data_3MN8
# 
_entry.id   3MN8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3MN8         
RCSB  RCSB058756   
WWPDB D_1000058756 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1QMU 'Structure of duck carboxypeptidase D domain II'                       unspecified 
PDB 1H8L 'Structure of duck carboxypeptidase D domain II in complex with GEMSA' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3MN8 
_pdbx_database_status.recvd_initial_deposition_date   2010-04-21 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Tanco, S.'        1 
'Arolas, J.L.'     2 
'Guevara, T.'      3 
'Lorenzo, J.'      4 
'Aviles, F.X.'     5 
'Gomis-Ruth, F.X.' 6 
# 
_citation.id                        primary 
_citation.title                     
'Structure-Function Analysis of the Short Splicing Variant Carboxypeptidase Encoded by Drosophila melanogaster silver.' 
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            401 
_citation.page_first                465 
_citation.page_last                 477 
_citation.year                      2010 
_citation.journal_id_ASTM           JMOBAK 
_citation.country                   UK 
_citation.journal_id_ISSN           0022-2836 
_citation.journal_id_CSD            0070 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20600119 
_citation.pdbx_database_id_DOI      10.1016/j.jmb.2010.06.035 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Tanco, S.'        1 
primary 'Arolas, J.L.'     2 
primary 'Guevara, T.'      3 
primary 'Lorenzo, J.'      4 
primary 'Aviles, F.X.'     5 
primary 'Gomis-Ruth, F.X.' 6 
# 
_cell.entry_id           3MN8 
_cell.length_a           97.020 
_cell.length_b           135.700 
_cell.length_c           141.710 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              16 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3MN8 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
# 
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 LP15968p                                  48610.375 4   ? ? 'UNP residues 1-435' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE                    221.208   4   ? ? ?                    ? 
3 non-polymer syn 'ZINC ION'                                65.409    4   ? ? ?                    ? 
4 non-polymer syn '(2-GUANIDINOETHYLMERCAPTO)SUCCINIC ACID' 235.261   4   ? ? ?                    ? 
5 non-polymer syn GLYCEROL                                  92.094    4   ? ? ?                    ? 
6 water       nat water                                     18.015    211 ? ? ?                    ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        metallocarboxypeptidase 
# 
_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       
;MPTLGLLFASIGIAVLAMGVPHCRGYTIKEDESFLQQPHYASQEQLEDLFAGLEKAYPNQAKVHFLGRSLEGRNLLALQI
SRNTRSRNLLTPPVKYIANMHGDETVGRQLLVYMAQYLLGNHERISDLGQLVNSTDIYLVPTMNPDGYALSQEGNCESLP
NYVGRGNAANIDLNRDFPDRLEQSHVHQLRAQSRQPETAALVNWIVSKPFVLSANFHGGAVVASYPYDNSLAHNECCEES
LTPDDRVFKQLAHTYSDNHPIMRKGNNCNDSFSGGITNGAHWYELSGGMQDFNYAFSNCFELTIELSCCKYPAASTLPQE
WQRNKASLLQLLRQAHIGIKGLVTDASGFPIADANVYVAGLEEKPMRTSKRGEYWRLLTPGLYSVHASAFGYQTSAPQQV
RVTNDNQEALRLDFKLAPVETNFDGISSFYSPYYF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPTLGLLFASIGIAVLAMGVPHCRGYTIKEDESFLQQPHYASQEQLEDLFAGLEKAYPNQAKVHFLGRSLEGRNLLALQI
SRNTRSRNLLTPPVKYIANMHGDETVGRQLLVYMAQYLLGNHERISDLGQLVNSTDIYLVPTMNPDGYALSQEGNCESLP
NYVGRGNAANIDLNRDFPDRLEQSHVHQLRAQSRQPETAALVNWIVSKPFVLSANFHGGAVVASYPYDNSLAHNECCEES
LTPDDRVFKQLAHTYSDNHPIMRKGNNCNDSFSGGITNGAHWYELSGGMQDFNYAFSNCFELTIELSCCKYPAASTLPQE
WQRNKASLLQLLRQAHIGIKGLVTDASGFPIADANVYVAGLEEKPMRTSKRGEYWRLLTPGLYSVHASAFGYQTSAPQQV
RVTNDNQEALRLDFKLAPVETNFDGISSFYSPYYF
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_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   MET n 
1 2   PRO n 
1 3   THR n 
1 4   LEU n 
1 5   GLY n 
1 6   LEU n 
1 7   LEU n 
1 8   PHE n 
1 9   ALA n 
1 10  SER n 
1 11  ILE n 
1 12  GLY n 
1 13  ILE n 
1 14  ALA n 
1 15  VAL n 
1 16  LEU n 
1 17  ALA n 
1 18  MET n 
1 19  GLY n 
1 20  VAL n 
1 21  PRO n 
1 22  HIS n 
1 23  CYS n 
1 24  ARG n 
1 25  GLY n 
1 26  TYR n 
1 27  THR n 
1 28  ILE n 
1 29  LYS n 
1 30  GLU n 
1 31  ASP n 
1 32  GLU n 
1 33  SER n 
1 34  PHE n 
1 35  LEU n 
1 36  GLN n 
1 37  GLN n 
1 38  PRO n 
1 39  HIS n 
1 40  TYR n 
1 41  ALA n 
1 42  SER n 
1 43  GLN n 
1 44  GLU n 
1 45  GLN n 
1 46  LEU n 
1 47  GLU n 
1 48  ASP n 
1 49  LEU n 
1 50  PHE n 
1 51  ALA n 
1 52  GLY n 
1 53  LEU n 
1 54  GLU n 
1 55  LYS n 
1 56  ALA n 
1 57  TYR n 
1 58  PRO n 
1 59  ASN n 
1 60  GLN n 
1 61  ALA n 
1 62  LYS n 
1 63  VAL n 
1 64  HIS n 
1 65  PHE n 
1 66  LEU n 
1 67  GLY n 
1 68  ARG n 
1 69  SER n 
1 70  LEU n 
1 71  GLU n 
1 72  GLY n 
1 73  ARG n 
1 74  ASN n 
1 75  LEU n 
1 76  LEU n 
1 77  ALA n 
1 78  LEU n 
1 79  GLN n 
1 80  ILE n 
1 81  SER n 
1 82  ARG n 
1 83  ASN n 
1 84  THR n 
1 85  ARG n 
1 86  SER n 
1 87  ARG n 
1 88  ASN n 
1 89  LEU n 
1 90  LEU n 
1 91  THR n 
1 92  PRO n 
1 93  PRO n 
1 94  VAL n 
1 95  LYS n 
1 96  TYR n 
1 97  ILE n 
1 98  ALA n 
1 99  ASN n 
1 100 MET n 
1 101 HIS n 
1 102 GLY n 
1 103 ASP n 
1 104 GLU n 
1 105 THR n 
1 106 VAL n 
1 107 GLY n 
1 108 ARG n 
1 109 GLN n 
1 110 LEU n 
1 111 LEU n 
1 112 VAL n 
1 113 TYR n 
1 114 MET n 
1 115 ALA n 
1 116 GLN n 
1 117 TYR n 
1 118 LEU n 
1 119 LEU n 
1 120 GLY n 
1 121 ASN n 
1 122 HIS n 
1 123 GLU n 
1 124 ARG n 
1 125 ILE n 
1 126 SER n 
1 127 ASP n 
1 128 LEU n 
1 129 GLY n 
1 130 GLN n 
1 131 LEU n 
1 132 VAL n 
1 133 ASN n 
1 134 SER n 
1 135 THR n 
1 136 ASP n 
1 137 ILE n 
1 138 TYR n 
1 139 LEU n 
1 140 VAL n 
1 141 PRO n 
1 142 THR n 
1 143 MET n 
1 144 ASN n 
1 145 PRO n 
1 146 ASP n 
1 147 GLY n 
1 148 TYR n 
1 149 ALA n 
1 150 LEU n 
1 151 SER n 
1 152 GLN n 
1 153 GLU n 
1 154 GLY n 
1 155 ASN n 
1 156 CYS n 
1 157 GLU n 
1 158 SER n 
1 159 LEU n 
1 160 PRO n 
1 161 ASN n 
1 162 TYR n 
1 163 VAL n 
1 164 GLY n 
1 165 ARG n 
1 166 GLY n 
1 167 ASN n 
1 168 ALA n 
1 169 ALA n 
1 170 ASN n 
1 171 ILE n 
1 172 ASP n 
1 173 LEU n 
1 174 ASN n 
1 175 ARG n 
1 176 ASP n 
1 177 PHE n 
1 178 PRO n 
1 179 ASP n 
1 180 ARG n 
1 181 LEU n 
1 182 GLU n 
1 183 GLN n 
1 184 SER n 
1 185 HIS n 
1 186 VAL n 
1 187 HIS n 
1 188 GLN n 
1 189 LEU n 
1 190 ARG n 
1 191 ALA n 
1 192 GLN n 
1 193 SER n 
1 194 ARG n 
1 195 GLN n 
1 196 PRO n 
1 197 GLU n 
1 198 THR n 
1 199 ALA n 
1 200 ALA n 
1 201 LEU n 
1 202 VAL n 
1 203 ASN n 
1 204 TRP n 
1 205 ILE n 
1 206 VAL n 
1 207 SER n 
1 208 LYS n 
1 209 PRO n 
1 210 PHE n 
1 211 VAL n 
1 212 LEU n 
1 213 SER n 
1 214 ALA n 
1 215 ASN n 
1 216 PHE n 
1 217 HIS n 
1 218 GLY n 
1 219 GLY n 
1 220 ALA n 
1 221 VAL n 
1 222 VAL n 
1 223 ALA n 
1 224 SER n 
1 225 TYR n 
1 226 PRO n 
1 227 TYR n 
1 228 ASP n 
1 229 ASN n 
1 230 SER n 
1 231 LEU n 
1 232 ALA n 
1 233 HIS n 
1 234 ASN n 
1 235 GLU n 
1 236 CYS n 
1 237 CYS n 
1 238 GLU n 
1 239 GLU n 
1 240 SER n 
1 241 LEU n 
1 242 THR n 
1 243 PRO n 
1 244 ASP n 
1 245 ASP n 
1 246 ARG n 
1 247 VAL n 
1 248 PHE n 
1 249 LYS n 
1 250 GLN n 
1 251 LEU n 
1 252 ALA n 
1 253 HIS n 
1 254 THR n 
1 255 TYR n 
1 256 SER n 
1 257 ASP n 
1 258 ASN n 
1 259 HIS n 
1 260 PRO n 
1 261 ILE n 
1 262 MET n 
1 263 ARG n 
1 264 LYS n 
1 265 GLY n 
1 266 ASN n 
1 267 ASN n 
1 268 CYS n 
1 269 ASN n 
1 270 ASP n 
1 271 SER n 
1 272 PHE n 
1 273 SER n 
1 274 GLY n 
1 275 GLY n 
1 276 ILE n 
1 277 THR n 
1 278 ASN n 
1 279 GLY n 
1 280 ALA n 
1 281 HIS n 
1 282 TRP n 
1 283 TYR n 
1 284 GLU n 
1 285 LEU n 
1 286 SER n 
1 287 GLY n 
1 288 GLY n 
1 289 MET n 
1 290 GLN n 
1 291 ASP n 
1 292 PHE n 
1 293 ASN n 
1 294 TYR n 
1 295 ALA n 
1 296 PHE n 
1 297 SER n 
1 298 ASN n 
1 299 CYS n 
1 300 PHE n 
1 301 GLU n 
1 302 LEU n 
1 303 THR n 
1 304 ILE n 
1 305 GLU n 
1 306 LEU n 
1 307 SER n 
1 308 CYS n 
1 309 CYS n 
1 310 LYS n 
1 311 TYR n 
1 312 PRO n 
1 313 ALA n 
1 314 ALA n 
1 315 SER n 
1 316 THR n 
1 317 LEU n 
1 318 PRO n 
1 319 GLN n 
1 320 GLU n 
1 321 TRP n 
1 322 GLN n 
1 323 ARG n 
1 324 ASN n 
1 325 LYS n 
1 326 ALA n 
1 327 SER n 
1 328 LEU n 
1 329 LEU n 
1 330 GLN n 
1 331 LEU n 
1 332 LEU n 
1 333 ARG n 
1 334 GLN n 
1 335 ALA n 
1 336 HIS n 
1 337 ILE n 
1 338 GLY n 
1 339 ILE n 
1 340 LYS n 
1 341 GLY n 
1 342 LEU n 
1 343 VAL n 
1 344 THR n 
1 345 ASP n 
1 346 ALA n 
1 347 SER n 
1 348 GLY n 
1 349 PHE n 
1 350 PRO n 
1 351 ILE n 
1 352 ALA n 
1 353 ASP n 
1 354 ALA n 
1 355 ASN n 
1 356 VAL n 
1 357 TYR n 
1 358 VAL n 
1 359 ALA n 
1 360 GLY n 
1 361 LEU n 
1 362 GLU n 
1 363 GLU n 
1 364 LYS n 
1 365 PRO n 
1 366 MET n 
1 367 ARG n 
1 368 THR n 
1 369 SER n 
1 370 LYS n 
1 371 ARG n 
1 372 GLY n 
1 373 GLU n 
1 374 TYR n 
1 375 TRP n 
1 376 ARG n 
1 377 LEU n 
1 378 LEU n 
1 379 THR n 
1 380 PRO n 
1 381 GLY n 
1 382 LEU n 
1 383 TYR n 
1 384 SER n 
1 385 VAL n 
1 386 HIS n 
1 387 ALA n 
1 388 SER n 
1 389 ALA n 
1 390 PHE n 
1 391 GLY n 
1 392 TYR n 
1 393 GLN n 
1 394 THR n 
1 395 SER n 
1 396 ALA n 
1 397 PRO n 
1 398 GLN n 
1 399 GLN n 
1 400 VAL n 
1 401 ARG n 
1 402 VAL n 
1 403 THR n 
1 404 ASN n 
1 405 ASP n 
1 406 ASN n 
1 407 GLN n 
1 408 GLU n 
1 409 ALA n 
1 410 LEU n 
1 411 ARG n 
1 412 LEU n 
1 413 ASP n 
1 414 PHE n 
1 415 LYS n 
1 416 LEU n 
1 417 ALA n 
1 418 PRO n 
1 419 VAL n 
1 420 GLU n 
1 421 THR n 
1 422 ASN n 
1 423 PHE n 
1 424 ASP n 
1 425 GLY n 
1 426 ILE n 
1 427 SER n 
1 428 SER n 
1 429 PHE n 
1 430 TYR n 
1 431 SER n 
1 432 PRO n 
1 433 TYR n 
1 434 TYR n 
1 435 PHE 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               'Fruit fly' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 svr-RF 
_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      'Drosophila melanogaster' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     7227 
_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      'Pichia pastoris' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4922 
_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               KM71H 
_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          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pPICZalphaA 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    D3DME3_DROME 
_struct_ref.pdbx_db_accession          D3DME3 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPTLGLLFASIGIAVLAMGVPHCRGYTIKEDESFLQQPHYASQEQLEDLFAGLEKAYPNQAKVHFLGRSLEGRNLLALQI
SRNTRSRNLLTPPVKYIANMHGDETVGRQLLVYMAQYLLGNHERISDLGQLVNSTDIYLVPTMNPDGYALSQEGNCESLP
NYVGRGNAANIDLNRDFPDRLEQSHVHQLRAQSRQPETAALVNWIVSKPFVLSANFHGGAVVASYPYDNSLAHNECCEES
LTPDDRVFKQLAHTYSDNHPIMRKGNNCNDSFSGGITNGAHWYELSGGMQDFNYAFSNCFELTIELSCCKYPAASTLPQE
WQRNKASLLQLLRQAHIGIKGLVTDASGFPIADANVYVAGLEEKPMRTSKRGEYWRLLTPGLYSVHASAFGYQTSAPQQV
RVTNDNQEALRLDFKLAPVETNFDGISSFYSPYYF
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
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 3MN8 A 1 ? 435 ? D3DME3 1 ? 435 ? 1 435 
2 1 3MN8 B 1 ? 435 ? D3DME3 1 ? 435 ? 1 435 
3 1 3MN8 C 1 ? 435 ? D3DME3 1 ? 435 ? 1 435 
4 1 3MN8 D 1 ? 435 ? D3DME3 1 ? 435 ? 1 435 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                   ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                  ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                           ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                  ? 'C3 H7 N O2 S'   121.158 
GEM non-polymer         . '(2-GUANIDINOETHYLMERCAPTO)SUCCINIC ACID' 
'2-GUANIDINOETHYLTHIO)SUCCINIC ACID; GUANIDINOETHYL MERCAPTOSUCCINIC ACID; GEMSA' 'C7 H13 N3 O4 S' 235.261 
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  
GOL non-polymer         . GLYCEROL                                  'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE                                 ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                     ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                   ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                    ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                ? 'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE                    ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE                             ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                   ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                    ? 'C3 H7 N O3'     105.093 
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 
ZN  non-polymer         . 'ZINC ION'                                ? 'Zn 2'           65.409  
# 
_exptl.entry_id          3MN8 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.40 
_exptl_crystal.density_percent_sol   48.72 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            277.15 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    
'8% PEG 4000, 0.2M KSCN, 0.1M sodium cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277.15K' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100.0 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315r' 
_diffrn_detector.pdbx_collection_date   2009-04-02 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9724 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.9724 
# 
_reflns.entry_id                     3MN8 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             49.0 
_reflns.d_resolution_high            2.7 
_reflns.number_obs                   52035 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         ? 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 3MN8 
_refine.ls_number_reflns_obs                     52035 
_refine.ls_number_reflns_all                     52035 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             49.00 
_refine.ls_d_res_high                            2.700 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_R_factor_obs                          0.2116 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2108 
_refine.ls_R_factor_R_free                       0.2817 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 1.47 
_refine.ls_number_reflns_R_free                  765 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            1.00 
_refine.occupancy_max                            1.00 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            -13.9933 
_refine.aniso_B[2][2]                            15.5254 
_refine.aniso_B[3][3]                            -4.0673 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            -0.0000 
_refine.aniso_B[2][3]                            -0.0000 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 0.325 
_refine.solvent_model_param_bsol                 59.132 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  
;THE CURRENTLY DEPOSITED COORDINATES WERE SUBJECTED TO A VERY FINAL REFINEMENT STEP UNDER CONSIDERATION OF DIFFERENT TLS GROUPS. ACCORDINGLY, THERE ARE MINOR DIFFERENCES BETWEEN THE CURRENT STATISTICS AND THOSE REPORTED IN THE PRIMARY PUBLICATION, WHICH ARE NOT SIGNIFICANT.
;
_refine.pdbx_starting_model                      'PDB ENTRY 1H8L' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       TWIN_LSQ_F 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            . 
_refine.pdbx_overall_phase_error                 35.98 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        12113 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         144 
_refine_hist.number_atoms_solvent             211 
_refine_hist.number_atoms_total               12468 
_refine_hist.d_res_high                       2.700 
_refine_hist.d_res_low                        49.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.008  ? ? 12561 'X-RAY DIFFRACTION' ? 
f_angle_d          1.118  ? ? 16995 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 20.171 ? ? 4553  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.071  ? ? 1823  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.004  ? ? 2267  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_ens_id 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.weight_B_iso 
1 A 2203 ?     ? POSITIONAL 1 1 'X-RAY DIFFRACTION' ? ? ? 
2 B 2203 0.133 ? POSITIONAL 1 2 'X-RAY DIFFRACTION' ? ? ? 
3 C 2203 0.134 ? POSITIONAL 1 3 'X-RAY DIFFRACTION' ? ? ? 
4 D 2203 0.115 ? POSITIONAL 1 4 'X-RAY DIFFRACTION' ? ? ? 
1 A 570  ?     ? POSITIONAL 2 5 'X-RAY DIFFRACTION' ? ? ? 
2 B 570  0.160 ? POSITIONAL 2 6 'X-RAY DIFFRACTION' ? ? ? 
3 C 570  0.139 ? POSITIONAL 2 7 'X-RAY DIFFRACTION' ? ? ? 
4 D 570  0.144 ? POSITIONAL 2 8 'X-RAY DIFFRACTION' ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.number_reflns_obs 
'X-RAY DIFFRACTION' . 2.70   2.9088  10085 0.2454 99.00 0.3340 . . 147 . . . . 
'X-RAY DIFFRACTION' . 2.9088 3.2009  10098 0.2221 98.00 0.3208 . . 156 . . . . 
'X-RAY DIFFRACTION' . 3.2009 3.6627  10180 0.2017 99.00 0.2881 . . 142 . . . . 
'X-RAY DIFFRACTION' . 3.6627 4.6092  10245 0.1879 99.00 0.2433 . . 150 . . . . 
'X-RAY DIFFRACTION' . 4.6092 24.0179 10570 0.2170 99.00 0.2782 . . 154 . . . . 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.details 
_struct_ncs_dom.pdbx_ens_id 
1 ? 1 
2 ? 1 
3 ? 1 
4 ? 1 
1 ? 2 
2 ? 2 
3 ? 2 
4 ? 2 
# 
loop_
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.selection_details 
1 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 1 'chain A and (resseq 39:158 or resseq 163:180 or resseq 195:336 )'  
2 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 1 'chain B and (resseq 39:158 or resseq 163:180 or resseq 195:336 )'  
3 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 1 'chain C and (resseq 39:158 or resseq 163:180 or resseq 195:336 )'  
4 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 1 'chain D and (resseq 39:158 or resseq 163:180 or resseq 195:336 )'  
1 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 2 'chain A and (resseq 337:344 or resseq 350:403 or resseq 407:417 )' 
2 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 2 'chain B and (resseq 337:344 or resseq 350:403 or resseq 407:417 )' 
3 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 2 'chain C and (resseq 337:344 or resseq 350:403 or resseq 407:417 )' 
4 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 2 'chain D and (resseq 337:344 or resseq 350:403 or resseq 407:417 )' 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1 ? 
2 ? 
# 
_struct.entry_id                  3MN8 
_struct.title                     'Structure of Drosophila melanogaster carboxypeptidase D isoform 1B short' 
_struct.pdbx_descriptor           LP15968p 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3MN8 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
'catalytic domain of alpha/beta-hydrolase fold, C-terminal, all-beta transthyretin-like domain, Hydrolase' 
# 
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 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 5 ? 
J N N 5 ? 
K N N 2 ? 
L N N 3 ? 
M N N 4 ? 
N N N 2 ? 
O N N 3 ? 
P N N 4 ? 
Q N N 5 ? 
R N N 2 ? 
S N N 3 ? 
T N N 4 ? 
U N N 6 ? 
V N N 6 ? 
W N N 6 ? 
X N N 6 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  1  GLU A 32  ? GLN A 36  ? GLU A 32  GLN A 36  5 ? 5  
HELX_P HELX_P2  2  SER A 42  ? TYR A 57  ? SER A 42  TYR A 57  1 ? 16 
HELX_P HELX_P3  3  THR A 105 ? HIS A 122 ? THR A 105 HIS A 122 1 ? 18 
HELX_P HELX_P4  4  ILE A 125 ? THR A 135 ? ILE A 125 THR A 135 1 ? 11 
HELX_P HELX_P5  5  ASN A 144 ? LEU A 150 ? ASN A 144 LEU A 150 1 ? 7  
HELX_P HELX_P6  6  LEU A 159 ? VAL A 163 ? LEU A 159 VAL A 163 5 ? 5  
HELX_P HELX_P7  7  ASP A 172 ? ASP A 176 ? ASP A 172 ASP A 176 5 ? 5  
HELX_P HELX_P8  8  GLN A 195 ? VAL A 206 ? GLN A 195 VAL A 206 1 ? 12 
HELX_P HELX_P9  9  ASP A 244 ? ASN A 258 ? ASP A 244 ASN A 258 1 ? 15 
HELX_P HELX_P10 10 ASN A 266 ? ASP A 270 ? ASN A 266 ASP A 270 5 ? 5  
HELX_P HELX_P11 11 PHE A 272 ? GLY A 274 ? PHE A 272 GLY A 274 5 ? 3  
HELX_P HELX_P12 12 GLY A 279 ? TYR A 283 ? GLY A 279 TYR A 283 1 ? 5  
HELX_P HELX_P13 13 GLY A 288 ? SER A 297 ? GLY A 288 SER A 297 1 ? 10 
HELX_P HELX_P14 14 ALA A 313 ? SER A 315 ? ALA A 313 SER A 315 5 ? 3  
HELX_P HELX_P15 15 THR A 316 ? GLN A 334 ? THR A 316 GLN A 334 1 ? 19 
HELX_P HELX_P16 16 ALA A 335 ? ILE A 337 ? ALA A 335 ILE A 337 5 ? 3  
HELX_P HELX_P17 17 SER B 42  ? TYR B 57  ? SER B 42  TYR B 57  1 ? 16 
HELX_P HELX_P18 18 THR B 105 ? GLU B 123 ? THR B 105 GLU B 123 1 ? 19 
HELX_P HELX_P19 19 ILE B 125 ? THR B 135 ? ILE B 125 THR B 135 1 ? 11 
HELX_P HELX_P20 20 ASN B 144 ? SER B 151 ? ASN B 144 SER B 151 1 ? 8  
HELX_P HELX_P21 21 LEU B 159 ? VAL B 163 ? LEU B 159 VAL B 163 5 ? 5  
HELX_P HELX_P22 22 ASP B 172 ? ASP B 176 ? ASP B 172 ASP B 176 5 ? 5  
HELX_P HELX_P23 23 GLN B 195 ? VAL B 206 ? GLN B 195 VAL B 206 1 ? 12 
HELX_P HELX_P24 24 ASP B 244 ? ASN B 258 ? ASP B 244 ASN B 258 1 ? 15 
HELX_P HELX_P25 25 PHE B 272 ? GLY B 274 ? PHE B 272 GLY B 274 5 ? 3  
HELX_P HELX_P26 26 GLY B 279 ? TYR B 283 ? GLY B 279 TYR B 283 1 ? 5  
HELX_P HELX_P27 27 GLY B 288 ? SER B 297 ? GLY B 288 SER B 297 1 ? 10 
HELX_P HELX_P28 28 ALA B 313 ? SER B 315 ? ALA B 313 SER B 315 5 ? 3  
HELX_P HELX_P29 29 THR B 316 ? GLN B 334 ? THR B 316 GLN B 334 1 ? 19 
HELX_P HELX_P30 30 ALA B 335 ? ILE B 337 ? ALA B 335 ILE B 337 5 ? 3  
HELX_P HELX_P31 31 GLU C 32  ? GLN C 36  ? GLU C 32  GLN C 36  5 ? 5  
HELX_P HELX_P32 32 SER C 42  ? TYR C 57  ? SER C 42  TYR C 57  1 ? 16 
HELX_P HELX_P33 33 THR C 105 ? GLU C 123 ? THR C 105 GLU C 123 1 ? 19 
HELX_P HELX_P34 34 ILE C 125 ? THR C 135 ? ILE C 125 THR C 135 1 ? 11 
HELX_P HELX_P35 35 ASN C 144 ? SER C 151 ? ASN C 144 SER C 151 1 ? 8  
HELX_P HELX_P36 36 LEU C 159 ? VAL C 163 ? LEU C 159 VAL C 163 5 ? 5  
HELX_P HELX_P37 37 ASP C 172 ? ASP C 176 ? ASP C 172 ASP C 176 5 ? 5  
HELX_P HELX_P38 38 GLN C 195 ? VAL C 206 ? GLN C 195 VAL C 206 1 ? 12 
HELX_P HELX_P39 39 ASP C 244 ? ASN C 258 ? ASP C 244 ASN C 258 1 ? 15 
HELX_P HELX_P40 40 PHE C 272 ? GLY C 274 ? PHE C 272 GLY C 274 5 ? 3  
HELX_P HELX_P41 41 GLY C 279 ? TYR C 283 ? GLY C 279 TYR C 283 1 ? 5  
HELX_P HELX_P42 42 GLY C 288 ? SER C 297 ? GLY C 288 SER C 297 1 ? 10 
HELX_P HELX_P43 43 ALA C 313 ? SER C 315 ? ALA C 313 SER C 315 5 ? 3  
HELX_P HELX_P44 44 THR C 316 ? ARG C 333 ? THR C 316 ARG C 333 1 ? 18 
HELX_P HELX_P45 45 GLN C 334 ? ILE C 337 ? GLN C 334 ILE C 337 5 ? 4  
HELX_P HELX_P46 46 GLU D 32  ? GLN D 36  ? GLU D 32  GLN D 36  5 ? 5  
HELX_P HELX_P47 47 SER D 42  ? TYR D 57  ? SER D 42  TYR D 57  1 ? 16 
HELX_P HELX_P48 48 THR D 105 ? HIS D 122 ? THR D 105 HIS D 122 1 ? 18 
HELX_P HELX_P49 49 ILE D 125 ? THR D 135 ? ILE D 125 THR D 135 1 ? 11 
HELX_P HELX_P50 50 ASN D 144 ? SER D 151 ? ASN D 144 SER D 151 1 ? 8  
HELX_P HELX_P51 51 ASP D 172 ? ASP D 176 ? ASP D 172 ASP D 176 5 ? 5  
HELX_P HELX_P52 52 GLN D 195 ? VAL D 206 ? GLN D 195 VAL D 206 1 ? 12 
HELX_P HELX_P53 53 ASP D 244 ? ASN D 258 ? ASP D 244 ASN D 258 1 ? 15 
HELX_P HELX_P54 54 ILE D 261 ? GLY D 265 ? ILE D 261 GLY D 265 5 ? 5  
HELX_P HELX_P55 55 PHE D 272 ? GLY D 274 ? PHE D 272 GLY D 274 5 ? 3  
HELX_P HELX_P56 56 GLY D 279 ? TYR D 283 ? GLY D 279 TYR D 283 1 ? 5  
HELX_P HELX_P57 57 GLY D 288 ? SER D 297 ? GLY D 288 SER D 297 1 ? 10 
HELX_P HELX_P58 58 ALA D 313 ? SER D 315 ? ALA D 313 SER D 315 5 ? 3  
HELX_P HELX_P59 59 THR D 316 ? GLN D 334 ? THR D 316 GLN D 334 1 ? 19 
HELX_P HELX_P60 60 ALA D 335 ? ILE D 337 ? ALA D 335 ILE D 337 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 156 SG  ? ? ? 1_555 A CYS 309 SG  ? ? A CYS 156 A CYS 309 1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf2  disulf ? ? A CYS 236 SG  ? ? ? 1_555 A CYS 237 SG  ? ? A CYS 236 A CYS 237 1_555 ? ? ? ? ? ? ? 2.056 ? 
disulf3  disulf ? ? A CYS 268 SG  ? ? ? 1_555 A CYS 308 SG  ? ? A CYS 268 A CYS 308 1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf4  disulf ? ? B CYS 156 SG  ? ? ? 1_555 B CYS 309 SG  ? ? B CYS 156 B CYS 309 1_555 ? ? ? ? ? ? ? 2.045 ? 
disulf5  disulf ? ? B CYS 236 SG  ? ? ? 1_555 B CYS 237 SG  ? ? B CYS 236 B CYS 237 1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf6  disulf ? ? B CYS 268 SG  ? ? ? 1_555 B CYS 308 SG  ? ? B CYS 268 B CYS 308 1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf7  disulf ? ? C CYS 156 SG  ? ? ? 1_555 C CYS 309 SG  ? ? C CYS 156 C CYS 309 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf8  disulf ? ? C CYS 236 SG  ? ? ? 1_555 C CYS 237 SG  ? ? C CYS 236 C CYS 237 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf9  disulf ? ? C CYS 268 SG  ? ? ? 1_555 C CYS 308 SG  ? ? C CYS 268 C CYS 308 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf10 disulf ? ? D CYS 156 SG  ? ? ? 1_555 D CYS 309 SG  ? ? D CYS 156 D CYS 309 1_555 ? ? ? ? ? ? ? 2.052 ? 
disulf11 disulf ? ? D CYS 236 SG  ? ? ? 1_555 D CYS 237 SG  ? ? D CYS 236 D CYS 237 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf12 disulf ? ? D CYS 268 SG  ? ? ? 1_555 D CYS 308 SG  ? ? D CYS 268 D CYS 308 1_555 ? ? ? ? ? ? ? 2.038 ? 
covale1  covale ? ? A ASN 133 ND2 ? ? ? 1_555 E NAG .   C1  ? ? A ASN 133 A NAG 501 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale2  covale ? ? B ASN 133 ND2 ? ? ? 1_555 K NAG .   C1  ? ? B ASN 133 B NAG 501 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale3  covale ? ? C ASN 133 ND2 ? ? ? 1_555 N NAG .   C1  ? ? C ASN 133 C NAG 501 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale4  covale ? ? D ASN 133 ND2 ? ? ? 1_555 R NAG .   C1  ? ? D ASN 133 D NAG 501 1_555 ? ? ? ? ? ? ? 1.452 ? 
metalc1  metalc ? ? D GLU 104 OE1 ? ? ? 1_555 S ZN  .   ZN  ? ? D GLU 104 D ZN  999 1_555 ? ? ? ? ? ? ? 2.019 ? 
metalc2  metalc ? ? A GLU 104 OE1 ? ? ? 1_555 F ZN  .   ZN  ? ? A GLU 104 A ZN  999 1_555 ? ? ? ? ? ? ? 2.019 ? 
metalc3  metalc ? ? C GLU 104 OE1 ? ? ? 1_555 O ZN  .   ZN  ? ? C GLU 104 C ZN  999 1_555 ? ? ? ? ? ? ? 2.022 ? 
metalc4  metalc ? ? B GLU 104 OE1 ? ? ? 1_555 L ZN  .   ZN  ? ? B GLU 104 B ZN  999 1_555 ? ? ? ? ? ? ? 2.028 ? 
metalc5  metalc ? ? B GLU 104 OE2 ? ? ? 1_555 L ZN  .   ZN  ? ? B GLU 104 B ZN  999 1_555 ? ? ? ? ? ? ? 2.029 ? 
metalc6  metalc ? ? A GLU 104 OE2 ? ? ? 1_555 F ZN  .   ZN  ? ? A GLU 104 A ZN  999 1_555 ? ? ? ? ? ? ? 2.035 ? 
metalc7  metalc ? ? D GLU 104 OE2 ? ? ? 1_555 S ZN  .   ZN  ? ? D GLU 104 D ZN  999 1_555 ? ? ? ? ? ? ? 2.044 ? 
metalc8  metalc ? ? C GLU 104 OE2 ? ? ? 1_555 O ZN  .   ZN  ? ? C GLU 104 C ZN  999 1_555 ? ? ? ? ? ? ? 2.054 ? 
metalc9  metalc ? ? F ZN  .   ZN  ? ? ? 1_555 G GEM .   O13 ? ? A ZN  999 A GEM 601 1_555 ? ? ? ? ? ? ? 2.088 ? 
metalc10 metalc ? ? L ZN  .   ZN  ? ? ? 1_555 M GEM .   O13 ? ? B ZN  999 B GEM 601 1_555 ? ? ? ? ? ? ? 2.096 ? 
metalc11 metalc ? ? S ZN  .   ZN  ? ? ? 1_555 T GEM .   O13 ? ? D ZN  999 D GEM 601 1_555 ? ? ? ? ? ? ? 2.114 ? 
metalc12 metalc ? ? O ZN  .   ZN  ? ? ? 1_555 P GEM .   O13 ? ? C ZN  999 C GEM 601 1_555 ? ? ? ? ? ? ? 2.114 ? 
metalc13 metalc ? ? D HIS 217 ND1 ? ? ? 1_555 S ZN  .   ZN  ? ? D HIS 217 D ZN  999 1_555 ? ? ? ? ? ? ? 2.131 ? 
metalc14 metalc ? ? A HIS 217 ND1 ? ? ? 1_555 F ZN  .   ZN  ? ? A HIS 217 A ZN  999 1_555 ? ? ? ? ? ? ? 2.132 ? 
metalc15 metalc ? ? C HIS 101 ND1 ? ? ? 1_555 O ZN  .   ZN  ? ? C HIS 101 C ZN  999 1_555 ? ? ? ? ? ? ? 2.141 ? 
metalc16 metalc ? ? B HIS 101 ND1 ? ? ? 1_555 L ZN  .   ZN  ? ? B HIS 101 B ZN  999 1_555 ? ? ? ? ? ? ? 2.141 ? 
metalc17 metalc ? ? A HIS 101 ND1 ? ? ? 1_555 F ZN  .   ZN  ? ? A HIS 101 A ZN  999 1_555 ? ? ? ? ? ? ? 2.146 ? 
metalc18 metalc ? ? C HIS 217 ND1 ? ? ? 1_555 O ZN  .   ZN  ? ? C HIS 217 C ZN  999 1_555 ? ? ? ? ? ? ? 2.153 ? 
metalc19 metalc ? ? D HIS 101 ND1 ? ? ? 1_555 S ZN  .   ZN  ? ? D HIS 101 D ZN  999 1_555 ? ? ? ? ? ? ? 2.157 ? 
metalc20 metalc ? ? B HIS 217 ND1 ? ? ? 1_555 L ZN  .   ZN  ? ? B HIS 217 B ZN  999 1_555 ? ? ? ? ? ? ? 2.160 ? 
metalc21 metalc ? ? S ZN  .   ZN  ? ? ? 1_555 T GEM .   O12 ? ? D ZN  999 D GEM 601 1_555 ? ? ? ? ? ? ? 2.571 ? 
metalc22 metalc ? ? L ZN  .   ZN  ? ? ? 1_555 M GEM .   O12 ? ? B ZN  999 B GEM 601 1_555 ? ? ? ? ? ? ? 2.579 ? 
metalc23 metalc ? ? F ZN  .   ZN  ? ? ? 1_555 G GEM .   O12 ? ? A ZN  999 A GEM 601 1_555 ? ? ? ? ? ? ? 2.585 ? 
metalc24 metalc ? ? O ZN  .   ZN  ? ? ? 1_555 P GEM .   O12 ? ? C ZN  999 C GEM 601 1_555 ? ? ? ? ? ? ? 2.590 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PRO 226 A . ? PRO 226 A TYR 227 A ? TYR 227 A 1 -5.52 
2 PRO 226 B . ? PRO 226 B TYR 227 B ? TYR 227 B 1 5.18  
3 PRO 226 C . ? PRO 226 C TYR 227 C ? TYR 227 C 1 -1.57 
4 PRO 226 D . ? PRO 226 D TYR 227 D ? TYR 227 D 1 -1.41 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 8 ? 
B ? 3 ? 
C ? 3 ? 
D ? 4 ? 
E ? 8 ? 
F ? 3 ? 
G ? 3 ? 
H ? 4 ? 
I ? 8 ? 
J ? 3 ? 
K ? 3 ? 
L ? 4 ? 
M ? 8 ? 
N ? 3 ? 
O ? 3 ? 
P ? 4 ? 
# 
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 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? parallel      
A 4 5 ? parallel      
A 5 6 ? parallel      
A 6 7 ? anti-parallel 
A 7 8 ? parallel      
B 1 2 ? anti-parallel 
B 2 3 ? parallel      
C 1 2 ? anti-parallel 
C 2 3 ? parallel      
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
E 3 4 ? parallel      
E 4 5 ? parallel      
E 5 6 ? parallel      
E 6 7 ? anti-parallel 
E 7 8 ? parallel      
F 1 2 ? anti-parallel 
F 2 3 ? parallel      
G 1 2 ? anti-parallel 
G 2 3 ? parallel      
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
H 3 4 ? anti-parallel 
I 1 2 ? anti-parallel 
I 2 3 ? anti-parallel 
I 3 4 ? parallel      
I 4 5 ? parallel      
I 5 6 ? parallel      
I 6 7 ? anti-parallel 
I 7 8 ? parallel      
J 1 2 ? anti-parallel 
J 2 3 ? parallel      
K 1 2 ? anti-parallel 
K 2 3 ? parallel      
L 1 2 ? anti-parallel 
L 2 3 ? anti-parallel 
L 3 4 ? anti-parallel 
M 1 2 ? anti-parallel 
M 2 3 ? anti-parallel 
M 3 4 ? parallel      
M 4 5 ? parallel      
M 5 6 ? parallel      
M 6 7 ? anti-parallel 
M 7 8 ? parallel      
N 1 2 ? anti-parallel 
N 2 3 ? parallel      
O 1 2 ? anti-parallel 
O 2 3 ? parallel      
P 1 2 ? anti-parallel 
P 2 3 ? anti-parallel 
P 3 4 ? 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 
A 1 ALA A 61  ? ARG A 68  ? ALA A 61  ARG A 68  
A 2 ASN A 74  ? ILE A 80  ? ASN A 74  ILE A 80  
A 3 ASP A 136 ? VAL A 140 ? ASP A 136 VAL A 140 
A 4 PRO A 93  ? ILE A 97  ? PRO A 93  ILE A 97  
A 5 LEU A 212 ? HIS A 217 ? LEU A 212 HIS A 217 
A 6 PHE A 300 ? GLU A 305 ? PHE A 300 GLU A 305 
A 7 VAL A 222 ? TYR A 225 ? VAL A 222 TYR A 225 
A 8 ILE A 276 ? ASN A 278 ? ILE A 276 ASN A 278 
B 1 GLU A 373 ? ARG A 376 ? GLU A 373 ARG A 376 
B 2 ILE A 339 ? THR A 344 ? ILE A 339 THR A 344 
B 3 LEU A 410 ? ARG A 411 ? LEU A 410 ARG A 411 
C 1 GLU A 373 ? ARG A 376 ? GLU A 373 ARG A 376 
C 2 ILE A 339 ? THR A 344 ? ILE A 339 THR A 344 
C 3 PHE A 414 ? LYS A 415 ? PHE A 414 LYS A 415 
D 1 MET A 366 ? ARG A 367 ? MET A 366 ARG A 367 
D 2 ASN A 355 ? VAL A 358 ? ASN A 355 VAL A 358 
D 3 GLY A 381 ? SER A 388 ? GLY A 381 SER A 388 
D 4 GLN A 398 ? VAL A 402 ? GLN A 398 VAL A 402 
E 1 ALA B 61  ? ARG B 68  ? ALA B 61  ARG B 68  
E 2 ASN B 74  ? ILE B 80  ? ASN B 74  ILE B 80  
E 3 ASP B 136 ? VAL B 140 ? ASP B 136 VAL B 140 
E 4 PRO B 93  ? ILE B 97  ? PRO B 93  ILE B 97  
E 5 LEU B 212 ? HIS B 217 ? LEU B 212 HIS B 217 
E 6 PHE B 300 ? GLU B 305 ? PHE B 300 GLU B 305 
E 7 VAL B 222 ? TYR B 225 ? VAL B 222 TYR B 225 
E 8 ILE B 276 ? ASN B 278 ? ILE B 276 ASN B 278 
F 1 GLU B 373 ? ARG B 376 ? GLU B 373 ARG B 376 
F 2 ILE B 339 ? THR B 344 ? ILE B 339 THR B 344 
F 3 LEU B 410 ? ARG B 411 ? LEU B 410 ARG B 411 
G 1 GLU B 373 ? ARG B 376 ? GLU B 373 ARG B 376 
G 2 ILE B 339 ? THR B 344 ? ILE B 339 THR B 344 
G 3 PHE B 414 ? LYS B 415 ? PHE B 414 LYS B 415 
H 1 MET B 366 ? ARG B 367 ? MET B 366 ARG B 367 
H 2 ASN B 355 ? VAL B 358 ? ASN B 355 VAL B 358 
H 3 GLY B 381 ? SER B 388 ? GLY B 381 SER B 388 
H 4 GLN B 398 ? VAL B 402 ? GLN B 398 VAL B 402 
I 1 ALA C 61  ? ARG C 68  ? ALA C 61  ARG C 68  
I 2 ASN C 74  ? ILE C 80  ? ASN C 74  ILE C 80  
I 3 ASP C 136 ? VAL C 140 ? ASP C 136 VAL C 140 
I 4 PRO C 93  ? ALA C 98  ? PRO C 93  ALA C 98  
I 5 LEU C 212 ? HIS C 217 ? LEU C 212 HIS C 217 
I 6 PHE C 300 ? GLU C 305 ? PHE C 300 GLU C 305 
I 7 VAL C 222 ? TYR C 225 ? VAL C 222 TYR C 225 
I 8 ILE C 276 ? ASN C 278 ? ILE C 276 ASN C 278 
J 1 GLU C 373 ? ARG C 376 ? GLU C 373 ARG C 376 
J 2 ILE C 339 ? THR C 344 ? ILE C 339 THR C 344 
J 3 LEU C 410 ? ARG C 411 ? LEU C 410 ARG C 411 
K 1 GLU C 373 ? ARG C 376 ? GLU C 373 ARG C 376 
K 2 ILE C 339 ? THR C 344 ? ILE C 339 THR C 344 
K 3 PHE C 414 ? LYS C 415 ? PHE C 414 LYS C 415 
L 1 MET C 366 ? ARG C 367 ? MET C 366 ARG C 367 
L 2 ASN C 355 ? VAL C 358 ? ASN C 355 VAL C 358 
L 3 GLY C 381 ? SER C 388 ? GLY C 381 SER C 388 
L 4 GLN C 398 ? VAL C 402 ? GLN C 398 VAL C 402 
M 1 ALA D 61  ? ARG D 68  ? ALA D 61  ARG D 68  
M 2 ASN D 74  ? ILE D 80  ? ASN D 74  ILE D 80  
M 3 ASP D 136 ? VAL D 140 ? ASP D 136 VAL D 140 
M 4 PRO D 93  ? ALA D 98  ? PRO D 93  ALA D 98  
M 5 LEU D 212 ? HIS D 217 ? LEU D 212 HIS D 217 
M 6 PHE D 300 ? GLU D 305 ? PHE D 300 GLU D 305 
M 7 VAL D 222 ? TYR D 225 ? VAL D 222 TYR D 225 
M 8 ILE D 276 ? ASN D 278 ? ILE D 276 ASN D 278 
N 1 GLU D 373 ? ARG D 376 ? GLU D 373 ARG D 376 
N 2 ILE D 339 ? THR D 344 ? ILE D 339 THR D 344 
N 3 LEU D 410 ? ARG D 411 ? LEU D 410 ARG D 411 
O 1 GLU D 373 ? ARG D 376 ? GLU D 373 ARG D 376 
O 2 ILE D 339 ? THR D 344 ? ILE D 339 THR D 344 
O 3 PHE D 414 ? LYS D 415 ? PHE D 414 LYS D 415 
P 1 MET D 366 ? ARG D 367 ? MET D 366 ARG D 367 
P 2 ASN D 355 ? VAL D 358 ? ASN D 355 VAL D 358 
P 3 GLY D 381 ? SER D 388 ? GLY D 381 SER D 388 
P 4 GLN D 398 ? VAL D 402 ? GLN D 398 VAL D 402 
# 
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 
A 1 2 N GLY A 67  ? N GLY A 67  O LEU A 75  ? O LEU A 75  
A 2 3 N ILE A 80  ? N ILE A 80  O ILE A 137 ? O ILE A 137 
A 3 4 O VAL A 140 ? O VAL A 140 N TYR A 96  ? N TYR A 96  
A 4 5 N ILE A 97  ? N ILE A 97  O ALA A 214 ? O ALA A 214 
A 5 6 N ASN A 215 ? N ASN A 215 O ILE A 304 ? O ILE A 304 
A 6 7 O THR A 303 ? O THR A 303 N SER A 224 ? N SER A 224 
A 7 8 N ALA A 223 ? N ALA A 223 O THR A 277 ? O THR A 277 
B 1 2 O ARG A 376 ? O ARG A 376 N ILE A 339 ? N ILE A 339 
B 2 3 N LYS A 340 ? N LYS A 340 O LEU A 410 ? O LEU A 410 
C 1 2 O ARG A 376 ? O ARG A 376 N ILE A 339 ? N ILE A 339 
C 2 3 N LEU A 342 ? N LEU A 342 O PHE A 414 ? O PHE A 414 
D 1 2 O MET A 366 ? O MET A 366 N VAL A 356 ? N VAL A 356 
D 2 3 N ASN A 355 ? N ASN A 355 O SER A 388 ? O SER A 388 
D 3 4 N VAL A 385 ? N VAL A 385 O GLN A 398 ? O GLN A 398 
E 1 2 N LYS B 62  ? N LYS B 62  O GLN B 79  ? O GLN B 79  
E 2 3 N ILE B 80  ? N ILE B 80  O ILE B 137 ? O ILE B 137 
E 3 4 O VAL B 140 ? O VAL B 140 N TYR B 96  ? N TYR B 96  
E 4 5 N ILE B 97  ? N ILE B 97  O ALA B 214 ? O ALA B 214 
E 5 6 N HIS B 217 ? N HIS B 217 O ILE B 304 ? O ILE B 304 
E 6 7 O THR B 303 ? O THR B 303 N SER B 224 ? N SER B 224 
E 7 8 N ALA B 223 ? N ALA B 223 O THR B 277 ? O THR B 277 
F 1 2 O ARG B 376 ? O ARG B 376 N ILE B 339 ? N ILE B 339 
F 2 3 N LYS B 340 ? N LYS B 340 O LEU B 410 ? O LEU B 410 
G 1 2 O ARG B 376 ? O ARG B 376 N ILE B 339 ? N ILE B 339 
G 2 3 N THR B 344 ? N THR B 344 O PHE B 414 ? O PHE B 414 
H 1 2 O MET B 366 ? O MET B 366 N VAL B 356 ? N VAL B 356 
H 2 3 N TYR B 357 ? N TYR B 357 O HIS B 386 ? O HIS B 386 
H 3 4 N VAL B 385 ? N VAL B 385 O GLN B 398 ? O GLN B 398 
I 1 2 N LYS C 62  ? N LYS C 62  O GLN C 79  ? O GLN C 79  
I 2 3 N ILE C 80  ? N ILE C 80  O ILE C 137 ? O ILE C 137 
I 3 4 O VAL C 140 ? O VAL C 140 N TYR C 96  ? N TYR C 96  
I 4 5 N ILE C 97  ? N ILE C 97  O ALA C 214 ? O ALA C 214 
I 5 6 N HIS C 217 ? N HIS C 217 O ILE C 304 ? O ILE C 304 
I 6 7 O THR C 303 ? O THR C 303 N SER C 224 ? N SER C 224 
I 7 8 N ALA C 223 ? N ALA C 223 O THR C 277 ? O THR C 277 
J 1 2 O ARG C 376 ? O ARG C 376 N ILE C 339 ? N ILE C 339 
J 2 3 N LYS C 340 ? N LYS C 340 O LEU C 410 ? O LEU C 410 
K 1 2 O ARG C 376 ? O ARG C 376 N ILE C 339 ? N ILE C 339 
K 2 3 N LEU C 342 ? N LEU C 342 O PHE C 414 ? O PHE C 414 
L 1 2 O MET C 366 ? O MET C 366 N VAL C 356 ? N VAL C 356 
L 2 3 N ASN C 355 ? N ASN C 355 O SER C 388 ? O SER C 388 
L 3 4 N VAL C 385 ? N VAL C 385 O GLN C 398 ? O GLN C 398 
M 1 2 N LYS D 62  ? N LYS D 62  O GLN D 79  ? O GLN D 79  
M 2 3 N ILE D 80  ? N ILE D 80  O ILE D 137 ? O ILE D 137 
M 3 4 O VAL D 140 ? O VAL D 140 N TYR D 96  ? N TYR D 96  
M 4 5 N ILE D 97  ? N ILE D 97  O ALA D 214 ? O ALA D 214 
M 5 6 N HIS D 217 ? N HIS D 217 O ILE D 304 ? O ILE D 304 
M 6 7 O THR D 303 ? O THR D 303 N SER D 224 ? N SER D 224 
M 7 8 N ALA D 223 ? N ALA D 223 O THR D 277 ? O THR D 277 
N 1 2 O ARG D 376 ? O ARG D 376 N ILE D 339 ? N ILE D 339 
N 2 3 N LYS D 340 ? N LYS D 340 O LEU D 410 ? O LEU D 410 
O 1 2 O ARG D 376 ? O ARG D 376 N ILE D 339 ? N ILE D 339 
O 2 3 N THR D 344 ? N THR D 344 O PHE D 414 ? O PHE D 414 
P 1 2 O MET D 366 ? O MET D 366 N VAL D 356 ? N VAL D 356 
P 2 3 N ASN D 355 ? N ASN D 355 O SER D 388 ? O SER D 388 
P 3 4 N VAL D 385 ? N VAL D 385 O GLN D 398 ? O GLN D 398 
# 
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 ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG A 501' 
AC2 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN A 999'  
AC3 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE GEM A 601' 
AC4 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE GOL A 801' 
AC5 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE GOL A 803' 
AC6 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG B 501' 
AC7 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN B 999'  
AC8 Software ? ? ? ? 14 'BINDING SITE FOR RESIDUE GEM B 601' 
AC9 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG C 501' 
BC1 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN C 999'  
BC2 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE GEM C 601' 
BC3 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE GOL C 804' 
BC4 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG D 501' 
BC5 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN D 999'  
BC6 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE GEM D 601' 
# 
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 3  ARG A 82  ? ARG A 82   . ? 1_555 ? 
2  AC1 3  GLY A 129 ? GLY A 129  . ? 1_555 ? 
3  AC1 3  ASN A 133 ? ASN A 133  . ? 1_555 ? 
4  AC2 4  HIS A 101 ? HIS A 101  . ? 1_555 ? 
5  AC2 4  GLU A 104 ? GLU A 104  . ? 1_555 ? 
6  AC2 4  HIS A 217 ? HIS A 217  . ? 1_555 ? 
7  AC2 4  GEM G .   ? GEM A 601  . ? 1_555 ? 
8  AC3 15 HIS A 101 ? HIS A 101  . ? 1_555 ? 
9  AC3 15 GLU A 104 ? GLU A 104  . ? 1_555 ? 
10 AC3 15 ARG A 165 ? ARG A 165  . ? 1_555 ? 
11 AC3 15 ASN A 174 ? ASN A 174  . ? 1_555 ? 
12 AC3 15 ARG A 175 ? ARG A 175  . ? 1_555 ? 
13 AC3 15 HIS A 217 ? HIS A 217  . ? 1_555 ? 
14 AC3 15 GLY A 218 ? GLY A 218  . ? 1_555 ? 
15 AC3 15 ASP A 228 ? ASP A 228  . ? 1_555 ? 
16 AC3 15 GLY A 279 ? GLY A 279  . ? 1_555 ? 
17 AC3 15 TRP A 282 ? TRP A 282  . ? 1_555 ? 
18 AC3 15 TYR A 283 ? TYR A 283  . ? 1_555 ? 
19 AC3 15 LEU A 285 ? LEU A 285  . ? 1_555 ? 
20 AC3 15 THR A 303 ? THR A 303  . ? 1_555 ? 
21 AC3 15 GLU A 305 ? GLU A 305  . ? 1_555 ? 
22 AC3 15 ZN  F .   ? ZN  A 999  . ? 1_555 ? 
23 AC4 1  ARG A 411 ? ARG A 411  . ? 1_555 ? 
24 AC5 2  GLN A 330 ? GLN A 330  . ? 1_555 ? 
25 AC5 2  GLN D 393 ? GLN D 393  . ? 4_555 ? 
26 AC6 3  ARG B 82  ? ARG B 82   . ? 1_555 ? 
27 AC6 3  GLY B 129 ? GLY B 129  . ? 1_555 ? 
28 AC6 3  ASN B 133 ? ASN B 133  . ? 1_555 ? 
29 AC7 4  HIS B 101 ? HIS B 101  . ? 1_555 ? 
30 AC7 4  GLU B 104 ? GLU B 104  . ? 1_555 ? 
31 AC7 4  HIS B 217 ? HIS B 217  . ? 1_555 ? 
32 AC7 4  GEM M .   ? GEM B 601  . ? 1_555 ? 
33 AC8 14 HIS B 101 ? HIS B 101  . ? 1_555 ? 
34 AC8 14 GLU B 104 ? GLU B 104  . ? 1_555 ? 
35 AC8 14 ARG B 165 ? ARG B 165  . ? 1_555 ? 
36 AC8 14 ASN B 174 ? ASN B 174  . ? 1_555 ? 
37 AC8 14 ARG B 175 ? ARG B 175  . ? 1_555 ? 
38 AC8 14 HIS B 217 ? HIS B 217  . ? 1_555 ? 
39 AC8 14 ASP B 228 ? ASP B 228  . ? 1_555 ? 
40 AC8 14 GLY B 279 ? GLY B 279  . ? 1_555 ? 
41 AC8 14 TRP B 282 ? TRP B 282  . ? 1_555 ? 
42 AC8 14 TYR B 283 ? TYR B 283  . ? 1_555 ? 
43 AC8 14 LEU B 285 ? LEU B 285  . ? 1_555 ? 
44 AC8 14 THR B 303 ? THR B 303  . ? 1_555 ? 
45 AC8 14 GLU B 305 ? GLU B 305  . ? 1_555 ? 
46 AC8 14 ZN  L .   ? ZN  B 999  . ? 1_555 ? 
47 AC9 4  ARG C 82  ? ARG C 82   . ? 1_555 ? 
48 AC9 4  GLY C 129 ? GLY C 129  . ? 1_555 ? 
49 AC9 4  ASN C 133 ? ASN C 133  . ? 1_555 ? 
50 AC9 4  HOH W .   ? HOH C 1051 . ? 1_555 ? 
51 BC1 4  HIS C 101 ? HIS C 101  . ? 1_555 ? 
52 BC1 4  GLU C 104 ? GLU C 104  . ? 1_555 ? 
53 BC1 4  HIS C 217 ? HIS C 217  . ? 1_555 ? 
54 BC1 4  GEM P .   ? GEM C 601  . ? 1_555 ? 
55 BC2 15 HIS C 101 ? HIS C 101  . ? 1_555 ? 
56 BC2 15 GLU C 104 ? GLU C 104  . ? 1_555 ? 
57 BC2 15 ARG C 165 ? ARG C 165  . ? 1_555 ? 
58 BC2 15 ASN C 174 ? ASN C 174  . ? 1_555 ? 
59 BC2 15 ARG C 175 ? ARG C 175  . ? 1_555 ? 
60 BC2 15 HIS C 217 ? HIS C 217  . ? 1_555 ? 
61 BC2 15 GLY C 218 ? GLY C 218  . ? 1_555 ? 
62 BC2 15 ASP C 228 ? ASP C 228  . ? 1_555 ? 
63 BC2 15 GLY C 279 ? GLY C 279  . ? 1_555 ? 
64 BC2 15 TYR C 283 ? TYR C 283  . ? 1_555 ? 
65 BC2 15 LEU C 285 ? LEU C 285  . ? 1_555 ? 
66 BC2 15 THR C 303 ? THR C 303  . ? 1_555 ? 
67 BC2 15 GLU C 305 ? GLU C 305  . ? 1_555 ? 
68 BC2 15 GOL Q .   ? GOL C 804  . ? 1_555 ? 
69 BC2 15 ZN  O .   ? ZN  C 999  . ? 1_555 ? 
70 BC3 4  ARG C 165 ? ARG C 165  . ? 1_555 ? 
71 BC3 4  TRP C 282 ? TRP C 282  . ? 1_555 ? 
72 BC3 4  LYS C 310 ? LYS C 310  . ? 1_555 ? 
73 BC3 4  GEM P .   ? GEM C 601  . ? 1_555 ? 
74 BC4 2  ARG D 82  ? ARG D 82   . ? 1_555 ? 
75 BC4 2  ASN D 133 ? ASN D 133  . ? 1_555 ? 
76 BC5 4  HIS D 101 ? HIS D 101  . ? 1_555 ? 
77 BC5 4  GLU D 104 ? GLU D 104  . ? 1_555 ? 
78 BC5 4  HIS D 217 ? HIS D 217  . ? 1_555 ? 
79 BC5 4  GEM T .   ? GEM D 601  . ? 1_555 ? 
80 BC6 15 HIS D 101 ? HIS D 101  . ? 1_555 ? 
81 BC6 15 GLU D 104 ? GLU D 104  . ? 1_555 ? 
82 BC6 15 ARG D 165 ? ARG D 165  . ? 1_555 ? 
83 BC6 15 ASN D 174 ? ASN D 174  . ? 1_555 ? 
84 BC6 15 ARG D 175 ? ARG D 175  . ? 1_555 ? 
85 BC6 15 HIS D 217 ? HIS D 217  . ? 1_555 ? 
86 BC6 15 GLY D 218 ? GLY D 218  . ? 1_555 ? 
87 BC6 15 SER D 224 ? SER D 224  . ? 1_555 ? 
88 BC6 15 ASP D 228 ? ASP D 228  . ? 1_555 ? 
89 BC6 15 GLY D 279 ? GLY D 279  . ? 1_555 ? 
90 BC6 15 TRP D 282 ? TRP D 282  . ? 1_555 ? 
91 BC6 15 TYR D 283 ? TYR D 283  . ? 1_555 ? 
92 BC6 15 LEU D 285 ? LEU D 285  . ? 1_555 ? 
93 BC6 15 GLU D 305 ? GLU D 305  . ? 1_555 ? 
94 BC6 15 ZN  S .   ? ZN  D 999  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3MN8 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    3MN8 
_atom_sites.fract_transf_matrix[1][1]   0.010307 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007369 
_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]   0.007057 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
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   . LYS A 1 29  ? 36.149  3.408   -19.172 1.00 54.13  ? 29   LYS A N   1 
ATOM   2     C  CA  . LYS A 1 29  ? 34.737  3.038   -19.124 1.00 81.05  ? 29   LYS A CA  1 
ATOM   3     C  C   . LYS A 1 29  ? 34.497  1.527   -19.324 1.00 94.14  ? 29   LYS A C   1 
ATOM   4     O  O   . LYS A 1 29  ? 35.324  0.692   -18.942 1.00 88.11  ? 29   LYS A O   1 
ATOM   5     C  CB  . LYS A 1 29  ? 33.931  3.849   -20.150 1.00 91.72  ? 29   LYS A CB  1 
ATOM   6     C  CG  . LYS A 1 29  ? 32.484  4.139   -19.736 1.00 92.64  ? 29   LYS A CG  1 
ATOM   7     C  CD  . LYS A 1 29  ? 31.627  4.544   -20.930 1.00 91.32  ? 29   LYS A CD  1 
ATOM   8     C  CE  . LYS A 1 29  ? 30.251  5.025   -20.492 1.00 78.94  ? 29   LYS A CE  1 
ATOM   9     N  NZ  . LYS A 1 29  ? 29.277  5.034   -21.622 1.00 67.13  ? 29   LYS A NZ  1 
ATOM   10    N  N   . GLU A 1 30  ? 33.366  1.202   -19.947 1.00 102.97 ? 30   GLU A N   1 
ATOM   11    C  CA  . GLU A 1 30  ? 32.824  -0.163  -20.012 1.00 96.96  ? 30   GLU A CA  1 
ATOM   12    C  C   . GLU A 1 30  ? 33.694  -1.238  -20.698 1.00 73.70  ? 30   GLU A C   1 
ATOM   13    O  O   . GLU A 1 30  ? 34.290  -1.014  -21.750 1.00 56.77  ? 30   GLU A O   1 
ATOM   14    C  CB  . GLU A 1 30  ? 31.442  -0.126  -20.680 1.00 97.20  ? 30   GLU A CB  1 
ATOM   15    C  CG  . GLU A 1 30  ? 30.522  0.968   -20.154 1.00 106.98 ? 30   GLU A CG  1 
ATOM   16    C  CD  . GLU A 1 30  ? 29.318  1.202   -21.055 1.00 117.21 ? 30   GLU A CD  1 
ATOM   17    O  OE1 . GLU A 1 30  ? 29.521  1.560   -22.239 1.00 107.80 ? 30   GLU A OE1 1 
ATOM   18    O  OE2 . GLU A 1 30  ? 28.170  1.035   -20.578 1.00 125.80 ? 30   GLU A OE2 1 
ATOM   19    N  N   . ASP A 1 31  ? 33.738  -2.419  -20.096 1.00 58.02  ? 31   ASP A N   1 
ATOM   20    C  CA  . ASP A 1 31  ? 34.366  -3.570  -20.723 1.00 51.73  ? 31   ASP A CA  1 
ATOM   21    C  C   . ASP A 1 31  ? 33.313  -4.366  -21.511 1.00 68.59  ? 31   ASP A C   1 
ATOM   22    O  O   . ASP A 1 31  ? 32.688  -5.292  -20.987 1.00 70.63  ? 31   ASP A O   1 
ATOM   23    C  CB  . ASP A 1 31  ? 35.035  -4.437  -19.657 1.00 43.72  ? 31   ASP A CB  1 
ATOM   24    C  CG  . ASP A 1 31  ? 35.453  -5.794  -20.182 1.00 56.30  ? 31   ASP A CG  1 
ATOM   25    O  OD1 . ASP A 1 31  ? 35.854  -6.656  -19.363 1.00 56.07  ? 31   ASP A OD1 1 
ATOM   26    O  OD2 . ASP A 1 31  ? 35.373  -6.002  -21.411 1.00 56.06  ? 31   ASP A OD2 1 
ATOM   27    N  N   . GLU A 1 32  ? 33.114  -3.988  -22.770 1.00 68.27  ? 32   GLU A N   1 
ATOM   28    C  CA  . GLU A 1 32  ? 32.178  -4.674  -23.657 1.00 58.20  ? 32   GLU A CA  1 
ATOM   29    C  C   . GLU A 1 32  ? 32.922  -5.459  -24.750 1.00 68.45  ? 32   GLU A C   1 
ATOM   30    O  O   . GLU A 1 32  ? 32.532  -5.439  -25.925 1.00 63.88  ? 32   GLU A O   1 
ATOM   31    C  CB  . GLU A 1 32  ? 31.251  -3.661  -24.328 1.00 50.23  ? 32   GLU A CB  1 
ATOM   32    C  CG  . GLU A 1 32  ? 30.349  -2.888  -23.390 1.00 58.85  ? 32   GLU A CG  1 
ATOM   33    C  CD  . GLU A 1 32  ? 29.502  -1.862  -24.133 1.00 73.27  ? 32   GLU A CD  1 
ATOM   34    O  OE1 . GLU A 1 32  ? 28.335  -2.180  -24.450 1.00 58.08  ? 32   GLU A OE1 1 
ATOM   35    O  OE2 . GLU A 1 32  ? 30.005  -0.746  -24.410 1.00 82.28  ? 32   GLU A OE2 1 
ATOM   36    N  N   . SER A 1 33  ? 33.995  -6.142  -24.363 1.00 59.55  ? 33   SER A N   1 
ATOM   37    C  CA  . SER A 1 33  ? 34.829  -6.858  -25.322 1.00 61.11  ? 33   SER A CA  1 
ATOM   38    C  C   . SER A 1 33  ? 34.050  -7.958  -26.046 1.00 66.61  ? 33   SER A C   1 
ATOM   39    O  O   . SER A 1 33  ? 34.354  -8.303  -27.201 1.00 47.76  ? 33   SER A O   1 
ATOM   40    C  CB  . SER A 1 33  ? 36.051  -7.457  -24.621 1.00 51.86  ? 33   SER A CB  1 
ATOM   41    O  OG  . SER A 1 33  ? 35.675  -8.481  -23.718 1.00 62.55  ? 33   SER A OG  1 
ATOM   42    N  N   . PHE A 1 34  ? 33.042  -8.494  -25.363 1.00 61.05  ? 34   PHE A N   1 
ATOM   43    C  CA  . PHE A 1 34  ? 32.236  -9.582  -25.906 1.00 49.38  ? 34   PHE A CA  1 
ATOM   44    C  C   . PHE A 1 34  ? 31.669  -9.293  -27.296 1.00 57.13  ? 34   PHE A C   1 
ATOM   45    O  O   . PHE A 1 34  ? 31.021  -10.149 -27.891 1.00 78.83  ? 34   PHE A O   1 
ATOM   46    C  CB  . PHE A 1 34  ? 31.124  -10.009 -24.923 1.00 51.23  ? 34   PHE A CB  1 
ATOM   47    C  CG  . PHE A 1 34  ? 30.263  -8.870  -24.397 1.00 49.72  ? 34   PHE A CG  1 
ATOM   48    C  CD1 . PHE A 1 34  ? 29.175  -8.400  -25.121 1.00 46.82  ? 34   PHE A CD1 1 
ATOM   49    C  CD2 . PHE A 1 34  ? 30.514  -8.307  -23.153 1.00 56.93  ? 34   PHE A CD2 1 
ATOM   50    C  CE1 . PHE A 1 34  ? 28.378  -7.373  -24.628 1.00 52.52  ? 34   PHE A CE1 1 
ATOM   51    C  CE2 . PHE A 1 34  ? 29.717  -7.276  -22.651 1.00 46.89  ? 34   PHE A CE2 1 
ATOM   52    C  CZ  . PHE A 1 34  ? 28.651  -6.812  -23.386 1.00 43.95  ? 34   PHE A CZ  1 
ATOM   53    N  N   . LEU A 1 35  ? 31.935  -8.100  -27.818 1.00 62.94  ? 35   LEU A N   1 
ATOM   54    C  CA  . LEU A 1 35  ? 31.446  -7.709  -29.136 1.00 80.51  ? 35   LEU A CA  1 
ATOM   55    C  C   . LEU A 1 35  ? 32.481  -7.902  -30.253 1.00 94.04  ? 35   LEU A C   1 
ATOM   56    O  O   . LEU A 1 35  ? 32.153  -7.779  -31.433 1.00 107.90 ? 35   LEU A O   1 
ATOM   57    C  CB  . LEU A 1 35  ? 31.013  -6.244  -29.113 1.00 84.39  ? 35   LEU A CB  1 
ATOM   58    C  CG  . LEU A 1 35  ? 30.199  -5.793  -27.902 1.00 83.00  ? 35   LEU A CG  1 
ATOM   59    C  CD1 . LEU A 1 35  ? 30.139  -4.266  -27.849 1.00 81.84  ? 35   LEU A CD1 1 
ATOM   60    C  CD2 . LEU A 1 35  ? 28.802  -6.419  -27.913 1.00 76.65  ? 35   LEU A CD2 1 
ATOM   61    N  N   . GLN A 1 36  ? 33.724  -8.201  -29.888 1.00 85.19  ? 36   GLN A N   1 
ATOM   62    C  CA  . GLN A 1 36  ? 34.832  -8.170  -30.847 1.00 74.74  ? 36   GLN A CA  1 
ATOM   63    C  C   . GLN A 1 36  ? 34.827  -9.355  -31.817 1.00 66.79  ? 36   GLN A C   1 
ATOM   64    O  O   . GLN A 1 36  ? 35.803  -9.593  -32.522 1.00 71.22  ? 36   GLN A O   1 
ATOM   65    C  CB  . GLN A 1 36  ? 36.157  -8.134  -30.083 1.00 82.23  ? 36   GLN A CB  1 
ATOM   66    C  CG  . GLN A 1 36  ? 37.384  -7.832  -30.924 1.00 103.24 ? 36   GLN A CG  1 
ATOM   67    C  CD  . GLN A 1 36  ? 37.632  -6.345  -31.064 1.00 119.98 ? 36   GLN A CD  1 
ATOM   68    O  OE1 . GLN A 1 36  ? 38.710  -5.916  -31.492 1.00 106.16 ? 36   GLN A OE1 1 
ATOM   69    N  NE2 . GLN A 1 36  ? 36.632  -5.544  -30.695 1.00 131.36 ? 36   GLN A NE2 1 
ATOM   70    N  N   . GLN A 1 37  ? 33.723  -10.089 -31.851 1.00 60.57  ? 37   GLN A N   1 
ATOM   71    C  CA  . GLN A 1 37  ? 33.676  -11.368 -32.543 1.00 66.59  ? 37   GLN A CA  1 
ATOM   72    C  C   . GLN A 1 37  ? 32.230  -11.857 -32.648 1.00 77.45  ? 37   GLN A C   1 
ATOM   73    O  O   . GLN A 1 37  ? 31.850  -12.859 -32.032 1.00 71.91  ? 37   GLN A O   1 
ATOM   74    C  CB  . GLN A 1 37  ? 34.520  -12.386 -31.774 1.00 70.54  ? 37   GLN A CB  1 
ATOM   75    C  CG  . GLN A 1 37  ? 34.292  -12.391 -30.247 1.00 57.62  ? 37   GLN A CG  1 
ATOM   76    C  CD  . GLN A 1 37  ? 33.380  -13.517 -29.773 1.00 63.94  ? 37   GLN A CD  1 
ATOM   77    O  OE1 . GLN A 1 37  ? 32.157  -13.375 -29.772 1.00 73.35  ? 37   GLN A OE1 1 
ATOM   78    N  NE2 . GLN A 1 37  ? 33.973  -14.634 -29.351 1.00 60.76  ? 37   GLN A NE2 1 
ATOM   79    N  N   . PRO A 1 38  ? 31.413  -11.144 -33.431 1.00 68.89  ? 38   PRO A N   1 
ATOM   80    C  CA  . PRO A 1 38  ? 29.980  -11.441 -33.521 1.00 64.10  ? 38   PRO A CA  1 
ATOM   81    C  C   . PRO A 1 38  ? 29.712  -12.842 -34.063 1.00 64.27  ? 38   PRO A C   1 
ATOM   82    O  O   . PRO A 1 38  ? 30.198  -13.205 -35.136 1.00 75.72  ? 38   PRO A O   1 
ATOM   83    C  CB  . PRO A 1 38  ? 29.462  -10.387 -34.500 1.00 67.93  ? 38   PRO A CB  1 
ATOM   84    C  CG  . PRO A 1 38  ? 30.522  -9.321  -34.530 1.00 76.52  ? 38   PRO A CG  1 
ATOM   85    C  CD  . PRO A 1 38  ? 31.811  -10.033 -34.307 1.00 73.50  ? 38   PRO A CD  1 
ATOM   86    N  N   . HIS A 1 39  ? 28.937  -13.618 -33.316 1.00 56.21  ? 39   HIS A N   1 
ATOM   87    C  CA  . HIS A 1 39  ? 28.619  -14.987 -33.690 1.00 53.70  ? 39   HIS A CA  1 
ATOM   88    C  C   . HIS A 1 39  ? 27.571  -15.561 -32.732 1.00 52.04  ? 39   HIS A C   1 
ATOM   89    O  O   . HIS A 1 39  ? 27.407  -15.081 -31.603 1.00 40.41  ? 39   HIS A O   1 
ATOM   90    C  CB  . HIS A 1 39  ? 29.891  -15.846 -33.695 1.00 46.32  ? 39   HIS A CB  1 
ATOM   91    C  CG  . HIS A 1 39  ? 30.371  -16.231 -32.326 1.00 41.18  ? 39   HIS A CG  1 
ATOM   92    N  ND1 . HIS A 1 39  ? 30.806  -15.307 -31.406 1.00 57.18  ? 39   HIS A ND1 1 
ATOM   93    C  CD2 . HIS A 1 39  ? 30.495  -17.444 -31.741 1.00 45.78  ? 39   HIS A CD2 1 
ATOM   94    C  CE1 . HIS A 1 39  ? 31.170  -15.937 -30.297 1.00 59.37  ? 39   HIS A CE1 1 
ATOM   95    N  NE2 . HIS A 1 39  ? 30.996  -17.228 -30.473 1.00 49.76  ? 39   HIS A NE2 1 
ATOM   96    N  N   . TYR A 1 40  ? 26.851  -16.581 -33.178 1.00 57.58  ? 40   TYR A N   1 
ATOM   97    C  CA  . TYR A 1 40  ? 25.870  -17.215 -32.299 1.00 55.69  ? 40   TYR A CA  1 
ATOM   98    C  C   . TYR A 1 40  ? 26.521  -18.305 -31.457 1.00 48.62  ? 40   TYR A C   1 
ATOM   99    O  O   . TYR A 1 40  ? 27.181  -19.193 -31.991 1.00 59.06  ? 40   TYR A O   1 
ATOM   100   C  CB  . TYR A 1 40  ? 24.675  -17.760 -33.100 1.00 59.12  ? 40   TYR A CB  1 
ATOM   101   C  CG  . TYR A 1 40  ? 23.688  -16.680 -33.518 1.00 59.75  ? 40   TYR A CG  1 
ATOM   102   C  CD1 . TYR A 1 40  ? 23.586  -16.266 -34.841 1.00 63.22  ? 40   TYR A CD1 1 
ATOM   103   C  CD2 . TYR A 1 40  ? 22.875  -16.058 -32.580 1.00 51.53  ? 40   TYR A CD2 1 
ATOM   104   C  CE1 . TYR A 1 40  ? 22.691  -15.273 -35.212 1.00 59.16  ? 40   TYR A CE1 1 
ATOM   105   C  CE2 . TYR A 1 40  ? 21.984  -15.068 -32.946 1.00 47.93  ? 40   TYR A CE2 1 
ATOM   106   C  CZ  . TYR A 1 40  ? 21.896  -14.680 -34.257 1.00 47.26  ? 40   TYR A CZ  1 
ATOM   107   O  OH  . TYR A 1 40  ? 21.010  -13.685 -34.595 1.00 38.78  ? 40   TYR A OH  1 
ATOM   108   N  N   . ALA A 1 41  ? 26.352  -18.229 -30.142 1.00 46.84  ? 41   ALA A N   1 
ATOM   109   C  CA  . ALA A 1 41  ? 26.942  -19.231 -29.255 1.00 45.58  ? 41   ALA A CA  1 
ATOM   110   C  C   . ALA A 1 41  ? 26.168  -20.559 -29.319 1.00 42.16  ? 41   ALA A C   1 
ATOM   111   O  O   . ALA A 1 41  ? 24.948  -20.596 -29.155 1.00 26.98  ? 41   ALA A O   1 
ATOM   112   C  CB  . ALA A 1 41  ? 27.016  -18.710 -27.831 1.00 37.28  ? 41   ALA A CB  1 
ATOM   113   N  N   . SER A 1 42  ? 26.896  -21.643 -29.577 1.00 50.58  ? 42   SER A N   1 
ATOM   114   C  CA  . SER A 1 42  ? 26.286  -22.968 -29.651 1.00 47.01  ? 42   SER A CA  1 
ATOM   115   C  C   . SER A 1 42  ? 25.980  -23.486 -28.254 1.00 45.38  ? 42   SER A C   1 
ATOM   116   O  O   . SER A 1 42  ? 26.372  -22.881 -27.262 1.00 54.95  ? 42   SER A O   1 
ATOM   117   C  CB  . SER A 1 42  ? 27.215  -23.952 -30.372 1.00 44.02  ? 42   SER A CB  1 
ATOM   118   O  OG  . SER A 1 42  ? 28.350  -24.268 -29.580 1.00 44.74  ? 42   SER A OG  1 
ATOM   119   N  N   . GLN A 1 43  ? 25.289  -24.613 -28.174 1.00 37.87  ? 43   GLN A N   1 
ATOM   120   C  CA  . GLN A 1 43  ? 25.080  -25.260 -26.889 1.00 31.13  ? 43   GLN A CA  1 
ATOM   121   C  C   . GLN A 1 43  ? 26.413  -25.459 -26.180 1.00 40.56  ? 43   GLN A C   1 
ATOM   122   O  O   . GLN A 1 43  ? 26.554  -25.071 -25.030 1.00 33.28  ? 43   GLN A O   1 
ATOM   123   C  CB  . GLN A 1 43  ? 24.384  -26.607 -27.066 1.00 43.76  ? 43   GLN A CB  1 
ATOM   124   C  CG  . GLN A 1 43  ? 24.004  -27.276 -25.762 1.00 49.72  ? 43   GLN A CG  1 
ATOM   125   C  CD  . GLN A 1 43  ? 23.024  -26.444 -24.935 1.00 57.67  ? 43   GLN A CD  1 
ATOM   126   O  OE1 . GLN A 1 43  ? 22.240  -25.651 -25.470 1.00 59.91  ? 43   GLN A OE1 1 
ATOM   127   N  NE2 . GLN A 1 43  ? 23.059  -26.635 -23.619 1.00 61.79  ? 43   GLN A NE2 1 
ATOM   128   N  N   . GLU A 1 44  ? 27.397  -26.052 -26.858 1.00 46.49  ? 44   GLU A N   1 
ATOM   129   C  CA  . GLU A 1 44  ? 28.701  -26.246 -26.226 1.00 48.56  ? 44   GLU A CA  1 
ATOM   130   C  C   . GLU A 1 44  ? 29.317  -24.907 -25.810 1.00 44.37  ? 44   GLU A C   1 
ATOM   131   O  O   . GLU A 1 44  ? 29.843  -24.773 -24.709 1.00 48.91  ? 44   GLU A O   1 
ATOM   132   C  CB  . GLU A 1 44  ? 29.676  -27.015 -27.125 1.00 52.11  ? 44   GLU A CB  1 
ATOM   133   C  CG  . GLU A 1 44  ? 30.948  -27.448 -26.386 1.00 74.89  ? 44   GLU A CG  1 
ATOM   134   C  CD  . GLU A 1 44  ? 32.176  -27.566 -27.281 1.00 95.50  ? 44   GLU A CD  1 
ATOM   135   O  OE1 . GLU A 1 44  ? 32.034  -27.472 -28.521 1.00 101.74 ? 44   GLU A OE1 1 
ATOM   136   O  OE2 . GLU A 1 44  ? 33.289  -27.753 -26.737 1.00 99.29  ? 44   GLU A OE2 1 
ATOM   137   N  N   . GLN A 1 45  ? 29.246  -23.915 -26.692 1.00 43.84  ? 45   GLN A N   1 
ATOM   138   C  CA  . GLN A 1 45  ? 29.833  -22.610 -26.405 1.00 41.87  ? 45   GLN A CA  1 
ATOM   139   C  C   . GLN A 1 45  ? 29.183  -21.937 -25.213 1.00 40.39  ? 45   GLN A C   1 
ATOM   140   O  O   . GLN A 1 45  ? 29.834  -21.191 -24.480 1.00 46.61  ? 45   GLN A O   1 
ATOM   141   C  CB  . GLN A 1 45  ? 29.769  -21.703 -27.629 1.00 40.98  ? 45   GLN A CB  1 
ATOM   142   C  CG  . GLN A 1 45  ? 30.707  -22.170 -28.739 1.00 49.92  ? 45   GLN A CG  1 
ATOM   143   C  CD  . GLN A 1 45  ? 31.073  -21.065 -29.697 1.00 52.02  ? 45   GLN A CD  1 
ATOM   144   O  OE1 . GLN A 1 45  ? 30.214  -20.519 -30.383 1.00 54.31  ? 45   GLN A OE1 1 
ATOM   145   N  NE2 . GLN A 1 45  ? 32.353  -20.727 -29.751 1.00 54.47  ? 45   GLN A NE2 1 
ATOM   146   N  N   . LEU A 1 46  ? 27.899  -22.217 -25.018 1.00 32.37  ? 46   LEU A N   1 
ATOM   147   C  CA  . LEU A 1 46  ? 27.140  -21.654 -23.899 1.00 42.73  ? 46   LEU A CA  1 
ATOM   148   C  C   . LEU A 1 46  ? 27.498  -22.282 -22.541 1.00 38.50  ? 46   LEU A C   1 
ATOM   149   O  O   . LEU A 1 46  ? 27.763  -21.580 -21.574 1.00 27.40  ? 46   LEU A O   1 
ATOM   150   C  CB  . LEU A 1 46  ? 25.636  -21.786 -24.169 1.00 42.85  ? 46   LEU A CB  1 
ATOM   151   C  CG  . LEU A 1 46  ? 24.697  -21.475 -23.004 1.00 38.15  ? 46   LEU A CG  1 
ATOM   152   C  CD1 . LEU A 1 46  ? 24.971  -20.070 -22.478 1.00 47.22  ? 46   LEU A CD1 1 
ATOM   153   C  CD2 . LEU A 1 46  ? 23.243  -21.634 -23.425 1.00 22.77  ? 46   LEU A CD2 1 
ATOM   154   N  N   . GLU A 1 47  ? 27.497  -23.608 -22.484 1.00 38.36  ? 47   GLU A N   1 
ATOM   155   C  CA  . GLU A 1 47  ? 27.876  -24.327 -21.280 1.00 45.70  ? 47   GLU A CA  1 
ATOM   156   C  C   . GLU A 1 47  ? 29.289  -23.929 -20.887 1.00 53.14  ? 47   GLU A C   1 
ATOM   157   O  O   . GLU A 1 47  ? 29.566  -23.649 -19.712 1.00 53.80  ? 47   GLU A O   1 
ATOM   158   C  CB  . GLU A 1 47  ? 27.777  -25.843 -21.503 1.00 33.82  ? 47   GLU A CB  1 
ATOM   159   C  CG  . GLU A 1 47  ? 26.349  -26.348 -21.719 1.00 32.66  ? 47   GLU A CG  1 
ATOM   160   C  CD  . GLU A 1 47  ? 26.299  -27.807 -22.128 1.00 47.22  ? 47   GLU A CD  1 
ATOM   161   O  OE1 . GLU A 1 47  ? 27.330  -28.320 -22.618 1.00 61.38  ? 47   GLU A OE1 1 
ATOM   162   O  OE2 . GLU A 1 47  ? 25.234  -28.443 -21.973 1.00 48.70  ? 47   GLU A OE2 1 
ATOM   163   N  N   . ASP A 1 48  ? 30.173  -23.883 -21.884 1.00 50.30  ? 48   ASP A N   1 
ATOM   164   C  CA  . ASP A 1 48  ? 31.565  -23.505 -21.668 1.00 55.56  ? 48   ASP A CA  1 
ATOM   165   C  C   . ASP A 1 48  ? 31.686  -22.104 -21.063 1.00 49.99  ? 48   ASP A C   1 
ATOM   166   O  O   . ASP A 1 48  ? 32.468  -21.887 -20.128 1.00 47.35  ? 48   ASP A O   1 
ATOM   167   C  CB  . ASP A 1 48  ? 32.372  -23.609 -22.969 1.00 56.37  ? 48   ASP A CB  1 
ATOM   168   C  CG  . ASP A 1 48  ? 32.591  -25.053 -23.417 1.00 71.30  ? 48   ASP A CG  1 
ATOM   169   O  OD1 . ASP A 1 48  ? 32.470  -25.978 -22.579 1.00 71.93  ? 48   ASP A OD1 1 
ATOM   170   O  OD2 . ASP A 1 48  ? 32.898  -25.261 -24.616 1.00 78.26  ? 48   ASP A OD2 1 
ATOM   171   N  N   . LEU A 1 49  ? 30.904  -21.157 -21.575 1.00 38.39  ? 49   LEU A N   1 
ATOM   172   C  CA  . LEU A 1 49  ? 31.016  -19.783 -21.097 1.00 44.54  ? 49   LEU A CA  1 
ATOM   173   C  C   . LEU A 1 49  ? 30.470  -19.603 -19.681 1.00 43.92  ? 49   LEU A C   1 
ATOM   174   O  O   . LEU A 1 49  ? 31.008  -18.806 -18.889 1.00 46.14  ? 49   LEU A O   1 
ATOM   175   C  CB  . LEU A 1 49  ? 30.346  -18.801 -22.054 1.00 49.59  ? 49   LEU A CB  1 
ATOM   176   C  CG  . LEU A 1 49  ? 30.664  -17.342 -21.712 1.00 47.73  ? 49   LEU A CG  1 
ATOM   177   C  CD1 . LEU A 1 49  ? 30.828  -16.517 -22.982 1.00 68.14  ? 49   LEU A CD1 1 
ATOM   178   C  CD2 . LEU A 1 49  ? 29.607  -16.751 -20.802 1.00 35.79  ? 49   LEU A CD2 1 
ATOM   179   N  N   . PHE A 1 50  ? 29.406  -20.345 -19.374 1.00 29.56  ? 50   PHE A N   1 
ATOM   180   C  CA  . PHE A 1 50  ? 28.782  -20.309 -18.058 1.00 30.38  ? 50   PHE A CA  1 
ATOM   181   C  C   . PHE A 1 50  ? 29.656  -20.921 -16.978 1.00 41.90  ? 50   PHE A C   1 
ATOM   182   O  O   . PHE A 1 50  ? 29.626  -20.479 -15.836 1.00 62.63  ? 50   PHE A O   1 
ATOM   183   C  CB  . PHE A 1 50  ? 27.437  -21.021 -18.082 1.00 41.37  ? 50   PHE A CB  1 
ATOM   184   C  CG  . PHE A 1 50  ? 26.294  -20.130 -18.454 1.00 36.27  ? 50   PHE A CG  1 
ATOM   185   C  CD1 . PHE A 1 50  ? 26.530  -18.861 -18.961 1.00 34.37  ? 50   PHE A CD1 1 
ATOM   186   C  CD2 . PHE A 1 50  ? 24.987  -20.558 -18.298 1.00 22.02  ? 50   PHE A CD2 1 
ATOM   187   C  CE1 . PHE A 1 50  ? 25.476  -18.036 -19.299 1.00 33.68  ? 50   PHE A CE1 1 
ATOM   188   C  CE2 . PHE A 1 50  ? 23.928  -19.741 -18.635 1.00 24.53  ? 50   PHE A CE2 1 
ATOM   189   C  CZ  . PHE A 1 50  ? 24.169  -18.482 -19.135 1.00 34.13  ? 50   PHE A CZ  1 
ATOM   190   N  N   . ALA A 1 51  ? 30.424  -21.944 -17.329 1.00 39.65  ? 51   ALA A N   1 
ATOM   191   C  CA  . ALA A 1 51  ? 31.377  -22.518 -16.384 1.00 45.38  ? 51   ALA A CA  1 
ATOM   192   C  C   . ALA A 1 51  ? 32.528  -21.544 -16.126 1.00 53.26  ? 51   ALA A C   1 
ATOM   193   O  O   . ALA A 1 51  ? 33.012  -21.422 -14.998 1.00 58.52  ? 51   ALA A O   1 
ATOM   194   C  CB  . ALA A 1 51  ? 31.903  -23.863 -16.896 1.00 31.10  ? 51   ALA A CB  1 
ATOM   195   N  N   . GLY A 1 52  ? 32.954  -20.849 -17.178 1.00 54.10  ? 52   GLY A N   1 
ATOM   196   C  CA  . GLY A 1 52  ? 34.079  -19.934 -17.076 1.00 53.75  ? 52   GLY A CA  1 
ATOM   197   C  C   . GLY A 1 52  ? 33.765  -18.789 -16.138 1.00 49.95  ? 52   GLY A C   1 
ATOM   198   O  O   . GLY A 1 52  ? 34.583  -18.386 -15.303 1.00 34.84  ? 52   GLY A O   1 
ATOM   199   N  N   . LEU A 1 53  ? 32.559  -18.263 -16.291 1.00 48.07  ? 53   LEU A N   1 
ATOM   200   C  CA  . LEU A 1 53  ? 32.094  -17.174 -15.453 1.00 53.08  ? 53   LEU A CA  1 
ATOM   201   C  C   . LEU A 1 53  ? 32.071  -17.595 -13.992 1.00 48.80  ? 53   LEU A C   1 
ATOM   202   O  O   . LEU A 1 53  ? 32.385  -16.806 -13.101 1.00 53.94  ? 53   LEU A O   1 
ATOM   203   C  CB  . LEU A 1 53  ? 30.698  -16.759 -15.907 1.00 44.26  ? 53   LEU A CB  1 
ATOM   204   C  CG  . LEU A 1 53  ? 30.635  -15.587 -16.893 1.00 54.91  ? 53   LEU A CG  1 
ATOM   205   C  CD1 . LEU A 1 53  ? 31.884  -15.412 -17.748 1.00 48.93  ? 53   LEU A CD1 1 
ATOM   206   C  CD2 . LEU A 1 53  ? 29.390  -15.622 -17.753 1.00 65.11  ? 53   LEU A CD2 1 
ATOM   207   N  N   . GLU A 1 54  ? 31.711  -18.852 -13.759 1.00 45.28  ? 54   GLU A N   1 
ATOM   208   C  CA  . GLU A 1 54  ? 31.552  -19.368 -12.406 1.00 58.99  ? 54   GLU A CA  1 
ATOM   209   C  C   . GLU A 1 54  ? 32.896  -19.407 -11.687 1.00 64.82  ? 54   GLU A C   1 
ATOM   210   O  O   . GLU A 1 54  ? 32.997  -19.088 -10.493 1.00 57.51  ? 54   GLU A O   1 
ATOM   211   C  CB  . GLU A 1 54  ? 30.917  -20.758 -12.441 1.00 67.61  ? 54   GLU A CB  1 
ATOM   212   C  CG  . GLU A 1 54  ? 30.265  -21.172 -11.137 1.00 76.40  ? 54   GLU A CG  1 
ATOM   213   C  CD  . GLU A 1 54  ? 29.390  -22.401 -11.290 1.00 76.35  ? 54   GLU A CD  1 
ATOM   214   O  OE1 . GLU A 1 54  ? 28.740  -22.775 -10.291 1.00 81.55  ? 54   GLU A OE1 1 
ATOM   215   O  OE2 . GLU A 1 54  ? 29.353  -22.986 -12.402 1.00 65.15  ? 54   GLU A OE2 1 
ATOM   216   N  N   . LYS A 1 55  ? 33.932  -19.787 -12.427 1.00 65.49  ? 55   LYS A N   1 
ATOM   217   C  CA  . LYS A 1 55  ? 35.278  -19.811 -11.874 1.00 61.80  ? 55   LYS A CA  1 
ATOM   218   C  C   . LYS A 1 55  ? 35.942  -18.435 -11.964 1.00 50.31  ? 55   LYS A C   1 
ATOM   219   O  O   . LYS A 1 55  ? 36.642  -18.004 -11.046 1.00 43.85  ? 55   LYS A O   1 
ATOM   220   C  CB  . LYS A 1 55  ? 36.134  -20.892 -12.543 1.00 55.43  ? 55   LYS A CB  1 
ATOM   221   C  CG  . LYS A 1 55  ? 36.119  -20.893 -14.053 1.00 53.85  ? 55   LYS A CG  1 
ATOM   222   C  CD  . LYS A 1 55  ? 37.079  -21.964 -14.585 1.00 63.63  ? 55   LYS A CD  1 
ATOM   223   C  CE  . LYS A 1 55  ? 38.531  -21.676 -14.177 1.00 67.99  ? 55   LYS A CE  1 
ATOM   224   N  NZ  . LYS A 1 55  ? 39.530  -22.639 -14.753 1.00 64.31  ? 55   LYS A NZ  1 
ATOM   225   N  N   . ALA A 1 56  ? 35.712  -17.745 -13.070 1.00 36.69  ? 56   ALA A N   1 
ATOM   226   C  CA  . ALA A 1 56  ? 36.139  -16.363 -13.177 1.00 44.89  ? 56   ALA A CA  1 
ATOM   227   C  C   . ALA A 1 56  ? 35.573  -15.523 -12.017 1.00 45.94  ? 56   ALA A C   1 
ATOM   228   O  O   . ALA A 1 56  ? 36.263  -14.654 -11.476 1.00 45.12  ? 56   ALA A O   1 
ATOM   229   C  CB  . ALA A 1 56  ? 35.723  -15.778 -14.533 1.00 30.44  ? 56   ALA A CB  1 
ATOM   230   N  N   . TYR A 1 57  ? 34.322  -15.785 -11.640 1.00 38.55  ? 57   TYR A N   1 
ATOM   231   C  CA  . TYR A 1 57  ? 33.649  -14.986 -10.620 1.00 42.41  ? 57   TYR A CA  1 
ATOM   232   C  C   . TYR A 1 57  ? 33.033  -15.860 -9.542  1.00 39.84  ? 57   TYR A C   1 
ATOM   233   O  O   . TYR A 1 57  ? 31.824  -15.972 -9.468  1.00 51.99  ? 57   TYR A O   1 
ATOM   234   C  CB  . TYR A 1 57  ? 32.563  -14.129 -11.257 1.00 31.19  ? 57   TYR A CB  1 
ATOM   235   C  CG  . TYR A 1 57  ? 33.062  -13.201 -12.337 1.00 49.02  ? 57   TYR A CG  1 
ATOM   236   C  CD1 . TYR A 1 57  ? 33.131  -13.623 -13.667 1.00 61.24  ? 57   TYR A CD1 1 
ATOM   237   C  CD2 . TYR A 1 57  ? 33.454  -11.897 -12.039 1.00 38.41  ? 57   TYR A CD2 1 
ATOM   238   C  CE1 . TYR A 1 57  ? 33.587  -12.770 -14.678 1.00 58.21  ? 57   TYR A CE1 1 
ATOM   239   C  CE2 . TYR A 1 57  ? 33.908  -11.032 -13.036 1.00 40.83  ? 57   TYR A CE2 1 
ATOM   240   C  CZ  . TYR A 1 57  ? 33.973  -11.471 -14.356 1.00 54.94  ? 57   TYR A CZ  1 
ATOM   241   O  OH  . TYR A 1 57  ? 34.425  -10.612 -15.344 1.00 46.73  ? 57   TYR A OH  1 
ATOM   242   N  N   . PRO A 1 58  ? 33.873  -16.468 -8.695  1.00 41.27  ? 58   PRO A N   1 
ATOM   243   C  CA  . PRO A 1 58  ? 33.491  -17.504 -7.728  1.00 40.97  ? 58   PRO A CA  1 
ATOM   244   C  C   . PRO A 1 58  ? 32.286  -17.150 -6.865  1.00 50.95  ? 58   PRO A C   1 
ATOM   245   O  O   . PRO A 1 58  ? 31.453  -18.024 -6.631  1.00 63.33  ? 58   PRO A O   1 
ATOM   246   C  CB  . PRO A 1 58  ? 34.736  -17.628 -6.844  1.00 39.06  ? 58   PRO A CB  1 
ATOM   247   C  CG  . PRO A 1 58  ? 35.854  -17.246 -7.733  1.00 34.36  ? 58   PRO A CG  1 
ATOM   248   C  CD  . PRO A 1 58  ? 35.318  -16.184 -8.654  1.00 33.14  ? 58   PRO A CD  1 
ATOM   249   N  N   . ASN A 1 59  ? 32.188  -15.906 -6.406  1.00 53.40  ? 59   ASN A N   1 
ATOM   250   C  CA  . ASN A 1 59  ? 31.165  -15.561 -5.412  1.00 66.38  ? 59   ASN A CA  1 
ATOM   251   C  C   . ASN A 1 59  ? 29.867  -14.957 -5.969  1.00 52.93  ? 59   ASN A C   1 
ATOM   252   O  O   . ASN A 1 59  ? 28.889  -14.776 -5.236  1.00 31.60  ? 59   ASN A O   1 
ATOM   253   C  CB  . ASN A 1 59  ? 31.749  -14.636 -4.339  1.00 71.84  ? 59   ASN A CB  1 
ATOM   254   C  CG  . ASN A 1 59  ? 33.034  -15.178 -3.732  1.00 77.51  ? 59   ASN A CG  1 
ATOM   255   O  OD1 . ASN A 1 59  ? 33.743  -15.971 -4.349  1.00 75.41  ? 59   ASN A OD1 1 
ATOM   256   N  ND2 . ASN A 1 59  ? 33.346  -14.737 -2.518  1.00 79.37  ? 59   ASN A ND2 1 
ATOM   257   N  N   . GLN A 1 60  ? 29.853  -14.666 -7.265  1.00 38.69  ? 60   GLN A N   1 
ATOM   258   C  CA  . GLN A 1 60  ? 28.758  -13.903 -7.840  1.00 39.63  ? 60   GLN A CA  1 
ATOM   259   C  C   . GLN A 1 60  ? 28.107  -14.584 -9.039  1.00 40.11  ? 60   GLN A C   1 
ATOM   260   O  O   . GLN A 1 60  ? 26.975  -14.273 -9.408  1.00 46.83  ? 60   GLN A O   1 
ATOM   261   C  CB  . GLN A 1 60  ? 29.254  -12.510 -8.205  1.00 42.45  ? 60   GLN A CB  1 
ATOM   262   C  CG  . GLN A 1 60  ? 30.709  -12.297 -7.814  1.00 62.29  ? 60   GLN A CG  1 
ATOM   263   C  CD  . GLN A 1 60  ? 30.960  -10.900 -7.309  1.00 68.66  ? 60   GLN A CD  1 
ATOM   264   O  OE1 . GLN A 1 60  ? 32.087  -10.387 -7.372  1.00 61.85  ? 60   GLN A OE1 1 
ATOM   265   N  NE2 . GLN A 1 60  ? 29.902  -10.266 -6.805  1.00 60.39  ? 60   GLN A NE2 1 
ATOM   266   N  N   . ALA A 1 61  ? 28.815  -15.521 -9.646  1.00 32.37  ? 61   ALA A N   1 
ATOM   267   C  CA  . ALA A 1 61  ? 28.235  -16.298 -10.731 1.00 36.27  ? 61   ALA A CA  1 
ATOM   268   C  C   . ALA A 1 61  ? 28.109  -17.751 -10.314 1.00 35.94  ? 61   ALA A C   1 
ATOM   269   O  O   . ALA A 1 61  ? 29.075  -18.347 -9.819  1.00 36.42  ? 61   ALA A O   1 
ATOM   270   C  CB  . ALA A 1 61  ? 29.071  -16.178 -11.987 1.00 43.33  ? 61   ALA A CB  1 
ATOM   271   N  N   . LYS A 1 62  ? 26.910  -18.302 -10.509 1.00 35.02  ? 62   LYS A N   1 
ATOM   272   C  CA  . LYS A 1 62  ? 26.618  -19.699 -10.196 1.00 30.39  ? 62   LYS A CA  1 
ATOM   273   C  C   . LYS A 1 62  ? 25.714  -20.309 -11.251 1.00 28.39  ? 62   LYS A C   1 
