HOH BA 6 .   ? 24.92673  0.68777   52.37977  1.000 40.40415  ? 593 HOH A O   1 
HETATM 5590 O  O   . HOH BA 6 .   ? -13.12846 -31.02529 38.17073  1.000 44.88434  ? 594 HOH A O   1 
HETATM 5591 O  O   . HOH BA 6 .   ? -10.71308 -30.67638 47.13592  1.000 28.89660  ? 595 HOH A O   1 
HETATM 5592 O  O   . HOH BA 6 .   ? 5.56001   -14.71259 47.54901  1.000 43.26832  ? 596 HOH A O   1 
HETATM 5593 O  O   . HOH BA 6 .   ? 16.990    -11.013   66.454    1.000 27.86613  ? 597 HOH A O   1 
HETATM 5594 O  O   . HOH BA 6 .   ? -4.41809  -45.76510 36.50915  1.000 53.91339  ? 598 HOH A O   1 
HETATM 5595 O  O   . HOH BA 6 .   ? 4.82158   12.47236  38.23436  1.000 42.52535  ? 599 HOH A O   1 
HETATM 5596 O  O   . HOH BA 6 .   ? -0.08185  -33.67802 46.36969  1.000 40.94311  ? 600 HOH A O   1 
HETATM 5597 O  O   . HOH BA 6 .   ? -9.79629  0.38302   46.85329  1.000 35.25247  ? 601 HOH A O   1 
HETATM 5598 O  O   . HOH BA 6 .   ? 6.102     -38.037   28.704    1.000 41.79290  ? 602 HOH A O   1 
HETATM 5599 O  O   . HOH BA 6 .   ? -14.26757 -36.46639 47.39722  1.000 44.52191  ? 603 HOH A O   1 
HETATM 5600 O  O   . HOH BA 6 .   ? 16.71162  -8.52300  34.26763  1.000 42.72060  ? 604 HOH A O   1 
HETATM 5601 O  O   . HOH BA 6 .   ? -4.55929  -0.98269  51.48135  1.000 46.39902  ? 605 HOH A O   1 
HETATM 5602 O  O   . HOH BA 6 .   ? 7.50673   12.72259  48.83450  1.000 28.09479  ? 606 HOH A O   1 
HETATM 5603 O  O   . HOH BA 6 .   ? 14.15101  -16.77628 51.64667  1.000 25.33364  ? 607 HOH A O   1 
HETATM 5604 O  O   . HOH BA 6 .   ? -7.45969  -7.75815  46.81350  1.000 59.45346  ? 608 HOH A O   1 
HETATM 5605 O  O   . HOH BA 6 .   ? 18.53788  -2.38035  58.95196  1.000 33.75392  ? 609 HOH A O   1 
HETATM 5606 O  O   . HOH BA 6 .   ? -1.07492  -2.04223  47.40223  1.000 21.88462  ? 610 HOH A O   1 
HETATM 5607 O  O   . HOH BA 6 .   ? 20.81128  -8.11320  36.43034  1.000 28.02401  ? 611 HOH A O   1 
HETATM 5608 O  O   . HOH BA 6 .   ? -12.71000 -14.67697 29.62886  1.000 52.88214  ? 612 HOH A O   1 
HETATM 5609 O  O   . HOH BA 6 .   ? -2.53245  -0.49540  52.63842  1.000 58.10280  ? 613 HOH A O   1 
HETATM 5610 O  O   . HOH BA 6 .   ? -1.85194  -23.94478 52.08861  1.000 31.39941  ? 614 HOH A O   1 
HETATM 5611 O  O   . HOH BA 6 .   ? -13.77450 -7.45229  39.20334  1.000 36.84626  ? 615 HOH A O   1 
HETATM 5612 O  O   . HOH BA 6 .   ? 4.11352   -37.52334 40.08114  1.000 33.34678  ? 616 HOH A O   1 
HETATM 5613 O  O   . HOH BA 6 .   ? -1.21385  -9.81792  56.88450  1.000 39.20166  ? 617 HOH A O   1 
HETATM 5614 O  O   . HOH BA 6 .   ? 17.54342  6.26086   22.98431  1.000 34.42701  ? 618 HOH A O   1 
HETATM 5615 O  O   . HOH BA 6 .   ? 1.47061   -2.54939  49.08332  1.000 22.24765  ? 619 HOH A O   1 
HETATM 5616 O  O   . HOH BA 6 .   ? 1.55610   -33.56901 24.79612  1.000 38.36993  ? 620 HOH A O   1 
HETATM 5617 O  O   . HOH BA 6 .   ? 23.46283  1.76764   55.84211  1.000 45.23172  ? 621 HOH A O   1 
HETATM 5618 O  O   . HOH BA 6 .   ? -6.17835  2.40164   48.84450  1.000 41.98267  ? 622 HOH A O   1 
HETATM 5619 O  O   . HOH BA 6 .   ? 0.16531   -36.17484 26.77664  1.000 45.92155  ? 623 HOH A O   1 
HETATM 5620 O  O   . HOH BA 6 .   ? 20.582    -14.326   46.742    1.000 40.88019  ? 624 HOH A O   1 
HETATM 5621 O  O   . HOH BA 6 .   ? 3.51982   -12.17764 45.98921  1.000 30.64599  ? 625 HOH A O   1 
HETATM 5622 O  O   . HOH BA 6 .   ? -10.86271 -16.88040 55.22965  1.000 35.55648  ? 626 HOH A O   1 
HETATM 5623 O  O   . HOH BA 6 .   ? 13.06976  13.23838  22.75100  1.000 32.60544  ? 627 HOH A O   1 
HETATM 5624 O  O   . HOH BA 6 .   ? 21.158    -13.338   64.452    1.000 42.01400  ? 628 HOH A O   1 
HETATM 5625 O  O   . HOH BA 6 .   ? 28.37415  -4.40554  54.97392  1.000 42.29404  ? 629 HOH A O   1 
HETATM 5626 O  O   . HOH BA 6 .   ? 14.65263  -27.65155 35.71744  1.000 22.79453  ? 630 HOH A O   1 
HETATM 5627 O  O   . HOH BA 6 .   ? 26.08775  5.36234   26.71877  1.000 38.60678  ? 631 HOH A O   1 
HETATM 5628 O  O   . HOH BA 6 .   ? 4.14381   -30.50206 19.53356  1.000 47.82875  ? 632 HOH A O   1 
HETATM 5629 O  O   . HOH BA 6 .   ? 12.80182  -4.89423  64.71624  1.000 37.10899  ? 633 HOH A O   1 
HETATM 5630 O  O   . HOH BA 6 .   ? -8.66189  -20.11062 39.65904  1.000 20.04211  ? 634 HOH A O   1 
HETATM 5631 O  O   . HOH BA 6 .   ? -9.683    -49.330   33.015    1.000 40.26737  ? 635 HOH A O   1 
HETATM 5632 O  O   . HOH BA 6 .   ? -17.16639 -27.12328 41.51511  1.000 42.08262  ? 636 HOH A O   1 
HETATM 5633 O  O   . HOH BA 6 .   ? -13.48428 -32.77534 30.58462  1.000 47.76406  ? 637 HOH A O   1 
HETATM 5634 O  O   . HOH BA 6 .   ? 9.72686   -33.68508 38.99013  1.000 38.23435  ? 638 HOH A O   1 
HETATM 5635 O  O   . HOH BA 6 .   ? 9.42995   -33.16344 27.63483  1.000 38.91856  ? 639 HOH A O   1 
HETATM 5636 O  O   . HOH BA 6 .   ? -8.31853  -36.12385 24.83473  1.000 37.76567  ? 640 HOH A O   1 
HETATM 5637 O  O   . HOH BA 6 .   ? 21.941    -12.439   37.998    1.000 43.85441  ? 641 HOH A O   1 
HETATM 5638 O  O   . HOH BA 6 .   ? 7.69837   -12.77901 41.51416  1.000 39.59149  ? 642 HOH A O   1 
HETATM 5639 O  O   . HOH BA 6 .   ? 18.26813  -15.65996 45.76376  1.000 34.50587  ? 643 HOH A O   1 
HETATM 5640 O  O   . HOH BA 6 .   ? 1.32733   0.18026   49.58066  1.000 30.20686  ? 644 HOH A O   1 
HETATM 5641 O  O   . HOH BA 6 .   ? 1.17978   5.60381   22.89255  1.000 42.37910  ? 645 HOH A O   1 
HETATM 5642 O  O   . HOH BA 6 .   ? -2.365    -45.259   40.219    1.000 40.80913  ? 646 HOH A O   1 
HETATM 5643 O  O   . HOH BA 6 .   ? 12.05841  -19.67941 44.19564  1.000 57.64011  ? 647 HOH A O   1 
HETATM 5644 O  O   . HOH BA 6 .   ? 7.58325   0.40165   61.69154  1.000 42.67634  ? 648 HOH A O   1 
HETATM 5645 O  O   . HOH BA 6 .   ? 1.832     -40.574   49.512    1.000 54.00230  ? 649 HOH A O   1 
HETATM 5646 O  O   . HOH BA 6 .   ? 6.27633   -29.20814 43.78516  1.000 32.49895  ? 650 HOH A O   1 
HETATM 5647 O  O   . HOH BA 6 .   ? 12.98539  15.59367  34.24566  1.000 49.08912  ? 651 HOH A O   1 
HETATM 5648 O  O   . HOH BA 6 .   ? 18.86108  4.92419   57.26398  1.000 42.98452  ? 652 HOH A O   1 
HETATM 5649 O  O   . HOH BA 6 .   ? 18.91044  12.90765  26.47454  1.000 46.35747  ? 653 HOH A O   1 
HETATM 5650 O  O   . HOH BA 6 .   ? 26.69527  -1.54904  52.16341  1.000 36.12285  ? 654 HOH A O   1 
HETATM 5651 O  O   . HOH BA 6 .   ? 9.71565   13.34256  39.60454  1.000 28.12443  ? 655 HOH A O   1 
HETATM 5652 O  O   . HOH BA 6 .   ? 7.46105   9.72654   18.75176  1.000 37.22651  ? 656 HOH A O   1 
HETATM 5653 O  O   . HOH BA 6 .   ? -15.48506 -33.60253 36.59676  1.000 48.94154  ? 657 HOH A O   1 
HETATM 5654 O  O   . HOH BA 6 .   ? -5.284    -51.965   29.255    1.000 46.21262  ? 658 HOH A O   1 
HETATM 5655 O  O   . HOH BA 6 .   ? 5.32274   4.45297   56.89035  1.000 39.28557  ? 659 HOH A O   1 
HETATM 5656 O  O   . HOH BA 6 .   ? 9.91888   -7.91259  57.98462  1.000 37.17594  ? 660 HOH A O   1 
HETATM 5657 O  O   . HOH BA 6 .   ? -10.57322 -1.59282  48.55668  1.000 34.53806  ? 661 HOH A O   1 
HETATM 5658 O  O   . HOH BA 6 .   ? 8.92364   -20.49253 47.90555  1.000 48.48128  ? 662 HOH A O   1 
HETATM 5659 O  O   . HOH BA 6 .   ? 1.550     14.586    31.695    1.000 55.21683  ? 663 HOH A O   1 
HETATM 5660 O  O   . HOH BA 6 .   ? 11.52335  -17.40907 50.95515  1.000 36.10914  ? 664 HOH A O   1 
HETATM 5661 O  O   . HOH BA 6 .   ? 17.18595  -18.46956 54.62927  1.000 41.48039  ? 665 HOH A O   1 
HETATM 5662 O  O   . HOH BA 6 .   ? 5.05381   -35.21571 42.84264  1.000 38.08035  ? 666 HOH A O   1 
HETATM 5663 O  O   . HOH BA 6 .   ? 3.98953   -28.45976 22.39111  1.000 48.44025  ? 667 HOH A O   1 
HETATM 5664 O  O   . HOH BA 6 .   ? 13.56310  -18.31824 41.39831  1.000 57.91292  ? 668 HOH A O   1 
HETATM 5665 O  O   . HOH BA 6 .   ? 6.32743   -14.73974 38.02143  1.000 52.77989  ? 669 HOH A O   1 
HETATM 5666 O  O   . HOH BA 6 .   ? 10.69344  -17.98712 23.51264  1.000 53.60409  ? 670 HOH A O   1 
HETATM 5667 O  O   . HOH BA 6 .   ? 12.28940  -12.73847 37.85729  1.000 65.81892  ? 671 HOH A O   1 
HETATM 5668 O  O   . HOH BA 6 .   ? 14.54563  -19.11110 39.37392  1.000 58.65444  ? 672 HOH A O   1 
HETATM 5669 O  O   . HOH BA 6 .   ? 27.363    -3.134    49.945    1.000 31.68352  ? 673 HOH A O   1 
HETATM 5670 O  O   . HOH BA 6 .   ? 8.40734   -18.16760 33.45929  1.000 47.61298  ? 674 HOH A O   1 
HETATM 5671 O  O   . HOH BA 6 .   ? 23.01469  4.32164   56.08669  1.000 47.42641  ? 675 HOH A O   1 
HETATM 5672 O  O   . HOH BA 6 .   ? 2.69041   0.63985   51.91126  1.000 33.43426  ? 676 HOH A O   1 
HETATM 5673 O  O   . HOH BA 6 .   ? 5.43678   -10.48413 55.22025  1.000 42.68531  ? 677 HOH A O   1 
HETATM 5674 O  O   . HOH BA 6 .   ? 6.17681   -8.94228  31.26719  1.000 58.84132  ? 678 HOH A O   1 
HETATM 5675 O  O   . HOH BA 6 .   ? -18.12853 -27.28036 37.43905  1.000 39.42868  ? 679 HOH A O   1 
HETATM 5676 O  O   . HOH BA 6 .   ? 16.422    -17.610   27.963    1.000 50.21437  ? 680 HOH A O   1 
HETATM 5677 O  O   . HOH BA 6 .   ? 12.87248  16.02083  25.30772  1.000 55.71120  ? 681 HOH A O   1 
HETATM 5678 O  O   . HOH BA 6 .   ? -4.67919  -15.69975 19.48132  1.000 40.81818  ? 682 HOH A O   1 
HETATM 5679 O  O   . HOH BA 6 .   ? -15.57720 -17.32207 28.37851  1.000 46.09639  ? 683 HOH A O   1 
HETATM 5680 O  O   . HOH BA 6 .   ? 12.05237  15.06029  53.53316  1.000 50.13277  ? 684 HOH A O   1 
HETATM 5681 O  O   . HOH BA 6 .   ? 14.44970  -8.01247  32.13504  1.000 39.30219  ? 685 HOH A O   1 
HETATM 5682 O  O   . HOH BA 6 .   ? 16.56142  -8.37799  19.90766  1.000 52.86955  ? 686 HOH A O   1 
HETATM 5683 O  O   . HOH BA 6 .   ? 5.71835   -28.15839 17.96957  1.000 61.54298  ? 687 HOH A O   1 
HETATM 5684 O  O   . HOH BA 6 .   ? 2.65717   -31.11708 44.00293  1.000 45.37278  ? 688 HOH A O   1 
HETATM 5685 O  O   . HOH BA 6 .   ? 10.62250  -21.20894 45.26298  1.000 59.82240  ? 689 HOH A O   1 
HETATM 5686 O  O   . HOH BA 6 .   ? -11.74852 -22.50613 52.35418  1.000 30.76203  ? 690 HOH A O   1 
HETATM 5687 O  O   . HOH BA 6 .   ? 17.04370  -14.18056 41.69798  1.000 57.50885  ? 691 HOH A O   1 
HETATM 5688 O  O   . HOH BA 6 .   ? -17.39116 -16.40749 49.74549  1.000 51.44679  ? 692 HOH A O   1 
HETATM 5689 O  O   . HOH BA 6 .   ? -10.19869 -9.07465  50.76326  1.000 36.41318  ? 693 HOH A O   1 
HETATM 5690 O  O   . HOH BA 6 .   ? 1.54497   2.73131   53.76607  1.000 49.35132  ? 694 HOH A O   1 
HETATM 5691 O  O   . HOH BA 6 .   ? 6.70435   -31.64295 43.17787  1.000 48.15969  ? 695 HOH A O   1 
HETATM 5692 O  O   . HOH BA 6 .   ? -6.63372  1.35105   50.94368  1.000 44.02266  ? 696 HOH A O   1 
HETATM 5693 O  O   . HOH BA 6 .   ? 8.35863   -10.06682 22.30481  1.000 43.29756  ? 697 HOH A O   1 
HETATM 5694 O  O   . HOH BA 6 .   ? 9.60930   -31.63398 43.63061  1.000 38.13787  ? 698 HOH A O   1 
HETATM 5695 O  O   . HOH BA 6 .   ? 9.73761   1.92045   65.67114  1.000 53.89647  ? 699 HOH A O   1 
HETATM 5696 O  O   . HOH CA 6 .   ? -10.51896 -16.37760 88.17668  1.000 69.48071  ? 501 HOH B O   1 
HETATM 5697 O  O   . HOH CA 6 .   ? -14.21727 -25.95554 95.84471  1.000 41.75685  ? 502 HOH B O   1 
HETATM 5698 O  O   . HOH CA 6 .   ? -7.54440  -46.48374 75.43550  1.000 49.80173  ? 503 HOH B O   1 
HETATM 5699 O  O   . HOH CA 6 .   ? -17.27010 -12.01377 59.90559  1.000 31.56505  ? 504 HOH B O   1 
HETATM 5700 O  O   . HOH CA 6 .   ? -24.40152 -31.28788 85.72868  1.000 39.15528  ? 505 HOH B O   1 
HETATM 5701 O  O   . HOH CA 6 .   ? -9.24273  -41.20974 66.08341  1.000 32.00842  ? 506 HOH B O   1 
HETATM 5702 O  O   . HOH CA 6 .   ? -10.26085 -42.20134 97.77074  1.000 24.91718  ? 507 HOH B O   1 
HETATM 5703 O  O   . HOH CA 6 .   ? -17.77477 -0.85005  90.01664  1.000 36.92223  ? 508 HOH B O   1 
HETATM 5704 O  O   . HOH CA 6 .   ? 4.01368   -29.17745 56.79195  1.000 58.80178  ? 509 HOH B O   1 
HETATM 5705 O  O   . HOH CA 6 .   ? -17.89784 -39.00865 80.61509  1.000 46.16228  ? 510 HOH B O   1 
HETATM 5706 O  O   . HOH CA 6 .   ? 12.39206  -20.72966 76.29990  1.000 36.58901  ? 511 HOH B O   1 
HETATM 5707 O  O   . HOH CA 6 .   ? -34.41807 -13.08384 72.41866  1.000 44.55944  ? 512 HOH B O   1 
HETATM 5708 O  O   . HOH CA 6 .   ? -18.75119 -3.37314  64.01627  1.000 37.20424  ? 513 HOH B O   1 
HETATM 5709 O  O   . HOH CA 6 .   ? -29.32276 -21.94511 79.56628  1.000 50.35111  ? 514 HOH B O   1 
HETATM 5710 O  O   . HOH CA 6 .   ? -23.49333 -8.41823  85.35277  1.000 40.55847  ? 515 HOH B O   1 
HETATM 5711 O  O   . HOH CA 6 .   ? -20.28702 -18.27435 65.55213  1.000 27.01926  ? 516 HOH B O   1 
HETATM 5712 O  O   . HOH CA 6 .   ? -4.27055  -15.90220 58.38695  1.000 35.25469  ? 517 HOH B O   1 
HETATM 5713 O  O   . HOH CA 6 .   ? -9.33718  -13.31023 60.34292  1.000 45.14862  ? 518 HOH B O   1 
HETATM 5714 O  O   . HOH CA 6 .   ? -8.56995  -7.97289  62.22991  1.000 31.65738  ? 519 HOH B O   1 
HETATM 5715 O  O   . HOH CA 6 .   ? -9.06416  -21.67791 80.98398  1.000 45.62341  ? 520 HOH B O   1 
HETATM 5716 O  O   . HOH CA 6 .   ? -17.83211 -32.20778 95.30731  1.000 25.94232  ? 521 HOH B O   1 
HETATM 5717 O  O   . HOH CA 6 .   ? 11.465    -40.630   87.846    1.000 44.48321  ? 522 HOH B O   1 
HETATM 5718 O  O   . HOH CA 6 .   ? -9.42027  -14.85554 58.47105  1.000 38.88037  ? 523 HOH B O   1 
HETATM 5719 O  O   . HOH CA 6 .   ? -29.659   -22.839   84.714    1.000 68.34734  ? 524 HOH B O   1 
HETATM 5720 O  O   . HOH CA 6 .   ? -9.83570  -5.22292  73.60861  1.000 41.01736  ? 525 HOH B O   1 
HETATM 5721 O  O   . HOH CA 6 .   ? -13.01699 -30.32816 66.61270  1.000 32.04008  ? 526 HOH B O   1 
HETATM 5722 O  O   . HOH CA 6 .   ? -24.62020 -32.18906 68.39230  1.000 36.56221  ? 527 HOH B O   1 
HETATM 5723 O  O   . HOH CA 6 .   ? 11.80081  -36.67073 76.48601  1.000 40.16882  ? 528 HOH B O   1 
HETATM 5724 O  O   . HOH CA 6 .   ? -19.48093 -9.81021  59.97445  1.000 29.03948  ? 529 HOH B O   1 
HETATM 5725 O  O   . HOH CA 6 .   ? -11.03582 -32.47463 88.03284  1.000 26.12320  ? 530 HOH B O   1 
HETATM 5726 O  O   . HOH CA 6 .   ? -14.39114 -9.84213  59.18538  1.000 40.60743  ? 531 HOH B O   1 
HETATM 5727 O  O   . HOH CA 6 .   ? -15.03759 2.70390   62.67551  1.000 56.31986  ? 532 HOH B O   1 
HETATM 5728 O  O   . HOH CA 6 .   ? 3.39120   -47.43192 81.71729  1.000 35.70337  ? 533 HOH B O   1 
HETATM 5729 O  O   . HOH CA 6 .   ? -10.83856 -34.27043 101.74411 1.000 41.04149  ? 534 HOH B O   1 
HETATM 5730 O  O   . HOH CA 6 .   ? 1.31209   -29.58262 78.12215  1.000 36.40616  ? 535 HOH B O   1 
HETATM 5731 O  O   . HOH CA 6 .   ? -13.65334 -33.08076 88.03827  1.000 30.00730  ? 536 HOH B O   1 
HETATM 5732 O  O   . HOH CA 6 .   ? -17.71404 -37.24031 68.61188  1.000 45.79661  ? 537 HOH B O   1 
HETATM 5733 O  O   . HOH CA 6 .   ? -9.38810  -21.52814 69.30275  1.000 49.26093  ? 538 HOH B O   1 
HETATM 5734 O  O   . HOH CA 6 .   ? -7.63529  -27.83007 63.20804  1.000 41.97002  ? 539 HOH B O   1 
HETATM 5735 O  O   . HOH CA 6 .   ? -28.06035 5.29787   70.90041  1.000 57.43960  ? 540 HOH B O   1 
HETATM 5736 O  O   . HOH CA 6 .   ? -29.65318 -19.97455 68.15345  1.000 43.74300  ? 541 HOH B O   1 
HETATM 5737 O  O   . HOH CA 6 .   ? -30.43709 -10.41838 65.41059  1.000 43.37730  ? 542 HOH B O   1 
HETATM 5738 O  O   . HOH CA 6 .   ? -1.52545  -13.33572 73.61785  1.000 53.19376  ? 543 HOH B O   1 
HETATM 5739 O  O   . HOH CA 6 .   ? 8.64523   -37.23351 76.54785  1.000 32.91952  ? 544 HOH B O   1 
HETATM 5740 O  O   . HOH CA 6 .   ? -22.06893 -10.61112 92.03383  1.000 57.27899  ? 545 HOH B O   1 
HETATM 5741 O  O   . HOH CA 6 .   ? -23.16164 -12.36710 70.32905  1.000 21.64007  ? 546 HOH B O   1 
HETATM 5742 O  O   . HOH CA 6 .   ? -12.91020 0.61725   67.70042  1.000 33.77739  ? 547 HOH B O   1 
HETATM 5743 O  O   . HOH CA 6 .   ? -32.03044 2.05059   81.15332  1.000 56.76634  ? 548 HOH B O   1 
HETATM 5744 O  O   . HOH CA 6 .   ? -10.17893 -31.21016 78.10005  1.000 36.21850  ? 549 HOH B O   1 
HETATM 5745 O  O   . HOH CA 6 .   ? -14.42206 -30.67853 89.06001  1.000 35.38323  ? 550 HOH B O   1 
HETATM 5746 O  O   . HOH CA 6 .   ? -15.07216 -26.32685 61.39367  1.000 25.29744  ? 551 HOH B O   1 
HETATM 5747 O  O   . HOH CA 6 .   ? -12.90834 -1.54657  69.08312  1.000 37.44194  ? 552 HOH B O   1 
HETATM 5748 O  O   . HOH CA 6 .   ? 7.33960   -31.71090 85.82531  1.000 37.50712  ? 553 HOH B O   1 
HETATM 5749 O  O   . HOH CA 6 .   ? -27.78208 -2.03462  70.10900  1.000 37.39047  ? 554 HOH B O   1 
HETATM 5750 O  O   . HOH CA 6 .   ? 13.779    -32.048   72.984    1.000 48.61277  ? 555 HOH B O   1 
HETATM 5751 O  O   . HOH CA 6 .   ? -2.34337  -19.31301 58.15210  1.000 51.74096  ? 556 HOH B O   1 
HETATM 5752 O  O   . HOH CA 6 .   ? -6.97335  -18.39263 69.18850  1.000 41.10524  ? 557 HOH B O   1 
HETATM 5753 O  O   . HOH CA 6 .   ? -19.50220 1.51515   87.96920  1.000 38.43947  ? 558 HOH B O   1 
HETATM 5754 O  O   . HOH CA 6 .   ? -16.80043 -4.20782  60.60480  1.000 39.86039  ? 559 HOH B O   1 
HETATM 5755 O  O   . HOH CA 6 .   ? -5.75917  -11.49997 63.74733  1.000 45.29409  ? 560 HOH B O   1 
HETATM 5756 O  O   . HOH CA 6 .   ? -17.04376 -6.05630  65.46310  1.000 31.55212  ? 561 HOH B O   1 
HETATM 5757 O  O   . HOH CA 6 .   ? -10.36969 -32.16383 66.08072  1.000 44.39306  ? 562 HOH B O   1 
HETATM 5758 O  O   . HOH CA 6 .   ? 1.936     -45.660   57.487    1.000 37.52669  ? 563 HOH B O   1 
HETATM 5759 O  O   . HOH CA 6 .   ? -8.27447  -29.03811 93.57949  1.000 37.22485  ? 564 HOH B O   1 
HETATM 5760 O  O   . HOH CA 6 .   ? -20.41906 -37.85079 90.19940  1.000 42.22354  ? 565 HOH B O   1 
HETATM 5761 O  O   . HOH CA 6 .   ? -5.76304  -4.55406  90.08069  1.000 51.92530  ? 566 HOH B O   1 
HETATM 5762 O  O   . HOH CA 6 .   ? -2.87333  -30.05530 61.02936  1.000 52.43600  ? 567 HOH B O   1 
HETATM 5763 O  O   . HOH CA 6 .   ? -16.14443 -38.83881 97.96433  1.000 33.06120  ? 568 HOH B O   1 
HETATM 5764 O  O   . HOH CA 6 .   ? 8.50657   -21.44622 58.88923  1.000 37.73747  ? 569 HOH B O   1 
HETATM 5765 O  O   . HOH CA 6 .   ? -18.44114 -24.63955 61.75087  1.000 43.58373  ? 570 HOH B O   1 
HETATM 5766 O  O   . HOH CA 6 .   ? 4.67625   -44.46905 87.58858  1.000 30.16980  ? 571 HOH B O   1 
HETATM 5767 O  O   . HOH CA 6 .   ? 5.98935   -22.38040 60.65491  1.000 65.54852  ? 572 HOH B O   1 
HETATM 5768 O  O   . HOH CA 6 .   ? -31.18079 -18.30554 73.12432  1.000 47.20383  ? 573 HOH B O   1 
HETATM 5769 O  O   . HOH CA 6 .   ? -17.93499 -3.32517  90.78074  1.000 37.68202  ? 574 HOH B O   1 
HETATM 5770 O  O   . HOH CA 6 .   ? -28.66035 -28.07665 73.68787  1.000 37.69264  ? 575 HOH B O   1 
HETATM 5771 O  O   . HOH CA 6 .   ? -6.54542  1.34105   78.56969  1.000 48.90798  ? 576 HOH B O   1 
HETATM 5772 O  O   . HOH CA 6 .   ? -28.03773 -26.25789 63.97771  1.000 70.04989  ? 577 HOH B O   1 
HETATM 5773 O  O   . HOH CA 6 .   ? -6.18723  -12.49040 69.46051  1.000 41.29978  ? 578 HOH B O   1 
HETATM 5774 O  O   . HOH CA 6 .   ? 3.21336   -15.36535 68.86909  1.000 51.61390  ? 579 HOH B O   1 
HETATM 5775 O  O   . HOH CA 6 .   ? -22.327   -33.888   77.677    1.000 48.45816  ? 580 HOH B O   1 
HETATM 5776 O  O   . HOH CA 6 .   ? -9.11355  -45.60850 95.28424  1.000 51.44663  ? 581 HOH B O   1 
HETATM 5777 O  O   . HOH CA 6 .   ? -22.15681 -37.41182 69.14364  1.000 48.72939  ? 582 HOH B O   1 
HETATM 5778 O  O   . HOH CA 6 .   ? -13.14270 -46.11306 92.30080  1.000 39.53086  ? 583 HOH B O   1 
HETATM 5779 O  O   . HOH CA 6 .   ? -3.00145  -15.28313 62.79399  1.000 40.41069  ? 584 HOH B O   1 
HETATM 5780 O  O   . HOH CA 6 .   ? 1.36710   -30.43530 57.10783  1.000 48.44560  ? 585 HOH B O   1 
HETATM 5781 O  O   . HOH CA 6 .   ? -21.33888 -30.75864 80.26367  1.000 74.65271  ? 586 HOH B O   1 
HETATM 5782 O  O   . HOH CA 6 .   ? -14.84495 -28.24689 60.00326  1.000 45.40065  ? 587 HOH B O   1 
HETATM 5783 O  O   . HOH CA 6 .   ? -20.32845 -24.90113 63.84331  1.000 42.11972  ? 588 HOH B O   1 
HETATM 5784 O  O   . HOH CA 6 .   ? 2.02415   -24.05166 61.98612  1.000 47.58244  ? 589 HOH B O   1 
HETATM 5785 O  O   . HOH CA 6 .   ? -7.07380  -11.56691 60.95224  1.000 30.76803  ? 590 HOH B O   1 
HETATM 5786 O  O   . HOH CA 6 .   ? -7.37766  -3.05760  73.03785  1.000 41.70740  ? 591 HOH B O   1 
HETATM 5787 O  O   . HOH CA 6 .   ? -16.66898 -27.44778 57.75923  1.000 46.86635  ? 592 HOH B O   1 
HETATM 5788 O  O   . HOH CA 6 .   ? -37.25847 -11.26918 81.48565  1.000 43.04241  ? 593 HOH B O   1 
HETATM 5789 O  O   . HOH CA 6 .   ? -13.22251 -32.23846 65.19083  1.000 38.45043  ? 594 HOH B O   1 
HETATM 5790 O  O   . HOH CA 6 .   ? -21.92738 -38.30619 83.02667  1.000 56.28466  ? 595 HOH B O   1 
HETATM 5791 O  O   . HOH CA 6 .   ? -2.17469  -21.44885 55.95973  1.000 45.70832  ? 596 HOH B O   1 
HETATM 5792 O  O   . HOH CA 6 .   ? -25.55591 -27.48402 86.68102  1.000 46.92554  ? 597 HOH B O   1 
HETATM 5793 O  O   . HOH CA 6 .   ? -13.27188 -35.13208 65.42737  1.000 42.16713  ? 598 HOH B O   1 
HETATM 5794 O  O   . HOH CA 6 .   ? -7.89909  -8.44994  95.53361  1.000 45.40382  ? 599 HOH B O   1 
HETATM 5795 O  O   . HOH CA 6 .   ? -2.27518  -14.62411 76.57099  1.000 53.39150  ? 600 HOH B O   1 
HETATM 5796 O  O   . HOH CA 6 .   ? -12.591   -36.208   101.703   1.000 36.05691  ? 601 HOH B O   1 
HETATM 5797 O  O   . HOH CA 6 .   ? -11.55770 -1.46383  71.26007  1.000 37.82106  ? 602 HOH B O   1 
HETATM 5798 O  O   . HOH CA 6 .   ? -23.34862 15.29175  80.91228  1.000 76.64662  ? 603 HOH B O   1 
HETATM 5799 O  O   . HOH CA 6 .   ? -14.97402 -36.33064 99.91864  1.000 48.13044  ? 604 HOH B O   1 
HETATM 5800 O  O   . HOH CA 6 .   ? -20.77217 -13.24089 54.36999  1.000 42.28063  ? 605 HOH B O   1 
HETATM 5801 O  O   . HOH CA 6 .   ? -1.40766  -5.68155  68.10832  1.000 38.45237  ? 606 HOH B O   1 
HETATM 5802 O  O   . HOH CA 6 .   ? -14.24602 -32.13344 61.83046  1.000 52.88692  ? 607 HOH B O   1 
HETATM 5803 O  O   . HOH CA 6 .   ? -2.92651  -25.27964 58.45188  1.000 50.59165  ? 608 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLN A 3   ? 0.81764 0.61159 1.07969 -0.09162 -0.01635 -0.09575 29  GLN A N   
2    C CA  . GLN A 3   ? 0.82218 0.61315 1.06515 -0.09060 -0.02221 -0.10876 29  GLN A CA  
3    C C   . GLN A 3   ? 0.77555 0.57263 0.99994 -0.08909 -0.02515 -0.10910 29  GLN A C   
4    O O   . GLN A 3   ? 0.78431 0.57783 0.98766 -0.08776 -0.02858 -0.11783 29  GLN A O   
5    C CB  . GLN A 3   ? 0.85928 0.64899 1.11061 -0.09544 -0.02985 -0.12068 29  GLN A CB  
6    C CG  . GLN A 3   ? 0.88875 0.67018 1.15454 -0.09652 -0.02771 -0.12381 29  GLN A CG  
7    C CD  . GLN A 3   ? 0.91401 0.69077 1.17813 -0.10028 -0.03564 -0.13888 29  GLN A CD  
8    O OE1 . GLN A 3   ? 0.92949 0.70254 1.21209 -0.10314 -0.03637 -0.14208 29  GLN A OE1 
9    N NE2 . GLN A 3   ? 0.91322 0.68899 1.15381 -0.10055 -0.04184 -0.14820 29  GLN A NE2 
10   N N   . LYS A 4   ? 0.73602 0.54150 0.96796 -0.08949 -0.02319 -0.09957 30  LYS A N   
11   C CA  . LYS A 4   ? 0.70200 0.51381 0.91954 -0.08798 -0.02597 -0.09909 30  LYS A CA  
12   C C   . LYS A 4   ? 0.64879 0.45634 0.84628 -0.08256 -0.02075 -0.09512 30  LYS A C   
13   O O   . LYS A 4   ? 0.64801 0.45368 0.84927 -0.08012 -0.01360 -0.08492 30  LYS A O   
14   C CB  . LYS A 4   ? 0.71276 0.53472 0.94708 -0.08990 -0.02409 -0.09029 30  LYS A CB  
15   C CG  . LYS A 4   ? 0.74084 0.56743 1.00164 -0.09500 -0.02650 -0.09177 30  LYS A CG  
16   C CD  . LYS A 4   ? 0.75503 0.59335 1.02590 -0.09718 -0.03305 -0.09388 30  LYS A CD  
17   C CE  . LYS A 4   ? 0.76381 0.61016 1.05302 -0.09813 -0.02450 -0.08242 30  LYS A CE  
18   N NZ  . LYS A 4   ? 0.77805 0.63697 1.08596 -0.10052 -0.03056 -0.08518 30  LYS A NZ  
19   N N   . THR A 5   ? 0.62279 0.42822 0.79850 -0.08086 -0.02460 -0.10297 31  THR A N   
20   C CA  . THR A 5   ? 0.58590 0.38720 0.74337 -0.07579 -0.01982 -0.10119 31  THR A CA  
21   C C   . THR A 5   ? 0.53579 0.34164 0.67668 -0.07456 -0.02289 -0.10157 31  THR A C   
22   O O   . THR A 5   ? 0.54176 0.35032 0.67765 -0.07746 -0.03073 -0.10814 31  THR A O   
23   C CB  . THR A 5   ? 0.60048 0.39239 0.74668 -0.07465 -0.01918 -0.11120 31  THR A CB  
24   O OG1 . THR A 5   ? 0.61908 0.40668 0.78259 -0.07507 -0.01603 -0.11008 31  THR A OG1 
25   C CG2 . THR A 5   ? 0.60028 0.38927 0.72982 -0.06938 -0.01402 -0.11017 31  THR A CG2 
26   N N   . LEU A 6   ? 0.49568 0.30211 0.62864 -0.07021 -0.01754 -0.09433 32  LEU A N   
27   C CA  . LEU A 6   ? 0.45877 0.26842 0.57557 -0.06839 -0.01949 -0.09438 32  LEU A CA  
28   C C   . LEU A 6   ? 0.44432 0.25023 0.54895 -0.06315 -0.01315 -0.09107 32  LEU A C   
29   O O   . LEU A 6   ? 0.43183 0.23736 0.54508 -0.06062 -0.00784 -0.08229 32  LEU A O   
30   C CB  . LEU A 6   ? 0.43792 0.25653 0.56586 -0.06937 -0.02045 -0.08648 32  LEU A CB  
31   C CG  . LEU A 6   ? 0.34322 0.16561 0.45777 -0.06707 -0.02234 -0.08520 32  LEU A CG  
32   C CD1 . LEU A 6   ? 0.35347 0.17433 0.45194 -0.06852 -0.03109 -0.09562 32  LEU A CD1 
33   C CD2 . LEU A 6   ? 0.38045 0.21152 0.51029 -0.06811 -0.02187 -0.07749 32  LEU A CD2 
34   N N   . HIS A 7   ? 0.45205 0.25476 0.53661 -0.06172 -0.01401 -0.09790 33  HIS A N   
35   C CA  . HIS A 7   ? 0.45415 0.25387 0.52874 -0.05689 -0.00786 -0.09649 33  HIS A CA  
36   C C   . HIS A 7   ? 0.44954 0.25263 0.51062 -0.05505 -0.00842 -0.09402 33  HIS A C   
37   O O   . HIS A 7   ? 0.45608 0.25792 0.50190 -0.05695 -0.01293 -0.10065 33  HIS A O   
38   C CB  . HIS A 7   ? 0.49535 0.28750 0.55895 -0.05669 -0.00596 -0.10704 33  HIS A CB  
39   C CG  . HIS A 7   ? 0.55788 0.34834 0.62272 -0.05170 0.00152  -0.10523 33  HIS A CG  
40   N ND1 . HIS A 7   ? 0.59362 0.37842 0.65151 -0.05066 0.00566  -0.11418 33  HIS A ND1 
41   C CD2 . HIS A 7   ? 0.56493 0.35879 0.63830 -0.04752 0.00522  -0.09577 33  HIS A CD2 
42   C CE1 . HIS A 7   ? 0.58457 0.37093 0.64992 -0.04599 0.01182  -0.11032 33  HIS A CE1 
43   N NE2 . HIS A 7   ? 0.56922 0.36067 0.64327 -0.04402 0.01076  -0.09909 33  HIS A NE2 
44   N N   . ILE A 8   ? 0.42996 0.23621 0.49551 -0.05145 -0.00446 -0.08457 34  ILE A N   
45   C CA  . ILE A 8   ? 0.40992 0.21962 0.46569 -0.04951 -0.00464 -0.08109 34  ILE A CA  
46   C C   . ILE A 8   ? 0.40142 0.20917 0.44980 -0.04484 0.00097  -0.07956 34  ILE A C   
47   O O   . ILE A 8   ? 0.37439 0.18058 0.43193 -0.04228 0.00446  -0.07623 34  ILE A O   
48   C CB  . ILE A 8   ? 0.39573 0.21088 0.46320 -0.04964 -0.00508 -0.07131 34  ILE A CB  
49   C CG1 . ILE A 8   ? 0.40590 0.22434 0.48681 -0.05436 -0.00940 -0.07239 34  ILE A CG1 
50   C CG2 . ILE A 8   ? 0.36879 0.18977 0.42421 -0.04714 -0.00616 -0.06756 34  ILE A CG2 
51   C CD1 . ILE A 8   ? 0.39816 0.22189 0.49181 -0.05515 -0.00783 -0.06329 34  ILE A CD1 
52   N N   . TYR A 9   ? 0.40155 0.20956 0.43477 -0.04382 0.00140  -0.08191 35  TYR A N   
53   C CA  . TYR A 9   ? 0.39453 0.20212 0.42198 -0.03970 0.00684  -0.08041 35  TYR A CA  
54   C C   . TYR A 9   ? 0.35762 0.16984 0.37820 -0.03785 0.00588  -0.07398 35  TYR A C   
55   O O   . TYR A 9   ? 0.31486 0.13013 0.32103 -0.03885 0.00231  -0.07497 35  TYR A O   
56   C CB  . TYR A 9   ? 0.44761 0.25067 0.46068 -0.04033 0.01026  -0.08999 35  TYR A CB  
57   C CG  . TYR A 9   ? 0.46183 0.26507 0.47906 -0.03639 0.01748  -0.08999 35  TYR A CG  
58   C CD1 . TYR A 9   ? 0.43363 0.23888 0.46937 -0.03321 0.01865  -0.08453 35  TYR A CD1 
59   C CD2 . TYR A 9   ? 0.46207 0.26331 0.46542 -0.03617 0.02314  -0.09539 35  TYR A CD2 
60   C CE1 . TYR A 9   ? 0.44644 0.25283 0.48962 -0.02968 0.02416  -0.08501 35  TYR A CE1 
61   C CE2 . TYR A 9   ? 0.46612 0.26889 0.47754 -0.03294 0.03048  -0.09587 35  TYR A CE2 
62   C CZ  . TYR A 9   ? 0.48049 0.28640 0.51322 -0.02957 0.03040  -0.09096 35  TYR A CZ  
63   O OH  . TYR A 9   ? 0.50763 0.31589 0.55161 -0.02644 0.03669  -0.09185 35  TYR A OH  
64   N N   . ASN A 10  ? 0.35362 0.16813 0.38207 -0.03430 0.00749  -0.06569 36  ASN A N   
65   C CA  . ASN A 10  ? 0.33892 0.16031 0.36040 -0.03169 0.00564  -0.05766 36  ASN A CA  
66   C C   . ASN A 10  ? 0.34967 0.17018 0.37371 -0.02756 0.00847  -0.05376 36  ASN A C   
67   O O   . ASN A 10  ? 0.36418 0.17948 0.39892 -0.02651 0.01120  -0.05595 36  ASN A O   
68   C CB  . ASN A 10  ? 0.31471 0.14043 0.34313 -0.03255 0.00283  -0.05040 36  ASN A CB  
69   C CG  . ASN A 10  ? 0.31851 0.15144 0.33870 -0.03047 0.00126  -0.04447 36  ASN A CG  
70   O OD1 . ASN A 10  ? 0.32897 0.16371 0.33819 -0.02858 0.00097  -0.04560 36  ASN A OD1 
71   N ND2 . ASN A 10  ? 0.27319 0.10962 0.29911 -0.03102 0.00113  -0.03831 36  ASN A ND2 
72   N N   . TRP A 11  ? 0.34745 0.17300 0.36342 -0.02512 0.00719  -0.04846 37  TRP A N   
73   C CA  . TRP A 11  ? 0.36819 0.19339 0.38774 -0.02133 0.00779  -0.04403 37  TRP A CA  
74   C C   . TRP A 11  ? 0.36431 0.18643 0.39402 -0.02029 0.00560  -0.03735 37  TRP A C   
75   O O   . TRP A 11  ? 0.33098 0.15314 0.36198 -0.02238 0.00450  -0.03393 37  TRP A O   
76   C CB  . TRP A 11  ? 0.37057 0.20120 0.37935 -0.01932 0.00610  -0.03989 37  TRP A CB  
77   C CG  . TRP A 11  ? 0.40271 0.23446 0.40111 -0.01975 0.00813  -0.04446 37  TRP A CG  
78   C CD1 . TRP A 11  ? 0.41342 0.24664 0.40066 -0.02203 0.00680  -0.04704 37  TRP A CD1 
79   C CD2 . TRP A 11  ? 0.44071 0.27132 0.43894 -0.01807 0.01157  -0.04630 37  TRP A CD2 
80   N NE1 . TRP A 11  ? 0.44135 0.27303 0.41842 -0.02202 0.00940  -0.04967 37  TRP A NE1 
81   C CE2 . TRP A 11  ? 0.44688 0.27732 0.43127 -0.01982 0.01335  -0.04946 37  TRP A CE2 
82   C CE3 . TRP A 11  ? 0.46216 0.29155 0.47190 -0.01542 0.01287  -0.04544 37  TRP A CE3 
83   C CZ2 . TRP A 11  ? 0.47025 0.29900 0.45114 -0.01946 0.01825  -0.05149 37  TRP A CZ2 
84   C CZ3 . TRP A 11  ? 0.46450 0.29373 0.47421 -0.01487 0.01728  -0.04833 37  TRP A CZ3 
85   C CH2 . TRP A 11  ? 0.47107 0.29982 0.46604 -0.01710 0.02085  -0.05119 37  TRP A CH2 
86   N N   . SER A 12  ? 0.37894 0.19777 0.41639 -0.01721 0.00474  -0.03516 38  SER A N   
87   C CA  . SER A 12  ? 0.40378 0.21779 0.44729 -0.01588 0.00091  -0.02728 38  SER A CA  
88   C C   . SER A 12  ? 0.38123 0.19792 0.41159 -0.01522 -0.00162 -0.01960 38  SER A C   
89   O O   . SER A 12  ? 0.38373 0.20536 0.40504 -0.01370 -0.00198 -0.01999 38  SER A O   
90   C CB  . SER A 12  ? 0.45306 0.26355 0.50833 -0.01229 -0.00154 -0.02673 38  SER A CB  
91   O OG  . SER A 12  ? 0.52733 0.34022 0.59176 -0.01238 0.00223  -0.03344 38  SER A OG  
92   N N   . ASP A 13  ? 0.39107 0.20364 0.42031 -0.01667 -0.00248 -0.01283 39  ASP A N   
93   C CA  . ASP A 13  ? 0.43778 0.25107 0.45352 -0.01653 -0.00300 -0.00574 39  ASP A CA  
94   C C   . ASP A 13  ? 0.41659 0.23906 0.42432 -0.01744 0.00002  -0.00907 39  ASP A C   
95   O O   . ASP A 13  ? 0.41789 0.24286 0.41480 -0.01584 -0.00033 -0.00652 39  ASP A O   
96   C CB  . ASP A 13  ? 0.48307 0.29223 0.49241 -0.01281 -0.00847 -0.00102 39  ASP A CB  
97   C CG  . ASP A 13  ? 0.55156 0.35630 0.54536 -0.01324 -0.00906 0.00726  39  ASP A CG  
98   O OD1 . ASP A 13  ? 0.58787 0.38657 0.58097 -0.01589 -0.00701 0.01279  39  ASP A OD1 
99   O OD2 . ASP A 13  ? 0.58476 0.39123 0.56645 -0.01122 -0.01091 0.00802  39  ASP A OD2 
100  N N   . TYR A 14  ? 0.38805 0.21481 0.40141 -0.01995 0.00220  -0.01515 40  TYR A N   
101  C CA  . TYR A 14  ? 0.37841 0.21321 0.38680 -0.02081 0.00327  -0.01823 40  TYR A CA  
102  C C   . TYR A 14  ? 0.38253 0.22007 0.39649 -0.02442 0.00557  -0.01713 40  TYR A C   
103  O O   . TYR A 14  ? 0.40061 0.24422 0.41683 -0.02596 0.00493  -0.02135 40  TYR A O   
104  C CB  . TYR A 14  ? 0.36372 0.20062 0.37199 -0.02102 0.00248  -0.02595 40  TYR A CB  
105  C CG  . TYR A 14  ? 0.36293 0.20607 0.36271 -0.02013 0.00144  -0.02756 40  TYR A CG  
106  C CD1 . TYR A 14  ? 0.35883 0.20503 0.35262 -0.01769 0.00130  -0.02333 40  TYR A CD1 
107  C CD2 . TYR A 14  ? 0.35206 0.19664 0.34878 -0.02175 0.00014  -0.03335 40  TYR A CD2 
108  C CE1 . TYR A 14  ? 0.35009 0.20125 0.33833 -0.01659 0.00003  -0.02470 40  TYR A CE1 
109  C CE2 . TYR A 14  ? 0.32052 0.16932 0.30953 -0.02080 -0.00198 -0.03373 40  TYR A CE2 
110  C CZ  . TYR A 14  ? 0.34260 0.19498 0.32902 -0.01806 -0.00196 -0.02934 40  TYR A CZ  
111  O OH  . TYR A 14  ? 0.35013 0.20602 0.33104 -0.01685 -0.00435 -0.02963 40  TYR A OH  
112  N N   . ILE A 15  ? 0.36993 0.20243 0.38692 -0.02598 0.00790  -0.01116 41  ILE A N   
113  C CA  . ILE A 15  ? 0.37031 0.20495 0.39530 -0.02998 0.01170  -0.00945 41  ILE A CA  
114  C C   . ILE A 15  ? 0.38044 0.20822 0.39998 -0.03064 0.01566  -0.00038 41  ILE A C   
115  O O   . ILE A 15  ? 0.39146 0.21111 0.40350 -0.02843 0.01321  0.00408  41  ILE A O   
116  C CB  . ILE A 15  ? 0.37006 0.20295 0.40924 -0.03356 0.01060  -0.01435 41  ILE A CB  
117  C CG1 . ILE A 15  ? 0.36209 0.20212 0.41217 -0.03741 0.01208  -0.01679 41  ILE A CG1 
118  C CG2 . ILE A 15  ? 0.36922 0.19178 0.41416 -0.03487 0.01173  -0.00948 41  ILE A CG2 
119  C CD1 . ILE A 15  ? 0.35862 0.19748 0.42158 -0.04103 0.00910  -0.02360 41  ILE A CD1 
120  N N   . ALA A 16  ? 0.37897 0.20947 0.40212 -0.03383 0.02176  0.00248  42  ALA A N   
121  C CA  . ALA A 16  ? 0.43416 0.25641 0.44916 -0.03546 0.02729  0.01150  42  ALA A CA  
122  C C   . ALA A 16  ? 0.47719 0.28858 0.49872 -0.03778 0.02611  0.01589  42  ALA A C   
123  O O   . ALA A 16  ? 0.48788 0.30056 0.52567 -0.03997 0.02439  0.01112  42  ALA A O   
124  C CB  . ALA A 16  ? 0.44390 0.27177 0.46428 -0.03902 0.03643  0.01278  42  ALA A CB  
125  N N   . PRO A 17  ? 0.50015 0.29962 0.50867 -0.03734 0.02621  0.02491  43  PRO A N   
126  C CA  . PRO A 17  ? 0.50294 0.29054 0.51826 -0.03867 0.02326  0.02980  43  PRO A CA  
127  C C   . PRO A 17  ? 0.50227 0.28843 0.53449 -0.04449 0.02912  0.03082  43  PRO A C   
128  O O   . PRO A 17  ? 0.50297 0.28151 0.54713 -0.04556 0.02595  0.03155  43  PRO A O   
129  C CB  . PRO A 17  ? 0.52163 0.29614 0.51579 -0.03750 0.02212  0.04075  43  PRO A CB  
130  C CG  . PRO A 17  ? 0.52049 0.30075 0.49778 -0.03379 0.02087  0.03836  43  PRO A CG  
131  C CD  . PRO A 17  ? 0.51255 0.30754 0.49834 -0.03512 0.02721  0.03058  43  PRO A CD  
132  N N   . ASP A 18  ? 0.50078 0.29407 0.53718 -0.04832 0.03759  0.03040  44  ASP A N   
133  C CA  . ASP A 18  ? 0.50024 0.29218 0.55492 -0.05449 0.04379  0.03184  44  ASP A CA  
134  C C   . ASP A 18  ? 0.47148 0.27765 0.54705 -0.05665 0.04397  0.02141  44  ASP A C   
135  O O   . ASP A 18  ? 0.49833 0.30575 0.59192 -0.06215 0.04934  0.02157  44  ASP A O   
136  C CB  . ASP A 18  ? 0.56153 0.34720 0.60643 -0.05855 0.05514  0.04191  44  ASP A CB  
137  C CG  . ASP A 18  ? 0.59280 0.38706 0.62472 -0.05697 0.06110  0.04049  44  ASP A CG  
138  O OD1 . ASP A 18  ? 0.59081 0.38996 0.61143 -0.05153 0.05459  0.03603  44  ASP A OD1 
139  O OD2 . ASP A 18  ? 0.61874 0.41464 0.65323 -0.06130 0.07306  0.04353  44  ASP A OD2 
140  N N   . THR A 19  ? 0.41653 0.23262 0.49046 -0.05274 0.03765  0.01267  45  THR A N   
141  C CA  . THR A 19  ? 0.38620 0.21438 0.47733 -0.05459 0.03554  0.00330  45  THR A CA  
142  C C   . THR A 19  ? 0.36901 0.19399 0.47854 -0.05820 0.03157  -0.00185 45  THR A C   
143  O O   . THR A 19  ? 0.35402 0.18345 0.48317 -0.06313 0.03371  -0.00445 45  THR A O   
144  C CB  . THR A 19  ? 0.35504 0.19124 0.43683 -0.04965 0.02867  -0.00375 45  THR A CB  
145  O OG1 . THR A 19  ? 0.33762 0.17625 0.40377 -0.04637 0.03225  0.00039  45  THR A OG1 
146  C CG2 . THR A 19  ? 0.35679 0.20397 0.45379 -0.05147 0.02464  -0.01242 45  THR A CG2 
147  N N   . VAL A 20  ? 0.35754 0.17475 0.46279 -0.05588 0.02588  -0.00412 46  VAL A N   
148  C CA  . VAL A 20  ? 0.38992 0.20295 0.51139 -0.05892 0.02218  -0.01068 46  VAL A CA  
149  C C   . VAL A 20  ? 0.43228 0.23914 0.56689 -0.06377 0.02738  -0.00403 46  VAL A C   
150  O O   . VAL A 20  ? 0.44141 0.25259 0.59168 -0.06734 0.02590  -0.00914 46  VAL A O   
151  C CB  . VAL A 20  ? 0.38618 0.19236 0.50023 -0.05476 0.01691  -0.01439 46  VAL A CB  
152  C CG1 . VAL A 20  ? 0.39847 0.20415 0.52275 -0.05630 0.01351  -0.02103 46  VAL A CG1 
153  C CG2 . VAL A 20  ? 0.30701 0.12014 0.40785 -0.05055 0.01278  -0.02112 46  VAL A CG2 
154  N N   . ALA A 21  ? 0.44561 0.24296 0.57110 -0.06364 0.03282  0.00779  47  ALA A N   
155  C CA  . ALA A 21  ? 0.46507 0.25645 0.59829 -0.06793 0.03788  0.01557  47  ALA A CA  
156  C C   . ALA A 21  ? 0.49004 0.28989 0.63878 -0.07365 0.04543  0.01530  47  ALA A C   
157  O O   . ALA A 21  ? 0.50614 0.30751 0.67145 -0.07769 0.04645  0.01429  47  ALA A O   
158  C CB  . ALA A 21  ? 0.46642 0.24412 0.58183 -0.06675 0.04151  0.02912  47  ALA A CB  
159  N N   . ASN A 22  ? 0.49210 0.29795 0.63756 -0.07391 0.05104  0.01572  48  ASN A N   
160  C CA  . ASN A 22  ? 0.49384 0.30974 0.65787 -0.07893 0.05856  0.01444  48  ASN A CA  
161  C C   . ASN A 22  ? 0.48230 0.31019 0.66817 -0.08021 0.04998  0.00215  48  ASN A C   
162  O O   . ASN A 22  ? 0.49405 0.32777 0.70095 -0.08474 0.05263  0.00084  48  ASN A O   
163  C CB  . ASN A 22  ? 0.47825 0.30327 0.62949 -0.07611 0.06412  0.01583  48  ASN A CB  
164  C CG  . ASN A 22  ? 0.49250 0.30659 0.61727 -0.07464 0.07193  0.02736  48  ASN A CG  
165  O OD1 . ASN A 22  ? 0.50419 0.30425 0.62428 -0.07768 0.07642  0.03658  48  ASN A OD1 
166  N ND2 . ASN A 22  ? 0.48471 0.30395 0.59102 -0.07003 0.07280  0.02696  48  ASN A ND2 
167  N N   . PHE A 23  ? 0.47580 0.30675 0.65580 -0.07635 0.03948  -0.00689 49  PHE A N   
168  C CA  . PHE A 23  ? 0.47557 0.31538 0.67058 -0.07754 0.02989  -0.01846 49  PHE A CA  
169  C C   . PHE A 23  ? 0.50394 0.33969 0.70845 -0.07988 0.02710  -0.02035 49  PHE A C   
170  O O   . PHE A 23  ? 0.51339 0.35608 0.73752 -0.08345 0.02409  -0.02597 49  PHE A O   
171  C CB  . PHE A 23  ? 0.45392 0.29458 0.63457 -0.07308 0.02006  -0.02676 49  PHE A CB  
172  C CG  . PHE A 23  ? 0.43510 0.28191 0.62439 -0.07431 0.00924  -0.03841 49  PHE A CG  
173  C CD1 . PHE A 23  ? 0.41892 0.27661 0.62205 -0.07609 0.00461  -0.04342 49  PHE A CD1 
174  C CD2 . PHE A 23  ? 0.44153 0.28262 0.62470 -0.07364 0.00342  -0.04443 49  PHE A CD2 
175  C CE1 . PHE A 23  ? 0.42130 0.28306 0.62955 -0.07726 -0.00713 -0.05363 49  PHE A CE1 
176  C CE2 . PHE A 23  ? 0.44182 0.28649 0.62885 -0.07517 -0.00631 -0.05519 49  PHE A CE2 
177  C CZ  . PHE A 23  ? 0.43491 0.28944 0.63323 -0.07703 -0.01233 -0.05952 49  PHE A CZ  
178  N N   . GLU A 24  ? 0.52291 0.34738 0.71516 -0.07773 0.02753  -0.01586 50  GLU A N   
179  C CA  . GLU A 24  ? 0.54649 0.36594 0.74809 -0.07957 0.02536  -0.01753 50  GLU A CA  
180  C C   . GLU A 24  ? 0.57389 0.39339 0.79270 -0.08497 0.03322  -0.01060 50  GLU A C   
181  O O   . GLU A 24  ? 0.57561 0.39811 0.81258 -0.08833 0.03084  -0.01569 50  GLU A O   
182  C CB  . GLU A 24  ? 0.55113 0.35873 0.73789 -0.07554 0.02420  -0.01352 50  GLU A CB  
183  C CG  . GLU A 24  ? 0.55628 0.36394 0.72988 -0.07056 0.01710  -0.02209 50  GLU A CG  
184  C CD  . GLU A 24  ? 0.59584 0.39333 0.75933 -0.06628 0.01643  -0.01804 50  GLU A CD  
185  O OE1 . GLU A 24  ? 0.61088 0.40205 0.76518 -0.06467 0.01986  -0.00730 50  GLU A OE1 
186  O OE2 . GLU A 24  ? 0.60829 0.40380 0.77327 -0.06455 0.01234  -0.02573 50  GLU A OE2 
187  N N   . LYS A 25  ? 0.58177 0.39720 0.79404 -0.08604 0.04312  0.00101  51  LYS A N   
188  C CA  . LYS A 25  ? 0.60324 0.41773 0.82937 -0.09151 0.05269  0.00843  51  LYS A CA  
189  C C   . LYS A 25  ? 0.58824 0.41738 0.83921 -0.09534 0.05437  0.00191  51  LYS A C   
190  O O   . LYS A 25  ? 0.60690 0.43789 0.87779 -0.09986 0.05787  0.00246  51  LYS A O   
191  C CB  . LYS A 25  ? 0.61828 0.42437 0.82707 -0.09196 0.06373  0.02197  51  LYS A CB  
192  C CG  . LYS A 25  ? 0.64977 0.45087 0.86666 -0.09769 0.07479  0.03150  51  LYS A CG  
193  C CD  . LYS A 25  ? 0.66702 0.47252 0.88160 -0.10037 0.08856  0.03735  51  LYS A CD  
194  C CE  . LYS A 25  ? 0.65246 0.47640 0.89297 -0.10194 0.08938  0.02713  51  LYS A CE  
195  N NZ  . LYS A 25  ? 0.65332 0.48253 0.89410 -0.10411 0.10414  0.03163  51  LYS A NZ  
196  N N   . GLU A 26  ? 0.55976 0.39934 0.81151 -0.09347 0.05124  -0.00435 52  GLU A N   
197  C CA  . GLU A 26  ? 0.54119 0.39534 0.81874 -0.09650 0.05150  -0.01039 52  GLU A CA  
198  C C   . GLU A 26  ? 0.53435 0.39419 0.82718 -0.09710 0.03820  -0.02228 52  GLU A C   
199  O O   . GLU A 26  ? 0.52818 0.39561 0.84667 -0.10089 0.03832  -0.02541 52  GLU A O   
200  C CB  . GLU A 26  ? 0.53043 0.39314 0.80441 -0.09414 0.05243  -0.01229 52  GLU A CB  
201  C CG  . GLU A 26  ? 0.53055 0.40936 0.83324 -0.09619 0.05020  -0.01938 52  GLU A CG  
202  C CD  . GLU A 26  ? 0.53817 0.42496 0.83926 -0.09374 0.05213  -0.02045 52  GLU A CD  
203  O OE1 . GLU A 26  ? 0.53474 0.41394 0.81201 -0.09112 0.05778  -0.01479 52  GLU A OE1 
204  O OE2 . GLU A 26  ? 0.54586 0.44623 0.87034 -0.09419 0.04735  -0.02704 52  GLU A OE2 
205  N N   . THR A 27  ? 0.52263 0.37840 0.79944 -0.09347 0.02705  -0.02920 53  THR A N   
206  C CA  . THR A 27  ? 0.50817 0.36813 0.79359 -0.09398 0.01415  -0.04125 53  THR A CA  
207  C C   . THR A 27  ? 0.51778 0.36873 0.80396 -0.09512 0.01154  -0.04362 53  THR A C   
208  O O   . THR A 27  ? 0.52807 0.38206 0.82613 -0.09708 0.00300  -0.05287 53  THR A O   
209  C CB  . THR A 27  ? 0.48064 0.34126 0.74660 -0.08980 0.00393  -0.04877 53  THR A CB  
210  O OG1 . THR A 27  ? 0.47254 0.32229 0.71374 -0.08590 0.00626  -0.04521 53  THR A OG1 
211  C CG2 . THR A 27  ? 0.45420 0.32471 0.72343 -0.08874 0.00426  -0.04808 53  THR A CG2 
212  N N   . GLY A 28  ? 0.52852 0.36806 0.80269 -0.09387 0.01794  -0.03571 54  GLY A N   
213  C CA  . GLY A 28  ? 0.54034 0.37088 0.81542 -0.09416 0.01520  -0.03826 54  GLY A CA  
214  C C   . GLY A 28  ? 0.54242 0.36852 0.80064 -0.09029 0.00648  -0.04766 54  GLY A C   
215  O O   . GLY A 28  ? 0.53812 0.35769 0.79885 -0.09053 0.00376  -0.05220 54  GLY A O   
216  N N   . ILE A 29  ? 0.53236 0.36142 0.77374 -0.08687 0.00286  -0.05089 55  ILE A N   
217  C CA  . ILE A 29  ? 0.51737 0.34204 0.74048 -0.08335 -0.00370 -0.05970 55  ILE A CA  
218  C C   . ILE A 29  ? 0.51366 0.32928 0.72180 -0.07885 0.00118  -0.05326 55  ILE A C   
219  O O   . ILE A 29  ? 0.52321 0.33763 0.72665 -0.07742 0.00712  -0.04280 55  ILE A O   
220  C CB  . ILE A 29  ? 0.49848 0.32998 0.71045 -0.08202 -0.01001 -0.06579 55  ILE A CB  
221  C CG1 . ILE A 29  ? 0.50479 0.34591 0.73435 -0.08615 -0.01650 -0.07135 55  ILE A CG1 
222  C CG2 . ILE A 29  ? 0.49126 0.31701 0.68216 -0.07906 -0.01537 -0.07494 55  ILE A CG2 
223  C CD1 . ILE A 29  ? 0.50907 0.35711 0.73016 -0.08487 -0.02373 -0.07574 55  ILE A CD1 
224  N N   . LYS A 30  ? 0.51263 0.32159 0.71373 -0.07663 -0.00140 -0.05966 56  LYS A N   
225  C CA  . LYS A 30  ? 0.50803 0.30967 0.69719 -0.07165 0.00165  -0.05530 56  LYS A CA  
226  C C   . LYS A 30  ? 0.47304 0.27666 0.64294 -0.06786 -0.00071 -0.06057 56  LYS A C   
227  O O   . LYS A 30  ? 0.46856 0.27179 0.63102 -0.06783 -0.00480 -0.07164 56  LYS A O   
228  C CB  . LYS A 30  ? 0.54396 0.33798 0.73940 -0.07101 0.00132  -0.05945 56  LYS A CB  
229  C CG  . LYS A 30  ? 0.56767 0.35513 0.75517 -0.06554 0.00366  -0.05535 56  LYS A CG  
230  C CD  . LYS A 30  ? 0.60290 0.38664 0.78829 -0.06340 0.00206  -0.06661 56  LYS A CD  
231  C CE  . LYS A 30  ? 0.63592 0.41400 0.83829 -0.06548 0.00217  -0.06861 56  LYS A CE  
232  N NZ  . LYS A 30  ? 0.64875 0.42030 0.85912 -0.06293 0.00490  -0.05767 56  LYS A NZ  
233  N N   . VAL A 31  ? 0.44669 0.25132 0.60728 -0.06495 0.00212  -0.05267 57  VAL A N   
234  C CA  . VAL A 31  ? 0.42675 0.23353 0.57016 -0.06145 0.00054  -0.05637 57  VAL A CA  
235  C C   . VAL A 31  ? 0.42926 0.23013 0.56486 -0.05640 0.00249  -0.05547 57  VAL A C   
236  O O   . VAL A 31  ? 0.42616 0.22282 0.56461 -0.05428 0.00516  -0.04599 57  VAL A O   
237  C CB  . VAL A 31  ? 0.41507 0.22682 0.55438 -0.06113 0.00228  -0.04918 57  VAL A CB  
238  C CG1 . VAL A 31  ? 0.39012 0.20306 0.51207 -0.05717 0.00085  -0.05240 57  VAL A CG1 
239  C CG2 . VAL A 31  ? 0.42256 0.24192 0.57341 -0.06585 0.00026  -0.05112 57  VAL A CG2 
240  N N   . VAL A 32  ? 0.42188 0.22196 0.54770 -0.05462 0.00108  -0.06524 58  VAL A N   
241  C CA  . VAL A 32  ? 0.40394 0.20060 0.52407 -0.04965 0.00353  -0.06576 58  VAL A CA  
242  C C   . VAL A 32  ? 0.38207 0.18225 0.48782 -0.04690 0.00387  -0.06426 58  VAL A C   
243  O O   . VAL A 32  ? 0.37255 0.17453 0.46632 -0.04759 0.00257  -0.07197 58  VAL A O   
244  C CB  . VAL A 32  ? 0.40862 0.20177 0.52734 -0.04962 0.00389  -0.07744 58  VAL A CB  
245  C CG1 . VAL A 32  ? 0.40401 0.19496 0.52258 -0.04442 0.00755  -0.07752 58  VAL A CG1 
246  C CG2 . VAL A 32  ? 0.39990 0.18967 0.53316 -0.05296 0.00283  -0.07992 58  VAL A CG2 
247  N N   . TYR A 33  ? 0.37370 0.17367 0.47948 -0.04394 0.00518  -0.05420 59  TYR A N   
248  C CA  . TYR A 33  ? 0.37802 0.18116 0.47198 -0.04147 0.00535  -0.05148 59  TYR A CA  
249  C C   . TYR A 33  ? 0.39282 0.19453 0.48369 -0.03644 0.00684  -0.05193 59  TYR A C   
250  O O   . TYR A 33  ? 0.40732 0.20599 0.50414 -0.03359 0.00660  -0.04455 59  TYR A O   
251  C CB  . TYR A 33  ? 0.37770 0.18095 0.47299 -0.04205 0.00573  -0.04040 59  TYR A CB  
252  C CG  . TYR A 33  ? 0.37435 0.18119 0.45852 -0.04043 0.00576  -0.03856 59  TYR A CG  
253  C CD1 . TYR A 33  ? 0.36741 0.17953 0.44868 -0.04313 0.00465  -0.04266 59  TYR A CD1 
254  C CD2 . TYR A 33  ? 0.36837 0.17316 0.44629 -0.03612 0.00601  -0.03288 59  TYR A CD2 
255  C CE1 . TYR A 33  ? 0.33271 0.15129 0.40131 -0.04057 0.00429  -0.03993 59  TYR A CE1 
256  C CE2 . TYR A 33  ? 0.35317 0.16220 0.42002 -0.03432 0.00592  -0.03118 59  TYR A CE2 
257  C CZ  . TYR A 33  ? 0.33669 0.15399 0.39735 -0.03618 0.00535  -0.03425 59  TYR A CZ  
258  O OH  . TYR A 33  ? 0.33918 0.16309 0.38729 -0.03357 0.00485  -0.03184 59  TYR A OH  
259  N N   . ASP A 34  ? 0.38574 0.18925 0.46755 -0.03557 0.00819  -0.06050 60  ASP A N   
260  C CA  . ASP A 34  ? 0.37856 0.18241 0.45928 -0.03125 0.01082  -0.06194 60  ASP A CA  
261  C C   . ASP A 34  ? 0.38477 0.19198 0.45382 -0.02956 0.01093  -0.05984 60  ASP A C   
262  O O   . ASP A 34  ? 0.37171 0.18067 0.43068 -0.03200 0.00971  -0.06139 60  ASP A O   
263  C CB  . ASP A 34  ? 0.38850 0.19094 0.46773 -0.03170 0.01444  -0.07321 60  ASP A CB  
264  C CG  . ASP A 34  ? 0.41166 0.21045 0.50480 -0.03234 0.01489  -0.07569 60  ASP A CG  
265  O OD1 . ASP A 34  ? 0.41862 0.21601 0.52440 -0.03087 0.01303  -0.06776 60  ASP A OD1 
266  O OD2 . ASP A 34  ? 0.41534 0.21161 0.50574 -0.03441 0.01694  -0.08558 60  ASP A OD2 
267  N N   . VAL A 35  ? 0.38773 0.19594 0.45984 -0.02537 0.01184  -0.05651 61  VAL A N   
268  C CA  . VAL A 35  ? 0.39816 0.20923 0.46146 -0.02342 0.01164  -0.05373 61  VAL A CA  
269  C C   . VAL A 35  ? 0.40950 0.22278 0.47306 -0.02102 0.01596  -0.05926 61  VAL A C   
270  O O   . VAL A 35  ? 0.41930 0.23222 0.49342 -0.01979 0.01886  -0.06323 61  VAL A O   
271  C CB  . VAL A 35  ? 0.39836 0.20822 0.46497 -0.02092 0.00762  -0.04303 61  VAL A CB  
272  C CG1 . VAL A 35  ? 0.38983 0.19719 0.45511 -0.02394 0.00556  -0.03726 61  VAL A CG1 
273  C CG2 . VAL A 35  ? 0.40481 0.21255 0.48480 -0.01761 0.00601  -0.03978 61  VAL A CG2 
274  N N   . PHE A 36  ? 0.41263 0.22825 0.46577 -0.02053 0.01713  -0.05955 62  PHE A N   
275  C CA  . PHE A 36  ? 0.44169 0.25978 0.49582 -0.01856 0.02203  -0.06329 62  PHE A CA  
276  C C   . PHE A 36  ? 0.45073 0.27142 0.50343 -0.01599 0.01936  -0.05707 62  PHE A C   
277  O O   . PHE A 36  ? 0.41179 0.23187 0.45608 -0.01660 0.01550  -0.05237 62  PHE A O   
278  C CB  . PHE A 36  ? 0.46169 0.27823 0.50125 -0.02168 0.02794  -0.07203 62  PHE A CB  
279  C CG  . PHE A 36  ? 0.45138 0.26638 0.47321 -0.02451 0.02523  -0.07150 62  PHE A CG  
280  C CD1 . PHE A 36  ? 0.44192 0.25815 0.45491 -0.02376 0.02571  -0.06863 62  PHE A CD1 
281  C CD2 . PHE A 36  ? 0.45628 0.26854 0.47182 -0.02806 0.02186  -0.07411 62  PHE A CD2 
282  C CE1 . PHE A 36  ? 0.43940 0.25660 0.43618 -0.02562 0.02198  -0.06666 62  PHE A CE1 
283  C CE2 . PHE A 36  ? 0.45320 0.26545 0.45444 -0.03048 0.01822  -0.07333 62  PHE A CE2 
284  C CZ  . PHE A 36  ? 0.44811 0.26475 0.43933 -0.02858 0.01758  -0.06840 62  PHE A CZ  
285  N N   . ASP A 37  ? 0.47658 0.30034 0.53924 -0.01322 0.02162  -0.05757 63  ASP A N   
286  C CA  . ASP A 37  ? 0.50116 0.32743 0.56477 -0.01069 0.01841  -0.05249 63  ASP A CA  
287  C C   . ASP A 37  ? 0.51667 0.34501 0.57284 -0.01163 0.02445  -0.05655 63  ASP A C   
288  O O   . ASP A 37  ? 0.52027 0.35093 0.57834 -0.00978 0.02227  -0.05321 63  ASP A O   
289  C CB  . ASP A 37  ? 0.52069 0.34913 0.60358 -0.00694 0.01473  -0.04921 63  ASP A CB  
290  C CG  . ASP A 37  ? 0.54406 0.36840 0.63182 -0.00593 0.00769  -0.04298 63  ASP A CG  
291  O OD1 . ASP A 37  ? 0.55758 0.37824 0.63446 -0.00661 0.00292  -0.03713 63  ASP A OD1 
292  O OD2 . ASP A 37  ? 0.56096 0.38525 0.66395 -0.00460 0.00749  -0.04383 63  ASP A OD2 
293  N N   . SER A 38  ? 0.53657 0.36295 0.58321 -0.01477 0.03189  -0.06358 64  SER A N   
294  C CA  . SER A 38  ? 0.56311 0.38903 0.60003 -0.01645 0.03906  -0.06707 64  SER A CA  
295  C C   . SER A 38  ? 0.58834 0.40815 0.60347 -0.02087 0.04287  -0.07238 64  SER A C   
296  O O   . SER A 38  ? 0.59291 0.41028 0.60683 -0.02254 0.04392  -0.07711 64  SER A O   
297  C CB  . SER A 38  ? 0.59066 0.41985 0.64337 -0.01555 0.04736  -0.07137 64  SER A CB  
298  O OG  . SER A 38  ? 0.61581 0.44120 0.65509 -0.01910 0.05809  -0.07727 64  SER A OG  
299  N N   . ASN A 39  ? 0.58775 0.40409 0.58490 -0.02284 0.04403  -0.07150 65  ASN A N   
300  C CA  . ASN A 39  ? 0.63279 0.44290 0.60538 -0.02702 0.04502  -0.07515 65  ASN A CA  
301  C C   . ASN A 39  ? 0.65437 0.45812 0.61889 -0.03018 0.05597  -0.08387 65  ASN A C   
302  O O   . ASN A 39  ? 0.67613 0.47302 0.62130 -0.03386 0.05588  -0.08884 65  ASN A O   
303  C CB  . ASN A 39  ? 0.65792 0.47008 0.61387 -0.02706 0.04091  -0.06882 65  ASN A CB  
304  C CG  . ASN A 39  ? 0.70759 0.51641 0.65769 -0.02818 0.05012  -0.06981 65  ASN A CG  
305  O OD1 . ASN A 39  ? 0.74978 0.55143 0.67824 -0.03178 0.05474  -0.07242 65  ASN A OD1 
306  N ND2 . ASN A 39  ? 0.70596 0.51916 0.67502 -0.02541 0.05255  -0.06752 65  ASN A ND2 
307  N N   . GLU A 40  ? 0.64147 0.44846 0.62063 -0.02882 0.06485  -0.08559 66  GLU A N   
308  C CA  . GLU A 40  ? 0.63010 0.43237 0.60294 -0.03183 0.07728  -0.09373 66  GLU A CA  
309  C C   . GLU A 40  ? 0.62569 0.42736 0.60219 -0.03235 0.07648  -0.09973 66  GLU A C   
310  O O   . GLU A 40  ? 0.66530 0.45932 0.62246 -0.03627 0.08207  -0.10677 66  GLU A O   
311  C CB  . GLU A 40  ? 0.62568 0.43349 0.62077 -0.03009 0.08705  -0.09438 66  GLU A CB  
312  C CG  . GLU A 40  ? 0.65579 0.46195 0.64539 -0.03092 0.09118  -0.09046 66  GLU A CG  
313  C CD  . GLU A 40  ? 0.67011 0.48593 0.68352 -0.02616 0.08265  -0.08319 66  GLU A CD  
314  O OE1 . GLU A 40  ? 0.67233 0.48756 0.68397 -0.02643 0.08405  -0.07954 66  GLU A OE1 
315  O OE2 . GLU A 40  ? 0.66560 0.48839 0.69799 -0.02238 0.07418  -0.08099 66  GLU A OE2 
316  N N   . VAL A 41  ? 0.59684 0.40526 0.59636 -0.02865 0.06920  -0.09681 67  VAL A N   
317  C CA  . VAL A 41  ? 0.60808 0.41534 0.61366 -0.02899 0.06805  -0.10190 67  VAL A CA  
318  C C   . VAL A 41  ? 0.62452 0.42508 0.60710 -0.03265 0.06194  -0.10455 67  VAL A C   
319  O O   . VAL A 41  ? 0.65586 0.45066 0.62730 -0.03561 0.06554  -0.11259 67  VAL A O   
320  C CB  . VAL A 41  ? 0.60547 0.41921 0.63732 -0.02464 0.06036  -0.09622 67  VAL A CB  
321  C CG1 . VAL A 41  ? 0.60924 0.42028 0.64558 -0.02543 0.05772  -0.10024 67  VAL A CG1 
322  C CG2 . VAL A 41  ? 0.60262 0.42268 0.65871 -0.02128 0.06543  -0.09522 67  VAL A CG2 
323  N N   . LEU A 42  ? 0.60169 0.40292 0.57761 -0.03264 0.05229  -0.09818 68  LEU A N   
324  C CA  . LEU A 42  ? 0.56692 0.36301 0.52493 -0.03621 0.04487  -0.10033 68  LEU A CA  
325  C C   . LEU A 42  ? 0.55970 0.34677 0.48755 -0.04062 0.04890  -0.10625 68  LEU A C   
326  O O   . LEU A 42  ? 0.55142 0.33283 0.46581 -0.04385 0.04623  -0.11274 68  LEU A O   
327  C CB  . LEU A 42  ? 0.52637 0.32526 0.48450 -0.03555 0.03552  -0.09229 68  LEU A CB  
328  C CG  . LEU A 42  ? 0.52664 0.32218 0.46597 -0.03920 0.02688  -0.09317 68  LEU A CG  
329  C CD1 . LEU A 42  ? 0.50856 0.30183 0.45529 -0.04156 0.02267  -0.09883 68  LEU A CD1 
330  C CD2 . LEU A 42  ? 0.52135 0.32589 0.46262 -0.03677 0.01821  -0.08267 68  LEU A CD2 
331  N N   . GLU A 43  ? 0.55491 0.33944 0.47054 -0.04102 0.05487  -0.10382 69  GLU A N   
332  C CA  . GLU A 43  ? 0.60336 0.37692 0.48555 -0.04561 0.05824  -0.10759 69  GLU A CA  
333  C C   . GLU A 43  ? 0.61782 0.38654 0.49356 -0.04789 0.06927  -0.11683 69  GLU A C   
334  O O   . GLU A 43  ? 0.63486 0.39443 0.48389 -0.05197 0.06773  -0.12213 69  GLU A O   
335  C CB  . GLU A 43  ? 0.62380 0.39475 0.49556 -0.04557 0.06268  -0.10174 69  GLU A CB  
336  C CG  . GLU A 43  ? 0.62927 0.40953 0.50519 -0.04245 0.04938  -0.09045 69  GLU A CG  
337  C CD  . GLU A 43  ? 0.65367 0.43691 0.53049 -0.04058 0.05302  -0.08310 69  GLU A CD  
338  O OE1 . GLU A 43  ? 0.66352 0.44297 0.54199 -0.04159 0.06610  -0.08625 69  GLU A OE1 
339  O OE2 . GLU A 43  ? 0.64129 0.43065 0.51900 -0.03821 0.04331  -0.07468 69  GLU A OE2 
340  N N   . GLY A 44  ? 0.59881 0.37340 0.49888 -0.04533 0.07971  -0.11888 70  GLY A N   
341  C CA  . GLY A 44  ? 0.60896 0.37942 0.50634 -0.04738 0.09114  -0.12811 70  GLY A CA  
342  C C   . GLY A 44  ? 0.62073 0.38944 0.51857 -0.04807 0.08440  -0.13445 70  GLY A C   
343  O O   . GLY A 44  ? 0.65687 0.41701 0.53388 -0.05175 0.08858  -0.14248 70  GLY A O   
344  N N   . LYS A 45  ? 0.59639 0.37222 0.51698 -0.04482 0.07387  -0.13079 71  LYS A N   
345  C CA  . LYS A 45  ? 0.61226 0.38577 0.53500 -0.04578 0.06684  -0.13633 71  LYS A CA  
346  C C   . LYS A 45  ? 0.62433 0.39004 0.51728 -0.05012 0.05729  -0.13897 71  LYS A C   
347  O O   . LYS A 45  ? 0.65349 0.41264 0.53440 -0.05282 0.05600  -0.14746 71  LYS A O   
348  C CB  . LYS A 45  ? 0.59472 0.37616 0.54651 -0.04207 0.05815  -0.13014 71  LYS A CB  
349  C CG  . LYS A 45  ? 0.59861 0.38613 0.57992 -0.03801 0.06486  -0.12909 71  LYS A CG  
350  C CD  . LYS A 45  ? 0.59423 0.38786 0.59885 -0.03472 0.05559  -0.12074 71  LYS A CD  
351  C CE  . LYS A 45  ? 0.59477 0.39312 0.62736 -0.03089 0.06027  -0.11983 71  LYS A CE  
352  N NZ  . LYS A 45  ? 0.57836 0.38043 0.62961 -0.02822 0.05113  -0.11111 71  LYS A NZ  
353  N N   . LEU A 46  ? 0.61458 0.38057 0.49552 -0.05083 0.04976  -0.13194 72  LEU A N   
354  C CA  . LEU A 46  ? 0.63264 0.39190 0.48727 -0.05480 0.03829  -0.13333 72  LEU A CA  
355  C C   . LEU A 46  ? 0.69743 0.44526 0.51715 -0.05882 0.04378  -0.13920 72  LEU A C   
356  O O   . LEU A 46  ? 0.70848 0.44970 0.50951 -0.06206 0.03591  -0.14502 72  LEU A O   
357  C CB  . LEU A 46  ? 0.59661 0.35834 0.44743 -0.05436 0.02942  -0.12376 72  LEU A CB  
358  C CG  . LEU A 46  ? 0.56061 0.33090 0.43728 -0.05236 0.01992  -0.11857 72  LEU A CG  
359  C CD1 . LEU A 46  ? 0.54469 0.31948 0.41749 -0.05101 0.01222  -0.10832 72  LEU A CD1 
360  C CD2 . LEU A 46  ? 0.55956 0.32864 0.43934 -0.05504 0.00981  -0.12436 72  LEU A CD2 
361  N N   . MET A 47  ? 0.73624 0.48113 0.54659 -0.05897 0.05715  -0.13759 73  MET A N   
362  C CA  . MET A 47  ? 0.81764 0.55025 0.59302 -0.06337 0.06444  -0.14224 73  MET A CA  
363  C C   . MET A 47  ? 0.84710 0.57671 0.62520 -0.06440 0.07498  -0.15306 73  MET A C   
364  O O   . MET A 47  ? 0.87700 0.59531 0.62409 -0.06855 0.07893  -0.15850 73  MET A O   
365  C CB  . MET A 47  ? 0.85734 0.58649 0.62143 -0.06402 0.07621  -0.13638 73  MET A CB  
366  C CG  . MET A 47  ? 0.91453 0.63769 0.65332 -0.06553 0.06546  -0.12768 73  MET A CG  
367  S SD  . MET A 47  ? 0.98599 0.70352 0.71263 -0.06643 0.07929  -0.12055 73  MET A SD  
368  C CE  . MET A 47  ? 0.98541 0.71649 0.75800 -0.06211 0.09494  -0.12294 73  MET A CE  
369  N N   . ALA A 48  ? 0.84366 0.58219 0.65714 -0.06071 0.07911  -0.15589 74  ALA A N   
370  C CA  . ALA A 48  ? 0.86175 0.59708 0.68000 -0.06138 0.08698  -0.16653 74  ALA A CA  
371  C C   . ALA A 48  ? 0.90885 0.63981 0.71900 -0.06292 0.07337  -0.17300 74  ALA A C   
372  O O   . ALA A 48  ? 0.98192 0.70501 0.77907 -0.06525 0.07779  -0.18300 74  ALA A O   
373  C CB  . ALA A 48  ? 0.82214 0.56775 0.68169 -0.05676 0.09456  -0.16636 74  ALA A CB  
374  N N   . GLY A 49  ? 0.87544 0.61119 0.69414 -0.06192 0.05722  -0.16793 75  GLY A N   
375  C CA  . GLY A 49  ? 0.86065 0.59306 0.67482 -0.06379 0.04301  -0.17365 75  GLY A CA  
376  C C   . GLY A 49  ? 0.81411 0.55075 0.66055 -0.06123 0.04163  -0.17751 75  GLY A C   
377  O O   . GLY A 49  ? 0.81027 0.55103 0.67948 -0.05817 0.05266  -0.17733 75  GLY A O   
378  N N   . SER A 50  ? 0.74739 0.48261 0.59640 -0.06278 0.02704  -0.18057 76  SER A N   
379  C CA  . SER A 50  ? 0.72233 0.45853 0.59815 -0.06145 0.02369  -0.18372 76  SER A CA  
380  C C   . SER A 50  ? 0.66091 0.40688 0.57008 -0.05728 0.02815  -0.17385 76  SER A C   
381  O O   . SER A 50  ? 0.64786 0.39493 0.57730 -0.05496 0.03591  -0.17534 76  SER A O   
382  C CB  . SER A 50  ? 0.75852 0.48625 0.62846 -0.06215 0.03222  -0.19568 76  SER A CB  
383  O OG  . SER A 50  ? 0.81432 0.53307 0.66357 -0.06580 0.02155  -0.20518 76  SER A OG  
384  N N   . THR A 51  ? 0.61070 0.36380 0.52524 -0.05639 0.02267  -0.16357 77  THR A N   
385  C CA  . THR A 51  ? 0.55229 0.31448 0.49453 -0.05245 0.02589  -0.15337 77  THR A CA  
386  C C   . THR A 51  ? 0.53776 0.30202 0.50429 -0.05235 0.01935  -0.15026 77  THR A C   
387  O O   . THR A 51  ? 0.54651 0.31654 0.53624 -0.04901 0.02341  -0.14340 77  THR A O   
388  C CB  . THR A 51  ? 0.50762 0.27568 0.44573 -0.05175 0.02255  -0.14384 77  THR A CB  
389  O OG1 . THR A 51  ? 0.48939 0.25830 0.42741 -0.05443 0.00943  -0.14140 77  THR A OG1 
390  C CG2 . THR A 51  ? 0.51266 0.27676 0.42259 -0.05316 0.02791  -0.14606 77  THR A CG2 
391  N N   . GLY A 52  ? 0.52359 0.28306 0.48524 -0.05623 0.00919  -0.15471 78  GLY A N   
392  C CA  . GLY A 52  ? 0.51888 0.28047 0.50301 -0.05736 0.00392  -0.15066 78  GLY A CA  
393  C C   . GLY A 52  ? 0.49952 0.26941 0.49573 -0.05755 -0.00161 -0.13943 78  GLY A C   
394  O O   . GLY A 52  ? 0.52071 0.29404 0.53747 -0.05844 -0.00388 -0.13453 78  GLY A O   
395  N N   . PHE A 53  ? 0.45868 0.23209 0.44337 -0.05682 -0.00299 -0.13530 79  PHE A N   
396  C CA  . PHE A 53  ? 0.45622 0.23759 0.45168 -0.05687 -0.00736 -0.12541 79  PHE A CA  
397  C C   . PHE A 53  ? 0.46326 0.24419 0.45091 -0.06179 -0.01873 -0.12828 79  PHE A C   
398  O O   . PHE A 53  ? 0.48123 0.25537 0.44594 -0.06418 -0.02388 -0.13615 79  PHE A O   
399  C CB  . PHE A 53  ? 0.46211 0.24779 0.45184 -0.05321 -0.00241 -0.11916 79  PHE A CB  
400  C CG  . PHE A 53  ? 0.48603 0.27396 0.48709 -0.04840 0.00716  -0.11512 79  PHE A CG  
401  C CD1 . PHE A 53  ? 0.48906 0.28067 0.51262 -0.04642 0.00827  -0.10814 79  PHE A CD1 
402  C CD2 . PHE A 53  ? 0.51678 0.30327 0.50659 -0.04614 0.01486  -0.11803 79  PHE A CD2 
403  C CE1 . PHE A 53  ? 0.49715 0.29061 0.53177 -0.04200 0.01485  -0.10446 79  PHE A CE1 
404  C CE2 . PHE A 53  ? 0.52454 0.31412 0.52835 -0.04191 0.02260  -0.11469 79  PHE A CE2 
405  C CZ  . PHE A 53  ? 0.50923 0.30223 0.53548 -0.03969 0.02159  -0.10801 79  PHE A CZ  
406  N N   . ASP A 54  ? 0.44174 0.23064 0.44959 -0.06309 -0.02296 -0.12170 80  ASP A N   
407  C CA  . ASP A 54  ? 0.44741 0.24039 0.45572 -0.06689 -0.03410 -0.12290 80  ASP A CA  
408  C C   . ASP A 54  ? 0.44856 0.24804 0.45434 -0.06464 -0.03726 -0.11672 80  ASP A C   
409  O O   . ASP A 54  ? 0.44480 0.24511 0.44085 -0.06622 -0.04823 -0.11893 80  ASP A O   
410  C CB  . ASP A 54  ? 0.47014 0.26991 0.50575 -0.06909 -0.03703 -0.11938 80  ASP A CB  
411  C CG  . ASP A 54  ? 0.52064 0.31391 0.56110 -0.07119 -0.03493 -0.12534 80  ASP A CG  
412  O OD1 . ASP A 54  ? 0.54867 0.33393 0.57263 -0.07439 -0.03967 -0.13549 80  ASP A OD1 
413  O OD2 . ASP A 54  ? 0.53023 0.32548 0.58991 -0.06969 -0.02886 -0.11985 80  ASP A OD2 
414  N N   . LEU A 55  ? 0.42168 0.22529 0.43556 -0.06052 -0.02929 -0.10841 81  LEU A N   
415  C CA  . LEU A 55  ? 0.40069 0.21270 0.40839 -0.05689 -0.03018 -0.09899 81  LEU A CA  
416  C C   . LEU A 55  ? 0.39557 0.20578 0.39418 -0.05261 -0.02018 -0.09517 81  LEU A C   
417  O O   . LEU A 55  ? 0.41678 0.22428 0.42689 -0.05130 -0.01262 -0.09442 81  LEU A O   
418  C CB  . LEU A 55  ? 0.37419 0.19689 0.40467 -0.05621 -0.03132 -0.08983 81  LEU A CB  
419  C CG  . LEU A 55  ? 0.37087 0.19865 0.41557 -0.06006 -0.04133 -0.09209 81  LEU A CG  
420  C CD1 . LEU A 55  ? 0.32577 0.16381 0.39367 -0.05937 -0.03831 -0.08284 81  LEU A CD1 
421  C CD2 . LEU A 55  ? 0.37462 0.20338 0.40255 -0.06027 -0.05241 -0.09489 81  LEU A CD2 
422  N N   . VAL A 56  ? 0.39278 0.20406 0.37231 -0.05051 -0.02092 -0.09265 82  VAL A N   
423  C CA  . VAL A 56  ? 0.39366 0.20428 0.36602 -0.04669 -0.01225 -0.08886 82  VAL A CA  
424  C C   . VAL A 56  ? 0.38574 0.20454 0.35456 -0.04350 -0.01505 -0.07965 82  VAL A C   
425  O O   . VAL A 56  ? 0.39043 0.21359 0.35728 -0.04430 -0.02356 -0.07783 82  VAL A O   
426  C CB  . VAL A 56  ? 0.40694 0.20756 0.35748 -0.04795 -0.00726 -0.09691 82  VAL A CB  
427  C CG1 . VAL A 56  ? 0.40848 0.20092 0.36597 -0.05010 -0.00138 -0.10646 82  VAL A CG1 
428  C CG2 . VAL A 56  ? 0.43054 0.22711 0.35768 -0.05085 -0.01589 -0.10029 82  VAL A CG2 
429  N N   . VAL A 57  ? 0.39315 0.21386 0.36315 -0.03975 -0.00834 -0.07429 83  VAL A N   
430  C CA  . VAL A 57  ? 0.40335 0.23102 0.37101 -0.03648 -0.01002 -0.06617 83  VAL A CA  
431  C C   . VAL A 57  ? 0.41650 0.24047 0.36834 -0.03480 -0.00550 -0.06609 83  VAL A C   
432  O O   . VAL A 57  ? 0.39559 0.22066 0.35298 -0.03192 0.00043  -0.06287 83  VAL A O   
433  C CB  . VAL A 57  ? 0.40800 0.24160 0.39235 -0.03374 -0.00725 -0.05884 83  VAL A CB  
434  C CG1 . VAL A 57  ? 0.42906 0.26988 0.41170 -0.03095 -0.00973 -0.05200 83  VAL A CG1 
435  C CG2 . VAL A 57  ? 0.40299 0.23776 0.40355 -0.03625 -0.00876 -0.05913 83  VAL A CG2 
436  N N   . PRO A 58  ? 0.44628 0.26509 0.37841 -0.03677 -0.00836 -0.06926 84  PRO A N   
437  C CA  . PRO A 58  ? 0.44143 0.25600 0.35814 -0.03579 -0.00307 -0.06820 84  PRO A CA  
438  C C   . PRO A 58  ? 0.42067 0.24053 0.33427 -0.03310 -0.00794 -0.06035 84  PRO A C   
439  O O   . PRO A 58  ? 0.39361 0.22035 0.31608 -0.03197 -0.01533 -0.05655 84  PRO A O   
440  C CB  . PRO A 58  ? 0.46456 0.26843 0.35820 -0.04004 -0.00384 -0.07539 84  PRO A CB  
441  C CG  . PRO A 58  ? 0.48617 0.29178 0.38070 -0.04206 -0.01590 -0.07662 84  PRO A CG  
442  C CD  . PRO A 58  ? 0.46905 0.28381 0.39096 -0.04057 -0.01672 -0.07443 84  PRO A CD  
443  N N   . SER A 59  ? 0.43073 0.24705 0.33344 -0.03219 -0.00282 -0.05836 85  SER A N   
444  C CA  . SER A 59  ? 0.42611 0.24509 0.32384 -0.02998 -0.00737 -0.05161 85  SER A CA  
445  C C   . SER A 59  ? 0.44960 0.26322 0.32913 -0.03228 -0.01666 -0.05159 85  SER A C   
446  O O   . SER A 59  ? 0.49877 0.30369 0.36206 -0.03608 -0.01728 -0.05711 85  SER A O   
447  C CB  . SER A 59  ? 0.41563 0.23147 0.30846 -0.02889 0.00093  -0.04949 85  SER A CB  
448  O OG  . SER A 59  ? 0.43991 0.24578 0.31687 -0.03238 0.00843  -0.05467 85  SER A OG  
449  N N   . ALA A 60  ? 0.43492 0.25308 0.31721 -0.02987 -0.02460 -0.04561 86  ALA A N   
450  C CA  . ALA A 60  ? 0.49428 0.30716 0.36135 -0.03142 -0.03586 -0.04442 86  ALA A CA  
451  C C   . ALA A 60  ? 0.53459 0.33428 0.37350 -0.03383 -0.03299 -0.04357 86  ALA A C   
452  O O   . ALA A 60  ? 0.57823 0.36854 0.39616 -0.03686 -0.04087 -0.04478 86  ALA A O   
453  C CB  . ALA A 60  ? 0.47793 0.29898 0.35869 -0.02769 -0.04450 -0.03829 86  ALA A CB  
454  N N   . SER A 61  ? 0.52225 0.32020 0.35980 -0.03291 -0.02187 -0.04149 87  SER A N   
455  C CA  . SER A 61  ? 0.55309 0.33798 0.36475 -0.03580 -0.01652 -0.04027 87  SER A CA  
456  C C   . SER A 61  ? 0.56142 0.33631 0.35523 -0.04061 -0.00905 -0.04835 87  SER A C   
457  O O   . SER A 61  ? 0.60321 0.36452 0.36751 -0.04448 -0.00999 -0.04883 87  SER A O   
458  C CB  . SER A 61  ? 0.57133 0.35813 0.39131 -0.03379 -0.00611 -0.03641 87  SER A CB  
459  O OG  . SER A 61  ? 0.57783 0.37328 0.42027 -0.03198 0.00196  -0.04004 87  SER A OG  
460  N N   . PHE A 62  ? 0.54143 0.32158 0.35171 -0.04051 -0.00155 -0.05484 88  PHE A N   
461  C CA  . PHE A 62  ? 0.58221 0.35317 0.37874 -0.04479 0.00552  -0.06403 88  PHE A CA  
462  C C   . PHE A 62  ? 0.60953 0.37459 0.38977 -0.04778 -0.00701 -0.06778 88  PHE A C   
463  O O   . PHE A 62  ? 0.65717 0.40839 0.40876 -0.05233 -0.00524 -0.07284 88  PHE A O   
464  C CB  . PHE A 62  ? 0.58982 0.36813 0.41206 -0.04333 0.01403  -0.06960 88  PHE A CB  
465  C CG  . PHE A 62  ? 0.62875 0.39873 0.44234 -0.04718 0.02047  -0.08024 88  PHE A CG  
466  C CD1 . PHE A 62  ? 0.66083 0.42042 0.45897 -0.05022 0.03462  -0.08554 88  PHE A CD1 
467  C CD2 . PHE A 62  ? 0.62567 0.39784 0.44785 -0.04797 0.01336  -0.08550 88  PHE A CD2 
468  C CE1 . PHE A 62  ? 0.69371 0.44499 0.48405 -0.05369 0.04169  -0.09660 88  PHE A CE1 
469  C CE2 . PHE A 62  ? 0.66607 0.42981 0.48105 -0.05149 0.01920  -0.09623 88  PHE A CE2 
470  C CZ  . PHE A 62  ? 0.69069 0.44384 0.48925 -0.05420 0.03346  -0.10215 88  PHE A CZ  
471  N N   . LEU A 63  ? 0.60362 0.37854 0.40175 -0.04556 -0.01966 -0.06571 89  LEU A N   
472  C CA  . LEU A 63  ? 0.63009 0.40084 0.41759 -0.04821 -0.03388 -0.06898 89  LEU A CA  
473  C C   . LEU A 63  ? 0.70289 0.46200 0.45984 -0.05003 -0.04330 -0.06444 89  LEU A C   
474  O O   . LEU A 63  ? 0.72252 0.47015 0.45526 -0.05412 -0.05127 -0.06916 89  LEU A O   
475  C CB  . LEU A 63  ? 0.56841 0.35341 0.38568 -0.04529 -0.04429 -0.06650 89  LEU A CB  
476  C CG  . LEU A 63  ? 0.55880 0.34288 0.37396 -0.04729 -0.06147 -0.06863 89  LEU A CG  
477  C CD1 . LEU A 63  ? 0.52732 0.32087 0.37011 -0.04767 -0.06307 -0.07358 89  LEU A CD1 
478  C CD2 . LEU A 63  ? 0.55587 0.34475 0.37575 -0.04421 -0.07388 -0.06002 89  LEU A CD2 
479  N N   . GLU A 64  ? 0.74427 0.50493 0.50109 -0.04714 -0.04330 -0.05520 90  GLU A N   
480  C CA  . GLU A 64  ? 0.81543 0.56301 0.54226 -0.04883 -0.05144 -0.04940 90  GLU A CA  
481  C C   . GLU A 64  ? 0.85685 0.58660 0.54751 -0.05412 -0.04019 -0.05326 90  GLU A C   
482  O O   . GLU A 64  ? 0.89389 0.60834 0.55105 -0.05802 -0.04863 -0.05356 90  GLU A O   
483  C CB  . GLU A 64  ? 0.82787 0.58055 0.56528 -0.04455 -0.05182 -0.03901 90  GLU A CB  
484  C CG  . GLU A 64  ? 0.91621 0.65341 0.62237 -0.04634 -0.05752 -0.03157 90  GLU A CG  
485  C CD  . GLU A 64  ? 0.96083 0.70346 0.68168 -0.04172 -0.06051 -0.02160 90  GLU A CD  
486  O OE1 . GLU A 64  ? 0.94335 0.69965 0.69322 -0.03790 -0.05278 -0.02131 90  GLU A OE1 
487  O OE2 . GLU A 64  ? 0.99750 0.72969 0.70018 -0.04195 -0.07116 -0.01411 90  GLU A OE2 
488  N N   . ARG A 65  ? 0.86422 0.59510 0.56106 -0.05445 -0.02104 -0.05638 91  ARG A N   
489  C CA  . ARG A 65  ? 0.90471 0.61958 0.57106 -0.05967 -0.00680 -0.06141 91  ARG A CA  
490  C C   . ARG A 65  ? 0.93169 0.63755 0.58017 -0.06411 -0.00846 -0.07275 91  ARG A C   
491  O O   . ARG A 65  ? 0.97207 0.66038 0.58446 -0.06938 -0.00144 -0.07692 91  ARG A O   
492  C CB  . ARG A 65  ? 0.89369 0.61431 0.57924 -0.05861 0.01373  -0.06360 91  ARG A CB  
493  C CG  . ARG A 65  ? 0.87948 0.60358 0.57378 -0.05600 0.01834  -0.05366 91  ARG A CG  
494  C CD  . ARG A 65  ? 0.87717 0.60212 0.58281 -0.05676 0.03931  -0.05704 91  ARG A CD  
495  N NE  . ARG A 65  ? 0.85127 0.58986 0.59097 -0.05366 0.04384  -0.06347 91  ARG A NE  
496  C CZ  . ARG A 65  ? 0.82016 0.57366 0.59234 -0.04849 0.04072  -0.05944 91  ARG A CZ  
497  N NH1 . ARG A 65  ? 0.81243 0.56990 0.58903 -0.04573 0.03387  -0.05015 91  ARG A NH1 
498  N NH2 . ARG A 65  ? 0.80022 0.56342 0.59939 -0.04614 0.04418  -0.06473 91  ARG A NH2 
499  N N   . GLN A 66  ? 0.90615 0.62264 0.57826 -0.06248 -0.01692 -0.07811 92  GLN A N   
500  C CA  . GLN A 66  ? 0.90824 0.61716 0.56847 -0.06655 -0.01890 -0.08991 92  GLN A CA  
501  C C   . GLN A 66  ? 0.90163 0.60884 0.55459 -0.06756 -0.04189 -0.08987 92  GLN A C   
502  O O   . GLN A 66  ? 0.89735 0.60723 0.56115 -0.06887 -0.04784 -0.09832 92  GLN A O   
503  C CB  . GLN A 66  ? 0.87263 0.59324 0.56717 -0.06469 -0.00941 -0.09738 92  GLN A CB  
504  C CG  . GLN A 66  ? 0.86031 0.58356 0.56736 -0.06332 0.01150  -0.09819 92  GLN A CG  
505  C CD  . GLN A 66  ? 0.90595 0.61239 0.58255 -0.06840 0.02710  -0.10624 92  GLN A CD  
506  O OE1 . GLN A 66  ? 0.92878 0.62902 0.58679 -0.07144 0.02381  -0.11198 92  GLN A OE1 
507  N NE2 . GLN A 66  ? 0.91757 0.62382 0.59802 -0.06787 0.04411  -0.10404 92  GLN A NE2 
508  N N   . LEU A 67  ? 0.89580 0.59809 0.53211 -0.06705 -0.05558 -0.08053 93  LEU A N   
509  C CA  . LEU A 67  ? 0.89511 0.59797 0.53154 -0.06715 -0.07936 -0.07956 93  LEU A CA  
510  C C   . LEU A 67  ? 0.93635 0.62504 0.54073 -0.07221 -0.08673 -0.08673 93  LEU A C   
511  O O   . LEU A 67  ? 0.94112 0.63534 0.55753 -0.07231 -0.10267 -0.09019 93  LEU A O   
512  C CB  . LEU A 67  ? 0.90270 0.60626 0.53702 -0.06397 -0.09232 -0.06650 93  LEU A CB  
513  C CG  . LEU A 67  ? 0.84784 0.57224 0.52593 -0.05744 -0.09311 -0.05915 93  LEU A CG  
514  C CD1 . LEU A 67  ? 0.85833 0.58028 0.53074 -0.05451 -0.10287 -0.04695 93  LEU A CD1 
515  C CD2 . LEU A 67  ? 0.81222 0.55123 0.52415 -0.05583 -0.10480 -0.06337 93  LEU A CD2 
516  N N   . THR A 68  ? 0.94388 0.61883 0.51466 -0.07550 -0.07384 -0.08771 94  THR A N   
517  C CA  . THR A 68  ? 0.97301 0.63716 0.51533 -0.07931 -0.07889 -0.09252 94  THR A CA  
518  C C   . THR A 68  ? 0.98136 0.64513 0.52368 -0.08179 -0.06137 -0.10518 94  THR A C   
519  O O   . THR A 68  ? 1.01134 0.66562 0.52942 -0.08516 -0.06364 -0.11095 94  THR A O   
520  C CB  . THR A 68  ? 0.98906 0.63529 0.48936 -0.08175 -0.07909 -0.08366 94  THR A CB  
521  O OG1 . THR A 68  ? 0.98106 0.62088 0.46915 -0.08350 -0.05425 -0.08370 94  THR A OG1 
522  C CG2 . THR A 68  ? 0.98422 0.63060 0.48687 -0.07867 -0.09625 -0.07054 94  THR A CG2 
523  N N   . ALA A 69  ? 0.96643 0.63999 0.53622 -0.07997 -0.04464 -0.10973 95  ALA A N   
524  C CA  . ALA A 69  ? 0.99858 0.67240 0.57281 -0.08151 -0.02740 -0.12131 95  ALA A CA  
525  C C   . ALA A 69  ? 0.99308 0.67565 0.59054 -0.08123 -0.03609 -0.13133 95  ALA A C   
526  O O   . ALA A 69  ? 0.99196 0.67497 0.59596 -0.08204 -0.02368 -0.14163 95  ALA A O   
527  C CB  . ALA A 69  ? 0.99377 0.67445 0.59083 -0.07922 -0.00635 -0.12132 95  ALA A CB  
528  N N   . GLY A 70  ? 0.95649 0.64600 0.56863 -0.08014 -0.05672 -0.12872 96  GLY A N   
529  C CA  . GLY A 70  ? 0.94397 0.64188 0.58078 -0.08045 -0.06479 -0.13788 96  GLY A CA  
530  C C   . GLY A 70  ? 0.87369 0.58357 0.54938 -0.07797 -0.05277 -0.14213 96  GLY A C   
531  O O   . GLY A 70  ? 0.84806 0.56172 0.54078 -0.07878 -0.05249 -0.15184 96  GLY A O   
532  N N   . VAL A 71  ? 0.82423 0.53953 0.51475 -0.07492 -0.04334 -0.13485 97  VAL A N   
533  C CA  . VAL A 71  ? 0.77055 0.49629 0.49726 -0.07222 -0.03205 -0.13734 97  VAL A CA  
534  C C   . VAL A 71  ? 0.72662 0.46362 0.48571 -0.07093 -0.04490 -0.13476 97  VAL A C   
535  O O   . VAL A 71  ? 0.70172 0.44548 0.48923 -0.07028 -0.04102 -0.13959 97  VAL A O   
536  C CB  . VAL A 71  ? 0.75725 0.48395 0.48679 -0.06959 -0.01623 -0.13097 97  VAL A CB  
537  C CG1 . VAL A 71  ? 0.76471 0.48910 0.48074 -0.06885 -0.02458 -0.11998 97  VAL A CG1 
538  C CG2 . VAL A 71  ? 0.72203 0.46038 0.49090 -0.06607 -0.00810 -0.13079 97  VAL A CG2 
539  N N   . PHE A 72  ? 0.71600 0.45489 0.47285 -0.07052 -0.06021 -0.12693 98  PHE A N   
540  C CA  . PHE A 72  ? 0.65512 0.40521 0.44425 -0.06924 -0.07153 -0.12357 98  PHE A CA  
541  C C   . PHE A 72  ? 0.63821 0.38946 0.42705 -0.07169 -0.09095 -0.12632 98  PHE A C   
542  O O   . PHE A 72  ? 0.66300 0.40562 0.42229 -0.07351 -0.09943 -0.12699 98  PHE A O   
543  C CB  . PHE A 72  ? 0.59306 0.35273 0.39385 -0.06461 -0.07250 -0.11082 98  PHE A CB  
544  C CG  . PHE A 72  ? 0.59174 0.35574 0.40061 -0.06112 -0.05419 -0.10645 98  PHE A CG  
545  C CD1 . PHE A 72  ? 0.58025 0.35234 0.41790 -0.05945 -0.04425 -0.10795 98  PHE A CD1 
546  C CD2 . PHE A 72  ? 0.60584 0.36515 0.39433 -0.05966 -0.04782 -0.10052 98  PHE A CD2 
547  C CE1 . PHE A 72  ? 0.57665 0.35237 0.42275 -0.05612 -0.02972 -0.10400 98  PHE A CE1 
548  C CE2 . PHE A 72  ? 0.59449 0.35818 0.39323 -0.05662 -0.03219 -0.09708 98  PHE A CE2 
549  C CZ  . PHE A 72  ? 0.57999 0.35208 0.40767 -0.05471 -0.02386 -0.09900 98  PHE A CZ  
550  N N   . GLN A 73  ? 0.61931 0.38135 0.44249 -0.07178 -0.09770 -0.12733 99  GLN A N   
551  C CA  . GLN A 73  ? 0.63684 0.40347 0.47042 -0.07394 -0.11565 -0.12972 99  GLN A CA  
552  C C   . GLN A 73  ? 0.63282 0.40774 0.48151 -0.07124 -0.12954 -0.12021 99  GLN A C   
553  O O   . GLN A 73  ? 0.58632 0.37038 0.45857 -0.06806 -0.12346 -0.11377 99  GLN A O   
554  C CB  . GLN A 73  ? 0.64818 0.42241 0.51422 -0.07607 -0.11303 -0.13630 99  GLN A CB  
555  C CG  . GLN A 73  ? 0.65198 0.43735 0.54732 -0.07701 -0.12871 -0.13470 99  GLN A CG  
556  C CD  . GLN A 73  ? 0.68619 0.46728 0.56874 -0.08070 -0.14296 -0.14173 99  GLN A CD  
557  O OE1 . GLN A 73  ? 0.72495 0.49851 0.59413 -0.08406 -0.13797 -0.15143 99  GLN A OE1 
558  N NE2 . GLN A 73  ? 0.66931 0.45518 0.55738 -0.07990 -0.16108 -0.13716 99  GLN A NE2 
559  N N   . PRO A 74  ? 0.65570 0.42897 0.49353 -0.07182 -0.14740 -0.11859 100 PRO A N   
560  C CA  . PRO A 74  ? 0.63698 0.41954 0.49502 -0.06876 -0.16125 -0.11013 100 PRO A CA  
561  C C   . PRO A 74  ? 0.60158 0.40048 0.50766 -0.06857 -0.16302 -0.11080 100 PRO A C   
562  O O   . PRO A 74  ? 0.59409 0.39658 0.51501 -0.07164 -0.16620 -0.11742 100 PRO A O   
563  C CB  . PRO A 74  ? 0.66319 0.43918 0.49992 -0.06973 -0.18037 -0.10957 100 PRO A CB  
564  C CG  . PRO A 74  ? 0.69459 0.46193 0.51142 -0.07415 -0.17801 -0.11975 100 PRO A CG  
565  C CD  . PRO A 74  ? 0.69002 0.45222 0.49630 -0.07497 -0.15571 -0.12416 100 PRO A CD  
566  N N   . LEU A 75  ? 0.57404 0.38430 0.50515 -0.06469 -0.15842 -0.10302 101 LEU A N   
567  C CA  . LEU A 75  ? 0.56482 0.39129 0.54134 -0.06432 -0.15500 -0.10213 101 LEU A CA  
568  C C   . LEU A 75  ? 0.58645 0.42010 0.58704 -0.06578 -0.17464 -0.10407 101 LEU A C   
569  O O   . LEU A 75  ? 0.60632 0.44156 0.60585 -0.06324 -0.18842 -0.09936 101 LEU A O   
570  C CB  . LEU A 75  ? 0.50823 0.34697 0.50188 -0.05879 -0.14182 -0.09188 101 LEU A CB  
571  C CG  . LEU A 75  ? 0.49125 0.32735 0.47287 -0.05691 -0.12116 -0.08926 101 LEU A CG  
572  C CD1 . LEU A 75  ? 0.45702 0.30518 0.45687 -0.05183 -0.11092 -0.07988 101 LEU A CD1 
573  C CD2 . LEU A 75  ? 0.48203 0.31603 0.47348 -0.06051 -0.11202 -0.09582 101 LEU A CD2 
574  N N   . ASP A 76  ? 0.58258 0.42240 0.60655 -0.06899 -0.17407 -0.10954 102 ASP A N   
575  C CA  . ASP A 76  ? 0.58296 0.43362 0.63732 -0.06960 -0.18860 -0.11030 102 ASP A CA  
576  C C   . ASP A 76  ? 0.54972 0.41636 0.64507 -0.06673 -0.18539 -0.10394 102 ASP A C   
577  O O   . ASP A 76  ? 0.51953 0.39462 0.64262 -0.06788 -0.17156 -0.10346 102 ASP A O   
578  C CB  . ASP A 76  ? 0.57484 0.42676 0.64292 -0.07416 -0.18675 -0.11791 102 ASP A CB  
579  C CG  . ASP A 76  ? 0.57106 0.42974 0.66051 -0.07515 -0.20470 -0.12031 102 ASP A CG  
580  O OD1 . ASP A 76  ? 0.54997 0.41917 0.66427 -0.07196 -0.21379 -0.11510 102 ASP A OD1 
581  O OD2 . ASP A 76  ? 0.58319 0.43651 0.66595 -0.07900 -0.20965 -0.12779 102 ASP A OD2 
582  N N   . LYS A 77  ? 0.55506 0.42530 0.65411 -0.06299 -0.19748 -0.09878 103 LYS A N   
583  C CA  . LYS A 77  ? 0.51911 0.40454 0.65720 -0.06006 -0.19369 -0.09350 103 LYS A CA  
584  C C   . LYS A 77  ? 0.49019 0.39097 0.67522 -0.06158 -0.19436 -0.09556 103 LYS A C   
585  O O   . LYS A 77  ? 0.44112 0.35496 0.66128 -0.06051 -0.18399 -0.09239 103 LYS A O   
586  C CB  . LYS A 77  ? 0.53483 0.42026 0.66735 -0.05529 -0.20755 -0.08782 103 LYS A CB  
587  C CG  . LYS A 77  ? 0.54870 0.42228 0.63697 -0.05189 -0.20059 -0.08209 103 LYS A CG  
588  C CD  . LYS A 77  ? 0.52170 0.40160 0.61344 -0.04880 -0.17566 -0.07673 103 LYS A CD  
589  C CE  . LYS A 77  ? 0.52788 0.39454 0.57556 -0.04726 -0.16677 -0.07357 103 LYS A CE  
590  N NZ  . LYS A 77  ? 0.54635 0.40438 0.56987 -0.04456 -0.18065 -0.06904 103 LYS A NZ  
591  N N   . SER A 78  ? 0.50965 0.40858 0.69577 -0.06423 -0.20535 -0.10096 104 SER A N   
592  C CA  . SER A 78  ? 0.51884 0.43151 0.75002 -0.06581 -0.20583 -0.10313 104 SER A CA  
593  C C   . SER A 78  ? 0.52258 0.43944 0.77090 -0.06943 -0.18508 -0.10410 104 SER A C   
594  O O   . SER A 78  ? 0.50593 0.43601 0.79551 -0.07024 -0.17860 -0.10324 104 SER A O   
595  C CB  . SER A 78  ? 0.54845 0.45626 0.77429 -0.06780 -0.22400 -0.10897 104 SER A CB  
596  O OG  . SER A 78  ? 0.55764 0.45501 0.76043 -0.07254 -0.21846 -0.11521 104 SER A OG  
597  N N   . LYS A 79  ? 0.52821 0.43341 0.74589 -0.07142 -0.17394 -0.10543 105 LYS A N   
598  C CA  . LYS A 79  ? 0.51910 0.42562 0.74890 -0.07431 -0.15456 -0.10499 105 LYS A CA  
599  C C   . LYS A 79  ? 0.47749 0.38831 0.71495 -0.07218 -0.13778 -0.09794 105 LYS A C   
600  O O   . LYS A 79  ? 0.45597 0.36547 0.69770 -0.07406 -0.12107 -0.09590 105 LYS A O   
601  C CB  . LYS A 79  ? 0.54932 0.44081 0.74512 -0.07697 -0.15047 -0.11001 105 LYS A CB  
602  C CG  . LYS A 79  ? 0.60019 0.48334 0.77580 -0.07904 -0.16686 -0.11767 105 LYS A CG  
603  C CD  . LYS A 79  ? 0.62455 0.51687 0.83368 -0.08142 -0.17633 -0.12106 105 LYS A CD  
604  C CE  . LYS A 79  ? 0.66611 0.54932 0.85301 -0.08323 -0.19459 -0.12846 105 LYS A CE  
605  N NZ  . LYS A 79  ? 0.68024 0.57337 0.89943 -0.08336 -0.20992 -0.12998 105 LYS A NZ  
606  N N   . LEU A 80  ? 0.46957 0.38454 0.70825 -0.06827 -0.14211 -0.09396 106 LEU A N   
607  C CA  . LEU A 80  ? 0.44072 0.36068 0.68076 -0.06443 -0.12459 -0.08604 106 LEU A CA  
608  C C   . LEU A 80  ? 0.43890 0.37385 0.71353 -0.06163 -0.12678 -0.08301 106 LEU A C   
609  O O   . LEU A 80  ? 0.43839 0.37472 0.70346 -0.05638 -0.13283 -0.07960 106 LEU A O   
610  C CB  . LEU A 80  ? 0.42774 0.33761 0.62410 -0.05976 -0.12201 -0.08222 106 LEU A CB  
611  C CG  . LEU A 80  ? 0.43674 0.33183 0.59938 -0.06196 -0.11849 -0.08574 106 LEU A CG  
612  C CD1 . LEU A 80  ? 0.44684 0.33251 0.56960 -0.05785 -0.11944 -0.08301 106 LEU A CD1 
613  C CD2 . LEU A 80  ? 0.40990 0.30480 0.57922 -0.06343 -0.09924 -0.08316 106 LEU A CD2 
614  N N   . PRO A 81  ? 0.44705 0.39324 0.76415 -0.06513 -0.12125 -0.08431 107 PRO A N   
615  C CA  . PRO A 81  ? 0.46475 0.42610 0.81973 -0.06257 -0.12204 -0.08259 107 PRO A CA  
616  C C   . PRO A 81  ? 0.47733 0.44284 0.82563 -0.05694 -0.10505 -0.07526 107 PRO A C   
617  O O   . PRO A 81  ? 0.49216 0.46578 0.85587 -0.05239 -0.11011 -0.07394 107 PRO A O   
618  C CB  . PRO A 81  ? 0.46463 0.43597 0.85859 -0.06673 -0.11316 -0.08416 107 PRO A CB  
619  C CG  . PRO A 81  ? 0.46777 0.42906 0.84307 -0.07069 -0.11624 -0.08773 107 PRO A CG  
620  C CD  . PRO A 81  ? 0.45416 0.40030 0.78543 -0.07046 -0.11321 -0.08669 107 PRO A CD  
621  N N   . GLU A 82  ? 0.47641 0.43595 0.80267 -0.05701 -0.08597 -0.07075 108 GLU A N   
622  C CA  . GLU A 82  ? 0.47458 0.43664 0.79214 -0.05218 -0.06976 -0.06446 108 GLU A CA  
623  C C   . GLU A 82  ? 0.41465 0.36919 0.69589 -0.04627 -0.07629 -0.06180 108 GLU A C   
624  O O   . GLU A 82  ? 0.39300 0.34740 0.66173 -0.04229 -0.06373 -0.05706 108 GLU A O   
625  C CB  . GLU A 82  ? 0.52819 0.48547 0.83555 -0.05479 -0.04864 -0.06025 108 GLU A CB  
626  C CG  . GLU A 82  ? 0.57591 0.54079 0.92018 -0.06042 -0.03702 -0.06069 108 GLU A CG  
627  C CD  . GLU A 82  ? 0.62608 0.59757 0.98182 -0.05889 -0.01657 -0.05589 108 GLU A CD  
628  O OE1 . GLU A 82  ? 0.63826 0.61927 1.01071 -0.05485 -0.01779 -0.05683 108 GLU A OE1 
629  O OE2 . GLU A 82  ? 0.64433 0.61047 0.99161 -0.06175 0.00062  -0.05125 108 GLU A OE2 
630  N N   . TRP A 83  ? 0.40202 0.34942 0.66539 -0.04601 -0.09536 -0.06482 109 TRP A N   
631  C CA  . TRP A 83  ? 0.39171 0.33142 0.62230 -0.04099 -0.10191 -0.06187 109 TRP A CA  
632  C C   . TRP A 83  ? 0.36904 0.31726 0.61524 -0.03527 -0.10181 -0.05854 109 TRP A C   
633  O O   . TRP A 83  ? 0.35756 0.30049 0.57942 -0.03077 -0.09971 -0.05455 109 TRP A O   
634  C CB  . TRP A 83  ? 0.41780 0.34825 0.62974 -0.04251 -0.12333 -0.06582 109 TRP A CB  
635  C CG  . TRP A 83  ? 0.39926 0.31893 0.57307 -0.03863 -0.12895 -0.06244 109 TRP A CG  
636  C CD1 . TRP A 83  ? 0.38956 0.31003 0.56225 -0.03385 -0.13895 -0.05892 109 TRP A CD1 
637  C CD2 . TRP A 83  ? 0.38520 0.29121 0.51844 -0.03946 -0.12434 -0.06218 109 TRP A CD2 
638  N NE1 . TRP A 83  ? 0.38237 0.28997 0.51485 -0.03208 -0.14039 -0.05592 109 TRP A NE1 
639  C CE2 . TRP A 83  ? 0.39121 0.29030 0.49963 -0.03552 -0.13100 -0.05819 109 TRP A CE2 
640  C CE3 . TRP A 83  ? 0.35546 0.25429 0.47317 -0.04311 -0.11483 -0.06499 109 TRP A CE3 
641  C CZ2 . TRP A 83  ? 0.39797 0.28383 0.46712 -0.03557 -0.12723 -0.05713 109 TRP A CZ2 
642  C CZ3 . TRP A 83  ? 0.35772 0.24400 0.43805 -0.04262 -0.11167 -0.06451 109 TRP A CZ3 
643  C CH2 . TRP A 83  ? 0.37928 0.25947 0.43585 -0.03909 -0.11725 -0.06070 109 TRP A CH2 
644  N N   . LYS A 84  ? 0.34829 0.30961 0.63693 -0.03542 -0.10342 -0.06054 110 LYS A N   
645  C CA  . LYS A 84  ? 0.36857 0.33873 0.67760 -0.02983 -0.10192 -0.05846 110 LYS A CA  
646  C C   . LYS A 84  ? 0.35820 0.32898 0.65723 -0.02701 -0.07962 -0.05457 110 LYS A C   
647  O O   . LYS A 84  ? 0.36035 0.33472 0.66520 -0.02165 -0.07766 -0.05284 110 LYS A O   
648  C CB  . LYS A 84  ? 0.40403 0.38907 0.76569 -0.03119 -0.10532 -0.06242 110 LYS A CB  
649  C CG  . LYS A 84  ? 0.43426 0.42640 0.81957 -0.03637 -0.08594 -0.06394 110 LYS A CG  
650  C CD  . LYS A 84  ? 0.47219 0.47915 0.91260 -0.03855 -0.09014 -0.06857 110 LYS A CD  
651  C CE  . LYS A 84  ? 0.49866 0.51362 0.96453 -0.04249 -0.06506 -0.06855 110 LYS A CE  
652  N NZ  . LYS A 84  ? 0.51509 0.52855 0.99038 -0.05031 -0.06400 -0.07093 110 LYS A NZ  
653  N N   . ASN A 85  ? 0.34403 0.31043 0.62799 -0.03045 -0.06371 -0.05326 111 ASN A N   
654  C CA  . ASN A 85  ? 0.31794 0.28337 0.58978 -0.02821 -0.04392 -0.04960 111 ASN A CA  
655  C C   . ASN A 85  ? 0.31287 0.26863 0.54782 -0.02360 -0.04591 -0.04626 111 ASN A C   
656  O O   . ASN A 85  ? 0.30825 0.26394 0.53582 -0.02038 -0.03350 -0.04398 111 ASN A O   
657  C CB  . ASN A 85  ? 0.30913 0.27076 0.57399 -0.03330 -0.02868 -0.04818 111 ASN A CB  
658  C CG  . ASN A 85  ? 0.29747 0.26875 0.60071 -0.03814 -0.02145 -0.05051 111 ASN A CG  
659  O OD1 . ASN A 85  ? 0.30672 0.28943 0.64378 -0.03689 -0.02096 -0.05290 111 ASN A OD1 
660  N ND2 . ASN A 85  ? 0.28434 0.25094 0.58481 -0.04377 -0.01537 -0.04989 111 ASN A ND2 
661  N N   . LEU A 86  ? 0.30884 0.25585 0.52036 -0.02357 -0.06060 -0.04627 112 LEU A N   
662  C CA  . LEU A 86  ? 0.30199 0.23930 0.47944 -0.02005 -0.06135 -0.04300 112 LEU A CA  
663  C C   . LEU A 86  ? 0.31802 0.25852 0.50273 -0.01428 -0.06602 -0.04142 112 LEU A C   
664  O O   . LEU A 86  ? 0.32440 0.27166 0.53466 -0.01285 -0.07700 -0.04298 112 LEU A O   
665  C CB  . LEU A 86  ? 0.30159 0.22806 0.45263 -0.02218 -0.07433 -0.04383 112 LEU A CB  
666  C CG  . LEU A 86  ? 0.30849 0.22941 0.44849 -0.02733 -0.06948 -0.04594 112 LEU A CG  
667  C CD1 . LEU A 86  ? 0.30667 0.21817 0.42723 -0.02992 -0.08392 -0.04902 112 LEU A CD1 
668  C CD2 . LEU A 86  ? 0.31624 0.23152 0.43517 -0.02652 -0.05457 -0.04282 112 LEU A CD2 
669  N N   . ASP A 87  ? 0.34304 0.27831 0.50689 -0.01089 -0.05829 -0.03845 113 ASP A N   
670  C CA  . ASP A 87  ? 0.36124 0.29782 0.53016 -0.00530 -0.06151 -0.03694 113 ASP A CA  
671  C C   . ASP A 87  ? 0.35731 0.28779 0.51746 -0.00400 -0.08114 -0.03527 113 ASP A C   
672  O O   . ASP A 87  ? 0.36600 0.28551 0.49520 -0.00565 -0.08584 -0.03341 113 ASP A O   
673  C CB  . ASP A 87  ? 0.37818 0.30876 0.52404 -0.00273 -0.04988 -0.03457 113 ASP A CB  
674  C CG  . ASP A 87  ? 0.42244 0.35585 0.57968 0.00288  -0.04864 -0.03431 113 ASP A CG  
675  O OD1 . ASP A 87  ? 0.45638 0.39031 0.62449 0.00567  -0.06209 -0.03351 113 ASP A OD1 
676  O OD2 . ASP A 87  ? 0.43716 0.37126 0.59184 0.00452  -0.03473 -0.03499 113 ASP A OD2 
677  N N   . PRO A 88  ? 0.37728 0.31363 0.56329 -0.00119 -0.09287 -0.03572 114 PRO A N   
678  C CA  . PRO A 88  ? 0.39483 0.32299 0.56903 -0.00001 -0.11322 -0.03292 114 PRO A CA  
679  C C   . PRO A 88  ? 0.40250 0.31928 0.54706 0.00301  -0.11324 -0.02796 114 PRO A C   
680  O O   . PRO A 88  ? 0.42910 0.33422 0.54783 0.00184  -0.12544 -0.02485 114 PRO A O   
681  C CB  . PRO A 88  ? 0.40826 0.34653 0.62282 0.00336  -0.12409 -0.03421 114 PRO A CB  
682  C CG  . PRO A 88  ? 0.40146 0.35159 0.64375 0.00555  -0.10554 -0.03713 114 PRO A CG  
683  C CD  . PRO A 88  ? 0.38042 0.33044 0.60819 0.00094  -0.08817 -0.03877 114 PRO A CD  
684  N N   . GLU A 89  ? 0.39858 0.31750 0.54516 0.00643  -0.09949 -0.02737 115 GLU A N   
685  C CA  . GLU A 89  ? 0.43666 0.34493 0.55742 0.00886  -0.09853 -0.02304 115 GLU A CA  
686  C C   . GLU A 89  ? 0.40562 0.30390 0.49069 0.00478  -0.09336 -0.02191 115 GLU A C   
687  O O   . GLU A 89  ? 0.41395 0.30057 0.47362 0.00412  -0.10053 -0.01814 115 GLU A O   
688  C CB  . GLU A 89  ? 0.48647 0.39955 0.61917 0.01305  -0.08483 -0.02420 115 GLU A CB  
689  C CG  . GLU A 89  ? 0.54364 0.44797 0.66406 0.01697  -0.08781 -0.02016 115 GLU A CG  
690  C CD  . GLU A 89  ? 0.59096 0.50054 0.72820 0.02139  -0.07614 -0.02294 115 GLU A CD  
691  O OE1 . GLU A 89  ? 0.60804 0.52384 0.74975 0.02028  -0.06138 -0.02714 115 GLU A OE1 
692  O OE2 . GLU A 89  ? 0.61811 0.52446 0.76303 0.02585  -0.08174 -0.02097 115 GLU A OE2 
693  N N   . LEU A 90  ? 0.36003 0.26212 0.44345 0.00189  -0.08049 -0.02499 116 LEU A N   
694  C CA  . LEU A 90  ? 0.34505 0.23860 0.39975 -0.00174 -0.07556 -0.02468 116 LEU A CA  
695  C C   . LEU A 90  ? 0.35189 0.23908 0.39343 -0.00579 -0.08722 -0.02545 116 LEU A C   
696  O O   . LEU A 90  ? 0.35510 0.23168 0.36896 -0.00801 -0.08713 -0.02443 116 LEU A O   
697  C CB  . LEU A 90  ? 0.33231 0.23089 0.39111 -0.00362 -0.06093 -0.02729 116 LEU A CB  
698  C CG  . LEU A 90  ? 0.32496 0.22831 0.39278 -0.00022 -0.04897 -0.02725 116 LEU A CG  
699  C CD1 . LEU A 90  ? 0.28580 0.19231 0.35536 -0.00267 -0.03612 -0.02889 116 LEU A CD1 
700  C CD2 . LEU A 90  ? 0.32399 0.21956 0.37294 0.00240  -0.04718 -0.02463 116 LEU A CD2 
701  N N   . LEU A 91  ? 0.36777 0.26094 0.42923 -0.00700 -0.09709 -0.02787 117 LEU A N   
702  C CA  . LEU A 91  ? 0.38695 0.27293 0.43506 -0.01080 -0.11077 -0.02927 117 LEU A CA  
703  C C   . LEU A 91  ? 0.40523 0.27920 0.43075 -0.00949 -0.12337 -0.02461 117 LEU A C   
704  O O   . LEU A 91  ? 0.39278 0.25447 0.38804 -0.01290 -0.12722 -0.02452 117 LEU A O   
705  C CB  . LEU A 91  ? 0.31145 0.20692 0.38980 -0.01207 -0.12062 -0.03292 117 LEU A CB  
706  C CG  . LEU A 91  ? 0.33461 0.23725 0.42779 -0.01610 -0.11160 -0.03789 117 LEU A CG  
707  C CD1 . LEU A 91  ? 0.32208 0.23500 0.45037 -0.01719 -0.12171 -0.04129 117 LEU A CD1 
708  C CD2 . LEU A 91  ? 0.31098 0.20321 0.37621 -0.02090 -0.11072 -0.04054 117 LEU A CD2 
709  N N   . LYS A 92  ? 0.41787 0.29417 0.45729 -0.00471 -0.12930 -0.02067 118 LYS A N   
710  C CA  . LYS A 92  ? 0.46611 0.32950 0.48374 -0.00330 -0.14059 -0.01467 118 LYS A CA  
711  C C   . LYS A 92  ? 0.49182 0.34456 0.47799 -0.00435 -0.12883 -0.01187 118 LYS A C   
712  O O   . LYS A 92  ? 0.51186 0.35018 0.46786 -0.00647 -0.13489 -0.00825 118 LYS A O   
713  C CB  . LYS A 92  ? 0.47373 0.34214 0.51678 0.00260  -0.14746 -0.01109 118 LYS A CB  
714  C CG  . LYS A 92  ? 0.50734 0.38461 0.58283 0.00396  -0.16277 -0.01307 118 LYS A CG  
715  C CD  . LYS A 92  ? 0.55508 0.43312 0.65098 0.00999  -0.17294 -0.00853 118 LYS A CD  
716  C CE  . LYS A 92  ? 0.59490 0.48215 0.72704 0.01158  -0.18960 -0.01069 118 LYS A CE  
717  N NZ  . LYS A 92  ? 0.58491 0.49088 0.75771 0.01246  -0.17692 -0.01751 118 LYS A NZ  
718  N N   . LEU A 93  ? 0.48315 0.34220 0.47589 -0.00311 -0.11198 -0.01350 119 LEU A N   
719  C CA  . LEU A 93  ? 0.50392 0.35431 0.47202 -0.00408 -0.10093 -0.01150 119 LEU A CA  
720  C C   . LEU A 93  ? 0.51477 0.35690 0.45717 -0.00948 -0.09793 -0.01417 119 LEU A C   
721  O O   . LEU A 93  ? 0.51752 0.34720 0.43299 -0.01147 -0.09661 -0.01147 119 LEU A O   
722  C CB  . LEU A 93  ? 0.48674 0.34564 0.46849 -0.00169 -0.08570 -0.01333 119 LEU A CB  
723  C CG  . LEU A 93  ? 0.51222 0.37411 0.50888 0.00352  -0.08481 -0.01069 119 LEU A CG  
724  C CD1 . LEU A 93  ? 0.49269 0.36173 0.49902 0.00514  -0.07021 -0.01368 119 LEU A CD1 
725  C CD2 . LEU A 93  ? 0.52332 0.37258 0.50060 0.00416  -0.08876 -0.00490 119 LEU A CD2 
726  N N   . VAL A 94  ? 0.50588 0.35422 0.45699 -0.01211 -0.09587 -0.01973 120 VAL A N   
727  C CA  . VAL A 94  ? 0.53060 0.37112 0.45994 -0.01703 -0.09232 -0.02355 120 VAL A CA  
728  C C   . VAL A 94  ? 0.51107 0.34071 0.42020 -0.02032 -0.10659 -0.02397 120 VAL A C   
729  O O   . VAL A 94  ? 0.52181 0.34102 0.40555 -0.02447 -0.10342 -0.02685 120 VAL A O   
730  C CB  . VAL A 94  ? 0.54499 0.39415 0.49028 -0.01897 -0.08544 -0.02931 120 VAL A CB  
731  C CG1 . VAL A 94  ? 0.54108 0.39856 0.50127 -0.01623 -0.07204 -0.02851 120 VAL A CG1 
732  C CG2 . VAL A 94  ? 0.54595 0.40286 0.51319 -0.01957 -0.09654 -0.03185 120 VAL A CG2 
733  N N   . ALA A 95  ? 0.51936 0.35053 0.43909 -0.01863 -0.12252 -0.02161 121 ALA A N   
734  C CA  . ALA A 95  ? 0.54396 0.36283 0.44147 -0.02167 -0.13873 -0.02129 121 ALA A CA  
735  C C   . ALA A 95  ? 0.57737 0.37884 0.43733 -0.02311 -0.13770 -0.01603 121 ALA A C   
736  O O   . ALA A 95  ? 0.58788 0.37523 0.41830 -0.02713 -0.14659 -0.01663 121 ALA A O   
737  C CB  . ALA A 95  ? 0.52450 0.34876 0.44464 -0.01876 -0.15744 -0.01886 121 ALA A CB  
738  N N   . LYS A 96  ? 0.57127 0.37260 0.43097 -0.02031 -0.12675 -0.01109 122 LYS A N   
739  C CA  . LYS A 96  ? 0.64067 0.42557 0.46674 -0.02231 -0.12293 -0.00595 122 LYS A CA  
740  C C   . LYS A 96  ? 0.66694 0.44425 0.46874 -0.02744 -0.10935 -0.01138 122 LYS A C   
741  O O   . LYS A 96  ? 0.71002 0.47098 0.47804 -0.03108 -0.10766 -0.00909 122 LYS A O   
742  C CB  . LYS A 96  ? 0.65929 0.44698 0.49621 -0.01815 -0.11466 -0.00009 122 LYS A CB  
743  C CG  . LYS A 96  ? 0.68242 0.47478 0.54116 -0.01295 -0.12789 0.00534  122 LYS A CG  
744  C CD  . LYS A 96  ? 0.69181 0.49576 0.57754 -0.00807 -0.11750 0.00588  122 LYS A CD  
745  C CE  . LYS A 96  ? 0.71132 0.50505 0.58249 -0.00759 -0.11050 0.01205  122 LYS A CE  
746  N NZ  . LYS A 96  ? 0.68050 0.48457 0.57838 -0.00262 -0.10321 0.01191  122 LYS A NZ  
747  N N   . HIS A 97  ? 0.64999 0.43810 0.46864 -0.02787 -0.09906 -0.01845 123 HIS A N   
748  C CA  . HIS A 97  ? 0.65102 0.43300 0.45219 -0.03244 -0.08788 -0.02513 123 HIS A CA  
749  C C   . HIS A 97  ? 0.62858 0.40770 0.42317 -0.03617 -0.09738 -0.03213 123 HIS A C   
750  O O   . HIS A 97  ? 0.62045 0.39049 0.39433 -0.04055 -0.09046 -0.03822 123 HIS A O   
751  C CB  . HIS A 97  ? 0.63686 0.43040 0.45991 -0.03081 -0.07210 -0.02864 123 HIS A CB  
752  C CG  . HIS A 97  ? 0.65156 0.44823 0.48251 -0.02742 -0.06297 -0.02328 123 HIS A CG  
753  N ND1 . HIS A 97  ? 0.67399 0.45967 0.48439 -0.02893 -0.05536 -0.01994 123 HIS A ND1 
754  C CD2 . HIS A 97  ? 0.63591 0.44478 0.49280 -0.02296 -0.05994 -0.02121 123 HIS A CD2 
755  C CE1 . HIS A 97  ? 0.66435 0.45592 0.48981 -0.02545 -0.04917 -0.01617 123 HIS A CE1 
756  N NE2 . HIS A 97  ? 0.63683 0.44204 0.48904 -0.02171 -0.05208 -0.01712 123 HIS A NE2 
757  N N   . ASP A 98  ? 0.62988 0.41650 0.44341 -0.03463 -0.11276 -0.03210 124 ASP A N   
758  C CA  . ASP A 98  ? 0.64549 0.43155 0.45962 -0.03812 -0.12280 -0.03947 124 ASP A CA  
759  C C   . ASP A 98  ? 0.65151 0.43955 0.47622 -0.03652 -0.14439 -0.03624 124 ASP A C   
760  O O   . ASP A 98  ? 0.60612 0.40935 0.46702 -0.03358 -0.14893 -0.03645 124 ASP A O   
761  C CB  . ASP A 98  ? 0.64274 0.44253 0.48609 -0.03804 -0.11350 -0.04572 124 ASP A CB  
762  C CG  . ASP A 98  ? 0.66713 0.46736 0.51657 -0.04169 -0.12424 -0.05338 124 ASP A CG  
763  O OD1 . ASP A 98  ? 0.69600 0.48220 0.51665 -0.04588 -0.13238 -0.05740 124 ASP A OD1 
764  O OD2 . ASP A 98  ? 0.64966 0.46352 0.53209 -0.04073 -0.12409 -0.05561 124 ASP A OD2 
765  N N   . PRO A 99  ? 0.70895 0.48125 0.50309 -0.03847 -0.15823 -0.03300 125 PRO A N   
766  C CA  . PRO A 99  ? 0.71100 0.48418 0.51624 -0.03621 -0.18089 -0.02855 125 PRO A CA  
767  C C   . PRO A 99  ? 0.69860 0.48292 0.53280 -0.03714 -0.19284 -0.03563 125 PRO A C   
768  O O   . PRO A 99  ? 0.68789 0.46870 0.51293 -0.04184 -0.19229 -0.04414 125 PRO A O   
769  C CB  . PRO A 99  ? 0.77950 0.52960 0.53764 -0.03979 -0.19276 -0.02504 125 PRO A CB  
770  C CG  . PRO A 99  ? 0.80320 0.54174 0.52797 -0.04518 -0.17653 -0.03130 125 PRO A CG  
771  C CD  . PRO A 99  ? 0.75616 0.50810 0.50359 -0.04291 -0.15340 -0.03286 125 PRO A CD  
772  N N   . ASP A 100 ? 0.70014 0.49809 0.57193 -0.03266 -0.20283 -0.03248 126 ASP A N   
773  C CA  . ASP A 100 ? 0.70664 0.51790 0.61502 -0.03302 -0.21355 -0.03827 126 ASP A CA  
774  C C   . ASP A 100 ? 0.66997 0.49367 0.60023 -0.03477 -0.19592 -0.04539 126 ASP A C   
775  O O   . ASP A 100 ? 0.67781 0.50917 0.63152 -0.03714 -0.20251 -0.05176 126 ASP A O   
776  C CB  . ASP A 100 ? 0.78476 0.58421 0.67495 -0.03738 -0.23634 -0.04242 126 ASP A CB  
777  C CG  . ASP A 100 ? 0.88895 0.67452 0.75693 -0.03573 -0.25664 -0.03433 126 ASP A CG  
778  O OD1 . ASP A 100 ? 0.95663 0.72161 0.77608 -0.03927 -0.25947 -0.03281 126 ASP A OD1 
779  O OD2 . ASP A 100 ? 0.93408 0.72861 0.83324 -0.03093 -0.26934 -0.02938 126 ASP A OD2 
780  N N   . ASN A 101 ? 0.63199 0.45734 0.55615 -0.03370 -0.17438 -0.04402 127 ASN A N   
781  C CA  . ASN A 101 ? 0.58424 0.41945 0.52652 -0.03497 -0.15739 -0.04912 127 ASN A CA  
782  C C   . ASN A 101 ? 0.58049 0.41070 0.51606 -0.04074 -0.16134 -0.05814 127 ASN A C   
783  O O   . ASN A 101 ? 0.58148 0.42203 0.54628 -0.04228 -0.16081 -0.06283 127 ASN A O   
784  C CB  . ASN A 101 ? 0.54846 0.40224 0.53528 -0.03150 -0.15359 -0.04776 127 ASN A CB  
785  C CG  . ASN A 101 ? 0.55758 0.41587 0.55180 -0.02573 -0.14901 -0.04029 127 ASN A CG  
786  O OD1 . ASN A 101 ? 0.57196 0.43961 0.59413 -0.02236 -0.15668 -0.03810 127 ASN A OD1 
787  N ND2 . ASN A 101 ? 0.54870 0.40039 0.52006 -0.02460 -0.13635 -0.03698 127 ASN A ND2 
788  N N   . LYS A 102 ? 0.57772 0.39087 0.47364 -0.04429 -0.16444 -0.06083 128 LYS A N   
789  C CA  . LYS A 102 ? 0.60144 0.40676 0.48643 -0.04992 -0.17255 -0.07022 128 LYS A CA  
790  C C   . LYS A 102 ? 0.57399 0.38003 0.46105 -0.05261 -0.15483 -0.07709 128 LYS A C   
791  O O   . LYS A 102 ? 0.59419 0.40395 0.49891 -0.05581 -0.15795 -0.08438 128 LYS A O   
792  C CB  . LYS A 102 ? 0.64334 0.42806 0.48172 -0.05293 -0.18366 -0.07078 128 LYS A CB  
793  C CG  . LYS A 102 ? 0.68387 0.45802 0.50626 -0.05893 -0.19492 -0.08125 128 LYS A CG  
794  C CD  . LYS A 102 ? 0.72944 0.48354 0.50038 -0.06207 -0.19030 -0.08276 128 LYS A CD  
795  C CE  . LYS A 102 ? 0.77045 0.51585 0.52036 -0.06319 -0.20900 -0.08127 128 LYS A CE  
796  N NZ  . LYS A 102 ? 0.78966 0.51674 0.49149 -0.06692 -0.20135 -0.08410 128 LYS A NZ  
797  N N   . PHE A 103 ? 0.54044 0.34273 0.41195 -0.05138 -0.13683 -0.07491 129 PHE A N   
798  C CA  . PHE A 103 ? 0.52178 0.32230 0.39273 -0.05369 -0.12109 -0.08139 129 PHE A CA  
799  C C   . PHE A 103 ? 0.47490 0.28936 0.37650 -0.05042 -0.10635 -0.07783 129 PHE A C   
800  O O   . PHE A 103 ? 0.45452 0.27065 0.36809 -0.05231 -0.09785 -0.08293 129 PHE A O   
801  C CB  . PHE A 103 ? 0.54872 0.33423 0.38198 -0.05515 -0.11035 -0.08289 129 PHE A CB  
802  C CG  . PHE A 103 ? 0.63312 0.40112 0.42936 -0.05978 -0.12123 -0.08841 129 PHE A CG  
803  C CD1 . PHE A 103 ? 0.65915 0.42061 0.45051 -0.06461 -0.12591 -0.09945 129 PHE A CD1 
804  C CD2 . PHE A 103 ? 0.68391 0.44041 0.44831 -0.05961 -0.12662 -0.08259 129 PHE A CD2 
805  C CE1 . PHE A 103 ? 0.71035 0.45700 0.46664 -0.06845 -0.13460 -0.10416 129 PHE A CE1 
806  C CE2 . PHE A 103 ? 0.73336 0.47140 0.45873 -0.06430 -0.13663 -0.08716 129 PHE A CE2 
807  C CZ  . PHE A 103 ? 0.74025 0.47550 0.46299 -0.06816 -0.13956 -0.09749 129 PHE A CZ  
808  N N   . ALA A 104 ? 0.47026 0.29345 0.38370 -0.04570 -0.10346 -0.06931 130 ALA A N   
809  C CA  . ALA A 104 ? 0.44467 0.27710 0.37646 -0.04259 -0.08823 -0.06545 130 ALA A CA  
810  C C   . ALA A 104 ? 0.41403 0.26118 0.37923 -0.04003 -0.09046 -0.06142 130 ALA A C   
811  O O   . ALA A 104 ? 0.39382 0.24508 0.36671 -0.03829 -0.10169 -0.05847 130 ALA A O   
812  C CB  . ALA A 104 ? 0.36717 0.19568 0.28153 -0.03942 -0.07944 -0.05983 130 ALA A CB  
813  N N   . MET A 105 ? 0.39404 0.24833 0.37912 -0.03986 -0.07930 -0.06120 131 MET A N   
814  C CA  . MET A 105 ? 0.37470 0.24185 0.38828 -0.03747 -0.07612 -0.05688 131 MET A CA  
815  C C   . MET A 105 ? 0.34430 0.21329 0.35434 -0.03356 -0.06324 -0.05127 131 MET A C   
816  O O   . MET A 105 ? 0.32328 0.18851 0.32753 -0.03413 -0.05321 -0.05170 131 MET A O   
817  C CB  . MET A 105 ? 0.39374 0.26618 0.43144 -0.04089 -0.07318 -0.06011 131 MET A CB  
818  C CG  . MET A 105 ? 0.42607 0.31122 0.49357 -0.03942 -0.06901 -0.05624 131 MET A CG  
819  S SD  . MET A 105 ? 0.46372 0.35239 0.55450 -0.04349 -0.05874 -0.05732 131 MET A SD  
820  C CE  . MET A 105 ? 0.45421 0.33672 0.52721 -0.04115 -0.04353 -0.05261 131 MET A CE  
821  N N   . PRO A 106 ? 0.34574 0.21979 0.35973 -0.02952 -0.06381 -0.04637 132 PRO A N   
822  C CA  . PRO A 106 ? 0.31902 0.19361 0.32777 -0.02601 -0.05277 -0.04191 132 PRO A CA  
823  C C   . PRO A 106 ? 0.29880 0.17863 0.32267 -0.02629 -0.04185 -0.04074 132 PRO A C   
824  O O   . PRO A 106 ? 0.26795 0.15549 0.31320 -0.02721 -0.04127 -0.04076 132 PRO A O   
825  C CB  . PRO A 106 ? 0.28139 0.16063 0.29563 -0.02201 -0.05744 -0.03817 132 PRO A CB  
826  C CG  . PRO A 106 ? 0.28584 0.17122 0.31951 -0.02314 -0.06827 -0.04016 132 PRO A CG  
827  C CD  . PRO A 106 ? 0.29878 0.17782 0.32372 -0.02783 -0.07548 -0.04511 132 PRO A CD  
828  N N   . TYR A 107 ? 0.28940 0.16435 0.30231 -0.02568 -0.03319 -0.03943 133 TYR A N   
829  C CA  . TYR A 107 ? 0.28060 0.15703 0.30244 -0.02623 -0.02388 -0.03745 133 TYR A CA  
830  C C   . TYR A 107 ? 0.28956 0.16816 0.30919 -0.02243 -0.01729 -0.03279 133 TYR A C   
831  O O   . TYR A 107 ? 0.28027 0.16484 0.31217 -0.02183 -0.01325 -0.03073 133 TYR A O   
832  C CB  . TYR A 107 ? 0.27752 0.14589 0.29061 -0.02826 -0.02080 -0.03971 133 TYR A CB  
833  C CG  . TYR A 107 ? 0.29761 0.16470 0.31763 -0.02882 -0.01286 -0.03680 133 TYR A CG  
834  C CD1 . TYR A 107 ? 0.30674 0.17743 0.34319 -0.03145 -0.01042 -0.03564 133 TYR A CD1 
835  C CD2 . TYR A 107 ? 0.28585 0.14732 0.29669 -0.02695 -0.00825 -0.03489 133 TYR A CD2 
836  C CE1 . TYR A 107 ? 0.30469 0.17198 0.34475 -0.03230 -0.00338 -0.03174 133 TYR A CE1 
837  C CE2 . TYR A 107 ? 0.28277 0.14136 0.29855 -0.02732 -0.00297 -0.03133 133 TYR A CE2 
838  C CZ  . TYR A 107 ? 0.28441 0.14517 0.31305 -0.03005 -0.00048 -0.02934 133 TYR A CZ  
839  O OH  . TYR A 107 ? 0.28352 0.13933 0.31451 -0.03072 0.00459  -0.02457 133 TYR A OH  
840  N N   . MET A 108 ? 0.28895 0.16247 0.29354 -0.02010 -0.01567 -0.03164 134 MET A N   
841  C CA  . MET A 108 ? 0.28612 0.16055 0.28687 -0.01652 -0.01133 -0.02823 134 MET A CA  
842  C C   . MET A 108 ? 0.30971 0.18162 0.29934 -0.01416 -0.01517 -0.02831 134 MET A C   
843  O O   . MET A 108 ? 0.33177 0.19948 0.31308 -0.01559 -0.01954 -0.03036 134 MET A O   
844  C CB  . MET A 108 ? 0.25526 0.12498 0.25107 -0.01627 -0.00537 -0.02607 134 MET A CB  
845  C CG  . MET A 108 ? 0.27639 0.14621 0.28105 -0.01886 -0.00111 -0.02452 134 MET A CG  
846  S SD  . MET A 108 ? 0.27601 0.15159 0.28872 -0.01831 0.00498  -0.02146 134 MET A SD  
847  C CE  . MET A 108 ? 0.26675 0.14301 0.29404 -0.02327 0.00843  -0.02091 134 MET A CE  
848  N N   . TRP A 109 ? 0.27082 0.14414 0.25917 -0.01084 -0.01306 -0.02615 135 TRP A N   
849  C CA  . TRP A 109 ? 0.28439 0.15466 0.26381 -0.00871 -0.01600 -0.02556 135 TRP A CA  
850  C C   . TRP A 109 ? 0.29130 0.16058 0.26780 -0.00581 -0.01173 -0.02401 135 TRP A C   
851  O O   . TRP A 109 ? 0.29034 0.16174 0.27061 -0.00504 -0.00744 -0.02332 135 TRP A O   
852  C CB  . TRP A 109 ? 0.28890 0.16232 0.27353 -0.00751 -0.02259 -0.02531 135 TRP A CB  
853  C CG  . TRP A 109 ? 0.28353 0.16442 0.28341 -0.00535 -0.02089 -0.02510 135 TRP A CG  
854  C CD1 . TRP A 109 ? 0.27683 0.16395 0.29130 -0.00684 -0.01895 -0.02621 135 TRP A CD1 
855  C CD2 . TRP A 109 ? 0.28284 0.16546 0.28638 -0.00154 -0.01982 -0.02436 135 TRP A CD2 
856  N NE1 . TRP A 109 ? 0.26277 0.15567 0.28969 -0.00422 -0.01561 -0.02637 135 TRP A NE1 
857  C CE2 . TRP A 109 ? 0.28941 0.17948 0.30953 -0.00075 -0.01633 -0.02558 135 TRP A CE2 
858  C CE3 . TRP A 109 ? 0.30093 0.17917 0.29659 0.00108  -0.02082 -0.02318 135 TRP A CE3 
859  C CZ2 . TRP A 109 ? 0.31826 0.21134 0.34649 0.00283  -0.01347 -0.02639 135 TRP A CZ2 
860  C CZ3 . TRP A 109 ? 0.32506 0.20601 0.32890 0.00463  -0.01921 -0.02370 135 TRP A CZ3 
861  C CH2 . TRP A 109 ? 0.33445 0.22268 0.35403 0.00563  -0.01541 -0.02564 135 TRP A CH2 
862  N N   . ALA A 110 ? 0.30160 0.16662 0.27027 -0.00461 -0.01293 -0.02354 136 ALA A N   
863  C CA  . ALA A 110 ? 0.28896 0.15242 0.25557 -0.00201 -0.01063 -0.02282 136 ALA A CA  
864  C C   . ALA A 110 ? 0.31661 0.17717 0.27968 -0.00069 -0.01356 -0.02198 136 ALA A C   
865  O O   . ALA A 110 ? 0.33085 0.18973 0.29078 -0.00185 -0.01740 -0.02125 136 ALA A O   
866  C CB  . ALA A 110 ? 0.28390 0.14357 0.24709 -0.00273 -0.00780 -0.02302 136 ALA A CB  
867  N N   . THR A 111 ? 0.30986 0.16867 0.27258 0.00152  -0.01234 -0.02190 137 THR A N   
868  C CA  . THR A 111 ? 0.33756 0.19309 0.29902 0.00287  -0.01466 -0.02071 137 THR A CA  
869  C C   . THR A 111 ? 0.33217 0.18298 0.29096 0.00254  -0.01248 -0.02092 137 THR A C   
870  O O   . THR A 111 ? 0.30980 0.16067 0.26948 0.00223  -0.01035 -0.02230 137 THR A O   
871  C CB  . THR A 111 ? 0.36066 0.21904 0.32934 0.00630  -0.01584 -0.02130 137 THR A CB  
872  O OG1 . THR A 111 ? 0.36703 0.22633 0.33630 0.00772  -0.01238 -0.02360 137 THR A OG1 
873  C CG2 . THR A 111 ? 0.37166 0.23561 0.34806 0.00672  -0.01796 -0.02137 137 THR A CG2 
874  N N   . THR A 112 ? 0.33046 0.17673 0.28729 0.00250  -0.01353 -0.01918 138 THR A N   
875  C CA  . THR A 112 ? 0.33304 0.17514 0.29139 0.00221  -0.01138 -0.01943 138 THR A CA  
876  C C   . THR A 112 ? 0.30794 0.14997 0.27201 0.00539  -0.01365 -0.02020 138 THR A C   
877  O O   . THR A 112 ? 0.32760 0.16707 0.29243 0.00643  -0.01598 -0.01811 138 THR A O   
878  C CB  . THR A 112 ? 0.35582 0.19146 0.30777 -0.00071 -0.00936 -0.01682 138 THR A CB  
879  O OG1 . THR A 112 ? 0.34473 0.17973 0.29021 -0.00372 -0.00646 -0.01756 138 THR A OG1 
880  C CG2 . THR A 112 ? 0.35866 0.19058 0.31613 -0.00143 -0.00603 -0.01720 138 THR A CG2 
881  N N   . GLY A 113 ? 0.28023 0.12399 0.24762 0.00695  -0.01352 -0.02331 139 GLY A N   
882  C CA  . GLY A 113 ? 0.27042 0.11366 0.24149 0.00991  -0.01520 -0.02571 139 GLY A CA  
883  C C   . GLY A 113 ? 0.28493 0.12480 0.25912 0.00995  -0.01623 -0.02827 139 GLY A C   
884  O O   . GLY A 113 ? 0.29218 0.12984 0.26956 0.00774  -0.01539 -0.02733 139 GLY A O   
885  N N   . ILE A 114 ? 0.25586 0.09510 0.22973 0.01234  -0.01791 -0.03213 140 ILE A N   
886  C CA  . ILE A 114 ? 0.28411 0.11946 0.26100 0.01262  -0.02102 -0.03556 140 ILE A CA  
887  C C   . ILE A 114 ? 0.29022 0.12553 0.25956 0.01290  -0.02315 -0.03783 140 ILE A C   
888  O O   . ILE A 114 ? 0.29655 0.13240 0.25721 0.01430  -0.02180 -0.03945 140 ILE A O   
889  C CB  . ILE A 114 ? 0.29026 0.12225 0.27084 0.01494  -0.02246 -0.03903 140 ILE A CB  
890  C CG1 . ILE A 114 ? 0.30809 0.13842 0.29577 0.01471  -0.02137 -0.03537 140 ILE A CG1 
891  C CG2 . ILE A 114 ? 0.29940 0.12691 0.28339 0.01485  -0.02694 -0.04344 140 ILE A CG2 
892  C CD1 . ILE A 114 ? 0.31505 0.14146 0.30907 0.01729  -0.02290 -0.03850 140 ILE A CD1 
893  N N   . GLY A 115 ? 0.27813 0.11217 0.25123 0.01147  -0.02630 -0.03773 141 GLY A N   
894  C CA  . GLY A 115 ? 0.30351 0.13506 0.26981 0.01193  -0.03125 -0.03948 141 GLY A CA  
895  C C   . GLY A 115 ? 0.32141 0.14805 0.29088 0.01274  -0.03784 -0.04420 141 GLY A C   
896  O O   . GLY A 115 ? 0.29581 0.12208 0.27896 0.01189  -0.03878 -0.04506 141 GLY A O   
897  N N   . TYR A 116 ? 0.33772 0.15973 0.29365 0.01401  -0.04212 -0.04742 142 TYR A N   
898  C CA  . TYR A 116 ? 0.34759 0.16395 0.30465 0.01475  -0.04913 -0.05317 142 TYR A CA  
899  C C   . TYR A 116 ? 0.36908 0.17854 0.30824 0.01529  -0.05648 -0.05564 142 TYR A C   
900  O O   . TYR A 116 ? 0.36348 0.17164 0.28587 0.01538  -0.05355 -0.05327 142 TYR A O   
901  C CB  . TYR A 116 ? 0.36725 0.18247 0.32494 0.01620  -0.04508 -0.05715 142 TYR A CB  
902  C CG  . TYR A 116 ? 0.37614 0.19049 0.31761 0.01784  -0.03938 -0.05905 142 TYR A CG  
903  C CD1 . TYR A 116 ? 0.39929 0.20647 0.32555 0.01895  -0.04179 -0.06552 142 TYR A CD1 
904  C CD2 . TYR A 116 ? 0.37956 0.19990 0.32145 0.01803  -0.03125 -0.05497 142 TYR A CD2 
905  C CE1 . TYR A 116 ? 0.41946 0.22567 0.33177 0.02011  -0.03419 -0.06786 142 TYR A CE1 
906  C CE2 . TYR A 116 ? 0.40539 0.22586 0.33676 0.01932  -0.02490 -0.05710 142 TYR A CE2 
907  C CZ  . TYR A 116 ? 0.42368 0.23718 0.34053 0.02031  -0.02536 -0.06355 142 TYR A CZ  
908  O OH  . TYR A 116 ? 0.43613 0.24959 0.34327 0.02127  -0.01673 -0.06624 142 TYR A OH  
909  N N   . ASN A 117 ? 0.37148 0.17558 0.31410 0.01532  -0.06646 -0.06031 143 ASN A N   
910  C CA  . ASN A 117 ? 0.38484 0.17971 0.30779 0.01575  -0.07593 -0.06369 143 ASN A CA  
911  C C   . ASN A 117 ? 0.38922 0.17841 0.29550 0.01693  -0.07223 -0.07042 143 ASN A C   
912  O O   . ASN A 117 ? 0.36571 0.15394 0.28243 0.01744  -0.07309 -0.07611 143 ASN A O   
913  C CB  . ASN A 117 ? 0.40936 0.20108 0.34595 0.01520  -0.08981 -0.06645 143 ASN A CB  
914  C CG  . ASN A 117 ? 0.44167 0.22254 0.35643 0.01547  -0.10268 -0.06878 143 ASN A CG  
915  O OD1 . ASN A 117 ? 0.46018 0.23277 0.35129 0.01597  -0.10310 -0.07392 143 ASN A OD1 
916  N ND2 . ASN A 117 ? 0.45601 0.23598 0.37831 0.01514  -0.11348 -0.06517 143 ASN A ND2 
917  N N   . VAL A 118 ? 0.41467 0.19962 0.29606 0.01717  -0.06717 -0.06998 144 VAL A N   
918  C CA  . VAL A 118 ? 0.44659 0.22663 0.31267 0.01828  -0.06043 -0.07692 144 VAL A CA  
919  C C   . VAL A 118 ? 0.47336 0.24332 0.33183 0.01856  -0.07067 -0.08591 144 VAL A C   
920  O O   . VAL A 118 ? 0.46731 0.23627 0.33282 0.01971  -0.06788 -0.09304 144 VAL A O   
921  C CB  . VAL A 118 ? 0.47362 0.24972 0.31336 0.01772  -0.05250 -0.07471 144 VAL A CB  
922  C CG1 . VAL A 118 ? 0.50967 0.28004 0.33380 0.01872  -0.04407 -0.08318 144 VAL A CG1 
923  C CG2 . VAL A 118 ? 0.43315 0.21957 0.28357 0.01725  -0.04267 -0.06681 144 VAL A CG2 
924  N N   . ASP A 119 ? 0.49289 0.25459 0.33783 0.01753  -0.08379 -0.08578 145 ASP A N   
925  C CA  . ASP A 119 ? 0.55204 0.30212 0.38437 0.01746  -0.09522 -0.09493 145 ASP A CA  
926  C C   . ASP A 119 ? 0.52962 0.28487 0.39272 0.01757  -0.10125 -0.09908 145 ASP A C   
927  O O   . ASP A 119 ? 0.53947 0.29440 0.40398 0.01779  -0.09995 -0.10603 145 ASP A O   
928  C CB  . ASP A 119 ? 0.60760 0.34759 0.41942 0.01631  -0.11010 -0.09238 145 ASP A CB  
929  C CG  . ASP A 119 ? 0.67634 0.41023 0.45585 0.01555  -0.10320 -0.08700 145 ASP A CG  
930  O OD1 . ASP A 119 ? 0.71746 0.44366 0.47077 0.01539  -0.09434 -0.09239 145 ASP A OD1 
931  O OD2 . ASP A 119 ? 0.69008 0.42647 0.47138 0.01494  -0.10571 -0.07759 145 ASP A OD2 
932  N N   . LYS A 120 ? 0.51247 0.27645 0.40348 0.01689  -0.10505 -0.09317 146 LYS A N   
933  C CA  . LYS A 120 ? 0.51990 0.29311 0.44256 0.01608  -0.10753 -0.09426 146 LYS A CA  
934  C C   . LYS A 120 ? 0.48082 0.26060 0.41677 0.01658  -0.09416 -0.09524 146 LYS A C   
935  O O   . LYS A 120 ? 0.48268 0.26427 0.43128 0.01613  -0.09491 -0.09959 146 LYS A O   
936  C CB  . LYS A 120 ? 0.54372 0.32519 0.49253 0.01493  -0.11167 -0.08752 146 LYS A CB  
937  C CG  . LYS A 120 ? 0.62366 0.39860 0.56342 0.01485  -0.12582 -0.08562 146 LYS A CG  
938  C CD  . LYS A 120 ? 0.68415 0.46339 0.64868 0.01407  -0.13887 -0.08694 146 LYS A CD  
939  C CE  . LYS A 120 ? 0.72828 0.50330 0.69255 0.01435  -0.15283 -0.08326 146 LYS A CE  
940  N NZ  . LYS A 120 ? 0.74505 0.52612 0.73934 0.01405  -0.16539 -0.08441 146 LYS A NZ  
941  N N   . VAL A 121 ? 0.45626 0.23891 0.38997 0.01756  -0.08274 -0.09101 147 VAL A N   
942  C CA  . VAL A 121 ? 0.44914 0.23694 0.39498 0.01843  -0.07164 -0.09112 147 VAL A CA  
943  C C   . VAL A 121 ? 0.49077 0.27241 0.42361 0.01986  -0.06902 -0.09995 147 VAL A C   
944  O O   . VAL A 121 ? 0.45369 0.23752 0.40125 0.01991  -0.06659 -0.10281 147 VAL A O   
945  C CB  . VAL A 121 ? 0.41928 0.21052 0.36386 0.01948  -0.06192 -0.08510 147 VAL A CB  
946  C CG1 . VAL A 121 ? 0.40788 0.20101 0.35762 0.02143  -0.05221 -0.08688 147 VAL A CG1 
947  C CG2 . VAL A 121 ? 0.39179 0.19092 0.35571 0.01762  -0.06158 -0.07691 147 VAL A CG2 
948  N N   . LYS A 122 ? 0.53461 0.30759 0.43876 0.02078  -0.06860 -0.10434 148 LYS A N   
949  C CA  . LYS A 122 ? 0.58480 0.35176 0.47526 0.02184  -0.06403 -0.11367 148 LYS A CA  
950  C C   . LYS A 122 ? 0.60020 0.36253 0.48908 0.02035  -0.07443 -0.12033 148 LYS A C   
951  O O   . LYS A 122 ? 0.60033 0.35864 0.48400 0.02080  -0.07065 -0.12873 148 LYS A O   
952  C CB  . LYS A 122 ? 0.65105 0.40974 0.50904 0.02263  -0.05785 -0.11608 148 LYS A CB  
953  C CG  . LYS A 122 ? 0.70102 0.46455 0.56323 0.02474  -0.04322 -0.11384 148 LYS A CG  
954  C CD  . LYS A 122 ? 0.76905 0.52669 0.60414 0.02502  -0.03252 -0.11873 148 LYS A CD  
955  C CE  . LYS A 122 ? 0.79205 0.55005 0.60757 0.02287  -0.03083 -0.11031 148 LYS A CE  
956  N NZ  . LYS A 122 ? 0.79225 0.55663 0.60728 0.02333  -0.01447 -0.10776 148 LYS A NZ  
957  N N   . ALA A 123 ? 0.60533 0.36808 0.50011 0.01866  -0.08748 -0.11723 149 ALA A N   
958  C CA  . ALA A 123 ? 0.63855 0.39798 0.53685 0.01736  -0.09862 -0.12320 149 ALA A CA  
959  C C   . ALA A 123 ? 0.62141 0.38870 0.55275 0.01670  -0.09690 -0.12300 149 ALA A C   
960  O O   . ALA A 123 ? 0.63177 0.39575 0.56596 0.01624  -0.09908 -0.13028 149 ALA A O   
961  C CB  . ALA A 123 ? 0.66946 0.42627 0.56397 0.01621  -0.11437 -0.12000 149 ALA A CB  
962  N N   . VAL A 124 ? 0.59029 0.36707 0.54525 0.01632  -0.09252 -0.11454 150 VAL A N   
963  C CA  . VAL A 124 ? 0.59067 0.37378 0.57440 0.01520  -0.08984 -0.11273 150 VAL A CA  
964  C C   . VAL A 124 ? 0.58876 0.37295 0.57742 0.01669  -0.07725 -0.11231 150 VAL A C   
965  O O   . VAL A 124 ? 0.57657 0.36357 0.58564 0.01588  -0.07489 -0.11076 150 VAL A O   
966  C CB  . VAL A 124 ? 0.58089 0.37295 0.58738 0.01339  -0.09070 -0.10374 150 VAL A CB  
967  C CG1 . VAL A 124 ? 0.59161 0.38334 0.59866 0.01240  -0.10393 -0.10403 150 VAL A CG1 
968  C CG2 . VAL A 124 ? 0.57473 0.37075 0.57832 0.01419  -0.08097 -0.09618 150 VAL A CG2 
969  N N   . LEU A 125 ? 0.59377 0.37543 0.56536 0.01894  -0.06941 -0.11341 151 LEU A N   
970  C CA  . LEU A 125 ? 0.57880 0.36179 0.55771 0.02099  -0.05854 -0.11283 151 LEU A CA  
971  C C   . LEU A 125 ? 0.61124 0.38787 0.57131 0.02338  -0.05206 -0.12143 151 LEU A C   
972  O O   . LEU A 125 ? 0.58809 0.36557 0.55627 0.02565  -0.04340 -0.12196 151 LEU A O   
973  C CB  . LEU A 125 ? 0.54067 0.33036 0.52746 0.02155  -0.05253 -0.10281 151 LEU A CB  
974  C CG  . LEU A 125 ? 0.50309 0.29885 0.51171 0.01927  -0.05347 -0.09410 151 LEU A CG  
975  C CD1 . LEU A 125 ? 0.46579 0.26633 0.47629 0.01959  -0.04781 -0.08524 151 LEU A CD1 
976  C CD2 . LEU A 125 ? 0.50297 0.29777 0.52796 0.01920  -0.05155 -0.09457 151 LEU A CD2 
977  N N   . GLY A 126 ? 0.63392 0.40379 0.56899 0.02295  -0.05567 -0.12793 152 GLY A N   
978  C CA  . GLY A 126 ? 0.63764 0.40067 0.55263 0.02451  -0.04779 -0.13711 152 GLY A CA  
979  C C   . GLY A 126 ? 0.63605 0.40000 0.53772 0.02641  -0.03865 -0.13457 152 GLY A C   
980  O O   . GLY A 126 ? 0.61663 0.38638 0.52534 0.02675  -0.03849 -0.12550 152 GLY A O   
981  N N   . GLU A 127 ? 0.66600 0.42375 0.54784 0.02744  -0.02998 -0.14323 153 GLU A N   
982  C CA  . GLU A 127 ? 0.68604 0.44434 0.55634 0.02939  -0.01879 -0.14193 153 GLU A CA  
983  C C   . GLU A 127 ? 0.62558 0.39234 0.52333 0.03255  -0.01076 -0.13776 153 GLU A C   
984  O O   . GLU A 127 ? 0.62332 0.39250 0.51801 0.03431  -0.00352 -0.13416 153 GLU A O   
985  C CB  . GLU A 127 ? 0.75580 0.50639 0.60132 0.02946  -0.00895 -0.15282 153 GLU A CB  
986  C CG  . GLU A 127 ? 0.78810 0.53621 0.60992 0.02953  0.00120  -0.15021 153 GLU A CG  
987  C CD  . GLU A 127 ? 0.82189 0.56246 0.61291 0.02621  -0.00778 -0.14483 153 GLU A CD  
988  O OE1 . GLU A 127 ? 0.84185 0.57715 0.62322 0.02418  -0.02048 -0.14736 153 GLU A OE1 
989  O OE2 . GLU A 127 ? 0.81784 0.55728 0.59534 0.02549  -0.00243 -0.13783 153 GLU A OE2 
990  N N   . ASN A 128 ? 0.59415 0.36440 0.51736 0.03322  -0.01235 -0.13716 154 ASN A N   
991  C CA  . ASN A 128 ? 0.59686 0.37429 0.54563 0.03618  -0.00707 -0.13170 154 ASN A CA  
992  C C   . ASN A 128 ? 0.56455 0.34933 0.52879 0.03502  -0.01402 -0.11928 154 ASN A C   
993  O O   . ASN A 128 ? 0.56826 0.35841 0.55316 0.03675  -0.01234 -0.11334 154 ASN A O   
994  C CB  . ASN A 128 ? 0.63130 0.40658 0.59593 0.03779  -0.00528 -0.13590 154 ASN A CB  
995  C CG  . ASN A 128 ? 0.69520 0.46339 0.64774 0.03984  0.00461  -0.14787 154 ASN A CG  
996  O OD1 . ASN A 128 ? 0.73143 0.49938 0.67206 0.04138  0.01381  -0.15141 154 ASN A OD1 
997  N ND2 . ASN A 128 ? 0.72142 0.48331 0.67660 0.03989  0.00340  -0.15440 154 ASN A ND2 
998  N N   . ALA A 129 ? 0.54580 0.33036 0.49992 0.03208  -0.02182 -0.11507 155 ALA A N   
999  C CA  . ALA A 129 ? 0.49662 0.28734 0.46454 0.03038  -0.02699 -0.10421 155 ALA A CA  
1000 C C   . ALA A 129 ? 0.44301 0.23928 0.41890 0.03241  -0.02155 -0.09778 155 ALA A C   
1001 O O   . ALA A 129 ? 0.39425 0.19252 0.35793 0.03305  -0.01610 -0.09796 155 ALA A O   
1002 C CB  . ALA A 129 ? 0.48507 0.27453 0.44026 0.02749  -0.03482 -0.10158 155 ALA A CB  
1003 N N   . PRO A 130 ? 0.44259 0.24346 0.43771 0.03246  -0.02208 -0.09026 156 PRO A N   
1004 C CA  . PRO A 130 ? 0.41174 0.21748 0.41520 0.03431  -0.01870 -0.08421 156 PRO A CA  
1005 C C   . PRO A 130 ? 0.37590 0.18728 0.37086 0.03137  -0.01962 -0.07599 156 PRO A C   
1006 O O   . PRO A 130 ? 0.35309 0.16718 0.35572 0.02986  -0.02176 -0.06772 156 PRO A O   
1007 C CB  . PRO A 130 ? 0.40483 0.21177 0.42676 0.03437  -0.02064 -0.07795 156 PRO A CB  
1008 C CG  . PRO A 130 ? 0.43088 0.23528 0.45307 0.03095  -0.02538 -0.07714 156 PRO A CG  
1009 C CD  . PRO A 130 ? 0.44557 0.24628 0.45436 0.03054  -0.02632 -0.08676 156 PRO A CD  
1010 N N   . VAL A 131 ? 0.36959 0.18198 0.34713 0.03026  -0.01749 -0.07812 157 VAL A N   
1011 C CA  . VAL A 131 ? 0.37685 0.19431 0.34679 0.02757  -0.01798 -0.07086 157 VAL A CA  
1012 C C   . VAL A 131 ? 0.38891 0.21433 0.36522 0.02799  -0.01309 -0.06496 157 VAL A C   
1013 O O   . VAL A 131 ? 0.40824 0.23780 0.38123 0.02570  -0.01364 -0.05872 157 VAL A O   
1014 C CB  . VAL A 131 ? 0.37519 0.18977 0.32417 0.02632  -0.01762 -0.07401 157 VAL A CB  
1015 C CG1 . VAL A 131 ? 0.37140 0.17756 0.31358 0.02562  -0.02538 -0.07961 157 VAL A CG1 
1016 C CG2 . VAL A 131 ? 0.36495 0.17965 0.30524 0.02800  -0.00864 -0.07908 157 VAL A CG2 
1017 N N   . ASP A 132 ? 0.38173 0.20922 0.36881 0.03094  -0.00892 -0.06731 158 ASP A N   
1018 C CA  . ASP A 132 ? 0.36146 0.19656 0.35809 0.03160  -0.00609 -0.06237 158 ASP A CA  
1019 C C   . ASP A 132 ? 0.33472 0.16973 0.34609 0.03234  -0.01136 -0.05645 158 ASP A C   
1020 O O   . ASP A 132 ? 0.33293 0.17262 0.35561 0.03395  -0.01109 -0.05363 158 ASP A O   
1021 C CB  . ASP A 132 ? 0.37536 0.21344 0.37752 0.03442  0.00184  -0.06855 158 ASP A CB  
1022 C CG  . ASP A 132 ? 0.38751 0.22113 0.40241 0.03816  0.00224  -0.07514 158 ASP A CG  
1023 O OD1 . ASP A 132 ? 0.39084 0.21753 0.40580 0.03813  -0.00335 -0.07621 158 ASP A OD1 
1024 O OD2 . ASP A 132 ? 0.40978 0.24685 0.43695 0.04111  0.00845  -0.07959 158 ASP A OD2 
1025 N N   . SER A 133 ? 0.32544 0.15457 0.33707 0.03097  -0.01640 -0.05425 159 SER A N   
1026 C CA  . SER A 133 ? 0.34552 0.17173 0.36796 0.03119  -0.02075 -0.04806 159 SER A CA  
1027 C C   . SER A 133 ? 0.37564 0.19754 0.39302 0.02737  -0.02364 -0.04343 159 SER A C   
1028 O O   . SER A 133 ? 0.39424 0.21391 0.40654 0.02581  -0.02392 -0.04725 159 SER A O   
1029 C CB  . SER A 133 ? 0.34525 0.16618 0.38163 0.03482  -0.02180 -0.05224 159 SER A CB  
1030 O OG  . SER A 133 ? 0.34245 0.15690 0.38592 0.03402  -0.02664 -0.04583 159 SER A OG  
1031 N N   . TRP A 134 ? 0.36625 0.18643 0.38524 0.02572  -0.02583 -0.03530 160 TRP A N   
1032 C CA  . TRP A 134 ? 0.34580 0.16106 0.36187 0.02180  -0.02638 -0.03088 160 TRP A CA  
1033 C C   . TRP A 134 ? 0.34033 0.14814 0.36567 0.02189  -0.02776 -0.03362 160 TRP A C   
1034 O O   . TRP A 134 ? 0.36626 0.17067 0.39239 0.01843  -0.02718 -0.03204 160 TRP A O   
1035 C CB  . TRP A 134 ? 0.33002 0.14266 0.34247 0.01979  -0.02756 -0.02174 160 TRP A CB  
1036 C CG  . TRP A 134 ? 0.32848 0.14740 0.33093 0.01827  -0.02651 -0.01940 160 TRP A CG  
1037 C CD1 . TRP A 134 ? 0.34596 0.16885 0.34817 0.01991  -0.02892 -0.01731 160 TRP A CD1 
1038 C CD2 . TRP A 134 ? 0.31081 0.13254 0.30459 0.01482  -0.02326 -0.01941 160 TRP A CD2 
1039 N NE1 . TRP A 134 ? 0.27230 0.09991 0.26507 0.01738  -0.02731 -0.01621 160 TRP A NE1 
1040 C CE2 . TRP A 134 ? 0.32013 0.14686 0.30739 0.01439  -0.02353 -0.01744 160 TRP A CE2 
1041 C CE3 . TRP A 134 ? 0.30917 0.12975 0.30271 0.01218  -0.02063 -0.02122 160 TRP A CE3 
1042 C CZ2 . TRP A 134 ? 0.32768 0.15751 0.30708 0.01146  -0.02070 -0.01736 160 TRP A CZ2 
1043 C CZ3 . TRP A 134 ? 0.28858 0.11276 0.27570 0.00962  -0.01797 -0.02091 160 TRP A CZ3 
1044 C CH2 . TRP A 134 ? 0.26343 0.09180 0.24295 0.00930  -0.01774 -0.01905 160 TRP A CH2 
1045 N N   . ASP A 135 ? 0.32695 0.13266 0.36123 0.02560  -0.02896 -0.03819 161 ASP A N   
1046 C CA  . ASP A 135 ? 0.34117 0.14478 0.38260 0.02502  -0.02882 -0.04132 161 ASP A CA  
1047 C C   . ASP A 135 ? 0.32909 0.13461 0.36599 0.02249  -0.02866 -0.04665 161 ASP A C   
1048 O O   . ASP A 135 ? 0.33430 0.13788 0.37736 0.02013  -0.02934 -0.04692 161 ASP A O   
1049 C CB  . ASP A 135 ? 0.36760 0.17175 0.41643 0.02938  -0.02852 -0.04753 161 ASP A CB  
1050 C CG  . ASP A 135 ? 0.40621 0.20824 0.46508 0.03201  -0.03035 -0.04184 161 ASP A CG  
1051 O OD1 . ASP A 135 ? 0.42236 0.22010 0.48064 0.02994  -0.03262 -0.03253 161 ASP A OD1 
1052 O OD2 . ASP A 135 ? 0.42551 0.22948 0.49269 0.03611  -0.02957 -0.04670 161 ASP A OD2 
1053 N N   . LEU A 136 ? 0.29072 0.09953 0.31760 0.02294  -0.02853 -0.05071 162 LEU A N   
1054 C CA  . LEU A 136 ? 0.35033 0.16021 0.37239 0.02087  -0.03050 -0.05522 162 LEU A CA  
1055 C C   . LEU A 136 ? 0.36991 0.18037 0.39752 0.01665  -0.03082 -0.05007 162 LEU A C   
1056 O O   . LEU A 136 ? 0.36198 0.17296 0.39436 0.01476  -0.03343 -0.05316 162 LEU A O   
1057 C CB  . LEU A 136 ? 0.34578 0.15719 0.35419 0.02198  -0.03065 -0.05841 162 LEU A CB  
1058 C CG  . LEU A 136 ? 0.35420 0.16505 0.35497 0.02049  -0.03476 -0.06297 162 LEU A CG  
1059 C CD1 . LEU A 136 ? 0.33984 0.14691 0.33628 0.02209  -0.03675 -0.07172 162 LEU A CD1 
1060 C CD2 . LEU A 136 ? 0.34626 0.15983 0.33336 0.02031  -0.03400 -0.06138 162 LEU A CD2 
1061 N N   . ILE A 137 ? 0.36315 0.17294 0.39075 0.01504  -0.02817 -0.04274 163 ILE A N   
1062 C CA  . ILE A 137 ? 0.39122 0.20091 0.42334 0.01083  -0.02614 -0.03854 163 ILE A CA  
1063 C C   . ILE A 137 ? 0.39422 0.19786 0.43143 0.00857  -0.02274 -0.03140 163 ILE A C   
1064 O O   . ILE A 137 ? 0.41716 0.21928 0.46016 0.00461  -0.01937 -0.02862 163 ILE A O   
1065 C CB  . ILE A 137 ? 0.41757 0.22988 0.44194 0.00982  -0.02505 -0.03697 163 ILE A CB  
1066 C CG1 . ILE A 137 ? 0.44717 0.26186 0.47941 0.00618  -0.02359 -0.03673 163 ILE A CG1 
1067 C CG2 . ILE A 137 ? 0.42089 0.23302 0.43746 0.00926  -0.02134 -0.03000 163 ILE A CG2 
1068 C CD1 . ILE A 137 ? 0.45332 0.27118 0.48022 0.00548  -0.02280 -0.03625 163 ILE A CD1 
1069 N N   . LEU A 138 ? 0.38775 0.18708 0.42345 0.01084  -0.02350 -0.02813 164 LEU A N   
1070 C CA  . LEU A 138 ? 0.37727 0.16811 0.41453 0.00867  -0.02151 -0.01992 164 LEU A CA  
1071 C C   . LEU A 138 ? 0.38683 0.17395 0.43373 0.00965  -0.02267 -0.01982 164 LEU A C   
1072 O O   . LEU A 138 ? 0.37001 0.14853 0.41753 0.00804  -0.02160 -0.01223 164 LEU A O   
1073 C CB  . LEU A 138 ? 0.29969 0.08831 0.32612 0.01003  -0.02290 -0.01385 164 LEU A CB  
1074 C CG  . LEU A 138 ? 0.29419 0.08892 0.30780 0.00773  -0.01968 -0.01208 164 LEU A CG  
1075 C CD1 . LEU A 138 ? 0.29968 0.09281 0.30131 0.00794  -0.02122 -0.00523 164 LEU A CD1 
1076 C CD2 . LEU A 138 ? 0.29568 0.08827 0.31029 0.00256  -0.01362 -0.01051 164 LEU A CD2 
1077 N N   . LYS A 139 ? 0.39488 0.18674 0.44797 0.01203  -0.02504 -0.02783 165 LYS A N   
1078 C CA  . LYS A 139 ? 0.42814 0.21644 0.49167 0.01246  -0.02612 -0.02901 165 LYS A CA  
1079 C C   . LYS A 139 ? 0.39716 0.18688 0.46887 0.00878  -0.02550 -0.03228 165 LYS A C   
1080 O O   . LYS A 139 ? 0.38297 0.17882 0.45393 0.00894  -0.02769 -0.03926 165 LYS A O   
1081 C CB  . LYS A 139 ? 0.47360 0.26475 0.53925 0.01734  -0.02900 -0.03647 165 LYS A CB  
1082 C CG  . LYS A 139 ? 0.52024 0.30742 0.58981 0.02079  -0.03023 -0.03240 165 LYS A CG  
1083 C CD  . LYS A 139 ? 0.55556 0.34642 0.62839 0.02568  -0.03123 -0.04097 165 LYS A CD  
1084 C CE  . LYS A 139 ? 0.60588 0.39448 0.68788 0.02597  -0.03194 -0.04730 165 LYS A CE  
1085 N NZ  . LYS A 139 ? 0.63355 0.41595 0.72698 0.02678  -0.03322 -0.04174 165 LYS A NZ  
1086 N N   . PRO A 140 ? 0.41180 0.19564 0.49176 0.00532  -0.02308 -0.02727 166 PRO A N   
1087 C CA  . PRO A 140 ? 0.42091 0.20734 0.51226 0.00153  -0.02253 -0.03041 166 PRO A CA  
1088 C C   . PRO A 140 ? 0.42291 0.21401 0.52121 0.00346  -0.02823 -0.04034 166 PRO A C   
1089 O O   . PRO A 140 ? 0.40330 0.19953 0.50818 0.00148  -0.03050 -0.04496 166 PRO A O   
1090 C CB  . PRO A 140 ? 0.45266 0.23022 0.55164 -0.00202 -0.01855 -0.02295 166 PRO A CB  
1091 C CG  . PRO A 140 ? 0.45882 0.22835 0.54532 -0.00138 -0.01618 -0.01387 166 PRO A CG  
1092 C CD  . PRO A 140 ? 0.43149 0.20535 0.51054 0.00437  -0.02086 -0.01777 166 PRO A CD  
1093 N N   . GLU A 141 ? 0.44027 0.22924 0.53765 0.00730  -0.03094 -0.04402 167 GLU A N   
1094 C CA  . GLU A 141 ? 0.48596 0.27696 0.58756 0.00886  -0.03591 -0.05409 167 GLU A CA  
1095 C C   . GLU A 141 ? 0.46112 0.25763 0.55210 0.01012  -0.03920 -0.06088 167 GLU A C   
1096 O O   . GLU A 141 ? 0.47822 0.27616 0.57203 0.00950  -0.04433 -0.06826 167 GLU A O   
1097 C CB  . GLU A 141 ? 0.54680 0.33366 0.64935 0.01283  -0.03656 -0.05689 167 GLU A CB  
1098 C CG  . GLU A 141 ? 0.63598 0.41604 0.74794 0.01217  -0.03438 -0.04913 167 GLU A CG  
1099 C CD  . GLU A 141 ? 0.69622 0.47357 0.80056 0.01361  -0.03173 -0.04000 167 GLU A CD  
1100 O OE1 . GLU A 141 ? 0.74073 0.51844 0.84238 0.01813  -0.03271 -0.04152 167 GLU A OE1 
1101 O OE2 . GLU A 141 ? 0.73294 0.50743 0.83443 0.01014  -0.02868 -0.03157 167 GLU A OE2 
1102 N N   . ASN A 142 ? 0.43957 0.23828 0.51805 0.01178  -0.03708 -0.05839 168 ASN A N   
1103 C CA  . ASN A 142 ? 0.44297 0.24561 0.51027 0.01268  -0.04002 -0.06369 168 ASN A CA  
1104 C C   . ASN A 142 ? 0.44852 0.25534 0.51919 0.00925  -0.04104 -0.06101 168 ASN A C   
1105 O O   . ASN A 142 ? 0.31084 0.12004 0.37877 0.00906  -0.04656 -0.06629 168 ASN A O   
1106 C CB  . ASN A 142 ? 0.42436 0.22767 0.47856 0.01592  -0.03719 -0.06265 168 ASN A CB  
1107 C CG  . ASN A 142 ? 0.41790 0.21831 0.47046 0.01986  -0.03614 -0.06745 168 ASN A CG  
1108 O OD1 . ASN A 142 ? 0.43033 0.22824 0.48376 0.02065  -0.03846 -0.07520 168 ASN A OD1 
1109 N ND2 . ASN A 142 ? 0.37751 0.17807 0.42869 0.02238  -0.03282 -0.06330 168 ASN A ND2 
1110 N N   . LEU A 143 ? 0.44900 0.25580 0.52543 0.00656  -0.03594 -0.05305 169 LEU A N   
1111 C CA  . LEU A 143 ? 0.44080 0.25178 0.52361 0.00324  -0.03534 -0.05108 169 LEU A CA  
1112 C C   . LEU A 143 ? 0.45642 0.26960 0.55596 0.00087  -0.03967 -0.05516 169 LEU A C   
1113 O O   . LEU A 143 ? 0.46540 0.28367 0.57150 -0.00046 -0.04313 -0.05718 169 LEU A O   
1114 C CB  . LEU A 143 ? 0.39574 0.20420 0.47966 0.00048  -0.02740 -0.04238 169 LEU A CB  
1115 C CG  . LEU A 143 ? 0.33593 0.14807 0.41514 -0.00074 -0.02469 -0.04015 169 LEU A CG  
1116 C CD1 . LEU A 143 ? 0.30429 0.11812 0.36786 0.00293  -0.02758 -0.04234 169 LEU A CD1 
1117 C CD2 . LEU A 143 ? 0.31528 0.12247 0.39347 -0.00395 -0.01619 -0.03226 169 LEU A CD2 
1118 N N   . GLU A 144 ? 0.47425 0.28381 0.58266 0.00050  -0.04031 -0.05654 170 GLU A N   
1119 C CA  . GLU A 144 ? 0.48148 0.29324 0.60714 -0.00158 -0.04557 -0.06136 170 GLU A CA  
1120 C C   . GLU A 144 ? 0.45724 0.27118 0.57760 0.00053  -0.05571 -0.07015 170 GLU A C   
1121 O O   . GLU A 144 ? 0.45991 0.27814 0.59246 -0.00104 -0.06194 -0.07327 170 GLU A O   
1122 C CB  . GLU A 144 ? 0.53585 0.34229 0.67079 -0.00208 -0.04460 -0.06157 170 GLU A CB  
1123 C CG  . GLU A 144 ? 0.58567 0.38844 0.72952 -0.00547 -0.03612 -0.05274 170 GLU A CG  
1124 C CD  . GLU A 144 ? 0.62797 0.42293 0.77269 -0.00444 -0.03459 -0.05073 170 GLU A CD  
1125 O OE1 . GLU A 144 ? 0.63997 0.43375 0.78405 -0.00160 -0.04002 -0.05767 170 GLU A OE1 
1126 O OE2 . GLU A 144 ? 0.64243 0.43143 0.78789 -0.00650 -0.02804 -0.04222 170 GLU A OE2 
1127 N N   . LYS A 145 ? 0.45091 0.26121 0.55324 0.00409  -0.05767 -0.07431 171 LYS A N   
1128 C CA  . LYS A 145 ? 0.46157 0.27090 0.55326 0.00590  -0.06683 -0.08259 171 LYS A CA  
1129 C C   . LYS A 145 ? 0.46083 0.27337 0.54301 0.00628  -0.06954 -0.08110 171 LYS A C   
1130 O O   . LYS A 145 ? 0.46566 0.27724 0.54250 0.00686  -0.07926 -0.08652 171 LYS A O   
1131 C CB  . LYS A 145 ? 0.47657 0.27981 0.55157 0.00926  -0.06595 -0.08811 171 LYS A CB  
1132 C CG  . LYS A 145 ? 0.51010 0.30944 0.59500 0.00944  -0.06372 -0.09011 171 LYS A CG  
1133 C CD  . LYS A 145 ? 0.54494 0.33898 0.61557 0.01310  -0.06067 -0.09527 171 LYS A CD  
1134 C CE  . LYS A 145 ? 0.58145 0.37135 0.66401 0.01357  -0.05879 -0.09716 171 LYS A CE  
1135 N NZ  . LYS A 145 ? 0.60391 0.39520 0.70168 0.01196  -0.05372 -0.08719 171 LYS A NZ  
1136 N N   . LEU A 146 ? 0.44985 0.26503 0.52901 0.00601  -0.06198 -0.07388 172 LEU A N   
1137 C CA  . LEU A 146 ? 0.44756 0.26562 0.51942 0.00628  -0.06388 -0.07200 172 LEU A CA  
1138 C C   . LEU A 146 ? 0.45039 0.27461 0.54148 0.00338  -0.06464 -0.06884 172 LEU A C   
1139 O O   . LEU A 146 ? 0.44844 0.27514 0.53716 0.00372  -0.06815 -0.06814 172 LEU A O   
1140 C CB  . LEU A 146 ? 0.43022 0.24788 0.48902 0.00759  -0.05558 -0.06669 172 LEU A CB  
1141 C CG  . LEU A 146 ? 0.42770 0.24083 0.46670 0.01104  -0.05524 -0.07029 172 LEU A CG  
1142 C CD1 . LEU A 146 ? 0.39511 0.20887 0.42785 0.01210  -0.04711 -0.06447 172 LEU A CD1 
1143 C CD2 . LEU A 146 ? 0.42952 0.24013 0.45324 0.01235  -0.06287 -0.07503 172 LEU A CD2 
1144 N N   . LYS A 147 ? 0.45314 0.27956 0.56407 0.00056  -0.06098 -0.06697 173 LYS A N   
1145 C CA  . LYS A 147 ? 0.46065 0.29342 0.59217 -0.00239 -0.05887 -0.06410 173 LYS A CA  
1146 C C   . LYS A 147 ? 0.46769 0.30462 0.60884 -0.00173 -0.07091 -0.06883 173 LYS A C   
1147 O O   . LYS A 147 ? 0.46519 0.30756 0.61678 -0.00251 -0.07037 -0.06667 173 LYS A O   
1148 C CB  . LYS A 147 ? 0.49608 0.32928 0.64739 -0.00565 -0.05336 -0.06233 173 LYS A CB  
1149 C CG  . LYS A 147 ? 0.50234 0.34236 0.67780 -0.00903 -0.04909 -0.06004 173 LYS A CG  
1150 C CD  . LYS A 147 ? 0.51721 0.35807 0.71567 -0.01209 -0.04718 -0.06064 173 LYS A CD  
1151 C CE  . LYS A 147 ? 0.52882 0.37760 0.75469 -0.01531 -0.04232 -0.05943 173 LYS A CE  
1152 N NZ  . LYS A 147 ? 0.52024 0.37666 0.75686 -0.01339 -0.05271 -0.06383 173 LYS A NZ  
1153 N N   . SER A 148 ? 0.46503 0.29865 0.60286 -0.00014 -0.08244 -0.07550 174 SER A N   
1154 C CA  . SER A 148 ? 0.47335 0.30935 0.62158 0.00054  -0.09644 -0.07989 174 SER A CA  
1155 C C   . SER A 148 ? 0.46700 0.30173 0.60016 0.00269  -0.10175 -0.07870 174 SER A C   
1156 O O   . SER A 148 ? 0.48553 0.32464 0.63360 0.00280  -0.10941 -0.07861 174 SER A O   
1157 C CB  . SER A 148 ? 0.50089 0.33105 0.64399 0.00177  -0.10818 -0.08766 174 SER A CB  
1158 O OG  . SER A 148 ? 0.53025 0.35215 0.64377 0.00461  -0.11524 -0.09118 174 SER A OG  
1159 N N   . CYS A 149 ? 0.44212 0.27081 0.54764 0.00454  -0.09796 -0.07768 175 CYS A N   
1160 C CA  A CYS A 149 ? 0.45117 0.27698 0.54051 0.00643  -0.10281 -0.07626 175 CYS A CA  
1161 C CA  B CYS A 149 ? 0.45103 0.27669 0.53972 0.00645  -0.10254 -0.07625 175 CYS A CA  
1162 C C   . CYS A 149 ? 0.41398 0.24535 0.50857 0.00552  -0.09202 -0.06946 175 CYS A C   
1163 O O   . CYS A 149 ? 0.40913 0.23858 0.49347 0.00689  -0.09536 -0.06762 175 CYS A O   
1164 C CB  A CYS A 149 ? 0.46872 0.28462 0.52515 0.00880  -0.10411 -0.07916 175 CYS A CB  
1165 C CB  B CYS A 149 ? 0.46750 0.28366 0.52395 0.00873  -0.10260 -0.07892 175 CYS A CB  
1166 S SG  A CYS A 149 ? 0.46553 0.28046 0.50941 0.00927  -0.08813 -0.07698 175 CYS A SG  
1167 S SG  B CYS A 149 ? 0.51011 0.31626 0.55011 0.01017  -0.11740 -0.08808 175 CYS A SG  
1168 N N   . GLY A 150 ? 0.39655 0.23327 0.50534 0.00312  -0.07948 -0.06575 176 GLY A N   
1169 C CA  . GLY A 150 ? 0.36326 0.20441 0.47712 0.00185  -0.06923 -0.06021 176 GLY A CA  
1170 C C   . GLY A 150 ? 0.34652 0.18438 0.44214 0.00200  -0.05799 -0.05610 176 GLY A C   
1171 O O   . GLY A 150 ? 0.33431 0.16759 0.40885 0.00437  -0.05993 -0.05640 176 GLY A O   
1172 N N   . VAL A 151 ? 0.32908 0.16834 0.43262 -0.00059 -0.04660 -0.05222 177 VAL A N   
1173 C CA  . VAL A 151 ? 0.32363 0.15901 0.41204 -0.00067 -0.03711 -0.04782 177 VAL A CA  
1174 C C   . VAL A 151 ? 0.32702 0.16488 0.42207 -0.00311 -0.02808 -0.04403 177 VAL A C   
1175 O O   . VAL A 151 ? 0.34417 0.18559 0.45831 -0.00592 -0.02385 -0.04377 177 VAL A O   
1176 C CB  . VAL A 151 ? 0.33487 0.16577 0.42245 -0.00158 -0.03258 -0.04634 177 VAL A CB  
1177 C CG1 . VAL A 151 ? 0.32494 0.15085 0.39644 -0.00093 -0.02595 -0.04186 177 VAL A CG1 
1178 C CG2 . VAL A 151 ? 0.32657 0.15557 0.41194 0.00051  -0.04088 -0.05151 177 VAL A CG2 
1179 N N   . SER A 152 ? 0.30290 0.13880 0.38314 -0.00218 -0.02463 -0.04168 178 SER A N   
1180 C CA  . SER A 152 ? 0.33133 0.16813 0.41480 -0.00452 -0.01550 -0.03894 178 SER A CA  
1181 C C   . SER A 152 ? 0.32628 0.15662 0.39217 -0.00487 -0.00910 -0.03528 178 SER A C   
1182 O O   . SER A 152 ? 0.33981 0.16749 0.39119 -0.00215 -0.01346 -0.03523 178 SER A O   
1183 C CB  . SER A 152 ? 0.35806 0.19950 0.44498 -0.00320 -0.01909 -0.04039 178 SER A CB  
1184 O OG  . SER A 152 ? 0.38592 0.22443 0.45404 -0.00091 -0.02145 -0.03953 178 SER A OG  
1185 N N   . PHE A 153 ? 0.29197 0.11942 0.35985 -0.00841 0.00141  -0.03247 179 PHE A N   
1186 C CA  . PHE A 153 ? 0.26418 0.08637 0.31350 -0.00942 0.00749  -0.02824 179 PHE A CA  
1187 C C   . PHE A 153 ? 0.29186 0.11646 0.33761 -0.01108 0.01420  -0.02835 179 PHE A C   
1188 O O   . PHE A 153 ? 0.26223 0.08933 0.32512 -0.01265 0.01819  -0.03133 179 PHE A O   
1189 C CB  . PHE A 153 ? 0.28101 0.09568 0.32815 -0.01279 0.01472  -0.02370 179 PHE A CB  
1190 C CG  . PHE A 153 ? 0.29524 0.10586 0.33810 -0.01061 0.00846  -0.02197 179 PHE A CG  
1191 C CD1 . PHE A 153 ? 0.29749 0.11085 0.34722 -0.00696 -0.00122 -0.02663 179 PHE A CD1 
1192 C CD2 . PHE A 153 ? 0.32249 0.12534 0.35378 -0.01222 0.01211  -0.01580 179 PHE A CD2 
1193 C CE1 . PHE A 153 ? 0.30609 0.11563 0.35312 -0.00482 -0.00587 -0.02616 179 PHE A CE1 
1194 C CE2 . PHE A 153 ? 0.31405 0.11284 0.34446 -0.00981 0.00617  -0.01434 179 PHE A CE2 
1195 C CZ  . PHE A 153 ? 0.30436 0.10676 0.34389 -0.00603 -0.00221 -0.02009 179 PHE A CZ  
1196 N N   . LEU A 154 ? 0.29638 0.12021 0.32189 -0.01065 0.01511  -0.02571 180 LEU A N   
1197 C CA  . LEU A 154 ? 0.29959 0.12393 0.31946 -0.01273 0.02217  -0.02625 180 LEU A CA  
1198 C C   . LEU A 154 ? 0.32340 0.14193 0.34433 -0.01769 0.03471  -0.02502 180 LEU A C   
1199 O O   . LEU A 154 ? 0.31314 0.12540 0.32952 -0.01973 0.03765  -0.02119 180 LEU A O   
1200 C CB  . LEU A 154 ? 0.27923 0.10308 0.27738 -0.01174 0.01967  -0.02389 180 LEU A CB  
1201 C CG  . LEU A 154 ? 0.27167 0.10103 0.26669 -0.00776 0.01057  -0.02501 180 LEU A CG  
1202 C CD1 . LEU A 154 ? 0.28052 0.10911 0.25760 -0.00760 0.00914  -0.02247 180 LEU A CD1 
1203 C CD2 . LEU A 154 ? 0.25782 0.09156 0.26322 -0.00699 0.00981  -0.02852 180 LEU A CD2 
1204 N N   . ASP A 155 ? 0.32441 0.14417 0.35149 -0.01980 0.04290  -0.02830 181 ASP A N   
1205 C CA  . ASP A 155 ? 0.35809 0.17122 0.38098 -0.02506 0.05748  -0.02777 181 ASP A CA  
1206 C C   . ASP A 155 ? 0.37186 0.17873 0.36492 -0.02691 0.06062  -0.02540 181 ASP A C   
1207 O O   . ASP A 155 ? 0.38412 0.18827 0.37118 -0.02982 0.07035  -0.02838 181 ASP A O   
1208 C CB  . ASP A 155 ? 0.36792 0.18509 0.41470 -0.02651 0.06616  -0.03368 181 ASP A CB  
1209 C CG  . ASP A 155 ? 0.37656 0.18695 0.42472 -0.03241 0.08356  -0.03382 181 ASP A CG  
1210 O OD1 . ASP A 155 ? 0.37343 0.17606 0.40939 -0.03531 0.08726  -0.02852 181 ASP A OD1 
1211 O OD2 . ASP A 155 ? 0.37524 0.18732 0.43683 -0.03427 0.09416  -0.03916 181 ASP A OD2 
1212 N N   . ALA A 156 ? 0.36555 0.16988 0.34065 -0.02510 0.05163  -0.02061 182 ALA A N   
1213 C CA  . ALA A 156 ? 0.35294 0.15158 0.30066 -0.02630 0.05049  -0.01804 182 ALA A CA  
1214 C C   . ALA A 156 ? 0.34159 0.13078 0.27324 -0.02778 0.04882  -0.01081 182 ALA A C   
1215 O O   . ALA A 156 ? 0.35077 0.14159 0.28146 -0.02426 0.03799  -0.00760 182 ALA A O   
1216 C CB  . ALA A 156 ? 0.33203 0.13784 0.27715 -0.02207 0.03913  -0.01939 182 ALA A CB  
1217 N N   . PRO A 157 ? 0.36084 0.13913 0.27963 -0.03304 0.05984  -0.00797 183 PRO A N   
1218 C CA  . PRO A 157 ? 0.38180 0.14904 0.28543 -0.03470 0.05799  0.00028  183 PRO A CA  
1219 C C   . PRO A 157 ? 0.41500 0.17854 0.29684 -0.03256 0.04557  0.00479  183 PRO A C   
1220 O O   . PRO A 157 ? 0.43348 0.19363 0.31443 -0.03048 0.03733  0.01058  183 PRO A O   
1221 C CB  . PRO A 157 ? 0.39961 0.15461 0.28900 -0.04162 0.07416  0.00197  183 PRO A CB  
1222 C CG  . PRO A 157 ? 0.40316 0.16204 0.29195 -0.04312 0.08229  -0.00587 183 PRO A CG  
1223 C CD  . PRO A 157 ? 0.37446 0.14899 0.29210 -0.03788 0.07534  -0.01207 183 PRO A CD  
1224 N N   . GLU A 158 ? 0.41690 0.18103 0.28356 -0.03293 0.04351  0.00188  184 GLU A N   
1225 C CA  A GLU A 158 ? 0.45304 0.21411 0.30169 -0.03115 0.03073  0.00567  184 GLU A CA  
1226 C CA  B GLU A 158 ? 0.45298 0.21401 0.30162 -0.03116 0.03074  0.00570  184 GLU A CA  
1227 C C   . GLU A 158 ? 0.41469 0.18689 0.28191 -0.02488 0.01816  0.00547  184 GLU A C   
1228 O O   . GLU A 158 ? 0.40094 0.16973 0.26499 -0.02266 0.00882  0.01102  184 GLU A O   
1229 C CB  A GLU A 158 ? 0.47422 0.23475 0.30681 -0.03302 0.03096  0.00097  184 GLU A CB  
1230 C CB  B GLU A 158 ? 0.47469 0.23498 0.30692 -0.03309 0.03104  0.00107  184 GLU A CB  
1231 C CG  A GLU A 158 ? 0.52700 0.27372 0.33427 -0.03953 0.04301  0.00085  184 GLU A CG  
1232 C CG  B GLU A 158 ? 0.53228 0.28118 0.34524 -0.03945 0.04551  -0.00063 184 GLU A CG  
1233 C CD  A GLU A 158 ? 0.53316 0.28291 0.35505 -0.04208 0.05960  -0.00553 184 GLU A CD  
1234 C CD  B GLU A 158 ? 0.54263 0.28909 0.33736 -0.04149 0.04506  -0.00608 184 GLU A CD  
1235 O OE1 A GLU A 158 ? 0.56362 0.30182 0.36958 -0.04767 0.07315  -0.00522 184 GLU A OE1 
1236 O OE1 B GLU A 158 ? 0.53736 0.29401 0.34215 -0.03796 0.03573  -0.00989 184 GLU A OE1 
1237 O OE2 A GLU A 158 ? 0.53467 0.29777 0.38420 -0.03856 0.05916  -0.01077 184 GLU A OE2 
1238 O OE2 B GLU A 158 ? 0.59163 0.32519 0.36143 -0.04699 0.05464  -0.00684 184 GLU A OE2 
1239 N N   . GLU A 159 ? 0.39210 0.17684 0.27880 -0.02201 0.01815  -0.00089 185 GLU A N   
1240 C CA  . GLU A 159 ? 0.38272 0.17724 0.28456 -0.01658 0.00832  -0.00187 185 GLU A CA  
1241 C C   . GLU A 159 ? 0.38285 0.17646 0.29735 -0.01442 0.00652  0.00084  185 GLU A C   
1242 O O   . GLU A 159 ? 0.38776 0.18270 0.30567 -0.01083 -0.00206 0.00303  185 GLU A O   
1243 C CB  . GLU A 159 ? 0.38040 0.18583 0.29669 -0.01475 0.00962  -0.00845 185 GLU A CB  
1244 C CG  . GLU A 159 ? 0.42844 0.23384 0.33580 -0.01742 0.01366  -0.01208 185 GLU A CG  
1245 C CD  . GLU A 159 ? 0.43981 0.25520 0.35892 -0.01479 0.01060  -0.01662 185 GLU A CD  
1246 O OE1 . GLU A 159 ? 0.42349 0.24532 0.35452 -0.01106 0.00543  -0.01666 185 GLU A OE1 
1247 O OE2 . GLU A 159 ? 0.44478 0.26048 0.36020 -0.01666 0.01376  -0.02018 185 GLU A OE2 
1248 N N   . VAL A 160 ? 0.36590 0.15732 0.28980 -0.01657 0.01464  0.00009  186 VAL A N   
1249 C CA  . VAL A 160 ? 0.36607 0.15618 0.30369 -0.01489 0.01275  0.00176  186 VAL A CA  
1250 C C   . VAL A 160 ? 0.37730 0.15622 0.30294 -0.01568 0.00952  0.00960  186 VAL A C   
1251 O O   . VAL A 160 ? 0.33435 0.11322 0.26831 -0.01214 0.00235  0.01127  186 VAL A O   
1252 C CB  . VAL A 160 ? 0.38061 0.17081 0.33353 -0.01763 0.02186  -0.00098 186 VAL A CB  
1253 C CG1 . VAL A 160 ? 0.35452 0.14160 0.32118 -0.01669 0.01975  0.00075  186 VAL A CG1 
1254 C CG2 . VAL A 160 ? 0.38771 0.18868 0.35505 -0.01582 0.02177  -0.00820 186 VAL A CG2 
1255 N N   . PHE A 161 ? 0.38240 0.15056 0.28743 -0.02030 0.01456  0.01451  187 PHE A N   
1256 C CA  . PHE A 161 ? 0.38757 0.14265 0.27804 -0.02138 0.01043  0.02339  187 PHE A CA  
1257 C C   . PHE A 161 ? 0.41057 0.16755 0.29618 -0.01693 -0.00363 0.02553  187 PHE A C   
1258 O O   . PHE A 161 ? 0.42497 0.17649 0.31350 -0.01452 -0.01116 0.03093  187 PHE A O   
1259 C CB  . PHE A 161 ? 0.40799 0.14937 0.27272 -0.02791 0.01937  0.02810  187 PHE A CB  
1260 C CG  . PHE A 161 ? 0.43756 0.16987 0.30577 -0.03258 0.03147  0.03154  187 PHE A CG  
1261 C CD1 . PHE A 161 ? 0.45348 0.17629 0.32424 -0.03248 0.02830  0.03912  187 PHE A CD1 
1262 C CD2 . PHE A 161 ? 0.46819 0.20146 0.33989 -0.03713 0.04645  0.02700  187 PHE A CD2 
1263 C CE1 . PHE A 161 ? 0.44737 0.16152 0.32318 -0.03734 0.04014  0.04250  187 PHE A CE1 
1264 C CE2 . PHE A 161 ? 0.46657 0.19215 0.34489 -0.04186 0.05876  0.02986  187 PHE A CE2 
1265 C CZ  . PHE A 161 ? 0.44986 0.16577 0.32984 -0.04221 0.05573  0.03781  187 PHE A CZ  
1266 N N   . ALA A 162 ? 0.39847 0.16317 0.27946 -0.01575 -0.00738 0.02119  188 ALA A N   
1267 C CA  . ALA A 162 ? 0.39233 0.16092 0.27449 -0.01150 -0.02037 0.02220  188 ALA A CA  
1268 C C   . ALA A 162 ? 0.38583 0.16408 0.29274 -0.00582 -0.02482 0.01899  188 ALA A C   
1269 O O   . ALA A 162 ? 0.37277 0.14968 0.28549 -0.00221 -0.03401 0.02219  188 ALA A O   
1270 C CB  . ALA A 162 ? 0.37173 0.14723 0.24718 -0.01199 -0.02225 0.01738  188 ALA A CB  
1271 N N   . THR A 163 ? 0.38408 0.17129 0.30560 -0.00492 -0.01865 0.01240  189 THR A N   
1272 C CA  . THR A 163 ? 0.36968 0.16425 0.31091 -0.00010 -0.02175 0.00842  189 THR A CA  
1273 C C   . THR A 163 ? 0.40490 0.19126 0.35314 0.00097  -0.02355 0.01247  189 THR A C   
1274 O O   . THR A 163 ? 0.32178 0.10984 0.28129 0.00543  -0.02988 0.01195  189 THR A O   
1275 C CB  . THR A 163 ? 0.33394 0.13663 0.28522 -0.00014 -0.01573 0.00139  189 THR A CB  
1276 O OG1 . THR A 163 ? 0.32436 0.13343 0.26982 -0.00116 -0.01420 -0.00168 189 THR A OG1 
1277 C CG2 . THR A 163 ? 0.29033 0.09913 0.25705 0.00447  -0.01898 -0.00346 189 THR A CG2 
1278 N N   . VAL A 164 ? 0.33557 0.11254 0.27863 -0.00324 -0.01729 0.01636  190 VAL A N   
1279 C CA  . VAL A 164 ? 0.34468 0.11247 0.29519 -0.00291 -0.01837 0.02076  190 VAL A CA  
1280 C C   . VAL A 164 ? 0.41598 0.17441 0.35755 -0.00147 -0.02724 0.02899  190 VAL A C   
1281 O O   . VAL A 164 ? 0.41460 0.17016 0.36885 0.00224  -0.03316 0.03050  190 VAL A O   
1282 C CB  . VAL A 164 ? 0.35397 0.11380 0.30221 -0.00861 -0.00807 0.02326  190 VAL A CB  
1283 C CG1 . VAL A 164 ? 0.36852 0.11585 0.32107 -0.00935 -0.00907 0.03004  190 VAL A CG1 
1284 C CG2 . VAL A 164 ? 0.33711 0.10648 0.30180 -0.00887 -0.00229 0.01476  190 VAL A CG2 