ATOM   274   O  O   . LYS A 1 62  ? 24.742  -19.690 -11.669 1.00 46.87  ? 62   LYS A O   1 
ATOM   275   C  CB  . LYS A 1 62  ? 25.953  -19.813 -8.824  1.00 30.47  ? 62   LYS A CB  1 
ATOM   276   C  CG  . LYS A 1 62  ? 25.598  -21.241 -8.425  1.00 30.64  ? 62   LYS A CG  1 
ATOM   277   C  CD  . LYS A 1 62  ? 25.119  -21.287 -6.981  1.00 54.70  ? 62   LYS A CD  1 
ATOM   278   C  CE  . LYS A 1 62  ? 24.643  -22.672 -6.599  1.00 69.86  ? 62   LYS A CE  1 
ATOM   279   N  NZ  . LYS A 1 62  ? 25.672  -23.704 -6.888  1.00 80.84  ? 62   LYS A NZ  1 
ATOM   280   N  N   . VAL A 1 63  ? 26.041  -21.522 -11.685 1.00 34.91  ? 63   VAL A N   1 
ATOM   281   C  CA  . VAL A 1 63  ? 25.248  -22.207 -12.696 1.00 29.54  ? 63   VAL A CA  1 
ATOM   282   C  C   . VAL A 1 63  ? 24.241  -23.137 -12.060 1.00 36.36  ? 63   VAL A C   1 
ATOM   283   O  O   . VAL A 1 63  ? 24.566  -23.873 -11.132 1.00 43.80  ? 63   VAL A O   1 
ATOM   284   C  CB  . VAL A 1 63  ? 26.115  -23.038 -13.636 1.00 32.11  ? 63   VAL A CB  1 
ATOM   285   C  CG1 . VAL A 1 63  ? 25.241  -23.921 -14.497 1.00 24.81  ? 63   VAL A CG1 1 
ATOM   286   C  CG2 . VAL A 1 63  ? 26.991  -22.129 -14.500 1.00 45.17  ? 63   VAL A CG2 1 
ATOM   287   N  N   . HIS A 1 64  ? 23.024  -23.103 -12.590 1.00 38.10  ? 64   HIS A N   1 
ATOM   288   C  CA  . HIS A 1 64  ? 21.928  -23.933 -12.124 1.00 28.92  ? 64   HIS A CA  1 
ATOM   289   C  C   . HIS A 1 64  ? 21.409  -24.819 -13.245 1.00 32.63  ? 64   HIS A C   1 
ATOM   290   O  O   . HIS A 1 64  ? 21.174  -24.346 -14.364 1.00 24.23  ? 64   HIS A O   1 
ATOM   291   C  CB  . HIS A 1 64  ? 20.810  -23.043 -11.608 1.00 22.95  ? 64   HIS A CB  1 
ATOM   292   C  CG  . HIS A 1 64  ? 21.240  -22.153 -10.487 1.00 39.46  ? 64   HIS A CG  1 
ATOM   293   N  ND1 . HIS A 1 64  ? 21.168  -22.539 -9.165  1.00 43.38  ? 64   HIS A ND1 1 
ATOM   294   C  CD2 . HIS A 1 64  ? 21.781  -20.913 -10.492 1.00 39.20  ? 64   HIS A CD2 1 
ATOM   295   C  CE1 . HIS A 1 64  ? 21.630  -21.566 -8.402  1.00 41.58  ? 64   HIS A CE1 1 
ATOM   296   N  NE2 . HIS A 1 64  ? 22.005  -20.567 -9.182  1.00 43.02  ? 64   HIS A NE2 1 
ATOM   297   N  N   . PHE A 1 65  ? 21.248  -26.105 -12.935 1.00 35.57  ? 65   PHE A N   1 
ATOM   298   C  CA  . PHE A 1 65  ? 20.683  -27.085 -13.864 1.00 34.67  ? 65   PHE A CA  1 
ATOM   299   C  C   . PHE A 1 65  ? 19.177  -27.169 -13.634 1.00 35.89  ? 65   PHE A C   1 
ATOM   300   O  O   . PHE A 1 65  ? 18.731  -27.416 -12.509 1.00 39.35  ? 65   PHE A O   1 
ATOM   301   C  CB  . PHE A 1 65  ? 21.345  -28.446 -13.636 1.00 33.72  ? 65   PHE A CB  1 
ATOM   302   C  CG  . PHE A 1 65  ? 20.668  -29.594 -14.335 1.00 37.65  ? 65   PHE A CG  1 
ATOM   303   C  CD1 . PHE A 1 65  ? 19.684  -30.333 -13.698 1.00 42.21  ? 65   PHE A CD1 1 
ATOM   304   C  CD2 . PHE A 1 65  ? 21.038  -29.954 -15.616 1.00 45.07  ? 65   PHE A CD2 1 
ATOM   305   C  CE1 . PHE A 1 65  ? 19.068  -31.392 -14.336 1.00 51.23  ? 65   PHE A CE1 1 
ATOM   306   C  CE2 . PHE A 1 65  ? 20.432  -31.017 -16.256 1.00 52.74  ? 65   PHE A CE2 1 
ATOM   307   C  CZ  . PHE A 1 65  ? 19.443  -31.735 -15.616 1.00 59.29  ? 65   PHE A CZ  1 
ATOM   308   N  N   . LEU A 1 66  ? 18.401  -26.940 -14.691 1.00 33.29  ? 66   LEU A N   1 
ATOM   309   C  CA  . LEU A 1 66  ? 16.942  -26.924 -14.599 1.00 22.25  ? 66   LEU A CA  1 
ATOM   310   C  C   . LEU A 1 66  ? 16.387  -28.227 -15.146 1.00 35.97  ? 66   LEU A C   1 
ATOM   311   O  O   . LEU A 1 66  ? 15.331  -28.697 -14.722 1.00 50.43  ? 66   LEU A O   1 
ATOM   312   C  CB  . LEU A 1 66  ? 16.369  -25.757 -15.395 1.00 21.67  ? 66   LEU A CB  1 
ATOM   313   C  CG  . LEU A 1 66  ? 16.953  -24.374 -15.099 1.00 24.05  ? 66   LEU A CG  1 
ATOM   314   C  CD1 . LEU A 1 66  ? 16.162  -23.314 -15.817 1.00 26.39  ? 66   LEU A CD1 1 
ATOM   315   C  CD2 . LEU A 1 66  ? 16.937  -24.097 -13.623 1.00 21.34  ? 66   LEU A CD2 1 
ATOM   316   N  N   . GLY A 1 67  ? 17.101  -28.812 -16.097 1.00 28.56  ? 67   GLY A N   1 
ATOM   317   C  CA  . GLY A 1 67  ? 16.686  -30.080 -16.647 1.00 39.16  ? 67   GLY A CA  1 
ATOM   318   C  C   . GLY A 1 67  ? 17.293  -30.275 -18.012 1.00 42.10  ? 67   GLY A C   1 
ATOM   319   O  O   . GLY A 1 67  ? 18.178  -29.527 -18.413 1.00 38.71  ? 67   GLY A O   1 
ATOM   320   N  N   . ARG A 1 68  ? 16.806  -31.276 -18.735 1.00 41.45  ? 68   ARG A N   1 
ATOM   321   C  CA  . ARG A 1 68  ? 17.344  -31.577 -20.042 1.00 33.70  ? 68   ARG A CA  1 
ATOM   322   C  C   . ARG A 1 68  ? 16.246  -31.641 -21.110 1.00 42.10  ? 68   ARG A C   1 
ATOM   323   O  O   . ARG A 1 68  ? 15.080  -31.908 -20.807 1.00 37.13  ? 68   ARG A O   1 
ATOM   324   C  CB  . ARG A 1 68  ? 18.149  -32.872 -19.978 1.00 26.93  ? 68   ARG A CB  1 
ATOM   325   C  CG  . ARG A 1 68  ? 19.654  -32.672 -19.849 1.00 26.35  ? 68   ARG A CG  1 
ATOM   326   C  CD  . ARG A 1 68  ? 20.291  -33.893 -19.211 1.00 40.20  ? 68   ARG A CD  1 
ATOM   327   N  NE  . ARG A 1 68  ? 21.748  -33.842 -19.248 1.00 48.56  ? 68   ARG A NE  1 
ATOM   328   C  CZ  . ARG A 1 68  ? 22.542  -34.228 -18.253 1.00 60.19  ? 68   ARG A CZ  1 
ATOM   329   N  NH1 . ARG A 1 68  ? 22.029  -34.694 -17.122 1.00 65.87  ? 68   ARG A NH1 1 
ATOM   330   N  NH2 . ARG A 1 68  ? 23.855  -34.144 -18.392 1.00 73.83  ? 68   ARG A NH2 1 
ATOM   331   N  N   . SER A 1 69  ? 16.636  -31.370 -22.356 1.00 39.55  ? 69   SER A N   1 
ATOM   332   C  CA  . SER A 1 69  ? 15.731  -31.406 -23.490 1.00 17.64  ? 69   SER A CA  1 
ATOM   333   C  C   . SER A 1 69  ? 15.521  -32.851 -23.934 1.00 37.31  ? 69   SER A C   1 
ATOM   334   O  O   . SER A 1 69  ? 16.170  -33.775 -23.426 1.00 28.79  ? 69   SER A O   1 
ATOM   335   C  CB  . SER A 1 69  ? 16.327  -30.610 -24.635 1.00 22.99  ? 69   SER A CB  1 
ATOM   336   O  OG  . SER A 1 69  ? 17.357  -31.354 -25.274 1.00 31.91  ? 69   SER A OG  1 
ATOM   337   N  N   . LEU A 1 70  ? 14.614  -33.049 -24.888 1.00 42.04  ? 70   LEU A N   1 
ATOM   338   C  CA  . LEU A 1 70  ? 14.363  -34.384 -25.430 1.00 44.25  ? 70   LEU A CA  1 
ATOM   339   C  C   . LEU A 1 70  ? 15.665  -35.047 -25.837 1.00 45.36  ? 70   LEU A C   1 
ATOM   340   O  O   . LEU A 1 70  ? 15.887  -36.236 -25.581 1.00 46.87  ? 70   LEU A O   1 
ATOM   341   C  CB  . LEU A 1 70  ? 13.443  -34.315 -26.649 1.00 38.65  ? 70   LEU A CB  1 
ATOM   342   C  CG  . LEU A 1 70  ? 11.970  -34.024 -26.376 1.00 41.93  ? 70   LEU A CG  1 
ATOM   343   C  CD1 . LEU A 1 70  ? 11.198  -33.841 -27.675 1.00 46.95  ? 70   LEU A CD1 1 
ATOM   344   C  CD2 . LEU A 1 70  ? 11.362  -35.147 -25.565 1.00 37.86  ? 70   LEU A CD2 1 
ATOM   345   N  N   . GLU A 1 71  ? 16.527  -34.266 -26.470 1.00 34.99  ? 71   GLU A N   1 
ATOM   346   C  CA  . GLU A 1 71  ? 17.702  -34.828 -27.101 1.00 39.56  ? 71   GLU A CA  1 
ATOM   347   C  C   . GLU A 1 71  ? 18.957  -34.700 -26.243 1.00 43.16  ? 71   GLU A C   1 
ATOM   348   O  O   . GLU A 1 71  ? 20.080  -34.769 -26.750 1.00 38.24  ? 71   GLU A O   1 
ATOM   349   C  CB  . GLU A 1 71  ? 17.889  -34.188 -28.465 1.00 46.37  ? 71   GLU A CB  1 
ATOM   350   C  CG  . GLU A 1 71  ? 16.696  -34.399 -29.366 1.00 38.88  ? 71   GLU A CG  1 
ATOM   351   C  CD  . GLU A 1 71  ? 16.891  -33.764 -30.715 1.00 56.84  ? 71   GLU A CD  1 
ATOM   352   O  OE1 . GLU A 1 71  ? 17.430  -32.632 -30.761 1.00 61.99  ? 71   GLU A OE1 1 
ATOM   353   O  OE2 . GLU A 1 71  ? 16.499  -34.391 -31.722 1.00 57.88  ? 71   GLU A OE2 1 
ATOM   354   N  N   . GLY A 1 72  ? 18.747  -34.505 -24.941 1.00 44.36  ? 72   GLY A N   1 
ATOM   355   C  CA  . GLY A 1 72  ? 19.818  -34.580 -23.961 1.00 38.08  ? 72   GLY A CA  1 
ATOM   356   C  C   . GLY A 1 72  ? 20.522  -33.278 -23.624 1.00 42.58  ? 72   GLY A C   1 
ATOM   357   O  O   . GLY A 1 72  ? 21.395  -33.241 -22.754 1.00 53.00  ? 72   GLY A O   1 
ATOM   358   N  N   . ARG A 1 73  ? 20.156  -32.203 -24.307 1.00 41.94  ? 73   ARG A N   1 
ATOM   359   C  CA  . ARG A 1 73  ? 20.814  -30.926 -24.083 1.00 40.73  ? 73   ARG A CA  1 
ATOM   360   C  C   . ARG A 1 73  ? 20.434  -30.306 -22.743 1.00 46.69  ? 73   ARG A C   1 
ATOM   361   O  O   . ARG A 1 73  ? 19.266  -30.314 -22.345 1.00 49.41  ? 73   ARG A O   1 
ATOM   362   C  CB  . ARG A 1 73  ? 20.498  -29.978 -25.232 1.00 42.42  ? 73   ARG A CB  1 
ATOM   363   C  CG  . ARG A 1 73  ? 20.804  -30.594 -26.582 1.00 37.98  ? 73   ARG A CG  1 
ATOM   364   C  CD  . ARG A 1 73  ? 20.603  -29.589 -27.685 1.00 43.54  ? 73   ARG A CD  1 
ATOM   365   N  NE  . ARG A 1 73  ? 20.318  -30.269 -28.943 1.00 48.38  ? 73   ARG A NE  1 
ATOM   366   C  CZ  . ARG A 1 73  ? 21.236  -30.541 -29.864 1.00 42.68  ? 73   ARG A CZ  1 
ATOM   367   N  NH1 . ARG A 1 73  ? 20.898  -31.170 -30.980 1.00 39.71  ? 73   ARG A NH1 1 
ATOM   368   N  NH2 . ARG A 1 73  ? 22.493  -30.176 -29.669 1.00 55.31  ? 73   ARG A NH2 1 
ATOM   369   N  N   . ASN A 1 74  ? 21.431  -29.770 -22.049 1.00 44.34  ? 74   ASN A N   1 
ATOM   370   C  CA  . ASN A 1 74  ? 21.212  -29.185 -20.743 1.00 36.89  ? 74   ASN A CA  1 
ATOM   371   C  C   . ASN A 1 74  ? 20.507  -27.846 -20.806 1.00 38.81  ? 74   ASN A C   1 
ATOM   372   O  O   . ASN A 1 74  ? 20.906  -26.968 -21.559 1.00 34.36  ? 74   ASN A O   1 
ATOM   373   C  CB  . ASN A 1 74  ? 22.537  -29.034 -19.998 1.00 35.48  ? 74   ASN A CB  1 
ATOM   374   C  CG  . ASN A 1 74  ? 23.014  -30.343 -19.389 1.00 48.94  ? 74   ASN A CG  1 
ATOM   375   O  OD1 . ASN A 1 74  ? 22.215  -31.183 -18.954 1.00 50.21  ? 74   ASN A OD1 1 
ATOM   376   N  ND2 . ASN A 1 74  ? 24.323  -30.522 -19.354 1.00 58.56  ? 74   ASN A ND2 1 
ATOM   377   N  N   . LEU A 1 75  ? 19.455  -27.705 -20.005 1.00 41.07  ? 75   LEU A N   1 
ATOM   378   C  CA  . LEU A 1 75  ? 18.791  -26.425 -19.807 1.00 33.38  ? 75   LEU A CA  1 
ATOM   379   C  C   . LEU A 1 75  ? 19.410  -25.773 -18.582 1.00 32.29  ? 75   LEU A C   1 
ATOM   380   O  O   . LEU A 1 75  ? 19.253  -26.271 -17.468 1.00 46.30  ? 75   LEU A O   1 
ATOM   381   C  CB  . LEU A 1 75  ? 17.284  -26.615 -19.612 1.00 39.68  ? 75   LEU A CB  1 
ATOM   382   C  CG  . LEU A 1 75  ? 16.386  -26.895 -20.833 1.00 36.22  ? 75   LEU A CG  1 
ATOM   383   C  CD1 . LEU A 1 75  ? 17.161  -27.510 -21.984 1.00 50.93  ? 75   LEU A CD1 1 
ATOM   384   C  CD2 . LEU A 1 75  ? 15.227  -27.795 -20.461 1.00 38.88  ? 75   LEU A CD2 1 
ATOM   385   N  N   . LEU A 1 76  ? 20.116  -24.662 -18.796 1.00 34.45  ? 76   LEU A N   1 
ATOM   386   C  CA  . LEU A 1 76  ? 20.952  -24.051 -17.763 1.00 34.12  ? 76   LEU A CA  1 
ATOM   387   C  C   . LEU A 1 76  ? 20.570  -22.598 -17.468 1.00 37.12  ? 76   LEU A C   1 
ATOM   388   O  O   . LEU A 1 76  ? 20.168  -21.860 -18.367 1.00 33.91  ? 76   LEU A O   1 
ATOM   389   C  CB  . LEU A 1 76  ? 22.418  -24.076 -18.200 1.00 26.93  ? 76   LEU A CB  1 
ATOM   390   C  CG  . LEU A 1 76  ? 23.111  -25.415 -18.429 1.00 44.10  ? 76   LEU A CG  1 
ATOM   391   C  CD1 . LEU A 1 76  ? 24.441  -25.207 -19.152 1.00 45.47  ? 76   LEU A CD1 1 
ATOM   392   C  CD2 . LEU A 1 76  ? 23.320  -26.145 -17.111 1.00 50.95  ? 76   LEU A CD2 1 
ATOM   393   N  N   . ALA A 1 77  ? 20.731  -22.188 -16.210 1.00 39.26  ? 77   ALA A N   1 
ATOM   394   C  CA  . ALA A 1 77  ? 20.492  -20.802 -15.813 1.00 35.21  ? 77   ALA A CA  1 
ATOM   395   C  C   . ALA A 1 77  ? 21.653  -20.272 -15.001 1.00 37.60  ? 77   ALA A C   1 
ATOM   396   O  O   . ALA A 1 77  ? 22.025  -20.866 -13.991 1.00 38.73  ? 77   ALA A O   1 
ATOM   397   C  CB  . ALA A 1 77  ? 19.220  -20.684 -15.006 1.00 26.66  ? 77   ALA A CB  1 
ATOM   398   N  N   . LEU A 1 78  ? 22.216  -19.147 -15.434 1.00 37.75  ? 78   LEU A N   1 
ATOM   399   C  CA  . LEU A 1 78  ? 23.281  -18.516 -14.677 1.00 24.31  ? 78   LEU A CA  1 
ATOM   400   C  C   . LEU A 1 78  ? 22.685  -17.518 -13.723 1.00 22.88  ? 78   LEU A C   1 
ATOM   401   O  O   . LEU A 1 78  ? 22.044  -16.561 -14.152 1.00 28.68  ? 78   LEU A O   1 
ATOM   402   C  CB  . LEU A 1 78  ? 24.270  -17.796 -15.595 1.00 24.56  ? 78   LEU A CB  1 
ATOM   403   C  CG  . LEU A 1 78  ? 25.545  -17.269 -14.912 1.00 32.85  ? 78   LEU A CG  1 
ATOM   404   C  CD1 . LEU A 1 78  ? 26.489  -18.419 -14.555 1.00 18.74  ? 78   LEU A CD1 1 
ATOM   405   C  CD2 . LEU A 1 78  ? 26.285  -16.235 -15.771 1.00 27.85  ? 78   LEU A CD2 1 
ATOM   406   N  N   . GLN A 1 79  ? 22.902  -17.747 -12.434 1.00 21.70  ? 79   GLN A N   1 
ATOM   407   C  CA  . GLN A 1 79  ? 22.576  -16.775 -11.395 1.00 25.02  ? 79   GLN A CA  1 
ATOM   408   C  C   . GLN A 1 79  ? 23.716  -15.804 -11.118 1.00 26.28  ? 79   GLN A C   1 
ATOM   409   O  O   . GLN A 1 79  ? 24.871  -16.204 -11.011 1.00 25.40  ? 79   GLN A O   1 
ATOM   410   C  CB  . GLN A 1 79  ? 22.236  -17.487 -10.094 1.00 21.91  ? 79   GLN A CB  1 
ATOM   411   C  CG  . GLN A 1 79  ? 22.275  -16.598 -8.895  1.00 18.88  ? 79   GLN A CG  1 
ATOM   412   C  CD  . GLN A 1 79  ? 22.145  -17.389 -7.626  1.00 27.67  ? 79   GLN A CD  1 
ATOM   413   O  OE1 . GLN A 1 79  ? 22.465  -18.575 -7.591  1.00 23.97  ? 79   GLN A OE1 1 
ATOM   414   N  NE2 . GLN A 1 79  ? 21.679  -16.739 -6.568  1.00 22.10  ? 79   GLN A NE2 1 
ATOM   415   N  N   . ILE A 1 80  ? 23.366  -14.528 -10.982 1.00 36.89  ? 80   ILE A N   1 
ATOM   416   C  CA  . ILE A 1 80  ? 24.295  -13.474 -10.594 1.00 29.57  ? 80   ILE A CA  1 
ATOM   417   C  C   . ILE A 1 80  ? 23.736  -12.770 -9.369  1.00 38.64  ? 80   ILE A C   1 
ATOM   418   O  O   . ILE A 1 80  ? 22.586  -12.327 -9.375  1.00 46.25  ? 80   ILE A O   1 
ATOM   419   C  CB  . ILE A 1 80  ? 24.433  -12.439 -11.707 1.00 29.78  ? 80   ILE A CB  1 
ATOM   420   C  CG1 . ILE A 1 80  ? 24.979  -13.109 -12.973 1.00 26.12  ? 80   ILE A CG1 1 
ATOM   421   C  CG2 . ILE A 1 80  ? 25.307  -11.283 -11.243 1.00 29.42  ? 80   ILE A CG2 1 
ATOM   422   C  CD1 . ILE A 1 80  ? 24.852  -12.290 -14.231 1.00 24.69  ? 80   ILE A CD1 1 
ATOM   423   N  N   . SER A 1 81  ? 24.540  -12.662 -8.317  1.00 44.17  ? 81   SER A N   1 
ATOM   424   C  CA  . SER A 1 81  ? 24.069  -12.065 -7.074  1.00 35.33  ? 81   SER A CA  1 
ATOM   425   C  C   . SER A 1 81  ? 25.211  -11.442 -6.299  1.00 42.77  ? 81   SER A C   1 
ATOM   426   O  O   . SER A 1 81  ? 26.378  -11.694 -6.600  1.00 54.55  ? 81   SER A O   1 
ATOM   427   C  CB  . SER A 1 81  ? 23.418  -13.134 -6.216  1.00 30.48  ? 81   SER A CB  1 
ATOM   428   O  OG  . SER A 1 81  ? 24.331  -14.189 -6.002  1.00 52.60  ? 81   SER A OG  1 
ATOM   429   N  N   . ARG A 1 82  ? 24.878  -10.632 -5.296  1.00 48.91  ? 82   ARG A N   1 
ATOM   430   C  CA  . ARG A 1 82  ? 25.896  -10.084 -4.400  1.00 49.95  ? 82   ARG A CA  1 
ATOM   431   C  C   . ARG A 1 82  ? 26.669  -11.261 -3.831  1.00 55.03  ? 82   ARG A C   1 
ATOM   432   O  O   . ARG A 1 82  ? 27.904  -11.280 -3.849  1.00 60.88  ? 82   ARG A O   1 
ATOM   433   C  CB  . ARG A 1 82  ? 25.251  -9.249  -3.281  1.00 52.35  ? 82   ARG A CB  1 
ATOM   434   C  CG  . ARG A 1 82  ? 26.207  -8.710  -2.207  1.00 51.74  ? 82   ARG A CG  1 
ATOM   435   C  CD  . ARG A 1 82  ? 26.104  -7.197  -2.059  1.00 63.09  ? 82   ARG A CD  1 
ATOM   436   N  NE  . ARG A 1 82  ? 25.662  -6.782  -0.734  1.00 68.45  ? 82   ARG A NE  1 
ATOM   437   C  CZ  . ARG A 1 82  ? 25.771  -5.548  -0.236  1.00 78.65  ? 82   ARG A CZ  1 
ATOM   438   N  NH1 . ARG A 1 82  ? 25.323  -5.298  0.988   1.00 72.22  ? 82   ARG A NH1 1 
ATOM   439   N  NH2 . ARG A 1 82  ? 26.324  -4.563  -0.938  1.00 83.50  ? 82   ARG A NH2 1 
ATOM   440   N  N   . ASN A 1 83  ? 25.927  -12.259 -3.358  1.00 43.65  ? 83   ASN A N   1 
ATOM   441   C  CA  . ASN A 1 83  ? 26.526  -13.460 -2.792  1.00 39.62  ? 83   ASN A CA  1 
ATOM   442   C  C   . ASN A 1 83  ? 25.780  -14.703 -3.214  1.00 31.63  ? 83   ASN A C   1 
ATOM   443   O  O   . ASN A 1 83  ? 24.692  -14.977 -2.717  1.00 42.52  ? 83   ASN A O   1 
ATOM   444   C  CB  . ASN A 1 83  ? 26.540  -13.378 -1.270  1.00 58.45  ? 83   ASN A CB  1 
ATOM   445   C  CG  . ASN A 1 83  ? 26.762  -14.735 -0.612  1.00 70.83  ? 83   ASN A CG  1 
ATOM   446   O  OD1 . ASN A 1 83  ? 27.457  -15.598 -1.154  1.00 71.44  ? 83   ASN A OD1 1 
ATOM   447   N  ND2 . ASN A 1 83  ? 26.172  -14.925 0.569   1.00 72.65  ? 83   ASN A ND2 1 
ATOM   448   N  N   . THR A 1 84  ? 26.380  -15.470 -4.114  1.00 40.88  ? 84   THR A N   1 
ATOM   449   C  CA  . THR A 1 84  ? 25.700  -16.620 -4.708  1.00 37.25  ? 84   THR A CA  1 
ATOM   450   C  C   . THR A 1 84  ? 25.352  -17.738 -3.712  1.00 30.19  ? 84   THR A C   1 
ATOM   451   O  O   . THR A 1 84  ? 24.523  -18.596 -3.997  1.00 36.56  ? 84   THR A O   1 
ATOM   452   C  CB  . THR A 1 84  ? 26.500  -17.178 -5.887  1.00 33.05  ? 84   THR A CB  1 
ATOM   453   O  OG1 . THR A 1 84  ? 25.621  -17.394 -6.992  1.00 45.87  ? 84   THR A OG1 1 
ATOM   454   C  CG2 . THR A 1 84  ? 27.184  -18.471 -5.509  1.00 29.28  ? 84   THR A CG2 1 
ATOM   455   N  N   . ARG A 1 85  ? 25.960  -17.720 -2.535  1.00 26.17  ? 85   ARG A N   1 
ATOM   456   C  CA  . ARG A 1 85  ? 25.647  -18.739 -1.540  1.00 37.24  ? 85   ARG A CA  1 
ATOM   457   C  C   . ARG A 1 85  ? 24.171  -18.747 -1.147  1.00 41.71  ? 85   ARG A C   1 
ATOM   458   O  O   . ARG A 1 85  ? 23.520  -19.786 -1.163  1.00 52.26  ? 85   ARG A O   1 
ATOM   459   C  CB  . ARG A 1 85  ? 26.511  -18.565 -0.295  1.00 58.30  ? 85   ARG A CB  1 
ATOM   460   C  CG  . ARG A 1 85  ? 27.995  -18.791 -0.533  1.00 76.79  ? 85   ARG A CG  1 
ATOM   461   C  CD  . ARG A 1 85  ? 28.695  -19.185 0.759   1.00 96.19  ? 85   ARG A CD  1 
ATOM   462   N  NE  . ARG A 1 85  ? 28.535  -20.606 1.076   1.00 106.16 ? 85   ARG A NE  1 
ATOM   463   C  CZ  . ARG A 1 85  ? 27.608  -21.105 1.892   1.00 101.77 ? 85   ARG A CZ  1 
ATOM   464   N  NH1 . ARG A 1 85  ? 27.559  -22.415 2.112   1.00 96.76  ? 85   ARG A NH1 1 
ATOM   465   N  NH2 . ARG A 1 85  ? 26.730  -20.301 2.486   1.00 97.32  ? 85   ARG A NH2 1 
ATOM   466   N  N   . SER A 1 86  ? 23.643  -17.583 -0.786  1.00 55.27  ? 86   SER A N   1 
ATOM   467   C  CA  . SER A 1 86  ? 22.236  -17.470 -0.402  1.00 50.29  ? 86   SER A CA  1 
ATOM   468   C  C   . SER A 1 86  ? 21.534  -16.373 -1.195  1.00 56.68  ? 86   SER A C   1 
ATOM   469   O  O   . SER A 1 86  ? 21.957  -16.003 -2.292  1.00 73.84  ? 86   SER A O   1 
ATOM   470   C  CB  . SER A 1 86  ? 22.107  -17.189 1.100   1.00 44.94  ? 86   SER A CB  1 
ATOM   471   O  OG  . SER A 1 86  ? 22.668  -18.234 1.893   1.00 49.21  ? 86   SER A OG  1 
ATOM   472   N  N   . ARG A 1 87  ? 20.441  -15.877 -0.639  1.00 51.84  ? 87   ARG A N   1 
ATOM   473   C  CA  . ARG A 1 87  ? 19.781  -14.692 -1.161  1.00 42.48  ? 87   ARG A CA  1 
ATOM   474   C  C   . ARG A 1 87  ? 19.544  -13.792 0.037   1.00 40.58  ? 87   ARG A C   1 
ATOM   475   O  O   . ARG A 1 87  ? 18.885  -14.193 0.991   1.00 30.21  ? 87   ARG A O   1 
ATOM   476   C  CB  . ARG A 1 87  ? 18.443  -15.053 -1.819  1.00 19.30  ? 87   ARG A CB  1 
ATOM   477   C  CG  . ARG A 1 87  ? 18.068  -14.181 -3.015  1.00 22.94  ? 87   ARG A CG  1 
ATOM   478   C  CD  . ARG A 1 87  ? 16.627  -14.374 -3.430  1.00 23.33  ? 87   ARG A CD  1 
ATOM   479   N  NE  . ARG A 1 87  ? 15.732  -13.596 -2.581  1.00 39.38  ? 87   ARG A NE  1 
ATOM   480   C  CZ  . ARG A 1 87  ? 15.005  -14.099 -1.594  1.00 39.76  ? 87   ARG A CZ  1 
ATOM   481   N  NH1 . ARG A 1 87  ? 15.047  -15.393 -1.316  1.00 51.10  ? 87   ARG A NH1 1 
ATOM   482   N  NH2 . ARG A 1 87  ? 14.233  -13.301 -0.888  1.00 47.39  ? 87   ARG A NH2 1 
ATOM   483   N  N   . ASN A 1 88  ? 20.101  -12.589 0.016   1.00 44.90  ? 88   ASN A N   1 
ATOM   484   C  CA  . ASN A 1 88  ? 19.896  -11.676 1.134   1.00 32.73  ? 88   ASN A CA  1 
ATOM   485   C  C   . ASN A 1 88  ? 18.416  -11.381 1.330   1.00 39.66  ? 88   ASN A C   1 
ATOM   486   O  O   . ASN A 1 88  ? 17.673  -11.160 0.368   1.00 43.53  ? 88   ASN A O   1 
ATOM   487   C  CB  . ASN A 1 88  ? 20.672  -10.382 0.926   1.00 45.32  ? 88   ASN A CB  1 
ATOM   488   C  CG  . ASN A 1 88  ? 22.162  -10.620 0.812   1.00 63.07  ? 88   ASN A CG  1 
ATOM   489   O  OD1 . ASN A 1 88  ? 22.790  -10.257 -0.189  1.00 73.40  ? 88   ASN A OD1 1 
ATOM   490   N  ND2 . ASN A 1 88  ? 22.739  -11.246 1.835   1.00 68.14  ? 88   ASN A ND2 1 
ATOM   491   N  N   . LEU A 1 89  ? 17.984  -11.388 2.581   1.00 30.96  ? 89   LEU A N   1 
ATOM   492   C  CA  . LEU A 1 89  ? 16.597  -11.128 2.884   1.00 29.09  ? 89   LEU A CA  1 
ATOM   493   C  C   . LEU A 1 89  ? 16.121  -9.921  2.078   1.00 35.08  ? 89   LEU A C   1 
ATOM   494   O  O   . LEU A 1 89  ? 16.797  -8.900  2.015   1.00 37.92  ? 89   LEU A O   1 
ATOM   495   C  CB  . LEU A 1 89  ? 16.427  -10.871 4.379   1.00 27.72  ? 89   LEU A CB  1 
ATOM   496   C  CG  . LEU A 1 89  ? 14.997  -11.008 4.902   1.00 25.28  ? 89   LEU A CG  1 
ATOM   497   C  CD1 . LEU A 1 89  ? 14.627  -12.477 4.948   1.00 13.61  ? 89   LEU A CD1 1 
ATOM   498   C  CD2 . LEU A 1 89  ? 14.861  -10.387 6.272   1.00 37.16  ? 89   LEU A CD2 1 
ATOM   499   N  N   . LEU A 1 90  ? 14.964  -10.064 1.448   1.00 32.38  ? 90   LEU A N   1 
ATOM   500   C  CA  . LEU A 1 90  ? 14.315  -8.968  0.742   1.00 37.57  ? 90   LEU A CA  1 
ATOM   501   C  C   . LEU A 1 90  ? 15.030  -8.530  -0.531  1.00 37.16  ? 90   LEU A C   1 
ATOM   502   O  O   . LEU A 1 90  ? 14.669  -7.515  -1.121  1.00 32.35  ? 90   LEU A O   1 
ATOM   503   C  CB  . LEU A 1 90  ? 14.071  -7.778  1.673   1.00 34.00  ? 90   LEU A CB  1 
ATOM   504   C  CG  . LEU A 1 90  ? 12.975  -8.047  2.709   1.00 36.50  ? 90   LEU A CG  1 
ATOM   505   C  CD1 . LEU A 1 90  ? 12.773  -6.884  3.673   1.00 14.77  ? 90   LEU A CD1 1 
ATOM   506   C  CD2 . LEU A 1 90  ? 11.683  -8.383  1.986   1.00 30.07  ? 90   LEU A CD2 1 
ATOM   507   N  N   . THR A 1 91  ? 16.034  -9.291  -0.953  1.00 27.18  ? 91   THR A N   1 
ATOM   508   C  CA  . THR A 1 91  ? 16.550  -9.130  -2.304  1.00 37.50  ? 91   THR A CA  1 
ATOM   509   C  C   . THR A 1 91  ? 15.644  -9.870  -3.271  1.00 38.00  ? 91   THR A C   1 
ATOM   510   O  O   . THR A 1 91  ? 15.378  -11.061 -3.071  1.00 23.73  ? 91   THR A O   1 
ATOM   511   C  CB  . THR A 1 91  ? 17.980  -9.670  -2.484  1.00 27.42  ? 91   THR A CB  1 
ATOM   512   O  OG1 . THR A 1 91  ? 18.896  -8.885  -1.706  1.00 22.27  ? 91   THR A OG1 1 
ATOM   513   C  CG2 . THR A 1 91  ? 18.375  -9.584  -3.947  1.00 11.37  ? 91   THR A CG2 1 
ATOM   514   N  N   . PRO A 1 92  ? 15.164  -9.158  -4.314  1.00 33.78  ? 92   PRO A N   1 
ATOM   515   C  CA  . PRO A 1 92  ? 14.264  -9.680  -5.350  1.00 30.20  ? 92   PRO A CA  1 
ATOM   516   C  C   . PRO A 1 92  ? 14.951  -10.663 -6.286  1.00 39.74  ? 92   PRO A C   1 
ATOM   517   O  O   . PRO A 1 92  ? 15.944  -10.309 -6.931  1.00 35.53  ? 92   PRO A O   1 
ATOM   518   C  CB  . PRO A 1 92  ? 13.868  -8.430  -6.146  1.00 25.31  ? 92   PRO A CB  1 
ATOM   519   C  CG  . PRO A 1 92  ? 14.310  -7.257  -5.316  1.00 26.66  ? 92   PRO A CG  1 
ATOM   520   C  CD  . PRO A 1 92  ? 15.458  -7.727  -4.506  1.00 21.14  ? 92   PRO A CD  1 
ATOM   521   N  N   . PRO A 1 93  ? 14.426  -11.892 -6.367  1.00 39.14  ? 93   PRO A N   1 
ATOM   522   C  CA  . PRO A 1 93  ? 14.876  -12.796 -7.426  1.00 37.27  ? 93   PRO A CA  1 
ATOM   523   C  C   . PRO A 1 93  ? 14.156  -12.418 -8.713  1.00 40.09  ? 93   PRO A C   1 
ATOM   524   O  O   . PRO A 1 93  ? 12.972  -12.069 -8.712  1.00 30.83  ? 93   PRO A O   1 
ATOM   525   C  CB  . PRO A 1 93  ? 14.437  -14.191 -6.941  1.00 10.89  ? 93   PRO A CB  1 
ATOM   526   C  CG  . PRO A 1 93  ? 13.503  -13.958 -5.799  1.00 19.51  ? 93   PRO A CG  1 
ATOM   527   C  CD  . PRO A 1 93  ? 13.334  -12.467 -5.576  1.00 20.18  ? 93   PRO A CD  1 
ATOM   528   N  N   . VAL A 1 94  ? 14.883  -12.468 -9.817  1.00 28.64  ? 94   VAL A N   1 
ATOM   529   C  CA  . VAL A 1 94  ? 14.332  -12.083 -11.094 1.00 19.59  ? 94   VAL A CA  1 
ATOM   530   C  C   . VAL A 1 94  ? 14.913  -13.032 -12.126 1.00 31.05  ? 94   VAL A C   1 
ATOM   531   O  O   . VAL A 1 94  ? 15.959  -13.640 -11.876 1.00 37.75  ? 94   VAL A O   1 
ATOM   532   C  CB  . VAL A 1 94  ? 14.726  -10.638 -11.439 1.00 29.01  ? 94   VAL A CB  1 
ATOM   533   C  CG1 . VAL A 1 94  ? 14.090  -10.210 -12.747 1.00 58.51  ? 94   VAL A CG1 1 
ATOM   534   C  CG2 . VAL A 1 94  ? 14.336  -9.692  -10.306 1.00 30.28  ? 94   VAL A CG2 1 
ATOM   535   N  N   . LYS A 1 95  ? 14.242  -13.173 -13.271 1.00 26.53  ? 95   LYS A N   1 
ATOM   536   C  CA  . LYS A 1 95  ? 14.743  -14.018 -14.361 1.00 30.73  ? 95   LYS A CA  1 
ATOM   537   C  C   . LYS A 1 95  ? 14.520  -13.435 -15.759 1.00 33.95  ? 95   LYS A C   1 
ATOM   538   O  O   . LYS A 1 95  ? 13.550  -12.714 -16.013 1.00 26.59  ? 95   LYS A O   1 
ATOM   539   C  CB  . LYS A 1 95  ? 14.150  -15.427 -14.283 1.00 22.00  ? 95   LYS A CB  1 
ATOM   540   C  CG  . LYS A 1 95  ? 12.648  -15.502 -14.483 1.00 23.97  ? 95   LYS A CG  1 
ATOM   541   C  CD  . LYS A 1 95  ? 12.007  -16.293 -13.345 1.00 25.96  ? 95   LYS A CD  1 
ATOM   542   C  CE  . LYS A 1 95  ? 10.753  -17.022 -13.815 1.00 27.43  ? 95   LYS A CE  1 
ATOM   543   N  NZ  . LYS A 1 95  ? 9.762   -16.151 -14.504 1.00 39.95  ? 95   LYS A NZ  1 
ATOM   544   N  N   . TYR A 1 96  ? 15.447  -13.745 -16.655 1.00 34.32  ? 96   TYR A N   1 
ATOM   545   C  CA  . TYR A 1 96  ? 15.277  -13.480 -18.081 1.00 38.44  ? 96   TYR A CA  1 
ATOM   546   C  C   . TYR A 1 96  ? 15.350  -14.802 -18.846 1.00 36.84  ? 96   TYR A C   1 
ATOM   547   O  O   . TYR A 1 96  ? 16.324  -15.553 -18.710 1.00 26.24  ? 96   TYR A O   1 
ATOM   548   C  CB  . TYR A 1 96  ? 16.368  -12.539 -18.592 1.00 31.09  ? 96   TYR A CB  1 
ATOM   549   C  CG  . TYR A 1 96  ? 16.050  -11.074 -18.419 1.00 33.15  ? 96   TYR A CG  1 
ATOM   550   C  CD1 . TYR A 1 96  ? 14.739  -10.644 -18.254 1.00 23.91  ? 96   TYR A CD1 1 
ATOM   551   C  CD2 . TYR A 1 96  ? 17.061  -10.115 -18.434 1.00 34.50  ? 96   TYR A CD2 1 
ATOM   552   C  CE1 . TYR A 1 96  ? 14.442  -9.305  -18.116 1.00 21.82  ? 96   TYR A CE1 1 
ATOM   553   C  CE2 . TYR A 1 96  ? 16.773  -8.768  -18.289 1.00 36.00  ? 96   TYR A CE2 1 
ATOM   554   C  CZ  . TYR A 1 96  ? 15.456  -8.370  -18.125 1.00 38.67  ? 96   TYR A CZ  1 
ATOM   555   O  OH  . TYR A 1 96  ? 15.129  -7.040  -17.968 1.00 42.20  ? 96   TYR A OH  1 
ATOM   556   N  N   . ILE A 1 97  ? 14.324  -15.119 -19.629 1.00 34.10  ? 97   ILE A N   1 
ATOM   557   C  CA  . ILE A 1 97  ? 14.431  -16.305 -20.473 1.00 39.14  ? 97   ILE A CA  1 
ATOM   558   C  C   . ILE A 1 97  ? 14.421  -15.896 -21.936 1.00 36.25  ? 97   ILE A C   1 
ATOM   559   O  O   . ILE A 1 97  ? 13.818  -14.882 -22.292 1.00 28.30  ? 97   ILE A O   1 
ATOM   560   C  CB  . ILE A 1 97  ? 13.343  -17.376 -20.194 1.00 34.78  ? 97   ILE A CB  1 
ATOM   561   C  CG1 . ILE A 1 97  ? 13.397  -17.881 -18.738 1.00 34.05  ? 97   ILE A CG1 1 
ATOM   562   C  CG2 . ILE A 1 97  ? 13.563  -18.565 -21.112 1.00 26.76  ? 97   ILE A CG2 1 
ATOM   563   C  CD1 . ILE A 1 97  ? 12.591  -17.088 -17.753 1.00 35.03  ? 97   ILE A CD1 1 
ATOM   564   N  N   . ALA A 1 98  ? 15.101  -16.674 -22.775 1.00 29.19  ? 98   ALA A N   1 
ATOM   565   C  CA  . ALA A 1 98  ? 15.122  -16.410 -24.206 1.00 17.61  ? 98   ALA A CA  1 
ATOM   566   C  C   . ALA A 1 98  ? 14.977  -17.690 -25.034 1.00 33.18  ? 98   ALA A C   1 
ATOM   567   O  O   . ALA A 1 98  ? 14.985  -18.798 -24.504 1.00 42.35  ? 98   ALA A O   1 
ATOM   568   C  CB  . ALA A 1 98  ? 16.395  -15.687 -24.573 1.00 17.36  ? 98   ALA A CB  1 
ATOM   569   N  N   . ASN A 1 99  ? 14.831  -17.515 -26.340 1.00 36.69  ? 99   ASN A N   1 
ATOM   570   C  CA  . ASN A 1 99  ? 14.910  -18.611 -27.297 1.00 30.31  ? 99   ASN A CA  1 
ATOM   571   C  C   . ASN A 1 99  ? 13.993  -19.796 -27.022 1.00 45.08  ? 99   ASN A C   1 
ATOM   572   O  O   . ASN A 1 99  ? 14.376  -20.944 -27.286 1.00 49.91  ? 99   ASN A O   1 
ATOM   573   C  CB  . ASN A 1 99  ? 16.352  -19.110 -27.420 1.00 35.20  ? 99   ASN A CB  1 
ATOM   574   C  CG  . ASN A 1 99  ? 16.561  -19.981 -28.648 1.00 38.85  ? 99   ASN A CG  1 
ATOM   575   O  OD1 . ASN A 1 99  ? 17.019  -21.115 -28.551 1.00 34.73  ? 99   ASN A OD1 1 
ATOM   576   N  ND2 . ASN A 1 99  ? 16.203  -19.455 -29.810 1.00 41.19  ? 99   ASN A ND2 1 
ATOM   577   N  N   . MET A 1 100 ? 12.790  -19.535 -26.509 1.00 42.99  ? 100  MET A N   1 
ATOM   578   C  CA  . MET A 1 100 ? 11.855  -20.632 -26.277 1.00 38.29  ? 100  MET A CA  1 
ATOM   579   C  C   . MET A 1 100 ? 11.382  -21.155 -27.619 1.00 40.83  ? 100  MET A C   1 
ATOM   580   O  O   . MET A 1 100 ? 11.175  -22.356 -27.802 1.00 45.52  ? 100  MET A O   1 
ATOM   581   C  CB  . MET A 1 100 ? 10.686  -20.212 -25.387 1.00 40.80  ? 100  MET A CB  1 
ATOM   582   C  CG  . MET A 1 100 ? 9.584   -19.441 -26.081 1.00 47.57  ? 100  MET A CG  1 
ATOM   583   S  SD  . MET A 1 100 ? 8.257   -19.073 -24.919 1.00 46.17  ? 100  MET A SD  1 
ATOM   584   C  CE  . MET A 1 100 ? 8.054   -20.674 -24.139 1.00 32.91  ? 100  MET A CE  1 
ATOM   585   N  N   . HIS A 1 101 ? 11.219  -20.242 -28.566 1.00 37.72  ? 101  HIS A N   1 
ATOM   586   C  CA  . HIS A 1 101 ? 11.087  -20.632 -29.954 1.00 29.57  ? 101  HIS A CA  1 
ATOM   587   C  C   . HIS A 1 101 ? 12.498  -20.608 -30.525 1.00 41.74  ? 101  HIS A C   1 
ATOM   588   O  O   . HIS A 1 101 ? 13.099  -19.531 -30.710 1.00 29.01  ? 101  HIS A O   1 
ATOM   589   C  CB  . HIS A 1 101 ? 10.147  -19.694 -30.705 1.00 19.89  ? 101  HIS A CB  1 
ATOM   590   C  CG  . HIS A 1 101 ? 8.752   -19.695 -30.163 1.00 39.45  ? 101  HIS A CG  1 
ATOM   591   N  ND1 . HIS A 1 101 ? 8.237   -18.653 -29.424 1.00 49.93  ? 101  HIS A ND1 1 
ATOM   592   C  CD2 . HIS A 1 101 ? 7.775   -20.629 -30.230 1.00 52.50  ? 101  HIS A CD2 1 
ATOM   593   C  CE1 . HIS A 1 101 ? 6.994   -18.937 -29.076 1.00 53.90  ? 101  HIS A CE1 1 
ATOM   594   N  NE2 . HIS A 1 101 ? 6.689   -20.130 -29.552 1.00 52.22  ? 101  HIS A NE2 1 
ATOM   595   N  N   . GLY A 1 102 ? 13.027  -21.813 -30.754 1.00 35.72  ? 102  GLY A N   1 
ATOM   596   C  CA  . GLY A 1 102 ? 14.388  -22.014 -31.221 1.00 27.64  ? 102  GLY A CA  1 
ATOM   597   C  C   . GLY A 1 102 ? 14.856  -21.145 -32.384 1.00 33.56  ? 102  GLY A C   1 
ATOM   598   O  O   . GLY A 1 102 ? 16.043  -20.836 -32.490 1.00 49.68  ? 102  GLY A O   1 
ATOM   599   N  N   . ASP A 1 103 ? 13.939  -20.754 -33.265 1.00 43.58  ? 103  ASP A N   1 
ATOM   600   C  CA  . ASP A 1 103 ? 14.300  -19.927 -34.416 1.00 43.70  ? 103  ASP A CA  1 
ATOM   601   C  C   . ASP A 1 103 ? 14.252  -18.423 -34.120 1.00 37.63  ? 103  ASP A C   1 
ATOM   602   O  O   . ASP A 1 103 ? 14.568  -17.609 -34.978 1.00 48.55  ? 103  ASP A O   1 
ATOM   603   C  CB  . ASP A 1 103 ? 13.415  -20.271 -35.614 1.00 48.39  ? 103  ASP A CB  1 
ATOM   604   C  CG  . ASP A 1 103 ? 11.946  -20.404 -35.243 1.00 50.34  ? 103  ASP A CG  1 
ATOM   605   O  OD1 . ASP A 1 103 ? 11.194  -20.994 -36.043 1.00 57.91  ? 103  ASP A OD1 1 
ATOM   606   O  OD2 . ASP A 1 103 ? 11.538  -19.923 -34.163 1.00 59.55  ? 103  ASP A OD2 1 
ATOM   607   N  N   . GLU A 1 104 ? 13.839  -18.065 -32.908 1.00 35.21  ? 104  GLU A N   1 
ATOM   608   C  CA  . GLU A 1 104 ? 13.851  -16.675 -32.461 1.00 33.19  ? 104  GLU A CA  1 
ATOM   609   C  C   . GLU A 1 104 ? 15.057  -16.487 -31.553 1.00 44.68  ? 104  GLU A C   1 
ATOM   610   O  O   . GLU A 1 104 ? 15.005  -16.792 -30.352 1.00 45.94  ? 104  GLU A O   1 
ATOM   611   C  CB  . GLU A 1 104 ? 12.563  -16.340 -31.719 1.00 26.36  ? 104  GLU A CB  1 
ATOM   612   C  CG  . GLU A 1 104 ? 11.295  -16.586 -32.526 1.00 44.67  ? 104  GLU A CG  1 
ATOM   613   C  CD  . GLU A 1 104 ? 10.063  -16.478 -31.669 1.00 53.68  ? 104  GLU A CD  1 
ATOM   614   O  OE1 . GLU A 1 104 ? 10.197  -16.004 -30.526 1.00 61.52  ? 104  GLU A OE1 1 
ATOM   615   O  OE2 . GLU A 1 104 ? 8.971   -16.876 -32.118 1.00 66.19  ? 104  GLU A OE2 1 
ATOM   616   N  N   . THR A 1 105 ? 16.127  -15.955 -32.135 1.00 45.21  ? 105  THR A N   1 
ATOM   617   C  CA  . THR A 1 105 ? 17.477  -16.138 -31.614 1.00 33.94  ? 105  THR A CA  1 
ATOM   618   C  C   . THR A 1 105 ? 18.154  -14.920 -30.965 1.00 30.98  ? 105  THR A C   1 
ATOM   619   O  O   . THR A 1 105 ? 19.056  -15.084 -30.154 1.00 29.13  ? 105  THR A O   1 
ATOM   620   C  CB  . THR A 1 105 ? 18.383  -16.651 -32.757 1.00 47.23  ? 105  THR A CB  1 
ATOM   621   O  OG1 . THR A 1 105 ? 18.360  -15.715 -33.848 1.00 35.58  ? 105  THR A OG1 1 
ATOM   622   C  CG2 . THR A 1 105 ? 17.876  -17.997 -33.266 1.00 52.39  ? 105  THR A CG2 1 
ATOM   623   N  N   . VAL A 1 106 ? 17.749  -13.703 -31.325 1.00 34.13  ? 106  VAL A N   1 
ATOM   624   C  CA  . VAL A 1 106 ? 18.434  -12.506 -30.821 1.00 31.76  ? 106  VAL A CA  1 
ATOM   625   C  C   . VAL A 1 106 ? 18.475  -12.465 -29.276 1.00 39.54  ? 106  VAL A C   1 
ATOM   626   O  O   . VAL A 1 106 ? 19.533  -12.263 -28.671 1.00 44.85  ? 106  VAL A O   1 
ATOM   627   C  CB  . VAL A 1 106 ? 17.812  -11.199 -31.395 1.00 45.49  ? 106  VAL A CB  1 
ATOM   628   C  CG1 . VAL A 1 106 ? 18.537  -9.955  -30.865 1.00 41.31  ? 106  VAL A CG1 1 
ATOM   629   C  CG2 . VAL A 1 106 ? 17.820  -11.225 -32.919 1.00 43.94  ? 106  VAL A CG2 1 
ATOM   630   N  N   . GLY A 1 107 ? 17.323  -12.670 -28.640 1.00 48.94  ? 107  GLY A N   1 
ATOM   631   C  CA  . GLY A 1 107 ? 17.243  -12.690 -27.187 1.00 33.93  ? 107  GLY A CA  1 
ATOM   632   C  C   . GLY A 1 107 ? 18.295  -13.607 -26.597 1.00 39.59  ? 107  GLY A C   1 
ATOM   633   O  O   . GLY A 1 107 ? 18.959  -13.273 -25.605 1.00 39.90  ? 107  GLY A O   1 
ATOM   634   N  N   . ARG A 1 108 ? 18.438  -14.776 -27.217 1.00 39.43  ? 108  ARG A N   1 
ATOM   635   C  CA  . ARG A 1 108 ? 19.475  -15.731 -26.844 1.00 37.31  ? 108  ARG A CA  1 
ATOM   636   C  C   . ARG A 1 108 ? 20.798  -15.014 -26.655 1.00 30.03  ? 108  ARG A C   1 
ATOM   637   O  O   . ARG A 1 108 ? 21.366  -15.018 -25.562 1.00 40.63  ? 108  ARG A O   1 
ATOM   638   C  CB  . ARG A 1 108 ? 19.627  -16.828 -27.906 1.00 29.01  ? 108  ARG A CB  1 
ATOM   639   C  CG  . ARG A 1 108 ? 20.965  -17.526 -27.836 1.00 37.49  ? 108  ARG A CG  1 
ATOM   640   C  CD  . ARG A 1 108 ? 21.186  -18.542 -28.949 1.00 48.15  ? 108  ARG A CD  1 
ATOM   641   N  NE  . ARG A 1 108 ? 20.630  -19.841 -28.600 1.00 50.35  ? 108  ARG A NE  1 
ATOM   642   C  CZ  . ARG A 1 108 ? 21.311  -20.948 -28.306 1.00 40.63  ? 108  ARG A CZ  1 
ATOM   643   N  NH1 . ARG A 1 108 ? 22.638  -20.988 -28.319 1.00 38.91  ? 108  ARG A NH1 1 
ATOM   644   N  NH2 . ARG A 1 108 ? 20.627  -22.043 -28.005 1.00 38.65  ? 108  ARG A NH2 1 
ATOM   645   N  N   . GLN A 1 109 ? 21.280  -14.384 -27.719 1.00 34.30  ? 109  GLN A N   1 
ATOM   646   C  CA  . GLN A 1 109 ? 22.592  -13.737 -27.678 1.00 46.20  ? 109  GLN A CA  1 
ATOM   647   C  C   . GLN A 1 109 ? 22.634  -12.539 -26.744 1.00 38.50  ? 109  GLN A C   1 
ATOM   648   O  O   . GLN A 1 109 ? 23.665  -12.298 -26.097 1.00 41.53  ? 109  GLN A O   1 
ATOM   649   C  CB  . GLN A 1 109 ? 23.072  -13.335 -29.074 1.00 47.17  ? 109  GLN A CB  1 
ATOM   650   C  CG  . GLN A 1 109 ? 23.860  -14.416 -29.774 1.00 43.44  ? 109  GLN A CG  1 
ATOM   651   C  CD  . GLN A 1 109 ? 24.943  -14.982 -28.891 1.00 49.76  ? 109  GLN A CD  1 
ATOM   652   O  OE1 . GLN A 1 109 ? 24.952  -16.177 -28.583 1.00 60.82  ? 109  GLN A OE1 1 
ATOM   653   N  NE2 . GLN A 1 109 ? 25.863  -14.127 -28.470 1.00 39.31  ? 109  GLN A NE2 1 
ATOM   654   N  N   . LEU A 1 110 ? 21.525  -11.799 -26.663 1.00 24.82  ? 110  LEU A N   1 
ATOM   655   C  CA  . LEU A 1 110 ? 21.454  -10.654 -25.753 1.00 32.50  ? 110  LEU A CA  1 
ATOM   656   C  C   . LEU A 1 110 ? 21.656  -11.050 -24.286 1.00 44.21  ? 110  LEU A C   1 
ATOM   657   O  O   . LEU A 1 110 ? 22.257  -10.301 -23.500 1.00 44.29  ? 110  LEU A O   1 
ATOM   658   C  CB  . LEU A 1 110 ? 20.134  -9.906  -25.909 1.00 33.76  ? 110  LEU A CB  1 
ATOM   659   C  CG  . LEU A 1 110 ? 19.973  -9.101  -27.202 1.00 38.28  ? 110  LEU A CG  1 
ATOM   660   C  CD1 . LEU A 1 110 ? 18.676  -8.326  -27.152 1.00 48.81  ? 110  LEU A CD1 1 
ATOM   661   C  CD2 . LEU A 1 110 ? 21.118  -8.149  -27.400 1.00 24.76  ? 110  LEU A CD2 1 
ATOM   662   N  N   . LEU A 1 111 ? 21.156  -12.225 -23.915 1.00 30.08  ? 111  LEU A N   1 
ATOM   663   C  CA  . LEU A 1 111 ? 21.308  -12.687 -22.547 1.00 19.43  ? 111  LEU A CA  1 
ATOM   664   C  C   . LEU A 1 111 ? 22.722  -13.172 -22.316 1.00 31.82  ? 111  LEU A C   1 
ATOM   665   O  O   . LEU A 1 111 ? 23.263  -13.037 -21.224 1.00 48.39  ? 111  LEU A O   1 
ATOM   666   C  CB  . LEU A 1 111 ? 20.310  -13.793 -22.230 1.00 43.68  ? 111  LEU A CB  1 
ATOM   667   C  CG  . LEU A 1 111 ? 18.881  -13.301 -22.025 1.00 42.40  ? 111  LEU A CG  1 
ATOM   668   C  CD1 . LEU A 1 111 ? 17.962  -14.443 -21.605 1.00 37.23  ? 111  LEU A CD1 1 
ATOM   669   C  CD2 . LEU A 1 111 ? 18.904  -12.201 -20.976 1.00 38.88  ? 111  LEU A CD2 1 
ATOM   670   N  N   . VAL A 1 112 ? 23.327  -13.741 -23.349 1.00 40.22  ? 112  VAL A N   1 
ATOM   671   C  CA  . VAL A 1 112 ? 24.709  -14.165 -23.254 1.00 33.21  ? 112  VAL A CA  1 
ATOM   672   C  C   . VAL A 1 112 ? 25.566  -12.932 -23.036 1.00 39.32  ? 112  VAL A C   1 
ATOM   673   O  O   . VAL A 1 112 ? 26.434  -12.910 -22.161 1.00 44.56  ? 112  VAL A O   1 
ATOM   674   C  CB  . VAL A 1 112 ? 25.136  -14.898 -24.524 1.00 38.99  ? 112  VAL A CB  1 
ATOM   675   C  CG1 . VAL A 1 112 ? 26.643  -14.885 -24.662 1.00 18.39  ? 112  VAL A CG1 1 
ATOM   676   C  CG2 . VAL A 1 112 ? 24.590  -16.331 -24.501 1.00 40.05  ? 112  VAL A CG2 1 
ATOM   677   N  N   . TYR A 1 113 ? 25.296  -11.896 -23.824 1.00 37.55  ? 113  TYR A N   1 
ATOM   678   C  CA  . TYR A 1 113 ? 25.923  -10.585 -23.643 1.00 42.50  ? 113  TYR A CA  1 
ATOM   679   C  C   . TYR A 1 113 ? 25.709  -9.969  -22.243 1.00 40.48  ? 113  TYR A C   1 
ATOM   680   O  O   . TYR A 1 113 ? 26.647  -9.478  -21.620 1.00 41.11  ? 113  TYR A O   1 
ATOM   681   C  CB  . TYR A 1 113 ? 25.403  -9.613  -24.707 1.00 40.80  ? 113  TYR A CB  1 
ATOM   682   C  CG  . TYR A 1 113 ? 25.850  -9.927  -26.121 1.00 51.38  ? 113  TYR A CG  1 
ATOM   683   C  CD1 . TYR A 1 113 ? 25.153  -9.425  -27.220 1.00 54.92  ? 113  TYR A CD1 1 
ATOM   684   C  CD2 . TYR A 1 113 ? 26.974  -10.713 -26.361 1.00 57.63  ? 113  TYR A CD2 1 
ATOM   685   C  CE1 . TYR A 1 113 ? 25.563  -9.701  -28.521 1.00 48.02  ? 113  TYR A CE1 1 
ATOM   686   C  CE2 . TYR A 1 113 ? 27.392  -10.994 -27.656 1.00 48.47  ? 113  TYR A CE2 1 
ATOM   687   C  CZ  . TYR A 1 113 ? 26.679  -10.488 -28.727 1.00 47.72  ? 113  TYR A CZ  1 
ATOM   688   O  OH  . TYR A 1 113 ? 27.085  -10.769 -30.007 1.00 53.72  ? 113  TYR A OH  1 
ATOM   689   N  N   . MET A 1 114 ? 24.473  -9.978  -21.759 1.00 29.49  ? 114  MET A N   1 
ATOM   690   C  CA  . MET A 1 114 ? 24.186  -9.422  -20.442 1.00 37.76  ? 114  MET A CA  1 
ATOM   691   C  C   . MET A 1 114 ? 25.050  -10.067 -19.348 1.00 38.25  ? 114  MET A C   1 
ATOM   692   O  O   . MET A 1 114 ? 25.700  -9.368  -18.584 1.00 44.27  ? 114  MET A O   1 
ATOM   693   C  CB  . MET A 1 114 ? 22.689  -9.546  -20.114 1.00 31.48  ? 114  MET A CB  1 
ATOM   694   C  CG  . MET A 1 114 ? 22.286  -9.006  -18.727 1.00 29.06  ? 114  MET A CG  1 
ATOM   695   S  SD  . MET A 1 114 ? 22.544  -7.219  -18.489 1.00 40.19  ? 114  MET A SD  1 
ATOM   696   C  CE  . MET A 1 114 ? 21.608  -6.610  -19.893 1.00 62.52  ? 114  MET A CE  1 
ATOM   697   N  N   . ALA A 1 115 ? 25.056  -11.396 -19.293 1.00 28.33  ? 115  ALA A N   1 
ATOM   698   C  CA  . ALA A 1 115 ? 25.832  -12.149 -18.313 1.00 31.88  ? 115  ALA A CA  1 
ATOM   699   C  C   . ALA A 1 115 ? 27.246  -11.601 -18.200 1.00 41.12  ? 115  ALA A C   1 
ATOM   700   O  O   . ALA A 1 115 ? 27.676  -11.157 -17.134 1.00 47.79  ? 115  ALA A O   1 
ATOM   701   C  CB  . ALA A 1 115 ? 25.877  -13.630 -18.705 1.00 34.79  ? 115  ALA A CB  1 
ATOM   702   N  N   . GLN A 1 116 ? 27.971  -11.645 -19.311 1.00 38.48  ? 116  GLN A N   1 
ATOM   703   C  CA  . GLN A 1 116 ? 29.318  -11.114 -19.360 1.00 31.76  ? 116  GLN A CA  1 
ATOM   704   C  C   . GLN A 1 116 ? 29.350  -9.647  -18.937 1.00 36.26  ? 116  GLN A C   1 
ATOM   705   O  O   . GLN A 1 116 ? 30.154  -9.259  -18.087 1.00 42.64  ? 116  GLN A O   1 
ATOM   706   C  CB  . GLN A 1 116 ? 29.864  -11.260 -20.769 1.00 23.24  ? 116  GLN A CB  1 
ATOM   707   C  CG  . GLN A 1 116 ? 30.003  -12.705 -21.243 1.00 28.06  ? 116  GLN A CG  1 
ATOM   708   C  CD  . GLN A 1 116 ? 30.308  -12.793 -22.744 1.00 37.80  ? 116  GLN A CD  1 
ATOM   709   O  OE1 . GLN A 1 116 ? 31.466  -12.702 -23.173 1.00 34.32  ? 116  GLN A OE1 1 
ATOM   710   N  NE2 . GLN A 1 116 ? 29.261  -12.946 -23.546 1.00 34.91  ? 116  GLN A NE2 1 
ATOM   711   N  N   . TYR A 1 117 ? 28.462  -8.847  -19.528 1.00 27.35  ? 117  TYR A N   1 
ATOM   712   C  CA  . TYR A 1 117 ? 28.384  -7.414  -19.256 1.00 25.52  ? 117  TYR A CA  1 
ATOM   713   C  C   . TYR A 1 117 ? 28.272  -7.098  -17.765 1.00 33.88  ? 117  TYR A C   1 
ATOM   714   O  O   . TYR A 1 117 ? 29.077  -6.359  -17.199 1.00 41.79  ? 117  TYR A O   1 
ATOM   715   C  CB  . TYR A 1 117 ? 27.201  -6.798  -19.999 1.00 28.68  ? 117  TYR A CB  1 
ATOM   716   C  CG  . TYR A 1 117 ? 27.097  -5.303  -19.825 1.00 25.31  ? 117  TYR A CG  1 
ATOM   717   C  CD1 . TYR A 1 117 ? 27.849  -4.442  -20.609 1.00 33.72  ? 117  TYR A CD1 1 
ATOM   718   C  CD2 . TYR A 1 117 ? 26.254  -4.752  -18.871 1.00 32.09  ? 117  TYR A CD2 1 
ATOM   719   C  CE1 . TYR A 1 117 ? 27.770  -3.071  -20.453 1.00 39.02  ? 117  TYR A CE1 1 
ATOM   720   C  CE2 . TYR A 1 117 ? 26.159  -3.375  -18.701 1.00 37.83  ? 117  TYR A CE2 1 
ATOM   721   C  CZ  . TYR A 1 117 ? 26.922  -2.540  -19.498 1.00 41.57  ? 117  TYR A CZ  1 
ATOM   722   O  OH  . TYR A 1 117 ? 26.845  -1.179  -19.339 1.00 35.04  ? 117  TYR A OH  1 
ATOM   723   N  N   . LEU A 1 118 ? 27.263  -7.661  -17.126 1.00 29.39  ? 118  LEU A N   1 
ATOM   724   C  CA  . LEU A 1 118 ? 27.067  -7.459  -15.704 1.00 35.02  ? 118  LEU A CA  1 
ATOM   725   C  C   . LEU A 1 118 ? 28.292  -7.854  -14.903 1.00 43.59  ? 118  LEU A C   1 
ATOM   726   O  O   . LEU A 1 118 ? 28.812  -7.066  -14.122 1.00 53.64  ? 118  LEU A O   1 
ATOM   727   C  CB  . LEU A 1 118 ? 25.853  -8.248  -15.213 1.00 37.45  ? 118  LEU A CB  1 
ATOM   728   C  CG  . LEU A 1 118 ? 24.531  -7.597  -15.596 1.00 41.95  ? 118  LEU A CG  1 
ATOM   729   C  CD1 . LEU A 1 118 ? 23.352  -8.450  -15.156 1.00 48.32  ? 118  LEU A CD1 1 
ATOM   730   C  CD2 . LEU A 1 118 ? 24.459  -6.190  -15.004 1.00 44.67  ? 118  LEU A CD2 1 
ATOM   731   N  N   . LEU A 1 119 ? 28.749  -9.082  -15.085 1.00 42.26  ? 119  LEU A N   1 
ATOM   732   C  CA  . LEU A 1 119 ? 29.868  -9.565  -14.295 1.00 47.95  ? 119  LEU A CA  1 
ATOM   733   C  C   . LEU A 1 119 ? 31.115  -8.727  -14.486 1.00 47.04  ? 119  LEU A C   1 
ATOM   734   O  O   . LEU A 1 119 ? 31.678  -8.230  -13.513 1.00 49.75  ? 119  LEU A O   1 
ATOM   735   C  CB  . LEU A 1 119 ? 30.156  -11.030 -14.602 1.00 49.30  ? 119  LEU A CB  1 
ATOM   736   C  CG  . LEU A 1 119 ? 29.206  -11.975 -13.874 1.00 43.62  ? 119  LEU A CG  1 
ATOM   737   C  CD1 . LEU A 1 119 ? 29.427  -13.421 -14.329 1.00 44.84  ? 119  LEU A CD1 1 
ATOM   738   C  CD2 . LEU A 1 119 ? 29.380  -11.813 -12.361 1.00 29.91  ? 119  LEU A CD2 1 
ATOM   739   N  N   . GLY A 1 120 ? 31.532  -8.561  -15.738 1.00 43.80  ? 120  GLY A N   1 
ATOM   740   C  CA  . GLY A 1 120 ? 32.778  -7.874  -16.046 1.00 39.95  ? 120  GLY A CA  1 
ATOM   741   C  C   . GLY A 1 120 ? 32.753  -6.369  -15.812 1.00 42.96  ? 120  GLY A C   1 
ATOM   742   O  O   . GLY A 1 120 ? 33.788  -5.705  -15.908 1.00 43.59  ? 120  GLY A O   1 
ATOM   743   N  N   . ASN A 1 121 ? 31.580  -5.827  -15.495 1.00 41.16  ? 121  ASN A N   1 
ATOM   744   C  CA  . ASN A 1 121 ? 31.466  -4.398  -15.259 1.00 44.33  ? 121  ASN A CA  1 
ATOM   745   C  C   . ASN A 1 121 ? 30.955  -3.982  -13.883 1.00 44.65  ? 121  ASN A C   1 
ATOM   746   O  O   . ASN A 1 121 ? 31.176  -2.844  -13.465 1.00 45.90  ? 121  ASN A O   1 
ATOM   747   C  CB  . ASN A 1 121 ? 30.619  -3.758  -16.346 1.00 47.21  ? 121  ASN A CB  1 
ATOM   748   C  CG  . ASN A 1 121 ? 31.363  -3.647  -17.650 1.00 52.22  ? 121  ASN A CG  1 
ATOM   749   O  OD1 . ASN A 1 121 ? 32.104  -2.687  -17.879 1.00 50.98  ? 121  ASN A OD1 1 
ATOM   750   N  ND2 . ASN A 1 121 ? 31.178  -4.634  -18.518 1.00 57.38  ? 121  ASN A ND2 1 
ATOM   751   N  N   . HIS A 1 122 ? 30.296  -4.903  -13.185 1.00 28.20  ? 122  HIS A N   1 
ATOM   752   C  CA  . HIS A 1 122 ? 29.639  -4.603  -11.907 1.00 42.88  ? 122  HIS A CA  1 
ATOM   753   C  C   . HIS A 1 122 ? 30.543  -3.964  -10.835 1.00 50.21  ? 122  HIS A C   1 
ATOM   754   O  O   . HIS A 1 122 ? 30.069  -3.193  -9.997  1.00 51.27  ? 122  HIS A O   1 
ATOM   755   C  CB  . HIS A 1 122 ? 28.945  -5.852  -11.330 1.00 57.15  ? 122  HIS A CB  1 
ATOM   756   C  CG  . HIS A 1 122 ? 29.830  -6.692  -10.459 1.00 63.93  ? 122  HIS A CG  1 
ATOM   757   N  ND1 . HIS A 1 122 ? 30.588  -7.732  -10.953 1.00 68.75  ? 122  HIS A ND1 1 
ATOM   758   C  CD2 . HIS A 1 122 ? 30.080  -6.641  -9.128  1.00 55.31  ? 122  HIS A CD2 1 
ATOM   759   C  CE1 . HIS A 1 122 ? 31.267  -8.287  -9.963  1.00 68.79  ? 122  HIS A CE1 1 
ATOM   760   N  NE2 . HIS A 1 122 ? 30.978  -7.644  -8.846  1.00 58.48  ? 122  HIS A NE2 1 
ATOM   761   N  N   . GLU A 1 123 ? 31.831  -4.281  -10.841 1.00 49.11  ? 123  GLU A N   1 
ATOM   762   C  CA  . GLU A 1 123 ? 32.732  -3.631  -9.892  1.00 57.40  ? 123  GLU A CA  1 
ATOM   763   C  C   . GLU A 1 123 ? 33.254  -2.282  -10.401 1.00 54.13  ? 123  GLU A C   1 
ATOM   764   O  O   . GLU A 1 123 ? 33.688  -1.448  -9.609  1.00 46.41  ? 123  GLU A O   1 
ATOM   765   C  CB  . GLU A 1 123 ? 33.896  -4.548  -9.505  1.00 71.57  ? 123  GLU A CB  1 
ATOM   766   C  CG  . GLU A 1 123 ? 33.483  -5.744  -8.657  1.00 91.32  ? 123  GLU A CG  1 
ATOM   767   C  CD  . GLU A 1 123 ? 34.652  -6.377  -7.914  1.00 107.68 ? 123  GLU A CD  1 
ATOM   768   O  OE1 . GLU A 1 123 ? 35.812  -6.201  -8.347  1.00 113.09 ? 123  GLU A OE1 1 
ATOM   769   O  OE2 . GLU A 1 123 ? 34.409  -7.054  -6.890  1.00 114.25 ? 123  GLU A OE2 1 
ATOM   770   N  N   . ARG A 1 124 ? 33.196  -2.072  -11.717 1.00 52.96  ? 124  ARG A N   1 
ATOM   771   C  CA  . ARG A 1 124 ? 33.723  -0.851  -12.327 1.00 54.30  ? 124  ARG A CA  1 
ATOM   772   C  C   . ARG A 1 124 ? 32.661  0.222   -12.453 1.00 49.14  ? 124  ARG A C   1 
ATOM   773   O  O   . ARG A 1 124 ? 32.934  1.406   -12.247 1.00 49.93  ? 124  ARG A O   1 
ATOM   774   C  CB  . ARG A 1 124 ? 34.334  -1.106  -13.719 1.00 71.38  ? 124  ARG A CB  1 
ATOM   775   C  CG  . ARG A 1 124 ? 34.183  -2.520  -14.288 1.00 76.85  ? 124  ARG A CG  1 
ATOM   776   C  CD  . ARG A 1 124 ? 34.442  -2.538  -15.799 1.00 78.61  ? 124  ARG A CD  1 
ATOM   777   N  NE  . ARG A 1 124 ? 35.528  -1.643  -16.204 1.00 84.93  ? 124  ARG A NE  1 
ATOM   778   C  CZ  . ARG A 1 124 ? 36.740  -2.046  -16.591 1.00 92.79  ? 124  ARG A CZ  1 
ATOM   779   N  NH1 . ARG A 1 124 ? 37.033  -3.342  -16.637 1.00 95.54  ? 124  ARG A NH1 1 
ATOM   780   N  NH2 . ARG A 1 124 ? 37.665  -1.155  -16.941 1.00 88.30  ? 124  ARG A NH2 1 
ATOM   781   N  N   . ILE A 1 125 ? 31.454  -0.194  -12.814 1.00 40.49  ? 125  ILE A N   1 
ATOM   782   C  CA  . ILE A 1 125 ? 30.360  0.751   -13.002 1.00 47.47  ? 125  ILE A CA  1 
ATOM   783   C  C   . ILE A 1 125 ? 29.345  0.723   -11.848 1.00 57.30  ? 125  ILE A C   1 
ATOM   784   O  O   . ILE A 1 125 ? 28.661  -0.283  -11.637 1.00 60.89  ? 125  ILE A O   1 
ATOM   785   C  CB  . ILE A 1 125 ? 29.636  0.527   -14.346 1.00 48.98  ? 125  ILE A CB  1 
ATOM   786   C  CG1 . ILE A 1 125 ? 30.459  1.093   -15.508 1.00 54.18  ? 125  ILE A CG1 1 
ATOM   787   C  CG2 . ILE A 1 125 ? 28.266  1.186   -14.316 1.00 48.69  ? 125  ILE A CG2 1 
ATOM   788   C  CD1 . ILE A 1 125 ? 31.803  0.418   -15.721 1.00 57.86  ? 125  ILE A CD1 1 
ATOM   789   N  N   . SER A 1 126 ? 29.246  1.845   -11.129 1.00 73.62  ? 126  SER A N   1 
ATOM   790   C  CA  . SER A 1 126 ? 28.426  1.975   -9.912  1.00 68.62  ? 126  SER A CA  1 
ATOM   791   C  C   . SER A 1 126 ? 26.971  1.503   -10.066 1.00 57.22  ? 126  SER A C   1 
ATOM   792   O  O   . SER A 1 126 ? 26.529  0.615   -9.343  1.00 42.51  ? 126  SER A O   1 
ATOM   793   C  CB  . SER A 1 126 ? 28.470  3.417   -9.387  1.00 64.28  ? 126  SER A CB  1 
ATOM   794   O  OG  . SER A 1 126 ? 28.266  3.460   -7.986  1.00 66.28  ? 126  SER A OG  1 
ATOM   795   N  N   . ASP A 1 127 ? 26.231  2.103   -10.996 1.00 61.06  ? 127  ASP A N   1 
ATOM   796   C  CA  . ASP A 1 127 ? 24.869  1.661   -11.311 1.00 63.95  ? 127  ASP A CA  1 
ATOM   797   C  C   . ASP A 1 127 ? 24.728  0.136   -11.285 1.00 56.95  ? 127  ASP A C   1 
ATOM   798   O  O   . ASP A 1 127 ? 23.911  -0.409  -10.538 1.00 61.49  ? 127  ASP A O   1 
ATOM   799   C  CB  . ASP A 1 127 ? 24.438  2.180   -12.690 1.00 76.52  ? 127  ASP A CB  1 
ATOM   800   C  CG  . ASP A 1 127 ? 23.936  3.611   -12.651 1.00 85.58  ? 127  ASP A CG  1 
ATOM   801   O  OD1 . ASP A 1 127 ? 23.269  3.983   -11.662 1.00 84.77  ? 127  ASP A OD1 1 
ATOM   802   O  OD2 . ASP A 1 127 ? 24.194  4.359   -13.619 1.00 91.95  ? 127  ASP A OD2 1 
ATOM   803   N  N   . LEU A 1 128 ? 25.526  -0.538  -12.114 1.00 53.54  ? 128  LEU A N   1 
ATOM   804   C  CA  . LEU A 1 128 ? 25.531  -1.998  -12.221 1.00 42.39  ? 128  LEU A CA  1 
ATOM   805   C  C   . LEU A 1 128 ? 25.894  -2.668  -10.896 1.00 49.31  ? 128  LEU A C   1 
ATOM   806   O  O   . LEU A 1 128 ? 25.209  -3.590  -10.438 1.00 46.63  ? 128  LEU A O   1 
ATOM   807   C  CB  . LEU A 1 128 ? 26.523  -2.440  -13.302 1.00 44.83  ? 128  LEU A CB  1 
ATOM   808   C  CG  . LEU A 1 128 ? 26.300  -1.916  -14.725 1.00 45.43  ? 128  LEU A CG  1 
ATOM   809   C  CD1 . LEU A 1 128 ? 27.425  -2.377  -15.671 1.00 47.82  ? 128  LEU A CD1 1 
ATOM   810   C  CD2 . LEU A 1 128 ? 24.942  -2.348  -15.246 1.00 37.39  ? 128  LEU A CD2 1 
ATOM   811   N  N   . GLY A 1 129 ? 26.985  -2.211  -10.287 1.00 50.64  ? 129  GLY A N   1 
ATOM   812   C  CA  . GLY A 1 129 ? 27.388  -2.718  -8.990  1.00 48.85  ? 129  GLY A CA  1 
ATOM   813   C  C   . GLY A 1 129 ? 26.203  -2.690  -8.052  1.00 49.10  ? 129  GLY A C   1 
ATOM   814   O  O   . GLY A 1 129 ? 26.013  -3.604  -7.245  1.00 54.75  ? 129  GLY A O   1 
ATOM   815   N  N   . GLN A 1 130 ? 25.390  -1.643  -8.180  1.00 32.98  ? 130  GLN A N   1 
ATOM   816   C  CA  . GLN A 1 130 ? 24.272  -1.437  -7.271  1.00 43.69  ? 130  GLN A CA  1 
ATOM   817   C  C   . GLN A 1 130 ? 23.106  -2.305  -7.689  1.00 38.02  ? 130  GLN A C   1 
ATOM   818   O  O   . GLN A 1 130 ? 22.381  -2.843  -6.849  1.00 37.19  ? 130  GLN A O   1 
ATOM   819   C  CB  . GLN A 1 130 ? 23.866  0.034   -7.239  1.00 47.85  ? 130  GLN A CB  1 
ATOM   820   C  CG  . GLN A 1 130 ? 23.241  0.466   -5.911  1.00 56.56  ? 130  GLN A CG  1 
ATOM   821   C  CD  . GLN A 1 130 ? 21.788  0.057   -5.793  1.00 54.11  ? 130  GLN A CD  1 
ATOM   822   O  OE1 . GLN A 1 130 ? 21.149  -0.250  -6.795  1.00 64.97  ? 130  GLN A OE1 1 
ATOM   823   N  NE2 . GLN A 1 130 ? 21.255  0.056   -4.572  1.00 52.42  ? 130  GLN A NE2 1 
ATOM   824   N  N   . LEU A 1 131 ? 22.929  -2.439  -8.995  1.00 32.45  ? 131  LEU A N   1 
ATOM   825   C  CA  . LEU A 1 131 ? 21.921  -3.343  -9.528  1.00 38.21  ? 131  LEU A CA  1 
ATOM   826   C  C   . LEU A 1 131 ? 22.154  -4.763  -9.005  1.00 30.51  ? 131  LEU A C   1 
ATOM   827   O  O   . LEU A 1 131 ? 21.249  -5.416  -8.493  1.00 28.81  ? 131  LEU A O   1 
ATOM   828   C  CB  . LEU A 1 131 ? 21.981  -3.348  -11.057 1.00 33.88  ? 131  LEU A CB  1 
ATOM   829   C  CG  . LEU A 1 131 ? 20.983  -4.287  -11.730 1.00 37.82  ? 131  LEU A CG  1 
ATOM   830   C  CD1 . LEU A 1 131 ? 19.571  -3.790  -11.468 1.00 29.34  ? 131  LEU A CD1 1 
ATOM   831   C  CD2 . LEU A 1 131 ? 21.273  -4.401  -13.222 1.00 32.46  ? 131  LEU A CD2 1 
ATOM   832   N  N   . VAL A 1 132 ? 23.391  -5.222  -9.127  1.00 31.06  ? 132  VAL A N   1 
ATOM   833   C  CA  . VAL A 1 132 ? 23.755  -6.585  -8.755  1.00 38.44  ? 132  VAL A CA  1 
ATOM   834   C  C   . VAL A 1 132 ? 23.647  -6.836  -7.254  1.00 49.12  ? 132  VAL A C   1 
ATOM   835   O  O   . VAL A 1 132 ? 23.191  -7.906  -6.827  1.00 56.82  ? 132  VAL A O   1 
ATOM   836   C  CB  . VAL A 1 132 ? 25.189  -6.928  -9.217  1.00 37.35  ? 132  VAL A CB  1 
ATOM   837   C  CG1 . VAL A 1 132 ? 25.608  -8.277  -8.666  1.00 46.60  ? 132  VAL A CG1 1 
ATOM   838   C  CG2 . VAL A 1 132 ? 25.264  -6.933  -10.732 1.00 30.19  ? 132  VAL A CG2 1 
ATOM   839   N  N   . ASN A 1 133 ? 24.087  -5.855  -6.467  1.00 43.73  ? 133  ASN A N   1 
ATOM   840   C  CA  . ASN A 1 133 ? 24.019  -5.934  -5.018  1.00 35.08  ? 133  ASN A CA  1 
ATOM   841   C  C   . ASN A 1 133 ? 22.586  -6.121  -4.511  1.00 37.99  ? 133  ASN A C   1 
ATOM   842   O  O   . ASN A 1 133 ? 22.349  -6.809  -3.513  1.00 43.87  ? 133  ASN A O   1 
ATOM   843   C  CB  . ASN A 1 133 ? 24.620  -4.670  -4.402  1.00 48.38  ? 133  ASN A CB  1 
ATOM   844   C  CG  . ASN A 1 133 ? 26.125  -4.740  -4.274  1.00 49.07  ? 133  ASN A CG  1 
ATOM   845   O  OD1 . ASN A 1 133 ? 26.765  -5.655  -4.795  1.00 41.88  ? 133  ASN A OD1 1 
ATOM   846   N  ND2 . ASN A 1 133 ? 26.700  -3.771  -3.571  1.00 57.67  ? 133  ASN A ND2 1 
ATOM   847   N  N   . SER A 1 134 ? 21.634  -5.519  -5.216  1.00 31.36  ? 134  SER A N   1 
ATOM   848   C  CA  . SER A 1 134 ? 20.277  -5.374  -4.703  1.00 36.34  ? 134  SER A CA  1 
ATOM   849   C  C   . SER A 1 134 ? 19.291  -6.324  -5.350  1.00 38.92  ? 134  SER A C   1 
ATOM   850   O  O   . SER A 1 134 ? 18.133  -6.392  -4.936  1.00 39.10  ? 134  SER A O   1 
ATOM   851   C  CB  . SER A 1 134 ? 19.794  -3.938  -4.913  1.00 38.35  ? 134  SER A CB  1 
ATOM   852   O  OG  . SER A 1 134 ? 19.960  -3.547  -6.267  1.00 35.99  ? 134  SER A OG  1 
ATOM   853   N  N   . THR A 1 135 ? 19.746  -7.043  -6.371  1.00 43.56  ? 135  THR A N   1 
ATOM   854   C  CA  . THR A 1 135 ? 18.870  -7.945  -7.115  1.00 40.61  ? 135  THR A CA  1 
ATOM   855   C  C   . THR A 1 135 ? 19.508  -9.300  -7.325  1.00 30.10  ? 135  THR A C   1 
ATOM   856   O  O   . THR A 1 135 ? 20.714  -9.402  -7.560  1.00 43.64  ? 135  THR A O   1 
ATOM   857   C  CB  . THR A 1 135 ? 18.511  -7.385  -8.505  1.00 47.09  ? 135  THR A CB  1 
ATOM   858   O  OG1 . THR A 1 135 ? 18.454  -5.949  -8.465  1.00 34.07  ? 135  THR A OG1 1 
ATOM   859   C  CG2 . THR A 1 135 ? 17.171  -7.943  -8.958  1.00 39.38  ? 135  THR A CG2 1 
ATOM   860   N  N   . ASP A 1 136 ? 18.688  -10.339 -7.243  1.00 35.13  ? 136  ASP A N   1 
ATOM   861   C  CA  . ASP A 1 136 ? 19.137  -11.704 -7.493  1.00 34.92  ? 136  ASP A CA  1 
ATOM   862   C  C   . ASP A 1 136 ? 18.721  -12.106 -8.900  1.00 37.40  ? 136  ASP A C   1 
ATOM   863   O  O   . ASP A 1 136 ? 17.537  -12.347 -9.169  1.00 27.30  ? 136  ASP A O   1 
ATOM   864   C  CB  . ASP A 1 136 ? 18.504  -12.647 -6.489  1.00 50.01  ? 136  ASP A CB  1 
ATOM   865   C  CG  . ASP A 1 136 ? 19.502  -13.582 -5.873  1.00 63.46  ? 136  ASP A CG  1 
ATOM   866   O  OD1 . ASP A 1 136 ? 20.456  -13.107 -5.220  1.00 59.80  ? 136  ASP A OD1 1 
ATOM   867   O  OD2 . ASP A 1 136 ? 19.320  -14.802 -6.031  1.00 79.46  ? 136  ASP A OD2 1 
ATOM   868   N  N   . ILE A 1 137 ? 19.697  -12.184 -9.795  1.00 21.81  ? 137  ILE A N   1 
ATOM   869   C  CA  . ILE A 1 137 ? 19.396  -12.265 -11.200 1.00 12.82  ? 137  ILE A CA  1 
ATOM   870   C  C   . ILE A 1 137 ? 19.727  -13.618 -11.833 1.00 29.48  ? 137  ILE A C   1 
ATOM   871   O  O   . ILE A 1 137 ? 20.827  -14.148 -11.662 1.00 30.61  ? 137  ILE A O   1 
ATOM   872   C  CB  . ILE A 1 137 ? 20.106  -11.149 -11.947 1.00 23.67  ? 137  ILE A CB  1 
ATOM   873   C  CG1 . ILE A 1 137 ? 19.628  -9.773  -11.433 1.00 26.06  ? 137  ILE A CG1 1 
ATOM   874   C  CG2 . ILE A 1 137 ? 19.897  -11.313 -13.445 1.00 27.51  ? 137  ILE A CG2 1 
ATOM   875   C  CD1 . ILE A 1 137 ? 20.555  -8.596  -11.817 1.00 19.88  ? 137  ILE A CD1 1 
ATOM   876   N  N   . TYR A 1 138 ? 18.759  -14.167 -12.567 1.00 34.27  ? 138  TYR A N   1 
ATOM   877   C  CA  . TYR A 1 138 ? 18.929  -15.421 -13.303 1.00 25.92  ? 138  TYR A CA  1 
ATOM   878   C  C   . TYR A 1 138 ? 18.734  -15.254 -14.819 1.00 30.46  ? 138  TYR A C   1 
ATOM   879   O  O   . TYR A 1 138 ? 17.709  -14.720 -15.281 1.00 23.13  ? 138  TYR A O   1 
ATOM   880   C  CB  . TYR A 1 138 ? 17.944  -16.470 -12.800 1.00 30.80  ? 138  TYR A CB  1 
ATOM   881   C  CG  . TYR A 1 138 ? 18.122  -16.849 -11.357 1.00 30.85  ? 138  TYR A CG  1 
ATOM   882   C  CD1 . TYR A 1 138 ? 17.650  -16.036 -10.346 1.00 24.34  ? 138  TYR A CD1 1 
ATOM   883   C  CD2 . TYR A 1 138 ? 18.748  -18.035 -11.010 1.00 27.47  ? 138  TYR A CD2 1 
ATOM   884   C  CE1 . TYR A 1 138 ? 17.798  -16.392 -9.029  1.00 29.98  ? 138  TYR A CE1 1 
ATOM   885   C  CE2 . TYR A 1 138 ? 18.899  -18.400 -9.701  1.00 22.62  ? 138  TYR A CE2 1 
ATOM   886   C  CZ  . TYR A 1 138 ? 18.423  -17.577 -8.711  1.00 31.54  ? 138  TYR A CZ  1 
ATOM   887   O  OH  . TYR A 1 138 ? 18.574  -17.917 -7.383  1.00 38.91  ? 138  TYR A OH  1 
ATOM   888   N  N   . LEU A 1 139 ? 19.716  -15.735 -15.580 1.00 34.98  ? 139  LEU A N   1 
ATOM   889   C  CA  . LEU A 1 139 ? 19.711  -15.615 -17.035 1.00 32.89  ? 139  LEU A CA  1 
ATOM   890   C  C   . LEU A 1 139 ? 19.645  -16.981 -17.731 1.00 37.72  ? 139  LEU A C   1 
ATOM   891   O  O   . LEU A 1 139 ? 20.504  -17.856 -17.526 1.00 31.42  ? 139  LEU A O   1 
ATOM   892   C  CB  . LEU A 1 139 ? 20.936  -14.832 -17.514 1.00 19.97  ? 139  LEU A CB  1 
ATOM   893   C  CG  . LEU A 1 139 ? 21.222  -13.494 -16.826 1.00 28.64  ? 139  LEU A CG  1 
ATOM   894   C  CD1 . LEU A 1 139 ? 22.461  -12.833 -17.439 1.00 20.02  ? 139  LEU A CD1 1 
ATOM   895   C  CD2 . LEU A 1 139 ? 20.000  -12.579 -16.912 1.00 25.02  ? 139  LEU A CD2 1 
ATOM   896   N  N   . VAL A 1 140 ? 18.609  -17.149 -18.550 1.00 38.42  ? 140  VAL A N   1 
ATOM   897   C  CA  . VAL A 1 140 ? 18.405  -18.361 -19.330 1.00 36.81  ? 140  VAL A CA  1 
ATOM   898   C  C   . VAL A 1 140 ? 18.403  -18.010 -20.826 1.00 41.08  ? 140  VAL A C   1 
ATOM   899   O  O   . VAL A 1 140 ? 17.341  -17.774 -21.424 1.00 45.18  ? 140  VAL A O   1 
ATOM   900   C  CB  . VAL A 1 140 ? 17.069  -19.045 -18.953 1.00 36.81  ? 140  VAL A CB  1 
ATOM   901   C  CG1 . VAL A 1 140 ? 16.965  -20.434 -19.592 1.00 18.13  ? 140  VAL A CG1 1 
ATOM   902   C  CG2 . VAL A 1 140 ? 16.918  -19.133 -17.435 1.00 41.91  ? 140  VAL A CG2 1 
ATOM   903   N  N   . PRO A 1 141 ? 19.598  -17.960 -21.435 1.00 38.78  ? 141  PRO A N   1 
ATOM   904   C  CA  . PRO A 1 141 ? 19.770  -17.645 -22.861 1.00 43.74  ? 141  PRO A CA  1 
ATOM   905   C  C   . PRO A 1 141 ? 18.892  -18.491 -23.793 1.00 40.31  ? 141  PRO A C   1 
ATOM   906   O  O   . PRO A 1 141 ? 18.362  -17.971 -24.775 1.00 43.31  ? 141  PRO A O   1 
ATOM   907   C  CB  . PRO A 1 141 ? 21.256  -17.948 -23.104 1.00 33.44  ? 141  PRO A CB  1 
ATOM   908   C  CG  . PRO A 1 141 ? 21.890  -17.723 -21.796 1.00 37.41  ? 141  PRO A CG  1 
ATOM   909   C  CD  . PRO A 1 141 ? 20.892  -18.165 -20.761 1.00 44.90  ? 141  PRO A CD  1 
ATOM   910   N  N   . THR A 1 142 ? 18.759  -19.783 -23.507 1.00 39.16  ? 142  THR A N   1 
ATOM   911   C  CA  . THR A 1 142 ? 17.859  -20.635 -24.278 1.00 41.38  ? 142  THR A CA  1 
ATOM   912   C  C   . THR A 1 142 ? 17.041  -21.567 -23.401 1.00 45.31  ? 142  THR A C   1 
ATOM   913   O  O   . THR A 1 142 ? 17.481  -22.010 -22.329 1.00 38.35  ? 142  THR A O   1 
ATOM   914   C  CB  . THR A 1 142 ? 18.580  -21.488 -25.344 1.00 36.40  ? 142  THR A CB  1 
ATOM   915   O  OG1 . THR A 1 142 ? 17.606  -22.274 -26.042 1.00 45.18  ? 142  THR A OG1 1 
ATOM   916   C  CG2 . THR A 1 142 ? 19.567  -22.433 -24.703 1.00 34.18  ? 142  THR A CG2 1 
ATOM   917   N  N   . MET A 1 143 ? 15.848  -21.864 -23.898 1.00 53.02  ? 143  MET A N   1 
ATOM   918   C  CA  . MET A 1 143 ? 14.883  -22.720 -23.227 1.00 41.76  ? 143  MET A CA  1 
ATOM   919   C  C   . MET A 1 143 ? 14.495  -23.812 -24.235 1.00 45.39  ? 143  MET A C   1 
ATOM   920   O  O   . MET A 1 143 ? 13.711  -24.717 -23.937 1.00 38.37  ? 143  MET A O   1 
ATOM   921   C  CB  . MET A 1 143 ? 13.682  -21.867 -22.821 1.00 31.00  ? 143  MET A CB  1 
ATOM   922   C  CG  . MET A 1 143 ? 12.671  -22.547 -21.956 1.00 38.22  ? 143  MET A CG  1 
ATOM   923   S  SD  . MET A 1 143 ? 11.175  -21.548 -21.834 1.00 40.50  ? 143  MET A SD  1 
ATOM   924   C  CE  . MET A 1 143 ? 9.949   -22.853 -21.702 1.00 28.22  ? 143  MET A CE  1 
ATOM   925   N  N   . ASN A 1 144 ? 15.067  -23.718 -25.435 1.00 34.12  ? 144  ASN A N   1 
ATOM   926   C  CA  . ASN A 1 144 ? 14.808  -24.688 -26.483 1.00 35.06  ? 144  ASN A CA  1 
ATOM   927   C  C   . ASN A 1 144 ? 16.045  -24.954 -27.351 1.00 48.07  ? 144  ASN A C   1 
ATOM   928   O  O   . ASN A 1 144 ? 16.120  -24.514 -28.507 1.00 38.97  ? 144  ASN A O   1 
ATOM   929   C  CB  . ASN A 1 144 ? 13.637  -24.235 -27.341 1.00 35.67  ? 144  ASN A CB  1 
ATOM   930   C  CG  . ASN A 1 144 ? 13.231  -25.277 -28.356 1.00 46.59  ? 144  ASN A CG  1 
ATOM   931   O  OD1 . ASN A 1 144 ? 13.722  -26.412 -28.331 1.00 50.48  ? 144  ASN A OD1 1 
ATOM   932   N  ND2 . ASN A 1 144 ? 12.330  -24.903 -29.258 1.00 47.99  ? 144  ASN A ND2 1 
ATOM   933   N  N   . PRO A 1 145 ? 17.019  -25.689 -26.785 1.00 43.43  ? 145  PRO A N   1 
ATOM   934   C  CA  . PRO A 1 145 ? 18.265  -26.059 -27.470 1.00 34.76  ? 145  PRO A CA  1 
ATOM   935   C  C   . PRO A 1 145 ? 17.993  -26.919 -28.704 1.00 38.22  ? 145  PRO A C   1 
ATOM   936   O  O   . PRO A 1 145 ? 18.620  -26.751 -29.752 1.00 47.73  ? 145  PRO A O   1 
ATOM   937   C  CB  . PRO A 1 145 ? 19.018  -26.900 -26.423 1.00 29.82  ? 145  PRO A CB  1 
ATOM   938   C  CG  . PRO A 1 145 ? 18.269  -26.742 -25.140 1.00 32.23  ? 145  PRO A CG  1 
ATOM   939   C  CD  . PRO A 1 145 ? 16.878  -26.345 -25.471 1.00 28.58  ? 145  PRO A CD  1 
ATOM   940   N  N   . ASP A 1 146 ? 17.068  -27.856 -28.554 1.00 33.73  ? 146  ASP A N   1 
ATOM   941   C  CA  . ASP A 1 146 ? 16.763  -28.796 -29.605 1.00 39.32  ? 146  ASP A CA  1 
ATOM   942   C  C   . ASP A 1 146 ? 16.120  -28.019 -30.735 1.00 40.02  ? 146  ASP A C   1 
ATOM   943   O  O   . ASP A 1 146 ? 16.378  -28.275 -31.917 1.00 51.24  ? 146  ASP A O   1 
ATOM   944   C  CB  . ASP A 1 146 ? 15.831  -29.904 -29.085 1.00 43.55  ? 146  ASP A CB  1 
ATOM   945   C  CG  . ASP A 1 146 ? 16.521  -30.840 -28.087 1.00 40.75  ? 146  ASP A CG  1 
ATOM   946   O  OD1 . ASP A 1 146 ? 17.632  -30.519 -27.616 1.00 36.05  ? 146  ASP A OD1 1 
ATOM   947   O  OD2 . ASP A 1 146 ? 15.954  -31.903 -27.772 1.00 35.44  ? 146  ASP A OD2 1 
ATOM   948   N  N   . GLY A 1 147 ? 15.288  -27.055 -30.358 1.00 31.21  ? 147  GLY A N   1 
ATOM   949   C  CA  . GLY A 1 147 ? 14.606  -26.219 -31.328 1.00 35.88  ? 147  GLY A CA  1 
ATOM   950   C  C   . GLY A 1 147 ? 15.616  -25.382 -32.070 1.00 34.57  ? 147  GLY A C   1 
ATOM   951   O  O   . GLY A 1 147 ? 15.559  -25.248 -33.296 1.00 42.41  ? 147  GLY A O   1 
ATOM   952   N  N   . TYR A 1 148 ? 16.556  -24.836 -31.309 1.00 33.29  ? 148  TYR A N   1 
ATOM   953   C  CA  . TYR A 1 148 ? 17.610  -23.997 -31.859 1.00 48.52  ? 148  TYR A CA  1 
ATOM   954   C  C   . TYR A 1 148 ? 18.469  -24.778 -32.844 1.00 52.92  ? 148  TYR A C   1 
ATOM   955   O  O   . TYR A 1 148 ? 18.576  -24.418 -34.018 1.00 39.28  ? 148  TYR A O   1 
ATOM   956   C  CB  . TYR A 1 148 ? 18.474  -23.449 -30.730 1.00 43.70  ? 148  TYR A CB  1 
ATOM   957   C  CG  . TYR A 1 148 ? 19.700  -22.696 -31.192 1.00 44.79  ? 148  TYR A CG  1 
ATOM   958   C  CD1 . TYR A 1 148 ? 19.587  -21.453 -31.807 1.00 48.01  ? 148  TYR A CD1 1 
ATOM   959   C  CD2 . TYR A 1 148 ? 20.974  -23.214 -30.996 1.00 39.00  ? 148  TYR A CD2 1 
ATOM   960   C  CE1 . TYR A 1 148 ? 20.707  -20.749 -32.227 1.00 32.38  ? 148  TYR A CE1 1 
ATOM   961   C  CE2 . TYR A 1 148 ? 22.098  -22.512 -31.405 1.00 38.46  ? 148  TYR A CE2 1 
ATOM   962   C  CZ  . TYR A 1 148 ? 21.951  -21.281 -32.023 1.00 43.05  ? 148  TYR A CZ  1 
ATOM   963   O  OH  . TYR A 1 148 ? 23.057  -20.582 -32.437 1.00 63.23  ? 148  TYR A OH  1 
ATOM   964   N  N   . ALA A 1 149 ? 19.070  -25.856 -32.351 1.00 52.35  ? 149  ALA A N   1 
ATOM   965   C  CA  . ALA A 1 149 ? 19.870  -26.755 -33.178 1.00 44.36  ? 149  ALA A CA  1 
ATOM   966   C  C   . ALA A 1 149 ? 19.230  -27.066 -34.531 1.00 31.17  ? 149  ALA A C   1 
ATOM   967   O  O   . ALA A 1 149 ? 19.936  -27.291 -35.511 1.00 41.07  ? 149  ALA A O   1 
ATOM   968   C  CB  . ALA A 1 149 ? 20.162  -28.054 -32.424 1.00 24.47  ? 149  ALA A CB  1 
ATOM   969   N  N   . LEU A 1 150 ? 17.905  -27.094 -34.583 1.00 37.76  ? 150  LEU A N   1 
ATOM   970   C  CA  . LEU A 1 150 ? 17.209  -27.427 -35.824 1.00 53.06  ? 150  LEU A CA  1 
ATOM   971   C  C   . LEU A 1 150 ? 16.913  -26.197 -36.690 1.00 59.50  ? 150  LEU A C   1 
ATOM   972   O  O   . LEU A 1 150 ? 16.443  -26.327 -37.824 1.00 64.23  ? 150  LEU A O   1 
ATOM   973   C  CB  . LEU A 1 150 ? 15.931  -28.220 -35.538 1.00 47.36  ? 150  LEU A CB  1 
ATOM   974   C  CG  . LEU A 1 150 ? 16.175  -29.636 -35.000 1.00 50.56  ? 150  LEU A CG  1 
ATOM   975   C  CD1 . LEU A 1 150 ? 15.050  -30.076 -34.108 1.00 44.42  ? 150  LEU A CD1 1 
ATOM   976   C  CD2 . LEU A 1 150 ? 16.370  -30.631 -36.127 1.00 47.29  ? 150  LEU A CD2 1 
ATOM   977   N  N   . SER A 1 151 ? 17.219  -25.010 -36.164 1.00 56.24  ? 151  SER A N   1 
ATOM   978   C  CA  . SER A 1 151 ? 16.966  -23.753 -36.878 1.00 51.21  ? 151  SER A CA  1 
ATOM   979   C  C   . SER A 1 151 ? 18.152  -23.277 -37.742 1.00 57.51  ? 151  SER A C   1 
ATOM   980   O  O   . SER A 1 151 ? 19.296  -23.677 -37.512 1.00 60.94  ? 151  SER A O   1 
ATOM   981   C  CB  . SER A 1 151 ? 16.541  -22.658 -35.893 1.00 44.05  ? 151  SER A CB  1 
ATOM   982   O  OG  . SER A 1 151 ? 15.345  -23.020 -35.214 1.00 36.13  ? 151  SER A OG  1 
ATOM   983   N  N   . GLN A 1 152 ? 17.874  -22.425 -38.734 1.00 51.10  ? 152  GLN A N   1 
ATOM   984   C  CA  . GLN A 1 152 ? 18.897  -21.958 -39.670 1.00 44.18  ? 152  GLN A CA  1 
ATOM   985   C  C   . GLN A 1 152 ? 19.191  -20.467 -39.589 1.00 47.99  ? 152  GLN A C   1 
ATOM   986   O  O   . GLN A 1 152 ? 18.366  -19.636 -39.978 1.00 53.57  ? 152  GLN A O   1 
ATOM   987   C  CB  . GLN A 1 152 ? 18.485  -22.294 -41.104 1.00 72.64  ? 152  GLN A CB  1 
ATOM   988   C  CG  . GLN A 1 152 ? 19.441  -21.752 -42.165 1.00 77.49  ? 152  GLN A CG  1 
ATOM   989   C  CD  . GLN A 1 152 ? 18.971  -22.038 -43.570 1.00 78.18  ? 152  GLN A CD  1 
ATOM   990   O  OE1 . GLN A 1 152 ? 19.470  -21.457 -44.534 1.00 91.81  ? 152  GLN A OE1 1 
ATOM   991   N  NE2 . GLN A 1 152 ? 18.001  -22.935 -43.696 1.00 74.00  ? 152  GLN A NE2 1 
ATOM   992   N  N   . GLU A 1 153 ? 20.379  -20.132 -39.105 1.00 47.26  ? 153  GLU A N   1 
ATOM   993   C  CA  . GLU A 1 153 ? 20.797  -18.737 -39.031 1.00 50.95  ? 153  GLU A CA  1 
ATOM   994   C  C   . GLU A 1 153 ? 20.537  -18.032 -40.357 1.00 56.76  ? 153  GLU A C   1 
ATOM   995   O  O   . GLU A 1 153 ? 20.891  -18.541 -41.420 1.00 59.61  ? 153  GLU A O   1 
ATOM   996   C  CB  . GLU A 1 153 ? 22.281  -18.635 -38.672 1.00 45.02  ? 153  GLU A CB  1 
ATOM   997   C  CG  . GLU A 1 153 ? 22.781  -17.209 -38.578 1.00 52.97  ? 153  GLU A CG  1 
ATOM   998   C  CD  . GLU A 1 153 ? 24.264  -17.131 -38.284 1.00 58.00  ? 153  GLU A CD  1 
ATOM   999   O  OE1 . GLU A 1 153 ? 24.863  -16.061 -38.549 1.00 59.18  ? 153  GLU A OE1 1 
ATOM   1000  O  OE2 . GLU A 1 153 ? 24.823  -18.139 -37.790 1.00 51.37  ? 153  GLU A OE2 1 
ATOM   1001  N  N   . GLY A 1 154 ? 19.915  -16.859 -40.290 1.00 57.35  ? 154  GLY A N   1 
ATOM   1002  C  CA  . GLY A 1 154 ? 19.612  -16.086 -41.482 1.00 48.35  ? 154  GLY A CA  1 
ATOM   1003  C  C   . GLY A 1 154 ? 18.122  -16.024 -41.752 1.00 54.16  ? 154  GLY A C   1 
ATOM   1004  O  O   . GLY A 1 154 ? 17.634  -15.076 -42.357 1.00 63.65  ? 154  GLY A O   1 
ATOM   1005  N  N   . ASN A 1 155 ? 17.392  -17.031 -41.289 1.00 50.51  ? 155  ASN A N   1 
ATOM   1006  C  CA  . ASN A 1 155 ? 15.950  -17.084 -41.503 1.00 52.34  ? 155  ASN A CA  1 