1285 N N   . LEU A 165 ? 0.41868 0.17152 0.33866 -0.00424 -0.02914 0.03412  191 LEU A N   
1286 C CA  . LEU A 165 ? 0.43138 0.17444 0.34149 -0.00288 -0.04011 0.04245  191 LEU A CA  
1287 C C   . LEU A 165 ? 0.43060 0.18367 0.35826 0.00380  -0.05085 0.03886  191 LEU A C   
1288 O O   . LEU A 165 ? 0.43087 0.17815 0.36645 0.00726  -0.05989 0.04372  191 LEU A O   
1289 C CB  . LEU A 165 ? 0.43664 0.17187 0.31785 -0.00742 -0.04098 0.04710  191 LEU A CB  
1290 C CG  . LEU A 165 ? 0.46443 0.18403 0.32285 -0.01441 -0.03127 0.05362  191 LEU A CG  
1291 C CD1 . LEU A 165 ? 0.49830 0.20986 0.32545 -0.01857 -0.03292 0.05655  191 LEU A CD1 
1292 C CD2 . LEU A 165 ? 0.47403 0.17853 0.33200 -0.01476 -0.03407 0.06345  191 LEU A CD2 
1293 N N   . ASN A 166 ? 0.42496 0.19262 0.36021 0.00562  -0.04946 0.03047  192 ASN A N   
1294 C CA  . ASN A 166 ? 0.43710 0.21514 0.39139 0.01151  -0.05663 0.02603  192 ASN A CA  
1295 C C   . ASN A 166 ? 0.42487 0.20491 0.40072 0.01562  -0.05508 0.02218  192 ASN A C   
1296 O O   . ASN A 166 ? 0.42275 0.20389 0.41423 0.02052  -0.06214 0.02211  192 ASN A O   
1297 C CB  . ASN A 166 ? 0.44414 0.23597 0.40052 0.01162  -0.05333 0.01833  192 ASN A CB  
1298 C CG  . ASN A 166 ? 0.43899 0.24174 0.41552 0.01698  -0.05815 0.01339  192 ASN A CG  
1299 O OD1 . ASN A 166 ? 0.43690 0.23992 0.41745 0.01898  -0.06762 0.01624  192 ASN A OD1 
1300 N ND2 . ASN A 166 ? 0.41514 0.22645 0.40458 0.01917  -0.05162 0.00578  192 ASN A ND2 
1301 N N   . TYR A 167 ? 0.41838 0.19871 0.39670 0.01372  -0.04625 0.01829  193 TYR A N   
1302 C CA  . TYR A 167 ? 0.41430 0.19514 0.41117 0.01706  -0.04508 0.01358  193 TYR A CA  
1303 C C   . TYR A 167 ? 0.41768 0.18581 0.42000 0.01823  -0.05038 0.02070  193 TYR A C   
1304 O O   . TYR A 167 ? 0.38397 0.15248 0.40456 0.02288  -0.05342 0.01728  193 TYR A O   
1305 C CB  . TYR A 167 ? 0.41022 0.19268 0.40795 0.01410  -0.03646 0.00849  193 TYR A CB  
1306 C CG  . TYR A 167 ? 0.41403 0.19565 0.42882 0.01677  -0.03585 0.00272  193 TYR A CG  
1307 C CD1 . TYR A 167 ? 0.42958 0.21967 0.45503 0.02121  -0.03649 -0.00621 193 TYR A CD1 
1308 C CD2 . TYR A 167 ? 0.43505 0.20654 0.45466 0.01443  -0.03402 0.00579  193 TYR A CD2 
1309 C CE1 . TYR A 167 ? 0.45490 0.24293 0.49350 0.02345  -0.03604 -0.01266 193 TYR A CE1 
1310 C CE2 . TYR A 167 ? 0.46900 0.24074 0.50414 0.01653  -0.03365 -0.00039 193 TYR A CE2 
1311 C CZ  . TYR A 167 ? 0.48239 0.26391 0.52524 0.02092  -0.03443 -0.00979 193 TYR A CZ  
1312 O OH  . TYR A 167 ? 0.51554 0.29961 0.56899 0.02232  -0.03306 -0.01643 193 TYR A OH  
1313 N N   . LEU A 168 ? 0.45805 0.21374 0.44417 0.01397  -0.05109 0.03055  194 LEU A N   
1314 C CA  . LEU A 168 ? 0.48686 0.22792 0.47532 0.01443  -0.05641 0.03931  194 LEU A CA  
1315 C C   . LEU A 168 ? 0.51322 0.25073 0.50221 0.01832  -0.06936 0.04539  194 LEU A C   
1316 O O   . LEU A 168 ? 0.55328 0.27774 0.54184 0.01871  -0.07552 0.05435  194 LEU A O   
1317 C CB  . LEU A 168 ? 0.51106 0.23825 0.47986 0.00746  -0.05031 0.04802  194 LEU A CB  
1318 C CG  . LEU A 168 ? 0.51684 0.24599 0.49047 0.00339  -0.03802 0.04298  194 LEU A CG  
1319 C CD1 . LEU A 168 ? 0.53845 0.25281 0.49525 -0.00368 -0.03068 0.05220  194 LEU A CD1 
1320 C CD2 . LEU A 168 ? 0.50067 0.23214 0.49978 0.00692  -0.03823 0.03653  194 LEU A CD2 
1321 N N   . GLY A 169 ? 0.50618 0.25551 0.49770 0.02105  -0.07378 0.04088  195 GLY A N   
1322 C CA  . GLY A 169 ? 0.54030 0.28809 0.53675 0.02491  -0.08719 0.04561  195 GLY A CA  
1323 C C   . GLY A 169 ? 0.58111 0.31796 0.55084 0.02093  -0.09481 0.05583  195 GLY A C   
1324 O O   . GLY A 169 ? 0.60663 0.34100 0.57971 0.02396  -0.10850 0.06050  195 GLY A O   
1325 N N   . LYS A 170 ? 0.57861 0.30840 0.52227 0.01423  -0.08664 0.05899  196 LYS A N   
1326 C CA  . LYS A 170 ? 0.58549 0.30276 0.49867 0.00967  -0.09236 0.06793  196 LYS A CA  
1327 C C   . LYS A 170 ? 0.57102 0.29944 0.47621 0.00881  -0.09421 0.06209  196 LYS A C   
1328 O O   . LYS A 170 ? 0.55731 0.30273 0.48070 0.01151  -0.09036 0.05214  196 LYS A O   
1329 C CB  . LYS A 170 ? 0.58174 0.28550 0.47089 0.00248  -0.08056 0.07326  196 LYS A CB  
1330 C CG  . LYS A 170 ? 0.57923 0.27812 0.48359 0.00251  -0.07282 0.07423  196 LYS A CG  
1331 C CD  . LYS A 170 ? 0.61213 0.29235 0.51325 0.00322  -0.08209 0.08662  196 LYS A CD  
1332 C CE  . LYS A 170 ? 0.65189 0.31549 0.52774 -0.00445 -0.07236 0.09572  196 LYS A CE  
1333 N NZ  . LYS A 170 ? 0.68692 0.34053 0.56256 -0.00376 -0.07833 0.10630  196 LYS A NZ  
1334 N N   . ASP A 171 ? 0.58113 0.29860 0.45753 0.00468  -0.10020 0.06839  197 ASP A N   
1335 C CA  . ASP A 171 ? 0.56607 0.29166 0.43193 0.00278  -0.10164 0.06284  197 ASP A CA  
1336 C C   . ASP A 171 ? 0.52421 0.25765 0.38549 -0.00112 -0.08424 0.05490  197 ASP A C   
1337 O O   . ASP A 171 ? 0.51733 0.24027 0.35960 -0.00633 -0.07373 0.05799  197 ASP A O   
1338 C CB  . ASP A 171 ? 0.60953 0.31843 0.44134 -0.00144 -0.11191 0.07118  197 ASP A CB  
1339 C CG  . ASP A 171 ? 0.63112 0.34757 0.45421 -0.00300 -0.11665 0.06506  197 ASP A CG  
1340 O OD1 . ASP A 171 ? 0.61065 0.34540 0.45547 -0.00076 -0.11181 0.05521  197 ASP A OD1 
1341 O OD2 . ASP A 171 ? 0.67763 0.38048 0.47084 -0.00676 -0.12551 0.07021  197 ASP A OD2 
1342 N N   . PRO A 172 ? 0.50446 0.25553 0.38369 0.00112  -0.08041 0.04500  198 PRO A N   
1343 C CA  . PRO A 172 ? 0.48510 0.24301 0.36173 -0.00214 -0.06541 0.03795  198 PRO A CA  
1344 C C   . PRO A 172 ? 0.49118 0.23953 0.33774 -0.00871 -0.05971 0.03931  198 PRO A C   
1345 O O   . PRO A 172 ? 0.47189 0.22057 0.31468 -0.01211 -0.04604 0.03602  198 PRO A O   
1346 C CB  . PRO A 172 ? 0.47412 0.24979 0.37063 0.00128  -0.06641 0.02915  198 PRO A CB  
1347 C CG  . PRO A 172 ? 0.47139 0.25150 0.38977 0.00719  -0.07693 0.03020  198 PRO A CG  
1348 C CD  . PRO A 172 ? 0.49214 0.25724 0.39707 0.00679  -0.08889 0.04005  198 PRO A CD  
1349 N N   . ASN A 173 ? 0.51248 0.25192 0.33802 -0.01061 -0.06998 0.04347  199 ASN A N   
1350 C CA  . ASN A 173 ? 0.54628 0.27311 0.33852 -0.01726 -0.06438 0.04492  199 ASN A CA  
1351 C C   . ASN A 173 ? 0.56105 0.26683 0.32638 -0.01988 -0.07189 0.05630  199 ASN A C   
1352 O O   . ASN A 173 ? 0.60026 0.29568 0.33965 -0.02253 -0.08140 0.05913  199 ASN A O   
1353 C CB  . ASN A 173 ? 0.55826 0.29072 0.34284 -0.01848 -0.06944 0.03864  199 ASN A CB  
1354 C CG  . ASN A 173 ? 0.55964 0.31089 0.36848 -0.01640 -0.06199 0.02853  199 ASN A CG  
1355 O OD1 . ASN A 173 ? 0.58023 0.33363 0.38632 -0.01932 -0.04827 0.02352  199 ASN A OD1 
1356 N ND2 . ASN A 173 ? 0.54525 0.30963 0.37861 -0.01142 -0.07086 0.02568  199 ASN A ND2 
1357 N N   . SER A 174 ? 0.53889 0.23720 0.30956 -0.01931 -0.06848 0.06302  200 SER A N   
1358 C CA  . SER A 174 ? 0.56481 0.24124 0.30987 -0.02197 -0.07504 0.07534  200 SER A CA  
1359 C C   . SER A 174 ? 0.60780 0.26789 0.31180 -0.03010 -0.06572 0.07758  200 SER A C   
1360 O O   . SER A 174 ? 0.57671 0.24093 0.27833 -0.03395 -0.04827 0.07088  200 SER A O   
1361 C CB  . SER A 174 ? 0.55552 0.22695 0.31569 -0.02076 -0.06958 0.08123  200 SER A CB  
1362 O OG  . SER A 174 ? 0.60529 0.25310 0.33684 -0.02496 -0.07172 0.09386  200 SER A OG  
1363 N N   . THR A 175 ? 0.65273 0.29352 0.32410 -0.03267 -0.07773 0.08679  201 THR A N   
1364 C CA  . THR A 175 ? 0.70713 0.32828 0.33327 -0.04085 -0.06944 0.08993  201 THR A CA  
1365 C C   . THR A 175 ? 0.76008 0.35965 0.36562 -0.04540 -0.06147 0.10214  201 THR A C   
1366 O O   . THR A 175 ? 0.72111 0.30023 0.28445 -0.05264 -0.05487 0.10697  201 THR A O   
1367 C CB  . THR A 175 ? 0.73149 0.34250 0.32814 -0.04188 -0.08806 0.09185  201 THR A CB  
1368 O OG1 . THR A 175 ? 0.73870 0.34245 0.33982 -0.03734 -0.11004 0.10221  201 THR A OG1 
1369 C CG2 . THR A 175 ? 0.68068 0.31176 0.29535 -0.03913 -0.09240 0.07891  201 THR A CG2 
1370 N N   . LYS A 176 ? 0.74988 0.35262 0.38358 -0.04165 -0.06131 0.10699  202 LYS A N   
1371 C CA  . LYS A 176 ? 0.75913 0.34599 0.38261 -0.04544 -0.05303 0.11751  202 LYS A CA  
1372 C C   . LYS A 176 ? 0.70488 0.29563 0.34240 -0.04916 -0.02892 0.11277  202 LYS A C   
1373 O O   . LYS A 176 ? 0.66698 0.27835 0.34446 -0.04430 -0.02577 0.10428  202 LYS A O   
1374 C CB  . LYS A 176 ? 0.77344 0.36380 0.42403 -0.03881 -0.06796 0.12441  202 LYS A CB  
1375 C CG  . LYS A 176 ? 0.79739 0.39395 0.45627 -0.03228 -0.09246 0.12432  202 LYS A CG  
1376 C CD  . LYS A 176 ? 0.84989 0.44422 0.52428 -0.02763 -0.10642 0.13320  202 LYS A CD  
1377 C CE  . LYS A 176 ? 0.86975 0.47375 0.56228 -0.02056 -0.12947 0.13128  202 LYS A CE  
1378 N NZ  . LYS A 176 ? 0.89435 0.49620 0.56066 -0.02307 -0.13822 0.12748  202 LYS A NZ  
1379 N N   . ALA A 177 ? 0.70151 0.28007 0.31341 -0.05700 -0.01153 0.11534  203 ALA A N   
1380 C CA  . ALA A 177 ? 0.70153 0.28398 0.32891 -0.06114 0.01209  0.11042  203 ALA A CA  
1381 C C   . ALA A 177 ? 0.72031 0.30820 0.38350 -0.05818 0.01359  0.11405  203 ALA A C   
1382 O O   . ALA A 177 ? 0.69653 0.29449 0.38790 -0.05849 0.02661  0.10722  203 ALA A O   
1383 C CB  . ALA A 177 ? 0.72393 0.29356 0.31908 -0.06992 0.03067  0.11194  203 ALA A CB  
1384 N N   . ASP A 178 ? 0.74403 0.32607 0.40848 -0.05519 -0.00005 0.12405  204 ASP A N   
1385 C CA  . ASP A 178 ? 0.74189 0.32809 0.44025 -0.05234 0.00063  0.12742  204 ASP A CA  
1386 C C   . ASP A 178 ? 0.67209 0.27526 0.40935 -0.04529 -0.00545 0.11819  204 ASP A C   
1387 O O   . ASP A 178 ? 0.64923 0.25891 0.41705 -0.04445 0.00178  0.11542  204 ASP A O   
1388 C CB  . ASP A 178 ? 0.79073 0.36730 0.48340 -0.04971 -0.01442 0.13961  204 ASP A CB  
1389 C CG  . ASP A 178 ? 0.88998 0.44937 0.55313 -0.05708 -0.00442 0.14983  204 ASP A CG  
1390 O OD1 . ASP A 178 ? 0.92225 0.47785 0.56875 -0.06427 0.01467  0.14665  204 ASP A OD1 
1391 O OD2 . ASP A 178 ? 0.93219 0.48192 0.58981 -0.05558 -0.01513 0.16077  204 ASP A OD2 
1392 N N   . ASP A 179 ? 0.65149 0.26207 0.38863 -0.04032 -0.01889 0.11287  205 ASP A N   
1393 C CA  . ASP A 179 ? 0.62083 0.25495 0.39739 -0.03315 -0.02292 0.10134  205 ASP A CA  
1394 C C   . ASP A 179 ? 0.61822 0.26676 0.41161 -0.03552 -0.00550 0.09007  205 ASP A C   
1395 O O   . ASP A 179 ? 0.58948 0.25189 0.41607 -0.03161 -0.00426 0.08293  205 ASP A O   
1396 C CB  . ASP A 179 ? 0.60589 0.25139 0.38220 -0.02771 -0.03839 0.09636  205 ASP A CB  
1397 C CG  . ASP A 179 ? 0.63952 0.27651 0.41535 -0.02286 -0.05861 0.10520  205 ASP A CG  
1398 O OD1 . ASP A 179 ? 0.66452 0.29424 0.45188 -0.02149 -0.06086 0.11223  205 ASP A OD1 
1399 O OD2 . ASP A 179 ? 0.65148 0.29202 0.41956 -0.02016 -0.07217 0.10412  205 ASP A OD2 
1400 N N   . TYR A 180 ? 0.62725 0.27203 0.39833 -0.04182 0.00762  0.08801  206 TYR A N   
1401 C CA  . TYR A 180 ? 0.60486 0.26308 0.39387 -0.04389 0.02349  0.07736  206 TYR A CA  
1402 C C   . TYR A 180 ? 0.61156 0.26251 0.41229 -0.04889 0.03871  0.08046  206 TYR A C   
1403 O O   . TYR A 180 ? 0.59900 0.26295 0.43272 -0.04710 0.04347  0.07318  206 TYR A O   
1404 C CB  . TYR A 180 ? 0.54487 0.20275 0.30920 -0.04818 0.03181  0.07252  206 TYR A CB  
1405 C CG  . TYR A 180 ? 0.53486 0.20182 0.29233 -0.04364 0.01758  0.06778  206 TYR A CG  
1406 C CD1 . TYR A 180 ? 0.50142 0.18883 0.28194 -0.03958 0.01702  0.05630  206 TYR A CD1 
1407 C CD2 . TYR A 180 ? 0.56051 0.21494 0.28915 -0.04363 0.00405  0.07514  206 TYR A CD2 
1408 C CE1 . TYR A 180 ? 0.49294 0.18843 0.26920 -0.03599 0.00504  0.05218  206 TYR A CE1 
1409 C CE2 . TYR A 180 ? 0.57598 0.23924 0.30189 -0.03982 -0.00926 0.07038  206 TYR A CE2 
1410 C CZ  . TYR A 180 ? 0.51720 0.20120 0.26762 -0.03619 -0.00787 0.05885  206 TYR A CZ  
1411 O OH  . TYR A 180 ? 0.50892 0.20145 0.25842 -0.03295 -0.02010 0.05433  206 TYR A OH  
1412 N N   . THR A 181 ? 0.62636 0.25575 0.40011 -0.05552 0.04622  0.09138  207 THR A N   
1413 C CA  . THR A 181 ? 0.63453 0.25672 0.42061 -0.06106 0.06202  0.09482  207 THR A CA  
1414 C C   . THR A 181 ? 0.60908 0.23428 0.42449 -0.05677 0.05279  0.09843  207 THR A C   
1415 O O   . THR A 181 ? 0.60091 0.23105 0.44260 -0.05908 0.06270  0.09643  207 THR A O   
1416 C CB  . THR A 181 ? 0.70528 0.31159 0.45778 -0.06844 0.07241  0.10385  207 THR A CB  
1417 O OG1 . THR A 181 ? 0.74640 0.34058 0.47325 -0.06634 0.05600  0.11459  207 THR A OG1 
1418 C CG2 . THR A 181 ? 0.70908 0.31326 0.43675 -0.07360 0.08620  0.09776  207 THR A CG2 
1419 N N   . GLY A 182 ? 0.59934 0.22252 0.41334 -0.05054 0.03385  0.10291  208 GLY A N   
1420 C CA  . GLY A 182 ? 0.60347 0.22804 0.44409 -0.04633 0.02521  0.10630  208 GLY A CA  
1421 C C   . GLY A 182 ? 0.56734 0.20750 0.44242 -0.03960 0.01858  0.09511  208 GLY A C   
1422 O O   . GLY A 182 ? 0.56001 0.21010 0.45836 -0.04082 0.02813  0.08635  208 GLY A O   
1423 N N   . PRO A 183 ? 0.55383 0.19773 0.43378 -0.03216 0.00164  0.09456  209 PRO A N   
1424 C CA  . PRO A 183 ? 0.51965 0.17895 0.43331 -0.02537 -0.00474 0.08400  209 PRO A CA  
1425 C C   . PRO A 183 ? 0.50252 0.18215 0.42762 -0.02416 0.00057  0.07039  209 PRO A C   
1426 O O   . PRO A 183 ? 0.49147 0.18147 0.44334 -0.02209 0.00243  0.06163  209 PRO A O   
1427 C CB  . PRO A 183 ? 0.52269 0.18338 0.43631 -0.01810 -0.02227 0.08651  209 PRO A CB  
1428 C CG  . PRO A 183 ? 0.55796 0.20808 0.43645 -0.02087 -0.02639 0.09515  209 PRO A CG  
1429 C CD  . PRO A 183 ? 0.57927 0.21584 0.43737 -0.02944 -0.01246 0.10294  209 PRO A CD  
1430 N N   . ALA A 184 ? 0.50144 0.18609 0.40665 -0.02537 0.00211  0.06834  210 ALA A N   
1431 C CA  . ALA A 184 ? 0.43667 0.13925 0.35264 -0.02427 0.00680  0.05636  210 ALA A CA  
1432 C C   . ALA A 184 ? 0.43254 0.13696 0.36210 -0.02932 0.02141  0.05230  210 ALA A C   
1433 O O   . ALA A 184 ? 0.40969 0.12720 0.36330 -0.02698 0.02202  0.04281  210 ALA A O   
1434 C CB  . ALA A 184 ? 0.44064 0.14582 0.33240 -0.02530 0.00623  0.05559  210 ALA A CB  
1435 N N   . THR A 185 ? 0.47135 0.16207 0.38581 -0.03648 0.03326  0.05945  211 THR A N   
1436 C CA  . THR A 185 ? 0.49794 0.18974 0.42929 -0.04178 0.04824  0.05611  211 THR A CA  
1437 C C   . THR A 185 ? 0.50239 0.19478 0.46407 -0.04030 0.04565  0.05469  211 THR A C   
1438 O O   . THR A 185 ? 0.50790 0.21170 0.49584 -0.04079 0.05009  0.04624  211 THR A O   
1439 C CB  . THR A 185 ? 0.55328 0.22806 0.46077 -0.05020 0.06287  0.06493  211 THR A CB  
1440 O OG1 . THR A 185 ? 0.55051 0.22687 0.43377 -0.05214 0.06787  0.06250  211 THR A OG1 
1441 C CG2 . THR A 185 ? 0.56192 0.23894 0.49313 -0.05562 0.07796  0.06249  211 THR A CG2 
1442 N N   . ASP A 186 ? 0.50290 0.18438 0.46265 -0.03816 0.03681  0.06229  212 ASP A N   
1443 C CA  . ASP A 186 ? 0.48745 0.17366 0.47636 -0.03617 0.03158  0.05950  212 ASP A CA  
1444 C C   . ASP A 186 ? 0.45944 0.16264 0.47056 -0.03001 0.02381  0.04624  212 ASP A C   
1445 O O   . ASP A 186 ? 0.44884 0.16259 0.48163 -0.03060 0.02531  0.03831  212 ASP A O   
1446 C CB  . ASP A 186 ? 0.50975 0.18282 0.49290 -0.03377 0.02131  0.06923  212 ASP A CB  
1447 C CG  . ASP A 186 ? 0.57088 0.22802 0.53506 -0.04032 0.02812  0.08289  212 ASP A CG  
1448 O OD1 . ASP A 186 ? 0.58531 0.24221 0.54889 -0.04721 0.04214  0.08331  212 ASP A OD1 
1449 O OD2 . ASP A 186 ? 0.58069 0.22666 0.53159 -0.03825 0.01974  0.09304  212 ASP A OD2 
1450 N N   . LEU A 187 ? 0.44519 0.15259 0.44904 -0.02403 0.01492  0.04344  213 LEU A N   
1451 C CA  . LEU A 187 ? 0.42491 0.14768 0.44653 -0.01836 0.00795  0.03141  213 LEU A CA  
1452 C C   . LEU A 187 ? 0.43632 0.17132 0.46509 -0.02048 0.01456  0.02309  213 LEU A C   
1453 O O   . LEU A 187 ? 0.44955 0.19687 0.49511 -0.01846 0.01118  0.01378  213 LEU A O   
1454 C CB  . LEU A 187 ? 0.40147 0.13014 0.41241 -0.01204 -0.00251 0.03018  213 LEU A CB  
1455 C CG  . LEU A 187 ? 0.35537 0.09852 0.38011 -0.00658 -0.00821 0.01823  213 LEU A CG  
1456 C CD1 . LEU A 187 ? 0.35294 0.10003 0.39472 -0.00422 -0.01048 0.01250  213 LEU A CD1 
1457 C CD2 . LEU A 187 ? 0.34974 0.09898 0.36473 -0.00125 -0.01605 0.01742  213 LEU A CD2 
1458 N N   . LEU A 188 ? 0.41510 0.15019 0.42752 -0.02421 0.02257  0.02571  214 LEU A N   
1459 C CA  . LEU A 188 ? 0.39426 0.14037 0.41609 -0.02588 0.02877  0.01796  214 LEU A CA  
1460 C C   . LEU A 188 ? 0.41458 0.16369 0.45906 -0.02989 0.03515  0.01532  214 LEU A C   
1461 O O   . LEU A 188 ? 0.39959 0.16218 0.46187 -0.02842 0.03261  0.00663  214 LEU A O   
1462 C CB  . LEU A 188 ? 0.38112 0.12635 0.38083 -0.02914 0.03668  0.02079  214 LEU A CB  
1463 C CG  . LEU A 188 ? 0.38172 0.13373 0.36449 -0.02465 0.02844  0.01907  214 LEU A CG  
1464 C CD1 . LEU A 188 ? 0.39279 0.14027 0.35106 -0.02857 0.03586  0.02253  214 LEU A CD1 
1465 C CD2 . LEU A 188 ? 0.35237 0.11939 0.35035 -0.02041 0.02322  0.00908  214 LEU A CD2 
1466 N N   . LEU A 189 ? 0.41925 0.15792 0.46217 -0.03474 0.04205  0.02296  215 LEU A N   
1467 C CA  . LEU A 189 ? 0.43939 0.18336 0.50500 -0.03844 0.04768  0.02038  215 LEU A CA  
1468 C C   . LEU A 189 ? 0.44760 0.19832 0.53193 -0.03440 0.03640  0.01448  215 LEU A C   
1469 O O   . LEU A 189 ? 0.47077 0.23162 0.57730 -0.03528 0.03695  0.00803  215 LEU A O   
1470 C CB  . LEU A 189 ? 0.47665 0.20672 0.53378 -0.04510 0.05920  0.03065  215 LEU A CB  
1471 C CG  . LEU A 189 ? 0.51537 0.24077 0.55734 -0.05085 0.07515  0.03398  215 LEU A CG  
1472 C CD1 . LEU A 189 ? 0.55640 0.26591 0.58338 -0.05735 0.08594  0.04524  215 LEU A CD1 
1473 C CD2 . LEU A 189 ? 0.49436 0.23477 0.56063 -0.05234 0.08293  0.02460  215 LEU A CD2 
1474 N N   . LYS A 190 ? 0.44387 0.18913 0.51983 -0.02985 0.02649  0.01616  216 LYS A N   
1475 C CA  . LYS A 190 ? 0.46491 0.21694 0.55548 -0.02557 0.01703  0.00892  216 LYS A CA  
1476 C C   . LYS A 190 ? 0.43799 0.20494 0.53544 -0.02155 0.01093  -0.00184 216 LYS A C   
1477 O O   . LYS A 190 ? 0.42505 0.20005 0.53855 -0.02039 0.00629  -0.00903 216 LYS A O   
1478 C CB  . LYS A 190 ? 0.51013 0.25379 0.59073 -0.02114 0.00950  0.01247  216 LYS A CB  
1479 C CG  . LYS A 190 ? 0.53938 0.28711 0.63493 -0.01785 0.00279  0.00617  216 LYS A CG  
1480 C CD  . LYS A 190 ? 0.55885 0.29632 0.64815 -0.01470 -0.00168 0.01165  216 LYS A CD  
1481 C CE  . LYS A 190 ? 0.57873 0.29991 0.65984 -0.01977 0.00402  0.02430  216 LYS A CE  
1482 N NZ  . LYS A 190 ? 0.58777 0.29849 0.66338 -0.01620 -0.00157 0.03042  216 LYS A NZ  
1483 N N   . LEU A 191 ? 0.42498 0.19482 0.50969 -0.01962 0.01047  -0.00267 217 LEU A N   
1484 C CA  . LEU A 191 ? 0.40100 0.18339 0.48931 -0.01610 0.00471  -0.01156 217 LEU A CA  
1485 C C   . LEU A 191 ? 0.41749 0.20853 0.51953 -0.01928 0.00924  -0.01512 217 LEU A C   
1486 O O   . LEU A 191 ? 0.40551 0.20656 0.51571 -0.01688 0.00285  -0.02237 217 LEU A O   
1487 C CB  . LEU A 191 ? 0.36744 0.14958 0.43816 -0.01271 0.00228  -0.01101 217 LEU A CB  
1488 C CG  . LEU A 191 ? 0.35311 0.13013 0.41344 -0.00824 -0.00357 -0.00896 217 LEU A CG  
1489 C CD1 . LEU A 191 ? 0.31335 0.09036 0.35922 -0.00605 -0.00478 -0.00755 217 LEU A CD1 
1490 C CD2 . LEU A 191 ? 0.33018 0.11394 0.39794 -0.00393 -0.01090 -0.01674 217 LEU A CD2 
1491 N N   . ARG A 192 ? 0.44044 0.22743 0.54522 -0.02462 0.02034  -0.01005 218 ARG A N   
1492 C CA  . ARG A 192 ? 0.43360 0.22935 0.55301 -0.02740 0.02662  -0.01343 218 ARG A CA  
1493 C C   . ARG A 192 ? 0.42938 0.23650 0.57373 -0.02660 0.02056  -0.02067 218 ARG A C   
1494 O O   . ARG A 192 ? 0.42329 0.24028 0.57616 -0.02515 0.01754  -0.02588 218 ARG A O   
1495 C CB  . ARG A 192 ? 0.47255 0.26077 0.59214 -0.03386 0.04195  -0.00685 218 ARG A CB  
1496 C CG  . ARG A 192 ? 0.49041 0.28789 0.62936 -0.03695 0.05111  -0.01073 218 ARG A CG  
1497 C CD  . ARG A 192 ? 0.52472 0.32829 0.65694 -0.03459 0.05029  -0.01458 218 ARG A CD  
1498 N NE  . ARG A 192 ? 0.55929 0.37288 0.71381 -0.03658 0.05776  -0.01916 218 ARG A NE  
1499 C CZ  . ARG A 192 ? 0.56974 0.39641 0.74577 -0.03353 0.04886  -0.02593 218 ARG A CZ  
1500 N NH1 . ARG A 192 ? 0.56498 0.39518 0.73946 -0.02891 0.03314  -0.02902 218 ARG A NH1 
1501 N NH2 . ARG A 192 ? 0.57357 0.40913 0.77243 -0.03511 0.05595  -0.02965 218 ARG A NH2 
1502 N N   . PRO A 193 ? 0.43798 0.24404 0.59549 -0.02748 0.01797  -0.02128 219 PRO A N   
1503 C CA  . PRO A 193 ? 0.41154 0.22838 0.59427 -0.02706 0.01169  -0.02841 219 PRO A CA  
1504 C C   . PRO A 193 ? 0.37910 0.20320 0.55838 -0.02194 -0.00173 -0.03552 219 PRO A C   
1505 O O   . PRO A 193 ? 0.34805 0.18096 0.54686 -0.02154 -0.00815 -0.04125 219 PRO A O   
1506 C CB  . PRO A 193 ? 0.43550 0.24723 0.62777 -0.02854 0.01062  -0.02736 219 PRO A CB  
1507 C CG  . PRO A 193 ? 0.45826 0.25725 0.63689 -0.03188 0.02108  -0.01807 219 PRO A CG  
1508 C CD  . PRO A 193 ? 0.45530 0.24986 0.60767 -0.02938 0.02091  -0.01514 219 PRO A CD  
1509 N N   . ASN A 194 ? 0.38753 0.20780 0.54331 -0.01816 -0.00617 -0.03517 220 ASN A N   
1510 C CA  . ASN A 194 ? 0.37175 0.19706 0.52102 -0.01373 -0.01742 -0.04133 220 ASN A CA  
1511 C C   . ASN A 194 ? 0.35527 0.18454 0.49571 -0.01240 -0.01710 -0.04138 220 ASN A C   
1512 O O   . ASN A 194 ? 0.35243 0.18521 0.48734 -0.00917 -0.02614 -0.04583 220 ASN A O   
1513 C CB  . ASN A 194 ? 0.38618 0.20544 0.51775 -0.01013 -0.02219 -0.04210 220 ASN A CB  
1514 C CG  . ASN A 194 ? 0.42565 0.24117 0.56685 -0.01078 -0.02404 -0.04329 220 ASN A CG  
1515 O OD1 . ASN A 194 ? 0.45667 0.27638 0.61381 -0.01133 -0.02997 -0.04864 220 ASN A OD1 
1516 N ND2 . ASN A 194 ? 0.44217 0.24932 0.57470 -0.01064 -0.01977 -0.03824 220 ASN A ND2 
1517 N N   . ILE A 195 ? 0.34604 0.17378 0.48436 -0.01500 -0.00686 -0.03664 221 ILE A N   
1518 C CA  . ILE A 195 ? 0.32909 0.16001 0.45975 -0.01393 -0.00559 -0.03672 221 ILE A CA  
1519 C C   . ILE A 195 ? 0.33588 0.17592 0.48983 -0.01554 -0.00463 -0.03964 221 ILE A C   
1520 O O   . ILE A 195 ? 0.32177 0.16335 0.49379 -0.01935 0.00382  -0.03850 221 ILE A O   
1521 C CB  . ILE A 195 ? 0.34621 0.16967 0.46112 -0.01585 0.00488  -0.03081 221 ILE A CB  
1522 C CG1 . ILE A 195 ? 0.34489 0.15943 0.44152 -0.01404 0.00281  -0.02746 221 ILE A CG1 
1523 C CG2 . ILE A 195 ? 0.36540 0.19195 0.47215 -0.01457 0.00577  -0.03165 221 ILE A CG2 
1524 C CD1 . ILE A 195 ? 0.34084 0.14568 0.42303 -0.01652 0.01187  -0.02062 221 ILE A CD1 
1525 N N   . ARG A 196 ? 0.32187 0.16768 0.47668 -0.01260 -0.01309 -0.04321 222 ARG A N   
1526 C CA  . ARG A 196 ? 0.33731 0.19226 0.51722 -0.01325 -0.01452 -0.04617 222 ARG A CA  
1527 C C   . ARG A 196 ? 0.34247 0.19912 0.52706 -0.01560 -0.00170 -0.04400 222 ARG A C   
1528 O O   . ARG A 196 ? 0.36566 0.22789 0.57501 -0.01833 0.00559  -0.04503 222 ARG A O   
1529 C CB  . ARG A 196 ? 0.34860 0.20716 0.52715 -0.00930 -0.02911 -0.04994 222 ARG A CB  
1530 C CG  . ARG A 196 ? 0.34868 0.21658 0.55604 -0.00924 -0.03355 -0.05290 222 ARG A CG  
1531 C CD  . ARG A 196 ? 0.34673 0.21536 0.55019 -0.00536 -0.04985 -0.05565 222 ARG A CD  
1532 N NE  . ARG A 196 ? 0.35654 0.22152 0.55430 -0.00384 -0.06262 -0.05903 222 ARG A NE  
1533 C CZ  . ARG A 196 ? 0.35306 0.21408 0.53814 -0.00066 -0.07732 -0.06146 222 ARG A CZ  
1534 N NH1 . ARG A 196 ? 0.33479 0.19509 0.51265 0.00135  -0.08150 -0.06002 222 ARG A NH1 
1535 N NH2 . ARG A 196 ? 0.34626 0.20271 0.52482 0.00038  -0.08781 -0.06541 222 ARG A NH2 
1536 N N   . TYR A 197 ? 0.32707 0.17910 0.48951 -0.01464 0.00179  -0.04165 223 TYR A N   
1537 C CA  . TYR A 197 ? 0.33575 0.18824 0.50037 -0.01698 0.01430  -0.04052 223 TYR A CA  
1538 C C   . TYR A 197 ? 0.36481 0.20849 0.50043 -0.01690 0.01894  -0.03707 223 TYR A C   
1539 O O   . TYR A 197 ? 0.38263 0.22215 0.49964 -0.01413 0.01105  -0.03602 223 TYR A O   
1540 C CB  . TYR A 197 ? 0.33843 0.19992 0.51995 -0.01501 0.01028  -0.04402 223 TYR A CB  
1541 C CG  . TYR A 197 ? 0.32573 0.18721 0.49317 -0.01057 -0.00286 -0.04469 223 TYR A CG  
1542 C CD1 . TYR A 197 ? 0.31615 0.17318 0.46210 -0.00953 -0.00024 -0.04287 223 TYR A CD1 
1543 C CD2 . TYR A 197 ? 0.32679 0.19182 0.50252 -0.00774 -0.01775 -0.04722 223 TYR A CD2 
1544 C CE1 . TYR A 197 ? 0.31682 0.17319 0.45064 -0.00591 -0.01098 -0.04305 223 TYR A CE1 
1545 C CE2 . TYR A 197 ? 0.31915 0.18209 0.48023 -0.00420 -0.02888 -0.04739 223 TYR A CE2 
1546 C CZ  . TYR A 197 ? 0.32478 0.18356 0.46537 -0.00335 -0.02483 -0.04505 223 TYR A CZ  
1547 O OH  . TYR A 197 ? 0.33664 0.19258 0.46312 -0.00020 -0.03490 -0.04479 223 TYR A OH  
1548 N N   . PHE A 198 ? 0.35979 0.20054 0.49280 -0.02012 0.03246  -0.03588 224 PHE A N   
1549 C CA  . PHE A 198 ? 0.36941 0.20165 0.47657 -0.02069 0.03774  -0.03325 224 PHE A CA  
1550 C C   . PHE A 198 ? 0.38289 0.21978 0.49267 -0.01981 0.04027  -0.03637 224 PHE A C   
1551 O O   . PHE A 198 ? 0.38879 0.22772 0.51119 -0.02269 0.05181  -0.03842 224 PHE A O   
1552 C CB  . PHE A 198 ? 0.36243 0.18378 0.45873 -0.02596 0.05216  -0.02913 224 PHE A CB  
1553 C CG  . PHE A 198 ? 0.35258 0.16715 0.44287 -0.02659 0.04911  -0.02470 224 PHE A CG  
1554 C CD1 . PHE A 198 ? 0.35796 0.16252 0.42338 -0.02580 0.04648  -0.02013 224 PHE A CD1 
1555 C CD2 . PHE A 198 ? 0.35509 0.17356 0.46603 -0.02782 0.04859  -0.02513 224 PHE A CD2 
1556 C CE1 . PHE A 198 ? 0.34544 0.14347 0.40748 -0.02592 0.04325  -0.01589 224 PHE A CE1 
1557 C CE2 . PHE A 198 ? 0.35452 0.16642 0.46084 -0.02832 0.04565  -0.02121 224 PHE A CE2 
1558 C CZ  . PHE A 198 ? 0.36635 0.16787 0.44850 -0.02722 0.04291  -0.01648 224 PHE A CZ  
1559 N N   . HIS A 199 ? 0.37174 0.21001 0.47058 -0.01594 0.03031  -0.03690 225 HIS A N   
1560 C CA  . HIS A 199 ? 0.36581 0.20801 0.46695 -0.01472 0.03101  -0.03937 225 HIS A CA  
1561 C C   . HIS A 199 ? 0.35996 0.19848 0.43947 -0.01209 0.02413  -0.03806 225 HIS A C   
1562 O O   . HIS A 199 ? 0.38635 0.22325 0.45684 -0.00969 0.01497  -0.03655 225 HIS A O   
1563 C CB  . HIS A 199 ? 0.37511 0.22746 0.50135 -0.01224 0.02330  -0.04225 225 HIS A CB  
1564 C CG  . HIS A 199 ? 0.38561 0.24252 0.52388 -0.01222 0.02871  -0.04502 225 HIS A CG  
1565 N ND1 . HIS A 199 ? 0.38519 0.24200 0.51459 -0.00966 0.02344  -0.04505 225 HIS A ND1 
1566 C CD2 . HIS A 199 ? 0.39171 0.25339 0.55184 -0.01445 0.03962  -0.04816 225 HIS A CD2 
1567 C CE1 . HIS A 199 ? 0.38814 0.24935 0.53309 -0.01009 0.02999  -0.04803 225 HIS A CE1 
1568 N NE2 . HIS A 199 ? 0.39674 0.26126 0.56089 -0.01289 0.04020  -0.05032 225 HIS A NE2 
1569 N N   . SER A 200 ? 0.35490 0.19222 0.42738 -0.01269 0.02932  -0.03924 226 SER A N   
1570 C CA  . SER A 200 ? 0.37721 0.21395 0.42860 -0.01081 0.02408  -0.03734 226 SER A CA  
1571 C C   . SER A 200 ? 0.33964 0.18001 0.39888 -0.00785 0.01684  -0.03901 226 SER A C   
1572 O O   . SER A 200 ? 0.34820 0.18847 0.39340 -0.00712 0.01515  -0.03792 226 SER A O   
1573 C CB  . SER A 200 ? 0.42387 0.25640 0.45645 -0.01395 0.03356  -0.03664 226 SER A CB  
1574 O OG  . SER A 200 ? 0.44192 0.26897 0.46626 -0.01719 0.04074  -0.03426 226 SER A OG  
1575 N N   . SER A 201 ? 0.32968 0.17519 0.40934 -0.00612 0.01139  -0.04040 227 SER A N   
1576 C CA  . SER A 201 ? 0.33383 0.18217 0.41884 -0.00326 0.00326  -0.04036 227 SER A CA  
1577 C C   . SER A 201 ? 0.34642 0.19847 0.44489 -0.00069 -0.00843 -0.04006 227 SER A C   
1578 O O   . SER A 201 ? 0.36066 0.21106 0.45445 0.00192  -0.01869 -0.03847 227 SER A O   
1579 C CB  . SER A 201 ? 0.31419 0.16564 0.41143 -0.00423 0.01081  -0.04288 227 SER A CB  
1580 O OG  . SER A 201 ? 0.33519 0.19361 0.45875 -0.00367 0.01018  -0.04484 227 SER A OG  
1581 N N   . GLN A 202 ? 0.34417 0.20027 0.45914 -0.00172 -0.00724 -0.04161 228 GLN A N   
1582 C CA  . GLN A 202 ? 0.35680 0.21648 0.48659 0.00038  -0.01938 -0.04222 228 GLN A CA  
1583 C C   . GLN A 202 ? 0.34228 0.19647 0.45363 0.00224  -0.03004 -0.04088 228 GLN A C   
1584 O O   . GLN A 202 ? 0.35431 0.20769 0.46858 0.00458  -0.04307 -0.04103 228 GLN A O   
1585 C CB  . GLN A 202 ? 0.39376 0.25921 0.54664 -0.00167 -0.01487 -0.04459 228 GLN A CB  
1586 C CG  . GLN A 202 ? 0.45126 0.32221 0.62708 0.00021  -0.02747 -0.04631 228 GLN A CG  
1587 C CD  . GLN A 202 ? 0.49464 0.37221 0.69668 -0.00219 -0.02194 -0.04892 228 GLN A CD  
1588 O OE1 . GLN A 202 ? 0.49595 0.37522 0.70495 -0.00523 -0.00689 -0.04968 228 GLN A OE1 
1589 N NE2 . GLN A 202 ? 0.51557 0.39609 0.73219 -0.00108 -0.03400 -0.05054 228 GLN A NE2 
1590 N N   . TYR A 203 ? 0.32266 0.17213 0.41485 0.00129  -0.02520 -0.03985 229 TYR A N   
1591 C CA  . TYR A 203 ? 0.33548 0.18009 0.41142 0.00308  -0.03356 -0.03963 229 TYR A CA  
1592 C C   . TYR A 203 ? 0.30090 0.14058 0.36186 0.00559  -0.04196 -0.03826 229 TYR A C   
1593 O O   . TYR A 203 ? 0.32909 0.16373 0.37858 0.00735  -0.05117 -0.03902 229 TYR A O   
1594 C CB  . TYR A 203 ? 0.32791 0.16898 0.38962 0.00189  -0.02642 -0.03876 229 TYR A CB  
1595 C CG  . TYR A 203 ? 0.30827 0.14793 0.35347 0.00159  -0.02040 -0.03632 229 TYR A CG  
1596 C CD1 . TYR A 203 ? 0.28885 0.12769 0.31448 0.00340  -0.02373 -0.03462 229 TYR A CD1 
1597 C CD2 . TYR A 203 ? 0.29882 0.13953 0.34717 -0.00088 -0.01046 -0.03580 229 TYR A CD2 
1598 C CE1 . TYR A 203 ? 0.31237 0.15237 0.32519 0.00283  -0.01850 -0.03224 229 TYR A CE1 
1599 C CE2 . TYR A 203 ? 0.29037 0.13113 0.32267 -0.00146 -0.00598 -0.03373 229 TYR A CE2 
1600 C CZ  . TYR A 203 ? 0.29053 0.13141 0.30665 0.00042  -0.01059 -0.03184 229 TYR A CZ  
1601 O OH  . TYR A 203 ? 0.27136 0.11288 0.27503 -0.00038 -0.00689 -0.03015 229 TYR A OH  
1602 N N   . ILE A 204 ? 0.28103 0.12070 0.34120 0.00559  -0.03893 -0.03649 230 ILE A N   
1603 C CA  . ILE A 204 ? 0.31593 0.15143 0.36158 0.00746  -0.04601 -0.03373 230 ILE A CA  
1604 C C   . ILE A 204 ? 0.33364 0.16512 0.38562 0.00952  -0.06033 -0.03406 230 ILE A C   
1605 O O   . ILE A 204 ? 0.34277 0.16920 0.37667 0.01075  -0.06836 -0.03329 230 ILE A O   
1606 C CB  . ILE A 204 ? 0.31092 0.14764 0.35886 0.00675  -0.04002 -0.03189 230 ILE A CB  
1607 C CG1 . ILE A 204 ? 0.29210 0.13176 0.33287 0.00440  -0.02751 -0.03220 230 ILE A CG1 
1608 C CG2 . ILE A 204 ? 0.29930 0.13173 0.33119 0.00805  -0.04590 -0.02782 230 ILE A CG2 
1609 C CD1 . ILE A 204 ? 0.28936 0.12974 0.33390 0.00322  -0.02113 -0.03213 230 ILE A CD1 
1610 N N   . ASN A 205 ? 0.34103 0.17776 0.41735 0.00967  -0.06265 -0.03479 231 ASN A N   
1611 C CA  . ASN A 205 ? 0.35481 0.18871 0.43960 0.01171  -0.07820 -0.03475 231 ASN A CA  
1612 C C   . ASN A 205 ? 0.37509 0.20804 0.46018 0.01176  -0.08556 -0.03820 231 ASN A C   
1613 O O   . ASN A 205 ? 0.38907 0.21344 0.46564 0.01347  -0.10083 -0.03848 231 ASN A O   
1614 C CB  . ASN A 205 ? 0.32885 0.17139 0.44420 0.01199  -0.07837 -0.03520 231 ASN A CB  
1615 C CG  . ASN A 205 ? 0.38475 0.22205 0.50630 0.01466  -0.09628 -0.03317 231 ASN A CG  
1616 O OD1 . ASN A 205 ? 0.38150 0.20730 0.48178 0.01606  -0.10431 -0.02906 231 ASN A OD1 
1617 N ND2 . ASN A 205 ? 0.39577 0.24038 0.54648 0.01526  -0.10320 -0.03568 231 ASN A ND2 
1618 N N   . ASP A 206 ? 0.36479 0.20454 0.45780 0.00974  -0.07556 -0.04079 232 ASP A N   
1619 C CA  . ASP A 206 ? 0.35134 0.19036 0.44606 0.00960  -0.08209 -0.04424 232 ASP A CA  
1620 C C   . ASP A 206 ? 0.37345 0.20165 0.43791 0.01071  -0.08713 -0.04506 232 ASP A C   
1621 O O   . ASP A 206 ? 0.38337 0.20622 0.44295 0.01156  -0.09870 -0.04828 232 ASP A O   
1622 C CB  . ASP A 206 ? 0.35790 0.20507 0.46773 0.00692  -0.06956 -0.04579 232 ASP A CB  
1623 C CG  . ASP A 206 ? 0.36671 0.22334 0.50952 0.00583  -0.06821 -0.04715 232 ASP A CG  
1624 O OD1 . ASP A 206 ? 0.37238 0.23058 0.52863 0.00757  -0.07769 -0.04707 232 ASP A OD1 
1625 O OD2 . ASP A 206 ? 0.37046 0.23230 0.52642 0.00325  -0.05785 -0.04819 232 ASP A OD2 
1626 N N   . LEU A 207 ? 0.36699 0.19144 0.41115 0.01068  -0.07874 -0.04290 233 LEU A N   
1627 C CA  . LEU A 207 ? 0.37162 0.19061 0.38650 0.01167  -0.08037 -0.04277 233 LEU A CA  
1628 C C   . LEU A 207 ? 0.37522 0.18679 0.37329 0.01308  -0.09144 -0.04036 233 LEU A C   
1629 O O   . LEU A 207 ? 0.40877 0.21297 0.38692 0.01383  -0.09869 -0.04239 233 LEU A O   
1630 C CB  . LEU A 207 ? 0.33549 0.15787 0.33708 0.01102  -0.06697 -0.04001 233 LEU A CB  
1631 C CG  . LEU A 207 ? 0.32314 0.14911 0.32847 0.01004  -0.05763 -0.04166 233 LEU A CG  
1632 C CD1 . LEU A 207 ? 0.30592 0.13551 0.30188 0.00939  -0.04692 -0.03815 233 LEU A CD1 
1633 C CD2 . LEU A 207 ? 0.31262 0.13426 0.30738 0.01112  -0.06129 -0.04573 233 LEU A CD2 
1634 N N   . ALA A 208 ? 0.35356 0.16567 0.35814 0.01333  -0.09266 -0.03602 234 ALA A N   
1635 C CA  . ALA A 208 ? 0.35693 0.16032 0.34473 0.01447  -0.10344 -0.03208 234 ALA A CA  
1636 C C   . ALA A 208 ? 0.37760 0.17421 0.36872 0.01565  -0.12130 -0.03471 234 ALA A C   
1637 O O   . ALA A 208 ? 0.40015 0.18616 0.36562 0.01625  -0.13124 -0.03311 234 ALA A O   
1638 C CB  . ALA A 208 ? 0.31813 0.12322 0.31755 0.01464  -0.10177 -0.02706 234 ALA A CB  
1639 N N   . ASN A 209 ? 0.36840 0.17028 0.39046 0.01566  -0.12565 -0.03888 235 ASN A N   
1640 C CA  . ASN A 209 ? 0.39931 0.19576 0.43051 0.01668  -0.14432 -0.04195 235 ASN A CA  
1641 C C   . ASN A 209 ? 0.39838 0.19210 0.42214 0.01602  -0.14794 -0.04867 235 ASN A C   
1642 O O   . ASN A 209 ? 0.40393 0.19163 0.43087 0.01661  -0.16490 -0.05212 235 ASN A O   
1643 C CB  . ASN A 209 ? 0.41619 0.22102 0.49035 0.01695  -0.14760 -0.04322 235 ASN A CB  
1644 C CG  . ASN A 209 ? 0.45116 0.25565 0.53457 0.01839  -0.15043 -0.03757 235 ASN A CG  
1645 O OD1 . ASN A 209 ? 0.46450 0.25849 0.52406 0.01962  -0.15942 -0.03246 235 ASN A OD1 
1646 N ND2 . ASN A 209 ? 0.44857 0.26919 0.56460 0.01779  -0.14002 -0.03756 235 ASN A ND2 
1647 N N   . GLY A 210 ? 0.39270 0.19006 0.40766 0.01489  -0.13361 -0.05083 236 GLY A N   
1648 C CA  . GLY A 210 ? 0.40205 0.19655 0.41201 0.01439  -0.13582 -0.05753 236 GLY A CA  
1649 C C   . GLY A 210 ? 0.40641 0.21297 0.45068 0.01314  -0.13269 -0.06049 236 GLY A C   
1650 O O   . GLY A 210 ? 0.39986 0.20634 0.44356 0.01270  -0.13456 -0.06534 236 GLY A O   
1651 N N   . ASP A 211 ? 0.40910 0.22763 0.48251 0.01235  -0.12611 -0.05730 237 ASP A N   
1652 C CA  . ASP A 211 ? 0.42187 0.25300 0.52653 0.01052  -0.12010 -0.05910 237 ASP A CA  
1653 C C   . ASP A 211 ? 0.40753 0.24280 0.50867 0.00853  -0.10297 -0.05870 237 ASP A C   
1654 O O   . ASP A 211 ? 0.41013 0.25120 0.52890 0.00677  -0.09919 -0.06068 237 ASP A O   
1655 C CB  . ASP A 211 ? 0.40603 0.24747 0.54109 0.01010  -0.11719 -0.05655 237 ASP A CB  
1656 C CG  . ASP A 211 ? 0.45433 0.29223 0.59859 0.01241  -0.13601 -0.05657 237 ASP A CG  
1657 O OD1 . ASP A 211 ? 0.47754 0.31029 0.62223 0.01340  -0.15227 -0.06017 237 ASP A OD1 
1658 O OD2 . ASP A 211 ? 0.46732 0.30676 0.61811 0.01334  -0.13534 -0.05296 237 ASP A OD2 
1659 N N   . ILE A 212 ? 0.40791 0.23953 0.48751 0.00879  -0.09345 -0.05589 238 ILE A N   
1660 C CA  . ILE A 212 ? 0.39049 0.22342 0.46315 0.00754  -0.08013 -0.05516 238 ILE A CA  
1661 C C   . ILE A 212 ? 0.37994 0.20352 0.42311 0.00944  -0.08204 -0.05680 238 ILE A C   
1662 O O   . ILE A 212 ? 0.39427 0.21105 0.41905 0.01098  -0.08615 -0.05574 238 ILE A O   
1663 C CB  . ILE A 212 ? 0.38089 0.21889 0.45829 0.00600  -0.06599 -0.05053 238 ILE A CB  
1664 C CG1 . ILE A 212 ? 0.37283 0.21930 0.47870 0.00361  -0.06082 -0.05009 238 ILE A CG1 
1665 C CG2 . ILE A 212 ? 0.39785 0.23373 0.46201 0.00540  -0.05562 -0.04910 238 ILE A CG2 
1666 C CD1 . ILE A 212 ? 0.37256 0.22136 0.49159 0.00156  -0.05778 -0.05184 238 ILE A CD1 
1667 N N   . CYS A 213 ? 0.38275 0.20528 0.42183 0.00929  -0.07850 -0.05947 239 CYS A N   
1668 C CA  A CYS A 213 ? 0.39544 0.20993 0.40988 0.01121  -0.07922 -0.06266 239 CYS A CA  
1669 C CA  B CYS A 213 ? 0.39374 0.20807 0.40743 0.01126  -0.07922 -0.06242 239 CYS A CA  
1670 C C   . CYS A 213 ? 0.36107 0.17672 0.36845 0.01154  -0.06692 -0.06008 239 CYS A C   
1671 O O   . CYS A 213 ? 0.32564 0.13551 0.31375 0.01345  -0.06565 -0.06244 239 CYS A O   
1672 C CB  A CYS A 213 ? 0.41989 0.23166 0.43557 0.01135  -0.08547 -0.06886 239 CYS A CB  
1673 C CB  B CYS A 213 ? 0.42422 0.23454 0.43596 0.01166  -0.08707 -0.06896 239 CYS A CB  
1674 S SG  A CYS A 213 ? 0.42811 0.24725 0.46798 0.00916  -0.07699 -0.06808 239 CYS A SG  
1675 S SG  B CYS A 213 ? 0.44520 0.25050 0.45739 0.01198  -0.10561 -0.07228 239 CYS A SG  
1676 N N   . VAL A 214 ? 0.34156 0.16354 0.36352 0.00972  -0.05809 -0.05567 240 VAL A N   
1677 C CA  . VAL A 214 ? 0.35485 0.17685 0.37069 0.01004  -0.04869 -0.05262 240 VAL A CA  
1678 C C   . VAL A 214 ? 0.34810 0.17443 0.37505 0.00756  -0.04129 -0.04733 240 VAL A C   
1679 O O   . VAL A 214 ? 0.33636 0.16616 0.37992 0.00523  -0.04020 -0.04669 240 VAL A O   
1680 C CB  . VAL A 214 ? 0.38786 0.20826 0.40565 0.01061  -0.04655 -0.05477 240 VAL A CB  
1681 C CG1 . VAL A 214 ? 0.39842 0.22155 0.43549 0.00798  -0.04573 -0.05407 240 VAL A CG1 
1682 C CG2 . VAL A 214 ? 0.38766 0.20709 0.39926 0.01168  -0.03937 -0.05149 240 VAL A CG2 
1683 N N   . ALA A 215 ? 0.34738 0.17365 0.36456 0.00786  -0.03571 -0.04385 241 ALA A N   
1684 C CA  . ALA A 215 ? 0.32778 0.15694 0.35066 0.00536  -0.02865 -0.03959 241 ALA A CA  
1685 C C   . ALA A 215 ? 0.30865 0.13905 0.31862 0.00554  -0.02277 -0.03561 241 ALA A C   
1686 O O   . ALA A 215 ? 0.32255 0.15412 0.32063 0.00769  -0.02415 -0.03590 241 ALA A O   
1687 C CB  . ALA A 215 ? 0.32333 0.15523 0.35002 0.00498  -0.03069 -0.03962 241 ALA A CB  
1688 N N   . ILE A 216 ? 0.28471 0.11426 0.29711 0.00300  -0.01623 -0.03204 242 ILE A N   
1689 C CA  . ILE A 216 ? 0.28920 0.11968 0.28961 0.00250  -0.01205 -0.02819 242 ILE A CA  
1690 C C   . ILE A 216 ? 0.28925 0.12324 0.28742 0.00155  -0.01025 -0.02827 242 ILE A C   
1691 O O   . ILE A 216 ? 0.28603 0.12012 0.29356 -0.00051 -0.00720 -0.02908 242 ILE A O   
1692 C CB  . ILE A 216 ? 0.25900 0.08481 0.25863 -0.00030 -0.00647 -0.02410 242 ILE A CB  
1693 C CG1 . ILE A 216 ? 0.26359 0.08471 0.26794 0.00062  -0.00866 -0.02353 242 ILE A CG1 
1694 C CG2 . ILE A 216 ? 0.26134 0.08708 0.24681 -0.00086 -0.00455 -0.02045 242 ILE A CG2 
1695 C CD1 . ILE A 216 ? 0.27257 0.08683 0.27412 -0.00235 -0.00363 -0.01806 242 ILE A CD1 
1696 N N   . GLY A 217 ? 0.29484 0.13165 0.28304 0.00298  -0.01165 -0.02775 243 GLY A N   
1697 C CA  . GLY A 217 ? 0.27617 0.11550 0.26336 0.00225  -0.01072 -0.02793 243 GLY A CA  
1698 C C   . GLY A 217 ? 0.30122 0.14284 0.27806 0.00225  -0.00955 -0.02620 243 GLY A C   
1699 O O   . GLY A 217 ? 0.31147 0.15405 0.28290 0.00374  -0.01094 -0.02544 243 GLY A O   
1700 N N   . TRP A 218 ? 0.29953 0.14209 0.27623 0.00056  -0.00699 -0.02613 244 TRP A N   
1701 C CA  . TRP A 218 ? 0.30151 0.14636 0.27109 0.00019  -0.00661 -0.02518 244 TRP A CA  
1702 C C   . TRP A 218 ? 0.32078 0.16745 0.28897 0.00208  -0.00973 -0.02524 244 TRP A C   
1703 O O   . TRP A 218 ? 0.32359 0.16876 0.29527 0.00296  -0.01238 -0.02591 244 TRP A O   
1704 C CB  . TRP A 218 ? 0.29789 0.14190 0.26816 -0.00248 -0.00261 -0.02595 244 TRP A CB  
1705 C CG  . TRP A 218 ? 0.31623 0.15666 0.28271 -0.00505 0.00194  -0.02587 244 TRP A CG  
1706 C CD1 . TRP A 218 ? 0.33241 0.17077 0.28878 -0.00592 0.00144  -0.02381 244 TRP A CD1 
1707 C CD2 . TRP A 218 ? 0.33758 0.17499 0.30967 -0.00728 0.00797  -0.02768 244 TRP A CD2 
1708 N NE1 . TRP A 218 ? 0.35865 0.19148 0.30998 -0.00889 0.00673  -0.02359 244 TRP A NE1 
1709 C CE2 . TRP A 218 ? 0.35223 0.18474 0.31356 -0.00993 0.01205  -0.02632 244 TRP A CE2 
1710 C CE3 . TRP A 218 ? 0.32128 0.15931 0.30746 -0.00733 0.01035  -0.03029 244 TRP A CE3 
1711 C CZ2 . TRP A 218 ? 0.35130 0.17916 0.31352 -0.01310 0.02049  -0.02771 244 TRP A CZ2 
1712 C CZ3 . TRP A 218 ? 0.32322 0.15823 0.31483 -0.01006 0.01850  -0.03232 244 TRP A CZ3 
1713 C CH2 . TRP A 218 ? 0.33005 0.15985 0.30874 -0.01315 0.02452  -0.03113 244 TRP A CH2 
1714 N N   . ALA A 219 ? 0.32102 0.17030 0.28414 0.00250  -0.00953 -0.02436 245 ALA A N   
1715 C CA  . ALA A 219 ? 0.32386 0.17384 0.28330 0.00391  -0.01043 -0.02420 245 ALA A CA  
1716 C C   . ALA A 219 ? 0.34431 0.19208 0.30344 0.00317  -0.01135 -0.02315 245 ALA A C   
1717 O O   . ALA A 219 ? 0.35882 0.20349 0.31341 0.00439  -0.01406 -0.02282 245 ALA A O   
1718 C CB  . ALA A 219 ? 0.30854 0.16254 0.26682 0.00377  -0.00827 -0.02363 245 ALA A CB  
1719 N N   . GLY A 220 ? 0.33557 0.18373 0.29864 0.00117  -0.00966 -0.02269 246 GLY A N   
1720 C CA  . GLY A 220 ? 0.32140 0.16678 0.28661 0.00070  -0.01095 -0.02136 246 GLY A CA  
1721 C C   . GLY A 220 ? 0.29940 0.14136 0.26974 0.00211  -0.01541 -0.02184 246 GLY A C   
1722 O O   . GLY A 220 ? 0.32877 0.16687 0.29677 0.00300  -0.01971 -0.01982 246 GLY A O   
1723 N N   . ASP A 221 ? 0.27362 0.11631 0.25133 0.00213  -0.01485 -0.02421 247 ASP A N   
1724 C CA  . ASP A 221 ? 0.29666 0.13713 0.28391 0.00331  -0.01945 -0.02534 247 ASP A CA  
1725 C C   . ASP A 221 ? 0.30004 0.13782 0.27981 0.00535  -0.02590 -0.02506 247 ASP A C   
1726 O O   . ASP A 221 ? 0.31349 0.14755 0.29556 0.00652  -0.03297 -0.02453 247 ASP A O   
1727 C CB  . ASP A 221 ? 0.30989 0.15171 0.30727 0.00224  -0.01560 -0.02794 247 ASP A CB  
1728 C CG  . ASP A 221 ? 0.36749 0.21006 0.36962 -0.00013 -0.00847 -0.02917 247 ASP A CG  
1729 O OD1 . ASP A 221 ? 0.36319 0.20547 0.36434 -0.00064 -0.00778 -0.02862 247 ASP A OD1 
1730 O OD2 . ASP A 221 ? 0.37716 0.21959 0.38306 -0.00179 -0.00309 -0.03082 247 ASP A OD2 
1731 N N   . VAL A 222 ? 0.29161 0.13044 0.26226 0.00587  -0.02415 -0.02576 248 VAL A N   
1732 C CA  . VAL A 222 ? 0.30856 0.14394 0.27057 0.00765  -0.02911 -0.02696 248 VAL A CA  
1733 C C   . VAL A 222 ? 0.35439 0.18561 0.30257 0.00793  -0.03119 -0.02444 248 VAL A C   
1734 O O   . VAL A 222 ? 0.38696 0.21226 0.32754 0.00896  -0.03809 -0.02465 248 VAL A O   
1735 C CB  . VAL A 222 ? 0.27807 0.11538 0.23612 0.00834  -0.02562 -0.02896 248 VAL A CB  
1736 C CG1 . VAL A 222 ? 0.26981 0.10265 0.21851 0.01011  -0.02987 -0.03172 248 VAL A CG1 
1737 C CG2 . VAL A 222 ? 0.27991 0.11917 0.24959 0.00761  -0.02365 -0.03004 248 VAL A CG2 
1738 N N   . TRP A 223 ? 0.35743 0.19070 0.30135 0.00666  -0.02555 -0.02187 249 TRP A N   
1739 C CA  . TRP A 223 ? 0.39119 0.21948 0.32216 0.00619  -0.02599 -0.01849 249 TRP A CA  
1740 C C   . TRP A 223 ? 0.42277 0.24555 0.35677 0.00626  -0.03316 -0.01552 249 TRP A C   
1741 O O   . TRP A 223 ? 0.46706 0.28198 0.38774 0.00661  -0.03838 -0.01282 249 TRP A O   
1742 C CB  . TRP A 223 ? 0.39018 0.22237 0.32047 0.00434  -0.01811 -0.01652 249 TRP A CB  
1743 C CG  . TRP A 223 ? 0.39817 0.23543 0.32700 0.00463  -0.01212 -0.01904 249 TRP A CG  
1744 C CD1 . TRP A 223 ? 0.40289 0.24692 0.34070 0.00375  -0.00776 -0.01977 249 TRP A CD1 
1745 C CD2 . TRP A 223 ? 0.42453 0.25993 0.34342 0.00605  -0.01051 -0.02158 249 TRP A CD2 
1746 N NE1 . TRP A 223 ? 0.41676 0.26390 0.35357 0.00487  -0.00419 -0.02207 249 TRP A NE1 
1747 C CE2 . TRP A 223 ? 0.40984 0.25195 0.33561 0.00632  -0.00482 -0.02362 249 TRP A CE2 
1748 C CE3 . TRP A 223 ? 0.46372 0.29170 0.36825 0.00713  -0.01380 -0.02284 249 TRP A CE3 
1749 C CZ2 . TRP A 223 ? 0.42402 0.26636 0.34572 0.00790  -0.00114 -0.02713 249 TRP A CZ2 
1750 C CZ3 . TRP A 223 ? 0.49781 0.32527 0.39503 0.00831  -0.00960 -0.02687 249 TRP A CZ3 
1751 C CH2 . TRP A 223 ? 0.48221 0.31718 0.38941 0.00882  -0.00273 -0.02911 249 TRP A CH2 
1752 N N   . GLN A 224 ? 0.40511 0.23101 0.35627 0.00594  -0.03362 -0.01604 250 GLN A N   
1753 C CA  . GLN A 224 ? 0.42092 0.24222 0.38056 0.00660  -0.04096 -0.01395 250 GLN A CA  
1754 C C   . GLN A 224 ? 0.40906 0.22590 0.36870 0.00853  -0.05134 -0.01526 250 GLN A C   
1755 O O   . GLN A 224 ? 0.38667 0.19595 0.34142 0.00943  -0.06049 -0.01197 250 GLN A O   
1756 C CB  . GLN A 224 ? 0.45673 0.28277 0.43698 0.00593  -0.03741 -0.01606 250 GLN A CB  
1757 C CG  . GLN A 224 ? 0.51685 0.33898 0.51132 0.00695  -0.04407 -0.01453 250 GLN A CG  
1758 C CD  . GLN A 224 ? 0.55672 0.38339 0.57224 0.00619  -0.03829 -0.01817 250 GLN A CD  
1759 O OE1 . GLN A 224 ? 0.55627 0.38772 0.57960 0.00557  -0.03333 -0.02242 250 GLN A OE1 
1760 N NE2 . GLN A 224 ? 0.57745 0.40158 0.60161 0.00601  -0.03819 -0.01662 250 GLN A NE2 
1761 N N   . ALA A 225 ? 0.39057 0.21108 0.35565 0.00906  -0.05101 -0.01984 251 ALA A N   
1762 C CA  . ALA A 225 ? 0.38091 0.19740 0.34787 0.01057  -0.06148 -0.02214 251 ALA A CA  
1763 C C   . ALA A 225 ? 0.39920 0.20721 0.34065 0.01116  -0.06705 -0.02090 251 ALA A C   
1764 O O   . ALA A 225 ? 0.42308 0.22342 0.35967 0.01217  -0.07905 -0.01991 251 ALA A O   
1765 C CB  . ALA A 225 ? 0.32498 0.14664 0.30320 0.01047  -0.05852 -0.02721 251 ALA A CB  
1766 N N   . SER A 226 ? 0.40454 0.21320 0.32939 0.01045  -0.05853 -0.02122 252 SER A N   
1767 C CA  . SER A 226 ? 0.42631 0.22630 0.32502 0.01055  -0.06074 -0.02090 252 SER A CA  
1768 C C   . SER A 226 ? 0.40979 0.20089 0.29416 0.00979  -0.06490 -0.01428 252 SER A C   
1769 O O   . SER A 226 ? 0.41067 0.19081 0.27583 0.01010  -0.07382 -0.01307 252 SER A O   
1770 C CB  . SER A 226 ? 0.44365 0.24746 0.33274 0.00996  -0.04863 -0.02303 252 SER A CB  
1771 O OG  . SER A 226 ? 0.50925 0.30528 0.37364 0.00903  -0.04560 -0.02085 252 SER A OG  
1772 N N   . ASN A 227 ? 0.40518 0.19956 0.29771 0.00860  -0.05919 -0.00980 253 ASN A N   
1773 C CA  . ASN A 227 ? 0.41684 0.20199 0.29810 0.00769  -0.06297 -0.00261 253 ASN A CA  
1774 C C   . ASN A 227 ? 0.42217 0.20113 0.31239 0.00942  -0.07820 -0.00040 253 ASN A C   
1775 O O   . ASN A 227 ? 0.44884 0.21558 0.32179 0.00934  -0.08679 0.00520  253 ASN A O   
1776 C CB  . ASN A 227 ? 0.41835 0.20874 0.30978 0.00588  -0.05333 0.00070  253 ASN A CB  
1777 C CG  . ASN A 227 ? 0.43317 0.22721 0.31375 0.00388  -0.04017 0.00017  253 ASN A CG  
1778 O OD1 . ASN A 227 ? 0.47571 0.26536 0.33651 0.00360  -0.03747 -0.00094 253 ASN A OD1 
1779 N ND2 . ASN A 227 ? 0.39640 0.19831 0.29093 0.00242  -0.03198 0.00028  253 ASN A ND2 
1780 N N   . ARG A 228 ? 0.39637 0.18294 0.31376 0.01086  -0.08174 -0.00449 254 ARG A N   
1781 C CA  . ARG A 228 ? 0.40335 0.18547 0.33488 0.01281  -0.09666 -0.00358 254 ARG A CA  
1782 C C   . ARG A 228 ? 0.43504 0.20809 0.34924 0.01380  -0.10966 -0.00504 254 ARG A C   
1783 O O   . ARG A 228 ? 0.44015 0.20251 0.34756 0.01482  -0.12417 -0.00077 254 ARG A O   
1784 C CB  . ARG A 228 ? 0.38711 0.18016 0.35286 0.01363  -0.09471 -0.00884 254 ARG A CB  
1785 C CG  . ARG A 228 ? 0.43355 0.22432 0.42241 0.01574  -0.10878 -0.00878 254 ARG A CG  
1786 C CD  . ARG A 228 ? 0.43511 0.23705 0.45870 0.01585  -0.10251 -0.01425 254 ARG A CD  
1787 N NE  . ARG A 228 ? 0.43476 0.24203 0.46597 0.01453  -0.08900 -0.01364 254 ARG A NE  
1788 C CZ  . ARG A 228 ? 0.44262 0.25886 0.49285 0.01342  -0.07779 -0.01853 254 ARG A CZ  
1789 N NH1 . ARG A 228 ? 0.43148 0.25290 0.49661 0.01333  -0.07733 -0.02363 254 ARG A NH1 
1790 N NH2 . ARG A 228 ? 0.41848 0.23767 0.47174 0.01203  -0.06684 -0.01836 254 ARG A NH2 
1791 N N   . ALA A 229 ? 0.44477 0.22093 0.35130 0.01353  -0.10554 -0.01120 255 ALA A N   
1792 C CA  . ALA A 229 ? 0.47768 0.24428 0.36486 0.01413  -0.11705 -0.01402 255 ALA A CA  
1793 C C   . ALA A 229 ? 0.51956 0.27166 0.36908 0.01302  -0.11946 -0.00847 255 ALA A C   
1794 O O   . ALA A 229 ? 0.45029 0.18972 0.28381 0.01359  -0.13498 -0.00670 255 ALA A O   
1795 C CB  . ALA A 229 ? 0.46785 0.24013 0.35400 0.01393  -0.10983 -0.02196 255 ALA A CB  
1796 N N   . LYS A 230 ? 0.52313 0.27616 0.35793 0.01113  -0.10436 -0.00554 256 LYS A N   
1797 C CA  . LYS A 230 ? 0.54346 0.28234 0.34220 0.00929  -0.10335 0.00018  256 LYS A CA  
1798 C C   . LYS A 230 ? 0.53901 0.26694 0.33432 0.00942  -0.11572 0.00947  256 LYS A C   
1799 O O   . LYS A 230 ? 0.54265 0.25418 0.30859 0.00888  -0.12635 0.01364  256 LYS A O   
1800 C CB  . LYS A 230 ? 0.55066 0.29485 0.34251 0.00700  -0.08359 0.00144  256 LYS A CB  
1801 C CG  . LYS A 230 ? 0.55220 0.30353 0.34103 0.00696  -0.07208 -0.00685 256 LYS A CG  
1802 C CD  . LYS A 230 ? 0.57385 0.32932 0.35661 0.00469  -0.05404 -0.00514 256 LYS A CD  
1803 C CE  . LYS A 230 ? 0.58699 0.34925 0.36943 0.00517  -0.04328 -0.01343 256 LYS A CE  
1804 N NZ  . LYS A 230 ? 0.59996 0.36616 0.37865 0.00300  -0.02629 -0.01217 256 LYS A NZ  
1805 N N   . GLU A 231 ? 0.48820 0.22386 0.31254 0.01011  -0.11475 0.01277  257 GLU A N   
1806 C CA  . GLU A 231 ? 0.52795 0.25362 0.35428 0.01069  -0.12644 0.02158  257 GLU A CA  
1807 C C   . GLU A 231 ? 0.54816 0.26603 0.37853 0.01329  -0.14864 0.02122  257 GLU A C   
1808 O O   . GLU A 231 ? 0.58570 0.28787 0.39856 0.01350  -0.16250 0.02899  257 GLU A O   
1809 C CB  . GLU A 231 ? 0.54790 0.28451 0.40850 0.01117  -0.11999 0.02282  257 GLU A CB  
1810 C CG  . GLU A 231 ? 0.62676 0.35295 0.48625 0.01082  -0.12511 0.03292  257 GLU A CG  
1811 C CD  . GLU A 231 ? 0.68399 0.40315 0.55914 0.01401  -0.14581 0.03590  257 GLU A CD  
1812 O OE1 . GLU A 231 ? 0.68956 0.41760 0.59099 0.01645  -0.15248 0.02888  257 GLU A OE1 
1813 O OE2 . GLU A 231 ? 0.72808 0.43251 0.59069 0.01398  -0.15554 0.04554  257 GLU A OE2 
1814 N N   . ALA A 232 ? 0.54608 0.27406 0.40007 0.01511  -0.15296 0.01259  258 ALA A N   
1815 C CA  . ALA A 232 ? 0.56875 0.29079 0.43130 0.01741  -0.17461 0.01102  258 ALA A CA  
1816 C C   . ALA A 232 ? 0.59875 0.30542 0.42163 0.01661  -0.18544 0.01021  258 ALA A C   
1817 O O   . ALA A 232 ? 0.60557 0.30303 0.42822 0.01821  -0.20676 0.01065  258 ALA A O   
1818 C CB  . ALA A 232 ? 0.44839 0.18590 0.34961 0.01889  -0.17418 0.00176  258 ALA A CB  
1819 N N   . LYS A 233 ? 0.59715 0.30048 0.38735 0.01415  -0.17154 0.00852  259 LYS A N   
1820 C CA  . LYS A 233 ? 0.60275 0.29115 0.35238 0.01298  -0.17838 0.00587  259 LYS A CA  
1821 C C   . LYS A 233 ? 0.58163 0.27251 0.34425 0.01465  -0.19206 -0.00390 259 LYS A C   
1822 O O   . LYS A 233 ? 0.59721 0.27311 0.33438 0.01458  -0.20866 -0.00522 259 LYS A O   
1823 C CB  . LYS A 233 ? 0.63907 0.30557 0.35377 0.01208  -0.19239 0.01597  259 LYS A CB  
1824 C CG  . LYS A 233 ? 0.66295 0.32443 0.36257 0.00977  -0.17904 0.02642  259 LYS A CG  
1825 C CD  . LYS A 233 ? 0.73728 0.37495 0.40200 0.00876  -0.19455 0.03759  259 LYS A CD  
1826 C CE  . LYS A 233 ? 0.78027 0.41377 0.44127 0.00677  -0.18395 0.04927  259 LYS A CE  
1827 N NZ  . LYS A 233 ? 0.83158 0.44995 0.44375 0.00225  -0.17048 0.05416  259 LYS A NZ  
1828 N N   . ASN A 234 ? 0.54457 0.25335 0.34600 0.01581  -0.18538 -0.01080 260 ASN A N   
1829 C CA  . ASN A 234 ? 0.54072 0.25316 0.36062 0.01698  -0.19693 -0.01997 260 ASN A CA  
1830 C C   . ASN A 234 ? 0.54667 0.25746 0.34522 0.01576  -0.18922 -0.02904 260 ASN A C   
1831 O O   . ASN A 234 ? 0.53467 0.24586 0.34385 0.01631  -0.19952 -0.03717 260 ASN A O   
1832 C CB  . ASN A 234 ? 0.49117 0.22209 0.36205 0.01824  -0.19216 -0.02296 260 ASN A CB  
1833 C CG  . ASN A 234 ? 0.48320 0.22760 0.36318 0.01718  -0.16803 -0.02380 260 ASN A CG  
1834 O OD1 . ASN A 234 ? 0.49267 0.23440 0.34523 0.01577  -0.15501 -0.02311 260 ASN A OD1 
1835 N ND2 . ASN A 234 ? 0.47006 0.22855 0.38890 0.01772  -0.16202 -0.02549 260 ASN A ND2 
1836 N N   . GLY A 235 ? 0.52383 0.23288 0.29546 0.01412  -0.17135 -0.02833 261 GLY A N   
1837 C CA  . GLY A 235 ? 0.58979 0.29720 0.34310 0.01331  -0.16265 -0.03739 261 GLY A CA  
1838 C C   . GLY A 235 ? 0.56578 0.29010 0.35031 0.01396  -0.14946 -0.04403 261 GLY A C   
1839 O O   . GLY A 235 ? 0.56829 0.29152 0.34451 0.01383  -0.14500 -0.05258 261 GLY A O   
1840 N N   . VAL A 236 ? 0.53725 0.27584 0.35620 0.01458  -0.14317 -0.04043 262 VAL A N   
1841 C CA  . VAL A 236 ? 0.49787 0.25101 0.34393 0.01484  -0.13051 -0.04513 262 VAL A CA  
1842 C C   . VAL A 236 ? 0.48559 0.24373 0.32101 0.01405  -0.11084 -0.04283 262 VAL A C   
1843 O O   . VAL A 236 ? 0.47075 0.23059 0.30440 0.01340  -0.10498 -0.03551 262 VAL A O   
1844 C CB  . VAL A 236 ? 0.46372 0.22838 0.34998 0.01543  -0.13288 -0.04300 262 VAL A CB  
1845 C CG1 . VAL A 236 ? 0.45046 0.22793 0.35916 0.01512  -0.11863 -0.04642 262 VAL A CG1 
1846 C CG2 . VAL A 236 ? 0.41780 0.17877 0.32019 0.01620  -0.15231 -0.04611 262 VAL A CG2 
1847 N N   . ASN A 237 ? 0.47592 0.23633 0.30667 0.01415  -0.10117 -0.04934 263 ASN A N   
1848 C CA  . ASN A 237 ? 0.49466 0.26002 0.31795 0.01367  -0.08340 -0.04841 263 ASN A CA  
1849 C C   . ASN A 237 ? 0.46733 0.24692 0.32123 0.01425  -0.07477 -0.04915 263 ASN A C   
1850 O O   . ASN A 237 ? 0.44412 0.22648 0.30893 0.01508  -0.07390 -0.05529 263 ASN A O   
1851 C CB  . ASN A 237 ? 0.54284 0.30004 0.34013 0.01364  -0.07807 -0.05532 263 ASN A CB  
1852 C CG  . ASN A 237 ? 0.60743 0.34862 0.36758 0.01232  -0.08376 -0.05363 263 ASN A CG  
1853 O OD1 . ASN A 237 ? 0.62693 0.36477 0.37547 0.01099  -0.08187 -0.04544 263 ASN A OD1 
1854 N ND2 . ASN A 237 ? 0.62598 0.35587 0.36592 0.01242  -0.09097 -0.06133 263 ASN A ND2 
1855 N N   . VAL A 238 ? 0.45361 0.24090 0.32000 0.01361  -0.06867 -0.04280 264 VAL A N   
1856 C CA  . VAL A 238 ? 0.45367 0.25269 0.34456 0.01368  -0.06075 -0.04248 264 VAL A CA  
1857 C C   . VAL A 238 ? 0.43522 0.23889 0.32013 0.01334  -0.04724 -0.04119 264 VAL A C   
1858 O O   . VAL A 238 ? 0.45300 0.25464 0.32514 0.01227  -0.04300 -0.03694 264 VAL A O   
1859 C CB  . VAL A 238 ? 0.46122 0.26524 0.37172 0.01303  -0.06371 -0.03765 264 VAL A CB  
1860 C CG1 . VAL A 238 ? 0.42242 0.23648 0.35210 0.01251  -0.05443 -0.03719 264 VAL A CG1 
1861 C CG2 . VAL A 238 ? 0.49647 0.29723 0.41895 0.01352  -0.07701 -0.03955 264 VAL A CG2 
1862 N N   . SER A 239 ? 0.41405 0.22360 0.30982 0.01417  -0.04094 -0.04457 265 SER A N   
1863 C CA  A SER A 239 ? 0.40281 0.21789 0.29850 0.01422  -0.02960 -0.04390 265 SER A CA  
1864 C CA  B SER A 239 ? 0.40308 0.21816 0.29877 0.01423  -0.02960 -0.04392 265 SER A CA  
1865 C C   . SER A 239 ? 0.37581 0.19961 0.29233 0.01421  -0.02657 -0.04215 265 SER A C   
1866 O O   . SER A 239 ? 0.36584 0.19046 0.29510 0.01423  -0.03108 -0.04280 265 SER A O   
1867 C CB  A SER A 239 ? 0.41636 0.22819 0.30221 0.01567  -0.02475 -0.05023 265 SER A CB  
1868 C CB  B SER A 239 ? 0.41669 0.22852 0.30261 0.01568  -0.02478 -0.05027 265 SER A CB  
1869 O OG  A SER A 239 ? 0.42049 0.23784 0.30815 0.01575  -0.01383 -0.04956 265 SER A OG  
1870 O OG  B SER A 239 ? 0.44542 0.24856 0.30696 0.01498  -0.02387 -0.05132 265 SER A OG  
1871 N N   . PHE A 240 ? 0.37711 0.20671 0.29654 0.01383  -0.01887 -0.03983 266 PHE A N   
1872 C CA  . PHE A 240 ? 0.35865 0.19501 0.29332 0.01359  -0.01651 -0.03779 266 PHE A CA  
1873 C C   . PHE A 240 ? 0.37328 0.21314 0.31195 0.01519  -0.01095 -0.04001 266 PHE A C   
1874 O O   . PHE A 240 ? 0.42090 0.26119 0.35305 0.01552  -0.00546 -0.04144 266 PHE A O   
1875 C CB  . PHE A 240 ? 0.36782 0.20793 0.30525 0.01148  -0.01474 -0.03291 266 PHE A CB  
1876 C CG  . PHE A 240 ? 0.36788 0.21326 0.31645 0.01081  -0.01287 -0.03111 266 PHE A CG  
1877 C CD1 . PHE A 240 ? 0.34917 0.19390 0.30511 0.01004  -0.01536 -0.03039 266 PHE A CD1 
1878 C CD2 . PHE A 240 ? 0.38904 0.23927 0.34037 0.01067  -0.00870 -0.03019 266 PHE A CD2 
1879 C CE1 . PHE A 240 ? 0.36078 0.20802 0.32199 0.00898  -0.01368 -0.02838 266 PHE A CE1 
1880 C CE2 . PHE A 240 ? 0.38356 0.23704 0.34240 0.00995  -0.00905 -0.02839 266 PHE A CE2 
1881 C CZ  . PHE A 240 ? 0.36236 0.21351 0.32379 0.00903  -0.01152 -0.02729 266 PHE A CZ  
1882 N N   . SER A 241 ? 0.33929 0.18112 0.28962 0.01609  -0.01209 -0.04009 267 SER A N   
1883 C CA  . SER A 241 ? 0.35715 0.20180 0.31494 0.01822  -0.00872 -0.04202 267 SER A CA  
1884 C C   . SER A 241 ? 0.38136 0.22973 0.34982 0.01774  -0.01017 -0.03773 267 SER A C   
1885 O O   . SER A 241 ? 0.38361 0.22965 0.35420 0.01648  -0.01354 -0.03520 267 SER A O   
1886 C CB  . SER A 241 ? 0.35325 0.19307 0.31270 0.02059  -0.01014 -0.04743 267 SER A CB  
1887 O OG  . SER A 241 ? 0.32438 0.16614 0.29690 0.02267  -0.00962 -0.04757 267 SER A OG  
1888 N N   . ILE A 242 ? 0.38390 0.23749 0.35872 0.01847  -0.00752 -0.03702 268 ILE A N   
1889 C CA  . ILE A 242 ? 0.33882 0.19481 0.32303 0.01863  -0.01059 -0.03348 268 ILE A CA  
1890 C C   . ILE A 242 ? 0.31844 0.17306 0.31293 0.02210  -0.01165 -0.03586 268 ILE A C   
1891 O O   . ILE A 242 ? 0.33582 0.19412 0.33812 0.02440  -0.00802 -0.03939 268 ILE A O   
1892 C CB  . ILE A 242 ? 0.31803 0.18053 0.30648 0.01750  -0.00911 -0.03174 268 ILE A CB  
1893 C CG1 . ILE A 242 ? 0.32897 0.19203 0.30806 0.01441  -0.00674 -0.03055 268 ILE A CG1 
1894 C CG2 . ILE A 242 ? 0.31510 0.17821 0.30912 0.01700  -0.01488 -0.02764 268 ILE A CG2 
1895 C CD1 . ILE A 242 ? 0.34722 0.21625 0.33166 0.01280  -0.00473 -0.02942 268 ILE A CD1 
1896 N N   . PRO A 243 ? 0.31402 0.16309 0.31038 0.02250  -0.01574 -0.03420 269 PRO A N   
1897 C CA  . PRO A 243 ? 0.34053 0.18663 0.34727 0.02595  -0.01684 -0.03694 269 PRO A CA  
1898 C C   . PRO A 243 ? 0.33245 0.18264 0.35313 0.02857  -0.01853 -0.03572 269 PRO A C   
1899 O O   . PRO A 243 ? 0.35013 0.20429 0.37203 0.02729  -0.02104 -0.03155 269 PRO A O   
1900 C CB  . PRO A 243 ? 0.34562 0.18434 0.35138 0.02466  -0.02102 -0.03329 269 PRO A CB  
1901 C CG  . PRO A 243 ? 0.32697 0.16518 0.32169 0.02092  -0.02005 -0.03177 269 PRO A CG  
1902 C CD  . PRO A 243 ? 0.30612 0.15062 0.29601 0.01957  -0.01827 -0.03029 269 PRO A CD  
1903 N N   . LYS A 244 ? 0.32726 0.17611 0.36017 0.03240  -0.01778 -0.04002 270 LYS A N   
1904 C CA  . LYS A 244 ? 0.35711 0.21048 0.40838 0.03572  -0.01929 -0.04018 270 LYS A CA  
1905 C C   . LYS A 244 ? 0.35039 0.20026 0.40723 0.03596  -0.02898 -0.03226 270 LYS A C   
1906 O O   . LYS A 244 ? 0.34409 0.19848 0.41461 0.03781  -0.03313 -0.03044 270 LYS A O   
1907 C CB  . LYS A 244 ? 0.38039 0.23243 0.44462 0.04001  -0.01507 -0.04790 270 LYS A CB  
1908 C CG  . LYS A 244 ? 0.41049 0.25304 0.47714 0.04149  -0.01929 -0.04785 270 LYS A CG  
1909 C CD  . LYS A 244 ? 0.45335 0.29304 0.52319 0.04411  -0.01292 -0.05810 270 LYS A CD  
1910 C CE  . LYS A 244 ? 0.47382 0.30597 0.55870 0.04748  -0.01722 -0.05914 270 LYS A CE  
1911 N NZ  . LYS A 244 ? 0.49570 0.32079 0.57689 0.04525  -0.02555 -0.04984 270 LYS A NZ  
1912 N N   . GLU A 245 ? 0.35166 0.19296 0.39830 0.03392  -0.03281 -0.02738 271 GLU A N   
1913 C CA  . GLU A 245 ? 0.35659 0.19184 0.40266 0.03330  -0.04144 -0.01883 271 GLU A CA  
1914 C C   . GLU A 245 ? 0.34702 0.18453 0.38083 0.02959  -0.04441 -0.01375 271 GLU A C   
1915 O O   . GLU A 245 ? 0.37931 0.21073 0.40812 0.02851  -0.05202 -0.00658 271 GLU A O   
1916 C CB  . GLU A 245 ? 0.36906 0.19335 0.40762 0.03155  -0.04236 -0.01522 271 GLU A CB  
1917 C CG  . GLU A 245 ? 0.37555 0.19566 0.42690 0.03495  -0.04091 -0.02018 271 GLU A CG  
1918 C CD  . GLU A 245 ? 0.40378 0.22528 0.44972 0.03390  -0.03387 -0.02801 271 GLU A CD  
1919 O OE1 . GLU A 245 ? 0.39831 0.22388 0.43145 0.03071  -0.03052 -0.02863 271 GLU A OE1 
1920 O OE2 . GLU A 245 ? 0.41966 0.23738 0.47422 0.03630  -0.03256 -0.03369 271 GLU A OE2 
1921 N N   . GLY A 246 ? 0.34291 0.18766 0.37062 0.02748  -0.03892 -0.01725 272 GLY A N   
1922 C CA  . GLY A 246 ? 0.34140 0.18780 0.35771 0.02371  -0.04093 -0.01380 272 GLY A CA  
1923 C C   . GLY A 246 ? 0.35430 0.19683 0.35341 0.01956  -0.03629 -0.01306 272 GLY A C   
1924 O O   . GLY A 246 ? 0.35630 0.19489 0.35308 0.01942  -0.03261 -0.01459 272 GLY A O   
1925 N N   . ALA A 247 ? 0.35398 0.19775 0.34299 0.01615  -0.03678 -0.01129 273 ALA A N   
1926 C CA  . ALA A 247 ? 0.35691 0.19764 0.33236 0.01227  -0.03199 -0.01108 273 ALA A CA  
1927 C C   . ALA A 247 ? 0.35542 0.19493 0.31993 0.00879  -0.03449 -0.00859 273 ALA A C   
1928 O O   . ALA A 247 ? 0.33480 0.17769 0.30321 0.00932  -0.04005 -0.00805 273 ALA A O   
1929 C CB  . ALA A 247 ? 0.35314 0.19941 0.33051 0.01238  -0.02560 -0.01625 273 ALA A CB  
1930 N N   . MET A 248 ? 0.36798 0.20248 0.32003 0.00514  -0.03030 -0.00780 274 MET A N   
1931 C CA  . MET A 248 ? 0.39351 0.22585 0.33327 0.00146  -0.03107 -0.00706 274 MET A CA  
1932 C C   . MET A 248 ? 0.37912 0.21976 0.32405 0.00102  -0.02865 -0.01145 274 MET A C   
1933 O O   . MET A 248 ? 0.34605 0.19039 0.29605 0.00157  -0.02315 -0.01435 274 MET A O   
1934 C CB  . MET A 248 ? 0.44372 0.26786 0.37014 -0.00239 -0.02511 -0.00582 274 MET A CB  
1935 C CG  . MET A 248 ? 0.49684 0.31674 0.40782 -0.00647 -0.02486 -0.00605 274 MET A CG  
1936 S SD  . MET A 248 ? 0.55133 0.36439 0.45180 -0.01096 -0.01348 -0.00752 274 MET A SD  
1937 C CE  . MET A 248 ? 0.52668 0.34751 0.43315 -0.01172 -0.00998 -0.01392 274 MET A CE  
1938 N N   . ALA A 249 ? 0.38269 0.22541 0.32646 -0.00012 -0.03361 -0.01166 275 ALA A N   
1939 C CA  . ALA A 249 ? 0.33592 0.18535 0.28499 -0.00125 -0.03150 -0.01528 275 ALA A CA  
1940 C C   . ALA A 249 ? 0.34548 0.19003 0.28132 -0.00552 -0.03079 -0.01645 275 ALA A C   
1941 O O   . ALA A 249 ? 0.35130 0.18827 0.27355 -0.00758 -0.03492 -0.01450 275 ALA A O   
1942 C CB  . ALA A 249 ? 0.27807 0.13483 0.24100 0.00049  -0.03708 -0.01594 275 ALA A CB  
1943 N N   . PHE A 250 ? 0.34477 0.19245 0.28353 -0.00691 -0.02543 -0.01971 276 PHE A N   
1944 C CA  . PHE A 250 ? 0.37324 0.21678 0.30247 -0.01074 -0.02379 -0.02234 276 PHE A CA  
1945 C C   . PHE A 250 ? 0.35073 0.20050 0.29032 -0.01150 -0.02372 -0.02521 276 PHE A C   
1946 O O   . PHE A 250 ? 0.33478 0.19056 0.28607 -0.00955 -0.02088 -0.02503 276 PHE A O   
1947 C CB  . PHE A 250 ? 0.39074 0.22930 0.31406 -0.01213 -0.01553 -0.02360 276 PHE A CB  
1948 C CG  . PHE A 250 ? 0.40698 0.24988 0.34183 -0.00960 -0.01107 -0.02363 276 PHE A CG  
1949 C CD1 . PHE A 250 ? 0.39975 0.24602 0.34232 -0.00970 -0.00823 -0.02583 276 PHE A CD1 
1950 C CD2 . PHE A 250 ? 0.40571 0.24804 0.34296 -0.00728 -0.01063 -0.02138 276 PHE A CD2 
1951 C CE1 . PHE A 250 ? 0.40961 0.25810 0.35990 -0.00748 -0.00600 -0.02538 276 PHE A CE1 
1952 C CE2 . PHE A 250 ? 0.41039 0.25559 0.35640 -0.00516 -0.00816 -0.02201 276 PHE A CE2 
1953 C CZ  . PHE A 250 ? 0.42642 0.27444 0.37785 -0.00525 -0.00631 -0.02382 276 PHE A CZ  
1954 N N   . PHE A 251 ? 0.34658 0.19371 0.28053 -0.01473 -0.02671 -0.02790 277 PHE A N   
1955 C CA  . PHE A 251 ? 0.35283 0.20527 0.29803 -0.01605 -0.02822 -0.03048 277 PHE A CA  
1956 C C   . PHE A 251 ? 0.36761 0.21566 0.30822 -0.01928 -0.02382 -0.03471 277 PHE A C   
1957 O O   . PHE A 251 ? 0.39035 0.23049 0.31606 -0.02150 -0.02251 -0.03698 277 PHE A O   
1958 C CB  . PHE A 251 ? 0.36903 0.22317 0.31690 -0.01698 -0.03842 -0.03084 277 PHE A CB  
1959 C CG  . PHE A 251 ? 0.37381 0.23340 0.33221 -0.01344 -0.04320 -0.02737 277 PHE A CG  
1960 C CD1 . PHE A 251 ? 0.39066 0.25977 0.36979 -0.01219 -0.04373 -0.02775 277 PHE A CD1 
1961 C CD2 . PHE A 251 ? 0.37139 0.22607 0.32026 -0.01153 -0.04644 -0.02388 277 PHE A CD2 
1962 C CE1 . PHE A 251 ? 0.38004 0.25433 0.37151 -0.00871 -0.04708 -0.02563 277 PHE A CE1 
1963 C CE2 . PHE A 251 ? 0.38000 0.23918 0.34087 -0.00793 -0.05103 -0.02116 277 PHE A CE2 
1964 C CZ  . PHE A 251 ? 0.39417 0.26350 0.37701 -0.00632 -0.05123 -0.02250 277 PHE A CZ  
1965 N N   . ASP A 252 ? 0.33236 0.18470 0.28575 -0.01966 -0.02084 -0.03580 278 ASP A N   
1966 C CA  . ASP A 252 ? 0.34355 0.19245 0.29751 -0.02286 -0.01888 -0.04029 278 ASP A CA  
1967 C C   . ASP A 252 ? 0.33937 0.19114 0.30039 -0.02532 -0.02586 -0.04256 278 ASP A C   
1968 O O   . ASP A 252 ? 0.31098 0.17004 0.28443 -0.02411 -0.02910 -0.04004 278 ASP A O   
1969 C CB  . ASP A 252 ? 0.37939 0.22958 0.34386 -0.02201 -0.01230 -0.03934 278 ASP A CB  
1970 C CG  . ASP A 252 ? 0.41521 0.26131 0.37483 -0.02040 -0.00665 -0.03904 278 ASP A CG  
1971 O OD1 . ASP A 252 ? 0.43862 0.27909 0.38757 -0.02172 -0.00485 -0.04212 278 ASP A OD1 
1972 O OD2 . ASP A 252 ? 0.42209 0.27011 0.38852 -0.01805 -0.00402 -0.03585 278 ASP A OD2 
1973 N N   . VAL A 253 ? 0.35396 0.19987 0.30805 -0.02889 -0.02810 -0.04803 279 VAL A N   
1974 C CA  . VAL A 253 ? 0.35916 0.20664 0.31897 -0.03170 -0.03684 -0.05119 279 VAL A CA  
1975 C C   . VAL A 253 ? 0.36148 0.20548 0.32657 -0.03523 -0.03447 -0.05694 279 VAL A C   
1976 O O   . VAL A 253 ? 0.37348 0.21084 0.33084 -0.03595 -0.02777 -0.06009 279 VAL A O   
1977 C CB  . VAL A 253 ? 0.39125 0.23271 0.33284 -0.03299 -0.04644 -0.05275 279 VAL A CB  
1978 C CG1 . VAL A 253 ? 0.37690 0.22108 0.31570 -0.02935 -0.04960 -0.04652 279 VAL A CG1 
1979 C CG2 . VAL A 253 ? 0.42302 0.25260 0.34136 -0.03550 -0.04233 -0.05740 279 VAL A CG2 
1980 N N   . PHE A 254 ? 0.34300 0.19165 0.32417 -0.03745 -0.03971 -0.05859 280 PHE A N   
1981 C CA  . PHE A 254 ? 0.35477 0.19916 0.34134 -0.04153 -0.04015 -0.06506 280 PHE A CA  
1982 C C   . PHE A 254 ? 0.38439 0.22196 0.35568 -0.04476 -0.05036 -0.07175 280 PHE A C   
1983 O O   . PHE A 254 ? 0.39674 0.23720 0.36703 -0.04462 -0.06087 -0.07050 280 PHE A O   
1984 C CB  . PHE A 254 ? 0.35212 0.20419 0.36486 -0.04303 -0.04032 -0.06353 280 PHE A CB  
1985 C CG  . PHE A 254 ? 0.33231 0.18374 0.35547 -0.04270 -0.02998 -0.06069 280 PHE A CG  
1986 C CD1 . PHE A 254 ? 0.32053 0.16607 0.35009 -0.04596 -0.02801 -0.06551 280 PHE A CD1 
1987 C CD2 . PHE A 254 ? 0.28433 0.13982 0.31016 -0.03917 -0.02308 -0.05319 280 PHE A CD2 
1988 C CE1 . PHE A 254 ? 0.29712 0.14066 0.33639 -0.04548 -0.01983 -0.06183 280 PHE A CE1 
1989 C CE2 . PHE A 254 ? 0.36823 0.22133 0.40106 -0.03893 -0.01540 -0.04971 280 PHE A CE2 
1990 C CZ  . PHE A 254 ? 0.28587 0.13291 0.32585 -0.04198 -0.01401 -0.05348 280 PHE A CZ  
1991 N N   . ALA A 255 ? 0.38215 0.20980 0.34104 -0.04757 -0.04758 -0.07905 281 ALA A N   
1992 C CA  . ALA A 255 ? 0.39738 0.21559 0.33601 -0.05119 -0.05635 -0.08647 281 ALA A CA  
1993 C C   . ALA A 255 ? 0.40751 0.21920 0.35026 -0.05530 -0.05475 -0.09593 281 ALA A C   
1994 O O   . ALA A 255 ? 0.41363 0.22533 0.36882 -0.05477 -0.04450 -0.09656 281 ALA A O   
1995 C CB  . ALA A 255 ? 0.39567 0.20435 0.30363 -0.05049 -0.05269 -0.08655 281 ALA A CB  
1996 N N   . MET A 256 ? 0.42896 0.23422 0.36131 -0.05938 -0.06601 -0.10340 282 MET A N   
1997 C CA  . MET A 256 ? 0.43736 0.23555 0.37351 -0.06378 -0.06641 -0.11386 282 MET A CA  
1998 C C   . MET A 256 ? 0.49088 0.27348 0.39309 -0.06648 -0.06484 -0.12303 282 MET A C   
1999 O O   . MET A 256 ? 0.49115 0.26720 0.36851 -0.06817 -0.07540 -0.12454 282 MET A O   
2000 C CB  . MET A 256 ? 0.42374 0.22634 0.37734 -0.06711 -0.08108 -0.11689 282 MET A CB  
2001 C CG  . MET A 256 ? 0.46253 0.26033 0.42588 -0.07164 -0.08101 -0.12685 282 MET A CG  
2002 S SD  . MET A 256 ? 0.46304 0.26978 0.44802 -0.07528 -0.09717 -0.12880 282 MET A SD  
2003 C CE  . MET A 256 ? 0.41784 0.23963 0.43717 -0.07214 -0.09758 -0.11753 282 MET A CE  
2004 N N   . PRO A 257 ? 0.50858 0.28407 0.40818 -0.06699 -0.05179 -0.12919 283 PRO A N   
2005 C CA  . PRO A 257 ? 0.53946 0.30478 0.41115 -0.06874 -0.04708 -0.13794 283 PRO A CA  
2006 C C   . PRO A 257 ? 0.58479 0.34742 0.44886 -0.07287 -0.05901 -0.14652 283 PRO A C   
2007 O O   . PRO A 257 ? 0.59211 0.36046 0.47926 -0.07510 -0.06659 -0.14843 283 PRO A O   
2008 C CB  . PRO A 257 ? 0.51490 0.28016 0.40136 -0.06653 -0.03168 -0.14194 283 PRO A CB  
2009 C CG  . PRO A 257 ? 0.47447 0.24724 0.38571 -0.06354 -0.02663 -0.13250 283 PRO A CG  
2010 C CD  . PRO A 257 ? 0.47466 0.25543 0.40016 -0.06447 -0.03947 -0.12658 283 PRO A CD  
2011 N N   . ALA A 258 ? 0.62059 0.37416 0.45129 -0.07428 -0.05995 -0.15117 284 ALA A N   
2012 C CA  . ALA A 258 ? 0.64642 0.39627 0.46427 -0.07823 -0.07300 -0.15857 284 ALA A CA  
2013 C C   . ALA A 258 ? 0.65373 0.40459 0.49098 -0.08065 -0.07030 -0.17011 284 ALA A C   
2014 O O   . ALA A 258 ? 0.67819 0.43099 0.52228 -0.08453 -0.08245 -0.17454 284 ALA A O   
2015 C CB  . ALA A 258 ? 0.68597 0.42371 0.46089 -0.07926 -0.07228 -0.16074 284 ALA A CB  
2016 N N   . ASP A 259 ? 0.64972 0.39907 0.49774 -0.07803 -0.05545 -0.17453 285 ASP A N   
2017 C CA  . ASP A 259 ? 0.68283 0.43096 0.54966 -0.07867 -0.05361 -0.18552 285 ASP A CA  
2018 C C   . ASP A 259 ? 0.64931 0.40551 0.55664 -0.07705 -0.05253 -0.18042 285 ASP A C   
2019 O O   . ASP A 259 ? 0.64613 0.38538 0.55173 -0.07553 -0.05137 -0.17823 285 ASP A O   
2020 C CB  . ASP A 259 ? 0.72437 0.46192 0.57536 -0.07515 -0.04106 -0.19102 285 ASP A CB  
2021 C CG  . ASP A 259 ? 0.73343 0.47308 0.59162 -0.07065 -0.02624 -0.18183 285 ASP A CG  
2022 O OD1 . ASP A 259 ? 0.70615 0.45362 0.57581 -0.06946 -0.02716 -0.17142 285 ASP A OD1 
2023 O OD2 . ASP A 259 ? 0.75121 0.48578 0.60533 -0.06866 -0.01309 -0.18554 285 ASP A OD2 
2024 N N   . ALA A 260 ? 0.62363 0.38662 0.53959 -0.08173 -0.05236 -0.17004 286 ALA A N   
2025 C CA  . ALA A 260 ? 0.59688 0.35917 0.53541 -0.08170 -0.05171 -0.15894 286 ALA A CA  
2026 C C   . ALA A 260 ? 0.60064 0.36312 0.55395 -0.08585 -0.05856 -0.16360 286 ALA A C   
2027 O O   . ALA A 260 ? 0.51202 0.27739 0.46143 -0.08978 -0.07025 -0.16881 286 ALA A O   
2028 C CB  . ALA A 260 ? 0.57098 0.34788 0.52735 -0.07856 -0.05753 -0.14844 286 ALA A CB  
2029 N N   . LYS A 261 ? 0.58991 0.35121 0.56321 -0.08401 -0.05227 -0.16155 287 LYS A N   
2030 C CA  . LYS A 261 ? 0.60471 0.36528 0.59345 -0.08792 -0.05688 -0.16645 287 LYS A CA  
2031 C C   . LYS A 261 ? 0.55646 0.33179 0.57968 -0.08836 -0.06194 -0.15864 287 LYS A C   
2032 O O   . LYS A 261 ? 0.52046 0.29724 0.55653 -0.09236 -0.06928 -0.16288 287 LYS A O   
2033 C CB  . LYS A 261 ? 0.62818 0.38079 0.62321 -0.08552 -0.04741 -0.16911 287 LYS A CB  
2034 C CG  . LYS A 261 ? 0.67210 0.41141 0.63921 -0.08261 -0.04146 -0.17616 287 LYS A CG  
2035 C CD  . LYS A 261 ? 0.74096 0.46560 0.67660 -0.08756 -0.04969 -0.18849 287 LYS A CD  
2036 C CE  . LYS A 261 ? 0.77172 0.48667 0.68252 -0.08147 -0.04547 -0.19562 287 LYS A CE  
2037 N NZ  . LYS A 261 ? 0.78040 0.49600 0.66655 -0.07967 -0.05609 -0.20047 287 LYS A NZ  
2038 N N   . ASN A 262 ? 0.53184 0.31735 0.57004 -0.08446 -0.05796 -0.14759 288 ASN A N   
2039 C CA  . ASN A 262 ? 0.54427 0.34256 0.61412 -0.08467 -0.06046 -0.13935 288 ASN A CA  
2040 C C   . ASN A 262 ? 0.56600 0.37358 0.63559 -0.08367 -0.06789 -0.13466 288 ASN A C   
2041 O O   . ASN A 262 ? 0.53079 0.34514 0.60978 -0.08030 -0.06266 -0.12533 288 ASN A O   
2042 C CB  . ASN A 262 ? 0.54162 0.34264 0.62992 -0.08119 -0.04863 -0.12983 288 ASN A CB  
2043 C CG  . ASN A 262 ? 0.54549 0.33702 0.63273 -0.08058 -0.04165 -0.13390 288 ASN A CG  
2044 O OD1 . ASN A 262 ? 0.52541 0.31454 0.62471 -0.08371 -0.04392 -0.13839 288 ASN A OD1 
2045 N ND2 . ASN A 262 ? 0.52889 0.31554 0.60393 -0.07624 -0.03338 -0.13246 288 ASN A ND2 
2046 N N   . LYS A 263 ? 0.58649 0.39397 0.64521 -0.08641 -0.08086 -0.14102 289 LYS A N   
2047 C CA  . LYS A 263 ? 0.58258 0.39827 0.64091 -0.08472 -0.09014 -0.13657 289 LYS A CA  
2048 C C   . LYS A 263 ? 0.58394 0.41372 0.67845 -0.08477 -0.09264 -0.12928 289 LYS A C   
2049 O O   . LYS A 263 ? 0.58737 0.42508 0.68974 -0.08193 -0.09293 -0.12197 289 LYS A O   
2050 C CB  . LYS A 263 ? 0.59765 0.40869 0.63333 -0.08712 -0.10474 -0.14447 289 LYS A CB  
2051 C CG  . LYS A 263 ? 0.63210 0.42963 0.62854 -0.08701 -0.10081 -0.15083 289 LYS A CG  
2052 C CD  . LYS A 263 ? 0.68218 0.47610 0.65312 -0.08827 -0.11581 -0.15521 289 LYS A CD  
2053 C CE  . LYS A 263 ? 0.70457 0.48716 0.63673 -0.08692 -0.10985 -0.15830 289 LYS A CE  
2054 N NZ  . LYS A 263 ? 0.71434 0.48674 0.63452 -0.08946 -0.09671 -0.16839 289 LYS A NZ  
2055 N N   . ASP A 264 ? 0.57938 0.41205 0.69678 -0.08812 -0.09355 -0.13139 290 ASP A N   
2056 C CA  . ASP A 264 ? 0.56456 0.41039 0.71804 -0.08872 -0.09350 -0.12483 290 ASP A CA  
2057 C C   . ASP A 264 ? 0.51985 0.36945 0.68466 -0.08591 -0.07884 -0.11431 290 ASP A C   
2058 O O   . ASP A 264 ? 0.51414 0.37350 0.69426 -0.08445 -0.07776 -0.10751 290 ASP A O   
2059 C CB  . ASP A 264 ? 0.60430 0.45060 0.77865 -0.09296 -0.09542 -0.12928 290 ASP A CB  
2060 C CG  . ASP A 264 ? 0.62278 0.48292 0.83283 -0.09448 -0.10030 -0.12583 290 ASP A CG  
2061 O OD1 . ASP A 264 ? 0.64773 0.51211 0.86163 -0.09565 -0.11506 -0.13073 290 ASP A OD1 
2062 O OD2 . ASP A 264 ? 0.61790 0.48429 0.85209 -0.09448 -0.08915 -0.11806 290 ASP A OD2 
2063 N N   . GLU A 265 ? 0.48871 0.33014 0.64595 -0.08503 -0.06756 -0.11287 291 GLU A N   
2064 C CA  . GLU A 265 ? 0.44075 0.28378 0.60490 -0.08226 -0.05457 -0.10251 291 GLU A CA  
2065 C C   . GLU A 265 ? 0.37494 0.21872 0.52251 -0.07819 -0.05323 -0.09858 291 GLU A C   
2066 O O   . GLU A 265 ? 0.36853 0.21773 0.52627 -0.07647 -0.04637 -0.08983 291 GLU A O   
2067 C CB  . GLU A 265 ? 0.46704 0.30041 0.62557 -0.08148 -0.04545 -0.10211 291 GLU A CB  
2068 C CG  . GLU A 265 ? 0.50153 0.33366 0.67927 -0.08519 -0.04527 -0.10447 291 GLU A CG  
2069 C CD  . GLU A 265 ? 0.54650 0.37289 0.71490 -0.08813 -0.05476 -0.11694 291 GLU A CD  
2070 O OE1 . GLU A 265 ? 0.56343 0.38700 0.70964 -0.08779 -0.06206 -0.12343 291 GLU A OE1 
2071 O OE2 . GLU A 265 ? 0.56252 0.38624 0.74456 -0.09102 -0.05488 -0.12021 291 GLU A OE2 
2072 N N   . ALA A 266 ? 0.36563 0.20317 0.48679 -0.07689 -0.05922 -0.10498 292 ALA A N   
2073 C CA  . ALA A 266 ? 0.37501 0.21275 0.48036 -0.07306 -0.05894 -0.10163 292 ALA A CA  
2074 C C   . ALA A 266 ? 0.39421 0.24254 0.51352 -0.07284 -0.06655 -0.09808 292 ALA A C   
2075 O O   . ALA A 266 ? 0.39688 0.25047 0.51695 -0.06931 -0.06096 -0.09019 292 ALA A O   
2076 C CB  . ALA A 266 ? 0.37643 0.20423 0.44976 -0.07240 -0.06353 -0.10942 292 ALA A CB  
2077 N N   . TYR A 267 ? 0.37761 0.23079 0.50710 -0.07569 -0.07861 -0.10280 293 TYR A N   
2078 C CA  . TYR A 267 ? 0.36878 0.23340 0.51728 -0.07520 -0.08616 -0.09952 293 TYR A CA  
2079 C C   . TYR A 267 ? 0.36377 0.23803 0.54364 -0.07581 -0.07489 -0.09193 293 TYR A C   
2080 O O   . TYR A 267 ? 0.36557 0.24820 0.55598 -0.07354 -0.07265 -0.08622 293 TYR A O   
2081 C CB  . TYR A 267 ? 0.38117 0.24902 0.53615 -0.07786 -0.10219 -0.10612 293 TYR A CB  
2082 C CG  . TYR A 267 ? 0.40864 0.26834 0.53136 -0.07681 -0.11548 -0.11125 293 TYR A CG  
2083 C CD1 . TYR A 267 ? 0.41325 0.27297 0.52247 -0.07312 -0.12018 -0.10725 293 TYR A CD1 
2084 C CD2 . TYR A 267 ? 0.42285 0.27366 0.52698 -0.07973 -0.12285 -0.11980 293 TYR A CD2 
2085 C CE1 . TYR A 267 ? 0.45045 0.30113 0.52722 -0.07232 -0.13187 -0.11048 293 TYR A CE1 
2086 C CE2 . TYR A 267 ? 0.45915 0.30104 0.53008 -0.07922 -0.13375 -0.12380 293 TYR A CE2 
2087 C CZ  . TYR A 267 ? 0.47932 0.32099 0.53608 -0.07547 -0.13822 -0.11851 293 TYR A CZ  
2088 O OH  . TYR A 267 ? 0.52693 0.35838 0.54821 -0.07507 -0.14852 -0.12101 293 TYR A OH  
2089 N N   . GLN A 268 ? 0.36149 0.23454 0.55426 -0.07855 -0.06653 -0.09104 294 GLN A N   
2090 C CA  . GLN A 268 ? 0.38477 0.26423 0.60201 -0.07953 -0.05368 -0.08277 294 GLN A CA  
2091 C C   . GLN A 268 ? 0.39470 0.27081 0.59976 -0.07617 -0.04221 -0.07499 294 GLN A C   
2092 O O   . GLN A 268 ? 0.40643 0.29051 0.62353 -0.07509 -0.03473 -0.06805 294 GLN A O   
2093 C CB  . GLN A 268 ? 0.41043 0.28615 0.63839 -0.08279 -0.04726 -0.08248 294 GLN A CB  
2094 C CG  . GLN A 268 ? 0.43365 0.31435 0.68130 -0.08658 -0.05671 -0.08903 294 GLN A CG  
2095 C CD  . GLN A 268 ? 0.45608 0.33429 0.71988 -0.08987 -0.04864 -0.08705 294 GLN A CD  
2096 O OE1 . GLN A 268 ? 0.49070 0.36307 0.75157 -0.09186 -0.05396 -0.09377 294 GLN A OE1 
2097 N NE2 . GLN A 268 ? 0.44065 0.32227 0.72042 -0.09063 -0.03541 -0.07773 294 GLN A NE2 
2098 N N   . PHE A 269 ? 0.40062 0.26613 0.57970 -0.07361 -0.03984 -0.07563 295 PHE A N   
2099 C CA  . PHE A 269 ? 0.37462 0.23919 0.53691 -0.06857 -0.02947 -0.06686 295 PHE A CA  
2100 C C   . PHE A 269 ? 0.35037 0.22290 0.50170 -0.06395 -0.03263 -0.06426 295 PHE A C   
2101 O O   . PHE A 269 ? 0.34979 0.22657 0.49944 -0.06087 -0.02407 -0.05644 295 PHE A O   
2102 C CB  . PHE A 269 ? 0.39102 0.24385 0.53137 -0.06654 -0.02713 -0.06887 295 PHE A CB  
2103 C CG  . PHE A 269 ? 0.38939 0.24008 0.51757 -0.06212 -0.01705 -0.05978 295 PHE A CG  
2104 C CD1 . PHE A 269 ? 0.39255 0.23963 0.53081 -0.06329 -0.00787 -0.05235 295 PHE A CD1 
2105 C CD2 . PHE A 269 ? 0.38148 0.23275 0.48777 -0.05708 -0.01750 -0.05840 295 PHE A CD2 
2106 C CE1 . PHE A 269 ? 0.38431 0.22820 0.50968 -0.05931 -0.00077 -0.04405 295 PHE A CE1 
2107 C CE2 . PHE A 269 ? 0.38602 0.23520 0.48236 -0.05320 -0.00984 -0.05075 295 PHE A CE2 
2108 C CZ  . PHE A 269 ? 0.38548 0.23088 0.49071 -0.05421 -0.00219 -0.04372 295 PHE A CZ  
2109 N N   . LEU A 270 ? 0.33524 0.20855 0.47771 -0.06348 -0.04521 -0.07071 296 LEU A N   
2110 C CA  . LEU A 270 ? 0.31721 0.19711 0.45112 -0.05914 -0.04942 -0.06791 296 LEU A CA  
2111 C C   . LEU A 270 ? 0.31504 0.20758 0.47670 -0.05939 -0.04786 -0.06426 296 LEU A C   
2112 O O   . LEU A 270 ? 0.30236 0.20056 0.46208 -0.05534 -0.04237 -0.05858 296 LEU A O   
2113 C CB  . LEU A 270 ? 0.32683 0.20275 0.44454 -0.05922 -0.06438 -0.07487 296 LEU A CB  
2114 C CG  . LEU A 270 ? 0.33815 0.20159 0.42441 -0.05837 -0.06387 -0.07854 296 LEU A CG  
2115 C CD1 . LEU A 270 ? 0.33947 0.19712 0.40788 -0.05970 -0.07855 -0.08556 296 LEU A CD1 
2116 C CD2 . LEU A 270 ? 0.34530 0.20804 0.41407 -0.05319 -0.05450 -0.07169 296 LEU A CD2 
2117 N N   . ASN A 271 ? 0.32866 0.22572 0.51813 -0.06428 -0.05203 -0.06812 297 ASN A N   
2118 C CA  . ASN A 271 ? 0.35099 0.26056 0.57187 -0.06514 -0.04811 -0.06520 297 ASN A CA  
2119 C C   . ASN A 271 ? 0.34261 0.25305 0.56679 -0.06472 -0.02927 -0.05691 297 ASN A C   
2120 O O   . ASN A 271 ? 0.34967 0.26868 0.58498 -0.06266 -0.02207 -0.05278 297 ASN A O   
2121 C CB  . ASN A 271 ? 0.38083 0.29443 0.63337 -0.07122 -0.05563 -0.07134 297 ASN A CB  
2122 C CG  . ASN A 271 ? 0.41704 0.33903 0.68509 -0.07065 -0.07239 -0.07630 297 ASN A CG  
2123 O OD1 . ASN A 271 ? 0.41537 0.34721 0.69547 -0.06718 -0.07142 -0.07303 297 ASN A OD1 
2124 N ND2 . ASN A 271 ? 0.45455 0.37188 0.72242 -0.07396 -0.08859 -0.08455 297 ASN A ND2 
2125 N N   . TYR A 272 ? 0.33008 0.23068 0.54417 -0.06668 -0.02131 -0.05453 298 TYR A N   
2126 C CA  . TYR A 272 ? 0.32728 0.22544 0.53780 -0.06622 -0.00503 -0.04573 298 TYR A CA  
2127 C C   . TYR A 272 ? 0.33052 0.22883 0.51701 -0.05994 -0.00117 -0.04105 298 TYR A C   
2128 O O   . TYR A 272 ? 0.31104 0.21292 0.49978 -0.05877 0.00989  -0.03529 298 TYR A O   
2129 C CB  . TYR A 272 ? 0.34131 0.22703 0.54374 -0.06879 -0.00064 -0.04400 298 TYR A CB  
2130 C CG  . TYR A 272 ? 0.34257 0.22291 0.53929 -0.06890 0.01418  -0.03406 298 TYR A CG  
2131 C CD1 . TYR A 272 ? 0.33977 0.22214 0.55800 -0.07377 0.02484  -0.02942 298 TYR A CD1 
2132 C CD2 . TYR A 272 ? 0.35220 0.22450 0.52168 -0.06448 0.01725  -0.02918 298 TYR A CD2 
2133 C CE1 . TYR A 272 ? 0.35551 0.23054 0.56393 -0.07432 0.03818  -0.01961 298 TYR A CE1 
2134 C CE2 . TYR A 272 ? 0.35591 0.22156 0.51740 -0.06465 0.02865  -0.01980 298 TYR A CE2 
2135 C CZ  . TYR A 272 ? 0.38530 0.25157 0.56416 -0.06962 0.03908  -0.01477 298 TYR A CZ  
2136 O OH  . TYR A 272 ? 0.41912 0.27652 0.58560 -0.07020 0.05028  -0.00473 298 TYR A OH  
2137 N N   . LEU A 273 ? 0.33151 0.22524 0.49454 -0.05620 -0.00959 -0.04387 299 LEU A N   
2138 C CA  . LEU A 273 ? 0.31616 0.20993 0.45818 -0.05048 -0.00717 -0.04013 299 LEU A CA  
2139 C C   . LEU A 273 ? 0.34362 0.24825 0.49662 -0.04794 -0.00953 -0.04048 299 LEU A C   
2140 O O   . LEU A 273 ? 0.35086 0.25721 0.49462 -0.04400 -0.00337 -0.03649 299 LEU A O   
2141 C CB  . LEU A 273 ? 0.32609 0.21239 0.44343 -0.04786 -0.01486 -0.04340 299 LEU A CB  
2142 C CG  . LEU A 273 ? 0.33582 0.21120 0.43969 -0.04828 -0.01056 -0.04236 299 LEU A CG  
2143 C CD1 . LEU A 273 ? 0.33091 0.20029 0.41314 -0.04582 -0.01663 -0.04661 299 LEU A CD1 
2144 C CD2 . LEU A 273 ? 0.33910 0.21190 0.43663 -0.04626 0.00031  -0.03416 299 LEU A CD2 
2145 N N   . LEU A 274 ? 0.34599 0.25758 0.51971 -0.04998 -0.01922 -0.04562 300 LEU A N   
2146 C CA  . LEU A 274 ? 0.33713 0.25939 0.52671 -0.04734 -0.02251 -0.04615 300 LEU A CA  
2147 C C   . LEU A 274 ? 0.33031 0.26067 0.54334 -0.04850 -0.00840 -0.04289 300 LEU A C   
2148 O O   . LEU A 274 ? 0.33519 0.27436 0.56188 -0.04557 -0.00781 -0.04317 300 LEU A O   
2149 C CB  . LEU A 274 ? 0.34161 0.26831 0.54789 -0.04917 -0.03917 -0.05254 300 LEU A CB  
2150 C CG  . LEU A 274 ? 0.34544 0.26491 0.52596 -0.04692 -0.05402 -0.05555 300 LEU A CG  
2151 C CD1 . LEU A 274 ? 0.35443 0.27530 0.54845 -0.05005 -0.07132 -0.06212 300 LEU A CD1 
2152 C CD2 . LEU A 274 ? 0.34015 0.26144 0.50841 -0.04091 -0.05550 -0.05219 300 LEU A CD2 
2153 N N   . ARG A 275 ? 0.31783 0.24462 0.53583 -0.05276 0.00344  -0.03981 301 ARG A N   
2154 C CA  . ARG A 275 ? 0.31354 0.24566 0.54858 -0.05444 0.01960  -0.03602 301 ARG A CA  
2155 C C   . ARG A 275 ? 0.26459 0.19444 0.47731 -0.04947 0.02888  -0.03164 301 ARG A C   
2156 O O   . ARG A 275 ? 0.28259 0.20272 0.46524 -0.04704 0.02836  -0.02864 301 ARG A O   
2157 C CB  . ARG A 275 ? 0.32755 0.25303 0.56706 -0.06038 0.03026  -0.03221 301 ARG A CB  
2158 C CG  . ARG A 275 ? 0.34539 0.27401 0.61367 -0.06627 0.02380  -0.03688 301 ARG A CG  
2159 C CD  . ARG A 275 ? 0.35427 0.27634 0.63010 -0.07235 0.03717  -0.03181 301 ARG A CD  
2160 N NE  . ARG A 275 ? 0.38251 0.30268 0.67693 -0.07774 0.02896  -0.03638 301 ARG A NE  
2161 C CZ  . ARG A 275 ? 0.40332 0.31499 0.70261 -0.08312 0.03670  -0.03266 301 ARG A CZ  
2162 N NH1 . ARG A 275 ? 0.41377 0.32403 0.73066 -0.08762 0.02815  -0.03804 301 ARG A NH1 
2163 N NH2 . ARG A 275 ? 0.39414 0.29779 0.67897 -0.08383 0.05231  -0.02341 301 ARG A NH2 
2164 N N   . PRO A 276 ? 0.28247 0.22092 0.51037 -0.04785 0.03736  -0.03187 302 PRO A N   
2165 C CA  . PRO A 276 ? 0.29393 0.22945 0.49968 -0.04306 0.04541  -0.02904 302 PRO A CA  
2166 C C   . PRO A 276 ? 0.31924 0.24290 0.49869 -0.04459 0.05775  -0.02254 302 PRO A C   
2167 O O   . PRO A 276 ? 0.33676 0.25289 0.48735 -0.04074 0.05605  -0.02029 302 PRO A O   
2168 C CB  . PRO A 276 ? 0.28984 0.23700 0.52355 -0.04236 0.05446  -0.03172 302 PRO A CB  
2169 C CG  . PRO A 276 ? 0.28851 0.24621 0.55786 -0.04443 0.04335  -0.03685 302 PRO A CG  
2170 C CD  . PRO A 276 ? 0.28031 0.23192 0.54811 -0.04983 0.03853  -0.03595 302 PRO A CD  
2171 N N   . ASP A 277 ? 0.32476 0.24580 0.51383 -0.05031 0.06941  -0.01909 303 ASP A N   
2172 C CA  . ASP A 277 ? 0.35234 0.26038 0.51517 -0.05196 0.08054  -0.01170 303 ASP A CA  
2173 C C   . ASP A 277 ? 0.33802 0.23492 0.47714 -0.05086 0.07008  -0.00906 303 ASP A C   
2174 O O   . ASP A 277 ? 0.36041 0.24723 0.47125 -0.04860 0.07230  -0.00438 303 ASP A O   
2175 C CB  . ASP A 277 ? 0.38076 0.28723 0.56000 -0.05898 0.09511  -0.00780 303 ASP A CB  
2176 C CG  . ASP A 277 ? 0.39798 0.30764 0.60356 -0.06374 0.08776  -0.01015 303 ASP A CG  
2177 O OD1 . ASP A 277 ? 0.40751 0.30646 0.60445 -0.06715 0.08763  -0.00555 303 ASP A OD1 
2178 O OD2 . ASP A 277 ? 0.39664 0.31895 0.63227 -0.06402 0.08124  -0.01682 303 ASP A OD2 
2179 N N   . VAL A 278 ? 0.33280 0.23117 0.48376 -0.05234 0.05834  -0.01271 304 VAL A N   
2180 C CA  . VAL A 278 ? 0.31029 0.19848 0.44271 -0.05148 0.04968  -0.01155 304 VAL A CA  
2181 C C   . VAL A 278 ? 0.28591 0.17186 0.39409 -0.04525 0.04295  -0.01239 304 VAL A C   
2182 O O   . VAL A 278 ? 0.30767 0.18397 0.39339 -0.04337 0.04439  -0.00783 304 VAL A O   
2183 C CB  . VAL A 278 ? 0.31088 0.20150 0.46066 -0.05421 0.03867  -0.01746 304 VAL A CB  
2184 C CG1 . VAL A 278 ? 0.32778 0.20868 0.45889 -0.05255 0.03030  -0.01821 304 VAL A CG1 
2185 C CG2 . VAL A 278 ? 0.33589 0.22693 0.51020 -0.06092 0.04525  -0.01627 304 VAL A CG2 
2186 N N   . VAL A 279 ? 0.27738 0.17179 0.39101 -0.04210 0.03479  -0.01798 305 VAL A N   
2187 C CA  . VAL A 279 ? 0.27739 0.16944 0.37022 -0.03678 0.02821  -0.01891 305 VAL A CA  
2188 C C   . VAL A 279 ? 0.29093 0.18140 0.36945 -0.03364 0.03656  -0.01540 305 VAL A C   
2189 O O   . VAL A 279 ? 0.30091 0.18572 0.35886 -0.03009 0.03369  -0.01416 305 VAL A O   
2190 C CB  . VAL A 279 ? 0.26267 0.16225 0.36401 -0.03474 0.01683  -0.02484 305 VAL A CB  
2191 C CG1 . VAL A 279 ? 0.25606 0.16593 0.37459 -0.03324 0.01975  -0.02634 305 VAL A CG1 
2192 C CG2 . VAL A 279 ? 0.26667 0.16132 0.34614 -0.03065 0.00954  -0.02563 305 VAL A CG2 
2193 N N   . ALA A 280 ? 0.30079 0.19552 0.38996 -0.03520 0.04759  -0.01421 306 ALA A N   
2194 C CA  . ALA A 280 ? 0.31616 0.20718 0.38850 -0.03288 0.05683  -0.01150 306 ALA A CA  
2195 C C   . ALA A 280 ? 0.32073 0.19826 0.36905 -0.03409 0.06057  -0.00492 306 ALA A C   
2196 O O   . ALA A 280 ? 0.33336 0.20454 0.35931 -0.03077 0.05973  -0.00331 306 ALA A O   
2197 C CB  . ALA A 280 ? 0.32225 0.22022 0.41198 -0.03486 0.06987  -0.01250 306 ALA A CB  
2198 N N   . HIS A 281 ? 0.32837 0.20078 0.38200 -0.03885 0.06369  -0.00095 307 HIS A N   
2199 C CA  . HIS A 281 ? 0.35863 0.21701 0.39130 -0.03984 0.06456  0.00609  307 HIS A CA  
2200 C C   . HIS A 281 ? 0.35466 0.20864 0.37501 -0.03591 0.05194  0.00504  307 HIS A C   
2201 O O   . HIS A 281 ? 0.37043 0.21512 0.36951 -0.03363 0.05017  0.00899  307 HIS A O   
2202 C CB  . HIS A 281 ? 0.40153 0.25559 0.44709 -0.04572 0.06902  0.01013  307 HIS A CB  
2203 C CG  . HIS A 281 ? 0.46182 0.30025 0.48821 -0.04707 0.06993  0.01862  307 HIS A CG  
2204 N ND1 . HIS A 281 ? 0.49214 0.32035 0.49346 -0.04676 0.07660  0.02506  307 HIS A ND1 
2205 C CD2 . HIS A 281 ? 0.47212 0.30240 0.50096 -0.04873 0.06434  0.02174  307 HIS A CD2 
2206 C CE1 . HIS A 281 ? 0.50509 0.31930 0.49388 -0.04804 0.07381  0.03266  307 HIS A CE1 
2207 N NE2 . HIS A 281 ? 0.48464 0.30020 0.49142 -0.04907 0.06671  0.03075  307 HIS A NE2 
2208 N N   . ILE A 282 ? 0.33183 0.19198 0.36542 -0.03528 0.04307  -0.00059 308 ILE A N   
2209 C CA  . ILE A 282 ? 0.30890 0.16544 0.33259 -0.03194 0.03321  -0.00253 308 ILE A CA  
2210 C C   . ILE A 282 ? 0.30907 0.16626 0.31736 -0.02710 0.03121  -0.00337 308 ILE A C   
2211 O O   . ILE A 282 ? 0.32292 0.17311 0.31711 -0.02462 0.02722  -0.00141 308 ILE A O   
2212 C CB  . ILE A 282 ? 0.27406 0.13637 0.31150 -0.03262 0.02552  -0.00916 308 ILE A CB  
2213 C CG1 . ILE A 282 ? 0.27817 0.13839 0.33090 -0.03757 0.02651  -0.00917 308 ILE A CG1 
2214 C CG2 . ILE A 282 ? 0.26918 0.12763 0.29566 -0.02943 0.01799  -0.01164 308 ILE A CG2 
2215 C CD1 . ILE A 282 ? 0.27240 0.13610 0.33541 -0.03869 0.01825  -0.01651 308 ILE A CD1 
2216 N N   . SER A 283 ? 0.30412 0.16971 0.31742 -0.02566 0.03347  -0.00661 309 SER A N   
2217 C CA  . SER A 283 ? 0.30034 0.16627 0.30091 -0.02124 0.03188  -0.00794 309 SER A CA  
2218 C C   . SER A 283 ? 0.32951 0.18673 0.31106 -0.02069 0.03742  -0.00332 309 SER A C   
2219 O O   . SER A 283 ? 0.31685 0.16962 0.28374 -0.01742 0.03312  -0.00332 309 SER A O   
2220 C CB  . SER A 283 ? 0.29503 0.17112 0.30793 -0.01981 0.03346  -0.01231 309 SER A CB  
2221 O OG  . SER A 283 ? 0.29497 0.17633 0.31665 -0.01866 0.02433  -0.01632 309 SER A OG  
2222 N N   . ASP A 284 ? 0.34856 0.20243 0.32942 -0.02420 0.04688  0.00065  310 ASP A N   
2223 C CA  . ASP A 284 ? 0.41009 0.25277 0.36814 -0.02444 0.05183  0.00587  310 ASP A CA  
2224 C C   . ASP A 284 ? 0.45657 0.28853 0.40129 -0.02346 0.04296  0.01031  310 ASP A C   
2225 O O   . ASP A 284 ? 0.47863 0.30217 0.40299 -0.02137 0.04017  0.01258  310 ASP A O   
2226 C CB  . ASP A 284 ? 0.42286 0.26227 0.38224 -0.02942 0.06458  0.01026  310 ASP A CB  
2227 C CG  . ASP A 284 ? 0.43539 0.28468 0.40786 -0.03006 0.07529  0.00563  310 ASP A CG  
2228 O OD1 . ASP A 284 ? 0.44133 0.29678 0.41447 -0.02606 0.07321  0.00002  310 ASP A OD1 
2229 O OD2 . ASP A 284 ? 0.47157 0.32239 0.45586 -0.03462 0.08604  0.00753  310 ASP A OD2 
2230 N N   . HIS A 285 ? 0.46048 0.29236 0.41774 -0.02489 0.03796  0.01104  311 HIS A N   
2231 C CA  . HIS A 285 ? 0.46810 0.29030 0.41749 -0.02360 0.02970  0.01474  311 HIS A CA  
2232 C C   . HIS A 285 ? 0.43885 0.26415 0.38773 -0.01915 0.02055  0.00992  311 HIS A C   
2233 O O   . HIS A 285 ? 0.43368 0.25178 0.37006 -0.01665 0.01477  0.01217  311 HIS A O   
2234 C CB  . HIS A 285 ? 0.52301 0.34292 0.48716 -0.02664 0.02855  0.01649  311 HIS A CB  
2235 C CG  . HIS A 285 ? 0.57499 0.38577 0.53633 -0.02485 0.02006  0.01938  311 HIS A CG  
2236 N ND1 . HIS A 285 ? 0.60516 0.40280 0.55148 -0.02482 0.01797  0.02749  311 HIS A ND1 
2237 C CD2 . HIS A 285 ? 0.57347 0.38596 0.54582 -0.02295 0.01316  0.01505  311 HIS A CD2 
2238 C CE1 . HIS A 285 ? 0.60246 0.39499 0.55400 -0.02259 0.00915  0.02806  311 HIS A CE1 
2239 N NE2 . HIS A 285 ? 0.59033 0.39203 0.55821 -0.02150 0.00720  0.02016  311 HIS A NE2 
2240 N N   . VAL A 286 ? 0.40740 0.24265 0.36976 -0.01839 0.01882  0.00351  312 VAL A N   
2241 C CA  . VAL A 286 ? 0.37076 0.20791 0.33419 -0.01518 0.01158  -0.00062 312 VAL A CA  
2242 C C   . VAL A 286 ? 0.36440 0.20496 0.31989 -0.01198 0.01058  -0.00334 312 VAL A C   
2243 O O   . VAL A 286 ? 0.32077 0.16163 0.27609 -0.00951 0.00524  -0.00594 312 VAL A O   
2244 C CB  . VAL A 286 ? 0.35440 0.19784 0.33210 -0.01633 0.00987  -0.00587 312 VAL A CB  
2245 C CG1 . VAL A 286 ? 0.33713 0.17695 0.32434 -0.01968 0.01082  -0.00450 312 VAL A CG1 
2246 C CG2 . VAL A 286 ? 0.35017 0.20280 0.33366 -0.01675 0.01216  -0.00945 312 VAL A CG2 
2247 N N   . PHE A 287 ? 0.38267 0.22553 0.33315 -0.01211 0.01636  -0.00324 313 PHE A N   
2248 C CA  . PHE A 287 ? 0.39863 0.24386 0.34243 -0.00904 0.01599  -0.00639 313 PHE A CA  
2249 C C   . PHE A 287 ? 0.37185 0.22480 0.32628 -0.00734 0.01219  -0.01125 313 PHE A C   
2250 O O   . PHE A 287 ? 0.35609 0.20863 0.30656 -0.00462 0.00823  -0.01335 313 PHE A O   
2251 C CB  . PHE A 287 ? 0.44809 0.28474 0.37638 -0.00683 0.01093  -0.00471 313 PHE A CB  
2252 C CG  . PHE A 287 ? 0.51868 0.34658 0.42945 -0.00798 0.01500  -0.00054 313 PHE A CG  
2253 C CD1 . PHE A 287 ? 0.53428 0.36091 0.43280 -0.00682 0.01923  -0.00291 313 PHE A CD1 
2254 C CD2 . PHE A 287 ? 0.55285 0.37243 0.45813 -0.01042 0.01496  0.00573  313 PHE A CD2 
2255 C CE1 . PHE A 287 ? 0.55998 0.37671 0.43811 -0.00839 0.02400  0.00062  313 PHE A CE1 
2256 C CE2 . PHE A 287 ? 0.56685 0.37615 0.45204 -0.01199 0.01890  0.01054  313 PHE A CE2 
2257 C CZ  . PHE A 287 ? 0.58040 0.38804 0.45050 -0.01115 0.02377  0.00784  313 PHE A CZ  
2258 N N   . TYR A 288 ? 0.36719 0.22620 0.33466 -0.00925 0.01291  -0.01280 314 TYR A N   
2259 C CA  . TYR A 288 ? 0.33182 0.19691 0.30706 -0.00818 0.00913  -0.01657 314 TYR A CA  
2260 C C   . TYR A 288 ? 0.28879 0.16142 0.27607 -0.00896 0.01229  -0.01810 314 TYR A C   
2261 O O   . TYR A 288 ? 0.29680 0.17097 0.29115 -0.01172 0.01713  -0.01684 314 TYR A O   
2262 C CB  . TYR A 288 ? 0.40885 0.27306 0.38801 -0.00984 0.00470  -0.01790 314 TYR A CB  
2263 C CG  . TYR A 288 ? 0.48638 0.34551 0.45897 -0.00843 0.00141  -0.01827 314 TYR A CG  
2264 C CD1 . TYR A 288 ? 0.51619 0.37612 0.48712 -0.00713 -0.00156 -0.02064 314 TYR A CD1 
2265 C CD2 . TYR A 288 ? 0.50584 0.35896 0.47551 -0.00855 0.00129  -0.01597 314 TYR A CD2 
2266 C CE1 . TYR A 288 ? 0.54076 0.39657 0.50874 -0.00631 -0.00294 -0.02132 314 TYR A CE1 
2267 C CE2 . TYR A 288 ? 0.53107 0.38060 0.49964 -0.00718 -0.00164 -0.01689 314 TYR A CE2 
2268 C CZ  . TYR A 288 ? 0.55239 0.40375 0.52089 -0.00623 -0.00295 -0.01988 314 TYR A CZ  
2269 O OH  . TYR A 288 ? 0.56298 0.41124 0.53322 -0.00530 -0.00428 -0.02110 314 TYR A OH  
2270 N N   . ALA A 289 ? 0.24803 0.12514 0.23972 -0.00659 0.00940  -0.02064 315 ALA A N   
2271 C CA  . ALA A 289 ? 0.24654 0.13150 0.25419 -0.00687 0.01021  -0.02249 315 ALA A CA  
2272 C C   . ALA A 289 ? 0.25842 0.14588 0.27525 -0.00961 0.00437  -0.02346 315 ALA A C   
2273 O O   . ALA A 289 ? 0.24932 0.13328 0.25899 -0.00980 -0.00189 -0.02402 315 ALA A O   
2274 C CB  . ALA A 289 ? 0.25851 0.14634 0.26933 -0.00310 0.00739  -0.02452 315 ALA A CB  
2275 N N   . ASN A 290 ? 0.28031 0.17329 0.31295 -0.01209 0.00693  -0.02411 316 ASN A N   
2276 C CA  . ASN A 290 ? 0.29428 0.18972 0.33719 -0.01491 0.00018  -0.02600 316 ASN A CA  
2277 C C   . ASN A 290 ? 0.29168 0.19371 0.34811 -0.01321 -0.00715 -0.02829 316 ASN A C   
2278 O O   . ASN A 290 ? 0.30302 0.20865 0.36485 -0.00989 -0.00537 -0.02846 316 ASN A O   
2279 C CB  . ASN A 290 ? 0.24701 0.14423 0.30224 -0.01915 0.00574  -0.02549 316 ASN A CB  
2280 C CG  . ASN A 290 ? 0.24845 0.15279 0.32057 -0.01940 0.01406  -0.02543 316 ASN A CG  
2281 O OD1 . ASN A 290 ? 0.25960 0.17208 0.35160 -0.01919 0.01070  -0.02815 316 ASN A OD1 
2282 N ND2 . ASN A 290 ? 0.25371 0.15442 0.31813 -0.01997 0.02502  -0.02243 316 ASN A ND2 
2283 N N   . ALA A 291 ? 0.26634 0.16905 0.32824 -0.01546 -0.01629 -0.03032 317 ALA A N   
2284 C CA  . ALA A 291 ? 0.26347 0.17070 0.33689 -0.01403 -0.02663 -0.03192 317 ALA A CA  
2285 C C   . ALA A 291 ? 0.26511 0.18212 0.36771 -0.01561 -0.02678 -0.03399 317 ALA A C   
2286 O O   . ALA A 291 ? 0.26339 0.18432 0.37932 -0.01504 -0.03793 -0.03567 317 ALA A O   
2287 C CB  . ALA A 291 ? 0.28897 0.18966 0.34859 -0.01571 -0.03818 -0.03315 317 ALA A CB  
2288 N N   . ASN A 292 ? 0.27793 0.19841 0.39121 -0.01774 -0.01492 -0.03365 318 ASN A N   
2289 C CA  . ASN A 292 ? 0.29978 0.22982 0.44354 -0.02002 -0.01230 -0.03571 318 ASN A CA  
2290 C C   . ASN A 292 ? 0.32236 0.25901 0.47998 -0.01672 -0.00281 -0.03586 318 ASN A C   
2291 O O   . ASN A 292 ? 0.31428 0.24814 0.46155 -0.01643 0.01056  -0.03404 318 ASN A O   
2292 C CB  . ASN A 292 ? 0.29025 0.21868 0.43751 -0.02526 -0.00377 -0.03496 318 ASN A CB  
2293 C CG  . ASN A 292 ? 0.27996 0.21762 0.46063 -0.02893 -0.00375 -0.03769 318 ASN A CG  
2294 O OD1 . ASN A 292 ? 0.24730 0.19388 0.45118 -0.02781 0.00199  -0.03881 318 ASN A OD1 
2295 N ND2 . ASN A 292 ? 0.28155 0.21712 0.46681 -0.03344 -0.00984 -0.03945 318 ASN A ND2 
2296 N N   . LYS A 293 ? 0.33509 0.27969 0.51589 -0.01418 -0.01015 -0.03834 319 LYS A N   
2297 C CA  . LYS A 293 ? 0.35005 0.30125 0.54766 -0.01064 -0.00102 -0.03981 319 LYS A CA  
2298 C C   . LYS A 293 ? 0.35144 0.30864 0.56825 -0.01410 0.01571  -0.04097 319 LYS A C   
2299 O O   . LYS A 293 ? 0.36013 0.31601 0.57042 -0.01305 0.03078  -0.04082 319 LYS A O   
2300 C CB  . LYS A 293 ? 0.37758 0.33594 0.60018 -0.00705 -0.01413 -0.04215 319 LYS A CB  
2301 C CG  . LYS A 293 ? 0.42374 0.38985 0.67002 -0.00304 -0.00479 -0.04493 319 LYS A CG  
2302 C CD  . LYS A 293 ? 0.46145 0.42863 0.71730 0.00260  -0.01919 -0.04528 319 LYS A CD  
2303 C CE  . LYS A 293 ? 0.48679 0.45765 0.75588 0.00749  -0.00816 -0.04810 319 LYS A CE  
2304 N NZ  . LYS A 293 ? 0.49798 0.46373 0.75992 0.01314  -0.02014 -0.04657 319 LYS A NZ  
2305 N N   . ALA A 294 ? 0.34558 0.30838 0.58509 -0.01870 0.01362  -0.04226 320 ALA A N   
2306 C CA  . ALA A 294 ? 0.35941 0.32769 0.61969 -0.02289 0.03033  -0.04292 320 ALA A CA  
2307 C C   . ALA A 294 ? 0.34574 0.30403 0.57740 -0.02564 0.04547  -0.03863 320 ALA A C   
2308 O O   . ALA A 294 ? 0.33920 0.29909 0.57914 -0.02824 0.06296  -0.03821 320 ALA A O   
2309 C CB  . ALA A 294 ? 0.36497 0.33949 0.65323 -0.02799 0.02349  -0.04483 320 ALA A CB  
2310 N N   . ALA A 295 ? 0.32949 0.27691 0.52793 -0.02521 0.03921  -0.03531 321 ALA A N   
2311 C CA  . ALA A 295 ? 0.32660 0.26350 0.49791 -0.02733 0.05047  -0.03068 321 ALA A CA  
2312 C C   . ALA A 295 ? 0.33732 0.26937 0.48741 -0.02339 0.05904  -0.02993 321 ALA A C   
2313 O O   . ALA A 295 ? 0.36294 0.28640 0.49233 -0.02522 0.06984  -0.02622 321 ALA A O   
2314 C CB  . ALA A 295 ? 0.30336 0.23102 0.45201 -0.02831 0.04006  -0.02814 321 ALA A CB  
2315 N N   . THR A 296 ? 0.31934 0.25558 0.47359 -0.01814 0.05366  -0.03330 322 THR A N   
2316 C CA  . THR A 296 ? 0.33431 0.26491 0.46748 -0.01426 0.05987  -0.03355 322 THR A CA  
2317 C C   . THR A 296 ? 0.36157 0.29048 0.49243 -0.01618 0.07940  -0.03383 322 THR A C   
2318 O O   . THR A 296 ? 0.37525 0.29344 0.47604 -0.01625 0.08523  -0.03119 322 THR A O   
2319 C CB  . THR A 296 ? 0.30063 0.23654 0.44489 -0.00858 0.05127  -0.03744 322 THR A CB  
2320 O OG1 . THR A 296 ? 0.27837 0.21149 0.41358 -0.00714 0.03435  -0.03590 322 THR A OG1 
2321 C CG2 . THR A 296 ? 0.30185 0.23243 0.42869 -0.00481 0.05889  -0.03910 322 THR A CG2 
2322 N N   . PRO A 297 ? 0.35175 0.28978 0.51184 -0.01801 0.09030  -0.03696 323 PRO A N   
2323 C CA  . PRO A 297 ? 0.34776 0.28216 0.50123 -0.02048 0.11139  -0.03723 323 PRO A CA  
2324 C C   . PRO A 297 ? 0.34686 0.27055 0.47798 -0.02628 0.11922  -0.03051 323 PRO A C   
2325 O O   . PRO A 297 ? 0.34015 0.25528 0.45080 -0.02816 0.13452  -0.02899 323 PRO A O   
2326 C CB  . PRO A 297 ? 0.36501 0.31320 0.56165 -0.02167 0.12046  -0.04226 323 PRO A CB  
2327 C CG  . PRO A 297 ? 0.36352 0.32194 0.58639 -0.01771 0.10174  -0.04537 323 PRO A CG  
2328 C CD  . PRO A 297 ? 0.34137 0.29297 0.54227 -0.01805 0.08447  -0.04070 323 PRO A CD  
2329 N N   . LEU A 298 ? 0.33821 0.26082 0.47146 -0.02922 0.10904  -0.02649 324 LEU A N   
2330 C CA  . LEU A 298 ? 0.32222 0.23396 0.43702 -0.03451 0.11478  -0.01954 324 LEU A CA  
2331 C C   . LEU A 298 ? 0.34133 0.23935 0.41748 -0.03249 0.10731  -0.01499 324 LEU A C   
2332 O O   . LEU A 298 ? 0.37465 0.26112 0.43068 -0.03607 0.11265  -0.00860 324 LEU A O   
2333 C CB  . LEU A 298 ? 0.30540 0.22178 0.44295 -0.03867 0.10743  -0.01819 324 LEU A CB  
2334 C CG  . LEU A 298 ? 0.35792 0.28224 0.52870 -0.04428 0.11987  -0.01906 324 LEU A CG  
2335 C CD1 . LEU A 298 ? 0.35124 0.28857 0.55076 -0.04197 0.12729  -0.02593 324 LEU A CD1 
2336 C CD2 . LEU A 298 ? 0.36559 0.29479 0.55950 -0.04756 0.10806  -0.01943 324 LEU A CD2 
2337 N N   . VAL A 299 ? 0.32518 0.22383 0.39213 -0.02699 0.09481  -0.01781 325 VAL A N   
2338 C CA  . VAL A 299 ? 0.35390 0.24074 0.38847 -0.02487 0.08763  -0.01437 325 VAL A CA  
2339 C C   . VAL A 299 ? 0.39410 0.27087 0.40249 -0.02489 0.09932  -0.01292 325 VAL A C   
2340 O O   . VAL A 299 ? 0.40316 0.28348 0.41686 -0.02418 0.11073  -0.01724 325 VAL A O   
2341 C CB  . VAL A 299 ? 0.35240 0.24288 0.38657 -0.01948 0.07322  -0.01812 325 VAL A CB  
2342 C CG1 . VAL A 299 ? 0.35890 0.23829 0.36408 -0.01739 0.06608  -0.01523 325 VAL A CG1 
2343 C CG2 . VAL A 299 ? 0.27978 0.17807 0.33514 -0.02001 0.06182  -0.01955 325 VAL A CG2 
2344 N N   . SER A 300 ? 0.40486 0.26820 0.38479 -0.02578 0.09630  -0.00710 326 SER A N   
2345 C CA  . SER A 300 ? 0.43346 0.28437 0.38275 -0.02601 0.10453  -0.00522 326 SER A CA  
2346 C C   . SER A 300 ? 0.45195 0.30514 0.39533 -0.02100 0.10373  -0.01234 326 SER A C   
2347 O O   . SER A 300 ? 0.47641 0.33621 0.42972 -0.01675 0.09198  -0.01614 326 SER A O   
2348 C CB  . SER A 300 ? 0.46457 0.30113 0.38656 -0.02646 0.09546  0.00188  326 SER A CB  
2349 O OG  . SER A 300 ? 0.49839 0.33444 0.41244 -0.02150 0.08144  -0.00079 326 SER A OG  
2350 N N   . ALA A 301 ? 0.47316 0.31969 0.39938 -0.02183 0.11711  -0.01428 327 ALA A N   
2351 C CA  . ALA A 301 ? 0.49571 0.34227 0.41426 -0.01732 0.11740  -0.02175 327 ALA A CA  
2352 C C   . ALA A 301 ? 0.50677 0.34534 0.40351 -0.01381 0.10163  -0.02104 327 ALA A C   
2353 O O   . ALA A 301 ? 0.50060 0.34209 0.39961 -0.00941 0.09660  -0.02731 327 ALA A O   
2354 C CB  . ALA A 301 ? 0.53312 0.37125 0.43241 -0.01959 0.13581  -0.02428 327 ALA A CB  
2355 N N   . GLU A 302 ? 0.52255 0.35103 0.40079 -0.01566 0.09363  -0.01358 328 GLU A N   
2356 C CA  . GLU A 302 ? 0.54416 0.36621 0.40705 -0.01246 0.07802  -0.01295 328 GLU A CA  
2357 C C   . GLU A 302 ? 0.46989 0.30359 0.35708 -0.00898 0.06622  -0.01588 328 GLU A C   
2358 O O   . GLU A 302 ? 0.46979 0.30289 0.35314 -0.00532 0.05751  -0.01954 328 GLU A O   
2359 C CB  . GLU A 302 ? 0.61234 0.42202 0.45615 -0.01507 0.07169  -0.00406 328 GLU A CB  
2360 C CG  . GLU A 302 ? 0.66950 0.47122 0.49755 -0.01207 0.05599  -0.00325 328 GLU A CG  
2361 C CD  . GLU A 302 ? 0.73748 0.52849 0.55403 -0.01411 0.04818  0.00575  328 GLU A CD  
2362 O OE1 . GLU A 302 ? 0.75083 0.54214 0.57545 -0.01765 0.05391  0.01122  328 GLU A OE1 
2363 O OE2 . GLU A 302 ? 0.77476 0.55691 0.57628 -0.01214 0.03580  0.00726  328 GLU A OE2 
2364 N N   . VAL A 303 ? 0.42987 0.27326 0.34125 -0.01043 0.06589  -0.01438 329 VAL A N   
2365 C CA  . VAL A 303 ? 0.38508 0.23770 0.31592 -0.00785 0.05518  -0.01664 329 VAL A CA  
2366 C C   . VAL A 303 ? 0.36700 0.23096 0.31952 -0.00565 0.05851  -0.02266 329 VAL A C   
2367 O O   . VAL A 303 ? 0.34192 0.20952 0.30073 -0.00214 0.05059  -0.02586 329 VAL A O   
2368 C CB  . VAL A 303 ? 0.40051 0.25537 0.34284 -0.01065 0.05076  -0.01220 329 VAL A CB  
2369 C CG1 . VAL A 303 ? 0.37435 0.23714 0.33294 -0.00857 0.04073  -0.01489 329 VAL A CG1 
2370 C CG2 . VAL A 303 ? 0.42485 0.26804 0.34866 -0.01211 0.04628  -0.00620 329 VAL A CG2 
2371 N N   . ARG A 304 ? 0.38317 0.25245 0.34883 -0.00773 0.07026  -0.02401 330 ARG A N   
2372 C CA  . ARG A 304 ? 0.36842 0.24932 0.36021 -0.00549 0.07237  -0.02954 330 ARG A CA  
2373 C C   . ARG A 304 ? 0.37298 0.25249 0.35944 -0.00111 0.07361  -0.03538 330 ARG A C   
2374 O O   . ARG A 304 ? 0.35553 0.24192 0.35924 0.00245  0.06748  -0.03891 330 ARG A O   
2375 C CB  . ARG A 304 ? 0.37302 0.25993 0.38277 -0.00892 0.08600  -0.03015 330 ARG A CB  
2376 C CG  . ARG A 304 ? 0.41590 0.31328 0.45178 -0.00624 0.09176  -0.03690 330 ARG A CG  
2377 C CD  . ARG A 304 ? 0.45742 0.36262 0.51786 -0.01008 0.10434  -0.03751 330 ARG A CD  
2378 N NE  . ARG A 304 ? 0.48545 0.38183 0.52740 -0.01547 0.11625  -0.03265 330 ARG A NE  
2379 C CZ  . ARG A 304 ? 0.50918 0.39763 0.53247 -0.01693 0.13184  -0.03378 330 ARG A CZ  
2380 N NH1 . ARG A 304 ? 0.51800 0.40700 0.54024 -0.01322 0.13786  -0.04083 330 ARG A NH1 
2381 N NH2 . ARG A 304 ? 0.52881 0.40751 0.53330 -0.02226 0.14153  -0.02786 330 ARG A NH2 
2382 N N   . GLU A 305 ? 0.38501 0.25442 0.34675 -0.00140 0.08077  -0.03643 331 GLU A N   
2383 C CA  . GLU A 305 ? 0.43330 0.30007 0.38895 0.00236  0.08318  -0.04322 331 GLU A CA  
2384 C C   . GLU A 305 ? 0.41550 0.27573 0.35576 0.00521  0.06982  -0.04330 331 GLU A C   
2385 O O   . GLU A 305 ? 0.41538 0.27176 0.34878 0.00812  0.07045  -0.04908 331 GLU A O   
2386 C CB  . GLU A 305 ? 0.51637 0.37445 0.45153 0.00025  0.09869  -0.04578 331 GLU A CB  
2387 C CG  . GLU A 305 ? 0.58395 0.44916 0.53821 -0.00247 0.11519  -0.04735 331 GLU A CG  
2388 C CD  . GLU A 305 ? 0.67373 0.52965 0.60692 -0.00448 0.13295  -0.05127 331 GLU A CD  
2389 O OE1 . GLU A 305 ? 0.71716 0.55839 0.61390 -0.00590 0.13185  -0.04900 331 GLU A OE1 
2390 O OE2 . GLU A 305 ? 0.70703 0.56983 0.66011 -0.00472 0.14797  -0.05685 331 GLU A OE2 
2391 N N   . ASN A 306 ? 0.38094 0.23978 0.31749 0.00431  0.05842  -0.03769 332 ASN A N   
2392 C CA  . ASN A 306 ? 0.37974 0.23413 0.30784 0.00672  0.04616  -0.03780 332 ASN A CA  
2393 C C   . ASN A 306 ? 0.37557 0.23822 0.32545 0.00976  0.03966  -0.04002 332 ASN A C   
2394 O O   . ASN A 306 ? 0.34114 0.21024 0.30549 0.00886  0.03519  -0.03689 332 ASN A O   
2395 C CB  . ASN A 306 ? 0.38908 0.23883 0.30743 0.00453  0.03805  -0.03141 332 ASN A CB  
2396 C CG  . ASN A 306 ? 0.40461 0.24854 0.31347 0.00651  0.02708  -0.03186 332 ASN A CG  
2397 O OD1 . ASN A 306 ? 0.41176 0.25748 0.32705 0.00934  0.02339  -0.03595 332 ASN A OD1 
2398 N ND2 . ASN A 306 ? 0.40646 0.24323 0.30225 0.00497  0.02159  -0.02748 332 ASN A ND2 
2399 N N   . PRO A 307 ? 0.39512 0.25655 0.34677 0.01318  0.03853  -0.04527 333 PRO A N   
2400 C CA  . PRO A 307 ? 0.38111 0.24863 0.35264 0.01600  0.03196  -0.04620 333 PRO A CA  
2401 C C   . PRO A 307 ? 0.37282 0.23914 0.34295 0.01548  0.02077  -0.04167 333 PRO A C   
2402 O O   . PRO A 307 ? 0.35628 0.22710 0.34048 0.01646  0.01535  -0.04020 333 PRO A O   
2403 C CB  . PRO A 307 ? 0.39859 0.26227 0.36916 0.01948  0.03378  -0.05284 333 PRO A CB  
2404 C CG  . PRO A 307 ? 0.41617 0.26978 0.36091 0.01823  0.03583  -0.05457 333 PRO A CG  
2405 C CD  . PRO A 307 ? 0.42522 0.27810 0.35944 0.01446  0.04229  -0.05056 333 PRO A CD  
2406 N N   . GLY A 308 ? 0.39340 0.25314 0.34710 0.01390  0.01720  -0.03944 334 GLY A N   
2407 C CA  . GLY A 308 ? 0.37162 0.23041 0.32544 0.01293  0.00894  -0.03567 334 GLY A CA  
2408 C C   . GLY A 308 ? 0.37987 0.24255 0.33829 0.01013  0.00839  -0.03136 334 GLY A C   
2409 O O   . GLY A 308 ? 0.38893 0.25089 0.34811 0.00913  0.00297  -0.02898 334 GLY A O   
2410 N N   . ILE A 309 ? 0.38981 0.25617 0.35191 0.00854  0.01468  -0.03080 335 ILE A N   
2411 C CA  . ILE A 309 ? 0.37964 0.24992 0.34878 0.00567  0.01426  -0.02762 335 ILE A CA  
2412 C C   . ILE A 309 ? 0.38568 0.26436 0.37324 0.00587  0.01587  -0.02896 335 ILE A C   
2413 O O   . ILE A 309 ? 0.36021 0.24224 0.35639 0.00504  0.01007  -0.02776 335 ILE A O   
2414 C CB  . ILE A 309 ? 0.36839 0.23484 0.32800 0.00275  0.01922  -0.02484 335 ILE A CB  
2415 C CG1 . ILE A 309 ? 0.36719 0.22475 0.30996 0.00302  0.01534  -0.02330 335 ILE A CG1 
2416 C CG2 . ILE A 309 ? 0.32480 0.19456 0.29328 -0.00036 0.01824  -0.02213 335 ILE A CG2 
2417 C CD1 . ILE A 309 ? 0.35345 0.20486 0.28470 0.00042  0.01855  -0.01939 335 ILE A CD1 
2418 N N   . TYR A 310 ? 0.38738 0.26911 0.38150 0.00690  0.02358  -0.03187 336 TYR A N   
2419 C CA  . TYR A 310 ? 0.34965 0.24017 0.36616 0.00769  0.02503  -0.03390 336 TYR A CA  
2420 C C   . TYR A 310 ? 0.34696 0.23831 0.37070 0.01206  0.02481  -0.03795 336 TYR A C   
2421 O O   . TYR A 310 ? 0.36589 0.25738 0.39114 0.01332  0.03411  -0.04202 336 TYR A O   
2422 C CB  . TYR A 310 ? 0.34418 0.23855 0.36838 0.00504  0.03609  -0.03451 336 TYR A CB  
2423 C CG  . TYR A 310 ? 0.32630 0.22303 0.35579 0.00089  0.03446  -0.03100 336 TYR A CG  
2424 C CD1 . TYR A 310 ? 0.31586 0.22126 0.36872 -0.00002 0.03112  -0.03178 336 TYR A CD1 
2425 C CD2 . TYR A 310 ? 0.29588 0.18563 0.30832 -0.00204 0.03518  -0.02719 336 TYR A CD2 
2426 C CE1 . TYR A 310 ? 0.30534 0.21227 0.36353 -0.00407 0.02911  -0.02954 336 TYR A CE1 
2427 C CE2 . TYR A 310 ? 0.30165 0.19276 0.32023 -0.00581 0.03382  -0.02456 336 TYR A CE2 
2428 C CZ  . TYR A 310 ? 0.30388 0.20352 0.34488 -0.00697 0.03107  -0.02609 336 TYR A CZ  
2429 O OH  . TYR A 310 ? 0.30420 0.20461 0.35178 -0.01097 0.02925  -0.02439 336 TYR A OH  
2430 N N   . PRO A 311 ? 0.33975 0.23059 0.36751 0.01429  0.01507  -0.03709 337 PRO A N   
2431 C CA  . PRO A 311 ? 0.36854 0.25866 0.40380 0.01855  0.01406  -0.04045 337 PRO A CA  
2432 C C   . PRO A 311 ? 0.38621 0.28467 0.44743 0.02067  0.01667  -0.04345 337 PRO A C   
2433 O O   . PRO A 311 ? 0.36513 0.27037 0.44022 0.01876  0.01579  -0.04209 337 PRO A O   
2434 C CB  . PRO A 311 ? 0.37573 0.26181 0.40715 0.01927  0.00263  -0.03681 337 PRO A CB  
2435 C CG  . PRO A 311 ? 0.35383 0.24215 0.38478 0.01594  -0.00246 -0.03279 337 PRO A CG  
2436 C CD  . PRO A 311 ? 0.35890 0.24830 0.38301 0.01270  0.00513  -0.03293 337 PRO A CD  
2437 N N   . PRO A 312 ? 0.41154 0.30981 0.48239 0.02464  0.01969  -0.04810 338 PRO A N   
2438 C CA  . PRO A 312 ? 0.42474 0.33144 0.52516 0.02730  0.02208  -0.05156 338 PRO A CA  
2439 C C   . PRO A 312 ? 0.45009 0.36009 0.56720 0.02870  0.00780  -0.04741 338 PRO A C   
2440 O O   . PRO A 312 ? 0.46721 0.37171 0.57065 0.02774  -0.00277 -0.04218 338 PRO A O   
2441 C CB  . PRO A 312 ? 0.43806 0.34127 0.54157 0.03147  0.02808  -0.05795 338 PRO A CB  
2442 C CG  . PRO A 312 ? 0.42126 0.31420 0.50042 0.03151  0.02257  -0.05616 338 PRO A CG  
2443 C CD  . PRO A 312 ? 0.42724 0.31748 0.48414 0.02683  0.02165  -0.05137 338 PRO A CD  
2444 N N   . ALA A 313 ? 0.46867 0.38727 0.61616 0.03093  0.00771  -0.04997 339 ALA A N   
2445 C CA  . ALA A 313 ? 0.47784 0.39965 0.64249 0.03201  -0.00739 -0.04591 339 ALA A CA  
2446 C C   . ALA A 313 ? 0.48771 0.40137 0.64737 0.03550  -0.01913 -0.04251 339 ALA A C   
2447 O O   . ALA A 313 ? 0.49048 0.40034 0.64400 0.03458  -0.03283 -0.03645 339 ALA A O   
2448 C CB  . ALA A 313 ? 0.47777 0.41094 0.68053 0.03415  -0.00537 -0.05002 339 ALA A CB  
2449 N N   . ASP A 314 ? 0.48739 0.39710 0.64857 0.03920  -0.01370 -0.04639 340 ASP A N   
2450 C CA  . ASP A 314 ? 0.51762 0.41870 0.67593 0.04232  -0.02408 -0.04288 340 ASP A CA  
2451 C C   . ASP A 314 ? 0.48995 0.38131 0.61649 0.03885  -0.02883 -0.03704 340 ASP A C   
2452 O O   . ASP A 314 ? 0.48188 0.36593 0.60333 0.03948  -0.03996 -0.03114 340 ASP A O   
2453 C CB  . ASP A 314 ? 0.56342 0.46194 0.73109 0.04674  -0.01624 -0.04952 340 ASP A CB  
2454 C CG  . ASP A 314 ? 0.61914 0.51321 0.76294 0.04464  -0.00387 -0.05416 340 ASP A CG  
2455 O OD1 . ASP A 314 ? 0.64514 0.53225 0.78479 0.04707  -0.00176 -0.05769 340 ASP A OD1 
2456 O OD2 . ASP A 314 ? 0.64403 0.54079 0.77345 0.04050  0.00281  -0.05420 340 ASP A OD2 
2457 N N   . VAL A 315 ? 0.45210 0.34265 0.55783 0.03511  -0.02037 -0.03836 341 VAL A N   
2458 C CA  . VAL A 315 ? 0.39330 0.27605 0.47308 0.03169  -0.02406 -0.03348 341 VAL A CA  
2459 C C   . VAL A 315 ? 0.38200 0.26605 0.45621 0.02815  -0.03159 -0.02829 341 VAL A C   
2460 O O   . VAL A 315 ? 0.37138 0.24819 0.43164 0.02649  -0.03915 -0.02300 341 VAL A O   
2461 C CB  . VAL A 315 ? 0.34217 0.22298 0.40407 0.02949  -0.01387 -0.03689 341 VAL A CB  
2462 C CG1 . VAL A 315 ? 0.31785 0.19204 0.35804 0.02603  -0.01737 -0.03239 341 VAL A CG1 
2463 C CG2 . VAL A 315 ? 0.35546 0.23286 0.41942 0.03272  -0.00794 -0.04270 341 VAL A CG2 
2464 N N   . ARG A 316 ? 0.37781 0.27037 0.46258 0.02660  -0.02903 -0.03012 342 ARG A N   
2465 C CA  . ARG A 316 ? 0.38765 0.28132 0.46840 0.02308  -0.03662 -0.02652 342 ARG A CA  
2466 C C   . ARG A 316 ? 0.37852 0.26895 0.46559 0.02460  -0.05124 -0.02209 342 ARG A C   
2467 O O   . ARG A 316 ? 0.36983 0.25497 0.44169 0.02153  -0.05930 -0.01798 342 ARG A O   
2468 C CB  . ARG A 316 ? 0.41783 0.32155 0.51415 0.02128  -0.03129 -0.02980 342 ARG A CB  
2469 C CG  . ARG A 316 ? 0.44935 0.35377 0.53376 0.01849  -0.01838 -0.03215 342 ARG A CG  
2470 C CD  . ARG A 316 ? 0.48096 0.39484 0.58479 0.01730  -0.01022 -0.03560 342 ARG A CD  
2471 N NE  . ARG A 316 ? 0.49185 0.40456 0.58147 0.01334  -0.00077 -0.03558 342 ARG A NE  
2472 C CZ  . ARG A 316 ? 0.50025 0.41395 0.58721 0.00918  -0.00293 -0.03364 342 ARG A CZ  
2473 N NH1 . ARG A 316 ? 0.49150 0.40290 0.56632 0.00594  0.00553  -0.03304 342 ARG A NH1 
2474 N NH2 . ARG A 316 ? 0.51256 0.42845 0.60840 0.00821  -0.01431 -0.03231 342 ARG A NH2 
2475 N N   . ALA A 317 ? 0.36914 0.26156 0.47768 0.02930  -0.05502 -0.02291 343 ALA A N   
2476 C CA  . ALA A 317 ? 0.37711 0.26479 0.49168 0.03121  -0.07067 -0.01767 343 ALA A CA  
2477 C C   . ALA A 317 ? 0.40494 0.27889 0.49491 0.03051  -0.07563 -0.01156 343 ALA A C   
2478 O O   . ALA A 317 ? 0.42310 0.28965 0.50794 0.03052  -0.08898 -0.00545 343 ALA A O   
2479 C CB  . ALA A 317 ? 0.36982 0.26295 0.51721 0.03697  -0.07318 -0.02027 343 ALA A CB  
2480 N N   . LYS A 318 ? 0.40061 0.27032 0.47528 0.02963  -0.06548 -0.01289 344 LYS A N   
2481 C CA  . LYS A 318 ? 0.39103 0.24828 0.44502 0.02837  -0.06783 -0.00762 344 LYS A CA  
2482 C C   . LYS A 318 ? 0.35815 0.21138 0.38630 0.02296  -0.06349 -0.00628 344 LYS A C   
2483 O O   . LYS A 318 ? 0.35363 0.19737 0.36531 0.02120  -0.06226 -0.00284 344 LYS A O   
2484 C CB  . LYS A 318 ? 0.38698 0.24157 0.44639 0.03145  -0.06092 -0.01044 344 LYS A CB  
2485 C CG  . LYS A 318 ? 0.40867 0.26418 0.49319 0.03709  -0.06571 -0.01138 344 LYS A CG  
2486 C CD  . LYS A 318 ? 0.43226 0.28297 0.51986 0.03969  -0.05942 -0.01463 344 LYS A CD  
2487 C CE  . LYS A 318 ? 0.44745 0.29837 0.56205 0.04561  -0.06388 -0.01618 344 LYS A CE  
2488 N NZ  . LYS A 318 ? 0.44053 0.30419 0.57943 0.04840  -0.05957 -0.02317 344 LYS A NZ  
2489 N N   . LEU A 319 ? 0.34617 0.20624 0.37258 0.02023  -0.06056 -0.00915 345 LEU A N   
2490 C CA  . LEU A 319 ? 0.33594 0.19209 0.34065 0.01538  -0.05703 -0.00838 345 LEU A CA  
2491 C C   . LEU A 319 ? 0.36608 0.21306 0.35441 0.01258  -0.06669 -0.00298 345 LEU A C   
2492 O O   . LEU A 319 ? 0.35558 0.20123 0.35025 0.01397  -0.07803 -0.00008 345 LEU A O   
2493 C CB  . LEU A 319 ? 0.31576 0.18079 0.32473 0.01332  -0.05155 -0.01285 345 LEU A CB  
2494 C CG  . LEU A 319 ? 0.30400 0.17504 0.31970 0.01453  -0.04036 -0.01753 345 LEU A CG  
2495 C CD1 . LEU A 319 ? 0.28480 0.16320 0.30532 0.01215  -0.03603 -0.02038 345 LEU A CD1 
2496 C CD2 . LEU A 319 ? 0.29792 0.16276 0.29843 0.01349  -0.03446 -0.01738 345 LEU A CD2 
2497 N N   . PHE A 320 ? 0.38141 0.22131 0.34819 0.00852  -0.06220 -0.00183 346 PHE A N   
2498 C CA  . PHE A 320 ? 0.40546 0.23456 0.35109 0.00500  -0.06886 0.00264  346 PHE A CA  
2499 C C   . PHE A 320 ? 0.38489 0.21150 0.31334 0.00026  -0.06070 0.00002  346 PHE A C   
2500 O O   . PHE A 320 ? 0.34334 0.17422 0.27545 0.00007  -0.05053 -0.00343 346 PHE A O   
2501 C CB  . PHE A 320 ? 0.44417 0.26108 0.37966 0.00552  -0.07194 0.00929  346 PHE A CB  
2502 C CG  . PHE A 320 ? 0.46075 0.27454 0.39269 0.00489  -0.06069 0.00901  346 PHE A CG  
2503 C CD1 . PHE A 320 ? 0.46755 0.27354 0.37968 0.00021  -0.05346 0.00991  346 PHE A CD1 
2504 C CD2 . PHE A 320 ? 0.45208 0.27053 0.40176 0.00885  -0.05729 0.00711  346 PHE A CD2 
2505 C CE1 . PHE A 320 ? 0.47318 0.27715 0.38636 -0.00047 -0.04378 0.00932  346 PHE A CE1 
2506 C CE2 . PHE A 320 ? 0.45595 0.27143 0.40390 0.00808  -0.04864 0.00631  346 PHE A CE2 
2507 C CZ  . PHE A 320 ? 0.46644 0.27516 0.39763 0.00344  -0.04227 0.00763  346 PHE A CZ  
2508 N N   . THR A 321 ? 0.41018 0.22908 0.31986 -0.00350 -0.06585 0.00137  347 THR A N   
2509 C CA  . THR A 321 ? 0.46257 0.27706 0.35481 -0.00817 -0.05799 -0.00156 347 THR A CA  
2510 C C   . THR A 321 ? 0.49290 0.29235 0.36002 -0.01147 -0.05587 0.00306  347 THR A C   
2511 O O   . THR A 321 ? 0.51237 0.30346 0.37230 -0.01066 -0.06328 0.00941  347 THR A O   
2512 C CB  . THR A 321 ? 0.50161 0.31824 0.39049 -0.01073 -0.06351 -0.00554 347 THR A CB  
2513 O OG1 . THR A 321 ? 0.52485 0.33575 0.40683 -0.01082 -0.07801 -0.00202 347 THR A OG1 
2514 C CG2 . THR A 321 ? 0.49566 0.32659 0.40914 -0.00860 -0.06174 -0.01019 347 THR A CG2 
2515 N N   . LEU A 322 ? 0.50835 0.30380 0.36288 -0.01532 -0.04506 -0.00002 348 LEU A N   
2516 C CA  . LEU A 322 ? 0.58030 0.36171 0.41190 -0.01921 -0.03872 0.00345  348 LEU A CA  
2517 C C   . LEU A 322 ? 0.62834 0.39781 0.43198 -0.02351 -0.04469 0.00407  348 LEU A C   
2518 O O   . LEU A 322 ? 0.62111 0.39167 0.41866 -0.02616 -0.04232 -0.00218 348 LEU A O   
2519 C CB  . LEU A 322 ? 0.59007 0.37339 0.42512 -0.02118 -0.02334 -0.00106 348 LEU A CB  
2520 C CG  . LEU A 322 ? 0.63404 0.40521 0.45358 -0.02494 -0.01305 0.00213  348 LEU A CG  
2521 C CD1 . LEU A 322 ? 0.63164 0.40347 0.46488 -0.02225 -0.01205 0.00699  348 LEU A CD1 
2522 C CD2 . LEU A 322 ? 0.63028 0.40261 0.45092 -0.02797 0.00109  -0.00437 348 LEU A CD2 
2523 N N   . LYS A 323 ? 0.66834 0.42520 0.45402 -0.02431 -0.05306 0.01157  349 LYS A N   
2524 C CA  . LYS A 323 ? 0.72616 0.46841 0.47939 -0.02894 -0.05930 0.01275  349 LYS A CA  
2525 C C   . LYS A 323 ? 0.71103 0.44061 0.43847 -0.03476 -0.04357 0.01167  349 LYS A C   
2526 O O   . LYS A 323 ? 0.69062 0.41836 0.42211 -0.03522 -0.03142 0.01424  349 LYS A O   
2527 C CB  . LYS A 323 ? 0.81298 0.54395 0.55356 -0.02789 -0.07520 0.02220  349 LYS A CB  
2528 C CG  . LYS A 323 ? 0.84399 0.58658 0.61294 -0.02182 -0.09079 0.02376  349 LYS A CG  
2529 C CD  . LYS A 323 ? 0.89354 0.62553 0.65826 -0.01960 -0.10134 0.03435  349 LYS A CD  
2530 C CE  . LYS A 323 ? 0.90551 0.64749 0.69880 -0.01354 -0.11770 0.03573  349 LYS A CE  
2531 N NZ  . LYS A 323 ? 0.96962 0.69691 0.75159 -0.01229 -0.13303 0.04638  349 LYS A NZ  
2532 N N   . VAL A 324 ? 0.72895 0.44964 0.43090 -0.03943 -0.04340 0.00710  350 VAL A N   
2533 C CA  . VAL A 324 ? 0.75173 0.45846 0.42603 -0.04551 -0.02767 0.00530  350 VAL A CA  
2534 C C   . VAL A 324 ? 0.80930 0.49676 0.45411 -0.04842 -0.02939 0.01579  350 VAL A C   
2535 O O   . VAL A 324 ? 0.84270 0.52007 0.46854 -0.04849 -0.04623 0.02178  350 VAL A O   
2536 C CB  . VAL A 324 ? 0.76039 0.46162 0.41401 -0.04972 -0.02747 -0.00349 350 VAL A CB  
2537 C CG1 . VAL A 324 ? 0.78589 0.47023 0.40707 -0.05640 -0.01052 -0.00558 350 VAL A CG1 
2538 C CG2 . VAL A 324 ? 0.71323 0.43236 0.39749 -0.04715 -0.02391 -0.01315 350 VAL A CG2 
2539 N N   . GLN A 325 ? 0.84558 0.52736 0.48762 -0.05095 -0.01252 0.01845  351 GLN A N   
2540 C CA  . GLN A 325 ? 0.92789 0.59148 0.54579 -0.05382 -0.01188 0.02958  351 GLN A CA  
2541 C C   . GLN A 325 ? 1.07462 0.71672 0.64758 -0.06187 -0.00097 0.02934  351 GLN A C   
2542 O O   . GLN A 325 ? 1.08334 0.72647 0.65111 -0.06528 0.01318  0.01950  351 GLN A O   
2543 C CB  . GLN A 325 ? 0.86520 0.53419 0.50799 -0.05233 0.00023  0.03333  351 GLN A CB  
2544 C CG  . GLN A 325 ? 0.78492 0.46880 0.46341 -0.04492 -0.01186 0.03623  351 GLN A CG  
2545 C CD  . GLN A 325 ? 0.76308 0.43683 0.43084 -0.04277 -0.03023 0.04693  351 GLN A CD  
2546 O OE1 . GLN A 325 ? 0.78886 0.44210 0.42191 -0.04717 -0.03253 0.05486  351 GLN A OE1 
2547 N NE2 . GLN A 325 ? 0.70772 0.39504 0.40525 -0.03599 -0.04331 0.04726  351 GLN A NE2 
2548 N N   . ASP A 326 ? 1.17741 0.79886 0.71726 -0.06490 -0.00761 0.04038  352 ASP A N   
2549 C CA  . ASP A 326 ? 1.27093 0.86841 0.76275 -0.07317 0.00371  0.04202  352 ASP A CA  
2550 C C   . ASP A 326 ? 1.25588 0.85185 0.75389 -0.07735 0.03144  0.04041  352 ASP A C   
2551 O O   . ASP A 326 ? 1.24175 0.84875 0.77365 -0.07417 0.03690  0.04352  352 ASP A O   
2552 C CB  . ASP A 326 ? 1.36925 0.94415 0.82536 -0.07504 -0.01158 0.05622  352 ASP A CB  
2553 C CG  . ASP A 326 ? 1.49425 1.04588 0.90865 -0.08328 0.00431  0.06048  352 ASP A CG  
2554 O OD1 . ASP A 326 ? 1.55651 1.10082 0.94416 -0.08784 0.00908  0.05262  352 ASP A OD1 
2555 O OD2 . ASP A 326 ? 1.53856 1.08484 0.95777 -0.08419 0.01207  0.06962  352 ASP A OD2 
2556 N N   . PRO A 327 ? 1.24517 0.82798 0.71285 -0.08452 0.04952  0.03451  353 PRO A N   
2557 C CA  . PRO A 327 ? 1.20804 0.79228 0.68853 -0.08839 0.07752  0.03062  353 PRO A CA  
2558 C C   . PRO A 327 ? 1.16831 0.74716 0.65834 -0.08948 0.08548  0.04214  353 PRO A C   
2559 O O   . PRO A 327 ? 1.13905 0.73143 0.66608 -0.08845 0.10033  0.03836  353 PRO A O   
2560 C CB  . PRO A 327 ? 1.26219 0.82564 0.69542 -0.09687 0.09269  0.02534  353 PRO A CB  
2561 C CG  . PRO A 327 ? 1.28513 0.84945 0.70251 -0.09515 0.07452  0.01836  353 PRO A CG  
2562 C CD  . PRO A 327 ? 1.28118 0.85230 0.71097 -0.08850 0.04556  0.02729  353 PRO A CD  
2563 N N   . LYS A 328 ? 1.15040 0.70939 0.60957 -0.09164 0.07568  0.05603  354 LYS A N   
2564 C CA  . LYS A 328 ? 1.11238 0.66835 0.58667 -0.09221 0.08275  0.06618  354 LYS A CA  
2565 C C   . LYS A 328 ? 1.00383 0.58144 0.53008 -0.08457 0.07494  0.06626  354 LYS A C   
2566 O O   . LYS A 328 ? 0.96346 0.54723 0.51818 -0.08511 0.08898  0.06684  354 LYS A O   
2567 C CB  . LYS A 328 ? 1.15802 0.69929 0.60670 -0.09257 0.06785  0.07835  354 LYS A CB  
2568 C CG  . LYS A 328 ? 1.20639 0.73359 0.61137 -0.09588 0.05951  0.07686  354 LYS A CG  
2569 C CD  . LYS A 328 ? 1.22106 0.73918 0.61204 -0.09295 0.03423  0.08917  354 LYS A CD  
2570 C CE  . LYS A 328 ? 1.25079 0.75469 0.60015 -0.09604 0.02301  0.08796  354 LYS A CE  
2571 N NZ  . LYS A 328 ? 1.24835 0.75055 0.59562 -0.09086 -0.00766 0.09602  354 LYS A NZ  
2572 N N   . ILE A 329 ? 0.96457 0.55562 0.50678 -0.07719 0.05231  0.06444  355 ILE A N   
2573 C CA  . ILE A 329 ? 0.90521 0.51885 0.49718 -0.06945 0.04493  0.06217  355 ILE A CA  
2574 C C   . ILE A 329 ? 0.90202 0.53463 0.52749 -0.06871 0.06108  0.04971  355 ILE A C   
2575 O O   . ILE A 329 ? 0.88145 0.52646 0.54331 -0.06576 0.06542  0.04883  355 ILE A O   
2576 C CB  . ILE A 329 ? 0.86450 0.48824 0.46531 -0.06237 0.01970  0.06166  355 ILE A CB  
2577 C CG1 . ILE A 329 ? 0.87794 0.48273 0.44993 -0.06256 0.00188  0.07470  355 ILE A CG1 
2578 C CG2 . ILE A 329 ? 0.80911 0.45534 0.45855 -0.05474 0.01402  0.05827  355 ILE A CG2 
2579 C CD1 . ILE A 329 ? 0.87624 0.47132 0.45474 -0.06262 0.00329  0.08668  355 ILE A CD1 
2580 N N   . ASP A 330 ? 0.92468 0.55878 0.53843 -0.07145 0.06963  0.03975  356 ASP A N   
2581 C CA  . ASP A 330 ? 0.92914 0.58007 0.57511 -0.07062 0.08416  0.02812  356 ASP A CA  
2582 C C   . ASP A 330 ? 0.93056 0.57734 0.58765 -0.07535 0.10624  0.02922  356 ASP A C   
2583 O O   . ASP A 330 ? 0.90359 0.56607 0.60106 -0.07244 0.11163  0.02490  356 ASP A O   
2584 C CB  . ASP A 330 ? 0.99312 0.64362 0.62236 -0.07297 0.08915  0.01747  356 ASP A CB  
2585 C CG  . ASP A 330 ? 1.03084 0.70281 0.69875 -0.06885 0.09313  0.00578  356 ASP A CG  
2586 O OD1 . ASP A 330 ? 1.05767 0.74325 0.74227 -0.06299 0.07718  0.00318  356 ASP A OD1 
2587 O OD2 . ASP A 330 ? 1.06765 0.74228 0.74972 -0.07163 0.11240  -0.00062 356 ASP A OD2 
2588 N N   . ARG A 331 ? 0.95019 0.57515 0.57164 -0.08294 0.11894  0.03520  357 ARG A N   
2589 C CA  . ARG A 331 ? 0.94219 0.56210 0.57443 -0.08839 0.14183  0.03660  357 ARG A CA  
2590 C C   . ARG A 331 ? 0.88420 0.50864 0.54497 -0.08547 0.13603  0.04501  357 ARG A C   
2591 O O   . ARG A 331 ? 0.85597 0.49146 0.55403 -0.08536 0.14744  0.04119  357 ARG A O   
2592 C CB  . ARG A 331 ? 1.02869 0.62164 0.61175 -0.09768 0.15667  0.04256  357 ARG A CB  
2593 C CG  . ARG A 331 ? 1.07404 0.66259 0.63992 -0.10305 0.17637  0.03114  357 ARG A CG  
2594 C CD  . ARG A 331 ? 1.09910 0.68042 0.62744 -0.10240 0.16175  0.02807  357 ARG A CD  
2595 N NE  . ARG A 331 ? 1.11325 0.69518 0.63334 -0.10543 0.17655  0.01412  357 ARG A NE  
2596 C CZ  . ARG A 331 ? 1.08726 0.68433 0.62278 -0.10040 0.16645  0.00342  357 ARG A CZ  
2597 N NH1 . ARG A 331 ? 1.08966 0.68554 0.61786 -0.10344 0.18091  -0.00942 357 ARG A NH1 
2598 N NH2 . ARG A 331 ? 1.05620 0.66891 0.61481 -0.09252 0.14258  0.00546  357 ARG A NH2 
2599 N N   . VAL A 332 ? 0.86054 0.47603 0.50541 -0.08308 0.11774  0.05610  358 VAL A N   
2600 C CA  . VAL A 332 ? 0.80963 0.42827 0.48108 -0.07988 0.11079  0.06369  358 VAL A CA  
2601 C C   . VAL A 332 ? 0.71986 0.36422 0.43998 -0.07247 0.10401  0.05467  358 VAL A C   
2602 O O   . VAL A 332 ? 0.70311 0.35449 0.45593 -0.07199 0.11014  0.05416  358 VAL A O   
2603 C CB  . VAL A 332 ? 0.82799 0.43351 0.47555 -0.07744 0.08992  0.07594  358 VAL A CB  
2604 C CG1 . VAL A 332 ? 0.79926 0.41626 0.48319 -0.07042 0.07593  0.07889  358 VAL A CG1 
2605 C CG2 . VAL A 332 ? 0.86734 0.44747 0.47673 -0.08479 0.09783  0.08768  358 VAL A CG2 
2606 N N   . ARG A 333 ? 0.67945 0.33727 0.40416 -0.06705 0.09150  0.04726  359 ARG A N   
2607 C CA  . ARG A 333 ? 0.65575 0.33617 0.42123 -0.06030 0.08479  0.03902  359 ARG A CA  
2608 C C   . ARG A 333 ? 0.65887 0.34926 0.45206 -0.06238 0.10215  0.03024  359 ARG A C   
2609 O O   . ARG A 333 ? 0.65195 0.35412 0.48038 -0.05932 0.10121  0.02766  359 ARG A O   
2610 C CB  . ARG A 333 ? 0.62910 0.31938 0.38979 -0.05553 0.07076  0.03330  359 ARG A CB  
2611 C CG  . ARG A 333 ? 0.59617 0.30548 0.38995 -0.04781 0.05783  0.02892  359 ARG A CG  
2612 C CD  . ARG A 333 ? 0.60437 0.31738 0.38733 -0.04360 0.04060  0.02868  359 ARG A CD  
2613 N NE  . ARG A 333 ? 0.62350 0.33049 0.37944 -0.04714 0.04317  0.02519  359 ARG A NE  
2614 C CZ  . ARG A 333 ? 0.62723 0.33688 0.37289 -0.04477 0.02981  0.02348  359 ARG A CZ  
2615 N NH1 . ARG A 333 ? 0.57157 0.29043 0.33295 -0.03881 0.01409  0.02515  359 ARG A NH1 
2616 N NH2 . ARG A 333 ? 0.67920 0.38218 0.40010 -0.04855 0.03268  0.01939  359 ARG A NH2 
2617 N N   . THR A 334 ? 0.66781 0.35318 0.44633 -0.06757 0.11778  0.02506  360 THR A N   
2618 C CA  . THR A 334 ? 0.65331 0.34879 0.46178 -0.06919 0.13411  0.01600  360 THR A CA  
2619 C C   . THR A 334 ? 0.65061 0.34177 0.47799 -0.07324 0.14718  0.02015  360 THR A C   
2620 O O   . THR A 334 ? 0.62332 0.32806 0.49078 -0.07117 0.14972  0.01480  360 THR A O   
2621 C CB  . THR A 334 ? 0.67961 0.36922 0.46795 -0.07398 0.14924  0.00901  360 THR A CB  
2622 O OG1 . THR A 334 ? 0.68602 0.37871 0.45699 -0.07053 0.13590  0.00529  360 THR A OG1 
2623 C CG2 . THR A 334 ? 0.64930 0.35147 0.47444 -0.07443 0.16431  -0.00140 360 THR A CG2 
2624 N N   . ARG A 335 ? 0.68365 0.35523 0.48297 -0.07922 0.15479  0.02998  361 ARG A N   
2625 C CA  . ARG A 335 ? 0.69231 0.35876 0.51052 -0.08379 0.16818  0.03448  361 ARG A CA  
2626 C C   . ARG A 335 ? 0.63792 0.31275 0.48557 -0.07839 0.15278  0.03806  361 ARG A C   
2627 O O   . ARG A 335 ? 0.60013 0.28199 0.48377 -0.07922 0.15953  0.03557  361 ARG A O   
2628 C CB  . ARG A 335 ? 0.79100 0.43225 0.56918 -0.09195 0.18035  0.04536  361 ARG A CB  
2629 C CG  . ARG A 335 ? 0.83218 0.47527 0.63475 -0.09540 0.19440  0.04735  361 ARG A CG  
2630 C CD  . ARG A 335 ? 0.91186 0.53687 0.67815 -0.10158 0.20527  0.05547  361 ARG A CD  
2631 N NE  . ARG A 335 ? 0.94196 0.56630 0.72734 -0.10283 0.20710  0.06281  361 ARG A NE  
2632 C CZ  . ARG A 335 ? 0.97027 0.59717 0.77557 -0.10725 0.22624  0.06019  361 ARG A CZ  
2633 N NH1 . ARG A 335 ? 0.99266 0.62327 0.80274 -0.11035 0.24556  0.04991  361 ARG A NH1 
2634 N NH2 . ARG A 335 ? 0.95697 0.58264 0.77921 -0.10846 0.22606  0.06744  361 ARG A NH2 
2635 N N   . ALA A 336 ? 0.62905 0.30340 0.46375 -0.07282 0.13197  0.04303  362 ALA A N   
2636 C CA  . ALA A 336 ? 0.59572 0.27807 0.45791 -0.06725 0.11761  0.04478  362 ALA A CA  
2637 C C   . ALA A 336 ? 0.57341 0.27754 0.47425 -0.06189 0.11297  0.03331  362 ALA A C   
2638 O O   . ALA A 336 ? 0.58733 0.29806 0.51966 -0.06026 0.11061  0.03166  362 ALA A O   
2639 C CB  . ALA A 336 ? 0.59372 0.27144 0.43527 -0.06220 0.09740  0.05142  362 ALA A CB  
2640 N N   . TRP A 337 ? 0.54187 0.25621 0.44014 -0.05934 0.11109  0.02537  363 TRP A N   
2641 C CA  . TRP A 337 ? 0.50061 0.23368 0.43268 -0.05464 0.10674  0.01532  363 TRP A CA  
2642 C C   . TRP A 337 ? 0.51461 0.25186 0.47692 -0.05861 0.12228  0.01019  363 TRP A C   
2643 O O   . TRP A 337 ? 0.50138 0.25025 0.49780 -0.05553 0.11696  0.00516  363 TRP A O   
2644 C CB  . TRP A 337 ? 0.47826 0.21887 0.39927 -0.05178 0.10243  0.00907  363 TRP A CB  
2645 C CG  . TRP A 337 ? 0.45189 0.20984 0.40092 -0.04586 0.09309  0.00097  363 TRP A CG  
2646 C CD1 . TRP A 337 ? 0.42913 0.19657 0.39526 -0.04547 0.09868  -0.00741 363 TRP A CD1 
2647 C CD2 . TRP A 337 ? 0.40522 0.17158 0.36659 -0.03960 0.07653  0.00071  363 TRP A CD2 
2648 N NE1 . TRP A 337 ? 0.39318 0.17351 0.37967 -0.03951 0.08567  -0.01182 363 TRP A NE1 
2649 C CE2 . TRP A 337 ? 0.38040 0.16018 0.36311 -0.03605 0.07274  -0.00730 363 TRP A CE2 
2650 C CE3 . TRP A 337 ? 0.41740 0.18045 0.37392 -0.03665 0.06499  0.00626  363 TRP A CE3 
2651 C CZ2 . TRP A 337 ? 0.34623 0.13517 0.34156 -0.03023 0.05853  -0.00967 363 TRP A CZ2 
2652 C CZ3 . TRP A 337 ? 0.39684 0.17011 0.36860 -0.03064 0.05192  0.00272  363 TRP A CZ3 
2653 C CH2 . TRP A 337 ? 0.36286 0.14845 0.35188 -0.02776 0.04912  -0.00506 363 TRP A CH2 
2654 N N   . THR A 338 ? 0.53961 0.26708 0.49016 -0.06560 0.14157  0.01099  364 THR A N   
2655 C CA  . THR A 338 ? 0.52641 0.25733 0.50870 -0.07002 0.15836  0.00637  364 THR A CA  
2656 C C   . THR A 338 ? 0.50710 0.23849 0.51106 -0.07062 0.15621  0.01109  364 THR A C   
2657 O O   . THR A 338 ? 0.48537 0.23221 0.52841 -0.06871 0.15556  0.00505  364 THR A O   
2658 C CB  . THR A 338 ? 0.56765 0.28642 0.52925 -0.07782 0.18137  0.00662  364 THR A CB  
2659 O OG1 . THR A 338 ? 0.58942 0.31046 0.53120 -0.07621 0.18112  0.00080  364 THR A OG1 
2660 C CG2 . THR A 338 ? 0.56055 0.28856 0.55989 -0.08077 0.19816  0.00021  364 THR A CG2 
2661 N N   . LYS A 339 ? 0.52124 0.23840 0.50052 -0.07228 0.15256  0.02163  365 LYS A N   
2662 C CA  . LYS A 339 ? 0.53379 0.25299 0.53291 -0.07193 0.14798  0.02598  365 LYS A CA  
2663 C C   . LYS A 339 ? 0.54771 0.28110 0.57416 -0.06461 0.12850  0.02110  365 LYS A C   
2664 O O   . LYS A 339 ? 0.55233 0.29558 0.61012 -0.06376 0.12578  0.01828  365 LYS A O   
2665 C CB  . LYS A 339 ? 0.55428 0.25431 0.51975 -0.07464 0.14632  0.03880  365 LYS A CB  
2666 C CG  . LYS A 339 ? 0.54422 0.24424 0.52831 -0.07404 0.13958  0.04398  365 LYS A CG  
2667 C CD  . LYS A 339 ? 0.57474 0.25494 0.52529 -0.07687 0.13815  0.05745  365 LYS A CD  
2668 C CE  . LYS A 339 ? 0.58242 0.26129 0.55305 -0.07739 0.13403  0.06265  365 LYS A CE  
2669 N NZ  . LYS A 339 ? 0.56656 0.22767 0.51224 -0.08376 0.14380  0.07458  365 LYS A NZ  
2670 N N   . VAL A 340 ? 0.56297 0.29716 0.57658 -0.05938 0.11489  0.01961  366 VAL A N   
2671 C CA  . VAL A 340 ? 0.53229 0.27890 0.56672 -0.05234 0.09695  0.01464  366 VAL A CA  
2672 C C   . VAL A 340 ? 0.51707 0.28240 0.58429 -0.05006 0.09580  0.00412  366 VAL A C   
2673 O O   . VAL A 340 ? 0.49088 0.26677 0.58305 -0.04702 0.08611  0.00021  366 VAL A O   
2674 C CB  . VAL A 340 ? 0.50541 0.25006 0.51667 -0.04703 0.08370  0.01557  366 VAL A CB  
2675 C CG1 . VAL A 340 ? 0.48019 0.23832 0.51190 -0.04017 0.06848  0.00825  366 VAL A CG1 
2676 C CG2 . VAL A 340 ? 0.51370 0.24425 0.49984 -0.04717 0.07856  0.02592  366 VAL A CG2 
2677 N N   . LYS A 341 ? 0.54714 0.31615 0.61402 -0.05146 0.10495  -0.00064 367 LYS A N   
2678 C CA  . LYS A 341 ? 0.57467 0.36127 0.67213 -0.04847 0.10183  -0.00992 367 LYS A CA  
2679 C C   . LYS A 341 ? 0.64495 0.43964 0.77485 -0.05132 0.11021  -0.01257 367 LYS A C   
2680 O O   . LYS A 341 ? 0.65192 0.46168 0.81066 -0.04826 0.10438  -0.01957 367 LYS A O   
2681 C CB  . LYS A 341 ? 0.55103 0.33864 0.64017 -0.04884 0.10912  -0.01434 367 LYS A CB  
2682 C CG  . LYS A 341 ? 0.51416 0.30852 0.59823 -0.04255 0.09378  -0.01811 367 LYS A CG  
2683 C CD  . LYS A 341 ? 0.49237 0.28220 0.55443 -0.04347 0.10036  -0.01960 367 LYS A CD  
2684 C CE  . LYS A 341 ? 0.47718 0.26843 0.55414 -0.04768 0.11768  -0.02481 367 LYS A CE  
2685 N NZ  . LYS A 341 ? 0.48552 0.27666 0.54357 -0.04717 0.12114  -0.02808 367 LYS A NZ  
2686 N N   . SER A 342 ? 0.69823 0.48308 0.82414 -0.05698 0.12318  -0.00682 368 SER A N   
2687 C CA  . SER A 342 ? 0.73980 0.53214 0.89793 -0.05992 0.13296  -0.00950 368 SER A CA  
2688 C C   . SER A 342 ? 0.76453 0.56630 0.94867 -0.05668 0.11823  -0.01145 368 SER A C   
2689 O O   . SER A 342 ? 0.77574 0.58618 0.99161 -0.05817 0.12339  -0.01496 368 SER A O   
2690 C CB  . SER A 342 ? 0.75900 0.53662 0.90187 -0.06722 0.15214  -0.00226 368 SER A CB  
2691 O OG  . SER A 342 ? 0.77574 0.54698 0.90179 -0.07112 0.16970  -0.00334 368 SER A OG  
2692 N N   . GLY A 343 ? 0.77479 0.57478 0.94672 -0.05230 0.10074  -0.00993 369 GLY A N   
2693 C CA  . GLY A 343 ? 0.78683 0.59388 0.97890 -0.04938 0.08692  -0.01262 369 GLY A CA  
2694 C C   . GLY A 343 ? 0.78779 0.61196 1.00850 -0.04547 0.07725  -0.02166 369 GLY A C   
2695 O O   . GLY A 343 ? 0.79273 0.62254 1.02338 -0.04193 0.06230  -0.02507 369 GLY A O   
2696 N N   . GLN B 3   ? 1.03078 1.27729 0.80911 0.28011  -0.10834 -0.10811 29  GLN B N   
2697 C CA  . GLN B 3   ? 1.02903 1.27384 0.79417 0.27987  -0.11156 -0.10888 29  GLN B CA  
2698 C C   . GLN B 3   ? 0.95406 1.22814 0.73507 0.27221  -0.09802 -0.09984 29  GLN B C   
2699 O O   . GLN B 3   ? 0.95756 1.23281 0.73088 0.26946  -0.09938 -0.09818 29  GLN B O   
2700 C CB  . GLN B 3   ? 1.08629 1.32589 0.82650 0.29844  -0.11444 -0.12231 29  GLN B CB  
2701 C CG  . GLN B 3   ? 1.13287 1.34937 0.85915 0.30970  -0.12467 -0.13264 29  GLN B CG  
2702 C CD  . GLN B 3   ? 1.14061 1.37652 0.87199 0.32408  -0.11418 -0.13893 29  GLN B CD  
2703 O OE1 . GLN B 3   ? 1.14889 1.40793 0.87927 0.33370  -0.10298 -0.14144 29  GLN B OE1 
2704 N NE2 . GLN B 3   ? 1.13457 1.36125 0.87207 0.32555  -0.11791 -0.14088 29  GLN B NE2 
2705 N N   . LYS B 4   ? 0.89263 1.18855 0.69492 0.26864  -0.08597 -0.09390 30  LYS B N   
2706 C CA  . LYS B 4   ? 0.84128 1.16606 0.65893 0.26259  -0.07275 -0.08577 30  LYS B CA  
2707 C C   . LYS B 4   ? 0.76716 1.08810 0.59638 0.24553  -0.07440 -0.07397 30  LYS B C   
2708 O O   . LYS B 4   ? 0.75401 1.06378 0.59363 0.23680  -0.07721 -0.06798 30  LYS B O   
2709 C CB  . LYS B 4   ? 0.85341 1.19976 0.68893 0.26475  -0.06142 -0.08350 30  LYS B CB  
2710 C CG  . LYS B 4   ? 0.88716 1.25629 0.72034 0.27861  -0.05255 -0.08971 30  LYS B CG  
2711 C CD  . LYS B 4   ? 0.87983 1.27668 0.73565 0.27586  -0.04030 -0.08299 30  LYS B CD  
2712 C CE  . LYS B 4   ? 0.88283 1.27327 0.74835 0.27666  -0.04230 -0.08351 30  LYS B CE  
2713 N NZ  . LYS B 4   ? 0.87828 1.29425 0.75684 0.28459  -0.03342 -0.08411 30  LYS B NZ  
2714 N N   . THR B 5   ? 0.71866 1.04802 0.54550 0.24126  -0.07274 -0.07040 31  THR B N   
2715 C CA  . THR B 5   ? 0.67272 1.00046 0.51142 0.22583  -0.07424 -0.05898 31  THR B CA  
2716 C C   . THR B 5   ? 0.62228 0.97841 0.47462 0.22077  -0.06118 -0.05149 31  THR B C   
2717 O O   . THR B 5   ? 0.62204 0.99841 0.47341 0.22886  -0.05184 -0.05502 31  THR B O   
2718 C CB  . THR B 5   ? 0.69259 0.99893 0.51567 0.22316  -0.08816 -0.06044 31  THR B CB  
2719 O OG1 . THR B 5   ? 0.69670 1.01489 0.50967 0.22650  -0.08492 -0.06218 31  THR B OG1 
2720 C CG2 . THR B 5   ? 0.71472 0.99419 0.51696 0.23279  -0.10141 -0.07130 31  THR B CG2 
2721 N N   . LEU B 6   ? 0.57096 0.92858 0.43695 0.20720  -0.06070 -0.04042 32  LEU B N   
2722 C CA  . LEU B 6   ? 0.54219 0.92413 0.42164 0.20089  -0.04958 -0.03224 32  LEU B CA  
2723 C C   . LEU B 6   ? 0.55434 0.93050 0.44076 0.18819  -0.05443 -0.02274 32  LEU B C   
2724 O O   . LEU B 6   ? 0.57662 0.93759 0.47112 0.18056  -0.06034 -0.01712 32  LEU B O   
2725 C CB  . LEU B 6   ? 0.50103 0.89715 0.39860 0.19825  -0.03887 -0.02672 32  LEU B CB  
2726 C CG  . LEU B 6   ? 0.46044 0.88114 0.37185 0.19222  -0.02762 -0.01836 32  LEU B CG  
2727 C CD1 . LEU B 6   ? 0.45693 0.89663 0.36028 0.20015  -0.02217 -0.02340 32  LEU B CD1 
2728 C CD2 . LEU B 6   ? 0.43969 0.86767 0.36607 0.18974  -0.01992 -0.01328 32  LEU B CD2 
2729 N N   . HIS B 7   ? 0.54144 0.92995 0.42542 0.18602  -0.05188 -0.02039 33  HIS B N   
2730 C CA  . HIS B 7   ? 0.54317 0.92758 0.43373 0.17451  -0.05710 -0.01152 33  HIS B CA  
2731 C C   . HIS B 7   ? 0.51811 0.92591 0.42583 0.16731  -0.04521 -0.00194 33  HIS B C   
2732 O O   . HIS B 7   ? 0.49654 0.92276 0.40035 0.17166  -0.03718 -0.00398 33  HIS B O   
2733 C CB  . HIS B 7   ? 0.58433 0.95823 0.45402 0.17783  -0.06715 -0.01708 33  HIS B CB  
2734 C CG  . HIS B 7   ? 0.62578 0.97153 0.47885 0.18230  -0.08219 -0.02455 33  HIS B CG  
2735 N ND1 . HIS B 7   ? 0.64360 0.98122 0.48263 0.19452  -0.08337 -0.03547 33  HIS B ND1 
2736 C CD2 . HIS B 7   ? 0.64904 0.97212 0.49767 0.17600  -0.09764 -0.02230 33  HIS B CD2 
2737 C CE1 . HIS B 7   ? 0.67275 0.98288 0.49780 0.19578  -0.09891 -0.04007 33  HIS B CE1 
2738 N NE2 . HIS B 7   ? 0.67294 0.97366 0.50374 0.18431  -0.10815 -0.03200 33  HIS B NE2 
2739 N N   . ILE B 8   ? 0.50514 0.91191 0.43163 0.15666  -0.04396 0.00887  34  ILE B N   
2740 C CA  . ILE B 8   ? 0.46568 0.89152 0.40874 0.14982  -0.03327 0.01848  34  ILE B CA  
2741 C C   . ILE B 8   ? 0.44909 0.87156 0.40209 0.13895  -0.03831 0.02829  34  ILE B C   
2742 O O   . ILE B 8   ? 0.44515 0.85117 0.40331 0.13397  -0.04680 0.03209  34  ILE B O   
2743 C CB  . ILE B 8   ? 0.43388 0.86223 0.39045 0.14877  -0.02498 0.02280  34  ILE B CB  
2744 C CG1 . ILE B 8   ? 0.43781 0.86949 0.38585 0.15936  -0.02131 0.01335  34  ILE B CG1 
2745 C CG2 . ILE B 8   ? 0.40025 0.84535 0.37187 0.14206  -0.01505 0.03273  34  ILE B CG2 
2746 C CD1 . ILE B 8   ? 0.42018 0.84815 0.37733 0.15924  -0.01615 0.01617  34  ILE B CD1 
2747 N N   . TYR B 9   ? 0.44508 0.88337 0.40177 0.13510  -0.03346 0.03296  35  TYR B N   
2748 C CA  . TYR B 9   ? 0.46704 0.90514 0.43512 0.12484  -0.03732 0.04299  35  TYR B CA  
2749 C C   . TYR B 9   ? 0.45156 0.90633 0.43729 0.11953  -0.02550 0.05254  35  TYR B C   
2750 O O   . TYR B 9   ? 0.44126 0.91268 0.42444 0.12146  -0.01776 0.05168  35  TYR B O   
2751 C CB  . TYR B 9   ? 0.49703 0.93564 0.45062 0.12512  -0.04413 0.03979  35  TYR B CB  
2752 C CG  . TYR B 9   ? 0.52895 0.95585 0.48863 0.11609  -0.05595 0.04684  35  TYR B CG  
2753 C CD1 . TYR B 9   ? 0.54883 0.95771 0.51595 0.11214  -0.06565 0.04988  35  TYR B CD1 
2754 C CD2 . TYR B 9   ? 0.53370 0.96743 0.49240 0.11119  -0.05806 0.05105  35  TYR B CD2 
2755 C CE1 . TYR B 9   ? 0.56849 0.96750 0.54392 0.10332  -0.07742 0.05743  35  TYR B CE1 
2756 C CE2 . TYR B 9   ? 0.55813 0.98098 0.52365 0.10274  -0.07009 0.05791  35  TYR B CE2 
2757 C CZ  . TYR B 9   ? 0.58102 0.98702 0.55587 0.09872  -0.07990 0.06130  35  TYR B CZ  
2758 O OH  . TYR B 9   ? 0.59440 0.99042 0.57874 0.08975  -0.09277 0.06921  35  TYR B OH  
2759 N N   . ASN B 10  ? 0.44272 0.89249 0.44587 0.11317  -0.02410 0.06203  36  ASN B N   
2760 C CA  . ASN B 10  ? 0.43562 0.89719 0.45368 0.10949  -0.01295 0.07090  36  ASN B CA  
2761 C C   . ASN B 10  ? 0.44033 0.89861 0.47654 0.10063  -0.01484 0.08318  36  ASN B C   
2762 O O   . ASN B 10  ? 0.34369 0.79021 0.38314 0.09695  -0.02489 0.08531  36  ASN B O   
2763 C CB  . ASN B 10  ? 0.41353 0.87218 0.43269 0.11431  -0.00530 0.06925  36  ASN B CB  
2764 C CG  . ASN B 10  ? 0.35778 0.82746 0.38663 0.11241  0.00585  0.07640  36  ASN B CG  
2765 O OD1 . ASN B 10  ? 0.34418 0.82688 0.37657 0.10892  0.00872  0.08045  36  ASN B OD1 
2766 N ND2 . ASN B 10  ? 0.32729 0.78992 0.35892 0.11485  0.01152  0.07803  36  ASN B ND2 
2767 N N   . TRP B 11  ? 0.43245 0.90116 0.48098 0.09738  -0.00549 0.09171  37  TRP B N   
2768 C CA  . TRP B 11  ? 0.43996 0.90746 0.50785 0.09034  -0.00466 0.10436  37  TRP B CA  
2769 C C   . TRP B 11  ? 0.42317 0.87743 0.49977 0.09059  -0.00338 0.10873  37  TRP B C   
2770 O O   . TRP B 11  ? 0.40161 0.84858 0.46935 0.09629  -0.00067 0.10267  37  TRP B O   
2771 C CB  . TRP B 11  ? 0.45771 0.93799 0.53386 0.08868  0.00587  0.11151  37  TRP B CB  
2772 C CG  . TRP B 11  ? 0.49537 0.98859 0.56688 0.08630  0.00424  0.11050  37  TRP B CG  
2773 C CD1 . TRP B 11  ? 0.52187 1.02451 0.57903 0.09017  0.00631  0.10259  37  TRP B CD1 
2774 C CD2 . TRP B 11  ? 0.51872 1.01721 0.60061 0.07945  0.00039  0.11845  37  TRP B CD2 
2775 N NE1 . TRP B 11  ? 0.54496 1.05781 0.60152 0.08604  0.00431  0.10511  37  TRP B NE1 
2776 C CE2 . TRP B 11  ? 0.54303 1.05284 0.61403 0.07944  0.00020  0.11444  37  TRP B CE2 
2777 C CE3 . TRP B 11  ? 0.52807 1.02324 0.62845 0.07331  -0.00301 0.12916  37  TRP B CE3 
2778 C CZ2 . TRP B 11  ? 0.54541 1.06155 0.62133 0.07348  -0.00380 0.12013  37  TRP B CZ2 
2779 C CZ3 . TRP B 11  ? 0.54122 1.04351 0.64816 0.06753  -0.00731 0.13484  37  TRP B CZ3 
2780 C CH2 . TRP B 11  ? 0.54397 1.05577 0.63768 0.06762  -0.00796 0.12999  37  TRP B CH2 
2781 N N   . SER B 12  ? 0.43093 0.88241 0.52588 0.08429  -0.00533 0.12008  38  SER B N   
2782 C CA  . SER B 12  ? 0.43991 0.88063 0.54585 0.08391  -0.00231 0.12694  38  SER B CA  
2783 C C   . SER B 12  ? 0.40692 0.85032 0.51592 0.08761  0.01264  0.13182  38  SER B C   
2784 O O   . SER B 12  ? 0.38824 0.84231 0.50257 0.08673  0.01972  0.13693  38  SER B O   
2785 C CB  . SER B 12  ? 0.47209 0.91114 0.59957 0.07595  -0.00835 0.13922  38  SER B CB  
2786 O OG  . SER B 12  ? 0.50514 0.93184 0.62979 0.07347  -0.02257 0.13585  38  SER B OG  
2787 N N   . ASP B 13  ? 0.41182 0.84355 0.51555 0.09206  0.01670  0.13002  39  ASP B N   
2788 C CA  . ASP B 13  ? 0.41530 0.84451 0.51843 0.09644  0.02999  0.13437  39  ASP B CA  
2789 C C   . ASP B 13  ? 0.41852 0.85691 0.50992 0.10023  0.03532  0.12850  39  ASP B C   
2790 O O   . ASP B 13  ? 0.43102 0.87190 0.52511 0.10158  0.04493  0.13465  39  ASP B O   
2791 C CB  . ASP B 13  ? 0.42211 0.85293 0.54531 0.09308  0.03770  0.14977  39  ASP B CB  
2792 C CG  . ASP B 13  ? 0.44242 0.86398 0.56262 0.09867  0.05067  0.15474  39  ASP B CG  
2793 O OD1 . ASP B 13  ? 0.45392 0.86207 0.56486 0.10223  0.05073  0.15087  39  ASP B OD1 
2794 O OD2 . ASP B 13  ? 0.44951 0.87572 0.57506 0.09994  0.06049  0.16244  39  ASP B OD2 
2795 N N   . TYR B 14  ? 0.41195 0.85511 0.49019 0.10219  0.02888  0.11697  40  TYR B N   
2796 C CA  . TYR B 14  ? 0.38775 0.84074 0.45595 0.10537  0.03281  0.11145  40  TYR B CA  
2797 C C   . TYR B 14  ? 0.35758 0.80381 0.41115 0.11223  0.03310  0.10163  40  TYR B C   
2798 O O   . TYR B 14  ? 0.32621 0.78151 0.37102 0.11502  0.03250  0.09438  40  TYR B O   
2799 C CB  . TYR B 14  ? 0.38480 0.85180 0.45084 0.10247  0.02679  0.10744  40  TYR B CB  
2800 C CG  . TYR B 14  ? 0.35020 0.83051 0.41476 0.10213  0.03242  0.10880  40  TYR B CG  
2801 C CD1 . TYR B 14  ? 0.31504 0.79509 0.38659 0.10124  0.04060  0.11767  40  TYR B CD1 
2802 C CD2 . TYR B 14  ? 0.32020 0.81262 0.37579 0.10303  0.02961  0.10166  40  TYR B CD2 
2803 C CE1 . TYR B 14  ? 0.29756 0.78798 0.36710 0.10056  0.04438  0.11913  40  TYR B CE1 
2804 C CE2 . TYR B 14  ? 0.30470 0.80937 0.35990 0.10190  0.03419  0.10387  40  TYR B CE2 
2805 C CZ  . TYR B 14  ? 0.30325 0.80632 0.36540 0.10031  0.04084  0.11248  40  TYR B CZ  
2806 O OH  . TYR B 14  ? 0.30199 0.81553 0.36308 0.09883  0.04407  0.11487  40  TYR B OH  
2807 N N   . ILE B 15  ? 0.36056 0.79116 0.41229 0.11492  0.03395  0.10198  41  ILE B N   