ATOM   1007  C  C   . ASN A 1 155 ? 15.134  -16.056 -40.704 1.00 63.30  ? 155  ASN A C   1 
ATOM   1008  O  O   . ASN A 1 155 ? 14.801  -16.276 -39.530 1.00 68.66  ? 155  ASN A O   1 
ATOM   1009  C  CB  . ASN A 1 155 ? 15.431  -18.497 -41.231 1.00 50.68  ? 155  ASN A CB  1 
ATOM   1010  C  CG  . ASN A 1 155 ? 15.352  -19.331 -42.492 1.00 59.42  ? 155  ASN A CG  1 
ATOM   1011  O  OD1 . ASN A 1 155 ? 15.505  -20.556 -42.466 1.00 56.61  ? 155  ASN A OD1 1 
ATOM   1012  N  ND2 . ASN A 1 155 ? 15.114  -18.664 -43.613 1.00 76.27  ? 155  ASN A ND2 1 
ATOM   1013  N  N   . CYS A 1 156 ? 14.809  -14.936 -41.344 1.00 56.38  ? 156  CYS A N   1 
ATOM   1014  C  CA  . CYS A 1 156 ? 13.933  -13.960 -40.719 1.00 62.48  ? 156  CYS A CA  1 
ATOM   1015  C  C   . CYS A 1 156 ? 12.581  -14.609 -40.445 1.00 61.08  ? 156  CYS A C   1 
ATOM   1016  O  O   . CYS A 1 156 ? 11.968  -14.392 -39.394 1.00 66.33  ? 156  CYS A O   1 
ATOM   1017  C  CB  . CYS A 1 156 ? 13.784  -12.720 -41.606 1.00 67.47  ? 156  CYS A CB  1 
ATOM   1018  S  SG  . CYS A 1 156 ? 15.246  -11.656 -41.624 1.00 60.27  ? 156  CYS A SG  1 
ATOM   1019  N  N   . GLU A 1 157 ? 12.125  -15.416 -41.398 1.00 60.02  ? 157  GLU A N   1 
ATOM   1020  C  CA  . GLU A 1 157 ? 10.902  -16.197 -41.231 1.00 61.40  ? 157  GLU A CA  1 
ATOM   1021  C  C   . GLU A 1 157 ? 11.207  -17.642 -40.838 1.00 57.85  ? 157  GLU A C   1 
ATOM   1022  O  O   . GLU A 1 157 ? 12.201  -18.220 -41.274 1.00 63.28  ? 157  GLU A O   1 
ATOM   1023  C  CB  . GLU A 1 157 ? 10.063  -16.172 -42.511 1.00 68.79  ? 157  GLU A CB  1 
ATOM   1024  C  CG  . GLU A 1 157 ? 9.406   -14.827 -42.799 1.00 85.26  ? 157  GLU A CG  1 
ATOM   1025  C  CD  . GLU A 1 157 ? 10.117  -14.043 -43.889 1.00 98.76  ? 157  GLU A CD  1 
ATOM   1026  O  OE1 . GLU A 1 157 ? 9.833   -14.294 -45.084 1.00 103.61 ? 157  GLU A OE1 1 
ATOM   1027  O  OE2 . GLU A 1 157 ? 10.950  -13.174 -43.549 1.00 96.16  ? 157  GLU A OE2 1 
ATOM   1028  N  N   . SER A 1 158 ? 10.342  -18.220 -40.014 1.00 57.72  ? 158  SER A N   1 
ATOM   1029  C  CA  . SER A 1 158 ? 10.521  -19.589 -39.546 1.00 50.36  ? 158  SER A CA  1 
ATOM   1030  C  C   . SER A 1 158 ? 10.503  -20.568 -40.715 1.00 44.83  ? 158  SER A C   1 
ATOM   1031  O  O   . SER A 1 158 ? 10.205  -20.187 -41.842 1.00 53.85  ? 158  SER A O   1 
ATOM   1032  C  CB  . SER A 1 158 ? 9.436   -19.944 -38.519 1.00 54.59  ? 158  SER A CB  1 
ATOM   1033  O  OG  . SER A 1 158 ? 9.651   -21.230 -37.962 1.00 69.23  ? 158  SER A OG  1 
ATOM   1034  N  N   . LEU A 1 159 ? 10.819  -21.830 -40.439 1.00 38.15  ? 159  LEU A N   1 
ATOM   1035  C  CA  . LEU A 1 159 ? 10.999  -22.847 -41.479 1.00 36.91  ? 159  LEU A CA  1 
ATOM   1036  C  C   . LEU A 1 159 ? 9.718   -23.622 -41.752 1.00 74.51  ? 159  LEU A C   1 
ATOM   1037  O  O   . LEU A 1 159 ? 8.736   -23.466 -41.033 1.00 68.69  ? 159  LEU A O   1 
ATOM   1038  C  CB  . LEU A 1 159 ? 12.082  -23.845 -41.052 1.00 102.62 ? 159  LEU A CB  1 
ATOM   1039  C  CG  . LEU A 1 159 ? 13.575  -23.487 -41.063 1.00 97.07  ? 159  LEU A CG  1 
ATOM   1040  C  CD1 . LEU A 1 159 ? 14.365  -24.583 -40.349 1.00 91.57  ? 159  LEU A CD1 1 
ATOM   1041  C  CD2 . LEU A 1 159 ? 14.114  -23.257 -42.481 1.00 88.49  ? 159  LEU A CD2 1 
ATOM   1042  N  N   . PRO A 1 160 ? 9.728   -24.467 -42.799 1.00 85.30  ? 160  PRO A N   1 
ATOM   1043  C  CA  . PRO A 1 160 ? 8.610   -25.376 -43.080 1.00 79.74  ? 160  PRO A CA  1 
ATOM   1044  C  C   . PRO A 1 160 ? 8.192   -26.177 -41.847 1.00 76.78  ? 160  PRO A C   1 
ATOM   1045  O  O   . PRO A 1 160 ? 9.045   -26.605 -41.072 1.00 85.27  ? 160  PRO A O   1 
ATOM   1046  C  CB  . PRO A 1 160 ? 9.193   -26.302 -44.145 1.00 48.37  ? 160  PRO A CB  1 
ATOM   1047  C  CG  . PRO A 1 160 ? 10.140  -25.421 -44.886 1.00 51.95  ? 160  PRO A CG  1 
ATOM   1048  C  CD  . PRO A 1 160 ? 10.753  -24.519 -43.862 1.00 67.98  ? 160  PRO A CD  1 
ATOM   1049  N  N   . ASN A 1 161 ? 6.891   -26.372 -41.671 1.00 70.28  ? 161  ASN A N   1 
ATOM   1050  C  CA  . ASN A 1 161 ? 6.373   -27.088 -40.503 1.00 74.32  ? 161  ASN A CA  1 
ATOM   1051  C  C   . ASN A 1 161 ? 6.514   -26.312 -39.190 1.00 59.20  ? 161  ASN A C   1 
ATOM   1052  O  O   . ASN A 1 161 ? 6.057   -26.766 -38.145 1.00 45.83  ? 161  ASN A O   1 
ATOM   1053  C  CB  . ASN A 1 161 ? 7.047   -28.460 -40.373 1.00 76.16  ? 161  ASN A CB  1 
ATOM   1054  C  CG  . ASN A 1 161 ? 6.817   -29.337 -41.584 1.00 88.62  ? 161  ASN A CG  1 
ATOM   1055  O  OD1 . ASN A 1 161 ? 7.741   -29.968 -42.093 1.00 96.78  ? 161  ASN A OD1 1 
ATOM   1056  N  ND2 . ASN A 1 161 ? 5.578   -29.378 -42.056 1.00 94.50  ? 161  ASN A ND2 1 
ATOM   1057  N  N   . TYR A 1 162 ? 7.120   -25.131 -39.258 1.00 61.35  ? 162  TYR A N   1 
ATOM   1058  C  CA  . TYR A 1 162 ? 7.579   -24.433 -38.062 1.00 79.19  ? 162  TYR A CA  1 
ATOM   1059  C  C   . TYR A 1 162 ? 8.603   -25.296 -37.345 1.00 82.27  ? 162  TYR A C   1 
ATOM   1060  O  O   . TYR A 1 162 ? 8.633   -25.380 -36.105 1.00 75.36  ? 162  TYR A O   1 
ATOM   1061  C  CB  . TYR A 1 162 ? 6.426   -24.051 -37.141 1.00 71.08  ? 162  TYR A CB  1 
ATOM   1062  C  CG  . TYR A 1 162 ? 5.694   -22.837 -37.633 1.00 66.75  ? 162  TYR A CG  1 
ATOM   1063  C  CD1 . TYR A 1 162 ? 4.497   -22.960 -38.318 1.00 51.98  ? 162  TYR A CD1 1 
ATOM   1064  C  CD2 . TYR A 1 162 ? 6.211   -21.563 -37.434 1.00 82.43  ? 162  TYR A CD2 1 
ATOM   1065  C  CE1 . TYR A 1 162 ? 3.823   -21.850 -38.778 1.00 55.06  ? 162  TYR A CE1 1 
ATOM   1066  C  CE2 . TYR A 1 162 ? 5.541   -20.442 -37.893 1.00 87.08  ? 162  TYR A CE2 1 
ATOM   1067  C  CZ  . TYR A 1 162 ? 4.349   -20.592 -38.568 1.00 67.58  ? 162  TYR A CZ  1 
ATOM   1068  O  OH  . TYR A 1 162 ? 3.682   -19.478 -39.026 1.00 73.65  ? 162  TYR A OH  1 
ATOM   1069  N  N   . VAL A 1 163 ? 9.439   -25.944 -38.152 1.00 61.39  ? 163  VAL A N   1 
ATOM   1070  C  CA  . VAL A 1 163 ? 10.552  -26.702 -37.617 1.00 61.79  ? 163  VAL A CA  1 
ATOM   1071  C  C   . VAL A 1 163 ? 11.605  -25.754 -37.046 1.00 57.24  ? 163  VAL A C   1 
ATOM   1072  O  O   . VAL A 1 163 ? 11.969  -24.739 -37.657 1.00 50.28  ? 163  VAL A O   1 
ATOM   1073  C  CB  . VAL A 1 163 ? 11.171  -27.638 -38.661 1.00 51.26  ? 163  VAL A CB  1 
ATOM   1074  C  CG1 . VAL A 1 163 ? 12.580  -28.033 -38.248 1.00 40.85  ? 163  VAL A CG1 1 
ATOM   1075  C  CG2 . VAL A 1 163 ? 10.278  -28.873 -38.868 1.00 41.84  ? 163  VAL A CG2 1 
ATOM   1076  N  N   . GLY A 1 164 ? 12.069  -26.088 -35.848 1.00 49.39  ? 164  GLY A N   1 
ATOM   1077  C  CA  . GLY A 1 164 ? 13.002  -25.248 -35.117 1.00 47.67  ? 164  GLY A CA  1 
ATOM   1078  C  C   . GLY A 1 164 ? 12.296  -24.379 -34.089 1.00 40.02  ? 164  GLY A C   1 
ATOM   1079  O  O   . GLY A 1 164 ? 12.837  -24.092 -33.025 1.00 38.74  ? 164  GLY A O   1 
ATOM   1080  N  N   . ARG A 1 165 ? 11.077  -23.960 -34.416 1.00 47.61  ? 165  ARG A N   1 
ATOM   1081  C  CA  . ARG A 1 165 ? 10.282  -23.148 -33.511 1.00 42.86  ? 165  ARG A CA  1 
ATOM   1082  C  C   . ARG A 1 165 ? 9.888   -23.987 -32.300 1.00 40.60  ? 165  ARG A C   1 
ATOM   1083  O  O   . ARG A 1 165 ? 10.173  -23.617 -31.165 1.00 51.87  ? 165  ARG A O   1 
ATOM   1084  C  CB  . ARG A 1 165 ? 9.047   -22.582 -34.233 1.00 44.94  ? 165  ARG A CB  1 
ATOM   1085  C  CG  . ARG A 1 165 ? 8.129   -21.745 -33.345 1.00 45.25  ? 165  ARG A CG  1 
ATOM   1086  C  CD  . ARG A 1 165 ? 6.948   -21.165 -34.123 1.00 39.42  ? 165  ARG A CD  1 
ATOM   1087  N  NE  . ARG A 1 165 ? 5.810   -20.865 -33.252 1.00 27.96  ? 165  ARG A NE  1 
ATOM   1088  C  CZ  . ARG A 1 165 ? 5.537   -19.659 -32.761 1.00 33.92  ? 165  ARG A CZ  1 
ATOM   1089  N  NH1 . ARG A 1 165 ? 6.319   -18.632 -33.054 1.00 34.34  ? 165  ARG A NH1 1 
ATOM   1090  N  NH2 . ARG A 1 165 ? 4.477   -19.475 -31.981 1.00 42.18  ? 165  ARG A NH2 1 
ATOM   1091  N  N   . GLY A 1 166 ? 9.251   -25.128 -32.541 1.00 36.80  ? 166  GLY A N   1 
ATOM   1092  C  CA  . GLY A 1 166 ? 8.843   -26.013 -31.462 1.00 31.47  ? 166  GLY A CA  1 
ATOM   1093  C  C   . GLY A 1 166 ? 10.035  -26.857 -31.072 1.00 35.50  ? 166  GLY A C   1 
ATOM   1094  O  O   . GLY A 1 166 ? 11.109  -26.709 -31.661 1.00 43.16  ? 166  GLY A O   1 
ATOM   1095  N  N   . ASN A 1 167 ? 9.865   -27.732 -30.081 1.00 39.80  ? 167  ASN A N   1 
ATOM   1096  C  CA  . ASN A 1 167 ? 10.978  -28.571 -29.640 1.00 34.37  ? 167  ASN A CA  1 
ATOM   1097  C  C   . ASN A 1 167 ? 11.226  -29.706 -30.620 1.00 43.60  ? 167  ASN A C   1 
ATOM   1098  O  O   . ASN A 1 167 ? 10.842  -29.624 -31.793 1.00 47.65  ? 167  ASN A O   1 
ATOM   1099  C  CB  . ASN A 1 167 ? 10.813  -29.070 -28.190 1.00 32.31  ? 167  ASN A CB  1 
ATOM   1100  C  CG  . ASN A 1 167 ? 9.694   -30.091 -28.025 1.00 39.46  ? 167  ASN A CG  1 
ATOM   1101  O  OD1 . ASN A 1 167 ? 9.044   -30.499 -28.992 1.00 41.37  ? 167  ASN A OD1 1 
ATOM   1102  N  ND2 . ASN A 1 167 ? 9.469   -30.510 -26.783 1.00 33.17  ? 167  ASN A ND2 1 
ATOM   1103  N  N   . ALA A 1 168 ? 11.881  -30.759 -30.150 1.00 45.96  ? 168  ALA A N   1 
ATOM   1104  C  CA  . ALA A 1 168 ? 12.251  -31.855 -31.040 1.00 50.54  ? 168  ALA A CA  1 
ATOM   1105  C  C   . ALA A 1 168 ? 11.038  -32.690 -31.434 1.00 64.87  ? 168  ALA A C   1 
ATOM   1106  O  O   . ALA A 1 168 ? 11.074  -33.393 -32.442 1.00 69.91  ? 168  ALA A O   1 
ATOM   1107  C  CB  . ALA A 1 168 ? 13.327  -32.731 -30.403 1.00 48.32  ? 168  ALA A CB  1 
ATOM   1108  N  N   . ALA A 1 169 ? 9.970   -32.618 -30.637 1.00 65.25  ? 169  ALA A N   1 
ATOM   1109  C  CA  . ALA A 1 169 ? 8.723   -33.320 -30.959 1.00 50.02  ? 169  ALA A CA  1 
ATOM   1110  C  C   . ALA A 1 169 ? 7.789   -32.405 -31.761 1.00 50.71  ? 169  ALA A C   1 
ATOM   1111  O  O   . ALA A 1 169 ? 6.641   -32.766 -32.055 1.00 46.36  ? 169  ALA A O   1 
ATOM   1112  C  CB  . ALA A 1 169 ? 8.043   -33.818 -29.688 1.00 32.26  ? 169  ALA A CB  1 
ATOM   1113  N  N   . ASN A 1 170 ? 8.296   -31.222 -32.111 1.00 45.89  ? 170  ASN A N   1 
ATOM   1114  C  CA  . ASN A 1 170 ? 7.554   -30.249 -32.901 1.00 46.69  ? 170  ASN A CA  1 
ATOM   1115  C  C   . ASN A 1 170 ? 6.317   -29.696 -32.215 1.00 45.99  ? 170  ASN A C   1 
ATOM   1116  O  O   . ASN A 1 170 ? 5.357   -29.314 -32.889 1.00 55.63  ? 170  ASN A O   1 
ATOM   1117  C  CB  . ASN A 1 170 ? 7.161   -30.832 -34.257 1.00 69.13  ? 170  ASN A CB  1 
ATOM   1118  C  CG  . ASN A 1 170 ? 8.160   -30.514 -35.331 1.00 76.13  ? 170  ASN A CG  1 
ATOM   1119  O  OD1 . ASN A 1 170 ? 8.749   -31.414 -35.928 1.00 81.75  ? 170  ASN A OD1 1 
ATOM   1120  N  ND2 . ASN A 1 170 ? 8.366   -29.228 -35.585 1.00 76.09  ? 170  ASN A ND2 1 
ATOM   1121  N  N   . ILE A 1 171 ? 6.321   -29.643 -30.886 1.00 36.82  ? 171  ILE A N   1 
ATOM   1122  C  CA  . ILE A 1 171 ? 5.247   -28.914 -30.213 1.00 51.21  ? 171  ILE A CA  1 
ATOM   1123  C  C   . ILE A 1 171 ? 5.720   -27.547 -29.748 1.00 38.76  ? 171  ILE A C   1 
ATOM   1124  O  O   . ILE A 1 171 ? 6.891   -27.365 -29.405 1.00 29.01  ? 171  ILE A O   1 
ATOM   1125  C  CB  . ILE A 1 171 ? 4.543   -29.699 -29.059 1.00 48.12  ? 171  ILE A CB  1 
ATOM   1126  C  CG1 . ILE A 1 171 ? 5.272   -29.515 -27.730 1.00 43.31  ? 171  ILE A CG1 1 
ATOM   1127  C  CG2 . ILE A 1 171 ? 4.340   -31.173 -29.433 1.00 46.07  ? 171  ILE A CG2 1 
ATOM   1128  C  CD1 . ILE A 1 171 ? 4.748   -28.355 -26.892 1.00 53.13  ? 171  ILE A CD1 1 
ATOM   1129  N  N   . ASP A 1 172 ? 4.787   -26.594 -29.763 1.00 49.75  ? 172  ASP A N   1 
ATOM   1130  C  CA  . ASP A 1 172 ? 5.065   -25.196 -29.448 1.00 48.46  ? 172  ASP A CA  1 
ATOM   1131  C  C   . ASP A 1 172 ? 5.065   -24.979 -27.933 1.00 47.02  ? 172  ASP A C   1 
ATOM   1132  O  O   . ASP A 1 172 ? 4.009   -24.952 -27.293 1.00 51.68  ? 172  ASP A O   1 
ATOM   1133  C  CB  . ASP A 1 172 ? 4.046   -24.279 -30.149 1.00 44.36  ? 172  ASP A CB  1 
ATOM   1134  C  CG  . ASP A 1 172 ? 4.368   -22.790 -29.991 1.00 49.16  ? 172  ASP A CG  1 
ATOM   1135  O  OD1 . ASP A 1 172 ? 4.977   -22.398 -28.955 1.00 51.94  ? 172  ASP A OD1 1 
ATOM   1136  O  OD2 . ASP A 1 172 ? 3.998   -22.015 -30.911 1.00 41.30  ? 172  ASP A OD2 1 
ATOM   1137  N  N   . LEU A 1 173 ? 6.260   -24.830 -27.367 1.00 41.49  ? 173  LEU A N   1 
ATOM   1138  C  CA  . LEU A 1 173 ? 6.400   -24.717 -25.927 1.00 39.45  ? 173  LEU A CA  1 
ATOM   1139  C  C   . LEU A 1 173 ? 5.584   -23.550 -25.368 1.00 33.76  ? 173  LEU A C   1 
ATOM   1140  O  O   . LEU A 1 173 ? 5.202   -23.559 -24.198 1.00 31.60  ? 173  LEU A O   1 
ATOM   1141  C  CB  . LEU A 1 173 ? 7.877   -24.608 -25.547 1.00 33.92  ? 173  LEU A CB  1 
ATOM   1142  C  CG  . LEU A 1 173 ? 8.712   -25.853 -25.867 1.00 31.32  ? 173  LEU A CG  1 
ATOM   1143  C  CD1 . LEU A 1 173 ? 10.194  -25.605 -25.605 1.00 21.01  ? 173  LEU A CD1 1 
ATOM   1144  C  CD2 . LEU A 1 173 ? 8.203   -27.069 -25.085 1.00 41.60  ? 173  LEU A CD2 1 
ATOM   1145  N  N   . ASN A 1 174 ? 5.294   -22.557 -26.204 1.00 30.12  ? 174  ASN A N   1 
ATOM   1146  C  CA  . ASN A 1 174 ? 4.502   -21.429 -25.745 1.00 16.87  ? 174  ASN A CA  1 
ATOM   1147  C  C   . ASN A 1 174 ? 3.035   -21.741 -25.886 1.00 30.97  ? 174  ASN A C   1 
ATOM   1148  O  O   . ASN A 1 174 ? 2.201   -20.835 -25.870 1.00 47.16  ? 174  ASN A O   1 
ATOM   1149  C  CB  . ASN A 1 174 ? 4.837   -20.150 -26.501 1.00 23.16  ? 174  ASN A CB  1 
ATOM   1150  C  CG  . ASN A 1 174 ? 4.613   -18.898 -25.665 1.00 35.91  ? 174  ASN A CG  1 
ATOM   1151  O  OD1 . ASN A 1 174 ? 4.535   -18.954 -24.430 1.00 40.05  ? 174  ASN A OD1 1 
ATOM   1152  N  ND2 . ASN A 1 174 ? 4.528   -17.755 -26.337 1.00 33.83  ? 174  ASN A ND2 1 
ATOM   1153  N  N   . ARG A 1 175 ? 2.721   -23.023 -26.056 1.00 23.26  ? 175  ARG A N   1 
ATOM   1154  C  CA  . ARG A 1 175 ? 1.344   -23.500 -25.891 1.00 36.98  ? 175  ARG A CA  1 
ATOM   1155  C  C   . ARG A 1 175 ? 1.261   -24.623 -24.864 1.00 38.68  ? 175  ARG A C   1 
ATOM   1156  O  O   . ARG A 1 175 ? 0.191   -25.165 -24.613 1.00 45.10  ? 175  ARG A O   1 
ATOM   1157  C  CB  . ARG A 1 175 ? 0.746   -23.991 -27.203 1.00 21.96  ? 175  ARG A CB  1 
ATOM   1158  C  CG  . ARG A 1 175 ? 0.833   -22.991 -28.312 1.00 38.10  ? 175  ARG A CG  1 
ATOM   1159  C  CD  . ARG A 1 175 ? 0.274   -21.627 -27.924 1.00 38.33  ? 175  ARG A CD  1 
ATOM   1160  N  NE  . ARG A 1 175 ? 0.164   -20.814 -29.120 1.00 47.35  ? 175  ARG A NE  1 
ATOM   1161  C  CZ  . ARG A 1 175 ? 0.953   -19.807 -29.478 1.00 45.24  ? 175  ARG A CZ  1 
ATOM   1162  N  NH1 . ARG A 1 175 ? 0.712   -19.201 -30.627 1.00 49.92  ? 175  ARG A NH1 1 
ATOM   1163  N  NH2 . ARG A 1 175 ? 1.944   -19.384 -28.713 1.00 54.02  ? 175  ARG A NH2 1 
ATOM   1164  N  N   . ASP A 1 176 ? 2.393   -24.960 -24.258 1.00 49.19  ? 176  ASP A N   1 
ATOM   1165  C  CA  . ASP A 1 176 ? 2.487   -26.201 -23.495 1.00 45.80  ? 176  ASP A CA  1 
ATOM   1166  C  C   . ASP A 1 176 ? 2.383   -26.038 -21.977 1.00 40.76  ? 176  ASP A C   1 
ATOM   1167  O  O   . ASP A 1 176 ? 2.393   -27.026 -21.243 1.00 40.20  ? 176  ASP A O   1 
ATOM   1168  C  CB  . ASP A 1 176 ? 3.779   -26.930 -23.858 1.00 42.72  ? 176  ASP A CB  1 
ATOM   1169  C  CG  . ASP A 1 176 ? 3.741   -28.390 -23.488 1.00 47.81  ? 176  ASP A CG  1 
ATOM   1170  O  OD1 . ASP A 1 176 ? 2.660   -28.994 -23.612 1.00 40.73  ? 176  ASP A OD1 1 
ATOM   1171  O  OD2 . ASP A 1 176 ? 4.791   -28.930 -23.082 1.00 58.50  ? 176  ASP A OD2 1 
ATOM   1172  N  N   . PHE A 1 177 ? 2.285   -24.797 -21.508 1.00 43.38  ? 177  PHE A N   1 
ATOM   1173  C  CA  . PHE A 1 177 ? 2.203   -24.526 -20.073 1.00 26.31  ? 177  PHE A CA  1 
ATOM   1174  C  C   . PHE A 1 177 ? 0.752   -24.625 -19.626 1.00 29.98  ? 177  PHE A C   1 
ATOM   1175  O  O   . PHE A 1 177 ? -0.153  -24.451 -20.432 1.00 45.41  ? 177  PHE A O   1 
ATOM   1176  C  CB  . PHE A 1 177 ? 2.798   -23.145 -19.743 1.00 23.52  ? 177  PHE A CB  1 
ATOM   1177  C  CG  . PHE A 1 177 ? 4.318   -23.101 -19.804 1.00 33.03  ? 177  PHE A CG  1 
ATOM   1178  C  CD1 . PHE A 1 177 ? 4.987   -23.044 -21.034 1.00 41.07  ? 177  PHE A CD1 1 
ATOM   1179  C  CD2 . PHE A 1 177 ? 5.074   -23.125 -18.644 1.00 23.09  ? 177  PHE A CD2 1 
ATOM   1180  C  CE1 . PHE A 1 177 ? 6.375   -23.010 -21.096 1.00 30.32  ? 177  PHE A CE1 1 
ATOM   1181  C  CE2 . PHE A 1 177 ? 6.461   -23.095 -18.700 1.00 28.63  ? 177  PHE A CE2 1 
ATOM   1182  C  CZ  . PHE A 1 177 ? 7.112   -23.036 -19.926 1.00 34.35  ? 177  PHE A CZ  1 
ATOM   1183  N  N   . PRO A 1 178 ? 0.529   -24.939 -18.343 1.00 29.50  ? 178  PRO A N   1 
ATOM   1184  C  CA  . PRO A 1 178 ? -0.819  -24.955 -17.774 1.00 26.10  ? 178  PRO A CA  1 
ATOM   1185  C  C   . PRO A 1 178 ? -1.540  -23.609 -17.980 1.00 42.35  ? 178  PRO A C   1 
ATOM   1186  O  O   . PRO A 1 178 ? -0.954  -22.527 -17.820 1.00 27.23  ? 178  PRO A O   1 
ATOM   1187  C  CB  . PRO A 1 178 ? -0.562  -25.204 -16.284 1.00 31.35  ? 178  PRO A CB  1 
ATOM   1188  C  CG  . PRO A 1 178 ? 0.774   -25.888 -16.224 1.00 23.10  ? 178  PRO A CG  1 
ATOM   1189  C  CD  . PRO A 1 178 ? 1.561   -25.330 -17.363 1.00 31.64  ? 178  PRO A CD  1 
ATOM   1190  N  N   . ASP A 1 179 ? -2.819  -23.688 -18.338 1.00 45.98  ? 179  ASP A N   1 
ATOM   1191  C  CA  . ASP A 1 179 ? -3.614  -22.500 -18.600 1.00 38.95  ? 179  ASP A CA  1 
ATOM   1192  C  C   . ASP A 1 179 ? -4.472  -22.172 -17.392 1.00 44.86  ? 179  ASP A C   1 
ATOM   1193  O  O   . ASP A 1 179 ? -5.070  -23.063 -16.788 1.00 43.25  ? 179  ASP A O   1 
ATOM   1194  C  CB  . ASP A 1 179 ? -4.501  -22.711 -19.824 1.00 46.61  ? 179  ASP A CB  1 
ATOM   1195  C  CG  . ASP A 1 179 ? -5.135  -21.419 -20.310 1.00 61.86  ? 179  ASP A CG  1 
ATOM   1196  O  OD1 . ASP A 1 179 ? -4.415  -20.397 -20.372 1.00 64.25  ? 179  ASP A OD1 1 
ATOM   1197  O  OD2 . ASP A 1 179 ? -6.348  -21.422 -20.632 1.00 64.12  ? 179  ASP A OD2 1 
ATOM   1198  N  N   . ARG A 1 180 ? -4.526  -20.891 -17.037 1.00 47.40  ? 180  ARG A N   1 
ATOM   1199  C  CA  . ARG A 1 180 ? -5.308  -20.450 -15.890 1.00 49.48  ? 180  ARG A CA  1 
ATOM   1200  C  C   . ARG A 1 180 ? -6.784  -20.792 -16.097 1.00 50.55  ? 180  ARG A C   1 
ATOM   1201  O  O   . ARG A 1 180 ? -7.512  -21.050 -15.143 1.00 51.26  ? 180  ARG A O   1 
ATOM   1202  C  CB  . ARG A 1 180 ? -5.134  -18.951 -15.696 1.00 43.33  ? 180  ARG A CB  1 
ATOM   1203  C  CG  . ARG A 1 180 ? -5.493  -18.184 -16.927 1.00 42.98  ? 180  ARG A CG  1 
ATOM   1204  C  CD  . ARG A 1 180 ? -5.032  -16.763 -16.847 1.00 47.95  ? 180  ARG A CD  1 
ATOM   1205  N  NE  . ARG A 1 180 ? -5.533  -16.031 -18.001 1.00 55.89  ? 180  ARG A NE  1 
ATOM   1206  C  CZ  . ARG A 1 180 ? -6.698  -15.399 -18.025 1.00 44.65  ? 180  ARG A CZ  1 
ATOM   1207  N  NH1 . ARG A 1 180 ? -7.476  -15.400 -16.946 1.00 41.86  ? 180  ARG A NH1 1 
ATOM   1208  N  NH2 . ARG A 1 180 ? -7.078  -14.760 -19.122 1.00 30.14  ? 180  ARG A NH2 1 
ATOM   1209  N  N   . LEU A 1 181 ? -7.224  -20.816 -17.346 1.00 45.12  ? 181  LEU A N   1 
ATOM   1210  C  CA  . LEU A 1 181 ? -8.624  -21.131 -17.622 1.00 46.35  ? 181  LEU A CA  1 
ATOM   1211  C  C   . LEU A 1 181 ? -8.905  -22.639 -17.765 1.00 49.50  ? 181  LEU A C   1 
ATOM   1212  O  O   . LEU A 1 181 ? -9.910  -23.037 -18.352 1.00 62.36  ? 181  LEU A O   1 
ATOM   1213  C  CB  . LEU A 1 181 ? -9.099  -20.353 -18.845 1.00 46.53  ? 181  LEU A CB  1 
ATOM   1214  C  CG  . LEU A 1 181 ? -8.857  -18.849 -18.704 1.00 47.45  ? 181  LEU A CG  1 
ATOM   1215  C  CD1 . LEU A 1 181 ? -8.951  -18.140 -20.057 1.00 62.89  ? 181  LEU A CD1 1 
ATOM   1216  C  CD2 . LEU A 1 181 ? -9.824  -18.249 -17.690 1.00 35.96  ? 181  LEU A CD2 1 
ATOM   1217  N  N   . GLU A 1 182 ? -8.022  -23.466 -17.209 1.00 57.41  ? 182  GLU A N   1 
ATOM   1218  C  CA  . GLU A 1 182 ? -8.208  -24.920 -17.182 1.00 56.39  ? 182  GLU A CA  1 
ATOM   1219  C  C   . GLU A 1 182 ? -8.256  -25.526 -18.574 1.00 55.20  ? 182  GLU A C   1 
ATOM   1220  O  O   . GLU A 1 182 ? -9.315  -25.972 -19.018 1.00 65.03  ? 182  GLU A O   1 
ATOM   1221  C  CB  . GLU A 1 182 ? -9.489  -25.286 -16.429 1.00 63.07  ? 182  GLU A CB  1 
ATOM   1222  C  CG  . GLU A 1 182 ? -9.663  -26.777 -16.202 1.00 66.42  ? 182  GLU A CG  1 
ATOM   1223  C  CD  . GLU A 1 182 ? -8.992  -27.253 -14.925 1.00 67.42  ? 182  GLU A CD  1 
ATOM   1224  O  OE1 . GLU A 1 182 ? -8.986  -28.482 -14.683 1.00 65.71  ? 182  GLU A OE1 1 
ATOM   1225  O  OE2 . GLU A 1 182 ? -8.481  -26.398 -14.160 1.00 64.85  ? 182  GLU A OE2 1 
ATOM   1226  N  N   . ALA A 1 191 ? 0.036   -30.847 -13.306 1.00 63.01  ? 191  ALA A N   1 
ATOM   1227  C  CA  . ALA A 1 191 ? 0.093   -32.306 -13.234 1.00 71.10  ? 191  ALA A CA  1 
ATOM   1228  C  C   . ALA A 1 191 ? 0.851   -32.895 -14.431 1.00 77.60  ? 191  ALA A C   1 
ATOM   1229  O  O   . ALA A 1 191 ? 0.369   -33.795 -15.121 1.00 85.91  ? 191  ALA A O   1 
ATOM   1230  C  CB  . ALA A 1 191 ? -1.314  -32.883 -13.139 1.00 81.54  ? 191  ALA A CB  1 
ATOM   1231  N  N   . GLN A 1 192 ? 2.060   -32.374 -14.622 1.00 73.16  ? 192  GLN A N   1 
ATOM   1232  C  CA  . GLN A 1 192 ? 2.956   -32.615 -15.766 1.00 65.80  ? 192  GLN A CA  1 
ATOM   1233  C  C   . GLN A 1 192 ? 2.642   -33.644 -16.858 1.00 71.19  ? 192  GLN A C   1 
ATOM   1234  O  O   . GLN A 1 192 ? 1.488   -33.950 -17.170 1.00 66.46  ? 192  GLN A O   1 
ATOM   1235  C  CB  . GLN A 1 192 ? 4.395   -32.832 -15.282 1.00 52.74  ? 192  GLN A CB  1 
ATOM   1236  C  CG  . GLN A 1 192 ? 5.005   -31.596 -14.644 1.00 58.45  ? 192  GLN A CG  1 
ATOM   1237  C  CD  . GLN A 1 192 ? 4.259   -30.314 -14.999 1.00 54.96  ? 192  GLN A CD  1 
ATOM   1238  O  OE1 . GLN A 1 192 ? 4.169   -29.932 -16.166 1.00 58.64  ? 192  GLN A OE1 1 
ATOM   1239  N  NE2 . GLN A 1 192 ? 3.725   -29.642 -13.984 1.00 44.95  ? 192  GLN A NE2 1 
ATOM   1240  N  N   . SER A 1 193 ? 3.731   -34.137 -17.442 1.00 74.47  ? 193  SER A N   1 
ATOM   1241  C  CA  . SER A 1 193 ? 3.730   -34.902 -18.681 1.00 69.25  ? 193  SER A CA  1 
ATOM   1242  C  C   . SER A 1 193 ? 3.635   -33.992 -19.904 1.00 64.80  ? 193  SER A C   1 
ATOM   1243  O  O   . SER A 1 193 ? 3.103   -34.384 -20.939 1.00 69.00  ? 193  SER A O   1 
ATOM   1244  C  CB  . SER A 1 193 ? 2.638   -35.963 -18.708 1.00 70.94  ? 193  SER A CB  1 
ATOM   1245  O  OG  . SER A 1 193 ? 2.951   -36.953 -19.683 1.00 72.37  ? 193  SER A OG  1 
ATOM   1246  N  N   . ARG A 1 194 ? 4.144   -32.771 -19.773 1.00 43.91  ? 194  ARG A N   1 
ATOM   1247  C  CA  . ARG A 1 194 ? 4.272   -31.875 -20.910 1.00 38.74  ? 194  ARG A CA  1 
ATOM   1248  C  C   . ARG A 1 194 ? 5.603   -32.174 -21.573 1.00 55.09  ? 194  ARG A C   1 
ATOM   1249  O  O   . ARG A 1 194 ? 6.165   -33.263 -21.406 1.00 55.08  ? 194  ARG A O   1 
ATOM   1250  C  CB  . ARG A 1 194 ? 4.292   -30.429 -20.436 1.00 21.84  ? 194  ARG A CB  1 
ATOM   1251  C  CG  . ARG A 1 194 ? 3.503   -30.196 -19.199 1.00 39.29  ? 194  ARG A CG  1 
ATOM   1252  C  CD  . ARG A 1 194 ? 2.297   -29.351 -19.507 1.00 62.66  ? 194  ARG A CD  1 
ATOM   1253  N  NE  . ARG A 1 194 ? 1.504   -29.064 -18.314 1.00 54.07  ? 194  ARG A NE  1 
ATOM   1254  C  CZ  . ARG A 1 194 ? 0.266   -28.591 -18.363 1.00 63.00  ? 194  ARG A CZ  1 
ATOM   1255  N  NH1 . ARG A 1 194 ? -0.295  -28.356 -19.542 1.00 70.84  ? 194  ARG A NH1 1 
ATOM   1256  N  NH2 . ARG A 1 194 ? -0.410  -28.360 -17.245 1.00 72.01  ? 194  ARG A NH2 1 
ATOM   1257  N  N   . GLN A 1 195 ? 6.122   -31.194 -22.306 1.00 44.09  ? 195  GLN A N   1 
ATOM   1258  C  CA  . GLN A 1 195 ? 7.468   -31.295 -22.834 1.00 34.97  ? 195  GLN A CA  1 
ATOM   1259  C  C   . GLN A 1 195 ? 8.479   -31.096 -21.705 1.00 39.04  ? 195  GLN A C   1 
ATOM   1260  O  O   . GLN A 1 195 ? 8.279   -30.279 -20.801 1.00 29.57  ? 195  GLN A O   1 
ATOM   1261  C  CB  . GLN A 1 195 ? 7.703   -30.290 -23.957 1.00 35.61  ? 195  GLN A CB  1 
ATOM   1262  C  CG  . GLN A 1 195 ? 6.722   -30.424 -25.108 1.00 41.10  ? 195  GLN A CG  1 
ATOM   1263  C  CD  . GLN A 1 195 ? 6.720   -31.806 -25.750 1.00 45.11  ? 195  GLN A CD  1 
ATOM   1264  O  OE1 . GLN A 1 195 ? 7.757   -32.308 -26.183 1.00 52.28  ? 195  GLN A OE1 1 
ATOM   1265  N  NE2 . GLN A 1 195 ? 5.543   -32.413 -25.839 1.00 31.61  ? 195  GLN A NE2 1 
ATOM   1266  N  N   . PRO A 1 196 ? 9.574   -31.866 -21.760 1.00 37.91  ? 196  PRO A N   1 
ATOM   1267  C  CA  . PRO A 1 196 ? 10.655  -31.843 -20.776 1.00 24.76  ? 196  PRO A CA  1 
ATOM   1268  C  C   . PRO A 1 196 ? 10.946  -30.401 -20.427 1.00 27.47  ? 196  PRO A C   1 
ATOM   1269  O  O   . PRO A 1 196 ? 11.069  -30.032 -19.268 1.00 30.75  ? 196  PRO A O   1 
ATOM   1270  C  CB  . PRO A 1 196 ? 11.845  -32.404 -21.560 1.00 20.25  ? 196  PRO A CB  1 
ATOM   1271  C  CG  . PRO A 1 196 ? 11.253  -33.265 -22.583 1.00 36.77  ? 196  PRO A CG  1 
ATOM   1272  C  CD  . PRO A 1 196 ? 9.923   -32.665 -22.945 1.00 29.66  ? 196  PRO A CD  1 
ATOM   1273  N  N   . GLU A 1 197 ? 11.042  -29.584 -21.464 1.00 31.82  ? 197  GLU A N   1 
ATOM   1274  C  CA  . GLU A 1 197 ? 11.512  -28.222 -21.320 1.00 32.70  ? 197  GLU A CA  1 
ATOM   1275  C  C   . GLU A 1 197 ? 10.503  -27.425 -20.524 1.00 25.21  ? 197  GLU A C   1 
ATOM   1276  O  O   . GLU A 1 197 ? 10.864  -26.642 -19.657 1.00 25.59  ? 197  GLU A O   1 
ATOM   1277  C  CB  . GLU A 1 197 ? 11.741  -27.596 -22.704 1.00 34.32  ? 197  GLU A CB  1 
ATOM   1278  C  CG  . GLU A 1 197 ? 12.864  -28.249 -23.531 1.00 28.91  ? 197  GLU A CG  1 
ATOM   1279  C  CD  . GLU A 1 197 ? 12.381  -29.425 -24.374 1.00 42.24  ? 197  GLU A CD  1 
ATOM   1280  O  OE1 . GLU A 1 197 ? 13.229  -30.041 -25.074 1.00 45.49  ? 197  GLU A OE1 1 
ATOM   1281  O  OE2 . GLU A 1 197 ? 11.158  -29.716 -24.340 1.00 24.48  ? 197  GLU A OE2 1 
ATOM   1282  N  N   . THR A 1 198 ? 9.232   -27.646 -20.826 1.00 26.42  ? 198  THR A N   1 
ATOM   1283  C  CA  . THR A 1 198 ? 8.149   -26.985 -20.123 1.00 27.08  ? 198  THR A CA  1 
ATOM   1284  C  C   . THR A 1 198 ? 8.201   -27.395 -18.656 1.00 33.31  ? 198  THR A C   1 
ATOM   1285  O  O   . THR A 1 198 ? 8.304   -26.552 -17.763 1.00 41.67  ? 198  THR A O   1 
ATOM   1286  C  CB  . THR A 1 198 ? 6.790   -27.402 -20.706 1.00 36.97  ? 198  THR A CB  1 
ATOM   1287  O  OG1 . THR A 1 198 ? 6.834   -27.382 -22.146 1.00 29.76  ? 198  THR A OG1 1 
ATOM   1288  C  CG2 . THR A 1 198 ? 5.683   -26.492 -20.184 1.00 32.37  ? 198  THR A CG2 1 
ATOM   1289  N  N   . ALA A 1 199 ? 8.132   -28.702 -18.414 1.00 33.25  ? 199  ALA A N   1 
ATOM   1290  C  CA  . ALA A 1 199 ? 8.160   -29.248 -17.058 1.00 28.19  ? 199  ALA A CA  1 
ATOM   1291  C  C   . ALA A 1 199 ? 9.295   -28.650 -16.233 1.00 33.36  ? 199  ALA A C   1 
ATOM   1292  O  O   . ALA A 1 199 ? 9.096   -28.248 -15.095 1.00 35.62  ? 199  ALA A O   1 
ATOM   1293  C  CB  . ALA A 1 199 ? 8.281   -30.781 -17.096 1.00 17.80  ? 199  ALA A CB  1 
ATOM   1294  N  N   . ALA A 1 200 ? 10.489  -28.604 -16.812 1.00 26.35  ? 200  ALA A N   1 
ATOM   1295  C  CA  . ALA A 1 200 ? 11.649  -28.056 -16.132 1.00 20.13  ? 200  ALA A CA  1 
ATOM   1296  C  C   . ALA A 1 200 ? 11.370  -26.638 -15.657 1.00 29.11  ? 200  ALA A C   1 
ATOM   1297  O  O   . ALA A 1 200 ? 11.619  -26.286 -14.502 1.00 41.98  ? 200  ALA A O   1 
ATOM   1298  C  CB  . ALA A 1 200 ? 12.860  -28.067 -17.065 1.00 26.31  ? 200  ALA A CB  1 
ATOM   1299  N  N   . LEU A 1 201 ? 10.845  -25.821 -16.554 1.00 22.05  ? 201  LEU A N   1 
ATOM   1300  C  CA  . LEU A 1 201 ? 10.625  -24.422 -16.242 1.00 30.24  ? 201  LEU A CA  1 
ATOM   1301  C  C   . LEU A 1 201 ? 9.473   -24.233 -15.280 1.00 36.59  ? 201  LEU A C   1 
ATOM   1302  O  O   . LEU A 1 201 ? 9.514   -23.374 -14.397 1.00 33.28  ? 201  LEU A O   1 
ATOM   1303  C  CB  . LEU A 1 201 ? 10.408  -23.612 -17.523 1.00 29.79  ? 201  LEU A CB  1 
ATOM   1304  C  CG  . LEU A 1 201 ? 11.762  -23.042 -17.930 1.00 36.62  ? 201  LEU A CG  1 
ATOM   1305  C  CD1 . LEU A 1 201 ? 12.502  -24.006 -18.845 1.00 22.76  ? 201  LEU A CD1 1 
ATOM   1306  C  CD2 . LEU A 1 201 ? 11.617  -21.664 -18.543 1.00 52.38  ? 201  LEU A CD2 1 
ATOM   1307  N  N   . VAL A 1 202 ? 8.431   -25.031 -15.458 1.00 26.69  ? 202  VAL A N   1 
ATOM   1308  C  CA  . VAL A 1 202 ? 7.330   -24.997 -14.516 1.00 32.44  ? 202  VAL A CA  1 
ATOM   1309  C  C   . VAL A 1 202 ? 7.892   -25.173 -13.113 1.00 38.17  ? 202  VAL A C   1 
ATOM   1310  O  O   . VAL A 1 202 ? 7.645   -24.354 -12.232 1.00 37.93  ? 202  VAL A O   1 
ATOM   1311  C  CB  . VAL A 1 202 ? 6.315   -26.101 -14.807 1.00 26.85  ? 202  VAL A CB  1 
ATOM   1312  C  CG1 . VAL A 1 202 ? 5.380   -26.284 -13.613 1.00 17.66  ? 202  VAL A CG1 1 
ATOM   1313  C  CG2 . VAL A 1 202 ? 5.540   -25.772 -16.090 1.00 25.38  ? 202  VAL A CG2 1 
ATOM   1314  N  N   . ASN A 1 203 ? 8.673   -26.235 -12.934 1.00 26.12  ? 203  ASN A N   1 
ATOM   1315  C  CA  . ASN A 1 203 ? 9.249   -26.587 -11.645 1.00 25.99  ? 203  ASN A CA  1 
ATOM   1316  C  C   . ASN A 1 203 ? 10.052  -25.450 -11.084 1.00 23.63  ? 203  ASN A C   1 
ATOM   1317  O  O   . ASN A 1 203 ? 10.014  -25.159 -9.888  1.00 29.42  ? 203  ASN A O   1 
ATOM   1318  C  CB  . ASN A 1 203 ? 10.185  -27.783 -11.801 1.00 26.96  ? 203  ASN A CB  1 
ATOM   1319  C  CG  . ASN A 1 203 ? 9.476   -29.099 -11.639 1.00 49.67  ? 203  ASN A CG  1 
ATOM   1320  O  OD1 . ASN A 1 203 ? 8.241   -29.181 -11.706 1.00 49.94  ? 203  ASN A OD1 1 
ATOM   1321  N  ND2 . ASN A 1 203 ? 10.255  -30.153 -11.417 1.00 61.89  ? 203  ASN A ND2 1 
ATOM   1322  N  N   . TRP A 1 204 ? 10.804  -24.823 -11.972 1.00 21.31  ? 204  TRP A N   1 
ATOM   1323  C  CA  . TRP A 1 204 ? 11.695  -23.752 -11.589 1.00 18.72  ? 204  TRP A CA  1 
ATOM   1324  C  C   . TRP A 1 204 ? 10.896  -22.547 -11.144 1.00 24.79  ? 204  TRP A C   1 
ATOM   1325  O  O   . TRP A 1 204 ? 11.091  -22.016 -10.046 1.00 36.33  ? 204  TRP A O   1 
ATOM   1326  C  CB  . TRP A 1 204 ? 12.597  -23.400 -12.766 1.00 22.98  ? 204  TRP A CB  1 
ATOM   1327  C  CG  . TRP A 1 204 ? 13.724  -22.513 -12.407 1.00 34.34  ? 204  TRP A CG  1 
ATOM   1328  C  CD1 . TRP A 1 204 ? 14.583  -22.663 -11.355 1.00 29.49  ? 204  TRP A CD1 1 
ATOM   1329  C  CD2 . TRP A 1 204 ? 14.142  -21.326 -13.105 1.00 35.47  ? 204  TRP A CD2 1 
ATOM   1330  N  NE1 . TRP A 1 204 ? 15.502  -21.632 -11.346 1.00 39.03  ? 204  TRP A NE1 1 
ATOM   1331  C  CE2 . TRP A 1 204 ? 15.253  -20.801 -12.411 1.00 30.29  ? 204  TRP A CE2 1 
ATOM   1332  C  CE3 . TRP A 1 204 ? 13.679  -20.654 -14.240 1.00 19.41  ? 204  TRP A CE3 1 
ATOM   1333  C  CZ2 . TRP A 1 204 ? 15.905  -19.636 -12.818 1.00 23.06  ? 204  TRP A CZ2 1 
ATOM   1334  C  CZ3 . TRP A 1 204 ? 14.327  -19.502 -14.639 1.00 25.67  ? 204  TRP A CZ3 1 
ATOM   1335  C  CH2 . TRP A 1 204 ? 15.426  -19.005 -13.933 1.00 27.44  ? 204  TRP A CH2 1 
ATOM   1336  N  N   . ILE A 1 205 ? 9.966   -22.138 -11.992 1.00 28.16  ? 205  ILE A N   1 
ATOM   1337  C  CA  . ILE A 1 205 ? 9.182   -20.925 -11.752 1.00 39.22  ? 205  ILE A CA  1 
ATOM   1338  C  C   . ILE A 1 205 ? 8.487   -20.937 -10.381 1.00 43.33  ? 205  ILE A C   1 
ATOM   1339  O  O   . ILE A 1 205 ? 8.417   -19.902 -9.706  1.00 54.41  ? 205  ILE A O   1 
ATOM   1340  C  CB  . ILE A 1 205 ? 8.165   -20.668 -12.915 1.00 26.67  ? 205  ILE A CB  1 
ATOM   1341  C  CG1 . ILE A 1 205 ? 8.906   -20.439 -14.236 1.00 26.93  ? 205  ILE A CG1 1 
ATOM   1342  C  CG2 . ILE A 1 205 ? 7.280   -19.476 -12.624 1.00 27.54  ? 205  ILE A CG2 1 
ATOM   1343  C  CD1 . ILE A 1 205 ? 8.034   -20.572 -15.467 1.00 22.35  ? 205  ILE A CD1 1 
ATOM   1344  N  N   . VAL A 1 206 ? 7.995   -22.104 -9.967  1.00 30.12  ? 206  VAL A N   1 
ATOM   1345  C  CA  . VAL A 1 206 ? 7.286   -22.228 -8.691  1.00 30.08  ? 206  VAL A CA  1 
ATOM   1346  C  C   . VAL A 1 206 ? 8.240   -22.547 -7.538  1.00 32.07  ? 206  VAL A C   1 
ATOM   1347  O  O   . VAL A 1 206 ? 7.828   -22.615 -6.377  1.00 34.94  ? 206  VAL A O   1 
ATOM   1348  C  CB  . VAL A 1 206 ? 6.177   -23.308 -8.745  1.00 29.88  ? 206  VAL A CB  1 
ATOM   1349  C  CG1 . VAL A 1 206 ? 5.094   -22.922 -9.749  1.00 22.11  ? 206  VAL A CG1 1 
ATOM   1350  C  CG2 . VAL A 1 206 ? 6.771   -24.665 -9.082  1.00 30.35  ? 206  VAL A CG2 1 
ATOM   1351  N  N   . SER A 1 207 ? 9.521   -22.716 -7.861  1.00 36.95  ? 207  SER A N   1 
ATOM   1352  C  CA  . SER A 1 207 ? 10.508  -23.144 -6.870  1.00 29.25  ? 207  SER A CA  1 
ATOM   1353  C  C   . SER A 1 207 ? 11.081  -21.973 -6.074  1.00 23.28  ? 207  SER A C   1 
ATOM   1354  O  O   . SER A 1 207 ? 11.646  -22.160 -4.997  1.00 28.76  ? 207  SER A O   1 
ATOM   1355  C  CB  . SER A 1 207 ? 11.628  -23.953 -7.541  1.00 28.14  ? 207  SER A CB  1 
ATOM   1356  O  OG  . SER A 1 207 ? 12.645  -23.117 -8.070  1.00 30.82  ? 207  SER A OG  1 
ATOM   1357  N  N   . LYS A 1 208 ? 10.926  -20.771 -6.608  1.00 23.88  ? 208  LYS A N   1 
ATOM   1358  C  CA  . LYS A 1 208 ? 11.417  -19.566 -5.956  1.00 25.40  ? 208  LYS A CA  1 
ATOM   1359  C  C   . LYS A 1 208 ? 10.428  -18.426 -6.138  1.00 22.34  ? 208  LYS A C   1 
ATOM   1360  O  O   . LYS A 1 208 ? 9.681   -18.386 -7.108  1.00 43.02  ? 208  LYS A O   1 
ATOM   1361  C  CB  . LYS A 1 208 ? 12.767  -19.150 -6.552  1.00 36.63  ? 208  LYS A CB  1 
ATOM   1362  C  CG  . LYS A 1 208 ? 13.842  -20.195 -6.405  1.00 36.79  ? 208  LYS A CG  1 
ATOM   1363  C  CD  . LYS A 1 208 ? 15.216  -19.698 -6.824  1.00 34.37  ? 208  LYS A CD  1 
ATOM   1364  C  CE  . LYS A 1 208 ? 16.267  -20.703 -6.328  1.00 49.05  ? 208  LYS A CE  1 
ATOM   1365  N  NZ  . LYS A 1 208 ? 17.694  -20.376 -6.634  1.00 54.43  ? 208  LYS A NZ  1 
ATOM   1366  N  N   . PRO A 1 209 ? 10.439  -17.481 -5.205  1.00 24.62  ? 209  PRO A N   1 
ATOM   1367  C  CA  . PRO A 1 209 ? 9.502   -16.360 -5.226  1.00 17.51  ? 209  PRO A CA  1 
ATOM   1368  C  C   . PRO A 1 209 ? 9.928   -15.278 -6.226  1.00 31.78  ? 209  PRO A C   1 
ATOM   1369  O  O   . PRO A 1 209 ? 10.165  -14.125 -5.855  1.00 31.20  ? 209  PRO A O   1 
ATOM   1370  C  CB  . PRO A 1 209 ? 9.620   -15.820 -3.808  1.00 13.54  ? 209  PRO A CB  1 
ATOM   1371  C  CG  . PRO A 1 209 ? 11.055  -16.099 -3.452  1.00 11.13  ? 209  PRO A CG  1 
ATOM   1372  C  CD  . PRO A 1 209 ? 11.327  -17.441 -4.024  1.00 14.30  ? 209  PRO A CD  1 
ATOM   1373  N  N   . PHE A 1 210 ? 10.022  -15.644 -7.495  1.00 27.61  ? 210  PHE A N   1 
ATOM   1374  C  CA  . PHE A 1 210 ? 10.382  -14.668 -8.511  1.00 28.06  ? 210  PHE A CA  1 
ATOM   1375  C  C   . PHE A 1 210 ? 9.454   -13.469 -8.502  1.00 27.83  ? 210  PHE A C   1 
ATOM   1376  O  O   . PHE A 1 210 ? 8.243   -13.605 -8.380  1.00 42.24  ? 210  PHE A O   1 
ATOM   1377  C  CB  . PHE A 1 210 ? 10.425  -15.315 -9.886  1.00 17.13  ? 210  PHE A CB  1 
ATOM   1378  C  CG  . PHE A 1 210 ? 11.589  -16.225 -10.062 1.00 20.79  ? 210  PHE A CG  1 
ATOM   1379  C  CD1 . PHE A 1 210 ? 11.423  -17.601 -10.051 1.00 23.75  ? 210  PHE A CD1 1 
ATOM   1380  C  CD2 . PHE A 1 210 ? 12.862  -15.709 -10.185 1.00 18.29  ? 210  PHE A CD2 1 
ATOM   1381  C  CE1 . PHE A 1 210 ? 12.499  -18.445 -10.199 1.00 13.55  ? 210  PHE A CE1 1 
ATOM   1382  C  CE2 . PHE A 1 210 ? 13.942  -16.550 -10.332 1.00 30.97  ? 210  PHE A CE2 1 
ATOM   1383  C  CZ  . PHE A 1 210 ? 13.761  -17.921 -10.337 1.00 18.68  ? 210  PHE A CZ  1 
ATOM   1384  N  N   . VAL A 1 211 ? 10.044  -12.292 -8.627  1.00 21.41  ? 211  VAL A N   1 
ATOM   1385  C  CA  . VAL A 1 211 ? 9.309   -11.046 -8.485  1.00 31.89  ? 211  VAL A CA  1 
ATOM   1386  C  C   . VAL A 1 211 ? 8.932   -10.478 -9.845  1.00 30.87  ? 211  VAL A C   1 
ATOM   1387  O  O   . VAL A 1 211 ? 7.814   -10.019 -10.048 1.00 37.04  ? 211  VAL A O   1 
ATOM   1388  C  CB  . VAL A 1 211 ? 10.133  -9.987  -7.708  1.00 26.48  ? 211  VAL A CB  1 
ATOM   1389  C  CG1 . VAL A 1 211 ? 9.481   -8.618  -7.816  1.00 23.77  ? 211  VAL A CG1 1 
ATOM   1390  C  CG2 . VAL A 1 211 ? 10.322  -10.403 -6.234  1.00 14.30  ? 211  VAL A CG2 1 
ATOM   1391  N  N   . LEU A 1 212 ? 9.877   -10.525 -10.772 1.00 30.91  ? 212  LEU A N   1 
ATOM   1392  C  CA  . LEU A 1 212 ? 9.710   -9.957  -12.104 1.00 19.52  ? 212  LEU A CA  1 
ATOM   1393  C  C   . LEU A 1 212 ? 10.410  -10.867 -13.111 1.00 23.28  ? 212  LEU A C   1 
ATOM   1394  O  O   . LEU A 1 212 ? 11.335  -11.588 -12.751 1.00 36.91  ? 212  LEU A O   1 
ATOM   1395  C  CB  . LEU A 1 212 ? 10.317  -8.546  -12.139 1.00 25.85  ? 212  LEU A CB  1 
ATOM   1396  C  CG  . LEU A 1 212 ? 10.563  -7.810  -13.465 1.00 25.05  ? 212  LEU A CG  1 
ATOM   1397  C  CD1 . LEU A 1 212 ? 9.306   -7.768  -14.300 1.00 32.80  ? 212  LEU A CD1 1 
ATOM   1398  C  CD2 . LEU A 1 212 ? 11.069  -6.390  -13.194 1.00 28.60  ? 212  LEU A CD2 1 
ATOM   1399  N  N   . SER A 1 213 ? 9.984   -10.822 -14.370 1.00 27.38  ? 213  SER A N   1 
ATOM   1400  C  CA  . SER A 1 213 ? 10.532  -11.707 -15.396 1.00 24.12  ? 213  SER A CA  1 
ATOM   1401  C  C   . SER A 1 213 ? 10.204  -11.241 -16.810 1.00 27.58  ? 213  SER A C   1 
ATOM   1402  O  O   . SER A 1 213 ? 9.250   -10.506 -17.041 1.00 28.70  ? 213  SER A O   1 
ATOM   1403  C  CB  . SER A 1 213 ? 9.985   -13.125 -15.200 1.00 24.40  ? 213  SER A CB  1 
ATOM   1404  O  OG  . SER A 1 213 ? 10.363  -13.960 -16.276 1.00 37.22  ? 213  SER A OG  1 
ATOM   1405  N  N   . ALA A 1 214 ? 10.994  -11.689 -17.769 1.00 33.73  ? 214  ALA A N   1 
ATOM   1406  C  CA  . ALA A 1 214 ? 10.707  -11.388 -19.159 1.00 30.41  ? 214  ALA A CA  1 
ATOM   1407  C  C   . ALA A 1 214 ? 11.159  -12.554 -20.004 1.00 21.12  ? 214  ALA A C   1 
ATOM   1408  O  O   . ALA A 1 214 ? 12.167  -13.179 -19.683 1.00 24.65  ? 214  ALA A O   1 
ATOM   1409  C  CB  . ALA A 1 214 ? 11.420  -10.125 -19.579 1.00 27.24  ? 214  ALA A CB  1 
ATOM   1410  N  N   . ASN A 1 215 ? 10.405  -12.878 -21.057 1.00 32.15  ? 215  ASN A N   1 
ATOM   1411  C  CA  . ASN A 1 215 ? 10.911  -13.821 -22.051 1.00 40.35  ? 215  ASN A CA  1 
ATOM   1412  C  C   . ASN A 1 215 ? 10.876  -13.270 -23.494 1.00 45.93  ? 215  ASN A C   1 
ATOM   1413  O  O   . ASN A 1 215 ? 9.966   -12.522 -23.885 1.00 33.21  ? 215  ASN A O   1 
ATOM   1414  C  CB  . ASN A 1 215 ? 10.350  -15.255 -21.885 1.00 34.85  ? 215  ASN A CB  1 
ATOM   1415  C  CG  . ASN A 1 215 ? 8.954   -15.415 -22.418 1.00 33.73  ? 215  ASN A CG  1 
ATOM   1416  O  OD1 . ASN A 1 215 ? 8.748   -16.111 -23.411 1.00 47.36  ? 215  ASN A OD1 1 
ATOM   1417  N  ND2 . ASN A 1 215 ? 7.977   -14.792 -21.758 1.00 32.58  ? 215  ASN A ND2 1 
ATOM   1418  N  N   . PHE A 1 216 ? 11.913  -13.613 -24.258 1.00 37.45  ? 216  PHE A N   1 
ATOM   1419  C  CA  . PHE A 1 216 ? 12.206  -12.915 -25.487 1.00 16.66  ? 216  PHE A CA  1 
ATOM   1420  C  C   . PHE A 1 216 ? 11.882  -13.752 -26.696 1.00 29.29  ? 216  PHE A C   1 
ATOM   1421  O  O   . PHE A 1 216 ? 12.170  -14.948 -26.748 1.00 28.03  ? 216  PHE A O   1 
ATOM   1422  C  CB  . PHE A 1 216 ? 13.666  -12.473 -25.496 1.00 21.13  ? 216  PHE A CB  1 
ATOM   1423  C  CG  . PHE A 1 216 ? 14.025  -11.621 -24.323 1.00 34.21  ? 216  PHE A CG  1 
ATOM   1424  C  CD1 . PHE A 1 216 ? 14.489  -12.187 -23.149 1.00 35.52  ? 216  PHE A CD1 1 
ATOM   1425  C  CD2 . PHE A 1 216 ? 13.858  -10.248 -24.377 1.00 38.67  ? 216  PHE A CD2 1 
ATOM   1426  C  CE1 . PHE A 1 216 ? 14.796  -11.395 -22.059 1.00 32.21  ? 216  PHE A CE1 1 
ATOM   1427  C  CE2 . PHE A 1 216 ? 14.163  -9.451  -23.279 1.00 32.64  ? 216  PHE A CE2 1 
ATOM   1428  C  CZ  . PHE A 1 216 ? 14.630  -10.023 -22.127 1.00 23.62  ? 216  PHE A CZ  1 
ATOM   1429  N  N   . HIS A 1 217 ? 11.281  -13.091 -27.674 1.00 25.94  ? 217  HIS A N   1 
ATOM   1430  C  CA  . HIS A 1 217 ? 10.849  -13.724 -28.891 1.00 29.12  ? 217  HIS A CA  1 
ATOM   1431  C  C   . HIS A 1 217 ? 11.275  -12.854 -30.058 1.00 33.00  ? 217  HIS A C   1 
ATOM   1432  O  O   . HIS A 1 217 ? 11.753  -11.739 -29.867 1.00 29.30  ? 217  HIS A O   1 
ATOM   1433  C  CB  . HIS A 1 217 ? 9.326   -13.869 -28.884 1.00 32.26  ? 217  HIS A CB  1 
ATOM   1434  C  CG  . HIS A 1 217 ? 8.815   -14.818 -27.846 1.00 35.76  ? 217  HIS A CG  1 
ATOM   1435  N  ND1 . HIS A 1 217 ? 8.374   -16.086 -28.152 1.00 29.25  ? 217  HIS A ND1 1 
ATOM   1436  C  CD2 . HIS A 1 217 ? 8.688   -14.689 -26.502 1.00 31.41  ? 217  HIS A CD2 1 
ATOM   1437  C  CE1 . HIS A 1 217 ? 7.986   -16.696 -27.047 1.00 33.34  ? 217  HIS A CE1 1 
ATOM   1438  N  NE2 . HIS A 1 217 ? 8.169   -15.870 -26.030 1.00 27.17  ? 217  HIS A NE2 1 
ATOM   1439  N  N   . GLY A 1 218 ? 11.091  -13.367 -31.267 1.00 33.24  ? 218  GLY A N   1 
ATOM   1440  C  CA  . GLY A 1 218 ? 11.411  -12.612 -32.458 1.00 36.01  ? 218  GLY A CA  1 
ATOM   1441  C  C   . GLY A 1 218 ? 10.250  -12.725 -33.412 1.00 41.65  ? 218  GLY A C   1 
ATOM   1442  O  O   . GLY A 1 218 ? 9.380   -13.581 -33.237 1.00 51.07  ? 218  GLY A O   1 
ATOM   1443  N  N   . GLY A 1 219 ? 10.224  -11.859 -34.412 1.00 36.51  ? 219  GLY A N   1 
ATOM   1444  C  CA  . GLY A 1 219 ? 9.156   -11.883 -35.387 1.00 36.67  ? 219  GLY A CA  1 
ATOM   1445  C  C   . GLY A 1 219 ? 8.572   -10.497 -35.468 1.00 53.73  ? 219  GLY A C   1 
ATOM   1446  O  O   . GLY A 1 219 ? 8.005   -10.088 -36.486 1.00 61.87  ? 219  GLY A O   1 
ATOM   1447  N  N   . ALA A 1 220 ? 8.731   -9.756  -34.382 1.00 41.67  ? 220  ALA A N   1 
ATOM   1448  C  CA  . ALA A 1 220 ? 8.219   -8.401  -34.345 1.00 47.76  ? 220  ALA A CA  1 
ATOM   1449  C  C   . ALA A 1 220 ? 8.998   -7.629  -33.304 1.00 42.62  ? 220  ALA A C   1 
ATOM   1450  O  O   . ALA A 1 220 ? 9.883   -8.183  -32.663 1.00 41.77  ? 220  ALA A O   1 
ATOM   1451  C  CB  . ALA A 1 220 ? 6.721   -8.402  -34.032 1.00 48.05  ? 220  ALA A CB  1 
ATOM   1452  N  N   . VAL A 1 221 ? 8.669   -6.349  -33.150 1.00 45.81  ? 221  VAL A N   1 
ATOM   1453  C  CA  . VAL A 1 221 ? 9.354   -5.475  -32.208 1.00 42.40  ? 221  VAL A CA  1 
ATOM   1454  C  C   . VAL A 1 221 ? 8.337   -4.786  -31.304 1.00 48.03  ? 221  VAL A C   1 
ATOM   1455  O  O   . VAL A 1 221 ? 7.753   -3.766  -31.683 1.00 51.13  ? 221  VAL A O   1 
ATOM   1456  C  CB  . VAL A 1 221 ? 10.170  -4.401  -32.938 1.00 37.22  ? 221  VAL A CB  1 
ATOM   1457  C  CG1 . VAL A 1 221 ? 11.182  -3.791  -31.983 1.00 38.12  ? 221  VAL A CG1 1 
ATOM   1458  C  CG2 . VAL A 1 221 ? 10.874  -4.994  -34.158 1.00 38.65  ? 221  VAL A CG2 1 
ATOM   1459  N  N   . VAL A 1 222 ? 8.129   -5.335  -30.108 1.00 45.46  ? 222  VAL A N   1 
ATOM   1460  C  CA  . VAL A 1 222 ? 7.057   -4.856  -29.233 1.00 49.34  ? 222  VAL A CA  1 
ATOM   1461  C  C   . VAL A 1 222 ? 7.135   -5.462  -27.830 1.00 45.25  ? 222  VAL A C   1 
ATOM   1462  O  O   . VAL A 1 222 ? 7.649   -6.568  -27.639 1.00 48.10  ? 222  VAL A O   1 
ATOM   1463  C  CB  . VAL A 1 222 ? 5.656   -5.187  -29.836 1.00 51.47  ? 222  VAL A CB  1 
ATOM   1464  C  CG1 . VAL A 1 222 ? 5.413   -6.704  -29.813 1.00 47.02  ? 222  VAL A CG1 1 
ATOM   1465  C  CG2 . VAL A 1 222 ? 4.516   -4.429  -29.113 1.00 44.97  ? 222  VAL A CG2 1 
ATOM   1466  N  N   . ALA A 1 223 ? 6.600   -4.730  -26.860 1.00 33.54  ? 223  ALA A N   1 
ATOM   1467  C  CA  . ALA A 1 223 ? 6.556   -5.173  -25.482 1.00 37.46  ? 223  ALA A CA  1 
ATOM   1468  C  C   . ALA A 1 223 ? 5.125   -5.611  -25.131 1.00 46.20  ? 223  ALA A C   1 
ATOM   1469  O  O   . ALA A 1 223 ? 4.202   -4.779  -25.058 1.00 28.00  ? 223  ALA A O   1 
ATOM   1470  C  CB  . ALA A 1 223 ? 7.029   -4.051  -24.569 1.00 33.33  ? 223  ALA A CB  1 
ATOM   1471  N  N   . SER A 1 224 ? 4.964   -6.922  -24.926 1.00 39.73  ? 224  SER A N   1 
ATOM   1472  C  CA  . SER A 1 224 ? 3.661   -7.558  -24.730 1.00 22.52  ? 224  SER A CA  1 
ATOM   1473  C  C   . SER A 1 224 ? 3.498   -8.070  -23.308 1.00 29.27  ? 224  SER A C   1 
ATOM   1474  O  O   . SER A 1 224 ? 4.433   -8.610  -22.722 1.00 36.36  ? 224  SER A O   1 
ATOM   1475  C  CB  . SER A 1 224 ? 3.500   -8.731  -25.706 1.00 37.89  ? 224  SER A CB  1 
ATOM   1476  O  OG  . SER A 1 224 ? 2.223   -9.351  -25.604 1.00 55.16  ? 224  SER A OG  1 
ATOM   1477  N  N   . TYR A 1 225 ? 2.295   -7.929  -22.765 1.00 37.62  ? 225  TYR A N   1 
ATOM   1478  C  CA  . TYR A 1 225 ? 2.027   -8.272  -21.371 1.00 27.62  ? 225  TYR A CA  1 
ATOM   1479  C  C   . TYR A 1 225 ? 0.705   -9.000  -21.282 1.00 31.10  ? 225  TYR A C   1 
ATOM   1480  O  O   . TYR A 1 225 ? -0.089  -8.951  -22.226 1.00 42.04  ? 225  TYR A O   1 
ATOM   1481  C  CB  . TYR A 1 225 ? 1.963   -6.995  -20.525 1.00 34.82  ? 225  TYR A CB  1 
ATOM   1482  C  CG  . TYR A 1 225 ? 1.040   -5.932  -21.089 1.00 25.62  ? 225  TYR A CG  1 
ATOM   1483  C  CD1 . TYR A 1 225 ? 1.471   -5.063  -22.084 1.00 33.54  ? 225  TYR A CD1 1 
ATOM   1484  C  CD2 . TYR A 1 225 ? -0.251  -5.797  -20.626 1.00 28.00  ? 225  TYR A CD2 1 
ATOM   1485  C  CE1 . TYR A 1 225 ? 0.635   -4.086  -22.600 1.00 42.89  ? 225  TYR A CE1 1 
ATOM   1486  C  CE2 . TYR A 1 225 ? -1.097  -4.824  -21.134 1.00 45.74  ? 225  TYR A CE2 1 
ATOM   1487  C  CZ  . TYR A 1 225 ? -0.648  -3.970  -22.120 1.00 51.00  ? 225  TYR A CZ  1 
ATOM   1488  O  OH  . TYR A 1 225 ? -1.486  -2.999  -22.631 1.00 55.91  ? 225  TYR A OH  1 
ATOM   1489  N  N   . PRO A 1 226 ? 0.457   -9.669  -20.147 1.00 23.64  ? 226  PRO A N   1 
ATOM   1490  C  CA  . PRO A 1 226 ? -0.771  -10.431 -19.858 1.00 30.45  ? 226  PRO A CA  1 
ATOM   1491  C  C   . PRO A 1 226 ? -2.075  -9.608  -19.952 1.00 35.42  ? 226  PRO A C   1 
ATOM   1492  O  O   . PRO A 1 226 ? -2.063  -8.372  -19.830 1.00 38.33  ? 226  PRO A O   1 
ATOM   1493  C  CB  . PRO A 1 226 ? -0.555  -10.908 -18.412 1.00 37.39  ? 226  PRO A CB  1 
ATOM   1494  C  CG  . PRO A 1 226 ? 0.929   -10.915 -18.229 1.00 45.15  ? 226  PRO A CG  1 
ATOM   1495  C  CD  . PRO A 1 226 ? 1.455   -9.782  -19.070 1.00 32.11  ? 226  PRO A CD  1 
ATOM   1496  N  N   . TYR A 1 227 ? -3.197  -10.285 -20.184 1.00 29.53  ? 227  TYR A N   1 
ATOM   1497  C  CA  . TYR A 1 227 ? -3.228  -11.708 -20.462 1.00 24.78  ? 227  TYR A CA  1 
ATOM   1498  C  C   . TYR A 1 227 ? -3.110  -11.938 -21.967 1.00 32.03  ? 227  TYR A C   1 
ATOM   1499  O  O   . TYR A 1 227 ? -3.349  -11.021 -22.770 1.00 25.61  ? 227  TYR A O   1 
ATOM   1500  C  CB  . TYR A 1 227 ? -4.551  -12.311 -19.984 1.00 40.26  ? 227  TYR A CB  1 
ATOM   1501  C  CG  . TYR A 1 227 ? -4.750  -12.381 -18.491 1.00 37.00  ? 227  TYR A CG  1 
ATOM   1502  C  CD1 . TYR A 1 227 ? -3.956  -13.209 -17.698 1.00 20.61  ? 227  TYR A CD1 1 
ATOM   1503  C  CD2 . TYR A 1 227 ? -5.769  -11.658 -17.880 1.00 36.61  ? 227  TYR A CD2 1 
ATOM   1504  C  CE1 . TYR A 1 227 ? -4.157  -13.297 -16.339 1.00 17.31  ? 227  TYR A CE1 1 
ATOM   1505  C  CE2 . TYR A 1 227 ? -5.972  -11.734 -16.522 1.00 35.01  ? 227  TYR A CE2 1 
ATOM   1506  C  CZ  . TYR A 1 227 ? -5.160  -12.555 -15.757 1.00 36.50  ? 227  TYR A CZ  1 
ATOM   1507  O  OH  . TYR A 1 227 ? -5.355  -12.633 -14.403 1.00 43.99  ? 227  TYR A OH  1 
ATOM   1508  N  N   . ASP A 1 228 ? -2.764  -13.172 -22.337 1.00 39.25  ? 228  ASP A N   1 
ATOM   1509  C  CA  . ASP A 1 228 ? -2.606  -13.578 -23.736 1.00 28.46  ? 228  ASP A CA  1 
ATOM   1510  C  C   . ASP A 1 228 ? -3.895  -14.202 -24.258 1.00 33.87  ? 228  ASP A C   1 
ATOM   1511  O  O   . ASP A 1 228 ? -4.041  -14.444 -25.456 1.00 41.67  ? 228  ASP A O   1 
ATOM   1512  C  CB  . ASP A 1 228 ? -1.454  -14.585 -23.881 1.00 37.29  ? 228  ASP A CB  1 
ATOM   1513  C  CG  . ASP A 1 228 ? -0.073  -13.912 -23.935 1.00 52.31  ? 228  ASP A CG  1 
ATOM   1514  O  OD1 . ASP A 1 228 ? -0.015  -12.677 -24.126 1.00 52.49  ? 228  ASP A OD1 1 
ATOM   1515  O  OD2 . ASP A 1 228 ? 0.958   -14.621 -23.800 1.00 49.52  ? 228  ASP A OD2 1 
ATOM   1516  N  N   . ASN A 1 229 ? -4.826  -14.475 -23.351 1.00 34.52  ? 229  ASN A N   1 
ATOM   1517  C  CA  . ASN A 1 229 ? -6.097  -15.084 -23.740 1.00 46.29  ? 229  ASN A CA  1 
ATOM   1518  C  C   . ASN A 1 229 ? -7.260  -14.688 -22.821 1.00 45.47  ? 229  ASN A C   1 
ATOM   1519  O  O   . ASN A 1 229 ? -7.064  -13.971 -21.832 1.00 32.79  ? 229  ASN A O   1 
ATOM   1520  C  CB  . ASN A 1 229 ? -5.965  -16.612 -23.839 1.00 34.38  ? 229  ASN A CB  1 
ATOM   1521  C  CG  . ASN A 1 229 ? -5.895  -17.292 -22.480 1.00 38.51  ? 229  ASN A CG  1 
ATOM   1522  O  OD1 . ASN A 1 229 ? -5.877  -16.641 -21.422 1.00 31.89  ? 229  ASN A OD1 1 
ATOM   1523  N  ND2 . ASN A 1 229 ? -5.854  -18.621 -22.502 1.00 36.50  ? 229  ASN A ND2 1 
ATOM   1524  N  N   . SER A 1 230 ? -8.464  -15.153 -23.153 1.00 43.36  ? 230  SER A N   1 
ATOM   1525  C  CA  . SER A 1 230 ? -9.639  -14.841 -22.344 1.00 39.79  ? 230  SER A CA  1 
ATOM   1526  C  C   . SER A 1 230 ? -10.676 -15.948 -22.408 1.00 31.13  ? 230  SER A C   1 
ATOM   1527  O  O   . SER A 1 230 ? -10.562 -16.860 -23.225 1.00 36.38  ? 230  SER A O   1 
ATOM   1528  C  CB  . SER A 1 230 ? -10.255 -13.518 -22.800 1.00 30.76  ? 230  SER A CB  1 
ATOM   1529  O  OG  . SER A 1 230 ? -10.771 -13.628 -24.107 1.00 37.76  ? 230  SER A OG  1 
ATOM   1530  N  N   . LEU A 1 231 ? -11.675 -15.863 -21.535 1.00 35.81  ? 231  LEU A N   1 
ATOM   1531  C  CA  . LEU A 1 231 ? -12.850 -16.743 -21.585 1.00 53.49  ? 231  LEU A CA  1 
ATOM   1532  C  C   . LEU A 1 231 ? -13.656 -16.554 -22.884 1.00 61.43  ? 231  LEU A C   1 
ATOM   1533  O  O   . LEU A 1 231 ? -14.269 -17.498 -23.396 1.00 64.72  ? 231  LEU A O   1 
ATOM   1534  C  CB  . LEU A 1 231 ? -13.772 -16.511 -20.374 1.00 52.42  ? 231  LEU A CB  1 
ATOM   1535  C  CG  . LEU A 1 231 ? -13.542 -17.242 -19.046 1.00 45.97  ? 231  LEU A CG  1 
ATOM   1536  C  CD1 . LEU A 1 231 ? -14.399 -16.624 -17.966 1.00 46.98  ? 231  LEU A CD1 1 
ATOM   1537  C  CD2 . LEU A 1 231 ? -13.840 -18.734 -19.148 1.00 41.57  ? 231  LEU A CD2 1 
ATOM   1538  N  N   . ALA A 1 232 ? -13.666 -15.332 -23.408 1.00 56.64  ? 232  ALA A N   1 
ATOM   1539  C  CA  . ALA A 1 232 ? -14.336 -15.064 -24.672 1.00 55.89  ? 232  ALA A CA  1 
ATOM   1540  C  C   . ALA A 1 232 ? -13.658 -15.840 -25.805 1.00 60.98  ? 232  ALA A C   1 
ATOM   1541  O  O   . ALA A 1 232 ? -14.292 -16.207 -26.802 1.00 57.54  ? 232  ALA A O   1 
ATOM   1542  C  CB  . ALA A 1 232 ? -14.339 -13.558 -24.967 1.00 39.71  ? 232  ALA A CB  1 
ATOM   1543  N  N   . HIS A 1 233 ? -12.364 -16.098 -25.631 1.00 64.61  ? 233  HIS A N   1 
ATOM   1544  C  CA  . HIS A 1 233 ? -11.537 -16.727 -26.668 1.00 59.03  ? 233  HIS A CA  1 
ATOM   1545  C  C   . HIS A 1 233 ? -11.693 -16.047 -28.015 1.00 56.06  ? 233  HIS A C   1 
ATOM   1546  O  O   . HIS A 1 233 ? -12.026 -16.674 -29.012 1.00 58.47  ? 233  HIS A O   1 
ATOM   1547  C  CB  . HIS A 1 233 ? -11.791 -18.237 -26.761 1.00 46.58  ? 233  HIS A CB  1 
ATOM   1548  C  CG  . HIS A 1 233 ? -11.306 -18.989 -25.561 1.00 48.74  ? 233  HIS A CG  1 
ATOM   1549  N  ND1 . HIS A 1 233 ? -12.152 -19.434 -24.567 1.00 60.19  ? 233  HIS A ND1 1 
ATOM   1550  C  CD2 . HIS A 1 233 ? -10.055 -19.321 -25.166 1.00 48.60  ? 233  HIS A CD2 1 
ATOM   1551  C  CE1 . HIS A 1 233 ? -11.444 -20.033 -23.624 1.00 61.35  ? 233  HIS A CE1 1 
ATOM   1552  N  NE2 . HIS A 1 233 ? -10.168 -19.972 -23.960 1.00 50.82  ? 233  HIS A NE2 1 
ATOM   1553  N  N   . ASN A 1 234 ? -11.446 -14.743 -28.018 1.00 59.09  ? 234  ASN A N   1 
ATOM   1554  C  CA  . ASN A 1 234 ? -11.449 -13.951 -29.238 1.00 59.32  ? 234  ASN A CA  1 
ATOM   1555  C  C   . ASN A 1 234 ? -10.152 -14.151 -30.020 1.00 52.78  ? 234  ASN A C   1 
ATOM   1556  O  O   . ASN A 1 234 ? -9.092  -14.367 -29.437 1.00 48.33  ? 234  ASN A O   1 
ATOM   1557  C  CB  . ASN A 1 234 ? -11.649 -12.474 -28.883 1.00 59.66  ? 234  ASN A CB  1 
ATOM   1558  C  CG  . ASN A 1 234 ? -12.897 -12.241 -28.020 1.00 59.44  ? 234  ASN A CG  1 
ATOM   1559  O  OD1 . ASN A 1 234 ? -13.955 -12.843 -28.256 1.00 56.04  ? 234  ASN A OD1 1 
ATOM   1560  N  ND2 . ASN A 1 234 ? -12.778 -11.360 -27.025 1.00 49.13  ? 234  ASN A ND2 1 
ATOM   1561  N  N   . GLU A 1 235 ? -10.230 -14.101 -31.343 1.00 64.60  ? 235  GLU A N   1 
ATOM   1562  C  CA  . GLU A 1 235 ? -9.026  -14.268 -32.160 1.00 64.77  ? 235  GLU A CA  1 
ATOM   1563  C  C   . GLU A 1 235 ? -7.991  -13.190 -31.848 1.00 63.37  ? 235  GLU A C   1 
ATOM   1564  O  O   . GLU A 1 235 ? -6.810  -13.488 -31.655 1.00 54.77  ? 235  GLU A O   1 
ATOM   1565  C  CB  . GLU A 1 235 ? -9.365  -14.252 -33.650 1.00 61.12  ? 235  GLU A CB  1 
ATOM   1566  C  CG  . GLU A 1 235 ? -8.149  -14.327 -34.568 1.00 68.79  ? 235  GLU A CG  1 
ATOM   1567  C  CD  . GLU A 1 235 ? -8.524  -14.150 -36.034 1.00 85.46  ? 235  GLU A CD  1 
ATOM   1568  O  OE1 . GLU A 1 235 ? -7.885  -14.801 -36.884 1.00 103.63 ? 235  GLU A OE1 1 
ATOM   1569  O  OE2 . GLU A 1 235 ? -9.460  -13.372 -36.345 1.00 70.66  ? 235  GLU A OE2 1 
ATOM   1570  N  N   . CYS A 1 236 ? -8.440  -11.940 -31.785 1.00 65.88  ? 236  CYS A N   1 
ATOM   1571  C  CA  . CYS A 1 236 ? -7.518  -10.825 -31.644 1.00 60.33  ? 236  CYS A CA  1 
ATOM   1572  C  C   . CYS A 1 236 ? -8.217  -9.513  -31.301 1.00 61.20  ? 236  CYS A C   1 
ATOM   1573  O  O   . CYS A 1 236 ? -9.439  -9.460  -31.103 1.00 64.25  ? 236  CYS A O   1 
ATOM   1574  C  CB  . CYS A 1 236 ? -6.754  -10.630 -32.956 1.00 66.42  ? 236  CYS A CB  1 
ATOM   1575  S  SG  . CYS A 1 236 ? -7.625  -9.589  -34.157 1.00 68.46  ? 236  CYS A SG  1 
ATOM   1576  N  N   . CYS A 1 237 ? -7.411  -8.454  -31.239 1.00 58.02  ? 237  CYS A N   1 
ATOM   1577  C  CA  . CYS A 1 237 ? -7.885  -7.072  -31.241 1.00 44.35  ? 237  CYS A CA  1 
ATOM   1578  C  C   . CYS A 1 237 ? -8.872  -6.798  -30.126 1.00 42.42  ? 237  CYS A C   1 
ATOM   1579  O  O   . CYS A 1 237 ? -9.712  -5.909  -30.243 1.00 46.23  ? 237  CYS A O   1 
ATOM   1580  C  CB  . CYS A 1 237 ? -8.529  -6.730  -32.592 1.00 53.19  ? 237  CYS A CB  1 
ATOM   1581  S  SG  . CYS A 1 237 ? -7.768  -7.542  -34.033 1.00 66.22  ? 237  CYS A SG  1 
ATOM   1582  N  N   . GLU A 1 238 ? -8.777  -7.567  -29.047 1.00 44.22  ? 238  GLU A N   1 
ATOM   1583  C  CA  . GLU A 1 238 ? -9.618  -7.326  -27.879 1.00 47.42  ? 238  GLU A CA  1 
ATOM   1584  C  C   . GLU A 1 238 ? -8.832  -7.557  -26.584 1.00 53.98  ? 238  GLU A C   1 
ATOM   1585  O  O   . GLU A 1 238 ? -8.399  -8.685  -26.299 1.00 51.96  ? 238  GLU A O   1 
ATOM   1586  C  CB  . GLU A 1 238 ? -10.878 -8.201  -27.934 1.00 57.34  ? 238  GLU A CB  1 
ATOM   1587  C  CG  . GLU A 1 238 ? -12.195 -7.438  -27.820 1.00 70.74  ? 238  GLU A CG  1 
ATOM   1588  C  CD  . GLU A 1 238 ? -13.351 -8.172  -28.486 1.00 85.39  ? 238  GLU A CD  1 
ATOM   1589  O  OE1 . GLU A 1 238 ? -14.530 -7.810  -28.248 1.00 91.01  ? 238  GLU A OE1 1 
ATOM   1590  O  OE2 . GLU A 1 238 ? -13.075 -9.113  -29.259 1.00 82.53  ? 238  GLU A OE2 1 
ATOM   1591  N  N   . GLU A 1 239 ? -8.650  -6.477  -25.819 1.00 59.93  ? 239  GLU A N   1 
ATOM   1592  C  CA  . GLU A 1 239 ? -7.914  -6.500  -24.555 1.00 52.42  ? 239  GLU A CA  1 
ATOM   1593  C  C   . GLU A 1 239 ? -8.474  -7.482  -23.521 1.00 51.05  ? 239  GLU A C   1 
ATOM   1594  O  O   . GLU A 1 239 ? -9.671  -7.479  -23.208 1.00 52.88  ? 239  GLU A O   1 
ATOM   1595  C  CB  . GLU A 1 239 ? -7.853  -5.096  -23.941 1.00 61.76  ? 239  GLU A CB  1 
ATOM   1596  C  CG  . GLU A 1 239 ? -6.893  -4.145  -24.637 1.00 77.30  ? 239  GLU A CG  1 
ATOM   1597  C  CD  . GLU A 1 239 ? -6.815  -2.789  -23.954 1.00 87.93  ? 239  GLU A CD  1 
ATOM   1598  O  OE1 . GLU A 1 239 ? -5.722  -2.173  -23.976 1.00 88.43  ? 239  GLU A OE1 1 
ATOM   1599  O  OE2 . GLU A 1 239 ? -7.841  -2.343  -23.391 1.00 86.60  ? 239  GLU A OE2 1 
ATOM   1600  N  N   . SER A 1 240 ? -7.588  -8.324  -22.998 1.00 44.38  ? 240  SER A N   1 
ATOM   1601  C  CA  . SER A 1 240 ? -7.911  -9.195  -21.875 1.00 29.34  ? 240  SER A CA  1 
ATOM   1602  C  C   . SER A 1 240 ? -6.994  -8.828  -20.707 1.00 36.26  ? 240  SER A C   1 
ATOM   1603  O  O   . SER A 1 240 ? -6.051  -9.550  -20.381 1.00 35.90  ? 240  SER A O   1 
ATOM   1604  C  CB  . SER A 1 240 ? -7.737  -10.662 -22.263 1.00 29.33  ? 240  SER A CB  1 
ATOM   1605  O  OG  . SER A 1 240 ? -7.920  -11.495 -21.134 1.00 37.46  ? 240  SER A OG  1 
ATOM   1606  N  N   . LEU A 1 241 ? -7.288  -7.698  -20.078 1.00 40.49  ? 241  LEU A N   1 
ATOM   1607  C  CA  . LEU A 1 241 ? -6.375  -7.098  -19.113 1.00 28.59  ? 241  LEU A CA  1 
ATOM   1608  C  C   . LEU A 1 241 ? -6.249  -7.829  -17.781 1.00 36.61  ? 241  LEU A C   1 
ATOM   1609  O  O   . LEU A 1 241 ? -7.041  -8.702  -17.436 1.00 37.90  ? 241  LEU A O   1 
ATOM   1610  C  CB  . LEU A 1 241 ? -6.719  -5.625  -18.888 1.00 28.13  ? 241  LEU A CB  1 
ATOM   1611  C  CG  . LEU A 1 241 ? -6.700  -4.823  -20.189 1.00 39.78  ? 241  LEU A CG  1 
ATOM   1612  C  CD1 . LEU A 1 241 ? -7.172  -3.391  -19.985 1.00 34.70  ? 241  LEU A CD1 1 
ATOM   1613  C  CD2 . LEU A 1 241 ? -5.303  -4.857  -20.795 1.00 27.66  ? 241  LEU A CD2 1 
ATOM   1614  N  N   . THR A 1 242 ? -5.220  -7.440  -17.041 1.00 51.99  ? 242  THR A N   1 
ATOM   1615  C  CA  . THR A 1 242 ? -4.844  -8.083  -15.803 1.00 37.97  ? 242  THR A CA  1 
ATOM   1616  C  C   . THR A 1 242 ? -5.190  -7.153  -14.649 1.00 45.71  ? 242  THR A C   1 
ATOM   1617  O  O   . THR A 1 242 ? -5.236  -5.927  -14.821 1.00 48.12  ? 242  THR A O   1 
ATOM   1618  C  CB  . THR A 1 242 ? -3.332  -8.378  -15.841 1.00 43.14  ? 242  THR A CB  1 
ATOM   1619  O  OG1 . THR A 1 242 ? -3.122  -9.766  -16.140 1.00 51.41  ? 242  THR A OG1 1 
ATOM   1620  C  CG2 . THR A 1 242 ? -2.652  -8.033  -14.541 1.00 28.97  ? 242  THR A CG2 1 
ATOM   1621  N  N   . PRO A 1 243 ? -5.460  -7.722  -13.466 1.00 34.68  ? 243  PRO A N   1 
ATOM   1622  C  CA  . PRO A 1 243 ? -5.712  -6.840  -12.324 1.00 33.23  ? 243  PRO A CA  1 
ATOM   1623  C  C   . PRO A 1 243 ? -4.559  -5.852  -12.163 1.00 33.99  ? 243  PRO A C   1 
ATOM   1624  O  O   . PRO A 1 243 ? -4.757  -4.726  -11.736 1.00 36.73  ? 243  PRO A O   1 
ATOM   1625  C  CB  . PRO A 1 243 ? -5.750  -7.806  -11.129 1.00 28.77  ? 243  PRO A CB  1 
ATOM   1626  C  CG  . PRO A 1 243 ? -6.082  -9.129  -11.713 1.00 39.39  ? 243  PRO A CG  1 
ATOM   1627  C  CD  . PRO A 1 243 ? -5.508  -9.147  -13.104 1.00 39.61  ? 243  PRO A CD  1 
ATOM   1628  N  N   . ASP A 1 244 ? -3.355  -6.288  -12.508 1.00 32.32  ? 244  ASP A N   1 
ATOM   1629  C  CA  . ASP A 1 244 ? -2.173  -5.461  -12.359 1.00 32.35  ? 244  ASP A CA  1 
ATOM   1630  C  C   . ASP A 1 244 ? -1.802  -4.750  -13.649 1.00 35.56  ? 244  ASP A C   1 
ATOM   1631  O  O   . ASP A 1 244 ? -0.625  -4.561  -13.948 1.00 44.40  ? 244  ASP A O   1 
ATOM   1632  C  CB  . ASP A 1 244 ? -1.003  -6.307  -11.848 1.00 34.65  ? 244  ASP A CB  1 
ATOM   1633  C  CG  . ASP A 1 244 ? -0.972  -6.397  -10.323 1.00 50.08  ? 244  ASP A CG  1 
ATOM   1634  O  OD1 . ASP A 1 244 ? -0.604  -5.383  -9.688  1.00 60.84  ? 244  ASP A OD1 1 
ATOM   1635  O  OD2 . ASP A 1 244 ? -1.324  -7.461  -9.758  1.00 45.87  ? 244  ASP A OD2 1 
ATOM   1636  N  N   . ASP A 1 245 ? -2.809  -4.324  -14.397 1.00 32.63  ? 245  ASP A N   1 
ATOM   1637  C  CA  . ASP A 1 245 ? -2.554  -3.732  -15.701 1.00 43.57  ? 245  ASP A CA  1 
ATOM   1638  C  C   . ASP A 1 245 ? -1.673  -2.489  -15.671 1.00 43.52  ? 245  ASP A C   1 
ATOM   1639  O  O   . ASP A 1 245 ? -0.788  -2.337  -16.510 1.00 44.29  ? 245  ASP A O   1 
ATOM   1640  C  CB  . ASP A 1 245 ? -3.848  -3.401  -16.433 1.00 35.64  ? 245  ASP A CB  1 
ATOM   1641  C  CG  . ASP A 1 245 ? -3.616  -3.208  -17.902 1.00 50.43  ? 245  ASP A CG  1 
ATOM   1642  O  OD1 . ASP A 1 245 ? -3.080  -4.145  -18.534 1.00 62.93  ? 245  ASP A OD1 1 
ATOM   1643  O  OD2 . ASP A 1 245 ? -3.942  -2.125  -18.416 1.00 55.46  ? 245  ASP A OD2 1 
ATOM   1644  N  N   . ARG A 1 246 ? -1.940  -1.587  -14.733 1.00 33.55  ? 246  ARG A N   1 
ATOM   1645  C  CA  . ARG A 1 246 ? -1.124  -0.390  -14.611 1.00 40.37  ? 246  ARG A CA  1 
ATOM   1646  C  C   . ARG A 1 246 ? 0.357   -0.771  -14.542 1.00 44.38  ? 246  ARG A C   1 
ATOM   1647  O  O   . ARG A 1 246 ? 1.164   -0.320  -15.351 1.00 48.60  ? 246  ARG A O   1 
ATOM   1648  C  CB  . ARG A 1 246 ? -1.514  0.408   -13.371 1.00 28.57  ? 246  ARG A CB  1 
ATOM   1649  C  CG  . ARG A 1 246 ? -2.972  0.763   -13.298 1.00 43.85  ? 246  ARG A CG  1 
ATOM   1650  C  CD  . ARG A 1 246 ? -3.331  1.271   -11.909 1.00 63.16  ? 246  ARG A CD  1 
ATOM   1651  N  NE  . ARG A 1 246 ? -3.345  2.731   -11.827 1.00 78.28  ? 246  ARG A NE  1 
ATOM   1652  C  CZ  . ARG A 1 246 ? -3.454  3.412   -10.690 1.00 91.69  ? 246  ARG A CZ  1 
ATOM   1653  N  NH1 . ARG A 1 246 ? -3.551  2.769   -9.531  1.00 95.49  ? 246  ARG A NH1 1 
ATOM   1654  N  NH2 . ARG A 1 246 ? -3.459  4.736   -10.707 1.00 96.81  ? 246  ARG A NH2 1 
ATOM   1655  N  N   . VAL A 1 247 ? 0.711   -1.609  -13.575 1.00 32.38  ? 247  VAL A N   1 
ATOM   1656  C  CA  . VAL A 1 247 ? 2.099   -2.013  -13.411 1.00 39.45  ? 247  VAL A CA  1 
ATOM   1657  C  C   . VAL A 1 247 ? 2.619   -2.663  -14.685 1.00 34.43  ? 247  VAL A C   1 
ATOM   1658  O  O   . VAL A 1 247 ? 3.744   -2.398  -15.134 1.00 32.72  ? 247  VAL A O   1 
ATOM   1659  C  CB  . VAL A 1 247 ? 2.280   -2.985  -12.232 1.00 35.48  ? 247  VAL A CB  1 
ATOM   1660  C  CG1 . VAL A 1 247 ? 3.643   -3.637  -12.300 1.00 20.16  ? 247  VAL A CG1 1 
ATOM   1661  C  CG2 . VAL A 1 247 ? 2.107   -2.250  -10.914 1.00 28.71  ? 247  VAL A CG2 1 
ATOM   1662  N  N   . PHE A 1 248 ? 1.790   -3.512  -15.273 1.00 42.10  ? 248  PHE A N   1 
ATOM   1663  C  CA  . PHE A 1 248 ? 2.210   -4.215  -16.470 1.00 39.67  ? 248  PHE A CA  1 
ATOM   1664  C  C   . PHE A 1 248 ? 2.534   -3.233  -17.573 1.00 37.63  ? 248  PHE A C   1 
ATOM   1665  O  O   . PHE A 1 248 ? 3.583   -3.336  -18.207 1.00 36.85  ? 248  PHE A O   1 
ATOM   1666  C  CB  . PHE A 1 248 ? 1.185   -5.268  -16.901 1.00 26.25  ? 248  PHE A CB  1 
ATOM   1667  C  CG  . PHE A 1 248 ? 1.501   -6.632  -16.373 1.00 31.18  ? 248  PHE A CG  1 
ATOM   1668  C  CD1 . PHE A 1 248 ? 2.692   -7.247  -16.712 1.00 35.39  ? 248  PHE A CD1 1 
ATOM   1669  C  CD2 . PHE A 1 248 ? 0.642   -7.278  -15.516 1.00 25.40  ? 248  PHE A CD2 1 
ATOM   1670  C  CE1 . PHE A 1 248 ? 3.008   -8.491  -16.225 1.00 41.05  ? 248  PHE A CE1 1 
ATOM   1671  C  CE2 . PHE A 1 248 ? 0.954   -8.524  -15.020 1.00 30.80  ? 248  PHE A CE2 1 
ATOM   1672  C  CZ  . PHE A 1 248 ? 2.143   -9.134  -15.380 1.00 19.58  ? 248  PHE A CZ  1 
ATOM   1673  N  N   . LYS A 1 249 ? 1.647   -2.261  -17.768 1.00 36.59  ? 249  LYS A N   1 
ATOM   1674  C  CA  . LYS A 1 249 ? 1.855   -1.208  -18.760 1.00 28.14  ? 249  LYS A CA  1 
ATOM   1675  C  C   . LYS A 1 249 ? 3.125   -0.403  -18.471 1.00 36.84  ? 249  LYS A C   1 
ATOM   1676  O  O   . LYS A 1 249 ? 3.818   0.024   -19.398 1.00 38.36  ? 249  LYS A O   1 
ATOM   1677  C  CB  . LYS A 1 249 ? 0.631   -0.293  -18.840 1.00 27.03  ? 249  LYS A CB  1 
ATOM   1678  C  CG  . LYS A 1 249 ? -0.281  -0.620  -20.011 1.00 31.30  ? 249  LYS A CG  1 
ATOM   1679  C  CD  . LYS A 1 249 ? -1.661  0.023   -19.915 1.00 31.29  ? 249  LYS A CD  1 
ATOM   1680  C  CE  . LYS A 1 249 ? -2.540  -0.491  -21.054 1.00 31.11  ? 249  LYS A CE  1 
ATOM   1681  N  NZ  . LYS A 1 249 ? -3.992  -0.373  -20.749 1.00 49.13  ? 249  LYS A NZ  1 
ATOM   1682  N  N   . GLN A 1 250 ? 3.434   -0.211  -17.186 1.00 38.29  ? 250  GLN A N   1 
ATOM   1683  C  CA  . GLN A 1 250 ? 4.655   0.491   -16.785 1.00 39.70  ? 250  GLN A CA  1 
ATOM   1684  C  C   . GLN A 1 250 ? 5.901   -0.330  -17.139 1.00 35.85  ? 250  GLN A C   1 
ATOM   1685  O  O   . GLN A 1 250 ? 6.890   0.198   -17.642 1.00 36.00  ? 250  GLN A O   1 
ATOM   1686  C  CB  . GLN A 1 250 ? 4.634   0.840   -15.286 1.00 32.03  ? 250  GLN A CB  1 
ATOM   1687  C  CG  . GLN A 1 250 ? 5.868   1.628   -14.842 1.00 40.57  ? 250  GLN A CG  1 
ATOM   1688  C  CD  . GLN A 1 250 ? 5.705   2.319   -13.493 1.00 47.96  ? 250  GLN A CD  1 
ATOM   1689  O  OE1 . GLN A 1 250 ? 4.647   2.864   -13.176 1.00 62.94  ? 250  GLN A OE1 1 
ATOM   1690  N  NE2 . GLN A 1 250 ? 6.770   2.320   -12.706 1.00 41.77  ? 250  GLN A NE2 1 
ATOM   1691  N  N   . LEU A 1 251 ? 5.835   -1.628  -16.886 1.00 29.08  ? 251  LEU A N   1 
ATOM   1692  C  CA  . LEU A 1 251 ? 6.917   -2.525  -17.256 1.00 30.20  ? 251  LEU A CA  1 
ATOM   1693  C  C   . LEU A 1 251 ? 7.163   -2.506  -18.750 1.00 29.51  ? 251  LEU A C   1 
ATOM   1694  O  O   . LEU A 1 251 ? 8.277   -2.248  -19.205 1.00 42.89  ? 251  LEU A O   1 
ATOM   1695  C  CB  . LEU A 1 251 ? 6.602   -3.944  -16.798 1.00 40.57  ? 251  LEU A CB  1 
ATOM   1696  C  CG  . LEU A 1 251 ? 6.522   -4.068  -15.279 1.00 43.76  ? 251  LEU A CG  1 
ATOM   1697  C  CD1 . LEU A 1 251 ? 6.064   -5.455  -14.859 1.00 42.98  ? 251  LEU A CD1 1 
ATOM   1698  C  CD2 . LEU A 1 251 ? 7.856   -3.684  -14.634 1.00 25.19  ? 251  LEU A CD2 1 
ATOM   1699  N  N   . ALA A 1 252 ? 6.117   -2.787  -19.514 1.00 36.15  ? 252  ALA A N   1 
ATOM   1700  C  CA  . ALA A 1 252 ? 6.210   -2.777  -20.971 1.00 42.82  ? 252  ALA A CA  1 
ATOM   1701  C  C   . ALA A 1 252 ? 6.757   -1.456  -21.503 1.00 44.18  ? 252  ALA A C   1 
ATOM   1702  O  O   . ALA A 1 252 ? 7.538   -1.441  -22.463 1.00 48.63  ? 252  ALA A O   1 
ATOM   1703  C  CB  . ALA A 1 252 ? 4.843   -3.077  -21.592 1.00 37.44  ? 252  ALA A CB  1 
ATOM   1704  N  N   . HIS A 1 253 ? 6.338   -0.350  -20.889 1.00 33.72  ? 253  HIS A N   1 
ATOM   1705  C  CA  . HIS A 1 253 ? 6.763   0.971   -21.345 1.00 35.14  ? 253  HIS A CA  1 
ATOM   1706  C  C   . HIS A 1 253 ? 8.203   1.228   -20.976 1.00 42.38  ? 253  HIS A C   1 
ATOM   1707  O  O   . HIS A 1 253 ? 8.936   1.858   -21.739 1.00 44.62  ? 253  HIS A O   1 
ATOM   1708  C  CB  . HIS A 1 253 ? 5.883   2.076   -20.776 1.00 33.10  ? 253  HIS A CB  1 
ATOM   1709  C  CG  . HIS A 1 253 ? 4.758   2.479   -21.684 1.00 46.40  ? 253  HIS A CG  1 
ATOM   1710  N  ND1 . HIS A 1 253 ? 3.434   2.449   -21.295 1.00 42.48  ? 253  HIS A ND1 1 
ATOM   1711  C  CD2 . HIS A 1 253 ? 4.761   2.920   -22.966 1.00 49.70  ? 253  HIS A CD2 1 
ATOM   1712  C  CE1 . HIS A 1 253 ? 2.670   2.849   -22.296 1.00 38.03  ? 253  HIS A CE1 1 
ATOM   1713  N  NE2 . HIS A 1 253 ? 3.452   3.144   -23.321 1.00 56.12  ? 253  HIS A NE2 1 
ATOM   1714  N  N   . THR A 1 254 ? 8.608   0.732   -19.809 1.00 28.97  ? 254  THR A N   1 
ATOM   1715  C  CA  . THR A 1 254 ? 10.003  0.839   -19.392 1.00 31.81  ? 254  THR A CA  1 
ATOM   1716  C  C   . THR A 1 254 ? 10.946  0.297   -20.464 1.00 36.78  ? 254  THR A C   1 
ATOM   1717  O  O   . THR A 1 254 ? 11.967  0.905   -20.770 1.00 41.32  ? 254  THR A O   1 
ATOM   1718  C  CB  . THR A 1 254 ? 10.280  0.061   -18.107 1.00 28.16  ? 254  THR A CB  1 
ATOM   1719  O  OG1 . THR A 1 254 ? 9.408   0.520   -17.069 1.00 33.60  ? 254  THR A OG1 1 
ATOM   1720  C  CG2 . THR A 1 254 ? 11.717  0.264   -17.689 1.00 24.32  ? 254  THR A CG2 1 
ATOM   1721  N  N   . TYR A 1 255 ? 10.607  -0.859  -21.027 1.00 35.58  ? 255  TYR A N   1 
ATOM   1722  C  CA  . TYR A 1 255 ? 11.451  -1.474  -22.045 1.00 36.96  ? 255  TYR A CA  1 
ATOM   1723  C  C   . TYR A 1 255 ? 11.340  -0.736  -23.383 1.00 39.92  ? 255  TYR A C   1 
ATOM   1724  O  O   . TYR A 1 255 ? 12.345  -0.379  -24.004 1.00 42.21  ? 255  TYR A O   1 
ATOM   1725  C  CB  . TYR A 1 255 ? 11.098  -2.958  -22.220 1.00 33.04  ? 255  TYR A CB  1 
ATOM   1726  C  CG  . TYR A 1 255 ? 12.169  -3.736  -22.948 1.00 39.58  ? 255  TYR A CG  1 
ATOM   1727  C  CD1 . TYR A 1 255 ? 12.297  -3.648  -24.338 1.00 49.18  ? 255  TYR A CD1 1 
ATOM   1728  C  CD2 . TYR A 1 255 ? 13.065  -4.548  -22.248 1.00 27.84  ? 255  TYR A CD2 1 
ATOM   1729  C  CE1 . TYR A 1 255 ? 13.287  -4.355  -25.018 1.00 47.49  ? 255  TYR A CE1 1 
ATOM   1730  C  CE2 . TYR A 1 255 ? 14.061  -5.259  -22.913 1.00 34.30  ? 255  TYR A CE2 1 
ATOM   1731  C  CZ  . TYR A 1 255 ? 14.167  -5.157  -24.301 1.00 41.73  ? 255  TYR A CZ  1 
ATOM   1732  O  OH  . TYR A 1 255 ? 15.147  -5.855  -24.972 1.00 34.35  ? 255  TYR A OH  1 
ATOM   1733  N  N   . SER A 1 256 ? 10.112  -0.504  -23.824 1.00 39.90  ? 256  SER A N   1 
ATOM   1734  C  CA  . SER A 1 256 ? 9.913   0.104   -25.125 1.00 38.25  ? 256  SER A CA  1 
ATOM   1735  C  C   . SER A 1 256 ? 10.431  1.542   -25.128 1.00 49.25  ? 256  SER A C   1 
ATOM   1736  O  O   . SER A 1 256 ? 11.151  1.948   -26.043 1.00 53.36  ? 256  SER A O   1 
ATOM   1737  C  CB  . SER A 1 256 ? 8.435   0.048   -25.516 1.00 39.78  ? 256  SER A CB  1 
ATOM   1738  O  OG  . SER A 1 256 ? 8.239   0.506   -26.844 1.00 55.72  ? 256  SER A OG  1 
ATOM   1739  N  N   . ASP A 1 257 ? 10.060  2.309   -24.105 1.00 51.02  ? 257  ASP A N   1 
ATOM   1740  C  CA  . ASP A 1 257 ? 10.466  3.713   -24.016 1.00 43.05  ? 257  ASP A CA  1 