2808 C CA  . ILE B 15  ? 0.34394 0.76569 0.38231 0.12148  0.03353  0.09329  41  ILE B CA  
2809 C C   . ILE B 15  ? 0.34957 0.75338 0.38827 0.12318  0.03814  0.09876  41  ILE B C   
2810 O O   . ILE B 15  ? 0.35103 0.74985 0.40070 0.11932  0.03938  0.10761  41  ILE B O   
2811 C CB  . ILE B 15  ? 0.33397 0.75538 0.36396 0.12398  0.02366  0.08211  41  ILE B CB  
2812 C CG1 . ILE B 15  ? 0.34133 0.76107 0.35867 0.13127  0.02356  0.07227  41  ILE B CG1 
2813 C CG2 . ILE B 15  ? 0.33506 0.74195 0.36771 0.12220  0.01738  0.08347  41  ILE B CG2 
2814 C CD1 . ILE B 15  ? 0.35103 0.77264 0.35933 0.13540  0.01518  0.06094  41  ILE B CD1 
2815 N N   . ALA B 16  ? 0.35526 0.74934 0.38227 0.12897  0.04074  0.09423  42  ALA B N   
2816 C CA  . ALA B 16  ? 0.41127 0.78624 0.43499 0.13143  0.04530  0.09884  42  ALA B CA  
2817 C C   . ALA B 16  ? 0.47069 0.83530 0.49569 0.13040  0.03840  0.09703  42  ALA B C   
2818 O O   . ALA B 16  ? 0.48691 0.85489 0.50820 0.13085  0.02910  0.08802  42  ALA B O   
2819 C CB  . ALA B 16  ? 0.40970 0.77460 0.41843 0.13792  0.04729  0.09325  42  ALA B CB  
2820 N N   . PRO B 17  ? 0.46875 0.82010 0.49850 0.12927  0.04278  0.10593  43  PRO B N   
2821 C CA  . PRO B 17  ? 0.46997 0.81181 0.50359 0.12666  0.03534  0.10625  43  PRO B CA  
2822 C C   . PRO B 17  ? 0.47219 0.80237 0.49067 0.13155  0.02708  0.09419  43  PRO B C   
2823 O O   . PRO B 17  ? 0.48545 0.80998 0.50497 0.12951  0.01750  0.09130  43  PRO B O   
2824 C CB  . PRO B 17  ? 0.46533 0.79562 0.50631 0.12551  0.04450  0.11947  43  PRO B CB  
2825 C CG  . PRO B 17  ? 0.45996 0.79857 0.50566 0.12606  0.05594  0.12735  43  PRO B CG  
2826 C CD  . PRO B 17  ? 0.46385 0.80869 0.49634 0.13022  0.05491  0.11718  43  PRO B CD  
2827 N N   . ASP B 18  ? 0.46746 0.79303 0.47199 0.13799  0.02948  0.08721  44  ASP B N   
2828 C CA  . ASP B 18  ? 0.47025 0.78364 0.46102 0.14339  0.02217  0.07645  44  ASP B CA  
2829 C C   . ASP B 18  ? 0.44009 0.76557 0.42353 0.14798  0.01728  0.06432  44  ASP B C   
2830 O O   . ASP B 18  ? 0.47039 0.78738 0.44264 0.15379  0.01236  0.05526  44  ASP B O   
2831 C CB  . ASP B 18  ? 0.49497 0.78895 0.47511 0.14770  0.02793  0.07890  44  ASP B CB  
2832 C CG  . ASP B 18  ? 0.50876 0.80570 0.48301 0.15104  0.03556  0.07977  44  ASP B CG  
2833 O OD1 . ASP B 18  ? 0.50591 0.81856 0.48860 0.14814  0.04010  0.08409  44  ASP B OD1 
2834 O OD2 . ASP B 18  ? 0.52443 0.80667 0.48497 0.15642  0.03603  0.07622  44  ASP B OD2 
2835 N N   . THR B 19  ? 0.39901 0.74438 0.38904 0.14567  0.01866  0.06442  45  THR B N   
2836 C CA  . THR B 19  ? 0.40519 0.76409 0.38977 0.15006  0.01548  0.05441  45  THR B CA  
2837 C C   . THR B 19  ? 0.42289 0.78054 0.40142 0.15342  0.00544  0.04410  45  THR B C   
2838 O O   . THR B 19  ? 0.41721 0.77237 0.38671 0.16026  0.00182  0.03477  45  THR B O   
2839 C CB  . THR B 19  ? 0.37742 0.75738 0.37026 0.14622  0.01941  0.05800  45  THR B CB  
2840 O OG1 . THR B 19  ? 0.37944 0.75804 0.37851 0.14254  0.02798  0.06887  45  THR B OG1 
2841 C CG2 . THR B 19  ? 0.36008 0.75410 0.34858 0.15074  0.01921  0.05061  45  THR B CG2 
2842 N N   . VAL B 20  ? 0.41642 0.77483 0.39945 0.14905  0.00021  0.04574  46  VAL B N   
2843 C CA  . VAL B 20  ? 0.43465 0.78999 0.40937 0.15268  -0.01017 0.03581  46  VAL B CA  
2844 C C   . VAL B 20  ? 0.45089 0.78521 0.41646 0.15700  -0.01603 0.03083  46  VAL B C   
2845 O O   . VAL B 20  ? 0.48709 0.81846 0.44180 0.16423  -0.02235 0.01980  46  VAL B O   
2846 C CB  . VAL B 20  ? 0.38289 0.73987 0.36341 0.14629  -0.01604 0.03974  46  VAL B CB  
2847 C CG1 . VAL B 20  ? 0.45014 0.79767 0.41877 0.15044  -0.02825 0.02970  46  VAL B CG1 
2848 C CG2 . VAL B 20  ? 0.37019 0.74794 0.35707 0.14309  -0.01144 0.04282  46  VAL B CG2 
2849 N N   . ALA B 21  ? 0.42797 0.74727 0.39751 0.15311  -0.01365 0.03917  47  ALA B N   
2850 C CA  . ALA B 21  ? 0.44186 0.73976 0.40229 0.15653  -0.01919 0.03544  47  ALA B CA  
2851 C C   . ALA B 21  ? 0.44015 0.73537 0.39018 0.16474  -0.01741 0.02752  47  ALA B C   
2852 O O   . ALA B 21  ? 0.44617 0.73093 0.38567 0.17087  -0.02516 0.01807  47  ALA B O   
2853 C CB  . ALA B 21  ? 0.46026 0.74407 0.42774 0.15055  -0.01506 0.04774  47  ALA B CB  
2854 N N   . ASN B 22  ? 0.42631 0.73001 0.37911 0.16507  -0.00821 0.03135  48  ASN B N   
2855 C CA  . ASN B 22  ? 0.43978 0.74139 0.38424 0.17218  -0.00775 0.02467  48  ASN B CA  
2856 C C   . ASN B 22  ? 0.44821 0.76497 0.39012 0.17844  -0.01275 0.01345  48  ASN B C   
2857 O O   . ASN B 22  ? 0.44156 0.75212 0.37558 0.18571  -0.01763 0.00492  48  ASN B O   
2858 C CB  . ASN B 22  ? 0.44168 0.74818 0.38929 0.17055  0.00178  0.03185  48  ASN B CB  
2859 C CG  . ASN B 22  ? 0.45789 0.74533 0.40339 0.16767  0.00760  0.04166  48  ASN B CG  
2860 O OD1 . ASN B 22  ? 0.46784 0.73728 0.40870 0.16763  0.00437  0.04242  48  ASN B OD1 
2861 N ND2 . ASN B 22  ? 0.45368 0.74430 0.40178 0.16562  0.01639  0.04956  48  ASN B ND2 
2862 N N   . PHE B 23  ? 0.45370 0.79030 0.40207 0.17617  -0.01130 0.01367  49  PHE B N   
2863 C CA  . PHE B 23  ? 0.46780 0.81953 0.41317 0.18274  -0.01464 0.00386  49  PHE B CA  
2864 C C   . PHE B 23  ? 0.51846 0.85736 0.45332 0.18850  -0.02456 -0.00555 49  PHE B C   
2865 O O   . PHE B 23  ? 0.54754 0.88878 0.47616 0.19741  -0.02790 -0.01506 49  PHE B O   
2866 C CB  . PHE B 23  ? 0.44555 0.81821 0.39780 0.17869  -0.01110 0.00689  49  PHE B CB  
2867 C CG  . PHE B 23  ? 0.43179 0.82006 0.37977 0.18575  -0.01324 -0.00221 49  PHE B CG  
2868 C CD1 . PHE B 23  ? 0.42021 0.82542 0.37155 0.19058  -0.00883 -0.00479 49  PHE B CD1 
2869 C CD2 . PHE B 23  ? 0.46352 0.84898 0.40385 0.18781  -0.01976 -0.00761 49  PHE B CD2 
2870 C CE1 . PHE B 23  ? 0.42704 0.84812 0.37541 0.19779  -0.00920 -0.01211 49  PHE B CE1 
2871 C CE2 . PHE B 23  ? 0.46393 0.86267 0.39798 0.19569  -0.02052 -0.01585 49  PHE B CE2 
2872 C CZ  . PHE B 23  ? 0.44285 0.86049 0.38157 0.20091  -0.01438 -0.01785 49  PHE B CZ  
2873 N N   . GLU B 24  ? 0.53787 0.86279 0.47116 0.18367  -0.02989 -0.00265 50  GLU B N   
2874 C CA  . GLU B 24  ? 0.54871 0.85773 0.47057 0.18852  -0.04095 -0.01108 50  GLU B CA  
2875 C C   . GLU B 24  ? 0.56865 0.86004 0.48284 0.19417  -0.04444 -0.01583 50  GLU B C   
2876 O O   . GLU B 24  ? 0.58578 0.87164 0.48969 0.20299  -0.05148 -0.02651 50  GLU B O   
2877 C CB  . GLU B 24  ? 0.54847 0.84456 0.47235 0.18045  -0.04692 -0.00486 50  GLU B CB  
2878 C CG  . GLU B 24  ? 0.54580 0.85541 0.47428 0.17580  -0.04731 -0.00210 50  GLU B CG  
2879 C CD  . GLU B 24  ? 0.56772 0.86422 0.50117 0.16682  -0.05421 0.00565  50  GLU B CD  
2880 O OE1 . GLU B 24  ? 0.57311 0.85754 0.51351 0.16138  -0.05274 0.01401  50  GLU B OE1 
2881 O OE2 . GLU B 24  ? 0.57897 0.87683 0.50936 0.16525  -0.06127 0.00389  50  GLU B OE2 
2882 N N   . LYS B 25  ? 0.55823 0.83954 0.47610 0.18980  -0.03960 -0.00799 51  LYS B N   
2883 C CA  . LYS B 25  ? 0.56276 0.82498 0.47191 0.19468  -0.04319 -0.01180 51  LYS B CA  
2884 C C   . LYS B 25  ? 0.53238 0.80451 0.43884 0.20372  -0.04248 -0.02012 51  LYS B C   
2885 O O   . LYS B 25  ? 0.53929 0.79948 0.43680 0.21115  -0.04940 -0.02841 51  LYS B O   
2886 C CB  . LYS B 25  ? 0.59238 0.84132 0.50420 0.18849  -0.03690 -0.00080 51  LYS B CB  
2887 C CG  . LYS B 25  ? 0.62052 0.84634 0.52881 0.18423  -0.04219 0.00363  51  LYS B CG  
2888 C CD  . LYS B 25  ? 0.63521 0.84624 0.54282 0.18085  -0.03492 0.01345  51  LYS B CD  
2889 C CE  . LYS B 25  ? 0.62761 0.84694 0.54803 0.17231  -0.02514 0.02698  51  LYS B CE  
2890 N NZ  . LYS B 25  ? 0.63472 0.84933 0.56264 0.16530  -0.02982 0.03306  51  LYS B NZ  
2891 N N   . GLU B 26  ? 0.50336 0.79745 0.41848 0.20310  -0.03476 -0.01760 52  GLU B N   
2892 C CA  . GLU B 26  ? 0.49218 0.79742 0.40807 0.21077  -0.03430 -0.02377 52  GLU B CA  
2893 C C   . GLU B 26  ? 0.49399 0.81226 0.40748 0.21950  -0.03859 -0.03425 52  GLU B C   
2894 O O   . GLU B 26  ? 0.50607 0.82237 0.41578 0.22845  -0.04298 -0.04224 52  GLU B O   
2895 C CB  . GLU B 26  ? 0.47293 0.79656 0.39932 0.20666  -0.02547 -0.01667 52  GLU B CB  
2896 C CG  . GLU B 26  ? 0.48015 0.81740 0.41058 0.21342  -0.02564 -0.02142 52  GLU B CG  
2897 C CD  . GLU B 26  ? 0.48863 0.84415 0.42970 0.20868  -0.01836 -0.01404 52  GLU B CD  
2898 O OE1 . GLU B 26  ? 0.49775 0.84913 0.44037 0.20084  -0.01318 -0.00515 52  GLU B OE1 
2899 O OE2 . GLU B 26  ? 0.49902 0.87311 0.44743 0.21295  -0.01795 -0.01670 52  GLU B OE2 
2900 N N   . THR B 27  ? 0.49447 0.82533 0.40935 0.21771  -0.03739 -0.03428 53  THR B N   
2901 C CA  . THR B 27  ? 0.50594 0.85107 0.41723 0.22679  -0.03923 -0.04337 53  THR B CA  
2902 C C   . THR B 27  ? 0.55064 0.87831 0.44765 0.23211  -0.04913 -0.05165 53  THR B C   
2903 O O   . THR B 27  ? 0.58362 0.91708 0.47380 0.24289  -0.05181 -0.06114 53  THR B O   
2904 C CB  . THR B 27  ? 0.47486 0.84371 0.39309 0.22300  -0.03224 -0.03920 53  THR B CB  
2905 O OG1 . THR B 27  ? 0.46604 0.82616 0.38171 0.21504  -0.03447 -0.03455 53  THR B OG1 
2906 C CG2 . THR B 27  ? 0.41068 0.79566 0.34246 0.21725  -0.02345 -0.03066 53  THR B CG2 
2907 N N   . GLY B 28  ? 0.54745 0.85376 0.43983 0.22522  -0.05475 -0.04793 54  GLY B N   
2908 C CA  . GLY B 28  ? 0.54937 0.83775 0.42810 0.22870  -0.06568 -0.05465 54  GLY B CA  
2909 C C   . GLY B 28  ? 0.57029 0.86607 0.44525 0.22720  -0.06725 -0.05515 54  GLY B C   
2910 O O   . GLY B 28  ? 0.59411 0.87308 0.45588 0.22998  -0.07775 -0.06072 54  GLY B O   
2911 N N   . ILE B 29  ? 0.55317 0.87180 0.43799 0.22289  -0.05807 -0.04947 55  ILE B N   
2912 C CA  . ILE B 29  ? 0.56619 0.89143 0.44666 0.22102  -0.05949 -0.04934 55  ILE B CA  
2913 C C   . ILE B 29  ? 0.58846 0.89850 0.47199 0.20912  -0.06523 -0.04092 55  ILE B C   
2914 O O   . ILE B 29  ? 0.56769 0.87500 0.46354 0.20007  -0.06126 -0.03112 55  ILE B O   
2915 C CB  . ILE B 29  ? 0.54420 0.89856 0.43492 0.21962  -0.04781 -0.04510 55  ILE B CB  
2916 C CG1 . ILE B 29  ? 0.55417 0.92519 0.44561 0.23078  -0.04205 -0.05172 55  ILE B CG1 
2917 C CG2 . ILE B 29  ? 0.53198 0.89227 0.41620 0.21814  -0.04935 -0.04514 55  ILE B CG2 
2918 C CD1 . ILE B 29  ? 0.54230 0.94192 0.44672 0.22823  -0.03057 -0.04588 55  ILE B CD1 
2919 N N   . LYS B 30  ? 0.60548 0.90485 0.47759 0.20944  -0.07487 -0.04431 56  LYS B N   
2920 C CA  . LYS B 30  ? 0.62757 0.91436 0.50436 0.19783  -0.08174 -0.03571 56  LYS B CA  
2921 C C   . LYS B 30  ? 0.58816 0.89417 0.47383 0.19115  -0.07537 -0.02868 56  LYS B C   
2922 O O   . LYS B 30  ? 0.59157 0.90323 0.46632 0.19563  -0.07761 -0.03400 56  LYS B O   
2923 C CB  . LYS B 30  ? 0.69290 0.95532 0.55214 0.20099  -0.09787 -0.04263 56  LYS B CB  
2924 C CG  . LYS B 30  ? 0.73807 0.97717 0.59074 0.20404  -0.10623 -0.04664 56  LYS B CG  
2925 C CD  . LYS B 30  ? 0.76849 1.00404 0.60282 0.21974  -0.10910 -0.06128 56  LYS B CD  
2926 C CE  . LYS B 30  ? 0.77886 0.99786 0.61061 0.22344  -0.11297 -0.06465 56  LYS B CE  
2927 N NZ  . LYS B 30  ? 0.75654 0.98780 0.60486 0.21940  -0.10090 -0.05762 56  LYS B NZ  
2928 N N   . VAL B 31  ? 0.55512 0.86992 0.45918 0.18102  -0.06745 -0.01674 57  VAL B N   
2929 C CA  . VAL B 31  ? 0.52617 0.85976 0.44050 0.17433  -0.06063 -0.00918 57  VAL B CA  
2930 C C   . VAL B 31  ? 0.54241 0.86511 0.46262 0.16394  -0.06910 -0.00094 57  VAL B C   
2931 O O   . VAL B 31  ? 0.54848 0.86098 0.48040 0.15640  -0.07029 0.00782  57  VAL B O   
2932 C CB  . VAL B 31  ? 0.47386 0.82351 0.40418 0.17034  -0.04701 -0.00104 57  VAL B CB  
2933 C CG1 . VAL B 31  ? 0.43823 0.80645 0.37841 0.16365  -0.04073 0.00656  57  VAL B CG1 
2934 C CG2 . VAL B 31  ? 0.46395 0.82312 0.38994 0.17994  -0.04064 -0.00851 57  VAL B CG2 
2935 N N   . VAL B 32  ? 0.53928 0.86381 0.45145 0.16369  -0.07513 -0.00322 58  VAL B N   
2936 C CA  . VAL B 32  ? 0.53722 0.85472 0.45699 0.15315  -0.08338 0.00553  58  VAL B CA  
2937 C C   . VAL B 32  ? 0.50666 0.84622 0.44196 0.14634  -0.07268 0.01490  58  VAL B C   
2938 O O   . VAL B 32  ? 0.45577 0.80956 0.38404 0.14975  -0.06874 0.01121  58  VAL B O   
2939 C CB  . VAL B 32  ? 0.57516 0.87822 0.47503 0.15662  -0.09801 -0.00221 58  VAL B CB  
2940 C CG1 . VAL B 32  ? 0.58193 0.87230 0.49103 0.14490  -0.11016 0.00740  58  VAL B CG1 
2941 C CG2 . VAL B 32  ? 0.58993 0.87378 0.47009 0.16699  -0.10652 -0.01432 58  VAL B CG2 
2942 N N   . TYR B 33  ? 0.51779 0.85983 0.47369 0.13717  -0.06764 0.02734  59  TYR B N   
2943 C CA  . TYR B 33  ? 0.50425 0.86629 0.47576 0.13158  -0.05599 0.03663  59  TYR B CA  
2944 C C   . TYR B 33  ? 0.53434 0.89554 0.51739 0.12150  -0.06267 0.04637  59  TYR B C   
2945 O O   . TYR B 33  ? 0.54630 0.90295 0.54697 0.11363  -0.06289 0.05763  59  TYR B O   
2946 C CB  . TYR B 33  ? 0.48027 0.84503 0.46500 0.13005  -0.04469 0.04360  59  TYR B CB  
2947 C CG  . TYR B 33  ? 0.44844 0.83240 0.44535 0.12681  -0.03189 0.05122  59  TYR B CG  
2948 C CD1 . TYR B 33  ? 0.42674 0.82545 0.41766 0.13263  -0.02353 0.04576  59  TYR B CD1 
2949 C CD2 . TYR B 33  ? 0.44704 0.83405 0.46216 0.11808  -0.02847 0.06443  59  TYR B CD2 
2950 C CE1 . TYR B 33  ? 0.41233 0.82660 0.41341 0.12937  -0.01319 0.05288  59  TYR B CE1 
2951 C CE2 . TYR B 33  ? 0.42882 0.83143 0.45353 0.11580  -0.01734 0.07113  59  TYR B CE2 
2952 C CZ  . TYR B 33  ? 0.40781 0.82308 0.42461 0.12124  -0.01025 0.06513  59  TYR B CZ  
2953 O OH  . TYR B 33  ? 0.33283 0.76173 0.35818 0.11866  -0.00053 0.07191  59  TYR B OH  
2954 N N   . ASP B 34  ? 0.54754 0.91304 0.52062 0.12204  -0.06815 0.04246  60  ASP B N   
2955 C CA  . ASP B 34  ? 0.56140 0.92723 0.54497 0.11261  -0.07497 0.05149  60  ASP B CA  
2956 C C   . ASP B 34  ? 0.52215 0.90867 0.52314 0.10739  -0.06231 0.06128  60  ASP B C   
2957 O O   . ASP B 34  ? 0.49597 0.89671 0.49623 0.11175  -0.04964 0.05923  60  ASP B O   
2958 C CB  . ASP B 34  ? 0.59746 0.95725 0.56071 0.11554  -0.08630 0.04347  60  ASP B CB  
2959 C CG  . ASP B 34  ? 0.64377 0.97871 0.58996 0.11941  -0.10192 0.03542  60  ASP B CG  
2960 O OD1 . ASP B 34  ? 0.65654 0.97741 0.61371 0.11391  -0.10918 0.04121  60  ASP B OD1 
2961 O OD2 . ASP B 34  ? 0.67133 1.00028 0.59267 0.12825  -0.10685 0.02367  60  ASP B OD2 
2962 N N   . VAL B 35  ? 0.52447 0.91196 0.54164 0.09792  -0.06673 0.07233  61  VAL B N   
2963 C CA  . VAL B 35  ? 0.50544 0.90989 0.54159 0.09263  -0.05542 0.08320  61  VAL B CA  
2964 C C   . VAL B 35  ? 0.51072 0.91853 0.55409 0.08506  -0.06333 0.08979  61  VAL B C   
2965 O O   . VAL B 35  ? 0.52533 0.91951 0.56845 0.08075  -0.07811 0.09111  61  VAL B O   
2966 C CB  . VAL B 35  ? 0.51404 0.91632 0.57058 0.08910  -0.04811 0.09390  61  VAL B CB  
2967 C CG1 . VAL B 35  ? 0.51271 0.90327 0.58503 0.08091  -0.05926 0.10359  61  VAL B CG1 
2968 C CG2 . VAL B 35  ? 0.50500 0.92382 0.57525 0.08728  -0.03386 0.10235  61  VAL B CG2 
2969 N N   . PHE B 36  ? 0.52447 0.94939 0.57359 0.08334  -0.05443 0.09394  62  PHE B N   
2970 C CA  . PHE B 36  ? 0.58350 1.01378 0.64205 0.07589  -0.05991 0.10166  62  PHE B CA  
2971 C C   . PHE B 36  ? 0.63082 1.07401 0.71378 0.07096  -0.04867 0.11468  62  PHE B C   
2972 O O   . PHE B 36  ? 0.63331 1.08172 0.72101 0.07437  -0.03588 0.11616  62  PHE B O   
2973 C CB  . PHE B 36  ? 0.57995 1.01779 0.61898 0.07902  -0.06079 0.09389  62  PHE B CB  
2974 C CG  . PHE B 36  ? 0.54204 0.99662 0.57593 0.08436  -0.04568 0.09040  62  PHE B CG  
2975 C CD1 . PHE B 36  ? 0.50789 0.97776 0.55441 0.08028  -0.03691 0.09857  62  PHE B CD1 
2976 C CD2 . PHE B 36  ? 0.52819 0.98282 0.54527 0.09339  -0.04112 0.07936  62  PHE B CD2 
2977 C CE1 . PHE B 36  ? 0.47957 0.96346 0.52154 0.08445  -0.02469 0.09598  62  PHE B CE1 
2978 C CE2 . PHE B 36  ? 0.49381 0.96405 0.50826 0.09754  -0.02856 0.07716  62  PHE B CE2 
2979 C CZ  . PHE B 36  ? 0.47394 0.95834 0.50064 0.09273  -0.02073 0.08559  62  PHE B CZ  
2980 N N   . ASP B 37  ? 0.65802 1.10522 0.75557 0.06339  -0.05391 0.12420  63  ASP B N   
2981 C CA  . ASP B 37  ? 0.68143 1.13922 0.80382 0.05902  -0.04443 0.13762  63  ASP B CA  
2982 C C   . ASP B 37  ? 0.70367 1.17589 0.82834 0.05672  -0.04016 0.14109  63  ASP B C   
2983 O O   . ASP B 37  ? 0.69286 1.17413 0.83553 0.05477  -0.03074 0.15122  63  ASP B O   
2984 C CB  . ASP B 37  ? 0.70402 1.15493 0.85043 0.05146  -0.05294 0.14983  63  ASP B CB  
2985 C CG  . ASP B 37  ? 0.73659 1.17782 0.89002 0.05311  -0.05007 0.15214  63  ASP B CG  
2986 O OD1 . ASP B 37  ? 0.76514 1.19267 0.91977 0.04996  -0.06323 0.15216  63  ASP B OD1 
2987 O OD2 . ASP B 37  ? 0.73660 1.18248 0.89297 0.05758  -0.03522 0.15397  63  ASP B OD2 
2988 N N   . SER B 38  ? 0.74921 1.22311 0.85543 0.05736  -0.04641 0.13335  64  SER B N   
2989 C CA  . SER B 38  ? 0.77349 1.26121 0.87887 0.05581  -0.04121 0.13571  64  SER B CA  
2990 C C   . SER B 38  ? 0.80478 1.29326 0.88342 0.05946  -0.04518 0.12428  64  SER B C   
2991 O O   . SER B 38  ? 0.83045 1.30739 0.89208 0.06277  -0.05383 0.11537  64  SER B O   
2992 C CB  . SER B 38  ? 0.79020 1.28064 0.91606 0.04750  -0.04741 0.14793  64  SER B CB  
2993 O OG  . SER B 38  ? 0.77927 1.27801 0.92742 0.04644  -0.03599 0.15881  64  SER B OG  
2994 N N   . ASN B 39  ? 0.78901 1.29085 0.86387 0.05906  -0.03861 0.12523  65  ASN B N   
2995 C CA  . ASN B 39  ? 0.82115 1.32831 0.87195 0.06395  -0.03680 0.11538  65  ASN B CA  
2996 C C   . ASN B 39  ? 0.83521 1.33049 0.86691 0.06436  -0.05051 0.10882  65  ASN B C   
2997 O O   . ASN B 39  ? 0.84821 1.33960 0.85826 0.07153  -0.05093 0.09806  65  ASN B O   
2998 C CB  . ASN B 39  ? 0.83851 1.36110 0.89145 0.06127  -0.02950 0.12017  65  ASN B CB  
2999 C CG  . ASN B 39  ? 0.86979 1.40133 0.93885 0.06127  -0.01712 0.12665  65  ASN B CG  
3000 O OD1 . ASN B 39  ? 0.88356 1.41579 0.97187 0.05656  -0.01628 0.13678  65  ASN B OD1 
3001 N ND2 . ASN B 39  ? 0.88569 1.42351 0.94656 0.06699  -0.00771 0.12110  65  ASN B ND2 
3002 N N   . GLU B 40  ? 0.81119 1.29967 0.85002 0.05722  -0.06219 0.11533  66  GLU B N   
3003 C CA  . GLU B 40  ? 0.80667 1.28252 0.82432 0.05721  -0.07608 0.10977  66  GLU B CA  
3004 C C   . GLU B 40  ? 0.79742 1.25628 0.79779 0.06337  -0.08378 0.09969  66  GLU B C   
3005 O O   . GLU B 40  ? 0.82979 1.28111 0.80255 0.06910  -0.08843 0.09012  66  GLU B O   
3006 C CB  . GLU B 40  ? 0.81877 1.28760 0.85087 0.04777  -0.08940 0.11959  66  GLU B CB  
3007 C CG  . GLU B 40  ? 0.80282 1.28723 0.85559 0.04171  -0.08246 0.13066  66  GLU B CG  
3008 C CD  . GLU B 40  ? 0.79787 1.28813 0.88175 0.03874  -0.07557 0.14077  66  GLU B CD  
3009 O OE1 . GLU B 40  ? 0.80253 1.28569 0.89166 0.04116  -0.07524 0.13919  66  GLU B OE1 
3010 O OE2 . GLU B 40  ? 0.78881 1.29009 0.89091 0.03450  -0.07024 0.15042  66  GLU B OE2 
3011 N N   . VAL B 41  ? 0.75118 1.20330 0.76624 0.06291  -0.08474 0.10173  67  VAL B N   
3012 C CA  . VAL B 41  ? 0.74845 1.18289 0.74792 0.06846  -0.09300 0.09255  67  VAL B CA  
3013 C C   . VAL B 41  ? 0.72859 1.16770 0.70395 0.07956  -0.08373 0.08000  67  VAL B C   
3014 O O   . VAL B 41  ? 0.74490 1.17295 0.69341 0.08572  -0.09076 0.07031  67  VAL B O   
3015 C CB  . VAL B 41  ? 0.73784 1.16683 0.75914 0.06585  -0.09302 0.09810  67  VAL B CB  
3016 C CG1 . VAL B 41  ? 0.75713 1.16358 0.76437 0.06878  -0.10693 0.09089  67  VAL B CG1 
3017 C CG2 . VAL B 41  ? 0.72791 1.16045 0.77953 0.05542  -0.09618 0.11313  67  VAL B CG2 
3018 N N   . LEU B 42  ? 0.68769 1.14276 0.67225 0.08268  -0.06798 0.08039  68  LEU B N   
3019 C CA  . LEU B 42  ? 0.65827 1.11997 0.62477 0.09292  -0.05879 0.06984  68  LEU B CA  
3020 C C   . LEU B 42  ? 0.66213 1.13231 0.60880 0.09626  -0.05642 0.06561  68  LEU B C   
3021 O O   . LEU B 42  ? 0.65390 1.12078 0.57740 0.10547  -0.05616 0.05537  68  LEU B O   
3022 C CB  . LEU B 42  ? 0.61169 1.08847 0.59395 0.09408  -0.04383 0.07286  68  LEU B CB  
3023 C CG  . LEU B 42  ? 0.57486 1.06586 0.54508 0.10237  -0.03234 0.06561  68  LEU B CG  
3024 C CD1 . LEU B 42  ? 0.56431 1.04654 0.52219 0.11185  -0.03297 0.05512  68  LEU B CD1 
3025 C CD2 . LEU B 42  ? 0.53949 1.04726 0.52687 0.09961  -0.01961 0.07255  68  LEU B CD2 
3026 N N   . GLU B 43  ? 0.67507 1.15588 0.63000 0.08930  -0.05441 0.07369  69  GLU B N   
3027 C CA  . GLU B 43  ? 0.71977 1.20993 0.65664 0.09190  -0.05078 0.07097  69  GLU B CA  
3028 C C   . GLU B 43  ? 0.77597 1.24797 0.68605 0.09523  -0.06377 0.06427  69  GLU B C   
3029 O O   . GLU B 43  ? 0.78226 1.25590 0.66797 0.10389  -0.06008 0.05619  69  GLU B O   
3030 C CB  . GLU B 43  ? 0.70904 1.21264 0.66123 0.08305  -0.04696 0.08169  69  GLU B CB  
3031 C CG  . GLU B 43  ? 0.68356 1.20478 0.65604 0.08154  -0.03315 0.08722  69  GLU B CG  
3032 C CD  . GLU B 43  ? 0.68073 1.21334 0.66680 0.07341  -0.03013 0.09757  69  GLU B CD  
3033 O OE1 . GLU B 43  ? 0.65537 1.20071 0.65519 0.07227  -0.01974 0.10224  69  GLU B OE1 
3034 O OE2 . GLU B 43  ? 0.69434 1.22168 0.67638 0.06833  -0.03897 0.10098  69  GLU B OE2 
3035 N N   . GLY B 44  ? 0.82579 1.27962 0.73955 0.08887  -0.07924 0.06786  70  GLY B N   
3036 C CA  . GLY B 44  ? 0.85319 1.28531 0.73960 0.09203  -0.09393 0.06135  70  GLY B CA  
3037 C C   . GLY B 44  ? 0.88299 1.30088 0.74875 0.10294  -0.09670 0.04941  70  GLY B C   
3038 O O   . GLY B 44  ? 0.89302 1.30062 0.72757 0.11154  -0.10001 0.04047  70  GLY B O   
3039 N N   . LYS B 45  ? 0.83745 1.25387 0.71903 0.10344  -0.09500 0.04910  71  LYS B N   
3040 C CA  . LYS B 45  ? 0.83984 1.24360 0.70303 0.11420  -0.09694 0.03770  71  LYS B CA  
3041 C C   . LYS B 45  ? 0.87946 1.29783 0.72458 0.12604  -0.08256 0.02928  71  LYS B C   
3042 O O   . LYS B 45  ? 0.90489 1.31084 0.72184 0.13689  -0.08602 0.01875  71  LYS B O   
3043 C CB  . LYS B 45  ? 0.79687 1.19924 0.68225 0.11205  -0.09560 0.04006  71  LYS B CB  
3044 C CG  . LYS B 45  ? 0.79067 1.17190 0.68651 0.10397  -0.11270 0.04523  71  LYS B CG  
3045 C CD  . LYS B 45  ? 0.76355 1.14956 0.68786 0.09931  -0.10756 0.05193  71  LYS B CD  
3046 C CE  . LYS B 45  ? 0.78813 1.15057 0.70792 0.10069  -0.12070 0.04804  71  LYS B CE  
3047 N NZ  . LYS B 45  ? 0.80657 1.16255 0.70200 0.11373  -0.11795 0.03429  71  LYS B NZ  
3048 N N   . LEU B 46  ? 0.88539 1.32983 0.74635 0.12440  -0.06663 0.03423  72  LEU B N   
3049 C CA  . LEU B 46  ? 0.91877 1.37975 0.76782 0.13489  -0.05258 0.02788  72  LEU B CA  
3050 C C   . LEU B 46  ? 1.00300 1.46563 0.82655 0.13951  -0.05156 0.02508  72  LEU B C   
3051 O O   . LEU B 46  ? 1.01947 1.48176 0.82029 0.15181  -0.04703 0.01614  72  LEU B O   
3052 C CB  . LEU B 46  ? 0.85746 1.34410 0.73155 0.13112  -0.03755 0.03464  72  LEU B CB  
3053 C CG  . LEU B 46  ? 0.83184 1.31931 0.72193 0.13295  -0.03357 0.03336  72  LEU B CG  
3054 C CD1 . LEU B 46  ? 0.80012 1.31106 0.71015 0.13002  -0.01959 0.03963  72  LEU B CD1 
3055 C CD2 . LEU B 46  ? 0.84613 1.32588 0.71714 0.14603  -0.03375 0.02136  72  LEU B CD2 
3056 N N   . MET B 47  ? 1.05599 1.52045 0.88238 0.13044  -0.05514 0.03283  73  MET B N   
3057 C CA  . MET B 47  ? 1.07094 1.53506 0.87095 0.13463  -0.05445 0.03062  73  MET B CA  
3058 C C   . MET B 47  ? 1.08687 1.52082 0.85547 0.14048  -0.07008 0.02260  73  MET B C   
3059 O O   . MET B 47  ? 1.12044 1.54932 0.85986 0.14727  -0.06969 0.01844  73  MET B O   
3060 C CB  . MET B 47  ? 1.07848 1.55183 0.88938 0.12317  -0.05464 0.04122  73  MET B CB  
3061 C CG  . MET B 47  ? 1.09958 1.60209 0.91919 0.12310  -0.03725 0.04590  73  MET B CG  
3062 S SD  . MET B 47  ? 1.17231 1.68119 0.95801 0.13819  -0.02683 0.03724  73  MET B SD  
3063 C CE  . MET B 47  ? 1.20347 1.68936 0.95652 0.13756  -0.04001 0.03622  73  MET B CE  
3064 N N   . ALA B 48  ? 1.06111 1.47349 0.83417 0.13774  -0.08446 0.02093  74  ALA B N   
3065 C CA  . ALA B 48  ? 1.07878 1.46197 0.82005 0.14666  -0.09794 0.01076  74  ALA B CA  
3066 C C   . ALA B 48  ? 1.06134 1.45099 0.78543 0.16251  -0.08587 0.00023  74  ALA B C   
3067 O O   . ALA B 48  ? 1.06830 1.45496 0.76186 0.17348  -0.08194 -0.00625 74  ALA B O   
3068 C CB  . ALA B 48  ? 1.08724 1.44853 0.84060 0.14016  -0.11483 0.01195  74  ALA B CB  
3069 N N   . GLY B 49  ? 1.04030 1.43937 0.78435 0.16402  -0.07938 -0.00094 75  GLY B N   
3070 C CA  . GLY B 49  ? 1.03160 1.43724 0.76474 0.17845  -0.06894 -0.01030 75  GLY B CA  
3071 C C   . GLY B 49  ? 1.02967 1.40959 0.75300 0.18427  -0.08138 -0.01872 75  GLY B C   
3072 O O   . GLY B 49  ? 1.05125 1.40854 0.77690 0.17652  -0.09823 -0.01675 75  GLY B O   
3073 N N   . SER B 50  ? 0.97810 1.36245 0.69148 0.19807  -0.07291 -0.02766 76  SER B N   
3074 C CA  . SER B 50  ? 0.95882 1.31997 0.66099 0.20575  -0.08310 -0.03680 76  SER B CA  
3075 C C   . SER B 50  ? 0.89492 1.24768 0.62412 0.19304  -0.09286 -0.03070 76  SER B C   
3076 O O   . SER B 50  ? 0.90287 1.22733 0.62251 0.19223  -0.10979 -0.03410 76  SER B O   
3077 C CB  . SER B 50  ? 1.00845 1.33700 0.67105 0.21413  -0.09828 -0.04550 76  SER B CB  
3078 O OG  . SER B 50  ? 1.02862 1.33036 0.68249 0.21819  -0.11231 -0.05265 76  SER B OG  
3079 N N   . THR B 51  ? 0.82644 1.20296 0.58888 0.18318  -0.08233 -0.02113 77  THR B N   
3080 C CA  . THR B 51  ? 0.76013 1.13096 0.54941 0.17041  -0.08947 -0.01307 77  THR B CA  
3081 C C   . THR B 51  ? 0.73507 1.09440 0.52771 0.17506  -0.09281 -0.01851 77  THR B C   
3082 O O   . THR B 51  ? 0.70707 1.05438 0.51567 0.16600  -0.10199 -0.01309 77  THR B O   
3083 C CB  . THR B 51  ? 0.69600 1.09417 0.51625 0.16040  -0.07625 -0.00179 77  THR B CB  
3084 O OG1 . THR B 51  ? 0.67463 1.09138 0.50458 0.16668  -0.06177 -0.00425 77  THR B OG1 
3085 C CG2 . THR B 51  ? 0.68816 1.10025 0.50347 0.15752  -0.07090 0.00267  77  THR B CG2 
3086 N N   . GLY B 52  ? 0.74628 1.10918 0.52491 0.18898  -0.08556 -0.02848 78  GLY B N   
3087 C CA  . GLY B 52  ? 0.72914 1.08276 0.51162 0.19371  -0.08774 -0.03361 78  GLY B CA  
3088 C C   . GLY B 52  ? 0.67741 1.05111 0.48950 0.18857  -0.07564 -0.02725 78  GLY B C   
3089 O O   . GLY B 52  ? 0.64977 1.01513 0.46665 0.19123  -0.07762 -0.03041 78  GLY B O   
3090 N N   . PHE B 53  ? 0.64255 1.04050 0.47304 0.18143  -0.06393 -0.01843 79  PHE B N   
3091 C CA  . PHE B 53  ? 0.61412 1.02961 0.47013 0.17699  -0.05268 -0.01231 79  PHE B CA  
3092 C C   . PHE B 53  ? 0.59651 1.03238 0.45039 0.18757  -0.03925 -0.01756 79  PHE B C   
3093 O O   . PHE B 53  ? 0.60493 1.05097 0.44439 0.19496  -0.03415 -0.02149 79  PHE B O   
3094 C CB  . PHE B 53  ? 0.60820 1.03787 0.48539 0.16390  -0.04774 0.00036  79  PHE B CB  
3095 C CG  . PHE B 53  ? 0.65016 1.06373 0.53214 0.15324  -0.06023 0.00707  79  PHE B CG  
3096 C CD1 . PHE B 53  ? 0.65636 1.07850 0.54509 0.14465  -0.05979 0.01531  79  PHE B CD1 
3097 C CD2 . PHE B 53  ? 0.68114 1.07135 0.56233 0.15142  -0.07289 0.00589  79  PHE B CD2 
3098 C CE1 . PHE B 53  ? 0.67267 1.08104 0.56815 0.13480  -0.07185 0.02220  79  PHE B CE1 
3099 C CE2 . PHE B 53  ? 0.69377 1.07051 0.58237 0.14102  -0.08494 0.01338  79  PHE B CE2 
3100 C CZ  . PHE B 53  ? 0.68718 1.07341 0.58359 0.13283  -0.08442 0.02158  79  PHE B CZ  
3101 N N   . ASP B 54  ? 0.57872 1.02025 0.44735 0.18832  -0.03364 -0.01700 80  ASP B N   
3102 C CA  . ASP B 54  ? 0.56118 1.02428 0.43442 0.19602  -0.02120 -0.01944 80  ASP B CA  
3103 C C   . ASP B 54  ? 0.50662 0.99140 0.40225 0.18717  -0.01076 -0.00906 80  ASP B C   
3104 O O   . ASP B 54  ? 0.47979 0.98613 0.37951 0.19142  -0.00064 -0.00875 80  ASP B O   
3105 C CB  . ASP B 54  ? 0.58564 1.03999 0.45864 0.20399  -0.02274 -0.02645 80  ASP B CB  
3106 C CG  . ASP B 54  ? 0.63598 1.06785 0.48547 0.21405  -0.03337 -0.03745 80  ASP B CG  
3107 O OD1 . ASP B 54  ? 0.64655 1.05476 0.49315 0.20958  -0.04516 -0.03770 80  ASP B OD1 
3108 O OD2 . ASP B 54  ? 0.66068 1.09821 0.49447 0.22670  -0.02996 -0.04544 80  ASP B OD2 
3109 N N   . LEU B 55  ? 0.49656 0.97584 0.40674 0.17533  -0.01315 -0.00019 81  LEU B N   
3110 C CA  . LEU B 55  ? 0.46499 0.96119 0.39436 0.16712  -0.00433 0.00973  81  LEU B CA  
3111 C C   . LEU B 55  ? 0.46596 0.95654 0.40339 0.15538  -0.00837 0.01891  81  LEU B C   
3112 O O   . LEU B 55  ? 0.47667 0.94878 0.41554 0.15141  -0.01679 0.02025  81  LEU B O   
3113 C CB  . LEU B 55  ? 0.44166 0.93667 0.38376 0.16720  -0.00067 0.01113  81  LEU B CB  
3114 C CG  . LEU B 55  ? 0.44499 0.95039 0.38532 0.17732  0.00463  0.00454  81  LEU B CG  
3115 C CD1 . LEU B 55  ? 0.44700 0.94471 0.39713 0.17687  0.00523  0.00562  81  LEU B CD1 
3116 C CD2 . LEU B 55  ? 0.43073 0.96218 0.37657 0.17764  0.01408  0.00804  81  LEU B CD2 
3117 N N   . VAL B 56  ? 0.46011 0.96692 0.40379 0.14979  -0.00264 0.02575  82  VAL B N   
3118 C CA  . VAL B 56  ? 0.45403 0.95834 0.40730 0.13891  -0.00556 0.03520  82  VAL B CA  
3119 C C   . VAL B 56  ? 0.43987 0.96009 0.40971 0.13296  0.00389  0.04418  82  VAL B C   
3120 O O   . VAL B 56  ? 0.44265 0.97863 0.41357 0.13646  0.01175  0.04324  82  VAL B O   
3121 C CB  . VAL B 56  ? 0.45189 0.95588 0.39216 0.13765  -0.01092 0.03453  82  VAL B CB  
3122 C CG1 . VAL B 56  ? 0.46945 0.95236 0.39213 0.14264  -0.02278 0.02642  82  VAL B CG1 
3123 C CG2 . VAL B 56  ? 0.45485 0.97856 0.38678 0.14263  -0.00251 0.03231  82  VAL B CG2 
3124 N N   . VAL B 57  ? 0.42833 0.94395 0.41150 0.12411  0.00272  0.05336  83  VAL B N   
3125 C CA  . VAL B 57  ? 0.39418 0.92122 0.39156 0.11866  0.01071  0.06220  83  VAL B CA  
3126 C C   . VAL B 57  ? 0.40732 0.94028 0.40923 0.11080  0.00932  0.06984  83  VAL B C   
3127 O O   . VAL B 57  ? 0.42745 0.95340 0.44097 0.10436  0.00703  0.07751  83  VAL B O   
3128 C CB  . VAL B 57  ? 0.36169 0.87792 0.37106 0.11658  0.01263  0.06705  83  VAL B CB  
3129 C CG1 . VAL B 57  ? 0.34006 0.86614 0.35918 0.11383  0.02118  0.07399  83  VAL B CG1 
3130 C CG2 . VAL B 57  ? 0.36372 0.86898 0.36664 0.12385  0.01092  0.05907  83  VAL B CG2 
3131 N N   . PRO B 58  ? 0.40304 0.94887 0.39658 0.11125  0.01079  0.06859  84  PRO B N   
3132 C CA  . PRO B 58  ? 0.38668 0.93772 0.38404 0.10356  0.00921  0.07612  84  PRO B CA  
3133 C C   . PRO B 58  ? 0.34582 0.91059 0.35469 0.09907  0.01724  0.08403  84  PRO B C   
3134 O O   . PRO B 58  ? 0.34122 0.91089 0.35442 0.10186  0.02350  0.08363  84  PRO B O   
3135 C CB  . PRO B 58  ? 0.41416 0.96997 0.39319 0.10728  0.00671  0.07021  84  PRO B CB  
3136 C CG  . PRO B 58  ? 0.41638 0.98138 0.38824 0.11623  0.01335  0.06292  84  PRO B CG  
3137 C CD  . PRO B 58  ? 0.40768 0.96314 0.38712 0.11927  0.01368  0.06041  84  PRO B CD  
3138 N N   . SER B 59  ? 0.34144 0.91096 0.35461 0.09211  0.01605  0.09128  85  SER B N   
3139 C CA  . SER B 59  ? 0.34542 0.92734 0.36694 0.08792  0.02255  0.09856  85  SER B CA  
3140 C C   . SER B 59  ? 0.37613 0.97430 0.38910 0.09119  0.02778  0.09533  85  SER B C   
3141 O O   . SER B 59  ? 0.39175 0.99275 0.39147 0.09646  0.02678  0.08829  85  SER B O   
3142 C CB  . SER B 59  ? 0.33847 0.92099 0.36592 0.07998  0.01913  0.10687  85  SER B CB  
3143 O OG  . SER B 59  ? 0.34108 0.91936 0.35798 0.07924  0.01144  0.10392  85  SER B OG  
3144 N N   . ALA B 60  ? 0.37910 0.98768 0.39982 0.08830  0.03339  0.10107  86  ALA B N   
3145 C CA  . ALA B 60  ? 0.38682 1.01283 0.40315 0.09014  0.03840  0.10024  86  ALA B CA  
3146 C C   . ALA B 60  ? 0.44652 1.08183 0.45472 0.08664  0.03750  0.10272  86  ALA B C   
3147 O O   . ALA B 60  ? 0.48614 1.13279 0.48450 0.09081  0.04053  0.09908  86  ALA B O   
3148 C CB  . ALA B 60  ? 0.35086 0.97502 0.37608 0.08645  0.04025  0.10560  86  ALA B CB  
3149 N N   . SER B 61  ? 0.45499 1.08535 0.46683 0.07948  0.03358  0.10917  87  SER B N   
3150 C CA  . SER B 61  ? 0.49432 1.13175 0.49771 0.07550  0.03196  0.11218  87  SER B CA  
3151 C C   . SER B 61  ? 0.53270 1.16251 0.51968 0.07963  0.02676  0.10519  87  SER B C   
3152 O O   . SER B 61  ? 0.56624 1.20342 0.53985 0.08037  0.02766  0.10450  87  SER B O   
3153 C CB  . SER B 61  ? 0.48813 1.12152 0.50085 0.06689  0.02844  0.12122  87  SER B CB  
3154 O OG  . SER B 61  ? 0.46470 1.10141 0.49010 0.06412  0.03255  0.12720  87  SER B OG  
3155 N N   . PHE B 62  ? 0.55539 1.16929 0.54179 0.08250  0.02100  0.10024  88  PHE B N   
3156 C CA  . PHE B 62  ? 0.63437 1.23826 0.60285 0.08747  0.01485  0.09262  88  PHE B CA  
3157 C C   . PHE B 62  ? 0.66336 1.27598 0.61800 0.09709  0.02097  0.08470  88  PHE B C   
3158 O O   . PHE B 62  ? 0.68301 1.29637 0.61884 0.10108  0.02030  0.08090  88  PHE B O   
3159 C CB  . PHE B 62  ? 0.67708 1.26192 0.64974 0.08811  0.00686  0.08968  88  PHE B CB  
3160 C CG  . PHE B 62  ? 0.73663 1.30699 0.69042 0.09233  -0.00222 0.08237  88  PHE B CG  
3161 C CD1 . PHE B 62  ? 0.76745 1.33059 0.71212 0.08781  -0.01059 0.08481  88  PHE B CD1 
3162 C CD2 . PHE B 62  ? 0.75553 1.31755 0.69940 0.10103  -0.00340 0.07295  88  PHE B CD2 
3163 C CE1 . PHE B 62  ? 0.79716 1.34376 0.72195 0.09190  -0.02045 0.07795  88  PHE B CE1 
3164 C CE2 . PHE B 62  ? 0.78950 1.33542 0.71365 0.10546  -0.01283 0.06592  88  PHE B CE2 
3165 C CZ  . PHE B 62  ? 0.80709 1.34464 0.72105 0.10089  -0.02160 0.06840  88  PHE B CZ  
3166 N N   . LEU B 63  ? 0.66272 1.28155 0.62607 0.10144  0.02706  0.08241  89  LEU B N   
3167 C CA  . LEU B 63  ? 0.67525 1.30552 0.62973 0.11068  0.03382  0.07619  89  LEU B CA  
3168 C C   . LEU B 63  ? 0.68871 1.33911 0.63990 0.10928  0.04108  0.08113  89  LEU B C   
3169 O O   . LEU B 63  ? 0.70484 1.36300 0.64169 0.11685  0.04547  0.07669  89  LEU B O   
3170 C CB  . LEU B 63  ? 0.66326 1.29663 0.63092 0.11398  0.03797  0.07454  89  LEU B CB  
3171 C CG  . LEU B 63  ? 0.65883 1.30728 0.62403 0.12283  0.04553  0.06999  89  LEU B CG  
3172 C CD1 . LEU B 63  ? 0.65658 1.29427 0.62195 0.13052  0.04359  0.06184  89  LEU B CD1 
3173 C CD2 . LEU B 63  ? 0.64409 1.30140 0.62555 0.11680  0.04847  0.07729  89  LEU B CD2 
3174 N N   . GLU B 64  ? 0.68592 1.34463 0.64982 0.10000  0.04266  0.09073  90  GLU B N   
3175 C CA  . GLU B 64  ? 0.70481 1.37293 0.66948 0.09623  0.04518  0.09553  90  GLU B CA  
3176 C C   . GLU B 64  ? 0.71905 1.38597 0.66307 0.09696  0.04359  0.09472  90  GLU B C   
3177 O O   . GLU B 64  ? 0.71937 1.39117 0.65603 0.10015  0.04709  0.09345  90  GLU B O   
3178 C CB  . GLU B 64  ? 0.70737 1.37607 0.68885 0.08558  0.04336  0.10508  90  GLU B CB  
3179 C CG  . GLU B 64  ? 0.73097 1.40695 0.71302 0.08017  0.04414  0.11093  90  GLU B CG  
3180 C CD  . GLU B 64  ? 0.73904 1.41354 0.73563 0.07066  0.04145  0.11968  90  GLU B CD  
3181 O OE1 . GLU B 64  ? 0.73583 1.40212 0.74075 0.06852  0.03922  0.12125  90  GLU B OE1 
3182 O OE2 . GLU B 64  ? 0.74700 1.42756 0.74556 0.06576  0.04166  0.12509  90  GLU B OE2 
3183 N N   . ARG B 65  ? 0.72491 1.37823 0.66189 0.09342  0.03560  0.09513  91  ARG B N   
3184 C CA  . ARG B 65  ? 0.74497 1.38961 0.66155 0.09331  0.03020  0.09393  91  ARG B CA  
3185 C C   . ARG B 65  ? 0.77315 1.41013 0.66668 0.10492  0.02998  0.08357  91  ARG B C   
3186 O O   . ARG B 65  ? 0.79783 1.43197 0.66964 0.10761  0.02923  0.08222  91  ARG B O   
3187 C CB  . ARG B 65  ? 0.73309 1.35931 0.65414 0.08575  0.01833  0.09667  91  ARG B CB  
3188 C CG  . ARG B 65  ? 0.71116 1.34352 0.65068 0.07496  0.01814  0.10734  91  ARG B CG  
3189 C CD  . ARG B 65  ? 0.71295 1.32839 0.65888 0.06846  0.00679  0.11052  91  ARG B CD  
3190 N NE  . ARG B 65  ? 0.73201 1.32924 0.66252 0.07267  -0.00264 0.10333  91  ARG B NE  
3191 C CZ  . ARG B 65  ? 0.73289 1.31545 0.67146 0.07299  -0.00980 0.10091  91  ARG B CZ  
3192 N NH1 . ARG B 65  ? 0.70664 1.29105 0.66788 0.07000  -0.00723 0.10511  91  ARG B NH1 
3193 N NH2 . ARG B 65  ? 0.76075 1.32566 0.68374 0.07642  -0.01978 0.09466  91  ARG B NH2 
3194 N N   . GLN B 66  ? 0.76805 1.40005 0.66399 0.11235  0.03037  0.07618  92  GLN B N   
3195 C CA  . GLN B 66  ? 0.78943 1.41358 0.66328 0.12474  0.03039  0.06579  92  GLN B CA  
3196 C C   . GLN B 66  ? 0.77878 1.42269 0.65535 0.13384  0.04288  0.06320  92  GLN B C   
3197 O O   . GLN B 66  ? 0.78868 1.42708 0.65864 0.14403  0.04335  0.05455  92  GLN B O   
3198 C CB  . GLN B 66  ? 0.79475 1.39545 0.66656 0.12716  0.01958  0.05869  92  GLN B CB  
3199 C CG  . GLN B 66  ? 0.81016 1.38758 0.65918 0.12787  0.00729  0.05467  92  GLN B CG  
3200 C CD  . GLN B 66  ? 0.77814 1.34722 0.63726 0.11515  -0.00216 0.06278  92  GLN B CD  
3201 O OE1 . GLN B 66  ? 0.74576 1.31680 0.62927 0.10739  -0.00330 0.06858  92  GLN B OE1 
3202 N NE2 . GLN B 66  ? 0.79427 1.35348 0.63407 0.11350  -0.00888 0.06345  92  GLN B NE2 
3203 N N   . LEU B 67  ? 0.75508 1.41375 0.64872 0.12870  0.04978  0.07018  93  LEU B N   
3204 C CA  . LEU B 67  ? 0.75005 1.41955 0.65537 0.13458  0.05723  0.06879  93  LEU B CA  
3205 C C   . LEU B 67  ? 0.77686 1.44459 0.66188 0.14603  0.06173  0.06267  93  LEU B C   
3206 O O   . LEU B 67  ? 0.78824 1.45813 0.67318 0.15613  0.06561  0.05685  93  LEU B O   
3207 C CB  . LEU B 67  ? 0.72981 1.41190 0.65712 0.12481  0.06004  0.07897  93  LEU B CB  
3208 C CG  . LEU B 67  ? 0.69934 1.38264 0.64925 0.11696  0.05728  0.08388  93  LEU B CG  
3209 C CD1 . LEU B 67  ? 0.69062 1.38154 0.65509 0.10668  0.05754  0.09408  93  LEU B CD1 
3210 C CD2 . LEU B 67  ? 0.69317 1.37692 0.65110 0.12388  0.05885  0.07888  93  LEU B CD2 
3211 N N   . THR B 68  ? 0.78284 1.44539 0.64972 0.14504  0.06124  0.06403  94  THR B N   
3212 C CA  . THR B 68  ? 0.79591 1.45425 0.64080 0.15616  0.06610  0.05884  94  THR B CA  
3213 C C   . THR B 68  ? 0.81784 1.45401 0.63092 0.16533  0.05924  0.04859  94  THR B C   
3214 O O   . THR B 68  ? 0.83861 1.46700 0.62975 0.17646  0.06268  0.04283  94  THR B O   
3215 C CB  . THR B 68  ? 0.79025 1.45322 0.63069 0.15059  0.06978  0.06624  94  THR B CB  
3216 O OG1 . THR B 68  ? 0.80091 1.44951 0.62429 0.14439  0.06144  0.06708  94  THR B OG1 
3217 C CG2 . THR B 68  ? 0.76152 1.44295 0.63181 0.13964  0.07323  0.07701  94  THR B CG2 
3218 N N   . ALA B 69  ? 0.81164 1.43584 0.62065 0.16105  0.04870  0.04661  95  ALA B N   
3219 C CA  . ALA B 69  ? 0.84655 1.44627 0.62465 0.16865  0.03834  0.03738  95  ALA B CA  
3220 C C   . ALA B 69  ? 0.85874 1.45268 0.62899 0.18273  0.03995  0.02679  95  ALA B C   
3221 O O   . ALA B 69  ? 0.90898 1.48093 0.64985 0.19223  0.03287  0.01783  95  ALA B O   
3222 C CB  . ALA B 69  ? 0.86149 1.44716 0.64448 0.15814  0.02398  0.03976  95  ALA B CB  
3223 N N   . GLY B 70  ? 0.80507 1.41593 0.60016 0.18427  0.04768  0.02754  96  GLY B N   
3224 C CA  . GLY B 70  ? 0.79772 1.40458 0.58712 0.19795  0.04984  0.01798  96  GLY B CA  
3225 C C   . GLY B 70  ? 0.79242 1.38118 0.57117 0.20097  0.03835  0.01020  96  GLY B C   
3226 O O   . GLY B 70  ? 0.81725 1.39169 0.57675 0.21387  0.03567  -0.00007 96  GLY B O   
3227 N N   . VAL B 71  ? 0.77792 1.35929 0.57630 0.18741  0.02956  0.01526  97  VAL B N   
3228 C CA  . VAL B 71  ? 0.78498 1.34354 0.58639 0.18648  0.01735  0.00978  97  VAL B CA  
3229 C C   . VAL B 71  ? 0.75987 1.32947 0.58619 0.18656  0.02230  0.00999  97  VAL B C   
3230 O O   . VAL B 71  ? 0.76124 1.31408 0.58654 0.19029  0.01501  0.00344  97  VAL B O   
3231 C CB  . VAL B 71  ? 0.78213 1.32416 0.59002 0.17255  0.00443  0.01547  97  VAL B CB  
3232 C CG1 . VAL B 71  ? 0.74357 1.30327 0.58220 0.15954  0.00942  0.02667  97  VAL B CG1 
3233 C CG2 . VAL B 71  ? 0.79650 1.31135 0.60122 0.17289  -0.00973 0.00955  97  VAL B CG2 
3234 N N   . PHE B 72  ? 0.73195 1.32767 0.57933 0.18262  0.03357  0.01735  98  PHE B N   
3235 C CA  . PHE B 72  ? 0.69476 1.30065 0.56446 0.18278  0.03795  0.01801  98  PHE B CA  
3236 C C   . PHE B 72  ? 0.68084 1.30630 0.54944 0.19512  0.04929  0.01451  98  PHE B C   
3237 O O   . PHE B 72  ? 0.69040 1.32379 0.54942 0.20007  0.05525  0.01496  98  PHE B O   
3238 C CB  . PHE B 72  ? 0.67096 1.29012 0.56618 0.16934  0.04091  0.02926  98  PHE B CB  
3239 C CG  . PHE B 72  ? 0.67600 1.27770 0.57764 0.15801  0.03098  0.03341  98  PHE B CG  
3240 C CD1 . PHE B 72  ? 0.66117 1.27003 0.57320 0.14652  0.03166  0.04334  98  PHE B CD1 
3241 C CD2 . PHE B 72  ? 0.69250 1.27108 0.59079 0.15895  0.02102  0.02802  98  PHE B CD2 
3242 C CE1 . PHE B 72  ? 0.65740 1.25169 0.57719 0.13691  0.02327  0.04784  98  PHE B CE1 
3243 C CE2 . PHE B 72  ? 0.68471 1.24926 0.59159 0.14862  0.01267  0.03319  98  PHE B CE2 
3244 C CZ  . PHE B 72  ? 0.66745 1.24040 0.58554 0.13795  0.01416  0.04312  98  PHE B CZ  
3245 N N   . GLN B 73  ? 0.64351 1.27180 0.52614 0.19875  0.05048  0.01176  99  GLN B N   
3246 C CA  . GLN B 73  ? 0.61420 1.25561 0.50537 0.20772  0.05764  0.00977  99  GLN B CA  
3247 C C   . GLN B 73  ? 0.55270 1.20806 0.47335 0.19750  0.06061  0.01971  99  GLN B C   
3248 O O   . GLN B 73  ? 0.50904 1.16215 0.44250 0.18843  0.05749  0.02385  99  GLN B O   
3249 C CB  . GLN B 73  ? 0.63352 1.26478 0.51727 0.21957  0.05464  -0.00101 99  GLN B CB  
3250 C CG  . GLN B 73  ? 0.68769 1.30278 0.54122 0.23313  0.05139  -0.01192 99  GLN B CG  
3251 C CD  . GLN B 73  ? 0.72495 1.32804 0.57495 0.24431  0.04745  -0.02187 99  GLN B CD  
3252 O OE1 . GLN B 73  ? 0.72420 1.34188 0.59007 0.24925  0.05339  -0.02162 99  GLN B OE1 
3253 N NE2 . GLN B 73  ? 0.75682 1.33012 0.58785 0.24698  0.03536  -0.02989 99  GLN B NE2 
3254 N N   . PRO B 74  ? 0.54517 1.21309 0.47522 0.19866  0.06606  0.02407  100 PRO B N   
3255 C CA  . PRO B 74  ? 0.51293 1.19015 0.46704 0.18968  0.06686  0.03263  100 PRO B CA  
3256 C C   . PRO B 74  ? 0.49108 1.16333 0.45372 0.19373  0.06407  0.02797  100 PRO B C   
3257 O O   . PRO B 74  ? 0.48910 1.15781 0.44316 0.20609  0.06435  0.01912  100 PRO B O   
3258 C CB  . PRO B 74  ? 0.53668 1.22808 0.49459 0.19222  0.07353  0.03739  100 PRO B CB  
3259 C CG  . PRO B 74  ? 0.56317 1.25127 0.50022 0.20659  0.07672  0.02871  100 PRO B CG  
3260 C CD  . PRO B 74  ? 0.56521 1.23830 0.48273 0.20769  0.07174  0.02231  100 PRO B CD  
3261 N N   . LEU B 75  ? 0.46771 1.13805 0.44595 0.18365  0.06107  0.03381  101 LEU B N   
3262 C CA  . LEU B 75  ? 0.46606 1.12911 0.45157 0.18633  0.05776  0.02987  101 LEU B CA  
3263 C C   . LEU B 75  ? 0.47956 1.15175 0.47609 0.19015  0.06016  0.03111  101 LEU B C   
3264 O O   . LEU B 75  ? 0.47437 1.15609 0.48338 0.18244  0.06205  0.04007  101 LEU B O   
3265 C CB  . LEU B 75  ? 0.43397 1.08929 0.42963 0.17487  0.05398  0.03584  101 LEU B CB  
3266 C CG  . LEU B 75  ? 0.42076 1.06612 0.40832 0.17230  0.05136  0.03413  101 LEU B CG  
3267 C CD1 . LEU B 75  ? 0.39473 1.03237 0.39350 0.16176  0.04872  0.04108  101 LEU B CD1 
3268 C CD2 . LEU B 75  ? 0.42534 1.06243 0.40106 0.18380  0.04951  0.02306  101 LEU B CD2 
3269 N N   . ASP B 76  ? 0.49146 1.16078 0.48355 0.20216  0.05979  0.02231  102 ASP B N   
3270 C CA  . ASP B 76  ? 0.50914 1.18710 0.51240 0.20701  0.06181  0.02284  102 ASP B CA  
3271 C C   . ASP B 76  ? 0.49301 1.16760 0.51234 0.19913  0.05775  0.02743  102 ASP B C   
3272 O O   . ASP B 76  ? 0.49619 1.15935 0.51503 0.20260  0.05321  0.02165  102 ASP B O   
3273 C CB  . ASP B 76  ? 0.55137 1.22481 0.54411 0.22263  0.06163  0.01148  102 ASP B CB  
3274 C CG  . ASP B 76  ? 0.59350 1.27847 0.59720 0.22907  0.06508  0.01237  102 ASP B CG  
3275 O OD1 . ASP B 76  ? 0.59674 1.29381 0.61711 0.22101  0.06747  0.02206  102 ASP B OD1 
3276 O OD2 . ASP B 76  ? 0.62034 1.30208 0.61617 0.24244  0.06516  0.00349  102 ASP B OD2 
3277 N N   . LYS B 77  ? 0.47336 1.15719 0.50620 0.18897  0.05909  0.03789  103 LYS B N   
3278 C CA  . LYS B 77  ? 0.45998 1.14031 0.50693 0.18186  0.05495  0.04273  103 LYS B CA  
3279 C C   . LYS B 77  ? 0.47406 1.15588 0.52967 0.18985  0.05330  0.03846  103 LYS B C   
3280 O O   . LYS B 77  ? 0.47207 1.14643 0.53568 0.18709  0.04829  0.03922  103 LYS B O   
3281 C CB  . LYS B 77  ? 0.44794 1.13892 0.50693 0.17054  0.05642  0.05472  103 LYS B CB  
3282 C CG  . LYS B 77  ? 0.43671 1.12552 0.48853 0.16184  0.05707  0.05967  103 LYS B CG  
3283 C CD  . LYS B 77  ? 0.41421 1.08619 0.46059 0.15740  0.05243  0.05798  103 LYS B CD  
3284 C CE  . LYS B 77  ? 0.41990 1.08925 0.45701 0.15180  0.05324  0.06038  103 LYS B CE  
3285 N NZ  . LYS B 77  ? 0.43119 1.11038 0.47457 0.14248  0.05482  0.07054  103 LYS B NZ  
3286 N N   . SER B 78  ? 0.47251 1.16337 0.52644 0.20028  0.05727  0.03408  104 SER B N   
3287 C CA  . SER B 78  ? 0.46828 1.16029 0.53032 0.20897  0.05547  0.02939  104 SER B CA  
3288 C C   . SER B 78  ? 0.48239 1.15649 0.53577 0.21518  0.04932  0.01950  104 SER B C   
3289 O O   . SER B 78  ? 0.50487 1.17598 0.56684 0.21938  0.04527  0.01679  104 SER B O   
3290 C CB  . SER B 78  ? 0.44538 1.14963 0.50499 0.22023  0.06174  0.02631  104 SER B CB  
3291 O OG  . SER B 78  ? 0.44563 1.14394 0.50269 0.23254  0.05922  0.01672  104 SER B OG  
3292 N N   . LYS B 79  ? 0.46435 1.12664 0.50180 0.21592  0.04815  0.01442  105 LYS B N   
3293 C CA  . LYS B 79  ? 0.43534 1.08068 0.46435 0.22184  0.04254  0.00555  105 LYS B CA  
3294 C C   . LYS B 79  ? 0.38731 1.02097 0.41884 0.21213  0.03849  0.00967  105 LYS B C   
3295 O O   . LYS B 79  ? 0.36580 0.98512 0.39090 0.21615  0.03421  0.00369  105 LYS B O   
3296 C CB  . LYS B 79  ? 0.45385 1.09344 0.46357 0.23105  0.04351  -0.00346 105 LYS B CB  
3297 C CG  . LYS B 79  ? 0.49550 1.14621 0.49930 0.24069  0.04878  -0.00644 105 LYS B CG  
3298 C CD  . LYS B 79  ? 0.53612 1.17873 0.51783 0.25019  0.04886  -0.01555 105 LYS B CD  
3299 C CE  . LYS B 79  ? 0.56412 1.19134 0.53624 0.26187  0.04295  -0.02736 105 LYS B CE  
3300 N NZ  . LYS B 79  ? 0.59175 1.20866 0.53991 0.27159  0.04201  -0.03682 105 LYS B NZ  
3301 N N   . LEU B 80  ? 0.36804 1.00703 0.40844 0.20012  0.03979  0.01997  106 LEU B N   
3302 C CA  . LEU B 80  ? 0.35238 0.98065 0.39583 0.19137  0.03645  0.02505  106 LEU B CA  
3303 C C   . LEU B 80  ? 0.33794 0.97011 0.39664 0.18664  0.03370  0.03173  106 LEU B C   
3304 O O   . LEU B 80  ? 0.35275 0.99153 0.41862 0.17698  0.03484  0.04096  106 LEU B O   
3305 C CB  . LEU B 80  ? 0.33320 0.96216 0.37231 0.18166  0.03926  0.03141  106 LEU B CB  
3306 C CG  . LEU B 80  ? 0.36908 0.99167 0.39470 0.18366  0.04025  0.02682  106 LEU B CG  
3307 C CD1 . LEU B 80  ? 0.38483 0.99348 0.40478 0.19125  0.03652  0.01886  106 LEU B CD1 
3308 C CD2 . LEU B 80  ? 0.39689 1.03000 0.41418 0.18930  0.04405  0.02315  106 LEU B CD2 
3309 N N   . PRO B 81  ? 0.33576 0.96356 0.39973 0.19351  0.02906  0.02737  107 PRO B N   
3310 C CA  . PRO B 81  ? 0.36075 0.99324 0.44038 0.18967  0.02506  0.03381  107 PRO B CA  
3311 C C   . PRO B 81  ? 0.39393 1.01746 0.47571 0.18105  0.02122  0.04104  107 PRO B C   
3312 O O   . PRO B 81  ? 0.40966 1.03991 0.50367 0.17472  0.01860  0.04915  107 PRO B O   
3313 C CB  . PRO B 81  ? 0.36766 0.99375 0.44948 0.20024  0.01959  0.02607  107 PRO B CB  
3314 C CG  . PRO B 81  ? 0.36325 0.97503 0.42907 0.20741  0.01913  0.01682  107 PRO B CG  
3315 C CD  . PRO B 81  ? 0.34025 0.95791 0.39629 0.20519  0.02604  0.01656  107 PRO B CD  
3316 N N   . GLU B 82  ? 0.39717 1.00587 0.46779 0.18103  0.02062  0.03889  108 GLU B N   
3317 C CA  . GLU B 82  ? 0.40507 0.99911 0.47327 0.17315  0.01752  0.04557  108 GLU B CA  
3318 C C   . GLU B 82  ? 0.38460 0.98826 0.45319 0.16460  0.02286  0.05289  108 GLU B C   
3319 O O   . GLU B 82  ? 0.37179 0.95781 0.43308 0.15820  0.02171  0.05722  108 GLU B O   
3320 C CB  . GLU B 82  ? 0.45190 1.01339 0.50330 0.17473  0.01428  0.04032  108 GLU B CB  
3321 C CG  . GLU B 82  ? 0.50169 1.04998 0.55078 0.18263  0.00797  0.03329  108 GLU B CG  
3322 C CD  . GLU B 82  ? 0.56080 1.11468 0.62250 0.18233  0.00172  0.03736  108 GLU B CD  
3323 O OE1 . GLU B 82  ? 0.58435 1.12809 0.64572 0.17536  -0.00177 0.04458  108 GLU B OE1 
3324 O OE2 . GLU B 82  ? 0.57962 1.14754 0.65164 0.18929  -0.00021 0.03359  108 GLU B OE2 
3325 N N   . TRP B 83  ? 0.38937 1.00727 0.45932 0.16163  0.02780  0.05410  109 TRP B N   
3326 C CA  . TRP B 83  ? 0.39645 1.01851 0.46414 0.15233  0.03152  0.06099  109 TRP B CA  
3327 C C   . TRP B 83  ? 0.37737 1.00030 0.45350 0.14408  0.02841  0.07090  109 TRP B C   
3328 O O   . TRP B 83  ? 0.36248 0.98277 0.43528 0.13691  0.02992  0.07662  109 TRP B O   
3329 C CB  . TRP B 83  ? 0.40577 1.04319 0.47370 0.15194  0.03623  0.06109  109 TRP B CB  
3330 C CG  . TRP B 83  ? 0.40475 1.04572 0.46860 0.14357  0.03932  0.06714  109 TRP B CG  
3331 C CD1 . TRP B 83  ? 0.39180 1.04051 0.46281 0.13460  0.03933  0.07672  109 TRP B CD1 
3332 C CD2 . TRP B 83  ? 0.41770 1.05471 0.46988 0.14361  0.04187  0.06417  109 TRP B CD2 
3333 N NE1 . TRP B 83  ? 0.38984 1.03894 0.45373 0.12927  0.04182  0.07960  109 TRP B NE1 
3334 C CE2 . TRP B 83  ? 0.40918 1.05138 0.46196 0.13458  0.04324  0.07210  109 TRP B CE2 
3335 C CE3 . TRP B 83  ? 0.43658 1.06649 0.47847 0.15048  0.04238  0.05583  109 TRP B CE3 
3336 C CZ2 . TRP B 83  ? 0.44046 1.08096 0.48435 0.13230  0.04492  0.07185  109 TRP B CZ2 
3337 C CZ3 . TRP B 83  ? 0.45058 1.07967 0.48412 0.14802  0.04408  0.05592  109 TRP B CZ3 
3338 C CH2 . TRP B 83  ? 0.45581 1.09016 0.49060 0.13901  0.04527  0.06385  109 TRP B CH2 
3339 N N   . LYS B 84  ? 0.36048 0.98659 0.44767 0.14526  0.02304  0.07321  110 LYS B N   
3340 C CA  . LYS B 84  ? 0.34191 0.96792 0.43706 0.13830  0.01771  0.08269  110 LYS B CA  
3341 C C   . LYS B 84  ? 0.34308 0.94465 0.42636 0.13690  0.01435  0.08376  110 LYS B C   
3342 O O   . LYS B 84  ? 0.35330 0.94657 0.43661 0.13025  0.00981  0.09130  110 LYS B O   
3343 C CB  . LYS B 84  ? 0.35746 0.98858 0.46632 0.14023  0.01045  0.08446  110 LYS B CB  
3344 C CG  . LYS B 84  ? 0.38258 1.00144 0.48835 0.15015  0.00520  0.07654  110 LYS B CG  
3345 C CD  . LYS B 84  ? 0.41279 1.03701 0.53341 0.15162  -0.00296 0.07870  110 LYS B CD  
3346 C CE  . LYS B 84  ? 0.43072 1.03706 0.54460 0.16070  -0.00814 0.06966  110 LYS B CE  
3347 N NZ  . LYS B 84  ? 0.43634 1.04919 0.56662 0.16267  -0.01725 0.07203  110 LYS B NZ  
3348 N N   . ASN B 85  ? 0.33624 0.91858 0.40555 0.14169  0.01632  0.07638  111 ASN B N   
3349 C CA  . ASN B 85  ? 0.31492 0.86779 0.36946 0.13929  0.01503  0.07777  111 ASN B CA  
3350 C C   . ASN B 85  ? 0.30574 0.86169 0.35806 0.13235  0.01988  0.08402  111 ASN B C   
3351 O O   . ASN B 85  ? 0.30839 0.84447 0.35208 0.12901  0.01857  0.08857  111 ASN B O   
3352 C CB  . ASN B 85  ? 0.30354 0.83731 0.34595 0.14573  0.01634  0.06947  111 ASN B CB  
3353 C CG  . ASN B 85  ? 0.32887 0.85093 0.36969 0.15223  0.01000  0.06388  111 ASN B CG  
3354 O OD1 . ASN B 85  ? 0.28793 0.81172 0.33555 0.15155  0.00367  0.06681  111 ASN B OD1 
3355 N ND2 . ASN B 85  ? 0.29144 0.80069 0.32349 0.15825  0.01068  0.05616  111 ASN B ND2 
3356 N N   . LEU B 86  ? 0.29474 0.87418 0.35361 0.13073  0.02542  0.08434  112 LEU B N   
3357 C CA  . LEU B 86  ? 0.28284 0.86566 0.33989 0.12422  0.02945  0.09002  112 LEU B CA  
3358 C C   . LEU B 86  ? 0.30273 0.88998 0.36554 0.11685  0.02620  0.09955  112 LEU B C   
3359 O O   . LEU B 86  ? 0.31667 0.91813 0.39035 0.11564  0.02260  0.10253  112 LEU B O   
3360 C CB  . LEU B 86  ? 0.26164 0.86063 0.31924 0.12347  0.03427  0.08732  112 LEU B CB  
3361 C CG  . LEU B 86  ? 0.26983 0.86363 0.32023 0.13022  0.03637  0.07820  112 LEU B CG  
3362 C CD1 . LEU B 86  ? 0.27034 0.87445 0.31742 0.12921  0.03877  0.07559  112 LEU B CD1 
3363 C CD2 . LEU B 86  ? 0.27598 0.85248 0.31935 0.13012  0.03763  0.07836  112 LEU B CD2 
3364 N N   . ASP B 87  ? 0.33094 0.90584 0.38713 0.11198  0.02707  0.10480  113 ASP B N   
3365 C CA  . ASP B 87  ? 0.38884 0.96424 0.44797 0.10500  0.02310  0.11384  113 ASP B CA  
3366 C C   . ASP B 87  ? 0.40676 1.01202 0.47794 0.09952  0.02558  0.11865  113 ASP B C   
3367 O O   . ASP B 87  ? 0.40424 1.01326 0.47121 0.09777  0.03067  0.11682  113 ASP B O   
3368 C CB  . ASP B 87  ? 0.42989 0.98338 0.47764 0.10261  0.02408  0.11784  113 ASP B CB  
3369 C CG  . ASP B 87  ? 0.47352 1.02045 0.52043 0.09670  0.01823  0.12640  113 ASP B CG  
3370 O OD1 . ASP B 87  ? 0.50236 1.02540 0.53999 0.09865  0.01256  0.12726  113 ASP B OD1 
3371 O OD2 . ASP B 87  ? 0.48727 1.05134 0.54139 0.09018  0.01872  0.13233  113 ASP B OD2 
3372 N N   . PRO B 88  ? 0.43682 1.05530 0.51892 0.09542  0.02082  0.12462  114 PRO B N   
3373 C CA  . PRO B 88  ? 0.45635 1.09035 0.54277 0.08853  0.02338  0.12844  114 PRO B CA  
3374 C C   . PRO B 88  ? 0.48713 1.11986 0.56859 0.08143  0.02498  0.13442  114 PRO B C   
3375 O O   . PRO B 88  ? 0.49223 1.13207 0.57107 0.07795  0.02826  0.13458  114 PRO B O   
3376 C CB  . PRO B 88  ? 0.44799 1.09201 0.54796 0.08505  0.01691  0.13484  114 PRO B CB  
3377 C CG  . PRO B 88  ? 0.44589 1.07368 0.54455 0.08741  0.00820  0.13660  114 PRO B CG  
3378 C CD  . PRO B 88  ? 0.44778 1.05458 0.53218 0.09523  0.01171  0.12705  114 PRO B CD  
3379 N N   . GLU B 89  ? 0.50826 1.13206 0.58818 0.08012  0.02203  0.13953  115 GLU B N   
3380 C CA  . GLU B 89  ? 0.51756 1.13952 0.59306 0.07396  0.02355  0.14518  115 GLU B CA  
3381 C C   . GLU B 89  ? 0.50679 1.12152 0.57255 0.07563  0.02936  0.13903  115 GLU B C   
3382 O O   . GLU B 89  ? 0.52213 1.14183 0.58563 0.07080  0.03034  0.14044  115 GLU B O   
3383 C CB  . GLU B 89  ? 0.55945 1.15557 0.62572 0.07289  0.01838  0.14929  115 GLU B CB  
3384 C CG  . GLU B 89  ? 0.59894 1.19602 0.66527 0.06473  0.01511  0.15862  115 GLU B CG  
3385 C CD  . GLU B 89  ? 0.63273 1.19871 0.68575 0.06532  0.00989  0.16160  115 GLU B CD  
3386 O OE1 . GLU B 89  ? 0.64595 1.19046 0.68840 0.07230  0.01219  0.15643  115 GLU B OE1 
3387 O OE2 . GLU B 89  ? 0.65409 1.21621 0.70626 0.05917  0.00356  0.16935  115 GLU B OE2 
3388 N N   . LEU B 90  ? 0.49661 1.09941 0.55730 0.08256  0.03197  0.13260  116 LEU B N   
3389 C CA  . LEU B 90  ? 0.48676 1.08270 0.54063 0.08406  0.03536  0.12699  116 LEU B CA  
3390 C C   . LEU B 90  ? 0.46592 1.07243 0.51939 0.08500  0.03610  0.12124  116 LEU B C   
3391 O O   . LEU B 90  ? 0.47413 1.08163 0.52360 0.08365  0.03729  0.11937  116 LEU B O   
3392 C CB  . LEU B 90  ? 0.49742 1.07917 0.54731 0.09115  0.03783  0.12217  116 LEU B CB  
3393 C CG  . LEU B 90  ? 0.49707 1.06147 0.54296 0.09214  0.03758  0.12708  116 LEU B CG  
3394 C CD1 . LEU B 90  ? 0.50249 1.04618 0.54097 0.09908  0.03909  0.12149  116 LEU B CD1 
3395 C CD2 . LEU B 90  ? 0.47924 1.04069 0.52400 0.08735  0.03939  0.13366  116 LEU B CD2 
3396 N N   . LEU B 91  ? 0.44456 1.05986 0.50259 0.08797  0.03541  0.11878  117 LEU B N   
3397 C CA  . LEU B 91  ? 0.42461 1.05122 0.48220 0.09006  0.03714  0.11414  117 LEU B CA  
3398 C C   . LEU B 91  ? 0.40758 1.04489 0.46554 0.08343  0.03739  0.11978  117 LEU B C   
3399 O O   . LEU B 91  ? 0.40090 1.04255 0.45377 0.08464  0.03942  0.11647  117 LEU B O   
3400 C CB  . LEU B 91  ? 0.42542 1.06015 0.49010 0.09423  0.03644  0.11208  117 LEU B CB  
3401 C CG  . LEU B 91  ? 0.42533 1.05367 0.48751 0.10342  0.03711  0.10281  117 LEU B CG  
3402 C CD1 . LEU B 91  ? 0.41642 1.05151 0.48794 0.10686  0.03489  0.10235  117 LEU B CD1 
3403 C CD2 . LEU B 91  ? 0.43410 1.06525 0.48911 0.10819  0.04020  0.09541  117 LEU B CD2 
3404 N N   . LYS B 92  ? 0.40164 1.04375 0.46544 0.07664  0.03499  0.12866  118 LYS B N   
3405 C CA  . LYS B 92  ? 0.42406 1.07557 0.48813 0.06987  0.03485  0.13494  118 LYS B CA  
3406 C C   . LYS B 92  ? 0.45565 1.09911 0.51254 0.06746  0.03485  0.13495  118 LYS B C   
3407 O O   . LYS B 92  ? 0.47748 1.12784 0.53120 0.06565  0.03589  0.13516  118 LYS B O   
3408 C CB  . LYS B 92  ? 0.40771 1.06508 0.47997 0.06268  0.03138  0.14518  118 LYS B CB  
3409 C CG  . LYS B 92  ? 0.40239 1.06932 0.48513 0.06379  0.03025  0.14690  118 LYS B CG  
3410 C CD  . LYS B 92  ? 0.42135 1.09489 0.51349 0.05535  0.02553  0.15831  118 LYS B CD  
3411 C CE  . LYS B 92  ? 0.44824 1.13230 0.55386 0.05553  0.02327  0.16105  118 LYS B CE  
3412 N NZ  . LYS B 92  ? 0.45831 1.13302 0.56765 0.06014  0.01884  0.15800  118 LYS B NZ  
3413 N N   . LEU B 93  ? 0.45851 1.08799 0.51350 0.06777  0.03387  0.13523  119 LEU B N   
3414 C CA  . LEU B 93  ? 0.45069 1.07240 0.50124 0.06559  0.03388  0.13598  119 LEU B CA  
3415 C C   . LEU B 93  ? 0.46007 1.08387 0.50557 0.06928  0.03596  0.12899  119 LEU B C   
3416 O O   . LEU B 93  ? 0.45688 1.08503 0.49995 0.06601  0.03565  0.13069  119 LEU B O   
3417 C CB  . LEU B 93  ? 0.46019 1.06643 0.51022 0.06756  0.03404  0.13680  119 LEU B CB  
3418 C CG  . LEU B 93  ? 0.45354 1.05649 0.50616 0.06323  0.03200  0.14561  119 LEU B CG  
3419 C CD1 . LEU B 93  ? 0.44592 1.03297 0.49634 0.06703  0.03398  0.14609  119 LEU B CD1 
3420 C CD2 . LEU B 93  ? 0.44646 1.05568 0.49954 0.05583  0.02983  0.15197  119 LEU B CD2 
3421 N N   . VAL B 94  ? 0.46849 1.09013 0.51222 0.07637  0.03778  0.12130  120 VAL B N   
3422 C CA  . VAL B 94  ? 0.48900 1.11416 0.52730 0.08069  0.03949  0.11471  120 VAL B CA  
3423 C C   . VAL B 94  ? 0.50469 1.14525 0.54123 0.08169  0.04094  0.11361  120 VAL B C   
3424 O O   . VAL B 94  ? 0.52030 1.16657 0.55095 0.08378  0.04222  0.11047  120 VAL B O   
3425 C CB  . VAL B 94  ? 0.49200 1.11004 0.52852 0.08842  0.04072  0.10695  120 VAL B CB  
3426 C CG1 . VAL B 94  ? 0.50232 1.12155 0.53318 0.09189  0.04164  0.10181  120 VAL B CG1 
3427 C CG2 . VAL B 94  ? 0.48869 1.09242 0.52814 0.08828  0.04020  0.10909  120 VAL B CG2 
3428 N N   . ALA B 95  ? 0.53002 1.17835 0.57174 0.08063  0.04112  0.11669  121 ALA B N   
3429 C CA  . ALA B 95  ? 0.57010 1.23375 0.61160 0.08163  0.04351  0.11721  121 ALA B CA  
3430 C C   . ALA B 95  ? 0.59952 1.26923 0.63893 0.07532  0.04305  0.12302  121 ALA B C   
3431 O O   . ALA B 95  ? 0.62258 1.30335 0.65828 0.07737  0.04587  0.12217  121 ALA B O   
3432 C CB  . ALA B 95  ? 0.57326 1.24488 0.62354 0.08086  0.04373  0.12114  121 ALA B CB  
3433 N N   . LYS B 96  ? 0.58090 1.24346 0.62224 0.06822  0.03979  0.12902  122 LYS B N   
3434 C CA  . LYS B 96  ? 0.58908 1.25575 0.62787 0.06254  0.03876  0.13380  122 LYS B CA  
3435 C C   . LYS B 96  ? 0.57534 1.24226 0.60590 0.06629  0.04022  0.12817  122 LYS B C   
3436 O O   . LYS B 96  ? 0.59061 1.26492 0.61732 0.06360  0.04059  0.13060  122 LYS B O   
3437 C CB  . LYS B 96  ? 0.60470 1.26203 0.64679 0.05558  0.03493  0.14050  122 LYS B CB  
3438 C CG  . LYS B 96  ? 0.64140 1.29870 0.69031 0.05184  0.03296  0.14676  122 LYS B CG  
3439 C CD  . LYS B 96  ? 0.68234 1.35221 0.73463 0.04514  0.03173  0.15495  122 LYS B CD  
3440 C CE  . LYS B 96  ? 0.69957 1.36554 0.75662 0.03829  0.02755  0.16379  122 LYS B CE  
3441 N NZ  . LYS B 96  ? 0.71304 1.39190 0.77426 0.03115  0.02581  0.17270  122 LYS B NZ  
3442 N N   . HIS B 97  ? 0.56385 1.22329 0.59132 0.07234  0.04093  0.12112  123 HIS B N   
3443 C CA  . HIS B 97  ? 0.56761 1.22888 0.58652 0.07688  0.04223  0.11550  123 HIS B CA  
3444 C C   . HIS B 97  ? 0.57251 1.24124 0.58496 0.08587  0.04588  0.10805  123 HIS B C   
3445 O O   . HIS B 97  ? 0.58172 1.25610 0.58416 0.08933  0.04768  0.10493  123 HIS B O   
3446 C CB  . HIS B 97  ? 0.57319 1.22291 0.59257 0.07825  0.04082  0.11299  123 HIS B CB  
3447 C CG  . HIS B 97  ? 0.55594 1.19816 0.58070 0.07090  0.03811  0.12016  123 HIS B CG  
3448 N ND1 . HIS B 97  ? 0.55181 1.19624 0.57429 0.06743  0.03686  0.12315  123 HIS B ND1 
3449 C CD2 . HIS B 97  ? 0.54430 1.17680 0.57595 0.06705  0.03660  0.12514  123 HIS B CD2 
3450 C CE1 . HIS B 97  ? 0.54512 1.18174 0.57443 0.06181  0.03479  0.12977  123 HIS B CE1 
3451 N NE2 . HIS B 97  ? 0.54096 1.16957 0.57493 0.06189  0.03480  0.13081  123 HIS B NE2 
3452 N N   . ASP B 98  ? 0.55795 1.22614 0.57476 0.09022  0.04704  0.10517  124 ASP B N   
3453 C CA  . ASP B 98  ? 0.56172 1.23628 0.57344 0.09984  0.05059  0.09799  124 ASP B CA  
3454 C C   . ASP B 98  ? 0.55153 1.23500 0.57120 0.09947  0.05256  0.10173  124 ASP B C   
3455 O O   . ASP B 98  ? 0.51944 1.19906 0.54677 0.09955  0.05137  0.10199  124 ASP B O   
3456 C CB  . ASP B 98  ? 0.58587 1.25142 0.59562 0.10676  0.04994  0.09017  124 ASP B CB  
3457 C CG  . ASP B 98  ? 0.63002 1.30112 0.63497 0.11739  0.05315  0.08260  124 ASP B CG  
3458 O OD1 . ASP B 98  ? 0.66301 1.34212 0.65892 0.12223  0.05628  0.08022  124 ASP B OD1 
3459 O OD2 . ASP B 98  ? 0.64258 1.30926 0.65201 0.12148  0.05266  0.07897  124 ASP B OD2 
3460 N N   . PRO B 99  ? 0.58228 1.27811 0.60055 0.09916  0.05580  0.10516  125 PRO B N   
3461 C CA  . PRO B 99  ? 0.58854 1.29487 0.61677 0.09711  0.05771  0.11120  125 PRO B CA  
3462 C C   . PRO B 99  ? 0.59997 1.30866 0.63224 0.10512  0.05989  0.10623  125 PRO B C   
3463 O O   . PRO B 99  ? 0.60964 1.31814 0.63405 0.11485  0.06256  0.09795  125 PRO B O   
3464 C CB  . PRO B 99  ? 0.61024 1.32920 0.63376 0.09754  0.06217  0.11446  125 PRO B CB  
3465 C CG  . PRO B 99  ? 0.62000 1.33472 0.62848 0.10387  0.06359  0.10690  125 PRO B CG  
3466 C CD  . PRO B 99  ? 0.59596 1.29681 0.60301 0.10094  0.05825  0.10406  125 PRO B CD  
3467 N N   . ASP B 100 ? 0.59169 1.30243 0.63607 0.10110  0.05834  0.11146  126 ASP B N   
3468 C CA  . ASP B 100 ? 0.61757 1.33096 0.66895 0.10709  0.05947  0.10834  126 ASP B CA  
3469 C C   . ASP B 100 ? 0.58471 1.28478 0.63086 0.11351  0.05740  0.09882  126 ASP B C   
3470 O O   . ASP B 100 ? 0.59228 1.29402 0.64185 0.12056  0.05849  0.09415  126 ASP B O   
3471 C CB  . ASP B 100 ? 0.68070 1.40933 0.73285 0.11468  0.06584  0.10743  126 ASP B CB  
3472 C CG  . ASP B 100 ? 0.73526 1.47300 0.80206 0.11583  0.06685  0.11085  126 ASP B CG  
3473 O OD1 . ASP B 100 ? 0.75719 1.49294 0.82469 0.12419  0.06751  0.10380  126 ASP B OD1 
3474 O OD2 . ASP B 100 ? 0.75155 1.49874 0.82985 0.10829  0.06656  0.12088  126 ASP B OD2 
3475 N N   . ASN B 101 ? 0.56050 1.24791 0.59938 0.11123  0.05445  0.09633  127 ASN B N   
3476 C CA  . ASN B 101 ? 0.53720 1.21171 0.57160 0.11650  0.05249  0.08842  127 ASN B CA  
3477 C C   . ASN B 101 ? 0.54009 1.21796 0.56739 0.12825  0.05538  0.07904  127 ASN B C   
3478 O O   . ASN B 101 ? 0.54510 1.21892 0.57430 0.13445  0.05470  0.07354  127 ASN B O   
3479 C CB  . ASN B 101 ? 0.52753 1.19438 0.57073 0.11440  0.04950  0.09008  127 ASN B CB  
3480 C CG  . ASN B 101 ? 0.49811 1.15871 0.54556 0.10442  0.04643  0.09836  127 ASN B CG  
3481 O OD1 . ASN B 101 ? 0.47999 1.14479 0.53627 0.09973  0.04508  0.10492  127 ASN B OD1 
3482 N ND2 . ASN B 101 ? 0.47687 1.12788 0.51854 0.10145  0.04518  0.09843  127 ASN B ND2 
3483 N N   . LYS B 102 ? 0.52815 1.21290 0.54611 0.13200  0.05850  0.07701  128 LYS B N   
3484 C CA  . LYS B 102 ? 0.53911 1.22778 0.54875 0.14429  0.06183  0.06857  128 LYS B CA  
3485 C C   . LYS B 102 ? 0.52606 1.20417 0.52275 0.15092  0.05993  0.05941  128 LYS B C   
3486 O O   . LYS B 102 ? 0.53461 1.21074 0.52577 0.16150  0.06060  0.05110  128 LYS B O   
3487 C CB  . LYS B 102 ? 0.56681 1.26828 0.57118 0.14707  0.06720  0.07087  128 LYS B CB  
3488 C CG  . LYS B 102 ? 0.59263 1.30793 0.61006 0.14460  0.07072  0.07853  128 LYS B CG  
3489 C CD  . LYS B 102 ? 0.60786 1.32308 0.63808 0.14589  0.06916  0.07820  128 LYS B CD  
3490 C CE  . LYS B 102 ? 0.61953 1.33300 0.64462 0.15908  0.07071  0.06814  128 LYS B CE  
3491 N NZ  . LYS B 102 ? 0.61126 1.32465 0.64980 0.15955  0.06860  0.06837  128 LYS B NZ  
3492 N N   . PHE B 103 ? 0.50530 1.17681 0.49717 0.14519  0.05738  0.06094  129 PHE B N   
3493 C CA  . PHE B 103 ? 0.49646 1.15950 0.47561 0.15098  0.05561  0.05327  129 PHE B CA  
3494 C C   . PHE B 103 ? 0.44426 1.09605 0.42938 0.14700  0.05180  0.05345  129 PHE B C   
3495 O O   . PHE B 103 ? 0.45115 1.09623 0.42795 0.15343  0.05041  0.04640  129 PHE B O   
3496 C CB  . PHE B 103 ? 0.51687 1.18132 0.48315 0.14894  0.05592  0.05445  129 PHE B CB  
3497 C CG  . PHE B 103 ? 0.53064 1.20305 0.48609 0.15531  0.06021  0.05268  129 PHE B CG  
3498 C CD1 . PHE B 103 ? 0.53327 1.21607 0.49604 0.14936  0.06325  0.06078  129 PHE B CD1 
3499 C CD2 . PHE B 103 ? 0.56295 1.23093 0.49938 0.16774  0.06120  0.04303  129 PHE B CD2 
3500 C CE1 . PHE B 103 ? 0.56107 1.25121 0.51412 0.15561  0.06836  0.05992  129 PHE B CE1 
3501 C CE2 . PHE B 103 ? 0.59085 1.26408 0.51590 0.17459  0.06589  0.04159  129 PHE B CE2 
3502 C CZ  . PHE B 103 ? 0.58721 1.27233 0.52136 0.16848  0.07008  0.05037  129 PHE B CZ  
3503 N N   . ALA B 104 ? 0.40693 1.05559 0.40484 0.13731  0.05024  0.06131  130 ALA B N   
3504 C CA  . ALA B 104 ? 0.37990 1.01718 0.38286 0.13270  0.04755  0.06342  130 ALA B CA  
3505 C C   . ALA B 104 ? 0.36897 0.99908 0.38171 0.13175  0.04642  0.06476  130 ALA B C   
3506 O O   . ALA B 104 ? 0.37144 1.00594 0.39066 0.12845  0.04680  0.06914  130 ALA B O   
3507 C CB  . ALA B 104 ? 0.37202 1.00866 0.37821 0.12230  0.04656  0.07206  130 ALA B CB  
3508 N N   . MET B 105 ? 0.36093 0.98048 0.37446 0.13487  0.04502  0.06136  131 MET B N   
3509 C CA  . MET B 105 ? 0.32746 0.93755 0.34850 0.13356  0.04382  0.06344  131 MET B CA  
3510 C C   . MET B 105 ? 0.30051 0.89982 0.32514 0.12698  0.04324  0.06974  131 MET B C   
3511 O O   . MET B 105 ? 0.26709 0.85744 0.28880 0.12801  0.04204  0.06785  131 MET B O   
3512 C CB  . MET B 105 ? 0.33807 0.94351 0.35736 0.14332  0.04298  0.05503  131 MET B CB  
3513 C CG  . MET B 105 ? 0.34796 0.94225 0.37329 0.14295  0.04161  0.05697  131 MET B CG  
3514 S SD  . MET B 105 ? 0.37442 0.95007 0.39303 0.15184  0.03741  0.04721  131 MET B SD  
3515 C CE  . MET B 105 ? 0.38578 0.98122 0.40649 0.16133  0.03894  0.04073  131 MET B CE  
3516 N N   . PRO B 106 ? 0.29073 0.88656 0.32053 0.11987  0.04299  0.07746  132 PRO B N   
3517 C CA  . PRO B 106 ? 0.31592 0.90133 0.34834 0.11442  0.04320  0.08395  132 PRO B CA  
3518 C C   . PRO B 106 ? 0.32826 0.90059 0.36143 0.11896  0.04380  0.08212  132 PRO B C   
3519 O O   . PRO B 106 ? 0.32146 0.88726 0.35436 0.12277  0.04306  0.07986  132 PRO B O   
3520 C CB  . PRO B 106 ? 0.34494 0.93021 0.38116 0.10817  0.04261  0.09141  132 PRO B CB  
3521 C CG  . PRO B 106 ? 0.36118 0.95423 0.39920 0.11134  0.04183  0.08864  132 PRO B CG  
3522 C CD  . PRO B 106 ? 0.25847 0.86077 0.29244 0.11703  0.04253  0.08110  132 PRO B CD  
3523 N N   . TYR B 107 ? 0.33297 0.89350 0.36475 0.11704  0.04290  0.08326  133 TYR B N   
3524 C CA  . TYR B 107 ? 0.33533 0.87530 0.36517 0.11955  0.04189  0.08194  133 TYR B CA  
3525 C C   . TYR B 107 ? 0.31735 0.84583 0.35064 0.11600  0.04477  0.09044  133 TYR B C   
3526 O O   . TYR B 107 ? 0.33396 0.85144 0.36467 0.11859  0.04575  0.09105  133 TYR B O   
3527 C CB  . TYR B 107 ? 0.36242 0.89680 0.39016 0.11948  0.03867  0.07907  133 TYR B CB  
3528 C CG  . TYR B 107 ? 0.38737 0.90171 0.41423 0.12145  0.03718  0.07831  133 TYR B CG  
3529 C CD1 . TYR B 107 ? 0.40525 0.90945 0.42683 0.12751  0.03614  0.07235  133 TYR B CD1 
3530 C CD2 . TYR B 107 ? 0.27125 0.77723 0.30345 0.11710  0.03652  0.08413  133 TYR B CD2 
3531 C CE1 . TYR B 107 ? 0.28236 0.76783 0.30252 0.12899  0.03485  0.07223  133 TYR B CE1 
3532 C CE2 . TYR B 107 ? 0.27701 0.76584 0.30986 0.11845  0.03560  0.08473  133 TYR B CE2 
3533 C CZ  . TYR B 107 ? 0.28281 0.76107 0.30886 0.12432  0.03492  0.07874  133 TYR B CZ  
3534 O OH  . TYR B 107 ? 0.28966 0.75039 0.31579 0.12534  0.03411  0.07994  133 TYR B OH  
3535 N N   . MET B 108 ? 0.30033 0.83024 0.33851 0.11066  0.04591  0.09705  134 MET B N   
3536 C CA  . MET B 108 ? 0.31222 0.83302 0.35379 0.10793  0.04944  0.10577  134 MET B CA  
3537 C C   . MET B 108 ? 0.34168 0.87586 0.38793 0.10192  0.04988  0.11185  134 MET B C   
3538 O O   . MET B 108 ? 0.36706 0.91632 0.41377 0.09955  0.04765  0.10965  134 MET B O   
3539 C CB  . MET B 108 ? 0.28469 0.79097 0.32981 0.10806  0.05090  0.10929  134 MET B CB  
3540 C CG  . MET B 108 ? 0.27109 0.76326 0.31138 0.11333  0.04998  0.10380  134 MET B CG  
3541 S SD  . MET B 108 ? 0.29910 0.77291 0.33140 0.11843  0.05389  0.10510  134 MET B SD  
3542 C CE  . MET B 108 ? 0.30671 0.77330 0.33158 0.12436  0.04956  0.09452  134 MET B CE  
3543 N N   . TRP B 109 ? 0.34487 0.87219 0.39314 0.09997  0.05284  0.11962  135 TRP B N   
3544 C CA  . TRP B 109 ? 0.36636 0.89969 0.41733 0.09370  0.05155  0.12540  135 TRP B CA  
3545 C C   . TRP B 109 ? 0.39002 0.91107 0.44414 0.09317  0.05517  0.13383  135 TRP B C   
3546 O O   . TRP B 109 ? 0.39326 0.90144 0.44469 0.09813  0.05950  0.13556  135 TRP B O   
3547 C CB  . TRP B 109 ? 0.32922 0.86908 0.37591 0.09146  0.04882  0.12479  135 TRP B CB  
3548 C CG  . TRP B 109 ? 0.30501 0.83722 0.34779 0.09516  0.05031  0.12583  135 TRP B CG  
3549 C CD1 . TRP B 109 ? 0.29018 0.82041 0.32967 0.10083  0.05064  0.12046  135 TRP B CD1 
3550 C CD2 . TRP B 109 ? 0.30128 0.82736 0.34213 0.09399  0.05129  0.13291  135 TRP B CD2 
3551 N NE1 . TRP B 109 ? 0.27573 0.79310 0.30955 0.10231  0.04978  0.12322  135 TRP B NE1 
3552 C CE2 . TRP B 109 ? 0.28702 0.80220 0.32110 0.09850  0.05048  0.13092  135 TRP B CE2 
3553 C CE3 . TRP B 109 ? 0.28309 0.80747 0.32546 0.08961  0.05115  0.14020  135 TRP B CE3 
3554 C CZ2 . TRP B 109 ? 0.29770 0.79892 0.32492 0.09873  0.04910  0.13593  135 TRP B CZ2 
3555 C CZ3 . TRP B 109 ? 0.27339 0.78871 0.31036 0.09059  0.05171  0.14572  135 TRP B CZ3 
3556 C CH2 . TRP B 109 ? 0.29353 0.79470 0.32179 0.09494  0.04981  0.14318  135 TRP B CH2 
3557 N N   . ALA B 110 ? 0.39647 0.92150 0.45553 0.08782  0.05375  0.13923  136 ALA B N   
3558 C CA  . ALA B 110 ? 0.41418 0.92923 0.47699 0.08746  0.05698  0.14767  136 ALA B CA  
3559 C C   . ALA B 110 ? 0.43860 0.96002 0.50130 0.08187  0.05365  0.15173  136 ALA B C   
3560 O O   . ALA B 110 ? 0.45354 0.98672 0.51348 0.07803  0.04929  0.14842  136 ALA B O   
3561 C CB  . ALA B 110 ? 0.39231 0.90568 0.46598 0.08732  0.05915  0.15170  136 ALA B CB  
3562 N N   . THR B 111 ? 0.44543 0.95914 0.51104 0.08187  0.05611  0.15937  137 THR B N   
3563 C CA  . THR B 111 ? 0.43929 0.95803 0.50472 0.07716  0.05314  0.16414  137 THR B CA  
3564 C C   . THR B 111 ? 0.43779 0.95577 0.51285 0.07512  0.05402  0.17121  137 THR B C   
3565 O O   . THR B 111 ? 0.44275 0.95424 0.52516 0.07809  0.05790  0.17379  137 THR B O   
3566 C CB  . THR B 111 ? 0.42811 0.93874 0.48552 0.08003  0.05479  0.16737  137 THR B CB  
3567 O OG1 . THR B 111 ? 0.42844 0.92278 0.48445 0.08684  0.06144  0.17161  137 THR B OG1 
3568 C CG2 . THR B 111 ? 0.42318 0.93694 0.47311 0.08136  0.05308  0.16161  137 THR B CG2 
3569 N N   . THR B 112 ? 0.41997 0.94551 0.49601 0.06985  0.05025  0.17503  138 THR B N   