ATOM   1741  C  C   . ASP A 1 257 ? 11.984  3.830   -24.182 1.00 45.36  ? 257  ASP A C   1 
ATOM   1742  O  O   . ASP A 1 257 ? 12.478  4.768   -24.805 1.00 49.97  ? 257  ASP A O   1 
ATOM   1743  C  CB  . ASP A 1 257 ? 10.016  4.348   -22.684 1.00 37.05  ? 257  ASP A CB  1 
ATOM   1744  C  CG  . ASP A 1 257 ? 8.516   4.661   -22.644 1.00 59.57  ? 257  ASP A CG  1 
ATOM   1745  O  OD1 . ASP A 1 257 ? 7.807   4.286   -23.595 1.00 67.86  ? 257  ASP A OD1 1 
ATOM   1746  O  OD2 . ASP A 1 257 ? 8.039   5.284   -21.661 1.00 66.14  ? 257  ASP A OD2 1 
ATOM   1747  N  N   . ASN A 1 258 ? 12.713  2.865   -23.627 1.00 44.01  ? 258  ASN A N   1 
ATOM   1748  C  CA  . ASN A 1 258 ? 14.172  2.857   -23.691 1.00 43.93  ? 258  ASN A CA  1 
ATOM   1749  C  C   . ASN A 1 258 ? 14.756  2.180   -24.933 1.00 48.11  ? 258  ASN A C   1 
ATOM   1750  O  O   . ASN A 1 258 ? 15.968  2.002   -25.035 1.00 50.27  ? 258  ASN A O   1 
ATOM   1751  C  CB  . ASN A 1 258 ? 14.750  2.218   -22.430 1.00 36.57  ? 258  ASN A CB  1 
ATOM   1752  C  CG  . ASN A 1 258 ? 14.747  3.171   -21.252 1.00 49.17  ? 258  ASN A CG  1 
ATOM   1753  O  OD1 . ASN A 1 258 ? 15.607  4.052   -21.148 1.00 50.69  ? 258  ASN A OD1 1 
ATOM   1754  N  ND2 . ASN A 1 258 ? 13.772  3.011   -20.360 1.00 44.73  ? 258  ASN A ND2 1 
ATOM   1755  N  N   . HIS A 1 259 ? 13.892  1.805   -25.872 1.00 56.21  ? 259  HIS A N   1 
ATOM   1756  C  CA  . HIS A 1 259 ? 14.316  1.098   -27.073 1.00 52.98  ? 259  HIS A CA  1 
ATOM   1757  C  C   . HIS A 1 259 ? 14.018  1.980   -28.271 1.00 51.25  ? 259  HIS A C   1 
ATOM   1758  O  O   . HIS A 1 259 ? 12.862  2.159   -28.641 1.00 60.06  ? 259  HIS A O   1 
ATOM   1759  C  CB  . HIS A 1 259 ? 13.585  -0.248  -27.192 1.00 52.03  ? 259  HIS A CB  1 
ATOM   1760  C  CG  . HIS A 1 259 ? 14.145  -1.155  -28.251 1.00 55.92  ? 259  HIS A CG  1 
ATOM   1761  N  ND1 . HIS A 1 259 ? 14.192  -0.805  -29.585 1.00 53.46  ? 259  HIS A ND1 1 
ATOM   1762  C  CD2 . HIS A 1 259 ? 14.668  -2.403  -28.173 1.00 52.82  ? 259  HIS A CD2 1 
ATOM   1763  C  CE1 . HIS A 1 259 ? 14.722  -1.796  -30.280 1.00 46.18  ? 259  HIS A CE1 1 
ATOM   1764  N  NE2 . HIS A 1 259 ? 15.024  -2.777  -29.448 1.00 46.15  ? 259  HIS A NE2 1 
ATOM   1765  N  N   . PRO A 1 260 ? 15.064  2.538   -28.883 1.00 59.21  ? 260  PRO A N   1 
ATOM   1766  C  CA  . PRO A 1 260 ? 14.956  3.572   -29.925 1.00 58.57  ? 260  PRO A CA  1 
ATOM   1767  C  C   . PRO A 1 260 ? 14.029  3.205   -31.083 1.00 52.24  ? 260  PRO A C   1 
ATOM   1768  O  O   . PRO A 1 260 ? 13.551  4.099   -31.771 1.00 56.77  ? 260  PRO A O   1 
ATOM   1769  C  CB  . PRO A 1 260 ? 16.389  3.689   -30.449 1.00 53.34  ? 260  PRO A CB  1 
ATOM   1770  C  CG  . PRO A 1 260 ? 17.244  3.223   -29.326 1.00 59.28  ? 260  PRO A CG  1 
ATOM   1771  C  CD  . PRO A 1 260 ? 16.460  2.144   -28.631 1.00 51.85  ? 260  PRO A CD  1 
ATOM   1772  N  N   . ILE A 1 261 ? 13.798  1.916   -31.305 1.00 54.69  ? 261  ILE A N   1 
ATOM   1773  C  CA  . ILE A 1 261 ? 13.025  1.460   -32.465 1.00 61.17  ? 261  ILE A CA  1 
ATOM   1774  C  C   . ILE A 1 261 ? 11.642  0.935   -32.080 1.00 49.52  ? 261  ILE A C   1 
ATOM   1775  O  O   . ILE A 1 261 ? 10.637  1.223   -32.750 1.00 47.56  ? 261  ILE A O   1 
ATOM   1776  C  CB  . ILE A 1 261 ? 13.794  0.369   -33.256 1.00 62.11  ? 261  ILE A CB  1 
ATOM   1777  C  CG1 . ILE A 1 261 ? 14.993  0.988   -33.987 1.00 50.65  ? 261  ILE A CG1 1 
ATOM   1778  C  CG2 . ILE A 1 261 ? 12.863  -0.363  -34.235 1.00 54.93  ? 261  ILE A CG2 1 
ATOM   1779  C  CD1 . ILE A 1 261 ? 15.907  -0.036  -34.619 1.00 55.57  ? 261  ILE A CD1 1 
ATOM   1780  N  N   . MET A 1 262 ? 11.613  0.160   -30.999 1.00 44.72  ? 262  MET A N   1 
ATOM   1781  C  CA  . MET A 1 262 ? 10.374  -0.330  -30.395 1.00 46.14  ? 262  MET A CA  1 
ATOM   1782  C  C   . MET A 1 262 ? 9.462   0.823   -29.967 1.00 46.00  ? 262  MET A C   1 
ATOM   1783  O  O   . MET A 1 262 ? 8.257   0.771   -30.171 1.00 55.86  ? 262  MET A O   1 
ATOM   1784  C  CB  . MET A 1 262 ? 10.704  -1.225  -29.192 1.00 39.27  ? 262  MET A CB  1 
ATOM   1785  C  CG  . MET A 1 262 ? 9.512   -1.947  -28.579 1.00 29.59  ? 262  MET A CG  1 
ATOM   1786  S  SD  . MET A 1 262 ? 10.082  -3.081  -27.293 1.00 54.48  ? 262  MET A SD  1 
ATOM   1787  C  CE  . MET A 1 262 ? 11.128  -4.155  -28.266 1.00 30.69  ? 262  MET A CE  1 
ATOM   1788  N  N   . ARG A 1 263 ? 10.053  1.861   -29.382 1.00 50.42  ? 263  ARG A N   1 
ATOM   1789  C  CA  . ARG A 1 263 ? 9.345   3.072   -28.975 1.00 48.10  ? 263  ARG A CA  1 
ATOM   1790  C  C   . ARG A 1 263 ? 8.447   3.650   -30.070 1.00 48.16  ? 263  ARG A C   1 
ATOM   1791  O  O   . ARG A 1 263 ? 7.519   4.396   -29.775 1.00 63.91  ? 263  ARG A O   1 
ATOM   1792  C  CB  . ARG A 1 263 ? 10.370  4.124   -28.541 1.00 52.24  ? 263  ARG A CB  1 
ATOM   1793  C  CG  . ARG A 1 263 ? 9.801   5.403   -27.977 1.00 64.37  ? 263  ARG A CG  1 
ATOM   1794  C  CD  . ARG A 1 263 ? 10.922  6.257   -27.397 1.00 80.00  ? 263  ARG A CD  1 
ATOM   1795  N  NE  . ARG A 1 263 ? 11.947  6.588   -28.391 1.00 86.44  ? 263  ARG A NE  1 
ATOM   1796  C  CZ  . ARG A 1 263 ? 13.261  6.473   -28.196 1.00 75.15  ? 263  ARG A CZ  1 
ATOM   1797  N  NH1 . ARG A 1 263 ? 13.733  6.026   -27.042 1.00 63.40  ? 263  ARG A NH1 1 
ATOM   1798  N  NH2 . ARG A 1 263 ? 14.111  6.807   -29.159 1.00 71.80  ? 263  ARG A NH2 1 
ATOM   1799  N  N   . LYS A 1 264 ? 8.721   3.308   -31.326 1.00 61.39  ? 264  LYS A N   1 
ATOM   1800  C  CA  . LYS A 1 264 ? 8.024   3.916   -32.471 1.00 71.93  ? 264  LYS A CA  1 
ATOM   1801  C  C   . LYS A 1 264 ? 6.633   3.338   -32.743 1.00 65.57  ? 264  LYS A C   1 
ATOM   1802  O  O   . LYS A 1 264 ? 5.653   4.077   -32.890 1.00 65.83  ? 264  LYS A O   1 
ATOM   1803  C  CB  . LYS A 1 264 ? 8.891   3.828   -33.728 1.00 68.12  ? 264  LYS A CB  1 
ATOM   1804  C  CG  . LYS A 1 264 ? 10.244  4.501   -33.561 1.00 67.87  ? 264  LYS A CG  1 
ATOM   1805  C  CD  . LYS A 1 264 ? 11.012  4.550   -34.865 1.00 75.48  ? 264  LYS A CD  1 
ATOM   1806  C  CE  . LYS A 1 264 ? 12.232  5.443   -34.731 1.00 81.38  ? 264  LYS A CE  1 
ATOM   1807  N  NZ  . LYS A 1 264 ? 11.853  6.835   -34.345 1.00 89.11  ? 264  LYS A NZ  1 
ATOM   1808  N  N   . GLY A 1 265 ? 6.553   2.018   -32.829 1.00 58.63  ? 265  GLY A N   1 
ATOM   1809  C  CA  . GLY A 1 265 ? 5.267   1.352   -32.831 1.00 50.71  ? 265  GLY A CA  1 
ATOM   1810  C  C   . GLY A 1 265 ? 4.796   0.903   -34.188 1.00 55.18  ? 265  GLY A C   1 
ATOM   1811  O  O   . GLY A 1 265 ? 3.697   0.355   -34.305 1.00 56.99  ? 265  GLY A O   1 
ATOM   1812  N  N   . ASN A 1 266 ? 5.627   1.122   -35.206 1.00 56.27  ? 266  ASN A N   1 
ATOM   1813  C  CA  . ASN A 1 266 ? 5.248   0.819   -36.586 1.00 56.83  ? 266  ASN A CA  1 
ATOM   1814  C  C   . ASN A 1 266 ? 6.213   -0.128  -37.290 1.00 59.40  ? 266  ASN A C   1 
ATOM   1815  O  O   . ASN A 1 266 ? 6.450   -0.010  -38.497 1.00 65.62  ? 266  ASN A O   1 
ATOM   1816  C  CB  . ASN A 1 266 ? 5.109   2.110   -37.388 1.00 62.67  ? 266  ASN A CB  1 
ATOM   1817  C  CG  . ASN A 1 266 ? 6.286   3.042   -37.198 1.00 75.27  ? 266  ASN A CG  1 
ATOM   1818  O  OD1 . ASN A 1 266 ? 7.242   2.723   -36.484 1.00 76.20  ? 266  ASN A OD1 1 
ATOM   1819  N  ND2 . ASN A 1 266 ? 6.221   4.208   -37.834 1.00 75.69  ? 266  ASN A ND2 1 
ATOM   1820  N  N   . ASN A 1 267 ? 6.752   -1.076  -36.533 1.00 47.60  ? 267  ASN A N   1 
ATOM   1821  C  CA  . ASN A 1 267 ? 7.781   -1.978  -37.034 1.00 48.38  ? 267  ASN A CA  1 
ATOM   1822  C  C   . ASN A 1 267 ? 7.181   -3.240  -37.644 1.00 48.97  ? 267  ASN A C   1 
ATOM   1823  O  O   . ASN A 1 267 ? 6.051   -3.606  -37.318 1.00 49.16  ? 267  ASN A O   1 
ATOM   1824  C  CB  . ASN A 1 267 ? 8.741   -2.342  -35.899 1.00 55.00  ? 267  ASN A CB  1 
ATOM   1825  C  CG  . ASN A 1 267 ? 9.125   -1.132  -35.047 1.00 59.20  ? 267  ASN A CG  1 
ATOM   1826  O  OD1 . ASN A 1 267 ? 9.593   -0.114  -35.560 1.00 58.66  ? 267  ASN A OD1 1 
ATOM   1827  N  ND2 . ASN A 1 267 ? 8.924   -1.242  -33.741 1.00 52.46  ? 267  ASN A ND2 1 
ATOM   1828  N  N   . CYS A 1 268 ? 7.939   -3.881  -38.535 1.00 56.47  ? 268  CYS A N   1 
ATOM   1829  C  CA  . CYS A 1 268 ? 7.546   -5.139  -39.193 1.00 59.72  ? 268  CYS A CA  1 
ATOM   1830  C  C   . CYS A 1 268 ? 6.103   -5.167  -39.693 1.00 65.14  ? 268  CYS A C   1 
ATOM   1831  O  O   . CYS A 1 268 ? 5.428   -6.199  -39.588 1.00 62.87  ? 268  CYS A O   1 
ATOM   1832  C  CB  . CYS A 1 268 ? 7.788   -6.356  -38.279 1.00 47.37  ? 268  CYS A CB  1 
ATOM   1833  S  SG  . CYS A 1 268 ? 8.697   -6.034  -36.749 1.00 67.16  ? 268  CYS A SG  1 
ATOM   1834  N  N   . ASN A 1 269 ? 5.635   -4.043  -40.231 1.00 67.77  ? 269  ASN A N   1 
ATOM   1835  C  CA  . ASN A 1 269 ? 4.247   -3.918  -40.691 1.00 75.07  ? 269  ASN A CA  1 
ATOM   1836  C  C   . ASN A 1 269 ? 3.225   -3.889  -39.543 1.00 72.90  ? 269  ASN A C   1 
ATOM   1837  O  O   . ASN A 1 269 ? 2.009   -3.840  -39.780 1.00 67.96  ? 269  ASN A O   1 
ATOM   1838  C  CB  . ASN A 1 269 ? 3.884   -5.020  -41.704 1.00 77.00  ? 269  ASN A CB  1 
ATOM   1839  C  CG  . ASN A 1 269 ? 4.573   -4.835  -43.057 1.00 81.57  ? 269  ASN A CG  1 
ATOM   1840  O  OD1 . ASN A 1 269 ? 4.731   -5.792  -43.817 1.00 80.48  ? 269  ASN A OD1 1 
ATOM   1841  N  ND2 . ASN A 1 269 ? 4.978   -3.603  -43.362 1.00 83.54  ? 269  ASN A ND2 1 
ATOM   1842  N  N   . ASP A 1 270 ? 3.719   -3.909  -38.305 1.00 67.85  ? 270  ASP A N   1 
ATOM   1843  C  CA  . ASP A 1 270 ? 2.851   -3.893  -37.126 1.00 63.55  ? 270  ASP A CA  1 
ATOM   1844  C  C   . ASP A 1 270 ? 2.587   -2.471  -36.667 1.00 71.37  ? 270  ASP A C   1 
ATOM   1845  O  O   . ASP A 1 270 ? 3.410   -1.581  -36.896 1.00 72.62  ? 270  ASP A O   1 
ATOM   1846  C  CB  . ASP A 1 270 ? 3.483   -4.672  -35.977 1.00 53.29  ? 270  ASP A CB  1 
ATOM   1847  C  CG  . ASP A 1 270 ? 3.718   -6.130  -36.319 1.00 59.02  ? 270  ASP A CG  1 
ATOM   1848  O  OD1 . ASP A 1 270 ? 2.904   -6.708  -37.069 1.00 66.22  ? 270  ASP A OD1 1 
ATOM   1849  O  OD2 . ASP A 1 270 ? 4.716   -6.698  -35.830 1.00 58.25  ? 270  ASP A OD2 1 
ATOM   1850  N  N   . SER A 1 271 ? 1.438   -2.264  -36.026 1.00 64.41  ? 271  SER A N   1 
ATOM   1851  C  CA  . SER A 1 271 ? 1.122   -0.973  -35.426 1.00 59.20  ? 271  SER A CA  1 
ATOM   1852  C  C   . SER A 1 271 ? 0.798   -1.130  -33.945 1.00 66.09  ? 271  SER A C   1 
ATOM   1853  O  O   . SER A 1 271 ? -0.301  -1.559  -33.579 1.00 74.23  ? 271  SER A O   1 
ATOM   1854  C  CB  . SER A 1 271 ? -0.039  -0.297  -36.149 1.00 63.66  ? 271  SER A CB  1 
ATOM   1855  O  OG  . SER A 1 271 ? -0.400  0.920   -35.507 1.00 67.13  ? 271  SER A OG  1 
ATOM   1856  N  N   . PHE A 1 272 ? 1.764   -0.782  -33.097 1.00 60.59  ? 272  PHE A N   1 
ATOM   1857  C  CA  . PHE A 1 272 ? 1.630   -0.946  -31.653 1.00 46.13  ? 272  PHE A CA  1 
ATOM   1858  C  C   . PHE A 1 272 ? 1.866   0.383   -30.922 1.00 45.44  ? 272  PHE A C   1 
ATOM   1859  O  O   . PHE A 1 272 ? 3.006   0.805   -30.750 1.00 44.98  ? 272  PHE A O   1 
ATOM   1860  C  CB  . PHE A 1 272 ? 2.626   -1.993  -31.156 1.00 40.06  ? 272  PHE A CB  1 
ATOM   1861  C  CG  . PHE A 1 272 ? 2.295   -3.407  -31.566 1.00 51.11  ? 272  PHE A CG  1 
ATOM   1862  C  CD1 . PHE A 1 272 ? 3.223   -4.176  -32.266 1.00 54.02  ? 272  PHE A CD1 1 
ATOM   1863  C  CD2 . PHE A 1 272 ? 1.070   -3.981  -31.232 1.00 46.26  ? 272  PHE A CD2 1 
ATOM   1864  C  CE1 . PHE A 1 272 ? 2.941   -5.501  -32.631 1.00 41.58  ? 272  PHE A CE1 1 
ATOM   1865  C  CE2 . PHE A 1 272 ? 0.775   -5.300  -31.596 1.00 43.85  ? 272  PHE A CE2 1 
ATOM   1866  C  CZ  . PHE A 1 272 ? 1.718   -6.061  -32.300 1.00 40.23  ? 272  PHE A CZ  1 
ATOM   1867  N  N   . SER A 1 273 ? 0.785   1.037   -30.499 1.00 58.31  ? 273  SER A N   1 
ATOM   1868  C  CA  . SER A 1 273 ? 0.868   2.343   -29.835 1.00 61.25  ? 273  SER A CA  1 
ATOM   1869  C  C   . SER A 1 273 ? 1.861   2.325   -28.674 1.00 65.17  ? 273  SER A C   1 
ATOM   1870  O  O   . SER A 1 273 ? 1.684   1.584   -27.696 1.00 64.80  ? 273  SER A O   1 
ATOM   1871  C  CB  . SER A 1 273 ? -0.516  2.790   -29.337 1.00 60.03  ? 273  SER A CB  1 
ATOM   1872  O  OG  . SER A 1 273 ? -0.433  3.972   -28.552 1.00 61.27  ? 273  SER A OG  1 
ATOM   1873  N  N   . GLY A 1 274 ? 2.903   3.146   -28.790 1.00 56.57  ? 274  GLY A N   1 
ATOM   1874  C  CA  . GLY A 1 274 ? 3.906   3.256   -27.745 1.00 53.27  ? 274  GLY A CA  1 
ATOM   1875  C  C   . GLY A 1 274 ? 4.842   2.062   -27.739 1.00 53.00  ? 274  GLY A C   1 
ATOM   1876  O  O   . GLY A 1 274 ? 5.721   1.932   -26.876 1.00 43.52  ? 274  GLY A O   1 
ATOM   1877  N  N   . GLY A 1 275 ? 4.641   1.182   -28.713 1.00 44.77  ? 275  GLY A N   1 
ATOM   1878  C  CA  . GLY A 1 275 ? 5.497   0.026   -28.881 1.00 40.49  ? 275  GLY A CA  1 
ATOM   1879  C  C   . GLY A 1 275 ? 5.193   -1.108  -27.929 1.00 42.82  ? 275  GLY A C   1 
ATOM   1880  O  O   . GLY A 1 275 ? 6.000   -2.018  -27.765 1.00 45.66  ? 275  GLY A O   1 
ATOM   1881  N  N   . ILE A 1 276 ? 4.027   -1.054  -27.299 1.00 44.60  ? 276  ILE A N   1 
ATOM   1882  C  CA  . ILE A 1 276 ? 3.594   -2.127  -26.419 1.00 46.27  ? 276  ILE A CA  1 
ATOM   1883  C  C   . ILE A 1 276 ? 2.204   -2.598  -26.819 1.00 45.98  ? 276  ILE A C   1 
ATOM   1884  O  O   . ILE A 1 276 ? 1.477   -1.894  -27.531 1.00 49.95  ? 276  ILE A O   1 
ATOM   1885  C  CB  . ILE A 1 276 ? 3.544   -1.670  -24.961 1.00 42.17  ? 276  ILE A CB  1 
ATOM   1886  C  CG1 . ILE A 1 276 ? 2.438   -0.635  -24.786 1.00 42.17  ? 276  ILE A CG1 1 
ATOM   1887  C  CG2 . ILE A 1 276 ? 4.881   -1.085  -24.543 1.00 47.99  ? 276  ILE A CG2 1 
ATOM   1888  C  CD1 . ILE A 1 276 ? 2.229   -0.228  -23.361 1.00 39.83  ? 276  ILE A CD1 1 
ATOM   1889  N  N   . THR A 1 277 ? 1.837   -3.790  -26.352 1.00 41.70  ? 277  THR A N   1 
ATOM   1890  C  CA  . THR A 1 277 ? 0.518   -4.346  -26.628 1.00 42.91  ? 277  THR A CA  1 
ATOM   1891  C  C   . THR A 1 277 ? 0.125   -5.416  -25.635 1.00 48.23  ? 277  THR A C   1 
ATOM   1892  O  O   . THR A 1 277 ? 0.970   -6.058  -25.021 1.00 59.57  ? 277  THR A O   1 
ATOM   1893  C  CB  . THR A 1 277 ? 0.439   -4.993  -28.014 1.00 42.21  ? 277  THR A CB  1 
ATOM   1894  O  OG1 . THR A 1 277 ? -0.920  -5.376  -28.270 1.00 48.84  ? 277  THR A OG1 1 
ATOM   1895  C  CG2 . THR A 1 277 ? 1.339   -6.233  -28.079 1.00 32.37  ? 277  THR A CG2 1 
ATOM   1896  N  N   . ASN A 1 278 ? -1.176  -5.602  -25.486 1.00 47.91  ? 278  ASN A N   1 
ATOM   1897  C  CA  . ASN A 1 278 ? -1.714  -6.673  -24.676 1.00 32.43  ? 278  ASN A CA  1 
ATOM   1898  C  C   . ASN A 1 278 ? -1.647  -7.932  -25.525 1.00 49.88  ? 278  ASN A C   1 
ATOM   1899  O  O   . ASN A 1 278 ? -2.003  -7.898  -26.710 1.00 63.01  ? 278  ASN A O   1 
ATOM   1900  C  CB  . ASN A 1 278 ? -3.156  -6.332  -24.306 1.00 23.93  ? 278  ASN A CB  1 
ATOM   1901  C  CG  . ASN A 1 278 ? -3.876  -7.466  -23.642 1.00 39.41  ? 278  ASN A CG  1 
ATOM   1902  O  OD1 . ASN A 1 278 ? -4.949  -7.858  -24.096 1.00 49.00  ? 278  ASN A OD1 1 
ATOM   1903  N  ND2 . ASN A 1 278 ? -3.314  -7.995  -22.551 1.00 28.18  ? 278  ASN A ND2 1 
ATOM   1904  N  N   . GLY A 1 279 ? -1.169  -9.034  -24.946 1.00 35.07  ? 279  GLY A N   1 
ATOM   1905  C  CA  . GLY A 1 279 ? -1.080  -10.283 -25.691 1.00 33.70  ? 279  GLY A CA  1 
ATOM   1906  C  C   . GLY A 1 279 ? -2.358  -10.584 -26.468 1.00 44.20  ? 279  GLY A C   1 
ATOM   1907  O  O   . GLY A 1 279 ? -2.369  -10.628 -27.713 1.00 34.92  ? 279  GLY A O   1 
ATOM   1908  N  N   . ALA A 1 280 ? -3.442  -10.775 -25.720 1.00 36.67  ? 280  ALA A N   1 
ATOM   1909  C  CA  . ALA A 1 280 ? -4.743  -11.090 -26.297 1.00 35.82  ? 280  ALA A CA  1 
ATOM   1910  C  C   . ALA A 1 280 ? -5.128  -10.133 -27.418 1.00 43.94  ? 280  ALA A C   1 
ATOM   1911  O  O   . ALA A 1 280 ? -5.558  -10.571 -28.486 1.00 51.36  ? 280  ALA A O   1 
ATOM   1912  C  CB  . ALA A 1 280 ? -5.812  -11.083 -25.209 1.00 38.82  ? 280  ALA A CB  1 
ATOM   1913  N  N   . HIS A 1 281 ? -4.987  -8.829  -27.165 1.00 45.89  ? 281  HIS A N   1 
ATOM   1914  C  CA  . HIS A 1 281 ? -5.361  -7.813  -28.146 1.00 36.25  ? 281  HIS A CA  1 
ATOM   1915  C  C   . HIS A 1 281 ? -4.570  -7.966  -29.441 1.00 37.96  ? 281  HIS A C   1 
ATOM   1916  O  O   . HIS A 1 281 ? -5.106  -7.750  -30.529 1.00 46.00  ? 281  HIS A O   1 
ATOM   1917  C  CB  . HIS A 1 281 ? -5.197  -6.399  -27.595 1.00 43.23  ? 281  HIS A CB  1 
ATOM   1918  C  CG  . HIS A 1 281 ? -5.821  -5.354  -28.464 1.00 51.06  ? 281  HIS A CG  1 
ATOM   1919  N  ND1 . HIS A 1 281 ? -5.121  -4.682  -29.443 1.00 52.51  ? 281  HIS A ND1 1 
ATOM   1920  C  CD2 . HIS A 1 281 ? -7.092  -4.891  -28.526 1.00 57.18  ? 281  HIS A CD2 1 
ATOM   1921  C  CE1 . HIS A 1 281 ? -5.931  -3.840  -30.061 1.00 45.99  ? 281  HIS A CE1 1 
ATOM   1922  N  NE2 . HIS A 1 281 ? -7.134  -3.950  -29.526 1.00 54.71  ? 281  HIS A NE2 1 
ATOM   1923  N  N   . TRP A 1 282 ? -3.297  -8.326  -29.329 1.00 35.98  ? 282  TRP A N   1 
ATOM   1924  C  CA  . TRP A 1 282 ? -2.551  -8.708  -30.512 1.00 42.17  ? 282  TRP A CA  1 
ATOM   1925  C  C   . TRP A 1 282 ? -3.284  -9.881  -31.167 1.00 46.56  ? 282  TRP A C   1 
ATOM   1926  O  O   . TRP A 1 282 ? -3.977  -9.732  -32.188 1.00 45.23  ? 282  TRP A O   1 
ATOM   1927  C  CB  . TRP A 1 282 ? -1.130  -9.112  -30.137 1.00 35.96  ? 282  TRP A CB  1 
ATOM   1928  C  CG  . TRP A 1 282 ? -0.273  -9.365  -31.323 1.00 51.29  ? 282  TRP A CG  1 
ATOM   1929  C  CD1 . TRP A 1 282 ? -0.646  -9.301  -32.638 1.00 40.65  ? 282  TRP A CD1 1 
ATOM   1930  C  CD2 . TRP A 1 282 ? 1.114   -9.722  -31.312 1.00 53.30  ? 282  TRP A CD2 1 
ATOM   1931  N  NE1 . TRP A 1 282 ? 0.426   -9.594  -33.446 1.00 43.03  ? 282  TRP A NE1 1 
ATOM   1932  C  CE2 . TRP A 1 282 ? 1.522   -9.855  -32.661 1.00 47.70  ? 282  TRP A CE2 1 
ATOM   1933  C  CE3 . TRP A 1 282 ? 2.052   -9.940  -30.295 1.00 45.76  ? 282  TRP A CE3 1 
ATOM   1934  C  CZ2 . TRP A 1 282 ? 2.828   -10.210 -33.018 1.00 29.19  ? 282  TRP A CZ2 1 
ATOM   1935  C  CZ3 . TRP A 1 282 ? 3.346   -10.285 -30.650 1.00 40.44  ? 282  TRP A CZ3 1 
ATOM   1936  C  CH2 . TRP A 1 282 ? 3.720   -10.417 -32.005 1.00 40.24  ? 282  TRP A CH2 1 
ATOM   1937  N  N   . TYR A 1 283 ? -3.122  -11.049 -30.558 1.00 40.77  ? 283  TYR A N   1 
ATOM   1938  C  CA  . TYR A 1 283 ? -3.932  -12.219 -30.876 1.00 44.98  ? 283  TYR A CA  1 
ATOM   1939  C  C   . TYR A 1 283 ? -3.837  -13.180 -29.700 1.00 46.05  ? 283  TYR A C   1 
ATOM   1940  O  O   . TYR A 1 283 ? -2.788  -13.276 -29.049 1.00 35.97  ? 283  TYR A O   1 
ATOM   1941  C  CB  . TYR A 1 283 ? -3.464  -12.898 -32.165 1.00 43.36  ? 283  TYR A CB  1 
ATOM   1942  C  CG  . TYR A 1 283 ? -1.991  -13.296 -32.151 1.00 52.10  ? 283  TYR A CG  1 
ATOM   1943  C  CD1 . TYR A 1 283 ? -1.578  -14.526 -31.644 1.00 51.50  ? 283  TYR A CD1 1 
ATOM   1944  C  CD2 . TYR A 1 283 ? -1.017  -12.442 -32.644 1.00 49.56  ? 283  TYR A CD2 1 
ATOM   1945  C  CE1 . TYR A 1 283 ? -0.238  -14.889 -31.633 1.00 45.65  ? 283  TYR A CE1 1 
ATOM   1946  C  CE2 . TYR A 1 283 ? 0.319   -12.799 -32.630 1.00 48.89  ? 283  TYR A CE2 1 
ATOM   1947  C  CZ  . TYR A 1 283 ? 0.705   -14.020 -32.130 1.00 49.04  ? 283  TYR A CZ  1 
ATOM   1948  O  OH  . TYR A 1 283 ? 2.042   -14.367 -32.132 1.00 50.91  ? 283  TYR A OH  1 
ATOM   1949  N  N   . GLU A 1 284 ? -4.936  -13.878 -29.419 1.00 49.74  ? 284  GLU A N   1 
ATOM   1950  C  CA  . GLU A 1 284 ? -4.982  -14.770 -28.267 1.00 46.77  ? 284  GLU A CA  1 
ATOM   1951  C  C   . GLU A 1 284 ? -4.210  -16.054 -28.502 1.00 45.43  ? 284  GLU A C   1 
ATOM   1952  O  O   . GLU A 1 284 ? -4.086  -16.547 -29.625 1.00 45.71  ? 284  GLU A O   1 
ATOM   1953  C  CB  . GLU A 1 284 ? -6.421  -15.072 -27.826 1.00 38.93  ? 284  GLU A CB  1 
ATOM   1954  C  CG  . GLU A 1 284 ? -7.108  -13.882 -27.156 1.00 43.06  ? 284  GLU A CG  1 
ATOM   1955  C  CD  . GLU A 1 284 ? -8.395  -14.260 -26.437 1.00 51.73  ? 284  GLU A CD  1 
ATOM   1956  O  OE1 . GLU A 1 284 ? -9.147  -13.341 -26.022 1.00 48.29  ? 284  GLU A OE1 1 
ATOM   1957  O  OE2 . GLU A 1 284 ? -8.656  -15.475 -26.286 1.00 59.13  ? 284  GLU A OE2 1 
ATOM   1958  N  N   . LEU A 1 285 ? -3.671  -16.581 -27.419 1.00 35.12  ? 285  LEU A N   1 
ATOM   1959  C  CA  . LEU A 1 285 ? -2.995  -17.853 -27.467 1.00 40.76  ? 285  LEU A CA  1 
ATOM   1960  C  C   . LEU A 1 285 ? -3.140  -18.437 -26.078 1.00 40.71  ? 285  LEU A C   1 
ATOM   1961  O  O   . LEU A 1 285 ? -3.311  -17.701 -25.099 1.00 39.14  ? 285  LEU A O   1 
ATOM   1962  C  CB  . LEU A 1 285 ? -1.528  -17.656 -27.859 1.00 40.63  ? 285  LEU A CB  1 
ATOM   1963  C  CG  . LEU A 1 285 ? -0.581  -16.979 -26.860 1.00 31.12  ? 285  LEU A CG  1 
ATOM   1964  C  CD1 . LEU A 1 285 ? 0.010   -18.031 -25.953 1.00 19.52  ? 285  LEU A CD1 1 
ATOM   1965  C  CD2 . LEU A 1 285 ? 0.528   -16.209 -27.570 1.00 25.16  ? 285  LEU A CD2 1 
ATOM   1966  N  N   . SER A 1 286 ? -3.100  -19.757 -25.981 1.00 46.37  ? 286  SER A N   1 
ATOM   1967  C  CA  . SER A 1 286 ? -3.250  -20.387 -24.680 1.00 43.32  ? 286  SER A CA  1 
ATOM   1968  C  C   . SER A 1 286 ? -2.069  -21.278 -24.336 1.00 42.18  ? 286  SER A C   1 
ATOM   1969  O  O   . SER A 1 286 ? -1.432  -21.840 -25.230 1.00 49.93  ? 286  SER A O   1 
ATOM   1970  C  CB  . SER A 1 286 ? -4.560  -21.160 -24.609 1.00 39.72  ? 286  SER A CB  1 
ATOM   1971  O  OG  . SER A 1 286 ? -5.647  -20.281 -24.852 1.00 51.73  ? 286  SER A OG  1 
ATOM   1972  N  N   . GLY A 1 287 ? -1.771  -21.370 -23.037 1.00 32.93  ? 287  GLY A N   1 
ATOM   1973  C  CA  . GLY A 1 287 ? -0.742  -22.259 -22.540 1.00 21.36  ? 287  GLY A CA  1 
ATOM   1974  C  C   . GLY A 1 287 ? 0.632   -21.638 -22.564 1.00 31.30  ? 287  GLY A C   1 
ATOM   1975  O  O   . GLY A 1 287 ? 1.649   -22.335 -22.535 1.00 39.64  ? 287  GLY A O   1 
ATOM   1976  N  N   . GLY A 1 288 ? 0.668   -20.314 -22.612 1.00 30.58  ? 288  GLY A N   1 
ATOM   1977  C  CA  . GLY A 1 288 ? 1.933   -19.606 -22.633 1.00 34.06  ? 288  GLY A CA  1 
ATOM   1978  C  C   . GLY A 1 288 ? 2.612   -19.512 -21.274 1.00 33.73  ? 288  GLY A C   1 
ATOM   1979  O  O   . GLY A 1 288 ? 1.983   -19.613 -20.225 1.00 30.61  ? 288  GLY A O   1 
ATOM   1980  N  N   . MET A 1 289 ? 3.917   -19.291 -21.292 1.00 42.85  ? 289  MET A N   1 
ATOM   1981  C  CA  . MET A 1 289 ? 4.676   -19.161 -20.055 1.00 39.58  ? 289  MET A CA  1 
ATOM   1982  C  C   . MET A 1 289 ? 4.351   -17.851 -19.328 1.00 35.28  ? 289  MET A C   1 
ATOM   1983  O  O   . MET A 1 289 ? 4.289   -17.814 -18.102 1.00 35.41  ? 289  MET A O   1 
ATOM   1984  C  CB  . MET A 1 289 ? 6.172   -19.245 -20.365 1.00 33.04  ? 289  MET A CB  1 
ATOM   1985  C  CG  . MET A 1 289 ? 7.085   -19.189 -19.160 1.00 26.07  ? 289  MET A CG  1 
ATOM   1986  S  SD  . MET A 1 289 ? 8.763   -19.667 -19.636 1.00 41.95  ? 289  MET A SD  1 
ATOM   1987  C  CE  . MET A 1 289 ? 9.204   -18.392 -20.828 1.00 29.71  ? 289  MET A CE  1 
ATOM   1988  N  N   . GLN A 1 290 ? 4.142   -16.784 -20.096 1.00 26.36  ? 290  GLN A N   1 
ATOM   1989  C  CA  . GLN A 1 290 ? 3.884   -15.457 -19.537 1.00 23.50  ? 290  GLN A CA  1 
ATOM   1990  C  C   . GLN A 1 290 ? 2.751   -15.523 -18.540 1.00 26.42  ? 290  GLN A C   1 
ATOM   1991  O  O   . GLN A 1 290 ? 2.923   -15.272 -17.356 1.00 22.75  ? 290  GLN A O   1 
ATOM   1992  C  CB  . GLN A 1 290 ? 3.512   -14.463 -20.642 1.00 19.99  ? 290  GLN A CB  1 
ATOM   1993  C  CG  . GLN A 1 290 ? 3.268   -13.051 -20.145 1.00 21.33  ? 290  GLN A CG  1 
ATOM   1994  C  CD  . GLN A 1 290 ? 2.588   -12.163 -21.186 1.00 31.63  ? 290  GLN A CD  1 
ATOM   1995  O  OE1 . GLN A 1 290 ? 3.254   -11.461 -21.951 1.00 39.99  ? 290  GLN A OE1 1 
ATOM   1996  N  NE2 . GLN A 1 290 ? 1.252   -12.189 -21.214 1.00 19.45  ? 290  GLN A NE2 1 
ATOM   1997  N  N   . ASP A 1 291 ? 1.570   -15.864 -19.028 1.00 40.72  ? 291  ASP A N   1 
ATOM   1998  C  CA  . ASP A 1 291 ? 0.405   -15.861 -18.160 1.00 37.33  ? 291  ASP A CA  1 
ATOM   1999  C  C   . ASP A 1 291 ? 0.549   -16.906 -17.063 1.00 37.49  ? 291  ASP A C   1 
ATOM   2000  O  O   . ASP A 1 291 ? -0.084  -16.793 -16.009 1.00 34.85  ? 291  ASP A O   1 
ATOM   2001  C  CB  . ASP A 1 291 ? -0.894  -16.050 -18.963 1.00 41.26  ? 291  ASP A CB  1 
ATOM   2002  C  CG  . ASP A 1 291 ? -1.272  -14.806 -19.774 1.00 53.56  ? 291  ASP A CG  1 
ATOM   2003  O  OD1 . ASP A 1 291 ? -0.476  -13.838 -19.804 1.00 54.49  ? 291  ASP A OD1 1 
ATOM   2004  O  OD2 . ASP A 1 291 ? -2.368  -14.792 -20.377 1.00 51.45  ? 291  ASP A OD2 1 
ATOM   2005  N  N   . PHE A 1 292 ? 1.386   -17.915 -17.307 1.00 30.22  ? 292  PHE A N   1 
ATOM   2006  C  CA  . PHE A 1 292 ? 1.569   -18.958 -16.309 1.00 20.61  ? 292  PHE A CA  1 
ATOM   2007  C  C   . PHE A 1 292 ? 2.289   -18.406 -15.076 1.00 22.55  ? 292  PHE A C   1 
ATOM   2008  O  O   . PHE A 1 292 ? 1.897   -18.681 -13.937 1.00 36.56  ? 292  PHE A O   1 
ATOM   2009  C  CB  . PHE A 1 292 ? 2.301   -20.170 -16.868 1.00 12.07  ? 292  PHE A CB  1 
ATOM   2010  C  CG  . PHE A 1 292 ? 2.741   -21.129 -15.813 1.00 15.25  ? 292  PHE A CG  1 
ATOM   2011  C  CD1 . PHE A 1 292 ? 1.909   -22.161 -15.421 1.00 25.37  ? 292  PHE A CD1 1 
ATOM   2012  C  CD2 . PHE A 1 292 ? 3.978   -20.988 -15.189 1.00 14.55  ? 292  PHE A CD2 1 
ATOM   2013  C  CE1 . PHE A 1 292 ? 2.296   -23.053 -14.424 1.00 28.77  ? 292  PHE A CE1 1 
ATOM   2014  C  CE2 . PHE A 1 292 ? 4.376   -21.875 -14.204 1.00 31.66  ? 292  PHE A CE2 1 
ATOM   2015  C  CZ  . PHE A 1 292 ? 3.534   -22.907 -13.816 1.00 32.69  ? 292  PHE A CZ  1 
ATOM   2016  N  N   . ASN A 1 293 ? 3.321   -17.607 -15.307 1.00 24.53  ? 293  ASN A N   1 
ATOM   2017  C  CA  . ASN A 1 293 ? 3.971   -16.886 -14.220 1.00 33.80  ? 293  ASN A CA  1 
ATOM   2018  C  C   . ASN A 1 293 ? 2.985   -16.130 -13.318 1.00 31.51  ? 293  ASN A C   1 
ATOM   2019  O  O   . ASN A 1 293 ? 2.996   -16.275 -12.090 1.00 33.59  ? 293  ASN A O   1 
ATOM   2020  C  CB  . ASN A 1 293 ? 5.022   -15.923 -14.779 1.00 29.46  ? 293  ASN A CB  1 
ATOM   2021  C  CG  . ASN A 1 293 ? 6.352   -16.615 -15.081 1.00 34.98  ? 293  ASN A CG  1 
ATOM   2022  O  OD1 . ASN A 1 293 ? 7.287   -16.585 -14.268 1.00 21.16  ? 293  ASN A OD1 1 
ATOM   2023  N  ND2 . ASN A 1 293 ? 6.441   -17.239 -16.256 1.00 36.71  ? 293  ASN A ND2 1 
ATOM   2024  N  N   . TYR A 1 294 ? 2.122   -15.337 -13.938 1.00 26.84  ? 294  TYR A N   1 
ATOM   2025  C  CA  . TYR A 1 294 ? 1.254   -14.439 -13.188 1.00 43.75  ? 294  TYR A CA  1 
ATOM   2026  C  C   . TYR A 1 294 ? 0.202   -15.204 -12.400 1.00 36.47  ? 294  TYR A C   1 
ATOM   2027  O  O   . TYR A 1 294 ? -0.042  -14.922 -11.225 1.00 28.10  ? 294  TYR A O   1 
ATOM   2028  C  CB  . TYR A 1 294 ? 0.592   -13.429 -14.135 1.00 38.85  ? 294  TYR A CB  1 
ATOM   2029  C  CG  . TYR A 1 294 ? -0.244  -12.373 -13.442 1.00 38.87  ? 294  TYR A CG  1 
ATOM   2030  C  CD1 . TYR A 1 294 ? 0.338   -11.465 -12.547 1.00 35.84  ? 294  TYR A CD1 1 
ATOM   2031  C  CD2 . TYR A 1 294 ? -1.617  -12.270 -13.692 1.00 31.28  ? 294  TYR A CD2 1 
ATOM   2032  C  CE1 . TYR A 1 294 ? -0.430  -10.490 -11.915 1.00 39.93  ? 294  TYR A CE1 1 
ATOM   2033  C  CE2 . TYR A 1 294 ? -2.393  -11.301 -13.070 1.00 27.99  ? 294  TYR A CE2 1 
ATOM   2034  C  CZ  . TYR A 1 294 ? -1.798  -10.412 -12.180 1.00 39.54  ? 294  TYR A CZ  1 
ATOM   2035  O  OH  . TYR A 1 294 ? -2.573  -9.445  -11.564 1.00 32.15  ? 294  TYR A OH  1 
ATOM   2036  N  N   . ALA A 1 295 ? -0.400  -16.186 -13.062 1.00 42.70  ? 295  ALA A N   1 
ATOM   2037  C  CA  . ALA A 1 295 ? -1.553  -16.907 -12.528 1.00 33.51  ? 295  ALA A CA  1 
ATOM   2038  C  C   . ALA A 1 295 ? -1.194  -18.002 -11.528 1.00 31.66  ? 295  ALA A C   1 
ATOM   2039  O  O   . ALA A 1 295 ? -2.044  -18.410 -10.746 1.00 41.00  ? 295  ALA A O   1 
ATOM   2040  C  CB  . ALA A 1 295 ? -2.377  -17.489 -13.667 1.00 22.52  ? 295  ALA A CB  1 
ATOM   2041  N  N   . PHE A 1 296 ? 0.046   -18.485 -11.550 1.00 22.09  ? 296  PHE A N   1 
ATOM   2042  C  CA  . PHE A 1 296 ? 0.416   -19.606 -10.691 1.00 25.53  ? 296  PHE A CA  1 
ATOM   2043  C  C   . PHE A 1 296 ? 1.596   -19.258 -9.804  1.00 36.95  ? 296  PHE A C   1 
ATOM   2044  O  O   . PHE A 1 296 ? 2.203   -20.139 -9.181  1.00 29.04  ? 296  PHE A O   1 
ATOM   2045  C  CB  . PHE A 1 296 ? 0.746   -20.839 -11.532 1.00 38.07  ? 296  PHE A CB  1 
ATOM   2046  C  CG  . PHE A 1 296 ? -0.419  -21.350 -12.360 1.00 52.12  ? 296  PHE A CG  1 
ATOM   2047  C  CD1 . PHE A 1 296 ? -0.704  -20.807 -13.609 1.00 45.52  ? 296  PHE A CD1 1 
ATOM   2048  C  CD2 . PHE A 1 296 ? -1.226  -22.382 -11.888 1.00 54.27  ? 296  PHE A CD2 1 
ATOM   2049  C  CE1 . PHE A 1 296 ? -1.770  -21.285 -14.367 1.00 39.75  ? 296  PHE A CE1 1 
ATOM   2050  C  CE2 . PHE A 1 296 ? -2.300  -22.860 -12.648 1.00 42.96  ? 296  PHE A CE2 1 
ATOM   2051  C  CZ  . PHE A 1 296 ? -2.568  -22.310 -13.883 1.00 38.86  ? 296  PHE A CZ  1 
ATOM   2052  N  N   . SER A 1 297 ? 1.930   -17.971 -9.763  1.00 29.70  ? 297  SER A N   1 
ATOM   2053  C  CA  . SER A 1 297 ? 2.986   -17.497 -8.879  1.00 15.35  ? 297  SER A CA  1 
ATOM   2054  C  C   . SER A 1 297 ? 2.823   -16.006 -8.691  1.00 24.90  ? 297  SER A C   1 
ATOM   2055  O  O   . SER A 1 297 ? 1.849   -15.418 -9.160  1.00 36.56  ? 297  SER A O   1 
ATOM   2056  C  CB  . SER A 1 297 ? 4.377   -17.807 -9.448  1.00 21.74  ? 297  SER A CB  1 
ATOM   2057  O  OG  . SER A 1 297 ? 4.807   -16.825 -10.388 1.00 18.36  ? 297  SER A OG  1 
ATOM   2058  N  N   . ASN A 1 298 ? 3.784   -15.406 -8.002  1.00 20.63  ? 298  ASN A N   1 
ATOM   2059  C  CA  . ASN A 1 298 ? 3.801   -13.979 -7.770  1.00 14.31  ? 298  ASN A CA  1 
ATOM   2060  C  C   . ASN A 1 298 ? 4.357   -13.266 -8.996  1.00 26.84  ? 298  ASN A C   1 
ATOM   2061  O  O   . ASN A 1 298 ? 4.165   -12.066 -9.165  1.00 25.07  ? 298  ASN A O   1 
ATOM   2062  C  CB  . ASN A 1 298 ? 4.708   -13.665 -6.584  1.00 12.80  ? 298  ASN A CB  1 
ATOM   2063  C  CG  . ASN A 1 298 ? 4.133   -14.110 -5.260  1.00 19.75  ? 298  ASN A CG  1 
ATOM   2064  O  OD1 . ASN A 1 298 ? 2.924   -14.140 -5.065  1.00 30.26  ? 298  ASN A OD1 1 
ATOM   2065  N  ND2 . ASN A 1 298 ? 5.010   -14.438 -4.326  1.00 24.47  ? 298  ASN A ND2 1 
ATOM   2066  N  N   . CYS A 1 299 ? 5.067   -14.005 -9.842  1.00 13.12  ? 299  CYS A N   1 
ATOM   2067  C  CA  . CYS A 1 299 ? 5.917   -13.380 -10.847 1.00 17.17  ? 299  CYS A CA  1 
ATOM   2068  C  C   . CYS A 1 299 ? 5.142   -12.614 -11.916 1.00 30.33  ? 299  CYS A C   1 
ATOM   2069  O  O   . CYS A 1 299 ? 4.089   -13.062 -12.371 1.00 35.84  ? 299  CYS A O   1 
ATOM   2070  C  CB  . CYS A 1 299 ? 6.845   -14.404 -11.506 1.00 14.07  ? 299  CYS A CB  1 
ATOM   2071  S  SG  . CYS A 1 299 ? 8.255   -13.674 -12.402 1.00 33.48  ? 299  CYS A SG  1 
ATOM   2072  N  N   . PHE A 1 300 ? 5.688   -11.459 -12.306 1.00 25.51  ? 300  PHE A N   1 
ATOM   2073  C  CA  . PHE A 1 300 ? 5.142   -10.624 -13.367 1.00 25.48  ? 300  PHE A CA  1 
ATOM   2074  C  C   . PHE A 1 300 ? 6.024   -10.718 -14.620 1.00 28.12  ? 300  PHE A C   1 
ATOM   2075  O  O   . PHE A 1 300 ? 7.003   -9.990  -14.742 1.00 21.69  ? 300  PHE A O   1 
ATOM   2076  C  CB  . PHE A 1 300 ? 5.088   -9.159  -12.915 1.00 37.96  ? 300  PHE A CB  1 
ATOM   2077  C  CG  . PHE A 1 300 ? 4.065   -8.867  -11.842 1.00 39.64  ? 300  PHE A CG  1 
ATOM   2078  C  CD1 . PHE A 1 300 ? 3.517   -7.594  -11.732 1.00 29.90  ? 300  PHE A CD1 1 
ATOM   2079  C  CD2 . PHE A 1 300 ? 3.651   -9.850  -10.949 1.00 45.99  ? 300  PHE A CD2 1 
ATOM   2080  C  CE1 . PHE A 1 300 ? 2.575   -7.304  -10.746 1.00 37.70  ? 300  PHE A CE1 1 
ATOM   2081  C  CE2 . PHE A 1 300 ? 2.714   -9.567  -9.952  1.00 45.48  ? 300  PHE A CE2 1 
ATOM   2082  C  CZ  . PHE A 1 300 ? 2.180   -8.295  -9.848  1.00 37.10  ? 300  PHE A CZ  1 
ATOM   2083  N  N   . GLU A 1 301 ? 5.681   -11.610 -15.547 1.00 31.29  ? 301  GLU A N   1 
ATOM   2084  C  CA  . GLU A 1 301 ? 6.476   -11.792 -16.761 1.00 18.25  ? 301  GLU A CA  1 
ATOM   2085  C  C   . GLU A 1 301 ? 5.938   -10.999 -17.949 1.00 28.36  ? 301  GLU A C   1 
ATOM   2086  O  O   . GLU A 1 301 ? 4.739   -11.017 -18.240 1.00 33.33  ? 301  GLU A O   1 
ATOM   2087  C  CB  . GLU A 1 301 ? 6.570   -13.280 -17.111 1.00 25.47  ? 301  GLU A CB  1 
ATOM   2088  C  CG  . GLU A 1 301 ? 7.312   -13.587 -18.402 1.00 31.88  ? 301  GLU A CG  1 
ATOM   2089  C  CD  . GLU A 1 301 ? 7.703   -15.057 -18.515 1.00 41.78  ? 301  GLU A CD  1 
ATOM   2090  O  OE1 . GLU A 1 301 ? 8.533   -15.525 -17.696 1.00 50.77  ? 301  GLU A OE1 1 
ATOM   2091  O  OE2 . GLU A 1 301 ? 7.187   -15.753 -19.421 1.00 42.47  ? 301  GLU A OE2 1 
ATOM   2092  N  N   . LEU A 1 302 ? 6.835   -10.306 -18.641 1.00 36.00  ? 302  LEU A N   1 
ATOM   2093  C  CA  . LEU A 1 302 ? 6.514   -9.711  -19.938 1.00 36.19  ? 302  LEU A CA  1 
ATOM   2094  C  C   . LEU A 1 302 ? 6.969   -10.625 -21.052 1.00 30.39  ? 302  LEU A C   1 
ATOM   2095  O  O   . LEU A 1 302 ? 7.896   -11.414 -20.878 1.00 35.52  ? 302  LEU A O   1 
ATOM   2096  C  CB  . LEU A 1 302 ? 7.230   -8.371  -20.125 1.00 35.95  ? 302  LEU A CB  1 
ATOM   2097  C  CG  . LEU A 1 302 ? 6.816   -7.202  -19.241 1.00 38.60  ? 302  LEU A CG  1 
ATOM   2098  C  CD1 . LEU A 1 302 ? 7.525   -5.947  -19.724 1.00 34.05  ? 302  LEU A CD1 1 
ATOM   2099  C  CD2 . LEU A 1 302 ? 5.307   -7.024  -19.267 1.00 31.27  ? 302  LEU A CD2 1 
ATOM   2100  N  N   . THR A 1 303 ? 6.321   -10.501 -22.207 1.00 35.48  ? 303  THR A N   1 
ATOM   2101  C  CA  . THR A 1 303 ? 6.793   -11.134 -23.434 1.00 41.05  ? 303  THR A CA  1 
ATOM   2102  C  C   . THR A 1 303 ? 7.421   -10.040 -24.290 1.00 47.52  ? 303  THR A C   1 
ATOM   2103  O  O   . THR A 1 303 ? 6.770   -9.048  -24.612 1.00 45.09  ? 303  THR A O   1 
ATOM   2104  C  CB  . THR A 1 303 ? 5.641   -11.795 -24.242 1.00 48.44  ? 303  THR A CB  1 
ATOM   2105  O  OG1 . THR A 1 303 ? 4.828   -12.602 -23.381 1.00 49.88  ? 303  THR A OG1 1 
ATOM   2106  C  CG2 . THR A 1 303 ? 6.191   -12.665 -25.369 1.00 39.13  ? 303  THR A CG2 1 
ATOM   2107  N  N   . ILE A 1 304 ? 8.685   -10.204 -24.659 1.00 53.73  ? 304  ILE A N   1 
ATOM   2108  C  CA  . ILE A 1 304 ? 9.336   -9.171  -25.454 1.00 51.36  ? 304  ILE A CA  1 
ATOM   2109  C  C   . ILE A 1 304 ? 9.863   -9.644  -26.810 1.00 54.96  ? 304  ILE A C   1 
ATOM   2110  O  O   . ILE A 1 304 ? 10.671  -10.584 -26.903 1.00 41.02  ? 304  ILE A O   1 
ATOM   2111  C  CB  . ILE A 1 304 ? 10.437  -8.464  -24.674 1.00 38.14  ? 304  ILE A CB  1 
ATOM   2112  C  CG1 . ILE A 1 304 ? 9.831   -7.746  -23.477 1.00 34.67  ? 304  ILE A CG1 1 
ATOM   2113  C  CG2 . ILE A 1 304 ? 11.150  -7.465  -25.575 1.00 45.05  ? 304  ILE A CG2 1 
ATOM   2114  C  CD1 . ILE A 1 304 ? 10.839  -7.369  -22.441 1.00 49.19  ? 304  ILE A CD1 1 
ATOM   2115  N  N   . GLU A 1 305 ? 9.385   -8.966  -27.853 1.00 45.28  ? 305  GLU A N   1 
ATOM   2116  C  CA  . GLU A 1 305 ? 9.759   -9.262  -29.228 1.00 42.02  ? 305  GLU A CA  1 
ATOM   2117  C  C   . GLU A 1 305 ? 10.891  -8.319  -29.630 1.00 43.18  ? 305  GLU A C   1 
ATOM   2118  O  O   . GLU A 1 305 ? 10.744  -7.100  -29.554 1.00 52.71  ? 305  GLU A O   1 
ATOM   2119  C  CB  . GLU A 1 305 ? 8.543   -9.074  -30.148 1.00 33.72  ? 305  GLU A CB  1 
ATOM   2120  C  CG  . GLU A 1 305 ? 7.317   -9.940  -29.802 1.00 27.76  ? 305  GLU A CG  1 
ATOM   2121  C  CD  . GLU A 1 305 ? 7.469   -11.385 -30.258 1.00 39.84  ? 305  GLU A CD  1 
ATOM   2122  O  OE1 . GLU A 1 305 ? 6.540   -12.185 -30.039 1.00 38.24  ? 305  GLU A OE1 1 
ATOM   2123  O  OE2 . GLU A 1 305 ? 8.525   -11.724 -30.833 1.00 46.79  ? 305  GLU A OE2 1 
ATOM   2124  N  N   . LEU A 1 306 ? 12.015  -8.878  -30.066 1.00 34.76  ? 306  LEU A N   1 
ATOM   2125  C  CA  . LEU A 1 306 ? 13.227  -8.079  -30.274 1.00 46.76  ? 306  LEU A CA  1 
ATOM   2126  C  C   . LEU A 1 306 ? 13.479  -7.644  -31.716 1.00 48.53  ? 306  LEU A C   1 
ATOM   2127  O  O   . LEU A 1 306 ? 13.877  -6.504  -31.964 1.00 53.94  ? 306  LEU A O   1 
ATOM   2128  C  CB  . LEU A 1 306 ? 14.458  -8.814  -29.732 1.00 42.97  ? 306  LEU A CB  1 
ATOM   2129  C  CG  . LEU A 1 306 ? 14.352  -9.083  -28.238 1.00 44.85  ? 306  LEU A CG  1 
ATOM   2130  C  CD1 . LEU A 1 306 ? 15.416  -10.047 -27.763 1.00 46.79  ? 306  LEU A CD1 1 
ATOM   2131  C  CD2 . LEU A 1 306 ? 14.429  -7.778  -27.485 1.00 43.05  ? 306  LEU A CD2 1 
ATOM   2132  N  N   . SER A 1 307 ? 13.253  -8.545  -32.664 1.00 45.01  ? 307  SER A N   1 
ATOM   2133  C  CA  . SER A 1 307 ? 13.544  -8.242  -34.056 1.00 35.95  ? 307  SER A CA  1 
ATOM   2134  C  C   . SER A 1 307 ? 12.400  -8.643  -34.966 1.00 49.08  ? 307  SER A C   1 
ATOM   2135  O  O   . SER A 1 307 ? 11.579  -9.499  -34.616 1.00 58.18  ? 307  SER A O   1 
ATOM   2136  C  CB  . SER A 1 307 ? 14.818  -8.954  -34.496 1.00 39.86  ? 307  SER A CB  1 
ATOM   2137  O  OG  . SER A 1 307 ? 14.780  -10.325 -34.121 1.00 51.39  ? 307  SER A OG  1 
ATOM   2138  N  N   . CYS A 1 308 ? 12.347  -8.002  -36.130 1.00 51.65  ? 308  CYS A N   1 
ATOM   2139  C  CA  . CYS A 1 308 ? 11.442  -8.398  -37.193 1.00 43.85  ? 308  CYS A CA  1 
ATOM   2140  C  C   . CYS A 1 308 ? 11.924  -9.705  -37.785 1.00 48.19  ? 308  CYS A C   1 
ATOM   2141  O  O   . CYS A 1 308 ? 11.131  -10.604 -38.069 1.00 50.30  ? 308  CYS A O   1 
ATOM   2142  C  CB  . CYS A 1 308 ? 11.391  -7.324  -38.279 1.00 41.57  ? 308  CYS A CB  1 
ATOM   2143  S  SG  . CYS A 1 308 ? 10.445  -5.873  -37.803 1.00 66.01  ? 308  CYS A SG  1 
ATOM   2144  N  N   . CYS A 1 309 ? 13.235  -9.804  -37.975 1.00 48.61  ? 309  CYS A N   1 
ATOM   2145  C  CA  . CYS A 1 309 ? 13.840  -11.055 -38.419 1.00 42.59  ? 309  CYS A CA  1 
ATOM   2146  C  C   . CYS A 1 309 ? 14.086  -12.021 -37.248 1.00 52.91  ? 309  CYS A C   1 
ATOM   2147  O  O   . CYS A 1 309 ? 14.863  -11.732 -36.325 1.00 43.05  ? 309  CYS A O   1 
ATOM   2148  C  CB  . CYS A 1 309 ? 15.138  -10.783 -39.155 1.00 40.13  ? 309  CYS A CB  1 
ATOM   2149  S  SG  . CYS A 1 309 ? 15.889  -12.284 -39.797 1.00 74.45  ? 309  CYS A SG  1 
ATOM   2150  N  N   . LYS A 1 310 ? 13.419  -13.169 -37.291 1.00 55.00  ? 310  LYS A N   1 
ATOM   2151  C  CA  . LYS A 1 310 ? 13.514  -14.139 -36.207 1.00 51.76  ? 310  LYS A CA  1 
ATOM   2152  C  C   . LYS A 1 310 ? 14.960  -14.557 -35.933 1.00 50.17  ? 310  LYS A C   1 
ATOM   2153  O  O   . LYS A 1 310 ? 15.412  -14.555 -34.787 1.00 54.01  ? 310  LYS A O   1 
ATOM   2154  C  CB  . LYS A 1 310 ? 12.652  -15.366 -36.514 1.00 53.98  ? 310  LYS A CB  1 
ATOM   2155  C  CG  . LYS A 1 310 ? 11.169  -15.069 -36.583 1.00 53.55  ? 310  LYS A CG  1 
ATOM   2156  C  CD  . LYS A 1 310 ? 10.336  -16.334 -36.814 1.00 49.34  ? 310  LYS A CD  1 
ATOM   2157  C  CE  . LYS A 1 310 ? 8.905   -16.150 -36.255 1.00 55.89  ? 310  LYS A CE  1 
ATOM   2158  N  NZ  . LYS A 1 310 ? 8.049   -17.385 -36.307 1.00 61.43  ? 310  LYS A NZ  1 
ATOM   2159  N  N   . TYR A 1 311 ? 15.679  -14.912 -36.996 1.00 56.23  ? 311  TYR A N   1 
ATOM   2160  C  CA  . TYR A 1 311 ? 17.063  -15.384 -36.887 1.00 58.32  ? 311  TYR A CA  1 
ATOM   2161  C  C   . TYR A 1 311 ? 17.995  -14.560 -37.771 1.00 53.57  ? 311  TYR A C   1 
ATOM   2162  O  O   . TYR A 1 311 ? 18.327  -14.989 -38.870 1.00 55.29  ? 311  TYR A O   1 
ATOM   2163  C  CB  . TYR A 1 311 ? 17.158  -16.850 -37.327 1.00 55.22  ? 311  TYR A CB  1 
ATOM   2164  C  CG  . TYR A 1 311 ? 18.336  -17.622 -36.752 1.00 47.59  ? 311  TYR A CG  1 
ATOM   2165  C  CD1 . TYR A 1 311 ? 18.240  -18.992 -36.518 1.00 48.60  ? 311  TYR A CD1 1 
ATOM   2166  C  CD2 . TYR A 1 311 ? 19.531  -16.991 -36.432 1.00 50.54  ? 311  TYR A CD2 1 
ATOM   2167  C  CE1 . TYR A 1 311 ? 19.295  -19.717 -35.989 1.00 43.16  ? 311  TYR A CE1 1 
ATOM   2168  C  CE2 . TYR A 1 311 ? 20.598  -17.707 -35.888 1.00 50.24  ? 311  TYR A CE2 1 
ATOM   2169  C  CZ  . TYR A 1 311 ? 20.469  -19.072 -35.675 1.00 45.89  ? 311  TYR A CZ  1 
ATOM   2170  O  OH  . TYR A 1 311 ? 21.514  -19.799 -35.150 1.00 42.89  ? 311  TYR A OH  1 
ATOM   2171  N  N   . PRO A 1 312 ? 18.420  -13.375 -37.297 1.00 56.07  ? 312  PRO A N   1 
ATOM   2172  C  CA  . PRO A 1 312 ? 19.286  -12.522 -38.123 1.00 46.82  ? 312  PRO A CA  1 
ATOM   2173  C  C   . PRO A 1 312 ? 20.723  -13.030 -38.110 1.00 61.77  ? 312  PRO A C   1 
ATOM   2174  O  O   . PRO A 1 312 ? 21.006  -14.042 -37.462 1.00 67.32  ? 312  PRO A O   1 
ATOM   2175  C  CB  . PRO A 1 312 ? 19.193  -11.144 -37.450 1.00 43.64  ? 312  PRO A CB  1 
ATOM   2176  C  CG  . PRO A 1 312 ? 18.144  -11.291 -36.331 1.00 60.51  ? 312  PRO A CG  1 
ATOM   2177  C  CD  . PRO A 1 312 ? 18.082  -12.750 -36.006 1.00 58.37  ? 312  PRO A CD  1 
ATOM   2178  N  N   . ALA A 1 313 ? 21.611  -12.343 -38.824 1.00 64.67  ? 313  ALA A N   1 
ATOM   2179  C  CA  . ALA A 1 313 ? 23.022  -12.730 -38.888 1.00 63.89  ? 313  ALA A CA  1 
ATOM   2180  C  C   . ALA A 1 313 ? 23.816  -12.079 -37.764 1.00 53.06  ? 313  ALA A C   1 
ATOM   2181  O  O   . ALA A 1 313 ? 23.438  -11.022 -37.255 1.00 55.28  ? 313  ALA A O   1 
ATOM   2182  C  CB  . ALA A 1 313 ? 23.630  -12.367 -40.253 1.00 60.51  ? 313  ALA A CB  1 
ATOM   2183  N  N   . ALA A 1 314 ? 24.926  -12.712 -37.396 1.00 47.12  ? 314  ALA A N   1 
ATOM   2184  C  CA  . ALA A 1 314 ? 25.759  -12.247 -36.293 1.00 52.87  ? 314  ALA A CA  1 
ATOM   2185  C  C   . ALA A 1 314 ? 26.067  -10.741 -36.319 1.00 54.74  ? 314  ALA A C   1 
ATOM   2186  O  O   . ALA A 1 314 ? 25.954  -10.065 -35.299 1.00 60.74  ? 314  ALA A O   1 
ATOM   2187  C  CB  . ALA A 1 314 ? 27.049  -13.053 -36.242 1.00 54.59  ? 314  ALA A CB  1 
ATOM   2188  N  N   . SER A 1 315 ? 26.459  -10.224 -37.480 1.00 52.35  ? 315  SER A N   1 
ATOM   2189  C  CA  . SER A 1 315 ? 26.880  -8.823  -37.609 1.00 55.21  ? 315  SER A CA  1 
ATOM   2190  C  C   . SER A 1 315 ? 25.815  -7.883  -37.073 1.00 47.96  ? 315  SER A C   1 
ATOM   2191  O  O   . SER A 1 315 ? 26.102  -6.741  -36.709 1.00 51.58  ? 315  SER A O   1 
ATOM   2192  C  CB  . SER A 1 315 ? 27.200  -8.476  -39.076 1.00 53.51  ? 315  SER A CB  1 
ATOM   2193  O  OG  . SER A 1 315 ? 26.051  -8.603  -39.908 1.00 51.39  ? 315  SER A OG  1 
ATOM   2194  N  N   . THR A 1 316 ? 24.584  -8.383  -37.042 1.00 37.62  ? 316  THR A N   1 
ATOM   2195  C  CA  . THR A 1 316 ? 23.444  -7.652  -36.515 1.00 38.50  ? 316  THR A CA  1 
ATOM   2196  C  C   . THR A 1 316 ? 23.541  -7.518  -35.000 1.00 47.54  ? 316  THR A C   1 
ATOM   2197  O  O   . THR A 1 316 ? 23.146  -6.495  -34.428 1.00 53.06  ? 316  THR A O   1 
ATOM   2198  C  CB  . THR A 1 316 ? 22.128  -8.366  -36.889 1.00 40.38  ? 316  THR A CB  1 
ATOM   2199  O  OG1 . THR A 1 316 ? 21.682  -7.892  -38.163 1.00 50.78  ? 316  THR A OG1 1 
ATOM   2200  C  CG2 . THR A 1 316 ? 21.046  -8.106  -35.864 1.00 47.66  ? 316  THR A CG2 1 
ATOM   2201  N  N   . LEU A 1 317 ? 24.093  -8.549  -34.365 1.00 40.29  ? 317  LEU A N   1 
ATOM   2202  C  CA  . LEU A 1 317 ? 24.104  -8.690  -32.910 1.00 37.51  ? 317  LEU A CA  1 
ATOM   2203  C  C   . LEU A 1 317 ? 24.650  -7.492  -32.121 1.00 40.01  ? 317  LEU A C   1 
ATOM   2204  O  O   . LEU A 1 317 ? 24.069  -7.099  -31.099 1.00 44.48  ? 317  LEU A O   1 
ATOM   2205  C  CB  . LEU A 1 317 ? 24.850  -9.963  -32.515 1.00 32.48  ? 317  LEU A CB  1 
ATOM   2206  C  CG  . LEU A 1 317 ? 24.399  -11.270 -33.173 1.00 43.28  ? 317  LEU A CG  1 
ATOM   2207  C  CD1 . LEU A 1 317 ? 25.372  -12.382 -32.799 1.00 59.21  ? 317  LEU A CD1 1 
ATOM   2208  C  CD2 . LEU A 1 317 ? 22.951  -11.650 -32.808 1.00 33.75  ? 317  LEU A CD2 1 
ATOM   2209  N  N   . PRO A 1 318 ? 25.781  -6.923  -32.563 1.00 38.88  ? 318  PRO A N   1 
ATOM   2210  C  CA  . PRO A 1 318 ? 26.319  -5.778  -31.826 1.00 39.53  ? 318  PRO A CA  1 
ATOM   2211  C  C   . PRO A 1 318 ? 25.348  -4.602  -31.756 1.00 54.23  ? 318  PRO A C   1 
ATOM   2212  O  O   . PRO A 1 318 ? 25.242  -3.988  -30.690 1.00 61.99  ? 318  PRO A O   1 
ATOM   2213  C  CB  . PRO A 1 318 ? 27.563  -5.420  -32.623 1.00 42.53  ? 318  PRO A CB  1 
ATOM   2214  C  CG  . PRO A 1 318 ? 28.015  -6.730  -33.176 1.00 42.04  ? 318  PRO A CG  1 
ATOM   2215  C  CD  . PRO A 1 318 ? 26.747  -7.441  -33.543 1.00 42.55  ? 318  PRO A CD  1 
ATOM   2216  N  N   . GLN A 1 319 ? 24.648  -4.308  -32.855 1.00 49.03  ? 319  GLN A N   1 
ATOM   2217  C  CA  . GLN A 1 319 ? 23.571  -3.295  -32.868 1.00 51.05  ? 319  GLN A CA  1 
ATOM   2218  C  C   . GLN A 1 319 ? 22.404  -3.603  -31.906 1.00 50.32  ? 319  GLN A C   1 
ATOM   2219  O  O   . GLN A 1 319 ? 21.931  -2.728  -31.151 1.00 40.09  ? 319  GLN A O   1 
ATOM   2220  C  CB  . GLN A 1 319 ? 23.000  -3.131  -34.285 1.00 62.31  ? 319  GLN A CB  1 
ATOM   2221  C  CG  . GLN A 1 319 ? 23.629  -2.021  -35.114 1.00 77.13  ? 319  GLN A CG  1 
ATOM   2222  C  CD  . GLN A 1 319 ? 24.442  -2.560  -36.279 1.00 97.97  ? 319  GLN A CD  1 
ATOM   2223  O  OE1 . GLN A 1 319 ? 24.494  -1.951  -37.351 1.00 105.73 ? 319  GLN A OE1 1 
ATOM   2224  N  NE2 . GLN A 1 319 ? 25.077  -3.716  -36.074 1.00 95.35  ? 319  GLN A NE2 1 
ATOM   2225  N  N   . GLU A 1 320 ? 21.922  -4.844  -31.968 1.00 51.42  ? 320  GLU A N   1 
ATOM   2226  C  CA  . GLU A 1 320 ? 20.853  -5.291  -31.091 1.00 38.52  ? 320  GLU A CA  1 
ATOM   2227  C  C   . GLU A 1 320 ? 21.268  -5.085  -29.646 1.00 40.91  ? 320  GLU A C   1 
ATOM   2228  O  O   . GLU A 1 320 ? 20.450  -4.701  -28.802 1.00 50.06  ? 320  GLU A O   1 
ATOM   2229  C  CB  . GLU A 1 320 ? 20.510  -6.763  -31.341 1.00 38.76  ? 320  GLU A CB  1 
ATOM   2230  C  CG  . GLU A 1 320 ? 20.066  -7.074  -32.779 1.00 61.05  ? 320  GLU A CG  1 
ATOM   2231  C  CD  . GLU A 1 320 ? 18.745  -6.399  -33.182 1.00 66.95  ? 320  GLU A CD  1 
ATOM   2232  O  OE1 . GLU A 1 320 ? 18.192  -5.609  -32.385 1.00 62.50  ? 320  GLU A OE1 1 
ATOM   2233  O  OE2 . GLU A 1 320 ? 18.253  -6.666  -34.305 1.00 65.72  ? 320  GLU A OE2 1 
ATOM   2234  N  N   . TRP A 1 321 ? 22.544  -5.321  -29.354 1.00 33.15  ? 321  TRP A N   1 
ATOM   2235  C  CA  . TRP A 1 321 ? 23.022  -5.108  -27.991 1.00 47.58  ? 321  TRP A CA  1 
ATOM   2236  C  C   . TRP A 1 321 ? 22.863  -3.650  -27.544 1.00 53.22  ? 321  TRP A C   1 
ATOM   2237  O  O   . TRP A 1 321 ? 22.331  -3.383  -26.463 1.00 49.76  ? 321  TRP A O   1 
ATOM   2238  C  CB  . TRP A 1 321 ? 24.474  -5.568  -27.803 1.00 50.73  ? 321  TRP A CB  1 
ATOM   2239  C  CG  . TRP A 1 321 ? 25.052  -5.046  -26.517 1.00 49.19  ? 321  TRP A CG  1 
ATOM   2240  C  CD1 . TRP A 1 321 ? 25.956  -4.043  -26.381 1.00 37.17  ? 321  TRP A CD1 1 
ATOM   2241  C  CD2 . TRP A 1 321 ? 24.714  -5.467  -25.185 1.00 59.77  ? 321  TRP A CD2 1 
ATOM   2242  N  NE1 . TRP A 1 321 ? 26.223  -3.822  -25.056 1.00 41.67  ? 321  TRP A NE1 1 
ATOM   2243  C  CE2 . TRP A 1 321 ? 25.472  -4.681  -24.296 1.00 52.23  ? 321  TRP A CE2 1 
ATOM   2244  C  CE3 . TRP A 1 321 ? 23.843  -6.432  -24.658 1.00 57.69  ? 321  TRP A CE3 1 
ATOM   2245  C  CZ2 . TRP A 1 321 ? 25.392  -4.830  -22.904 1.00 39.65  ? 321  TRP A CZ2 1 
ATOM   2246  C  CZ3 . TRP A 1 321 ? 23.772  -6.582  -23.275 1.00 44.30  ? 321  TRP A CZ3 1 
ATOM   2247  C  CH2 . TRP A 1 321 ? 24.544  -5.787  -22.418 1.00 32.02  ? 321  TRP A CH2 1 
ATOM   2248  N  N   . GLN A 1 322 ? 23.313  -2.713  -28.375 1.00 51.25  ? 322  GLN A N   1 
ATOM   2249  C  CA  . GLN A 1 322 ? 23.281  -1.301  -28.006 1.00 55.59  ? 322  GLN A CA  1 
ATOM   2250  C  C   . GLN A 1 322 ? 21.864  -0.763  -27.817 1.00 56.07  ? 322  GLN A C   1 
ATOM   2251  O  O   . GLN A 1 322 ? 21.640  0.121   -26.987 1.00 56.47  ? 322  GLN A O   1 
ATOM   2252  C  CB  . GLN A 1 322 ? 24.034  -0.448  -29.021 1.00 52.72  ? 322  GLN A CB  1 
ATOM   2253  C  CG  . GLN A 1 322 ? 25.118  0.397   -28.392 1.00 61.74  ? 322  GLN A CG  1 
ATOM   2254  C  CD  . GLN A 1 322 ? 26.265  -0.440  -27.862 1.00 69.10  ? 322  GLN A CD  1 
ATOM   2255  O  OE1 . GLN A 1 322 ? 26.769  -0.203  -26.761 1.00 72.17  ? 322  GLN A OE1 1 
ATOM   2256  N  NE2 . GLN A 1 322 ? 26.681  -1.433  -28.644 1.00 63.75  ? 322  GLN A NE2 1 
ATOM   2257  N  N   . ARG A 1 323 ? 20.914  -1.297  -28.580 1.00 44.57  ? 323  ARG A N   1 
ATOM   2258  C  CA  . ARG A 1 323 ? 19.510  -0.890  -28.450 1.00 43.55  ? 323  ARG A CA  1 
ATOM   2259  C  C   . ARG A 1 323 ? 18.850  -1.417  -27.175 1.00 49.12  ? 323  ARG A C   1 
ATOM   2260  O  O   . ARG A 1 323 ? 18.199  -0.671  -26.434 1.00 49.94  ? 323  ARG A O   1 
ATOM   2261  C  CB  . ARG A 1 323 ? 18.713  -1.365  -29.664 1.00 36.72  ? 323  ARG A CB  1 
ATOM   2262  C  CG  . ARG A 1 323 ? 19.366  -0.986  -30.970 1.00 51.62  ? 323  ARG A CG  1 
ATOM   2263  C  CD  . ARG A 1 323 ? 18.675  -1.639  -32.144 1.00 55.13  ? 323  ARG A CD  1 
ATOM   2264  N  NE  . ARG A 1 323 ? 19.012  -0.994  -33.410 1.00 55.20  ? 323  ARG A NE  1 
ATOM   2265  C  CZ  . ARG A 1 323 ? 18.687  -1.497  -34.593 1.00 76.90  ? 323  ARG A CZ  1 
ATOM   2266  N  NH1 . ARG A 1 323 ? 18.024  -2.648  -34.652 1.00 71.74  ? 323  ARG A NH1 1 
ATOM   2267  N  NH2 . ARG A 1 323 ? 19.022  -0.858  -35.709 1.00 94.28  ? 323  ARG A NH2 1 
ATOM   2268  N  N   . ASN A 1 324 ? 19.019  -2.710  -26.923 1.00 38.11  ? 324  ASN A N   1 
ATOM   2269  C  CA  . ASN A 1 324 ? 18.316  -3.355  -25.835 1.00 31.58  ? 324  ASN A CA  1 
ATOM   2270  C  C   . ASN A 1 324 ? 19.013  -3.153  -24.503 1.00 42.06  ? 324  ASN A C   1 
ATOM   2271  O  O   . ASN A 1 324 ? 18.417  -3.354  -23.442 1.00 47.42  ? 324  ASN A O   1 
ATOM   2272  C  CB  . ASN A 1 324 ? 18.158  -4.839  -26.128 1.00 40.89  ? 324  ASN A CB  1 
ATOM   2273  C  CG  . ASN A 1 324 ? 17.278  -5.102  -27.334 1.00 49.54  ? 324  ASN A CG  1 
ATOM   2274  O  OD1 . ASN A 1 324 ? 16.089  -5.387  -27.189 1.00 53.56  ? 324  ASN A OD1 1 
ATOM   2275  N  ND2 . ASN A 1 324 ? 17.856  -5.005  -28.535 1.00 50.25  ? 324  ASN A ND2 1 
ATOM   2276  N  N   . LYS A 1 325 ? 20.277  -2.749  -24.564 1.00 38.50  ? 325  LYS A N   1 
ATOM   2277  C  CA  . LYS A 1 325 ? 21.100  -2.548  -23.368 1.00 42.38  ? 325  LYS A CA  1 
ATOM   2278  C  C   . LYS A 1 325 ? 20.379  -1.798  -22.239 1.00 38.71  ? 325  LYS A C   1 
ATOM   2279  O  O   . LYS A 1 325 ? 20.244  -2.323  -21.135 1.00 42.39  ? 325  LYS A O   1 
ATOM   2280  C  CB  . LYS A 1 325 ? 22.383  -1.807  -23.753 1.00 42.59  ? 325  LYS A CB  1 
ATOM   2281  C  CG  . LYS A 1 325 ? 23.489  -1.808  -22.714 1.00 29.57  ? 325  LYS A CG  1 
ATOM   2282  C  CD  . LYS A 1 325 ? 24.580  -0.896  -23.214 1.00 43.14  ? 325  LYS A CD  1 
ATOM   2283  C  CE  . LYS A 1 325 ? 25.778  -0.886  -22.308 1.00 56.27  ? 325  LYS A CE  1 
ATOM   2284  N  NZ  . LYS A 1 325 ? 26.857  -0.075  -22.933 1.00 62.19  ? 325  LYS A NZ  1 
ATOM   2285  N  N   . ALA A 1 326 ? 19.933  -0.575  -22.532 1.00 39.43  ? 326  ALA A N   1 
ATOM   2286  C  CA  . ALA A 1 326 ? 19.236  0.278   -21.569 1.00 45.36  ? 326  ALA A CA  1 
ATOM   2287  C  C   . ALA A 1 326 ? 17.880  -0.288  -21.118 1.00 54.98  ? 326  ALA A C   1 
ATOM   2288  O  O   . ALA A 1 326 ? 17.522  -0.220  -19.931 1.00 47.15  ? 326  ALA A O   1 
ATOM   2289  C  CB  . ALA A 1 326 ? 19.055  1.675   -22.145 1.00 38.93  ? 326  ALA A CB  1 
ATOM   2290  N  N   . SER A 1 327 ? 17.127  -0.838  -22.068 1.00 52.51  ? 327  SER A N   1 
ATOM   2291  C  CA  . SER A 1 327 ? 15.819  -1.429  -21.778 1.00 37.72  ? 327  SER A CA  1 
ATOM   2292  C  C   . SER A 1 327 ? 15.902  -2.672  -20.879 1.00 25.15  ? 327  SER A C   1 
ATOM   2293  O  O   . SER A 1 327 ? 14.985  -2.959  -20.122 1.00 35.04  ? 327  SER A O   1 
ATOM   2294  C  CB  . SER A 1 327 ? 15.109  -1.778  -23.090 1.00 33.50  ? 327  SER A CB  1 
ATOM   2295  O  OG  . SER A 1 327 ? 15.222  -0.713  -24.031 1.00 39.77  ? 327  SER A OG  1 
ATOM   2296  N  N   . LEU A 1 328 ? 17.001  -3.411  -20.973 1.00 22.96  ? 328  LEU A N   1 
ATOM   2297  C  CA  . LEU A 1 328 ? 17.181  -4.622  -20.175 1.00 32.69  ? 328  LEU A CA  1 
ATOM   2298  C  C   . LEU A 1 328 ? 17.619  -4.273  -18.753 1.00 36.06  ? 328  LEU A C   1 
ATOM   2299  O  O   . LEU A 1 328 ? 17.244  -4.927  -17.779 1.00 37.07  ? 328  LEU A O   1 
ATOM   2300  C  CB  . LEU A 1 328 ? 18.203  -5.565  -20.835 1.00 36.98  ? 328  LEU A CB  1 
ATOM   2301  C  CG  . LEU A 1 328 ? 17.859  -6.297  -22.147 1.00 26.58  ? 328  LEU A CG  1 
ATOM   2302  C  CD1 . LEU A 1 328 ? 19.119  -6.576  -22.935 1.00 20.31  ? 328  LEU A CD1 1 
ATOM   2303  C  CD2 . LEU A 1 328 ? 17.100  -7.594  -21.884 1.00 20.53  ? 328  LEU A CD2 1 
ATOM   2304  N  N   . LEU A 1 329 ? 18.415  -3.225  -18.633 1.00 35.87  ? 329  LEU A N   1 
ATOM   2305  C  CA  . LEU A 1 329 ? 18.816  -2.754  -17.318 1.00 46.05  ? 329  LEU A CA  1 
ATOM   2306  C  C   . LEU A 1 329 ? 17.646  -2.083  -16.597 1.00 41.31  ? 329  LEU A C   1 
ATOM   2307  O  O   . LEU A 1 329 ? 17.321  -2.422  -15.458 1.00 50.61  ? 329  LEU A O   1 
ATOM   2308  C  CB  . LEU A 1 329 ? 19.981  -1.773  -17.448 1.00 52.24  ? 329  LEU A CB  1 
ATOM   2309  C  CG  . LEU A 1 329 ? 21.401  -2.339  -17.545 1.00 48.02  ? 329  LEU A CG  1 
ATOM   2310  C  CD1 . LEU A 1 329 ? 21.424  -3.876  -17.478 1.00 37.22  ? 329  LEU A CD1 1 
ATOM   2311  C  CD2 . LEU A 1 329 ? 22.119  -1.787  -18.798 1.00 42.80  ? 329  LEU A CD2 1 
ATOM   2312  N  N   . GLN A 1 330 ? 17.017  -1.129  -17.272 1.00 29.00  ? 330  GLN A N   1 
ATOM   2313  C  CA  . GLN A 1 330 ? 15.922  -0.375  -16.680 1.00 40.94  ? 330  GLN A CA  1 
ATOM   2314  C  C   . GLN A 1 330 ? 14.745  -1.259  -16.273 1.00 41.52  ? 330  GLN A C   1 
ATOM   2315  O  O   . GLN A 1 330 ? 14.121  -1.024  -15.243 1.00 48.40  ? 330  GLN A O   1 
ATOM   2316  C  CB  . GLN A 1 330 ? 15.472  0.739   -17.626 1.00 53.30  ? 330  GLN A CB  1 
ATOM   2317  C  CG  . GLN A 1 330 ? 16.496  1.834   -17.769 1.00 54.92  ? 330  GLN A CG  1 
ATOM   2318  C  CD  . GLN A 1 330 ? 16.892  2.411   -16.423 1.00 56.95  ? 330  GLN A CD  1 
ATOM   2319  O  OE1 . GLN A 1 330 ? 16.110  3.106   -15.783 1.00 56.99  ? 330  GLN A OE1 1 
ATOM   2320  N  NE2 . GLN A 1 330 ? 18.114  2.126   -15.990 1.00 64.74  ? 330  GLN A NE2 1 
ATOM   2321  N  N   . LEU A 1 331 ? 14.441  -2.271  -17.080 1.00 37.19  ? 331  LEU A N   1 
ATOM   2322  C  CA  . LEU A 1 331 ? 13.367  -3.207  -16.753 1.00 28.11  ? 331  LEU A CA  1 
ATOM   2323  C  C   . LEU A 1 331 ? 13.740  -3.931  -15.475 1.00 25.90  ? 331  LEU A C   1 
ATOM   2324  O  O   . LEU A 1 331 ? 12.926  -4.072  -14.567 1.00 30.78  ? 331  LEU A O   1 
ATOM   2325  C  CB  . LEU A 1 331 ? 13.154  -4.215  -17.881 1.00 25.29  ? 331  LEU A CB  1 
ATOM   2326  C  CG  . LEU A 1 331 ? 11.963  -5.171  -17.758 1.00 38.68  ? 331  LEU A CG  1 
ATOM   2327  C  CD1 . LEU A 1 331 ? 11.843  -6.029  -19.001 1.00 28.76  ? 331  LEU A CD1 1 
ATOM   2328  C  CD2 . LEU A 1 331 ? 12.099  -6.070  -16.548 1.00 62.32  ? 331  LEU A CD2 1 
ATOM   2329  N  N   . LEU A 1 332 ? 14.981  -4.385  -15.402 1.00 22.23  ? 332  LEU A N   1 
ATOM   2330  C  CA  . LEU A 1 332 ? 15.421  -5.093  -14.210 1.00 35.95  ? 332  LEU A CA  1 
ATOM   2331  C  C   . LEU A 1 332 ? 15.183  -4.233  -12.990 1.00 30.99  ? 332  LEU A C   1 
ATOM   2332  O  O   . LEU A 1 332 ? 14.671  -4.716  -11.989 1.00 35.41  ? 332  LEU A O   1 
ATOM   2333  C  CB  . LEU A 1 332 ? 16.890  -5.511  -14.313 1.00 44.24  ? 332  LEU A CB  1 
ATOM   2334  C  CG  . LEU A 1 332 ? 17.109  -6.678  -15.292 1.00 39.91  ? 332  LEU A CG  1 
ATOM   2335  C  CD1 . LEU A 1 332 ? 18.577  -6.928  -15.581 1.00 33.42  ? 332  LEU A CD1 1 
ATOM   2336  C  CD2 . LEU A 1 332 ? 16.442  -7.942  -14.787 1.00 25.49  ? 332  LEU A CD2 1 
ATOM   2337  N  N   . ARG A 1 333 ? 15.518  -2.949  -13.084 1.00 36.89  ? 333  ARG A N   1 
ATOM   2338  C  CA  . ARG A 1 333 ? 15.358  -2.033  -11.942 1.00 28.07  ? 333  ARG A CA  1 
ATOM   2339  C  C   . ARG A 1 333 ? 13.900  -1.800  -11.554 1.00 28.72  ? 333  ARG A C   1 
ATOM   2340  O  O   . ARG A 1 333 ? 13.613  -1.255  -10.488 1.00 51.97  ? 333  ARG A O   1 
ATOM   2341  C  CB  . ARG A 1 333 ? 16.080  -0.708  -12.188 1.00 24.80  ? 333  ARG A CB  1 
ATOM   2342  C  CG  . ARG A 1 333 ? 17.516  -0.912  -12.646 1.00 44.83  ? 333  ARG A CG  1 
ATOM   2343  C  CD  . ARG A 1 333 ? 18.424  0.275   -12.363 1.00 61.63  ? 333  ARG A CD  1 
ATOM   2344  N  NE  . ARG A 1 333 ? 18.871  0.300   -10.982 1.00 63.78  ? 333  ARG A NE  1 
ATOM   2345  C  CZ  . ARG A 1 333 ? 20.131  0.254   -10.546 1.00 66.76  ? 333  ARG A CZ  1 
ATOM   2346  N  NH1 . ARG A 1 333 ? 20.333  0.293   -9.242  1.00 61.27  ? 333  ARG A NH1 1 
ATOM   2347  N  NH2 . ARG A 1 333 ? 21.176  0.180   -11.367 1.00 63.78  ? 333  ARG A NH2 1 
ATOM   2348  N  N   . GLN A 1 334 ? 12.982  -2.234  -12.412 1.00 29.04  ? 334  GLN A N   1 
ATOM   2349  C  CA  . GLN A 1 334 ? 11.556  -2.188  -12.105 1.00 20.96  ? 334  GLN A CA  1 
ATOM   2350  C  C   . GLN A 1 334 ? 11.174  -3.247  -11.057 1.00 36.96  ? 334  GLN A C   1 
ATOM   2351  O  O   . GLN A 1 334 ? 10.114  -3.171  -10.434 1.00 48.18  ? 334  GLN A O   1 
ATOM   2352  C  CB  . GLN A 1 334 ? 10.734  -2.371  -13.379 1.00 37.65  ? 334  GLN A CB  1 
ATOM   2353  C  CG  . GLN A 1 334 ? 10.687  -1.149  -14.297 1.00 33.08  ? 334  GLN A CG  1 
ATOM   2354  C  CD  . GLN A 1 334 ? 9.847   -0.020  -13.709 1.00 39.83  ? 334  GLN A CD  1 
ATOM   2355  O  OE1 . GLN A 1 334 ? 8.631   -0.142  -13.561 1.00 47.24  ? 334  GLN A OE1 1 
ATOM   2356  N  NE2 . GLN A 1 334 ? 10.497  1.080   -13.371 1.00 33.78  ? 334  GLN A NE2 1 
ATOM   2357  N  N   . ALA A 1 335 ? 12.039  -4.229  -10.841 1.00 23.88  ? 335  ALA A N   1 
ATOM   2358  C  CA  . ALA A 1 335 ? 11.808  -5.177  -9.768  1.00 29.83  ? 335  ALA A CA  1 
ATOM   2359  C  C   . ALA A 1 335 ? 11.994  -4.499  -8.412  1.00 35.53  ? 335  ALA A C   1 
ATOM   2360  O  O   . ALA A 1 335 ? 11.976  -5.150  -7.366  1.00 36.47  ? 335  ALA A O   1 
ATOM   2361  C  CB  . ALA A 1 335 ? 12.733  -6.374  -9.897  1.00 21.99  ? 335  ALA A CB  1 
ATOM   2362  N  N   . HIS A 1 336 ? 12.174  -3.188  -8.417  1.00 29.33  ? 336  HIS A N   1 
ATOM   2363  C  CA  . HIS A 1 336 ? 12.398  -2.503  -7.154  1.00 36.39  ? 336  HIS A CA  1 
ATOM   2364  C  C   . HIS A 1 336 ? 11.310  -1.532  -6.786  1.00 37.70  ? 336  HIS A C   1 
ATOM   2365  O  O   . HIS A 1 336 ? 11.321  -0.977  -5.687  1.00 20.18  ? 336  HIS A O   1 
ATOM   2366  C  CB  . HIS A 1 336 ? 13.751  -1.830  -7.155  1.00 33.52  ? 336  HIS A CB  1 
ATOM   2367  C  CG  . HIS A 1 336 ? 14.882  -2.801  -7.263  1.00 47.52  ? 336  HIS A CG  1 
ATOM   2368  N  ND1 . HIS A 1 336 ? 15.273  -3.602  -6.211  1.00 49.49  ? 336  HIS A ND1 1 
ATOM   2369  C  CD2 . HIS A 1 336 ? 15.686  -3.121  -8.304  1.00 39.36  ? 336  HIS A CD2 1 
ATOM   2370  C  CE1 . HIS A 1 336 ? 16.287  -4.359  -6.595  1.00 42.48  ? 336  HIS A CE1 1 
ATOM   2371  N  NE2 . HIS A 1 336 ? 16.556  -4.088  -7.859  1.00 41.13  ? 336  HIS A NE2 1 
ATOM   2372  N  N   . ILE A 1 337 ? 10.356  -1.357  -7.696  1.00 35.39  ? 337  ILE A N   1 
ATOM   2373  C  CA  . ILE A 1 337 ? 9.228   -0.480  -7.427  1.00 31.97  ? 337  ILE A CA  1 
ATOM   2374  C  C   . ILE A 1 337 ? 8.302   -1.070  -6.391  1.00 27.77  ? 337  ILE A C   1 
ATOM   2375  O  O   . ILE A 1 337 ? 8.390   -2.256  -6.044  1.00 39.67  ? 337  ILE A O   1 
ATOM   2376  C  CB  . ILE A 1 337 ? 8.422   -0.157  -8.696  1.00 41.60  ? 337  ILE A CB  1 
ATOM   2377  C  CG1 . ILE A 1 337 ? 7.755   -1.421  -9.239  1.00 42.07  ? 337  ILE A CG1 1 
ATOM   2378  C  CG2 . ILE A 1 337 ? 9.316   0.515   -9.744  1.00 36.72  ? 337  ILE A CG2 1 
ATOM   2379  C  CD1 . ILE A 1 337 ? 7.058   -1.199  -10.561 1.00 38.94  ? 337  ILE A CD1 1 
ATOM   2380  N  N   . GLY A 1 338 ? 7.412   -0.221  -5.898  1.00 34.61  ? 338  GLY A N   1 
ATOM   2381  C  CA  . GLY A 1 338 ? 6.419   -0.642  -4.933  1.00 41.11  ? 338  GLY A CA  1 
ATOM   2382  C  C   . GLY A 1 338 ? 6.985   -0.812  -3.541  1.00 24.51  ? 338  GLY A C   1 
ATOM   2383  O  O   . GLY A 1 338 ? 7.718   0.049   -3.046  1.00 26.54  ? 338  GLY A O   1 
ATOM   2384  N  N   . ILE A 1 339 ? 6.631   -1.928  -2.914  1.00 19.50  ? 339  ILE A N   1 
ATOM   2385  C  CA  . ILE A 1 339 ? 7.009   -2.180  -1.536  1.00 34.05  ? 339  ILE A CA  1 
ATOM   2386  C  C   . ILE A 1 339 ? 7.479   -3.597  -1.351  1.00 35.38  ? 339  ILE A C   1 
ATOM   2387  O  O   . ILE A 1 339 ? 7.483   -4.413  -2.280  1.00 33.30  ? 339  ILE A O   1 
ATOM   2388  C  CB  . ILE A 1 339 ? 5.839   -1.993  -0.557  1.00 30.88  ? 339  ILE A CB  1 
ATOM   2389  C  CG1 . ILE A 1 339 ? 4.681   -2.915  -0.965  1.00 35.02  ? 339  ILE A CG1 1 
ATOM   2390  C  CG2 . ILE A 1 339 ? 5.433   -0.518  -0.473  1.00 23.03  ? 339  ILE A CG2 1 
ATOM   2391  C  CD1 . ILE A 1 339 ? 3.474   -2.889  -0.031  1.00 27.15  ? 339  ILE A CD1 1 
ATOM   2392  N  N   . LYS A 1 340 ? 7.877   -3.874  -0.121  1.00 28.38  ? 340  LYS A N   1 
ATOM   2393  C  CA  . LYS A 1 340 ? 8.349   -5.184  0.252   1.00 31.60  ? 340  LYS A CA  1 
ATOM   2394  C  C   . LYS A 1 340 ? 8.415   -5.211  1.760   1.00 39.54  ? 340  LYS A C   1 
ATOM   2395  O  O   . LYS A 1 340 ? 8.468   -4.146  2.400   1.00 26.16  ? 340  LYS A O   1 
ATOM   2396  C  CB  . LYS A 1 340 ? 9.717   -5.484  -0.369  1.00 38.40  ? 340  LYS A CB  1 
ATOM   2397  C  CG  . LYS A 1 340 ? 10.875  -4.603  0.070   1.00 27.91  ? 340  LYS A CG  1 
ATOM   2398  C  CD  . LYS A 1 340 ? 12.166  -5.163  -0.521  1.00 22.72  ? 340  LYS A CD  1 
ATOM   2399  C  CE  . LYS A 1 340 ? 13.365  -4.292  -0.245  1.00 16.94  ? 340  LYS A CE  1 
ATOM   2400  N  NZ  . LYS A 1 340 ? 14.513  -4.750  -1.078  1.00 22.65  ? 340  LYS A NZ  1 
ATOM   2401  N  N   . GLY A 1 341 ? 8.375   -6.417  2.326   1.00 22.44  ? 341  GLY A N   1 
ATOM   2402  C  CA  . GLY A 1 341 ? 8.363   -6.553  3.768   1.00 16.97  ? 341  GLY A CA  1 
ATOM   2403  C  C   . GLY A 1 341 ? 8.218   -7.962  4.292   1.00 25.36  ? 341  GLY A C   1 
ATOM   2404  O  O   . GLY A 1 341 ? 8.317   -8.954  3.560   1.00 17.30  ? 341  GLY A O   1 
ATOM   2405  N  N   . LEU A 1 342 ? 7.978   -8.041  5.592   1.00 35.72  ? 342  LEU A N   1 
ATOM   2406  C  CA  . LEU A 1 342 ? 7.891   -9.319  6.265   1.00 36.16  ? 342  LEU A CA  1 
ATOM   2407  C  C   . LEU A 1 342 ? 6.572   -9.462  6.970   1.00 38.38  ? 342  LEU A C   1 
ATOM   2408  O  O   . LEU A 1 342 ? 6.107   -8.539  7.647   1.00 42.35  ? 342  LEU A O   1 
ATOM   2409  C  CB  . LEU A 1 342 ? 9.005   -9.452  7.295   1.00 31.01  ? 342  LEU A CB  1 
ATOM   2410  C  CG  . LEU A 1 342 ? 10.429  -9.284  6.761   1.00 30.35  ? 342  LEU A CG  1 
ATOM   2411  C  CD1 . LEU A 1 342 ? 11.385  -9.241  7.936   1.00 30.84  ? 342  LEU A CD1 1 
ATOM   2412  C  CD2 . LEU A 1 342 ? 10.812  -10.388 5.762   1.00 27.79  ? 342  LEU A CD2 1 
ATOM   2413  N  N   . VAL A 1 343 ? 5.966   -10.627 6.806   1.00 29.54  ? 343  VAL A N   1 
ATOM   2414  C  CA  . VAL A 1 343 ? 4.830   -10.986 7.623   1.00 30.98  ? 343  VAL A CA  1 
ATOM   2415  C  C   . VAL A 1 343 ? 5.410   -11.935 8.645   1.00 37.14  ? 343  VAL A C   1 
ATOM   2416  O  O   . VAL A 1 343 ? 5.982   -12.980 8.310   1.00 28.75  ? 343  VAL A O   1 
ATOM   2417  C  CB  . VAL A 1 343 ? 3.708   -11.653 6.817   1.00 35.41  ? 343  VAL A CB  1 
ATOM   2418  C  CG1 . VAL A 1 343 ? 2.591   -12.115 7.742   1.00 12.22  ? 343  VAL A CG1 1 
ATOM   2419  C  CG2 . VAL A 1 343 ? 3.192   -10.696 5.753   1.00 28.11  ? 343  VAL A CG2 1 
ATOM   2420  N  N   . THR A 1 344 ? 5.279   -11.550 9.904   1.00 50.67  ? 344  THR A N   1 
ATOM   2421  C  CA  . THR A 1 344 ? 5.984   -12.242 10.952  1.00 51.32  ? 344  THR A CA  1 
ATOM   2422  C  C   . THR A 1 344 ? 5.090   -12.600 12.131  1.00 50.09  ? 344  THR A C   1 
ATOM   2423  O  O   . THR A 1 344 ? 3.992   -12.059 12.291  1.00 43.78  ? 344  THR A O   1 
ATOM   2424  C  CB  . THR A 1 344 ? 7.133   -11.384 11.464  1.00 51.15  ? 344  THR A CB  1 
ATOM   2425  O  OG1 . THR A 1 344 ? 8.026   -12.202 12.223  1.00 71.11  ? 344  THR A OG1 1 
ATOM   2426  C  CG2 . THR A 1 344 ? 6.598   -10.248 12.342  1.00 35.32  ? 344  THR A CG2 1 
ATOM   2427  N  N   . ASP A 1 345 ? 5.584   -13.541 12.927  1.00 38.70  ? 345  ASP A N   1 
ATOM   2428  C  CA  . ASP A 1 345 ? 5.027   -13.899 14.219  1.00 35.66  ? 345  ASP A CA  1 
ATOM   2429  C  C   . ASP A 1 345 ? 4.959   -12.716 15.136  1.00 46.95  ? 345  ASP A C   1 
ATOM   2430  O  O   . ASP A 1 345 ? 5.536   -11.654 14.857  1.00 32.26  ? 345  ASP A O   1 
ATOM   2431  C  CB  . ASP A 1 345 ? 5.994   -14.846 14.920  1.00 27.89  ? 345  ASP A CB  1 
ATOM   2432  C  CG  . ASP A 1 345 ? 5.516   -16.240 14.922  1.00 31.41  ? 345  ASP A CG  1 
ATOM   2433  O  OD1 . ASP A 1 345 ? 6.289   -17.129 15.345  1.00 55.83  ? 345  ASP A OD1 1 
ATOM   2434  O  OD2 . ASP A 1 345 ? 4.360   -16.435 14.502  1.00 27.84  ? 345  ASP A OD2 1 
ATOM   2435  N  N   . ALA A 1 346 ? 4.286   -12.942 16.262  1.00 61.83  ? 346  ALA A N   1 
ATOM   2436  C  CA  . ALA A 1 346 ? 4.483   -12.142 17.464  1.00 63.06  ? 346  ALA A CA  1 
ATOM   2437  C  C   . ALA A 1 346 ? 5.848   -12.511 18.024  1.00 53.12  ? 346  ALA A C   1 
ATOM   2438  O  O   . ALA A 1 346 ? 6.545   -11.659 18.579  1.00 53.35  ? 346  ALA A O   1 
ATOM   2439  C  CB  . ALA A 1 346 ? 3.397   -12.419 18.486  1.00 61.55  ? 346  ALA A CB  1 
ATOM   2440  N  N   . SER A 1 347 ? 6.215   -13.787 17.870  1.00 29.10  ? 347  SER A N   1 
ATOM   2441  C  CA  . SER A 1 347 ? 7.585   -14.239 18.107  1.00 34.29  ? 347  SER A CA  1 
ATOM   2442  C  C   . SER A 1 347 ? 8.544   -13.497 17.188  1.00 38.76  ? 347  SER A C   1 
ATOM   2443  O  O   . SER A 1 347 ? 9.752   -13.680 17.273  1.00 41.89  ? 347  SER A O   1 
ATOM   2444  C  CB  . SER A 1 347 ? 7.727   -15.741 17.828  1.00 49.52  ? 347  SER A CB  1 
ATOM   2445  O  OG  . SER A 1 347 ? 6.861   -16.513 18.644  1.00 56.26  ? 347  SER A OG  1 
ATOM   2446  N  N   . GLY A 1 348 ? 7.998   -12.674 16.296  1.00 45.36  ? 348  GLY A N   1 
ATOM   2447  C  CA  . GLY A 1 348 ? 8.801   -11.997 15.294  1.00 47.16  ? 348  GLY A CA  1 
ATOM   2448  C  C   . GLY A 1 348 ? 9.387   -12.998 14.317  1.00 30.83  ? 348  GLY A C   1 
ATOM   2449  O  O   . GLY A 1 348 ? 10.510  -12.840 13.842  1.00 40.29  ? 348  GLY A O   1 
ATOM   2450  N  N   . PHE A 1 349 ? 8.604   -14.030 14.018  1.00 19.86  ? 349  PHE A N   1 
ATOM   2451  C  CA  . PHE A 1 349 ? 9.066   -15.170 13.244  1.00 23.63  ? 349  PHE A CA  1 
ATOM   2452  C  C   . PHE A 1 349 ? 8.259   -15.343 11.956  1.00 33.80  ? 349  PHE A C   1 
ATOM   2453  O  O   . PHE A 1 349 ? 7.028   -15.363 11.982  1.00 35.72  ? 349  PHE A O   1 
ATOM   2454  C  CB  . PHE A 1 349 ? 8.984   -16.453 14.079  1.00 20.35  ? 349  PHE A CB  1 
ATOM   2455  C  CG  . PHE A 1 349 ? 9.512   -17.645 13.366  1.00 38.48  ? 349  PHE A CG  1 
ATOM   2456  C  CD1 . PHE A 1 349 ? 10.839  -18.023 13.518  1.00 49.89  ? 349  PHE A CD1 1 
ATOM   2457  C  CD2 . PHE A 1 349 ? 8.707   -18.355 12.488  1.00 40.70  ? 349  PHE A CD2 1 
ATOM   2458  C  CE1 . PHE A 1 349 ? 11.351  -19.116 12.831  1.00 39.97  ? 349  PHE A CE1 1 
ATOM   2459  C  CE2 . PHE A 1 349 ? 9.208   -19.450 11.797  1.00 28.53  ? 349  PHE A CE2 1 
ATOM   2460  C  CZ  . PHE A 1 349 ? 10.534  -19.828 11.970  1.00 31.56  ? 349  PHE A CZ  1 
ATOM   2461  N  N   . PRO A 1 350 ? 8.958   -15.506 10.824  1.00 34.82  ? 350  PRO A N   1 
ATOM   2462  C  CA  . PRO A 1 350 ? 8.324   -15.402 9.506   1.00 32.45  ? 350  PRO A CA  1 
ATOM   2463  C  C   . PRO A 1 350 ? 7.161   -16.352 9.295   1.00 34.94  ? 350  PRO A C   1 
ATOM   2464  O  O   . PRO A 1 350 ? 7.286   -17.542 9.581   1.00 36.52  ? 350  PRO A O   1 
ATOM   2465  C  CB  . PRO A 1 350 ? 9.462   -15.752 8.532   1.00 30.07  ? 350  PRO A CB  1 
ATOM   2466  C  CG  . PRO A 1 350 ? 10.472  -16.463 9.343   1.00 33.38  ? 350  PRO A CG  1 
ATOM   2467  C  CD  . PRO A 1 350 ? 10.378  -15.882 10.724  1.00 30.42  ? 350  PRO A CD  1 
ATOM   2468  N  N   . ILE A 1 351 ? 6.049   -15.822 8.791   1.00 32.90  ? 351  ILE A N   1 
ATOM   2469  C  CA  . ILE A 1 351 ? 4.943   -16.656 8.343   1.00 32.31  ? 351  ILE A CA  1 
ATOM   2470  C  C   . ILE A 1 351 ? 5.029   -16.896 6.835   1.00 35.80  ? 351  ILE A C   1 
ATOM   2471  O  O   . ILE A 1 351 ? 4.979   -15.957 6.028   1.00 30.55  ? 351  ILE A O   1 
ATOM   2472  C  CB  . ILE A 1 351 ? 3.576   -16.036 8.666   1.00 37.05  ? 351  ILE A CB  1 
ATOM   2473  C  CG1 . ILE A 1 351 ? 3.527   -15.550 10.117  1.00 33.72  ? 351  ILE A CG1 1 
ATOM   2474  C  CG2 . ILE A 1 351 ? 2.481   -17.047 8.408   1.00 20.43  ? 351  ILE A CG2 1 
ATOM   2475  C  CD1 . ILE A 1 351 ? 2.263   -14.766 10.457  1.00 23.81  ? 351  ILE A CD1 1 
ATOM   2476  N  N   . ALA A 1 352 ? 5.153   -18.160 6.457   1.00 34.61  ? 352  ALA A N   1 
ATOM   2477  C  CA  . ALA A 1 352 ? 5.296   -18.522 5.059   1.00 28.10  ? 352  ALA A CA  1 
ATOM   2478  C  C   . ALA A 1 352 ? 3.920   -18.705 4.459   1.00 33.62  ? 352  ALA A C   1 
ATOM   2479  O  O   . ALA A 1 352 ? 2.975   -19.048 5.164   1.00 37.21  ? 352  ALA A O   1 
ATOM   2480  C  CB  . ALA A 1 352 ? 6.101   -19.784 4.935   1.00 21.01  ? 352  ALA A CB  1 
ATOM   2481  N  N   . ASP A 1 353 ? 3.802   -18.458 3.162   1.00 32.20  ? 353  ASP A N   1 
ATOM   2482  C  CA  . ASP A 1 353 ? 2.510   -18.575 2.481   1.00 31.92  ? 353  ASP A CA  1 
ATOM   2483  C  C   . ASP A 1 353 ? 1.407   -17.653 3.007   1.00 27.98  ? 353  ASP A C   1 
ATOM   2484  O  O   . ASP A 1 353 ? 0.224   -17.891 2.780   1.00 23.55  ? 353  ASP A O   1 
ATOM   2485  C  CB  . ASP A 1 353 ? 2.028   -20.022 2.504   1.00 44.85  ? 353  ASP A CB  1 
ATOM   2486  C  CG  . ASP A 1 353 ? 2.227   -20.711 1.169   1.00 71.16  ? 353  ASP A CG  1 
ATOM   2487  O  OD1 . ASP A 1 353 ? 1.257   -20.769 0.389   1.00 81.26  ? 353  ASP A OD1 1 
ATOM   2488  O  OD2 . ASP A 1 353 ? 3.350   -21.182 0.890   1.00 79.74  ? 353  ASP A OD2 1 
ATOM   2489  N  N   . ALA A 1 354 ? 1.795   -16.600 3.715   1.00 34.61  ? 354  ALA A N   1 
ATOM   2490  C  CA  . ALA A 1 354 ? 0.841   -15.569 4.081   1.00 40.98  ? 354  ALA A CA  1 
ATOM   2491  C  C   . ALA A 1 354 ? 0.391   -14.839 2.822   1.00 39.19  ? 354  ALA A C   1 
ATOM   2492  O  O   . ALA A 1 354 ? 1.064   -14.895 1.787   1.00 25.25  ? 354  ALA A O   1 
ATOM   2493  C  CB  . ALA A 1 354 ? 1.457   -14.595 5.070   1.00 31.45  ? 354  ALA A CB  1 
ATOM   2494  N  N   . ASN A 1 355 ? -0.751  -14.164 2.910   1.00 34.31  ? 355  ASN A N   1 
ATOM   2495  C  CA  . ASN A 1 355 ? -1.231  -13.344 1.807   1.00 37.41  ? 355  ASN A CA  1 
ATOM   2496  C  C   . ASN A 1 355 ? -1.170  -11.859 2.126   1.00 42.38  ? 355  ASN A C   1 
ATOM   2497  O  O   . ASN A 1 355 ? -1.553  -11.423 3.214   1.00 53.38  ? 355  ASN A O   1 
ATOM   2498  C  CB  . ASN A 1 355 ? -2.649  -13.744 1.402   1.00 45.29  ? 355  ASN A CB  1 
ATOM   2499  C  CG  . ASN A 1 355 ? -2.676  -14.983 0.528   1.00 54.71  ? 355  ASN A CG  1 
ATOM   2500  O  OD1 . ASN A 1 355 ? -3.313  -15.982 0.868   1.00 61.13  ? 355  ASN A OD1 1 
ATOM   2501  N  ND2 . ASN A 1 355 ? -1.980  -14.927 -0.606  1.00 52.48  ? 355  ASN A ND2 1 
ATOM   2502  N  N   . VAL A 1 356 ? -0.678  -11.087 1.170   1.00 34.43  ? 356  VAL A N   1 
ATOM   2503  C  CA  . VAL A 1 356 ? -0.593  -9.640  1.308   1.00 37.30  ? 356  VAL A CA  1 
ATOM   2504  C  C   . VAL A 1 356 ? -1.457  -8.961  0.244   1.00 39.76  ? 356  VAL A C   1 
ATOM   2505  O  O   . VAL A 1 356 ? -1.180  -9.067  -0.959  1.00 41.07  ? 356  VAL A O   1 
ATOM   2506  C  CB  . VAL A 1 356 ? 0.874   -9.148  1.214   1.00 44.52  ? 356  VAL A CB  1 
ATOM   2507  C  CG1 . VAL A 1 356 ? 0.930   -7.626  1.138   1.00 40.90  ? 356  VAL A CG1 1 
ATOM   2508  C  CG2 . VAL A 1 356 ? 1.698   -9.678  2.402   1.00 25.49  ? 356  VAL A CG2 1 
ATOM   2509  N  N   . TYR A 1 357 ? -2.505  -8.270  0.697   1.00 34.44  ? 357  TYR A N   1 
ATOM   2510  C  CA  . TYR A 1 357 ? -3.483  -7.677  -0.198  1.00 30.60  ? 357  TYR A CA  1 
ATOM   2511  C  C   . TYR A 1 357 ? -3.365  -6.161  -0.299  1.00 42.08  ? 357  TYR A C   1 
ATOM   2512  O  O   . TYR A 1 357 ? -3.101  -5.487  0.701   1.00 26.28  ? 357  TYR A O   1 
ATOM   2513  C  CB  . TYR A 1 357 ? -4.903  -8.010  0.260   1.00 35.17  ? 357  TYR A CB  1 
ATOM   2514  C  CG  . TYR A 1 357 ? -5.378  -9.441  0.071   1.00 40.98  ? 357  TYR A CG  1 
ATOM   2515  C  CD1 . TYR A 1 357 ? -5.275  -10.370 1.101   1.00 45.33  ? 357  TYR A CD1 1 
ATOM   2516  C  CD2 . TYR A 1 357 ? -5.978  -9.847  -1.119  1.00 34.32  ? 357  TYR A CD2 1 
ATOM   2517  C  CE1 . TYR A 1 357 ? -5.734  -11.676 0.936   1.00 46.02  ? 357  TYR A CE1 1 
ATOM   2518  C  CE2 . TYR A 1 357 ? -6.435  -11.140 -1.292  1.00 32.92  ? 357  TYR A CE2 1 
ATOM   2519  C  CZ  . TYR A 1 357 ? -6.311  -12.051 -0.268  1.00 38.62  ? 357  TYR A CZ  1 
ATOM   2520  O  OH  . TYR A 1 357 ? -6.770  -13.338 -0.451  1.00 43.63  ? 357  TYR A OH  1 
ATOM   2521  N  N   . VAL A 1 358 ? -3.591  -5.644  -1.512  1.00 53.78  ? 358  VAL A N   1 
ATOM   2522  C  CA  . VAL A 1 358 ? -3.673  -4.209  -1.774  1.00 45.19  ? 358  VAL A CA  1 
ATOM   2523  C  C   . VAL A 1 358 ? -5.071  -3.852  -2.251  1.00 48.72  ? 358  VAL A C   1 
ATOM   2524  O  O   . VAL A 1 358 ? -5.560  -4.413  -3.231  1.00 48.57  ? 358  VAL A O   1 
ATOM   2525  C  CB  . VAL A 1 358 ? -2.641  -3.755  -2.844  1.00 35.50  ? 358  VAL A CB  1 
ATOM   2526  C  CG1 . VAL A 1 358 ? -2.800  -2.262  -3.177  1.00 34.30  ? 358  VAL A CG1 1 
ATOM   2527  C  CG2 . VAL A 1 358 ? -1.211  -4.052  -2.381  1.00 32.08  ? 358  VAL A CG2 1 
ATOM   2528  N  N   . ALA A 1 359 ? -5.713  -2.923  -1.553  1.00 47.60  ? 359  ALA A N   1 
ATOM   2529  C  CA  . ALA A 1 359 ? -7.049  -2.479  -1.933  1.00 51.99  ? 359  ALA A CA  1 
ATOM   2530  C  C   . ALA A 1 359 ? -7.127  -2.131  -3.415  1.00 40.95  ? 359  ALA A C   1 
ATOM   2531  O  O   . ALA A 1 359 ? -6.417  -1.245  -3.892  1.00 43.51  ? 359  ALA A O   1 
ATOM   2532  C  CB  . ALA A 1 359 ? -7.474  -1.289  -1.086  1.00 49.24  ? 359  ALA A CB  1 
ATOM   2533  N  N   . GLY A 1 360 ? -8.002  -2.827  -4.134  1.00 36.03  ? 360  GLY A N   1 
ATOM   2534  C  CA  . GLY A 1 360 ? -8.183  -2.594  -5.555  1.00 28.76  ? 360  GLY A CA  1 
ATOM   2535  C  C   . GLY A 1 360 ? -7.324  -3.530  -6.380  1.00 36.46  ? 360  GLY A C   1 
ATOM   2536  O  O   . GLY A 1 360 ? -7.385  -3.540  -7.606  1.00 52.87  ? 360  GLY A O   1 
ATOM   2537  N  N   . LEU A 1 361 ? -6.498  -4.308  -5.697  1.00 34.06  ? 361  LEU A N   1 
ATOM   2538  C  CA  . LEU A 1 361 ? -5.677  -5.320  -6.347  1.00 36.83  ? 361  LEU A CA  1 
ATOM   2539  C  C   . LEU A 1 361 ? -5.757  -6.622  -5.554  1.00 47.95  ? 361  LEU A C   1 
ATOM   2540  O  O   . LEU A 1 361 ? -4.817  -7.423  -5.551  1.00 39.43  ? 361  LEU A O   1 
ATOM   2541  C  CB  . LEU A 1 361 ? -4.227  -4.852  -6.445  1.00 24.55  ? 361  LEU A CB  1 
ATOM   2542  C  CG  . LEU A 1 361 ? -3.977  -3.573  -7.254  1.00 37.99  ? 361  LEU A CG  1 
ATOM   2543  C  CD1 . LEU A 1 361 ? -2.553  -3.086  -7.044  1.00 37.53  ? 361  LEU A CD1 1 
ATOM   2544  C  CD2 . LEU A 1 361 ? -4.266  -3.761  -8.738  1.00 29.33  ? 361  LEU A CD2 1 
ATOM   2545  N  N   . GLU A 1 362 ? -6.888  -6.816  -4.882  1.00 45.94  ? 362  GLU A N   1 
ATOM   2546  C  CA  . GLU A 1 362 ? -7.083  -7.954  -3.996  1.00 40.14  ? 362  GLU A CA  1 
ATOM   2547  C  C   . GLU A 1 362 ? -7.220  -9.277  -4.747  1.00 42.15  ? 362  GLU A C   1 
ATOM   2548  O  O   . GLU A 1 362 ? -7.167  -10.349 -4.147  1.00 40.63  ? 362  GLU A O   1 
ATOM   2549  C  CB  . GLU A 1 362 ? -8.308  -7.726  -3.099  1.00 44.79  ? 362  GLU A CB  1 
ATOM   2550  C  CG  . GLU A 1 362 ? -7.983  -7.116  -1.740  1.00 60.95  ? 362  GLU A CG  1 
ATOM   2551  C  CD  . GLU A 1 362 ? -8.825  -5.894  -1.418  1.00 80.69  ? 362  GLU A CD  1 
ATOM   2552  O  OE1 . GLU A 1 362 ? -9.288  -5.216  -2.368  1.00 82.95  ? 362  GLU A OE1 1 
ATOM   2553  O  OE2 . GLU A 1 362 ? -9.009  -5.609  -0.211  1.00 81.81  ? 362  GLU A OE2 1 
ATOM   2554  N  N   . GLU A 1 363 ? -7.403  -9.205  -6.058  1.00 36.42  ? 363  GLU A N   1 
ATOM   2555  C  CA  . GLU A 1 363 ? -7.489  -10.418 -6.858  1.00 36.79  ? 363  GLU A CA  1 
ATOM   2556  C  C   . GLU A 1 363 ? -6.096  -11.007 -7.114  1.00 37.49  ? 363  GLU A C   1 
ATOM   2557  O  O   . GLU A 1 363 ? -5.951  -12.199 -7.415  1.00 37.25  ? 363  GLU A O   1 
ATOM   2558  C  CB  . GLU A 1 363 ? -8.245  -10.160 -8.164  1.00 49.35  ? 363  GLU A CB  1 
ATOM   2559  C  CG  . GLU A 1 363 ? -9.749  -10.012 -7.979  1.00 71.25  ? 363  GLU A CG  1 
ATOM   2560  C  CD  . GLU A 1 363 ? -10.486 -9.786  -9.283  1.00 84.30  ? 363  GLU A CD  1 
ATOM   2561  O  OE1 . GLU A 1 363 ? -10.166 -8.808  -9.991  1.00 83.50  ? 363  GLU A OE1 1 
ATOM   2562  O  OE2 . GLU A 1 363 ? -11.395 -10.583 -9.593  1.00 94.16  ? 363  GLU A OE2 1 
ATOM   2563  N  N   . LYS A 1 364 ? -5.070  -10.176 -6.977  1.00 31.21  ? 364  LYS A N   1 
ATOM   2564  C  CA  . LYS A 1 364 ? -3.701  -10.660 -7.082  1.00 34.21  ? 364  LYS A CA  1 
ATOM   2565  C  C   . LYS A 1 364 ? -2.918  -10.423 -5.798  1.00 37.79  ? 364  LYS A C   1 
ATOM   2566  O  O   . LYS A 1 364 ? -2.122  -9.495  -5.720  1.00 43.33  ? 364  LYS A O   1 
ATOM   2567  C  CB  . LYS A 1 364 ? -2.979  -10.001 -8.252  1.00 35.20  ? 364  LYS A CB  1 
ATOM   2568  C  CG  . LYS A 1 364 ? -1.563  -10.515 -8.475  1.00 28.08  ? 364  LYS A CG  1 
ATOM   2569  C  CD  . LYS A 1 364 ? -1.561  -12.023 -8.568  1.00 30.08  ? 364  LYS A CD  1 
ATOM   2570  C  CE  . LYS A 1 364 ? -0.259  -12.584 -9.129  1.00 30.11  ? 364  LYS A CE  1 
ATOM   2571  N  NZ  . LYS A 1 364 ? -0.221  -14.053 -8.876  1.00 27.57  ? 364  LYS A NZ  1 
ATOM   2572  N  N   . PRO A 1 365 ? -3.146  -11.269 -4.785  1.00 36.11  ? 365  PRO A N   1 
ATOM   2573  C  CA  . PRO A 1 365 ? -2.368  -11.240 -3.546  1.00 35.39  ? 365  PRO A CA  1 
ATOM   2574  C  C   . PRO A 1 365 ? -0.955  -11.752 -3.783  1.00 40.78  ? 365  PRO A C   1 
ATOM   2575  O  O   . PRO A 1 365 ? -0.720  -12.519 -4.722  1.00 37.00  ? 365  PRO A O   1 
ATOM   2576  C  CB  . PRO A 1 365 ? -3.107  -12.227 -2.636  1.00 43.91  ? 365  PRO A CB  1 
ATOM   2577  C  CG  . PRO A 1 365 ? -4.295  -12.703 -3.398  1.00 45.48  ? 365  PRO A CG  1 
ATOM   2578  C  CD  . PRO A 1 365 ? -4.062  -12.415 -4.834  1.00 46.06  ? 365  PRO A CD  1 
ATOM   2579  N  N   . MET A 1 366 ? -0.023  -11.329 -2.938  1.00 39.85  ? 366  MET A N   1 
ATOM   2580  C  CA  . MET A 1 366 ? 1.322   -11.883 -2.966  1.00 30.80  ? 366  MET A CA  1 
ATOM   2581  C  C   . MET A 1 366 ? 1.383   -12.930 -1.894  1.00 31.92  ? 366  MET A C   1 
ATOM   2582  O  O   . MET A 1 366 ? 0.850   -12.727 -0.815  1.00 40.56  ? 366  MET A O   1 
ATOM   2583  C  CB  . MET A 1 366 ? 2.365   -10.815 -2.665  1.00 41.34  ? 366  MET A CB  1 
ATOM   2584  C  CG  . MET A 1 366 ? 2.563   -9.794  -3.774  1.00 41.26  ? 366  MET A CG  1 
ATOM   2585  S  SD  . MET A 1 366 ? 3.093   -10.544 -5.320  1.00 30.72  ? 366  MET A SD  1 
ATOM   2586  C  CE  . MET A 1 366 ? 1.573   -10.437 -6.277  1.00 44.19  ? 366  MET A CE  1 
ATOM   2587  N  N   . ARG A 1 367 ? 2.033   -14.046 -2.194  1.00 29.15  ? 367  ARG A N   1 
ATOM   2588  C  CA  . ARG A 1 367 ? 2.203   -15.119 -1.224  1.00 31.61  ? 367  ARG A CA  1 
ATOM   2589  C  C   . ARG A 1 367 ? 3.613   -15.040 -0.643  1.00 31.08  ? 367  ARG A C   1 
ATOM   2590  O  O   . ARG A 1 367 ? 4.593   -15.080 -1.385  1.00 51.63  ? 367  ARG A O   1 
ATOM   2591  C  CB  . ARG A 1 367 ? 1.947   -16.463 -1.916  1.00 42.60  ? 367  ARG A CB  1 
ATOM   2592  C  CG  . ARG A 1 367 ? 2.132   -17.674 -1.056  1.00 54.56  ? 367  ARG A CG  1 
ATOM   2593  C  CD  . ARG A 1 367 ? 3.466   -18.310 -1.374  1.00 68.77  ? 367  ARG A CD  1 
ATOM   2594  N  NE  . ARG A 1 367 ? 3.331   -19.751 -1.452  1.00 83.46  ? 367  ARG A NE  1 
ATOM   2595  C  CZ  . ARG A 1 367 ? 3.485   -20.508 -2.536  1.00 91.58  ? 367  ARG A CZ  1 
ATOM   2596  N  NH1 . ARG A 1 367 ? 3.828   -19.998 -3.714  1.00 98.13  ? 367  ARG A NH1 1 
ATOM   2597  N  NH2 . ARG A 1 367 ? 3.306   -21.815 -2.414  1.00 90.23  ? 367  ARG A NH2 1 
ATOM   2598  N  N   . THR A 1 368 ? 3.733   -14.889 0.673   1.00 18.91  ? 368  THR A N   1 
ATOM   2599  C  CA  . THR A 1 368 ? 5.066   -14.728 1.255   1.00 26.08  ? 368  THR A CA  1 
ATOM   2600  C  C   . THR A 1 368 ? 5.933   -15.965 1.077   1.00 31.20  ? 368  THR A C   1 
ATOM   2601  O  O   . THR A 1 368 ? 5.432   -17.097 0.971   1.00 30.41  ? 368  THR A O   1 
ATOM   2602  C  CB  . THR A 1 368 ? 5.045   -14.371 2.749   1.00 22.12  ? 368  THR A CB  1 
ATOM   2603  O  OG1 . THR A 1 368 ? 4.521   -15.471 3.499   1.00 21.63  ? 368  THR A OG1 1 
ATOM   2604  C  CG2 . THR A 1 368 ? 4.213   -13.111 2.997   1.00 18.73  ? 368  THR A CG2 1 
ATOM   2605  N  N   . SER A 1 369 ? 7.242   -15.729 1.048   1.00 25.89  ? 369  SER A N   1 
ATOM   2606  C  CA  . SER A 1 369 ? 8.238   -16.782 0.937   1.00 16.48  ? 369  SER A CA  1 
ATOM   2607  C  C   . SER A 1 369 ? 8.370   -17.540 2.263   1.00 34.89  ? 369  SER A C   1 
ATOM   2608  O  O   . SER A 1 369 ? 7.725   -17.201 3.260   1.00 45.06  ? 369  SER A O   1 
ATOM   2609  C  CB  . SER A 1 369 ? 9.585   -16.168 0.564   1.00 13.61  ? 369  SER A CB  1 
ATOM   2610  O  OG  . SER A 1 369 ? 10.176  -15.548 1.697   1.00 19.15  ? 369  SER A OG  1 
ATOM   2611  N  N   . LYS A 1 370 ? 9.209   -18.571 2.274   1.00 31.13  ? 370  LYS A N   1 
ATOM   2612  C  CA  . LYS A 1 370 ? 9.464   -19.327 3.496   1.00 32.83  ? 370  LYS A CA  1 
ATOM   2613  C  C   . LYS A 1 370 ? 9.953   -18.427 4.618   1.00 23.97  ? 370  LYS A C   1 
ATOM   2614  O  O   . LYS A 1 370 ? 9.755   -18.732 5.786   1.00 44.79  ? 370  LYS A O   1 
ATOM   2615  C  CB  . LYS A 1 370 ? 10.466  -20.461 3.233   1.00 27.11  ? 370  LYS A CB  1 
ATOM   2616  C  CG  . LYS A 1 370 ? 9.893   -21.574 2.356   1.00 28.95  ? 370  LYS A CG  1 
ATOM   2617  C  CD  . LYS A 1 370 ? 10.965  -22.456 1.718   1.00 28.29  ? 370  LYS A CD  1 
ATOM   2618  C  CE  . LYS A 1 370 ? 10.312  -23.474 0.770   1.00 28.03  ? 370  LYS A CE  1 
ATOM   2619  N  NZ  . LYS A 1 370 ? 11.230  -24.576 0.358   1.00 39.40  ? 370  LYS A NZ  1 
ATOM   2620  N  N   . ARG A 1 371 ? 10.576  -17.313 4.254   1.00 16.86  ? 371  ARG A N   1 
ATOM   2621  C  CA  . ARG A 1 371 ? 11.068  -16.357 5.233   1.00 27.59  ? 371  ARG A CA  1 
ATOM   2622  C  C   . ARG A 1 371 ? 10.071  -15.212 5.411   1.00 24.39  ? 371  ARG A C   1 
ATOM   2623  O  O   . ARG A 1 371 ? 10.376  -14.188 5.998   1.00 35.76  ? 371  ARG A O   1 
ATOM   2624  C  CB  . ARG A 1 371 ? 12.479  -15.855 4.851   1.00 32.53  ? 371  ARG A CB  1 
ATOM   2625  C  CG  . ARG A 1 371 ? 13.408  -16.991 4.361   1.00 30.07  ? 371  ARG A CG  1 
ATOM   2626  C  CD  . ARG A 1 371 ? 14.898  -16.783 4.610   1.00 35.75  ? 371  ARG A CD  1 
ATOM   2627  N  NE  . ARG A 1 371 ? 15.476  -15.706 3.830   1.00 44.20  ? 371  ARG A NE  1 
ATOM   2628  C  CZ  . ARG A 1 371 ? 16.337  -15.818 2.826   1.00 59.30  ? 371  ARG A CZ  1 
ATOM   2629  N  NH1 . ARG A 1 371 ? 16.734  -14.709 2.241   1.00 59.79  ? 371  ARG A NH1 1 
ATOM   2630  N  NH2 . ARG A 1 371 ? 16.797  -16.988 2.393   1.00 73.38  ? 371  ARG A NH2 1 
ATOM   2631  N  N   . GLY A 1 372 ? 8.865   -15.402 4.905   1.00 27.75  ? 372  GLY A N   1 
ATOM   2632  C  CA  . GLY A 1 372 ? 7.798   -14.441 5.109   1.00 37.24  ? 372  GLY A CA  1 
ATOM   2633  C  C   . GLY A 1 372 ? 7.997   -13.150 4.348   1.00 25.58  ? 372  GLY A C   1 
ATOM   2634  O  O   . GLY A 1 372 ? 7.433   -12.117 4.688   1.00 21.85  ? 372  GLY A O   1 
ATOM   2635  N  N   . GLU A 1 373 ? 8.802   -13.212 3.303   1.00 22.17  ? 373  GLU A N   1 
ATOM   2636  C  CA  . GLU A 1 373 ? 9.054   -12.041 2.488   1.00 35.34  ? 373  GLU A CA  1 
ATOM   2637  C  C   . GLU A 1 373 ? 8.014   -11.887 1.393   1.00 39.17  ? 373  GLU A C   1 
ATOM   2638  O  O   . GLU A 1 373 ? 7.464   -12.873 0.897   1.00 40.14  ? 373  GLU A O   1 
ATOM   2639  C  CB  . GLU A 1 373 ? 10.432  -12.121 1.830   1.00 33.04  ? 373  GLU A CB  1 
ATOM   2640  C  CG  . GLU A 1 373 ? 11.417  -13.042 2.494   1.00 40.59  ? 373  GLU A CG  1 
ATOM   2641  C  CD  . GLU A 1 373 ? 12.663  -13.232 1.643   1.00 39.58  ? 373  GLU A CD  1 
ATOM   2642  O  OE1 . GLU A 1 373 ? 13.406  -12.239 1.473   1.00 24.43  ? 373  GLU A OE1 1 
ATOM   2643  O  OE2 . GLU A 1 373 ? 12.891  -14.365 1.141   1.00 35.27  ? 373  GLU A OE2 1 
ATOM   2644  N  N   . TYR A 1 374 ? 7.765   -10.639 1.008   1.00 30.15  ? 374  TYR A N   1 
ATOM   2645  C  CA  . TYR A 1 374 ? 6.931   -10.345 -0.147  1.00 32.91  ? 374  TYR A CA  1 
ATOM   2646  C  C   . TYR A 1 374 ? 7.442   -9.061  -0.791  1.00 42.14  ? 374  TYR A C   1 
ATOM   2647  O  O   . TYR A 1 374 ? 7.996   -8.183  -0.121  1.00 31.36  ? 374  TYR A O   1 
ATOM   2648  C  CB  . TYR A 1 374 ? 5.471   -10.166 0.255   1.00 27.00  ? 374  TYR A CB  1 
ATOM   2649  C  CG  . TYR A 1 374 ? 5.208   -8.818  0.880   1.00 33.31  ? 374  TYR A CG  1 
ATOM   2650  C  CD1 . TYR A 1 374 ? 5.300   -8.635  2.263   1.00 21.73  ? 374  TYR A CD1 1 
ATOM   2651  C  CD2 . TYR A 1 374 ? 4.896   -7.715  0.085   1.00 32.27  ? 374  TYR A CD2 1 
ATOM   2652  C  CE1 . TYR A 1 374 ? 5.085   -7.379  2.833   1.00 33.36  ? 374  TYR A CE1 1 
ATOM   2653  C  CE2 . TYR A 1 374 ? 4.679   -6.466  0.645   1.00 32.64  ? 374  TYR A CE2 1 
ATOM   2654  C  CZ  . TYR A 1 374 ? 4.774   -6.306  2.016   1.00 31.31  ? 374  TYR A CZ  1 
ATOM   2655  O  OH  . TYR A 1 374 ? 4.552   -5.069  2.560   1.00 33.58  ? 374  TYR A OH  1 
ATOM   2656  N  N   . TRP A 1 375 ? 7.270   -8.973  -2.103  1.00 33.20  ? 375  TRP A N   1 
ATOM   2657  C  CA  . TRP A 1 375 ? 7.556   -7.764  -2.837  1.00 17.18  ? 375  TRP A CA  1 
ATOM   2658  C  C   . TRP A 1 375 ? 6.308   -7.485  -3.640  1.00 32.88  ? 375  TRP A C   1 
ATOM   2659  O  O   . TRP A 1 375 ? 5.855   -8.352  -4.392  1.00 37.48  ? 375  TRP A O   1 
ATOM   2660  C  CB  . TRP A 1 375 ? 8.713   -7.973  -3.813  1.00 21.54  ? 375  TRP A CB  1 
ATOM   2661  C  CG  . TRP A 1 375 ? 9.951   -8.508  -3.197  1.00 23.82  ? 375  TRP A CG  1 
ATOM   2662  C  CD1 . TRP A 1 375 ? 11.103  -7.815  -2.915  1.00 22.84  ? 375  TRP A CD1 1 
ATOM   2663  C  CD2 . TRP A 1 375 ? 10.189  -9.863  -2.802  1.00 27.76  ? 375  TRP A CD2 1 
ATOM   2664  N  NE1 . TRP A 1 375 ? 12.033  -8.659  -2.351  1.00 19.69  ? 375  TRP A NE1 1 
ATOM   2665  C  CE2 . TRP A 1 375 ? 11.495  -9.919  -2.268  1.00 29.42  ? 375  TRP A CE2 1 
ATOM   2666  C  CE3 . TRP A 1 375 ? 9.420   -11.036 -2.838  1.00 17.01  ? 375  TRP A CE3 1 
ATOM   2667  C  CZ2 . TRP A 1 375 ? 12.040  -11.093 -1.773  1.00 22.42  ? 375  TRP A CZ2 1 
ATOM   2668  C  CZ3 . TRP A 1 375 ? 9.961   -12.196 -2.338  1.00 16.69  ? 375  TRP A CZ3 1 
ATOM   2669  C  CH2 . TRP A 1 375 ? 11.257  -12.220 -1.816  1.00 18.42  ? 375  TRP A CH2 1 
ATOM   2670  N  N   . ARG A 1 376 ? 5.742   -6.293  -3.494  1.00 27.93  ? 376  ARG A N   1 
ATOM   2671  C  CA  . ARG A 1 376 ? 4.558   -5.951  -4.263  1.00 21.18  ? 376  ARG A CA  1 
ATOM   2672  C  C   . ARG A 1 376 ? 4.864   -4.773  -5.164  1.00 33.96  ? 376  ARG A C   1 
ATOM   2673  O  O   . ARG A 1 376 ? 4.984   -3.620  -4.722  1.00 23.31  ? 376  ARG A O   1 
ATOM   2674  C  CB  . ARG A 1 376 ? 3.367   -5.661  -3.352  1.00 25.89  ? 376  ARG A CB  1 
ATOM   2675  C  CG  . ARG A 1 376 ? 2.099   -5.229  -4.081  1.00 35.50  ? 376  ARG A CG  1 
ATOM   2676  C  CD  . ARG A 1 376 ? 1.540   -6.325  -4.965  1.00 33.46  ? 376  ARG A CD  1 
ATOM   2677  N  NE  . ARG A 1 376 ? 0.348   -5.884  -5.691  1.00 41.17  ? 376  ARG A NE  1 
ATOM   2678  C  CZ  . ARG A 1 376 ? -0.288  -6.597  -6.618  1.00 46.42  ? 376  ARG A CZ  1 
ATOM   2679  N  NH1 . ARG A 1 376 ? 0.143   -7.801  -6.961  1.00 68.32  ? 376  ARG A NH1 1 
ATOM   2680  N  NH2 . ARG A 1 376 ? -1.364  -6.106  -7.208  1.00 53.41  ? 376  ARG A NH2 1 
ATOM   2681  N  N   . LEU A 1 377 ? 5.016   -5.081  -6.442  1.00 30.83  ? 377  LEU A N   1 
ATOM   2682  C  CA  . LEU A 1 377 ? 5.338   -4.057  -7.413  1.00 29.47  ? 377  LEU A CA  1 
ATOM   2683  C  C   . LEU A 1 377 ? 4.170   -3.105  -7.499  1.00 25.08  ? 377  LEU A C   1 
ATOM   2684  O  O   . LEU A 1 377 ? 3.025   -3.530  -7.616  1.00 39.22  ? 377  LEU A O   1 
ATOM   2685  C  CB  . LEU A 1 377 ? 5.597   -4.691  -8.775  1.00 22.50  ? 377  LEU A CB  1 
ATOM   2686  C  CG  . LEU A 1 377 ? 6.706   -5.735  -8.817  1.00 29.04  ? 377  LEU A CG  1 
ATOM   2687  C  CD1 . LEU A 1 377 ? 7.012   -6.085  -10.260 1.00 28.52  ? 377  LEU A CD1 1 
ATOM   2688  C  CD2 . LEU A 1 377 ? 7.950   -5.239  -8.094  1.00 26.58  ? 377  LEU A CD2 1 
ATOM   2689  N  N   . LEU A 1 378 ? 4.451   -1.814  -7.464  1.00 36.31  ? 378  LEU A N   1 
ATOM   2690  C  CA  . LEU A 1 378 ? 3.377   -0.838  -7.524  1.00 32.64  ? 378  LEU A CA  1 
ATOM   2691  C  C   . LEU A 1 378 ? 3.718   0.374   -8.386  1.00 18.09  ? 378  LEU A C   1 
ATOM   2692  O  O   . LEU A 1 378 ? 4.847   0.831   -8.448  1.00 31.29  ? 378  LEU A O   1 
ATOM   2693  C  CB  . LEU A 1 378 ? 2.955   -0.406  -6.108  1.00 27.21  ? 378  LEU A CB  1 
ATOM   2694  C  CG  . LEU A 1 378 ? 2.201   -1.409  -5.213  1.00 22.92  ? 378  LEU A CG  1 
ATOM   2695  C  CD1 . LEU A 1 378 ? 2.087   -0.907  -3.791  1.00 25.44  ? 378  LEU A CD1 1 
ATOM   2696  C  CD2 . LEU A 1 378 ? 0.813   -1.712  -5.754  1.00 23.68  ? 378  LEU A CD2 1 
ATOM   2697  N  N   . THR A 1 379 ? 2.708   0.862   -9.075  1.00 36.01  ? 379  THR A N   1 
ATOM   2698  C  CA  . THR A 1 379 ? 2.751   2.148   -9.720  1.00 40.00  ? 379  THR A CA  1 
ATOM   2699  C  C   . THR A 1 379 ? 2.778   3.187   -8.615  1.00 44.47  ? 379  THR A C   1 
ATOM   2700  O  O   . THR A 1 379 ? 2.299   2.918   -7.513  1.00 36.28  ? 379  THR A O   1 
ATOM   2701  C  CB  . THR A 1 379 ? 1.475   2.311   -10.544 1.00 50.51  ? 379  THR A CB  1 
ATOM   2702  O  OG1 . THR A 1 379 ? 1.564   1.456   -11.690 1.00 59.55  ? 379  THR A OG1 1 
ATOM   2703  C  CG2 . THR A 1 379 ? 1.263   3.760   -10.993 1.00 66.23  ? 379  THR A CG2 1 
ATOM   2704  N  N   . PRO A 1 380 ? 3.358   4.366   -8.889  1.00 39.79  ? 380  PRO A N   1 
ATOM   2705  C  CA  . PRO A 1 380 ? 3.237   5.473   -7.929  1.00 43.23  ? 380  PRO A CA  1 
ATOM   2706  C  C   . PRO A 1 380 ? 1.776   5.759   -7.518  1.00 46.19  ? 380  PRO A C   1 
ATOM   2707  O  O   . PRO A 1 380 ? 0.842   5.584   -8.319  1.00 29.93  ? 380  PRO A O   1 
ATOM   2708  C  CB  . PRO A 1 380 ? 3.839   6.655   -8.690  1.00 33.79  ? 380  PRO A CB  1 
ATOM   2709  C  CG  . PRO A 1 380 ? 4.866   6.011   -9.590  1.00 39.55  ? 380  PRO A CG  1 
ATOM   2710  C  CD  . PRO A 1 380 ? 4.263   4.691   -10.007 1.00 32.90  ? 380  PRO A CD  1 
ATOM   2711  N  N   . GLY A 1 381 ? 1.593   6.189   -6.271  1.00 41.03  ? 381  GLY A N   1 
ATOM   2712  C  CA  . GLY A 1 381 ? 0.270   6.404   -5.718  1.00 37.99  ? 381  GLY A CA  1 
ATOM   2713  C  C   . GLY A 1 381 ? 0.224   6.034   -4.249  1.00 42.43  ? 381  GLY A C   1 
ATOM   2714  O  O   . GLY A 1 381 ? 1.263   5.765   -3.645  1.00 48.20  ? 381  GLY A O   1 
ATOM   2715  N  N   . LEU A 1 382 ? -0.967  6.030   -3.655  1.00 37.34  ? 382  LEU A N   1 
ATOM   2716  C  CA  . LEU A 1 382 ? -1.065  5.658   -2.255  1.00 40.67  ? 382  LEU A CA  1 
ATOM   2717  C  C   . LEU A 1 382 ? -2.034  4.511   -2.074  1.00 39.87  ? 382  LEU A C   1 
ATOM   2718  O  O   . LEU A 1 382 ? -3.089  4.478   -2.703  1.00 28.56  ? 382  LEU A O   1 
ATOM   2719  C  CB  . LEU A 1 382 ? -1.423  6.858   -1.372  1.00 52.04  ? 382  LEU A CB  1 
ATOM   2720  C  CG  . LEU A 1 382 ? -2.829  7.452   -1.367  1.00 70.79  ? 382  LEU A CG  1 
ATOM   2721  C  CD1 . LEU A 1 382 ? -3.846  6.519   -0.708  1.00 83.44  ? 382  LEU A CD1 1 
ATOM   2722  C  CD2 . LEU A 1 382 ? -2.796  8.781   -0.635  1.00 78.59  ? 382  LEU A CD2 1 
ATOM   2723  N  N   . TYR A 1 383 ? -1.663  3.572   -1.206  1.00 45.45  ? 383  TYR A N   1 
ATOM   2724  C  CA  . TYR A 1 383 ? -2.413  2.334   -1.053  1.00 34.04  ? 383  TYR A CA  1 
ATOM   2725  C  C   . TYR A 1 383 ? -2.671  1.908   0.397   1.00 38.48  ? 383  TYR A C   1 
ATOM   2726  O  O   . TYR A 1 383 ? -1.963  2.289   1.318   1.00 46.40  ? 383  TYR A O   1 
ATOM   2727  C  CB  . TYR A 1 383 ? -1.684  1.214   -1.768  1.00 35.80  ? 383  TYR A CB  1 
ATOM   2728  C  CG  . TYR A 1 383 ? -1.252  1.539   -3.175  1.00 44.15  ? 383  TYR A CG  1 
ATOM   2729  C  CD1 . TYR A 1 383 ? -0.157  2.367   -3.418  1.00 43.99  ? 383  TYR A CD1 1 
ATOM   2730  C  CD2 . TYR A 1 383 ? -1.918  0.987   -4.269  1.00 42.89  ? 383  TYR A CD2 1 
ATOM   2731  C  CE1 . TYR A 1 383 ? 0.254   2.656   -4.719  1.00 44.05  ? 383  TYR A CE1 1 
ATOM   2732  C  CE2 . TYR A 1 383 ? -1.518  1.264   -5.571  1.00 41.32  ? 383  TYR A CE2 1 
ATOM   2733  C  CZ  . TYR A 1 383 ? -0.432  2.098   -5.794  1.00 47.32  ? 383  TYR A CZ  1 
ATOM   2734  O  OH  . TYR A 1 383 ? -0.041  2.364   -7.092  1.00 34.74  ? 383  TYR A OH  1 
ATOM   2735  N  N   . SER A 1 384 ? -3.709  1.104   0.582   1.00 47.29  ? 384  SER A N   1 
ATOM   2736  C  CA  . SER A 1 384 ? -3.960  0.451   1.857   1.00 44.18  ? 384  SER A CA  1 
ATOM   2737  C  C   . SER A 1 384 ? -3.596  -1.018  1.719   1.00 46.98  ? 384  SER A C   1 
ATOM   2738  O  O   . SER A 1 384 ? -4.279  -1.795  1.043   1.00 29.90  ? 384  SER A O   1 
ATOM   2739  C  CB  . SER A 1 384 ? -5.422  0.607   2.272   1.00 34.49  ? 384  SER A CB  1 
ATOM   2740  O  OG  . SER A 1 384 ? -5.608  1.821   2.976   1.00 72.52  ? 384  SER A OG  1 
ATOM   2741  N  N   . VAL A 1 385 ? -2.493  -1.392  2.343   1.00 50.32  ? 385  VAL A N   1 
ATOM   2742  C  CA  . VAL A 1 385 ? -2.015  -2.762  2.255   1.00 46.64  ? 385  VAL A CA  1 
ATOM   2743  C  C   . VAL A 1 385 ? -2.374  -3.501  3.531   1.00 41.96  ? 385  VAL A C   1 
ATOM   2744  O  O   . VAL A 1 385 ? -2.312  -2.923  4.619   1.00 40.25  ? 385  VAL A O   1 
ATOM   2745  C  CB  . VAL A 1 385 ? -0.489  -2.793  2.073   1.00 31.83  ? 385  VAL A CB  1 
ATOM   2746  C  CG1 . VAL A 1 385 ? -0.042  -4.158  1.623   1.00 23.83  ? 385  VAL A CG1 1 
ATOM   2747  C  CG2 . VAL A 1 385 ? -0.063  -1.732  1.076   1.00 30.44  ? 385  VAL A CG2 1 
ATOM   2748  N  N   . HIS A 1 386 ? -2.765  -4.766  3.401   1.00 28.79  ? 386  HIS A N   1 
ATOM   2749  C  CA  . HIS A 1 386 ? -2.975  -5.622  4.569   1.00 25.72  ? 386  HIS A CA  1 
ATOM   2750  C  C   . HIS A 1 386 ? -2.597  -7.065  4.304   1.00 31.60  ? 386  HIS A C   1 
ATOM   2751  O  O   . HIS A 1 386 ? -2.489  -7.486  3.147   1.00 26.31  ? 386  HIS A O   1 
ATOM   2752  C  CB  . HIS A 1 386 ? -4.414  -5.521  5.108   1.00 55.76  ? 386  HIS A CB  1 
ATOM   2753  C  CG  . HIS A 1 386 ? -5.436  -6.311  4.336   1.00 66.44  ? 386  HIS A CG  1 
ATOM   2754  N  ND1 . HIS A 1 386 ? -5.148  -7.010  3.188   1.00 78.96  ? 386  HIS A ND1 1 
ATOM   2755  C  CD2 . HIS A 1 386 ? -6.763  -6.487  4.562   1.00 69.35  ? 386  HIS A CD2 1 
ATOM   2756  C  CE1 . HIS A 1 386 ? -6.249  -7.595  2.742   1.00 58.62  ? 386  HIS A CE1 1 
ATOM   2757  N  NE2 . HIS A 1 386 ? -7.239  -7.294  3.558   1.00 53.83  ? 386  HIS A NE2 1 
ATOM   2758  N  N   . ALA A 1 387 ? -2.409  -7.823  5.380   1.00 33.91  ? 387  ALA A N   1 
ATOM   2759  C  CA  . ALA A 1 387 ? -1.927  -9.188  5.265   1.00 33.77  ? 387  ALA A CA  1 
ATOM   2760  C  C   . ALA A 1 387 ? -2.835  -10.145 6.006   1.00 41.26  ? 387  ALA A C   1 
ATOM   2761  O  O   . ALA A 1 387 ? -3.434  -9.802  7.029   1.00 41.55  ? 387  ALA A O   1 
ATOM   2762  C  CB  . ALA A 1 387 ? -0.493  -9.294  5.791   1.00 35.92  ? 387  ALA A CB  1 
ATOM   2763  N  N   . SER A 1 388 ? -2.938  -11.357 5.483   1.00 23.50  ? 388  SER A N   1 
ATOM   2764  C  CA  . SER A 1 388 ? -3.716  -12.374 6.156   1.00 31.41  ? 388  SER A CA  1 
ATOM   2765  C  C   . SER A 1 388 ? -3.075  -13.745 5.971   1.00 42.14  ? 388  SER A C   1 
ATOM   2766  O  O   . SER A 1 388 ? -2.211  -13.940 5.104   1.00 34.12  ? 388  SER A O   1 
ATOM   2767  C  CB  . SER A 1 388 ? -5.145  -12.371 5.628   1.00 36.32  ? 388  SER A CB  1 
ATOM   2768  O  OG  . SER A 1 388 ? -5.156  -12.538 4.221   1.00 41.93  ? 388  SER A OG  1 
ATOM   2769  N  N   . ALA A 1 389 ? -3.497  -14.685 6.808   1.00 46.43  ? 389  ALA A N   1 
ATOM   2770  C  CA  . ALA A 1 389 ? -2.990  -16.048 6.778   1.00 37.28  ? 389  ALA A CA  1 
ATOM   2771  C  C   . ALA A 1 389 ? -3.895  -16.941 7.624   1.00 43.52  ? 389  ALA A C   1 
ATOM   2772  O  O   . ALA A 1 389 ? -4.424  -16.517 8.654   1.00 55.75  ? 389  ALA A O   1 
ATOM   2773  C  CB  . ALA A 1 389 ? -1.543  -16.101 7.292   1.00 27.10  ? 389  ALA A CB  1 
ATOM   2774  N  N   . PHE A 1 390 ? -4.074  -18.177 7.176   1.00 44.27  ? 390  PHE A N   1 
ATOM   2775  C  CA  . PHE A 1 390 ? -4.849  -19.165 7.914   1.00 59.19  ? 390  PHE A CA  1 
ATOM   2776  C  C   . PHE A 1 390 ? -4.283  -19.335 9.325   1.00 57.35  ? 390  PHE A C   1 
ATOM   2777  O  O   . PHE A 1 390 ? -3.071  -19.450 9.508   1.00 58.46  ? 390  PHE A O   1 
ATOM   2778  C  CB  . PHE A 1 390 ? -4.832  -20.497 7.154   1.00 73.89  ? 390  PHE A CB  1 
ATOM   2779  C  CG  . PHE A 1 390 ? -5.516  -21.627 7.871   1.00 94.00  ? 390  PHE A CG  1 
ATOM   2780  C  CD1 . PHE A 1 390 ? -4.777  -22.651 8.445   1.00 103.69 ? 390  PHE A CD1 1 
ATOM   2781  C  CD2 . PHE A 1 390 ? -6.894  -21.676 7.961   1.00 103.67 ? 390  PHE A CD2 1 
ATOM   2782  C  CE1 . PHE A 1 390 ? -5.403  -23.702 9.107   1.00 107.80 ? 390  PHE A CE1 1 
ATOM   2783  C  CE2 . PHE A 1 390 ? -7.524  -22.724 8.621   1.00 109.69 ? 390  PHE A CE2 1 
ATOM   2784  C  CZ  . PHE A 1 390 ? -6.776  -23.737 9.195   1.00 108.21 ? 390  PHE A CZ  1 
ATOM   2785  N  N   . GLY A 1 391 ? -5.158  -19.333 10.325  1.00 51.76  ? 391  GLY A N   1 
ATOM   2786  C  CA  . GLY A 1 391 ? -4.715  -19.488 11.696  1.00 51.74  ? 391  GLY A CA  1 
ATOM   2787  C  C   . GLY A 1 391 ? -4.231  -18.171 12.260  1.00 48.05  ? 391  GLY A C   1 
ATOM   2788  O  O   . GLY A 1 391 ? -3.714  -18.111 13.376  1.00 39.34  ? 391  GLY A O   1 
ATOM   2789  N  N   . TYR A 1 392 ? -4.402  -17.108 11.482  1.00 52.29  ? 392  TYR A N   1 
ATOM   2790  C  CA  . TYR A 1 392 ? -4.018  -15.773 11.921  1.00 53.53  ? 392  TYR A CA  1 
ATOM   2791  C  C   . TYR A 1 392 ? -5.121  -14.763 11.693  1.00 50.74  ? 392  TYR A C   1 
ATOM   2792  O  O   . TYR A 1 392 ? -5.809  -14.806 10.678  1.00 54.43  ? 392  TYR A O   1 
ATOM   2793  C  CB  . TYR A 1 392 ? -2.744  -15.317 11.216  1.00 52.81  ? 392  TYR A CB  1 
ATOM   2794  C  CG  . TYR A 1 392 ? -1.527  -16.079 11.654  1.00 62.06  ? 392  TYR A CG  1 
ATOM   2795  C  CD1 . TYR A 1 392 ? -0.718  -15.599 12.686  1.00 70.68  ? 392  TYR A CD1 1 
ATOM   2796  C  CD2 . TYR A 1 392 ? -1.189  -17.286 11.058  1.00 48.35  ? 392  TYR A CD2 1 
ATOM   2797  C  CE1 . TYR A 1 392 ? 0.401   -16.297 13.105  1.00 65.93  ? 392  TYR A CE1 1 
ATOM   2798  C  CE2 . TYR A 1 392 ? -0.071  -17.992 11.469  1.00 55.23  ? 392  TYR A CE2 1 
ATOM   2799  C  CZ  . TYR A 1 392 ? 0.721   -17.494 12.493  1.00 66.60  ? 392  TYR A CZ  1 
ATOM   2800  O  OH  . TYR A 1 392 ? 1.840   -18.194 12.904  1.00 69.22  ? 392  TYR A OH  1 
ATOM   2801  N  N   . GLN A 1 393 ? -5.287  -13.864 12.657  1.00 61.41  ? 393  GLN A N   1 
ATOM   2802  C  CA  . GLN A 1 393 ? -6.207  -12.745 12.512  1.00 57.39  ? 393  GLN A CA  1 
ATOM   2803  C  C   . GLN A 1 393 ? -5.632  -11.797 11.466  1.00 57.53  ? 393  GLN A C   1 
ATOM   2804  O  O   . GLN A 1 393 ? -4.461  -11.414 11.527  1.00 47.67  ? 393  GLN A O   1 
ATOM   2805  C  CB  . GLN A 1 393 ? -6.430  -12.031 13.849  1.00 37.13  ? 393  GLN A CB  1 
ATOM   2806  C  CG  . GLN A 1 393 ? -6.842  -12.971 14.972  1.00 53.31  ? 393  GLN A CG  1 
ATOM   2807  C  CD  . GLN A 1 393 ? -7.139  -12.260 16.288  1.00 70.04  ? 393  GLN A CD  1 
ATOM   2808  O  OE1 . GLN A 1 393 ? -6.719  -11.119 16.511  1.00 69.21  ? 393  GLN A OE1 1 
ATOM   2809  N  NE2 . GLN A 1 393 ? -7.867  -12.943 17.173  1.00 69.23  ? 393  GLN A NE2 1 
ATOM   2810  N  N   . THR A 1 394 ? -6.462  -11.453 10.489  1.00 59.52  ? 394  THR A N   1 
ATOM   2811  C  CA  . THR A 1 394 ? -6.039  -10.598 9.396   1.00 58.55  ? 394  THR A CA  1 
ATOM   2812  C  C   . THR A 1 394 ? -5.609  -9.254  9.945   1.00 54.79  ? 394  THR A C   1 
ATOM   2813  O  O   . THR A 1 394 ? -6.370  -8.606  10.655  1.00 59.12  ? 394  THR A O   1 
ATOM   2814  C  CB  . THR A 1 394 ? -7.175  -10.382 8.391   1.00 51.76  ? 394  THR A CB  1 
ATOM   2815  O  OG1 . THR A 1 394 ? -7.639  -11.649 7.916   1.00 48.77  ? 394  THR A OG1 1 
ATOM   2816  C  CG2 . THR A 1 394 ? -6.686  -9.555  7.217   1.00 59.47  ? 394  THR A CG2 1 
ATOM   2817  N  N   . SER A 1 395 ? -4.388  -8.841  9.620   1.00 45.68  ? 395  SER A N   1 
ATOM   2818  C  CA  . SER A 1 395 ? -3.848  -7.590  10.138  1.00 47.06  ? 395  SER A CA  1 
ATOM   2819  C  C   . SER A 1 395 ? -4.739  -6.398  9.848   1.00 54.91  ? 395  SER A C   1 
ATOM   2820  O  O   . SER A 1 395 ? -5.532  -6.403  8.896   1.00 51.98  ? 395  SER A O   1 
ATOM   2821  C  CB  . SER A 1 395 ? -2.489  -7.295  9.519   1.00 41.51  ? 395  SER A CB  1 
ATOM   2822  O  OG  . SER A 1 395 ? -2.651  -6.857  8.181   1.00 40.05  ? 395  SER A OG  1 
ATOM   2823  N  N   . ALA A 1 396 ? -4.586  -5.365  10.672  1.00 48.29  ? 396  ALA A N   1 
ATOM   2824  C  CA  . ALA A 1 396 ? -5.170  -4.072  10.372  1.00 41.62  ? 396  ALA A CA  1 
ATOM   2825  C  C   . ALA A 1 396 ? -4.447  -3.524  9.142   1.00 55.19  ? 396  ALA A C   1 
ATOM   2826  O  O   . ALA A 1 396 ? -3.297  -3.884  8.877   1.00 63.99  ? 396  ALA A O   1 
ATOM   2827  C  CB  . ALA A 1 396 ? -5.013  -3.129  11.556  1.00 30.87  ? 396  ALA A CB  1 
ATOM   2828  N  N   . PRO A 1 397 ? -5.117  -2.646  8.388   1.00 49.48  ? 397  PRO A N   1 
ATOM   2829  C  CA  . PRO A 1 397 ? -4.552  -2.125  7.143   1.00 40.01  ? 397  PRO A CA  1 
ATOM   2830  C  C   . PRO A 1 397 ? -3.529  -1.029  7.403   1.00 43.80  ? 397  PRO A C   1 
ATOM   2831  O  O   . PRO A 1 397 ? -3.622  -0.306  8.396   1.00 44.80  ? 397  PRO A O   1 
ATOM   2832  C  CB  . PRO A 1 397 ? -5.773  -1.528  6.419   1.00 46.19  ? 397  PRO A CB  1 
ATOM   2833  C  CG  . PRO A 1 397 ? -6.990  -1.852  7.295   1.00 54.41  ? 397  PRO A CG  1 
ATOM   2834  C  CD  . PRO A 1 397 ? -6.455  -2.092  8.663   1.00 56.70  ? 397  PRO A CD  1 
ATOM   2835  N  N   . GLN A 1 398 ? -2.557  -0.915  6.508   1.00 49.49  ? 398  GLN A N   1 
ATOM   2836  C  CA  . GLN A 1 398 ? -1.603  0.178   6.567   1.00 50.02  ? 398  GLN A CA  1 
ATOM   2837  C  C   . GLN A 1 398 ? -1.673  0.974   5.262   1.00 48.16  ? 398  GLN A C   1 
ATOM   2838  O  O   . GLN A 1 398 ? -1.817  0.415   4.167   1.00 47.41  ? 398  GLN A O   1 
ATOM   2839  C  CB  . GLN A 1 398 ? -0.174  -0.328  6.865   1.00 46.98  ? 398  GLN A CB  1 
ATOM   2840  C  CG  . GLN A 1 398 ? 0.001   -0.958  8.274   1.00 32.97  ? 398  GLN A CG  1 
ATOM   2841  C  CD  . GLN A 1 398 ? 1.364   -1.632  8.512   1.00 45.35  ? 398  GLN A CD  1 
ATOM   2842  O  OE1 . GLN A 1 398 ? 2.416   -1.058  8.245   1.00 50.39  ? 398  GLN A OE1 1 
ATOM   2843  N  NE2 . GLN A 1 398 ? 1.336   -2.853  9.035   1.00 51.28  ? 398  GLN A NE2 1 
ATOM   2844  N  N   . GLN A 1 399 ? -1.601  2.291   5.399   1.00 55.03  ? 399  GLN A N   1 
ATOM   2845  C  CA  . GLN A 1 399 ? -1.599  3.198   4.264   1.00 55.73  ? 399  GLN A CA  1 
ATOM   2846  C  C   . GLN A 1 399 ? -0.168  3.613   3.949   1.00 59.55  ? 399  GLN A C   1 
ATOM   2847  O  O   . GLN A 1 399 ? 0.595   3.981   4.837   1.00 67.30  ? 399  GLN A O   1 
ATOM   2848  C  CB  . GLN A 1 399 ? -2.446  4.418   4.586   1.00 60.52  ? 399  GLN A CB  1 
ATOM   2849  C  CG  . GLN A 1 399 ? -2.118  5.640   3.762   1.00 80.41  ? 399  GLN A CG  1 
ATOM   2850  C  CD  . GLN A 1 399 ? -2.548  6.922   4.450   1.00 96.74  ? 399  GLN A CD  1 
ATOM   2851  O  OE1 . GLN A 1 399 ? -1.927  7.361   5.417   1.00 102.82 ? 399  GLN A OE1 1 
ATOM   2852  N  NE2 . GLN A 1 399 ? -3.621  7.525   3.957   1.00 102.25 ? 399  GLN A NE2 1 
ATOM   2853  N  N   . VAL A 1 400 ? 0.198   3.543   2.679   1.00 53.80  ? 400  VAL A N   1 
ATOM   2854  C  CA  . VAL A 1 400 ? 1.549   3.872   2.272   1.00 45.60  ? 400  VAL A CA  1 
ATOM   2855  C  C   . VAL A 1 400 ? 1.537   4.684   0.991   1.00 43.62  ? 400  VAL A C   1 
ATOM   2856  O  O   . VAL A 1 400 ? 0.778   4.398   0.061   1.00 42.19  ? 400  VAL A O   1 
ATOM   2857  C  CB  . VAL A 1 400 ? 2.401   2.601   2.064   1.00 52.01  ? 400  VAL A CB  1 
ATOM   2858  C  CG1 . VAL A 1 400 ? 1.888   1.806   0.883   1.00 52.98  ? 400  VAL A CG1 1 
ATOM   2859  C  CG2 . VAL A 1 400 ? 3.862   2.972   1.859   1.00 67.45  ? 400  VAL A CG2 1 
ATOM   2860  N  N   . ARG A 1 401 ? 2.381   5.706   0.949   1.00 53.83  ? 401  ARG A N   1 
ATOM   2861  C  CA  . ARG A 1 401 ? 2.528   6.524   -0.247  1.00 57.02  ? 401  ARG A CA  1 
ATOM   2862  C  C   . ARG A 1 401 ? 3.683   5.978   -1.090  1.00 35.12  ? 401  ARG A C   1 
ATOM   2863  O  O   . ARG A 1 401 ? 4.855   6.120   -0.744  1.00 39.11  ? 401  ARG A O   1 
ATOM   2864  C  CB  . ARG A 1 401 ? 2.738   7.998   0.133   1.00 53.31  ? 401  ARG A CB  1 
ATOM   2865  C  CG  . ARG A 1 401 ? 3.088   8.899   -1.029  1.00 60.97  ? 401  ARG A CG  1 
ATOM   2866  C  CD  . ARG A 1 401 ? 3.779   10.160  -0.537  1.00 77.01  ? 401  ARG A CD  1 
ATOM   2867  N  NE  . ARG A 1 401 ? 2.898   10.920  0.315   1.00 90.57  ? 401  ARG A NE  1 
ATOM   2868  C  CZ  . ARG A 1 401 ? 3.149   11.387  1.534   1.00 98.41  ? 401  ARG A CZ  1 
ATOM   2869  N  NH1 . ARG A 1 401 ? 4.316   11.219  2.146   1.00 105.89 ? 401  ARG A NH1 1 
ATOM   2870  N  NH2 . ARG A 1 401 ? 2.180   12.051  2.139   1.00 93.57  ? 401  ARG A NH2 1 
ATOM   2871  N  N   . VAL A 1 402 ? 3.345   5.328   -2.190  1.00 35.83  ? 402  VAL A N   1 
ATOM   2872  C  CA  . VAL A 1 402 ? 4.377   4.780   -3.063  1.00 42.74  ? 402  VAL A CA  1 
ATOM   2873  C  C   . VAL A 1 402 ? 4.879   5.791   -4.082  1.00 53.83  ? 402  VAL A C   1 
ATOM   2874  O  O   . VAL A 1 402 ? 4.207   6.081   -5.082  1.00 30.31  ? 402  VAL A O   1 
ATOM   2875  C  CB  . VAL A 1 402 ? 3.920   3.535   -3.819  1.00 23.06  ? 402  VAL A CB  1 
ATOM   2876  C  CG1 . VAL A 1 402 ? 4.991   3.122   -4.818  1.00 18.77  ? 402  VAL A CG1 1 
ATOM   2877  C  CG2 . VAL A 1 402 ? 3.621   2.426   -2.846  1.00 24.57  ? 402  VAL A CG2 1 
ATOM   2878  N  N   . THR A 1 403 ? 6.056   6.339   -3.790  1.00 70.24  ? 403  THR A N   1 
ATOM   2879  C  CA  . THR A 1 403 ? 6.847   7.079   -4.758  1.00 72.17  ? 403  THR A CA  1 
ATOM   2880  C  C   . THR A 1 403 ? 7.924   6.123   -5.214  1.00 73.08  ? 403  THR A C   1 
ATOM   2881  O  O   . THR A 1 403 ? 8.566   5.466   -4.391  1.00 79.93  ? 403  THR A O   1 
ATOM   2882  C  CB  . THR A 1 403 ? 7.507   8.341   -4.149  1.00 69.58  ? 403  THR A CB  1 
ATOM   2883  O  OG1 . THR A 1 403 ? 8.452   8.877   -5.081  1.00 82.26  ? 403  THR A OG1 1 
ATOM   2884  C  CG2 . THR A 1 403 ? 8.232   8.016   -2.849  1.00 61.04  ? 403  THR A CG2 1 
ATOM   2885  N  N   . ASN A 1 404 ? 8.099   6.002   -6.523  1.00 70.61  ? 404  ASN A N   1 
ATOM   2886  C  CA  . ASN A 1 404 ? 9.126   5.103   -7.028  1.00 71.74  ? 404  ASN A CA  1 
ATOM   2887  C  C   . ASN A 1 404 ? 10.343  5.909   -7.432  1.00 70.00  ? 404  ASN A C   1 
ATOM   2888  O  O   . ASN A 1 404 ? 10.810  5.841   -8.575  1.00 44.21  ? 404  ASN A O   1 
ATOM   2889  C  CB  . ASN A 1 404 ? 8.601   4.238   -8.179  1.00 65.50  ? 404  ASN A CB  1 
ATOM   2890  C  CG  . ASN A 1 404 ? 7.597   3.200   -7.708  1.00 43.59  ? 404  ASN A CG  1 
ATOM   2891  O  OD1 . ASN A 1 404 ? 7.783   2.570   -6.663  1.00 37.19  ? 404  ASN A OD1 1 
ATOM   2892  N  ND2 . ASN A 1 404 ? 6.519   3.030   -8.467  1.00 20.10  ? 404  ASN A ND2 1 
ATOM   2893  N  N   . ASP A 1 405 ? 10.840  6.675   -6.464  1.00 82.18  ? 405  ASP A N   1 
ATOM   2894  C  CA  . ASP A 1 405 ? 11.979  7.565   -6.655  1.00 94.43  ? 405  ASP A CA  1 
ATOM   2895  C  C   . ASP A 1 405 ? 13.261  6.938   -6.108  1.00 72.09  ? 405  ASP A C   1 
ATOM   2896  O  O   . ASP A 1 405 ? 14.322  7.012   -6.750  1.00 53.29  ? 405  ASP A O   1 
ATOM   2897  C  CB  . ASP A 1 405 ? 11.712  8.919   -5.977  1.00 108.85 ? 405  ASP A CB  1 
ATOM   2898  C  CG  . ASP A 1 405 ? 12.692  10.006  -6.413  1.00 119.70 ? 405  ASP A CG  1 
ATOM   2899  O  OD1 . ASP A 1 405 ? 13.827  9.684   -6.834  1.00 111.72 ? 405  ASP A OD1 1 
ATOM   2900  O  OD2 . ASP A 1 405 ? 12.325  11.197  -6.330  1.00 132.92 ? 405  ASP A OD2 1 
ATOM   2901  N  N   . ASN A 1 406 ? 13.164  6.320   -4.930  1.00 55.91  ? 406  ASN A N   1 
ATOM   2902  C  CA  . ASN A 1 406 ? 14.344  5.726   -4.313  1.00 63.85  ? 406  ASN A CA  1 
ATOM   2903  C  C   . ASN A 1 406 ? 14.700  4.359   -4.862  1.00 56.88  ? 406  ASN A C   1 
ATOM   2904  O  O   . ASN A 1 406 ? 13.888  3.693   -5.512  1.00 27.63  ? 406  ASN A O   1 
ATOM   2905  C  CB  . ASN A 1 406 ? 14.247  5.643   -2.791  1.00 76.51  ? 406  ASN A CB  1 
ATOM   2906  C  CG  . ASN A 1 406 ? 15.476  4.986   -2.176  1.00 80.41  ? 406  ASN A CG  1 
ATOM   2907  O  OD1 . ASN A 1 406 ? 16.586  5.515   -2.263  1.00 70.38  ? 406  ASN A OD1 1 
ATOM   2908  N  ND2 . ASN A 1 406 ? 15.288  3.810   -1.583  1.00 85.35  ? 406  ASN A ND2 1 
ATOM   2909  N  N   . GLN A 1 407 ? 15.929  3.953   -4.561  1.00 68.34  ? 407  GLN A N   1 
ATOM   2910  C  CA  . GLN A 1 407 ? 16.540  2.797   -5.182  1.00 69.69  ? 407  GLN A CA  1 
ATOM   2911  C  C   . GLN A 1 407 ? 15.854  1.483   -4.842  1.00 63.42  ? 407  GLN A C   1 
ATOM   2912  O  O   . GLN A 1 407 ? 15.851  0.561   -5.653  1.00 65.18  ? 407  GLN A O   1 
ATOM   2913  C  CB  . GLN A 1 407 ? 18.025  2.735   -4.828  1.00 77.03  ? 407  GLN A CB  1 
ATOM   2914  C  CG  . GLN A 1 407 ? 18.909  3.536   -5.768  1.00 75.39  ? 407  GLN A CG  1 
ATOM   2915  C  CD  . GLN A 1 407 ? 20.379  3.469   -5.387  1.00 90.64  ? 407  GLN A CD  1 
ATOM   2916  O  OE1 . GLN A 1 407 ? 20.723  3.302   -4.215  1.00 93.00  ? 407  GLN A OE1 1 
ATOM   2917  N  NE2 . GLN A 1 407 ? 21.257  3.605   -6.379  1.00 100.99 ? 407  GLN A NE2 1 
ATOM   2918  N  N   . GLU A 1 408 ? 15.274  1.390   -3.652  1.00 57.32  ? 408  GLU A N   1 
ATOM   2919  C  CA  . GLU A 1 408 ? 14.655  0.137   -3.236  1.00 50.30  ? 408  GLU A CA  1 
ATOM   2920  C  C   . GLU A 1 408 ? 13.238  0.301   -2.685  1.00 57.29  ? 408  GLU A C   1 
ATOM   2921  O  O   . GLU A 1 408 ? 12.903  1.320   -2.068  1.00 63.10  ? 408  GLU A O   1 
ATOM   2922  C  CB  . GLU A 1 408 ? 15.571  -0.633  -2.275  1.00 45.71  ? 408  GLU A CB  1 
ATOM   2923  C  CG  . GLU A 1 408 ? 16.854  -1.087  -2.963  1.00 59.84  ? 408  GLU A CG  1 
ATOM   2924  C  CD  . GLU A 1 408 ? 17.723  -1.999  -2.120  1.00 66.58  ? 408  GLU A CD  1 
ATOM   2925  O  OE1 . GLU A 1 408 ? 18.956  -1.805  -2.149  1.00 50.78  ? 408  GLU A OE1 1 
ATOM   2926  O  OE2 . GLU A 1 408 ? 17.188  -2.906  -1.441  1.00 82.40  ? 408  GLU A OE2 1 
ATOM   2927  N  N   . ALA A 1 409 ? 12.410  -0.711  -2.950  1.00 55.42  ? 409  ALA A N   1 
ATOM   2928  C  CA  . ALA A 1 409 ? 11.007  -0.717  -2.568  1.00 35.45  ? 409  ALA A CA  1 
ATOM   2929  C  C   . ALA A 1 409 ? 10.838  -0.353  -1.103  1.00 48.91  ? 409  ALA A C   1 
ATOM   2930  O  O   . ALA A 1 409 ? 11.641  -0.743  -0.248  1.00 42.87  ? 409  ALA A O   1 
ATOM   2931  C  CB  . ALA A 1 409 ? 10.389  -2.072  -2.847  1.00 31.43  ? 409  ALA A CB  1 
ATOM   2932  N  N   . LEU A 1 410 ? 9.785   0.406   -0.833  1.00 49.23  ? 410  LEU A N   1 
ATOM   2933  C  CA  . LEU A 1 410 ? 9.469   0.847   0.509   1.00 35.99  ? 410  LEU A CA  1 
ATOM   2934  C  C   . LEU A 1 410 ? 9.196   -0.340  1.426   1.00 34.72  ? 410  LEU A C   1 
ATOM   2935  O  O   . LEU A 1 410 ? 8.372   -1.206  1.105   1.00 30.53  ? 410  LEU A O   1 
ATOM   2936  C  CB  . LEU A 1 410 ? 8.260   1.772   0.465   1.00 45.73  ? 410  LEU A CB  1 
ATOM   2937  C  CG  . LEU A 1 410 ? 8.638   3.180   0.034   1.00 64.21  ? 410  LEU A CG  1 
ATOM   2938  C  CD1 . LEU A 1 410 ? 7.451   3.896   -0.592  1.00 78.20  ? 410  LEU A CD1 1 
ATOM   2939  C  CD2 . LEU A 1 410 ? 9.190   3.932   1.241   1.00 67.61  ? 410  LEU A CD2 1 
ATOM   2940  N  N   . ARG A 1 411 ? 9.897   -0.380  2.560   1.00 38.35  ? 411  ARG A N   1 
ATOM   2941  C  CA  . ARG A 1 411 ? 9.707   -1.448  3.534   1.00 38.14  ? 411  ARG A CA  1 
ATOM   2942  C  C   . ARG A 1 411 ? 8.386   -1.288  4.261   1.00 38.99  ? 411  ARG A C   1 
ATOM   2943  O  O   . ARG A 1 411 ? 7.955   -0.173  4.540   1.00 39.35  ? 411  ARG A O   1 
ATOM   2944  C  CB  . ARG A 1 411 ? 10.833  -1.485  4.556   1.00 23.51  ? 411  ARG A CB  1 
ATOM   2945  C  CG  . ARG A 1 411 ? 10.562  -2.496  5.649   1.00 32.41  ? 411  ARG A CG  1 
ATOM   2946  C  CD  . ARG A 1 411 ? 10.793  -3.917  5.167   1.00 25.60  ? 411  ARG A CD  1 
ATOM   2947  N  NE  . ARG A 1 411 ? 12.138  -4.353  5.509   1.00 34.21  ? 411  ARG A NE  1 
ATOM   2948  C  CZ  . ARG A 1 411 ? 12.451  -5.050  6.602   1.00 43.70  ? 411  ARG A CZ  1 
ATOM   2949  N  NH1 . ARG A 1 411 ? 11.505  -5.418  7.452   1.00 43.08  ? 411  ARG A NH1 1 
ATOM   2950  N  NH2 . ARG A 1 411 ? 13.710  -5.401  6.841   1.00 43.60  ? 411  ARG A NH2 1 
ATOM   2951  N  N   . LEU A 1 412 ? 7.747   -2.407  4.573   1.00 37.00  ? 412  LEU A N   1 
ATOM   2952  C  CA  . LEU A 1 412 ? 6.448   -2.383  5.220   1.00 37.43  ? 412  LEU A CA  1 
ATOM   2953  C  C   . LEU A 1 412 ? 6.164   -3.789  5.710   1.00 40.57  ? 412  LEU A C   1 
ATOM   2954  O  O   . LEU A 1 412 ? 5.967   -4.700  4.914   1.00 34.87  ? 412  LEU A O   1 
ATOM   2955  C  CB  . LEU A 1 412 ? 5.365   -1.934  4.232   1.00 41.05  ? 412  LEU A CB  1 
ATOM   2956  C  CG  . LEU A 1 412 ? 3.944   -1.735  4.774   1.00 47.80  ? 412  LEU A CG  1 
ATOM   2957  C  CD1 . LEU A 1 412 ? 3.879   -0.511  5.661   1.00 59.59  ? 412  LEU A CD1 1 
ATOM   2958  C  CD2 . LEU A 1 412 ? 2.937   -1.611  3.645   1.00 28.96  ? 412  LEU A CD2 1 
ATOM   2959  N  N   . ASP A 1 413 ? 6.165   -3.966  7.027   1.00 48.51  ? 413  ASP A N   1 
ATOM   2960  C  CA  . ASP A 1 413 ? 6.054   -5.296  7.622   1.00 38.54  ? 413  ASP A CA  1 
ATOM   2961  C  C   . ASP A 1 413 ? 4.712   -5.503  8.286   1.00 37.99  ? 413  ASP A C   1 
ATOM   2962  O  O   . ASP A 1 413 ? 3.934   -4.571  8.453   1.00 42.00  ? 413  ASP A O   1 
ATOM   2963  C  CB  . ASP A 1 413 ? 7.149   -5.521  8.673   1.00 37.17  ? 413  ASP A CB  1 
ATOM   2964  C  CG  . ASP A 1 413 ? 8.545   -5.518  8.085   1.00 37.49  ? 413  ASP A CG  1 
ATOM   2965  O  OD1 . ASP A 1 413 ? 8.693   -5.502  6.843   1.00 40.94  ? 413  ASP A OD1 1 
ATOM   2966  O  OD2 . ASP A 1 413 ? 9.499   -5.543  8.884   1.00 43.16  ? 413  ASP A OD2 1 
ATOM   2967  N  N   . PHE A 1 414 ? 4.470   -6.741  8.686   1.00 43.66  ? 414  PHE A N   1 
ATOM   2968  C  CA  . PHE A 1 414 ? 3.248   -7.101  9.367   1.00 38.62  ? 414  PHE A CA  1 
ATOM   2969  C  C   . PHE A 1 414 ? 3.513   -8.113  10.471  1.00 50.05  ? 414  PHE A C   1 
ATOM   2970  O  O   . PHE A 1 414 ? 4.228   -9.100  10.264  1.00 49.81  ? 414  PHE A O   1 
ATOM   2971  C  CB  . PHE A 1 414 ? 2.246   -7.675  8.370   1.00 42.79  ? 414  PHE A CB  1 
ATOM   2972  C  CG  . PHE A 1 414 ? 1.840   -6.701  7.307   1.00 49.31  ? 414  PHE A CG  1 
ATOM   2973  C  CD1 . PHE A 1 414 ? 2.556   -6.619  6.122   1.00 48.62  ? 414  PHE A CD1 1 
ATOM   2974  C  CD2 . PHE A 1 414 ? 0.749   -5.856  7.494   1.00 54.52  ? 414  PHE A CD2 1 
ATOM   2975  C  CE1 . PHE A 1 414 ? 2.188   -5.720  5.132   1.00 51.53  ? 414  PHE A CE1 1 
ATOM   2976  C  CE2 . PHE A 1 414 ? 0.373   -4.949  6.514   1.00 52.26  ? 414  PHE A CE2 1 
ATOM   2977  C  CZ  . PHE A 1 414 ? 1.092   -4.882  5.327   1.00 54.23  ? 414  PHE A CZ  1 
ATOM   2978  N  N   . LYS A 1 415 ? 2.953   -7.845  11.648  1.00 47.05  ? 415  LYS A N   1 
ATOM   2979  C  CA  . LYS A 1 415 ? 2.814   -8.861  12.681  1.00 50.61  ? 415  LYS A CA  1 
ATOM   2980  C  C   . LYS A 1 415 ? 1.351   -9.300  12.771  1.00 51.27  ? 415  LYS A C   1 
ATOM   2981  O  O   . LYS A 1 415 ? 0.437   -8.472  12.827  1.00 40.92  ? 415  LYS A O   1 
ATOM   2982  C  CB  . LYS A 1 415 ? 3.327   -8.369  14.035  1.00 47.44  ? 415  LYS A CB  1 
ATOM   2983  C  CG  . LYS A 1 415 ? 4.821   -8.151  14.064  1.00 65.27  ? 415  LYS A CG  1 
ATOM   2984  C  CD  . LYS A 1 415 ? 5.356   -8.136  15.488  1.00 80.59  ? 415  LYS A CD  1 
ATOM   2985  C  CE  . LYS A 1 415 ? 6.877   -8.293  15.515  1.00 84.87  ? 415  LYS A CE  1 
ATOM   2986  N  NZ  . LYS A 1 415 ? 7.389   -8.499  16.906  1.00 87.54  ? 415  LYS A NZ  1 
ATOM   2987  N  N   . LEU A 1 416 ? 1.146   -10.613 12.758  1.00 51.41  ? 416  LEU A N   1 
ATOM   2988  C  CA  . LEU A 1 416 ? -0.185  -11.198 12.829  1.00 45.99  ? 416  LEU A CA  1 
ATOM   2989  C  C   . LEU A 1 416 ? -0.298  -12.040 14.076  1.00 47.88  ? 416  LEU A C   1 
ATOM   2990  O  O   . LEU A 1 416 ? 0.629   -12.785 14.409  1.00 47.98  ? 416  LEU A O   1 
ATOM   2991  C  CB  . LEU A 1 416 ? -0.443  -12.099 11.622  1.00 49.27  ? 416  LEU A CB  1 
ATOM   2992  C  CG  . LEU A 1 416 ? -0.212  -11.521 10.231  1.00 37.20  ? 416  LEU A CG  1 
ATOM   2993  C  CD1 . LEU A 1 416 ? -0.601  -12.529 9.145   1.00 25.40  ? 416  LEU A CD1 1 
ATOM   2994  C  CD2 . LEU A 1 416 ? -0.997  -10.240 10.088  1.00 40.22  ? 416  LEU A CD2 1 
ATOM   2995  N  N   . ALA A 1 417 ? -1.436  -11.927 14.759  1.00 50.77  ? 417  ALA A N   1 
ATOM   2996  C  CA  . ALA A 1 417 ? -1.686  -12.723 15.953  1.00 37.70  ? 417  ALA A CA  1 
ATOM   2997  C  C   . ALA A 1 417 ? -2.424  -13.986 15.550  1.00 39.51  ? 417  ALA A C   1 
ATOM   2998  O  O   . ALA A 1 417 ? -3.190  -13.973 14.596  1.00 53.82  ? 417  ALA A O   1 
ATOM   2999  C  CB  . ALA A 1 417 ? -2.483  -11.932 16.963  1.00 26.91  ? 417  ALA A CB  1 
ATOM   3000  N  N   . PRO A 1 418 ? -2.165  -15.100 16.241  1.00 33.34  ? 418  PRO A N   1 
ATOM   3001  C  CA  . PRO A 1 418 ? -2.942  -16.270 15.851  1.00 37.31  ? 418  PRO A CA  1 
ATOM   3002  C  C   . PRO A 1 418 ? -4.388  -15.991 16.225  1.00 59.96  ? 418  PRO A C   1 
ATOM   3003  O  O   . PRO A 1 418 ? -4.620  -15.268 17.191  1.00 70.26  ? 418  PRO A O   1 
ATOM   3004  C  CB  . PRO A 1 418 ? -2.364  -17.387 16.732  1.00 46.45  ? 418  PRO A CB  1 
ATOM   3005  C  CG  . PRO A 1 418 ? -1.052  -16.853 17.256  1.00 40.48  ? 418  PRO A CG  1 
ATOM   3006  C  CD  . PRO A 1 418 ? -1.237  -15.379 17.350  1.00 36.80  ? 418  PRO A CD  1 
ATOM   3007  N  N   . VAL A 1 419 ? -5.336  -16.535 15.470  1.00 72.49  ? 419  VAL A N   1 
ATOM   3008  C  CA  . VAL A 1 419 ? -6.759  -16.385 15.777  1.00 75.25  ? 419  VAL A CA  1 
ATOM   3009  C  C   . VAL A 1 419 ? -7.069  -16.521 17.274  1.00 65.19  ? 419  VAL A C   1 
ATOM   3010  O  O   . VAL A 1 419 ? -8.036  -15.937 17.772  1.00 48.17  ? 419  VAL A O   1 
ATOM   3011  C  CB  . VAL A 1 419 ? -7.604  -17.413 14.995  1.00 65.28  ? 419  VAL A CB  1 
ATOM   3012  C  CG1 . VAL A 1 419 ? -7.550  -17.111 13.513  1.00 58.31  ? 419  VAL A CG1 1 
ATOM   3013  C  CG2 . VAL A 1 419 ? -7.114  -18.835 15.267  1.00 49.97  ? 419  VAL A CG2 1 
ATOM   3014  N  N   . ILE B 1 28  ? -7.931  -57.923 12.194  1.00 41.90  ? 28   ILE B N   1 
ATOM   3015  C  CA  . ILE B 1 28  ? -7.355  -57.538 10.908  1.00 67.37  ? 28   ILE B CA  1 
ATOM   3016  C  C   . ILE B 1 28  ? -7.519  -56.027 10.699  1.00 59.20  ? 28   ILE B C   1 
ATOM   3017  O  O   . ILE B 1 28  ? -7.708  -55.536 9.585   1.00 62.12  ? 28   ILE B O   1 
ATOM   3018  C  CB  . ILE B 1 28  ? -7.948  -58.359 9.735   1.00 56.08  ? 28   ILE B CB  1 
ATOM   3019  C  CG1 . ILE B 1 28  ? -7.983  -59.857 10.082  1.00 60.14  ? 28   ILE B CG1 1 
ATOM   3020  C  CG2 . ILE B 1 28  ? -7.117  -58.161 8.467   1.00 56.81  ? 28   ILE B CG2 1 
ATOM   3021  C  CD1 . ILE B 1 28  ? -9.034  -60.269 11.126  1.00 54.13  ? 28   ILE B CD1 1 
ATOM   3022  N  N   . LYS B 1 29  ? -7.410  -55.304 11.807  1.00 56.37  ? 29   LYS B N   1 
ATOM   3023  C  CA  . LYS B 1 29  ? -7.604  -53.863 11.854  1.00 61.16  ? 29   LYS B CA  1 
ATOM   3024  C  C   . LYS B 1 29  ? -6.691  -53.093 10.900  1.00 54.77  ? 29   LYS B C   1 
ATOM   3025  O  O   . LYS B 1 29  ? -6.908  -51.907 10.658  1.00 66.11  ? 29   LYS B O   1 
ATOM   3026  C  CB  . LYS B 1 29  ? -7.414  -53.380 13.297  1.00 68.18  ? 29   LYS B CB  1 
ATOM   3027  C  CG  . LYS B 1 29  ? -7.746  -51.920 13.537  1.00 63.76  ? 29   LYS B CG  1 
ATOM   3028  C  CD  . LYS B 1 29  ? -7.951  -51.644 15.022  1.00 57.34  ? 29   LYS B CD  1 
ATOM   3029  C  CE  . LYS B 1 29  ? -8.141  -50.152 15.268  1.00 62.06  ? 29   LYS B CE  1 
ATOM   3030  N  NZ  . LYS B 1 29  ? -8.573  -49.841 16.664  1.00 58.97  ? 29   LYS B NZ  1 
ATOM   3031  N  N   . GLU B 1 30  ? -5.681  -53.762 10.352  1.00 59.16  ? 30   GLU B N   1 
ATOM   3032  C  CA  . GLU B 1 30  ? -4.793  -53.129 9.367   1.00 65.26  ? 30   GLU B CA  1 
ATOM   3033  C  C   . GLU B 1 30  ? -5.295  -53.284 7.942   1.00 56.42  ? 30   GLU B C   1 
ATOM   3034  O  O   . GLU B 1 30  ? -5.741  -54.355 7.530   1.00 63.44  ? 30   GLU B O   1 
ATOM   3035  C  CB  . GLU B 1 30  ? -3.378  -53.684 9.447   1.00 67.01  ? 30   GLU B CB  1 
ATOM   3036  C  CG  . GLU B 1 30  ? -2.529  -53.074 10.524  1.00 65.16  ? 30   GLU B CG  1 
ATOM   3037  C  CD  . GLU B 1 30  ? -1.113  -53.610 10.498  1.00 64.87  ? 30   GLU B CD  1 
ATOM   3038  O  OE1 . GLU B 1 30  ? -0.926  -54.853 10.441  1.00 51.61  ? 30   GLU B OE1 1 
ATOM   3039  O  OE2 . GLU B 1 30  ? -0.192  -52.777 10.537  1.00 57.13  ? 30   GLU B OE2 1 
ATOM   3040  N  N   . ASP B 1 31  ? -5.194  -52.200 7.191   1.00 39.47  ? 31   ASP B N   1 
ATOM   3041  C  CA  . ASP B 1 31  ? -5.672  -52.167 5.829   1.00 45.81  ? 31   ASP B CA  1 
ATOM   3042  C  C   . ASP B 1 31  ? -4.487  -52.363 4.904   1.00 58.56  ? 31   ASP B C   1 
ATOM   3043  O  O   . ASP B 1 31  ? -3.852  -51.401 4.473   1.00 49.77  ? 31   ASP B O   1 
ATOM   3044  C  CB  . ASP B 1 31  ? -6.360  -50.832 5.550   1.00 57.34  ? 31   ASP B CB  1 
ATOM   3045  C  CG  . ASP B 1 31  ? -6.993  -50.779 4.181   1.00 62.81  ? 31   ASP B CG  1 
ATOM   3046  O  OD1 . ASP B 1 31  ? -7.691  -49.775 3.878   1.00 53.49  ? 31   ASP B OD1 1 
ATOM   3047  O  OD2 . ASP B 1 31  ? -6.784  -51.748 3.414   1.00 54.97  ? 31   ASP B OD2 1 
ATOM   3048  N  N   . GLU B 1 32  ? -4.178  -53.625 4.630   1.00 57.97  ? 32   GLU B N   1 
ATOM   3049  C  CA  . GLU B 1 32  ? -3.128  -53.973 3.693   1.00 31.62  ? 32   GLU B CA  1 
ATOM   3050  C  C   . GLU B 1 32  ? -3.798  -54.716 2.554   1.00 46.86  ? 32   GLU B C   1 
ATOM   3051  O  O   . GLU B 1 32  ? -3.589  -55.913 2.360   1.00 55.41  ? 32   GLU B O   1 
ATOM   3052  C  CB  . GLU B 1 32  ? -2.081  -54.845 4.374   1.00 34.88  ? 32   GLU B CB  1 
ATOM   3053  C  CG  . GLU B 1 32  ? -1.893  -54.479 5.843   1.00 59.84  ? 32   GLU B CG  1 
ATOM   3054  C  CD  . GLU B 1 32  ? -0.794  -55.269 6.521   1.00 55.49  ? 32   GLU B CD  1 
ATOM   3055  O  OE1 . GLU B 1 32  ? 0.385   -54.937 6.283   1.00 42.03  ? 32   GLU B OE1 1 
ATOM   3056  O  OE2 . GLU B 1 32  ? -1.109  -56.207 7.295   1.00 53.19  ? 32   GLU B OE2 1 
ATOM   3057  N  N   . SER B 1 33  ? -4.635  -53.995 1.817   1.00 43.55  ? 33   SER B N   1 
ATOM   3058  C  CA  . SER B 1 33  ? -5.315  -54.559 0.665   1.00 56.51  ? 33   SER B CA  1 
ATOM   3059  C  C   . SER B 1 33  ? -4.501  -54.334 -0.604  1.00 67.57  ? 33   SER B C   1 
ATOM   3060  O  O   . SER B 1 33  ? -4.953  -54.675 -1.700  1.00 72.01  ? 33   SER B O   1 
ATOM   3061  C  CB  . SER B 1 33  ? -6.693  -53.927 0.505   1.00 74.84  ? 33   SER B CB  1 
ATOM   3062  O  OG  . SER B 1 33  ? -6.575  -52.588 0.061   1.00 97.29  ? 33   SER B OG  1 
ATOM   3063  N  N   . PHE B 1 34  ? -3.313  -53.747 -0.456  1.00 62.23  ? 34   PHE B N   1 
ATOM   3064  C  CA  . PHE B 1 34  ? -2.423  -53.511 -1.599  1.00 58.98  ? 34   PHE B CA  1 
ATOM   3065  C  C   . PHE B 1 34  ? -1.643  -54.773 -1.908  1.00 59.54  ? 34   PHE B C   1 
ATOM   3066  O  O   . PHE B 1 34  ? -1.069  -54.916 -2.985  1.00 57.02  ? 34   PHE B O   1 
ATOM   3067  C  CB  . PHE B 1 34  ? -1.450  -52.359 -1.327  1.00 40.08  ? 34   PHE B CB  1 
ATOM   3068  C  CG  . PHE B 1 34  ? -0.984  -52.290 0.097   1.00 34.79  ? 34   PHE B CG  1 
ATOM   3069  C  CD1 . PHE B 1 34  ? -0.061  -53.200 0.584   1.00 36.75  ? 34   PHE B CD1 1 
ATOM   3070  C  CD2 . PHE B 1 34  ? -1.467  -51.312 0.948   1.00 37.97  ? 34   PHE B CD2 1 
ATOM   3071  C  CE1 . PHE B 1 34  ? 0.369   -53.142 1.900   1.00 46.39  ? 34   PHE B CE1 1 
ATOM   3072  C  CE2 . PHE B 1 34  ? -1.040  -51.243 2.269   1.00 50.66  ? 34   PHE B CE2 1 
ATOM   3073  C  CZ  . PHE B 1 34  ? -0.122  -52.161 2.745   1.00 51.70  ? 34   PHE B CZ  1 
ATOM   3074  N  N   . LEU B 1 35  ? -1.629  -55.679 -0.939  1.00 64.56  ? 35   LEU B N   1 
ATOM   3075  C  CA  . LEU B 1 35  ? -1.001  -56.983 -1.085  1.00 69.63  ? 35   LEU B CA  1 
ATOM   3076  C  C   . LEU B 1 35  ? -1.966  -57.906 -1.856  1.00 79.58  ? 35   LEU B C   1 
ATOM   3077  O  O   . LEU B 1 35  ? -1.788  -59.126 -1.911  1.00 73.72  ? 35   LEU B O   1 
ATOM   3078  C  CB  . LEU B 1 35  ? -0.641  -57.537 0.312   1.00 66.49  ? 35   LEU B CB  1 
ATOM   3079  C  CG  . LEU B 1 35  ? 0.175   -56.598 1.236   1.00 48.37  ? 35   LEU B CG  1 
ATOM   3080  C  CD1 . LEU B 1 35  ? 0.025   -56.913 2.717   1.00 32.43  ? 35   LEU B CD1 1 
ATOM   3081  C  CD2 . LEU B 1 35  ? 1.656   -56.549 0.863   1.00 26.19  ? 35   LEU B CD2 1 
ATOM   3082  N  N   . GLN B 1 36  ? -2.986  -57.291 -2.456  1.00 87.82  ? 36   GLN B N   1 
ATOM   3083  C  CA  . GLN B 1 36  ? -4.016  -57.994 -3.222  1.00 87.09  ? 36   GLN B CA  1 
ATOM   3084  C  C   . GLN B 1 36  ? -3.540  -58.220 -4.648  1.00 76.85  ? 36   GLN B C   1 
ATOM   3085  O  O   . GLN B 1 36  ? -3.159  -57.270 -5.331  1.00 83.43  ? 36   GLN B O   1 
ATOM   3086  C  CB  . GLN B 1 36  ? -5.299  -57.162 -3.254  1.00 96.54  ? 36   GLN B CB  1 
ATOM   3087  C  CG  . GLN B 1 36  ? -6.560  -57.953 -3.537  1.00 98.87  ? 36   GLN B CG  1 
ATOM   3088  C  CD  . GLN B 1 36  ? -7.056  -58.705 -2.318  1.00 104.36 ? 36   GLN B CD  1 
ATOM   3089  O  OE1 . GLN B 1 36  ? -8.083  -59.383 -2.371  1.00 121.49 ? 36   GLN B OE1 1 
ATOM   3090  N  NE2 . GLN B 1 36  ? -6.330  -58.589 -1.210  1.00 86.07  ? 36   GLN B NE2 1 
ATOM   3091  N  N   . GLN B 1 37  ? -3.583  -59.472 -5.098  1.00 63.72  ? 37   GLN B N   1 
ATOM   3092  C  CA  . GLN B 1 37  ? -3.019  -59.858 -6.388  1.00 60.05  ? 37   GLN B CA  1 
ATOM   3093  C  C   . GLN B 1 37  ? -1.698  -59.151 -6.597  1.00 67.57  ? 37   GLN B C   1 
ATOM   3094  O  O   . GLN B 1 37  ? -1.644  -58.129 -7.288  1.00 79.24  ? 37   GLN B O   1 
ATOM   3095  C  CB  . GLN B 1 37  ? -3.950  -59.475 -7.531  1.00 69.82  ? 37   GLN B CB  1 
ATOM   3096  C  CG  . GLN B 1 37  ? -5.386  -59.843 -7.314  1.00 100.78 ? 37   GLN B CG  1 
ATOM   3097  C  CD  . GLN B 1 37  ? -6.297  -59.016 -8.183  1.00 115.58 ? 37   GLN B CD  1 
ATOM   3098  O  OE1 . GLN B 1 37  ? -6.070  -58.883 -9.388  1.00 119.19 ? 37   GLN B OE1 1 
ATOM   3099  N  NE2 . GLN B 1 37  ? -7.328  -58.437 -7.577  1.00 116.86 ? 37   GLN B NE2 1 
ATOM   3100  N  N   . PRO B 1 38  ? -0.623  -59.682 -6.001  1.00 54.14  ? 38   PRO B N   1 
ATOM   3101  C  CA  . PRO B 1 38  ? 0.684   -59.022 -6.102  1.00 44.29  ? 38   PRO B CA  1 
ATOM   3102  C  C   . PRO B 1 38  ? 1.226   -59.044 -7.531  1.00 54.05  ? 38   PRO B C   1 
ATOM   3103  O  O   . PRO B 1 38  ? 1.027   -60.003 -8.293  1.00 53.70  ? 38   PRO B O   1 
ATOM   3104  C  CB  . PRO B 1 38  ? 1.580   -59.841 -5.163  1.00 43.14  ? 38   PRO B CB  1 
ATOM   3105  C  CG  . PRO B 1 38  ? 0.650   -60.732 -4.383  1.00 60.14  ? 38   PRO B CG  1 
ATOM   3106  C  CD  . PRO B 1 38  ? -0.559  -60.937 -5.239  1.00 46.75  ? 38   PRO B CD  1 
ATOM   3107  N  N   . HIS B 1 39  ? 1.922   -57.969 -7.878  1.00 55.71  ? 39   HIS B N   1 
ATOM   3108  C  CA  . HIS B 1 39  ? 2.398   -57.756 -9.231  1.00 49.88  ? 39   HIS B CA  1 
ATOM   3109  C  C   . HIS B 1 39  ? 3.288   -56.531 -9.194  1.00 51.25  ? 39   HIS B C   1 
ATOM   3110  O  O   . HIS B 1 39  ? 3.168   -55.693 -8.297  1.00 47.52  ? 39   HIS B O   1 
ATOM   3111  C  CB  . HIS B 1 39  ? 1.210   -57.509 -10.171 1.00 53.33  ? 39   HIS B CB  1 
ATOM   3112  C  CG  . HIS B 1 39  ? 0.569   -56.165 -9.996  1.00 47.55  ? 39   HIS B CG  1 
ATOM   3113  N  ND1 . HIS B 1 39  ? 0.017   -55.753 -8.802  1.00 59.06  ? 39   HIS B ND1 1 
ATOM   3114  C  CD2 . HIS B 1 39  ? 0.398   -55.140 -10.863 1.00 50.17  ? 39   HIS B CD2 1 
ATOM   3115  C  CE1 . HIS B 1 39  ? -0.465  -54.530 -8.941  1.00 57.39  ? 39   HIS B CE1 1 
ATOM   3116  N  NE2 . HIS B 1 39  ? -0.247  -54.135 -10.181 1.00 52.92  ? 39   HIS B NE2 1 
ATOM   3117  N  N   . TYR B 1 40  ? 4.183   -56.413 -10.164 1.00 60.83  ? 40   TYR B N   1 
ATOM   3118  C  CA  . TYR B 1 40  ? 5.062   -55.251 -10.203 1.00 58.19  ? 40   TYR B CA  1 
ATOM   3119  C  C   . TYR B 1 40  ? 4.394   -54.081 -10.916 1.00 51.26  ? 40   TYR B C   1 
ATOM   3120  O  O   . TYR B 1 40  ? 3.890   -54.227 -12.029 1.00 58.15  ? 40   TYR B O   1 
ATOM   3121  C  CB  . TYR B 1 40  ? 6.403   -55.596 -10.856 1.00 61.68  ? 40   TYR B CB  1 
ATOM   3122  C  CG  . TYR B 1 40  ? 7.348   -56.339 -9.941  1.00 58.62  ? 40   TYR B CG  1 
ATOM   3123  C  CD1 . TYR B 1 40  ? 7.569   -57.707 -10.095 1.00 61.82  ? 40   TYR B CD1 1 
ATOM   3124  C  CD2 . TYR B 1 40  ? 8.013   -55.671 -8.915  1.00 43.11  ? 40   TYR B CD2 1 
ATOM   3125  C  CE1 . TYR B 1 40  ? 8.435   -58.387 -9.253  1.00 65.37  ? 40   TYR B CE1 1 
ATOM   3126  C  CE2 . TYR B 1 40  ? 8.881   -56.339 -8.075  1.00 47.09  ? 40   TYR B CE2 1 
ATOM   3127  C  CZ  . TYR B 1 40  ? 9.090   -57.695 -8.244  1.00 54.74  ? 40   TYR B CZ  1 
ATOM   3128  O  OH  . TYR B 1 40  ? 9.952   -58.354 -7.396  1.00 49.54  ? 40   TYR B OH  1 
ATOM   3129  N  N   . ALA B 1 41  ? 4.389   -52.926 -10.261 1.00 40.60  ? 41   ALA B N   1 
ATOM   3130  C  CA  . ALA B 1 41  ? 3.764   -51.731 -10.803 1.00 36.26  ? 41   ALA B CA  1 
ATOM   3131  C  C   . ALA B 1 41  ? 4.602   -51.161 -11.928 1.00 35.24  ? 41   ALA B C   1 
ATOM   3132  O  O   . ALA B 1 41  ? 5.777   -50.873 -11.730 1.00 41.67  ? 41   ALA B O   1 
ATOM   3133  C  CB  . ALA B 1 41  ? 3.597   -50.696 -9.703  1.00 41.06  ? 41   ALA B CB  1 
ATOM   3134  N  N   . SER B 1 42  ? 4.009   -50.985 -13.108 1.00 47.12  ? 42   SER B N   1 
ATOM   3135  C  CA  . SER B 1 42  ? 4.756   -50.439 -14.246 1.00 45.99  ? 42   SER B CA  1 
ATOM   3136  C  C   . SER B 1 42  ? 4.899   -48.929 -14.117 1.00 51.06  ? 42   SER B C   1 
ATOM   3137  O  O   . SER B 1 42  ? 4.322   -48.314 -13.216 1.00 53.88  ? 42   SER B O   1 
ATOM   3138  C  CB  . SER B 1 42  ? 4.049   -50.744 -15.553 1.00 45.06  ? 42   SER B CB  1 
ATOM   3139  O  OG  . SER B 1 42  ? 2.944   -49.873 -15.707 1.00 49.78  ? 42   SER B OG  1 
ATOM   3140  N  N   . GLN B 1 43  ? 5.656   -48.328 -15.026 1.00 40.24  ? 43   GLN B N   1 
ATOM   3141  C  CA  . GLN B 1 43  ? 5.760   -46.879 -15.059 1.00 36.58  ? 43   GLN B CA  1 
ATOM   3142  C  C   . GLN B 1 43  ? 4.357   -46.240 -15.117 1.00 42.92  ? 43   GLN B C   1 
ATOM   3143  O  O   . GLN B 1 43  ? 4.052   -45.298 -14.369 1.00 35.90  ? 43   GLN B O   1 
ATOM   3144  C  CB  . GLN B 1 43  ? 6.643   -46.427 -16.228 1.00 36.84  ? 43   GLN B CB  1 
ATOM   3145  C  CG  . GLN B 1 43  ? 6.888   -44.926 -16.275 1.00 52.43  ? 43   GLN B CG  1 
ATOM   3146  C  CD  . GLN B 1 43  ? 7.670   -44.421 -15.076 1.00 55.47  ? 43   GLN B CD  1 
ATOM   3147  O  OE1 . GLN B 1 43  ? 8.460   -45.157 -14.486 1.00 61.97  ? 43   GLN B OE1 1 
ATOM   3148  N  NE2 . GLN B 1 43  ? 7.457   -43.158 -14.714 1.00 56.29  ? 43   GLN B NE2 1 
ATOM   3149  N  N   . GLU B 1 44  ? 3.488   -46.759 -15.980 1.00 46.06  ? 44   GLU B N   1 
ATOM   3150  C  CA  . GLU B 1 44  ? 2.134   -46.208 -16.051 1.00 49.24  ? 44   GLU B CA  1 
ATOM   3151  C  C   . GLU B 1 44  ? 1.378   -46.394 -14.745 1.00 54.96  ? 44   GLU B C   1 
ATOM   3152  O  O   . GLU B 1 44  ? 0.793   -45.444 -14.216 1.00 60.90  ? 44   GLU B O   1 
ATOM   3153  C  CB  . GLU B 1 44  ? 1.314   -46.815 -17.183 1.00 53.43  ? 44   GLU B CB  1 
ATOM   3154  C  CG  . GLU B 1 44  ? 0.001   -46.068 -17.399 1.00 74.19  ? 44   GLU B CG  1 
ATOM   3155  C  CD  . GLU B 1 44  ? -1.057  -46.898 -18.099 1.00 95.22  ? 44   GLU B CD  1 
ATOM   3156  O  OE1 . GLU B 1 44  ? -0.737  -48.007 -18.576 1.00 104.09 ? 44   GLU B OE1 1 
ATOM   3157  O  OE2 . GLU B 1 44  ? -2.217  -46.439 -18.167 1.00 97.65  ? 44   GLU B OE2 1 
ATOM   3158  N  N   . GLN B 1 45  ? 1.391   -47.623 -14.227 1.00 58.01  ? 45   GLN B N   1 
ATOM   3159  C  CA  . GLN B 1 45  ? 0.660   -47.952 -12.998 1.00 52.83  ? 45   GLN B CA  1 
ATOM   3160  C  C   . GLN B 1 45  ? 1.095   -47.093 -11.824 1.00 48.82  ? 45   GLN B C   1 
ATOM   3161  O  O   . GLN B 1 45  ? 0.294   -46.809 -10.924 1.00 42.44  ? 45   GLN B O   1 
ATOM   3162  C  CB  . GLN B 1 45  ? 0.810   -49.431 -12.632 1.00 43.04  ? 45   GLN B CB  1 
ATOM   3163  C  CG  . GLN B 1 45  ? 0.139   -50.368 -13.616 1.00 49.57  ? 45   GLN B CG  1 
ATOM   3164  C  CD  . GLN B 1 45  ? -0.158  -51.730 -13.014 1.00 57.52  ? 45   GLN B CD  1 
ATOM   3165  O  OE1 . GLN B 1 45  ? 0.744   -52.414 -12.514 1.00 54.09  ? 45   GLN B OE1 1 
ATOM   3166  N  NE2 . GLN B 1 45  ? -1.429  -52.132 -13.053 1.00 59.81  ? 45   GLN B NE2 1 
ATOM   3167  N  N   . LEU B 1 46  ? 2.363   -46.680 -11.849 1.00 44.03  ? 46   LEU B N   1 
ATOM   3168  C  CA  . LEU B 1 46  ? 2.960   -45.902 -10.761 1.00 45.89  ? 46   LEU B CA  1 
ATOM   3169  C  C   . LEU B 1 46  ? 2.526   -44.446 -10.793 1.00 49.99  ? 46   LEU B C   1 
ATOM   3170  O  O   . LEU B 1 46  ? 2.200   -43.857 -9.756  1.00 45.17  ? 46   LEU B O   1 
ATOM   3171  C  CB  . LEU B 1 46  ? 4.485   -45.973 -10.824 1.00 40.75  ? 46   LEU B CB  1 
ATOM   3172  C  CG  . LEU B 1 46  ? 5.228   -45.032 -9.875  1.00 44.01  ? 46   LEU B CG  1 
ATOM   3173  C  CD1 . LEU B 1 46  ? 4.723   -45.170 -8.437  1.00 55.14  ? 46   LEU B CD1 1 
ATOM   3174  C  CD2 . LEU B 1 46  ? 6.730   -45.272 -9.941  1.00 32.93  ? 46   LEU B CD2 1 
ATOM   3175  N  N   . GLU B 1 47  ? 2.541   -43.861 -11.984 1.00 47.59  ? 47   GLU B N   1 
ATOM   3176  C  CA  . GLU B 1 47  ? 2.102   -42.486 -12.134 1.00 45.64  ? 47   GLU B CA  1 
ATOM   3177  C  C   . GLU B 1 47  ? 0.629   -42.423 -11.815 1.00 49.71  ? 47   GLU B C   1 
ATOM   3178  O  O   . GLU B 1 47  ? 0.179   -41.535 -11.093 1.00 54.46  ? 47   GLU B O   1 
ATOM   3179  C  CB  . GLU B 1 47  ? 2.355   -42.002 -13.552 1.00 51.04  ? 47   GLU B CB  1 
ATOM   3180  C  CG  . GLU B 1 47  ? 3.834   -41.929 -13.920 1.00 42.19  ? 47   GLU B CG  1 
ATOM   3181  C  CD  . GLU B 1 47  ? 4.040   -41.652 -15.395 1.00 53.43  ? 47   GLU B CD  1 
ATOM   3182  O  OE1 . GLU B 1 47  ? 3.165   -42.042 -16.202 1.00 54.46  ? 47   GLU B OE1 1 
ATOM   3183  O  OE2 . GLU B 1 47  ? 5.076   -41.052 -15.753 1.00 62.05  ? 47   GLU B OE2 1 
ATOM   3184  N  N   . ASP B 1 48  ? -0.116  -43.391 -12.342 1.00 54.56  ? 48   ASP B N   1 
ATOM   3185  C  CA  . ASP B 1 48  ? -1.550  -43.485 -12.086 1.00 59.99  ? 48   ASP B CA  1 
ATOM   3186  C  C   . ASP B 1 48  ? -1.860  -43.562 -10.588 1.00 52.16  ? 48   ASP B C   1 
ATOM   3187  O  O   . ASP B 1 48  ? -2.733  -42.843 -10.090 1.00 47.43  ? 48   ASP B O   1 
ATOM   3188  C  CB  . ASP B 1 48  ? -2.158  -44.688 -12.822 1.00 66.03  ? 48   ASP B CB  1 
ATOM   3189  C  CG  . ASP B 1 48  ? -2.203  -44.492 -14.333 1.00 75.67  ? 48   ASP B CG  1 
ATOM   3190  O  OD1 . ASP B 1 48  ? -2.191  -43.325 -14.780 1.00 76.66  ? 48   ASP B OD1 1 
ATOM   3191  O  OD2 . ASP B 1 48  ? -2.263  -45.502 -15.076 1.00 85.49  ? 48   ASP B OD2 1 
ATOM   3192  N  N   . LEU B 1 49  ? -1.144  -44.419 -9.863  1.00 40.88  ? 49   LEU B N   1 
ATOM   3193  C  CA  . LEU B 1 49  ? -1.460  -44.603 -8.444  1.00 45.30  ? 49   LEU B CA  1 
ATOM   3194  C  C   . LEU B 1 49  ? -1.104  -43.379 -7.607  1.00 39.55  ? 49   LEU B C   1 
ATOM   3195  O  O   . LEU B 1 49  ? -1.771  -43.081 -6.629  1.00 40.50  ? 49   LEU B O   1 
ATOM   3196  C  CB  . LEU B 1 49  ? -0.797  -45.857 -7.873  1.00 53.95  ? 49   LEU B CB  1 
ATOM   3197  C  CG  . LEU B 1 49  ? -1.289  -46.278 -6.486  1.00 44.42  ? 49   LEU B CG  1 
ATOM   3198  C  CD1 . LEU B 1 49  ? -1.249  -47.798 -6.326  1.00 63.22  ? 49   LEU B CD1 1 
ATOM   3199  C  CD2 . LEU B 1 49  ? -0.478  -45.610 -5.410  1.00 39.44  ? 49   LEU B CD2 1 
ATOM   3200  N  N   . PHE B 1 50  ? -0.048  -42.677 -7.999  1.00 40.64  ? 50   PHE B N   1 
ATOM   3201  C  CA  . PHE B 1 50  ? 0.359   -41.456 -7.316  1.00 35.43  ? 50   PHE B CA  1 
ATOM   3202  C  C   . PHE B 1 50  ? -0.655  -40.338 -7.516  1.00 42.25  ? 50   PHE B C   1 
ATOM   3203  O  O   . PHE B 1 50  ? -0.891  -39.542 -6.608  1.00 59.82  ? 50   PHE B O   1 
ATOM   3204  C  CB  . PHE B 1 50  ? 1.753   -41.014 -7.786  1.00 43.53  ? 50   PHE B CB  1 
ATOM   3205  C  CG  . PHE B 1 50  ? 2.883   -41.643 -7.006  1.00 42.95  ? 50   PHE B CG  1 
ATOM   3206  C  CD1 . PHE B 1 50  ? 2.629   -42.646 -6.077  1.00 41.68  ? 50   PHE B CD1 1 
ATOM   3207  C  CD2 . PHE B 1 50  ? 4.190   -41.228 -7.194  1.00 33.10  ? 50   PHE B CD2 1 
ATOM   3208  C  CE1 . PHE B 1 50  ? 3.652   -43.226 -5.349  1.00 33.15  ? 50   PHE B CE1 1 