3570 C CA  . THR B 112 ? 0.40399 0.92980 0.48933 0.06782  0.05042  0.18266  138 THR B CA  
3571 C C   . THR B 112 ? 0.38853 0.90460 0.47044 0.07137  0.05368  0.18899  138 THR B C   
3572 O O   . THR B 112 ? 0.37730 0.89748 0.45326 0.06837  0.05050  0.19058  138 THR B O   
3573 C CB  . THR B 112 ? 0.40823 0.94882 0.49586 0.06008  0.04416  0.18322  138 THR B CB  
3574 O OG1 . THR B 112 ? 0.40474 0.95461 0.49150 0.05818  0.04161  0.17654  138 THR B OG1 
3575 C CG2 . THR B 112 ? 0.39665 0.93854 0.49631 0.05797  0.04370  0.19104  138 THR B CG2 
3576 N N   . GLY B 113 ? 0.39151 0.89461 0.47665 0.07811  0.06035  0.19314  139 GLY B N   
3577 C CA  . GLY B 113 ? 0.41644 0.90756 0.49521 0.08398  0.06510  0.19885  139 GLY B CA  
3578 C C   . GLY B 113 ? 0.43942 0.92584 0.52915 0.08712  0.06956  0.20725  139 GLY B C   
3579 O O   . GLY B 113 ? 0.42629 0.92233 0.52923 0.08210  0.06639  0.20994  139 GLY B O   
3580 N N   . ILE B 114 ? 0.45113 0.92183 0.53454 0.09607  0.07715  0.21174  140 ILE B N   
3581 C CA  . ILE B 114 ? 0.45523 0.92030 0.54787 0.10104  0.08277  0.22060  140 ILE B CA  
3582 C C   . ILE B 114 ? 0.49329 0.94481 0.58922 0.10918  0.09168  0.22212  140 ILE B C   
3583 O O   . ILE B 114 ? 0.51194 0.94849 0.59321 0.11647  0.09705  0.21988  140 ILE B O   
3584 C CB  . ILE B 114 ? 0.44276 0.89936 0.52318 0.10586  0.08498  0.22619  140 ILE B CB  
3585 C CG1 . ILE B 114 ? 0.41635 0.88567 0.49232 0.09669  0.07561  0.22540  140 ILE B CG1 
3586 C CG2 . ILE B 114 ? 0.45347 0.90584 0.54489 0.11189  0.09129  0.23552  140 ILE B CG2 
3587 C CD1 . ILE B 114 ? 0.41569 0.86992 0.47746 0.09988  0.07331  0.22933  140 ILE B CD1 
3588 N N   . GLY B 115 ? 0.50141 0.95748 0.61603 0.10765  0.09296  0.22656  141 GLY B N   
3589 C CA  . GLY B 115 ? 0.50078 0.94443 0.62129 0.11536  0.10227  0.23109  141 GLY B CA  
3590 C C   . GLY B 115 ? 0.51229 0.94895 0.63730 0.12276  0.10902  0.24073  141 GLY B C   
3591 O O   . GLY B 115 ? 0.51397 0.96050 0.64769 0.11907  0.10497  0.24513  141 GLY B O   
3592 N N   . TYR B 116 ? 0.51761 0.93663 0.63567 0.13386  0.11963  0.24409  142 TYR B N   
3593 C CA  . TYR B 116 ? 0.53575 0.94596 0.65345 0.14326  0.12716  0.25269  142 TYR B CA  
3594 C C   . TYR B 116 ? 0.52784 0.92085 0.64482 0.15445  0.13940  0.25756  142 TYR B C   
3595 O O   . TYR B 116 ? 0.51677 0.90081 0.62649 0.15633  0.14248  0.25339  142 TYR B O   
3596 C CB  . TYR B 116 ? 0.57783 0.97993 0.67275 0.14794  0.12675  0.25113  142 TYR B CB  
3597 C CG  . TYR B 116 ? 0.61464 0.99669 0.68374 0.15523  0.13084  0.24552  142 TYR B CG  
3598 C CD1 . TYR B 116 ? 0.61392 0.99930 0.67480 0.14864  0.12436  0.23652  142 TYR B CD1 
3599 C CD2 . TYR B 116 ? 0.64863 1.00702 0.70058 0.16925  0.14099  0.24923  142 TYR B CD2 
3600 C CE1 . TYR B 116 ? 0.63624 1.00245 0.67349 0.15501  0.12709  0.23173  142 TYR B CE1 
3601 C CE2 . TYR B 116 ? 0.66970 1.00650 0.69559 0.17583  0.14353  0.24387  142 TYR B CE2 
3602 C CZ  . TYR B 116 ? 0.66295 1.00396 0.68209 0.16828  0.13617  0.23532  142 TYR B CZ  
3603 O OH  . TYR B 116 ? 0.68285 1.00149 0.67596 0.17455  0.13755  0.23031  142 TYR B OH  
3604 N N   . ASN B 117 ? 0.53388 0.92250 0.65823 0.16221  0.14656  0.26690  143 ASN B N   
3605 C CA  . ASN B 117 ? 0.54996 0.92124 0.67207 0.17481  0.15957  0.27316  143 ASN B CA  
3606 C C   . ASN B 117 ? 0.57487 0.92487 0.66858 0.18833  0.16657  0.27254  143 ASN B C   
3607 O O   . ASN B 117 ? 0.57629 0.92648 0.66574 0.19228  0.16661  0.27622  143 ASN B O   
3608 C CB  . ASN B 117 ? 0.54453 0.92333 0.69160 0.17603  0.16359  0.28442  143 ASN B CB  
3609 C CG  . ASN B 117 ? 0.53737 0.89993 0.68418 0.18866  0.17751  0.29193  143 ASN B CG  
3610 O OD1 . ASN B 117 ? 0.53417 0.88041 0.66477 0.20230  0.18658  0.29524  143 ASN B OD1 
3611 N ND2 . ASN B 117 ? 0.52298 0.88983 0.68757 0.18448  0.17937  0.29531  143 ASN B ND2 
3612 N N   . VAL B 118 ? 0.58431 0.91458 0.65734 0.19564  0.17218  0.26808  144 VAL B N   
3613 C CA  . VAL B 118 ? 0.61767 0.92306 0.65887 0.20841  0.17751  0.26624  144 VAL B CA  
3614 C C   . VAL B 118 ? 0.64054 0.93503 0.68114 0.22215  0.18819  0.27584  144 VAL B C   
3615 O O   . VAL B 118 ? 0.65947 0.94877 0.68743 0.22712  0.18742  0.27745  144 VAL B O   
3616 C CB  . VAL B 118 ? 0.64155 0.92602 0.66210 0.21390  0.18176  0.26032  144 VAL B CB  
3617 C CG1 . VAL B 118 ? 0.66758 0.92517 0.65104 0.22329  0.18208  0.25544  144 VAL B CG1 
3618 C CG2 . VAL B 118 ? 0.62589 0.92507 0.65470 0.20049  0.17272  0.25276  144 VAL B CG2 
3619 N N   . ASP B 119 ? 0.64431 0.93527 0.69855 0.22824  0.19809  0.28296  145 ASP B N   
3620 C CA  . ASP B 119 ? 0.67447 0.95295 0.72708 0.24319  0.21010  0.29262  145 ASP B CA  
3621 C C   . ASP B 119 ? 0.65854 0.95249 0.72572 0.24147  0.20699  0.29888  145 ASP B C   
3622 O O   . ASP B 119 ? 0.67109 0.95189 0.72027 0.25299  0.21127  0.30110  145 ASP B O   
3623 C CB  . ASP B 119 ? 0.70100 0.97961 0.77254 0.24593  0.21938  0.30067  145 ASP B CB  
3624 C CG  . ASP B 119 ? 0.71698 0.99032 0.78429 0.24153  0.21903  0.29480  145 ASP B CG  
3625 O OD1 . ASP B 119 ? 0.70127 0.99301 0.79319 0.22916  0.21408  0.29567  145 ASP B OD1 
3626 O OD2 . ASP B 119 ? 0.74068 0.99031 0.77904 0.25068  0.22340  0.28930  145 ASP B OD2 
3627 N N   . LYS B 120 ? 0.63092 0.95130 0.72911 0.22729  0.19904  0.30157  146 LYS B N   
3628 C CA  . LYS B 120 ? 0.63787 0.97345 0.75223 0.22502  0.19573  0.30817  146 LYS B CA  
3629 C C   . LYS B 120 ? 0.63221 0.96972 0.72891 0.22270  0.18771  0.30276  146 LYS B C   
3630 O O   . LYS B 120 ? 0.61962 0.95499 0.71177 0.23023  0.19038  0.30828  146 LYS B O   
3631 C CB  . LYS B 120 ? 0.62736 0.98804 0.77629 0.20935  0.18734  0.31113  146 LYS B CB  
3632 C CG  . LYS B 120 ? 0.65394 1.01498 0.82411 0.21076  0.19490  0.31949  146 LYS B CG  
3633 C CD  . LYS B 120 ? 0.65710 1.04070 0.86085 0.19816  0.18705  0.32535  146 LYS B CD  
3634 C CE  . LYS B 120 ? 0.64884 1.04372 0.86705 0.18394  0.17875  0.32082  146 LYS B CE  
3635 N NZ  . LYS B 120 ? 0.64780 1.05889 0.89911 0.17491  0.17438  0.32909  146 LYS B NZ  
3636 N N   . VAL B 121 ? 0.64051 0.98183 0.72655 0.21217  0.17788  0.29268  147 VAL B N   
3637 C CA  . VAL B 121 ? 0.67055 1.01450 0.74000 0.20700  0.16870  0.28852  147 VAL B CA  
3638 C C   . VAL B 121 ? 0.76044 1.07605 0.79592 0.22172  0.17439  0.28972  147 VAL B C   
3639 O O   . VAL B 121 ? 0.78598 1.10036 0.81387 0.22287  0.17061  0.29397  147 VAL B O   
3640 C CB  . VAL B 121 ? 0.63292 0.98221 0.69390 0.19426  0.15789  0.27775  147 VAL B CB  
3641 C CG1 . VAL B 121 ? 0.63896 0.97788 0.67123 0.19202  0.14922  0.27368  147 VAL B CG1 
3642 C CG2 . VAL B 121 ? 0.59005 0.96823 0.67992 0.17799  0.14792  0.27645  147 VAL B CG2 
3643 N N   . LYS B 122 ? 0.81288 1.10168 0.82488 0.23307  0.18194  0.28588  148 LYS B N   
3644 C CA  . LYS B 122 ? 0.87398 1.12995 0.84911 0.24647  0.18407  0.28489  148 LYS B CA  
3645 C C   . LYS B 122 ? 0.86070 1.10453 0.83641 0.26479  0.19928  0.29410  148 LYS B C   
3646 O O   . LYS B 122 ? 0.86005 1.07519 0.80525 0.27706  0.20076  0.29333  148 LYS B O   
3647 C CB  . LYS B 122 ? 0.94374 1.17168 0.88677 0.24967  0.18194  0.27465  148 LYS B CB  
3648 C CG  . LYS B 122 ? 0.98638 1.20149 0.92716 0.25904  0.19415  0.27353  148 LYS B CG  
3649 C CD  . LYS B 122 ? 1.04701 1.22323 0.94522 0.26791  0.19251  0.26516  148 LYS B CD  
3650 C CE  . LYS B 122 ? 1.07068 1.23988 0.94868 0.25682  0.17403  0.25704  148 LYS B CE  
3651 N NZ  . LYS B 122 ? 1.05403 1.24724 0.94627 0.23910  0.16251  0.25195  148 LYS B NZ  
3652 N N   . ALA B 123 ? 0.83753 1.10049 0.84714 0.26625  0.20835  0.30245  149 ALA B N   
3653 C CA  . ALA B 123 ? 0.84453 1.10345 0.86156 0.28100  0.22027  0.31343  149 ALA B CA  
3654 C C   . ALA B 123 ? 0.79321 1.06890 0.82118 0.27668  0.21440  0.31915  149 ALA B C   
3655 O O   . ALA B 123 ? 0.78972 1.05535 0.81092 0.29064  0.22228  0.32659  149 ALA B O   
3656 C CB  . ALA B 123 ? 0.88044 1.15138 0.92930 0.28025  0.22762  0.32125  149 ALA B CB  
3657 N N   . VAL B 124 ? 0.74003 1.04076 0.78450 0.25783  0.20073  0.31622  150 VAL B N   
3658 C CA  . VAL B 124 ? 0.71556 1.02940 0.76975 0.25062  0.19025  0.31927  150 VAL B CA  
3659 C C   . VAL B 124 ? 0.76256 1.05203 0.78047 0.24780  0.17496  0.31028  150 VAL B C   
3660 O O   . VAL B 124 ? 0.77603 1.05731 0.78727 0.25093  0.16904  0.31251  150 VAL B O   
3661 C CB  . VAL B 124 ? 0.64722 0.99711 0.73824 0.23117  0.18042  0.31903  150 VAL B CB  
3662 C CG1 . VAL B 124 ? 0.62881 0.98771 0.72608 0.22090  0.16467  0.31819  150 VAL B CG1 
3663 C CG2 . VAL B 124 ? 0.63257 0.99649 0.75849 0.23193  0.18779  0.32644  150 VAL B CG2 
3664 N N   . LEU B 125 ? 0.79667 1.07343 0.79092 0.24205  0.16778  0.30058  151 LEU B N   
3665 C CA  . LEU B 125 ? 0.84315 1.10304 0.80993 0.23492  0.15033  0.29259  151 LEU B CA  
3666 C C   . LEU B 125 ? 0.92219 1.14272 0.84716 0.24577  0.15064  0.28600  151 LEU B C   
3667 O O   . LEU B 125 ? 0.91410 1.12264 0.81971 0.23658  0.13567  0.27684  151 LEU B O   
3668 C CB  . LEU B 125 ? 0.81182 1.09494 0.79176 0.21413  0.13623  0.28548  151 LEU B CB  
3669 C CG  . LEU B 125 ? 0.82124 1.12448 0.81813 0.20009  0.12226  0.28622  151 LEU B CG  
3670 C CD1 . LEU B 125 ? 0.82072 1.14846 0.83184 0.18155  0.11197  0.27991  151 LEU B CD1 
3671 C CD2 . LEU B 125 ? 0.85531 1.13457 0.82461 0.20182  0.11066  0.28475  151 LEU B CD2 
3672 N N   . GLY B 126 ? 1.01296 1.21225 0.92586 0.26395  0.16621  0.28823  152 GLY B N   
3673 C CA  . GLY B 126 ? 1.09592 1.25389 0.96882 0.27400  0.16515  0.27920  152 GLY B CA  
3674 C C   . GLY B 126 ? 1.11860 1.26943 0.98020 0.26869  0.16264  0.27033  152 GLY B C   
3675 O O   . GLY B 126 ? 1.09264 1.27072 0.97552 0.25494  0.15861  0.26944  152 GLY B O   
3676 N N   . GLU B 127 ? 1.14514 1.25809 0.97214 0.27957  0.16431  0.26332  153 GLU B N   
3677 C CA  . GLU B 127 ? 1.17113 1.27318 0.98541 0.27728  0.16343  0.25551  153 GLU B CA  
3678 C C   . GLU B 127 ? 1.20375 1.30276 1.00655 0.26127  0.14266  0.24672  153 GLU B C   
3679 O O   . GLU B 127 ? 1.21975 1.30233 1.00532 0.26038  0.13923  0.23940  153 GLU B O   
3680 C CB  . GLU B 127 ? 1.20854 1.26997 0.98953 0.29552  0.17322  0.25170  153 GLU B CB  
3681 C CG  . GLU B 127 ? 1.21910 1.28062 1.00353 0.30017  0.18533  0.25065  153 GLU B CG  
3682 C CD  . GLU B 127 ? 1.27003 1.30457 1.03668 0.32158  0.20312  0.25282  153 GLU B CD  
3683 O OE1 . GLU B 127 ? 1.26731 1.31817 1.05729 0.32805  0.21924  0.26029  153 GLU B OE1 
3684 O OE2 . GLU B 127 ? 1.31532 1.31174 1.04511 0.33165  0.20022  0.24707  153 GLU B OE2 
3685 N N   . ASN B 128 ? 1.22782 1.34249 1.04061 0.24876  0.12881  0.24777  154 ASN B N   
3686 C CA  . ASN B 128 ? 1.22571 1.34406 1.03410 0.23245  0.10977  0.24125  154 ASN B CA  
3687 C C   . ASN B 128 ? 1.17274 1.33375 1.01472 0.21685  0.10451  0.24544  154 ASN B C   
3688 O O   . ASN B 128 ? 1.22688 1.39432 1.06966 0.20452  0.08905  0.24381  154 ASN B O   
3689 C CB  . ASN B 128 ? 1.27619 1.36221 1.05541 0.23198  0.09432  0.23671  154 ASN B CB  
3690 C CG  . ASN B 128 ? 1.32993 1.37232 1.07272 0.24287  0.09406  0.22973  154 ASN B CG  
3691 O OD1 . ASN B 128 ? 1.33980 1.37740 1.07675 0.24256  0.09570  0.22517  154 ASN B OD1 
3692 N ND2 . ASN B 128 ? 1.37301 1.38236 1.09031 0.25253  0.09139  0.22858  154 ASN B ND2 
3693 N N   . ALA B 129 ? 1.06266 1.25265 0.93283 0.21675  0.11695  0.25087  155 ALA B N   
3694 C CA  . ALA B 129 ? 0.97832 1.20782 0.88014 0.20261  0.11267  0.25486  155 ALA B CA  
3695 C C   . ALA B 129 ? 0.90427 1.14732 0.80830 0.18742  0.10023  0.24780  155 ALA B C   
3696 O O   . ALA B 129 ? 0.90159 1.13950 0.79944 0.18828  0.10284  0.24261  155 ALA B O   
3697 C CB  . ALA B 129 ? 0.95449 1.20864 0.88545 0.20576  0.12817  0.26183  155 ALA B CB  
3698 N N   . PRO B 130 ? 0.84906 1.10946 0.76198 0.17369  0.08690  0.24755  156 PRO B N   
3699 C CA  . PRO B 130 ? 0.79181 1.06677 0.70810 0.15984  0.07599  0.24131  156 PRO B CA  
3700 C C   . PRO B 130 ? 0.71742 1.02316 0.66098 0.15285  0.08190  0.23939  156 PRO B C   
3701 O O   . PRO B 130 ? 0.71942 1.05255 0.68459 0.14125  0.07713  0.23978  156 PRO B O   
3702 C CB  . PRO B 130 ? 0.81039 1.09433 0.73019 0.14800  0.06171  0.24221  156 PRO B CB  
3703 C CG  . PRO B 130 ? 0.84080 1.10684 0.75233 0.15691  0.06345  0.24756  156 PRO B CG  
3704 C CD  . PRO B 130 ? 0.84075 1.10650 0.75976 0.17059  0.08097  0.25280  156 PRO B CD  
3705 N N   . VAL B 131 ? 0.64662 0.94625 0.58779 0.15994  0.09172  0.23719  157 VAL B N   
3706 C CA  . VAL B 131 ? 0.63161 0.95722 0.59734 0.15422  0.09709  0.23542  157 VAL B CA  
3707 C C   . VAL B 131 ? 0.61250 0.95052 0.57939 0.14297  0.08744  0.22745  157 VAL B C   
3708 O O   . VAL B 131 ? 0.61406 0.97783 0.60220 0.13466  0.08728  0.22544  157 VAL B O   
3709 C CB  . VAL B 131 ? 0.65604 0.97066 0.62039 0.16644  0.11213  0.23753  157 VAL B CB  
3710 C CG1 . VAL B 131 ? 0.64561 0.98665 0.63737 0.16041  0.11705  0.23717  157 VAL B CG1 
3711 C CG2 . VAL B 131 ? 0.65919 0.96005 0.62048 0.17936  0.12275  0.24608  157 VAL B CG2 
3712 N N   . ASP B 132 ? 0.60631 0.92634 0.55102 0.14272  0.07888  0.22313  158 ASP B N   
3713 C CA  . ASP B 132 ? 0.57534 0.90833 0.52248 0.13212  0.06910  0.21657  158 ASP B CA  
3714 C C   . ASP B 132 ? 0.53516 0.88716 0.49162 0.11951  0.05787  0.21750  158 ASP B C   
3715 O O   . ASP B 132 ? 0.52149 0.88037 0.47613 0.11145  0.04850  0.21357  158 ASP B O   
3716 C CB  . ASP B 132 ? 0.60068 0.90681 0.52222 0.13671  0.06368  0.21242  158 ASP B CB  
3717 C CG  . ASP B 132 ? 0.63366 0.91341 0.53249 0.14032  0.05588  0.21563  158 ASP B CG  
3718 O OD1 . ASP B 132 ? 0.64876 0.92760 0.54970 0.14223  0.05750  0.22125  158 ASP B OD1 
3719 O OD2 . ASP B 132 ? 0.66736 0.92631 0.54606 0.14121  0.04715  0.21262  158 ASP B OD2 
3720 N N   . SER B 133 ? 0.50782 0.86859 0.47465 0.11782  0.05880  0.22317  159 SER B N   
3721 C CA  . SER B 133 ? 0.46069 0.83672 0.43420 0.10654  0.04854  0.22516  159 SER B CA  
3722 C C   . SER B 133 ? 0.43536 0.83715 0.43280 0.10121  0.05207  0.22794  159 SER B C   
3723 O O   . SER B 133 ? 0.43384 0.83678 0.44151 0.10772  0.06179  0.23070  159 SER B O   
3724 C CB  . SER B 133 ? 0.47281 0.82671 0.42911 0.10973  0.04231  0.23002  159 SER B CB  
3725 O OG  . SER B 133 ? 0.46921 0.83375 0.42811 0.09760  0.03013  0.23074  159 SER B OG  
3726 N N   . TRP B 134 ? 0.40293 0.82509 0.40928 0.08920  0.04377  0.22775  160 TRP B N   
3727 C CA  . TRP B 134 ? 0.38581 0.82893 0.41142 0.08363  0.04459  0.23090  160 TRP B CA  
3728 C C   . TRP B 134 ? 0.41775 0.85202 0.44293 0.08669  0.04386  0.23821  160 TRP B C   
3729 O O   . TRP B 134 ? 0.43131 0.87894 0.47309 0.08469  0.04578  0.24188  160 TRP B O   
3730 C CB  . TRP B 134 ? 0.36051 0.82647 0.39287 0.07065  0.03650  0.22853  160 TRP B CB  
3731 C CG  . TRP B 134 ? 0.32195 0.80312 0.36172 0.06812  0.03918  0.22188  160 TRP B CG  
3732 C CD1 . TRP B 134 ? 0.31547 0.80050 0.34917 0.06491  0.03587  0.21659  160 TRP B CD1 
3733 C CD2 . TRP B 134 ? 0.29230 0.78594 0.34703 0.06891  0.04504  0.22007  160 TRP B CD2 
3734 N NE1 . TRP B 134 ? 0.29425 0.79299 0.33698 0.06439  0.03983  0.21106  160 TRP B NE1 
3735 C CE2 . TRP B 134 ? 0.28148 0.78486 0.33643 0.06654  0.04498  0.21299  160 TRP B CE2 
3736 C CE3 . TRP B 134 ? 0.27605 0.77337 0.34486 0.07128  0.04958  0.22421  160 TRP B CE3 
3737 C CZ2 . TRP B 134 ? 0.26326 0.77715 0.32961 0.06662  0.04852  0.20917  160 TRP B CZ2 
3738 C CZ3 . TRP B 134 ? 0.25679 0.76599 0.33858 0.07048  0.05283  0.22133  160 TRP B CZ3 
3739 C CH2 . TRP B 134 ? 0.25386 0.76848 0.33286 0.06822  0.05135  0.21302  160 TRP B CH2 
3740 N N   . ASP B 135 ? 0.44818 0.85899 0.45434 0.09180  0.04038  0.24042  161 ASP B N   
3741 C CA  . ASP B 135 ? 0.47300 0.87115 0.47625 0.09771  0.04093  0.24707  161 ASP B CA  
3742 C C   . ASP B 135 ? 0.48357 0.87925 0.49757 0.10889  0.05393  0.25047  161 ASP B C   
3743 O O   . ASP B 135 ? 0.48143 0.87495 0.50153 0.11297  0.05580  0.25669  161 ASP B O   
3744 C CB  . ASP B 135 ? 0.51367 0.88198 0.49066 0.10349  0.03535  0.24789  161 ASP B CB  
3745 C CG  . ASP B 135 ? 0.54125 0.90923 0.51101 0.09155  0.02222  0.24308  161 ASP B CG  
3746 O OD1 . ASP B 135 ? 0.57096 0.91773 0.52293 0.09432  0.01837  0.23920  161 ASP B OD1 
3747 O OD2 . ASP B 135 ? 0.54490 0.93313 0.52694 0.07938  0.01572  0.24356  161 ASP B OD2 
3748 N N   . LEU B 136 ? 0.49329 0.88938 0.51045 0.11399  0.06288  0.24712  162 LEU B N   
3749 C CA  . LEU B 136 ? 0.49951 0.89708 0.53074 0.12322  0.07563  0.25137  162 LEU B CA  
3750 C C   . LEU B 136 ? 0.50740 0.93000 0.56609 0.11625  0.07503  0.25554  162 LEU B C   
3751 O O   . LEU B 136 ? 0.51684 0.94031 0.58914 0.12314  0.08260  0.26238  162 LEU B O   
3752 C CB  . LEU B 136 ? 0.49561 0.89166 0.52625 0.12719  0.08346  0.24674  162 LEU B CB  
3753 C CG  . LEU B 136 ? 0.50657 0.90699 0.55422 0.13507  0.09680  0.25129  162 LEU B CG  
3754 C CD1 . LEU B 136 ? 0.51165 0.89052 0.54979 0.15006  0.10681  0.25800  162 LEU B CD1 
3755 C CD2 . LEU B 136 ? 0.52287 0.92379 0.56942 0.13580  0.10146  0.24568  162 LEU B CD2 
3756 N N   . ILE B 137 ? 0.48846 0.93092 0.55530 0.10305  0.06598  0.25199  163 ILE B N   
3757 C CA  . ILE B 137 ? 0.49263 0.95713 0.58338 0.09593  0.06399  0.25508  163 ILE B CA  
3758 C C   . ILE B 137 ? 0.48686 0.96181 0.57773 0.08473  0.05211  0.25571  163 ILE B C   
3759 O O   . ILE B 137 ? 0.48706 0.97490 0.59483 0.08031  0.04929  0.26006  163 ILE B O   
3760 C CB  . ILE B 137 ? 0.50173 0.98144 0.60469 0.09164  0.06621  0.25024  163 ILE B CB  
3761 C CG1 . ILE B 137 ? 0.50650 1.00316 0.63514 0.08797  0.06618  0.25508  163 ILE B CG1 
3762 C CG2 . ILE B 137 ? 0.50243 0.99140 0.59644 0.08165  0.05786  0.24253  163 ILE B CG2 
3763 C CD1 . ILE B 137 ? 0.49368 0.98626 0.63708 0.09794  0.07732  0.26178  163 ILE B CD1 
3764 N N   . LEU B 138 ? 0.47434 0.94426 0.54767 0.07951  0.04441  0.25231  164 LEU B N   
3765 C CA  . LEU B 138 ? 0.44819 0.92905 0.52138 0.06815  0.03359  0.25339  164 LEU B CA  
3766 C C   . LEU B 138 ? 0.46535 0.93108 0.52690 0.06975  0.02803  0.25859  164 LEU B C   
3767 O O   . LEU B 138 ? 0.48519 0.95768 0.54450 0.06023  0.01854  0.26021  164 LEU B O   
3768 C CB  . LEU B 138 ? 0.42053 0.91084 0.48561 0.05930  0.02820  0.24706  164 LEU B CB  
3769 C CG  . LEU B 138 ? 0.40681 0.91290 0.48222 0.05696  0.03207  0.24134  164 LEU B CG  
3770 C CD1 . LEU B 138 ? 0.40366 0.92234 0.47290 0.04791  0.02645  0.23619  164 LEU B CD1 
3771 C CD2 . LEU B 138 ? 0.39746 0.91691 0.49188 0.05459  0.03266  0.24414  164 LEU B CD2 
3772 N N   . LYS B 139 ? 0.47752 0.92190 0.53029 0.08187  0.03364  0.26140  165 LYS B N   
3773 C CA  . LYS B 139 ? 0.49211 0.92063 0.53463 0.08505  0.02860  0.26678  165 LYS B CA  
3774 C C   . LYS B 139 ? 0.46625 0.89863 0.52615 0.09071  0.03344  0.27346  165 LYS B C   
3775 O O   . LYS B 139 ? 0.44967 0.88069 0.51950 0.10058  0.04479  0.27511  165 LYS B O   
3776 C CB  . LYS B 139 ? 0.53964 0.93907 0.55854 0.09605  0.03083  0.26597  165 LYS B CB  
3777 C CG  . LYS B 139 ? 0.56621 0.95557 0.56619 0.08875  0.02026  0.26132  165 LYS B CG  
3778 C CD  . LYS B 139 ? 0.59563 0.95116 0.57266 0.09676  0.01658  0.26119  165 LYS B CD  
3779 C CE  . LYS B 139 ? 0.60859 0.95900 0.58260 0.08876  0.00480  0.26311  165 LYS B CE  
3780 N NZ  . LYS B 139 ? 0.64232 0.95719 0.59194 0.09671  -0.00008 0.26285  165 LYS B NZ  
3781 N N   . PRO B 140 ? 0.46639 0.90415 0.53160 0.08470  0.02520  0.27801  166 PRO B N   
3782 C CA  . PRO B 140 ? 0.47471 0.91687 0.55877 0.09017  0.02905  0.28497  166 PRO B CA  
3783 C C   . PRO B 140 ? 0.50542 0.92617 0.58281 0.10681  0.03811  0.28929  166 PRO B C   
3784 O O   . PRO B 140 ? 0.49693 0.92286 0.59333 0.11466  0.04674  0.29477  166 PRO B O   
3785 C CB  . PRO B 140 ? 0.47176 0.91967 0.55669 0.07995  0.01626  0.28825  166 PRO B CB  
3786 C CG  . PRO B 140 ? 0.48752 0.92578 0.54903 0.07320  0.00726  0.28463  166 PRO B CG  
3787 C CD  . PRO B 140 ? 0.46954 0.91079 0.52539 0.07226  0.01194  0.27767  166 PRO B CD  
3788 N N   . GLU B 141 ? 0.53086 0.92709 0.58153 0.11278  0.03632  0.28739  167 GLU B N   
3789 C CA  . GLU B 141 ? 0.56069 0.93292 0.60005 0.13006  0.04492  0.29113  167 GLU B CA  
3790 C C   . GLU B 141 ? 0.54100 0.91297 0.58784 0.14139  0.06098  0.29110  167 GLU B C   
3791 O O   . GLU B 141 ? 0.54256 0.90682 0.59488 0.15532  0.07182  0.29699  167 GLU B O   
3792 C CB  . GLU B 141 ? 0.62053 0.96380 0.62634 0.13331  0.03777  0.28820  167 GLU B CB  
3793 C CG  . GLU B 141 ? 0.65770 0.99696 0.65478 0.12349  0.02199  0.28949  167 GLU B CG  
3794 C CD  . GLU B 141 ? 0.66445 1.02051 0.66496 0.10446  0.01130  0.28353  167 GLU B CD  
3795 O OE1 . GLU B 141 ? 0.65494 1.02806 0.66384 0.10019  0.01563  0.28053  167 GLU B OE1 
3796 O OE2 . GLU B 141 ? 0.68000 1.03164 0.67461 0.09413  -0.00098 0.28196  167 GLU B OE2 
3797 N N   . ASN B 142 ? 0.52191 0.90233 0.56935 0.13601  0.06306  0.28504  168 ASN B N   
3798 C CA  . ASN B 142 ? 0.52804 0.90885 0.58265 0.14527  0.07751  0.28497  168 ASN B CA  
3799 C C   . ASN B 142 ? 0.49364 0.90160 0.58249 0.14105  0.08254  0.28898  168 ASN B C   
3800 O O   . ASN B 142 ? 0.49144 0.90031 0.59340 0.15127  0.09564  0.29391  168 ASN B O   
3801 C CB  . ASN B 142 ? 0.53843 0.91402 0.57728 0.14185  0.07661  0.27658  168 ASN B CB  
3802 C CG  . ASN B 142 ? 0.56639 0.91300 0.57166 0.14635  0.07086  0.27314  168 ASN B CG  
3803 O OD1 . ASN B 142 ? 0.58999 0.91350 0.57962 0.15821  0.07337  0.27683  168 ASN B OD1 
3804 N ND2 . ASN B 142 ? 0.55616 0.90316 0.55013 0.13720  0.06258  0.26632  168 ASN B ND2 
3805 N N   . LEU B 143 ? 0.45974 0.88907 0.56282 0.12613  0.07204  0.28742  169 LEU B N   
3806 C CA  . LEU B 143 ? 0.44225 0.89504 0.57662 0.12134  0.07398  0.29142  169 LEU B CA  
3807 C C   . LEU B 143 ? 0.44517 0.89959 0.59796 0.12901  0.07820  0.30156  169 LEU B C   
3808 O O   . LEU B 143 ? 0.43773 0.90455 0.61618 0.13219  0.08585  0.30739  169 LEU B O   
3809 C CB  . LEU B 143 ? 0.41706 0.88852 0.55784 0.10456  0.06079  0.28741  169 LEU B CB  
3810 C CG  . LEU B 143 ? 0.38109 0.87078 0.53839 0.09764  0.06176  0.28414  169 LEU B CG  
3811 C CD1 . LEU B 143 ? 0.36887 0.85033 0.51463 0.10313  0.07022  0.27844  169 LEU B CD1 
3812 C CD2 . LEU B 143 ? 0.35975 0.86384 0.51630 0.08260  0.04901  0.27923  169 LEU B CD2 
3813 N N   . GLU B 144 ? 0.45352 0.89548 0.59448 0.13218  0.07303  0.30430  170 GLU B N   
3814 C CA  . GLU B 144 ? 0.44875 0.89089 0.60628 0.14115  0.07744  0.31404  170 GLU B CA  
3815 C C   . GLU B 144 ? 0.43794 0.86918 0.59743 0.15903  0.09509  0.31919  170 GLU B C   
3816 O O   . GLU B 144 ? 0.41266 0.85377 0.59806 0.16579  0.10288  0.32837  170 GLU B O   
3817 C CB  . GLU B 144 ? 0.48353 0.91117 0.62382 0.14172  0.06784  0.31511  170 GLU B CB  
3818 C CG  . GLU B 144 ? 0.51254 0.95417 0.65853 0.12513  0.05159  0.31387  170 GLU B CG  
3819 C CD  . GLU B 144 ? 0.55943 0.98370 0.67960 0.12273  0.04047  0.31210  170 GLU B CD  
3820 O OE1 . GLU B 144 ? 0.59002 0.99009 0.68810 0.13451  0.04453  0.31194  170 GLU B OE1 
3821 O OE2 . GLU B 144 ? 0.56499 0.99861 0.68584 0.10908  0.02729  0.31110  170 GLU B OE2 
3822 N N   . LYS B 145 ? 0.45016 0.86103 0.58284 0.16701  0.10159  0.31401  171 LYS B N   
3823 C CA  . LYS B 145 ? 0.46964 0.86814 0.60033 0.18459  0.11926  0.31869  171 LYS B CA  
3824 C C   . LYS B 145 ? 0.46024 0.87590 0.61352 0.18312  0.12898  0.32020  171 LYS B C   
3825 O O   . LYS B 145 ? 0.48962 0.90718 0.65850 0.19504  0.14374  0.32851  171 LYS B O   
3826 C CB  . LYS B 145 ? 0.47313 0.84009 0.56382 0.19401  0.12151  0.31259  171 LYS B CB  
3827 C CG  . LYS B 145 ? 0.50758 0.85083 0.57477 0.20192  0.11622  0.31383  171 LYS B CG  
3828 C CD  . LYS B 145 ? 0.55346 0.86920 0.58109 0.20212  0.10875  0.30531  171 LYS B CD  
3829 C CE  . LYS B 145 ? 0.60319 0.89680 0.60827 0.20576  0.09860  0.30603  171 LYS B CE  
3830 N NZ  . LYS B 145 ? 0.62334 0.90121 0.59993 0.19639  0.08361  0.29800  171 LYS B NZ  
3831 N N   . LEU B 146 ? 0.43366 0.86166 0.58906 0.16911  0.12118  0.31280  172 LEU B N   
3832 C CA  . LEU B 146 ? 0.41567 0.85791 0.59005 0.16691  0.12855  0.31336  172 LEU B CA  
3833 C C   . LEU B 146 ? 0.40070 0.86674 0.61001 0.15621  0.12264  0.31807  172 LEU B C   
3834 O O   . LEU B 146 ? 0.38819 0.85319 0.60648 0.15102  0.12274  0.31549  172 LEU B O   
3835 C CB  . LEU B 146 ? 0.40923 0.84834 0.56490 0.15859  0.12305  0.30204  172 LEU B CB  
3836 C CG  . LEU B 146 ? 0.43708 0.84871 0.55834 0.16883  0.12872  0.29675  172 LEU B CG  
3837 C CD1 . LEU B 146 ? 0.43393 0.84101 0.53317 0.15813  0.11591  0.28583  172 LEU B CD1 
3838 C CD2 . LEU B 146 ? 0.43792 0.84506 0.56178 0.17833  0.14382  0.29871  172 LEU B CD2 
3839 N N   . LYS B 147 ? 0.39990 0.87799 0.62272 0.15119  0.11386  0.32263  173 LYS B N   
3840 C CA  . LYS B 147 ? 0.39608 0.88637 0.64455 0.13935  0.10503  0.32522  173 LYS B CA  
3841 C C   . LYS B 147 ? 0.41084 0.89446 0.67704 0.14450  0.11425  0.33179  173 LYS B C   
3842 O O   . LYS B 147 ? 0.40275 0.89234 0.68597 0.13441  0.10880  0.33145  173 LYS B O   
3843 C CB  . LYS B 147 ? 0.40068 0.90124 0.65905 0.13601  0.09532  0.33037  173 LYS B CB  
3844 C CG  . LYS B 147 ? 0.39840 0.90879 0.68060 0.12339  0.08516  0.33294  173 LYS B CG  
3845 C CD  . LYS B 147 ? 0.41640 0.93273 0.70727 0.12210  0.07656  0.33880  173 LYS B CD  
3846 C CE  . LYS B 147 ? 0.44581 0.95355 0.74229 0.13825  0.08792  0.34814  173 LYS B CE  
3847 N NZ  . LYS B 147 ? 0.44896 0.96079 0.75552 0.13670  0.07850  0.35380  173 LYS B NZ  
3848 N N   . SER B 148 ? 0.43523 0.90631 0.69731 0.16053  0.12826  0.33831  174 SER B N   
3849 C CA  . SER B 148 ? 0.45808 0.92399 0.73821 0.16573  0.13759  0.34626  174 SER B CA  
3850 C C   . SER B 148 ? 0.45165 0.91310 0.73240 0.16186  0.14027  0.34210  174 SER B C   
3851 O O   . SER B 148 ? 0.44325 0.91018 0.74674 0.15552  0.13864  0.34640  174 SER B O   
3852 C CB  . SER B 148 ? 0.49002 0.94132 0.76059 0.18508  0.15315  0.35347  174 SER B CB  
3853 O OG  . SER B 148 ? 0.51352 0.96938 0.78833 0.18927  0.15059  0.35877  174 SER B OG  
3854 N N   . CYS B 149 ? 0.46454 0.91610 0.72116 0.16553  0.14378  0.33404  175 CYS B N   
3855 C CA  A CYS B 149 ? 0.47117 0.91732 0.72681 0.16292  0.14642  0.32978  175 CYS B CA  
3856 C CA  B CYS B 149 ? 0.47106 0.91716 0.72656 0.16296  0.14644  0.32975  175 CYS B CA  
3857 C C   . CYS B 149 ? 0.45762 0.91628 0.71916 0.14636  0.13272  0.32176  175 CYS B C   
3858 O O   . CYS B 149 ? 0.45069 0.90636 0.71217 0.14334  0.13360  0.31784  175 CYS B O   
3859 C CB  A CYS B 149 ? 0.48844 0.91661 0.71510 0.17437  0.15586  0.32436  175 CYS B CB  
3860 C CB  B CYS B 149 ? 0.48809 0.91633 0.71445 0.17443  0.15577  0.32433  175 CYS B CB  
3861 S SG  A CYS B 149 ? 0.49339 0.92070 0.69108 0.17317  0.14918  0.31428  175 CYS B SG  
3862 S SG  B CYS B 149 ? 0.51502 0.92308 0.72953 0.19643  0.17394  0.33334  175 CYS B SG  
3863 N N   . GLY B 150 ? 0.45396 0.92592 0.71969 0.13613  0.12031  0.31944  176 GLY B N   
3864 C CA  . GLY B 150 ? 0.44540 0.92849 0.71616 0.12123  0.10751  0.31249  176 GLY B CA  
3865 C C   . GLY B 150 ? 0.44147 0.92589 0.68931 0.11670  0.10176  0.30127  176 GLY B C   
3866 O O   . GLY B 150 ? 0.44197 0.91637 0.67277 0.12207  0.10785  0.29577  176 GLY B O   
3867 N N   . VAL B 151 ? 0.41255 0.90912 0.65985 0.10656  0.08977  0.29803  177 VAL B N   
3868 C CA  . VAL B 151 ? 0.41180 0.91240 0.63958 0.10056  0.08319  0.28809  177 VAL B CA  
3869 C C   . VAL B 151 ? 0.39061 0.90212 0.62609 0.08725  0.07167  0.28309  177 VAL B C   
3870 O O   . VAL B 151 ? 0.38990 0.90955 0.64166 0.08054  0.06412  0.28754  177 VAL B O   
3871 C CB  . VAL B 151 ? 0.42245 0.92792 0.63947 0.10099  0.07963  0.28917  177 VAL B CB  
3872 C CG1 . VAL B 151 ? 0.41051 0.92372 0.61172 0.09165  0.07076  0.27999  177 VAL B CG1 
3873 C CG2 . VAL B 151 ? 0.43077 0.92399 0.63518 0.11535  0.09139  0.29297  177 VAL B CG2 
3874 N N   . SER B 152 ? 0.38070 0.89168 0.60398 0.08403  0.07019  0.27398  178 SER B N   
3875 C CA  . SER B 152 ? 0.39067 0.91098 0.61861 0.07331  0.06049  0.26872  178 SER B CA  
3876 C C   . SER B 152 ? 0.35181 0.87794 0.55983 0.06807  0.05465  0.25922  178 SER B C   
3877 O O   . SER B 152 ? 0.33230 0.85262 0.52308 0.07295  0.05943  0.25487  178 SER B O   
3878 C CB  . SER B 152 ? 0.43467 0.95037 0.67035 0.07436  0.06423  0.26740  178 SER B CB  
3879 O OG  . SER B 152 ? 0.46007 0.98545 0.70450 0.06468  0.05431  0.26468  178 SER B OG  
3880 N N   . PHE B 153 ? 0.33415 0.87154 0.54469 0.05821  0.04410  0.25645  179 PHE B N   
3881 C CA  . PHE B 153 ? 0.32213 0.86684 0.51544 0.05259  0.03840  0.24790  179 PHE B CA  
3882 C C   . PHE B 153 ? 0.29942 0.85040 0.49592 0.04683  0.03259  0.24249  179 PHE B C   
3883 O O   . PHE B 153 ? 0.30167 0.85447 0.51542 0.04404  0.02875  0.24671  179 PHE B O   
3884 C CB  . PHE B 153 ? 0.34277 0.89636 0.53225 0.04656  0.03078  0.25014  179 PHE B CB  
3885 C CG  . PHE B 153 ? 0.33718 0.88843 0.51362 0.05037  0.03436  0.25112  179 PHE B CG  
3886 C CD1 . PHE B 153 ? 0.33259 0.87321 0.50934 0.06029  0.04375  0.25540  179 PHE B CD1 
3887 C CD2 . PHE B 153 ? 0.33464 0.89455 0.49850 0.04413  0.02822  0.24849  179 PHE B CD2 
3888 C CE1 . PHE B 153 ? 0.33028 0.86892 0.49484 0.06396  0.04635  0.25699  179 PHE B CE1 
3889 C CE2 . PHE B 153 ? 0.33020 0.88502 0.48124 0.04654  0.02993  0.24962  179 PHE B CE2 
3890 C CZ  . PHE B 153 ? 0.32869 0.87018 0.47840 0.05633  0.03809  0.25322  179 PHE B CZ  
3891 N N   . LEU B 154 ? 0.28719 0.84177 0.46762 0.04532  0.03156  0.23354  180 LEU B N   
3892 C CA  . LEU B 154 ? 0.27327 0.83552 0.45454 0.04080  0.02574  0.22797  180 LEU B CA  
3893 C C   . LEU B 154 ? 0.29141 0.86518 0.47482 0.03264  0.01472  0.22911  180 LEU B C   
3894 O O   . LEU B 154 ? 0.30989 0.88742 0.48665 0.02968  0.01199  0.23098  180 LEU B O   
3895 C CB  . LEU B 154 ? 0.26244 0.82569 0.42561 0.04256  0.02829  0.21812  180 LEU B CB  
3896 C CG  . LEU B 154 ? 0.25389 0.80510 0.41237 0.05020  0.03723  0.21517  180 LEU B CG  
3897 C CD1 . LEU B 154 ? 0.22749 0.77977 0.36715 0.05117  0.03816  0.20598  180 LEU B CD1 
3898 C CD2 . LEU B 154 ? 0.25666 0.80545 0.42865 0.05173  0.03832  0.21611  180 LEU B CD2 
3899 N N   . ASP B 155 ? 0.29426 0.87302 0.48646 0.02900  0.00737  0.22832  181 ASP B N   
3900 C CA  . ASP B 155 ? 0.30058 0.88863 0.49079 0.02178  -0.00485 0.22802  181 ASP B CA  
3901 C C   . ASP B 155 ? 0.28281 0.87285 0.44913 0.02046  -0.00668 0.21716  181 ASP B C   
3902 O O   . ASP B 155 ? 0.24584 0.83496 0.40566 0.01728  -0.01496 0.21252  181 ASP B O   
3903 C CB  . ASP B 155 ? 0.31768 0.90457 0.52612 0.01837  -0.01400 0.23250  181 ASP B CB  
3904 C CG  . ASP B 155 ? 0.35563 0.94333 0.56030 0.01080  -0.02759 0.23356  181 ASP B CG  
3905 O OD1 . ASP B 155 ? 0.36742 0.95774 0.55782 0.00840  -0.02859 0.23240  181 ASP B OD1 
3906 O OD2 . ASP B 155 ? 0.36942 0.95411 0.58481 0.00701  -0.03793 0.23588  181 ASP B OD2 
3907 N N   . ALA B 156 ? 0.27470 0.86659 0.42748 0.02341  0.00102  0.21332  182 ALA B N   
3908 C CA  . ALA B 156 ? 0.27652 0.87228 0.40851 0.02306  0.00130  0.20407  182 ALA B CA  
3909 C C   . ALA B 156 ? 0.26684 0.86814 0.38735 0.01981  0.00162  0.20555  182 ALA B C   
3910 O O   . ALA B 156 ? 0.23300 0.83400 0.35109 0.02248  0.00829  0.20672  182 ALA B O   
3911 C CB  . ALA B 156 ? 0.23247 0.82585 0.36044 0.02948  0.00973  0.19817  182 ALA B CB  
3912 N N   . PRO B 157 ? 0.27228 0.87738 0.38455 0.01392  -0.00601 0.20590  183 PRO B N   
3913 C CA  . PRO B 157 ? 0.28114 0.89149 0.38360 0.01000  -0.00605 0.20876  183 PRO B CA  
3914 C C   . PRO B 157 ? 0.29325 0.90972 0.38233 0.01178  0.00053  0.20377  183 PRO B C   
3915 O O   . PRO B 157 ? 0.27823 0.89618 0.36542 0.01075  0.00327  0.20755  183 PRO B O   
3916 C CB  . PRO B 157 ? 0.28597 0.89799 0.37989 0.00391  -0.01559 0.20897  183 PRO B CB  
3917 C CG  . PRO B 157 ? 0.29923 0.90730 0.39187 0.00566  -0.01962 0.20308  183 PRO B CG  
3918 C CD  . PRO B 157 ? 0.28808 0.89101 0.39874 0.01042  -0.01576 0.20434  183 PRO B CD  
3919 N N   . GLU B 158 ? 0.31338 0.93298 0.39358 0.01455  0.00248  0.19571  184 GLU B N   
3920 C CA  . GLU B 158 ? 0.33785 0.96508 0.40751 0.01634  0.00847  0.19147  184 GLU B CA  
3921 C C   . GLU B 158 ? 0.33054 0.95369 0.40681 0.02029  0.01473  0.19299  184 GLU B C   
3922 O O   . GLU B 158 ? 0.32084 0.94233 0.39145 0.01880  0.01527  0.19472  184 GLU B O   
3923 C CB  . GLU B 158 ? 0.36366 0.99364 0.42427 0.02024  0.00964  0.18238  184 GLU B CB  
3924 C CG  . GLU B 158 ? 0.39632 1.02957 0.44369 0.01738  0.00417  0.17992  184 GLU B CG  
3925 C CD  . GLU B 158 ? 0.44234 1.06537 0.49390 0.01630  -0.00421 0.18002  184 GLU B CD  
3926 O OE1 . GLU B 158 ? 0.47012 1.09172 0.50843 0.01527  -0.00976 0.17660  184 GLU B OE1 
3927 O OE2 . GLU B 158 ? 0.45500 1.07090 0.52288 0.01667  -0.00544 0.18397  184 GLU B OE2 
3928 N N   . GLU B 159 ? 0.33134 0.94579 0.41678 0.02556  0.01740  0.19158  185 GLU B N   
3929 C CA  . GLU B 159 ? 0.32664 0.92621 0.41126 0.03056  0.02186  0.19073  185 GLU B CA  
3930 C C   . GLU B 159 ? 0.30213 0.89503 0.39065 0.02940  0.02161  0.19872  185 GLU B C   
3931 O O   . GLU B 159 ? 0.30205 0.88913 0.38480 0.03075  0.02292  0.19913  185 GLU B O   
3932 C CB  . GLU B 159 ? 0.34706 0.93782 0.43937 0.03634  0.02516  0.18810  185 GLU B CB  
3933 C CG  . GLU B 159 ? 0.35390 0.95356 0.44576 0.03724  0.02400  0.18172  185 GLU B CG  
3934 C CD  . GLU B 159 ? 0.35957 0.94972 0.45450 0.04345  0.02792  0.17738  185 GLU B CD  
3935 O OE1 . GLU B 159 ? 0.35946 0.93599 0.45451 0.04728  0.03220  0.17866  185 GLU B OE1 
3936 O OE2 . GLU B 159 ? 0.36511 0.95892 0.46046 0.04471  0.02592  0.17243  185 GLU B OE2 
3937 N N   . VAL B 160 ? 0.28650 0.88084 0.38592 0.02716  0.01919  0.20544  186 VAL B N   
3938 C CA  . VAL B 160 ? 0.28163 0.87062 0.38546 0.02700  0.01921  0.21345  186 VAL B CA  
3939 C C   . VAL B 160 ? 0.27454 0.87083 0.36881 0.02122  0.01583  0.21595  186 VAL B C   
3940 O O   . VAL B 160 ? 0.25586 0.84619 0.34677 0.02234  0.01698  0.21954  186 VAL B O   
3941 C CB  . VAL B 160 ? 0.28147 0.87093 0.40071 0.02578  0.01611  0.22013  186 VAL B CB  
3942 C CG1 . VAL B 160 ? 0.23033 0.81549 0.35331 0.02588  0.01560  0.22843  186 VAL B CG1 
3943 C CG2 . VAL B 160 ? 0.29587 0.87653 0.42615 0.03144  0.02005  0.21934  186 VAL B CG2 
3944 N N   . PHE B 161 ? 0.27935 0.88833 0.36840 0.01499  0.01160  0.21461  187 PHE B N   
3945 C CA  . PHE B 161 ? 0.26191 0.87725 0.34137 0.00877  0.00846  0.21763  187 PHE B CA  
3946 C C   . PHE B 161 ? 0.27812 0.88952 0.35009 0.01070  0.00976  0.21248  187 PHE B C   
3947 O O   . PHE B 161 ? 0.29322 0.90241 0.36359 0.00783  0.00756  0.21590  187 PHE B O   
3948 C CB  . PHE B 161 ? 0.25894 0.88460 0.33170 0.00291  0.00389  0.21626  187 PHE B CB  
3949 C CG  . PHE B 161 ? 0.28390 0.90702 0.35956 -0.00211 -0.00319 0.22244  187 PHE B CG  
3950 C CD1 . PHE B 161 ? 0.30249 0.92395 0.37599 -0.00658 -0.00646 0.22941  187 PHE B CD1 
3951 C CD2 . PHE B 161 ? 0.29733 0.91867 0.37779 -0.00259 -0.00775 0.22149  187 PHE B CD2 
3952 C CE1 . PHE B 161 ? 0.32904 0.94654 0.40558 -0.01117 -0.01308 0.23444  187 PHE B CE1 
3953 C CE2 . PHE B 161 ? 0.33717 0.95569 0.42102 -0.00733 -0.01534 0.22742  187 PHE B CE2 
3954 C CZ  . PHE B 161 ? 0.34170 0.95917 0.42344 -0.01137 -0.01792 0.23410  187 PHE B CZ  
3955 N N   . ALA B 162 ? 0.25828 0.86892 0.32739 0.01515  0.01283  0.20444  188 ALA B N   
3956 C CA  . ALA B 162 ? 0.26013 0.86819 0.32486 0.01707  0.01381  0.20030  188 ALA B CA  
3957 C C   . ALA B 162 ? 0.26129 0.85675 0.32813 0.02094  0.01576  0.20366  188 ALA B C   
3958 O O   . ALA B 162 ? 0.24241 0.83709 0.30690 0.01920  0.01422  0.20543  188 ALA B O   
3959 C CB  . ALA B 162 ? 0.25535 0.86449 0.31687 0.02173  0.01683  0.19141  188 ALA B CB  
3960 N N   . THR B 163 ? 0.24443 0.83024 0.31616 0.02626  0.01941  0.20523  189 THR B N   
3961 C CA  . THR B 163 ? 0.24855 0.82142 0.32032 0.03133  0.02253  0.20910  189 THR B CA  
3962 C C   . THR B 163 ? 0.24843 0.81938 0.31827 0.02731  0.01898  0.21736  189 THR B C   
3963 O O   . THR B 163 ? 0.25015 0.81119 0.31334 0.02846  0.01803  0.21928  189 THR B O   
3964 C CB  . THR B 163 ? 0.23392 0.79765 0.31300 0.03818  0.02794  0.20984  189 THR B CB  
3965 O OG1 . THR B 163 ? 0.23188 0.79480 0.31132 0.04132  0.03021  0.20199  189 THR B OG1 
3966 C CG2 . THR B 163 ? 0.39373 0.94269 0.46987 0.04508  0.03269  0.21407  189 THR B CG2 
3967 N N   . VAL B 164 ? 0.23920 0.81693 0.31327 0.02244  0.01584  0.22222  190 VAL B N   
3968 C CA  . VAL B 164 ? 0.24515 0.81807 0.31654 0.01828  0.01083  0.22916  190 VAL B CA  
3969 C C   . VAL B 164 ? 0.26818 0.84385 0.33432 0.01143  0.00619  0.22709  190 VAL B C   
3970 O O   . VAL B 164 ? 0.26450 0.82804 0.32577 0.01039  0.00322  0.22998  190 VAL B O   
3971 C CB  . VAL B 164 ? 0.27758 0.85783 0.35451 0.01383  0.00732  0.23449  190 VAL B CB  
3972 C CG1 . VAL B 164 ? 0.25250 0.82497 0.32719 0.00914  0.00128  0.23955  190 VAL B CG1 
3973 C CG2 . VAL B 164 ? 0.27150 0.84569 0.36043 0.02036  0.01113  0.23532  190 VAL B CG2 
3974 N N   . LEU B 165 ? 0.27388 0.86451 0.34074 0.00697  0.00546  0.22245  191 LEU B N   
3975 C CA  . LEU B 165 ? 0.28385 0.88065 0.34851 0.00021  0.00216  0.22214  191 LEU B CA  
3976 C C   . LEU B 165 ? 0.29958 0.88883 0.36095 0.00322  0.00302  0.22100  191 LEU B C   
3977 O O   . LEU B 165 ? 0.32715 0.91220 0.38609 -0.00188 -0.00099 0.22453  191 LEU B O   
3978 C CB  . LEU B 165 ? 0.24507 0.85890 0.31025 -0.00281 0.00212  0.21759  191 LEU B CB  
3979 C CG  . LEU B 165 ? 0.24766 0.86859 0.31294 -0.00802 -0.00020 0.21942  191 LEU B CG  
3980 C CD1 . LEU B 165 ? 0.24881 0.88262 0.31068 -0.00840 0.00082  0.21380  191 LEU B CD1 
3981 C CD2 . LEU B 165 ? 0.25375 0.87282 0.31867 -0.01640 -0.00463 0.22558  191 LEU B CD2 
3982 N N   . ASN B 166 ? 0.29287 0.87881 0.35342 0.01106  0.00760  0.21641  192 ASN B N   
3983 C CA  . ASN B 166 ? 0.31268 0.88929 0.36843 0.01446  0.00807  0.21568  192 ASN B CA  
3984 C C   . ASN B 166 ? 0.32820 0.88223 0.37687 0.01721  0.00578  0.22039  192 ASN B C   
3985 O O   . ASN B 166 ? 0.35502 0.89833 0.39750 0.01594  0.00154  0.22195  192 ASN B O   
3986 C CB  . ASN B 166 ? 0.29413 0.87004 0.34966 0.02254  0.01372  0.20933  192 ASN B CB  
3987 C CG  . ASN B 166 ? 0.32451 0.89063 0.37369 0.02626  0.01381  0.20869  192 ASN B CG  
3988 O OD1 . ASN B 166 ? 0.34137 0.91570 0.39089 0.02186  0.01053  0.20922  192 ASN B OD1 
3989 N ND2 . ASN B 166 ? 0.31934 0.86753 0.36243 0.03459  0.01735  0.20827  192 ASN B ND2 
3990 N N   . TYR B 167 ? 0.33458 0.88002 0.38368 0.02143  0.00782  0.22297  193 TYR B N   
3991 C CA  . TYR B 167 ? 0.35254 0.87513 0.39381 0.02587  0.00595  0.22725  193 TYR B CA  
3992 C C   . TYR B 167 ? 0.37758 0.89488 0.41586 0.01764  -0.00216 0.23121  193 TYR B C   
3993 O O   . TYR B 167 ? 0.39389 0.89048 0.42213 0.01940  -0.00658 0.23306  193 TYR B O   
3994 C CB  . TYR B 167 ? 0.36047 0.87911 0.40564 0.03259  0.01095  0.23046  193 TYR B CB  
3995 C CG  . TYR B 167 ? 0.38091 0.87708 0.41842 0.03850  0.00987  0.23549  193 TYR B CG  
3996 C CD1 . TYR B 167 ? 0.38844 0.86336 0.41465 0.04821  0.01296  0.23487  193 TYR B CD1 
3997 C CD2 . TYR B 167 ? 0.39820 0.89291 0.43839 0.03515  0.00577  0.24067  193 TYR B CD2 
3998 C CE1 . TYR B 167 ? 0.40455 0.85695 0.42140 0.05514  0.01248  0.23909  193 TYR B CE1 
3999 C CE2 . TYR B 167 ? 0.41937 0.89279 0.45181 0.04173  0.00494  0.24502  193 TYR B CE2 
4000 C CZ  . TYR B 167 ? 0.43831 0.89046 0.45865 0.05211  0.00857  0.24414  193 TYR B CZ  
4001 O OH  . TYR B 167 ? 0.47974 0.90884 0.48999 0.06008  0.00824  0.24817  193 TYR B OH  
4002 N N   . LEU B 168 ? 0.35857 0.89235 0.40395 0.00873  -0.00462 0.23246  194 LEU B N   
4003 C CA  . LEU B 168 ? 0.38379 0.91356 0.42691 -0.00010 -0.01203 0.23654  194 LEU B CA  
4004 C C   . LEU B 168 ? 0.39576 0.93109 0.43795 -0.00738 -0.01610 0.23657  194 LEU B C   
4005 O O   . LEU B 168 ? 0.41542 0.95113 0.45741 -0.01625 -0.02207 0.24059  194 LEU B O   
4006 C CB  . LEU B 168 ? 0.41134 0.95511 0.46127 -0.00659 -0.01288 0.23855  194 LEU B CB  
4007 C CG  . LEU B 168 ? 0.43213 0.96866 0.48392 -0.00173 -0.01196 0.24157  194 LEU B CG  
4008 C CD1 . LEU B 168 ? 0.43227 0.98510 0.49100 -0.00763 -0.01253 0.24247  194 LEU B CD1 
4009 C CD2 . LEU B 168 ? 0.45520 0.97013 0.49975 -0.00104 -0.01749 0.24603  194 LEU B CD2 
4010 N N   . GLY B 169 ? 0.38849 0.92863 0.43081 -0.00399 -0.01324 0.23305  195 GLY B N   
4011 C CA  . GLY B 169 ? 0.39568 0.94257 0.43900 -0.01036 -0.01722 0.23450  195 GLY B CA  
4012 C C   . GLY B 169 ? 0.41190 0.98682 0.46500 -0.01837 -0.01557 0.23545  195 GLY B C   
4013 O O   . GLY B 169 ? 0.42404 1.00769 0.48014 -0.02486 -0.01888 0.23903  195 GLY B O   
4014 N N   . LYS B 170 ? 0.41225 1.00105 0.47006 -0.01778 -0.01107 0.23291  196 LYS B N   
4015 C CA  . LYS B 170 ? 0.41906 1.03223 0.48353 -0.02338 -0.00975 0.23289  196 LYS B CA  
4016 C C   . LYS B 170 ? 0.39403 1.02082 0.46129 -0.01681 -0.00473 0.22636  196 LYS B C   
4017 O O   . LYS B 170 ? 0.41049 1.02893 0.47545 -0.00929 -0.00190 0.22252  196 LYS B O   
4018 C CB  . LYS B 170 ? 0.44698 1.06291 0.51173 -0.02645 -0.01029 0.23347  196 LYS B CB  
4019 C CG  . LYS B 170 ? 0.49181 1.08957 0.55241 -0.03006 -0.01529 0.23856  196 LYS B CG  
4020 C CD  . LYS B 170 ? 0.52518 1.12806 0.58643 -0.03479 -0.01665 0.24017  196 LYS B CD  
4021 C CE  . LYS B 170 ? 0.55998 1.17965 0.62341 -0.04374 -0.01843 0.24310  196 LYS B CE  
4022 N NZ  . LYS B 170 ? 0.57633 1.19214 0.63984 -0.05079 -0.02332 0.24931  196 LYS B NZ  
4023 N N   . ASP B 171 ? 0.37439 1.01897 0.44400 -0.01889 -0.00439 0.22475  197 ASP B N   
4024 C CA  . ASP B 171 ? 0.36433 1.01590 0.43168 -0.01200 -0.00094 0.21746  197 ASP B CA  
4025 C C   . ASP B 171 ? 0.33225 0.97456 0.39582 -0.00505 0.00243  0.21079  197 ASP B C   
4026 O O   . ASP B 171 ? 0.32526 0.96798 0.38775 -0.00705 0.00194  0.21097  197 ASP B O   
4027 C CB  . ASP B 171 ? 0.40217 1.06896 0.46820 -0.01519 -0.00088 0.21729  197 ASP B CB  
4028 C CG  . ASP B 171 ? 0.41745 1.08826 0.47940 -0.00803 0.00383  0.20929  197 ASP B CG  
4029 O OD1 . ASP B 171 ? 0.41923 1.08250 0.48049 -0.00178 0.00599  0.20473  197 ASP B OD1 
4030 O OD2 . ASP B 171 ? 0.43732 1.11833 0.49659 -0.00846 0.00592  0.20746  197 ASP B OD2 
4031 N N   . PRO B 172 ? 0.30833 0.94250 0.37026 0.00258  0.00569  0.20567  198 PRO B N   
4032 C CA  . PRO B 172 ? 0.29052 0.91652 0.35020 0.00847  0.00882  0.20047  198 PRO B CA  
4033 C C   . PRO B 172 ? 0.27242 0.90676 0.32884 0.00866  0.01000  0.19546  198 PRO B C   
4034 O O   . PRO B 172 ? 0.27056 0.90176 0.32644 0.01015  0.01080  0.19429  198 PRO B O   
4035 C CB  . PRO B 172 ? 0.29836 0.91563 0.35698 0.01590  0.01235  0.19574  198 PRO B CB  
4036 C CG  . PRO B 172 ? 0.30839 0.92593 0.36870 0.01362  0.01037  0.20082  198 PRO B CG  
4037 C CD  . PRO B 172 ? 0.29132 0.92318 0.35393 0.00560  0.00652  0.20541  198 PRO B CD  
4038 N N   . ASN B 173 ? 0.26325 0.90882 0.31757 0.00740  0.01045  0.19323  199 ASN B N   
4039 C CA  . ASN B 173 ? 0.26201 0.91624 0.31182 0.00792  0.01220  0.18892  199 ASN B CA  
4040 C C   . ASN B 173 ? 0.26832 0.93338 0.31775 0.00072  0.01001  0.19417  199 ASN B C   
4041 O O   . ASN B 173 ? 0.27789 0.95335 0.32452 0.00087  0.01211  0.19250  199 ASN B O   
4042 C CB  . ASN B 173 ? 0.27616 0.93427 0.32284 0.01411  0.01617  0.18141  199 ASN B CB  
4043 C CG  . ASN B 173 ? 0.28849 0.93583 0.33478 0.02108  0.01857  0.17541  199 ASN B CG  
4044 O OD1 . ASN B 173 ? 0.31502 0.96042 0.35888 0.02377  0.01983  0.17181  199 ASN B OD1 
4045 N ND2 . ASN B 173 ? 0.25220 0.89308 0.30100 0.02370  0.01914  0.17496  199 ASN B ND2 
4046 N N   . SER B 174 ? 0.26076 0.92297 0.31305 -0.00529 0.00629  0.20078  200 SER B N   
4047 C CA  . SER B 174 ? 0.27648 0.94709 0.32861 -0.01302 0.00390  0.20643  200 SER B CA  
4048 C C   . SER B 174 ? 0.30332 0.98127 0.34798 -0.01286 0.00628  0.20303  200 SER B C   
4049 O O   . SER B 174 ? 0.30726 0.98167 0.34766 -0.00957 0.00748  0.19892  200 SER B O   
4050 C CB  . SER B 174 ? 0.26214 0.92557 0.31793 -0.01899 -0.00029 0.21323  200 SER B CB  
4051 O OG  . SER B 174 ? 0.26927 0.93915 0.32433 -0.02708 -0.00284 0.21877  200 SER B OG  
4052 N N   . THR B 175 ? 0.28027 0.96857 0.32269 -0.01640 0.00711  0.20549  201 THR B N   
4053 C CA  . THR B 175 ? 0.29189 0.98619 0.32486 -0.01644 0.00990  0.20329  201 THR B CA  
4054 C C   . THR B 175 ? 0.31240 1.00673 0.34289 -0.02504 0.00648  0.21000  201 THR B C   
4055 O O   . THR B 175 ? 0.31175 1.00952 0.33223 -0.02591 0.00851  0.20933  201 THR B O   
4056 C CB  . THR B 175 ? 0.33865 1.04409 0.36897 -0.01263 0.01505  0.20099  201 THR B CB  
4057 O OG1 . THR B 175 ? 0.35261 1.06468 0.39082 -0.01745 0.01326  0.20813  201 THR B OG1 
4058 C CG2 . THR B 175 ? 0.29501 0.99880 0.32497 -0.00340 0.01876  0.19290  201 THR B CG2 
4059 N N   . LYS B 176 ? 0.31749 1.00648 0.35532 -0.03110 0.00144  0.21638  202 LYS B N   
4060 C CA  . LYS B 176 ? 0.33338 1.01959 0.36891 -0.03948 -0.00257 0.22270  202 LYS B CA  
4061 C C   . LYS B 176 ? 0.31080 0.98527 0.34396 -0.03951 -0.00534 0.22201  202 LYS B C   
4062 O O   . LYS B 176 ? 0.29346 0.96025 0.33340 -0.03701 -0.00658 0.22201  202 LYS B O   
4063 C CB  . LYS B 176 ? 0.37807 1.06404 0.42221 -0.04631 -0.00683 0.23054  202 LYS B CB  
4064 C CG  . LYS B 176 ? 0.42416 1.12199 0.47304 -0.04658 -0.00542 0.23304  202 LYS B CG  
4065 C CD  . LYS B 176 ? 0.46960 1.16850 0.52475 -0.05591 -0.01071 0.24270  202 LYS B CD  
4066 C CE  . LYS B 176 ? 0.51570 1.21815 0.56532 -0.06333 -0.01206 0.24769  202 LYS B CE  
4067 N NZ  . LYS B 176 ? 0.53309 1.22562 0.58528 -0.07207 -0.01858 0.25465  202 LYS B NZ  
4068 N N   . ALA B 177 ? 0.31021 0.98258 0.33294 -0.04205 -0.00646 0.22207  203 ALA B N   
4069 C CA  . ALA B 177 ? 0.31087 0.97216 0.33101 -0.04255 -0.01052 0.22264  203 ALA B CA  
4070 C C   . ALA B 177 ? 0.45086 1.10291 0.47885 -0.04788 -0.01578 0.22939  203 ALA B C   
4071 O O   . ALA B 177 ? 0.43347 1.07638 0.46506 -0.04618 -0.01854 0.23054  203 ALA B O   
4072 C CB  . ALA B 177 ? 0.39214 1.05087 0.39699 -0.04472 -0.01235 0.22189  203 ALA B CB  
4073 N N   . ASP B 178 ? 0.30912 0.96291 0.33973 -0.05401 -0.01741 0.23440  204 ASP B N   
4074 C CA  . ASP B 178 ? 0.40231 1.04499 0.43814 -0.05884 -0.02262 0.24051  204 ASP B CA  
4075 C C   . ASP B 178 ? 0.29590 0.93233 0.34095 -0.05375 -0.02155 0.24017  204 ASP B C   
4076 O O   . ASP B 178 ? 0.29545 0.91906 0.34332 -0.05418 -0.02509 0.24376  204 ASP B O   
4077 C CB  . ASP B 178 ? 0.40760 1.05335 0.44297 -0.06694 -0.02504 0.24616  204 ASP B CB  
4078 C CG  . ASP B 178 ? 0.42050 1.06713 0.44536 -0.07271 -0.02733 0.24828  204 ASP B CG  
4079 O OD1 . ASP B 178 ? 0.41579 1.05807 0.43284 -0.07070 -0.02816 0.24548  204 ASP B OD1 
4080 O OD2 . ASP B 178 ? 0.43083 1.08180 0.45453 -0.07938 -0.02878 0.25324  204 ASP B OD2 
4081 N N   . ASP B 179 ? 0.28788 0.93170 0.33656 -0.04822 -0.01686 0.23594  205 ASP B N   
4082 C CA  . ASP B 179 ? 0.27845 0.91461 0.33338 -0.04241 -0.01546 0.23513  205 ASP B CA  
4083 C C   . ASP B 179 ? 0.33225 0.96181 0.38825 -0.03646 -0.01459 0.23336  205 ASP B C   
4084 O O   . ASP B 179 ? 0.29507 0.91382 0.35526 -0.03266 -0.01479 0.23547  205 ASP B O   
4085 C CB  . ASP B 179 ? 0.27241 0.91732 0.32989 -0.03785 -0.01146 0.23095  205 ASP B CB  
4086 C CG  . ASP B 179 ? 0.31957 0.96960 0.37933 -0.04355 -0.01333 0.23528  205 ASP B CG  
4087 O OD1 . ASP B 179 ? 0.33148 0.97609 0.39076 -0.05092 -0.01764 0.24140  205 ASP B OD1 
4088 O OD2 . ASP B 179 ? 0.31625 0.97530 0.37823 -0.04081 -0.01109 0.23315  205 ASP B OD2 
4089 N N   . TYR B 180 ? 0.33500 0.97026 0.38661 -0.03533 -0.01387 0.23018  206 TYR B N   
4090 C CA  . TYR B 180 ? 0.27404 0.90430 0.32761 -0.03077 -0.01436 0.23009  206 TYR B CA  
4091 C C   . TYR B 180 ? 0.28034 0.90122 0.33459 -0.03501 -0.02069 0.23614  206 TYR B C   
4092 O O   . TYR B 180 ? 0.27653 0.88963 0.33802 -0.03129 -0.02213 0.23953  206 TYR B O   
4093 C CB  . TYR B 180 ? 0.27661 0.91452 0.32372 -0.02790 -0.01252 0.22438  206 TYR B CB  
4094 C CG  . TYR B 180 ? 0.27108 0.91675 0.31791 -0.02229 -0.00665 0.21776  206 TYR B CG  
4095 C CD1 . TYR B 180 ? 0.26235 0.90602 0.31406 -0.01505 -0.00348 0.21509  206 TYR B CD1 
4096 C CD2 . TYR B 180 ? 0.27579 0.93007 0.31769 -0.02383 -0.00457 0.21462  206 TYR B CD2 
4097 C CE1 . TYR B 180 ? 0.25889 0.90681 0.30958 -0.00972 0.00086  0.20847  206 TYR B CE1 
4098 C CE2 . TYR B 180 ? 0.27208 0.93198 0.31413 -0.01811 -0.00018 0.20871  206 TYR B CE2 
4099 C CZ  . TYR B 180 ? 0.26382 0.91953 0.30975 -0.01118 0.00214  0.20520  206 TYR B CZ  
4100 O OH  . TYR B 180 ? 0.26176 0.92041 0.30670 -0.00549 0.00582  0.19897  206 TYR B OH  
4101 N N   . THR B 181 ? 0.29090 0.91207 0.33816 -0.04223 -0.02471 0.23786  207 THR B N   
4102 C CA  . THR B 181 ? 0.29833 0.90950 0.34588 -0.04642 -0.03188 0.24328  207 THR B CA  
4103 C C   . THR B 181 ? 0.31467 0.91609 0.36708 -0.04855 -0.03421 0.24855  207 THR B C   
4104 O O   . THR B 181 ? 0.30265 0.89430 0.35807 -0.04978 -0.03989 0.25321  207 THR B O   
4105 C CB  . THR B 181 ? 0.32145 0.93416 0.35747 -0.05312 -0.03586 0.24317  207 THR B CB  
4106 O OG1 . THR B 181 ? 0.31526 0.93563 0.34627 -0.05694 -0.03243 0.24222  207 THR B OG1 
4107 C CG2 . THR B 181 ? 0.35991 0.97615 0.38864 -0.05026 -0.03631 0.23856  207 THR B CG2 
4108 N N   . GLY B 182 ? 0.32413 0.92680 0.37722 -0.04868 -0.03092 0.24795  208 GLY B N   
4109 C CA  . GLY B 182 ? 0.33868 0.92976 0.39313 -0.05101 -0.03427 0.25250  208 GLY B CA  
4110 C C   . GLY B 182 ? 0.31735 0.89913 0.37735 -0.04303 -0.03194 0.25300  208 GLY B C   
4111 O O   . GLY B 182 ? 0.29953 0.87480 0.36478 -0.03752 -0.03261 0.25528  208 GLY B O   
4112 N N   . PRO B 183 ? 0.30721 0.88799 0.36616 -0.04194 -0.02942 0.25144  209 PRO B N   
4113 C CA  . PRO B 183 ? 0.31731 0.88483 0.37776 -0.03425 -0.02808 0.25215  209 PRO B CA  
4114 C C   . PRO B 183 ? 0.31280 0.88238 0.37864 -0.02455 -0.02266 0.25018  209 PRO B C   
4115 O O   . PRO B 183 ? 0.34375 0.90217 0.41242 -0.01765 -0.02239 0.25336  209 PRO B O   
4116 C CB  . PRO B 183 ? 0.30399 0.87192 0.36115 -0.03619 -0.02721 0.25033  209 PRO B CB  
4117 C CG  . PRO B 183 ? 0.29770 0.88481 0.35540 -0.04204 -0.02533 0.24787  209 PRO B CG  
4118 C CD  . PRO B 183 ? 0.30822 0.89907 0.36447 -0.04758 -0.02846 0.24991  209 PRO B CD  
4119 N N   . ALA B 184 ? 0.29416 0.87761 0.36142 -0.02326 -0.01825 0.24543  210 ALA B N   
4120 C CA  . ALA B 184 ? 0.30786 0.89343 0.38027 -0.01467 -0.01359 0.24403  210 ALA B CA  
4121 C C   . ALA B 184 ? 0.29990 0.88373 0.37889 -0.01327 -0.01646 0.24892  210 ALA B C   
4122 O O   . ALA B 184 ? 0.31754 0.89600 0.40367 -0.00538 -0.01441 0.25229  210 ALA B O   
4123 C CB  . ALA B 184 ? 0.30187 0.90172 0.37309 -0.01425 -0.00976 0.23769  210 ALA B CB  
4124 N N   . THR B 185 ? 0.30066 0.88877 0.37812 -0.02056 -0.02156 0.24986  211 THR B N   
4125 C CA  . THR B 185 ? 0.31796 0.90318 0.40309 -0.02027 -0.02641 0.25468  211 THR B CA  
4126 C C   . THR B 185 ? 0.32699 0.89949 0.41699 -0.01747 -0.02880 0.26103  211 THR B C   
4127 O O   . THR B 185 ? 0.33361 0.90348 0.43555 -0.01173 -0.02942 0.26567  211 THR B O   
4128 C CB  . THR B 185 ? 0.32986 0.91892 0.40910 -0.02903 -0.03239 0.25402  211 THR B CB  
4129 O OG1 . THR B 185 ? 0.31661 0.91617 0.39089 -0.02930 -0.03022 0.24826  211 THR B OG1 
4130 C CG2 . THR B 185 ? 0.33886 0.92235 0.42681 -0.02968 -0.03940 0.25925  211 THR B CG2 
4131 N N   . ASP B 186 ? 0.34030 0.90452 0.42231 -0.02090 -0.03035 0.26143  212 ASP B N   
4132 C CA  . ASP B 186 ? 0.35432 0.90398 0.43791 -0.01742 -0.03311 0.26683  212 ASP B CA  
4133 C C   . ASP B 186 ? 0.32946 0.87309 0.41812 -0.00527 -0.02706 0.26864  212 ASP B C   
4134 O O   . ASP B 186 ? 0.31709 0.85506 0.41450 0.00150  -0.02728 0.27454  212 ASP B O   
4135 C CB  . ASP B 186 ? 0.39016 0.93041 0.46278 -0.02355 -0.03674 0.26610  212 ASP B CB  
4136 C CG  . ASP B 186 ? 0.43293 0.97678 0.50120 -0.03475 -0.04293 0.26661  212 ASP B CG  
4137 O OD1 . ASP B 186 ? 0.43487 0.98484 0.50723 -0.03713 -0.04547 0.26782  212 ASP B OD1 
4138 O OD2 . ASP B 186 ? 0.45750 0.99724 0.51806 -0.04122 -0.04571 0.26621  212 ASP B OD2 
4139 N N   . LEU B 187 ? 0.31337 0.85797 0.39694 -0.00177 -0.02130 0.26397  213 LEU B N   
4140 C CA  . LEU B 187 ? 0.32709 0.86407 0.41268 0.01022  -0.01483 0.26554  213 LEU B CA  
4141 C C   . LEU B 187 ? 0.32347 0.86917 0.42442 0.01640  -0.01066 0.26788  213 LEU B C   
4142 O O   . LEU B 187 ? 0.34664 0.88282 0.45603 0.02565  -0.00556 0.27091  213 LEU B O   
4143 C CB  . LEU B 187 ? 0.30690 0.84187 0.38336 0.01176  -0.01041 0.25922  213 LEU B CB  
4144 C CG  . LEU B 187 ? 0.30899 0.83295 0.38364 0.02421  -0.00313 0.26001  213 LEU B CG  
4145 C CD1 . LEU B 187 ? 0.30462 0.80919 0.37525 0.03132  -0.00391 0.26552  213 LEU B CD1 
4146 C CD2 . LEU B 187 ? 0.30494 0.82499 0.36977 0.02445  -0.00072 0.25322  213 LEU B CD2 
4147 N N   . LEU B 188 ? 0.29652 0.85638 0.40272 0.01107  -0.01157 0.26411  214 LEU B N   
4148 C CA  . LEU B 188 ? 0.29029 0.85422 0.41357 0.01497  -0.00818 0.26373  214 LEU B CA  
4149 C C   . LEU B 188 ? 0.28248 0.84434 0.41991 0.01546  -0.01272 0.27127  214 LEU B C   
4150 O O   . LEU B 188 ? 0.28542 0.84543 0.43961 0.02227  -0.00806 0.27430  214 LEU B O   
4151 C CB  . LEU B 188 ? 0.30370 0.88051 0.42646 0.00893  -0.01025 0.25794  214 LEU B CB  
4152 C CG  . LEU B 188 ? 0.30692 0.88636 0.42266 0.01167  -0.00350 0.25024  214 LEU B CG  
4153 C CD1 . LEU B 188 ? 0.30606 0.89745 0.41668 0.00558  -0.00654 0.24453  214 LEU B CD1 
4154 C CD2 . LEU B 188 ? 0.24312 0.81663 0.37029 0.02098  0.00472  0.24939  214 LEU B CD2 
4155 N N   . LEU B 189 ? 0.28092 0.84326 0.41270 0.00838  -0.02178 0.27503  215 LEU B N   
4156 C CA  . LEU B 189 ? 0.29797 0.85740 0.44288 0.00903  -0.02704 0.28252  215 LEU B CA  
4157 C C   . LEU B 189 ? 0.29939 0.84566 0.44741 0.01926  -0.02172 0.28743  215 LEU B C   
4158 O O   . LEU B 189 ? 0.30323 0.84790 0.46909 0.02514  -0.02015 0.29316  215 LEU B O   
4159 C CB  . LEU B 189 ? 0.31643 0.87300 0.45099 -0.00199 -0.03641 0.28246  215 LEU B CB  
4160 C CG  . LEU B 189 ? 0.33395 0.89845 0.46438 -0.01167 -0.04156 0.27777  215 LEU B CG  
4161 C CD1 . LEU B 189 ? 0.36134 0.92158 0.47643 -0.02171 -0.04799 0.27671  215 LEU B CD1 
4162 C CD2 . LEU B 189 ? 0.33227 0.89911 0.48057 -0.01162 -0.04598 0.28063  215 LEU B CD2 
4163 N N   . LYS B 190 ? 0.31078 0.84689 0.44141 0.02183  -0.01926 0.28567  216 LYS B N   
4164 C CA  . LYS B 190 ? 0.32199 0.84211 0.45104 0.03313  -0.01376 0.28935  216 LYS B CA  
4165 C C   . LYS B 190 ? 0.29123 0.81010 0.43336 0.04414  -0.00178 0.28893  216 LYS B C   
4166 O O   . LYS B 190 ? 0.29076 0.80189 0.44264 0.05414  0.00348  0.29454  216 LYS B O   
4167 C CB  . LYS B 190 ? 0.37761 0.88523 0.48351 0.03322  -0.01479 0.28680  216 LYS B CB  
4168 C CG  . LYS B 190 ? 0.43660 0.93388 0.53171 0.02606  -0.02412 0.28766  216 LYS B CG  
4169 C CD  . LYS B 190 ? 0.48746 0.97254 0.56333 0.02211  -0.02572 0.28133  216 LYS B CD  
4170 C CE  . LYS B 190 ? 0.54419 1.01074 0.60899 0.01970  -0.03358 0.28290  216 LYS B CE  
4171 N NZ  . LYS B 190 ? 0.58760 1.03566 0.64896 0.03361  -0.03063 0.28762  216 LYS B NZ  
4172 N N   . LEU B 191 ? 0.28834 0.81483 0.43088 0.04280  0.00300  0.28272  217 LEU B N   
4173 C CA  . LEU B 191 ? 0.27260 0.79740 0.42592 0.05254  0.01440  0.28227  217 LEU B CA  
4174 C C   . LEU B 191 ? 0.29728 0.83374 0.47694 0.05247  0.01517  0.28661  217 LEU B C   
4175 O O   . LEU B 191 ? 0.30017 0.83445 0.49332 0.06177  0.02476  0.28998  217 LEU B O   
4176 C CB  . LEU B 191 ? 0.26691 0.79386 0.40973 0.05130  0.01848  0.27390  217 LEU B CB  
4177 C CG  . LEU B 191 ? 0.28690 0.80296 0.40589 0.05129  0.01765  0.26962  217 LEU B CG  
4178 C CD1 . LEU B 191 ? 0.26642 0.78817 0.37921 0.04911  0.02064  0.26162  217 LEU B CD1 
4179 C CD2 . LEU B 191 ? 0.30697 0.80253 0.41702 0.06329  0.02379  0.27268  217 LEU B CD2 
4180 N N   . ARG B 192 ? 0.27529 0.82326 0.46222 0.04223  0.00504  0.28712  218 ARG B N   
4181 C CA  . ARG B 192 ? 0.26272 0.82119 0.47400 0.04056  0.00339  0.29065  218 ARG B CA  
4182 C C   . ARG B 192 ? 0.25829 0.81509 0.49265 0.04923  0.00821  0.30048  218 ARG B C   
4183 O O   . ARG B 192 ? 0.25838 0.81376 0.50765 0.05174  0.01404  0.30130  218 ARG B O   
4184 C CB  . ARG B 192 ? 0.28869 0.85525 0.49926 0.02829  -0.01007 0.28976  218 ARG B CB  
4185 C CG  . ARG B 192 ? 0.31860 0.88828 0.53774 0.02269  -0.01282 0.28582  218 ARG B CG  
4186 C CD  . ARG B 192 ? 0.34809 0.91450 0.59173 0.02431  -0.01371 0.29275  218 ARG B CD  
4187 N NE  . ARG B 192 ? 0.38582 0.95343 0.63855 0.02019  -0.01647 0.28974  218 ARG B NE  
4188 C CZ  . ARG B 192 ? 0.39435 0.95858 0.66713 0.02434  -0.01170 0.29380  218 ARG B CZ  
4189 N NH1 . ARG B 192 ? 0.39243 0.95210 0.67754 0.03341  -0.00245 0.30087  218 ARG B NH1 
4190 N NH2 . ARG B 192 ? 0.39736 0.96252 0.67751 0.01970  -0.01629 0.29123  218 ARG B NH2 
4191 N N   . PRO B 193 ? 0.27127 0.82095 0.50524 0.05317  0.00664  0.30646  219 PRO B N   
4192 C CA  . PRO B 193 ? 0.28167 0.83116 0.53979 0.06233  0.01217  0.31633  219 PRO B CA  
4193 C C   . PRO B 193 ? 0.29030 0.83462 0.55420 0.07517  0.02815  0.31808  219 PRO B C   
4194 O O   . PRO B 193 ? 0.29230 0.83300 0.57462 0.08176  0.03477  0.32500  219 PRO B O   
4195 C CB  . PRO B 193 ? 0.29620 0.83579 0.54497 0.06534  0.00795  0.32045  219 PRO B CB  
4196 C CG  . PRO B 193 ? 0.28527 0.82505 0.51364 0.05280  -0.00450 0.31462  219 PRO B CG  
4197 C CD  . PRO B 193 ? 0.28282 0.82491 0.49628 0.04878  -0.00133 0.30533  219 PRO B CD  
4198 N N   . ASN B 194 ? 0.28813 0.82605 0.53270 0.07788  0.03481  0.31076  220 ASN B N   
4199 C CA  . ASN B 194 ? 0.31354 0.84494 0.56022 0.09006  0.04990  0.31204  220 ASN B CA  
4200 C C   . ASN B 194 ? 0.31477 0.84816 0.56384 0.08564  0.05271  0.30599  220 ASN B C   
4201 O O   . ASN B 194 ? 0.33651 0.86076 0.58460 0.09429  0.06431  0.30599  220 ASN B O   
4202 C CB  . ASN B 194 ? 0.32450 0.83639 0.54087 0.09769  0.05524  0.30727  220 ASN B CB  
4203 C CG  . ASN B 194 ? 0.35758 0.85791 0.56366 0.10143  0.05099  0.31112  220 ASN B CG  
4204 O OD1 . ASN B 194 ? 0.38935 0.88561 0.60718 0.11178  0.05716  0.31930  220 ASN B OD1 
4205 N ND2 . ASN B 194 ? 0.37199 0.86710 0.55649 0.09321  0.04043  0.30571  220 ASN B ND2 
4206 N N   . ILE B 195 ? 0.31032 0.85115 0.55893 0.07277  0.04191  0.30020  221 ILE B N   
4207 C CA  . ILE B 195 ? 0.31735 0.85730 0.56634 0.06844  0.04248  0.29377  221 ILE B CA  
4208 C C   . ILE B 195 ? 0.31350 0.85400 0.58614 0.06501  0.03962  0.29895  221 ILE B C   
4209 O O   . ILE B 195 ? 0.25800 0.80419 0.54103 0.05770  0.02948  0.30219  221 ILE B O   
4210 C CB  . ILE B 195 ? 0.32300 0.87071 0.55702 0.05790  0.03298  0.28463  221 ILE B CB  
4211 C CG1 . ILE B 195 ? 0.32070 0.86909 0.53363 0.06031  0.03490  0.28075  221 ILE B CG1 
4212 C CG2 . ILE B 195 ? 0.32062 0.86739 0.55478 0.05498  0.03360  0.27803  221 ILE B CG2 
4213 C CD1 . ILE B 195 ? 0.24227 0.79925 0.44068 0.05010  0.02602  0.27297  221 ILE B CD1 
4214 N N   . ARG B 196 ? 0.30639 0.84050 0.58765 0.06993  0.04788  0.30010  222 ARG B N   
4215 C CA  . ARG B 196 ? 0.30540 0.84039 0.61150 0.06682  0.04544  0.30645  222 ARG B CA  
4216 C C   . ARG B 196 ? 0.29465 0.83680 0.60453 0.05446  0.03251  0.30158  222 ARG B C   
4217 O O   . ARG B 196 ? 0.28781 0.83416 0.61407 0.04769  0.02291  0.30621  222 ARG B O   
4218 C CB  . ARG B 196 ? 0.30658 0.83296 0.62039 0.07536  0.05792  0.30985  222 ARG B CB  
4219 C CG  . ARG B 196 ? 0.31223 0.83988 0.65439 0.07307  0.05664  0.31874  222 ARG B CG  
4220 C CD  . ARG B 196 ? 0.28071 0.80012 0.62949 0.08149  0.06955  0.32282  222 ARG B CD  
4221 N NE  . ARG B 196 ? 0.32411 0.83523 0.66809 0.09488  0.08303  0.32833  222 ARG B NE  
4222 C CZ  . ARG B 196 ? 0.32915 0.83036 0.67060 0.10491  0.09637  0.33096  222 ARG B CZ  
4223 N NH1 . ARG B 196 ? 0.29736 0.79652 0.64193 0.10242  0.09773  0.32876  222 ARG B NH1 
4224 N NH2 . ARG B 196 ? 0.33825 0.83111 0.67330 0.11787  0.10826  0.33604  222 ARG B NH2 
4225 N N   . TYR B 197 ? 0.29229 0.83536 0.58683 0.05186  0.03170  0.29234  223 TYR B N   
4226 C CA  . TYR B 197 ? 0.31067 0.86034 0.60664 0.04163  0.01991  0.28745  223 TYR B CA  
4227 C C   . TYR B 197 ? 0.31402 0.86636 0.58605 0.04012  0.01950  0.27645  223 TYR B C   
4228 O O   . TYR B 197 ? 0.29331 0.84096 0.55055 0.04683  0.02870  0.27279  223 TYR B O   
4229 C CB  . TYR B 197 ? 0.32745 0.87546 0.64361 0.04022  0.01943  0.29111  223 TYR B CB  
4230 C CG  . TYR B 197 ? 0.34835 0.88954 0.66150 0.04773  0.03153  0.28945  223 TYR B CG  
4231 C CD1 . TYR B 197 ? 0.35598 0.89808 0.65588 0.04625  0.03099  0.28048  223 TYR B CD1 
4232 C CD2 . TYR B 197 ? 0.35182 0.88530 0.67483 0.05672  0.04348  0.29703  223 TYR B CD2 
4233 C CE1 . TYR B 197 ? 0.35805 0.89293 0.65468 0.05288  0.04134  0.27896  223 TYR B CE1 
4234 C CE2 . TYR B 197 ? 0.35133 0.87718 0.66995 0.06363  0.05424  0.29570  223 TYR B CE2 
4235 C CZ  . TYR B 197 ? 0.35936 0.88564 0.66488 0.06135  0.05277  0.28659  223 TYR B CZ  
4236 O OH  . TYR B 197 ? 0.35696 0.87491 0.65772 0.06802  0.06286  0.28527  223 TYR B OH  
4237 N N   . PHE B 198 ? 0.32841 0.88793 0.59660 0.03155  0.00830  0.27143  224 PHE B N   
4238 C CA  . PHE B 198 ? 0.34273 0.90670 0.59025 0.02963  0.00695  0.26111  224 PHE B CA  
4239 C C   . PHE B 198 ? 0.36203 0.92746 0.61672 0.02716  0.00304  0.25808  224 PHE B C   
4240 O O   . PHE B 198 ? 0.37417 0.94397 0.63647 0.02024  -0.00888 0.25896  224 PHE B O   
4241 C CB  . PHE B 198 ? 0.34632 0.91821 0.58023 0.02265  -0.00279 0.25785  224 PHE B CB  
4242 C CG  . PHE B 198 ? 0.33866 0.91008 0.56439 0.02430  -0.00014 0.26074  224 PHE B CG  
4243 C CD1 . PHE B 198 ? 0.33173 0.90478 0.53758 0.02632  0.00449  0.25532  224 PHE B CD1 
4244 C CD2 . PHE B 198 ? 0.34211 0.91165 0.58080 0.02364  -0.00321 0.26926  224 PHE B CD2 
4245 C CE1 . PHE B 198 ? 0.32544 0.89842 0.52457 0.02737  0.00543  0.25877  224 PHE B CE1 
4246 C CE2 . PHE B 198 ? 0.33291 0.90232 0.56422 0.02537  -0.00178 0.27228  224 PHE B CE2 
4247 C CZ  . PHE B 198 ? 0.32785 0.89909 0.53934 0.02707  0.00218  0.26723  224 PHE B CZ  
4248 N N   . HIS B 199 ? 0.37617 0.93697 0.62784 0.03283  0.01198  0.25473  225 HIS B N   
4249 C CA  . HIS B 199 ? 0.40458 0.96703 0.66292 0.03097  0.00835  0.25205  225 HIS B CA  
4250 C C   . HIS B 199 ? 0.41887 0.97942 0.66038 0.03604  0.01606  0.24337  225 HIS B C   
4251 O O   . HIS B 199 ? 0.43086 0.98464 0.66117 0.04230  0.02612  0.24187  225 HIS B O   
4252 C CB  . HIS B 199 ? 0.42084 0.97791 0.70440 0.03199  0.01028  0.26126  225 HIS B CB  
4253 C CG  . HIS B 199 ? 0.43342 0.99429 0.72980 0.02612  -0.00049 0.26165  225 HIS B CG  
4254 N ND1 . HIS B 199 ? 0.43385 0.99397 0.73017 0.02808  0.00182  0.25810  225 HIS B ND1 
4255 C CD2 . HIS B 199 ? 0.44149 1.00572 0.75037 0.01829  -0.01509 0.26528  225 HIS B CD2 
4256 C CE1 . HIS B 199 ? 0.44080 1.00424 0.74959 0.02178  -0.01116 0.25983  225 HIS B CE1 
4257 N NE2 . HIS B 199 ? 0.44517 1.01023 0.76115 0.01572  -0.02193 0.26406  225 HIS B NE2 
4258 N N   . SER B 200 ? 0.41906 0.98488 0.65874 0.03360  0.01022  0.23776  226 SER B N   
4259 C CA  . SER B 200 ? 0.44166 1.00735 0.66521 0.03781  0.01559  0.22861  226 SER B CA  
4260 C C   . SER B 200 ? 0.45714 1.01654 0.69051 0.04185  0.02114  0.22991  226 SER B C   
4261 O O   . SER B 200 ? 0.44563 1.00364 0.66657 0.04582  0.02569  0.22258  226 SER B O   
4262 C CB  . SER B 200 ? 0.44638 1.02058 0.65607 0.03366  0.00568  0.21984  226 SER B CB  
4263 O OG  . SER B 200 ? 0.44850 1.02723 0.64436 0.03056  0.00259  0.21766  226 SER B OG  
4264 N N   . SER B 201 ? 0.48613 1.04175 0.74184 0.04087  0.02088  0.23943  227 SER B N   
4265 C CA  . SER B 201 ? 0.49488 1.04573 0.76129 0.04376  0.02541  0.24177  227 SER B CA  
4266 C C   . SER B 201 ? 0.52336 1.06598 0.80936 0.04626  0.03272  0.25333  227 SER B C   
4267 O O   . SER B 201 ? 0.52849 1.06501 0.82092 0.05024  0.04004  0.25626  227 SER B O   
4268 C CB  . SER B 201 ? 0.47864 1.03755 0.75477 0.03803  0.01234  0.24060  227 SER B CB  
4269 O OG  . SER B 201 ? 0.47459 1.03544 0.77140 0.03133  0.00190  0.24928  227 SER B OG  
4270 N N   . GLN B 202 ? 0.52365 1.06633 0.81940 0.04431  0.03095  0.26034  228 GLN B N   
4271 C CA  . GLN B 202 ? 0.53252 1.06824 0.84680 0.04780  0.03857  0.27159  228 GLN B CA  
4272 C C   . GLN B 202 ? 0.48461 1.00925 0.78524 0.05809  0.05359  0.27136  228 GLN B C   
4273 O O   . GLN B 202 ? 0.49511 1.01227 0.80681 0.06356  0.06282  0.27926  228 GLN B O   
4274 C CB  . GLN B 202 ? 0.57907 1.11863 0.90848 0.04296  0.03130  0.27909  228 GLN B CB  
4275 C CG  . GLN B 202 ? 0.63275 1.16782 0.98649 0.04529  0.03677  0.29189  228 GLN B CG  
4276 C CD  . GLN B 202 ? 0.66561 1.20419 1.03312 0.04116  0.02973  0.29879  228 GLN B CD  
4277 O OE1 . GLN B 202 ? 0.67326 1.21817 1.03835 0.03364  0.01674  0.29540  228 GLN B OE1 
4278 N NE2 . GLN B 202 ? 0.68696 1.22108 1.06827 0.04657  0.03824  0.30863  228 GLN B NE2 
4279 N N   . TYR B 203 ? 0.42503 0.94805 0.70151 0.06098  0.05571  0.26281  229 TYR B N   
4280 C CA  . TYR B 203 ? 0.40379 0.91526 0.66647 0.07060  0.06758  0.26294  229 TYR B CA  
4281 C C   . TYR B 203 ? 0.41167 0.91282 0.66846 0.07739  0.07719  0.26137  229 TYR B C   
4282 O O   . TYR B 203 ? 0.41336 0.90289 0.66575 0.08624  0.08787  0.26525  229 TYR B O   
4283 C CB  . TYR B 203 ? 0.38195 0.89473 0.62179 0.07082  0.06552  0.25495  229 TYR B CB  
4284 C CG  . TYR B 203 ? 0.35041 0.86489 0.57204 0.06960  0.06337  0.24372  229 TYR B CG  
4285 C CD1 . TYR B 203 ? 0.33419 0.83808 0.53772 0.07683  0.07115  0.23863  229 TYR B CD1 
4286 C CD2 . TYR B 203 ? 0.33584 0.86234 0.55804 0.06177  0.05321  0.23833  229 TYR B CD2 
4287 C CE1 . TYR B 203 ? 0.32958 0.83518 0.51760 0.07585  0.06893  0.22859  229 TYR B CE1 
4288 C CE2 . TYR B 203 ? 0.32293 0.85185 0.52887 0.06162  0.05183  0.22821  229 TYR B CE2 
4289 C CZ  . TYR B 203 ? 0.32204 0.84063 0.51165 0.06844  0.05973  0.22341  229 TYR B CZ  
4290 O OH  . TYR B 203 ? 0.33011 0.85116 0.50474 0.06839  0.05808  0.21355  229 TYR B OH  
4291 N N   . ILE B 204 ? 0.42103 0.92590 0.67759 0.07397  0.07361  0.25623  230 ILE B N   
4292 C CA  . ILE B 204 ? 0.44211 0.93717 0.69383 0.08013  0.08246  0.25536  230 ILE B CA  
4293 C C   . ILE B 204 ? 0.46337 0.95336 0.73590 0.08306  0.08936  0.26735  230 ILE B C   
4294 O O   . ILE B 204 ? 0.48147 0.95878 0.74794 0.09189  0.10089  0.27035  230 ILE B O   
4295 C CB  . ILE B 204 ? 0.43861 0.94034 0.68674 0.07590  0.07646  0.24761  230 ILE B CB  
4296 C CG1 . ILE B 204 ? 0.43880 0.95363 0.70897 0.06685  0.06519  0.25159  230 ILE B CG1 
4297 C CG2 . ILE B 204 ? 0.42364 0.92877 0.64901 0.07512  0.07224  0.23589  230 ILE B CG2 
4298 C CD1 . ILE B 204 ? 0.43726 0.95147 0.72488 0.06629  0.06658  0.25763  230 ILE B CD1 
4299 N N   . ASN B 205 ? 0.47490 0.97436 0.77217 0.07584  0.08208  0.27484  231 ASN B N   
4300 C CA  . ASN B 205 ? 0.50272 0.99901 0.82265 0.07777  0.08793  0.28751  231 ASN B CA  
4301 C C   . ASN B 205 ? 0.50532 0.99451 0.82542 0.08517  0.09659  0.29420  231 ASN B C   
4302 O O   . ASN B 205 ? 0.50891 0.98883 0.83276 0.09312  0.10815  0.30135  231 ASN B O   
4303 C CB  . ASN B 205 ? 0.52382 1.03190 0.87091 0.06742  0.07589  0.29416  231 ASN B CB  
4304 C CG  . ASN B 205 ? 0.58394 1.09048 0.95421 0.06734  0.07991  0.30538  231 ASN B CG  
4305 O OD1 . ASN B 205 ? 0.61405 1.11437 0.97863 0.07187  0.08774  0.30472  231 ASN B OD1 
4306 N ND2 . ASN B 205 ? 0.60375 1.11586 1.00074 0.06196  0.07425  0.31629  231 ASN B ND2 
4307 N N   . ASP B 206 ? 0.49887 0.99241 0.81444 0.08320  0.09132  0.29228  232 ASP B N   
4308 C CA  . ASP B 206 ? 0.50302 0.99075 0.81880 0.09068  0.09895  0.29874  232 ASP B CA  
4309 C C   . ASP B 206 ? 0.49883 0.97235 0.79016 0.10237  0.11080  0.29477  232 ASP B C   
4310 O O   . ASP B 206 ? 0.50412 0.96966 0.79627 0.11147  0.12044  0.30182  232 ASP B O   
4311 C CB  . ASP B 206 ? 0.50443 1.00071 0.82085 0.08531  0.08962  0.29767  232 ASP B CB  
4312 C CG  . ASP B 206 ? 0.50076 1.00876 0.84183 0.07456  0.07755  0.30290  232 ASP B CG  
4313 O OD1 . ASP B 206 ? 0.49974 1.00991 0.85733 0.07076  0.07557  0.30699  232 ASP B OD1 
4314 O OD2 . ASP B 206 ? 0.49792 1.01247 0.84192 0.06979  0.06939  0.30334  232 ASP B OD2 
4315 N N   . LEU B 207 ? 0.50054 0.97031 0.77013 0.10274  0.11002  0.28394  233 LEU B N   
4316 C CA  . LEU B 207 ? 0.51665 0.97131 0.76285 0.11349  0.12007  0.28007  233 LEU B CA  
4317 C C   . LEU B 207 ? 0.55216 0.99604 0.80072 0.12004  0.13040  0.28431  233 LEU B C   
4318 O O   . LEU B 207 ? 0.57558 1.00566 0.81512 0.13116  0.14163  0.28820  233 LEU B O   
4319 C CB  . LEU B 207 ? 0.48400 0.93902 0.70734 0.11091  0.11455  0.26735  233 LEU B CB  
4320 C CG  . LEU B 207 ? 0.45666 0.91542 0.66655 0.10967  0.10924  0.26279  233 LEU B CG  
4321 C CD1 . LEU B 207 ? 0.43300 0.89726 0.62745 0.10382  0.10146  0.25120  233 LEU B CD1 
4322 C CD2 . LEU B 207 ? 0.46302 0.90777 0.65749 0.12125  0.11853  0.26509  233 LEU B CD2 
4323 N N   . ALA B 208 ? 0.55146 1.00122 0.81144 0.11364  0.12674  0.28395  234 ALA B N   
4324 C CA  . ALA B 208 ? 0.59007 1.03102 0.85438 0.11890  0.13613  0.28915  234 ALA B CA  
4325 C C   . ALA B 208 ? 0.63977 1.07850 0.92361 0.12383  0.14427  0.30298  234 ALA B C   
4326 O O   . ALA B 208 ? 0.69597 1.12231 0.97555 0.13322  0.15618  0.30793  234 ALA B O   
4327 C CB  . ALA B 208 ? 0.57970 1.02988 0.85579 0.11015  0.12929  0.28748  234 ALA B CB  
4328 N N   . ASN B 209 ? 0.60076 1.05109 0.90578 0.11799  0.13810  0.30962  235 ASN B N   
4329 C CA  . ASN B 209 ? 0.58900 1.03859 0.91400 0.12275  0.14552  0.32328  235 ASN B CA  
4330 C C   . ASN B 209 ? 0.59369 1.03452 0.90623 0.13347  0.15356  0.32525  235 ASN B C   