ATOM   3209  C  CE2 . PHE B 1 50  ? 5.233   -41.804 -6.467  1.00 37.48  ? 50   PHE B CE2 1 
ATOM   3210  C  CZ  . PHE B 1 50  ? 4.959   -42.804 -5.541  1.00 38.23  ? 50   PHE B CZ  1 
ATOM   3211  N  N   . ALA B 1 51  ? -1.259  -40.280 -8.701  1.00 32.90  ? 51   ALA B N   1 
ATOM   3212  C  CA  . ALA B 1 51  ? -2.293  -39.284 -8.965  1.00 45.47  ? 51   ALA B CA  1 
ATOM   3213  C  C   . ALA B 1 51  ? -3.515  -39.562 -8.106  1.00 58.55  ? 51   ALA B C   1 
ATOM   3214  O  O   . ALA B 1 51  ? -4.109  -38.648 -7.527  1.00 68.81  ? 51   ALA B O   1 
ATOM   3215  C  CB  . ALA B 1 51  ? -2.678  -39.277 -10.445 1.00 36.71  ? 51   ALA B CB  1 
ATOM   3216  N  N   . GLY B 1 52  ? -3.884  -40.839 -8.036  1.00 60.73  ? 52   GLY B N   1 
ATOM   3217  C  CA  . GLY B 1 52  ? -5.044  -41.273 -7.273  1.00 53.56  ? 52   GLY B CA  1 
ATOM   3218  C  C   . GLY B 1 52  ? -4.927  -40.881 -5.814  1.00 44.84  ? 52   GLY B C   1 
ATOM   3219  O  O   . GLY B 1 52  ? -5.871  -40.359 -5.220  1.00 39.70  ? 52   GLY B O   1 
ATOM   3220  N  N   . LEU B 1 53  ? -3.753  -41.124 -5.244  1.00 43.28  ? 53   LEU B N   1 
ATOM   3221  C  CA  . LEU B 1 53  ? -3.507  -40.798 -3.852  1.00 51.08  ? 53   LEU B CA  1 
ATOM   3222  C  C   . LEU B 1 53  ? -3.644  -39.308 -3.638  1.00 54.37  ? 53   LEU B C   1 
ATOM   3223  O  O   . LEU B 1 53  ? -4.240  -38.865 -2.651  1.00 61.06  ? 53   LEU B O   1 
ATOM   3224  C  CB  . LEU B 1 53  ? -2.121  -41.263 -3.419  1.00 47.57  ? 53   LEU B CB  1 
ATOM   3225  C  CG  . LEU B 1 53  ? -1.909  -42.779 -3.459  1.00 51.42  ? 53   LEU B CG  1 
ATOM   3226  C  CD1 . LEU B 1 53  ? -0.649  -43.160 -2.707  1.00 60.18  ? 53   LEU B CD1 1 
ATOM   3227  C  CD2 . LEU B 1 53  ? -3.104  -43.538 -2.910  1.00 38.00  ? 53   LEU B CD2 1 
ATOM   3228  N  N   . GLU B 1 54  ? -3.101  -38.537 -4.572  1.00 46.98  ? 54   GLU B N   1 
ATOM   3229  C  CA  . GLU B 1 54  ? -3.179  -37.089 -4.481  1.00 57.92  ? 54   GLU B CA  1 
ATOM   3230  C  C   . GLU B 1 54  ? -4.632  -36.600 -4.398  1.00 66.83  ? 54   GLU B C   1 
ATOM   3231  O  O   . GLU B 1 54  ? -4.971  -35.764 -3.555  1.00 61.51  ? 54   GLU B O   1 
ATOM   3232  C  CB  . GLU B 1 54  ? -2.453  -36.443 -5.658  1.00 67.26  ? 54   GLU B CB  1 
ATOM   3233  C  CG  . GLU B 1 54  ? -1.981  -35.027 -5.375  1.00 76.39  ? 54   GLU B CG  1 
ATOM   3234  C  CD  . GLU B 1 54  ? -1.026  -34.507 -6.432  1.00 78.43  ? 54   GLU B CD  1 
ATOM   3235  O  OE1 . GLU B 1 54  ? -0.479  -33.401 -6.237  1.00 76.11  ? 54   GLU B OE1 1 
ATOM   3236  O  OE2 . GLU B 1 54  ? -0.818  -35.202 -7.455  1.00 77.31  ? 54   GLU B OE2 1 
ATOM   3237  N  N   . LYS B 1 55  ? -5.500  -37.117 -5.261  1.00 66.61  ? 55   LYS B N   1 
ATOM   3238  C  CA  . LYS B 1 55  ? -6.898  -36.708 -5.196  1.00 59.99  ? 55   LYS B CA  1 
ATOM   3239  C  C   . LYS B 1 55  ? -7.620  -37.406 -4.037  1.00 50.01  ? 55   LYS B C   1 
ATOM   3240  O  O   . LYS B 1 55  ? -8.405  -36.785 -3.344  1.00 46.42  ? 55   LYS B O   1 
ATOM   3241  C  CB  . LYS B 1 55  ? -7.604  -36.932 -6.533  1.00 51.09  ? 55   LYS B CB  1 
ATOM   3242  C  CG  . LYS B 1 55  ? -7.365  -38.302 -7.145  1.00 49.59  ? 55   LYS B CG  1 
ATOM   3243  C  CD  . LYS B 1 55  ? -8.124  -38.474 -8.458  1.00 58.76  ? 55   LYS B CD  1 
ATOM   3244  C  CE  . LYS B 1 55  ? -9.641  -38.439 -8.250  1.00 65.17  ? 55   LYS B CE  1 
ATOM   3245  N  NZ  . LYS B 1 55  ? -10.402 -38.474 -9.536  1.00 64.19  ? 55   LYS B NZ  1 
ATOM   3246  N  N   . ALA B 1 56  ? -7.331  -38.683 -3.807  1.00 38.89  ? 56   ALA B N   1 
ATOM   3247  C  CA  . ALA B 1 56  ? -7.947  -39.407 -2.700  1.00 38.70  ? 56   ALA B CA  1 
ATOM   3248  C  C   . ALA B 1 56  ? -7.639  -38.737 -1.371  1.00 43.74  ? 56   ALA B C   1 
ATOM   3249  O  O   . ALA B 1 56  ? -8.449  -38.761 -0.442  1.00 49.74  ? 56   ALA B O   1 
ATOM   3250  C  CB  . ALA B 1 56  ? -7.475  -40.864 -2.673  1.00 40.91  ? 56   ALA B CB  1 
ATOM   3251  N  N   . TYR B 1 57  ? -6.458  -38.147 -1.280  1.00 37.48  ? 57   TYR B N   1 
ATOM   3252  C  CA  . TYR B 1 57  ? -5.995  -37.585 -0.027  1.00 40.90  ? 57   TYR B CA  1 
ATOM   3253  C  C   . TYR B 1 57  ? -5.424  -36.195 -0.249  1.00 40.28  ? 57   TYR B C   1 
ATOM   3254  O  O   . TYR B 1 57  ? -4.225  -35.968 -0.060  1.00 50.72  ? 57   TYR B O   1 
ATOM   3255  C  CB  . TYR B 1 57  ? -4.931  -38.495 0.592   1.00 44.61  ? 57   TYR B CB  1 
ATOM   3256  C  CG  . TYR B 1 57  ? -5.417  -39.897 0.834   1.00 56.75  ? 57   TYR B CG  1 
ATOM   3257  C  CD1 . TYR B 1 57  ? -5.362  -40.851 -0.172  1.00 56.20  ? 57   TYR B CD1 1 
ATOM   3258  C  CD2 . TYR B 1 57  ? -5.945  -40.270 2.068   1.00 55.13  ? 57   TYR B CD2 1 
ATOM   3259  C  CE1 . TYR B 1 57  ? -5.817  -42.144 0.042   1.00 57.82  ? 57   TYR B CE1 1 
ATOM   3260  C  CE2 . TYR B 1 57  ? -6.409  -41.564 2.291   1.00 43.25  ? 57   TYR B CE2 1 
ATOM   3261  C  CZ  . TYR B 1 57  ? -6.335  -42.494 1.275   1.00 53.11  ? 57   TYR B CZ  1 
ATOM   3262  O  OH  . TYR B 1 57  ? -6.777  -43.781 1.488   1.00 52.02  ? 57   TYR B OH  1 
ATOM   3263  N  N   . PRO B 1 58  ? -6.287  -35.255 -0.621  1.00 32.68  ? 58   PRO B N   1 
ATOM   3264  C  CA  . PRO B 1 58  ? -5.967  -33.892 -1.063  1.00 39.53  ? 58   PRO B CA  1 
ATOM   3265  C  C   . PRO B 1 58  ? -4.953  -33.128 -0.204  1.00 58.02  ? 58   PRO B C   1 
ATOM   3266  O  O   . PRO B 1 58  ? -4.166  -32.370 -0.767  1.00 72.80  ? 58   PRO B O   1 
ATOM   3267  C  CB  . PRO B 1 58  ? -7.324  -33.182 -1.017  1.00 42.21  ? 58   PRO B CB  1 
ATOM   3268  C  CG  . PRO B 1 58  ? -8.317  -34.270 -1.242  1.00 41.00  ? 58   PRO B CG  1 
ATOM   3269  C  CD  . PRO B 1 58  ? -7.736  -35.488 -0.554  1.00 40.68  ? 58   PRO B CD  1 
ATOM   3270  N  N   . ASN B 1 59  ? -4.966  -33.305 1.117   1.00 67.42  ? 59   ASN B N   1 
ATOM   3271  C  CA  . ASN B 1 59  ? -4.147  -32.471 2.014   1.00 65.21  ? 59   ASN B CA  1 
ATOM   3272  C  C   . ASN B 1 59  ? -2.882  -33.159 2.568   1.00 54.78  ? 59   ASN B C   1 
ATOM   3273  O  O   . ASN B 1 59  ? -2.090  -32.547 3.300   1.00 38.39  ? 59   ASN B O   1 
ATOM   3274  C  CB  . ASN B 1 59  ? -4.985  -31.972 3.204   1.00 75.58  ? 59   ASN B CB  1 
ATOM   3275  C  CG  . ASN B 1 59  ? -6.350  -31.411 2.794   1.00 83.77  ? 59   ASN B CG  1 
ATOM   3276  O  OD1 . ASN B 1 59  ? -6.899  -31.745 1.738   1.00 81.42  ? 59   ASN B OD1 1 
ATOM   3277  N  ND2 . ASN B 1 59  ? -6.911  -30.562 3.653   1.00 84.49  ? 59   ASN B ND2 1 
ATOM   3278  N  N   . GLN B 1 60  ? -2.699  -34.433 2.237   1.00 46.60  ? 60   GLN B N   1 
ATOM   3279  C  CA  . GLN B 1 60  ? -1.602  -35.196 2.818   1.00 41.34  ? 60   GLN B CA  1 
ATOM   3280  C  C   . GLN B 1 60  ? -0.719  -35.901 1.772   1.00 44.24  ? 60   GLN B C   1 
ATOM   3281  O  O   . GLN B 1 60  ? 0.439   -36.253 2.065   1.00 40.00  ? 60   GLN B O   1 
ATOM   3282  C  CB  . GLN B 1 60  ? -2.164  -36.191 3.824   1.00 40.47  ? 60   GLN B CB  1 
ATOM   3283  C  CG  . GLN B 1 60  ? -3.658  -36.047 3.995   1.00 60.56  ? 60   GLN B CG  1 
ATOM   3284  C  CD  . GLN B 1 60  ? -4.090  -36.103 5.439   1.00 62.55  ? 60   GLN B CD  1 
ATOM   3285  O  OE1 . GLN B 1 60  ? -5.218  -36.473 5.738   1.00 61.60  ? 60   GLN B OE1 1 
ATOM   3286  N  NE2 . GLN B 1 60  ? -3.195  -35.734 6.345   1.00 56.56  ? 60   GLN B NE2 1 
ATOM   3287  N  N   . ALA B 1 61  ? -1.266  -36.097 0.565   1.00 34.42  ? 61   ALA B N   1 
ATOM   3288  C  CA  . ALA B 1 61  ? -0.511  -36.662 -0.563  1.00 32.58  ? 61   ALA B CA  1 
ATOM   3289  C  C   . ALA B 1 61  ? -0.275  -35.649 -1.680  1.00 32.41  ? 61   ALA B C   1 
ATOM   3290  O  O   . ALA B 1 61  ? -1.215  -35.044 -2.199  1.00 39.07  ? 61   ALA B O   1 
ATOM   3291  C  CB  . ALA B 1 61  ? -1.204  -37.899 -1.121  1.00 41.05  ? 61   ALA B CB  1 
ATOM   3292  N  N   . LYS B 1 62  ? 0.985   -35.469 -2.060  1.00 33.81  ? 62   LYS B N   1 
ATOM   3293  C  CA  . LYS B 1 62  ? 1.321   -34.532 -3.125  1.00 28.86  ? 62   LYS B CA  1 
ATOM   3294  C  C   . LYS B 1 62  ? 2.433   -35.099 -3.993  1.00 25.58  ? 62   LYS B C   1 
ATOM   3295  O  O   . LYS B 1 62  ? 3.436   -35.594 -3.497  1.00 39.19  ? 62   LYS B O   1 
ATOM   3296  C  CB  . LYS B 1 62  ? 1.708   -33.166 -2.549  1.00 25.15  ? 62   LYS B CB  1 
ATOM   3297  C  CG  . LYS B 1 62  ? 2.185   -32.172 -3.576  1.00 37.28  ? 62   LYS B CG  1 
ATOM   3298  C  CD  . LYS B 1 62  ? 2.437   -30.831 -2.937  1.00 59.29  ? 62   LYS B CD  1 
ATOM   3299  C  CE  . LYS B 1 62  ? 3.031   -29.864 -3.936  1.00 72.07  ? 62   LYS B CE  1 
ATOM   3300  N  NZ  . LYS B 1 62  ? 2.109   -29.703 -5.078  1.00 81.62  ? 62   LYS B NZ  1 
ATOM   3301  N  N   . VAL B 1 63  ? 2.242   -35.035 -5.301  1.00 38.22  ? 63   VAL B N   1 
ATOM   3302  C  CA  . VAL B 1 63  ? 3.235   -35.548 -6.230  1.00 31.28  ? 63   VAL B CA  1 
ATOM   3303  C  C   . VAL B 1 63  ? 4.218   -34.452 -6.613  1.00 43.86  ? 63   VAL B C   1 
ATOM   3304  O  O   . VAL B 1 63  ? 3.853   -33.278 -6.755  1.00 38.40  ? 63   VAL B O   1 
ATOM   3305  C  CB  . VAL B 1 63  ? 2.582   -36.130 -7.500  1.00 33.44  ? 63   VAL B CB  1 
ATOM   3306  C  CG1 . VAL B 1 63  ? 3.632   -36.450 -8.544  1.00 28.29  ? 63   VAL B CG1 1 
ATOM   3307  C  CG2 . VAL B 1 63  ? 1.782   -37.372 -7.162  1.00 44.49  ? 63   VAL B CG2 1 
ATOM   3308  N  N   . HIS B 1 64  ? 5.473   -34.859 -6.772  1.00 49.14  ? 64   HIS B N   1 
ATOM   3309  C  CA  . HIS B 1 64  ? 6.563   -33.957 -7.098  1.00 33.06  ? 64   HIS B CA  1 
ATOM   3310  C  C   . HIS B 1 64  ? 7.331   -34.503 -8.285  1.00 33.96  ? 64   HIS B C   1 
ATOM   3311  O  O   . HIS B 1 64  ? 7.677   -35.685 -8.328  1.00 40.58  ? 64   HIS B O   1 
ATOM   3312  C  CB  . HIS B 1 64  ? 7.459   -33.775 -5.880  1.00 17.17  ? 64   HIS B CB  1 
ATOM   3313  C  CG  . HIS B 1 64  ? 6.731   -33.209 -4.703  1.00 32.88  ? 64   HIS B CG  1 
ATOM   3314  N  ND1 . HIS B 1 64  ? 6.603   -31.853 -4.492  1.00 46.85  ? 64   HIS B ND1 1 
ATOM   3315  C  CD2 . HIS B 1 64  ? 6.041   -33.810 -3.703  1.00 40.86  ? 64   HIS B CD2 1 
ATOM   3316  C  CE1 . HIS B 1 64  ? 5.886   -31.642 -3.401  1.00 47.10  ? 64   HIS B CE1 1 
ATOM   3317  N  NE2 . HIS B 1 64  ? 5.531   -32.814 -2.904  1.00 41.55  ? 64   HIS B NE2 1 
ATOM   3318  N  N   . PHE B 1 65  ? 7.556   -33.640 -9.265  1.00 34.60  ? 65   PHE B N   1 
ATOM   3319  C  CA  . PHE B 1 65  ? 8.283   -34.007 -10.469 1.00 38.93  ? 65   PHE B CA  1 
ATOM   3320  C  C   . PHE B 1 65  ? 9.754   -33.646 -10.297 1.00 38.99  ? 65   PHE B C   1 
ATOM   3321  O  O   . PHE B 1 65  ? 10.092  -32.466 -10.111 1.00 37.42  ? 65   PHE B O   1 
ATOM   3322  C  CB  . PHE B 1 65  ? 7.698   -33.272 -11.680 1.00 35.13  ? 65   PHE B CB  1 
ATOM   3323  C  CG  . PHE B 1 65  ? 8.560   -33.343 -12.908 1.00 41.60  ? 65   PHE B CG  1 
ATOM   3324  C  CD1 . PHE B 1 65  ? 9.526   -32.380 -13.150 1.00 45.86  ? 65   PHE B CD1 1 
ATOM   3325  C  CD2 . PHE B 1 65  ? 8.404   -34.374 -13.825 1.00 47.04  ? 65   PHE B CD2 1 
ATOM   3326  C  CE1 . PHE B 1 65  ? 10.326  -32.448 -14.277 1.00 53.88  ? 65   PHE B CE1 1 
ATOM   3327  C  CE2 . PHE B 1 65  ? 9.198   -34.446 -14.955 1.00 49.43  ? 65   PHE B CE2 1 
ATOM   3328  C  CZ  . PHE B 1 65  ? 10.160  -33.480 -15.179 1.00 59.04  ? 65   PHE B CZ  1 
ATOM   3329  N  N   . LEU B 1 66  ? 10.622  -34.659 -10.365 1.00 39.75  ? 66   LEU B N   1 
ATOM   3330  C  CA  . LEU B 1 66  ? 12.066  -34.468 -10.141 1.00 36.22  ? 66   LEU B CA  1 
ATOM   3331  C  C   . LEU B 1 66  ? 12.857  -34.258 -11.431 1.00 36.02  ? 66   LEU B C   1 
ATOM   3332  O  O   . LEU B 1 66  ? 13.883  -33.569 -11.452 1.00 45.82  ? 66   LEU B O   1 
ATOM   3333  C  CB  . LEU B 1 66  ? 12.665  -35.649 -9.379  1.00 25.43  ? 66   LEU B CB  1 
ATOM   3334  C  CG  . LEU B 1 66  ? 12.052  -36.069 -8.042  1.00 33.71  ? 66   LEU B CG  1 
ATOM   3335  C  CD1 . LEU B 1 66  ? 12.898  -37.180 -7.410  1.00 21.97  ? 66   LEU B CD1 1 
ATOM   3336  C  CD2 . LEU B 1 66  ? 11.913  -34.870 -7.093  1.00 28.13  ? 66   LEU B CD2 1 
ATOM   3337  N  N   . GLY B 1 67  ? 12.378  -34.860 -12.509 1.00 33.95  ? 67   GLY B N   1 
ATOM   3338  C  CA  . GLY B 1 67  ? 13.084  -34.789 -13.764 1.00 31.74  ? 67   GLY B CA  1 
ATOM   3339  C  C   . GLY B 1 67  ? 12.633  -35.920 -14.639 1.00 34.33  ? 67   GLY B C   1 
ATOM   3340  O  O   . GLY B 1 67  ? 11.691  -36.643 -14.310 1.00 42.49  ? 67   GLY B O   1 
ATOM   3341  N  N   . ARG B 1 68  ? 13.297  -36.069 -15.772 1.00 38.37  ? 68   ARG B N   1 
ATOM   3342  C  CA  . ARG B 1 68  ? 12.929  -37.113 -16.705 1.00 38.64  ? 68   ARG B CA  1 
ATOM   3343  C  C   . ARG B 1 68  ? 14.130  -37.971 -17.053 1.00 39.67  ? 68   ARG B C   1 
ATOM   3344  O  O   . ARG B 1 68  ? 15.266  -37.512 -16.996 1.00 39.46  ? 68   ARG B O   1 
ATOM   3345  C  CB  . ARG B 1 68  ? 12.291  -36.513 -17.954 1.00 28.93  ? 68   ARG B CB  1 
ATOM   3346  C  CG  . ARG B 1 68  ? 10.785  -36.683 -17.987 1.00 39.01  ? 68   ARG B CG  1 
ATOM   3347  C  CD  . ARG B 1 68  ? 10.132  -35.609 -18.811 1.00 39.60  ? 68   ARG B CD  1 
ATOM   3348  N  NE  . ARG B 1 68  ? 8.703   -35.845 -18.947 1.00 43.16  ? 68   ARG B NE  1 
ATOM   3349  C  CZ  . ARG B 1 68  ? 7.778   -34.892 -18.925 1.00 62.94  ? 68   ARG B CZ  1 
ATOM   3350  N  NH1 . ARG B 1 68  ? 8.127   -33.625 -18.760 1.00 63.68  ? 68   ARG B NH1 1 
ATOM   3351  N  NH2 . ARG B 1 68  ? 6.501   -35.214 -19.068 1.00 80.55  ? 68   ARG B NH2 1 
ATOM   3352  N  N   . SER B 1 69  ? 13.871  -39.229 -17.383 1.00 33.98  ? 69   SER B N   1 
ATOM   3353  C  CA  . SER B 1 69  ? 14.926  -40.137 -17.796 1.00 25.17  ? 69   SER B CA  1 
ATOM   3354  C  C   . SER B 1 69  ? 15.313  -39.842 -19.237 1.00 34.97  ? 69   SER B C   1 
ATOM   3355  O  O   . SER B 1 69  ? 14.737  -38.968 -19.894 1.00 32.88  ? 69   SER B O   1 
ATOM   3356  C  CB  . SER B 1 69  ? 14.453  -41.585 -17.707 1.00 33.52  ? 69   SER B CB  1 
ATOM   3357  O  OG  . SER B 1 69  ? 13.465  -41.856 -18.686 1.00 24.41  ? 69   SER B OG  1 
ATOM   3358  N  N   . LEU B 1 70  ? 16.296  -40.588 -19.723 1.00 32.16  ? 70   LEU B N   1 
ATOM   3359  C  CA  . LEU B 1 70  ? 16.787  -40.405 -21.073 1.00 42.46  ? 70   LEU B CA  1 
ATOM   3360  C  C   . LEU B 1 70  ? 15.622  -40.627 -22.003 1.00 39.76  ? 70   LEU B C   1 
ATOM   3361  O  O   . LEU B 1 70  ? 15.438  -39.918 -22.985 1.00 37.95  ? 70   LEU B O   1 
ATOM   3362  C  CB  . LEU B 1 70  ? 17.900  -41.415 -21.390 1.00 41.95  ? 70   LEU B CB  1 
ATOM   3363  C  CG  . LEU B 1 70  ? 19.278  -41.192 -20.760 1.00 42.63  ? 70   LEU B CG  1 
ATOM   3364  C  CD1 . LEU B 1 70  ? 20.177  -42.415 -20.944 1.00 46.46  ? 70   LEU B CD1 1 
ATOM   3365  C  CD2 . LEU B 1 70  ? 19.941  -39.934 -21.325 1.00 36.97  ? 70   LEU B CD2 1 
ATOM   3366  N  N   . GLU B 1 71  ? 14.824  -41.627 -21.676 1.00 41.44  ? 71   GLU B N   1 
ATOM   3367  C  CA  . GLU B 1 71  ? 13.806  -42.074 -22.599 1.00 39.46  ? 71   GLU B CA  1 
ATOM   3368  C  C   . GLU B 1 71  ? 12.460  -41.464 -22.245 1.00 38.63  ? 71   GLU B C   1 
ATOM   3369  O  O   . GLU B 1 71  ? 11.417  -42.032 -22.547 1.00 54.37  ? 71   GLU B O   1 
ATOM   3370  C  CB  . GLU B 1 71  ? 13.774  -43.603 -22.636 1.00 43.26  ? 71   GLU B CB  1 
ATOM   3371  C  CG  . GLU B 1 71  ? 15.109  -44.206 -23.109 1.00 41.74  ? 71   GLU B CG  1 
ATOM   3372  C  CD  . GLU B 1 71  ? 15.131  -45.732 -23.071 1.00 56.43  ? 71   GLU B CD  1 
ATOM   3373  O  OE1 . GLU B 1 71  ? 14.396  -46.328 -22.247 1.00 61.71  ? 71   GLU B OE1 1 
ATOM   3374  O  OE2 . GLU B 1 71  ? 15.893  -46.333 -23.861 1.00 53.95  ? 71   GLU B OE2 1 
ATOM   3375  N  N   . GLY B 1 72  ? 12.497  -40.301 -21.597 1.00 37.64  ? 72   GLY B N   1 
ATOM   3376  C  CA  . GLY B 1 72  ? 11.296  -39.532 -21.315 1.00 34.75  ? 72   GLY B CA  1 
ATOM   3377  C  C   . GLY B 1 72  ? 10.496  -39.854 -20.065 1.00 33.89  ? 72   GLY B C   1 
ATOM   3378  O  O   . GLY B 1 72  ? 9.640   -39.071 -19.673 1.00 44.94  ? 72   GLY B O   1 
ATOM   3379  N  N   . ARG B 1 73  ? 10.763  -40.989 -19.432 1.00 32.22  ? 73   ARG B N   1 
ATOM   3380  C  CA  . ARG B 1 73  ? 9.987   -41.401 -18.266 1.00 39.63  ? 73   ARG B CA  1 
ATOM   3381  C  C   . ARG B 1 73  ? 10.155  -40.463 -17.071 1.00 43.00  ? 73   ARG B C   1 
ATOM   3382  O  O   . ARG B 1 73  ? 11.270  -40.083 -16.730 1.00 44.36  ? 73   ARG B O   1 
ATOM   3383  C  CB  . ARG B 1 73  ? 10.336  -42.833 -17.863 1.00 44.54  ? 73   ARG B CB  1 
ATOM   3384  C  CG  . ARG B 1 73  ? 10.072  -43.864 -18.952 1.00 36.83  ? 73   ARG B CG  1 
ATOM   3385  C  CD  . ARG B 1 73  ? 10.489  -45.228 -18.464 1.00 42.70  ? 73   ARG B CD  1 
ATOM   3386  N  NE  . ARG B 1 73  ? 11.102  -46.006 -19.520 1.00 36.38  ? 73   ARG B NE  1 
ATOM   3387  C  CZ  . ARG B 1 73  ? 10.421  -46.818 -20.309 1.00 47.15  ? 73   ARG B CZ  1 
ATOM   3388  N  NH1 . ARG B 1 73  ? 11.044  -47.497 -21.267 1.00 47.33  ? 73   ARG B NH1 1 
ATOM   3389  N  NH2 . ARG B 1 73  ? 9.107   -46.937 -20.142 1.00 57.65  ? 73   ARG B NH2 1 
ATOM   3390  N  N   . ASN B 1 74  ? 9.037   -40.111 -16.436 1.00 53.01  ? 74   ASN B N   1 
ATOM   3391  C  CA  . ASN B 1 74  ? 9.009   -39.176 -15.306 1.00 45.78  ? 74   ASN B CA  1 
ATOM   3392  C  C   . ASN B 1 74  ? 9.570   -39.754 -14.016 1.00 46.03  ? 74   ASN B C   1 
ATOM   3393  O  O   . ASN B 1 74  ? 9.208   -40.863 -13.604 1.00 47.47  ? 74   ASN B O   1 
ATOM   3394  C  CB  . ASN B 1 74  ? 7.579   -38.683 -15.036 1.00 45.01  ? 74   ASN B CB  1 
ATOM   3395  C  CG  . ASN B 1 74  ? 7.119   -37.619 -16.026 1.00 57.46  ? 74   ASN B CG  1 
ATOM   3396  O  OD1 . ASN B 1 74  ? 7.890   -36.725 -16.402 1.00 60.61  ? 74   ASN B OD1 1 
ATOM   3397  N  ND2 . ASN B 1 74  ? 5.851   -37.701 -16.440 1.00 55.41  ? 74   ASN B ND2 1 
ATOM   3398  N  N   . LEU B 1 75  ? 10.451  -38.984 -13.379 1.00 46.68  ? 75   LEU B N   1 
ATOM   3399  C  CA  . LEU B 1 75  ? 10.996  -39.326 -12.065 1.00 43.59  ? 75   LEU B CA  1 
ATOM   3400  C  C   . LEU B 1 75  ? 10.169  -38.627 -10.978 1.00 33.36  ? 75   LEU B C   1 
ATOM   3401  O  O   . LEU B 1 75  ? 10.227  -37.402 -10.818 1.00 42.31  ? 75   LEU B O   1 
ATOM   3402  C  CB  . LEU B 1 75  ? 12.477  -38.926 -11.972 1.00 45.28  ? 75   LEU B CB  1 
ATOM   3403  C  CG  . LEU B 1 75  ? 13.556  -39.811 -12.622 1.00 41.36  ? 75   LEU B CG  1 
ATOM   3404  C  CD1 . LEU B 1 75  ? 12.974  -40.831 -13.584 1.00 49.33  ? 75   LEU B CD1 1 
ATOM   3405  C  CD2 . LEU B 1 75  ? 14.619  -38.964 -13.326 1.00 34.64  ? 75   LEU B CD2 1 
ATOM   3406  N  N   . LEU B 1 76  ? 9.402   -39.414 -10.229 1.00 29.96  ? 76   LEU B N   1 
ATOM   3407  C  CA  . LEU B 1 76  ? 8.352   -38.870 -9.379  1.00 27.95  ? 76   LEU B CA  1 
ATOM   3408  C  C   . LEU B 1 76  ? 8.560   -39.229 -7.925  1.00 34.03  ? 76   LEU B C   1 
ATOM   3409  O  O   . LEU B 1 76  ? 9.011   -40.331 -7.610  1.00 39.02  ? 76   LEU B O   1 
ATOM   3410  C  CB  . LEU B 1 76  ? 6.982   -39.399 -9.821  1.00 31.97  ? 76   LEU B CB  1 
ATOM   3411  C  CG  . LEU B 1 76  ? 6.406   -38.966 -11.169 1.00 39.43  ? 76   LEU B CG  1 
ATOM   3412  C  CD1 . LEU B 1 76  ? 5.205   -39.819 -11.494 1.00 49.32  ? 76   LEU B CD1 1 
ATOM   3413  C  CD2 . LEU B 1 76  ? 6.037   -37.491 -11.161 1.00 39.30  ? 76   LEU B CD2 1 
ATOM   3414  N  N   . ALA B 1 77  ? 8.208   -38.296 -7.041  1.00 46.28  ? 77   ALA B N   1 
ATOM   3415  C  CA  . ALA B 1 77  ? 8.254   -38.537 -5.603  1.00 36.33  ? 77   ALA B CA  1 
ATOM   3416  C  C   . ALA B 1 77  ? 6.939   -38.125 -4.992  1.00 38.42  ? 77   ALA B C   1 
ATOM   3417  O  O   . ALA B 1 77  ? 6.414   -37.052 -5.290  1.00 45.67  ? 77   ALA B O   1 
ATOM   3418  C  CB  . ALA B 1 77  ? 9.380   -37.766 -4.963  1.00 24.81  ? 77   ALA B CB  1 
ATOM   3419  N  N   . LEU B 1 78  ? 6.409   -38.986 -4.133  1.00 38.72  ? 78   LEU B N   1 
ATOM   3420  C  CA  . LEU B 1 78  ? 5.167   -38.689 -3.433  1.00 26.59  ? 78   LEU B CA  1 
ATOM   3421  C  C   . LEU B 1 78  ? 5.471   -38.253 -2.023  1.00 30.73  ? 78   LEU B C   1 
ATOM   3422  O  O   . LEU B 1 78  ? 6.079   -39.000 -1.241  1.00 27.34  ? 78   LEU B O   1 
ATOM   3423  C  CB  . LEU B 1 78  ? 4.244   -39.903 -3.388  1.00 26.49  ? 78   LEU B CB  1 
ATOM   3424  C  CG  . LEU B 1 78  ? 2.867   -39.609 -2.789  1.00 31.56  ? 78   LEU B CG  1 
ATOM   3425  C  CD1 . LEU B 1 78  ? 1.995   -38.899 -3.823  1.00 26.05  ? 78   LEU B CD1 1 
ATOM   3426  C  CD2 . LEU B 1 78  ? 2.208   -40.888 -2.305  1.00 36.01  ? 78   LEU B CD2 1 
ATOM   3427  N  N   . GLN B 1 79  ? 5.048   -37.033 -1.715  1.00 27.73  ? 79   GLN B N   1 
ATOM   3428  C  CA  . GLN B 1 79  ? 5.138   -36.487 -0.368  1.00 29.92  ? 79   GLN B CA  1 
ATOM   3429  C  C   . GLN B 1 79  ? 3.878   -36.768 0.452   1.00 33.33  ? 79   GLN B C   1 
ATOM   3430  O  O   . GLN B 1 79  ? 2.763   -36.526 -0.008  1.00 30.88  ? 79   GLN B O   1 
ATOM   3431  C  CB  . GLN B 1 79  ? 5.360   -34.976 -0.423  1.00 36.28  ? 79   GLN B CB  1 
ATOM   3432  C  CG  . GLN B 1 79  ? 4.851   -34.242 0.805   1.00 30.24  ? 79   GLN B CG  1 
ATOM   3433  C  CD  . GLN B 1 79  ? 5.001   -32.742 0.685   1.00 36.87  ? 79   GLN B CD  1 
ATOM   3434  O  OE1 . GLN B 1 79  ? 4.890   -32.179 -0.409  1.00 39.84  ? 79   GLN B OE1 1 
ATOM   3435  N  NE2 . GLN B 1 79  ? 5.255   -32.080 1.815   1.00 36.02  ? 79   GLN B NE2 1 
ATOM   3436  N  N   . ILE B 1 80  ? 4.070   -37.275 1.668   1.00 44.35  ? 80   ILE B N   1 
ATOM   3437  C  CA  . ILE B 1 80  ? 2.989   -37.463 2.625   1.00 36.07  ? 80   ILE B CA  1 
ATOM   3438  C  C   . ILE B 1 80  ? 3.332   -36.624 3.844   1.00 39.57  ? 80   ILE B C   1 
ATOM   3439  O  O   . ILE B 1 80  ? 4.454   -36.695 4.355   1.00 51.06  ? 80   ILE B O   1 
ATOM   3440  C  CB  . ILE B 1 80  ? 2.867   -38.935 3.071   1.00 28.34  ? 80   ILE B CB  1 
ATOM   3441  C  CG1 . ILE B 1 80  ? 2.603   -39.852 1.884   1.00 29.51  ? 80   ILE B CG1 1 
ATOM   3442  C  CG2 . ILE B 1 80  ? 1.741   -39.098 4.055   1.00 22.84  ? 80   ILE B CG2 1 
ATOM   3443  C  CD1 . ILE B 1 80  ? 2.874   -41.316 2.194   1.00 23.14  ? 80   ILE B CD1 1 
ATOM   3444  N  N   . SER B 1 81  ? 2.376   -35.841 4.318   1.00 32.94  ? 81   SER B N   1 
ATOM   3445  C  CA  . SER B 1 81  ? 2.638   -34.964 5.448   1.00 38.58  ? 81   SER B CA  1 
ATOM   3446  C  C   . SER B 1 81  ? 1.342   -34.626 6.179   1.00 47.22  ? 81   SER B C   1 
ATOM   3447  O  O   . SER B 1 81  ? 0.256   -34.924 5.693   1.00 48.28  ? 81   SER B O   1 
ATOM   3448  C  CB  . SER B 1 81  ? 3.293   -33.672 4.960   1.00 39.38  ? 81   SER B CB  1 
ATOM   3449  O  OG  . SER B 1 81  ? 2.425   -32.991 4.065   1.00 59.80  ? 81   SER B OG  1 
ATOM   3450  N  N   . ARG B 1 82  ? 1.463   -34.008 7.351   1.00 48.51  ? 82   ARG B N   1 
ATOM   3451  C  CA  . ARG B 1 82  ? 0.297   -33.504 8.057   1.00 48.27  ? 82   ARG B CA  1 
ATOM   3452  C  C   . ARG B 1 82  ? -0.444  -32.525 7.159   1.00 56.28  ? 82   ARG B C   1 
ATOM   3453  O  O   . ARG B 1 82  ? -1.674  -32.550 7.073   1.00 63.93  ? 82   ARG B O   1 
ATOM   3454  C  CB  . ARG B 1 82  ? 0.708   -32.806 9.359   1.00 52.60  ? 82   ARG B CB  1 
ATOM   3455  C  CG  . ARG B 1 82  ? -0.475  -32.273 10.202  1.00 53.28  ? 82   ARG B CG  1 
ATOM   3456  C  CD  . ARG B 1 82  ? -0.462  -32.804 11.657  1.00 65.83  ? 82   ARG B CD  1 
ATOM   3457  N  NE  . ARG B 1 82  ? -0.164  -31.786 12.663  1.00 75.25  ? 82   ARG B NE  1 
ATOM   3458  C  CZ  . ARG B 1 82  ? -0.374  -31.901 13.977  1.00 76.83  ? 82   ARG B CZ  1 
ATOM   3459  N  NH1 . ARG B 1 82  ? -0.059  -30.888 14.775  1.00 68.04  ? 82   ARG B NH1 1 
ATOM   3460  N  NH2 . ARG B 1 82  ? -0.903  -33.002 14.501  1.00 76.22  ? 82   ARG B NH2 1 
ATOM   3461  N  N   . ASN B 1 83  ? 0.318   -31.664 6.489   1.00 45.17  ? 83   ASN B N   1 
ATOM   3462  C  CA  . ASN B 1 83  ? -0.236  -30.654 5.594   1.00 34.65  ? 83   ASN B CA  1 
ATOM   3463  C  C   . ASN B 1 83  ? 0.683   -30.381 4.426   1.00 33.74  ? 83   ASN B C   1 
ATOM   3464  O  O   . ASN B 1 83  ? 1.685   -29.688 4.547   1.00 40.14  ? 83   ASN B O   1 
ATOM   3465  C  CB  . ASN B 1 83  ? -0.467  -29.342 6.321   1.00 49.50  ? 83   ASN B CB  1 
ATOM   3466  C  CG  . ASN B 1 83  ? -0.559  -28.182 5.367   1.00 62.54  ? 83   ASN B CG  1 
ATOM   3467  O  OD1 . ASN B 1 83  ? -1.058  -28.327 4.249   1.00 68.57  ? 83   ASN B OD1 1 
ATOM   3468  N  ND2 . ASN B 1 83  ? -0.066  -27.025 5.790   1.00 61.77  ? 83   ASN B ND2 1 
ATOM   3469  N  N   . THR B 1 84  ? 0.323   -30.910 3.276   1.00 45.69  ? 84   THR B N   1 
ATOM   3470  C  CA  . THR B 1 84  ? 1.212   -30.870 2.135   1.00 32.70  ? 84   THR B CA  1 
ATOM   3471  C  C   . THR B 1 84  ? 1.525   -29.452 1.676   1.00 23.33  ? 84   THR B C   1 
ATOM   3472  O  O   . THR B 1 84  ? 2.507   -29.221 0.988   1.00 37.96  ? 84   THR B O   1 
ATOM   3473  C  CB  . THR B 1 84  ? 0.641   -31.707 0.977   1.00 38.86  ? 84   THR B CB  1 
ATOM   3474  O  OG1 . THR B 1 84  ? 1.668   -32.567 0.470   1.00 56.25  ? 84   THR B OG1 1 
ATOM   3475  C  CG2 . THR B 1 84  ? 0.085   -30.809 -0.142  1.00 24.82  ? 84   THR B CG2 1 
ATOM   3476  N  N   . ARG B 1 85  ? 0.705   -28.491 2.065   1.00 35.15  ? 85   ARG B N   1 
ATOM   3477  C  CA  . ARG B 1 85  ? 0.899   -27.142 1.549   1.00 43.95  ? 85   ARG B CA  1 
ATOM   3478  C  C   . ARG B 1 85  ? 2.272   -26.634 1.920   1.00 47.03  ? 85   ARG B C   1 
ATOM   3479  O  O   . ARG B 1 85  ? 2.977   -26.073 1.089   1.00 48.86  ? 85   ARG B O   1 
ATOM   3480  C  CB  . ARG B 1 85  ? -0.151  -26.179 2.086   1.00 58.26  ? 85   ARG B CB  1 
ATOM   3481  C  CG  . ARG B 1 85  ? -1.553  -26.430 1.583   1.00 76.92  ? 85   ARG B CG  1 
ATOM   3482  C  CD  . ARG B 1 85  ? -2.403  -25.172 1.739   1.00 96.38  ? 85   ARG B CD  1 
ATOM   3483  N  NE  . ARG B 1 85  ? -2.199  -24.228 0.639   1.00 106.48 ? 85   ARG B NE  1 
ATOM   3484  C  CZ  . ARG B 1 85  ? -1.334  -23.216 0.653   1.00 102.58 ? 85   ARG B CZ  1 
ATOM   3485  N  NH1 . ARG B 1 85  ? -1.228  -22.419 -0.407  1.00 97.16  ? 85   ARG B NH1 1 
ATOM   3486  N  NH2 . ARG B 1 85  ? -0.574  -22.997 1.719   1.00 99.35  ? 85   ARG B NH2 1 
ATOM   3487  N  N   . SER B 1 86  ? 2.645   -26.825 3.179   1.00 48.34  ? 86   SER B N   1 
ATOM   3488  C  CA  . SER B 1 86  ? 3.963   -26.407 3.630   1.00 47.38  ? 86   SER B CA  1 
ATOM   3489  C  C   . SER B 1 86  ? 4.683   -27.522 4.375   1.00 64.31  ? 86   SER B C   1 
ATOM   3490  O  O   . SER B 1 86  ? 4.446   -28.714 4.133   1.00 77.73  ? 86   SER B O   1 
ATOM   3491  C  CB  . SER B 1 86  ? 3.867   -25.167 4.518   1.00 42.22  ? 86   SER B CB  1 
ATOM   3492  O  OG  . SER B 1 86  ? 3.388   -24.057 3.783   1.00 51.61  ? 86   SER B OG  1 
ATOM   3493  N  N   . ARG B 1 87  ? 5.587   -27.113 5.260   1.00 52.49  ? 87   ARG B N   1 
ATOM   3494  C  CA  . ARG B 1 87  ? 6.246   -28.022 6.180   1.00 44.77  ? 87   ARG B CA  1 
ATOM   3495  C  C   . ARG B 1 87  ? 6.285   -27.311 7.528   1.00 48.31  ? 87   ARG B C   1 
ATOM   3496  O  O   . ARG B 1 87  ? 6.923   -26.263 7.675   1.00 42.45  ? 87   ARG B O   1 
ATOM   3497  C  CB  . ARG B 1 87  ? 7.660   -28.356 5.711   1.00 25.59  ? 87   ARG B CB  1 
ATOM   3498  C  CG  . ARG B 1 87  ? 8.143   -29.759 6.064   1.00 31.68  ? 87   ARG B CG  1 
ATOM   3499  C  CD  . ARG B 1 87  ? 9.670   -29.919 5.853   1.00 33.64  ? 87   ARG B CD  1 
ATOM   3500  N  NE  . ARG B 1 87  ? 10.391  -29.355 6.985   1.00 39.17  ? 87   ARG B NE  1 
ATOM   3501  C  CZ  . ARG B 1 87  ? 11.022  -28.188 6.972   1.00 42.22  ? 87   ARG B CZ  1 
ATOM   3502  N  NH1 . ARG B 1 87  ? 11.062  -27.464 5.866   1.00 48.01  ? 87   ARG B NH1 1 
ATOM   3503  N  NH2 . ARG B 1 87  ? 11.625  -27.754 8.071   1.00 53.40  ? 87   ARG B NH2 1 
ATOM   3504  N  N   . ASN B 1 88  ? 5.571   -27.861 8.501   1.00 46.48  ? 88   ASN B N   1 
ATOM   3505  C  CA  . ASN B 1 88  ? 5.583   -27.296 9.831   1.00 38.07  ? 88   ASN B CA  1 
ATOM   3506  C  C   . ASN B 1 88  ? 7.005   -27.123 10.362  1.00 41.00  ? 88   ASN B C   1 
ATOM   3507  O  O   . ASN B 1 88  ? 7.867   -27.998 10.203  1.00 29.10  ? 88   ASN B O   1 
ATOM   3508  C  CB  . ASN B 1 88  ? 4.727   -28.138 10.779  1.00 43.51  ? 88   ASN B CB  1 
ATOM   3509  C  CG  . ASN B 1 88  ? 3.300   -28.255 10.307  1.00 49.30  ? 88   ASN B CG  1 
ATOM   3510  O  OD1 . ASN B 1 88  ? 2.781   -29.351 10.128  1.00 61.97  ? 88   ASN B OD1 1 
ATOM   3511  N  ND2 . ASN B 1 88  ? 2.667   -27.120 10.070  1.00 55.39  ? 88   ASN B ND2 1 
ATOM   3512  N  N   . LEU B 1 89  ? 7.234   -25.964 10.968  1.00 37.85  ? 89   LEU B N   1 
ATOM   3513  C  CA  . LEU B 1 89  ? 8.499   -25.653 11.603  1.00 37.89  ? 89   LEU B CA  1 
ATOM   3514  C  C   . LEU B 1 89  ? 8.986   -26.844 12.415  1.00 36.99  ? 89   LEU B C   1 
ATOM   3515  O  O   . LEU B 1 89  ? 8.247   -27.391 13.244  1.00 37.03  ? 89   LEU B O   1 
ATOM   3516  C  CB  . LEU B 1 89  ? 8.339   -24.431 12.515  1.00 29.79  ? 89   LEU B CB  1 
ATOM   3517  C  CG  . LEU B 1 89  ? 9.646   -23.704 12.844  1.00 39.11  ? 89   LEU B CG  1 
ATOM   3518  C  CD1 . LEU B 1 89  ? 10.222  -23.012 11.609  1.00 24.35  ? 89   LEU B CD1 1 
ATOM   3519  C  CD2 . LEU B 1 89  ? 9.461   -22.702 13.979  1.00 44.38  ? 89   LEU B CD2 1 
ATOM   3520  N  N   . LEU B 1 90  ? 10.224  -27.242 12.146  1.00 33.65  ? 90   LEU B N   1 
ATOM   3521  C  CA  . LEU B 1 90  ? 10.927  -28.306 12.879  1.00 42.98  ? 90   LEU B CA  1 
ATOM   3522  C  C   . LEU B 1 90  ? 10.437  -29.726 12.581  1.00 40.15  ? 90   LEU B C   1 
ATOM   3523  O  O   . LEU B 1 90  ? 10.841  -30.685 13.246  1.00 32.18  ? 90   LEU B O   1 
ATOM   3524  C  CB  . LEU B 1 90  ? 10.977  -28.019 14.382  1.00 28.58  ? 90   LEU B CB  1 
ATOM   3525  C  CG  . LEU B 1 90  ? 11.827  -26.794 14.722  1.00 29.86  ? 90   LEU B CG  1 
ATOM   3526  C  CD1 . LEU B 1 90  ? 11.694  -26.388 16.200  1.00 25.30  ? 90   LEU B CD1 1 
ATOM   3527  C  CD2 . LEU B 1 90  ? 13.284  -27.049 14.347  1.00 27.50  ? 90   LEU B CD2 1 
ATOM   3528  N  N   . THR B 1 91  ? 9.586   -29.855 11.565  1.00 35.67  ? 91   THR B N   1 
ATOM   3529  C  CA  . THR B 1 91  ? 9.227   -31.173 11.070  1.00 32.68  ? 91   THR B CA  1 
ATOM   3530  C  C   . THR B 1 91  ? 10.322  -31.658 10.153  1.00 35.97  ? 91   THR B C   1 
ATOM   3531  O  O   . THR B 1 91  ? 10.672  -30.996 9.178   1.00 31.13  ? 91   THR B O   1 
ATOM   3532  C  CB  . THR B 1 91  ? 7.897   -31.204 10.295  1.00 25.72  ? 91   THR B CB  1 
ATOM   3533  O  OG1 . THR B 1 91  ? 6.825   -30.871 11.177  1.00 27.16  ? 91   THR B OG1 1 
ATOM   3534  C  CG2 . THR B 1 91  ? 7.645   -32.612 9.739   1.00 18.89  ? 91   THR B CG2 1 
ATOM   3535  N  N   . PRO B 1 92  ? 10.863  -32.833 10.458  1.00 32.16  ? 92   PRO B N   1 
ATOM   3536  C  CA  . PRO B 1 92  ? 11.934  -33.419 9.650   1.00 29.39  ? 92   PRO B CA  1 
ATOM   3537  C  C   . PRO B 1 92  ? 11.416  -33.825 8.284   1.00 39.55  ? 92   PRO B C   1 
ATOM   3538  O  O   . PRO B 1 92  ? 10.453  -34.584 8.205   1.00 26.00  ? 92   PRO B O   1 
ATOM   3539  C  CB  . PRO B 1 92  ? 12.335  -34.679 10.433  1.00 36.76  ? 92   PRO B CB  1 
ATOM   3540  C  CG  . PRO B 1 92  ? 11.617  -34.577 11.777  1.00 41.51  ? 92   PRO B CG  1 
ATOM   3541  C  CD  . PRO B 1 92  ? 10.433  -33.702 11.562  1.00 28.46  ? 92   PRO B CD  1 
ATOM   3542  N  N   . PRO B 1 93  ? 12.060  -33.329 7.210   1.00 53.90  ? 93   PRO B N   1 
ATOM   3543  C  CA  . PRO B 1 93  ? 11.811  -33.906 5.886   1.00 42.14  ? 93   PRO B CA  1 
ATOM   3544  C  C   . PRO B 1 93  ? 12.692  -35.149 5.712   1.00 39.74  ? 93   PRO B C   1 
ATOM   3545  O  O   . PRO B 1 93  ? 13.885  -35.111 6.062   1.00 28.19  ? 93   PRO B O   1 
ATOM   3546  C  CB  . PRO B 1 93  ? 12.234  -32.782 4.936   1.00 31.28  ? 93   PRO B CB  1 
ATOM   3547  C  CG  . PRO B 1 93  ? 13.281  -31.980 5.709   1.00 30.54  ? 93   PRO B CG  1 
ATOM   3548  C  CD  . PRO B 1 93  ? 13.143  -32.324 7.183   1.00 36.79  ? 93   PRO B CD  1 
ATOM   3549  N  N   . VAL B 1 94  ? 12.103  -36.237 5.214   1.00 30.07  ? 94   VAL B N   1 
ATOM   3550  C  CA  . VAL B 1 94  ? 12.806  -37.515 5.090   1.00 21.92  ? 94   VAL B CA  1 
ATOM   3551  C  C   . VAL B 1 94  ? 12.483  -38.138 3.746   1.00 24.59  ? 94   VAL B C   1 
ATOM   3552  O  O   . VAL B 1 94  ? 11.447  -37.846 3.168   1.00 41.83  ? 94   VAL B O   1 
ATOM   3553  C  CB  . VAL B 1 94  ? 12.396  -38.484 6.196   1.00 30.25  ? 94   VAL B CB  1 
ATOM   3554  C  CG1 . VAL B 1 94  ? 13.107  -39.792 6.030   1.00 60.29  ? 94   VAL B CG1 1 
ATOM   3555  C  CG2 . VAL B 1 94  ? 12.725  -37.907 7.552   1.00 30.25  ? 94   VAL B CG2 1 
ATOM   3556  N  N   . LYS B 1 95  ? 13.372  -38.975 3.227   1.00 22.98  ? 95   LYS B N   1 
ATOM   3557  C  CA  . LYS B 1 95  ? 13.124  -39.595 1.930   1.00 33.10  ? 95   LYS B CA  1 
ATOM   3558  C  C   . LYS B 1 95  ? 13.524  -41.067 1.874   1.00 40.67  ? 95   LYS B C   1 
ATOM   3559  O  O   . LYS B 1 95  ? 14.474  -41.508 2.556   1.00 19.47  ? 95   LYS B O   1 
ATOM   3560  C  CB  . LYS B 1 95  ? 13.869  -38.841 0.844   1.00 19.80  ? 95   LYS B CB  1 
ATOM   3561  C  CG  . LYS B 1 95  ? 15.372  -38.760 1.096   1.00 27.64  ? 95   LYS B CG  1 
ATOM   3562  C  CD  . LYS B 1 95  ? 15.903  -37.370 0.758   1.00 30.29  ? 95   LYS B CD  1 
ATOM   3563  C  CE  . LYS B 1 95  ? 17.175  -37.442 -0.049  1.00 21.05  ? 95   LYS B CE  1 
ATOM   3564  N  NZ  . LYS B 1 95  ? 18.207  -38.177 0.706   1.00 40.34  ? 95   LYS B NZ  1 
ATOM   3565  N  N   . TYR B 1 96  ? 12.782  -41.811 1.056   1.00 32.15  ? 96   TYR B N   1 
ATOM   3566  C  CA  . TYR B 1 96  ? 13.149  -43.167 0.681   1.00 37.08  ? 96   TYR B CA  1 
ATOM   3567  C  C   . TYR B 1 96  ? 13.236  -43.234 -0.830  1.00 31.88  ? 96   TYR B C   1 
ATOM   3568  O  O   . TYR B 1 96  ? 12.264  -42.888 -1.514  1.00 26.60  ? 96   TYR B O   1 
ATOM   3569  C  CB  . TYR B 1 96  ? 12.080  -44.162 1.123   1.00 34.78  ? 96   TYR B CB  1 
ATOM   3570  C  CG  . TYR B 1 96  ? 12.203  -44.647 2.534   1.00 29.56  ? 96   TYR B CG  1 
ATOM   3571  C  CD1 . TYR B 1 96  ? 13.436  -44.658 3.184   1.00 34.48  ? 96   TYR B CD1 1 
ATOM   3572  C  CD2 . TYR B 1 96  ? 11.087  -45.124 3.221   1.00 31.96  ? 96   TYR B CD2 1 
ATOM   3573  C  CE1 . TYR B 1 96  ? 13.547  -45.122 4.502   1.00 29.23  ? 96   TYR B CE1 1 
ATOM   3574  C  CE2 . TYR B 1 96  ? 11.182  -45.587 4.525   1.00 36.64  ? 96   TYR B CE2 1 
ATOM   3575  C  CZ  . TYR B 1 96  ? 12.408  -45.586 5.162   1.00 42.25  ? 96   TYR B CZ  1 
ATOM   3576  O  OH  . TYR B 1 96  ? 12.476  -46.048 6.462   1.00 49.75  ? 96   TYR B OH  1 
ATOM   3577  N  N   . ILE B 1 97  ? 14.378  -43.690 -1.346  1.00 25.60  ? 97   ILE B N   1 
ATOM   3578  C  CA  . ILE B 1 97  ? 14.514  -43.973 -2.784  1.00 35.31  ? 97   ILE B CA  1 
ATOM   3579  C  C   . ILE B 1 97  ? 14.742  -45.468 -3.086  1.00 36.22  ? 97   ILE B C   1 
ATOM   3580  O  O   . ILE B 1 97  ? 15.371  -46.188 -2.287  1.00 22.84  ? 97   ILE B O   1 
ATOM   3581  C  CB  . ILE B 1 97  ? 15.641  -43.160 -3.453  1.00 33.34  ? 97   ILE B CB  1 
ATOM   3582  C  CG1 . ILE B 1 97  ? 15.473  -41.657 -3.210  1.00 34.34  ? 97   ILE B CG1 1 
ATOM   3583  C  CG2 . ILE B 1 97  ? 15.644  -43.424 -4.945  1.00 32.12  ? 97   ILE B CG2 1 
ATOM   3584  C  CD1 . ILE B 1 97  ? 16.032  -41.156 -1.894  1.00 31.93  ? 97   ILE B CD1 1 
ATOM   3585  N  N   . ALA B 1 98  ? 14.240  -45.933 -4.236  1.00 18.49  ? 98   ALA B N   1 
ATOM   3586  C  CA  . ALA B 1 98  ? 14.451  -47.326 -4.615  1.00 18.52  ? 98   ALA B CA  1 
ATOM   3587  C  C   . ALA B 1 98  ? 14.822  -47.516 -6.078  1.00 34.13  ? 98   ALA B C   1 
ATOM   3588  O  O   . ALA B 1 98  ? 14.818  -46.573 -6.869  1.00 41.12  ? 98   ALA B O   1 
ATOM   3589  C  CB  . ALA B 1 98  ? 13.230  -48.148 -4.294  1.00 27.40  ? 98   ALA B CB  1 
ATOM   3590  N  N   . ASN B 1 99  ? 15.155  -48.755 -6.423  1.00 38.87  ? 99   ASN B N   1 
ATOM   3591  C  CA  . ASN B 1 99  ? 15.292  -49.150 -7.810  1.00 25.44  ? 99   ASN B CA  1 
ATOM   3592  C  C   . ASN B 1 99  ? 16.205  -48.242 -8.630  1.00 38.25  ? 99   ASN B C   1 
ATOM   3593  O  O   . ASN B 1 99  ? 15.990  -48.060 -9.827  1.00 48.49  ? 99   ASN B O   1 
ATOM   3594  C  CB  . ASN B 1 99  ? 13.912  -49.199 -8.447  1.00 28.40  ? 99   ASN B CB  1 
ATOM   3595  C  CG  . ASN B 1 99  ? 13.899  -49.967 -9.737  1.00 46.12  ? 99   ASN B CG  1 
ATOM   3596  O  OD1 . ASN B 1 99  ? 13.271  -49.543 -10.722 1.00 45.55  ? 99   ASN B OD1 1 
ATOM   3597  N  ND2 . ASN B 1 99  ? 14.598  -51.111 -9.754  1.00 40.07  ? 99   ASN B ND2 1 
ATOM   3598  N  N   . MET B 1 100 ? 17.222  -47.669 -8.000  1.00 36.69  ? 100  MET B N   1 
ATOM   3599  C  CA  . MET B 1 100 ? 18.247  -46.966 -8.764  1.00 42.71  ? 100  MET B CA  1 
ATOM   3600  C  C   . MET B 1 100 ? 18.973  -47.954 -9.698  1.00 38.14  ? 100  MET B C   1 
ATOM   3601  O  O   . MET B 1 100 ? 19.380  -47.602 -10.810 1.00 39.28  ? 100  MET B O   1 
ATOM   3602  C  CB  . MET B 1 100 ? 19.222  -46.210 -7.840  1.00 43.69  ? 100  MET B CB  1 
ATOM   3603  C  CG  . MET B 1 100 ? 20.320  -47.055 -7.194  1.00 53.28  ? 100  MET B CG  1 
ATOM   3604  S  SD  . MET B 1 100 ? 21.461  -46.091 -6.167  1.00 38.42  ? 100  MET B SD  1 
ATOM   3605  C  CE  . MET B 1 100 ? 21.810  -44.706 -7.250  1.00 30.42  ? 100  MET B CE  1 
ATOM   3606  N  N   . HIS B 1 101 ? 19.129  -49.190 -9.231  1.00 33.20  ? 101  HIS B N   1 
ATOM   3607  C  CA  . HIS B 1 101 ? 19.546  -50.281 -10.090 1.00 30.88  ? 101  HIS B CA  1 
ATOM   3608  C  C   . HIS B 1 101 ? 18.260  -50.951 -10.578 1.00 37.30  ? 101  HIS B C   1 
ATOM   3609  O  O   . HIS B 1 101 ? 17.574  -51.661 -9.840  1.00 25.17  ? 101  HIS B O   1 
ATOM   3610  C  CB  . HIS B 1 101 ? 20.479  -51.247 -9.353  1.00 19.09  ? 101  HIS B CB  1 
ATOM   3611  C  CG  . HIS B 1 101 ? 21.823  -50.664 -9.023  1.00 37.20  ? 101  HIS B CG  1 
ATOM   3612  N  ND1 . HIS B 1 101 ? 22.231  -50.419 -7.731  1.00 46.69  ? 101  HIS B ND1 1 
ATOM   3613  C  CD2 . HIS B 1 101 ? 22.847  -50.266 -9.817  1.00 52.07  ? 101  HIS B CD2 1 
ATOM   3614  C  CE1 . HIS B 1 101 ? 23.452  -49.913 -7.739  1.00 47.40  ? 101  HIS B CE1 1 
ATOM   3615  N  NE2 . HIS B 1 101 ? 23.845  -49.804 -8.994  1.00 51.57  ? 101  HIS B NE2 1 
ATOM   3616  N  N   . GLY B 1 102 ? 17.914  -50.670 -11.827 1.00 35.12  ? 102  GLY B N   1 
ATOM   3617  C  CA  . GLY B 1 102 ? 16.623  -51.050 -12.352 1.00 26.88  ? 102  GLY B CA  1 
ATOM   3618  C  C   . GLY B 1 102 ? 16.298  -52.498 -12.089 1.00 30.29  ? 102  GLY B C   1 
ATOM   3619  O  O   . GLY B 1 102 ? 15.134  -52.858 -11.979 1.00 56.71  ? 102  GLY B O   1 
ATOM   3620  N  N   . ASP B 1 103 ? 17.315  -53.335 -11.984 1.00 30.12  ? 103  ASP B N   1 
ATOM   3621  C  CA  . ASP B 1 103 ? 17.077  -54.765 -11.870 1.00 44.50  ? 103  ASP B CA  1 
ATOM   3622  C  C   . ASP B 1 103 ? 17.042  -55.206 -10.420 1.00 33.02  ? 103  ASP B C   1 
ATOM   3623  O  O   . ASP B 1 103 ? 16.982  -56.403 -10.133 1.00 43.68  ? 103  ASP B O   1 
ATOM   3624  C  CB  . ASP B 1 103 ? 18.124  -55.559 -12.651 1.00 49.33  ? 103  ASP B CB  1 
ATOM   3625  C  CG  . ASP B 1 103 ? 19.533  -55.162 -12.286 1.00 55.41  ? 103  ASP B CG  1 
ATOM   3626  O  OD1 . ASP B 1 103 ? 20.472  -55.586 -12.993 1.00 65.28  ? 103  ASP B OD1 1 
ATOM   3627  O  OD2 . ASP B 1 103 ? 19.699  -54.415 -11.294 1.00 61.97  ? 103  ASP B OD2 1 
ATOM   3628  N  N   . GLU B 1 104 ? 17.075  -54.233 -9.514  1.00 30.13  ? 104  GLU B N   1 
ATOM   3629  C  CA  . GLU B 1 104 ? 16.887  -54.490 -8.080  1.00 20.55  ? 104  GLU B CA  1 
ATOM   3630  C  C   . GLU B 1 104 ? 15.555  -53.895 -7.652  1.00 26.77  ? 104  GLU B C   1 
ATOM   3631  O  O   . GLU B 1 104 ? 15.449  -52.690 -7.442  1.00 35.94  ? 104  GLU B O   1 
ATOM   3632  C  CB  . GLU B 1 104 ? 18.042  -53.890 -7.284  1.00 25.07  ? 104  GLU B CB  1 
ATOM   3633  C  CG  . GLU B 1 104 ? 19.447  -54.307 -7.813  1.00 52.74  ? 104  GLU B CG  1 
ATOM   3634  C  CD  . GLU B 1 104 ? 20.587  -53.582 -7.114  1.00 55.06  ? 104  GLU B CD  1 
ATOM   3635  O  OE1 . GLU B 1 104 ? 20.325  -52.918 -6.093  1.00 64.92  ? 104  GLU B OE1 1 
ATOM   3636  O  OE2 . GLU B 1 104 ? 21.740  -53.668 -7.581  1.00 59.49  ? 104  GLU B OE2 1 
ATOM   3637  N  N   . THR B 1 105 ? 14.540  -54.746 -7.522  1.00 32.89  ? 105  THR B N   1 
ATOM   3638  C  CA  . THR B 1 105 ? 13.154  -54.299 -7.670  1.00 36.41  ? 105  THR B CA  1 
ATOM   3639  C  C   . THR B 1 105 ? 12.268  -54.333 -6.427  1.00 31.78  ? 105  THR B C   1 
ATOM   3640  O  O   . THR B 1 105 ? 11.272  -53.608 -6.351  1.00 27.28  ? 105  THR B O   1 
ATOM   3641  C  CB  . THR B 1 105 ? 12.431  -55.108 -8.773  1.00 43.94  ? 105  THR B CB  1 
ATOM   3642  O  OG1 . THR B 1 105 ? 12.440  -56.503 -8.425  1.00 44.58  ? 105  THR B OG1 1 
ATOM   3643  C  CG2 . THR B 1 105 ? 13.107  -54.909 -10.130 1.00 41.67  ? 105  THR B CG2 1 
ATOM   3644  N  N   . VAL B 1 106 ? 12.601  -55.183 -5.468  1.00 27.35  ? 106  VAL B N   1 
ATOM   3645  C  CA  . VAL B 1 106 ? 11.755  -55.341 -4.290  1.00 29.91  ? 106  VAL B CA  1 
ATOM   3646  C  C   . VAL B 1 106 ? 11.488  -54.010 -3.577  1.00 30.15  ? 106  VAL B C   1 
ATOM   3647  O  O   . VAL B 1 106 ? 10.341  -53.684 -3.247  1.00 31.28  ? 106  VAL B O   1 
ATOM   3648  C  CB  . VAL B 1 106 ? 12.361  -56.342 -3.304  1.00 45.60  ? 106  VAL B CB  1 
ATOM   3649  C  CG1 . VAL B 1 106 ? 11.494  -56.463 -2.055  1.00 37.95  ? 106  VAL B CG1 1 
ATOM   3650  C  CG2 . VAL B 1 106 ? 12.548  -57.691 -3.982  1.00 39.80  ? 106  VAL B CG2 1 
ATOM   3651  N  N   . GLY B 1 107 ? 12.545  -53.245 -3.334  1.00 39.78  ? 107  GLY B N   1 
ATOM   3652  C  CA  . GLY B 1 107 ? 12.412  -51.929 -2.729  1.00 38.00  ? 107  GLY B CA  1 
ATOM   3653  C  C   . GLY B 1 107 ? 11.430  -51.017 -3.448  1.00 33.95  ? 107  GLY B C   1 
ATOM   3654  O  O   . GLY B 1 107 ? 10.677  -50.283 -2.827  1.00 42.23  ? 107  GLY B O   1 
ATOM   3655  N  N   . ARG B 1 108 ? 11.454  -51.058 -4.768  1.00 26.68  ? 108  ARG B N   1 
ATOM   3656  C  CA  . ARG B 1 108 ? 10.487  -50.359 -5.591  1.00 31.08  ? 108  ARG B CA  1 
ATOM   3657  C  C   . ARG B 1 108 ? 9.054   -50.626 -5.134  1.00 34.68  ? 108  ARG B C   1 
ATOM   3658  O  O   . ARG B 1 108 ? 8.300   -49.702 -4.818  1.00 41.72  ? 108  ARG B O   1 
ATOM   3659  C  CB  . ARG B 1 108 ? 10.684  -50.824 -7.032  1.00 37.89  ? 108  ARG B CB  1 
ATOM   3660  C  CG  . ARG B 1 108 ? 9.540   -50.589 -7.949  1.00 35.76  ? 108  ARG B CG  1 
ATOM   3661  C  CD  . ARG B 1 108 ? 9.956   -51.034 -9.330  1.00 42.21  ? 108  ARG B CD  1 
ATOM   3662  N  NE  . ARG B 1 108 ? 8.937   -50.645 -10.274 1.00 43.07  ? 108  ARG B NE  1 
ATOM   3663  C  CZ  . ARG B 1 108 ? 9.054   -49.724 -11.217 1.00 36.19  ? 108  ARG B CZ  1 
ATOM   3664  N  NH1 . ARG B 1 108 ? 7.994   -49.474 -11.970 1.00 30.88  ? 108  ARG B NH1 1 
ATOM   3665  N  NH2 . ARG B 1 108 ? 10.196  -49.070 -11.415 1.00 44.19  ? 108  ARG B NH2 1 
ATOM   3666  N  N   . GLN B 1 109 ? 8.677   -51.898 -5.089  1.00 43.85  ? 109  GLN B N   1 
ATOM   3667  C  CA  . GLN B 1 109 ? 7.323   -52.265 -4.692  1.00 44.63  ? 109  GLN B CA  1 
ATOM   3668  C  C   . GLN B 1 109 ? 7.034   -51.951 -3.228  1.00 37.18  ? 109  GLN B C   1 
ATOM   3669  O  O   . GLN B 1 109 ? 5.910   -51.600 -2.866  1.00 31.84  ? 109  GLN B O   1 
ATOM   3670  C  CB  . GLN B 1 109 ? 7.060   -53.742 -4.987  1.00 49.58  ? 109  GLN B CB  1 
ATOM   3671  C  CG  . GLN B 1 109 ? 6.498   -53.977 -6.381  1.00 54.37  ? 109  GLN B CG  1 
ATOM   3672  C  CD  . GLN B 1 109 ? 5.257   -53.129 -6.669  1.00 54.19  ? 109  GLN B CD  1 
ATOM   3673  O  OE1 . GLN B 1 109 ? 5.210   -52.406 -7.668  1.00 65.28  ? 109  GLN B OE1 1 
ATOM   3674  N  NE2 . GLN B 1 109 ? 4.253   -53.209 -5.789  1.00 38.18  ? 109  GLN B NE2 1 
ATOM   3675  N  N   . LEU B 1 110 ? 8.049   -52.092 -2.387  1.00 32.12  ? 110  LEU B N   1 
ATOM   3676  C  CA  . LEU B 1 110 ? 7.880   -51.818 -0.966  1.00 32.71  ? 110  LEU B CA  1 
ATOM   3677  C  C   . LEU B 1 110 ? 7.515   -50.354 -0.738  1.00 40.82  ? 110  LEU B C   1 
ATOM   3678  O  O   . LEU B 1 110 ? 6.750   -50.018 0.168   1.00 46.67  ? 110  LEU B O   1 
ATOM   3679  C  CB  . LEU B 1 110 ? 9.155   -52.174 -0.200  1.00 40.84  ? 110  LEU B CB  1 
ATOM   3680  C  CG  . LEU B 1 110 ? 9.464   -53.659 -0.024  1.00 36.78  ? 110  LEU B CG  1 
ATOM   3681  C  CD1 . LEU B 1 110 ? 10.732  -53.855 0.812   1.00 37.59  ? 110  LEU B CD1 1 
ATOM   3682  C  CD2 . LEU B 1 110 ? 8.266   -54.320 0.619   1.00 22.82  ? 110  LEU B CD2 1 
ATOM   3683  N  N   . LEU B 1 111 ? 8.059   -49.473 -1.567  1.00 43.71  ? 111  LEU B N   1 
ATOM   3684  C  CA  . LEU B 1 111 ? 7.784   -48.052 -1.417  1.00 34.10  ? 111  LEU B CA  1 
ATOM   3685  C  C   . LEU B 1 111 ? 6.396   -47.753 -1.923  1.00 32.22  ? 111  LEU B C   1 
ATOM   3686  O  O   . LEU B 1 111 ? 5.714   -46.884 -1.396  1.00 41.06  ? 111  LEU B O   1 
ATOM   3687  C  CB  . LEU B 1 111 ? 8.831   -47.213 -2.145  1.00 41.71  ? 111  LEU B CB  1 
ATOM   3688  C  CG  . LEU B 1 111 ? 10.213  -47.251 -1.468  1.00 40.44  ? 111  LEU B CG  1 
ATOM   3689  C  CD1 . LEU B 1 111 ? 11.164  -46.246 -2.091  1.00 33.99  ? 111  LEU B CD1 1 
ATOM   3690  C  CD2 . LEU B 1 111 ? 10.104  -47.009 0.047   1.00 42.66  ? 111  LEU B CD2 1 
ATOM   3691  N  N   . VAL B 1 112 ? 5.982   -48.492 -2.946  1.00 37.43  ? 112  VAL B N   1 
ATOM   3692  C  CA  . VAL B 1 112 ? 4.615   -48.406 -3.457  1.00 35.98  ? 112  VAL B CA  1 
ATOM   3693  C  C   . VAL B 1 112 ? 3.602   -48.868 -2.405  1.00 36.46  ? 112  VAL B C   1 
ATOM   3694  O  O   . VAL B 1 112 ? 2.524   -48.298 -2.262  1.00 39.48  ? 112  VAL B O   1 
ATOM   3695  C  CB  . VAL B 1 112 ? 4.443   -49.260 -4.736  1.00 38.79  ? 112  VAL B CB  1 
ATOM   3696  C  CG1 . VAL B 1 112 ? 2.994   -49.565 -4.959  1.00 21.49  ? 112  VAL B CG1 1 
ATOM   3697  C  CG2 . VAL B 1 112 ? 5.043   -48.550 -5.953  1.00 34.45  ? 112  VAL B CG2 1 
ATOM   3698  N  N   . TYR B 1 113 ? 3.960   -49.917 -1.676  1.00 40.93  ? 113  TYR B N   1 
ATOM   3699  C  CA  . TYR B 1 113 ? 3.154   -50.421 -0.574  1.00 39.25  ? 113  TYR B CA  1 
ATOM   3700  C  C   . TYR B 1 113 ? 3.130   -49.441 0.612   1.00 44.40  ? 113  TYR B C   1 
ATOM   3701  O  O   . TYR B 1 113 ? 2.099   -49.235 1.273   1.00 38.35  ? 113  TYR B O   1 
ATOM   3702  C  CB  . TYR B 1 113 ? 3.733   -51.755 -0.101  1.00 40.08  ? 113  TYR B CB  1 
ATOM   3703  C  CG  . TYR B 1 113 ? 3.537   -52.915 -1.052  1.00 45.75  ? 113  TYR B CG  1 
ATOM   3704  C  CD1 . TYR B 1 113 ? 4.284   -54.077 -0.916  1.00 50.51  ? 113  TYR B CD1 1 
ATOM   3705  C  CD2 . TYR B 1 113 ? 2.605   -52.855 -2.072  1.00 50.37  ? 113  TYR B CD2 1 
ATOM   3706  C  CE1 . TYR B 1 113 ? 4.114   -55.151 -1.769  1.00 52.09  ? 113  TYR B CE1 1 
ATOM   3707  C  CE2 . TYR B 1 113 ? 2.421   -53.927 -2.934  1.00 54.04  ? 113  TYR B CE2 1 
ATOM   3708  C  CZ  . TYR B 1 113 ? 3.179   -55.077 -2.779  1.00 56.85  ? 113  TYR B CZ  1 
ATOM   3709  O  OH  . TYR B 1 113 ? 3.010   -56.157 -3.630  1.00 55.42  ? 113  TYR B OH  1 
ATOM   3710  N  N   . MET B 1 114 ? 4.282   -48.852 0.900   1.00 45.19  ? 114  MET B N   1 
ATOM   3711  C  CA  . MET B 1 114 ? 4.378   -47.923 2.016   1.00 40.74  ? 114  MET B CA  1 
ATOM   3712  C  C   . MET B 1 114 ? 3.425   -46.756 1.779   1.00 46.38  ? 114  MET B C   1 
ATOM   3713  O  O   . MET B 1 114 ? 2.574   -46.448 2.626   1.00 52.30  ? 114  MET B O   1 
ATOM   3714  C  CB  . MET B 1 114 ? 5.818   -47.446 2.189   1.00 30.49  ? 114  MET B CB  1 
ATOM   3715  C  CG  . MET B 1 114 ? 6.048   -46.475 3.337   1.00 34.29  ? 114  MET B CG  1 
ATOM   3716  S  SD  . MET B 1 114 ? 5.616   -47.146 4.939   1.00 35.32  ? 114  MET B SD  1 
ATOM   3717  C  CE  . MET B 1 114 ? 6.668   -48.579 5.014   1.00 65.78  ? 114  MET B CE  1 
ATOM   3718  N  N   . ALA B 1 115 ? 3.549   -46.125 0.617   1.00 30.73  ? 115  ALA B N   1 
ATOM   3719  C  CA  . ALA B 1 115 ? 2.715   -44.982 0.296   1.00 30.99  ? 115  ALA B CA  1 
ATOM   3720  C  C   . ALA B 1 115 ? 1.287   -45.295 0.707   1.00 36.71  ? 115  ALA B C   1 
ATOM   3721  O  O   . ALA B 1 115 ? 0.781   -44.732 1.676   1.00 43.25  ? 115  ALA B O   1 
ATOM   3722  C  CB  . ALA B 1 115 ? 2.804   -44.663 -1.186  1.00 31.10  ? 115  ALA B CB  1 
ATOM   3723  N  N   . GLN B 1 116 ? 0.663   -46.220 -0.024  1.00 44.51  ? 116  GLN B N   1 
ATOM   3724  C  CA  . GLN B 1 116 ? -0.678  -46.733 0.282   1.00 40.29  ? 116  GLN B CA  1 
ATOM   3725  C  C   . GLN B 1 116 ? -0.872  -47.020 1.763   1.00 44.31  ? 116  GLN B C   1 
ATOM   3726  O  O   . GLN B 1 116 ? -1.766  -46.456 2.404   1.00 54.34  ? 116  GLN B O   1 
ATOM   3727  C  CB  . GLN B 1 116 ? -0.954  -48.009 -0.525  1.00 32.19  ? 116  GLN B CB  1 
ATOM   3728  C  CG  . GLN B 1 116 ? -0.924  -47.775 -2.038  1.00 38.37  ? 116  GLN B CG  1 
ATOM   3729  C  CD  . GLN B 1 116 ? -1.094  -49.049 -2.831  1.00 42.77  ? 116  GLN B CD  1 
ATOM   3730  O  OE1 . GLN B 1 116 ? -2.210  -49.416 -3.229  1.00 41.33  ? 116  GLN B OE1 1 
ATOM   3731  N  NE2 . GLN B 1 116 ? 0.017   -49.732 -3.073  1.00 43.52  ? 116  GLN B NE2 1 
ATOM   3732  N  N   . TYR B 1 117 ? -0.031  -47.895 2.305   1.00 37.85  ? 117  TYR B N   1 
ATOM   3733  C  CA  . TYR B 1 117 ? -0.115  -48.246 3.713   1.00 35.58  ? 117  TYR B CA  1 
ATOM   3734  C  C   . TYR B 1 117 ? -0.272  -47.015 4.610   1.00 35.90  ? 117  TYR B C   1 
ATOM   3735  O  O   . TYR B 1 117 ? -1.229  -46.916 5.384   1.00 39.20  ? 117  TYR B O   1 
ATOM   3736  C  CB  . TYR B 1 117 ? 1.117   -49.031 4.124   1.00 33.82  ? 117  TYR B CB  1 
ATOM   3737  C  CG  . TYR B 1 117 ? 1.075   -49.534 5.552   1.00 37.82  ? 117  TYR B CG  1 
ATOM   3738  C  CD1 . TYR B 1 117 ? 0.388   -50.693 5.885   1.00 36.73  ? 117  TYR B CD1 1 
ATOM   3739  C  CD2 . TYR B 1 117 ? 1.735   -48.853 6.561   1.00 34.85  ? 117  TYR B CD2 1 
ATOM   3740  C  CE1 . TYR B 1 117 ? 0.364   -51.152 7.179   1.00 41.81  ? 117  TYR B CE1 1 
ATOM   3741  C  CE2 . TYR B 1 117 ? 1.721   -49.307 7.854   1.00 35.22  ? 117  TYR B CE2 1 
ATOM   3742  C  CZ  . TYR B 1 117 ? 1.034   -50.450 8.158   1.00 42.08  ? 117  TYR B CZ  1 
ATOM   3743  O  OH  . TYR B 1 117 ? 1.029   -50.890 9.458   1.00 53.17  ? 117  TYR B OH  1 
ATOM   3744  N  N   . LEU B 1 118 ? 0.663   -46.077 4.494   1.00 40.07  ? 118  LEU B N   1 
ATOM   3745  C  CA  . LEU B 1 118 ? 0.661   -44.890 5.349   1.00 43.61  ? 118  LEU B CA  1 
ATOM   3746  C  C   . LEU B 1 118 ? -0.608  -44.060 5.214   1.00 50.85  ? 118  LEU B C   1 
ATOM   3747  O  O   . LEU B 1 118 ? -1.281  -43.789 6.208   1.00 62.23  ? 118  LEU B O   1 
ATOM   3748  C  CB  . LEU B 1 118 ? 1.885   -44.021 5.087   1.00 44.90  ? 118  LEU B CB  1 
ATOM   3749  C  CG  . LEU B 1 118 ? 3.190   -44.548 5.695   1.00 45.10  ? 118  LEU B CG  1 
ATOM   3750  C  CD1 . LEU B 1 118 ? 4.366   -43.673 5.283   1.00 48.51  ? 118  LEU B CD1 1 
ATOM   3751  C  CD2 . LEU B 1 118 ? 3.075   -44.620 7.217   1.00 45.98  ? 118  LEU B CD2 1 
ATOM   3752  N  N   . LEU B 1 119 ? -0.937  -43.657 3.992   1.00 44.82  ? 119  LEU B N   1 
ATOM   3753  C  CA  . LEU B 1 119 ? -2.151  -42.878 3.765   1.00 50.70  ? 119  LEU B CA  1 
ATOM   3754  C  C   . LEU B 1 119 ? -3.391  -43.599 4.295   1.00 54.87  ? 119  LEU B C   1 
ATOM   3755  O  O   . LEU B 1 119 ? -4.141  -43.061 5.118   1.00 48.90  ? 119  LEU B O   1 
ATOM   3756  C  CB  . LEU B 1 119 ? -2.318  -42.553 2.279   1.00 42.32  ? 119  LEU B CB  1 
ATOM   3757  C  CG  . LEU B 1 119 ? -1.486  -41.343 1.864   1.00 44.64  ? 119  LEU B CG  1 
ATOM   3758  C  CD1 . LEU B 1 119 ? -1.502  -41.134 0.349   1.00 46.02  ? 119  LEU B CD1 1 
ATOM   3759  C  CD2 . LEU B 1 119 ? -1.982  -40.109 2.581   1.00 29.55  ? 119  LEU B CD2 1 
ATOM   3760  N  N   . GLY B 1 120 ? -3.589  -44.827 3.826   1.00 50.83  ? 120  GLY B N   1 
ATOM   3761  C  CA  . GLY B 1 120 ? -4.786  -45.583 4.135   1.00 45.49  ? 120  GLY B CA  1 
ATOM   3762  C  C   . GLY B 1 120 ? -4.939  -45.941 5.598   1.00 44.15  ? 120  GLY B C   1 
ATOM   3763  O  O   . GLY B 1 120 ? -6.030  -46.318 6.037   1.00 50.38  ? 120  GLY B O   1 
ATOM   3764  N  N   . ASN B 1 121 ? -3.860  -45.824 6.364   1.00 40.66  ? 121  ASN B N   1 
ATOM   3765  C  CA  . ASN B 1 121 ? -3.923  -46.226 7.767   1.00 50.40  ? 121  ASN B CA  1 
ATOM   3766  C  C   . ASN B 1 121 ? -3.668  -45.128 8.808   1.00 48.24  ? 121  ASN B C   1 
ATOM   3767  O  O   . ASN B 1 121 ? -4.022  -45.282 9.977   1.00 58.90  ? 121  ASN B O   1 
ATOM   3768  C  CB  . ASN B 1 121 ? -3.006  -47.427 8.017   1.00 52.23  ? 121  ASN B CB  1 
ATOM   3769  C  CG  . ASN B 1 121 ? -3.564  -48.716 7.436   1.00 49.23  ? 121  ASN B CG  1 
ATOM   3770  O  OD1 . ASN B 1 121 ? -4.311  -49.433 8.102   1.00 42.89  ? 121  ASN B OD1 1 
ATOM   3771  N  ND2 . ASN B 1 121 ? -3.207  -49.013 6.189   1.00 54.97  ? 121  ASN B ND2 1 
ATOM   3772  N  N   . HIS B 1 122 ? -3.083  -44.018 8.378   1.00 34.62  ? 122  HIS B N   1 
ATOM   3773  C  CA  . HIS B 1 122 ? -2.674  -42.961 9.297   1.00 39.68  ? 122  HIS B CA  1 
ATOM   3774  C  C   . HIS B 1 122 ? -3.807  -42.421 10.171  1.00 48.31  ? 122  HIS B C   1 
ATOM   3775  O  O   . HIS B 1 122 ? -3.586  -42.047 11.324  1.00 52.45  ? 122  HIS B O   1 
ATOM   3776  C  CB  . HIS B 1 122 ? -1.984  -41.826 8.534   1.00 59.45  ? 122  HIS B CB  1 
ATOM   3777  C  CG  . HIS B 1 122 ? -2.924  -40.799 7.980   1.00 61.89  ? 122  HIS B CG  1 
ATOM   3778  N  ND1 . HIS B 1 122 ? -3.504  -40.910 6.735   1.00 62.91  ? 122  HIS B ND1 1 
ATOM   3779  C  CD2 . HIS B 1 122 ? -3.365  -39.626 8.496   1.00 55.77  ? 122  HIS B CD2 1 
ATOM   3780  C  CE1 . HIS B 1 122 ? -4.266  -39.853 6.509   1.00 63.87  ? 122  HIS B CE1 1 
ATOM   3781  N  NE2 . HIS B 1 122 ? -4.198  -39.060 7.563   1.00 59.70  ? 122  HIS B NE2 1 
ATOM   3782  N  N   . GLU B 1 123 ? -5.023  -42.384 9.642   1.00 56.36  ? 123  GLU B N   1 
ATOM   3783  C  CA  . GLU B 1 123 ? -6.141  -41.926 10.458  1.00 60.50  ? 123  GLU B CA  1 
ATOM   3784  C  C   . GLU B 1 123 ? -6.668  -43.010 11.373  1.00 51.93  ? 123  GLU B C   1 
ATOM   3785  O  O   . GLU B 1 123 ? -7.235  -42.707 12.417  1.00 52.42  ? 123  GLU B O   1 
ATOM   3786  C  CB  . GLU B 1 123 ? -7.264  -41.333 9.607   1.00 70.65  ? 123  GLU B CB  1 
ATOM   3787  C  CG  . GLU B 1 123 ? -6.902  -39.973 9.028   1.00 89.50  ? 123  GLU B CG  1 
ATOM   3788  C  CD  . GLU B 1 123 ? -8.119  -39.138 8.677   1.00 108.30 ? 123  GLU B CD  1 
ATOM   3789  O  OE1 . GLU B 1 123 ? -9.212  -39.720 8.509   1.00 113.09 ? 123  GLU B OE1 1 
ATOM   3790  O  OE2 . GLU B 1 123 ? -7.987  -37.898 8.567   1.00 115.22 ? 123  GLU B OE2 1 
ATOM   3791  N  N   . ARG B 1 124 ? -6.467  -44.269 10.993  1.00 51.23  ? 124  ARG B N   1 
ATOM   3792  C  CA  . ARG B 1 124 ? -6.959  -45.384 11.796  1.00 46.84  ? 124  ARG B CA  1 
ATOM   3793  C  C   . ARG B 1 124 ? -5.986  -45.843 12.876  1.00 49.44  ? 124  ARG B C   1 
ATOM   3794  O  O   . ARG B 1 124 ? -6.403  -46.137 13.995  1.00 59.53  ? 124  ARG B O   1 
ATOM   3795  C  CB  . ARG B 1 124 ? -7.336  -46.577 10.926  1.00 58.67  ? 124  ARG B CB  1 
ATOM   3796  C  CG  . ARG B 1 124 ? -6.976  -46.450 9.473   1.00 73.13  ? 124  ARG B CG  1 
ATOM   3797  C  CD  . ARG B 1 124 ? -6.956  -47.834 8.826   1.00 80.91  ? 124  ARG B CD  1 
ATOM   3798  N  NE  . ARG B 1 124 ? -8.049  -48.691 9.285   1.00 81.82  ? 124  ARG B NE  1 
ATOM   3799  C  CZ  . ARG B 1 124 ? -9.152  -48.941 8.587   1.00 85.18  ? 124  ARG B CZ  1 
ATOM   3800  N  NH1 . ARG B 1 124 ? -9.320  -48.403 7.386   1.00 87.88  ? 124  ARG B NH1 1 
ATOM   3801  N  NH2 . ARG B 1 124 ? -10.087 -49.733 9.088   1.00 85.47  ? 124  ARG B NH2 1 
ATOM   3802  N  N   . ILE B 1 125 ? -4.700  -45.918 12.546  1.00 41.32  ? 125  ILE B N   1 
ATOM   3803  C  CA  . ILE B 1 125 ? -3.694  -46.395 13.503  1.00 51.26  ? 125  ILE B CA  1 
ATOM   3804  C  C   . ILE B 1 125 ? -2.851  -45.266 14.100  1.00 55.48  ? 125  ILE B C   1 
ATOM   3805  O  O   . ILE B 1 125 ? -2.123  -44.584 13.384  1.00 56.14  ? 125  ILE B O   1 
ATOM   3806  C  CB  . ILE B 1 125 ? -2.753  -47.454 12.886  1.00 48.93  ? 125  ILE B CB  1 
ATOM   3807  C  CG1 . ILE B 1 125 ? -3.434  -48.830 12.834  1.00 51.80  ? 125  ILE B CG1 1 
ATOM   3808  C  CG2 . ILE B 1 125 ? -1.491  -47.561 13.712  1.00 42.32  ? 125  ILE B CG2 1 
ATOM   3809  C  CD1 . ILE B 1 125 ? -4.600  -48.931 11.866  1.00 53.60  ? 125  ILE B CD1 1 
ATOM   3810  N  N   . SER B 1 126 ? -2.948  -45.100 15.420  1.00 67.75  ? 126  SER B N   1 
ATOM   3811  C  CA  . SER B 1 126 ? -2.337  -43.979 16.149  1.00 68.83  ? 126  SER B CA  1 
ATOM   3812  C  C   . SER B 1 126 ? -0.847  -43.794 15.843  1.00 66.70  ? 126  SER B C   1 
ATOM   3813  O  O   . SER B 1 126 ? -0.408  -42.700 15.481  1.00 60.53  ? 126  SER B O   1 
ATOM   3814  C  CB  . SER B 1 126 ? -2.556  -44.143 17.667  1.00 69.88  ? 126  SER B CB  1 
ATOM   3815  O  OG  . SER B 1 126 ? -2.491  -42.901 18.357  1.00 69.50  ? 126  SER B OG  1 
ATOM   3816  N  N   . ASP B 1 127 ? -0.072  -44.862 15.996  1.00 66.26  ? 127  ASP B N   1 
ATOM   3817  C  CA  . ASP B 1 127 ? 1.361   -44.800 15.732  1.00 61.08  ? 127  ASP B CA  1 
ATOM   3818  C  C   . ASP B 1 127 ? 1.649   -44.091 14.421  1.00 48.78  ? 127  ASP B C   1 
ATOM   3819  O  O   . ASP B 1 127 ? 2.430   -43.143 14.378  1.00 48.74  ? 127  ASP B O   1 
ATOM   3820  C  CB  . ASP B 1 127 ? 1.963   -46.205 15.712  1.00 73.57  ? 127  ASP B CB  1 
ATOM   3821  C  CG  . ASP B 1 127 ? 2.204   -46.755 17.108  1.00 89.11  ? 127  ASP B CG  1 
ATOM   3822  O  OD1 . ASP B 1 127 ? 2.564   -45.956 18.003  1.00 91.18  ? 127  ASP B OD1 1 
ATOM   3823  O  OD2 . ASP B 1 127 ? 2.040   -47.982 17.308  1.00 90.90  ? 127  ASP B OD2 1 
ATOM   3824  N  N   . LEU B 1 128 ? 1.009   -44.557 13.356  1.00 41.66  ? 128  LEU B N   1 
ATOM   3825  C  CA  . LEU B 1 128 ? 1.230   -44.004 12.027  1.00 44.33  ? 128  LEU B CA  1 
ATOM   3826  C  C   . LEU B 1 128 ? 0.732   -42.562 11.945  1.00 48.52  ? 128  LEU B C   1 
ATOM   3827  O  O   . LEU B 1 128 ? 1.405   -41.682 11.392  1.00 41.18  ? 128  LEU B O   1 
ATOM   3828  C  CB  . LEU B 1 128 ? 0.502   -44.849 10.987  1.00 46.96  ? 128  LEU B CB  1 
ATOM   3829  C  CG  . LEU B 1 128 ? 0.853   -46.334 10.939  1.00 43.57  ? 128  LEU B CG  1 
ATOM   3830  C  CD1 . LEU B 1 128 ? -0.090  -47.074 9.980   1.00 46.33  ? 128  LEU B CD1 1 
ATOM   3831  C  CD2 . LEU B 1 128 ? 2.314   -46.520 10.547  1.00 42.52  ? 128  LEU B CD2 1 
ATOM   3832  N  N   . GLY B 1 129 ? -0.457  -42.333 12.490  1.00 36.42  ? 129  GLY B N   1 
ATOM   3833  C  CA  . GLY B 1 129 ? -1.044  -41.009 12.495  1.00 54.65  ? 129  GLY B CA  1 
ATOM   3834  C  C   . GLY B 1 129 ? -0.101  -40.035 13.161  1.00 52.60  ? 129  GLY B C   1 
ATOM   3835  O  O   . GLY B 1 129 ? -0.055  -38.849 12.821  1.00 56.22  ? 129  GLY B O   1 
ATOM   3836  N  N   . GLN B 1 130 ? 0.666   -40.550 14.112  1.00 25.55  ? 130  GLN B N   1 
ATOM   3837  C  CA  . GLN B 1 130 ? 1.623   -39.732 14.824  1.00 36.50  ? 130  GLN B CA  1 
ATOM   3838  C  C   . GLN B 1 130 ? 2.916   -39.616 14.020  1.00 42.77  ? 130  GLN B C   1 
ATOM   3839  O  O   . GLN B 1 130 ? 3.516   -38.535 13.954  1.00 44.54  ? 130  GLN B O   1 
ATOM   3840  C  CB  . GLN B 1 130 ? 1.882   -40.304 16.211  1.00 41.54  ? 130  GLN B CB  1 
ATOM   3841  C  CG  . GLN B 1 130 ? 2.310   -39.268 17.218  1.00 51.83  ? 130  GLN B CG  1 
ATOM   3842  C  CD  . GLN B 1 130 ? 3.766   -38.868 17.069  1.00 56.05  ? 130  GLN B CD  1 
ATOM   3843  O  OE1 . GLN B 1 130 ? 4.570   -39.590 16.463  1.00 49.69  ? 130  GLN B OE1 1 
ATOM   3844  N  NE2 . GLN B 1 130 ? 4.120   -37.715 17.635  1.00 63.12  ? 130  GLN B NE2 1 
ATOM   3845  N  N   . LEU B 1 131 ? 3.338   -40.718 13.398  1.00 44.86  ? 131  LEU B N   1 
ATOM   3846  C  CA  . LEU B 1 131 ? 4.472   -40.679 12.475  1.00 29.72  ? 131  LEU B CA  1 
ATOM   3847  C  C   . LEU B 1 131 ? 4.255   -39.566 11.476  1.00 24.49  ? 131  LEU B C   1 
ATOM   3848  O  O   . LEU B 1 131 ? 5.066   -38.653 11.377  1.00 32.11  ? 131  LEU B O   1 
ATOM   3849  C  CB  . LEU B 1 131 ? 4.619   -41.999 11.722  1.00 31.50  ? 131  LEU B CB  1 
ATOM   3850  C  CG  . LEU B 1 131 ? 5.786   -42.075 10.717  1.00 42.69  ? 131  LEU B CG  1 
ATOM   3851  C  CD1 . LEU B 1 131 ? 7.138   -41.953 11.415  1.00 32.18  ? 131  LEU B CD1 1 
ATOM   3852  C  CD2 . LEU B 1 131 ? 5.731   -43.356 9.890   1.00 42.91  ? 131  LEU B CD2 1 
ATOM   3853  N  N   . VAL B 1 132 ? 3.136   -39.643 10.757  1.00 31.09  ? 132  VAL B N   1 
ATOM   3854  C  CA  . VAL B 1 132 ? 2.813   -38.710 9.676   1.00 30.89  ? 132  VAL B CA  1 
ATOM   3855  C  C   . VAL B 1 132 ? 2.745   -37.253 10.140  1.00 41.92  ? 132  VAL B C   1 
ATOM   3856  O  O   . VAL B 1 132 ? 3.271   -36.347 9.474   1.00 54.82  ? 132  VAL B O   1 
ATOM   3857  C  CB  . VAL B 1 132 ? 1.483   -39.102 8.993   1.00 40.23  ? 132  VAL B CB  1 
ATOM   3858  C  CG1 . VAL B 1 132 ? 1.014   -38.011 8.025   1.00 44.32  ? 132  VAL B CG1 1 
ATOM   3859  C  CG2 . VAL B 1 132 ? 1.616   -40.458 8.292   1.00 34.09  ? 132  VAL B CG2 1 
ATOM   3860  N  N   . ASN B 1 133 ? 2.092   -37.034 11.279  1.00 37.86  ? 133  ASN B N   1 
ATOM   3861  C  CA  . ASN B 1 133 ? 1.958   -35.700 11.866  1.00 36.12  ? 133  ASN B CA  1 
ATOM   3862  C  C   . ASN B 1 133 ? 3.320   -35.038 12.122  1.00 40.12  ? 133  ASN B C   1 
ATOM   3863  O  O   . ASN B 1 133 ? 3.473   -33.816 12.014  1.00 43.03  ? 133  ASN B O   1 
ATOM   3864  C  CB  . ASN B 1 133 ? 1.190   -35.778 13.198  1.00 47.15  ? 133  ASN B CB  1 
ATOM   3865  C  CG  . ASN B 1 133 ? -0.332  -35.741 13.033  1.00 46.08  ? 133  ASN B CG  1 
ATOM   3866  O  OD1 . ASN B 1 133 ? -0.870  -35.802 11.921  1.00 38.76  ? 133  ASN B OD1 1 
ATOM   3867  N  ND2 . ASN B 1 133 ? -1.028  -35.634 14.166  1.00 49.93  ? 133  ASN B ND2 1 
ATOM   3868  N  N   . SER B 1 134 ? 4.311   -35.854 12.461  1.00 35.79  ? 134  SER B N   1 
ATOM   3869  C  CA  . SER B 1 134 ? 5.583   -35.341 12.961  1.00 39.10  ? 134  SER B CA  1 
ATOM   3870  C  C   . SER B 1 134 ? 6.717   -35.438 11.944  1.00 41.67  ? 134  SER B C   1 
ATOM   3871  O  O   . SER B 1 134 ? 7.829   -34.977 12.199  1.00 41.35  ? 134  SER B O   1 
ATOM   3872  C  CB  . SER B 1 134 ? 5.981   -36.093 14.232  1.00 41.68  ? 134  SER B CB  1 
ATOM   3873  O  OG  . SER B 1 134 ? 6.170   -37.474 13.958  1.00 44.28  ? 134  SER B OG  1 
ATOM   3874  N  N   . THR B 1 135 ? 6.436   -36.046 10.798  1.00 40.25  ? 135  THR B N   1 
ATOM   3875  C  CA  . THR B 1 135 ? 7.451   -36.224 9.778   1.00 38.49  ? 135  THR B CA  1 
ATOM   3876  C  C   . THR B 1 135 ? 6.941   -35.874 8.388   1.00 36.15  ? 135  THR B C   1 
ATOM   3877  O  O   . THR B 1 135 ? 5.807   -36.203 8.021   1.00 45.06  ? 135  THR B O   1 
ATOM   3878  C  CB  . THR B 1 135 ? 7.949   -37.672 9.747   1.00 47.79  ? 135  THR B CB  1 
ATOM   3879  O  OG1 . THR B 1 135 ? 7.886   -38.228 11.067  1.00 38.83  ? 135  THR B OG1 1 
ATOM   3880  C  CG2 . THR B 1 135 ? 9.394   -37.731 9.205   1.00 36.27  ? 135  THR B CG2 1 
ATOM   3881  N  N   . ASP B 1 136 ? 7.794   -35.203 7.622   1.00 34.22  ? 136  ASP B N   1 
ATOM   3882  C  CA  . ASP B 1 136 ? 7.531   -34.904 6.227   1.00 38.26  ? 136  ASP B CA  1 
ATOM   3883  C  C   . ASP B 1 136 ? 8.196   -35.974 5.380   1.00 39.49  ? 136  ASP B C   1 
ATOM   3884  O  O   . ASP B 1 136 ? 9.430   -36.044 5.319   1.00 38.01  ? 136  ASP B O   1 
ATOM   3885  C  CB  . ASP B 1 136 ? 8.121   -33.550 5.881   1.00 49.22  ? 136  ASP B CB  1 
ATOM   3886  C  CG  . ASP B 1 136 ? 7.134   -32.659 5.214   1.00 67.43  ? 136  ASP B CG  1 
ATOM   3887  O  OD1 . ASP B 1 136 ? 6.100   -32.363 5.849   1.00 70.43  ? 136  ASP B OD1 1 
ATOM   3888  O  OD2 . ASP B 1 136 ? 7.385   -32.253 4.061   1.00 80.05  ? 136  ASP B OD2 1 
ATOM   3889  N  N   . ILE B 1 137 ? 7.390   -36.802 4.724   1.00 30.41  ? 137  ILE B N   1 
ATOM   3890  C  CA  . ILE B 1 137 ? 7.907   -38.038 4.129   1.00 29.02  ? 137  ILE B CA  1 
ATOM   3891  C  C   . ILE B 1 137 ? 7.781   -38.093 2.617   1.00 28.46  ? 137  ILE B C   1 
ATOM   3892  O  O   . ILE B 1 137 ? 6.689   -37.905 2.090   1.00 33.23  ? 137  ILE B O   1 
ATOM   3893  C  CB  . ILE B 1 137 ? 7.163   -39.256 4.695   1.00 31.15  ? 137  ILE B CB  1 
ATOM   3894  C  CG1 . ILE B 1 137 ? 7.382   -39.348 6.202   1.00 32.03  ? 137  ILE B CG1 1 
ATOM   3895  C  CG2 . ILE B 1 137 ? 7.599   -40.531 3.988   1.00 26.63  ? 137  ILE B CG2 1 
ATOM   3896  C  CD1 . ILE B 1 137 ? 6.488   -40.371 6.891   1.00 28.43  ? 137  ILE B CD1 1 
ATOM   3897  N  N   . TYR B 1 138 ? 8.893   -38.386 1.934   1.00 39.08  ? 138  TYR B N   1 
ATOM   3898  C  CA  . TYR B 1 138 ? 8.934   -38.479 0.460   1.00 35.47  ? 138  TYR B CA  1 
ATOM   3899  C  C   . TYR B 1 138 ? 9.353   -39.863 -0.044  1.00 28.57  ? 138  TYR B C   1 
ATOM   3900  O  O   . TYR B 1 138 ? 10.390  -40.387 0.361   1.00 34.18  ? 138  TYR B O   1 
ATOM   3901  C  CB  . TYR B 1 138 ? 9.894   -37.445 -0.112  1.00 31.88  ? 138  TYR B CB  1 
ATOM   3902  C  CG  . TYR B 1 138 ? 9.486   -36.001 0.097   1.00 31.34  ? 138  TYR B CG  1 
ATOM   3903  C  CD1 . TYR B 1 138 ? 9.770   -35.338 1.291   1.00 33.29  ? 138  TYR B CD1 1 
ATOM   3904  C  CD2 . TYR B 1 138 ? 8.857   -35.289 -0.916  1.00 29.29  ? 138  TYR B CD2 1 
ATOM   3905  C  CE1 . TYR B 1 138 ? 9.421   -34.004 1.469   1.00 27.14  ? 138  TYR B CE1 1 
ATOM   3906  C  CE2 . TYR B 1 138 ? 8.507   -33.962 -0.748  1.00 33.61  ? 138  TYR B CE2 1 
ATOM   3907  C  CZ  . TYR B 1 138 ? 8.790   -33.323 0.439   1.00 30.12  ? 138  TYR B CZ  1 
ATOM   3908  O  OH  . TYR B 1 138 ? 8.423   -32.004 0.578   1.00 34.74  ? 138  TYR B OH  1 
ATOM   3909  N  N   . LEU B 1 139 ? 8.547   -40.445 -0.927  1.00 30.65  ? 139  LEU B N   1 
ATOM   3910  C  CA  . LEU B 1 139 ? 8.781   -41.810 -1.390  1.00 37.86  ? 139  LEU B CA  1 
ATOM   3911  C  C   . LEU B 1 139 ? 9.048   -41.850 -2.879  1.00 38.13  ? 139  LEU B C   1 
ATOM   3912  O  O   . LEU B 1 139 ? 8.173   -41.502 -3.673  1.00 36.12  ? 139  LEU B O   1 
ATOM   3913  C  CB  . LEU B 1 139 ? 7.587   -42.714 -1.091  1.00 13.68  ? 139  LEU B CB  1 
ATOM   3914  C  CG  . LEU B 1 139 ? 7.158   -42.795 0.372   1.00 34.48  ? 139  LEU B CG  1 
ATOM   3915  C  CD1 . LEU B 1 139 ? 6.018   -43.787 0.513   1.00 36.68  ? 139  LEU B CD1 1 
ATOM   3916  C  CD2 . LEU B 1 139 ? 8.294   -43.174 1.316   1.00 25.74  ? 139  LEU B CD2 1 
ATOM   3917  N  N   . VAL B 1 140 ? 10.249  -42.298 -3.246  1.00 37.80  ? 140  VAL B N   1 
ATOM   3918  C  CA  . VAL B 1 140 ? 10.631  -42.437 -4.647  1.00 39.84  ? 140  VAL B CA  1 
ATOM   3919  C  C   . VAL B 1 140 ? 10.826  -43.916 -5.023  1.00 39.88  ? 140  VAL B C   1 
ATOM   3920  O  O   . VAL B 1 140 ? 11.942  -44.441 -4.969  1.00 38.87  ? 140  VAL B O   1 
ATOM   3921  C  CB  . VAL B 1 140 ? 11.909  -41.632 -4.941  1.00 36.11  ? 140  VAL B CB  1 
ATOM   3922  C  CG1 . VAL B 1 140 ? 12.196  -41.586 -6.442  1.00 26.82  ? 140  VAL B CG1 1 
ATOM   3923  C  CG2 . VAL B 1 140 ? 11.781  -40.223 -4.369  1.00 37.66  ? 140  VAL B CG2 1 
ATOM   3924  N  N   . PRO B 1 141 ? 9.727   -44.595 -5.394  1.00 38.52  ? 141  PRO B N   1 
ATOM   3925  C  CA  . PRO B 1 141 ? 9.745   -46.027 -5.712  1.00 39.60  ? 141  PRO B CA  1 
ATOM   3926  C  C   . PRO B 1 141 ? 10.756  -46.393 -6.789  1.00 39.01  ? 141  PRO B C   1 
ATOM   3927  O  O   . PRO B 1 141 ? 11.364  -47.464 -6.703  1.00 41.32  ? 141  PRO B O   1 
ATOM   3928  C  CB  . PRO B 1 141 ? 8.319   -46.291 -6.197  1.00 39.56  ? 141  PRO B CB  1 
ATOM   3929  C  CG  . PRO B 1 141 ? 7.507   -45.301 -5.454  1.00 41.18  ? 141  PRO B CG  1 
ATOM   3930  C  CD  . PRO B 1 141 ? 8.355   -44.056 -5.392  1.00 43.02  ? 141  PRO B CD  1 
ATOM   3931  N  N   . THR B 1 142 ? 10.944  -45.529 -7.782  1.00 31.86  ? 142  THR B N   1 
ATOM   3932  C  CA  . THR B 1 142 ? 12.004  -45.767 -8.766  1.00 44.31  ? 142  THR B CA  1 
ATOM   3933  C  C   . THR B 1 142 ? 12.804  -44.526 -9.161  1.00 47.67  ? 142  THR B C   1 
ATOM   3934  O  O   . THR B 1 142 ? 12.275  -43.416 -9.264  1.00 43.89  ? 142  THR B O   1 
ATOM   3935  C  CB  . THR B 1 142 ? 11.497  -46.434 -10.054 1.00 35.51  ? 142  THR B CB  1 
ATOM   3936  O  OG1 . THR B 1 142 ? 12.623  -46.796 -10.871 1.00 38.49  ? 142  THR B OG1 1 
ATOM   3937  C  CG2 . THR B 1 142 ? 10.626  -45.469 -10.820 1.00 29.48  ? 142  THR B CG2 1 
ATOM   3938  N  N   . MET B 1 143 ? 14.090  -44.758 -9.399  1.00 52.80  ? 143  MET B N   1 
ATOM   3939  C  CA  . MET B 1 143 ? 15.037  -43.724 -9.779  1.00 41.49  ? 143  MET B CA  1 
ATOM   3940  C  C   . MET B 1 143 ? 15.629  -44.081 -11.150 1.00 44.75  ? 143  MET B C   1 
ATOM   3941  O  O   . MET B 1 143 ? 16.386  -43.312 -11.754 1.00 33.76  ? 143  MET B O   1 
ATOM   3942  C  CB  . MET B 1 143 ? 16.128  -43.656 -8.718  1.00 32.46  ? 143  MET B CB  1 
ATOM   3943  C  CG  . MET B 1 143 ? 17.089  -42.509 -8.861  1.00 39.49  ? 143  MET B CG  1 
ATOM   3944  S  SD  . MET B 1 143 ? 18.482  -42.755 -7.749  1.00 48.69  ? 143  MET B SD  1 
ATOM   3945  C  CE  . MET B 1 143 ? 19.794  -41.925 -8.662  1.00 27.80  ? 143  MET B CE  1 
ATOM   3946  N  N   . ASN B 1 144 ? 15.252  -45.257 -11.646 1.00 37.87  ? 144  ASN B N   1 
ATOM   3947  C  CA  . ASN B 1 144 ? 15.757  -45.737 -12.917 1.00 33.24  ? 144  ASN B CA  1 
ATOM   3948  C  C   . ASN B 1 144 ? 14.705  -46.512 -13.716 1.00 41.51  ? 144  ASN B C   1 
ATOM   3949  O  O   . ASN B 1 144 ? 14.818  -47.723 -13.899 1.00 46.85  ? 144  ASN B O   1 
ATOM   3950  C  CB  . ASN B 1 144 ? 16.998  -46.587 -12.684 1.00 29.70  ? 144  ASN B CB  1 
ATOM   3951  C  CG  . ASN B 1 144 ? 17.698  -46.931 -13.960 1.00 41.86  ? 144  ASN B CG  1 
ATOM   3952  O  OD1 . ASN B 1 144 ? 17.329  -46.451 -15.037 1.00 45.74  ? 144  ASN B OD1 1 
ATOM   3953  N  ND2 . ASN B 1 144 ? 18.719  -47.769 -13.860 1.00 46.99  ? 144  ASN B ND2 1 
ATOM   3954  N  N   . PRO B 1 145 ? 13.687  -45.798 -14.214 1.00 36.68  ? 145  PRO B N   1 
ATOM   3955  C  CA  . PRO B 1 145 ? 12.563  -46.371 -14.970 1.00 33.38  ? 145  PRO B CA  1 
ATOM   3956  C  C   . PRO B 1 145 ? 13.051  -47.039 -16.234 1.00 37.12  ? 145  PRO B C   1 
ATOM   3957  O  O   . PRO B 1 145 ? 12.459  -48.009 -16.706 1.00 44.49  ? 145  PRO B O   1 
ATOM   3958  C  CB  . PRO B 1 145 ? 11.720  -45.144 -15.366 1.00 26.50  ? 145  PRO B CB  1 
ATOM   3959  C  CG  . PRO B 1 145 ? 12.268  -43.984 -14.588 1.00 30.51  ? 145  PRO B CG  1 
ATOM   3960  C  CD  . PRO B 1 145 ? 13.674  -44.322 -14.211 1.00 31.95  ? 145  PRO B CD  1 
ATOM   3961  N  N   . ASP B 1 146 ? 14.120  -46.491 -16.797 1.00 42.17  ? 146  ASP B N   1 
ATOM   3962  C  CA  . ASP B 1 146 ? 14.622  -46.967 -18.072 1.00 41.84  ? 146  ASP B CA  1 
ATOM   3963  C  C   . ASP B 1 146 ? 15.352  -48.275 -17.827 1.00 41.29  ? 146  ASP B C   1 
ATOM   3964  O  O   . ASP B 1 146 ? 15.165  -49.249 -18.563 1.00 46.90  ? 146  ASP B O   1 
ATOM   3965  C  CB  . ASP B 1 146 ? 15.525  -45.912 -18.726 1.00 48.85  ? 146  ASP B CB  1 
ATOM   3966  C  CG  . ASP B 1 146 ? 14.751  -44.658 -19.157 1.00 45.52  ? 146  ASP B CG  1 
ATOM   3967  O  OD1 . ASP B 1 146 ? 13.547  -44.561 -18.832 1.00 36.59  ? 146  ASP B OD1 1 
ATOM   3968  O  OD2 . ASP B 1 146 ? 15.344  -43.774 -19.823 1.00 45.21  ? 146  ASP B OD2 1 
ATOM   3969  N  N   . GLY B 1 147 ? 16.158  -48.300 -16.767 1.00 32.75  ? 147  GLY B N   1 
ATOM   3970  C  CA  . GLY B 1 147 ? 16.846  -49.514 -16.358 1.00 30.28  ? 147  GLY B CA  1 
ATOM   3971  C  C   . GLY B 1 147 ? 15.844  -50.610 -16.030 1.00 39.73  ? 147  GLY B C   1 
ATOM   3972  O  O   . GLY B 1 147 ? 15.967  -51.762 -16.482 1.00 32.93  ? 147  GLY B O   1 
ATOM   3973  N  N   . TYR B 1 148 ? 14.840  -50.241 -15.238 1.00 40.76  ? 148  TYR B N   1 
ATOM   3974  C  CA  . TYR B 1 148 ? 13.753  -51.154 -14.904 1.00 49.08  ? 148  TYR B CA  1 
ATOM   3975  C  C   . TYR B 1 148 ? 13.109  -51.731 -16.160 1.00 55.07  ? 148  TYR B C   1 
ATOM   3976  O  O   . TYR B 1 148 ? 13.054  -52.946 -16.344 1.00 54.34  ? 148  TYR B O   1 
ATOM   3977  C  CB  . TYR B 1 148 ? 12.688  -50.453 -14.053 1.00 43.99  ? 148  TYR B CB  1 
ATOM   3978  C  CG  . TYR B 1 148 ? 11.466  -51.308 -13.774 1.00 38.01  ? 148  TYR B CG  1 
ATOM   3979  C  CD1 . TYR B 1 148 ? 11.565  -52.463 -13.005 1.00 46.05  ? 148  TYR B CD1 1 
ATOM   3980  C  CD2 . TYR B 1 148 ? 10.217  -50.957 -14.266 1.00 28.55  ? 148  TYR B CD2 1 
ATOM   3981  C  CE1 . TYR B 1 148 ? 10.462  -53.244 -12.738 1.00 39.67  ? 148  TYR B CE1 1 
ATOM   3982  C  CE2 . TYR B 1 148 ? 9.101   -51.738 -14.009 1.00 29.67  ? 148  TYR B CE2 1 
ATOM   3983  C  CZ  . TYR B 1 148 ? 9.228   -52.878 -13.245 1.00 46.24  ? 148  TYR B CZ  1 
ATOM   3984  O  OH  . TYR B 1 148 ? 8.110   -53.648 -12.988 1.00 59.49  ? 148  TYR B OH  1 
ATOM   3985  N  N   . ALA B 1 149 ? 12.619  -50.858 -17.029 1.00 48.27  ? 149  ALA B N   1 
ATOM   3986  C  CA  . ALA B 1 149 ? 11.916  -51.328 -18.210 1.00 44.75  ? 149  ALA B CA  1 
ATOM   3987  C  C   . ALA B 1 149 ? 12.738  -52.389 -18.947 1.00 41.98  ? 149  ALA B C   1 
ATOM   3988  O  O   . ALA B 1 149 ? 12.176  -53.302 -19.544 1.00 44.15  ? 149  ALA B O   1 
ATOM   3989  C  CB  . ALA B 1 149 ? 11.554  -50.154 -19.135 1.00 29.42  ? 149  ALA B CB  1 
ATOM   3990  N  N   . LEU B 1 150 ? 14.063  -52.280 -18.887 1.00 49.80  ? 150  LEU B N   1 
ATOM   3991  C  CA  . LEU B 1 150 ? 14.925  -53.184 -19.647 1.00 51.44  ? 150  LEU B CA  1 
ATOM   3992  C  C   . LEU B 1 150 ? 15.237  -54.466 -18.889 1.00 62.61  ? 150  LEU B C   1 
ATOM   3993  O  O   . LEU B 1 150 ? 15.796  -55.403 -19.460 1.00 66.22  ? 150  LEU B O   1 
ATOM   3994  C  CB  . LEU B 1 150 ? 16.222  -52.486 -20.045 1.00 43.07  ? 150  LEU B CB  1 
ATOM   3995  C  CG  . LEU B 1 150 ? 16.023  -51.371 -21.066 1.00 54.07  ? 150  LEU B CG  1 
ATOM   3996  C  CD1 . LEU B 1 150 ? 17.001  -50.229 -20.822 1.00 52.07  ? 150  LEU B CD1 1 
ATOM   3997  C  CD2 . LEU B 1 150 ? 16.143  -51.912 -22.494 1.00 53.51  ? 150  LEU B CD2 1 
ATOM   3998  N  N   . SER B 1 151 ? 14.885  -54.510 -17.605 1.00 57.94  ? 151  SER B N   1 
ATOM   3999  C  CA  . SER B 1 151 ? 15.149  -55.704 -16.802 1.00 49.55  ? 151  SER B CA  1 
ATOM   4000  C  C   . SER B 1 151 ? 14.036  -56.755 -16.928 1.00 57.52  ? 151  SER B C   1 
ATOM   4001  O  O   . SER B 1 151 ? 12.935  -56.476 -17.419 1.00 54.93  ? 151  SER B O   1 
ATOM   4002  C  CB  . SER B 1 151 ? 15.414  -55.347 -15.336 1.00 40.06  ? 151  SER B CB  1 
ATOM   4003  O  OG  . SER B 1 151 ? 16.501  -54.441 -15.207 1.00 41.03  ? 151  SER B OG  1 
ATOM   4004  N  N   . GLN B 1 152 ? 14.338  -57.972 -16.487 1.00 51.65  ? 152  GLN B N   1 
ATOM   4005  C  CA  . GLN B 1 152 ? 13.419  -59.091 -16.644 1.00 47.48  ? 152  GLN B CA  1 
ATOM   4006  C  C   . GLN B 1 152 ? 12.982  -59.682 -15.302 1.00 59.84  ? 152  GLN B C   1 
ATOM   4007  O  O   . GLN B 1 152 ? 13.803  -60.250 -14.567 1.00 66.55  ? 152  GLN B O   1 
ATOM   4008  C  CB  . GLN B 1 152 ? 14.068  -60.189 -17.488 1.00 62.67  ? 152  GLN B CB  1 
ATOM   4009  C  CG  . GLN B 1 152 ? 13.234  -61.447 -17.603 1.00 69.60  ? 152  GLN B CG  1 
ATOM   4010  C  CD  . GLN B 1 152 ? 13.948  -62.545 -18.344 1.00 78.18  ? 152  GLN B CD  1 
ATOM   4011  O  OE1 . GLN B 1 152 ? 13.546  -63.707 -18.298 1.00 90.42  ? 152  GLN B OE1 1 
ATOM   4012  N  NE2 . GLN B 1 152 ? 15.019  -62.187 -19.036 1.00 75.65  ? 152  GLN B NE2 1 
ATOM   4013  N  N   . GLU B 1 153 ? 11.692  -59.567 -14.989 1.00 48.57  ? 153  GLU B N   1 
ATOM   4014  C  CA  . GLU B 1 153 ? 11.180  -60.141 -13.750 1.00 50.60  ? 153  GLU B CA  1 
ATOM   4015  C  C   . GLU B 1 153 ? 11.601  -61.601 -13.657 1.00 55.56  ? 153  GLU B C   1 
ATOM   4016  O  O   . GLU B 1 153 ? 11.517  -62.346 -14.633 1.00 50.96  ? 153  GLU B O   1 
ATOM   4017  C  CB  . GLU B 1 153 ? 9.655   -60.010 -13.645 1.00 50.66  ? 153  GLU B CB  1 
ATOM   4018  C  CG  . GLU B 1 153 ? 9.071   -60.545 -12.327 1.00 53.17  ? 153  GLU B CG  1 
ATOM   4019  C  CD  . GLU B 1 153 ? 7.555   -60.394 -12.246 1.00 57.90  ? 153  GLU B CD  1 
ATOM   4020  O  OE1 . GLU B 1 153 ? 6.892   -61.268 -11.638 1.00 56.73  ? 153  GLU B OE1 1 
ATOM   4021  O  OE2 . GLU B 1 153 ? 7.026   -59.403 -12.799 1.00 57.77  ? 153  GLU B OE2 1 
ATOM   4022  N  N   . GLY B 1 154 ? 12.071  -61.992 -12.478 1.00 60.17  ? 154  GLY B N   1 
ATOM   4023  C  CA  . GLY B 1 154 ? 12.520  -63.350 -12.253 1.00 58.32  ? 154  GLY B CA  1 
ATOM   4024  C  C   . GLY B 1 154 ? 14.020  -63.434 -12.063 1.00 56.66  ? 154  GLY B C   1 
ATOM   4025  O  O   . GLY B 1 154 ? 14.515  -64.321 -11.381 1.00 65.81  ? 154  GLY B O   1 
ATOM   4026  N  N   . ASN B 1 155 ? 14.751  -62.503 -12.662 1.00 48.88  ? 155  ASN B N   1 
ATOM   4027  C  CA  . ASN B 1 155 ? 16.200  -62.567 -12.623 1.00 41.73  ? 155  ASN B CA  1 
ATOM   4028  C  C   . ASN B 1 155 ? 16.784  -62.252 -11.251 1.00 58.57  ? 155  ASN B C   1 
ATOM   4029  O  O   . ASN B 1 155 ? 16.877  -61.084 -10.852 1.00 74.68  ? 155  ASN B O   1 
ATOM   4030  C  CB  . ASN B 1 155 ? 16.796  -61.652 -13.683 1.00 31.91  ? 155  ASN B CB  1 
ATOM   4031  C  CG  . ASN B 1 155 ? 17.093  -62.382 -14.962 1.00 50.26  ? 155  ASN B CG  1 
ATOM   4032  O  OD1 . ASN B 1 155 ? 17.024  -61.807 -16.045 1.00 61.06  ? 155  ASN B OD1 1 
ATOM   4033  N  ND2 . ASN B 1 155 ? 17.419  -63.665 -14.850 1.00 66.50  ? 155  ASN B ND2 1 
ATOM   4034  N  N   . CYS B 1 156 ? 17.184  -63.292 -10.528 1.00 54.31  ? 156  CYS B N   1 
ATOM   4035  C  CA  . CYS B 1 156 ? 17.856  -63.088 -9.252  1.00 63.94  ? 156  CYS B CA  1 
ATOM   4036  C  C   . CYS B 1 156 ? 19.226  -62.451 -9.486  1.00 62.09  ? 156  CYS B C   1 
ATOM   4037  O  O   . CYS B 1 156 ? 19.701  -61.644 -8.686  1.00 62.15  ? 156  CYS B O   1 
ATOM   4038  C  CB  . CYS B 1 156 ? 17.973  -64.407 -8.480  1.00 69.37  ? 156  CYS B CB  1 
ATOM   4039  S  SG  . CYS B 1 156 ? 16.474  -64.845 -7.557  1.00 69.99  ? 156  CYS B SG  1 
ATOM   4040  N  N   . GLU B 1 157 ? 19.853  -62.813 -10.598 1.00 62.56  ? 157  GLU B N   1 
ATOM   4041  C  CA  . GLU B 1 157 ? 21.106  -62.193 -10.999 1.00 56.86  ? 157  GLU B CA  1 
ATOM   4042  C  C   . GLU B 1 157 ? 20.856  -61.240 -12.155 1.00 54.63  ? 157  GLU B C   1 
ATOM   4043  O  O   . GLU B 1 157 ? 19.936  -61.439 -12.938 1.00 58.91  ? 157  GLU B O   1 
ATOM   4044  C  CB  . GLU B 1 157 ? 22.120  -63.252 -11.407 1.00 68.21  ? 157  GLU B CB  1 
ATOM   4045  C  CG  . GLU B 1 157 ? 22.667  -64.069 -10.240 1.00 86.74  ? 157  GLU B CG  1 
ATOM   4046  C  CD  . GLU B 1 157 ? 22.075  -65.472 -10.158 1.00 100.59 ? 157  GLU B CD  1 
ATOM   4047  O  OE1 . GLU B 1 157 ? 22.647  -66.399 -10.775 1.00 106.75 ? 157  GLU B OE1 1 
ATOM   4048  O  OE2 . GLU B 1 157 ? 21.046  -65.649 -9.469  1.00 98.56  ? 157  GLU B OE2 1 
ATOM   4049  N  N   . SER B 1 158 ? 21.674  -60.201 -12.253 1.00 55.80  ? 158  SER B N   1 
ATOM   4050  C  CA  . SER B 1 158 ? 21.517  -59.202 -13.307 1.00 51.14  ? 158  SER B CA  1 
ATOM   4051  C  C   . SER B 1 158 ? 21.707  -59.830 -14.696 1.00 49.90  ? 158  SER B C   1 
ATOM   4052  O  O   . SER B 1 158 ? 22.028  -61.013 -14.800 1.00 57.02  ? 158  SER B O   1 
ATOM   4053  C  CB  . SER B 1 158 ? 22.497  -58.045 -13.087 1.00 49.27  ? 158  SER B CB  1 
ATOM   4054  O  OG  . SER B 1 158 ? 22.244  -56.980 -13.989 1.00 62.49  ? 158  SER B OG  1 
ATOM   4055  N  N   . LEU B 1 159 ? 21.505  -59.051 -15.760 1.00 38.81  ? 159  LEU B N   1 
ATOM   4056  C  CA  . LEU B 1 159 ? 21.614  -59.588 -17.124 1.00 48.20  ? 159  LEU B CA  1 
ATOM   4057  C  C   . LEU B 1 159 ? 23.049  -59.512 -17.640 1.00 54.17  ? 159  LEU B C   1 
ATOM   4058  O  O   . LEU B 1 159 ? 23.809  -58.619 -17.266 1.00 44.54  ? 159  LEU B O   1 
ATOM   4059  C  CB  . LEU B 1 159 ? 20.669  -58.851 -18.095 1.00 60.14  ? 159  LEU B CB  1 
ATOM   4060  C  CG  . LEU B 1 159 ? 19.141  -59.041 -18.015 1.00 57.64  ? 159  LEU B CG  1 
ATOM   4061  C  CD1 . LEU B 1 159 ? 18.375  -57.768 -18.407 1.00 41.28  ? 159  LEU B CD1 1 
ATOM   4062  C  CD2 . LEU B 1 159 ? 18.677  -60.227 -18.856 1.00 45.51  ? 159  LEU B CD2 1 
ATOM   4063  N  N   . PRO B 1 160 ? 23.428  -60.455 -18.508 1.00 50.99  ? 160  PRO B N   1 
ATOM   4064  C  CA  . PRO B 1 160 ? 24.748  -60.357 -19.140 1.00 45.93  ? 160  PRO B CA  1 
ATOM   4065  C  C   . PRO B 1 160 ? 24.955  -58.920 -19.586 1.00 57.33  ? 160  PRO B C   1 
ATOM   4066  O  O   . PRO B 1 160 ? 24.066  -58.371 -20.237 1.00 80.74  ? 160  PRO B O   1 
ATOM   4067  C  CB  . PRO B 1 160 ? 24.603  -61.248 -20.374 1.00 39.13  ? 160  PRO B CB  1 
ATOM   4068  C  CG  . PRO B 1 160 ? 23.525  -62.221 -20.017 1.00 34.30  ? 160  PRO B CG  1 
ATOM   4069  C  CD  . PRO B 1 160 ? 22.574  -61.480 -19.131 1.00 40.64  ? 160  PRO B CD  1 
ATOM   4070  N  N   . ASN B 1 161 ? 26.088  -58.322 -19.243 1.00 70.32  ? 161  ASN B N   1 
ATOM   4071  C  CA  . ASN B 1 161 ? 26.353  -56.918 -19.564 1.00 87.31  ? 161  ASN B CA  1 
ATOM   4072  C  C   . ASN B 1 161 ? 25.802  -56.003 -18.498 1.00 83.23  ? 161  ASN B C   1 
ATOM   4073  O  O   . ASN B 1 161 ? 26.032  -54.794 -18.525 1.00 90.05  ? 161  ASN B O   1 
ATOM   4074  C  CB  . ASN B 1 161 ? 25.733  -56.515 -20.901 1.00 100.27 ? 161  ASN B CB  1 
ATOM   4075  C  CG  . ASN B 1 161 ? 26.204  -57.374 -22.040 1.00 105.54 ? 161  ASN B CG  1 
ATOM   4076  O  OD1 . ASN B 1 161 ? 25.402  -57.858 -22.846 1.00 102.69 ? 161  ASN B OD1 1 
ATOM   4077  N  ND2 . ASN B 1 161 ? 27.516  -57.579 -22.114 1.00 107.48 ? 161  ASN B ND2 1 
ATOM   4078  N  N   . TYR B 1 162 ? 25.058  -56.591 -17.570 1.00 83.47  ? 162  TYR B N   1 
ATOM   4079  C  CA  . TYR B 1 162 ? 24.412  -55.835 -16.503 1.00 85.82  ? 162  TYR B CA  1 
ATOM   4080  C  C   . TYR B 1 162 ? 23.367  -54.881 -17.060 1.00 74.59  ? 162  TYR B C   1 
ATOM   4081  O  O   . TYR B 1 162 ? 23.041  -53.852 -16.454 1.00 67.81  ? 162  TYR B O   1 
ATOM   4082  C  CB  . TYR B 1 162 ? 25.455  -55.104 -15.668 1.00 80.32  ? 162  TYR B CB  1 
ATOM   4083  C  CG  . TYR B 1 162 ? 26.340  -56.058 -14.907 1.00 68.42  ? 162  TYR B CG  1 
ATOM   4084  C  CD1 . TYR B 1 162 ? 27.542  -56.512 -15.446 1.00 62.65  ? 162  TYR B CD1 1 
ATOM   4085  C  CD2 . TYR B 1 162 ? 25.959  -56.529 -13.657 1.00 55.20  ? 162  TYR B CD2 1 
ATOM   4086  C  CE1 . TYR B 1 162 ? 28.346  -57.398 -14.746 1.00 62.14  ? 162  TYR B CE1 1 
ATOM   4087  C  CE2 . TYR B 1 162 ? 26.754  -57.410 -12.954 1.00 59.08  ? 162  TYR B CE2 1 
ATOM   4088  C  CZ  . TYR B 1 162 ? 27.944  -57.841 -13.497 1.00 61.04  ? 162  TYR B CZ  1 
ATOM   4089  O  OH  . TYR B 1 162 ? 28.727  -58.720 -12.784 1.00 69.72  ? 162  TYR B OH  1 
ATOM   4090  N  N   . VAL B 1 163 ? 22.850  -55.244 -18.228 1.00 61.20  ? 163  VAL B N   1 
ATOM   4091  C  CA  . VAL B 1 163 ? 21.799  -54.488 -18.867 1.00 59.94  ? 163  VAL B CA  1 
ATOM   4092  C  C   . VAL B 1 163 ? 20.616  -54.428 -17.906 1.00 62.12  ? 163  VAL B C   1 
ATOM   4093  O  O   . VAL B 1 163 ? 20.274  -55.429 -17.273 1.00 63.36  ? 163  VAL B O   1 
ATOM   4094  C  CB  . VAL B 1 163 ? 21.399  -55.153 -20.195 1.00 45.03  ? 163  VAL B CB  1 
ATOM   4095  C  CG1 . VAL B 1 163 ? 19.992  -54.766 -20.585 1.00 42.14  ? 163  VAL B CG1 1 
ATOM   4096  C  CG2 . VAL B 1 163 ? 22.389  -54.790 -21.294 1.00 34.66  ? 163  VAL B CG2 1 
ATOM   4097  N  N   . GLY B 1 164 ? 20.010  -53.250 -17.773 1.00 50.99  ? 164  GLY B N   1 
ATOM   4098  C  CA  . GLY B 1 164 ? 18.887  -53.075 -16.870 1.00 36.53  ? 164  GLY B CA  1 
ATOM   4099  C  C   . GLY B 1 164 ? 19.322  -52.504 -15.542 1.00 34.75  ? 164  GLY B C   1 
ATOM   4100  O  O   . GLY B 1 164 ? 18.535  -51.833 -14.879 1.00 43.33  ? 164  GLY B O   1 
ATOM   4101  N  N   . ARG B 1 165 ? 20.573  -52.774 -15.155 1.00 42.61  ? 165  ARG B N   1 
ATOM   4102  C  CA  . ARG B 1 165 ? 21.148  -52.239 -13.919 1.00 44.27  ? 165  ARG B CA  1 
ATOM   4103  C  C   . ARG B 1 165 ? 21.448  -50.751 -14.093 1.00 38.00  ? 165  ARG B C   1 
ATOM   4104  O  O   . ARG B 1 165 ? 20.946  -49.915 -13.349 1.00 37.62  ? 165  ARG B O   1 
ATOM   4105  C  CB  . ARG B 1 165 ? 22.416  -53.008 -13.518 1.00 41.00  ? 165  ARG B CB  1 
ATOM   4106  C  CG  . ARG B 1 165 ? 23.073  -52.498 -12.223 1.00 44.08  ? 165  ARG B CG  1 
ATOM   4107  C  CD  . ARG B 1 165 ? 24.290  -53.333 -11.836 1.00 38.10  ? 165  ARG B CD  1 
ATOM   4108  N  NE  . ARG B 1 165 ? 25.295  -52.592 -11.068 1.00 31.25  ? 165  ARG B NE  1 
ATOM   4109  C  CZ  . ARG B 1 165 ? 25.378  -52.573 -9.739  1.00 36.89  ? 165  ARG B CZ  1 
ATOM   4110  N  NH1 . ARG B 1 165 ? 24.503  -53.246 -8.996  1.00 35.70  ? 165  ARG B NH1 1 
ATOM   4111  N  NH2 . ARG B 1 165 ? 26.340  -51.872 -9.146  1.00 31.41  ? 165  ARG B NH2 1 
ATOM   4112  N  N   . GLY B 1 166 ? 22.256  -50.429 -15.095 1.00 26.43  ? 166  GLY B N   1 
ATOM   4113  C  CA  . GLY B 1 166 ? 22.560  -49.047 -15.409 1.00 35.48  ? 166  GLY B CA  1 
ATOM   4114  C  C   . GLY B 1 166 ? 21.356  -48.398 -16.048 1.00 39.53  ? 166  GLY B C   1 
ATOM   4115  O  O   . GLY B 1 166 ? 20.344  -49.059 -16.281 1.00 52.07  ? 166  GLY B O   1 
ATOM   4116  N  N   . ASN B 1 167 ? 21.443  -47.105 -16.333 1.00 32.56  ? 167  ASN B N   1 
ATOM   4117  C  CA  . ASN B 1 167 ? 20.336  -46.463 -17.023 1.00 38.78  ? 167  ASN B CA  1 
ATOM   4118  C  C   . ASN B 1 167 ? 20.287  -46.891 -18.498 1.00 42.05  ? 167  ASN B C   1 
ATOM   4119  O  O   . ASN B 1 167 ? 20.755  -47.975 -18.847 1.00 41.00  ? 167  ASN B O   1 
ATOM   4120  C  CB  . ASN B 1 167 ? 20.337  -44.936 -16.830 1.00 29.78  ? 167  ASN B CB  1 
ATOM   4121  C  CG  . ASN B 1 167 ? 21.458  -44.247 -17.558 1.00 27.84  ? 167  ASN B CG  1 
ATOM   4122  O  OD1 . ASN B 1 167 ? 22.285  -44.891 -18.202 1.00 34.62  ? 167  ASN B OD1 1 
ATOM   4123  N  ND2 . ASN B 1 167 ? 21.491  -42.918 -17.466 1.00 21.56  ? 167  ASN B ND2 1 
ATOM   4124  N  N   . ALA B 1 168 ? 19.707  -46.055 -19.349 1.00 45.14  ? 168  ALA B N   1 
ATOM   4125  C  CA  . ALA B 1 168 ? 19.570  -46.385 -20.765 1.00 57.50  ? 168  ALA B CA  1 
ATOM   4126  C  C   . ALA B 1 168 ? 20.879  -46.219 -21.532 1.00 66.14  ? 168  ALA B C   1 
ATOM   4127  O  O   . ALA B 1 168 ? 21.033  -46.765 -22.631 1.00 71.25  ? 168  ALA B O   1 
ATOM   4128  C  CB  . ALA B 1 168 ? 18.462  -45.543 -21.408 1.00 60.28  ? 168  ALA B CB  1 
ATOM   4129  N  N   . ALA B 1 169 ? 21.811  -45.460 -20.959 1.00 56.70  ? 169  ALA B N   1 
ATOM   4130  C  CA  . ALA B 1 169 ? 23.118  -45.272 -21.578 1.00 44.36  ? 169  ALA B CA  1 
ATOM   4131  C  C   . ALA B 1 169 ? 24.074  -46.343 -21.092 1.00 40.38  ? 169  ALA B C   1 
ATOM   4132  O  O   . ALA B 1 169 ? 25.218  -46.390 -21.521 1.00 39.42  ? 169  ALA B O   1 
ATOM   4133  C  CB  . ALA B 1 169 ? 23.659  -43.896 -21.266 1.00 25.52  ? 169  ALA B CB  1 
ATOM   4134  N  N   . ASN B 1 170 ? 23.583  -47.185 -20.183 1.00 41.69  ? 170  ASN B N   1 
ATOM   4135  C  CA  . ASN B 1 170 ? 24.353  -48.282 -19.592 1.00 55.33  ? 170  ASN B CA  1 
ATOM   4136  C  C   . ASN B 1 170 ? 25.427  -47.854 -18.608 1.00 53.29  ? 170  ASN B C   1 
ATOM   4137  O  O   . ASN B 1 170 ? 26.436  -48.548 -18.437 1.00 60.92  ? 170  ASN B O   1 
ATOM   4138  C  CB  . ASN B 1 170 ? 24.964  -49.182 -20.668 1.00 70.69  ? 170  ASN B CB  1 
ATOM   4139  C  CG  . ASN B 1 170 ? 24.088  -50.364 -20.991 1.00 79.24  ? 170  ASN B CG  1 
ATOM   4140  O  OD1 . ASN B 1 170 ? 23.679  -50.550 -22.136 1.00 78.09  ? 170  ASN B OD1 1 
ATOM   4141  N  ND2 . ASN B 1 170 ? 23.781  -51.171 -19.975 1.00 83.71  ? 170  ASN B ND2 1 
ATOM   4142  N  N   . ILE B 1 171 ? 25.218  -46.715 -17.959 1.00 44.37  ? 171  ILE B N   1 
ATOM   4143  C  CA  . ILE B 1 171 ? 26.123  -46.316 -16.892 1.00 47.06  ? 171  ILE B CA  1 
ATOM   4144  C  C   . ILE B 1 171 ? 25.461  -46.542 -15.543 1.00 37.13  ? 171  ILE B C   1 
ATOM   4145  O  O   . ILE B 1 171 ? 24.254  -46.382 -15.393 1.00 33.50  ? 171  ILE B O   1 
ATOM   4146  C  CB  . ILE B 1 171 ? 26.600  -44.852 -17.036 1.00 46.88  ? 171  ILE B CB  1 
ATOM   4147  C  CG1 . ILE B 1 171 ? 25.623  -43.899 -16.372 1.00 32.35  ? 171  ILE B CG1 1 
ATOM   4148  C  CG2 . ILE B 1 171 ? 26.851  -44.490 -18.512 1.00 43.32  ? 171  ILE B CG2 1 
ATOM   4149  C  CD1 . ILE B 1 171 ? 25.984  -43.616 -14.944 1.00 48.48  ? 171  ILE B CD1 1 
ATOM   4150  N  N   . ASP B 1 172 ? 26.266  -46.927 -14.563 1.00 46.01  ? 172  ASP B N   1 
ATOM   4151  C  CA  . ASP B 1 172 ? 25.763  -47.227 -13.229 1.00 44.75  ? 172  ASP B CA  1 
ATOM   4152  C  C   . ASP B 1 172 ? 25.513  -45.951 -12.428 1.00 43.68  ? 172  ASP B C   1 
ATOM   4153  O  O   . ASP B 1 172 ? 26.450  -45.296 -11.980 1.00 45.90  ? 172  ASP B O   1 
ATOM   4154  C  CB  . ASP B 1 172 ? 26.761  -48.133 -12.487 1.00 45.53  ? 172  ASP B CB  1 
ATOM   4155  C  CG  . ASP B 1 172 ? 26.211  -48.654 -11.168 1.00 36.85  ? 172  ASP B CG  1 
ATOM   4156  O  OD1 . ASP B 1 172 ? 25.408  -47.940 -10.542 1.00 38.11  ? 172  ASP B OD1 1 
ATOM   4157  O  OD2 . ASP B 1 172 ? 26.578  -49.772 -10.752 1.00 41.20  ? 172  ASP B OD2 1 
ATOM   4158  N  N   . LEU B 1 173 ? 24.247  -45.605 -12.236 1.00 37.26  ? 173  LEU B N   1 
ATOM   4159  C  CA  . LEU B 1 173 ? 23.898  -44.401 -11.487 1.00 35.59  ? 173  LEU B CA  1 
ATOM   4160  C  C   . LEU B 1 173 ? 24.477  -44.350 -10.073 1.00 35.81  ? 173  LEU B C   1 
ATOM   4161  O  O   . LEU B 1 173 ? 24.518  -43.276 -9.468  1.00 39.56  ? 173  LEU B O   1 
ATOM   4162  C  CB  . LEU B 1 173 ? 22.384  -44.230 -11.417 1.00 22.40  ? 173  LEU B CB  1 
ATOM   4163  C  CG  . LEU B 1 173 ? 21.738  -44.039 -12.777 1.00 19.32  ? 173  LEU B CG  1 
ATOM   4164  C  CD1 . LEU B 1 173 ? 20.248  -44.035 -12.640 1.00 25.16  ? 173  LEU B CD1 1 
ATOM   4165  C  CD2 . LEU B 1 173 ? 22.222  -42.747 -13.375 1.00 38.81  ? 173  LEU B CD2 1 
ATOM   4166  N  N   . ASN B 1 174 ? 24.908  -45.487 -9.530  1.00 27.96  ? 174  ASN B N   1 
ATOM   4167  C  CA  . ASN B 1 174 ? 25.522  -45.482 -8.189  1.00 22.98  ? 174  ASN B CA  1 
ATOM   4168  C  C   . ASN B 1 174 ? 27.047  -45.270 -8.228  1.00 21.93  ? 174  ASN B C   1 
ATOM   4169  O  O   . ASN B 1 174 ? 27.742  -45.497 -7.245  1.00 42.37  ? 174  ASN B O   1 
ATOM   4170  C  CB  . ASN B 1 174 ? 25.149  -46.737 -7.382  1.00 27.80  ? 174  ASN B CB  1 
ATOM   4171  C  CG  . ASN B 1 174 ? 25.228  -46.515 -5.866  1.00 29.78  ? 174  ASN B CG  1 
ATOM   4172  O  OD1 . ASN B 1 174 ? 25.036  -45.400 -5.387  1.00 37.31  ? 174  ASN B OD1 1 
ATOM   4173  N  ND2 . ASN B 1 174 ? 25.491  -47.585 -5.110  1.00 23.60  ? 174  ASN B ND2 1 
ATOM   4174  N  N   . ARG B 1 175 ? 27.558  -44.834 -9.374  1.00 28.91  ? 175  ARG B N   1 
ATOM   4175  C  CA  . ARG B 1 175 ? 28.945  -44.380 -9.478  1.00 30.08  ? 175  ARG B CA  1 
ATOM   4176  C  C   . ARG B 1 175 ? 28.955  -42.987 -10.082 1.00 28.40  ? 175  ARG B C   1 
ATOM   4177  O  O   . ARG B 1 175 ? 30.020  -42.444 -10.352 1.00 41.65  ? 175  ARG B O   1 
ATOM   4178  C  CB  . ARG B 1 175 ? 29.786  -45.284 -10.387 1.00 20.72  ? 175  ARG B CB  1 
ATOM   4179  C  CG  . ARG B 1 175 ? 29.643  -46.796 -10.185 1.00 32.17  ? 175  ARG B CG  1 
ATOM   4180  C  CD  . ARG B 1 175 ? 30.449  -47.347 -9.017  1.00 29.91  ? 175  ARG B CD  1 
ATOM   4181  N  NE  . ARG B 1 175 ? 29.532  -47.862 -8.029  1.00 42.15  ? 175  ARG B NE  1 
ATOM   4182  C  CZ  . ARG B 1 175 ? 29.318  -49.132 -7.715  1.00 48.19  ? 175  ARG B CZ  1 
ATOM   4183  N  NH1 . ARG B 1 175 ? 30.001  -50.142 -8.248  1.00 38.84  ? 175  ARG B NH1 1 
ATOM   4184  N  NH2 . ARG B 1 175 ? 28.403  -49.372 -6.803  1.00 60.97  ? 175  ARG B NH2 1 
ATOM   4185  N  N   . ASP B 1 176 ? 27.772  -42.413 -10.292 1.00 33.00  ? 176  ASP B N   1 
ATOM   4186  C  CA  . ASP B 1 176 ? 27.641  -41.216 -11.121 1.00 36.27  ? 176  ASP B CA  1 
ATOM   4187  C  C   . ASP B 1 176 ? 27.549  -39.937 -10.299 1.00 30.12  ? 176  ASP B C   1 
ATOM   4188  O  O   . ASP B 1 176 ? 27.602  -38.838 -10.849 1.00 27.41  ? 176  ASP B O   1 
ATOM   4189  C  CB  . ASP B 1 176 ? 26.432  -41.338 -12.063 1.00 37.74  ? 176  ASP B CB  1 
ATOM   4190  C  CG  . ASP B 1 176 ? 26.476  -40.349 -13.214 1.00 44.35  ? 176  ASP B CG  1 
ATOM   4191  O  OD1 . ASP B 1 176 ? 27.589  -39.956 -13.641 1.00 44.19  ? 176  ASP B OD1 1 
ATOM   4192  O  OD2 . ASP B 1 176 ? 25.379  -39.978 -13.695 1.00 45.03  ? 176  ASP B OD2 1 
ATOM   4193  N  N   . PHE B 1 177 ? 27.437  -40.077 -8.984  1.00 23.85  ? 177  PHE B N   1 
ATOM   4194  C  CA  . PHE B 1 177 ? 27.272  -38.905 -8.126  1.00 27.83  ? 177  PHE B CA  1 
ATOM   4195  C  C   . PHE B 1 177 ? 28.611  -38.248 -7.807  1.00 27.38  ? 177  PHE B C   1 
ATOM   4196  O  O   . PHE B 1 177 ? 29.647  -38.897 -7.892  1.00 46.05  ? 177  PHE B O   1 
ATOM   4197  C  CB  . PHE B 1 177 ? 26.489  -39.261 -6.848  1.00 35.90  ? 177  PHE B CB  1 
ATOM   4198  C  CG  . PHE B 1 177 ? 25.003  -39.450 -7.080  1.00 36.06  ? 177  PHE B CG  1 
ATOM   4199  C  CD1 . PHE B 1 177 ? 24.519  -40.616 -7.663  1.00 40.87  ? 177  PHE B CD1 1 
ATOM   4200  C  CD2 . PHE B 1 177 ? 24.098  -38.456 -6.735  1.00 35.86  ? 177  PHE B CD2 1 
ATOM   4201  C  CE1 . PHE B 1 177 ? 23.170  -40.790 -7.886  1.00 41.30  ? 177  PHE B CE1 1 
ATOM   4202  C  CE2 . PHE B 1 177 ? 22.737  -38.627 -6.954  1.00 42.80  ? 177  PHE B CE2 1 
ATOM   4203  C  CZ  . PHE B 1 177 ? 22.274  -39.796 -7.532  1.00 44.52  ? 177  PHE B CZ  1 
ATOM   4204  N  N   . PRO B 1 178 ? 28.596  -36.941 -7.482  1.00 28.16  ? 178  PRO B N   1 
ATOM   4205  C  CA  . PRO B 1 178 ? 29.866  -36.271 -7.174  1.00 31.64  ? 178  PRO B CA  1 
ATOM   4206  C  C   . PRO B 1 178 ? 30.553  -36.908 -5.969  1.00 33.56  ? 178  PRO B C   1 
ATOM   4207  O  O   . PRO B 1 178 ? 29.909  -37.217 -4.975  1.00 27.07  ? 178  PRO B O   1 
ATOM   4208  C  CB  . PRO B 1 178 ? 29.446  -34.824 -6.864  1.00 28.01  ? 178  PRO B CB  1 
ATOM   4209  C  CG  . PRO B 1 178 ? 28.155  -34.633 -7.611  1.00 20.49  ? 178  PRO B CG  1 
ATOM   4210  C  CD  . PRO B 1 178 ? 27.469  -35.988 -7.581  1.00 22.34  ? 178  PRO B CD  1 
ATOM   4211  N  N   . ASP B 1 179 ? 31.857  -37.118 -6.068  1.00 35.38  ? 179  ASP B N   1 
ATOM   4212  C  CA  . ASP B 1 179 ? 32.561  -37.821 -5.015  1.00 41.62  ? 179  ASP B CA  1 
ATOM   4213  C  C   . ASP B 1 179 ? 33.183  -36.807 -4.084  1.00 40.63  ? 179  ASP B C   1 
ATOM   4214  O  O   . ASP B 1 179 ? 33.696  -35.779 -4.521  1.00 45.73  ? 179  ASP B O   1 
ATOM   4215  C  CB  . ASP B 1 179 ? 33.630  -38.741 -5.603  1.00 43.47  ? 179  ASP B CB  1 
ATOM   4216  C  CG  . ASP B 1 179 ? 34.204  -39.705 -4.582  1.00 50.62  ? 179  ASP B CG  1 
ATOM   4217  O  OD1 . ASP B 1 179 ? 33.436  -40.261 -3.770  1.00 54.16  ? 179  ASP B OD1 1 
ATOM   4218  O  OD2 . ASP B 1 179 ? 35.431  -39.923 -4.610  1.00 58.35  ? 179  ASP B OD2 1 
ATOM   4219  N  N   . ARG B 1 180 ? 33.112  -37.085 -2.794  1.00 31.34  ? 180  ARG B N   1 
ATOM   4220  C  CA  . ARG B 1 180 ? 33.717  -36.213 -1.812  1.00 46.73  ? 180  ARG B CA  1 
ATOM   4221  C  C   . ARG B 1 180 ? 35.244  -36.158 -2.011  1.00 48.59  ? 180  ARG B C   1 
ATOM   4222  O  O   . ARG B 1 180 ? 35.858  -35.112 -1.813  1.00 48.16  ? 180  ARG B O   1 
ATOM   4223  C  CB  . ARG B 1 180 ? 33.372  -36.711 -0.410  1.00 50.92  ? 180  ARG B CB  1 
ATOM   4224  C  CG  . ARG B 1 180 ? 33.762  -38.156 -0.210  1.00 49.12  ? 180  ARG B CG  1 
ATOM   4225  C  CD  . ARG B 1 180 ? 33.195  -38.734 1.053   1.00 50.96  ? 180  ARG B CD  1 
ATOM   4226  N  NE  . ARG B 1 180 ? 33.852  -39.994 1.368   1.00 54.34  ? 180  ARG B NE  1 
ATOM   4227  C  CZ  . ARG B 1 180 ? 34.948  -40.073 2.114   1.00 41.56  ? 180  ARG B CZ  1 
ATOM   4228  N  NH1 . ARG B 1 180 ? 35.470  -38.963 2.612   1.00 27.07  ? 180  ARG B NH1 1 
ATOM   4229  N  NH2 . ARG B 1 180 ? 35.519  -41.249 2.364   1.00 22.90  ? 180  ARG B NH2 1 
ATOM   4230  N  N   . LEU B 1 181 ? 35.852  -37.273 -2.421  1.00 46.69  ? 181  LEU B N   1 
ATOM   4231  C  CA  . LEU B 1 181 ? 37.321  -37.351 -2.566  1.00 39.90  ? 181  LEU B CA  1 
ATOM   4232  C  C   . LEU B 1 181 ? 37.902  -36.631 -3.791  1.00 53.62  ? 181  LEU B C   1 
ATOM   4233  O  O   . LEU B 1 181 ? 39.113  -36.375 -3.854  1.00 50.81  ? 181  LEU B O   1 
ATOM   4234  C  CB  . LEU B 1 181 ? 37.811  -38.803 -2.538  1.00 21.57  ? 181  LEU B CB  1 
ATOM   4235  C  CG  . LEU B 1 181 ? 37.501  -39.578 -1.252  1.00 26.11  ? 181  LEU B CG  1 
ATOM   4236  C  CD1 . LEU B 1 181 ? 38.215  -40.914 -1.259  1.00 33.19  ? 181  LEU B CD1 1 
ATOM   4237  C  CD2 . LEU B 1 181 ? 37.895  -38.780 -0.017  1.00 14.04  ? 181  LEU B CD2 1 
ATOM   4238  N  N   . GLU B 1 182 ? 37.052  -36.320 -4.766  1.00 36.40  ? 182  GLU B N   1 
ATOM   4239  C  CA  . GLU B 1 182 ? 37.461  -35.445 -5.851  1.00 41.05  ? 182  GLU B CA  1 
ATOM   4240  C  C   . GLU B 1 182 ? 36.365  -34.440 -6.119  1.00 53.90  ? 182  GLU B C   1 
ATOM   4241  O  O   . GLU B 1 182 ? 35.244  -34.799 -6.484  1.00 75.77  ? 182  GLU B O   1 
ATOM   4242  C  CB  . GLU B 1 182 ? 37.771  -36.242 -7.110  1.00 65.03  ? 182  GLU B CB  1 
ATOM   4243  C  CG  . GLU B 1 182 ? 38.908  -37.218 -6.936  1.00 85.92  ? 182  GLU B CG  1 
ATOM   4244  C  CD  . GLU B 1 182 ? 38.553  -38.608 -7.430  1.00 100.42 ? 182  GLU B CD  1 
ATOM   4245  O  OE1 . GLU B 1 182 ? 38.012  -38.718 -8.555  1.00 105.42 ? 182  GLU B OE1 1 
ATOM   4246  O  OE2 . GLU B 1 182 ? 38.816  -39.588 -6.693  1.00 97.46  ? 182  GLU B OE2 1 
ATOM   4247  N  N   . GLN B 1 183 ? 36.686  -33.171 -5.939  1.00 46.07  ? 183  GLN B N   1 
ATOM   4248  C  CA  . GLN B 1 183 ? 35.668  -32.146 -6.061  1.00 71.08  ? 183  GLN B CA  1 
ATOM   4249  C  C   . GLN B 1 183 ? 36.200  -30.938 -6.847  1.00 68.67  ? 183  GLN B C   1 
ATOM   4250  O  O   . GLN B 1 183 ? 37.228  -30.346 -6.489  1.00 67.57  ? 183  GLN B O   1 
ATOM   4251  C  CB  . GLN B 1 183 ? 35.169  -31.764 -4.664  1.00 81.83  ? 183  GLN B CB  1 
ATOM   4252  C  CG  . GLN B 1 183 ? 33.682  -31.523 -4.572  1.00 76.90  ? 183  GLN B CG  1 
ATOM   4253  C  CD  . GLN B 1 183 ? 33.340  -30.044 -4.626  1.00 81.48  ? 183  GLN B CD  1 
ATOM   4254  O  OE1 . GLN B 1 183 ? 33.826  -29.246 -3.817  1.00 69.87  ? 183  GLN B OE1 1 
ATOM   4255  N  NE2 . GLN B 1 183 ? 32.501  -29.670 -5.582  1.00 91.35  ? 183  GLN B NE2 1 
ATOM   4256  N  N   . SER B 1 184 ? 35.500  -30.594 -7.928  1.00 39.72  ? 184  SER B N   1 
ATOM   4257  C  CA  . SER B 1 184 ? 35.958  -29.564 -8.850  1.00 64.85  ? 184  SER B CA  1 
ATOM   4258  C  C   . SER B 1 184 ? 35.361  -28.192 -8.541  1.00 68.59  ? 184  SER B C   1 
ATOM   4259  O  O   . SER B 1 184 ? 35.646  -27.208 -9.234  1.00 75.63  ? 184  SER B O   1 
ATOM   4260  C  CB  . SER B 1 184 ? 35.631  -29.971 -10.289 1.00 88.41  ? 184  SER B CB  1 
ATOM   4261  O  OG  . SER B 1 184 ? 36.009  -31.318 -10.535 1.00 90.45  ? 184  SER B OG  1 
ATOM   4262  N  N   . GLN B 1 192 ? 26.973  -30.910 -12.123 1.00 41.94  ? 192  GLN B N   1 
ATOM   4263  C  CA  . GLN B 1 192 ? 27.526  -31.232 -13.433 1.00 59.70  ? 192  GLN B CA  1 
ATOM   4264  C  C   . GLN B 1 192 ? 26.563  -31.911 -14.420 1.00 70.10  ? 192  GLN B C   1 
ATOM   4265  O  O   . GLN B 1 192 ? 25.388  -32.201 -14.110 1.00 40.02  ? 192  GLN B O   1 
ATOM   4266  C  CB  . GLN B 1 192 ? 28.790  -32.081 -13.283 1.00 71.66  ? 192  GLN B CB  1 
ATOM   4267  C  CG  . GLN B 1 192 ? 30.072  -31.306 -13.497 1.00 79.64  ? 192  GLN B CG  1 
ATOM   4268  C  CD  . GLN B 1 192 ? 30.290  -30.952 -14.947 1.00 85.83  ? 192  GLN B CD  1 
ATOM   4269  O  OE1 . GLN B 1 192 ? 31.004  -31.655 -15.667 1.00 94.12  ? 192  GLN B OE1 1 
ATOM   4270  N  NE2 . GLN B 1 192 ? 29.673  -29.859 -15.391 1.00 83.08  ? 192  GLN B NE2 1 
ATOM   4271  N  N   . SER B 1 193 ? 27.097  -32.140 -15.620 1.00 73.59  ? 193  SER B N   1 
ATOM   4272  C  CA  . SER B 1 193 ? 26.396  -32.817 -16.698 1.00 66.44  ? 193  SER B CA  1 
ATOM   4273  C  C   . SER B 1 193 ? 26.583  -34.320 -16.554 1.00 61.26  ? 193  SER B C   1 
ATOM   4274  O  O   . SER B 1 193 ? 27.456  -34.931 -17.170 1.00 48.05  ? 193  SER B O   1 
ATOM   4275  C  CB  . SER B 1 193 ? 26.932  -32.349 -18.046 1.00 86.80  ? 193  SER B CB  1 
ATOM   4276  O  OG  . SER B 1 193 ? 27.092  -30.940 -18.051 1.00 104.53 ? 193  SER B OG  1 
ATOM   4277  N  N   . ARG B 1 194 ? 25.750  -34.905 -15.711 1.00 64.39  ? 194  ARG B N   1 
ATOM   4278  C  CA  . ARG B 1 194 ? 25.828  -36.316 -15.407 1.00 61.45  ? 194  ARG B CA  1 
ATOM   4279  C  C   . ARG B 1 194 ? 24.767  -37.038 -16.226 1.00 48.83  ? 194  ARG B C   1 
ATOM   4280  O  O   . ARG B 1 194 ? 24.470  -36.618 -17.342 1.00 58.28  ? 194  ARG B O   1 
ATOM   4281  C  CB  . ARG B 1 194 ? 25.591  -36.506 -13.911 1.00 62.28  ? 194  ARG B CB  1 
ATOM   4282  C  CG  . ARG B 1 194 ? 26.345  -35.495 -13.057 1.00 56.84  ? 194  ARG B CG  1 
ATOM   4283  C  CD  . ARG B 1 194 ? 27.451  -36.163 -12.262 1.00 64.35  ? 194  ARG B CD  1 
ATOM   4284  N  NE  . ARG B 1 194 ? 28.322  -35.194 -11.604 1.00 79.45  ? 194  ARG B NE  1 
ATOM   4285  C  CZ  . ARG B 1 194 ? 29.278  -35.513 -10.735 1.00 95.16  ? 194  ARG B CZ  1 
ATOM   4286  N  NH1 . ARG B 1 194 ? 29.490  -36.782 -10.404 1.00 91.31  ? 194  ARG B NH1 1 
ATOM   4287  N  NH2 . ARG B 1 194 ? 30.026  -34.562 -10.192 1.00 108.80 ? 194  ARG B NH2 1 
ATOM   4288  N  N   . GLN B 1 195 ? 24.221  -38.131 -15.688 1.00 40.48  ? 195  GLN B N   1 
ATOM   4289  C  CA  . GLN B 1 195 ? 23.016  -38.728 -16.252 1.00 38.56  ? 195  GLN B CA  1 
ATOM   4290  C  C   . GLN B 1 195 ? 21.829  -37.940 -15.743 1.00 39.07  ? 195  GLN B C   1 
ATOM   4291  O  O   . GLN B 1 195 ? 21.848  -37.425 -14.623 1.00 39.77  ? 195  GLN B O   1 
ATOM   4292  C  CB  . GLN B 1 195 ? 22.859  -40.206 -15.877 1.00 38.09  ? 195  GLN B CB  1 
ATOM   4293  C  CG  . GLN B 1 195 ? 23.960  -41.110 -16.396 1.00 41.94  ? 195  GLN B CG  1 
ATOM   4294  C  CD  . GLN B 1 195 ? 24.181  -40.989 -17.896 1.00 46.46  ? 195  GLN B CD  1 
ATOM   4295  O  OE1 . GLN B 1 195 ? 23.292  -41.280 -18.695 1.00 50.35  ? 195  GLN B OE1 1 
ATOM   4296  N  NE2 . GLN B 1 195 ? 25.380  -40.571 -18.282 1.00 24.53  ? 195  GLN B NE2 1 
ATOM   4297  N  N   . PRO B 1 196 ? 20.794  -37.834 -16.578 1.00 39.01  ? 196  PRO B N   1 
ATOM   4298  C  CA  . PRO B 1 196 ? 19.555  -37.105 -16.284 1.00 29.15  ? 196  PRO B CA  1 
ATOM   4299  C  C   . PRO B 1 196 ? 19.028  -37.449 -14.900 1.00 31.21  ? 196  PRO B C   1 
ATOM   4300  O  O   . PRO B 1 196 ? 18.548  -36.571 -14.176 1.00 35.76  ? 196  PRO B O   1 
ATOM   4301  C  CB  . PRO B 1 196 ? 18.580  -37.651 -17.329 1.00 30.08  ? 196  PRO B CB  1 
ATOM   4302  C  CG  . PRO B 1 196 ? 19.441  -38.097 -18.482 1.00 33.76  ? 196  PRO B CG  1 
ATOM   4303  C  CD  . PRO B 1 196 ? 20.763  -38.513 -17.888 1.00 30.79  ? 196  PRO B CD  1 
ATOM   4304  N  N   . GLU B 1 197 ? 19.104  -38.735 -14.560 1.00 24.88  ? 197  GLU B N   1 
ATOM   4305  C  CA  . GLU B 1 197 ? 18.547  -39.262 -13.318 1.00 29.59  ? 197  GLU B CA  1 
ATOM   4306  C  C   . GLU B 1 197 ? 19.371  -38.807 -12.112 1.00 25.71  ? 197  GLU B C   1 
ATOM   4307  O  O   . GLU B 1 197 ? 18.834  -38.382 -11.091 1.00 19.59  ? 197  GLU B O   1 
ATOM   4308  C  CB  . GLU B 1 197 ? 18.480  -40.800 -13.363 1.00 26.31  ? 197  GLU B CB  1 
ATOM   4309  C  CG  . GLU B 1 197 ? 17.479  -41.375 -14.360 1.00 32.53  ? 197  GLU B CG  1 
ATOM   4310  C  CD  . GLU B 1 197 ? 18.040  -41.495 -15.778 1.00 42.88  ? 197  GLU B CD  1 
ATOM   4311  O  OE1 . GLU B 1 197 ? 17.335  -42.045 -16.661 1.00 41.56  ? 197  GLU B OE1 1 
ATOM   4312  O  OE2 . GLU B 1 197 ? 19.185  -41.047 -16.001 1.00 43.03  ? 197  GLU B OE2 1 
ATOM   4313  N  N   . THR B 1 198 ? 20.683  -38.917 -12.250 1.00 32.43  ? 198  THR B N   1 
ATOM   4314  C  CA  . THR B 1 198 ? 21.605  -38.429 -11.245 1.00 30.88  ? 198  THR B CA  1 
ATOM   4315  C  C   . THR B 1 198 ? 21.378  -36.926 -11.029 1.00 35.26  ? 198  THR B C   1 
ATOM   4316  O  O   . THR B 1 198 ? 21.028  -36.494 -9.925  1.00 35.78  ? 198  THR B O   1 
ATOM   4317  C  CB  . THR B 1 198 ? 23.051  -38.701 -11.679 1.00 37.04  ? 198  THR B CB  1 
ATOM   4318  O  OG1 . THR B 1 198 ? 23.145  -40.035 -12.210 1.00 33.63  ? 198  THR B OG1 1 
ATOM   4319  C  CG2 . THR B 1 198 ? 24.001  -38.549 -10.501 1.00 31.48  ? 198  THR B CG2 1 
ATOM   4320  N  N   . ALA B 1 199 ? 21.565  -36.140 -12.091 1.00 28.97  ? 199  ALA B N   1 
ATOM   4321  C  CA  . ALA B 1 199 ? 21.308  -34.699 -12.051 1.00 25.42  ? 199  ALA B CA  1 
ATOM   4322  C  C   . ALA B 1 199 ? 19.982  -34.324 -11.353 1.00 36.34  ? 199  ALA B C   1 
ATOM   4323  O  O   . ALA B 1 199 ? 19.905  -33.345 -10.601 1.00 36.04  ? 199  ALA B O   1 
ATOM   4324  C  CB  . ALA B 1 199 ? 21.356  -34.129 -13.455 1.00 19.20  ? 199  ALA B CB  1 
ATOM   4325  N  N   . ALA B 1 200 ? 18.937  -35.108 -11.592 1.00 31.14  ? 200  ALA B N   1 
ATOM   4326  C  CA  . ALA B 1 200 ? 17.628  -34.816 -11.008 1.00 29.64  ? 200  ALA B CA  1 
ATOM   4327  C  C   . ALA B 1 200 ? 17.615  -34.968 -9.493  1.00 30.69  ? 200  ALA B C   1 
ATOM   4328  O  O   . ALA B 1 200 ? 17.128  -34.099 -8.764  1.00 38.42  ? 200  ALA B O   1 
ATOM   4329  C  CB  . ALA B 1 200 ? 16.546  -35.676 -11.647 1.00 29.09  ? 200  ALA B CB  1 
ATOM   4330  N  N   . LEU B 1 201 ? 18.155  -36.078 -9.018  1.00 30.16  ? 201  LEU B N   1 
ATOM   4331  C  CA  . LEU B 1 201 ? 18.261  -36.302 -7.579  1.00 30.23  ? 201  LEU B CA  1 
ATOM   4332  C  C   . LEU B 1 201 ? 19.252  -35.377 -6.870  1.00 33.82  ? 201  LEU B C   1 
ATOM   4333  O  O   . LEU B 1 201 ? 18.918  -34.791 -5.840  1.00 31.94  ? 201  LEU B O   1 
ATOM   4334  C  CB  . LEU B 1 201 ? 18.590  -37.758 -7.291  1.00 35.73  ? 201  LEU B CB  1 
ATOM   4335  C  CG  . LEU B 1 201 ? 17.303  -38.576 -7.234  1.00 41.13  ? 201  LEU B CG  1 
ATOM   4336  C  CD1 . LEU B 1 201 ? 16.812  -38.997 -8.638  1.00 34.12  ? 201  LEU B CD1 1 
ATOM   4337  C  CD2 . LEU B 1 201 ? 17.501  -39.768 -6.319  1.00 46.86  ? 201  LEU B CD2 1 
ATOM   4338  N  N   . VAL B 1 202 ? 20.462  -35.245 -7.410  1.00 26.62  ? 202  VAL B N   1 
ATOM   4339  C  CA  . VAL B 1 202 ? 21.391  -34.224 -6.925  1.00 30.82  ? 202  VAL B CA  1 
ATOM   4340  C  C   . VAL B 1 202 ? 20.613  -32.948 -6.596  1.00 41.02  ? 202  VAL B C   1 
ATOM   4341  O  O   . VAL B 1 202 ? 20.503  -32.551 -5.428  1.00 38.42  ? 202  VAL B O   1 
ATOM   4342  C  CB  . VAL B 1 202 ? 22.520  -33.913 -7.964  1.00 29.01  ? 202  VAL B CB  1 
ATOM   4343  C  CG1 . VAL B 1 202 ? 23.245  -32.620 -7.623  1.00 10.67  ? 202  VAL B CG1 1 
ATOM   4344  C  CG2 . VAL B 1 202 ? 23.513  -35.074 -8.036  1.00 23.35  ? 202  VAL B CG2 1 
ATOM   4345  N  N   . ASN B 1 203 ? 20.052  -32.331 -7.632  1.00 30.70  ? 203  ASN B N   1 
ATOM   4346  C  CA  . ASN B 1 203 ? 19.249  -31.122 -7.483  1.00 27.21  ? 203  ASN B CA  1 
ATOM   4347  C  C   . ASN B 1 203 ? 18.297  -31.211 -6.323  1.00 24.47  ? 203  ASN B C   1 
ATOM   4348  O  O   . ASN B 1 203 ? 18.182  -30.282 -5.510  1.00 39.72  ? 203  ASN B O   1 
ATOM   4349  C  CB  . ASN B 1 203 ? 18.441  -30.869 -8.751  1.00 31.03  ? 203  ASN B CB  1 
ATOM   4350  C  CG  . ASN B 1 203 ? 19.200  -30.053 -9.771  1.00 43.71  ? 203  ASN B CG  1 
ATOM   4351  O  OD1 . ASN B 1 203 ? 20.432  -29.979 -9.737  1.00 39.47  ? 203  ASN B OD1 1 
ATOM   4352  N  ND2 . ASN B 1 203 ? 18.465  -29.421 -10.687 1.00 54.35  ? 203  ASN B ND2 1 
ATOM   4353  N  N   . TRP B 1 204 ? 17.612  -32.341 -6.247  1.00 20.70  ? 204  TRP B N   1 
ATOM   4354  C  CA  . TRP B 1 204 ? 16.565  -32.521 -5.250  1.00 31.02  ? 204  TRP B CA  1 
ATOM   4355  C  C   . TRP B 1 204 ? 17.153  -32.570 -3.848  1.00 31.99  ? 204  TRP B C   1 
ATOM   4356  O  O   . TRP B 1 204 ? 16.695  -31.887 -2.927  1.00 36.57  ? 204  TRP B O   1 
ATOM   4357  C  CB  . TRP B 1 204 ? 15.802  -33.813 -5.559  1.00 34.36  ? 204  TRP B CB  1 
ATOM   4358  C  CG  . TRP B 1 204 ? 14.575  -34.017 -4.758  1.00 24.53  ? 204  TRP B CG  1 
ATOM   4359  C  CD1 . TRP B 1 204 ? 13.624  -33.091 -4.475  1.00 33.22  ? 204  TRP B CD1 1 
ATOM   4360  C  CD2 . TRP B 1 204 ? 14.153  -35.238 -4.142  1.00 17.33  ? 204  TRP B CD2 1 
ATOM   4361  N  NE1 . TRP B 1 204 ? 12.631  -33.658 -3.707  1.00 35.54  ? 204  TRP B NE1 1 
ATOM   4362  C  CE2 . TRP B 1 204 ? 12.937  -34.978 -3.493  1.00 21.39  ? 204  TRP B CE2 1 
ATOM   4363  C  CE3 . TRP B 1 204 ? 14.690  -36.525 -4.073  1.00 14.20  ? 204  TRP B CE3 1 
ATOM   4364  C  CZ2 . TRP B 1 204 ? 12.246  -35.960 -2.784  1.00 24.39  ? 204  TRP B CZ2 1 
ATOM   4365  C  CZ3 . TRP B 1 204 ? 14.009  -37.493 -3.375  1.00 20.54  ? 204  TRP B CZ3 1 
ATOM   4366  C  CH2 . TRP B 1 204 ? 12.797  -37.210 -2.741  1.00 23.48  ? 204  TRP B CH2 1 
ATOM   4367  N  N   . ILE B 1 205 ? 18.184  -33.389 -3.707  1.00 30.74  ? 205  ILE B N   1 
ATOM   4368  C  CA  . ILE B 1 205 ? 18.801  -33.647 -2.419  1.00 37.52  ? 205  ILE B CA  1 
ATOM   4369  C  C   . ILE B 1 205 ? 19.296  -32.357 -1.779  1.00 39.14  ? 205  ILE B C   1 
ATOM   4370  O  O   . ILE B 1 205 ? 19.226  -32.185 -0.563  1.00 48.51  ? 205  ILE B O   1 
ATOM   4371  C  CB  . ILE B 1 205 ? 19.982  -34.621 -2.581  1.00 32.88  ? 205  ILE B CB  1 
ATOM   4372  C  CG1 . ILE B 1 205 ? 19.481  -36.002 -3.019  1.00 34.05  ? 205  ILE B CG1 1 
ATOM   4373  C  CG2 . ILE B 1 205 ? 20.775  -34.713 -1.296  1.00 29.13  ? 205  ILE B CG2 1 
ATOM   4374  C  CD1 . ILE B 1 205 ? 20.601  -36.943 -3.471  1.00 31.59  ? 205  ILE B CD1 1 
ATOM   4375  N  N   . VAL B 1 206 ? 19.803  -31.449 -2.601  1.00 29.60  ? 206  VAL B N   1 
ATOM   4376  C  CA  . VAL B 1 206 ? 20.342  -30.197 -2.085  1.00 30.06  ? 206  VAL B CA  1 
ATOM   4377  C  C   . VAL B 1 206 ? 19.289  -29.117 -2.046  1.00 26.11  ? 206  VAL B C   1 
ATOM   4378  O  O   . VAL B 1 206 ? 19.575  -28.000 -1.648  1.00 36.20  ? 206  VAL B O   1 
ATOM   4379  C  CB  . VAL B 1 206 ? 21.537  -29.685 -2.922  1.00 36.70  ? 206  VAL B CB  1 
ATOM   4380  C  CG1 . VAL B 1 206 ? 22.719  -30.637 -2.787  1.00 31.18  ? 206  VAL B CG1 1 
ATOM   4381  C  CG2 . VAL B 1 206 ? 21.147  -29.507 -4.388  1.00 33.38  ? 206  VAL B CG2 1 
ATOM   4382  N  N   . SER B 1 207 ? 18.074  -29.464 -2.458  1.00 30.39  ? 207  SER B N   1 
ATOM   4383  C  CA  . SER B 1 207 ? 16.983  -28.509 -2.544  1.00 24.19  ? 207  SER B CA  1 
ATOM   4384  C  C   . SER B 1 207 ? 16.195  -28.399 -1.246  1.00 31.86  ? 207  SER B C   1 
ATOM   4385  O  O   . SER B 1 207 ? 15.469  -27.423 -1.028  1.00 46.74  ? 207  SER B O   1 
ATOM   4386  C  CB  . SER B 1 207 ? 16.038  -28.893 -3.679  1.00 22.04  ? 207  SER B CB  1 
ATOM   4387  O  OG  . SER B 1 207 ? 15.053  -29.813 -3.238  1.00 37.60  ? 207  SER B OG  1 
ATOM   4388  N  N   . LYS B 1 208 ? 16.315  -29.404 -0.389  1.00 37.00  ? 208  LYS B N   1 
ATOM   4389  C  CA  . LYS B 1 208 ? 15.629  -29.381 0.900   1.00 32.56  ? 208  LYS B CA  1 
ATOM   4390  C  C   . LYS B 1 208 ? 16.536  -29.945 1.969   1.00 29.78  ? 208  LYS B C   1 
ATOM   4391  O  O   . LYS B 1 208 ? 17.400  -30.767 1.677   1.00 45.68  ? 208  LYS B O   1 
ATOM   4392  C  CB  . LYS B 1 208 ? 14.333  -30.186 0.840   1.00 39.24  ? 208  LYS B CB  1 
ATOM   4393  C  CG  . LYS B 1 208 ? 13.292  -29.599 -0.086  1.00 44.88  ? 208  LYS B CG  1 
ATOM   4394  C  CD  . LYS B 1 208 ? 12.011  -30.432 -0.145  1.00 38.10  ? 208  LYS B CD  1 
ATOM   4395  C  CE  . LYS B 1 208 ? 10.931  -29.656 -0.937  1.00 50.25  ? 208  LYS B CE  1 
ATOM   4396  N  NZ  . LYS B 1 208 ? 9.617   -30.366 -1.120  1.00 43.04  ? 208  LYS B NZ  1 
ATOM   4397  N  N   . PRO B 1 209 ? 16.330  -29.511 3.218   1.00 26.76  ? 209  PRO B N   1 
ATOM   4398  C  CA  . PRO B 1 209 ? 17.159  -29.901 4.366   1.00 15.78  ? 209  PRO B CA  1 
ATOM   4399  C  C   . PRO B 1 209 ? 16.915  -31.316 4.855   1.00 24.23  ? 209  PRO B C   1 
ATOM   4400  O  O   . PRO B 1 209 ? 16.875  -31.516 6.066   1.00 30.83  ? 209  PRO B O   1 
ATOM   4401  C  CB  . PRO B 1 209 ? 16.731  -28.915 5.446   1.00 15.94  ? 209  PRO B CB  1 
ATOM   4402  C  CG  . PRO B 1 209 ? 15.306  -28.598 5.103   1.00 25.11  ? 209  PRO B CG  1 
ATOM   4403  C  CD  . PRO B 1 209 ? 15.269  -28.562 3.598   1.00 22.44  ? 209  PRO B CD  1 
ATOM   4404  N  N   . PHE B 1 210 ? 16.781  -32.280 3.948   1.00 24.69  ? 210  PHE B N   1 
ATOM   4405  C  CA  . PHE B 1 210 ? 16.616  -33.671 4.355   1.00 26.22  ? 210  PHE B CA  1 
ATOM   4406  C  C   . PHE B 1 210 ? 17.481  -34.055 5.564   1.00 30.27  ? 210  PHE B C   1 
ATOM   4407  O  O   . PHE B 1 210 ? 18.677  -33.776 5.607   1.00 38.64  ? 210  PHE B O   1 
ATOM   4408  C  CB  . PHE B 1 210 ? 16.840  -34.610 3.182   1.00 17.14  ? 210  PHE B CB  1 
ATOM   4409  C  CG  . PHE B 1 210 ? 15.796  -34.482 2.127   1.00 23.16  ? 210  PHE B CG  1 
ATOM   4410  C  CD1 . PHE B 1 210 ? 16.070  -33.852 0.930   1.00 26.46  ? 210  PHE B CD1 1 
ATOM   4411  C  CD2 . PHE B 1 210 ? 14.515  -34.967 2.346   1.00 29.75  ? 210  PHE B CD2 1 
ATOM   4412  C  CE1 . PHE B 1 210 ? 15.090  -33.719 -0.040  1.00 27.88  ? 210  PHE B CE1 1 
ATOM   4413  C  CE2 . PHE B 1 210 ? 13.525  -34.849 1.377   1.00 30.31  ? 210  PHE B CE2 1 
ATOM   4414  C  CZ  . PHE B 1 210 ? 13.809  -34.213 0.190   1.00 23.34  ? 210  PHE B CZ  1 
ATOM   4415  N  N   . VAL B 1 211 ? 16.836  -34.676 6.547   1.00 22.28  ? 211  VAL B N   1 
ATOM   4416  C  CA  . VAL B 1 211 ? 17.446  -35.064 7.805   1.00 15.85  ? 211  VAL B CA  1 
ATOM   4417  C  C   . VAL B 1 211 ? 17.957  -36.508 7.759   1.00 29.10  ? 211  VAL B C   1 
ATOM   4418  O  O   . VAL B 1 211 ? 19.036  -36.817 8.255   1.00 41.55  ? 211  VAL B O   1 
ATOM   4419  C  CB  . VAL B 1 211 ? 16.424  -34.980 8.919   1.00 14.33  ? 211  VAL B CB  1 
ATOM   4420  C  CG1 . VAL B 1 211 ? 16.937  -35.696 10.150  1.00 19.75  ? 211  VAL B CG1 1 
ATOM   4421  C  CG2 . VAL B 1 211 ? 16.080  -33.520 9.211   1.00 25.49  ? 211  VAL B CG2 1 
ATOM   4422  N  N   . LEU B 1 212 ? 17.172  -37.383 7.147   1.00 22.11  ? 212  LEU B N   1 
ATOM   4423  C  CA  . LEU B 1 212 ? 17.453  -38.810 7.102   1.00 26.78  ? 212  LEU B CA  1 
ATOM   4424  C  C   . LEU B 1 212 ? 16.981  -39.381 5.745   1.00 31.94  ? 212  LEU B C   1 
ATOM   4425  O  O   . LEU B 1 212 ? 16.058  -38.845 5.115   1.00 40.04  ? 212  LEU B O   1 
ATOM   4426  C  CB  . LEU B 1 212 ? 16.762  -39.500 8.286   1.00 30.07  ? 212  LEU B CB  1 
ATOM   4427  C  CG  . LEU B 1 212 ? 16.681  -41.021 8.385   1.00 24.72  ? 212  LEU B CG  1 
ATOM   4428  C  CD1 . LEU B 1 212 ? 18.078  -41.564 8.453   1.00 39.04  ? 212  LEU B CD1 1 
ATOM   4429  C  CD2 . LEU B 1 212 ? 15.872  -41.430 9.621   1.00 19.67  ? 212  LEU B CD2 1 
ATOM   4430  N  N   . SER B 1 213 ? 17.627  -40.451 5.290   1.00 27.68  ? 213  SER B N   1 
ATOM   4431  C  CA  . SER B 1 213 ? 17.304  -41.046 4.004   1.00 23.13  ? 213  SER B CA  1 
ATOM   4432  C  C   . SER B 1 213 ? 17.753  -42.512 3.901   1.00 28.60  ? 213  SER B C   1 
ATOM   4433  O  O   . SER B 1 213 ? 18.529  -42.998 4.722   1.00 25.61  ? 213  SER B O   1 
ATOM   4434  C  CB  . SER B 1 213 ? 17.944  -40.231 2.890   1.00 24.01  ? 213  SER B CB  1 
ATOM   4435  O  OG  . SER B 1 213 ? 17.676  -40.808 1.620   1.00 33.26  ? 213  SER B OG  1 
ATOM   4436  N  N   . ALA B 1 214 ? 17.245  -43.222 2.900   1.00 30.68  ? 214  ALA B N   1 
ATOM   4437  C  CA  . ALA B 1 214 ? 17.705  -44.579 2.620   1.00 27.58  ? 214  ALA B CA  1 
ATOM   4438  C  C   . ALA B 1 214 ? 17.431  -44.920 1.169   1.00 17.60  ? 214  ALA B C   1 
ATOM   4439  O  O   . ALA B 1 214 ? 16.390  -44.559 0.635   1.00 24.23  ? 214  ALA B O   1 
ATOM   4440  C  CB  . ALA B 1 214 ? 17.027  -45.593 3.545   1.00 28.87  ? 214  ALA B CB  1 
ATOM   4441  N  N   . ASN B 1 215 ? 18.365  -45.598 0.514   1.00 32.32  ? 215  ASN B N   1 
ATOM   4442  C  CA  . ASN B 1 215 ? 18.060  -46.128 -0.809  1.00 34.84  ? 215  ASN B CA  1 
ATOM   4443  C  C   . ASN B 1 215 ? 18.229  -47.639 -0.903  1.00 33.10  ? 215  ASN B C   1 
ATOM   4444  O  O   . ASN B 1 215 ? 19.139  -48.221 -0.304  1.00 25.09  ? 215  ASN B O   1 
ATOM   4445  C  CB  . ASN B 1 215 ? 18.789  -45.380 -1.931  1.00 41.00  ? 215  ASN B CB  1 
ATOM   4446  C  CG  . ASN B 1 215 ? 20.285  -45.644 -1.957  1.00 35.03  ? 215  ASN B CG  1 
ATOM   4447  O  OD1 . ASN B 1 215 ? 20.784  -46.378 -2.811  1.00 48.27  ? 215  ASN B OD1 1 
ATOM   4448  N  ND2 . ASN B 1 215 ? 21.007  -45.021 -1.054  1.00 19.91  ? 215  ASN B ND2 1 
ATOM   4449  N  N   . PHE B 1 216 ? 17.324  -48.260 -1.654  1.00 35.45  ? 216  PHE B N   1 
ATOM   4450  C  CA  . PHE B 1 216 ? 17.141  -49.704 -1.587  1.00 26.25  ? 216  PHE B CA  1 
ATOM   4451  C  C   . PHE B 1 216 ? 17.737  -50.425 -2.793  1.00 31.22  ? 216  PHE B C   1 
ATOM   4452  O  O   . PHE B 1 216 ? 17.642  -49.960 -3.928  1.00 37.92  ? 216  PHE B O   1 
ATOM   4453  C  CB  . PHE B 1 216 ? 15.661  -50.045 -1.353  1.00 23.39  ? 216  PHE B CB  1 
ATOM   4454  C  CG  . PHE B 1 216 ? 15.108  -49.431 -0.090  1.00 32.39  ? 216  PHE B CG  1 
ATOM   4455  C  CD1 . PHE B 1 216 ? 14.607  -48.141 -0.100  1.00 35.93  ? 216  PHE B CD1 1 
ATOM   4456  C  CD2 . PHE B 1 216 ? 15.138  -50.123 1.119   1.00 29.52  ? 216  PHE B CD2 1 
ATOM   4457  C  CE1 . PHE B 1 216 ? 14.128  -47.555 1.063   1.00 27.20  ? 216  PHE B CE1 1 
ATOM   4458  C  CE2 . PHE B 1 216 ? 14.663  -49.543 2.278   1.00 26.04  ? 216  PHE B CE2 1 
ATOM   4459  C  CZ  . PHE B 1 216 ? 14.158  -48.252 2.248   1.00 21.43  ? 216  PHE B CZ  1 
ATOM   4460  N  N   . HIS B 1 217 ? 18.395  -51.543 -2.509  1.00 26.76  ? 217  HIS B N   1 
ATOM   4461  C  CA  . HIS B 1 217 ? 19.090  -52.319 -3.513  1.00 30.83  ? 217  HIS B CA  1 
ATOM   4462  C  C   . HIS B 1 217 ? 18.749  -53.786 -3.324  1.00 35.64  ? 217  HIS B C   1 
ATOM   4463  O  O   . HIS B 1 217 ? 18.040  -54.160 -2.380  1.00 29.88  ? 217  HIS B O   1 
ATOM   4464  C  CB  . HIS B 1 217 ? 20.608  -52.117 -3.399  1.00 20.92  ? 217  HIS B CB  1 
ATOM   4465  C  CG  . HIS B 1 217 ? 21.063  -50.750 -3.792  1.00 28.48  ? 217  HIS B CG  1 
ATOM   4466  N  ND1 . HIS B 1 217 ? 21.740  -50.498 -4.972  1.00 28.04  ? 217  HIS B ND1 1 
ATOM   4467  C  CD2 . HIS B 1 217 ? 20.920  -49.551 -3.173  1.00 30.10  ? 217  HIS B CD2 1 
ATOM   4468  C  CE1 . HIS B 1 217 ? 22.000  -49.203 -5.055  1.00 29.85  ? 217  HIS B CE1 1 
ATOM   4469  N  NE2 . HIS B 1 217 ? 21.515  -48.607 -3.975  1.00 31.86  ? 217  HIS B NE2 1 
ATOM   4470  N  N   . GLY B 1 218 ? 19.256  -54.614 -4.229  1.00 30.92  ? 218  GLY B N   1 
ATOM   4471  C  CA  . GLY B 1 218 ? 19.047  -56.039 -4.143  1.00 31.91  ? 218  GLY B CA  1 
ATOM   4472  C  C   . GLY B 1 218 ? 20.357  -56.731 -4.416  1.00 32.56  ? 218  GLY B C   1 
ATOM   4473  O  O   . GLY B 1 218 ? 21.308  -56.082 -4.848  1.00 34.08  ? 218  GLY B O   1 
ATOM   4474  N  N   . GLY B 1 219 ? 20.402  -58.041 -4.171  1.00 32.58  ? 219  GLY B N   1 
ATOM   4475  C  CA  . GLY B 1 219 ? 21.603  -58.827 -4.384  1.00 25.47  ? 219  GLY B CA  1 
ATOM   4476  C  C   . GLY B 1 219 ? 22.103  -59.422 -3.083  1.00 44.74  ? 219  GLY B C   1 
ATOM   4477  O  O   . GLY B 1 219 ? 22.793  -60.448 -3.062  1.00 54.75  ? 219  GLY B O   1 
ATOM   4478  N  N   . ALA B 1 220 ? 21.746  -58.773 -1.982  1.00 41.75  ? 220  ALA B N   1 
ATOM   4479  C  CA  . ALA B 1 220 ? 22.115  -59.262 -0.664  1.00 47.29  ? 220  ALA B CA  1 
ATOM   4480  C  C   . ALA B 1 220 ? 21.124  -58.779 0.373   1.00 37.40  ? 220  ALA B C   1 
ATOM   4481  O  O   . ALA B 1 220 ? 20.190  -58.034 0.056   1.00 38.76  ? 220  ALA B O   1 
ATOM   4482  C  CB  . ALA B 1 220 ? 23.517  -58.814 -0.302  1.00 51.40  ? 220  ALA B CB  1 
ATOM   4483  N  N   . VAL B 1 221 ? 21.327  -59.208 1.614   1.00 32.66  ? 221  VAL B N   1 
ATOM   4484  C  CA  . VAL B 1 221 ? 20.449  -58.800 2.713   1.00 45.59  ? 221  VAL B CA  1 
ATOM   4485  C  C   . VAL B 1 221 ? 21.231  -58.207 3.890   1.00 48.95  ? 221  VAL B C   1 
ATOM   4486  O  O   . VAL B 1 221 ? 21.717  -58.941 4.763   1.00 34.16  ? 221  VAL B O   1 
ATOM   4487  C  CB  . VAL B 1 221 ? 19.582  -59.966 3.197   1.00 35.60  ? 221  VAL B CB  1 
ATOM   4488  C  CG1 . VAL B 1 221 ? 18.467  -59.458 4.096   1.00 31.18  ? 221  VAL B CG1 1 
ATOM   4489  C  CG2 . VAL B 1 221 ? 18.993  -60.672 2.009   1.00 38.66  ? 221  VAL B CG2 1 
ATOM   4490  N  N   . VAL B 1 222 ? 21.333  -56.875 3.904   1.00 45.17  ? 222  VAL B N   1 
ATOM   4491  C  CA  . VAL B 1 222 ? 22.215  -56.185 4.834   1.00 38.04  ? 222  VAL B CA  1 
ATOM   4492  C  C   . VAL B 1 222 ? 21.973  -54.683 4.899   1.00 42.81  ? 222  VAL B C   1 
ATOM   4493  O  O   . VAL B 1 222 ? 21.513  -54.070 3.937   1.00 53.96  ? 222  VAL B O   1 
ATOM   4494  C  CB  . VAL B 1 222 ? 23.663  -56.364 4.412   1.00 39.61  ? 222  VAL B CB  1 
ATOM   4495  C  CG1 . VAL B 1 222 ? 23.913  -55.598 3.116   1.00 21.91  ? 222  VAL B CG1 1 
ATOM   4496  C  CG2 . VAL B 1 222 ? 24.590  -55.885 5.526   1.00 47.28  ? 222  VAL B CG2 1 
ATOM   4497  N  N   . ALA B 1 223 ? 22.316  -54.098 6.041   1.00 36.08  ? 223  ALA B N   1 
ATOM   4498  C  CA  . ALA B 1 223 ? 22.213  -52.661 6.254   1.00 27.21  ? 223  ALA B CA  1 
ATOM   4499  C  C   . ALA B 1 223 ? 23.570  -51.970 6.088   1.00 33.53  ? 223  ALA B C   1 
ATOM   4500  O  O   . ALA B 1 223 ? 24.414  -52.012 6.984   1.00 27.48  ? 223  ALA B O   1 
ATOM   4501  C  CB  . ALA B 1 223 ? 21.647  -52.385 7.635   1.00 18.34  ? 223  ALA B CB  1 
ATOM   4502  N  N   . SER B 1 224 ? 23.768  -51.318 4.945   1.00 35.78  ? 224  SER B N   1 
ATOM   4503  C  CA  . SER B 1 224 ? 25.043  -50.671 4.644   1.00 32.18  ? 224  SER B CA  1 
ATOM   4504  C  C   . SER B 1 224 ? 25.015  -49.160 4.876   1.00 28.33  ? 224  SER B C   1 
ATOM   4505  O  O   . SER B 1 224 ? 24.006  -48.501 4.590   1.00 28.11  ? 224  SER B O   1 
ATOM   4506  C  CB  . SER B 1 224 ? 25.466  -50.979 3.209   1.00 30.42  ? 224  SER B CB  1 
ATOM   4507  O  OG  . SER B 1 224 ? 26.766  -50.474 2.950   1.00 40.06  ? 224  SER B OG  1 
ATOM   4508  N  N   . TYR B 1 225 ? 26.133  -48.632 5.386   1.00 27.28  ? 225  TYR B N   1 
ATOM   4509  C  CA  . TYR B 1 225 ? 26.278  -47.222 5.760   1.00 22.34  ? 225  TYR B CA  1 
ATOM   4510  C  C   . TYR B 1 225 ? 27.653  -46.645 5.379   1.00 27.26  ? 225  TYR B C   1 
ATOM   4511  O  O   . TYR B 1 225 ? 28.594  -47.393 5.140   1.00 20.44  ? 225  TYR B O   1 
ATOM   4512  C  CB  . TYR B 1 225 ? 26.041  -47.053 7.268   1.00 31.28  ? 225  TYR B CB  1 
ATOM   4513  C  CG  . TYR B 1 225 ? 26.958  -47.882 8.139   1.00 26.13  ? 225  TYR B CG  1 
ATOM   4514  C  CD1 . TYR B 1 225 ? 26.651  -49.204 8.435   1.00 36.93  ? 225  TYR B CD1 1 
ATOM   4515  C  CD2 . TYR B 1 225 ? 28.120  -47.343 8.677   1.00 26.21  ? 225  TYR B CD2 1 
ATOM   4516  C  CE1 . TYR B 1 225 ? 27.489  -49.974 9.231   1.00 38.76  ? 225  TYR B CE1 1 
ATOM   4517  C  CE2 . TYR B 1 225 ? 28.964  -48.105 9.478   1.00 41.59  ? 225  TYR B CE2 1 
ATOM   4518  C  CZ  . TYR B 1 225 ? 28.646  -49.419 9.749   1.00 47.05  ? 225  TYR B CZ  1 
ATOM   4519  O  OH  . TYR B 1 225 ? 29.488  -50.176 10.543  1.00 54.37  ? 225  TYR B OH  1 
ATOM   4520  N  N   . PRO B 1 226 ? 27.771  -45.302 5.330   1.00 26.30  ? 226  PRO B N   1 
ATOM   4521  C  CA  . PRO B 1 226 ? 28.991  -44.568 4.944   1.00 26.20  ? 226  PRO B CA  1 
ATOM   4522  C  C   . PRO B 1 226 ? 30.228  -44.809 5.822   1.00 28.07  ? 226  PRO B C   1 
ATOM   4523  O  O   . PRO B 1 226 ? 30.107  -45.011 7.026   1.00 34.20  ? 226  PRO B O   1 
ATOM   4524  C  CB  . PRO B 1 226 ? 28.566  -43.104 5.056   1.00 27.60  ? 226  PRO B CB  1 
ATOM   4525  C  CG  . PRO B 1 226 ? 27.100  -43.114 4.878   1.00 35.91  ? 226  PRO B CG  1 
ATOM   4526  C  CD  . PRO B 1 226 ? 26.612  -44.405 5.466   1.00 24.96  ? 226  PRO B CD  1 
ATOM   4527  N  N   . TYR B 1 227 ? 31.418  -44.728 5.229   1.00 24.40  ? 227  TYR B N   1 
ATOM   4528  C  CA  . TYR B 1 227 ? 31.584  -44.320 3.842   1.00 21.51  ? 227  TYR B CA  1 
ATOM   4529  C  C   . TYR B 1 227 ? 31.710  -45.542 2.959   1.00 32.78  ? 227  TYR B C   1 
ATOM   4530  O  O   . TYR B 1 227 ? 31.984  -46.637 3.446   1.00 34.32  ? 227  TYR B O   1 
ATOM   4531  C  CB  . TYR B 1 227 ? 32.841  -43.474 3.663   1.00 36.57  ? 227  TYR B CB  1 
ATOM   4532  C  CG  . TYR B 1 227 ? 32.797  -42.074 4.241   1.00 33.10  ? 227  TYR B CG  1 
ATOM   4533  C  CD1 . TYR B 1 227 ? 32.001  -41.076 3.669   1.00 23.74  ? 227  TYR B CD1 1 
ATOM   4534  C  CD2 . TYR B 1 227 ? 33.603  -41.734 5.326   1.00 31.39  ? 227  TYR B CD2 1 
ATOM   4535  C  CE1 . TYR B 1 227 ? 31.984  -39.778 4.194   1.00 31.65  ? 227  TYR B CE1 1 
ATOM   4536  C  CE2 . TYR B 1 227 ? 33.595  -40.453 5.861   1.00 39.16  ? 227  TYR B CE2 1 
ATOM   4537  C  CZ  . TYR B 1 227 ? 32.788  -39.471 5.297   1.00 45.31  ? 227  TYR B CZ  1 
ATOM   4538  O  OH  . TYR B 1 227 ? 32.792  -38.192 5.846   1.00 43.42  ? 227  TYR B OH  1 
ATOM   4539  N  N   . ASP B 1 228 ? 31.533  -45.339 1.655   1.00 39.49  ? 228  ASP B N   1 
ATOM   4540  C  CA  . ASP B 1 228 ? 31.626  -46.414 0.680   1.00 26.21  ? 228  ASP B CA  1 
ATOM   4541  C  C   . ASP B 1 228 ? 33.023  -46.486 0.088   1.00 29.75  ? 228  ASP B C   1 
ATOM   4542  O  O   . ASP B 1 228 ? 33.379  -47.468 -0.565  1.00 43.53  ? 228  ASP B O   1 
ATOM   4543  C  CB  . ASP B 1 228 ? 30.598  -46.215 -0.434  1.00 33.11  ? 228  ASP B CB  1 
ATOM   4544  C  CG  . ASP B 1 228 ? 29.206  -46.713 -0.055  1.00 46.32  ? 228  ASP B CG  1 
ATOM   4545  O  OD1 . ASP B 1 228 ? 29.057  -47.339 1.018   1.00 54.33  ? 228  ASP B OD1 1 
ATOM   4546  O  OD2 . ASP B 1 228 ? 28.258  -46.484 -0.845  1.00 53.54  ? 228  ASP B OD2 1 
ATOM   4547  N  N   . ASN B 1 229 ? 33.812  -45.441 0.296   1.00 24.09  ? 229  ASN B N   1 
ATOM   4548  C  CA  . ASN B 1 229 ? 35.190  -45.439 -0.205  1.00 41.95  ? 229  ASN B CA  1 
ATOM   4549  C  C   . ASN B 1 229 ? 36.144  -44.722 0.741   1.00 39.05  ? 229  ASN B C   1 
ATOM   4550  O  O   . ASN B 1 229 ? 35.737  -44.318 1.821   1.00 31.94  ? 229  ASN B O   1 
ATOM   4551  C  CB  . ASN B 1 229 ? 35.275  -44.862 -1.626  1.00 39.58  ? 229  ASN B CB  1 
ATOM   4552  C  CG  . ASN B 1 229 ? 34.905  -43.378 -1.695  1.00 31.90  ? 229  ASN B CG  1 
ATOM   4553  O  OD1 . ASN B 1 229 ? 34.657  -42.738 -0.683  1.00 24.78  ? 229  ASN B OD1 1 
ATOM   4554  N  ND2 . ASN B 1 229 ? 34.857  -42.839 -2.907  1.00 22.68  ? 229  ASN B ND2 1 
ATOM   4555  N  N   . SER B 1 230 ? 37.402  -44.566 0.337   1.00 39.74  ? 230  SER B N   1 
ATOM   4556  C  CA  . SER B 1 230 ? 38.400  -43.890 1.173   1.00 34.73  ? 230  SER B CA  1 
ATOM   4557  C  C   . SER B 1 230 ? 39.609  -43.411 0.368   1.00 35.88  ? 230  SER B C   1 
ATOM   4558  O  O   . SER B 1 230 ? 39.798  -43.817 -0.782  1.00 40.95  ? 230  SER B O   1 
ATOM   4559  C  CB  . SER B 1 230 ? 38.888  -44.829 2.267   1.00 24.81  ? 230  SER B CB  1 
ATOM   4560  O  OG  . SER B 1 230 ? 39.834  -45.750 1.756   1.00 32.18  ? 230  SER B OG  1 
ATOM   4561  N  N   . LEU B 1 231 ? 40.442  -42.568 0.973   1.00 35.20  ? 231  LEU B N   1 
ATOM   4562  C  CA  . LEU B 1 231 ? 41.667  -42.111 0.302   1.00 47.83  ? 231  LEU B CA  1 
ATOM   4563  C  C   . LEU B 1 231 ? 42.610  -43.257 -0.083  1.00 54.78  ? 231  LEU B C   1 
ATOM   4564  O  O   . LEU B 1 231 ? 43.334  -43.178 -1.084  1.00 53.50  ? 231  LEU B O   1 
ATOM   4565  C  CB  . LEU B 1 231 ? 42.414  -41.095 1.166   1.00 49.91  ? 231  LEU B CB  1 
ATOM   4566  C  CG  . LEU B 1 231 ? 41.967  -39.636 1.043   1.00 52.40  ? 231  LEU B CG  1 
ATOM   4567  C  CD1 . LEU B 1 231 ? 42.572  -38.771 2.156   1.00 36.03  ? 231  LEU B CD1 1 
ATOM   4568  C  CD2 . LEU B 1 231 ? 42.321  -39.096 -0.347  1.00 54.04  ? 231  LEU B CD2 1 
ATOM   4569  N  N   . ALA B 1 232 ? 42.595  -44.314 0.724   1.00 52.16  ? 232  ALA B N   1 
ATOM   4570  C  CA  . ALA B 1 232 ? 43.431  -45.493 0.506   1.00 42.13  ? 232  ALA B CA  1 
ATOM   4571  C  C   . ALA B 1 232 ? 43.019  -46.244 -0.751  1.00 49.89  ? 232  ALA B C   1 
ATOM   4572  O  O   . ALA B 1 232 ? 43.839  -46.915 -1.380  1.00 44.35  ? 232  ALA B O   1 
ATOM   4573  C  CB  . ALA B 1 232 ? 43.337  -46.411 1.700   1.00 29.16  ? 232  ALA B CB  1 
ATOM   4574  N  N   . HIS B 1 233 ? 41.739  -46.111 -1.099  1.00 57.07  ? 233  HIS B N   1 
ATOM   4575  C  CA  . HIS B 1 233 ? 41.093  -46.841 -2.198  1.00 46.94  ? 233  HIS B CA  1 
ATOM   4576  C  C   . HIS B 1 233 ? 41.319  -48.349 -2.146  1.00 56.44  ? 233  HIS B C   1 
ATOM   4577  O  O   . HIS B 1 233 ? 41.712  -48.957 -3.143  1.00 59.97  ? 233  HIS B O   1 
ATOM   4578  C  CB  . HIS B 1 233 ? 41.460  -46.262 -3.573  1.00 30.04  ? 233  HIS B CB  1 
ATOM   4579  C  CG  . HIS B 1 233 ? 40.889  -44.898 -3.823  1.00 33.75  ? 233  HIS B CG  1 
ATOM   4580  N  ND1 . HIS B 1 233 ? 41.628  -43.742 -3.695  1.00 50.15  ? 233  HIS B ND1 1 
ATOM   4581  C  CD2 . HIS B 1 233 ? 39.641  -44.505 -4.163  1.00 43.19  ? 233  HIS B CD2 1 
ATOM   4582  C  CE1 . HIS B 1 233 ? 40.863  -42.697 -3.958  1.00 48.76  ? 233  HIS B CE1 1 
ATOM   4583  N  NE2 . HIS B 1 233 ? 39.652  -43.132 -4.243  1.00 41.03  ? 233  HIS B NE2 1 
ATOM   4584  N  N   . ASN B 1 234 ? 41.055  -48.938 -0.978  1.00 58.46  ? 234  ASN B N   1 
ATOM   4585  C  CA  . ASN B 1 234 ? 41.149  -50.383 -0.779  1.00 58.68  ? 234  ASN B CA  1 
ATOM   4586  C  C   . ASN B 1 234 ? 39.993  -51.121 -1.453  1.00 50.35  ? 234  ASN B C   1 
ATOM   4587  O  O   . ASN B 1 234 ? 38.846  -50.675 -1.396  1.00 44.68  ? 234  ASN B O   1 
ATOM   4588  C  CB  . ASN B 1 234 ? 41.160  -50.723 0.718   1.00 52.98  ? 234  ASN B CB  1 
ATOM   4589  C  CG  . ASN B 1 234 ? 42.226  -49.976 1.481   1.00 35.12  ? 234  ASN B CG  1 
ATOM   4590  O  OD1 . ASN B 1 234 ? 43.321  -49.753 0.982   1.00 35.82  ? 234  ASN B OD1 1 
ATOM   4591  N  ND2 . ASN B 1 234 ? 41.908  -49.589 2.699   1.00 33.24  ? 234  ASN B ND2 1 
ATOM   4592  N  N   . GLU B 1 235 ? 40.293  -52.256 -2.078  1.00 52.36  ? 235  GLU B N   1 
ATOM   4593  C  CA  . GLU B 1 235 ? 39.253  -53.079 -2.696  1.00 53.82  ? 235  GLU B CA  1 
ATOM   4594  C  C   . GLU B 1 235 ? 38.097  -53.358 -1.734  1.00 58.67  ? 235  GLU B C   1 
ATOM   4595  O  O   . GLU B 1 235 ? 36.931  -53.146 -2.083  1.00 43.04  ? 235  GLU B O   1 
ATOM   4596  C  CB  . GLU B 1 235 ? 39.833  -54.405 -3.207  1.00 48.13  ? 235  GLU B CB  1 
ATOM   4597  C  CG  . GLU B 1 235 ? 38.800  -55.313 -3.866  1.00 68.21  ? 235  GLU B CG  1 
ATOM   4598  C  CD  . GLU B 1 235 ? 39.356  -56.678 -4.260  1.00 80.48  ? 235  GLU B CD  1 
ATOM   4599  O  OE1 . GLU B 1 235 ? 38.884  -57.243 -5.273  1.00 87.85  ? 235  GLU B OE1 1 
ATOM   4600  O  OE2 . GLU B 1 235 ? 40.258  -57.189 -3.559  1.00 71.71  ? 235  GLU B OE2 1 
ATOM   4601  N  N   . CYS B 1 236 ? 38.434  -53.817 -0.523  1.00 66.48  ? 236  CYS B N   1 
ATOM   4602  C  CA  . CYS B 1 236 ? 37.445  -54.309 0.437   1.00 57.86  ? 236  CYS B CA  1 
ATOM   4603  C  C   . CYS B 1 236 ? 37.997  -54.524 1.839   1.00 44.46  ? 236  CYS B C   1 
ATOM   4604  O  O   . CYS B 1 236 ? 39.182  -54.348 2.100   1.00 48.57  ? 236  CYS B O   1 
ATOM   4605  C  CB  . CYS B 1 236 ? 36.927  -55.666 -0.022  1.00 71.62  ? 236  CYS B CB  1 
ATOM   4606  S  SG  . CYS B 1 236 ? 37.987  -57.043 0.533   1.00 35.98  ? 236  CYS B SG  1 
ATOM   4607  N  N   . CYS B 1 237 ? 37.097  -54.936 2.728   1.00 56.74  ? 237  CYS B N   1 
ATOM   4608  C  CA  . CYS B 1 237 ? 37.434  -55.496 4.042   1.00 48.34  ? 237  CYS B CA  1 
ATOM   4609  C  C   . CYS B 1 237 ? 38.154  -54.530 4.953   1.00 33.98  ? 237  CYS B C   1 
ATOM   4610  O  O   . CYS B 1 237 ? 38.859  -54.948 5.868   1.00 46.31  ? 237  CYS B O   1 
ATOM   4611  C  CB  . CYS B 1 237 ? 38.247  -56.781 3.874   1.00 49.64  ? 237  CYS B CB  1 
ATOM   4612  S  SG  . CYS B 1 237 ? 37.708  -57.732 2.435   1.00 61.92  ? 237  CYS B SG  1 
ATOM   4613  N  N   . GLU B 1 238 ? 37.971  -53.241 4.705   1.00 27.17  ? 238  GLU B N   1 
ATOM   4614  C  CA  . GLU B 1 238 ? 38.605  -52.212 5.516   1.00 36.18  ? 238  GLU B CA  1 
ATOM   4615  C  C   . GLU B 1 238 ? 37.647  -51.063 5.772   1.00 39.84  ? 238  GLU B C   1 
ATOM   4616  O  O   . GLU B 1 238 ? 37.268  -50.350 4.851   1.00 42.39  ? 238  GLU B O   1 
ATOM   4617  C  CB  . GLU B 1 238 ? 39.885  -51.707 4.841   1.00 54.78  ? 238  GLU B CB  1 
ATOM   4618  C  CG  . GLU B 1 238 ? 41.114  -51.736 5.746   1.00 70.87  ? 238  GLU B CG  1 
ATOM   4619  C  CD  . GLU B 1 238 ? 42.401  -51.993 4.984   1.00 81.14  ? 238  GLU B CD  1 
ATOM   4620  O  OE1 . GLU B 1 238 ? 43.486  -51.847 5.583   1.00 91.16  ? 238  GLU B OE1 1 
ATOM   4621  O  OE2 . GLU B 1 238 ? 42.326  -52.347 3.789   1.00 78.39  ? 238  GLU B OE2 1 
ATOM   4622  N  N   . GLU B 1 239 ? 37.260  -50.895 7.033   1.00 55.24  ? 239  GLU B N   1 
ATOM   4623  C  CA  . GLU B 1 239 ? 36.292  -49.879 7.432   1.00 46.61  ? 239  GLU B CA  1 
ATOM   4624  C  C   . GLU B 1 239 ? 36.705  -48.466 7.070   1.00 40.15  ? 239  GLU B C   1 
ATOM   4625  O  O   . GLU B 1 239 ? 37.792  -48.020 7.421   1.00 49.63  ? 239  GLU B O   1 
ATOM   4626  C  CB  . GLU B 1 239 ? 36.055  -49.949 8.934   1.00 61.10  ? 239  GLU B CB  1 
ATOM   4627  C  CG  . GLU B 1 239 ? 35.100  -51.045 9.361   1.00 76.02  ? 239  GLU B CG  1 
ATOM   4628  C  CD  . GLU B 1 239 ? 34.762  -50.971 10.840  1.00 85.51  ? 239  GLU B CD  1 
ATOM   4629  O  OE1 . GLU B 1 239 ? 33.618  -51.317 11.208  1.00 80.97  ? 239  GLU B OE1 1 
ATOM   4630  O  OE2 . GLU B 1 239 ? 35.642  -50.556 11.630  1.00 88.58  ? 239  GLU B OE2 1 
ATOM   4631  N  N   . SER B 1 240 ? 35.824  -47.758 6.374   1.00 32.42  ? 240  SER B N   1 
ATOM   4632  C  CA  . SER B 1 240 ? 36.030  -46.346 6.124   1.00 19.93  ? 240  SER B CA  1 
ATOM   4633  C  C   . SER B 1 240 ? 34.915  -45.590 6.822   1.00 37.13  ? 240  SER B C   1 
ATOM   4634  O  O   . SER B 1 240 ? 33.932  -45.200 6.198   1.00 44.61  ? 240  SER B O   1 
ATOM   4635  C  CB  . SER B 1 240 ? 36.015  -46.044 4.632   1.00 27.85  ? 240  SER B CB  1 
ATOM   4636  O  OG  . SER B 1 240 ? 36.362  -44.688 4.409   1.00 40.04  ? 240  SER B OG  1 
ATOM   4637  N  N   . LEU B 1 241 ? 35.079  -45.376 8.121   1.00 44.91  ? 241  LEU B N   1 
ATOM   4638  C  CA  . LEU B 1 241 ? 33.999  -44.870 8.954   1.00 30.56  ? 241  LEU B CA  1 
ATOM   4639  C  C   . LEU B 1 241 ? 33.824  -43.356 8.910   1.00 38.79  ? 241  LEU B C   1 
ATOM   4640  O  O   . LEU B 1 241 ? 34.706  -42.618 8.494   1.00 36.67  ? 241  LEU B O   1 
ATOM   4641  C  CB  . LEU B 1 241 ? 34.180  -45.336 10.394  1.00 23.89  ? 241  LEU B CB  1 
ATOM   4642  C  CG  . LEU B 1 241 ? 34.350  -46.841 10.551  1.00 30.18  ? 241  LEU B CG  1 
ATOM   4643  C  CD1 . LEU B 1 241 ? 34.605  -47.189 12.015  1.00 29.02  ? 241  LEU B CD1 1 
ATOM   4644  C  CD2 . LEU B 1 241 ? 33.139  -47.565 10.003  1.00 8.66   ? 241  LEU B CD2 1 
ATOM   4645  N  N   . THR B 1 242 ? 32.660  -42.922 9.376   1.00 56.06  ? 242  THR B N   1 
ATOM   4646  C  CA  . THR B 1 242 ? 32.197  -41.552 9.275   1.00 36.14  ? 242  THR B CA  1 
ATOM   4647  C  C   . THR B 1 242 ? 32.286  -40.887 10.647  1.00 39.42  ? 242  THR B C   1 
ATOM   4648  O  O   . THR B 1 242 ? 32.262  -41.575 11.665  1.00 46.32  ? 242  THR B O   1 
ATOM   4649  C  CB  . THR B 1 242 ? 30.736  -41.585 8.791   1.00 41.75  ? 242  THR B CB  1 
ATOM   4650  O  OG1 . THR B 1 242 ? 30.685  -41.304 7.385   1.00 39.02  ? 242  THR B OG1 1 
ATOM   4651  C  CG2 . THR B 1 242 ? 29.875  -40.608 9.550   1.00 33.30  ? 242  THR B CG2 1 
ATOM   4652  N  N   . PRO B 1 243 ? 32.406  -39.549 10.692  1.00 36.73  ? 243  PRO B N   1 
ATOM   4653  C  CA  . PRO B 1 243 ? 32.417  -38.893 12.007  1.00 37.55  ? 243  PRO B CA  1 
ATOM   4654  C  C   . PRO B 1 243 ? 31.186  -39.302 12.799  1.00 33.13  ? 243  PRO B C   1 
ATOM   4655  O  O   . PRO B 1 243 ? 31.225  -39.380 14.022  1.00 34.15  ? 243  PRO B O   1 
ATOM   4656  C  CB  . PRO B 1 243 ? 32.347  -37.396 11.666  1.00 38.58  ? 243  PRO B CB  1 
ATOM   4657  C  CG  . PRO B 1 243 ? 32.887  -37.293 10.283  1.00 44.10  ? 243  PRO B CG  1 
ATOM   4658  C  CD  . PRO B 1 243 ? 32.554  -38.586 9.585   1.00 48.06  ? 243  PRO B CD  1 
ATOM   4659  N  N   . ASP B 1 244 ? 30.097  -39.570 12.091  1.00 37.15  ? 244  ASP B N   1 
ATOM   4660  C  CA  . ASP B 1 244 ? 28.852  -39.931 12.744  1.00 40.74  ? 244  ASP B CA  1 
ATOM   4661  C  C   . ASP B 1 244 ? 28.642  -41.433 12.721  1.00 41.26  ? 244  ASP B C   1 
ATOM   4662  O  O   . ASP B 1 244 ? 27.525  -41.902 12.491  1.00 45.50  ? 244  ASP B O   1 
ATOM   4663  C  CB  . ASP B 1 244 ? 27.672  -39.207 12.087  1.00 33.77  ? 244  ASP B CB  1 
ATOM   4664  C  CG  . ASP B 1 244 ? 27.470  -37.813 12.640  1.00 40.28  ? 244  ASP B CG  1 
ATOM   4665  O  OD1 . ASP B 1 244 ? 26.936  -37.680 13.756  1.00 46.68  ? 244  ASP B OD1 1 
ATOM   4666  O  OD2 . ASP B 1 244 ? 27.852  -36.841 11.965  1.00 51.54  ? 244  ASP B OD2 1 
ATOM   4667  N  N   . ASP B 1 245 ? 29.706  -42.191 12.974  1.00 34.53  ? 245  ASP B N   1 
ATOM   4668  C  CA  . ASP B 1 245 ? 29.591  -43.644 12.910  1.00 38.80  ? 245  ASP B CA  1 
ATOM   4669  C  C   . ASP B 1 245 ? 28.586  -44.216 13.906  1.00 39.31  ? 245  ASP B C   1 
ATOM   4670  O  O   . ASP B 1 245 ? 27.832  -45.130 13.584  1.00 46.47  ? 245  ASP B O   1 
ATOM   4671  C  CB  . ASP B 1 245 ? 30.934  -44.345 13.083  1.00 20.17  ? 245  ASP B CB  1 
ATOM   4672  C  CG  . ASP B 1 245 ? 30.908  -45.747 12.505  1.00 47.36  ? 245  ASP B CG  1 
ATOM   4673  O  OD1 . ASP B 1 245 ? 30.515  -45.890 11.325  1.00 64.21  ? 245  ASP B OD1 1 
ATOM   4674  O  OD2 . ASP B 1 245 ? 31.246  -46.711 13.217  1.00 47.95  ? 245  ASP B OD2 1 
ATOM   4675  N  N   . ARG B 1 246 ? 28.579  -43.688 15.120  1.00 23.20  ? 246  ARG B N   1 