4331 O O   . ASN B 209 ? 0.57616 1.01296 0.89978 0.14108  0.16315  0.33623  235 ASN B O   
4332 C CB  . ASN B 209 ? 0.57158 1.03690 0.92660 0.11176  0.13481  0.33052  235 ASN B CB  
4333 C CG  . ASN B 209 ? 0.55728 1.02968 0.93131 0.10336  0.12935  0.33396  235 ASN B CG  
4334 O OD1 . ASN B 209 ? 0.55639 1.02206 0.92634 0.10718  0.13653  0.33462  235 ASN B OD1 
4335 N ND2 . ASN B 209 ? 0.54575 1.03120 0.94057 0.09188  0.11603  0.33656  235 ASN B ND2 
4336 N N   . GLY B 210 ? 0.62075 1.05893 0.91103 0.13456  0.14997  0.31561  236 GLY B N   
4337 C CA  . GLY B 210 ? 0.63746 1.06814 0.91587 0.14428  0.15613  0.31759  236 GLY B CA  
4338 C C   . GLY B 210 ? 0.62962 1.07206 0.92365 0.13969  0.14952  0.32261  236 GLY B C   
4339 O O   . GLY B 210 ? 0.64743 1.08461 0.93610 0.14850  0.15559  0.32688  236 GLY B O   
4340 N N   . ASP B 211 ? 0.57881 1.03628 0.89129 0.12657  0.13705  0.32238  237 ASP B N   
4341 C CA  . ASP B 211 ? 0.59458 1.06273 0.92265 0.12156  0.12977  0.32738  237 ASP B CA  
4342 C C   . ASP B 211 ? 0.56806 1.03725 0.87669 0.12152  0.12472  0.31990  237 ASP B C   
4343 O O   . ASP B 211 ? 0.55820 1.03011 0.87193 0.12397  0.12457  0.32513  237 ASP B O   
4344 C CB  . ASP B 211 ? 0.62233 1.10430 0.97343 0.10763  0.11682  0.32885  237 ASP B CB  
4345 C CG  . ASP B 211 ? 0.67480 1.15765 1.04995 0.10700  0.12080  0.33896  237 ASP B CG  
4346 O OD1 . ASP B 211 ? 0.69925 1.17610 1.08193 0.11643  0.13257  0.34866  237 ASP B OD1 
4347 O OD2 . ASP B 211 ? 0.68767 1.17740 1.07429 0.09737  0.11217  0.33777  237 ASP B OD2 
4348 N N   . ILE B 212 ? 0.55650 1.02428 0.84382 0.11870  0.12046  0.30838  238 ILE B N   
4349 C CA  . ILE B 212 ? 0.55123 1.01965 0.81870 0.11913  0.11648  0.30172  238 ILE B CA  
4350 C C   . ILE B 212 ? 0.55631 1.01003 0.79733 0.12923  0.12524  0.29599  238 ILE B C   
4351 O O   . ILE B 212 ? 0.57349 1.01952 0.80857 0.13141  0.12980  0.29273  238 ILE B O   
4352 C CB  . ILE B 212 ? 0.52865 1.00994 0.79418 0.10596  0.10211  0.29346  238 ILE B CB  
4353 C CG1 . ILE B 212 ? 0.51992 0.99960 0.77522 0.10257  0.10050  0.28444  238 ILE B CG1 
4354 C CG2 . ILE B 212 ? 0.51924 1.01287 0.80994 0.09625  0.09268  0.29924  238 ILE B CG2 
4355 C CD1 . ILE B 212 ? 0.50711 0.99112 0.74237 0.09780  0.09320  0.27366  238 ILE B CD1 
4356 N N   . CYS B 213 ? 0.53231 0.98177 0.75739 0.13549  0.12717  0.29519  239 CYS B N   
4357 C CA  A CYS B 213 ? 0.51977 0.95308 0.71918 0.14648  0.13555  0.29115  239 CYS B CA  
4358 C CA  B CYS B 213 ? 0.52169 0.95507 0.72101 0.14654  0.13552  0.29122  239 CYS B CA  
4359 C C   . CYS B 213 ? 0.51153 0.94664 0.69043 0.14126  0.12814  0.28012  239 CYS B C   
4360 O O   . CYS B 213 ? 0.52015 0.94190 0.67902 0.14746  0.13307  0.27485  239 CYS B O   
4361 C CB  A CYS B 213 ? 0.52359 0.94797 0.71601 0.15924  0.14405  0.29832  239 CYS B CB  
4362 C CB  B CYS B 213 ? 0.52485 0.95038 0.71758 0.15861  0.14323  0.29826  239 CYS B CB  
4363 S SG  A CYS B 213 ? 0.50392 0.94278 0.70068 0.15433  0.13509  0.30099  239 CYS B SG  
4364 S SG  B CYS B 213 ? 0.54731 0.94956 0.70562 0.17390  0.15347  0.29445  239 CYS B SG  
4365 N N   . VAL B 214 ? 0.49021 0.94091 0.67322 0.13002  0.11642  0.27675  240 VAL B N   
4366 C CA  . VAL B 214 ? 0.47729 0.93136 0.64209 0.12451  0.10936  0.26717  240 VAL B CA  
4367 C C   . VAL B 214 ? 0.42954 0.90162 0.60508 0.11037  0.09673  0.26352  240 VAL B C   
4368 O O   . VAL B 214 ? 0.41191 0.89376 0.60464 0.10545  0.09214  0.26918  240 VAL B O   
4369 C CB  . VAL B 214 ? 0.51506 0.96412 0.66185 0.13044  0.11101  0.26835  240 VAL B CB  
4370 C CG1 . VAL B 214 ? 0.52201 0.98395 0.68069 0.12647  0.10575  0.27488  240 VAL B CG1 
4371 C CG2 . VAL B 214 ? 0.53346 0.98217 0.65934 0.12585  0.10541  0.25909  240 VAL B CG2 
4372 N N   . ALA B 215 ? 0.41010 0.88564 0.57464 0.10434  0.09119  0.25404  241 ALA B N   
4373 C CA  . ALA B 215 ? 0.40617 0.89684 0.57737 0.09227  0.08021  0.24959  241 ALA B CA  
4374 C C   . ALA B 215 ? 0.38667 0.88004 0.53968 0.08841  0.07561  0.23957  241 ALA B C   
4375 O O   . ALA B 215 ? 0.39173 0.87462 0.53027 0.09425  0.08059  0.23540  241 ALA B O   
4376 C CB  . ALA B 215 ? 0.40841 0.90176 0.59639 0.08865  0.07927  0.25041  241 ALA B CB  
4377 N N   . ILE B 216 ? 0.36064 0.86783 0.51439 0.07870  0.06602  0.23610  242 ILE B N   
4378 C CA  . ILE B 216 ? 0.35472 0.86713 0.49495 0.07396  0.06113  0.22661  242 ILE B CA  
4379 C C   . ILE B 216 ? 0.35052 0.86557 0.49719 0.07146  0.05975  0.22196  242 ILE B C   
4380 O O   . ILE B 216 ? 0.35738 0.87879 0.51946 0.06733  0.05637  0.22551  242 ILE B O   
4381 C CB  . ILE B 216 ? 0.34717 0.87313 0.48384 0.06541  0.05241  0.22574  242 ILE B CB  
4382 C CG1 . ILE B 216 ? 0.35926 0.88340 0.48996 0.06755  0.05344  0.23125  242 ILE B CG1 
4383 C CG2 . ILE B 216 ? 0.33116 0.86332 0.45520 0.06096  0.04811  0.21633  242 ILE B CG2 
4384 C CD1 . ILE B 216 ? 0.36609 0.90371 0.49574 0.05875  0.04509  0.23269  242 ILE B CD1 
4385 N N   . GLY B 217 ? 0.35693 0.86731 0.49259 0.07400  0.06187  0.21458  243 GLY B N   
4386 C CA  . GLY B 217 ? 0.37076 0.88354 0.51235 0.07264  0.06110  0.21066  243 GLY B CA  
4387 C C   . GLY B 217 ? 0.37988 0.89156 0.50714 0.07392  0.06100  0.20114  243 GLY B C   
4388 O O   . GLY B 217 ? 0.36421 0.86982 0.47765 0.07717  0.06294  0.19822  243 GLY B O   
4389 N N   . TRP B 218 ? 0.39768 0.91595 0.52928 0.07148  0.05820  0.19676  244 TRP B N   
4390 C CA  . TRP B 218 ? 0.41324 0.93080 0.53363 0.07362  0.05851  0.18792  244 TRP B CA  
4391 C C   . TRP B 218 ? 0.44003 0.94268 0.55853 0.08116  0.06638  0.18871  244 TRP B C   
4392 O O   . TRP B 218 ? 0.43608 0.93150 0.56525 0.08399  0.07140  0.19594  244 TRP B O   
4393 C CB  . TRP B 218 ? 0.41495 0.94544 0.54078 0.06962  0.05295  0.18347  244 TRP B CB  
4394 C CG  . TRP B 218 ? 0.42537 0.97044 0.55012 0.06304  0.04559  0.18222  244 TRP B CG  
4395 C CD1 . TRP B 218 ? 0.42145 0.97211 0.53275 0.06099  0.04315  0.17744  244 TRP B CD1 
4396 C CD2 . TRP B 218 ? 0.42548 0.98141 0.56338 0.05768  0.03939  0.18657  244 TRP B CD2 
4397 N NE1 . TRP B 218 ? 0.42789 0.99219 0.54154 0.05509  0.03704  0.17843  244 TRP B NE1 
4398 C CE2 . TRP B 218 ? 0.41774 0.98535 0.54731 0.05305  0.03401  0.18374  244 TRP B CE2 
4399 C CE3 . TRP B 218 ? 0.43045 0.98729 0.58716 0.05613  0.03713  0.19321  244 TRP B CE3 
4400 C CZ2 . TRP B 218 ? 0.41986 0.99438 0.55455 0.04716  0.02570  0.18592  244 TRP B CZ2 
4401 C CZ3 . TRP B 218 ? 0.43073 0.99491 0.59449 0.04978  0.02775  0.19559  244 TRP B CZ3 
4402 C CH2 . TRP B 218 ? 0.43436 1.00553 0.58533 0.04553  0.02195  0.19143  244 TRP B CH2 
4403 N N   . ALA B 219 ? 0.47878 0.97694 0.58369 0.08457  0.06756  0.18163  245 ALA B N   
4404 C CA  . ALA B 219 ? 0.49288 0.97531 0.59180 0.09230  0.07507  0.18229  245 ALA B CA  
4405 C C   . ALA B 219 ? 0.52351 1.00320 0.63359 0.09418  0.07877  0.18481  245 ALA B C   
4406 O O   . ALA B 219 ? 0.55300 1.02083 0.66733 0.09905  0.08603  0.19154  245 ALA B O   
4407 C CB  . ALA B 219 ? 0.49329 0.97339 0.57654 0.09483  0.07406  0.17415  245 ALA B CB  
4408 N N   . GLY B 220 ? 0.50092 0.99190 0.61594 0.09080  0.07404  0.17995  246 GLY B N   
4409 C CA  . GLY B 220 ? 0.49991 0.99013 0.62657 0.09219  0.07660  0.18277  246 GLY B CA  
4410 C C   . GLY B 220 ? 0.50186 0.99248 0.64788 0.08996  0.07824  0.19358  246 GLY B C   
4411 O O   . GLY B 220 ? 0.51760 1.00070 0.67252 0.09312  0.08422  0.19967  246 GLY B O   
4412 N N   . ASP B 221 ? 0.47884 0.97825 0.63209 0.08449  0.07300  0.19668  247 ASP B N   
4413 C CA  . ASP B 221 ? 0.44962 0.94987 0.62254 0.08219  0.07368  0.20737  247 ASP B CA  
4414 C C   . ASP B 221 ? 0.42489 0.90916 0.59680 0.08902  0.08384  0.21441  247 ASP B C   
4415 O O   . ASP B 221 ? 0.40415 0.88369 0.59045 0.09093  0.08897  0.22266  247 ASP B O   
4416 C CB  . ASP B 221 ? 0.46033 0.97200 0.63810 0.07559  0.06583  0.20869  247 ASP B CB  
4417 C CG  . ASP B 221 ? 0.46690 0.99459 0.65151 0.06908  0.05550  0.20505  247 ASP B CG  
4418 O OD1 . ASP B 221 ? 0.46910 1.00637 0.65094 0.06421  0.04860  0.20322  247 ASP B OD1 
4419 O OD2 . ASP B 221 ? 0.47848 1.00916 0.67080 0.06920  0.05381  0.20430  247 ASP B OD2 
4420 N N   . VAL B 222 ? 0.42699 0.90307 0.58212 0.09316  0.08675  0.21173  248 VAL B N   
4421 C CA  . VAL B 222 ? 0.44102 0.90150 0.59237 0.10118  0.09622  0.21795  248 VAL B CA  
4422 C C   . VAL B 222 ? 0.48968 0.93678 0.63577 0.10808  0.10445  0.21804  248 VAL B C   
4423 O O   . VAL B 222 ? 0.50465 0.94122 0.65662 0.11375  0.11291  0.22598  248 VAL B O   
4424 C CB  . VAL B 222 ? 0.42000 0.87567 0.55381 0.10401  0.09601  0.21493  248 VAL B CB  
4425 C CG1 . VAL B 222 ? 0.42719 0.86630 0.55548 0.11365  0.10579  0.22146  248 VAL B CG1 
4426 C CG2 . VAL B 222 ? 0.40968 0.87924 0.54887 0.09670  0.08790  0.21551  248 VAL B CG2 
4427 N N   . TRP B 223 ? 0.51972 0.96709 0.65462 0.10806  0.10238  0.20956  249 TRP B N   
4428 C CA  . TRP B 223 ? 0.55564 0.99011 0.68435 0.11448  0.10983  0.20955  249 TRP B CA  
4429 C C   . TRP B 223 ? 0.60581 1.04399 0.75515 0.11258  0.11232  0.21696  249 TRP B C   
4430 O O   . TRP B 223 ? 0.63724 1.06270 0.78772 0.11858  0.12148  0.22312  249 TRP B O   
4431 C CB  . TRP B 223 ? 0.52897 0.96464 0.64245 0.11467  0.10614  0.19887  249 TRP B CB  
4432 C CG  . TRP B 223 ? 0.49718 0.92685 0.59035 0.11746  0.10468  0.19285  249 TRP B CG  
4433 C CD1 . TRP B 223 ? 0.48347 0.92316 0.56848 0.11362  0.09701  0.18419  249 TRP B CD1 
4434 C CD2 . TRP B 223 ? 0.47374 0.88640 0.55273 0.12488  0.11083  0.19578  249 TRP B CD2 
4435 N NE1 . TRP B 223 ? 0.47169 0.90289 0.54034 0.11720  0.09753  0.18232  249 TRP B NE1 
4436 C CE2 . TRP B 223 ? 0.45976 0.87382 0.52344 0.12430  0.10570  0.18917  249 TRP B CE2 
4437 C CE3 . TRP B 223 ? 0.47159 0.86790 0.54901 0.13247  0.12027  0.20367  249 TRP B CE3 
4438 C CZ2 . TRP B 223 ? 0.44759 0.84697 0.49409 0.13058  0.10890  0.19053  249 TRP B CZ2 
4439 C CZ3 . TRP B 223 ? 0.46752 0.84818 0.52618 0.13976  0.12400  0.20411  249 TRP B CZ3 
4440 C CH2 . TRP B 223 ? 0.45810 0.84004 0.50115 0.13856  0.11794  0.19770  249 TRP B CH2 
4441 N N   . GLN B 224 ? 0.60819 1.06363 0.77405 0.10436  0.10404  0.21706  250 GLN B N   
4442 C CA  . GLN B 224 ? 0.64556 1.10619 0.83417 0.10150  0.10475  0.22555  250 GLN B CA  
4443 C C   . GLN B 224 ? 0.67037 1.12661 0.87435 0.10262  0.11005  0.23749  250 GLN B C   
4444 O O   . GLN B 224 ? 0.67689 1.12885 0.89448 0.10444  0.11614  0.24631  250 GLN B O   
4445 C CB  . GLN B 224 ? 0.66037 1.14040 0.86273 0.09272  0.09290  0.22303  250 GLN B CB  
4446 C CG  . GLN B 224 ? 0.70142 1.18743 0.92420 0.09001  0.09151  0.22931  250 GLN B CG  
4447 C CD  . GLN B 224 ? 0.75480 1.24159 0.96833 0.08596  0.07992  0.21792  250 GLN B CD  
4448 O OE1 . GLN B 224 ? 0.77682 1.26423 0.97130 0.08591  0.07475  0.20628  250 GLN B OE1 
4449 N NE2 . GLN B 224 ? 0.77486 1.25869 1.00024 0.08259  0.07518  0.22095  250 GLN B NE2 
4450 N N   . ALA B 225 ? 0.66985 1.12736 0.87219 0.10195  0.10814  0.23840  251 ALA B N   
4451 C CA  . ALA B 225 ? 0.68737 1.13969 0.90203 0.10504  0.11422  0.24930  251 ALA B CA  
4452 C C   . ALA B 225 ? 0.68855 1.12178 0.89138 0.11609  0.12721  0.25257  251 ALA B C   
4453 O O   . ALA B 225 ? 0.69588 1.12420 0.91231 0.11963  0.13467  0.26285  251 ALA B O   
4454 C CB  . ALA B 225 ? 0.70865 1.16559 0.92086 0.10320  0.10975  0.24885  251 ALA B CB  
4455 N N   . SER B 226 ? 0.67721 1.09922 0.85455 0.12184  0.12985  0.24426  252 SER B N   
4456 C CA  . SER B 226 ? 0.68856 1.09028 0.85108 0.13302  0.14150  0.24661  252 SER B CA  
4457 C C   . SER B 226 ? 0.69510 1.09145 0.86362 0.13493  0.14761  0.25047  252 SER B C   
4458 O O   . SER B 226 ? 0.70891 1.09316 0.87933 0.14232  0.15800  0.25855  252 SER B O   
4459 C CB  . SER B 226 ? 0.69341 1.08445 0.82756 0.13777  0.14100  0.23676  252 SER B CB  
4460 O OG  . SER B 226 ? 0.70739 1.09516 0.83125 0.13768  0.14029  0.22997  252 SER B OG  
4461 N N   . ASN B 227 ? 0.70164 1.10727 0.87333 0.12875  0.14154  0.24528  253 ASN B N   
4462 C CA  . ASN B 227 ? 0.72690 1.12888 0.90558 0.12994  0.14684  0.24973  253 ASN B CA  
4463 C C   . ASN B 227 ? 0.74555 1.15644 0.95438 0.12578  0.14814  0.26263  253 ASN B C   
4464 O O   . ASN B 227 ? 0.76318 1.16626 0.97861 0.12981  0.15684  0.27084  253 ASN B O   
4465 C CB  . ASN B 227 ? 0.72208 1.13280 0.89649 0.12507  0.13963  0.24095  253 ASN B CB  
4466 C CG  . ASN B 227 ? 0.72885 1.12871 0.87389 0.13030  0.13968  0.22946  253 ASN B CG  
4467 O OD1 . ASN B 227 ? 0.73889 1.12061 0.86580 0.13862  0.14685  0.22933  253 ASN B OD1 
4468 N ND2 . ASN B 227 ? 0.71394 1.12491 0.85432 0.12585  0.13122  0.21999  253 ASN B ND2 
4469 N N   . ARG B 228 ? 0.73404 1.16075 0.96144 0.11777  0.13943  0.26516  254 ARG B N   
4470 C CA  . ARG B 228 ? 0.73627 1.17104 0.99342 0.11361  0.13954  0.27820  254 ARG B CA  
4471 C C   . ARG B 228 ? 0.72994 1.15284 0.98867 0.12230  0.15105  0.28756  254 ARG B C   
4472 O O   . ARG B 228 ? 0.71368 1.13603 0.99109 0.12343  0.15705  0.29924  254 ARG B O   
4473 C CB  . ARG B 228 ? 0.74087 1.19320 1.01468 0.10351  0.12667  0.27811  254 ARG B CB  
4474 C CG  . ARG B 228 ? 0.77062 1.23180 1.07679 0.09802  0.12438  0.29171  254 ARG B CG  
4475 C CD  . ARG B 228 ? 0.79174 1.26813 1.11162 0.08821  0.11049  0.29090  254 ARG B CD  
4476 N NE  . ARG B 228 ? 0.80538 1.29225 1.12169 0.08125  0.09886  0.28175  254 ARG B NE  
4477 C CZ  . ARG B 228 ? 0.80809 1.30704 1.12856 0.07361  0.08585  0.27762  254 ARG B CZ  
4478 N NH1 . ARG B 228 ? 0.81132 1.31311 1.14010 0.07120  0.08274  0.28199  254 ARG B NH1 
4479 N NH2 . ARG B 228 ? 0.80329 1.31137 1.11903 0.06899  0.07578  0.26920  254 ARG B NH2 
4480 N N   . ALA B 229 ? 0.75103 1.16494 0.99098 0.12883  0.15414  0.28319  255 ALA B N   
4481 C CA  . ALA B 229 ? 0.77921 1.18031 1.01694 0.13927  0.16589  0.29131  255 ALA B CA  
4482 C C   . ALA B 229 ? 0.81867 1.20188 1.04193 0.14900  0.17779  0.29269  255 ALA B C   
4483 O O   . ALA B 229 ? 0.83811 1.21390 1.06888 0.15618  0.18826  0.30311  255 ALA B O   
4484 C CB  . ALA B 229 ? 0.78852 1.18413 1.00864 0.14417  0.16555  0.28630  255 ALA B CB  
4485 N N   . LYS B 230 ? 0.81986 1.19585 1.02215 0.14971  0.17645  0.28260  256 LYS B N   
4486 C CA  . LYS B 230 ? 0.84604 1.20404 1.03311 0.15843  0.18689  0.28341  256 LYS B CA  
4487 C C   . LYS B 230 ? 0.87624 1.23980 1.08628 0.15541  0.19079  0.29389  256 LYS B C   
4488 O O   . LYS B 230 ? 0.90111 1.25169 1.10883 0.16375  0.20241  0.30128  256 LYS B O   
4489 C CB  . LYS B 230 ? 0.83271 1.18353 0.99427 0.15858  0.18290  0.27040  256 LYS B CB  
4490 C CG  . LYS B 230 ? 0.85268 1.18040 0.98233 0.17010  0.18937  0.26488  256 LYS B CG  
4491 C CD  . LYS B 230 ? 0.84795 1.17618 0.95740 0.16736  0.18023  0.25163  256 LYS B CD  
4492 C CE  . LYS B 230 ? 0.85940 1.16541 0.93880 0.17809  0.18474  0.24712  256 LYS B CE  
4493 N NZ  . LYS B 230 ? 0.84673 1.14903 0.90439 0.17661  0.17758  0.23518  256 LYS B NZ  
4494 N N   . GLU B 231 ? 0.87663 1.25924 1.10890 0.14369  0.18100  0.29511  257 GLU B N   
4495 C CA  . GLU B 231 ? 0.90198 1.29166 1.15898 0.13939  0.18292  0.30609  257 GLU B CA  
4496 C C   . GLU B 231 ? 0.90693 1.30275 1.19119 0.13935  0.18675  0.32076  257 GLU B C   
4497 O O   . GLU B 231 ? 0.92116 1.31750 1.22300 0.13967  0.19267  0.33225  257 GLU B O   
4498 C CB  . GLU B 231 ? 0.91333 1.32092 1.18453 0.12708  0.16989  0.30250  257 GLU B CB  
4499 C CG  . GLU B 231 ? 0.93269 1.34864 1.23062 0.12118  0.16962  0.31396  257 GLU B CG  
4500 C CD  . GLU B 231 ? 0.95528 1.36068 1.23942 0.12514  0.17620  0.31225  257 GLU B CD  
4501 O OE1 . GLU B 231 ? 0.96163 1.35562 1.21574 0.13071  0.17800  0.30022  257 GLU B OE1 
4502 O OE2 . GLU B 231 ? 0.96544 1.37370 1.26909 0.12242  0.17916  0.32345  257 GLU B OE2 
4503 N N   . ALA B 232 ? 0.89960 1.30003 1.18791 0.13930  0.18380  0.32122  258 ALA B N   
4504 C CA  . ALA B 232 ? 0.88132 1.29004 1.19749 0.13821  0.18551  0.33493  258 ALA B CA  
4505 C C   . ALA B 232 ? 0.86430 1.25902 1.17513 0.15162  0.20080  0.34332  258 ALA B C   
4506 O O   . ALA B 232 ? 0.88348 1.28477 1.21837 0.15215  0.20410  0.35620  258 ALA B O   
4507 C CB  . ALA B 232 ? 0.87012 1.29074 1.19390 0.13181  0.17492  0.33212  258 ALA B CB  
4508 N N   . LYS B 233 ? 0.84205 1.21746 1.12204 0.16274  0.20982  0.33664  259 LYS B N   
4509 C CA  . LYS B 233 ? 0.84050 1.20003 1.11161 0.17702  0.22501  0.34408  259 LYS B CA  
4510 C C   . LYS B 233 ? 0.81062 1.17168 1.08614 0.18210  0.22720  0.34875  259 LYS B C   
4511 O O   . LYS B 233 ? 0.82185 1.17690 1.10307 0.19191  0.23886  0.35965  259 LYS B O   
4512 C CB  . LYS B 233 ? 0.86336 1.22455 1.15568 0.17851  0.23364  0.35809  259 LYS B CB  
4513 C CG  . LYS B 233 ? 0.86609 1.21177 1.13956 0.18424  0.24154  0.35545  259 LYS B CG  
4514 C CD  . LYS B 233 ? 0.86305 1.18435 1.10445 0.20029  0.25389  0.35220  259 LYS B CD  
4515 C CE  . LYS B 233 ? 0.85227 1.16646 1.10279 0.21087  0.26916  0.36672  259 LYS B CE  
4516 N NZ  . LYS B 233 ? 0.85312 1.14130 1.07030 0.22743  0.28138  0.36368  259 LYS B NZ  
4517 N N   . ASN B 234 ? 0.76276 1.13189 1.03538 0.17601  0.21651  0.34099  260 ASN B N   
4518 C CA  . ASN B 234 ? 0.73150 1.10289 1.00848 0.18016  0.21773  0.34533  260 ASN B CA  
4519 C C   . ASN B 234 ? 0.72303 1.07559 0.96749 0.19288  0.22435  0.33882  260 ASN B C   
4520 O O   . ASN B 234 ? 0.74858 1.09829 0.99408 0.20067  0.22999  0.34496  260 ASN B O   
4521 C CB  . ASN B 234 ? 0.70145 1.09152 0.99364 0.16710  0.20276  0.34181  260 ASN B CB  
4522 C CG  . ASN B 234 ? 0.66818 1.06056 0.94358 0.15922  0.19162  0.32699  260 ASN B CG  
4523 O OD1 . ASN B 234 ? 0.66518 1.04386 0.91397 0.16467  0.19488  0.31816  260 ASN B OD1 
4524 N ND2 . ASN B 234 ? 0.64772 1.05717 0.93839 0.14661  0.17826  0.32444  260 ASN B ND2 
4525 N N   . GLY B 235 ? 0.69170 1.03114 0.90767 0.19533  0.22346  0.32705  261 GLY B N   
4526 C CA  . GLY B 235 ? 0.69467 1.01343 0.87861 0.20806  0.22971  0.32153  261 GLY B CA  
4527 C C   . GLY B 235 ? 0.69373 1.01541 0.86534 0.20569  0.22087  0.31304  261 GLY B C   
4528 O O   . GLY B 235 ? 0.71506 1.01958 0.86090 0.21658  0.22555  0.30951  261 GLY B O   
4529 N N   . VAL B 236 ? 0.67695 1.01904 0.86540 0.19222  0.20824  0.31004  262 VAL B N   
4530 C CA  . VAL B 236 ? 0.67010 1.01705 0.84811 0.18879  0.19921  0.30227  262 VAL B CA  
4531 C C   . VAL B 236 ? 0.67695 1.02216 0.83613 0.18320  0.19124  0.28901  262 VAL B C   
4532 O O   . VAL B 236 ? 0.65603 1.01024 0.82448 0.17416  0.18580  0.28595  262 VAL B O   
4533 C CB  . VAL B 236 ? 0.63332 1.00257 0.83847 0.17760  0.18977  0.30640  262 VAL B CB  
4534 C CG1 . VAL B 236 ? 0.64576 1.01496 0.86362 0.18499  0.19712  0.31820  262 VAL B CG1 
4535 C CG2 . VAL B 236 ? 0.59974 0.98375 0.82937 0.16580  0.18376  0.30879  262 VAL B CG2 
4536 N N   . ASN B 237 ? 0.69976 1.03316 0.83246 0.18901  0.19063  0.28167  263 ASN B N   
4537 C CA  . ASN B 237 ? 0.73178 1.06346 0.84580 0.18434  0.18295  0.26951  263 ASN B CA  
4538 C C   . ASN B 237 ? 0.72245 1.07017 0.83897 0.17529  0.17114  0.26437  263 ASN B C   
4539 O O   . ASN B 237 ? 0.71996 1.06382 0.82640 0.18008  0.17131  0.26492  263 ASN B O   
4540 C CB  . ASN B 237 ? 0.78949 1.09525 0.87095 0.19664  0.18979  0.26497  263 ASN B CB  
4541 C CG  . ASN B 237 ? 0.87590 1.16732 0.94337 0.20899  0.19656  0.26923  263 ASN B CG  
4542 O OD1 . ASN B 237 ? 0.93122 1.23176 1.00191 0.20686  0.19171  0.26990  263 ASN B OD1 
4543 N ND2 . ASN B 237 ? 0.91062 1.17826 0.96083 0.22265  0.20802  0.27217  263 ASN B ND2 
4544 N N   . VAL B 238 ? 0.71445 1.07997 0.84402 0.16261  0.16105  0.25986  264 VAL B N   
4545 C CA  . VAL B 238 ? 0.71866 1.09874 0.84744 0.15367  0.14948  0.25361  264 VAL B CA  
4546 C C   . VAL B 238 ? 0.71374 1.08907 0.82069 0.15254  0.14503  0.24263  264 VAL B C   
4547 O O   . VAL B 238 ? 0.70105 1.07234 0.80429 0.15208  0.14606  0.23874  264 VAL B O   
4548 C CB  . VAL B 238 ? 0.72376 1.12537 0.87802 0.14113  0.14061  0.25520  264 VAL B CB  
4549 C CG1 . VAL B 238 ? 0.73369 1.13806 0.89816 0.13709  0.14073  0.25478  264 VAL B CG1 
4550 C CG2 . VAL B 238 ? 0.70825 1.12360 0.85797 0.13203  0.12872  0.24733  264 VAL B CG2 
4551 N N   . SER B 239 ? 0.71064 1.08656 0.80341 0.15223  0.14015  0.23837  265 SER B N   
4552 C CA  . SER B 239 ? 0.69777 1.06897 0.76950 0.15151  0.13566  0.22907  265 SER B CA  
4553 C C   . SER B 239 ? 0.65457 1.04504 0.72990 0.14083  0.12401  0.22418  265 SER B C   
4554 O O   . SER B 239 ? 0.63611 1.03884 0.72412 0.13626  0.12035  0.22830  265 SER B O   
4555 C CB  . SER B 239 ? 0.72956 1.07770 0.77491 0.16299  0.14164  0.22919  265 SER B CB  
4556 O OG  . SER B 239 ? 0.75625 1.08648 0.79922 0.17408  0.15338  0.23549  265 SER B OG  
4557 N N   . PHE B 240 ? 0.64062 1.03354 0.70448 0.13712  0.11832  0.21565  266 PHE B N   
4558 C CA  . PHE B 240 ? 0.61192 1.02292 0.67776 0.12722  0.10763  0.21030  266 PHE B CA  
4559 C C   . PHE B 240 ? 0.60032 1.00421 0.64440 0.12918  0.10484  0.20686  266 PHE B C   
4560 O O   . PHE B 240 ? 0.61248 0.99999 0.63885 0.13560  0.10808  0.20410  266 PHE B O   
4561 C CB  . PHE B 240 ? 0.59157 1.01453 0.66488 0.12040  0.10242  0.20351  266 PHE B CB  
4562 C CG  . PHE B 240 ? 0.56964 1.01052 0.64407 0.11114  0.09221  0.19773  266 PHE B CG  
4563 C CD1 . PHE B 240 ? 0.55927 1.01523 0.64769 0.10363  0.08669  0.20012  266 PHE B CD1 
4564 C CD2 . PHE B 240 ? 0.55202 0.99435 0.61324 0.11019  0.08823  0.19034  266 PHE B CD2 
4565 C CE1 . PHE B 240 ? 0.52991 1.00098 0.61743 0.09570  0.07801  0.19501  266 PHE B CE1 
4566 C CE2 . PHE B 240 ? 0.52994 0.98892 0.59264 0.10218  0.07966  0.18555  266 PHE B CE2 
4567 C CZ  . PHE B 240 ? 0.51641 0.98913 0.59134 0.09510  0.07485  0.18776  266 PHE B CZ  
4568 N N   . SER B 241 ? 0.57625 0.99158 0.62090 0.12319  0.09812  0.20763  267 SER B N   
4569 C CA  . SER B 241 ? 0.56266 0.97144 0.58740 0.12346  0.09384  0.20643  267 SER B CA  
4570 C C   . SER B 241 ? 0.55231 0.98139 0.58263 0.11208  0.08305  0.20180  267 SER B C   
4571 O O   . SER B 241 ? 0.55103 0.99766 0.59658 0.10531  0.07998  0.20391  267 SER B O   
4572 C CB  . SER B 241 ? 0.56475 0.95920 0.58047 0.12893  0.09582  0.21338  267 SER B CB  
4573 O OG  . SER B 241 ? 0.55973 0.94753 0.56040 0.12535  0.08594  0.21102  267 SER B OG  
4574 N N   . ILE B 242 ? 0.52575 0.95103 0.54389 0.11024  0.07692  0.19546  268 ILE B N   
4575 C CA  . ILE B 242 ? 0.48720 0.92909 0.50757 0.10067  0.06722  0.19215  268 ILE B CA  
4576 C C   . ILE B 242 ? 0.47622 0.90571 0.48320 0.10016  0.06128  0.19560  268 ILE B C   
4577 O O   . ILE B 242 ? 0.48215 0.89179 0.47228 0.10462  0.05883  0.19391  268 ILE B O   
4578 C CB  . ILE B 242 ? 0.46452 0.91152 0.48235 0.09901  0.06388  0.18409  268 ILE B CB  
4579 C CG1 . ILE B 242 ? 0.44685 0.89934 0.47409 0.10142  0.06970  0.18066  268 ILE B CG1 
4580 C CG2 . ILE B 242 ? 0.45631 0.92466 0.47984 0.08951  0.05586  0.18171  268 ILE B CG2 
4581 C CD1 . ILE B 242 ? 0.43698 0.89280 0.46113 0.10116  0.06676  0.17244  268 ILE B CD1 
4582 N N   . PRO B 243 ? 0.46048 0.89888 0.47312 0.09484  0.05779  0.20055  269 PRO B N   
4583 C CA  . PRO B 243 ? 0.47199 0.89485 0.47097 0.09532  0.05218  0.20484  269 PRO B CA  
4584 C C   . PRO B 243 ? 0.49305 0.91473 0.48266 0.08996  0.04216  0.20191  269 PRO B C   
4585 O O   . PRO B 243 ? 0.49674 0.93558 0.49365 0.08436  0.03943  0.19722  269 PRO B O   
4586 C CB  . PRO B 243 ? 0.47329 0.91080 0.48393 0.08920  0.05014  0.21027  269 PRO B CB  
4587 C CG  . PRO B 243 ? 0.46313 0.91624 0.49179 0.08923  0.05715  0.21019  269 PRO B CG  
4588 C CD  . PRO B 243 ? 0.44879 0.90893 0.47958 0.08884  0.05855  0.20293  269 PRO B CD  
4589 N N   . LYS B 244 ? 0.50019 0.90055 0.47351 0.09210  0.03630  0.20526  270 LYS B N   
4590 C CA  . LYS B 244 ? 0.52267 0.91788 0.48673 0.08736  0.02545  0.20389  270 LYS B CA  
4591 C C   . LYS B 244 ? 0.50310 0.92477 0.48023 0.07475  0.01812  0.20557  270 LYS B C   
4592 O O   . LYS B 244 ? 0.50376 0.93317 0.48227 0.06931  0.01140  0.20366  270 LYS B O   
4593 C CB  . LYS B 244 ? 0.55083 0.91388 0.49282 0.09270  0.01956  0.20762  270 LYS B CB  
4594 C CG  . LYS B 244 ? 0.57857 0.93914 0.51956 0.09072  0.01691  0.21429  270 LYS B CG  
4595 C CD  . LYS B 244 ? 0.63279 0.95573 0.55069 0.10051  0.01556  0.21604  270 LYS B CD  
4596 C CE  . LYS B 244 ? 0.65680 0.97458 0.57417 0.09732  0.01079  0.22062  270 LYS B CE  
4597 N NZ  . LYS B 244 ? 0.70061 0.98114 0.59473 0.10892  0.01140  0.22204  270 LYS B NZ  
4598 N N   . GLU B 245 ? 0.48975 0.92560 0.47682 0.07016  0.01941  0.20962  271 GLU B N   
4599 C CA  . GLU B 245 ? 0.47802 0.93842 0.47593 0.05851  0.01341  0.21180  271 GLU B CA  
4600 C C   . GLU B 245 ? 0.43776 0.92467 0.44970 0.05459  0.01722  0.20658  271 GLU B C   
4601 O O   . GLU B 245 ? 0.43708 0.94527 0.45705 0.04575  0.01350  0.20805  271 GLU B O   
4602 C CB  . GLU B 245 ? 0.50300 0.96725 0.50669 0.05500  0.01331  0.21651  271 GLU B CB  
4603 C CG  . GLU B 245 ? 0.54624 0.98333 0.53684 0.05877  0.00927  0.22057  271 GLU B CG  
4604 C CD  . GLU B 245 ? 0.57164 0.99244 0.55636 0.07102  0.01822  0.22227  271 GLU B CD  
4605 O OE1 . GLU B 245 ? 0.56420 0.99459 0.55773 0.07519  0.02731  0.21981  271 GLU B OE1 
4606 O OE2 . GLU B 245 ? 0.58988 0.98691 0.56217 0.07643  0.01642  0.22537  271 GLU B OE2 
4607 N N   . GLY B 246 ? 0.41760 0.90290 0.43157 0.06123  0.02449  0.20084  272 GLY B N   
4608 C CA  . GLY B 246 ? 0.39794 0.90504 0.42302 0.05901  0.02791  0.19524  272 GLY B CA  
4609 C C   . GLY B 246 ? 0.40426 0.91993 0.43890 0.06034  0.03453  0.19458  272 GLY B C   
4610 O O   . GLY B 246 ? 0.43607 0.94337 0.47137 0.06258  0.03685  0.19908  272 GLY B O   
4611 N N   . ALA B 247 ? 0.38572 0.91794 0.42807 0.05914  0.03697  0.18907  273 ALA B N   
4612 C CA  . ALA B 247 ? 0.37859 0.91424 0.43021 0.05958  0.03932  0.18639  273 ALA B CA  
4613 C C   . ALA B 247 ? 0.39603 0.94502 0.45097 0.05620  0.03658  0.17911  273 ALA B C   
4614 O O   . ALA B 247 ? 0.39423 0.94933 0.44645 0.05570  0.03500  0.17545  273 ALA B O   
4615 C CB  . ALA B 247 ? 0.38131 0.90214 0.43310 0.06789  0.04604  0.18545  273 ALA B CB  
4616 N N   . MET B 248 ? 0.40008 0.95326 0.45999 0.05424  0.03614  0.17774  274 MET B N   
4617 C CA  . MET B 248 ? 0.38872 0.95178 0.44824 0.05250  0.03445  0.17094  274 MET B CA  
4618 C C   . MET B 248 ? 0.36765 0.92411 0.42654 0.05873  0.03799  0.16448  274 MET B C   
4619 O O   . MET B 248 ? 0.32913 0.87523 0.39142 0.06285  0.04166  0.16577  274 MET B O   
4620 C CB  . MET B 248 ? 0.40195 0.97208 0.46539 0.04845  0.03263  0.17256  274 MET B CB  
4621 C CG  . MET B 248 ? 0.42793 1.00704 0.48955 0.04855  0.03209  0.16570  274 MET B CG  
4622 S SD  . MET B 248 ? 0.46192 1.05052 0.52839 0.04450  0.02996  0.16842  274 MET B SD  
4623 C CE  . MET B 248 ? 0.46675 1.06324 0.52990 0.04813  0.03084  0.15944  274 MET B CE  
4624 N N   . ALA B 249 ? 0.37065 0.93346 0.42581 0.05963  0.03710  0.15809  275 ALA B N   
4625 C CA  . ALA B 249 ? 0.35993 0.91826 0.41400 0.06538  0.03976  0.15143  275 ALA B CA  
4626 C C   . ALA B 249 ? 0.38012 0.94875 0.43362 0.06483  0.03859  0.14561  275 ALA B C   
4627 O O   . ALA B 249 ? 0.41284 0.99340 0.46384 0.06126  0.03610  0.14479  275 ALA B O   
4628 C CB  . ALA B 249 ? 0.33231 0.88991 0.38261 0.06844  0.04000  0.14877  275 ALA B CB  
4629 N N   . PHE B 250 ? 0.36618 0.93085 0.42183 0.06874  0.04068  0.14219  276 PHE B N   
4630 C CA  . PHE B 250 ? 0.36506 0.93990 0.41942 0.06986  0.03982  0.13634  276 PHE B CA  
4631 C C   . PHE B 250 ? 0.36189 0.93226 0.41451 0.07644  0.04187  0.12962  276 PHE B C   
4632 O O   . PHE B 250 ? 0.38334 0.94156 0.43743 0.07972  0.04440  0.13066  276 PHE B O   
4633 C CB  . PHE B 250 ? 0.38605 0.96484 0.44705 0.06751  0.03898  0.13978  276 PHE B CB  
4634 C CG  . PHE B 250 ? 0.40715 0.97384 0.47704 0.06857  0.04128  0.14526  276 PHE B CG  
4635 C CD1 . PHE B 250 ? 0.40149 0.96330 0.47598 0.07310  0.04338  0.14304  276 PHE B CD1 
4636 C CD2 . PHE B 250 ? 0.41616 0.97683 0.49023 0.06554  0.04166  0.15312  276 PHE B CD2 
4637 C CE1 . PHE B 250 ? 0.40603 0.95692 0.48946 0.07433  0.04643  0.14913  276 PHE B CE1 
4638 C CE2 . PHE B 250 ? 0.41216 0.96176 0.49455 0.06763  0.04493  0.15867  276 PHE B CE2 
4639 C CZ  . PHE B 250 ? 0.41005 0.95463 0.49730 0.07189  0.04762  0.15695  276 PHE B CZ  
4640 N N   . PHE B 251 ? 0.34984 0.93042 0.39842 0.07909  0.04108  0.12277  277 PHE B N   
4641 C CA  . PHE B 251 ? 0.35919 0.93744 0.40510 0.08579  0.04239  0.11556  277 PHE B CA  
4642 C C   . PHE B 251 ? 0.37764 0.96186 0.42310 0.08932  0.04157  0.11038  277 PHE B C   
4643 O O   . PHE B 251 ? 0.42521 1.01732 0.46649 0.08752  0.03894  0.10899  277 PHE B O   
4644 C CB  . PHE B 251 ? 0.35769 0.94206 0.39826 0.08748  0.04181  0.11126  277 PHE B CB  
4645 C CG  . PHE B 251 ? 0.35838 0.93741 0.40031 0.08497  0.04155  0.11591  277 PHE B CG  
4646 C CD1 . PHE B 251 ? 0.36235 0.93403 0.40427 0.08930  0.04257  0.11408  277 PHE B CD1 
4647 C CD2 . PHE B 251 ? 0.36686 0.94961 0.40992 0.07861  0.03996  0.12238  277 PHE B CD2 
4648 C CE1 . PHE B 251 ? 0.37663 0.94581 0.41970 0.08750  0.04201  0.11890  277 PHE B CE1 
4649 C CE2 . PHE B 251 ? 0.37797 0.95783 0.42248 0.07658  0.03926  0.12716  277 PHE B CE2 
4650 C CZ  . PHE B 251 ? 0.38419 0.95784 0.42872 0.08109  0.04028  0.12557  277 PHE B CZ  
4651 N N   . ASP B 252 ? 0.35562 0.92612 0.40113 0.09354  0.04110  0.10685  278 ASP B N   
4652 C CA  . ASP B 252 ? 0.34435 0.91011 0.38393 0.09755  0.03714  0.09905  278 ASP B CA  
4653 C C   . ASP B 252 ? 0.33758 0.90816 0.37039 0.10421  0.03842  0.09103  278 ASP B C   
4654 O O   . ASP B 252 ? 0.34439 0.91432 0.37933 0.10612  0.04148  0.09168  278 ASP B O   
4655 C CB  . ASP B 252 ? 0.34567 0.89398 0.38976 0.09813  0.03541  0.10023  278 ASP B CB  
4656 C CG  . ASP B 252 ? 0.35540 0.90054 0.40804 0.09205  0.03293  0.10783  278 ASP B CG  
4657 O OD1 . ASP B 252 ? 0.34793 0.90159 0.39902 0.08828  0.02960  0.10885  278 ASP B OD1 
4658 O OD2 . ASP B 252 ? 0.35743 0.89156 0.41856 0.09124  0.03441  0.11323  278 ASP B OD2 
4659 N N   . VAL B 253 ? 0.31742 0.89228 0.34156 0.10817  0.03569  0.08364  279 VAL B N   
4660 C CA  . VAL B 253 ? 0.30877 0.89123 0.32734 0.11529  0.03743  0.07631  279 VAL B CA  
4661 C C   . VAL B 253 ? 0.28352 0.85587 0.29255 0.12181  0.03290  0.06713  279 VAL B C   
4662 O O   . VAL B 253 ? 0.41111 0.97571 0.41496 0.12039  0.02779  0.06598  279 VAL B O   
4663 C CB  . VAL B 253 ? 0.32196 0.92540 0.33817 0.11505  0.04077  0.07708  279 VAL B CB  
4664 C CG1 . VAL B 253 ? 0.32111 0.92939 0.34543 0.10792  0.04298  0.08589  279 VAL B CG1 
4665 C CG2 . VAL B 253 ? 0.32811 0.93373 0.33534 0.11373  0.03795  0.07595  279 VAL B CG2 
4666 N N   . PHE B 254 ? 0.28612 0.85738 0.29268 0.12897  0.03376  0.06072  280 PHE B N   
4667 C CA  . PHE B 254 ? 0.33151 0.89526 0.32721 0.13680  0.02971  0.05095  280 PHE B CA  
4668 C C   . PHE B 254 ? 0.35431 0.93432 0.34140 0.14236  0.03213  0.04622  280 PHE B C   
4669 O O   . PHE B 254 ? 0.34450 0.94258 0.33694 0.14297  0.03798  0.04872  280 PHE B O   
4670 C CB  . PHE B 254 ? 0.33592 0.89038 0.33271 0.14256  0.02935  0.04624  280 PHE B CB  
4671 C CG  . PHE B 254 ? 0.34649 0.87877 0.34324 0.14119  0.02460  0.04618  280 PHE B CG  
4672 C CD1 . PHE B 254 ? 0.35287 0.87180 0.34001 0.14651  0.01841  0.03836  280 PHE B CD1 
4673 C CD2 . PHE B 254 ? 0.29473 0.81903 0.30061 0.13496  0.02648  0.05438  280 PHE B CD2 
4674 C CE1 . PHE B 254 ? 0.35177 0.85080 0.34007 0.14454  0.01387  0.03942  280 PHE B CE1 
4675 C CE2 . PHE B 254 ? 0.29881 0.80402 0.30570 0.13387  0.02334  0.05555  280 PHE B CE2 
4676 C CZ  . PHE B 254 ? 0.34347 0.83655 0.34240 0.13812  0.01688  0.04840  280 PHE B CZ  
4677 N N   . ALA B 255 ? 0.37121 0.94400 0.34455 0.14653  0.02743  0.03994  281 ALA B N   
4678 C CA  . ALA B 255 ? 0.38901 0.97408 0.35021 0.15359  0.03009  0.03485  281 ALA B CA  
4679 C C   . ALA B 255 ? 0.41137 0.97989 0.35542 0.16183  0.02326  0.02480  281 ALA B C   
4680 O O   . ALA B 255 ? 0.41068 0.95899 0.35270 0.15919  0.01518  0.02363  281 ALA B O   
4681 C CB  . ALA B 255 ? 0.38549 0.98101 0.34392 0.14759  0.03192  0.04085  281 ALA B CB  
4682 N N   . MET B 256 ? 0.44252 1.01949 0.37418 0.17218  0.02652  0.01797  282 MET B N   
4683 C CA  . MET B 256 ? 0.50235 1.06225 0.41508 0.18167  0.01985  0.00760  282 MET B CA  
4684 C C   . MET B 256 ? 0.53247 1.09183 0.42479 0.18546  0.01873  0.00482  282 MET B C   
4685 O O   . MET B 256 ? 0.51676 1.09590 0.40810 0.18665  0.02720  0.00805  282 MET B O   
4686 C CB  . MET B 256 ? 0.53370 1.09848 0.44528 0.19371  0.02349  -0.00003 282 MET B CB  
4687 C CG  . MET B 256 ? 0.56152 1.15185 0.47325 0.20125  0.03429  -0.00007 282 MET B CG  
4688 S SD  . MET B 256 ? 0.60093 1.19779 0.51643 0.21483  0.03790  -0.00772 282 MET B SD  
4689 C CE  . MET B 256 ? 0.62370 1.18692 0.52125 0.22093  0.02523  -0.01875 282 MET B CE  
4690 N N   . PRO B 257 ? 0.56822 1.10415 0.44344 0.18707  0.00788  -0.00057 283 PRO B N   
4691 C CA  . PRO B 257 ? 0.59670 1.12765 0.44831 0.19159  0.00534  -0.00398 283 PRO B CA  
4692 C C   . PRO B 257 ? 0.61443 1.15409 0.44941 0.20718  0.01266  -0.01217 283 PRO B C   
4693 O O   . PRO B 257 ? 0.59804 1.14177 0.43732 0.21560  0.01625  -0.01729 283 PRO B O   
4694 C CB  . PRO B 257 ? 0.61530 1.11554 0.45406 0.18981  -0.01029 -0.00818 283 PRO B CB  
4695 C CG  . PRO B 257 ? 0.59351 1.08791 0.45521 0.17966  -0.01412 -0.00240 283 PRO B CG  
4696 C CD  . PRO B 257 ? 0.57298 1.08482 0.45056 0.18293  -0.00345 -0.00199 283 PRO B CD  
4697 N N   . ALA B 258 ? 0.66054 1.20265 0.47571 0.21147  0.01502  -0.01307 284 ALA B N   
4698 C CA  . ALA B 258 ? 0.69651 1.24882 0.49481 0.22710  0.02410  -0.01954 284 ALA B CA  
4699 C C   . ALA B 258 ? 0.73487 1.26412 0.51100 0.24075  0.01657  -0.03210 284 ALA B C   
4700 O O   . ALA B 258 ? 0.74800 1.28670 0.51684 0.25509  0.02474  -0.03805 284 ALA B O   
4701 C CB  . ALA B 258 ? 0.71964 1.27772 0.49943 0.22834  0.02860  -0.01685 284 ALA B CB  
4702 N N   . ASP B 259 ? 0.74887 1.24827 0.51489 0.23674  0.00092  -0.03579 285 ASP B N   
4703 C CA  . ASP B 259 ? 0.79101 1.26440 0.53422 0.24864  -0.00883 -0.04756 285 ASP B CA  
4704 C C   . ASP B 259 ? 0.76049 1.22418 0.52017 0.24594  -0.01523 -0.04957 285 ASP B C   
4705 O O   . ASP B 259 ? 0.77129 1.20651 0.51727 0.24790  -0.02915 -0.05592 285 ASP B O   
4706 C CB  . ASP B 259 ? 0.85804 1.30129 0.57457 0.24693  -0.02397 -0.05063 285 ASP B CB  
4707 C CG  . ASP B 259 ? 0.89968 1.33233 0.63317 0.22886  -0.03533 -0.04229 285 ASP B CG  
4708 O OD1 . ASP B 259 ? 0.95040 1.35594 0.67817 0.22627  -0.05076 -0.04554 285 ASP B OD1 
4709 O OD2 . ASP B 259 ? 0.90739 1.35898 0.66059 0.21738  -0.02889 -0.03200 285 ASP B OD2 
4710 N N   . ALA B 260 ? 0.72835 1.21380 0.51614 0.24138  -0.00598 -0.04400 286 ALA B N   
4711 C CA  . ALA B 260 ? 0.71725 1.19342 0.52037 0.23826  -0.01129 -0.04498 286 ALA B CA  
4712 C C   . ALA B 260 ? 0.73452 1.19812 0.52194 0.25384  -0.01439 -0.05689 286 ALA B C   
4713 O O   . ALA B 260 ? 0.75648 1.23513 0.53771 0.26698  -0.00467 -0.06153 286 ALA B O   
4714 C CB  . ALA B 260 ? 0.70222 1.20337 0.53538 0.23130  -0.00062 -0.03672 286 ALA B CB  
4715 N N   . LYS B 261 ? 0.73318 1.16933 0.51490 0.25247  -0.02800 -0.06131 287 LYS B N   
4716 C CA  . LYS B 261 ? 0.75578 1.17644 0.52176 0.26679  -0.03292 -0.07282 287 LYS B CA  
4717 C C   . LYS B 261 ? 0.75246 1.18518 0.53923 0.26887  -0.02692 -0.07286 287 LYS B C   
4718 O O   . LYS B 261 ? 0.76092 1.19682 0.54061 0.28332  -0.02338 -0.08089 287 LYS B O   
4719 C CB  . LYS B 261 ? 0.77608 1.16049 0.52620 0.26413  -0.05147 -0.07725 287 LYS B CB  
4720 C CG  . LYS B 261 ? 0.81328 1.17996 0.53786 0.26432  -0.06063 -0.07914 287 LYS B CG  
4721 C CD  . LYS B 261 ? 0.84869 1.19100 0.53889 0.28114  -0.06905 -0.09241 287 LYS B CD  
4722 C CE  . LYS B 261 ? 0.86048 1.20062 0.52284 0.28901  -0.06727 -0.09551 287 LYS B CE  
4723 N NZ  . LYS B 261 ? 0.85120 1.18943 0.51778 0.27372  -0.07242 -0.08624 287 LYS B NZ  
4724 N N   . ASN B 262 ? 0.73888 1.17755 0.55053 0.25523  -0.02586 -0.06390 288 ASN B N   
4725 C CA  . ASN B 262 ? 0.74589 1.19117 0.57582 0.25569  -0.02231 -0.06335 288 ASN B CA  
4726 C C   . ASN B 262 ? 0.73835 1.21447 0.59134 0.24987  -0.00896 -0.05420 288 ASN B C   
4727 O O   . ASN B 262 ? 0.70737 1.18650 0.57814 0.23696  -0.00803 -0.04519 288 ASN B O   
4728 C CB  . ASN B 262 ? 0.74345 1.16572 0.57989 0.24582  -0.03296 -0.06080 288 ASN B CB  
4729 C CG  . ASN B 262 ? 0.76642 1.15787 0.58132 0.24756  -0.04793 -0.06693 288 ASN B CG  
4730 O OD1 . ASN B 262 ? 0.78268 1.15842 0.58165 0.25898  -0.05434 -0.07695 288 ASN B OD1 
4731 N ND2 . ASN B 262 ? 0.76828 1.15019 0.58295 0.23618  -0.05448 -0.06064 288 ASN B ND2 
4732 N N   . LYS B 263 ? 0.76090 1.25962 0.61321 0.25991  0.00137  -0.05618 289 LYS B N   
4733 C CA  . LYS B 263 ? 0.74870 1.27722 0.62290 0.25487  0.01322  -0.04729 289 LYS B CA  
4734 C C   . LYS B 263 ? 0.72673 1.25978 0.62077 0.25333  0.01423  -0.04540 289 LYS B C   
4735 O O   . LYS B 263 ? 0.70909 1.25269 0.62191 0.24243  0.01781  -0.03621 289 LYS B O   
4736 C CB  . LYS B 263 ? 0.77398 1.32569 0.64236 0.26629  0.02399  -0.04905 289 LYS B CB  
4737 C CG  . LYS B 263 ? 0.75767 1.34042 0.64587 0.25979  0.03564  -0.03850 289 LYS B CG  
4738 C CD  . LYS B 263 ? 0.77611 1.37491 0.65141 0.26745  0.04451  -0.03853 289 LYS B CD  
4739 C CE  . LYS B 263 ? 0.75855 1.38366 0.65665 0.26015  0.05381  -0.02697 289 LYS B CE  
4740 N NZ  . LYS B 263 ? 0.74264 1.37694 0.66308 0.26006  0.05507  -0.02418 289 LYS B NZ  
4741 N N   . ASP B 264 ? 0.71742 1.24140 0.60623 0.26456  0.01062  -0.05409 290 ASP B N   
4742 C CA  . ASP B 264 ? 0.68786 1.21416 0.59357 0.26410  0.01047  -0.05297 290 ASP B CA  
4743 C C   . ASP B 264 ? 0.64903 1.15650 0.56142 0.25099  0.00378  -0.04782 290 ASP B C   
4744 O O   . ASP B 264 ? 0.63090 1.14592 0.56049 0.24411  0.00669  -0.04104 290 ASP B O   
4745 C CB  . ASP B 264 ? 0.72189 1.23867 0.61816 0.27919  0.00637  -0.06401 290 ASP B CB  
4746 C CG  . ASP B 264 ? 0.74178 1.27199 0.65689 0.28275  0.00952  -0.06288 290 ASP B CG  
4747 O OD1 . ASP B 264 ? 0.74883 1.30559 0.67396 0.28983  0.01849  -0.06140 290 ASP B OD1 
4748 O OD2 . ASP B 264 ? 0.74325 1.25742 0.66354 0.27839  0.00286  -0.06285 290 ASP B OD2 
4749 N N   . GLU B 265 ? 0.63827 1.12056 0.53691 0.24761  -0.00532 -0.05045 291 GLU B N   
4750 C CA  . GLU B 265 ? 0.61266 1.07775 0.51786 0.23534  -0.01058 -0.04437 291 GLU B CA  
4751 C C   . GLU B 265 ? 0.55419 1.03248 0.47262 0.22260  -0.00450 -0.03293 291 GLU B C   
4752 O O   . GLU B 265 ? 0.53744 1.01220 0.46803 0.21400  -0.00359 -0.02588 291 GLU B O   
4753 C CB  . GLU B 265 ? 0.64644 1.08418 0.53573 0.23420  -0.02182 -0.04845 291 GLU B CB  
4754 C CG  . GLU B 265 ? 0.68850 1.10870 0.56189 0.24654  -0.02977 -0.06005 291 GLU B CG  
4755 C CD  . GLU B 265 ? 0.72837 1.15447 0.58454 0.25937  -0.02876 -0.06851 291 GLU B CD  
4756 O OE1 . GLU B 265 ? 0.75722 1.16133 0.59345 0.26585  -0.03862 -0.07660 291 GLU B OE1 
4757 O OE2 . GLU B 265 ? 0.72373 1.17555 0.58543 0.26330  -0.01821 -0.06679 291 GLU B OE2 
4758 N N   . ALA B 266 ? 0.52063 1.01255 0.43520 0.22171  -0.00047 -0.03098 292 ALA B N   
4759 C CA  . ALA B 266 ? 0.47294 0.97872 0.39982 0.21032  0.00533  -0.02030 292 ALA B CA  
4760 C C   . ALA B 266 ? 0.45523 0.98025 0.39962 0.20858  0.01318  -0.01476 292 ALA B C   
4761 O O   . ALA B 266 ? 0.43403 0.95907 0.39020 0.19872  0.01487  -0.00634 292 ALA B O   
4762 C CB  . ALA B 266 ? 0.46714 0.98426 0.38480 0.21114  0.00814  -0.02000 292 ALA B CB  
4763 N N   . TYR B 267 ? 0.43402 0.97475 0.38037 0.21841  0.01759  -0.01906 293 TYR B N   
4764 C CA  . TYR B 267 ? 0.41509 0.97356 0.37923 0.21654  0.02325  -0.01338 293 TYR B CA  
4765 C C   . TYR B 267 ? 0.41413 0.95598 0.38414 0.21420  0.01839  -0.01305 293 TYR B C   
4766 O O   . TYR B 267 ? 0.42146 0.96809 0.40407 0.20734  0.02053  -0.00563 293 TYR B O   
4767 C CB  . TYR B 267 ? 0.40182 0.98198 0.36887 0.22796  0.02882  -0.01731 293 TYR B CB  
4768 C CG  . TYR B 267 ? 0.39534 0.99871 0.36271 0.22766  0.03693  -0.01309 293 TYR B CG  
4769 C CD1 . TYR B 267 ? 0.38311 1.00332 0.36468 0.21748  0.04209  -0.00242 293 TYR B CD1 
4770 C CD2 . TYR B 267 ? 0.41260 1.01919 0.36417 0.23781  0.03917  -0.01965 293 TYR B CD2 
4771 C CE1 . TYR B 267 ? 0.38918 1.02184 0.36877 0.21403  0.04696  0.00260  293 TYR B CE1 
4772 C CE2 . TYR B 267 ? 0.41366 1.03937 0.36345 0.23750  0.04682  -0.01532 293 TYR B CE2 
4773 C CZ  . TYR B 267 ? 0.40391 1.03938 0.36810 0.22390  0.04941  -0.00361 293 TYR B CZ  
4774 O OH  . TYR B 267 ? 0.38077 1.02692 0.34218 0.22081  0.05413  0.00172  293 TYR B OH  
4775 N N   . GLN B 268 ? 0.40658 0.92709 0.36592 0.21998  0.01135  -0.02093 294 GLN B N   
4776 C CA  . GLN B 268 ? 0.41976 0.92095 0.38171 0.21731  0.00648  -0.02031 294 GLN B CA  
4777 C C   . GLN B 268 ? 0.39680 0.88738 0.36244 0.20488  0.00672  -0.01131 294 GLN B C   
4778 O O   . GLN B 268 ? 0.38301 0.86903 0.35613 0.20031  0.00762  -0.00594 294 GLN B O   
4779 C CB  . GLN B 268 ? 0.45351 0.93210 0.40170 0.22476  -0.00168 -0.02981 294 GLN B CB  
4780 C CG  . GLN B 268 ? 0.47878 0.96349 0.42435 0.23829  -0.00271 -0.03888 294 GLN B CG  
4781 C CD  . GLN B 268 ? 0.51175 0.97053 0.44395 0.24475  -0.01200 -0.04767 294 GLN B CD  
4782 O OE1 . GLN B 268 ? 0.51044 0.95052 0.44323 0.24086  -0.01667 -0.04630 294 GLN B OE1 
4783 N NE2 . GLN B 268 ? 0.54162 0.99779 0.46015 0.25501  -0.01486 -0.05662 294 GLN B NE2 
4784 N N   . PHE B 269 ? 0.39846 0.88429 0.35847 0.19978  0.00570  -0.00934 295 PHE B N   
4785 C CA  . PHE B 269 ? 0.40317 0.88058 0.36829 0.18862  0.00653  -0.00016 295 PHE B CA  
4786 C C   . PHE B 269 ? 0.39460 0.89004 0.37169 0.18223  0.01371  0.00864  295 PHE B C   
4787 O O   . PHE B 269 ? 0.32862 0.81679 0.31158 0.17565  0.01541  0.01590  295 PHE B O   
4788 C CB  . PHE B 269 ? 0.36187 0.83192 0.32013 0.18478  0.00274  0.00024  295 PHE B CB  
4789 C CG  . PHE B 269 ? 0.35541 0.81356 0.31967 0.17457  0.00234  0.00924  295 PHE B CG  
4790 C CD1 . PHE B 269 ? 0.36155 0.79766 0.32405 0.17337  -0.00216 0.00968  295 PHE B CD1 
4791 C CD2 . PHE B 269 ? 0.34400 0.81333 0.31614 0.16648  0.00683  0.01782  295 PHE B CD2 
4792 C CE1 . PHE B 269 ? 0.36641 0.79316 0.33593 0.16469  -0.00117 0.01901  295 PHE B CE1 
4793 C CE2 . PHE B 269 ? 0.33860 0.79810 0.31762 0.15808  0.00718  0.02657  295 PHE B CE2 
4794 C CZ  . PHE B 269 ? 0.34807 0.78692 0.32631 0.15738  0.00368  0.02744  295 PHE B CZ  
4795 N N   . LEU B 270 ? 0.37844 0.89661 0.35835 0.18437  0.01804  0.00845  296 LEU B N   
4796 C CA  . LEU B 270 ? 0.34631 0.88171 0.33772 0.17804  0.02392  0.01707  296 LEU B CA  
4797 C C   . LEU B 270 ? 0.33077 0.86584 0.33029 0.17873  0.02422  0.01915  296 LEU B C   
4798 O O   . LEU B 270 ? 0.30325 0.83674 0.30909 0.17170  0.02596  0.02705  296 LEU B O   
4799 C CB  . LEU B 270 ? 0.34483 0.90490 0.33743 0.18052  0.02864  0.01683  296 LEU B CB  
4800 C CG  . LEU B 270 ? 0.35433 0.91408 0.33581 0.18089  0.02773  0.01421  296 LEU B CG  
4801 C CD1 . LEU B 270 ? 0.35848 0.94283 0.34035 0.18336  0.03387  0.01526  296 LEU B CD1 
4802 C CD2 . LEU B 270 ? 0.32420 0.87228 0.30618 0.17069  0.02567  0.02078  296 LEU B CD2 
4803 N N   . ASN B 271 ? 0.33887 0.87390 0.33751 0.18750  0.02177  0.01214  297 ASN B N   
4804 C CA  . ASN B 271 ? 0.35013 0.88186 0.35565 0.18826  0.02006  0.01381  297 ASN B CA  
4805 C C   . ASN B 271 ? 0.34546 0.84985 0.34526 0.18465  0.01655  0.01568  297 ASN B C   
4806 O O   . ASN B 271 ? 0.33784 0.83651 0.34151 0.18123  0.01617  0.02095  297 ASN B O   
4807 C CB  . ASN B 271 ? 0.37961 0.91717 0.38616 0.19900  0.01762  0.00580  297 ASN B CB  
4808 C CG  . ASN B 271 ? 0.40288 0.96892 0.42316 0.20103  0.02171  0.00881  297 ASN B CG  
4809 O OD1 . ASN B 271 ? 0.42273 0.99450 0.45388 0.19610  0.02151  0.01568  297 ASN B OD1 
4810 N ND2 . ASN B 271 ? 0.40049 0.98382 0.41994 0.20854  0.02526  0.00414  297 ASN B ND2 
4811 N N   . TYR B 272 ? 0.35277 0.83922 0.34270 0.18553  0.01374  0.01188  298 TYR B N   
4812 C CA  . TYR B 272 ? 0.35536 0.81693 0.34028 0.18168  0.01199  0.01522  298 TYR B CA  
4813 C C   . TYR B 272 ? 0.33497 0.79702 0.32450 0.17262  0.01685  0.02556  298 TYR B C   
4814 O O   . TYR B 272 ? 0.32700 0.77480 0.31521 0.17015  0.01759  0.03053  298 TYR B O   
4815 C CB  . TYR B 272 ? 0.37326 0.81852 0.34904 0.18332  0.00792  0.01051  298 TYR B CB  
4816 C CG  . TYR B 272 ? 0.38844 0.80908 0.36000 0.17941  0.00697  0.01489  298 TYR B CG  
4817 C CD1 . TYR B 272 ? 0.40342 0.80662 0.36999 0.18272  0.00446  0.01335  298 TYR B CD1 
4818 C CD2 . TYR B 272 ? 0.40405 0.81886 0.37685 0.17264  0.00867  0.02112  298 TYR B CD2 
4819 C CE1 . TYR B 272 ? 0.41915 0.79957 0.38060 0.17971  0.00477  0.01801  298 TYR B CE1 
4820 C CE2 . TYR B 272 ? 0.41201 0.80601 0.38246 0.16950  0.00914  0.02633  298 TYR B CE2 
4821 C CZ  . TYR B 272 ? 0.42903 0.80579 0.39306 0.17322  0.00773  0.02479  298 TYR B CZ  
4822 O OH  . TYR B 272 ? 0.47230 0.82812 0.43280 0.17061  0.00935  0.03062  298 TYR B OH  
4823 N N   . LEU B 273 ? 0.31321 0.79033 0.30678 0.16820  0.02007  0.02884  299 LEU B N   
4824 C CA  . LEU B 273 ? 0.30367 0.78328 0.30242 0.16006  0.02454  0.03859  299 LEU B CA  
4825 C C   . LEU B 273 ? 0.29585 0.78582 0.30076 0.15825  0.02663  0.04330  299 LEU B C   
4826 O O   . LEU B 273 ? 0.29105 0.77572 0.29753 0.15284  0.02926  0.05112  299 LEU B O   
4827 C CB  . LEU B 273 ? 0.30014 0.79306 0.30125 0.15597  0.02622  0.04051  299 LEU B CB  
4828 C CG  . LEU B 273 ? 0.30717 0.78719 0.30407 0.15434  0.02337  0.03974  299 LEU B CG  
4829 C CD1 . LEU B 273 ? 0.60364 1.09583 0.60355 0.14897  0.02444  0.04352  299 LEU B CD1 
4830 C CD2 . LEU B 273 ? 0.37427 0.83373 0.37148 0.15121  0.02422  0.04547  299 LEU B CD2 
4831 N N   . LEU B 274 ? 0.29556 0.80000 0.30440 0.16280  0.02519  0.03920  300 LEU B N   
4832 C CA  . LEU B 274 ? 0.28950 0.80339 0.30576 0.16060  0.02540  0.04423  300 LEU B CA  
4833 C C   . LEU B 274 ? 0.40644 0.89937 0.41835 0.16204  0.02152  0.04498  300 LEU B C   
4834 O O   . LEU B 274 ? 0.39428 0.88889 0.41019 0.15909  0.02025  0.05036  300 LEU B O   
4835 C CB  . LEU B 274 ? 0.35137 0.88985 0.37603 0.16489  0.02542  0.04091  300 LEU B CB  
4836 C CG  . LEU B 274 ? 0.34427 0.90676 0.37409 0.16191  0.03032  0.04366  300 LEU B CG  
4837 C CD1 . LEU B 274 ? 0.28265 0.86871 0.31983 0.16810  0.03169  0.04015  300 LEU B CD1 
4838 C CD2 . LEU B 274 ? 0.32778 0.89563 0.36325 0.15286  0.03244  0.05375  300 LEU B CD2 
4839 N N   . ARG B 275 ? 0.30466 0.77665 0.30745 0.16637  0.01890  0.03997  301 ARG B N   
4840 C CA  . ARG B 275 ? 0.36299 0.81156 0.35843 0.16783  0.01543  0.04100  301 ARG B CA  
4841 C C   . ARG B 275 ? 0.36367 0.79871 0.35445 0.16207  0.01906  0.04976  301 ARG B C   
4842 O O   . ARG B 275 ? 0.35180 0.78478 0.34163 0.15877  0.02379  0.05296  301 ARG B O   
4843 C CB  . ARG B 275 ? 0.36371 0.79206 0.34935 0.17330  0.01242  0.03437  301 ARG B CB  
4844 C CG  . ARG B 275 ? 0.39446 0.83326 0.38262 0.18032  0.00854  0.02501  301 ARG B CG  
4845 C CD  . ARG B 275 ? 0.43445 0.85007 0.41164 0.18531  0.00440  0.01889  301 ARG B CD  
4846 N NE  . ARG B 275 ? 0.45749 0.88174 0.43517 0.19230  0.00108  0.00964  301 ARG B NE  
4847 C CZ  . ARG B 275 ? 0.45979 0.86646 0.42835 0.19738  -0.00366 0.00305  301 ARG B CZ  
4848 N NH1 . ARG B 275 ? 0.46444 0.87896 0.43244 0.20454  -0.00681 -0.00553 301 ARG B NH1 
4849 N NH2 . ARG B 275 ? 0.45393 0.83441 0.41298 0.19571  -0.00509 0.00528  301 ARG B NH2 
4850 N N   . PRO B 276 ? 0.37226 0.79723 0.35991 0.16108  0.01656  0.05405  302 PRO B N   
4851 C CA  . PRO B 276 ? 0.37295 0.78498 0.35468 0.15668  0.02040  0.06244  302 PRO B CA  
4852 C C   . PRO B 276 ? 0.37535 0.76405 0.34615 0.15799  0.02482  0.06403  302 PRO B C   
4853 O O   . PRO B 276 ? 0.41185 0.80001 0.38337 0.15432  0.03089  0.07027  302 PRO B O   
4854 C CB  . PRO B 276 ? 0.32358 0.72421 0.30052 0.15720  0.01436  0.06485  302 PRO B CB  
4855 C CG  . PRO B 276 ? 0.31913 0.74007 0.30794 0.15885  0.00857  0.06027  302 PRO B CG  
4856 C CD  . PRO B 276 ? 0.31873 0.74563 0.30931 0.16370  0.00956  0.05209  302 PRO B CD  
4857 N N   . ASP B 277 ? 0.35796 0.72784 0.31953 0.16313  0.02202  0.05914  303 ASP B N   
4858 C CA  . ASP B 277 ? 0.38652 0.73329 0.33770 0.16433  0.02666  0.06201  303 ASP B CA  
4859 C C   . ASP B 277 ? 0.37497 0.73197 0.33416 0.16151  0.03125  0.06282  303 ASP B C   
4860 O O   . ASP B 277 ? 0.34006 0.68816 0.29792 0.15940  0.03759  0.06966  303 ASP B O   
4861 C CB  . ASP B 277 ? 0.41487 0.73936 0.35408 0.17019  0.02184  0.05656  303 ASP B CB  
4862 C CG  . ASP B 277 ? 0.42997 0.76566 0.37510 0.17316  0.01645  0.04734  303 ASP B CG  
4863 O OD1 . ASP B 277 ? 0.44565 0.77145 0.38704 0.17480  0.01682  0.04479  303 ASP B OD1 
4864 O OD2 . ASP B 277 ? 0.42576 0.77991 0.37933 0.17413  0.01186  0.04307  303 ASP B OD2 
4865 N N   . VAL B 278 ? 0.37716 0.75253 0.34471 0.16173  0.02791  0.05636  304 VAL B N   
4866 C CA  . VAL B 278 ? 0.37735 0.76001 0.35092 0.15908  0.02991  0.05654  304 VAL B CA  
4867 C C   . VAL B 278 ? 0.31763 0.71317 0.29960 0.15288  0.03539  0.06446  304 VAL B C   
4868 O O   . VAL B 278 ? 0.36179 0.75108 0.34607 0.14991  0.03967  0.07054  304 VAL B O   
4869 C CB  . VAL B 278 ? 0.38745 0.78523 0.36479 0.16184  0.02453  0.04733  304 VAL B CB  
4870 C CG1 . VAL B 278 ? 0.32505 0.72858 0.30682 0.15878  0.02484  0.04757  304 VAL B CG1 
4871 C CG2 . VAL B 278 ? 0.37590 0.75951 0.34506 0.16847  0.01877  0.03953  304 VAL B CG2 
4872 N N   . VAL B 279 ? 0.30843 0.72257 0.29614 0.15073  0.03515  0.06510  305 VAL B N   
4873 C CA  . VAL B 279 ? 0.29887 0.72576 0.29423 0.14479  0.03946  0.07220  305 VAL B CA  
4874 C C   . VAL B 279 ? 0.30176 0.71336 0.29299 0.14338  0.04465  0.08103  305 VAL B C   
4875 O O   . VAL B 279 ? 0.32228 0.73712 0.31904 0.13940  0.04928  0.08793  305 VAL B O   
4876 C CB  . VAL B 279 ? 0.28974 0.74031 0.29173 0.14283  0.03773  0.07089  305 VAL B CB  
4877 C CG1 . VAL B 279 ? 0.29096 0.73818 0.29020 0.14353  0.03607  0.07290  305 VAL B CG1 
4878 C CG2 . VAL B 279 ? 0.28071 0.74593 0.29037 0.13668  0.04103  0.07672  305 VAL B CG2 
4879 N N   . ALA B 280 ? 0.31132 0.70445 0.29183 0.14726  0.04382  0.08104  306 ALA B N   
4880 C CA  . ALA B 280 ? 0.31854 0.69292 0.29112 0.14776  0.04925  0.08899  306 ALA B CA  
4881 C C   . ALA B 280 ? 0.32458 0.68543 0.29614 0.14873  0.05512  0.09299  306 ALA B C   
4882 O O   . ALA B 280 ? 0.32488 0.68155 0.29812 0.14736  0.06201  0.10140  306 ALA B O   
4883 C CB  . ALA B 280 ? 0.46979 0.82463 0.42814 0.15224  0.04569  0.08751  306 ALA B CB  
4884 N N   . HIS B 281 ? 0.33016 0.68423 0.29975 0.15120  0.05242  0.08762  307 HIS B N   
4885 C CA  . HIS B 281 ? 0.33560 0.67923 0.30708 0.15100  0.05706  0.09209  307 HIS B CA  
4886 C C   . HIS B 281 ? 0.32444 0.68598 0.31184 0.14511  0.05903  0.09660  307 HIS B C   
4887 O O   . HIS B 281 ? 0.34201 0.69888 0.33497 0.14344  0.06556  0.10545  307 HIS B O   
4888 C CB  . HIS B 281 ? 0.34393 0.67796 0.31046 0.15411  0.05163  0.08470  307 HIS B CB  
4889 C CG  . HIS B 281 ? 0.41635 0.73661 0.38368 0.15387  0.05557  0.08989  307 HIS B CG  
4890 N ND1 . HIS B 281 ? 0.42777 0.72899 0.38778 0.15621  0.06380  0.09825  307 HIS B ND1 
4891 C CD2 . HIS B 281 ? 0.41747 0.73965 0.39190 0.15166  0.05217  0.08845  307 HIS B CD2 
4892 C CE1 . HIS B 281 ? 0.44331 0.73738 0.40799 0.15502  0.06608  0.10249  307 HIS B CE1 
4893 N NE2 . HIS B 281 ? 0.43279 0.73889 0.40650 0.15181  0.05830  0.09667  307 HIS B NE2 
4894 N N   . ILE B 282 ? 0.31454 0.69649 0.30939 0.14223  0.05345  0.09105  308 ILE B N   
4895 C CA  . ILE B 282 ? 0.30552 0.70346 0.31361 0.13651  0.05387  0.09497  308 ILE B CA  
4896 C C   . ILE B 282 ? 0.29977 0.70178 0.31283 0.13364  0.06038  0.10445  308 ILE B C   
4897 O O   . ILE B 282 ? 0.29722 0.70186 0.32055 0.13014  0.06394  0.11206  308 ILE B O   
4898 C CB  . ILE B 282 ? 0.29883 0.71623 0.31003 0.13511  0.04722  0.08704  308 ILE B CB  
4899 C CG1 . ILE B 282 ? 0.30659 0.71864 0.31196 0.13917  0.04079  0.07745  308 ILE B CG1 
4900 C CG2 . ILE B 282 ? 0.29211 0.72322 0.31449 0.12922  0.04669  0.09114  308 ILE B CG2 
4901 C CD1 . ILE B 282 ? 0.34973 0.77945 0.35562 0.13990  0.03535  0.06927  308 ILE B CD1 
4902 N N   . SER B 283 ? 0.30676 0.70908 0.31320 0.13504  0.06124  0.10444  309 SER B N   
4903 C CA  . SER B 283 ? 0.30410 0.70751 0.31278 0.13313  0.06674  0.11307  309 SER B CA  
4904 C C   . SER B 283 ? 0.31517 0.69950 0.32063 0.13625  0.07495  0.12136  309 SER B C   
4905 O O   . SER B 283 ? 0.30213 0.68968 0.31580 0.13425  0.08059  0.12996  309 SER B O   
4906 C CB  . SER B 283 ? 0.31208 0.71593 0.31242 0.13418  0.06439  0.11131  309 SER B CB  
4907 O OG  . SER B 283 ? 0.30999 0.73636 0.31842 0.12932  0.06060  0.10969  309 SER B OG  
4908 N N   . ASP B 284 ? 0.32065 0.68491 0.31403 0.14164  0.07606  0.11928  310 ASP B N   
4909 C CA  . ASP B 284 ? 0.36289 0.70827 0.35188 0.14549  0.08502  0.12746  310 ASP B CA  
4910 C C   . ASP B 284 ? 0.35497 0.70802 0.36098 0.14178  0.08851  0.13387  310 ASP B C   
4911 O O   . ASP B 284 ? 0.35481 0.70336 0.36604 0.14277  0.09740  0.14412  310 ASP B O   
4912 C CB  . ASP B 284 ? 0.37443 0.69705 0.34686 0.15146  0.08444  0.12330  310 ASP B CB  
4913 C CG  . ASP B 284 ? 0.40421 0.71442 0.35899 0.15559  0.08114  0.11923  310 ASP B CG  
4914 O OD1 . ASP B 284 ? 0.41718 0.72902 0.36952 0.15531  0.08282  0.12304  310 ASP B OD1 
4915 O OD2 . ASP B 284 ? 0.43450 0.73242 0.37792 0.15896  0.07594  0.11245  310 ASP B OD2 
4916 N N   . HIS B 285 ? 0.34965 0.71371 0.36456 0.13780  0.08122  0.12834  311 HIS B N   
4917 C CA  . HIS B 285 ? 0.33327 0.70321 0.36478 0.13346  0.08215  0.13464  311 HIS B CA  
4918 C C   . HIS B 285 ? 0.32004 0.70847 0.36719 0.12790  0.08263  0.14052  311 HIS B C   
4919 O O   . HIS B 285 ? 0.30501 0.69436 0.36495 0.12633  0.08879  0.15120  311 HIS B O   
4920 C CB  . HIS B 285 ? 0.35801 0.73014 0.39139 0.13134  0.07266  0.12665  311 HIS B CB  
4921 C CG  . HIS B 285 ? 0.36843 0.74456 0.41850 0.12616  0.07112  0.13313  311 HIS B CG  
4922 N ND1 . HIS B 285 ? 0.38731 0.75204 0.44359 0.12665  0.07774  0.14295  311 HIS B ND1 
4923 C CD2 . HIS B 285 ? 0.36213 0.75171 0.42402 0.12025  0.06319  0.13189  311 HIS B CD2 
4924 C CE1 . HIS B 285 ? 0.38392 0.75598 0.45739 0.12059  0.07329  0.14790  311 HIS B CE1 
4925 N NE2 . HIS B 285 ? 0.36814 0.75409 0.44424 0.11667  0.06384  0.14096  311 HIS B NE2 
4926 N N   . VAL B 286 ? 0.31627 0.71985 0.36318 0.12500  0.07634  0.13425  312 VAL B N   
4927 C CA  . VAL B 286 ? 0.30933 0.73044 0.37026 0.11903  0.07465  0.13859  312 VAL B CA  
4928 C C   . VAL B 286 ? 0.30071 0.72449 0.36210 0.11947  0.08102  0.14549  312 VAL B C   
4929 O O   . VAL B 286 ? 0.27651 0.71264 0.35060 0.11486  0.08085  0.15118  312 VAL B O   
4930 C CB  . VAL B 286 ? 0.30909 0.74531 0.36876 0.11572  0.06514  0.12914  312 VAL B CB  
4931 C CG1 . VAL B 286 ? 0.32407 0.75559 0.38010 0.11671  0.05823  0.12111  312 VAL B CG1 
4932 C CG2 . VAL B 286 ? 0.29042 0.73109 0.33888 0.11787  0.06476  0.12374  312 VAL B CG2 
4933 N N   . PHE B 287 ? 0.31634 0.72739 0.36334 0.12497  0.08564  0.14513  313 PHE B N   
4934 C CA  . PHE B 287 ? 0.33691 0.74690 0.38082 0.12626  0.09066  0.15103  313 PHE B CA  
4935 C C   . PHE B 287 ? 0.36535 0.79382 0.41304 0.12081  0.08453  0.14828  313 PHE B C   
4936 O O   . PHE B 287 ? 0.37246 0.80819 0.42761 0.11827  0.08670  0.15490  313 PHE B O   
4937 C CB  . PHE B 287 ? 0.35618 0.76286 0.41105 0.12737  0.09975  0.16313  313 PHE B CB  
4938 C CG  . PHE B 287 ? 0.39433 0.77953 0.43978 0.13491  0.10898  0.16782  313 PHE B CG  
4939 C CD1 . PHE B 287 ? 0.40483 0.77614 0.43886 0.14128  0.11707  0.17346  313 PHE B CD1 
4940 C CD2 . PHE B 287 ? 0.41271 0.79003 0.45890 0.13602  0.10940  0.16664  313 PHE B CD2 
4941 C CE1 . PHE B 287 ? 0.42116 0.77103 0.44369 0.14919  0.12630  0.17789  313 PHE B CE1 
4942 C CE2 . PHE B 287 ? 0.43283 0.78980 0.46911 0.14305  0.11847  0.17148  313 PHE B CE2 
4943 C CZ  . PHE B 287 ? 0.43431 0.77749 0.45822 0.14993  0.12738  0.17712  313 PHE B CZ  
4944 N N   . TYR B 288 ? 0.37010 0.80639 0.41274 0.11932  0.07713  0.13881  314 TYR B N   
4945 C CA  . TYR B 288 ? 0.37737 0.83023 0.42083 0.11501  0.07201  0.13593  314 TYR B CA  
4946 C C   . TYR B 288 ? 0.35727 0.80603 0.38792 0.11786  0.06886  0.12971  314 TYR B C   
4947 O O   . TYR B 288 ? 0.35197 0.79003 0.37492 0.12216  0.06775  0.12430  314 TYR B O   
4948 C CB  . TYR B 288 ? 0.41188 0.88200 0.46367 0.11024  0.06586  0.13114  314 TYR B CB  
4949 C CG  . TYR B 288 ? 0.45108 0.92894 0.51670 0.10537  0.06599  0.13773  314 TYR B CG  
4950 C CD1 . TYR B 288 ? 0.47072 0.96260 0.54161 0.10029  0.06399  0.14080  314 TYR B CD1 
4951 C CD2 . TYR B 288 ? 0.47362 0.94471 0.54778 0.10545  0.06729  0.14138  314 TYR B CD2 
4952 C CE1 . TYR B 288 ? 0.48336 0.98154 0.56719 0.09573  0.06288  0.14692  314 TYR B CE1 
4953 C CE2 . TYR B 288 ? 0.49385 0.97219 0.58275 0.10054  0.06610  0.14815  314 TYR B CE2 
4954 C CZ  . TYR B 288 ? 0.49951 0.99107 0.59297 0.09584  0.06365  0.15065  314 TYR B CZ  
4955 O OH  . TYR B 288 ? 0.50769 1.00566 0.61606 0.09088  0.06133  0.15751  314 TYR B OH  
4956 N N   . ALA B 289 ? 0.35665 0.81375 0.38582 0.11513  0.06671  0.13102  315 ALA B N   
4957 C CA  . ALA B 289 ? 0.33961 0.79610 0.36013 0.11646  0.06221  0.12618  315 ALA B CA  
4958 C C   . ALA B 289 ? 0.33333 0.80785 0.35838 0.11472  0.05716  0.11836  315 ALA B C   
4959 O O   . ALA B 289 ? 0.34266 0.83451 0.37574 0.11040  0.05607  0.11825  315 ALA B O   
4960 C CB  . ALA B 289 ? 0.26540 0.72443 0.28375 0.11349  0.06087  0.13135  315 ALA B CB  
4961 N N   . ASN B 290 ? 0.30698 0.77644 0.32596 0.11874  0.05409  0.11189  316 ASN B N   
4962 C CA  . ASN B 290 ? 0.28460 0.77060 0.30707 0.11882  0.05000  0.10441  316 ASN B CA  
4963 C C   . ASN B 290 ? 0.27002 0.77032 0.29459 0.11623  0.04674  0.10505  316 ASN B C   
4964 O O   . ASN B 290 ? 0.28152 0.77606 0.30353 0.11427  0.04614  0.11065  316 ASN B O   
4965 C CB  . ASN B 290 ? 0.28664 0.76103 0.30324 0.12486  0.04805  0.09715  316 ASN B CB  
4966 C CG  . ASN B 290 ? 0.30097 0.75781 0.30830 0.12850  0.04638  0.09738  316 ASN B CG  
4967 O OD1 . ASN B 290 ? 0.29372 0.75714 0.30134 0.12810  0.04225  0.09642  316 ASN B OD1 
4968 N ND2 . ASN B 290 ? 0.31625 0.75003 0.31518 0.13208  0.04928  0.09920  316 ASN B ND2 
4969 N N   . ALA B 291 ? 0.27136 0.79018 0.30052 0.11647  0.04453  0.09964  317 ALA B N   
4970 C CA  . ALA B 291 ? 0.27285 0.80892 0.30688 0.11398  0.04203  0.10087  317 ALA B CA  
4971 C C   . ALA B 291 ? 0.28718 0.82034 0.32018 0.11845  0.03801  0.09653  317 ALA B C   
4972 O O   . ALA B 291 ? 0.30752 0.85853 0.34754 0.11740  0.03590  0.09660  317 ALA B O   
4973 C CB  . ALA B 291 ? 0.24369 0.80388 0.28377 0.11188  0.04327  0.09902  317 ALA B CB  
4974 N N   . ASN B 292 ? 0.28791 0.79917 0.31297 0.12337  0.03687  0.09340  318 ASN B N   
4975 C CA  . ASN B 292 ? 0.29318 0.79833 0.31631 0.12793  0.03200  0.08908  318 ASN B CA  
4976 C C   . ASN B 292 ? 0.30104 0.78806 0.31763 0.12669  0.02826  0.09455  318 ASN B C   
4977 O O   . ASN B 292 ? 0.28231 0.74573 0.28795 0.12826  0.03005  0.09679  318 ASN B O   
4978 C CB  . ASN B 292 ? 0.30726 0.79775 0.32369 0.13433  0.03207  0.08181  318 ASN B CB  
4979 C CG  . ASN B 292 ? 0.30151 0.79115 0.31824 0.13954  0.02668  0.07591  318 ASN B CG  
4980 O OD1 . ASN B 292 ? 0.31054 0.78859 0.32402 0.14002  0.02195  0.07792  318 ASN B OD1 
4981 N ND2 . ASN B 292 ? 0.29295 0.79360 0.31295 0.14386  0.02665  0.06857  318 ASN B ND2 
4982 N N   . LYS B 293 ? 0.29902 0.79643 0.32197 0.12413  0.02289  0.09717  319 LYS B N   
4983 C CA  . LYS B 293 ? 0.32697 0.80556 0.34250 0.12260  0.01716  0.10248  319 LYS B CA  
4984 C C   . LYS B 293 ? 0.32482 0.77719 0.32842 0.12884  0.01274  0.09824  319 LYS B C   
4985 O O   . LYS B 293 ? 0.32852 0.75400 0.31766 0.13008  0.01077  0.10136  319 LYS B O   
4986 C CB  . LYS B 293 ? 0.35567 0.85283 0.38308 0.11732  0.01112  0.10722  319 LYS B CB  
4987 C CG  . LYS B 293 ? 0.40728 0.88425 0.42655 0.11463  0.00330  0.11352  319 LYS B CG  
4988 C CD  . LYS B 293 ? 0.44798 0.94200 0.48106 0.10976  -0.00501 0.11789  319 LYS B CD  
4989 C CE  . LYS B 293 ? 0.47787 0.94815 0.50107 0.10690  -0.01502 0.12410  319 LYS B CE  
4990 N NZ  . LYS B 293 ? 0.48947 0.97524 0.52799 0.10152  -0.02490 0.12927  319 LYS B NZ  
4991 N N   . ALA B 294 ? 0.31433 0.77271 0.32223 0.13342  0.01110  0.09108  320 ALA B N   
4992 C CA  . ALA B 294 ? 0.33849 0.77194 0.33492 0.13934  0.00621  0.08673  320 ALA B CA  
4993 C C   . ALA B 294 ? 0.36239 0.77122 0.34355 0.14333  0.01196  0.08509  320 ALA B C   
4994 O O   . ALA B 294 ? 0.37456 0.75635 0.34138 0.14777  0.00871  0.08361  320 ALA B O   
4995 C CB  . ALA B 294 ? 0.30742 0.75496 0.31346 0.14356  0.00293  0.07949  320 ALA B CB  
4996 N N   . ALA B 295 ? 0.36205 0.77926 0.34615 0.14173  0.02014  0.08598  321 ALA B N   
4997 C CA  . ALA B 295 ? 0.36125 0.75909 0.33504 0.14495  0.02612  0.08557  321 ALA B CA  
4998 C C   . ALA B 295 ? 0.37401 0.75152 0.33637 0.14440  0.03022  0.09311  321 ALA B C   
4999 O O   . ALA B 295 ? 0.39156 0.74938 0.34389 0.14805  0.03542  0.09405  321 ALA B O   
5000 C CB  . ALA B 295 ? 0.32878 0.74445 0.31235 0.14336  0.03175  0.08358  321 ALA B CB  
5001 N N   . THR B 296 ? 0.39217 0.77368 0.35562 0.14031  0.02820  0.09884  322 THR B N   
5002 C CA  . THR B 296 ? 0.41809 0.78118 0.37040 0.14054  0.03255  0.10603  322 THR B CA  
5003 C C   . THR B 296 ? 0.44069 0.76826 0.37153 0.14724  0.03212  0.10636  322 THR B C   
5004 O O   . THR B 296 ? 0.44361 0.75547 0.36558 0.15060  0.04043  0.11009  322 THR B O   
5005 C CB  . THR B 296 ? 0.43207 0.80448 0.38829 0.13498  0.02830  0.11156  322 THR B CB  
5006 O OG1 . THR B 296 ? 0.30899 0.71273 0.28312 0.12906  0.03062  0.11218  322 THR B OG1 
5007 C CG2 . THR B 296 ? 0.33851 0.68937 0.28104 0.13645  0.03208  0.11859  322 THR B CG2 
5008 N N   . PRO B 297 ? 0.44500 0.75803 0.36649 0.14975  0.02308  0.10321  323 PRO B N   
5009 C CA  . PRO B 297 ? 0.44861 0.72454 0.34616 0.15668  0.02274  0.10357  323 PRO B CA  
5010 C C   . PRO B 297 ? 0.43431 0.69964 0.32662 0.16177  0.03024  0.10071  323 PRO B C   
5011 O O   . PRO B 297 ? 0.43685 0.67262 0.30930 0.16765  0.03443  0.10318  323 PRO B O   
5012 C CB  . PRO B 297 ? 0.45533 0.72274 0.34821 0.15720  0.00944  0.09990  323 PRO B CB  
5013 C CG  . PRO B 297 ? 0.44731 0.74538 0.36066 0.14991  0.00362  0.10091  323 PRO B CG  
5014 C CD  . PRO B 297 ? 0.43927 0.76761 0.37110 0.14666  0.01254  0.10004  323 PRO B CD  
5015 N N   . LEU B 298 ? 0.43483 0.72219 0.34324 0.15992  0.03197  0.09595  324 LEU B N   
5016 C CA  . LEU B 298 ? 0.41888 0.69715 0.32398 0.16375  0.03753  0.09340  324 LEU B CA  
5017 C C   . LEU B 298 ? 0.38499 0.66830 0.29610 0.16251  0.04888  0.09924  324 LEU B C   
5018 O O   . LEU B 298 ? 0.38124 0.65276 0.28810 0.16564  0.05447  0.09974  324 LEU B O   
5019 C CB  . LEU B 298 ? 0.42822 0.72491 0.34611 0.16299  0.03247  0.08512  324 LEU B CB  
5020 C CG  . LEU B 298 ? 0.46832 0.75733 0.38097 0.16600  0.02185  0.07874  324 LEU B CG  
5021 C CD1 . LEU B 298 ? 0.47051 0.77685 0.39302 0.16213  0.01412  0.07910  324 LEU B CD1 
5022 C CD2 . LEU B 298 ? 0.47902 0.77640 0.39852 0.16816  0.01975  0.07085  324 LEU B CD2 
5023 N N   . VAL B 299 ? 0.37191 0.67260 0.29377 0.15777  0.05193  0.10420  325 VAL B N   
5024 C CA  . VAL B 299 ? 0.35749 0.66287 0.28649 0.15654  0.06196  0.11074  325 VAL B CA  
5025 C C   . VAL B 299 ? 0.37627 0.65307 0.28765 0.16257  0.06957  0.11754  325 VAL B C   
5026 O O   . VAL B 299 ? 0.39013 0.64827 0.28493 0.16578  0.06677  0.11894  325 VAL B O   
5027 C CB  . VAL B 299 ? 0.36086 0.69106 0.30485 0.15008  0.06214  0.11417  325 VAL B CB  
5028 C CG1 . VAL B 299 ? 0.33586 0.67184 0.28946 0.14859  0.07142  0.12118  325 VAL B CG1 
5029 C CG2 . VAL B 299 ? 0.32583 0.68290 0.28437 0.14527  0.05540  0.10759  325 VAL B CG2 
5030 N N   . SER B 300 ? 0.37860 0.65104 0.29304 0.16446  0.07906  0.12222  326 SER B N   
5031 C CA  . SER B 300 ? 0.39767 0.64410 0.29599 0.17131  0.08861  0.12959  326 SER B CA  
5032 C C   . SER B 300 ? 0.40034 0.64444 0.29431 0.17201  0.09168  0.13597  326 SER B C   
5033 O O   . SER B 300 ? 0.41475 0.68177 0.32454 0.16597  0.08993  0.13735  326 SER B O   
5034 C CB  . SER B 300 ? 0.42303 0.67185 0.33184 0.17184  0.09888  0.13539  326 SER B CB  
5035 O OG  . SER B 300 ? 0.44578 0.71675 0.37486 0.16689  0.10339  0.14135  326 SER B OG  
5036 N N   . ALA B 301 ? 0.42365 0.63781 0.29395 0.17995  0.09601  0.13982  327 ALA B N   
5037 C CA  . ALA B 301 ? 0.45095 0.65722 0.31208 0.18207  0.09752  0.14514  327 ALA B CA  
5038 C C   . ALA B 301 ? 0.44648 0.67065 0.32568 0.18005  0.10729  0.15326  327 ALA B C   
5039 O O   . ALA B 301 ? 0.44113 0.67236 0.32307 0.17780  0.10548  0.15613  327 ALA B O   
5040 C CB  . ALA B 301 ? 0.47252 0.63965 0.30178 0.19265  0.10140  0.14784  327 ALA B CB  
5041 N N   . GLU B 302 ? 0.44322 0.67467 0.33563 0.18049  0.11687  0.15753  328 GLU B N   
5042 C CA  . GLU B 302 ? 0.44989 0.69927 0.36235 0.17822  0.12535  0.16593  328 GLU B CA  
5043 C C   . GLU B 302 ? 0.42705 0.70707 0.36091 0.16815  0.11717  0.16317  328 GLU B C   
5044 O O   . GLU B 302 ? 0.45082 0.74189 0.39489 0.16629  0.12033  0.16914  328 GLU B O   
5045 C CB  . GLU B 302 ? 0.45447 0.70789 0.38037 0.17894  0.13471  0.17104  328 GLU B CB  
5046 C CG  . GLU B 302 ? 0.44820 0.71674 0.39491 0.17792  0.14447  0.18170  328 GLU B CG  
5047 C CD  . GLU B 302 ? 0.39093 0.66582 0.35463 0.17688  0.15162  0.18734  328 GLU B CD  
5048 O OE1 . GLU B 302 ? 0.48743 0.75587 0.44658 0.17629  0.14815  0.18209  328 GLU B OE1 
5049 O OE2 . GLU B 302 ? 0.38704 0.67037 0.37010 0.17551  0.15774  0.19601  328 GLU B OE2 
5050 N N   . VAL B 303 ? 0.36665 0.66000 0.30663 0.16218  0.10694  0.15436  329 VAL B N   
5051 C CA  . VAL B 303 ? 0.38361 0.70489 0.34100 0.15334  0.09944  0.15137  329 VAL B CA  
5052 C C   . VAL B 303 ? 0.38403 0.70422 0.33137 0.15161  0.09036  0.14749  329 VAL B C   
5053 O O   . VAL B 303 ? 0.37537 0.71058 0.33100 0.14661  0.08765  0.14972  329 VAL B O   
5054 C CB  . VAL B 303 ? 0.36908 0.70711 0.33990 0.14843  0.09439  0.14466  329 VAL B CB  
5055 C CG1 . VAL B 303 ? 0.31555 0.68065 0.30078 0.14040  0.08696  0.14112  329 VAL B CG1 
5056 C CG2 . VAL B 303 ? 0.33278 0.67240 0.31566 0.14874  0.10181  0.14976  329 VAL B CG2 
5057 N N   . ARG B 304 ? 0.39119 0.69307 0.32100 0.15541  0.08496  0.14231  330 ARG B N   
5058 C CA  . ARG B 304 ? 0.39103 0.69263 0.31373 0.15289  0.07454  0.13897  330 ARG B CA  
5059 C C   . ARG B 304 ? 0.41808 0.70661 0.32949 0.15485  0.07538  0.14540  330 ARG B C   
5060 O O   . ARG B 304 ? 0.39496 0.69426 0.31018 0.14944  0.06801  0.14567  330 ARG B O   
5061 C CB  . ARG B 304 ? 0.40112 0.68360 0.30792 0.15691  0.06788  0.13271  330 ARG B CB  
5062 C CG  . ARG B 304 ? 0.41854 0.69971 0.31953 0.15412  0.05580  0.13003  330 ARG B CG  
5063 C CD  . ARG B 304 ? 0.47023 0.72753 0.35370 0.15907  0.04901  0.12502  330 ARG B CD  
5064 N NE  . ARG B 304 ? 0.53006 0.75094 0.38743 0.16755  0.05306  0.12865  330 ARG B NE  
5065 C CZ  . ARG B 304 ? 0.57505 0.77481 0.41896 0.17446  0.05838  0.12741  330 ARG B CZ  
5066 N NH1 . ARG B 304 ? 0.57130 0.78257 0.42622 0.17336  0.05932  0.12248  330 ARG B NH1 
5067 N NH2 . ARG B 304 ? 0.61907 0.78495 0.43710 0.18285  0.06275  0.13123  330 ARG B NH2 
5068 N N   . GLU B 305 ? 0.44125 0.70621 0.33827 0.16288  0.08445  0.15099  331 GLU B N   
5069 C CA  . GLU B 305 ? 0.48165 0.72835 0.36302 0.16702  0.08532  0.15661  331 GLU B CA  
5070 C C   . GLU B 305 ? 0.46213 0.72282 0.35742 0.16578  0.09347  0.16418  331 GLU B C   
5071 O O   . GLU B 305 ? 0.48423 0.72871 0.36653 0.17080  0.09627  0.16960  331 GLU B O   
5072 C CB  . GLU B 305 ? 0.55688 0.76571 0.40977 0.17842  0.09041  0.15822  331 GLU B CB  
5073 C CG  . GLU B 305 ? 0.63406 0.82691 0.47287 0.18020  0.08257  0.15098  331 GLU B CG  
5074 C CD  . GLU B 305 ? 0.74775 0.90239 0.55383 0.18784  0.07737  0.15112  331 GLU B CD  
5075 O OE1 . GLU B 305 ? 0.79501 0.93516 0.58829 0.19209  0.07991  0.15657  331 GLU B OE1 
5076 O OE2 . GLU B 305 ? 0.79294 0.93068 0.58515 0.18986  0.06997  0.14568  331 GLU B OE2 
5077 N N   . ASN B 306 ? 0.42082 0.70969 0.34131 0.15959  0.09659  0.16468  332 ASN B N   
5078 C CA  . ASN B 306 ? 0.41207 0.71692 0.34846 0.15688  0.10182  0.17160  332 ASN B CA  
5079 C C   . ASN B 306 ? 0.39237 0.71515 0.33619 0.14821  0.09170  0.17009  332 ASN B C   
5080 O O   . ASN B 306 ? 0.36958 0.71395 0.32625 0.14053  0.08498  0.16475  332 ASN B O   
5081 C CB  . ASN B 306 ? 0.38827 0.71335 0.34783 0.15365  0.10802  0.17339  332 ASN B CB  
5082 C CG  . ASN B 306 ? 0.38752 0.72480 0.36309 0.15254  0.11456  0.18210  332 ASN B CG  
5083 O OD1 . ASN B 306 ? 0.40045 0.74333 0.37703 0.14974  0.11100  0.18447  332 ASN B OD1 
5084 N ND2 . ASN B 306 ? 0.37918 0.71924 0.36873 0.15411  0.12266  0.18678  332 ASN B ND2 
5085 N N   . PRO B 307 ? 0.39379 0.70768 0.32904 0.14956  0.09047  0.17489  333 PRO B N   
5086 C CA  . PRO B 307 ? 0.38958 0.72020 0.33183 0.14069  0.08057  0.17435  333 PRO B CA  
5087 C C   . PRO B 307 ? 0.37715 0.73920 0.34449 0.13244  0.08135  0.17559  333 PRO B C   
5088 O O   . PRO B 307 ? 0.39593 0.77715 0.37168 0.12402  0.07327  0.17289  333 PRO B O   
5089 C CB  . PRO B 307 ? 0.40093 0.71112 0.32720 0.14544  0.08045  0.18025  333 PRO B CB  
5090 C CG  . PRO B 307 ? 0.40989 0.70356 0.33031 0.15590  0.09372  0.18554  333 PRO B CG  
5091 C CD  . PRO B 307 ? 0.40351 0.69155 0.32195 0.15960  0.09834  0.18139  333 PRO B CD  
5092 N N   . GLY B 308 ? 0.37880 0.74632 0.35831 0.13465  0.09062  0.18012  334 GLY B N   
5093 C CA  . GLY B 308 ? 0.38364 0.77833 0.38607 0.12702  0.09025  0.18116  334 GLY B CA  
5094 C C   . GLY B 308 ? 0.39212 0.80291 0.40439 0.12214  0.08670  0.17403  334 GLY B C   
5095 O O   . GLY B 308 ? 0.40176 0.83327 0.43062 0.11592  0.08515  0.17411  334 GLY B O   
5096 N N   . ILE B 309 ? 0.39654 0.79683 0.39787 0.12526  0.08484  0.16777  335 ILE B N   
5097 C CA  . ILE B 309 ? 0.38228 0.79566 0.39042 0.12189  0.08088  0.16018  335 ILE B CA  
5098 C C   . ILE B 309 ? 0.36016 0.77536 0.36002 0.11979  0.07227  0.15374  335 ILE B C   
5099 O O   . ILE B 309 ? 0.33635 0.77226 0.34515 0.11387  0.06696  0.14964  335 ILE B O   
5100 C CB  . ILE B 309 ? 0.40542 0.80650 0.41163 0.12761  0.08666  0.15875  335 ILE B CB  
5101 C CG1 . ILE B 309 ? 0.40850 0.81170 0.42766 0.12862  0.09494  0.16642  335 ILE B CG1 
5102 C CG2 . ILE B 309 ? 0.39348 0.80563 0.40435 0.12488  0.08142  0.15019  335 ILE B CG2 
5103 C CD1 . ILE B 309 ? 0.42495 0.81499 0.44268 0.13415  0.10156  0.16722  335 ILE B CD1 
5104 N N   . TYR B 310 ? 0.37533 0.76855 0.35799 0.12491  0.07069  0.15322  336 TYR B N   
5105 C CA  . TYR B 310 ? 0.36965 0.76301 0.34563 0.12277  0.06147  0.14875  336 TYR B CA  
5106 C C   . TYR B 310 ? 0.37717 0.76093 0.34387 0.12160  0.05713  0.15395  336 TYR B C   
5107 O O   . TYR B 310 ? 0.40049 0.75758 0.34891 0.12742  0.05604  0.15529  336 TYR B O   
5108 C CB  . TYR B 310 ? 0.36836 0.74223 0.33127 0.12892  0.06010  0.14357  336 TYR B CB  
5109 C CG  . TYR B 310 ? 0.34702 0.73455 0.31924 0.12805  0.05918  0.13634  336 TYR B CG  
5110 C CD1 . TYR B 310 ? 0.32702 0.72852 0.30387 0.12475  0.05135  0.13074  336 TYR B CD1 
5111 C CD2 . TYR B 310 ? 0.33286 0.71923 0.30968 0.13075  0.06594  0.13560  336 TYR B CD2 
5112 C CE1 . TYR B 310 ? 0.31042 0.72329 0.29439 0.12518  0.05059  0.12382  336 TYR B CE1 
5113 C CE2 . TYR B 310 ? 0.31513 0.71169 0.29866 0.13027  0.06401  0.12874  336 TYR B CE2 
5114 C CZ  . TYR B 310 ? 0.32256 0.73182 0.30872 0.12798  0.05649  0.12246  336 TYR B CZ  
5115 O OH  . TYR B 310 ? 0.32170 0.74001 0.31319 0.12870  0.05467  0.11532  336 TYR B OH  
5116 N N   . PRO B 311 ? 0.37129 0.77417 0.34838 0.11436  0.05398  0.15703  337 PRO B N   
5117 C CA  . PRO B 311 ? 0.38456 0.77758 0.35307 0.11287  0.04945  0.16271  337 PRO B CA  
5118 C C   . PRO B 311 ? 0.41444 0.79748 0.37261 0.11173  0.03907  0.16086  337 PRO B C   
5119 O O   . PRO B 311 ? 0.40929 0.80248 0.37277 0.10986  0.03493  0.15552  337 PRO B O   
5120 C CB  . PRO B 311 ? 0.35812 0.77792 0.34270 0.10425  0.04817  0.16573  337 PRO B CB  
5121 C CG  . PRO B 311 ? 0.33363 0.77740 0.33200 0.10045  0.04815  0.15989  337 PRO B CG  
5122 C CD  . PRO B 311 ? 0.34821 0.78121 0.34367 0.10732  0.05381  0.15537  337 PRO B CD  
5123 N N   . PRO B 312 ? 0.45267 0.81504 0.39608 0.11302  0.03391  0.16541  338 PRO B N   
5124 C CA  . PRO B 312 ? 0.49496 0.84684 0.42942 0.11084  0.02177  0.16472  338 PRO B CA  
5125 C C   . PRO B 312 ? 0.55100 0.93224 0.50303 0.10026  0.01426  0.16542  338 PRO B C   
5126 O O   . PRO B 312 ? 0.55397 0.96225 0.52249 0.09502  0.01868  0.16603  338 PRO B O   
5127 C CB  . PRO B 312 ? 0.50652 0.82895 0.42068 0.11458  0.01815  0.17026  338 PRO B CB  
5128 C CG  . PRO B 312 ? 0.49775 0.82688 0.41740 0.11537  0.02730  0.17479  338 PRO B CG  
5129 C CD  . PRO B 312 ? 0.46303 0.80823 0.39630 0.11746  0.03857  0.17149  338 PRO B CD  
5130 N N   . ALA B 313 ? 0.58785 0.96342 0.53632 0.09713  0.00267  0.16595  339 ALA B N   
5131 C CA  . ALA B 313 ? 0.59921 1.00417 0.56617 0.08764  -0.00366 0.16723  339 ALA B CA  
5132 C C   . ALA B 313 ? 0.62650 1.04428 0.59985 0.07977  -0.00591 0.17439  339 ALA B C   
5133 O O   . ALA B 313 ? 0.63055 1.07914 0.62153 0.07270  -0.00460 0.17554  339 ALA B O   
5134 C CB  . ALA B 313 ? 0.60879 1.00394 0.57237 0.08623  -0.01617 0.16715  339 ALA B CB  
5135 N N   . ASP B 314 ? 0.67072 1.06417 0.62856 0.08135  -0.00930 0.17929  340 ASP B N   
5136 C CA  . ASP B 314 ? 0.69978 1.10279 0.66228 0.07389  -0.01266 0.18632  340 ASP B CA  
5137 C C   . ASP B 314 ? 0.65394 1.07922 0.62878 0.07241  -0.00182 0.18635  340 ASP B C   
5138 O O   . ASP B 314 ? 0.64796 1.09623 0.63522 0.06399  -0.00335 0.19025  340 ASP B O   
5139 C CB  . ASP B 314 ? 0.79610 1.16483 0.73686 0.07762  -0.01854 0.19087  340 ASP B CB  
5140 C CG  . ASP B 314 ? 0.87310 1.21713 0.79783 0.08951  -0.00855 0.18831  340 ASP B CG  
5141 O OD1 . ASP B 314 ? 0.90366 1.25633 0.83478 0.09408  0.00182  0.18326  340 ASP B OD1 
5142 O OD2 . ASP B 314 ? 0.92339 1.23902 0.82894 0.09457  -0.01101 0.19179  340 ASP B OD2 
5143 N N   . VAL B 315 ? 0.62894 1.04721 0.60058 0.08028  0.00869  0.18259  341 VAL B N   
5144 C CA  . VAL B 315 ? 0.56859 1.00695 0.55294 0.07878  0.01768  0.18266  341 VAL B CA  
5145 C C   . VAL B 315 ? 0.54546 1.01340 0.54622 0.07459  0.02007  0.17790  341 VAL B C   
5146 O O   . VAL B 315 ? 0.52716 1.01754 0.53961 0.06912  0.02253  0.17926  341 VAL B O   
5147 C CB  . VAL B 315 ? 0.54349 0.96483 0.52101 0.08824  0.02758  0.18154  341 VAL B CB  
5148 C CG1 . VAL B 315 ? 0.52450 0.96674 0.51732 0.08624  0.03544  0.18171  341 VAL B CG1 
5149 C CG2 . VAL B 315 ? 0.54525 0.93833 0.50580 0.09343  0.02642  0.18680  341 VAL B CG2 
5150 N N   . ARG B 316 ? 0.53039 0.99762 0.53095 0.07757  0.01906  0.17223  342 ARG B N   
5151 C CA  . ARG B 316 ? 0.50736 1.00134 0.52190 0.07486  0.02106  0.16744  342 ARG B CA  
5152 C C   . ARG B 316 ? 0.47075 0.98850 0.49602 0.06578  0.01568  0.17152  342 ARG B C   
5153 O O   . ARG B 316 ? 0.44677 0.98969 0.48325 0.06263  0.01936  0.16983  342 ARG B O   
5154 C CB  . ARG B 316 ? 0.52422 1.01065 0.53573 0.08033  0.01991  0.16100  342 ARG B CB  
5155 C CG  . ARG B 316 ? 0.54829 1.02865 0.55797 0.08746  0.02801  0.15491  342 ARG B CG  
5156 C CD  . ARG B 316 ? 0.57872 1.05782 0.58820 0.09160  0.02626  0.14806  342 ARG B CD  
5157 N NE  . ARG B 316 ? 0.60890 1.06792 0.60919 0.09952  0.03150  0.14400  342 ARG B NE  
5158 C CZ  . ARG B 316 ? 0.60930 1.07487 0.61407 0.10283  0.03552  0.13760  342 ARG B CZ  
5159 N NH1 . ARG B 316 ? 0.61788 1.06399 0.61414 0.10945  0.04002  0.13518  342 ARG B NH1 
5160 N NH2 . ARG B 316 ? 0.60491 1.09570 0.62177 0.09987  0.03513  0.13391  342 ARG B NH2 
5161 N N   . ALA B 317 ? 0.47606 0.98529 0.49726 0.06163  0.00681  0.17732  343 ALA B N   
5162 C CA  . ALA B 317 ? 0.47340 1.00506 0.50579 0.05229  0.00152  0.18293  343 ALA B CA  
5163 C C   . ALA B 317 ? 0.45883 1.00460 0.49566 0.04667  0.00479  0.18746  343 ALA B C   
5164 O O   . ALA B 317 ? 0.44951 1.01900 0.49683 0.03932  0.00346  0.19131  343 ALA B O   
5165 C CB  . ALA B 317 ? 0.49107 1.00713 0.51772 0.04861  -0.01042 0.18897  343 ALA B CB  
5166 N N   . LYS B 318 ? 0.44157 0.97363 0.47109 0.05011  0.00917  0.18757  344 LYS B N   
5167 C CA  . LYS B 318 ? 0.42046 0.96294 0.45357 0.04504  0.01107  0.19213  344 LYS B CA  
5168 C C   . LYS B 318 ? 0.40682 0.96182 0.44591 0.04741  0.01974  0.18755  344 LYS B C   
5169 O O   . LYS B 318 ? 0.42910 0.99077 0.47080 0.04387  0.02114  0.19092  344 LYS B O   
5170 C CB  . LYS B 318 ? 0.41249 0.93067 0.43431 0.04659  0.00821  0.19725  344 LYS B CB  
5171 C CG  . LYS B 318 ? 0.42622 0.92963 0.44005 0.04337  -0.00248 0.20253  344 LYS B CG  
5172 C CD  . LYS B 318 ? 0.45762 0.93236 0.45651 0.04750  -0.00490 0.20632  344 LYS B CD  
5173 C CE  . LYS B 318 ? 0.49781 0.95148 0.48553 0.04563  -0.01681 0.20995  344 LYS B CE  
5174 N NZ  . LYS B 318 ? 0.53794 0.95645 0.50697 0.05269  -0.01832 0.21097  344 LYS B NZ  
5175 N N   . LEU B 319 ? 0.37641 0.93328 0.41728 0.05313  0.02448  0.18017  345 LEU B N   
5176 C CA  . LEU B 319 ? 0.35708 0.92535 0.40339 0.05475  0.03086  0.17584  345 LEU B CA  
5177 C C   . LEU B 319 ? 0.36132 0.94655 0.41325 0.04866  0.02752  0.17388  345 LEU B C   
5178 O O   . LEU B 319 ? 0.34569 0.94361 0.40035 0.04442  0.02448  0.17644  345 LEU B O   
5179 C CB  . LEU B 319 ? 0.35497 0.91725 0.40028 0.06226  0.03480  0.16793  345 LEU B CB  
5180 C CG  . LEU B 319 ? 0.36651 0.90197 0.40300 0.06947  0.03622  0.16712  345 LEU B CG  
5181 C CD1 . LEU B 319 ? 0.36511 0.89719 0.40105 0.07579  0.03937  0.15935  345 LEU B CD1 
5182 C CD2 . LEU B 319 ? 0.38084 0.90518 0.41621 0.07122  0.04015  0.17122  345 LEU B CD2 
5183 N N   . PHE B 320 ? 0.35572 0.94027 0.40800 0.04835  0.02830  0.17018  346 PHE B N   
5184 C CA  . PHE B 320 ? 0.34081 0.93816 0.39355 0.04399  0.02627  0.16812  346 PHE B CA  
5185 C C   . PHE B 320 ? 0.34215 0.93717 0.39339 0.04710  0.02852  0.16159  346 PHE B C   
5186 O O   . PHE B 320 ? 0.35657 0.94078 0.40853 0.05062  0.03082  0.16073  346 PHE B O   
5187 C CB  . PHE B 320 ? 0.32473 0.92859 0.37889 0.03655  0.02270  0.17561  346 PHE B CB  
5188 C CG  . PHE B 320 ? 0.32995 0.92518 0.38483 0.03609  0.02297  0.17912  346 PHE B CG  
5189 C CD1 . PHE B 320 ? 0.33908 0.93678 0.39406 0.03494  0.02305  0.17729  346 PHE B CD1 
5190 C CD2 . PHE B 320 ? 0.33513 0.92031 0.39026 0.03716  0.02338  0.18500  346 PHE B CD2 
5191 C CE1 . PHE B 320 ? 0.34717 0.93868 0.40476 0.03436  0.02319  0.18163  346 PHE B CE1 
5192 C CE2 . PHE B 320 ? 0.33497 0.91241 0.39146 0.03755  0.02430  0.18881  346 PHE B CE2 
5193 C CZ  . PHE B 320 ? 0.34343 0.92487 0.40248 0.03588  0.02403  0.18736  346 PHE B CZ  
5194 N N   . THR B 321 ? 0.33637 0.94264 0.38574 0.04597  0.02811  0.15778  347 THR B N   
5195 C CA  . THR B 321 ? 0.34856 0.95643 0.39576 0.04834  0.02958  0.15250  347 THR B CA  
5196 C C   . THR B 321 ? 0.36773 0.98561 0.41369 0.04300  0.02756  0.15581  347 THR B C   
5197 O O   . THR B 321 ? 0.35880 0.98420 0.40504 0.03804  0.02544  0.16045  347 THR B O   
5198 C CB  . THR B 321 ? 0.35808 0.97125 0.40228 0.05362  0.03162  0.14443  347 THR B CB  
5199 O OG1 . THR B 321 ? 0.37191 0.99743 0.41537 0.05160  0.03100  0.14516  347 THR B OG1 
5200 C CG2 . THR B 321 ? 0.37144 0.97465 0.41677 0.05904  0.03339  0.14104  347 THR B CG2 
5201 N N   . LEU B 322 ? 0.37872 0.99764 0.42370 0.04381  0.02807  0.15406  348 LEU B N   
5202 C CA  . LEU B 322 ? 0.37812 1.00681 0.42126 0.03900  0.02613  0.15746  348 LEU B CA  
5203 C C   . LEU B 322 ? 0.40476 1.04649 0.44129 0.04038  0.02725  0.15280  348 LEU B C   
5204 O O   . LEU B 322 ? 0.41274 1.05673 0.44518 0.04599  0.02957  0.14604  348 LEU B O   
5205 C CB  . LEU B 322 ? 0.35843 0.98507 0.40421 0.03904  0.02602  0.15886  348 LEU B CB  
5206 C CG  . LEU B 322 ? 0.36450 1.00134 0.40840 0.03364  0.02357  0.16354  348 LEU B CG  
5207 C CD1 . LEU B 322 ? 0.36096 0.99519 0.40889 0.02756  0.02065  0.17184  348 LEU B CD1 
5208 C CD2 . LEU B 322 ? 0.35421 0.99340 0.40195 0.03445  0.02357  0.16423  348 LEU B CD2 
5209 N N   . LYS B 323 ? 0.41903 1.06926 0.45439 0.03574  0.02596  0.15664  349 LYS B N   
5210 C CA  . LYS B 323 ? 0.43353 1.09591 0.46266 0.03732  0.02806  0.15337  349 LYS B CA  
5211 C C   . LYS B 323 ? 0.40013 1.06801 0.42193 0.03574  0.02771  0.15358  349 LYS B C   
5212 O O   . LYS B 323 ? 0.39059 1.05594 0.41412 0.03054  0.02470  0.15902  349 LYS B O   
5213 C CB  . LYS B 323 ? 0.48689 1.15646 0.51883 0.03291  0.02745  0.15846  349 LYS B CB  
5214 C CG  . LYS B 323 ? 0.52838 1.20105 0.56253 0.03698  0.02986  0.15575  349 LYS B CG  
5215 C CD  . LYS B 323 ? 0.55372 1.22586 0.59494 0.03172  0.02721  0.16302  349 LYS B CD  
5216 C CE  . LYS B 323 ? 0.58002 1.26184 0.62239 0.02440  0.02537  0.17070  349 LYS B CE  
5217 N NZ  . LYS B 323 ? 0.58023 1.26260 0.62936 0.01873  0.02204  0.17876  349 LYS B NZ  
5218 N N   . VAL B 324 ? 0.40029 1.07488 0.41248 0.04066  0.03081  0.14784  350 VAL B N   
5219 C CA  . VAL B 324 ? 0.41671 1.09404 0.41660 0.03994  0.03033  0.14743  350 VAL B CA  
5220 C C   . VAL B 324 ? 0.41057 1.09340 0.40869 0.03355  0.02957  0.15329  350 VAL B C   
5221 O O   . VAL B 324 ? 0.42812 1.11778 0.42845 0.03374  0.03225  0.15414  350 VAL B O   
5222 C CB  . VAL B 324 ? 0.43627 1.11551 0.42247 0.04871  0.03386  0.13876  350 VAL B CB  
5223 C CG1 . VAL B 324 ? 0.44902 1.12687 0.41681 0.04823  0.03226  0.13831  350 VAL B CG1 
5224 C CG2 . VAL B 324 ? 0.42541 1.09872 0.41214 0.05431  0.03372  0.13346  350 VAL B CG2 
5225 N N   . GLN B 325 ? 0.39412 1.07393 0.38824 0.02766  0.02563  0.15809  351 GLN B N   
5226 C CA  . GLN B 325 ? 0.38729 1.07038 0.37976 0.02067  0.02414  0.16424  351 GLN B CA  
5227 C C   . GLN B 325 ? 0.39839 1.08136 0.37164 0.02231  0.02513  0.16159  351 GLN B C   
5228 O O   . GLN B 325 ? 0.39703 1.07469 0.35657 0.02800  0.02477  0.15567  351 GLN B O   
5229 C CB  . GLN B 325 ? 0.37790 1.05548 0.37742 0.01292  0.01842  0.17180  351 GLN B CB  
5230 C CG  . GLN B 325 ? 0.34597 1.02080 0.36150 0.01140  0.01733  0.17533  351 GLN B CG  
5231 C CD  . GLN B 325 ? 0.33231 1.01150 0.35419 0.00707  0.01705  0.17987  351 GLN B CD  
5232 O OE1 . GLN B 325 ? 0.33489 1.02099 0.35156 0.00438  0.01812  0.18147  351 GLN B OE1 
5233 N NE2 . GLN B 325 ? 0.31290 0.98719 0.34466 0.00646  0.01546  0.18255  351 GLN B NE2 
5234 N N   . ASP B 326 ? 0.39857 1.08568 0.36904 0.01746  0.02579  0.16622  352 ASP B N   
5235 C CA  . ASP B 326 ? 0.39747 1.08066 0.34773 0.01763  0.02565  0.16530  352 ASP B CA  
5236 C C   . ASP B 326 ? 0.39467 1.06535 0.33621 0.01393  0.01730  0.16676  352 ASP B C   
5237 O O   . ASP B 326 ? 0.37849 1.04685 0.33305 0.00813  0.01235  0.17213  352 ASP B O   
5238 C CB  . ASP B 326 ? 0.39276 1.08215 0.34375 0.01166  0.02736  0.17177  352 ASP B CB  
5239 C CG  . ASP B 326 ? 0.41969 1.10433 0.34744 0.01328  0.02894  0.17046  352 ASP B CG  
5240 O OD1 . ASP B 326 ? 0.42112 1.09422 0.33650 0.00930  0.02244  0.17194  352 ASP B OD1 
5241 O OD2 . ASP B 326 ? 0.43005 1.12135 0.35114 0.01886  0.03634  0.16831  352 ASP B OD2 
5242 N N   . PRO B 327 ? 0.41759 1.07847 0.33655 0.01770  0.01452  0.16229  353 PRO B N   
5243 C CA  . PRO B 327 ? 0.41558 1.06253 0.32624 0.01387  0.00333  0.16430  353 PRO B CA  
5244 C C   . PRO B 327 ? 0.39988 1.04438 0.31715 0.00368  -0.00227 0.17313  353 PRO B C   
5245 O O   . PRO B 327 ? 0.39391 1.03034 0.31648 -0.00051 -0.01168 0.17700  353 PRO B O   
5246 C CB  . PRO B 327 ? 0.44277 1.07781 0.32433 0.01976  0.00086  0.15787  353 PRO B CB  
5247 C CG  . PRO B 327 ? 0.44615 1.08893 0.32396 0.02957  0.01119  0.15049  353 PRO B CG  
5248 C CD  . PRO B 327 ? 0.43769 1.09769 0.33775 0.02699  0.02013  0.15464  353 PRO B CD  
5249 N N   . LYS B 328 ? 0.40247 1.05352 0.32055 -0.00026 0.00254  0.17685  354 LYS B N   
5250 C CA  . LYS B 328 ? 0.39979 1.04839 0.32457 -0.00994 -0.00275 0.18519  354 LYS B CA  
5251 C C   . LYS B 328 ? 0.37686 1.02891 0.32556 -0.01376 -0.00482 0.19009  354 LYS B C   
5252 O O   . LYS B 328 ? 0.37898 1.02321 0.33272 -0.01909 -0.01283 0.19533  354 LYS B O   
5253 C CB  . LYS B 328 ? 0.40473 1.06123 0.32764 -0.01309 0.00316  0.18848  354 LYS B CB  
5254 C CG  . LYS B 328 ? 0.44167 1.09148 0.33847 -0.01063 0.00448  0.18599  354 LYS B CG  
5255 C CD  . LYS B 328 ? 0.45662 1.11751 0.35434 -0.01226 0.01238  0.18961  354 LYS B CD  
5256 C CE  . LYS B 328 ? 0.51468 1.16581 0.38713 -0.01333 0.01174  0.19075  354 LYS B CE  
5257 N NZ  . LYS B 328 ? 0.55431 1.19283 0.40041 -0.00449 0.01158  0.18277  354 LYS B NZ  
5258 N N   . ILE B 329 ? 0.34957 1.01188 0.31272 -0.01046 0.00190  0.18851  355 ILE B N   
5259 C CA  . ILE B 329 ? 0.39321 1.05639 0.37604 -0.01246 0.00057  0.19248  355 ILE B CA  
5260 C C   . ILE B 329 ? 0.32424 0.97964 0.30874 -0.00988 -0.00446 0.19187  355 ILE B C   
5261 O O   . ILE B 329 ? 0.31408 0.96531 0.31059 -0.01301 -0.00870 0.19761  355 ILE B O   
5262 C CB  . ILE B 329 ? 0.38228 1.05475 0.37687 -0.00851 0.00719  0.18998  355 ILE B CB  
5263 C CG1 . ILE B 329 ? 0.38856 1.06904 0.38370 -0.01193 0.00992  0.19275  355 ILE B CG1 
5264 C CG2 . ILE B 329 ? 0.29806 0.96778 0.30914 -0.00925 0.00562  0.19340  355 ILE B CG2 
5265 C CD1 . ILE B 329 ? 0.32080 0.99887 0.32069 -0.02109 0.00509  0.20106  355 ILE B CD1 
5266 N N   . ASP B 330 ? 0.39855 1.05123 0.37101 -0.00376 -0.00480 0.18537  356 ASP B N   
5267 C CA  . ASP B 330 ? 0.38408 1.02929 0.35887 -0.00143 -0.01185 0.18534  356 ASP B CA  
5268 C C   . ASP B 330 ? 0.37921 1.01394 0.35351 -0.00741 -0.02357 0.19112  356 ASP B C   
5269 O O   . ASP B 330 ? 0.35114 0.98025 0.34245 -0.00889 -0.02894 0.19507  356 ASP B O   
5270 C CB  . ASP B 330 ? 0.39200 1.03460 0.35182 0.00620  -0.01177 0.17675  356 ASP B CB  
5271 C CG  . ASP B 330 ? 0.39873 1.05009 0.36393 0.01295  -0.00181 0.17123  356 ASP B CG  
5272 O OD1 . ASP B 330 ? 0.38393 1.03825 0.36692 0.01275  0.00119  0.17382  356 ASP B OD1 
5273 O OD2 . ASP B 330 ? 0.41719 1.07034 0.36923 0.01896  0.00287  0.16378  356 ASP B OD2 
5274 N N   . ARG B 331 ? 0.39847 1.02752 0.35605 -0.01060 -0.02711 0.19062  357 ARG B N   
5275 C CA  . ARG B 331 ? 0.36722 0.98473 0.32404 -0.01669 -0.03914 0.19591  357 ARG B CA  
5276 C C   . ARG B 331 ? 0.35361 0.97322 0.32836 -0.02303 -0.03942 0.20430  357 ARG B C   
5277 O O   . ARG B 331 ? 0.34989 0.96261 0.33729 -0.02592 -0.04820 0.20960  357 ARG B O   
5278 C CB  . ARG B 331 ? 0.39320 1.00262 0.32525 -0.01837 -0.04213 0.19344  357 ARG B CB  
5279 C CG  . ARG B 331 ? 0.49259 1.09695 0.40281 -0.01092 -0.04178 0.18460  357 ARG B CG  
5280 C CD  . ARG B 331 ? 0.51222 1.10717 0.39557 -0.01152 -0.04318 0.18245  357 ARG B CD  
5281 N NE  . ARG B 331 ? 0.51121 1.11594 0.39560 -0.01498 -0.03343 0.18574  357 ARG B NE  
5282 C CZ  . ARG B 331 ? 0.52570 1.12542 0.38906 -0.01539 -0.03146 0.18503  357 ARG B CZ  
5283 N NH1 . ARG B 331 ? 0.50396 1.11395 0.37227 -0.01906 -0.02331 0.18908  357 ARG B NH1 
5284 N NH2 . ARG B 331 ? 0.56628 1.14947 0.40304 -0.01198 -0.03835 0.18054  357 ARG B NH2 
5285 N N   . VAL B 332 ? 0.34706 0.97544 0.32440 -0.02498 -0.03050 0.20563  358 VAL B N   
5286 C CA  . VAL B 332 ? 0.33578 0.96449 0.32822 -0.03033 -0.03096 0.21298  358 VAL B CA  
5287 C C   . VAL B 332 ? 0.31784 0.94658 0.32939 -0.02709 -0.03103 0.21571  358 VAL B C   
5288 O O   . VAL B 332 ? 0.31359 0.93614 0.33712 -0.02984 -0.03651 0.22193  358 VAL B O   
5289 C CB  . VAL B 332 ? 0.33242 0.97027 0.32546 -0.03253 -0.02277 0.21332  358 VAL B CB  
5290 C CG1 . VAL B 332 ? 0.32042 0.95703 0.32877 -0.03668 -0.02355 0.22003  358 VAL B CG1 
5291 C CG2 . VAL B 332 ? 0.35146 0.98839 0.32778 -0.03640 -0.02336 0.21292  358 VAL B CG2 
5292 N N   . ARG B 333 ? 0.30836 0.94333 0.32299 -0.02056 -0.02470 0.21113  359 ARG B N   
5293 C CA  . ARG B 333 ? 0.29286 0.92741 0.32434 -0.01640 -0.02387 0.21359  359 ARG B CA  
5294 C C   . ARG B 333 ? 0.29483 0.91894 0.33702 -0.01598 -0.03227 0.21457  359 ARG B C   
5295 O O   . ARG B 333 ? 0.31830 0.93782 0.37827 -0.01569 -0.03349 0.21972  359 ARG B O   
5296 C CB  . ARG B 333 ? 0.29846 0.93836 0.32986 -0.00962 -0.01535 0.20668  359 ARG B CB  
5297 C CG  . ARG B 333 ? 0.31699 0.96334 0.35231 -0.00911 -0.00731 0.20749  359 ARG B CG  
5298 C CD  . ARG B 333 ? 0.31449 0.96382 0.35244 -0.00193 -0.00046 0.20180  359 ARG B CD  
5299 N NE  . ARG B 333 ? 0.34357 0.99702 0.36964 0.00172  0.00135  0.19396  359 ARG B NE  
5300 C CZ  . ARG B 333 ? 0.36063 1.01795 0.38632 0.00743  0.00773  0.18706  359 ARG B CZ  
5301 N NH1 . ARG B 333 ? 0.26089 0.91589 0.29741 0.00981  0.01119  0.18645  359 ARG B NH1 
5302 N NH2 . ARG B 333 ? 0.28144 0.94154 0.29492 0.01147  0.00907  0.18007  359 ARG B NH2 
5303 N N   . THR B 334 ? 0.30789 0.92708 0.33985 -0.01564 -0.03813 0.20981  360 THR B N   
5304 C CA  . THR B 334 ? 0.31147 0.91985 0.35507 -0.01621 -0.04774 0.21116  360 THR B CA  
5305 C C   . THR B 334 ? 0.31426 0.91855 0.36593 -0.02229 -0.05634 0.22001  360 THR B C   
5306 O O   . THR B 334 ? 0.30706 0.90706 0.38017 -0.02219 -0.05981 0.22516  360 THR B O   
5307 C CB  . THR B 334 ? 0.32911 0.93039 0.35613 -0.01510 -0.05435 0.20431  360 THR B CB  
5308 O OG1 . THR B 334 ? 0.37035 0.97402 0.39330 -0.00848 -0.04696 0.19614  360 THR B OG1 
5309 C CG2 . THR B 334 ? 0.33546 0.92461 0.37466 -0.01739 -0.06709 0.20709  360 THR B CG2 
5310 N N   . ARG B 335 ? 0.32534 0.93085 0.36071 -0.02740 -0.05929 0.22225  361 ARG B N   
5311 C CA  . ARG B 335 ? 0.34119 0.93877 0.38338 -0.03346 -0.06672 0.22912  361 ARG B CA  
5312 C C   . ARG B 335 ? 0.31456 0.91445 0.37521 -0.03293 -0.06126 0.23520  361 ARG B C   
5313 O O   . ARG B 335 ? 0.31233 0.90610 0.38991 -0.03405 -0.06668 0.24120  361 ARG B O   
5314 C CB  . ARG B 335 ? 0.34718 0.94124 0.36751 -0.03909 -0.06851 0.22831  361 ARG B CB  
5315 C CG  . ARG B 335 ? 0.50015 1.08542 0.52576 -0.04552 -0.07632 0.23517  361 ARG B CG  
5316 C CD  . ARG B 335 ? 0.52989 1.10356 0.53822 -0.04990 -0.08754 0.23409  361 ARG B CD  
5317 N NE  . ARG B 335 ? 0.53531 1.10000 0.54790 -0.05611 -0.09536 0.24046  361 ARG B NE  
5318 C CZ  . ARG B 335 ? 0.53302 1.08784 0.55878 -0.05813 -0.10727 0.24472  361 ARG B CZ  
5319 N NH1 . ARG B 335 ? 0.52438 1.07709 0.56159 -0.05503 -0.11297 0.24366  361 ARG B NH1 
5320 N NH2 . ARG B 335 ? 0.53675 1.08353 0.56549 -0.06340 -0.11386 0.25023  361 ARG B NH2 
5321 N N   . ALA B 336 ? 0.30532 0.91275 0.36275 -0.03079 -0.05075 0.23379  362 ALA B N   
5322 C CA  . ALA B 336 ? 0.37265 0.97937 0.44356 -0.02947 -0.04615 0.23906  362 ALA B CA  
5323 C C   . ALA B 336 ? 0.34632 0.95193 0.43814 -0.02299 -0.04465 0.24111  362 ALA B C   
5324 O O   . ALA B 336 ? 0.27794 0.87834 0.38407 -0.02177 -0.04481 0.24719  362 ALA B O   
5325 C CB  . ALA B 336 ? 0.28848 0.90171 0.35111 -0.02869 -0.03667 0.23659  362 ALA B CB  
5326 N N   . TRP B 337 ? 0.33714 0.94580 0.43108 -0.01847 -0.04225 0.23566  363 TRP B N   
5327 C CA  . TRP B 337 ? 0.31997 0.92480 0.43445 -0.01288 -0.03923 0.23672  363 TRP B CA  
5328 C C   . TRP B 337 ? 0.33442 0.93416 0.46546 -0.01523 -0.04894 0.24281  363 TRP B C   
5329 O O   . TRP B 337 ? 0.32819 0.92432 0.47923 -0.01202 -0.04644 0.24848  363 TRP B O   
5330 C CB  . TRP B 337 ? 0.26745 0.87325 0.37842 -0.00855 -0.03464 0.22841  363 TRP B CB  
5331 C CG  . TRP B 337 ? 0.36200 0.96467 0.49162 -0.00233 -0.02879 0.22930  363 TRP B CG  
5332 C CD1 . TRP B 337 ? 0.33896 0.93804 0.48048 -0.00072 -0.03183 0.22837  363 TRP B CD1 
5333 C CD2 . TRP B 337 ? 0.24781 0.84943 0.38500 0.00320  -0.01904 0.23172  363 TRP B CD2 
5334 N NE1 . TRP B 337 ? 0.29480 0.89216 0.45184 0.00535  -0.02355 0.23056  363 TRP B NE1 
5335 C CE2 . TRP B 337 ? 0.25824 0.85635 0.41170 0.00833  -0.01540 0.23233  363 TRP B CE2 
5336 C CE3 . TRP B 337 ? 0.24471 0.84652 0.37541 0.00432  -0.01368 0.23371  363 TRP B CE3 
5337 C CZ2 . TRP B 337 ? 0.25229 0.84689 0.41409 0.01521  -0.00554 0.23464  363 TRP B CZ2 
5338 C CZ3 . TRP B 337 ? 0.23831 0.83507 0.37649 0.01119  -0.00517 0.23551  363 TRP B CZ3 
5339 C CH2 . TRP B 337 ? 0.25219 0.84532 0.40503 0.01691  -0.00062 0.23586  363 TRP B CH2 
5340 N N   . THR B 338 ? 0.35306 0.95023 0.47519 -0.02058 -0.05969 0.24163  364 THR B N   
5341 C CA  . THR B 338 ? 0.36331 0.95236 0.50026 -0.02407 -0.07025 0.24723  364 THR B CA  
5342 C C   . THR B 338 ? 0.34823 0.93305 0.49339 -0.02617 -0.07068 0.25464  364 THR B C   
5343 O O   . THR B 338 ? 0.32248 0.90247 0.48935 -0.02532 -0.07327 0.26098  364 THR B O   
5344 C CB  . THR B 338 ? 0.40255 0.98635 0.52302 -0.02957 -0.08267 0.24399  364 THR B CB  
5345 O OG1 . THR B 338 ? 0.43473 1.01943 0.54493 -0.02661 -0.08178 0.23612  364 THR B OG1 
5346 C CG2 . THR B 338 ? 0.41343 0.98728 0.55052 -0.03351 -0.09525 0.24976  364 THR B CG2 
5347 N N   . LYS B 339 ? 0.36115 0.94738 0.48960 -0.02876 -0.06803 0.25423  365 LYS B N   
5348 C CA  . LYS B 339 ? 0.39542 0.97681 0.52967 -0.03040 -0.06879 0.26091  365 LYS B CA  
5349 C C   . LYS B 339 ? 0.40273 0.98474 0.55431 -0.02288 -0.05961 0.26507  365 LYS B C   
5350 O O   . LYS B 339 ? 0.40765 0.98452 0.57567 -0.02129 -0.06140 0.27189  365 LYS B O   
5351 C CB  . LYS B 339 ? 0.42083 1.00274 0.53307 -0.03522 -0.06763 0.25925  365 LYS B CB  
5352 C CG  . LYS B 339 ? 0.43657 1.01268 0.55264 -0.03658 -0.06814 0.26550  365 LYS B CG  
5353 C CD  . LYS B 339 ? 0.45040 1.02618 0.54589 -0.04242 -0.06715 0.26364  365 LYS B CD  
5354 C CE  . LYS B 339 ? 0.45754 1.02509 0.55574 -0.04469 -0.07015 0.26961  365 LYS B CE  
5355 N NZ  . LYS B 339 ? 0.47955 1.04344 0.56029 -0.05326 -0.07459 0.26880  365 LYS B NZ  
5356 N N   . VAL B 340 ? 0.40343 0.99093 0.55077 -0.01754 -0.04962 0.26109  366 VAL B N   
5357 C CA  . VAL B 340 ? 0.40528 0.99135 0.56507 -0.00945 -0.04040 0.26452  366 VAL B CA  
5358 C C   . VAL B 340 ? 0.42440 1.00736 0.60819 -0.00490 -0.03922 0.26829  366 VAL B C   
5359 O O   . VAL B 340 ? 0.42040 0.99901 0.61870 0.00034  -0.03530 0.27479  366 VAL B O   
5360 C CB  . VAL B 340 ? 0.39231 0.98339 0.54132 -0.00505 -0.03110 0.25874  366 VAL B CB  
5361 C CG1 . VAL B 340 ? 0.38345 0.97090 0.54478 0.00440  -0.02153 0.26153  366 VAL B CG1 
5362 C CG2 . VAL B 340 ? 0.40022 0.99277 0.52894 -0.00939 -0.03139 0.25720  366 VAL B CG2 
5363 N N   . LYS B 341 ? 0.44124 1.02577 0.62947 -0.00664 -0.04271 0.26473  367 LYS B N   
5364 C CA  . LYS B 341 ? 0.43432 1.01514 0.64596 -0.00338 -0.04184 0.26862  367 LYS B CA  
5365 C C   . LYS B 341 ? 0.49120 1.06692 0.71916 -0.00705 -0.05093 0.27624  367 LYS B C   
5366 O O   . LYS B 341 ? 0.50665 1.07915 0.75691 -0.00443 -0.04991 0.28126  367 LYS B O   
5367 C CB  . LYS B 341 ? 0.41008 0.99317 0.62109 -0.00471 -0.04469 0.26276  367 LYS B CB  
5368 C CG  . LYS B 341 ? 0.38805 0.97232 0.59996 0.00237  -0.03295 0.25870  367 LYS B CG  
5369 C CD  . LYS B 341 ? 0.37892 0.96754 0.58101 0.00072  -0.03640 0.25072  367 LYS B CD  
5370 C CE  . LYS B 341 ? 0.39089 0.97679 0.60353 -0.00439 -0.04913 0.25252  367 LYS B CE  
5371 N NZ  . LYS B 341 ? 0.40165 0.99066 0.60145 -0.00531 -0.05408 0.24457  367 LYS B NZ  
5372 N N   . SER B 342 ? 0.51665 1.09087 0.73440 -0.01312 -0.05965 0.27748  368 SER B N   
5373 C CA  . SER B 342 ? 0.55581 1.12424 0.78802 -0.01701 -0.06952 0.28426  368 SER B CA  
5374 C C   . SER B 342 ? 0.57190 1.13769 0.81899 -0.01138 -0.06387 0.29226  368 SER B C   
5375 O O   . SER B 342 ? 0.57320 1.13450 0.83358 -0.01383 -0.07142 0.29839  368 SER B O   
5376 C CB  . SER B 342 ? 0.56610 1.13172 0.77917 -0.02574 -0.08144 0.28205  368 SER B CB  
5377 O OG  . SER B 342 ? 0.56971 1.13477 0.77041 -0.02605 -0.07883 0.28343  368 SER B OG  
5378 N N   . GLY B 343 ? 0.58379 1.15149 0.82842 -0.00343 -0.05139 0.29241  369 GLY B N   
5379 C CA  . GLY B 343 ? 0.59602 1.16061 0.85232 0.00367  -0.04562 0.29994  369 GLY B CA  
5380 C C   . GLY B 343 ? 0.60074 1.16358 0.88261 0.01117  -0.03790 0.30574  369 GLY B C   
5381 O O   . GLY B 343 ? 0.60483 1.16545 0.90657 0.00907  -0.04370 0.31144  369 GLY B O   
# 
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   27  ?   ?   ?   A . n 
A 1 2   GLU 2   28  ?   ?   ?   A . n 
A 1 3   GLN 3   29  29  GLN GLN A . n 
A 1 4   LYS 4   30  30  LYS LYS A . n 
A 1 5   THR 5   31  31  THR THR A . n 
A 1 6   LEU 6   32  32  LEU LEU A . n 
A 1 7   HIS 7   33  33  HIS HIS A . n 
A 1 8   ILE 8   34  34  ILE ILE A . n 
A 1 9   TYR 9   35  35  TYR TYR A . n 
A 1 10  ASN 10  36  36  ASN ASN A . n 
A 1 11  TRP 11  37  37  TRP TRP A . n 
A 1 12  SER 12  38  38  SER SER A . n 
A 1 13  ASP 13  39  39  ASP ASP A . n 
A 1 14  TYR 14  40  40  TYR TYR A . n 
A 1 15  ILE 15  41  41  ILE ILE A . n 
A 1 16  ALA 16  42  42  ALA ALA A . n 
A 1 17  PRO 17  43  43  PRO PRO A . n 
A 1 18  ASP 18  44  44  ASP ASP A . n 
A 1 19  THR 19  45  45  THR THR A . n 
A 1 20  VAL 20  46  46  VAL VAL A . n 
A 1 21  ALA 21  47  47  ALA ALA A . n 
A 1 22  ASN 22  48  48  ASN ASN A . n 
A 1 23  PHE 23  49  49  PHE PHE A . n 
A 1 24  GLU 24  50  50  GLU GLU A . n 
A 1 25  LYS 25  51  51  LYS LYS A . n 
A 1 26  GLU 26  52  52  GLU GLU A . n 
A 1 27  THR 27  53  53  THR THR A . n 
A 1 28  GLY 28  54  54  GLY GLY A . n 
A 1 29  ILE 29  55  55  ILE ILE A . n 
A 1 30  LYS 30  56  56  LYS LYS A . n 
A 1 31  VAL 31  57  57  VAL VAL A . n 
A 1 32  VAL 32  58  58  VAL VAL A . n 
A 1 33  TYR 33  59  59  TYR TYR A . n 
A 1 34  ASP 34  60  60  ASP ASP A . n 
A 1 35  VAL 35  61  61  VAL VAL A . n 
A 1 36  PHE 36  62  62  PHE PHE A . n 
A 1 37  ASP 37  63  63  ASP ASP A . n 
A 1 38  SER 38  64  64  SER SER A . n 
A 1 39  ASN 39  65  65  ASN ASN A . n 
A 1 40  GLU 40  66  66  GLU GLU A . n 
A 1 41  VAL 41  67  67  VAL VAL A . n 
A 1 42  LEU 42  68  68  LEU LEU A . n 
A 1 43  GLU 43  69  69  GLU GLU A . n 
A 1 44  GLY 44  70  70  GLY GLY A . n 
A 1 45  LYS 45  71  71  LYS LYS A . n 
A 1 46  LEU 46  72  72  LEU LEU A . n 
A 1 47  MET 47  73  73  MET MET A . n 
A 1 48  ALA 48  74  74  ALA ALA A . n 
A 1 49  GLY 49  75  75  GLY GLY A . n 
A 1 50  SER 50  76  76  SER SER A . n 
A 1 51  THR 51  77  77  THR THR A . n 
A 1 52  GLY 52  78  78  GLY GLY A . n 
A 1 53  PHE 53  79  79  PHE PHE A . n 
A 1 54  ASP 54  80  80  ASP ASP A . n 
A 1 55  LEU 55  81  81  LEU LEU A . n 
A 1 56  VAL 56  82  82  VAL VAL A . n 
A 1 57  VAL 57  83  83  VAL VAL A . n 
A 1 58  PRO 58  84  84  PRO PRO A . n 
A 1 59  SER 59  85  85  SER SER A . n 
A 1 60  ALA 60  86  86  ALA ALA A . n 
A 1 61  SER 61  87  87  SER SER A . n 
A 1 62  PHE 62  88  88  PHE PHE A . n 
A 1 63  LEU 63  89  89  LEU LEU A . n 
A 1 64  GLU 64  90  90  GLU GLU A . n 
A 1 65  ARG 65  91  91  ARG ARG A . n 
A 1 66  GLN 66  92  92  GLN GLN A . n 
A 1 67  LEU 67  93  93  LEU LEU A . n 
A 1 68  THR 68  94  94  THR THR A . n 
A 1 69  ALA 69  95  95  ALA ALA A . n 
A 1 70  GLY 70  96  96  GLY GLY A . n 
A 1 71  VAL 71  97  97  VAL VAL A . n 
A 1 72  PHE 72  98  98  PHE PHE A . n 
A 1 73  GLN 73  99  99  GLN GLN A . n 
A 1 74  PRO 74  100 100 PRO PRO A . n 
A 1 75  LEU 75  101 101 LEU LEU A . n 
A 1 76  ASP 76  102 102 ASP ASP A . n 
A 1 77  LYS 77  103 103 LYS LYS A . n 
A 1 78  SER 78  104 104 SER SER A . n 
A 1 79  LYS 79  105 105 LYS LYS A . n 
A 1 80  LEU 80  106 106 LEU LEU A . n 
A 1 81  PRO 81  107 107 PRO PRO A . n 
A 1 82  GLU 82  108 108 GLU GLU A . n 
A 1 83  TRP 83  109 109 TRP TRP A . n 
A 1 84  LYS 84  110 110 LYS LYS A . n 
A 1 85  ASN 85  111 111 ASN ASN A . n 
A 1 86  LEU 86  112 112 LEU LEU A . n 
A 1 87  ASP 87  113 113 ASP ASP A . n 
A 1 88  PRO 88  114 114 PRO PRO A . n 
A 1 89  GLU 89  115 115 GLU GLU A . n 
A 1 90  LEU 90  116 116 LEU LEU A . n 
A 1 91  LEU 91  117 117 LEU LEU A . n 
A 1 92  LYS 92  118 118 LYS LYS A . n 
A 1 93  LEU 93  119 119 LEU LEU A . n 
A 1 94  VAL 94  120 120 VAL VAL A . n 
A 1 95  ALA 95  121 121 ALA ALA A . n 
A 1 96  LYS 96  122 122 LYS LYS A . n 
A 1 97  HIS 97  123 123 HIS HIS A . n 
A 1 98  ASP 98  124 124 ASP ASP A . n 
A 1 99  PRO 99  125 125 PRO PRO A . n 
A 1 100 ASP 100 126 126 ASP ASP A . n 
A 1 101 ASN 101 127 127 ASN ASN A . n 
A 1 102 LYS 102 128 128 LYS LYS A . n 
A 1 103 PHE 103 129 129 PHE PHE A . n 
A 1 104 ALA 104 130 130 ALA ALA A . n 
A 1 105 MET 105 131 131 MET MET A . n 
A 1 106 PRO 106 132 132 PRO PRO A . n 
A 1 107 TYR 107 133 133 TYR TYR A . n 
A 1 108 MET 108 134 134 MET MET A . n 
A 1 109 TRP 109 135 135 TRP TRP A . n 
A 1 110 ALA 110 136 136 ALA ALA A . n 
A 1 111 THR 111 137 137 THR THR A . n 
A 1 112 THR 112 138 138 THR THR A . n 
A 1 113 GLY 113 139 139 GLY GLY A . n 
A 1 114 ILE 114 140 140 ILE ILE A . n 
A 1 115 GLY 115 141 141 GLY GLY A . n 
A 1 116 TYR 116 142 142 TYR TYR A . n 
A 1 117 ASN 117 143 143 ASN ASN A . n 
A 1 118 VAL 118 144 144 VAL VAL A . n 
A 1 119 ASP 119 145 145 ASP ASP A . n 
A 1 120 LYS 120 146 146 LYS LYS A . n 
A 1 121 VAL 121 147 147 VAL VAL A . n 
A 1 122 LYS 122 148 148 LYS LYS A . n 
A 1 123 ALA 123 149 149 ALA ALA A . n 
A 1 124 VAL 124 150 150 VAL VAL A . n 
A 1 125 LEU 125 151 151 LEU LEU A . n 
A 1 126 GLY 126 152 152 GLY GLY A . n 
A 1 127 GLU 127 153 153 GLU GLU A . n 
A 1 128 ASN 128 154 154 ASN ASN A . n 
A 1 129 ALA 129 155 155 ALA ALA A . n 
A 1 130 PRO 130 156 156 PRO PRO A . n 
A 1 131 VAL 131 157 157 VAL VAL A . n 
A 1 132 ASP 132 158 158 ASP ASP A . n 
A 1 133 SER 133 159 159 SER SER A . n 
A 1 134 TRP 134 160 160 TRP TRP A . n 
A 1 135 ASP 135 161 161 ASP ASP A . n 
A 1 136 LEU 136 162 162 LEU LEU A . n 
A 1 137 ILE 137 163 163 ILE ILE A . n 
A 1 138 LEU 138 164 164 LEU LEU A . n 
A 1 139 LYS 139 165 165 LYS LYS A . n 
A 1 140 PRO 140 166 166 PRO PRO A . n 
A 1 141 GLU 141 167 167 GLU GLU A . n 
A 1 142 ASN 142 168 168 ASN ASN A . n 
A 1 143 LEU 143 169 169 LEU LEU A . n 
A 1 144 GLU 144 170 170 GLU GLU A . n 
A 1 145 LYS 145 171 171 LYS LYS A . n 
A 1 146 LEU 146 172 172 LEU LEU A . n 
A 1 147 LYS 147 173 173 LYS LYS A . n 
A 1 148 SER 148 174 174 SER SER A . n 
A 1 149 CYS 149 175 175 CYS CYS A . n 
A 1 150 GLY 150 176 176 GLY GLY A . n 
A 1 151 VAL 151 177 177 VAL VAL A . n 
A 1 152 SER 152 178 178 SER SER A . n 
A 1 153 PHE 153 179 179 PHE PHE A . n 
A 1 154 LEU 154 180 180 LEU LEU A . n 
A 1 155 ASP 155 181 181 ASP ASP A . n 
A 1 156 ALA 156 182 182 ALA ALA A . n 
A 1 157 PRO 157 183 183 PRO PRO A . n 
A 1 158 GLU 158 184 184 GLU GLU A . n 
A 1 159 GLU 159 185 185 GLU GLU A . n 
A 1 160 VAL 160 186 186 VAL VAL A . n 
A 1 161 PHE 161 187 187 PHE PHE A . n 
A 1 162 ALA 162 188 188 ALA ALA A . n 
A 1 163 THR 163 189 189 THR THR A . n 
A 1 164 VAL 164 190 190 VAL VAL A . n 
A 1 165 LEU 165 191 191 LEU LEU A . n 
A 1 166 ASN 166 192 192 ASN ASN A . n 
A 1 167 TYR 167 193 193 TYR TYR A . n 
A 1 168 LEU 168 194 194 LEU LEU A . n 
A 1 169 GLY 169 195 195 GLY GLY A . n 
A 1 170 LYS 170 196 196 LYS LYS A . n 
A 1 171 ASP 171 197 197 ASP ASP A . n 
A 1 172 PRO 172 198 198 PRO PRO A . n 
A 1 173 ASN 173 199 199 ASN ASN A . n 
A 1 174 SER 174 200 200 SER SER A . n 
A 1 175 THR 175 201 201 THR THR A . n 
A 1 176 LYS 176 202 202 LYS LYS A . n 
A 1 177 ALA 177 203 203 ALA ALA A . n 
A 1 178 ASP 178 204 204 ASP ASP A . n 
A 1 179 ASP 179 205 205 ASP ASP A . n 
A 1 180 TYR 180 206 206 TYR TYR A . n 
A 1 181 THR 181 207 207 THR THR A . n 
A 1 182 GLY 182 208 208 GLY GLY A . n 
A 1 183 PRO 183 209 209 PRO PRO A . n 
A 1 184 ALA 184 210 210 ALA ALA A . n 
A 1 185 THR 185 211 211 THR THR A . n 
A 1 186 ASP 186 212 212 ASP ASP A . n 
A 1 187 LEU 187 213 213 LEU LEU A . n 
A 1 188 LEU 188 214 214 LEU LEU A . n 
A 1 189 LEU 189 215 215 LEU LEU A . n 
A 1 190 LYS 190 216 216 LYS LYS A . n 
A 1 191 LEU 191 217 217 LEU LEU A . n 
A 1 192 ARG 192 218 218 ARG ARG A . n 
A 1 193 PRO 193 219 219 PRO PRO A . n 
A 1 194 ASN 194 220 220 ASN ASN A . n 
A 1 195 ILE 195 221 221 ILE ILE A . n 
A 1 196 ARG 196 222 222 ARG ARG A . n 
A 1 197 TYR 197 223 223 TYR TYR A . n 
A 1 198 PHE 198 224 224 PHE PHE A . n 
A 1 199 HIS 199 225 225 HIS HIS A . n 
A 1 200 SER 200 226 226 SER SER A . n 
A 1 201 SER 201 227 227 SER SER A . n 
A 1 202 GLN 202 228 228 GLN GLN A . n 
A 1 203 TYR 203 229 229 TYR TYR A . n 
A 1 204 ILE 204 230 230 ILE ILE A . n 
A 1 205 ASN 205 231 231 ASN ASN A . n 
A 1 206 ASP 206 232 232 ASP ASP A . n 
A 1 207 LEU 207 233 233 LEU LEU A . n 
A 1 208 ALA 208 234 234 ALA ALA A . n 
A 1 209 ASN 209 235 235 ASN ASN A . n 
A 1 210 GLY 210 236 236 GLY GLY A . n 
A 1 211 ASP 211 237 237 ASP ASP A . n 
A 1 212 ILE 212 238 238 ILE ILE A . n 
A 1 213 CYS 213 239 239 CYS CYS A . n 
A 1 214 VAL 214 240 240 VAL VAL A . n 
A 1 215 ALA 215 241 241 ALA ALA A . n 
A 1 216 ILE 216 242 242 ILE ILE A . n 
A 1 217 GLY 217 243 243 GLY GLY A . n 
A 1 218 TRP 218 244 244 TRP TRP A . n 
A 1 219 ALA 219 245 245 ALA ALA A . n 
A 1 220 GLY 220 246 246 GLY GLY A . n 
A 1 221 ASP 221 247 247 ASP ASP A . n 
A 1 222 VAL 222 248 248 VAL VAL A . n 
A 1 223 TRP 223 249 249 TRP TRP A . n 
A 1 224 GLN 224 250 250 GLN GLN A . n 
A 1 225 ALA 225 251 251 ALA ALA A . n 
A 1 226 SER 226 252 252 SER SER A . n 
A 1 227 ASN 227 253 253 ASN ASN A . n 
A 1 228 ARG 228 254 254 ARG ARG A . n 
A 1 229 ALA 229 255 255 ALA ALA A . n 
A 1 230 LYS 230 256 256 LYS LYS A . n 
A 1 231 GLU 231 257 257 GLU GLU A . n 
A 1 232 ALA 232 258 258 ALA ALA A . n 
A 1 233 LYS 233 259 259 LYS LYS A . n 
A 1 234 ASN 234 260 260 ASN ASN A . n 
A 1 235 GLY 235 261 261 GLY GLY A . n 
A 1 236 VAL 236 262 262 VAL VAL A . n 
A 1 237 ASN 237 263 263 ASN ASN A . n 
A 1 238 VAL 238 264 264 VAL VAL A . n 
A 1 239 SER 239 265 265 SER SER A . n 
A 1 240 PHE 240 266 266 PHE PHE A . n 
A 1 241 SER 241 267 267 SER SER A . n 
A 1 242 ILE 242 268 268 ILE ILE A . n 
A 1 243 PRO 243 269 269 PRO PRO A . n 
A 1 244 LYS 244 270 270 LYS LYS A . n 
A 1 245 GLU 245 271 271 GLU GLU A . n 
A 1 246 GLY 246 272 272 GLY GLY A . n 
A 1 247 ALA 247 273 273 ALA ALA A . n 
A 1 248 MET 248 274 274 MET MET A . n 
A 1 249 ALA 249 275 275 ALA ALA A . n 
A 1 250 PHE 250 276 276 PHE PHE A . n 
A 1 251 PHE 251 277 277 PHE PHE A . n 
A 1 252 ASP 252 278 278 ASP ASP A . n 
A 1 253 VAL 253 279 279 VAL VAL A . n 
A 1 254 PHE 254 280 280 PHE PHE A . n 
A 1 255 ALA 255 281 281 ALA ALA A . n 
A 1 256 MET 256 282 282 MET MET A . n 
A 1 257 PRO 257 283 283 PRO PRO A . n 
A 1 258 ALA 258 284 284 ALA ALA A . n 
A 1 259 ASP 259 285 285 ASP ASP A . n 
A 1 260 ALA 260 286 286 ALA ALA A . n 
A 1 261 LYS 261 287 287 LYS LYS A . n 
A 1 262 ASN 262 288 288 ASN ASN A . n 
A 1 263 LYS 263 289 289 LYS LYS A . n 
A 1 264 ASP 264 290 290 ASP ASP A . n 
A 1 265 GLU 265 291 291 GLU GLU A . n 
A 1 266 ALA 266 292 292 ALA ALA A . n 
A 1 267 TYR 267 293 293 TYR TYR A . n 
A 1 268 GLN 268 294 294 GLN GLN A . n 
A 1 269 PHE 269 295 295 PHE PHE A . n 
A 1 270 LEU 270 296 296 LEU LEU A . n 
A 1 271 ASN 271 297 297 ASN ASN A . n 
A 1 272 TYR 272 298 298 TYR TYR A . n 
A 1 273 LEU 273 299 299 LEU LEU A . n 
A 1 274 LEU 274 300 300 LEU LEU A . n 
A 1 275 ARG 275 301 301 ARG ARG A . n 
A 1 276 PRO 276 302 302 PRO PRO A . n 
A 1 277 ASP 277 303 303 ASP ASP A . n 
A 1 278 VAL 278 304 304 VAL VAL A . n 
A 1 279 VAL 279 305 305 VAL VAL A . n 
A 1 280 ALA 280 306 306 ALA ALA A . n 
A 1 281 HIS 281 307 307 HIS HIS A . n 
A 1 282 ILE 282 308 308 ILE ILE A . n 
A 1 283 SER 283 309 309 SER SER A . n 
A 1 284 ASP 284 310 310 ASP ASP A . n 
A 1 285 HIS 285 311 311 HIS HIS A . n 
A 1 286 VAL 286 312 312 VAL VAL A . n 
A 1 287 PHE 287 313 313 PHE PHE A . n 
A 1 288 TYR 288 314 314 TYR TYR A . n 
A 1 289 ALA 289 315 315 ALA ALA A . n 
A 1 290 ASN 290 316 316 ASN ASN A . n 
A 1 291 ALA 291 317 317 ALA ALA A . n 
A 1 292 ASN 292 318 318 ASN ASN A . n 
A 1 293 LYS 293 319 319 LYS LYS A . n 
A 1 294 ALA 294 320 320 ALA ALA A . n 
A 1 295 ALA 295 321 321 ALA ALA A . n 
A 1 296 THR 296 322 322 THR THR A . n 
A 1 297 PRO 297 323 323 PRO PRO A . n 
A 1 298 LEU 298 324 324 LEU LEU A . n 
A 1 299 VAL 299 325 325 VAL VAL A . n 
A 1 300 SER 300 326 326 SER SER A . n 
A 1 301 ALA 301 327 327 ALA ALA A . n 
A 1 302 GLU 302 328 328 GLU GLU A . n 
A 1 303 VAL 303 329 329 VAL VAL A . n 
A 1 304 ARG 304 330 330 ARG ARG A . n 
A 1 305 GLU 305 331 331 GLU GLU A . n 
A 1 306 ASN 306 332 332 ASN ASN A . n 
A 1 307 PRO 307 333 333 PRO PRO A . n 
A 1 308 GLY 308 334 334 GLY GLY A . n 
A 1 309 ILE 309 335 335 ILE ILE A . n 
A 1 310 TYR 310 336 336 TYR TYR A . n 
A 1 311 PRO 311 337 337 PRO PRO A . n 
A 1 312 PRO 312 338 338 PRO PRO A . n 
A 1 313 ALA 313 339 339 ALA ALA A . n 
A 1 314 ASP 314 340 340 ASP ASP A . n 
A 1 315 VAL 315 341 341 VAL VAL A . n 
A 1 316 ARG 316 342 342 ARG ARG A . n 
A 1 317 ALA 317 343 343 ALA ALA A . n 
A 1 318 LYS 318 344 344 LYS LYS A . n 
A 1 319 LEU 319 345 345 LEU LEU A . n 
A 1 320 PHE 320 346 346 PHE PHE A . n 
A 1 321 THR 321 347 347 THR THR A . n 
A 1 322 LEU 322 348 348 LEU LEU A . n 
A 1 323 LYS 323 349 349 LYS LYS A . n 
A 1 324 VAL 324 350 350 VAL VAL A . n 
A 1 325 GLN 325 351 351 GLN GLN A . n 
A 1 326 ASP 326 352 352 ASP ASP A . n 
A 1 327 PRO 327 353 353 PRO PRO A . n 
A 1 328 LYS 328 354 354 LYS LYS A . n 
A 1 329 ILE 329 355 355 ILE ILE A . n 
A 1 330 ASP 330 356 356 ASP ASP A . n 
A 1 331 ARG 331 357 357 ARG ARG A . n 
A 1 332 VAL 332 358 358 VAL VAL A . n 
A 1 333 ARG 333 359 359 ARG ARG A . n 
A 1 334 THR 334 360 360 THR THR A . n 
A 1 335 ARG 335 361 361 ARG ARG A . n 
A 1 336 ALA 336 362 362 ALA ALA A . n 
A 1 337 TRP 337 363 363 TRP TRP A . n 
A 1 338 THR 338 364 364 THR THR A . n 
A 1 339 LYS 339 365 365 LYS LYS A . n 
A 1 340 VAL 340 366 366 VAL VAL A . n 
A 1 341 LYS 341 367 367 LYS LYS A . n 
A 1 342 SER 342 368 368 SER SER A . n 
A 1 343 GLY 343 369 369 GLY GLY A . n 
A 1 344 LYS 344 370 ?   ?   ?   A . n 
A 1 345 LEU 345 371 ?   ?   ?   A . n 
A 1 346 GLU 346 372 ?   ?   ?   A . n 
A 1 347 HIS 347 373 ?   ?   ?   A . n 
A 1 348 HIS 348 374 ?   ?   ?   A . n 
A 1 349 HIS 349 375 ?   ?   ?   A . n 
A 1 350 HIS 350 376 ?   ?   ?   A . n 
A 1 351 HIS 351 377 ?   ?   ?   A . n 
A 1 352 HIS 352 378 ?   ?   ?   A . n 
B 1 1   ALA 1   27  ?   ?   ?   B . n 
B 1 2   GLU 2   28  ?   ?   ?   B . n 
B 1 3   GLN 3   29  29  GLN GLN B . n 
B 1 4   LYS 4   30  30  LYS LYS B . n 
B 1 5   THR 5   31  31  THR THR B . n 
B 1 6   LEU 6   32  32  LEU LEU B . n 
B 1 7   HIS 7   33  33  HIS HIS B . n 
B 1 8   ILE 8   34  34  ILE ILE B . n 
B 1 9   TYR 9   35  35  TYR TYR B . n 
B 1 10  ASN 10  36  36  ASN ASN B . n 
B 1 11  TRP 11  37  37  TRP TRP B . n 
B 1 12  SER 12  38  38  SER SER B . n 
B 1 13  ASP 13  39  39  ASP ASP B . n 
B 1 14  TYR 14  40  40  TYR TYR B . n 
B 1 15  ILE 15  41  41  ILE ILE B . n 
B 1 16  ALA 16  42  42  ALA ALA B . n 
B 1 17  PRO 17  43  43  PRO PRO B . n 
B 1 18  ASP 18  44  44  ASP ASP B . n 
B 1 19  THR 19  45  45  THR THR B . n 
B 1 20  VAL 20  46  46  VAL VAL B . n 
B 1 21  ALA 21  47  47  ALA ALA B . n 
B 1 22  ASN 22  48  48  ASN ASN B . n 
B 1 23  PHE 23  49  49  PHE PHE B . n 
B 1 24  GLU 24  50  50  GLU GLU B . n 
B 1 25  LYS 25  51  51  LYS LYS B . n 
B 1 26  GLU 26  52  52  GLU GLU B . n 
B 1 27  THR 27  53  53  THR THR B . n 
B 1 28  GLY 28  54  54  GLY GLY B . n 
B 1 29  ILE 29  55  55  ILE ILE B . n 
B 1 30  LYS 30  56  56  LYS LYS B . n 
B 1 31  VAL 31  57  57  VAL VAL B . n 
B 1 32  VAL 32  58  58  VAL VAL B . n 
B 1 33  TYR 33  59  59  TYR TYR B . n 
B 1 34  ASP 34  60  60  ASP ASP B . n 
B 1 35  VAL 35  61  61  VAL VAL B . n 
B 1 36  PHE 36  62  62  PHE PHE B . n 
B 1 37  ASP 37  63  63  ASP ASP B . n 
B 1 38  SER 38  64  64  SER SER B . n 
B 1 39  ASN 39  65  65  ASN ASN B . n 
B 1 40  GLU 40  66  66  GLU GLU B . n 
B 1 41  VAL 41  67  67  VAL VAL B . n 
B 1 42  LEU 42  68  68  LEU LEU B . n 
B 1 43  GLU 43  69  69  GLU GLU B . n 
B 1 44  GLY 44  70  70  GLY GLY B . n 
B 1 45  LYS 45  71  71  LYS LYS B . n 
B 1 46  LEU 46  72  72  LEU LEU B . n 
B 1 47  MET 47  73  73  MET MET B . n 
B 1 48  ALA 48  74  74  ALA ALA B . n 
B 1 49  GLY 49  75  75  GLY GLY B . n 
B 1 50  SER 50  76  76  SER SER B . n 
B 1 51  THR 51  77  77  THR THR B . n 
B 1 52  GLY 52  78  78  GLY GLY B . n 
B 1 53  PHE 53  79  79  PHE PHE B . n 
B 1 54  ASP 54  80  80  ASP ASP B . n 
B 1 55  LEU 55  81  81  LEU LEU B . n 
B 1 56  VAL 56  82  82  VAL VAL B . n 
B 1 57  VAL 57  83  83  VAL VAL B . n 
B 1 58  PRO 58  84  84  PRO PRO B . n 
B 1 59  SER 59  85  85  SER SER B . n 
B 1 60  ALA 60  86  86  ALA ALA B . n 
B 1 61  SER 61  87  87  SER SER B . n 
B 1 62  PHE 62  88  88  PHE PHE B . n 
B 1 63  LEU 63  89  89  LEU LEU B . n 
B 1 64  GLU 64  90  90  GLU GLU B . n 
B 1 65  ARG 65  91  91  ARG ARG B . n 
B 1 66  GLN 66  92  92  GLN GLN B . n 
B 1 67  LEU 67  93  93  LEU LEU B . n 
B 1 68  THR 68  94  94  THR THR B . n 
B 1 69  ALA 69  95  95  ALA ALA B . n 
B 1 70  GLY 70  96  96  GLY GLY B . n 
B 1 71  VAL 71  97  97  VAL VAL B . n 
B 1 72  PHE 72  98  98  PHE PHE B . n 
B 1 73  GLN 73  99  99  GLN GLN B . n 
B 1 74  PRO 74  100 100 PRO PRO B . n 
B 1 75  LEU 75  101 101 LEU LEU B . n 
B 1 76  ASP 76  102 102 ASP ASP B . n 
B 1 77  LYS 77  103 103 LYS LYS B . n 
B 1 78  SER 78  104 104 SER SER B . n 
B 1 79  LYS 79  105 105 LYS LYS B . n 
B 1 80  LEU 80  106 106 LEU LEU B . n 
B 1 81  PRO 81  107 107 PRO PRO B . n 
B 1 82  GLU 82  108 108 GLU GLU B . n 
B 1 83  TRP 83  109 109 TRP TRP B . n 
B 1 84  LYS 84  110 110 LYS LYS B . n 
B 1 85  ASN 85  111 111 ASN ASN B . n 
B 1 86  LEU 86  112 112 LEU LEU B . n 
B 1 87  ASP 87  113 113 ASP ASP B . n 
B 1 88  PRO 88  114 114 PRO PRO B . n 
B 1 89  GLU 89  115 115 GLU GLU B . n 
B 1 90  LEU 90  116 116 LEU LEU B . n 
B 1 91  LEU 91  117 117 LEU LEU B . n 
B 1 92  LYS 92  118 118 LYS LYS B . n 
B 1 93  LEU 93  119 119 LEU LEU B . n 
B 1 94  VAL 94  120 120 VAL VAL B . n 
B 1 95  ALA 95  121 121 ALA ALA B . n 
B 1 96  LYS 96  122 122 LYS LYS B . n 
B 1 97  HIS 97  123 123 HIS HIS B . n 
B 1 98  ASP 98  124 124 ASP ASP B . n 
B 1 99  PRO 99  125 125 PRO PRO B . n 
B 1 100 ASP 100 126 126 ASP ASP B . n 
B 1 101 ASN 101 127 127 ASN ASN B . n 
B 1 102 LYS 102 128 128 LYS LYS B . n 
B 1 103 PHE 103 129 129 PHE PHE B . n 
B 1 104 ALA 104 130 130 ALA ALA B . n 
B 1 105 MET 105 131 131 MET MET B . n 
B 1 106 PRO 106 132 132 PRO PRO B . n 
B 1 107 TYR 107 133 133 TYR TYR B . n 
B 1 108 MET 108 134 134 MET MET B . n 
B 1 109 TRP 109 135 135 TRP TRP B . n 
B 1 110 ALA 110 136 136 ALA ALA B . n 
B 1 111 THR 111 137 137 THR THR B . n 
B 1 112 THR 112 138 138 THR THR B . n 
B 1 113 GLY 113 139 139 GLY GLY B . n 
B 1 114 ILE 114 140 140 ILE ILE B . n 
B 1 115 GLY 115 141 141 GLY GLY B . n 
B 1 116 TYR 116 142 142 TYR TYR B . n 
B 1 117 ASN 117 143 143 ASN ASN B . n 
B 1 118 VAL 118 144 144 VAL VAL B . n 
B 1 119 ASP 119 145 145 ASP ASP B . n 
B 1 120 LYS 120 146 146 LYS LYS B . n 
B 1 121 VAL 121 147 147 VAL VAL B . n 
B 1 122 LYS 122 148 148 LYS LYS B . n 
B 1 123 ALA 123 149 149 ALA ALA B . n 
B 1 124 VAL 124 150 150 VAL VAL B . n 
B 1 125 LEU 125 151 151 LEU LEU B . n 
B 1 126 GLY 126 152 152 GLY GLY B . n 
B 1 127 GLU 127 153 153 GLU GLU B . n 
B 1 128 ASN 128 154 154 ASN ASN B . n 
B 1 129 ALA 129 155 155 ALA ALA B . n 
B 1 130 PRO 130 156 156 PRO PRO B . n 
B 1 131 VAL 131 157 157 VAL VAL B . n 
B 1 132 ASP 132 158 158 ASP ASP B . n 
B 1 133 SER 133 159 159 SER SER B . n 
B 1 134 TRP 134 160 160 TRP TRP B . n 
B 1 135 ASP 135 161 161 ASP ASP B . n 
B 1 136 LEU 136 162 162 LEU LEU B . n 
B 1 137 ILE 137 163 163 ILE ILE B . n 
B 1 138 LEU 138 164 164 LEU LEU B . n 
B 1 139 LYS 139 165 165 LYS LYS B . n 
B 1 140 PRO 140 166 166 PRO PRO B . n 
B 1 141 GLU 141 167 167 GLU GLU B . n 
B 1 142 ASN 142 168 168 ASN ASN B . n 
B 1 143 LEU 143 169 169 LEU LEU B . n 
B 1 144 GLU 144 170 170 GLU GLU B . n 
B 1 145 LYS 145 171 171 LYS LYS B . n 
B 1 146 LEU 146 172 172 LEU LEU B . n 
B 1 147 LYS 147 173 173 LYS LYS B . n 
B 1 148 SER 148 174 174 SER SER B . n 
B 1 149 CYS 149 175 175 CYS CYS B . n 
B 1 150 GLY 150 176 176 GLY GLY B . n 
B 1 151 VAL 151 177 177 VAL VAL B . n 
B 1 152 SER 152 178 178 SER SER B . n 
B 1 153 PHE 153 179 179 PHE PHE B . n 
B 1 154 LEU 154 180 180 LEU LEU B . n 
B 1 155 ASP 155 181 181 ASP ASP B . n 
B 1 156 ALA 156 182 182 ALA ALA B . n 
B 1 157 PRO 157 183 183 PRO PRO B . n 
B 1 158 GLU 158 184 184 GLU GLU B . n 
B 1 159 GLU 159 185 185 GLU GLU B . n 
B 1 160 VAL 160 186 186 VAL VAL B . n 
B 1 161 PHE 161 187 187 PHE PHE B . n 
B 1 162 ALA 162 188 188 ALA ALA B . n 
B 1 163 THR 163 189 189 THR THR B . n 
B 1 164 VAL 164 190 190 VAL VAL B . n 
B 1 165 LEU 165 191 191 LEU LEU B . n 
B 1 166 ASN 166 192 192 ASN ASN B . n 
B 1 167 TYR 167 193 193 TYR TYR B . n 
B 1 168 LEU 168 194 194 LEU LEU B . n 
B 1 169 GLY 169 195 195 GLY GLY B . n 
B 1 170 LYS 170 196 196 LYS LYS B . n 
B 1 171 ASP 171 197 197 ASP ASP B . n 
B 1 172 PRO 172 198 198 PRO PRO B . n 
B 1 173 ASN 173 199 199 ASN ASN B . n 
B 1 174 SER 174 200 200 SER SER B . n 
B 1 175 THR 175 201 201 THR THR B . n 
B 1 176 LYS 176 202 202 LYS LYS B . n 
B 1 177 ALA 177 203 203 ALA ALA B . n 
B 1 178 ASP 178 204 204 ASP ASP B . n 
B 1 179 ASP 179 205 205 ASP ASP B . n 
B 1 180 TYR 180 206 206 TYR TYR B . n 
B 1 181 THR 181 207 207 THR THR B . n 
B 1 182 GLY 182 208 208 GLY GLY B . n 
B 1 183 PRO 183 209 209 PRO PRO B . n 
B 1 184 ALA 184 210 210 ALA ALA B . n 
B 1 185 THR 185 211 211 THR THR B . n 
B 1 186 ASP 186 212 212 ASP ASP B . n 
B 1 187 LEU 187 213 213 LEU LEU B . n 
B 1 188 LEU 188 214 214 LEU LEU B . n 
B 1 189 LEU 189 215 215 LEU LEU B . n 
B 1 190 LYS 190 216 216 LYS LYS B . n 
B 1 191 LEU 191 217 217 LEU LEU B . n 
B 1 192 ARG 192 218 218 ARG ARG B . n 
B 1 193 PRO 193 219 219 PRO PRO B . n 
B 1 194 ASN 194 220 220 ASN ASN B . n 
B 1 195 ILE 195 221 221 ILE ILE B . n 
B 1 196 ARG 196 222 222 ARG ARG B . n 
B 1 197 TYR 197 223 223 TYR TYR B . n 
B 1 198 PHE 198 224 224 PHE PHE B . n 
B 1 199 HIS 199 225 225 HIS HIS B . n 
B 1 200 SER 200 226 226 SER SER B . n 
B 1 201 SER 201 227 227 SER SER B . n 
B 1 202 GLN 202 228 228 GLN GLN B . n 
B 1 203 TYR 203 229 229 TYR TYR B . n 
B 1 204 ILE 204 230 230 ILE ILE B . n 
B 1 205 ASN 205 231 231 ASN ASN B . n 
B 1 206 ASP 206 232 232 ASP ASP B . n 
B 1 207 LEU 207 233 233 LEU LEU B . n 
B 1 208 ALA 208 234 234 ALA ALA B . n 
B 1 209 ASN 209 235 235 ASN ASN B . n 
B 1 210 GLY 210 236 236 GLY GLY B . n 
B 1 211 ASP 211 237 237 ASP ASP B . n 
B 1 212 ILE 212 238 238 ILE ILE B . n 
B 1 213 CYS 213 239 239 CYS CYS B . n 
B 1 214 VAL 214 240 240 VAL VAL B . n 
B 1 215 ALA 215 241 241 ALA ALA B . n 
B 1 216 ILE 216 242 242 ILE ILE B . n 
B 1 217 GLY 217 243 243 GLY GLY B . n 
B 1 218 TRP 218 244 244 TRP TRP B . n 
B 1 219 ALA 219 245 245 ALA ALA B . n 
B 1 220 GLY 220 246 246 GLY GLY B . n 
B 1 221 ASP 221 247 247 ASP ASP B . n 
B 1 222 VAL 222 248 248 VAL VAL B . n 
B 1 223 TRP 223 249 249 TRP TRP B . n 
B 1 224 GLN 224 250 250 GLN GLN B . n 
B 1 225 ALA 225 251 251 ALA ALA B . n 
B 1 226 SER 226 252 252 SER SER B . n 
B 1 227 ASN 227 253 253 ASN ASN B . n 
B 1 228 ARG 228 254 254 ARG ARG B . n 
B 1 229 ALA 229 255 255 ALA ALA B . n 
B 1 230 LYS 230 256 256 LYS LYS B . n 
B 1 231 GLU 231 257 257 GLU GLU B . n 
B 1 232 ALA 232 258 258 ALA ALA B . n 
B 1 233 LYS 233 259 259 LYS LYS B . n 
B 1 234 ASN 234 260 260 ASN ASN B . n 
B 1 235 GLY 235 261 261 GLY GLY B . n 
B 1 236 VAL 236 262 262 VAL VAL B . n 
B 1 237 ASN 237 263 263 ASN ASN B . n 
B 1 238 VAL 238 264 264 VAL VAL B . n 
B 1 239 SER 239 265 265 SER SER B . n 
B 1 240 PHE 240 266 266 PHE PHE B . n 
B 1 241 SER 241 267 267 SER SER B . n 
B 1 242 ILE 242 268 268 ILE ILE B . n 
B 1 243 PRO 243 269 269 PRO PRO B . n 
B 1 244 LYS 244 270 270 LYS LYS B . n 
B 1 245 GLU 245 271 271 GLU GLU B . n 
B 1 246 GLY 246 272 272 GLY GLY B . n 
B 1 247 ALA 247 273 273 ALA ALA B . n 
B 1 248 MET 248 274 274 MET MET B . n 
B 1 249 ALA 249 275 275 ALA ALA B . n 
B 1 250 PHE 250 276 276 PHE PHE B . n 
B 1 251 PHE 251 277 277 PHE PHE B . n 
B 1 252 ASP 252 278 278 ASP ASP B . n 
B 1 253 VAL 253 279 279 VAL VAL B . n 
B 1 254 PHE 254 280 280 PHE PHE B . n 
B 1 255 ALA 255 281 281 ALA ALA B . n 
B 1 256 MET 256 282 282 MET MET B . n 
B 1 257 PRO 257 283 283 PRO PRO B . n 
B 1 258 ALA 258 284 284 ALA ALA B . n 
B 1 259 ASP 259 285 285 ASP ASP B . n 
B 1 260 ALA 260 286 286 ALA ALA B . n 
B 1 261 LYS 261 287 287 LYS LYS B . n 
B 1 262 ASN 262 288 288 ASN ASN B . n 
B 1 263 LYS 263 289 289 LYS LYS B . n 
B 1 264 ASP 264 290 290 ASP ASP B . n 
B 1 265 GLU 265 291 291 GLU GLU B . n 
B 1 266 ALA 266 292 292 ALA ALA B . n 
B 1 267 TYR 267 293 293 TYR TYR B . n 
B 1 268 GLN 268 294 294 GLN GLN B . n 
B 1 269 PHE 269 295 295 PHE PHE B . n 
B 1 270 LEU 270 296 296 LEU LEU B . n 
B 1 271 ASN 271 297 297 ASN ASN B . n 
B 1 272 TYR 272 298 298 TYR TYR B . n 
B 1 273 LEU 273 299 299 LEU LEU B . n 
B 1 274 LEU 274 300 300 LEU LEU B . n 
B 1 275 ARG 275 301 301 ARG ARG B . n 
B 1 276 PRO 276 302 302 PRO PRO B . n 
B 1 277 ASP 277 303 303 ASP ASP B . n 
B 1 278 VAL 278 304 304 VAL VAL B . n 
B 1 279 VAL 279 305 305 VAL VAL B . n 
B 1 280 ALA 280 306 306 ALA ALA B . n 
B 1 281 HIS 281 307 307 HIS HIS B . n 
B 1 282 ILE 282 308 308 ILE ILE B . n 
B 1 283 SER 283 309 309 SER SER B . n 
B 1 284 ASP 284 310 310 ASP ASP B . n 
B 1 285 HIS 285 311 311 HIS HIS B . n 
B 1 286 VAL 286 312 312 VAL VAL B . n 
B 1 287 PHE 287 313 313 PHE PHE B . n 
B 1 288 TYR 288 314 314 TYR TYR B . n 
B 1 289 ALA 289 315 315 ALA ALA B . n 
B 1 290 ASN 290 316 316 ASN ASN B . n 
B 1 291 ALA 291 317 317 ALA ALA B . n 
B 1 292 ASN 292 318 318 ASN ASN B . n 
B 1 293 LYS 293 319 319 LYS LYS B . n 
B 1 294 ALA 294 320 320 ALA ALA B . n 
B 1 295 ALA 295 321 321 ALA ALA B . n 
B 1 296 THR 296 322 322 THR THR B . n 
B 1 297 PRO 297 323 323 PRO PRO B . n 
B 1 298 LEU 298 324 324 LEU LEU B . n 
B 1 299 VAL 299 325 325 VAL VAL B . n 
B 1 300 SER 300 326 326 SER SER B . n 
B 1 301 ALA 301 327 327 ALA ALA B . n 
B 1 302 GLU 302 328 328 GLU GLU B . n 
B 1 303 VAL 303 329 329 VAL VAL B . n 
B 1 304 ARG 304 330 330 ARG ARG B . n 
B 1 305 GLU 305 331 331 GLU GLU B . n 
B 1 306 ASN 306 332 332 ASN ASN B . n 
B 1 307 PRO 307 333 333 PRO PRO B . n 
B 1 308 GLY 308 334 334 GLY GLY B . n 
B 1 309 ILE 309 335 335 ILE ILE B . n 
B 1 310 TYR 310 336 336 TYR TYR B . n 
B 1 311 PRO 311 337 337 PRO PRO B . n 
B 1 312 PRO 312 338 338 PRO PRO B . n 
B 1 313 ALA 313 339 339 ALA ALA B . n 
B 1 314 ASP 314 340 340 ASP ASP B . n 
B 1 315 VAL 315 341 341 VAL VAL B . n 
B 1 316 ARG 316 342 342 ARG ARG B . n 
B 1 317 ALA 317 343 343 ALA ALA B . n 
B 1 318 LYS 318 344 344 LYS LYS B . n 
B 1 319 LEU 319 345 345 LEU LEU B . n 
B 1 320 PHE 320 346 346 PHE PHE B . n 
B 1 321 THR 321 347 347 THR THR B . n 
B 1 322 LEU 322 348 348 LEU LEU B . n 
B 1 323 LYS 323 349 349 LYS LYS B . n 
B 1 324 VAL 324 350 350 VAL VAL B . n 
B 1 325 GLN 325 351 351 GLN GLN B . n 
B 1 326 ASP 326 352 352 ASP ASP B . n 
B 1 327 PRO 327 353 353 PRO PRO B . n 
B 1 328 LYS 328 354 354 LYS LYS B . n 
B 1 329 ILE 329 355 355 ILE ILE B . n 
B 1 330 ASP 330 356 356 ASP ASP B . n 
B 1 331 ARG 331 357 357 ARG ARG B . n 
B 1 332 VAL 332 358 358 VAL VAL B . n 
B 1 333 ARG 333 359 359 ARG ARG B . n 
B 1 334 THR 334 360 360 THR THR B . n 
B 1 335 ARG 335 361 361 ARG ARG B . n 
B 1 336 ALA 336 362 362 ALA ALA B . n 
B 1 337 TRP 337 363 363 TRP TRP B . n 
B 1 338 THR 338 364 364 THR THR B . n 
B 1 339 LYS 339 365 365 LYS LYS B . n 
B 1 340 VAL 340 366 366 VAL VAL B . n 
B 1 341 LYS 341 367 367 LYS LYS B . n 
B 1 342 SER 342 368 368 SER SER B . n 
B 1 343 GLY 343 369 369 GLY GLY B . n 
B 1 344 LYS 344 370 ?   ?   ?   B . n 
B 1 345 LEU 345 371 ?   ?   ?   B . n 
B 1 346 GLU 346 372 ?   ?   ?   B . n 
B 1 347 HIS 347 373 ?   ?   ?   B . n 
B 1 348 HIS 348 374 ?   ?   ?   B . n 
B 1 349 HIS 349 375 ?   ?   ?   B . n 
B 1 350 HIS 350 376 ?   ?   ?   B . n 
B 1 351 HIS 351 377 ?   ?   ?   B . n 
B 1 352 HIS 352 378 ?   ?   ?   B . 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 
C  2 PGE 1   401 401 PGE PGE A . 
D  3 PEG 1   402 501 PEG PEG A . 
E  3 PEG 1   403 601 PEG PEG A . 
F  4 EDO 1   404 2   EDO EDO A . 
G  4 EDO 1   405 5   EDO EDO A . 
H  4 EDO 1   406 6   EDO EDO A . 
I  4 EDO 1   407 7   EDO EDO A . 
J  4 EDO 1   408 8   EDO EDO A . 
K  4 EDO 1   409 9   EDO EDO A . 
L  4 EDO 1   410 10  EDO EDO A . 
M  4 EDO 1   411 11  EDO EDO A . 
N  4 EDO 1   412 12  EDO EDO A . 
O  4 EDO 1   413 17  EDO EDO A . 
P  4 EDO 1   414 18  EDO EDO A . 
Q  5 CL  1   415 1   CL  CL  A . 
R  5 CL  1   416 3   CL  CL  A . 
S  3 PEG 1   401 401 PEG PEG B . 
T  3 PEG 1   402 501 PEG PEG B . 
U  3 PEG 1   403 601 PEG PEG B . 
V  3 PEG 1   404 701 PEG PEG B . 
W  4 EDO 1   405 4   EDO EDO B . 
X  4 EDO 1   406 14  EDO EDO B . 
Y  4 EDO 1   407 15  EDO EDO B . 
Z  4 EDO 1   408 16  EDO EDO B . 
AA 5 CL  1   409 2   CL  CL  B . 
BA 6 HOH 1   501 5   HOH HOH A . 
BA 6 HOH 2   502 104 HOH HOH A . 
BA 6 HOH 3   503 116 HOH HOH A . 
BA 6 HOH 4   504 201 HOH HOH A . 
BA 6 HOH 5   505 40  HOH HOH A . 
BA 6 HOH 6   506 295 HOH HOH A . 
BA 6 HOH 7   507 294 HOH HOH A . 
BA 6 HOH 8   508 37  HOH HOH A . 
BA 6 HOH 9   509 30  HOH HOH A . 
BA 6 HOH 10  510 69  HOH HOH A . 
BA 6 HOH 11  511 53  HOH HOH A . 
BA 6 HOH 12  512 39  HOH HOH A . 
BA 6 HOH 13  513 132 HOH HOH A . 
BA 6 HOH 14  514 237 HOH HOH A . 
BA 6 HOH 15  515 58  HOH HOH A . 
BA 6 HOH 16  516 44  HOH HOH A . 
BA 6 HOH 17  517 225 HOH HOH A . 
BA 6 HOH 18  518 50  HOH HOH A . 
BA 6 HOH 19  519 167 HOH HOH A . 
BA 6 HOH 20  520 8   HOH HOH A . 
BA 6 HOH 21  521 36  HOH HOH A . 
BA 6 HOH 22  522 61  HOH HOH A . 
BA 6 HOH 23  523 26  HOH HOH A . 
BA 6 HOH 24  524 79  HOH HOH A . 
BA 6 HOH 25  525 151 HOH HOH A . 
BA 6 HOH 26  526 32  HOH HOH A . 
BA 6 HOH 27  527 67  HOH HOH A . 
BA 6 HOH 28  528 1   HOH HOH A . 
BA 6 HOH 29  529 152 HOH HOH A . 
BA 6 HOH 30  530 115 HOH HOH A . 
BA 6 HOH 31  531 29  HOH HOH A . 
BA 6 HOH 32  532 11  HOH HOH A . 
BA 6 HOH 33  533 22  HOH HOH A . 
BA 6 HOH 34  534 17  HOH HOH A . 
BA 6 HOH 35  535 56  HOH HOH A . 
BA 6 HOH 36  536 227 HOH HOH A . 
BA 6 HOH 37  537 93  HOH HOH A . 
BA 6 HOH 38  538 109 HOH HOH A . 
BA 6 HOH 39  539 297 HOH HOH A . 
BA 6 HOH 40  540 88  HOH HOH A . 
BA 6 HOH 41  541 47  HOH HOH A . 
BA 6 HOH 42  542 233 HOH HOH A . 
BA 6 HOH 43  543 289 HOH HOH A . 
BA 6 HOH 44  544 16  HOH HOH A . 
BA 6 HOH 45  545 46  HOH HOH A . 
BA 6 HOH 46  546 82  HOH HOH A . 
BA 6 HOH 47  547 120 HOH HOH A . 
BA 6 HOH 48  548 9   HOH HOH A . 
BA 6 HOH 49  549 282 HOH HOH A . 
BA 6 HOH 50  550 84  HOH HOH A . 
BA 6 HOH 51  551 2   HOH HOH A . 
BA 6 HOH 52  552 154 HOH HOH A . 
BA 6 HOH 53  553 99  HOH HOH A . 
BA 6 HOH 54  554 235 HOH HOH A . 
BA 6 HOH 55  555 70  HOH HOH A . 
BA 6 HOH 56  556 102 HOH HOH A . 
BA 6 HOH 57  557 146 HOH HOH A . 
BA 6 HOH 58  558 125 HOH HOH A . 
BA 6 HOH 59  559 187 HOH HOH A . 
BA 6 HOH 60  560 85  HOH HOH A . 
BA 6 HOH 61  561 106 HOH HOH A . 
BA 6 HOH 62  562 96  HOH HOH A . 
BA 6 HOH 63  563 213 HOH HOH A . 
BA 6 HOH 64  564 189 HOH HOH A . 
BA 6 HOH 65  565 251 HOH HOH A . 
BA 6 HOH 66  566 90  HOH HOH A . 
BA 6 HOH 67  567 6   HOH HOH A . 
BA 6 HOH 68  568 18  HOH HOH A . 
BA 6 HOH 69  569 7   HOH HOH A . 
BA 6 HOH 70  570 80  HOH HOH A . 
BA 6 HOH 71  571 73  HOH HOH A . 
BA 6 HOH 72  572 55  HOH HOH A . 
BA 6 HOH 73  573 65  HOH HOH A . 
BA 6 HOH 74  574 173 HOH HOH A . 
BA 6 HOH 75  575 107 HOH HOH A . 
BA 6 HOH 76  576 14  HOH HOH A . 
BA 6 HOH 77  577 49  HOH HOH A . 
BA 6 HOH 78  578 299 HOH HOH A . 
BA 6 HOH 79  579 230 HOH HOH A . 
BA 6 HOH 80  580 34  HOH HOH A . 
BA 6 HOH 81  581 212 HOH HOH A . 
BA 6 HOH 82  582 110 HOH HOH A . 
BA 6 HOH 83  583 250 HOH HOH A . 
BA 6 HOH 84  584 286 HOH HOH A . 
BA 6 HOH 85  585 75  HOH HOH A . 
BA 6 HOH 86  586 276 HOH HOH A . 
BA 6 HOH 87  587 89  HOH HOH A . 
BA 6 HOH 88  588 293 HOH HOH A . 
BA 6 HOH 89  589 20  HOH HOH A . 
BA 6 HOH 90  590 307 HOH HOH A . 
BA 6 HOH 91  591 35  HOH HOH A . 
BA 6 HOH 92  592 136 HOH HOH A . 
BA 6 HOH 93  593 122 HOH HOH A . 
BA 6 HOH 94  594 210 HOH HOH A . 
BA 6 HOH 95  595 160 HOH HOH A . 
BA 6 HOH 96  596 68  HOH HOH A . 
BA 6 HOH 97  597 25  HOH HOH A . 
BA 6 HOH 98  598 140 HOH HOH A . 
BA 6 HOH 99  599 142 HOH HOH A . 
BA 6 HOH 100 600 139 HOH HOH A . 
BA 6 HOH 101 601 242 HOH HOH A . 
BA 6 HOH 102 602 182 HOH HOH A . 
BA 6 HOH 103 603 138 HOH HOH A . 
BA 6 HOH 104 604 224 HOH HOH A . 
BA 6 HOH 105 605 196 HOH HOH A . 
BA 6 HOH 106 606 105 HOH HOH A . 
BA 6 HOH 107 607 48  HOH HOH A . 
BA 6 HOH 108 608 97  HOH HOH A . 
BA 6 HOH 109 609 74  HOH HOH A . 
BA 6 HOH 110 610 31  HOH HOH A . 
BA 6 HOH 111 611 62  HOH HOH A . 
BA 6 HOH 112 612 129 HOH HOH A . 
BA 6 HOH 113 613 240 HOH HOH A . 
BA 6 HOH 114 614 54  HOH HOH A . 
BA 6 HOH 115 615 91  HOH HOH A . 
BA 6 HOH 116 616 169 HOH HOH A . 
BA 6 HOH 117 617 303 HOH HOH A . 
BA 6 HOH 118 618 133 HOH HOH A . 
BA 6 HOH 119 619 81  HOH HOH A . 
BA 6 HOH 120 620 215 HOH HOH A . 
BA 6 HOH 121 621 197 HOH HOH A . 
BA 6 HOH 122 622 241 HOH HOH A . 
BA 6 HOH 123 623 127 HOH HOH A . 
BA 6 HOH 124 624 113 HOH HOH A . 
BA 6 HOH 125 625 72  HOH HOH A . 
BA 6 HOH 126 626 108 HOH HOH A . 
BA 6 HOH 127 627 76  HOH HOH A . 
BA 6 HOH 128 628 200 HOH HOH A . 
BA 6 HOH 129 629 94  HOH HOH A . 
BA 6 HOH 130 630 21  HOH HOH A . 
BA 6 HOH 131 631 203 HOH HOH A . 
BA 6 HOH 132 632 153 HOH HOH A . 
BA 6 HOH 133 633 43  HOH HOH A . 
BA 6 HOH 134 634 27  HOH HOH A . 
BA 6 HOH 135 635 288 HOH HOH A . 
BA 6 HOH 136 636 157 HOH HOH A . 
BA 6 HOH 137 637 290 HOH HOH A . 
BA 6 HOH 138 638 149 HOH HOH A . 
BA 6 HOH 139 639 101 HOH HOH A . 
BA 6 HOH 140 640 59  HOH HOH A . 
BA 6 HOH 141 641 83  HOH HOH A . 
BA 6 HOH 142 642 159 HOH HOH A . 
BA 6 HOH 143 643 144 HOH HOH A . 
BA 6 HOH 144 644 117 HOH HOH A . 
BA 6 HOH 145 645 23  HOH HOH A . 
BA 6 HOH 146 646 232 HOH HOH A . 
BA 6 HOH 147 647 285 HOH HOH A . 
BA 6 HOH 148 648 186 HOH HOH A . 
BA 6 HOH 149 649 190 HOH HOH A . 
BA 6 HOH 150 650 4   HOH HOH A . 
BA 6 HOH 151 651 283 HOH HOH A . 
BA 6 HOH 152 652 228 HOH HOH A . 
BA 6 HOH 153 653 100 HOH HOH A . 
BA 6 HOH 154 654 175 HOH HOH A . 
BA 6 HOH 155 655 86  HOH HOH A . 
BA 6 HOH 156 656 236 HOH HOH A . 
BA 6 HOH 157 657 128 HOH HOH A . 
BA 6 HOH 158 658 145 HOH HOH A . 
BA 6 HOH 159 659 279 HOH HOH A . 
BA 6 HOH 160 660 226 HOH HOH A . 
BA 6 HOH 161 661 150 HOH HOH A . 
BA 6 HOH 162 662 300 HOH HOH A . 
BA 6 HOH 163 663 148 HOH HOH A . 
BA 6 HOH 164 664 238 HOH HOH A . 
BA 6 HOH 165 665 239 HOH HOH A . 
BA 6 HOH 166 666 193 HOH HOH A . 
BA 6 HOH 167 667 214 HOH HOH A . 
BA 6 HOH 168 668 221 HOH HOH A . 
BA 6 HOH 169 669 220 HOH HOH A . 
BA 6 HOH 170 670 302 HOH HOH A . 
BA 6 HOH 171 671 222 HOH HOH A . 
BA 6 HOH 172 672 301 HOH HOH A . 
BA 6 HOH 173 673 121 HOH HOH A . 
BA 6 HOH 174 674 216 HOH HOH A . 
BA 6 HOH 175 675 229 HOH HOH A . 
BA 6 HOH 176 676 280 HOH HOH A . 
BA 6 HOH 177 677 199 HOH HOH A . 
BA 6 HOH 178 678 217 HOH HOH A . 
BA 6 HOH 179 679 243 HOH HOH A . 
BA 6 HOH 180 680 234 HOH HOH A . 
BA 6 HOH 181 681 168 HOH HOH A . 
BA 6 HOH 182 682 219 HOH HOH A . 
BA 6 HOH 183 683 192 HOH HOH A . 
BA 6 HOH 184 684 298 HOH HOH A . 
BA 6 HOH 185 685 284 HOH HOH A . 
BA 6 HOH 186 686 188 HOH HOH A . 
BA 6 HOH 187 687 218 HOH HOH A . 
BA 6 HOH 188 688 211 HOH HOH A . 
BA 6 HOH 189 689 131 HOH HOH A . 
BA 6 HOH 190 690 244 HOH HOH A . 
BA 6 HOH 191 691 223 HOH HOH A . 
BA 6 HOH 192 692 247 HOH HOH A . 
BA 6 HOH 193 693 246 HOH HOH A . 
BA 6 HOH 194 694 231 HOH HOH A . 
BA 6 HOH 195 695 207 HOH HOH A . 
BA 6 HOH 196 696 281 HOH HOH A . 
BA 6 HOH 197 697 52  HOH HOH A . 
BA 6 HOH 198 698 208 HOH HOH A . 
BA 6 HOH 199 699 198 HOH HOH A . 
CA 6 HOH 1   501 255 HOH HOH B . 
CA 6 HOH 2   502 274 HOH HOH B . 
CA 6 HOH 3   503 111 HOH HOH B . 
CA 6 HOH 4   504 19  HOH HOH B . 
CA 6 HOH 5   505 265 HOH HOH B . 
CA 6 HOH 6   506 179 HOH HOH B . 
CA 6 HOH 7   507 15  HOH HOH B . 
CA 6 HOH 8   508 260 HOH HOH B . 
CA 6 HOH 9   509 209 HOH HOH B . 
CA 6 HOH 10  510 92  HOH HOH B . 
CA 6 HOH 11  511 33  HOH HOH B . 
CA 6 HOH 12  512 264 HOH HOH B . 
CA 6 HOH 13  513 143 HOH HOH B . 
CA 6 HOH 14  514 278 HOH HOH B . 
CA 6 HOH 15  515 262 HOH HOH B . 
CA 6 HOH 16  516 12  HOH HOH B . 
CA 6 HOH 17  517 45  HOH HOH B . 
CA 6 HOH 18  518 248 HOH HOH B . 
CA 6 HOH 19  519 249 HOH HOH B . 
CA 6 HOH 20  520 64  HOH HOH B . 
CA 6 HOH 21  521 42  HOH HOH B . 
CA 6 HOH 22  522 287 HOH HOH B . 
CA 6 HOH 23  523 87  HOH HOH B . 
CA 6 HOH 24  524 114 HOH HOH B . 
CA 6 HOH 25  525 165 HOH HOH B . 
CA 6 HOH 26  526 306 HOH HOH B . 
CA 6 HOH 27  527 134 HOH HOH B . 
CA 6 HOH 28  528 51  HOH HOH B . 
CA 6 HOH 29  529 141 HOH HOH B . 
CA 6 HOH 30  530 71  HOH HOH B . 
CA 6 HOH 31  531 95  HOH HOH B . 
CA 6 HOH 32  532 126 HOH HOH B . 
CA 6 HOH 33  533 183 HOH HOH B . 
CA 6 HOH 34  534 162 HOH HOH B . 
CA 6 HOH 35  535 13  HOH HOH B . 
CA 6 HOH 36  536 3   HOH HOH B . 
CA 6 HOH 37  537 305 HOH HOH B . 
CA 6 HOH 38  538 161 HOH HOH B . 
CA 6 HOH 39  539 147 HOH HOH B . 
CA 6 HOH 40  540 202 HOH HOH B . 
CA 6 HOH 41  541 119 HOH HOH B . 
CA 6 HOH 42  542 135 HOH HOH B . 
CA 6 HOH 43  543 291 HOH HOH B . 
CA 6 HOH 44  544 57  HOH HOH B . 
CA 6 HOH 45  545 263 HOH HOH B . 
CA 6 HOH 46  546 63  HOH HOH B . 
CA 6 HOH 47  547 98  HOH HOH B . 
CA 6 HOH 48  548 66  HOH HOH B . 
CA 6 HOH 49  549 24  HOH HOH B . 
CA 6 HOH 50  550 267 HOH HOH B . 
CA 6 HOH 51  551 28  HOH HOH B . 
CA 6 HOH 52  552 254 HOH HOH B . 
CA 6 HOH 53  553 60  HOH HOH B . 
CA 6 HOH 54  554 112 HOH HOH B . 
CA 6 HOH 55  555 256 HOH HOH B . 
CA 6 HOH 56  556 166 HOH HOH B . 
CA 6 HOH 57  557 170 HOH HOH B . 
CA 6 HOH 58  558 261 HOH HOH B . 
CA 6 HOH 59  559 77  HOH HOH B . 
CA 6 HOH 60  560 270 HOH HOH B . 
CA 6 HOH 61  561 10  HOH HOH B . 
CA 6 HOH 62  562 296 HOH HOH B . 
CA 6 HOH 63  563 171 HOH HOH B . 
CA 6 HOH 64  564 275 HOH HOH B . 
CA 6 HOH 65  565 130 HOH HOH B . 
CA 6 HOH 66  566 257 HOH HOH B . 
CA 6 HOH 67  567 176 HOH HOH B . 
CA 6 HOH 68  568 118 HOH HOH B . 
CA 6 HOH 69  569 78  HOH HOH B . 
CA 6 HOH 70  570 123 HOH HOH B . 
CA 6 HOH 71  571 158 HOH HOH B . 
CA 6 HOH 72  572 269 HOH HOH B . 
CA 6 HOH 73  573 195 HOH HOH B . 
CA 6 HOH 74  574 259 HOH HOH B . 
CA 6 HOH 75  575 185 HOH HOH B . 
CA 6 HOH 76  576 253 HOH HOH B . 
CA 6 HOH 77  577 178 HOH HOH B . 
CA 6 HOH 78  578 177 HOH HOH B . 
CA 6 HOH 79  579 156 HOH HOH B . 
CA 6 HOH 80  580 292 HOH HOH B . 
CA 6 HOH 81  581 268 HOH HOH B . 
CA 6 HOH 82  582 273 HOH HOH B . 
CA 6 HOH 83  583 103 HOH HOH B . 
CA 6 HOH 84  584 304 HOH HOH B . 
CA 6 HOH 85  585 163 HOH HOH B . 
CA 6 HOH 86  586 266 HOH HOH B . 
CA 6 HOH 87  587 271 HOH HOH B . 
CA 6 HOH 88  588 164 HOH HOH B . 
CA 6 HOH 89  589 172 HOH HOH B . 
CA 6 HOH 90  590 38  HOH HOH B . 
CA 6 HOH 91  591 41  HOH HOH B . 
CA 6 HOH 92  592 277 HOH HOH B . 
CA 6 HOH 93  593 137 HOH HOH B . 
CA 6 HOH 94  594 155 HOH HOH B . 
CA 6 HOH 95  595 204 HOH HOH B . 
CA 6 HOH 96  596 245 HOH HOH B . 
CA 6 HOH 97  597 191 HOH HOH B . 
CA 6 HOH 98  598 272 HOH HOH B . 
CA 6 HOH 99  599 258 HOH HOH B . 
CA 6 HOH 100 600 206 HOH HOH B . 
CA 6 HOH 101 601 124 HOH HOH B . 
CA 6 HOH 102 602 180 HOH HOH B . 
CA 6 HOH 103 603 252 HOH HOH B . 
CA 6 HOH 104 604 184 HOH HOH B . 
CA 6 HOH 105 605 174 HOH HOH B . 
CA 6 HOH 106 606 181 HOH HOH B . 
CA 6 HOH 107 607 205 HOH HOH B . 
CA 6 HOH 108 608 194 HOH HOH B . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,BA 
2 1 B,S,T,U,V,W,X,Y,Z,AA,CA              
# 
_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 2021-01-20 
2 'Structure model' 1 1 2021-05-19 
# 
_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_details.details             ? 
# 
_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' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.year'           
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 4.53223366733  -11.1388351315 38.4120870036 0.253157400701 ? -0.00698924803389 ? -0.0107343725169 
? 0.105133339039 ? -0.0242345333213 ? 0.203505280052 ? 1.28444989991  ? 0.22872650932   ? 0.0678705178667 ? 2.4049112405  ? 
0.2426379947    ? 0.483525779242 ? -0.0578729686057 ? 0.0842942422018 ? -0.0223827322983 ? -0.171992902906 ? 0.041224085436  ? 
0.0566710485539 ? -0.0146340179015 ? -0.0846620990966 ? -0.0020050380758 ? 
2 'X-RAY DIFFRACTION' ? refined -11.3895098736 -21.5254573933 77.0512959035 0.227260742154 ? 0.0770848592271   ? 0.049552876561   
? 0.78245009598  ? 0.146608164383   ? 0.303817001688 ? 0.350270942333 ? -0.317009129799 ? 0.546470070462  ? 1.55823986256 ? 
-0.582154076081 ? 0.890849254144 ? 0.0471240415878  ? -0.257048420583 ? 0.0527940090199  ? -0.014197258836 ? -0.151440385495 ? 
-0.198094805761 ? -0.0652410237127 ? -0.118025184235  ? -0.0131557615783 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? 
;(chain 'A' and resid 29 through 369)
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? 
;(chain 'B' and resid 29 through 369)
;
# 
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 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? MxCuBE ? ? ? .           1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.17.1_3660 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? 20180126    3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? 20180126    4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? 2.8.1       5 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? 20180126    6 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? 0.8.9.2     7 
# 
_pdbx_entry_details.entry_id                 6YED 
_pdbx_entry_details.has_ligand_of_interest   N 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE2 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    184 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   A 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    501 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
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 A 124 ? ? -151.71 86.44  
2  1 TYR A 133 ? ? -105.54 -69.32 
3  1 ASN A 199 ? ? -118.75 56.43  
4  1 SER A 227 ? ? -149.11 -32.87 
5  1 ASN A 288 ? ? -116.10 68.54  
6  1 VAL B 83  ? ? -118.56 79.09  
7  1 LEU B 106 ? ? -116.47 74.69  
8  1 ASP B 126 ? ? 59.84   13.90  
9  1 TYR B 133 ? ? -96.19  -70.53 
10 1 ASP B 181 ? ? -88.59  47.07  
11 1 ASN B 199 ? ? -111.94 56.10  
12 1 SER B 227 ? ? -147.51 -16.54 
13 1 ASN B 288 ? ? -113.12 78.81  
14 1 ILE B 335 ? ? -120.54 -52.89 
# 
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 A ALA 27  ? A ALA 1   
2  1 Y 1 A GLU 28  ? A GLU 2   
3  1 Y 1 A LYS 370 ? A LYS 344 
4  1 Y 1 A LEU 371 ? A LEU 345 
5  1 Y 1 A GLU 372 ? A GLU 346 
6  1 Y 1 A HIS 373 ? A HIS 347 
7  1 Y 1 A HIS 374 ? A HIS 348 
8  1 Y 1 A HIS 375 ? A HIS 349 
9  1 Y 1 A HIS 376 ? A HIS 350 
10 1 Y 1 A HIS 377 ? A HIS 351 
11 1 Y 1 A HIS 378 ? A HIS 352 
12 1 Y 1 B ALA 27  ? B ALA 1   
13 1 Y 1 B GLU 28  ? B GLU 2   
14 1 Y 1 B LYS 370 ? B LYS 344 
15 1 Y 1 B LEU 371 ? B LEU 345 
16 1 Y 1 B GLU 372 ? B GLU 346 
17 1 Y 1 B HIS 373 ? B HIS 347 
18 1 Y 1 B HIS 374 ? B HIS 348 
19 1 Y 1 B HIS 375 ? B HIS 349 
20 1 Y 1 B HIS 376 ? B HIS 350 
21 1 Y 1 B HIS 377 ? B HIS 351 
22 1 Y 1 B HIS 378 ? B HIS 352 
# 
_pdbx_audit_support.funding_organization   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           HO4022/2-3 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'TRIETHYLENE GLYCOL'    PGE 
3 'DI(HYDROXYETHYL)ETHER' PEG 
4 1,2-ETHANEDIOL          EDO 
5 'CHLORIDE ION'          CL  
6 water                   HOH 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