ATOM   4676  C  CA  . ARG B 1 246 ? 27.673  -44.209 16.130  1.00 40.28  ? 246  ARG B CA  1 
ATOM   4677  C  C   . ARG B 1 246 ? 26.255  -44.157 15.594  1.00 41.81  ? 246  ARG B C   1 
ATOM   4678  O  O   . ARG B 1 246 ? 25.567  -45.178 15.483  1.00 44.77  ? 246  ARG B O   1 
ATOM   4679  C  CB  . ARG B 1 246 ? 27.784  -43.401 17.428  1.00 41.95  ? 246  ARG B CB  1 
ATOM   4680  C  CG  . ARG B 1 246 ? 29.193  -43.362 18.003  1.00 47.05  ? 246  ARG B CG  1 
ATOM   4681  C  CD  . ARG B 1 246 ? 29.336  -42.300 19.065  1.00 54.83  ? 246  ARG B CD  1 
ATOM   4682  N  NE  . ARG B 1 246 ? 29.257  -42.864 20.404  1.00 77.25  ? 246  ARG B NE  1 
ATOM   4683  C  CZ  . ARG B 1 246 ? 29.188  -42.141 21.518  1.00 91.10  ? 246  ARG B CZ  1 
ATOM   4684  N  NH1 . ARG B 1 246 ? 29.176  -40.814 21.457  1.00 91.91  ? 246  ARG B NH1 1 
ATOM   4685  N  NH2 . ARG B 1 246 ? 29.123  -42.747 22.695  1.00 99.81  ? 246  ARG B NH2 1 
ATOM   4686  N  N   . VAL B 1 247 ? 25.832  -42.954 15.242  1.00 25.30  ? 247  VAL B N   1 
ATOM   4687  C  CA  . VAL B 1 247 ? 24.502  -42.762 14.714  1.00 34.00  ? 247  VAL B CA  1 
ATOM   4688  C  C   . VAL B 1 247 ? 24.219  -43.699 13.540  1.00 31.33  ? 247  VAL B C   1 
ATOM   4689  O  O   . VAL B 1 247 ? 23.186  -44.353 13.497  1.00 42.07  ? 247  VAL B O   1 
ATOM   4690  C  CB  . VAL B 1 247 ? 24.296  -41.311 14.282  1.00 32.12  ? 247  VAL B CB  1 
ATOM   4691  C  CG1 . VAL B 1 247 ? 23.087  -41.211 13.391  1.00 24.40  ? 247  VAL B CG1 1 
ATOM   4692  C  CG2 . VAL B 1 247 ? 24.158  -40.425 15.494  1.00 29.26  ? 247  VAL B CG2 1 
ATOM   4693  N  N   . PHE B 1 248 ? 25.140  -43.762 12.588  1.00 38.10  ? 248  PHE B N   1 
ATOM   4694  C  CA  . PHE B 1 248 ? 24.927  -44.576 11.398  1.00 29.32  ? 248  PHE B CA  1 
ATOM   4695  C  C   . PHE B 1 248 ? 24.749  -46.034 11.744  1.00 35.07  ? 248  PHE B C   1 
ATOM   4696  O  O   . PHE B 1 248 ? 23.951  -46.735 11.106  1.00 29.85  ? 248  PHE B O   1 
ATOM   4697  C  CB  . PHE B 1 248 ? 26.064  -44.399 10.394  1.00 30.00  ? 248  PHE B CB  1 
ATOM   4698  C  CG  . PHE B 1 248 ? 25.787  -43.339 9.374   1.00 37.05  ? 248  PHE B CG  1 
ATOM   4699  C  CD1 . PHE B 1 248 ? 24.797  -43.530 8.425   1.00 42.68  ? 248  PHE B CD1 1 
ATOM   4700  C  CD2 . PHE B 1 248 ? 26.475  -42.142 9.384   1.00 22.61  ? 248  PHE B CD2 1 
ATOM   4701  C  CE1 . PHE B 1 248 ? 24.515  -42.557 7.495   1.00 36.56  ? 248  PHE B CE1 1 
ATOM   4702  C  CE2 . PHE B 1 248 ? 26.190  -41.169 8.453   1.00 26.62  ? 248  PHE B CE2 1 
ATOM   4703  C  CZ  . PHE B 1 248 ? 25.207  -41.380 7.509   1.00 13.95  ? 248  PHE B CZ  1 
ATOM   4704  N  N   . LYS B 1 249 ? 25.482  -46.466 12.773  1.00 34.43  ? 249  LYS B N   1 
ATOM   4705  C  CA  . LYS B 1 249 ? 25.436  -47.842 13.260  1.00 33.08  ? 249  LYS B CA  1 
ATOM   4706  C  C   . LYS B 1 249 ? 24.125  -48.121 13.979  1.00 35.71  ? 249  LYS B C   1 
ATOM   4707  O  O   . LYS B 1 249 ? 23.620  -49.247 13.948  1.00 33.14  ? 249  LYS B O   1 
ATOM   4708  C  CB  . LYS B 1 249 ? 26.632  -48.131 14.176  1.00 31.56  ? 249  LYS B CB  1 
ATOM   4709  C  CG  . LYS B 1 249 ? 27.710  -48.944 13.501  1.00 20.63  ? 249  LYS B CG  1 
ATOM   4710  C  CD  . LYS B 1 249 ? 29.033  -48.945 14.248  1.00 30.66  ? 249  LYS B CD  1 
ATOM   4711  C  CE  . LYS B 1 249 ? 30.076  -49.721 13.437  1.00 39.60  ? 249  LYS B CE  1 
ATOM   4712  N  NZ  . LYS B 1 249 ? 31.490  -49.477 13.835  1.00 54.36  ? 249  LYS B NZ  1 
ATOM   4713  N  N   . GLN B 1 250 ? 23.580  -47.089 14.627  1.00 35.85  ? 250  GLN B N   1 
ATOM   4714  C  CA  . GLN B 1 250 ? 22.251  -47.184 15.223  1.00 35.28  ? 250  GLN B CA  1 
ATOM   4715  C  C   . GLN B 1 250 ? 21.175  -47.270 14.136  1.00 40.55  ? 250  GLN B C   1 
ATOM   4716  O  O   . GLN B 1 250 ? 20.234  -48.072 14.231  1.00 36.92  ? 250  GLN B O   1 
ATOM   4717  C  CB  . GLN B 1 250 ? 21.975  -46.006 16.156  1.00 31.08  ? 250  GLN B CB  1 
ATOM   4718  C  CG  . GLN B 1 250 ? 20.656  -46.138 16.927  1.00 37.09  ? 250  GLN B CG  1 
ATOM   4719  C  CD  . GLN B 1 250 ? 20.569  -45.202 18.117  1.00 39.98  ? 250  GLN B CD  1 
ATOM   4720  O  OE1 . GLN B 1 250 ? 21.529  -45.042 18.857  1.00 57.37  ? 250  GLN B OE1 1 
ATOM   4721  N  NE2 . GLN B 1 250 ? 19.416  -44.581 18.304  1.00 38.08  ? 250  GLN B NE2 1 
ATOM   4722  N  N   . LEU B 1 251 ? 21.321  -46.457 13.093  1.00 30.40  ? 251  LEU B N   1 
ATOM   4723  C  CA  . LEU B 1 251 ? 20.355  -46.472 12.005  1.00 29.64  ? 251  LEU B CA  1 
ATOM   4724  C  C   . LEU B 1 251 ? 20.330  -47.847 11.358  1.00 33.31  ? 251  LEU B C   1 
ATOM   4725  O  O   . LEU B 1 251 ? 19.285  -48.489 11.302  1.00 37.00  ? 251  LEU B O   1 
ATOM   4726  C  CB  . LEU B 1 251 ? 20.671  -45.383 10.986  1.00 40.12  ? 251  LEU B CB  1 
ATOM   4727  C  CG  . LEU B 1 251 ? 20.545  -43.945 11.499  1.00 42.45  ? 251  LEU B CG  1 
ATOM   4728  C  CD1 . LEU B 1 251 ? 21.053  -42.913 10.476  1.00 39.39  ? 251  LEU B CD1 1 
ATOM   4729  C  CD2 . LEU B 1 251 ? 19.120  -43.654 11.905  1.00 34.04  ? 251  LEU B CD2 1 
ATOM   4730  N  N   . ALA B 1 252 ? 21.495  -48.301 10.896  1.00 42.79  ? 252  ALA B N   1 
ATOM   4731  C  CA  . ALA B 1 252 ? 21.615  -49.614 10.253  1.00 42.47  ? 252  ALA B CA  1 
ATOM   4732  C  C   . ALA B 1 252 ? 21.029  -50.716 11.130  1.00 47.80  ? 252  ALA B C   1 
ATOM   4733  O  O   . ALA B 1 252 ? 20.291  -51.581 10.651  1.00 44.28  ? 252  ALA B O   1 
ATOM   4734  C  CB  . ALA B 1 252 ? 23.060  -49.920 9.923   1.00 23.95  ? 252  ALA B CB  1 
ATOM   4735  N  N   . HIS B 1 253 ? 21.363  -50.680 12.416  1.00 37.06  ? 253  HIS B N   1 
ATOM   4736  C  CA  . HIS B 1 253 ? 20.830  -51.653 13.357  1.00 35.96  ? 253  HIS B CA  1 
ATOM   4737  C  C   . HIS B 1 253 ? 19.321  -51.531 13.495  1.00 40.74  ? 253  HIS B C   1 
ATOM   4738  O  O   . HIS B 1 253 ? 18.631  -52.531 13.676  1.00 51.59  ? 253  HIS B O   1 
ATOM   4739  C  CB  . HIS B 1 253 ? 21.502  -51.530 14.729  1.00 31.97  ? 253  HIS B CB  1 
ATOM   4740  C  CG  . HIS B 1 253 ? 22.711  -52.395 14.879  1.00 34.39  ? 253  HIS B CG  1 
ATOM   4741  N  ND1 . HIS B 1 253 ? 23.973  -51.882 15.080  1.00 26.45  ? 253  HIS B ND1 1 
ATOM   4742  C  CD2 . HIS B 1 253 ? 22.854  -53.743 14.830  1.00 41.42  ? 253  HIS B CD2 1 
ATOM   4743  C  CE1 . HIS B 1 253 ? 24.841  -52.876 15.156  1.00 39.93  ? 253  HIS B CE1 1 
ATOM   4744  N  NE2 . HIS B 1 253 ? 24.187  -54.015 15.008  1.00 47.39  ? 253  HIS B NE2 1 
ATOM   4745  N  N   . THR B 1 254 ? 18.798  -50.314 13.408  1.00 31.42  ? 254  THR B N   1 
ATOM   4746  C  CA  . THR B 1 254 ? 17.364  -50.151 13.578  1.00 36.28  ? 254  THR B CA  1 
ATOM   4747  C  C   . THR B 1 254 ? 16.656  -50.968 12.513  1.00 26.70  ? 254  THR B C   1 
ATOM   4748  O  O   . THR B 1 254 ? 15.660  -51.626 12.783  1.00 31.23  ? 254  THR B O   1 
ATOM   4749  C  CB  . THR B 1 254 ? 16.921  -48.686 13.489  1.00 33.65  ? 254  THR B CB  1 
ATOM   4750  O  OG1 . THR B 1 254 ? 17.647  -47.904 14.443  1.00 35.58  ? 254  THR B OG1 1 
ATOM   4751  C  CG2 . THR B 1 254 ? 15.452  -48.571 13.791  1.00 19.97  ? 254  THR B CG2 1 
ATOM   4752  N  N   . TYR B 1 255 ? 17.192  -50.940 11.302  1.00 15.78  ? 255  TYR B N   1 
ATOM   4753  C  CA  . TYR B 1 255 ? 16.562  -51.647 10.209  1.00 24.43  ? 255  TYR B CA  1 
ATOM   4754  C  C   . TYR B 1 255 ? 16.799  -53.162 10.276  1.00 27.63  ? 255  TYR B C   1 
ATOM   4755  O  O   . TYR B 1 255 ? 15.876  -53.963 10.199  1.00 40.18  ? 255  TYR B O   1 
ATOM   4756  C  CB  . TYR B 1 255 ? 17.028  -51.093 8.870   1.00 16.80  ? 255  TYR B CB  1 
ATOM   4757  C  CG  . TYR B 1 255 ? 16.111  -51.503 7.750   1.00 40.01  ? 255  TYR B CG  1 
ATOM   4758  C  CD1 . TYR B 1 255 ? 16.060  -52.833 7.329   1.00 47.67  ? 255  TYR B CD1 1 
ATOM   4759  C  CD2 . TYR B 1 255 ? 15.264  -50.580 7.131   1.00 24.35  ? 255  TYR B CD2 1 
ATOM   4760  C  CE1 . TYR B 1 255 ? 15.209  -53.233 6.320   1.00 41.53  ? 255  TYR B CE1 1 
ATOM   4761  C  CE2 . TYR B 1 255 ? 14.407  -50.975 6.115   1.00 22.49  ? 255  TYR B CE2 1 
ATOM   4762  C  CZ  . TYR B 1 255 ? 14.391  -52.306 5.716   1.00 37.79  ? 255  TYR B CZ  1 
ATOM   4763  O  OH  . TYR B 1 255 ? 13.557  -52.728 4.709   1.00 40.28  ? 255  TYR B OH  1 
ATOM   4764  N  N   . SER B 1 256 ? 18.047  -53.555 10.414  1.00 34.72  ? 256  SER B N   1 
ATOM   4765  C  CA  . SER B 1 256 ? 18.371  -54.962 10.508  1.00 33.93  ? 256  SER B CA  1 
ATOM   4766  C  C   . SER B 1 256 ? 17.680  -55.604 11.714  1.00 48.07  ? 256  SER B C   1 
ATOM   4767  O  O   . SER B 1 256 ? 17.006  -56.621 11.569  1.00 44.06  ? 256  SER B O   1 
ATOM   4768  C  CB  . SER B 1 256 ? 19.884  -55.134 10.613  1.00 28.18  ? 256  SER B CB  1 
ATOM   4769  O  OG  . SER B 1 256 ? 20.252  -56.480 10.414  1.00 54.32  ? 256  SER B OG  1 
ATOM   4770  N  N   . ASP B 1 257 ? 17.854  -55.005 12.897  1.00 50.90  ? 257  ASP B N   1 
ATOM   4771  C  CA  . ASP B 1 257 ? 17.329  -55.552 14.154  1.00 37.12  ? 257  ASP B CA  1 
ATOM   4772  C  C   . ASP B 1 257 ? 15.849  -55.878 14.047  1.00 42.41  ? 257  ASP B C   1 
ATOM   4773  O  O   . ASP B 1 257 ? 15.376  -56.833 14.666  1.00 45.49  ? 257  ASP B O   1 
ATOM   4774  C  CB  . ASP B 1 257 ? 17.543  -54.582 15.320  1.00 33.47  ? 257  ASP B CB  1 
ATOM   4775  C  CG  . ASP B 1 257 ? 18.953  -54.650 15.902  1.00 61.62  ? 257  ASP B CG  1 
ATOM   4776  O  OD1 . ASP B 1 257 ? 19.803  -55.379 15.346  1.00 71.62  ? 257  ASP B OD1 1 
ATOM   4777  O  OD2 . ASP B 1 257 ? 19.216  -53.964 16.920  1.00 66.88  ? 257  ASP B OD2 1 
ATOM   4778  N  N   . ASN B 1 258 ? 15.132  -55.076 13.261  1.00 37.10  ? 258  ASN B N   1 
ATOM   4779  C  CA  . ASN B 1 258 ? 13.698  -55.263 13.032  1.00 47.12  ? 258  ASN B CA  1 
ATOM   4780  C  C   . ASN B 1 258 ? 13.358  -56.131 11.802  1.00 50.85  ? 258  ASN B C   1 
ATOM   4781  O  O   . ASN B 1 258 ? 12.189  -56.294 11.433  1.00 46.28  ? 258  ASN B O   1 
ATOM   4782  C  CB  . ASN B 1 258 ? 12.999  -53.899 12.930  1.00 43.82  ? 258  ASN B CB  1 
ATOM   4783  C  CG  . ASN B 1 258 ? 12.723  -53.270 14.299  1.00 44.81  ? 258  ASN B CG  1 
ATOM   4784  O  OD1 . ASN B 1 258 ? 11.697  -53.542 14.922  1.00 44.01  ? 258  ASN B OD1 1 
ATOM   4785  N  ND2 . ASN B 1 258 ? 13.636  -52.419 14.760  1.00 34.40  ? 258  ASN B ND2 1 
ATOM   4786  N  N   . HIS B 1 259 ? 14.383  -56.690 11.170  1.00 55.03  ? 259  HIS B N   1 
ATOM   4787  C  CA  . HIS B 1 259 ? 14.183  -57.520 9.991   1.00 51.47  ? 259  HIS B CA  1 
ATOM   4788  C  C   . HIS B 1 259 ? 14.613  -58.968 10.252  1.00 54.01  ? 259  HIS B C   1 
ATOM   4789  O  O   . HIS B 1 259 ? 15.809  -59.264 10.355  1.00 52.39  ? 259  HIS B O   1 
ATOM   4790  C  CB  . HIS B 1 259 ? 14.959  -56.935 8.831   1.00 51.05  ? 259  HIS B CB  1 
ATOM   4791  C  CG  . HIS B 1 259 ? 14.641  -57.567 7.519   1.00 52.69  ? 259  HIS B CG  1 
ATOM   4792  N  ND1 . HIS B 1 259 ? 14.708  -58.928 7.315   1.00 46.00  ? 259  HIS B ND1 1 
ATOM   4793  C  CD2 . HIS B 1 259 ? 14.274  -57.022 6.334   1.00 46.05  ? 259  HIS B CD2 1 
ATOM   4794  C  CE1 . HIS B 1 259 ? 14.394  -59.195 6.059   1.00 42.99  ? 259  HIS B CE1 1 
ATOM   4795  N  NE2 . HIS B 1 259 ? 14.128  -58.056 5.442   1.00 39.61  ? 259  HIS B NE2 1 
ATOM   4796  N  N   . PRO B 1 260 ? 13.627  -59.876 10.349  1.00 64.35  ? 260  PRO B N   1 
ATOM   4797  C  CA  . PRO B 1 260 ? 13.759  -61.254 10.845  1.00 60.45  ? 260  PRO B CA  1 
ATOM   4798  C  C   . PRO B 1 260 ? 14.923  -62.011 10.234  1.00 52.03  ? 260  PRO B C   1 
ATOM   4799  O  O   . PRO B 1 260 ? 15.546  -62.846 10.882  1.00 47.88  ? 260  PRO B O   1 
ATOM   4800  C  CB  . PRO B 1 260 ? 12.442  -61.899 10.412  1.00 50.25  ? 260  PRO B CB  1 
ATOM   4801  C  CG  . PRO B 1 260 ? 11.485  -60.780 10.408  1.00 60.05  ? 260  PRO B CG  1 
ATOM   4802  C  CD  . PRO B 1 260 ? 12.257  -59.599 9.887   1.00 59.36  ? 260  PRO B CD  1 
ATOM   4803  N  N   . ILE B 1 261 ? 15.219  -61.703 8.984   1.00 53.39  ? 261  ILE B N   1 
ATOM   4804  C  CA  . ILE B 1 261 ? 16.250  -62.418 8.258   1.00 52.08  ? 261  ILE B CA  1 
ATOM   4805  C  C   . ILE B 1 261 ? 17.567  -61.651 8.222   1.00 42.69  ? 261  ILE B C   1 
ATOM   4806  O  O   . ILE B 1 261 ? 18.629  -62.245 8.352   1.00 46.40  ? 261  ILE B O   1 
ATOM   4807  C  CB  . ILE B 1 261 ? 15.777  -62.710 6.827   1.00 56.91  ? 261  ILE B CB  1 
ATOM   4808  C  CG1 . ILE B 1 261 ? 14.595  -63.687 6.857   1.00 51.83  ? 261  ILE B CG1 1 
ATOM   4809  C  CG2 . ILE B 1 261 ? 16.939  -63.216 5.965   1.00 51.95  ? 261  ILE B CG2 1 
ATOM   4810  C  CD1 . ILE B 1 261 ? 13.919  -63.870 5.520   1.00 58.41  ? 261  ILE B CD1 1 
ATOM   4811  N  N   . MET B 1 262 ? 17.492  -60.331 8.057   1.00 36.15  ? 262  MET B N   1 
ATOM   4812  C  CA  . MET B 1 262 ? 18.688  -59.505 7.929   1.00 41.08  ? 262  MET B CA  1 
ATOM   4813  C  C   . MET B 1 262 ? 19.474  -59.505 9.230   1.00 45.44  ? 262  MET B C   1 
ATOM   4814  O  O   . MET B 1 262 ? 20.707  -59.495 9.229   1.00 37.41  ? 262  MET B O   1 
ATOM   4815  C  CB  . MET B 1 262 ? 18.298  -58.089 7.550   1.00 32.28  ? 262  MET B CB  1 
ATOM   4816  C  CG  . MET B 1 262 ? 19.457  -57.134 7.443   1.00 26.09  ? 262  MET B CG  1 
ATOM   4817  S  SD  . MET B 1 262 ? 18.818  -55.532 6.946   1.00 32.24  ? 262  MET B SD  1 
ATOM   4818  C  CE  . MET B 1 262 ? 18.135  -55.967 5.337   1.00 20.22  ? 262  MET B CE  1 
ATOM   4819  N  N   . ARG B 1 263 ? 18.725  -59.522 10.331  1.00 51.16  ? 263  ARG B N   1 
ATOM   4820  C  CA  . ARG B 1 263 ? 19.248  -59.644 11.692  1.00 47.34  ? 263  ARG B CA  1 
ATOM   4821  C  C   . ARG B 1 263 ? 20.251  -60.795 11.864  1.00 53.48  ? 263  ARG B C   1 
ATOM   4822  O  O   . ARG B 1 263 ? 21.102  -60.772 12.755  1.00 57.56  ? 263  ARG B O   1 
ATOM   4823  C  CB  . ARG B 1 263 ? 18.066  -59.841 12.649  1.00 54.81  ? 263  ARG B CB  1 
ATOM   4824  C  CG  . ARG B 1 263 ? 18.403  -59.788 14.137  1.00 68.39  ? 263  ARG B CG  1 
ATOM   4825  C  CD  . ARG B 1 263 ? 17.136  -59.745 14.991  1.00 75.31  ? 263  ARG B CD  1 
ATOM   4826  N  NE  . ARG B 1 263 ? 16.256  -60.881 14.717  1.00 84.19  ? 263  ARG B NE  1 
ATOM   4827  C  CZ  . ARG B 1 263 ? 14.924  -60.817 14.654  1.00 74.66  ? 263  ARG B CZ  1 
ATOM   4828  N  NH1 . ARG B 1 263 ? 14.289  -59.662 14.842  1.00 58.66  ? 263  ARG B NH1 1 
ATOM   4829  N  NH2 . ARG B 1 263 ? 14.219  -61.913 14.394  1.00 64.12  ? 263  ARG B NH2 1 
ATOM   4830  N  N   . LYS B 1 264 ? 20.148  -61.801 11.003  1.00 68.72  ? 264  LYS B N   1 
ATOM   4831  C  CA  . LYS B 1 264 ? 20.965  -63.011 11.115  1.00 71.46  ? 264  LYS B CA  1 
ATOM   4832  C  C   . LYS B 1 264 ? 22.412  -62.833 10.634  1.00 66.70  ? 264  LYS B C   1 
ATOM   4833  O  O   . LYS B 1 264 ? 23.350  -63.204 11.337  1.00 67.81  ? 264  LYS B O   1 
ATOM   4834  C  CB  . LYS B 1 264 ? 20.285  -64.165 10.380  1.00 69.11  ? 264  LYS B CB  1 
ATOM   4835  C  CG  . LYS B 1 264 ? 18.868  -64.430 10.871  1.00 65.57  ? 264  LYS B CG  1 
ATOM   4836  C  CD  . LYS B 1 264 ? 18.283  -65.666 10.214  1.00 76.88  ? 264  LYS B CD  1 
ATOM   4837  C  CE  . LYS B 1 264 ? 16.989  -66.076 10.888  1.00 81.05  ? 264  LYS B CE  1 
ATOM   4838  N  NZ  . LYS B 1 264 ? 17.216  -66.303 12.337  1.00 91.37  ? 264  LYS B NZ  1 
ATOM   4839  N  N   . GLY B 1 265 ? 22.583  -62.278 9.436   1.00 60.29  ? 265  GLY B N   1 
ATOM   4840  C  CA  . GLY B 1 265 ? 23.896  -61.872 8.964   1.00 49.63  ? 265  GLY B CA  1 
ATOM   4841  C  C   . GLY B 1 265 ? 24.600  -62.896 8.097   1.00 53.36  ? 265  GLY B C   1 
ATOM   4842  O  O   . GLY B 1 265 ? 25.767  -62.716 7.725   1.00 59.69  ? 265  GLY B O   1 
ATOM   4843  N  N   . ASN B 1 266 ? 23.892  -63.974 7.773   1.00 49.81  ? 266  ASN B N   1 
ATOM   4844  C  CA  . ASN B 1 266 ? 24.480  -65.059 6.986   1.00 57.71  ? 266  ASN B CA  1 
ATOM   4845  C  C   . ASN B 1 266 ? 23.715  -65.386 5.697   1.00 54.16  ? 266  ASN B C   1 
ATOM   4846  O  O   . ASN B 1 266 ? 23.642  -66.541 5.279   1.00 63.58  ? 266  ASN B O   1 
ATOM   4847  C  CB  . ASN B 1 266 ? 24.655  -66.314 7.852   1.00 60.18  ? 266  ASN B CB  1 
ATOM   4848  C  CG  . ASN B 1 266 ? 23.381  -66.707 8.583   1.00 69.21  ? 266  ASN B CG  1 
ATOM   4849  O  OD1 . ASN B 1 266 ? 22.356  -66.033 8.480   1.00 72.42  ? 266  ASN B OD1 1 
ATOM   4850  N  ND2 . ASN B 1 266 ? 23.443  -67.810 9.325   1.00 66.73  ? 266  ASN B ND2 1 
ATOM   4851  N  N   . ASN B 1 267 ? 23.173  -64.357 5.060   1.00 38.28  ? 267  ASN B N   1 
ATOM   4852  C  CA  . ASN B 1 267 ? 22.308  -64.528 3.900   1.00 39.79  ? 267  ASN B CA  1 
ATOM   4853  C  C   . ASN B 1 267 ? 23.096  -64.416 2.617   1.00 39.40  ? 267  ASN B C   1 
ATOM   4854  O  O   . ASN B 1 267 ? 24.205  -63.892 2.629   1.00 42.97  ? 267  ASN B O   1 
ATOM   4855  C  CB  . ASN B 1 267 ? 21.200  -63.481 3.920   1.00 49.09  ? 267  ASN B CB  1 
ATOM   4856  C  CG  . ASN B 1 267 ? 20.690  -63.215 5.317   1.00 52.30  ? 267  ASN B CG  1 
ATOM   4857  O  OD1 . ASN B 1 267 ? 20.173  -64.116 5.979   1.00 44.66  ? 267  ASN B OD1 1 
ATOM   4858  N  ND2 . ASN B 1 267 ? 20.852  -61.978 5.785   1.00 52.89  ? 267  ASN B ND2 1 
ATOM   4859  N  N   . CYS B 1 268 ? 22.516  -64.912 1.523   1.00 46.31  ? 268  CYS B N   1 
ATOM   4860  C  CA  . CYS B 1 268 ? 23.151  -64.919 0.197   1.00 55.04  ? 268  CYS B CA  1 
ATOM   4861  C  C   . CYS B 1 268 ? 24.662  -65.207 0.198   1.00 66.41  ? 268  CYS B C   1 
ATOM   4862  O  O   . CYS B 1 268 ? 25.419  -64.572 -0.546  1.00 64.48  ? 268  CYS B O   1 
ATOM   4863  C  CB  . CYS B 1 268 ? 22.886  -63.603 -0.542  1.00 39.48  ? 268  CYS B CB  1 
ATOM   4864  S  SG  . CYS B 1 268 ? 21.717  -62.526 0.292   1.00 65.15  ? 268  CYS B SG  1 
ATOM   4865  N  N   . ASN B 1 269 ? 25.098  -66.158 1.022   1.00 69.57  ? 269  ASN B N   1 
ATOM   4866  C  CA  . ASN B 1 269 ? 26.521  -66.500 1.120   1.00 73.89  ? 269  ASN B CA  1 
ATOM   4867  C  C   . ASN B 1 269 ? 27.383  -65.414 1.776   1.00 66.55  ? 269  ASN B C   1 
ATOM   4868  O  O   . ASN B 1 269 ? 28.603  -65.550 1.840   1.00 53.67  ? 269  ASN B O   1 
ATOM   4869  C  CB  . ASN B 1 269 ? 27.100  -66.866 -0.258  1.00 74.00  ? 269  ASN B CB  1 
ATOM   4870  C  CG  . ASN B 1 269 ? 26.538  -68.167 -0.807  1.00 78.27  ? 269  ASN B CG  1 
ATOM   4871  O  OD1 . ASN B 1 269 ? 26.512  -68.378 -2.018  1.00 73.82  ? 269  ASN B OD1 1 
ATOM   4872  N  ND2 . ASN B 1 269 ? 26.082  -69.043 0.083   1.00 83.31  ? 269  ASN B ND2 1 
ATOM   4873  N  N   . ASP B 1 270 ? 26.747  -64.347 2.259   1.00 58.73  ? 270  ASP B N   1 
ATOM   4874  C  CA  . ASP B 1 270 ? 27.452  -63.245 2.903   1.00 44.23  ? 270  ASP B CA  1 
ATOM   4875  C  C   . ASP B 1 270 ? 27.498  -63.433 4.412   1.00 57.01  ? 270  ASP B C   1 
ATOM   4876  O  O   . ASP B 1 270 ? 26.649  -64.105 4.989   1.00 53.28  ? 270  ASP B O   1 
ATOM   4877  C  CB  . ASP B 1 270 ? 26.767  -61.914 2.594   1.00 50.64  ? 270  ASP B CB  1 
ATOM   4878  C  CG  . ASP B 1 270 ? 26.651  -61.642 1.106   1.00 62.70  ? 270  ASP B CG  1 
ATOM   4879  O  OD1 . ASP B 1 270 ? 27.554  -62.066 0.348   1.00 69.75  ? 270  ASP B OD1 1 
ATOM   4880  O  OD2 . ASP B 1 270 ? 25.653  -60.999 0.696   1.00 62.59  ? 270  ASP B OD2 1 
ATOM   4881  N  N   . SER B 1 271 ? 28.495  -62.823 5.046   1.00 64.67  ? 271  SER B N   1 
ATOM   4882  C  CA  . SER B 1 271 ? 28.605  -62.814 6.500   1.00 53.85  ? 271  SER B CA  1 
ATOM   4883  C  C   . SER B 1 271 ? 28.742  -61.392 7.018   1.00 53.99  ? 271  SER B C   1 
ATOM   4884  O  O   . SER B 1 271 ? 29.827  -60.814 6.993   1.00 62.27  ? 271  SER B O   1 
ATOM   4885  C  CB  . SER B 1 271 ? 29.808  -63.632 6.956   1.00 54.71  ? 271  SER B CB  1 
ATOM   4886  O  OG  . SER B 1 271 ? 29.958  -63.558 8.363   1.00 56.09  ? 271  SER B OG  1 
ATOM   4887  N  N   . PHE B 1 272 ? 27.634  -60.835 7.493   1.00 49.41  ? 272  PHE B N   1 
ATOM   4888  C  CA  . PHE B 1 272 ? 27.615  -59.477 8.018   1.00 35.83  ? 272  PHE B CA  1 
ATOM   4889  C  C   . PHE B 1 272 ? 27.144  -59.495 9.441   1.00 32.88  ? 272  PHE B C   1 
ATOM   4890  O  O   . PHE B 1 272 ? 25.956  -59.667 9.688   1.00 44.11  ? 272  PHE B O   1 
ATOM   4891  C  CB  . PHE B 1 272 ? 26.655  -58.608 7.214   1.00 44.94  ? 272  PHE B CB  1 
ATOM   4892  C  CG  . PHE B 1 272 ? 27.112  -58.340 5.815   1.00 47.64  ? 272  PHE B CG  1 
ATOM   4893  C  CD1 . PHE B 1 272 ? 26.365  -58.772 4.730   1.00 47.43  ? 272  PHE B CD1 1 
ATOM   4894  C  CD2 . PHE B 1 272 ? 28.296  -57.658 5.589   1.00 29.34  ? 272  PHE B CD2 1 
ATOM   4895  C  CE1 . PHE B 1 272 ? 26.788  -58.521 3.446   1.00 41.30  ? 272  PHE B CE1 1 
ATOM   4896  C  CE2 . PHE B 1 272 ? 28.727  -57.404 4.319   1.00 28.77  ? 272  PHE B CE2 1 
ATOM   4897  C  CZ  . PHE B 1 272 ? 27.971  -57.834 3.238   1.00 37.45  ? 272  PHE B CZ  1 
ATOM   4898  N  N   . SER B 1 273 ? 28.073  -59.315 10.376  1.00 47.73  ? 273  SER B N   1 
ATOM   4899  C  CA  . SER B 1 273 ? 27.760  -59.330 11.804  1.00 47.82  ? 273  SER B CA  1 
ATOM   4900  C  C   . SER B 1 273 ? 26.641  -58.355 12.118  1.00 56.80  ? 273  SER B C   1 
ATOM   4901  O  O   . SER B 1 273 ? 26.753  -57.160 11.838  1.00 63.90  ? 273  SER B O   1 
ATOM   4902  C  CB  . SER B 1 273 ? 29.006  -58.984 12.624  1.00 59.29  ? 273  SER B CB  1 
ATOM   4903  O  OG  . SER B 1 273 ? 28.722  -58.860 14.010  1.00 60.34  ? 273  SER B OG  1 
ATOM   4904  N  N   . GLY B 1 274 ? 25.555  -58.870 12.684  1.00 53.55  ? 274  GLY B N   1 
ATOM   4905  C  CA  . GLY B 1 274 ? 24.416  -58.044 13.042  1.00 47.19  ? 274  GLY B CA  1 
ATOM   4906  C  C   . GLY B 1 274 ? 23.550  -57.687 11.849  1.00 54.58  ? 274  GLY B C   1 
ATOM   4907  O  O   . GLY B 1 274 ? 22.549  -56.973 11.989  1.00 54.37  ? 274  GLY B O   1 
ATOM   4908  N  N   . GLY B 1 275 ? 23.936  -58.188 10.676  1.00 50.66  ? 275  GLY B N   1 
ATOM   4909  C  CA  . GLY B 1 275 ? 23.223  -57.914 9.443   1.00 39.02  ? 275  GLY B CA  1 
ATOM   4910  C  C   . GLY B 1 275 ? 23.440  -56.491 8.972   1.00 46.55  ? 275  GLY B C   1 
ATOM   4911  O  O   . GLY B 1 275 ? 22.618  -55.940 8.241   1.00 52.25  ? 275  GLY B O   1 
ATOM   4912  N  N   . ILE B 1 276 ? 24.547  -55.891 9.394   1.00 46.49  ? 276  ILE B N   1 
ATOM   4913  C  CA  . ILE B 1 276 ? 24.925  -54.578 8.894   1.00 49.92  ? 276  ILE B CA  1 
ATOM   4914  C  C   . ILE B 1 276 ? 26.389  -54.570 8.462   1.00 44.51  ? 276  ILE B C   1 
ATOM   4915  O  O   . ILE B 1 276 ? 27.164  -55.458 8.837   1.00 42.90  ? 276  ILE B O   1 
ATOM   4916  C  CB  . ILE B 1 276 ? 24.714  -53.482 9.948   1.00 45.98  ? 276  ILE B CB  1 
ATOM   4917  C  CG1 . ILE B 1 276 ? 25.783  -53.584 11.037  1.00 38.19  ? 276  ILE B CG1 1 
ATOM   4918  C  CG2 . ILE B 1 276 ? 23.312  -53.567 10.528  1.00 42.68  ? 276  ILE B CG2 1 
ATOM   4919  C  CD1 . ILE B 1 276 ? 25.798  -52.412 11.990  1.00 35.71  ? 276  ILE B CD1 1 
ATOM   4920  N  N   . THR B 1 277 ? 26.762  -53.567 7.670   1.00 30.38  ? 277  THR B N   1 
ATOM   4921  C  CA  . THR B 1 277 ? 28.141  -53.436 7.228   1.00 39.94  ? 277  THR B CA  1 
ATOM   4922  C  C   . THR B 1 277 ? 28.491  -52.010 6.823   1.00 47.89  ? 277  THR B C   1 
ATOM   4923  O  O   . THR B 1 277 ? 27.620  -51.201 6.510   1.00 47.97  ? 277  THR B O   1 
ATOM   4924  C  CB  . THR B 1 277 ? 28.489  -54.393 6.058   1.00 27.19  ? 277  THR B CB  1 
ATOM   4925  O  OG1 . THR B 1 277 ? 29.905  -54.391 5.839   1.00 36.77  ? 277  THR B OG1 1 
ATOM   4926  C  CG2 . THR B 1 277 ? 27.816  -53.964 4.778   1.00 14.98  ? 277  THR B CG2 1 
ATOM   4927  N  N   . ASN B 1 278 ? 29.785  -51.719 6.849   1.00 46.45  ? 278  ASN B N   1 
ATOM   4928  C  CA  . ASN B 1 278 ? 30.311  -50.487 6.318   1.00 32.86  ? 278  ASN B CA  1 
ATOM   4929  C  C   . ASN B 1 278 ? 30.465  -50.686 4.825   1.00 42.10  ? 278  ASN B C   1 
ATOM   4930  O  O   . ASN B 1 278 ? 30.962  -51.724 4.382   1.00 46.83  ? 278  ASN B O   1 
ATOM   4931  C  CB  . ASN B 1 278 ? 31.665  -50.184 6.968   1.00 30.33  ? 278  ASN B CB  1 
ATOM   4932  C  CG  . ASN B 1 278 ? 32.335  -48.940 6.400   1.00 43.67  ? 278  ASN B CG  1 
ATOM   4933  O  OD1 . ASN B 1 278 ? 33.518  -48.969 6.033   1.00 44.79  ? 278  ASN B OD1 1 
ATOM   4934  N  ND2 . ASN B 1 278 ? 31.589  -47.838 6.335   1.00 29.36  ? 278  ASN B ND2 1 
ATOM   4935  N  N   . GLY B 1 279 ? 30.017  -49.704 4.048   1.00 32.28  ? 279  GLY B N   1 
ATOM   4936  C  CA  . GLY B 1 279 ? 30.154  -49.766 2.614   1.00 15.39  ? 279  GLY B CA  1 
ATOM   4937  C  C   . GLY B 1 279 ? 31.547  -50.251 2.280   1.00 37.29  ? 279  GLY B C   1 
ATOM   4938  O  O   . GLY B 1 279 ? 31.722  -51.372 1.805   1.00 39.14  ? 279  GLY B O   1 
ATOM   4939  N  N   . ALA B 1 280 ? 32.545  -49.417 2.568   1.00 32.56  ? 280  ALA B N   1 
ATOM   4940  C  CA  . ALA B 1 280 ? 33.915  -49.677 2.145   1.00 29.55  ? 280  ALA B CA  1 
ATOM   4941  C  C   . ALA B 1 280 ? 34.417  -51.045 2.596   1.00 37.08  ? 280  ALA B C   1 
ATOM   4942  O  O   . ALA B 1 280 ? 35.103  -51.733 1.847   1.00 44.18  ? 280  ALA B O   1 
ATOM   4943  C  CB  . ALA B 1 280 ? 34.843  -48.577 2.629   1.00 26.97  ? 280  ALA B CB  1 
ATOM   4944  N  N   . HIS B 1 281 ? 34.067  -51.439 3.815   1.00 35.72  ? 281  HIS B N   1 
ATOM   4945  C  CA  . HIS B 1 281 ? 34.490  -52.733 4.352   1.00 30.78  ? 281  HIS B CA  1 
ATOM   4946  C  C   . HIS B 1 281 ? 33.922  -53.888 3.531   1.00 30.38  ? 281  HIS B C   1 
ATOM   4947  O  O   . HIS B 1 281 ? 34.582  -54.894 3.322   1.00 30.69  ? 281  HIS B O   1 
ATOM   4948  C  CB  . HIS B 1 281 ? 34.094  -52.881 5.834   1.00 42.55  ? 281  HIS B CB  1 
ATOM   4949  C  CG  . HIS B 1 281 ? 34.754  -54.038 6.523   1.00 48.49  ? 281  HIS B CG  1 
ATOM   4950  N  ND1 . HIS B 1 281 ? 34.162  -55.279 6.633   1.00 46.33  ? 281  HIS B ND1 1 
ATOM   4951  C  CD2 . HIS B 1 281 ? 35.966  -54.148 7.119   1.00 52.23  ? 281  HIS B CD2 1 
ATOM   4952  C  CE1 . HIS B 1 281 ? 34.973  -56.099 7.276   1.00 40.95  ? 281  HIS B CE1 1 
ATOM   4953  N  NE2 . HIS B 1 281 ? 36.079  -55.440 7.575   1.00 54.37  ? 281  HIS B NE2 1 
ATOM   4954  N  N   . TRP B 1 282 ? 32.686  -53.759 3.079   1.00 28.58  ? 282  TRP B N   1 
ATOM   4955  C  CA  . TRP B 1 282 ? 32.161  -54.739 2.152   1.00 29.90  ? 282  TRP B CA  1 
ATOM   4956  C  C   . TRP B 1 282 ? 33.056  -54.711 0.921   1.00 43.69  ? 282  TRP B C   1 
ATOM   4957  O  O   . TRP B 1 282 ? 33.861  -55.617 0.696   1.00 48.74  ? 282  TRP B O   1 
ATOM   4958  C  CB  . TRP B 1 282 ? 30.745  -54.364 1.764   1.00 41.76  ? 282  TRP B CB  1 
ATOM   4959  C  CG  . TRP B 1 282 ? 30.092  -55.367 0.906   1.00 50.01  ? 282  TRP B CG  1 
ATOM   4960  C  CD1 . TRP B 1 282 ? 30.637  -56.527 0.439   1.00 43.63  ? 282  TRP B CD1 1 
ATOM   4961  C  CD2 . TRP B 1 282 ? 28.756  -55.318 0.416   1.00 42.95  ? 282  TRP B CD2 1 
ATOM   4962  N  NE1 . TRP B 1 282 ? 29.718  -57.202 -0.320  1.00 41.76  ? 282  TRP B NE1 1 
ATOM   4963  C  CE2 . TRP B 1 282 ? 28.553  -56.480 -0.349  1.00 39.65  ? 282  TRP B CE2 1 
ATOM   4964  C  CE3 . TRP B 1 282 ? 27.710  -54.402 0.548   1.00 43.30  ? 282  TRP B CE3 1 
ATOM   4965  C  CZ2 . TRP B 1 282 ? 27.351  -56.749 -0.985  1.00 34.05  ? 282  TRP B CZ2 1 
ATOM   4966  C  CZ3 . TRP B 1 282 ? 26.518  -54.671 -0.080  1.00 38.72  ? 282  TRP B CZ3 1 
ATOM   4967  C  CH2 . TRP B 1 282 ? 26.347  -55.838 -0.841  1.00 35.52  ? 282  TRP B CH2 1 
ATOM   4968  N  N   . TYR B 1 283 ? 32.903  -53.652 0.130   1.00 41.38  ? 283  TYR B N   1 
ATOM   4969  C  CA  . TYR B 1 283 ? 33.841  -53.306 -0.937  1.00 44.52  ? 283  TYR B CA  1 
ATOM   4970  C  C   . TYR B 1 283 ? 33.662  -51.841 -1.316  1.00 46.59  ? 283  TYR B C   1 
ATOM   4971  O  O   . TYR B 1 283 ? 32.548  -51.322 -1.312  1.00 42.14  ? 283  TYR B O   1 
ATOM   4972  C  CB  . TYR B 1 283 ? 33.636  -54.184 -2.162  1.00 30.51  ? 283  TYR B CB  1 
ATOM   4973  C  CG  . TYR B 1 283 ? 32.238  -54.137 -2.726  1.00 39.67  ? 283  TYR B CG  1 
ATOM   4974  C  CD1 . TYR B 1 283 ? 31.844  -53.124 -3.583  1.00 44.28  ? 283  TYR B CD1 1 
ATOM   4975  C  CD2 . TYR B 1 283 ? 31.314  -55.125 -2.410  1.00 50.34  ? 283  TYR B CD2 1 
ATOM   4976  C  CE1 . TYR B 1 283 ? 30.559  -53.090 -4.106  1.00 45.65  ? 283  TYR B CE1 1 
ATOM   4977  C  CE2 . TYR B 1 283 ? 30.039  -55.105 -2.926  1.00 47.51  ? 283  TYR B CE2 1 
ATOM   4978  C  CZ  . TYR B 1 283 ? 29.663  -54.086 -3.776  1.00 50.80  ? 283  TYR B CZ  1 
ATOM   4979  O  OH  . TYR B 1 283 ? 28.384  -54.071 -4.290  1.00 53.21  ? 283  TYR B OH  1 
ATOM   4980  N  N   . GLU B 1 284 ? 34.760  -51.172 -1.642  1.00 49.73  ? 284  GLU B N   1 
ATOM   4981  C  CA  . GLU B 1 284 ? 34.699  -49.750 -1.956  1.00 47.47  ? 284  GLU B CA  1 
ATOM   4982  C  C   . GLU B 1 284 ? 34.053  -49.470 -3.310  1.00 44.29  ? 284  GLU B C   1 
ATOM   4983  O  O   . GLU B 1 284 ? 34.137  -50.271 -4.246  1.00 46.92  ? 284  GLU B O   1 
ATOM   4984  C  CB  . GLU B 1 284 ? 36.091  -49.113 -1.889  1.00 46.27  ? 284  GLU B CB  1 
ATOM   4985  C  CG  . GLU B 1 284 ? 36.679  -49.034 -0.475  1.00 51.12  ? 284  GLU B CG  1 
ATOM   4986  C  CD  . GLU B 1 284 ? 37.870  -48.078 -0.382  1.00 39.60  ? 284  GLU B CD  1 
ATOM   4987  O  OE1 . GLU B 1 284 ? 38.638  -48.154 0.597   1.00 23.51  ? 284  GLU B OE1 1 
ATOM   4988  O  OE2 . GLU B 1 284 ? 38.032  -47.240 -1.292  1.00 46.61  ? 284  GLU B OE2 1 
ATOM   4989  N  N   . LEU B 1 285 ? 33.389  -48.329 -3.399  1.00 22.35  ? 285  LEU B N   1 
ATOM   4990  C  CA  . LEU B 1 285 ? 32.888  -47.870 -4.674  1.00 32.34  ? 285  LEU B CA  1 
ATOM   4991  C  C   . LEU B 1 285 ? 32.873  -46.366 -4.599  1.00 37.10  ? 285  LEU B C   1 
ATOM   4992  O  O   . LEU B 1 285 ? 32.868  -45.800 -3.505  1.00 32.67  ? 285  LEU B O   1 
ATOM   4993  C  CB  . LEU B 1 285 ? 31.486  -48.418 -4.950  1.00 35.91  ? 285  LEU B CB  1 
ATOM   4994  C  CG  . LEU B 1 285 ? 30.374  -47.991 -3.995  1.00 30.90  ? 285  LEU B CG  1 
ATOM   4995  C  CD1 . LEU B 1 285 ? 29.616  -46.771 -4.505  1.00 23.36  ? 285  LEU B CD1 1 
ATOM   4996  C  CD2 . LEU B 1 285 ? 29.443  -49.151 -3.809  1.00 28.17  ? 285  LEU B CD2 1 
ATOM   4997  N  N   . SER B 1 286 ? 32.873  -45.719 -5.758  1.00 41.98  ? 286  SER B N   1 
ATOM   4998  C  CA  . SER B 1 286 ? 32.898  -44.269 -5.798  1.00 45.66  ? 286  SER B CA  1 
ATOM   4999  C  C   . SER B 1 286 ? 31.750  -43.694 -6.620  1.00 37.47  ? 286  SER B C   1 
ATOM   5000  O  O   . SER B 1 286 ? 31.284  -44.302 -7.578  1.00 42.03  ? 286  SER B O   1 
ATOM   5001  C  CB  . SER B 1 286 ? 34.252  -43.774 -6.310  1.00 39.64  ? 286  SER B CB  1 
ATOM   5002  O  OG  . SER B 1 286 ? 35.305  -44.272 -5.489  1.00 46.15  ? 286  SER B OG  1 
ATOM   5003  N  N   . GLY B 1 287 ? 31.284  -42.520 -6.209  1.00 30.22  ? 287  GLY B N   1 
ATOM   5004  C  CA  . GLY B 1 287 ? 30.267  -41.808 -6.947  1.00 25.35  ? 287  GLY B CA  1 
ATOM   5005  C  C   . GLY B 1 287 ? 28.877  -42.248 -6.561  1.00 28.94  ? 287  GLY B C   1 
ATOM   5006  O  O   . GLY B 1 287 ? 27.911  -42.012 -7.299  1.00 26.70  ? 287  GLY B O   1 
ATOM   5007  N  N   . GLY B 1 288 ? 28.776  -42.880 -5.395  1.00 32.84  ? 288  GLY B N   1 
ATOM   5008  C  CA  . GLY B 1 288 ? 27.497  -43.312 -4.859  1.00 28.64  ? 288  GLY B CA  1 
ATOM   5009  C  C   . GLY B 1 288 ? 26.621  -42.193 -4.322  1.00 28.46  ? 288  GLY B C   1 
ATOM   5010  O  O   . GLY B 1 288 ? 27.098  -41.161 -3.839  1.00 26.60  ? 288  GLY B O   1 
ATOM   5011  N  N   . MET B 1 289 ? 25.315  -42.408 -4.394  1.00 35.65  ? 289  MET B N   1 
ATOM   5012  C  CA  . MET B 1 289 ? 24.350  -41.449 -3.862  1.00 36.93  ? 289  MET B CA  1 
ATOM   5013  C  C   . MET B 1 289 ? 24.466  -41.339 -2.340  1.00 34.06  ? 289  MET B C   1 
ATOM   5014  O  O   . MET B 1 289 ? 24.310  -40.255 -1.779  1.00 34.15  ? 289  MET B O   1 
ATOM   5015  C  CB  . MET B 1 289 ? 22.930  -41.866 -4.263  1.00 25.65  ? 289  MET B CB  1 
ATOM   5016  C  CG  . MET B 1 289 ? 21.851  -40.850 -3.960  1.00 30.43  ? 289  MET B CG  1 
ATOM   5017  S  SD  . MET B 1 289 ? 20.284  -41.268 -4.785  1.00 40.28  ? 289  MET B SD  1 
ATOM   5018  C  CE  . MET B 1 289 ? 19.975  -42.897 -4.116  1.00 30.02  ? 289  MET B CE  1 
ATOM   5019  N  N   . GLN B 1 290 ? 24.747  -42.466 -1.684  1.00 23.32  ? 290  GLN B N   1 
ATOM   5020  C  CA  . GLN B 1 290 ? 24.755  -42.530 -0.237  1.00 16.04  ? 290  GLN B CA  1 
ATOM   5021  C  C   . GLN B 1 290 ? 25.693  -41.479 0.319   1.00 23.01  ? 290  GLN B C   1 
ATOM   5022  O  O   . GLN B 1 290 ? 25.285  -40.577 1.042   1.00 25.35  ? 290  GLN B O   1 
ATOM   5023  C  CB  . GLN B 1 290 ? 25.199  -43.918 0.258   1.00 23.51  ? 290  GLN B CB  1 
ATOM   5024  C  CG  . GLN B 1 290 ? 25.120  -44.095 1.805   1.00 18.21  ? 290  GLN B CG  1 
ATOM   5025  C  CD  . GLN B 1 290 ? 25.890  -45.312 2.320   1.00 33.11  ? 290  GLN B CD  1 
ATOM   5026  O  OE1 . GLN B 1 290 ? 25.291  -46.311 2.711   1.00 43.40  ? 290  GLN B OE1 1 
ATOM   5027  N  NE2 . GLN B 1 290 ? 27.228  -45.227 2.327   1.00 28.96  ? 290  GLN B NE2 1 
ATOM   5028  N  N   . ASP B 1 291 ? 26.967  -41.619 -0.010  1.00 28.36  ? 291  ASP B N   1 
ATOM   5029  C  CA  . ASP B 1 291 ? 27.983  -40.762 0.566   1.00 29.78  ? 291  ASP B CA  1 
ATOM   5030  C  C   . ASP B 1 291 ? 27.777  -39.327 0.098   1.00 35.18  ? 291  ASP B C   1 
ATOM   5031  O  O   . ASP B 1 291 ? 28.163  -38.374 0.783   1.00 33.69  ? 291  ASP B O   1 
ATOM   5032  C  CB  . ASP B 1 291 ? 29.375  -41.278 0.208   1.00 31.67  ? 291  ASP B CB  1 
ATOM   5033  C  CG  . ASP B 1 291 ? 29.738  -42.568 0.948   1.00 49.58  ? 291  ASP B CG  1 
ATOM   5034  O  OD1 . ASP B 1 291 ? 28.871  -43.134 1.657   1.00 45.34  ? 291  ASP B OD1 1 
ATOM   5035  O  OD2 . ASP B 1 291 ? 30.902  -43.017 0.823   1.00 57.83  ? 291  ASP B OD2 1 
ATOM   5036  N  N   . PHE B 1 292 ? 27.147  -39.176 -1.063  1.00 30.25  ? 292  PHE B N   1 
ATOM   5037  C  CA  . PHE B 1 292 ? 26.855  -37.853 -1.585  1.00 14.66  ? 292  PHE B CA  1 
ATOM   5038  C  C   . PHE B 1 292 ? 25.942  -37.054 -0.642  1.00 20.28  ? 292  PHE B C   1 
ATOM   5039  O  O   . PHE B 1 292 ? 26.225  -35.887 -0.346  1.00 25.51  ? 292  PHE B O   1 
ATOM   5040  C  CB  . PHE B 1 292 ? 26.252  -37.924 -2.982  1.00 17.80  ? 292  PHE B CB  1 
ATOM   5041  C  CG  . PHE B 1 292 ? 25.769  -36.599 -3.479  1.00 28.69  ? 292  PHE B CG  1 
ATOM   5042  C  CD1 . PHE B 1 292 ? 26.650  -35.692 -4.037  1.00 24.37  ? 292  PHE B CD1 1 
ATOM   5043  C  CD2 . PHE B 1 292 ? 24.441  -36.241 -3.356  1.00 27.05  ? 292  PHE B CD2 1 
ATOM   5044  C  CE1 . PHE B 1 292 ? 26.222  -34.470 -4.476  1.00 23.27  ? 292  PHE B CE1 1 
ATOM   5045  C  CE2 . PHE B 1 292 ? 24.008  -35.009 -3.801  1.00 28.96  ? 292  PHE B CE2 1 
ATOM   5046  C  CZ  . PHE B 1 292 ? 24.898  -34.128 -4.361  1.00 26.11  ? 292  PHE B CZ  1 
ATOM   5047  N  N   . ASN B 1 293 ? 24.860  -37.680 -0.169  1.00 27.86  ? 293  ASN B N   1 
ATOM   5048  C  CA  . ASN B 1 293 ? 23.976  -37.085 0.864   1.00 35.62  ? 293  ASN B CA  1 
ATOM   5049  C  C   . ASN B 1 293 ? 24.726  -36.535 2.083   1.00 39.54  ? 293  ASN B C   1 
ATOM   5050  O  O   . ASN B 1 293 ? 24.460  -35.425 2.540   1.00 42.03  ? 293  ASN B O   1 
ATOM   5051  C  CB  . ASN B 1 293 ? 22.954  -38.107 1.379   1.00 24.13  ? 293  ASN B CB  1 
ATOM   5052  C  CG  . ASN B 1 293 ? 21.777  -38.290 0.448   1.00 28.33  ? 293  ASN B CG  1 
ATOM   5053  O  OD1 . ASN B 1 293 ? 20.757  -37.635 0.607   1.00 27.95  ? 293  ASN B OD1 1 
ATOM   5054  N  ND2 . ASN B 1 293 ? 21.904  -39.198 -0.518  1.00 26.53  ? 293  ASN B ND2 1 
ATOM   5055  N  N   . TYR B 1 294 ? 25.650  -37.329 2.618   1.00 32.41  ? 294  TYR B N   1 
ATOM   5056  C  CA  . TYR B 1 294 ? 26.341  -36.977 3.850   1.00 41.41  ? 294  TYR B CA  1 
ATOM   5057  C  C   . TYR B 1 294 ? 27.356  -35.883 3.591   1.00 43.22  ? 294  TYR B C   1 
ATOM   5058  O  O   . TYR B 1 294 ? 27.495  -34.940 4.378   1.00 32.20  ? 294  TYR B O   1 
ATOM   5059  C  CB  . TYR B 1 294 ? 27.051  -38.203 4.426   1.00 39.17  ? 294  TYR B CB  1 
ATOM   5060  C  CG  . TYR B 1 294 ? 27.702  -37.963 5.770   1.00 35.89  ? 294  TYR B CG  1 
ATOM   5061  C  CD1 . TYR B 1 294 ? 26.937  -37.692 6.903   1.00 37.14  ? 294  TYR B CD1 1 
ATOM   5062  C  CD2 . TYR B 1 294 ? 29.080  -38.034 5.918   1.00 31.84  ? 294  TYR B CD2 1 
ATOM   5063  C  CE1 . TYR B 1 294 ? 27.530  -37.484 8.146   1.00 33.40  ? 294  TYR B CE1 1 
ATOM   5064  C  CE2 . TYR B 1 294 ? 29.683  -37.826 7.165   1.00 32.84  ? 294  TYR B CE2 1 
ATOM   5065  C  CZ  . TYR B 1 294 ? 28.904  -37.551 8.273   1.00 29.92  ? 294  TYR B CZ  1 
ATOM   5066  O  OH  . TYR B 1 294 ? 29.512  -37.344 9.504   1.00 21.90  ? 294  TYR B OH  1 
ATOM   5067  N  N   . ALA B 1 295 ? 28.060  -36.007 2.471   1.00 36.49  ? 295  ALA B N   1 
ATOM   5068  C  CA  . ALA B 1 295 ? 29.214  -35.161 2.226   1.00 26.65  ? 295  ALA B CA  1 
ATOM   5069  C  C   . ALA B 1 295 ? 28.830  -33.806 1.691   1.00 25.51  ? 295  ALA B C   1 
ATOM   5070  O  O   . ALA B 1 295 ? 29.582  -32.851 1.861   1.00 29.99  ? 295  ALA B O   1 
ATOM   5071  C  CB  . ALA B 1 295 ? 30.173  -35.832 1.281   1.00 23.75  ? 295  ALA B CB  1 
ATOM   5072  N  N   . PHE B 1 296 ? 27.666  -33.729 1.047   1.00 31.09  ? 296  PHE B N   1 
ATOM   5073  C  CA  . PHE B 1 296 ? 27.221  -32.501 0.381   1.00 27.15  ? 296  PHE B CA  1 
ATOM   5074  C  C   . PHE B 1 296 ? 25.900  -31.949 0.930   1.00 33.43  ? 296  PHE B C   1 
ATOM   5075  O  O   . PHE B 1 296 ? 25.320  -31.034 0.348   1.00 32.65  ? 296  PHE B O   1 
ATOM   5076  C  CB  . PHE B 1 296 ? 27.100  -32.727 -1.135  1.00 35.29  ? 296  PHE B CB  1 
ATOM   5077  C  CG  . PHE B 1 296 ? 28.389  -33.117 -1.795  1.00 38.16  ? 296  PHE B CG  1 
ATOM   5078  C  CD1 . PHE B 1 296 ? 28.815  -34.435 -1.796  1.00 44.37  ? 296  PHE B CD1 1 
ATOM   5079  C  CD2 . PHE B 1 296 ? 29.180  -32.168 -2.407  1.00 37.05  ? 296  PHE B CD2 1 
ATOM   5080  C  CE1 . PHE B 1 296 ? 30.010  -34.800 -2.397  1.00 34.30  ? 296  PHE B CE1 1 
ATOM   5081  C  CE2 . PHE B 1 296 ? 30.376  -32.525 -3.007  1.00 42.08  ? 296  PHE B CE2 1 
ATOM   5082  C  CZ  . PHE B 1 296 ? 30.790  -33.841 -3.005  1.00 42.36  ? 296  PHE B CZ  1 
ATOM   5083  N  N   . SER B 1 297 ? 25.429  -32.509 2.042   1.00 37.16  ? 297  SER B N   1 
ATOM   5084  C  CA  . SER B 1 297 ? 24.198  -32.052 2.672   1.00 16.05  ? 297  SER B CA  1 
ATOM   5085  C  C   . SER B 1 297 ? 24.177  -32.490 4.125   1.00 25.13  ? 297  SER B C   1 
ATOM   5086  O  O   . SER B 1 297 ? 25.171  -33.017 4.628   1.00 39.64  ? 297  SER B O   1 
ATOM   5087  C  CB  . SER B 1 297 ? 22.980  -32.622 1.946   1.00 23.78  ? 297  SER B CB  1 
ATOM   5088  O  OG  . SER B 1 297 ? 22.635  -33.907 2.440   1.00 25.82  ? 297  SER B OG  1 
ATOM   5089  N  N   . ASN B 1 298 ? 23.047  -32.260 4.796   1.00 32.64  ? 298  ASN B N   1 
ATOM   5090  C  CA  . ASN B 1 298 ? 22.858  -32.673 6.192   1.00 28.40  ? 298  ASN B CA  1 
ATOM   5091  C  C   . ASN B 1 298 ? 22.373  -34.093 6.266   1.00 24.70  ? 298  ASN B C   1 
ATOM   5092  O  O   . ASN B 1 298 ? 22.392  -34.713 7.320   1.00 33.93  ? 298  ASN B O   1 
ATOM   5093  C  CB  . ASN B 1 298 ? 21.801  -31.806 6.875   1.00 17.95  ? 298  ASN B CB  1 
ATOM   5094  C  CG  . ASN B 1 298 ? 22.256  -30.385 7.077   1.00 26.21  ? 298  ASN B CG  1 
ATOM   5095  O  OD1 . ASN B 1 298 ? 23.465  -30.092 7.087   1.00 30.61  ? 298  ASN B OD1 1 
ATOM   5096  N  ND2 . ASN B 1 298 ? 21.292  -29.482 7.248   1.00 25.84  ? 298  ASN B ND2 1 
ATOM   5097  N  N   . CYS B 1 299 ? 21.908  -34.597 5.135   1.00 14.71  ? 299  CYS B N   1 
ATOM   5098  C  CA  . CYS B 1 299 ? 21.171  -35.847 5.125   1.00 19.54  ? 299  CYS B CA  1 
ATOM   5099  C  C   . CYS B 1 299 ? 22.015  -37.074 5.472   1.00 24.09  ? 299  CYS B C   1 
ATOM   5100  O  O   . CYS B 1 299 ? 23.161  -37.198 5.032   1.00 42.00  ? 299  CYS B O   1 
ATOM   5101  C  CB  . CYS B 1 299 ? 20.521  -36.025 3.774   1.00 6.70   ? 299  CYS B CB  1 
ATOM   5102  S  SG  . CYS B 1 299 ? 19.314  -37.280 3.784   1.00 30.67  ? 299  CYS B SG  1 
ATOM   5103  N  N   . PHE B 1 300 ? 21.446  -37.978 6.260   1.00 21.18  ? 300  PHE B N   1 
ATOM   5104  C  CA  . PHE B 1 300 ? 22.117  -39.235 6.609   1.00 31.34  ? 300  PHE B CA  1 
ATOM   5105  C  C   . PHE B 1 300 ? 21.440  -40.388 5.868   1.00 24.19  ? 300  PHE B C   1 
ATOM   5106  O  O   . PHE B 1 300 ? 20.440  -40.903 6.344   1.00 23.40  ? 300  PHE B O   1 
ATOM   5107  C  CB  . PHE B 1 300 ? 22.048  -39.526 8.129   1.00 38.01  ? 300  PHE B CB  1 
ATOM   5108  C  CG  . PHE B 1 300 ? 22.903  -38.617 8.992   1.00 41.23  ? 300  PHE B CG  1 
ATOM   5109  C  CD1 . PHE B 1 300 ? 23.303  -39.031 10.261  1.00 33.02  ? 300  PHE B CD1 1 
ATOM   5110  C  CD2 . PHE B 1 300 ? 23.288  -37.354 8.552   1.00 47.55  ? 300  PHE B CD2 1 
ATOM   5111  C  CE1 . PHE B 1 300 ? 24.076  -38.206 11.074  1.00 26.09  ? 300  PHE B CE1 1 
ATOM   5112  C  CE2 . PHE B 1 300 ? 24.057  -36.518 9.358   1.00 43.11  ? 300  PHE B CE2 1 
ATOM   5113  C  CZ  . PHE B 1 300 ? 24.448  -36.945 10.623  1.00 38.29  ? 300  PHE B CZ  1 
ATOM   5114  N  N   . GLU B 1 301 ? 21.989  -40.798 4.728   1.00 23.59  ? 301  GLU B N   1 
ATOM   5115  C  CA  . GLU B 1 301 ? 21.416  -41.886 3.932   1.00 17.45  ? 301  GLU B CA  1 
ATOM   5116  C  C   . GLU B 1 301 ? 22.067  -43.253 4.179   1.00 26.33  ? 301  GLU B C   1 
ATOM   5117  O  O   . GLU B 1 301 ? 23.286  -43.392 4.117   1.00 38.28  ? 301  GLU B O   1 
ATOM   5118  C  CB  . GLU B 1 301 ? 21.521  -41.552 2.438   1.00 26.57  ? 301  GLU B CB  1 
ATOM   5119  C  CG  . GLU B 1 301 ? 21.128  -42.688 1.497   1.00 23.08  ? 301  GLU B CG  1 
ATOM   5120  C  CD  . GLU B 1 301 ? 20.768  -42.191 0.110   1.00 32.19  ? 301  GLU B CD  1 
ATOM   5121  O  OE1 . GLU B 1 301 ? 19.816  -41.391 -0.013  1.00 42.48  ? 301  GLU B OE1 1 
ATOM   5122  O  OE2 . GLU B 1 301 ? 21.433  -42.599 -0.863  1.00 36.35  ? 301  GLU B OE2 1 
ATOM   5123  N  N   . LEU B 1 302 ? 21.250  -44.264 4.439   1.00 29.76  ? 302  LEU B N   1 
ATOM   5124  C  CA  . LEU B 1 302 ? 21.744  -45.627 4.493   1.00 35.81  ? 302  LEU B CA  1 
ATOM   5125  C  C   . LEU B 1 302 ? 21.561  -46.261 3.137   1.00 32.88  ? 302  LEU B C   1 
ATOM   5126  O  O   . LEU B 1 302 ? 20.731  -45.836 2.341   1.00 31.61  ? 302  LEU B O   1 
ATOM   5127  C  CB  . LEU B 1 302 ? 20.967  -46.448 5.520   1.00 35.60  ? 302  LEU B CB  1 
ATOM   5128  C  CG  . LEU B 1 302 ? 21.135  -46.132 7.009   1.00 38.85  ? 302  LEU B CG  1 
ATOM   5129  C  CD1 . LEU B 1 302 ? 20.325  -47.123 7.842   1.00 32.66  ? 302  LEU B CD1 1 
ATOM   5130  C  CD2 . LEU B 1 302 ? 22.612  -46.137 7.418   1.00 32.76  ? 302  LEU B CD2 1 
ATOM   5131  N  N   . THR B 1 303 ? 22.350  -47.288 2.878   1.00 39.03  ? 303  THR B N   1 
ATOM   5132  C  CA  . THR B 1 303 ? 22.101  -48.161 1.746   1.00 49.09  ? 303  THR B CA  1 
ATOM   5133  C  C   . THR B 1 303 ? 21.551  -49.466 2.299   1.00 47.57  ? 303  THR B C   1 
ATOM   5134  O  O   . THR B 1 303 ? 22.165  -50.085 3.176   1.00 36.16  ? 303  THR B O   1 
ATOM   5135  C  CB  . THR B 1 303 ? 23.386  -48.446 0.955   1.00 47.40  ? 303  THR B CB  1 
ATOM   5136  O  OG1 . THR B 1 303 ? 24.063  -47.212 0.690   1.00 46.49  ? 303  THR B OG1 1 
ATOM   5137  C  CG2 . THR B 1 303 ? 23.055  -49.149 -0.360  1.00 40.14  ? 303  THR B CG2 1 
ATOM   5138  N  N   . ILE B 1 304 ? 20.396  -49.880 1.791   1.00 48.88  ? 304  ILE B N   1 
ATOM   5139  C  CA  . ILE B 1 304 ? 19.765  -51.099 2.274   1.00 46.35  ? 304  ILE B CA  1 
ATOM   5140  C  C   . ILE B 1 304 ? 19.488  -52.119 1.179   1.00 47.13  ? 304  ILE B C   1 
ATOM   5141  O  O   . ILE B 1 304 ? 18.780  -51.825 0.197   1.00 26.35  ? 304  ILE B O   1 
ATOM   5142  C  CB  . ILE B 1 304 ? 18.481  -50.787 3.027   1.00 38.96  ? 304  ILE B CB  1 
ATOM   5143  C  CG1 . ILE B 1 304 ? 18.816  -49.891 4.206   1.00 27.77  ? 304  ILE B CG1 1 
ATOM   5144  C  CG2 . ILE B 1 304 ? 17.802  -52.077 3.498   1.00 42.55  ? 304  ILE B CG2 1 
ATOM   5145  C  CD1 . ILE B 1 304 ? 17.605  -49.363 4.891   1.00 56.93  ? 304  ILE B CD1 1 
ATOM   5146  N  N   . GLU B 1 305 ? 20.069  -53.307 1.383   1.00 38.43  ? 305  GLU B N   1 
ATOM   5147  C  CA  . GLU B 1 305 ? 19.934  -54.466 0.506   1.00 31.95  ? 305  GLU B CA  1 
ATOM   5148  C  C   . GLU B 1 305 ? 18.798  -55.348 1.003   1.00 43.79  ? 305  GLU B C   1 
ATOM   5149  O  O   . GLU B 1 305 ? 18.811  -55.803 2.153   1.00 47.72  ? 305  GLU B O   1 
ATOM   5150  C  CB  . GLU B 1 305 ? 21.228  -55.261 0.508   1.00 21.44  ? 305  GLU B CB  1 
ATOM   5151  C  CG  . GLU B 1 305 ? 22.409  -54.470 0.035   1.00 24.29  ? 305  GLU B CG  1 
ATOM   5152  C  CD  . GLU B 1 305 ? 22.435  -54.331 -1.474  1.00 39.96  ? 305  GLU B CD  1 
ATOM   5153  O  OE1 . GLU B 1 305 ? 23.335  -53.631 -1.998  1.00 40.10  ? 305  GLU B OE1 1 
ATOM   5154  O  OE2 . GLU B 1 305 ? 21.555  -54.930 -2.134  1.00 41.13  ? 305  GLU B OE2 1 
ATOM   5155  N  N   . LEU B 1 306 ? 17.818  -55.588 0.136   1.00 40.35  ? 306  LEU B N   1 
ATOM   5156  C  CA  . LEU B 1 306 ? 16.581  -56.225 0.568   1.00 43.31  ? 306  LEU B CA  1 
ATOM   5157  C  C   . LEU B 1 306 ? 16.534  -57.733 0.322   1.00 43.14  ? 306  LEU B C   1 
ATOM   5158  O  O   . LEU B 1 306 ? 16.146  -58.496 1.195   1.00 51.11  ? 306  LEU B O   1 
ATOM   5159  C  CB  . LEU B 1 306 ? 15.379  -55.530 -0.073  1.00 45.73  ? 306  LEU B CB  1 
ATOM   5160  C  CG  . LEU B 1 306 ? 15.217  -54.071 0.367   1.00 49.01  ? 306  LEU B CG  1 
ATOM   5161  C  CD1 . LEU B 1 306 ? 14.172  -53.369 -0.480  1.00 43.77  ? 306  LEU B CD1 1 
ATOM   5162  C  CD2 . LEU B 1 306 ? 14.865  -53.977 1.854   1.00 39.09  ? 306  LEU B CD2 1 
ATOM   5163  N  N   . SER B 1 307 ? 16.942  -58.167 -0.856  1.00 45.24  ? 307  SER B N   1 
ATOM   5164  C  CA  . SER B 1 307 ? 16.786  -59.565 -1.204  1.00 40.12  ? 307  SER B CA  1 
ATOM   5165  C  C   . SER B 1 307 ? 18.054  -60.162 -1.792  1.00 42.79  ? 307  SER B C   1 
ATOM   5166  O  O   . SER B 1 307 ? 18.877  -59.457 -2.374  1.00 43.04  ? 307  SER B O   1 
ATOM   5167  C  CB  . SER B 1 307 ? 15.633  -59.718 -2.197  1.00 48.12  ? 307  SER B CB  1 
ATOM   5168  O  OG  . SER B 1 307 ? 15.757  -58.787 -3.264  1.00 49.32  ? 307  SER B OG  1 
ATOM   5169  N  N   . CYS B 1 308 ? 18.204  -61.472 -1.638  1.00 51.83  ? 308  CYS B N   1 
ATOM   5170  C  CA  . CYS B 1 308 ? 19.284  -62.174 -2.304  1.00 51.45  ? 308  CYS B CA  1 
ATOM   5171  C  C   . CYS B 1 308 ? 19.004  -62.147 -3.795  1.00 56.50  ? 308  CYS B C   1 
ATOM   5172  O  O   . CYS B 1 308 ? 19.917  -61.955 -4.604  1.00 61.17  ? 308  CYS B O   1 
ATOM   5173  C  CB  . CYS B 1 308 ? 19.396  -63.614 -1.808  1.00 41.44  ? 308  CYS B CB  1 
ATOM   5174  S  SG  . CYS B 1 308 ? 20.180  -63.782 -0.186  1.00 54.13  ? 308  CYS B SG  1 
ATOM   5175  N  N   . CYS B 1 309 ? 17.735  -62.329 -4.156  1.00 45.48  ? 309  CYS B N   1 
ATOM   5176  C  CA  . CYS B 1 309 ? 17.324  -62.240 -5.554  1.00 39.60  ? 309  CYS B CA  1 
ATOM   5177  C  C   . CYS B 1 309 ? 16.994  -60.795 -5.931  1.00 51.86  ? 309  CYS B C   1 
ATOM   5178  O  O   . CYS B 1 309 ? 16.132  -60.148 -5.317  1.00 35.92  ? 309  CYS B O   1 
ATOM   5179  C  CB  . CYS B 1 309 ? 16.122  -63.139 -5.812  1.00 41.72  ? 309  CYS B CB  1 
ATOM   5180  S  SG  . CYS B 1 309 ? 15.503  -63.047 -7.477  1.00 53.24  ? 309  CYS B SG  1 
ATOM   5181  N  N   . LYS B 1 310 ? 17.692  -60.295 -6.945  1.00 55.76  ? 310  LYS B N   1 
ATOM   5182  C  CA  . LYS B 1 310 ? 17.545  -58.910 -7.376  1.00 52.38  ? 310  LYS B CA  1 
ATOM   5183  C  C   . LYS B 1 310 ? 16.114  -58.610 -7.805  1.00 58.78  ? 310  LYS B C   1 
ATOM   5184  O  O   . LYS B 1 310 ? 15.504  -57.629 -7.357  1.00 54.69  ? 310  LYS B O   1 
ATOM   5185  C  CB  . LYS B 1 310 ? 18.526  -58.603 -8.515  1.00 53.96  ? 310  LYS B CB  1 
ATOM   5186  C  CG  . LYS B 1 310 ? 19.987  -58.518 -8.056  1.00 50.40  ? 310  LYS B CG  1 
ATOM   5187  C  CD  . LYS B 1 310 ? 20.945  -58.138 -9.184  1.00 45.77  ? 310  LYS B CD  1 
ATOM   5188  C  CE  . LYS B 1 310 ? 22.275  -57.626 -8.616  1.00 52.48  ? 310  LYS B CE  1 
ATOM   5189  N  NZ  . LYS B 1 310 ? 23.163  -56.982 -9.630  1.00 58.65  ? 310  LYS B NZ  1 
ATOM   5190  N  N   . TYR B 1 311 ? 15.582  -59.472 -8.666  1.00 54.51  ? 311  TYR B N   1 
ATOM   5191  C  CA  . TYR B 1 311 ? 14.260  -59.278 -9.236  1.00 46.00  ? 311  TYR B CA  1 
ATOM   5192  C  C   . TYR B 1 311 ? 13.450  -60.536 -9.021  1.00 46.88  ? 311  TYR B C   1 
ATOM   5193  O  O   . TYR B 1 311 ? 13.324  -61.360 -9.924  1.00 48.32  ? 311  TYR B O   1 
ATOM   5194  C  CB  . TYR B 1 311 ? 14.392  -59.019 -10.733 1.00 47.75  ? 311  TYR B CB  1 
ATOM   5195  C  CG  . TYR B 1 311 ? 13.227  -58.304 -11.379 1.00 42.15  ? 311  TYR B CG  1 
ATOM   5196  C  CD1 . TYR B 1 311 ? 13.424  -57.514 -12.510 1.00 36.72  ? 311  TYR B CD1 1 
ATOM   5197  C  CD2 . TYR B 1 311 ? 11.933  -58.414 -10.873 1.00 47.29  ? 311  TYR B CD2 1 
ATOM   5198  C  CE1 . TYR B 1 311 ? 12.375  -56.851 -13.123 1.00 41.25  ? 311  TYR B CE1 1 
ATOM   5199  C  CE2 . TYR B 1 311 ? 10.869  -57.747 -11.483 1.00 45.36  ? 311  TYR B CE2 1 
ATOM   5200  C  CZ  . TYR B 1 311 ? 11.106  -56.970 -12.613 1.00 44.42  ? 311  TYR B CZ  1 
ATOM   5201  O  OH  . TYR B 1 311 ? 10.089  -56.301 -13.248 1.00 41.95  ? 311  TYR B OH  1 
ATOM   5202  N  N   . PRO B 1 312 ? 12.904  -60.699 -7.812  1.00 52.37  ? 312  PRO B N   1 
ATOM   5203  C  CA  . PRO B 1 312 ? 12.050  -61.849 -7.493  1.00 52.66  ? 312  PRO B CA  1 
ATOM   5204  C  C   . PRO B 1 312 ? 10.688  -61.776 -8.199  1.00 66.30  ? 312  PRO B C   1 
ATOM   5205  O  O   . PRO B 1 312 ? 10.416  -60.825 -8.937  1.00 71.19  ? 312  PRO B O   1 
ATOM   5206  C  CB  . PRO B 1 312 ? 11.871  -61.753 -5.966  1.00 37.59  ? 312  PRO B CB  1 
ATOM   5207  C  CG  . PRO B 1 312 ? 12.875  -60.740 -5.496  1.00 51.02  ? 312  PRO B CG  1 
ATOM   5208  C  CD  . PRO B 1 312 ? 13.106  -59.818 -6.653  1.00 57.44  ? 312  PRO B CD  1 
ATOM   5209  N  N   . ALA B 1 313 ? 9.844   -62.779 -7.976  1.00 64.26  ? 313  ALA B N   1 
ATOM   5210  C  CA  . ALA B 1 313 ? 8.517   -62.795 -8.578  1.00 64.25  ? 313  ALA B CA  1 
ATOM   5211  C  C   . ALA B 1 313 ? 7.488   -62.159 -7.651  1.00 51.95  ? 313  ALA B C   1 
ATOM   5212  O  O   . ALA B 1 313 ? 7.682   -62.096 -6.440  1.00 55.88  ? 313  ALA B O   1 
ATOM   5213  C  CB  . ALA B 1 313 ? 8.110   -64.219 -8.934  1.00 62.99  ? 313  ALA B CB  1 
ATOM   5214  N  N   . ALA B 1 314 ? 6.388   -61.702 -8.231  1.00 38.89  ? 314  ALA B N   1 
ATOM   5215  C  CA  . ALA B 1 314 ? 5.339   -61.031 -7.479  1.00 43.99  ? 314  ALA B CA  1 
ATOM   5216  C  C   . ALA B 1 314 ? 4.935   -61.727 -6.176  1.00 54.54  ? 314  ALA B C   1 
ATOM   5217  O  O   . ALA B 1 314 ? 4.922   -61.094 -5.125  1.00 63.31  ? 314  ALA B O   1 
ATOM   5218  C  CB  . ALA B 1 314 ? 4.125   -60.820 -8.357  1.00 49.43  ? 314  ALA B CB  1 
ATOM   5219  N  N   . SER B 1 315 ? 4.598   -63.015 -6.242  1.00 48.06  ? 315  SER B N   1 
ATOM   5220  C  CA  . SER B 1 315 ? 4.124   -63.760 -5.065  1.00 46.88  ? 315  SER B CA  1 
ATOM   5221  C  C   . SER B 1 315 ? 5.029   -63.574 -3.826  1.00 52.49  ? 315  SER B C   1 
ATOM   5222  O  O   . SER B 1 315 ? 4.587   -63.718 -2.668  1.00 43.57  ? 315  SER B O   1 
ATOM   5223  C  CB  . SER B 1 315 ? 3.945   -65.252 -5.402  1.00 45.14  ? 315  SER B CB  1 
ATOM   5224  O  OG  . SER B 1 315 ? 5.165   -65.861 -5.779  1.00 53.23  ? 315  SER B OG  1 
ATOM   5225  N  N   . THR B 1 316 ? 6.293   -63.243 -4.089  1.00 44.07  ? 316  THR B N   1 
ATOM   5226  C  CA  . THR B 1 316 ? 7.279   -62.982 -3.049  1.00 36.55  ? 316  THR B CA  1 
ATOM   5227  C  C   . THR B 1 316 ? 6.954   -61.703 -2.291  1.00 42.37  ? 316  THR B C   1 
ATOM   5228  O  O   . THR B 1 316 ? 7.115   -61.614 -1.073  1.00 48.45  ? 316  THR B O   1 
ATOM   5229  C  CB  . THR B 1 316 ? 8.680   -62.865 -3.684  1.00 44.26  ? 316  THR B CB  1 
ATOM   5230  O  OG1 . THR B 1 316 ? 9.234   -64.177 -3.865  1.00 49.12  ? 316  THR B OG1 1 
ATOM   5231  C  CG2 . THR B 1 316 ? 9.615   -62.038 -2.823  1.00 52.17  ? 316  THR B CG2 1 
ATOM   5232  N  N   . LEU B 1 317 ? 6.467   -60.717 -3.028  1.00 41.61  ? 317  LEU B N   1 
ATOM   5233  C  CA  . LEU B 1 317 ? 6.302   -59.363 -2.508  1.00 44.80  ? 317  LEU B CA  1 
ATOM   5234  C  C   . LEU B 1 317 ? 5.587   -59.285 -1.161  1.00 39.56  ? 317  LEU B C   1 
ATOM   5235  O  O   . LEU B 1 317 ? 6.062   -58.595 -0.261  1.00 35.47  ? 317  LEU B O   1 
ATOM   5236  C  CB  . LEU B 1 317 ? 5.604   -58.462 -3.540  1.00 40.86  ? 317  LEU B CB  1 
ATOM   5237  C  CG  . LEU B 1 317 ? 6.214   -58.390 -4.945  1.00 43.32  ? 317  LEU B CG  1 
ATOM   5238  C  CD1 . LEU B 1 317 ? 5.242   -57.732 -5.918  1.00 56.06  ? 317  LEU B CD1 1 
ATOM   5239  C  CD2 . LEU B 1 317 ? 7.542   -57.661 -4.919  1.00 30.51  ? 317  LEU B CD2 1 
ATOM   5240  N  N   . PRO B 1 318 ? 4.433   -59.968 -1.020  1.00 44.10  ? 318  PRO B N   1 
ATOM   5241  C  CA  . PRO B 1 318 ? 3.693   -59.820 0.245   1.00 47.14  ? 318  PRO B CA  1 
ATOM   5242  C  C   . PRO B 1 318 ? 4.503   -60.260 1.479   1.00 54.51  ? 318  PRO B C   1 
ATOM   5243  O  O   . PRO B 1 318 ? 4.390   -59.624 2.522   1.00 47.45  ? 318  PRO B O   1 
ATOM   5244  C  CB  . PRO B 1 318 ? 2.453   -60.699 0.035   1.00 40.81  ? 318  PRO B CB  1 
ATOM   5245  C  CG  . PRO B 1 318 ? 2.251   -60.721 -1.447  1.00 40.36  ? 318  PRO B CG  1 
ATOM   5246  C  CD  . PRO B 1 318 ? 3.665   -60.744 -2.013  1.00 49.18  ? 318  PRO B CD  1 
ATOM   5247  N  N   . GLN B 1 319 ? 5.304   -61.317 1.361   1.00 51.12  ? 319  GLN B N   1 
ATOM   5248  C  CA  . GLN B 1 319 ? 6.236   -61.693 2.419   1.00 45.61  ? 319  GLN B CA  1 
ATOM   5249  C  C   . GLN B 1 319 ? 7.241   -60.580 2.676   1.00 37.10  ? 319  GLN B C   1 
ATOM   5250  O  O   . GLN B 1 319 ? 7.501   -60.202 3.820   1.00 38.27  ? 319  GLN B O   1 
ATOM   5251  C  CB  . GLN B 1 319 ? 7.014   -62.947 2.027   1.00 64.30  ? 319  GLN B CB  1 
ATOM   5252  C  CG  . GLN B 1 319 ? 6.423   -64.238 2.519   1.00 79.45  ? 319  GLN B CG  1 
ATOM   5253  C  CD  . GLN B 1 319 ? 5.903   -65.087 1.381   1.00 98.68  ? 319  GLN B CD  1 
ATOM   5254  O  OE1 . GLN B 1 319 ? 5.922   -66.321 1.449   1.00 109.63 ? 319  GLN B OE1 1 
ATOM   5255  N  NE2 . GLN B 1 319 ? 5.437   -64.431 0.320   1.00 92.06  ? 319  GLN B NE2 1 
ATOM   5256  N  N   . GLU B 1 320 ? 7.827   -60.068 1.603   1.00 41.91  ? 320  GLU B N   1 
ATOM   5257  C  CA  . GLU B 1 320 ? 8.819   -59.005 1.734   1.00 50.08  ? 320  GLU B CA  1 
ATOM   5258  C  C   . GLU B 1 320 ? 8.232   -57.817 2.492   1.00 39.95  ? 320  GLU B C   1 
ATOM   5259  O  O   . GLU B 1 320 ? 8.870   -57.259 3.391   1.00 50.32  ? 320  GLU B O   1 
ATOM   5260  C  CB  . GLU B 1 320 ? 9.346   -58.563 0.362   1.00 53.01  ? 320  GLU B CB  1 
ATOM   5261  C  CG  . GLU B 1 320 ? 10.010  -59.675 -0.472  1.00 58.52  ? 320  GLU B CG  1 
ATOM   5262  C  CD  . GLU B 1 320 ? 11.340  -60.164 0.096   1.00 62.09  ? 320  GLU B CD  1 
ATOM   5263  O  OE1 . GLU B 1 320 ? 11.720  -59.729 1.201   1.00 53.39  ? 320  GLU B OE1 1 
ATOM   5264  O  OE2 . GLU B 1 320 ? 12.011  -60.990 -0.567  1.00 68.45  ? 320  GLU B OE2 1 
ATOM   5265  N  N   . TRP B 1 321 ? 7.012   -57.438 2.136   1.00 28.83  ? 321  TRP B N   1 
ATOM   5266  C  CA  . TRP B 1 321 ? 6.311   -56.408 2.886   1.00 42.90  ? 321  TRP B CA  1 
ATOM   5267  C  C   . TRP B 1 321 ? 6.314   -56.667 4.407   1.00 48.83  ? 321  TRP B C   1 
ATOM   5268  O  O   . TRP B 1 321 ? 6.728   -55.811 5.186   1.00 39.35  ? 321  TRP B O   1 
ATOM   5269  C  CB  . TRP B 1 321 ? 4.877   -56.232 2.365   1.00 44.76  ? 321  TRP B CB  1 
ATOM   5270  C  CG  . TRP B 1 321 ? 4.046   -55.378 3.268   1.00 51.93  ? 321  TRP B CG  1 
ATOM   5271  C  CD1 . TRP B 1 321 ? 3.005   -55.782 4.048   1.00 43.17  ? 321  TRP B CD1 1 
ATOM   5272  C  CD2 . TRP B 1 321 ? 4.218   -53.978 3.516   1.00 55.89  ? 321  TRP B CD2 1 
ATOM   5273  N  NE1 . TRP B 1 321 ? 2.511   -54.718 4.755   1.00 49.08  ? 321  TRP B NE1 1 
ATOM   5274  C  CE2 . TRP B 1 321 ? 3.238   -53.598 4.446   1.00 47.93  ? 321  TRP B CE2 1 
ATOM   5275  C  CE3 . TRP B 1 321 ? 5.105   -53.008 3.036   1.00 53.98  ? 321  TRP B CE3 1 
ATOM   5276  C  CZ2 . TRP B 1 321 ? 3.115   -52.289 4.909   1.00 42.16  ? 321  TRP B CZ2 1 
ATOM   5277  C  CZ3 . TRP B 1 321 ? 4.982   -51.709 3.491   1.00 45.02  ? 321  TRP B CZ3 1 
ATOM   5278  C  CH2 . TRP B 1 321 ? 3.991   -51.361 4.421   1.00 39.93  ? 321  TRP B CH2 1 
ATOM   5279  N  N   . GLN B 1 322 ? 5.859   -57.847 4.820   1.00 53.66  ? 322  GLN B N   1 
ATOM   5280  C  CA  . GLN B 1 322 ? 5.685   -58.139 6.237   1.00 57.06  ? 322  GLN B CA  1 
ATOM   5281  C  C   . GLN B 1 322 ? 7.008   -58.065 6.993   1.00 54.94  ? 322  GLN B C   1 
ATOM   5282  O  O   . GLN B 1 322 ? 7.055   -57.662 8.157   1.00 55.51  ? 322  GLN B O   1 
ATOM   5283  C  CB  . GLN B 1 322 ? 5.023   -59.506 6.432   1.00 58.84  ? 322  GLN B CB  1 
ATOM   5284  C  CG  . GLN B 1 322 ? 3.769   -59.471 7.307   1.00 61.55  ? 322  GLN B CG  1 
ATOM   5285  C  CD  . GLN B 1 322 ? 2.639   -58.693 6.667   1.00 66.08  ? 322  GLN B CD  1 
ATOM   5286  O  OE1 . GLN B 1 322 ? 1.965   -57.898 7.324   1.00 72.78  ? 322  GLN B OE1 1 
ATOM   5287  N  NE2 . GLN B 1 322 ? 2.428   -58.914 5.376   1.00 57.64  ? 322  GLN B NE2 1 
ATOM   5288  N  N   . ARG B 1 323 ? 8.085   -58.439 6.322   1.00 43.64  ? 323  ARG B N   1 
ATOM   5289  C  CA  . ARG B 1 323 ? 9.402   -58.407 6.942   1.00 40.68  ? 323  ARG B CA  1 
ATOM   5290  C  C   . ARG B 1 323 ? 9.945   -56.987 7.084   1.00 42.80  ? 323  ARG B C   1 
ATOM   5291  O  O   . ARG B 1 323 ? 10.517  -56.626 8.121   1.00 43.46  ? 323  ARG B O   1 
ATOM   5292  C  CB  . ARG B 1 323 ? 10.367  -59.238 6.112   1.00 41.45  ? 323  ARG B CB  1 
ATOM   5293  C  CG  . ARG B 1 323 ? 9.886   -60.653 5.872   1.00 41.91  ? 323  ARG B CG  1 
ATOM   5294  C  CD  . ARG B 1 323 ? 10.723  -61.332 4.812   1.00 47.28  ? 323  ARG B CD  1 
ATOM   5295  N  NE  . ARG B 1 323 ? 10.471  -62.770 4.753   1.00 56.12  ? 323  ARG B NE  1 
ATOM   5296  C  CZ  . ARG B 1 323 ? 11.015  -63.581 3.851   1.00 74.12  ? 323  ARG B CZ  1 
ATOM   5297  N  NH1 . ARG B 1 323 ? 11.831  -63.091 2.926   1.00 71.93  ? 323  ARG B NH1 1 
ATOM   5298  N  NH2 . ARG B 1 323 ? 10.743  -64.879 3.872   1.00 87.66  ? 323  ARG B NH2 1 
ATOM   5299  N  N   . ASN B 1 324 ? 9.773   -56.186 6.038   1.00 34.21  ? 324  ASN B N   1 
ATOM   5300  C  CA  . ASN B 1 324 ? 10.379  -54.854 6.001   1.00 39.67  ? 324  ASN B CA  1 
ATOM   5301  C  C   . ASN B 1 324 ? 9.541   -53.804 6.670   1.00 38.80  ? 324  ASN B C   1 
ATOM   5302  O  O   . ASN B 1 324 ? 10.032  -52.722 6.989   1.00 37.52  ? 324  ASN B O   1 
ATOM   5303  C  CB  . ASN B 1 324 ? 10.699  -54.442 4.568   1.00 30.28  ? 324  ASN B CB  1 
ATOM   5304  C  CG  . ASN B 1 324 ? 11.744  -55.333 3.953   1.00 35.29  ? 324  ASN B CG  1 
ATOM   5305  O  OD1 . ASN B 1 324 ? 12.927  -54.999 3.927   1.00 44.52  ? 324  ASN B OD1 1 
ATOM   5306  N  ND2 . ASN B 1 324 ? 11.324  -56.506 3.509   1.00 30.49  ? 324  ASN B ND2 1 
ATOM   5307  N  N   . LYS B 1 325 ? 8.278   -54.153 6.886   1.00 40.60  ? 325  LYS B N   1 
ATOM   5308  C  CA  . LYS B 1 325 ? 7.278   -53.242 7.409   1.00 39.30  ? 325  LYS B CA  1 
ATOM   5309  C  C   . LYS B 1 325 ? 7.789   -52.549 8.660   1.00 38.29  ? 325  LYS B C   1 
ATOM   5310  O  O   . LYS B 1 325 ? 7.912   -51.324 8.697   1.00 47.95  ? 325  LYS B O   1 
ATOM   5311  C  CB  . LYS B 1 325 ? 6.009   -54.027 7.722   1.00 43.92  ? 325  LYS B CB  1 
ATOM   5312  C  CG  . LYS B 1 325 ? 4.774   -53.209 8.017   1.00 26.34  ? 325  LYS B CG  1 
ATOM   5313  C  CD  . LYS B 1 325 ? 3.652   -54.184 8.328   1.00 44.70  ? 325  LYS B CD  1 
ATOM   5314  C  CE  . LYS B 1 325 ? 2.347   -53.493 8.639   1.00 58.41  ? 325  LYS B CE  1 
ATOM   5315  N  NZ  . LYS B 1 325 ? 1.291   -54.503 8.935   1.00 66.01  ? 325  LYS B NZ  1 
ATOM   5316  N  N   . ALA B 1 326 ? 8.092   -53.339 9.683   1.00 43.44  ? 326  ALA B N   1 
ATOM   5317  C  CA  . ALA B 1 326 ? 8.592   -52.804 10.952  1.00 52.28  ? 326  ALA B CA  1 
ATOM   5318  C  C   . ALA B 1 326 ? 9.891   -52.016 10.811  1.00 52.20  ? 326  ALA B C   1 
ATOM   5319  O  O   . ALA B 1 326 ? 10.072  -50.983 11.465  1.00 46.13  ? 326  ALA B O   1 
ATOM   5320  C  CB  . ALA B 1 326 ? 8.784   -53.927 11.957  1.00 46.76  ? 326  ALA B CB  1 
ATOM   5321  N  N   . SER B 1 327 ? 10.792  -52.518 9.967   1.00 49.72  ? 327  SER B N   1 
ATOM   5322  C  CA  . SER B 1 327 ? 12.102  -51.907 9.769   1.00 35.60  ? 327  SER B CA  1 
ATOM   5323  C  C   . SER B 1 327 ? 11.983  -50.549 9.091   1.00 31.12  ? 327  SER B C   1 
ATOM   5324  O  O   . SER B 1 327 ? 12.758  -49.627 9.369   1.00 30.95  ? 327  SER B O   1 
ATOM   5325  C  CB  . SER B 1 327 ? 12.990  -52.838 8.941   1.00 29.19  ? 327  SER B CB  1 
ATOM   5326  O  OG  . SER B 1 327 ? 13.085  -54.116 9.551   1.00 35.47  ? 327  SER B OG  1 
ATOM   5327  N  N   . LEU B 1 328 ? 11.005  -50.438 8.198   1.00 21.81  ? 328  LEU B N   1 
ATOM   5328  C  CA  . LEU B 1 328 ? 10.816  -49.253 7.409   1.00 15.68  ? 328  LEU B CA  1 
ATOM   5329  C  C   . LEU B 1 328 ? 10.205  -48.131 8.253   1.00 37.12  ? 328  LEU B C   1 
ATOM   5330  O  O   . LEU B 1 328 ? 10.520  -46.936 8.071   1.00 32.28  ? 328  LEU B O   1 
ATOM   5331  C  CB  . LEU B 1 328 ? 9.917   -49.591 6.233   1.00 21.10  ? 328  LEU B CB  1 
ATOM   5332  C  CG  . LEU B 1 328 ? 10.556  -50.234 5.011   1.00 18.83  ? 328  LEU B CG  1 
ATOM   5333  C  CD1 . LEU B 1 328 ? 9.523   -50.945 4.172   1.00 19.94  ? 328  LEU B CD1 1 
ATOM   5334  C  CD2 . LEU B 1 328 ? 11.237  -49.174 4.184   1.00 24.80  ? 328  LEU B CD2 1 
ATOM   5335  N  N   . LEU B 1 329 ? 9.329   -48.527 9.174   1.00 32.55  ? 329  LEU B N   1 
ATOM   5336  C  CA  . LEU B 1 329 ? 8.653   -47.591 10.069  1.00 37.91  ? 329  LEU B CA  1 
ATOM   5337  C  C   . LEU B 1 329 ? 9.577   -47.117 11.181  1.00 36.46  ? 329  LEU B C   1 
ATOM   5338  O  O   . LEU B 1 329 ? 9.685   -45.915 11.441  1.00 45.92  ? 329  LEU B O   1 
ATOM   5339  C  CB  . LEU B 1 329 ? 7.412   -48.244 10.671  1.00 40.12  ? 329  LEU B CB  1 
ATOM   5340  C  CG  . LEU B 1 329 ? 6.073   -48.174 9.928   1.00 42.92  ? 329  LEU B CG  1 
ATOM   5341  C  CD1 . LEU B 1 329 ? 6.187   -47.462 8.587   1.00 41.86  ? 329  LEU B CD1 1 
ATOM   5342  C  CD2 . LEU B 1 329 ? 5.467   -49.565 9.768   1.00 46.11  ? 329  LEU B CD2 1 
ATOM   5343  N  N   . GLN B 1 330 ? 10.228  -48.074 11.842  1.00 30.51  ? 330  GLN B N   1 
ATOM   5344  C  CA  . GLN B 1 330 ? 11.182  -47.794 12.918  1.00 42.00  ? 330  GLN B CA  1 
ATOM   5345  C  C   . GLN B 1 330 ? 12.397  -46.966 12.465  1.00 46.42  ? 330  GLN B C   1 
ATOM   5346  O  O   . GLN B 1 330 ? 12.862  -46.095 13.215  1.00 47.79  ? 330  GLN B O   1 
ATOM   5347  C  CB  . GLN B 1 330 ? 11.652  -49.100 13.568  1.00 51.70  ? 330  GLN B CB  1 
ATOM   5348  C  CG  . GLN B 1 330 ? 10.576  -49.804 14.359  1.00 52.22  ? 330  GLN B CG  1 
ATOM   5349  C  CD  . GLN B 1 330 ? 9.966   -48.899 15.413  1.00 60.99  ? 330  GLN B CD  1 
ATOM   5350  O  OE1 . GLN B 1 330 ? 10.595  -48.606 16.432  1.00 56.14  ? 330  GLN B OE1 1 
ATOM   5351  N  NE2 . GLN B 1 330 ? 8.733   -48.446 15.171  1.00 71.36  ? 330  GLN B NE2 1 
ATOM   5352  N  N   . LEU B 1 331 ? 12.911  -47.239 11.260  1.00 22.39  ? 331  LEU B N   1 
ATOM   5353  C  CA  . LEU B 1 331 ? 13.951  -46.394 10.685  1.00 23.64  ? 331  LEU B CA  1 
ATOM   5354  C  C   . LEU B 1 331 ? 13.485  -44.938 10.573  1.00 23.56  ? 331  LEU B C   1 
ATOM   5355  O  O   . LEU B 1 331 ? 14.124  -44.029 11.105  1.00 29.10  ? 331  LEU B O   1 
ATOM   5356  C  CB  . LEU B 1 331 ? 14.398  -46.919 9.325   1.00 32.28  ? 331  LEU B CB  1 
ATOM   5357  C  CG  . LEU B 1 331 ? 15.703  -46.330 8.761   1.00 39.48  ? 331  LEU B CG  1 
ATOM   5358  C  CD1 . LEU B 1 331 ? 16.102  -47.040 7.464   1.00 26.30  ? 331  LEU B CD1 1 
ATOM   5359  C  CD2 . LEU B 1 331 ? 15.596  -44.820 8.529   1.00 56.42  ? 331  LEU B CD2 1 
ATOM   5360  N  N   . LEU B 1 332 ? 12.370  -44.724 9.883   1.00 24.74  ? 332  LEU B N   1 
ATOM   5361  C  CA  . LEU B 1 332 ? 11.791  -43.387 9.740   1.00 28.79  ? 332  LEU B CA  1 
ATOM   5362  C  C   . LEU B 1 332 ? 11.733  -42.654 11.064  1.00 34.59  ? 332  LEU B C   1 
ATOM   5363  O  O   . LEU B 1 332 ? 12.104  -41.489 11.148  1.00 36.82  ? 332  LEU B O   1 
ATOM   5364  C  CB  . LEU B 1 332 ? 10.389  -43.478 9.152   1.00 42.27  ? 332  LEU B CB  1 
ATOM   5365  C  CG  . LEU B 1 332 ? 10.347  -43.904 7.681   1.00 47.21  ? 332  LEU B CG  1 
ATOM   5366  C  CD1 . LEU B 1 332 ? 8.923   -44.201 7.248   1.00 40.56  ? 332  LEU B CD1 1 
ATOM   5367  C  CD2 . LEU B 1 332 ? 10.980  -42.832 6.787   1.00 40.34  ? 332  LEU B CD2 1 
ATOM   5368  N  N   . ARG B 1 333 ? 11.263  -43.347 12.097  1.00 42.38  ? 333  ARG B N   1 
ATOM   5369  C  CA  . ARG B 1 333 ? 11.164  -42.787 13.439  1.00 31.65  ? 333  ARG B CA  1 
ATOM   5370  C  C   . ARG B 1 333 ? 12.511  -42.326 13.988  1.00 33.41  ? 333  ARG B C   1 
ATOM   5371  O  O   . ARG B 1 333 ? 12.569  -41.485 14.885  1.00 51.69  ? 333  ARG B O   1 
ATOM   5372  C  CB  . ARG B 1 333 ? 10.562  -43.825 14.372  1.00 27.09  ? 333  ARG B CB  1 
ATOM   5373  C  CG  . ARG B 1 333 ? 9.139   -44.153 14.054  1.00 40.47  ? 333  ARG B CG  1 
ATOM   5374  C  CD  . ARG B 1 333 ? 8.330   -44.026 15.316  1.00 59.55  ? 333  ARG B CD  1 
ATOM   5375  N  NE  . ARG B 1 333 ? 6.916   -43.984 15.028  1.00 64.51  ? 333  ARG B NE  1 
ATOM   5376  C  CZ  . ARG B 1 333 ? 6.055   -43.064 15.447  1.00 70.52  ? 333  ARG B CZ  1 
ATOM   5377  N  NH1 . ARG B 1 333 ? 6.429   -42.044 16.218  1.00 60.53  ? 333  ARG B NH1 1 
ATOM   5378  N  NH2 . ARG B 1 333 ? 4.788   -43.190 15.081  1.00 75.62  ? 333  ARG B NH2 1 
ATOM   5379  N  N   . GLN B 1 334 ? 13.592  -42.888 13.462  1.00 24.17  ? 334  GLN B N   1 
ATOM   5380  C  CA  . GLN B 1 334 ? 14.917  -42.459 13.866  1.00 24.76  ? 334  GLN B CA  1 
ATOM   5381  C  C   . GLN B 1 334 ? 15.186  -41.011 13.451  1.00 34.31  ? 334  GLN B C   1 
ATOM   5382  O  O   . GLN B 1 334 ? 16.132  -40.386 13.923  1.00 41.01  ? 334  GLN B O   1 
ATOM   5383  C  CB  . GLN B 1 334 ? 15.966  -43.384 13.269  1.00 32.84  ? 334  GLN B CB  1 
ATOM   5384  C  CG  . GLN B 1 334 ? 16.041  -44.725 13.956  1.00 38.54  ? 334  GLN B CG  1 
ATOM   5385  C  CD  . GLN B 1 334 ? 16.689  -44.639 15.322  1.00 40.76  ? 334  GLN B CD  1 
ATOM   5386  O  OE1 . GLN B 1 334 ? 17.864  -44.306 15.441  1.00 51.02  ? 334  GLN B OE1 1 
ATOM   5387  N  NE2 . GLN B 1 334 ? 15.927  -44.948 16.359  1.00 34.37  ? 334  GLN B NE2 1 
ATOM   5388  N  N   . ALA B 1 335 ? 14.351  -40.477 12.565  1.00 38.57  ? 335  ALA B N   1 
ATOM   5389  C  CA  . ALA B 1 335 ? 14.492  -39.087 12.136  1.00 38.19  ? 335  ALA B CA  1 
ATOM   5390  C  C   . ALA B 1 335 ? 14.103  -38.178 13.277  1.00 38.61  ? 335  ALA B C   1 
ATOM   5391  O  O   . ALA B 1 335 ? 13.997  -36.964 13.115  1.00 51.18  ? 335  ALA B O   1 
ATOM   5392  C  CB  . ALA B 1 335 ? 13.633  -38.795 10.916  1.00 22.67  ? 335  ALA B CB  1 
ATOM   5393  N  N   . HIS B 1 336 ? 13.892  -38.764 14.445  1.00 30.32  ? 336  HIS B N   1 
ATOM   5394  C  CA  . HIS B 1 336 ? 13.507  -37.961 15.595  1.00 37.36  ? 336  HIS B CA  1 
ATOM   5395  C  C   . HIS B 1 336 ? 14.498  -38.044 16.751  1.00 37.99  ? 336  HIS B C   1 
ATOM   5396  O  O   . HIS B 1 336 ? 14.304  -37.400 17.779  1.00 39.41  ? 336  HIS B O   1 
ATOM   5397  C  CB  . HIS B 1 336 ? 12.085  -38.310 16.037  1.00 31.09  ? 336  HIS B CB  1 
ATOM   5398  C  CG  . HIS B 1 336 ? 11.074  -38.091 14.961  1.00 38.83  ? 336  HIS B CG  1 
ATOM   5399  N  ND1 . HIS B 1 336 ? 10.621  -36.837 14.615  1.00 40.50  ? 336  HIS B ND1 1 
ATOM   5400  C  CD2 . HIS B 1 336 ? 10.454  -38.960 14.129  1.00 43.00  ? 336  HIS B CD2 1 
ATOM   5401  C  CE1 . HIS B 1 336 ? 9.748   -36.942 13.628  1.00 43.30  ? 336  HIS B CE1 1 
ATOM   5402  N  NE2 . HIS B 1 336 ? 9.631   -38.219 13.313  1.00 53.05  ? 336  HIS B NE2 1 
ATOM   5403  N  N   . ILE B 1 337 ? 15.576  -38.804 16.581  1.00 25.88  ? 337  ILE B N   1 
ATOM   5404  C  CA  . ILE B 1 337 ? 16.595  -38.854 17.622  1.00 32.39  ? 337  ILE B CA  1 
ATOM   5405  C  C   . ILE B 1 337 ? 17.439  -37.568 17.687  1.00 37.69  ? 337  ILE B C   1 
ATOM   5406  O  O   . ILE B 1 337 ? 17.355  -36.702 16.814  1.00 45.48  ? 337  ILE B O   1 
ATOM   5407  C  CB  . ILE B 1 337 ? 17.524  -40.081 17.480  1.00 39.22  ? 337  ILE B CB  1 
ATOM   5408  C  CG1 . ILE B 1 337 ? 18.331  -39.991 16.187  1.00 45.24  ? 337  ILE B CG1 1 
ATOM   5409  C  CG2 . ILE B 1 337 ? 16.719  -41.360 17.522  1.00 43.05  ? 337  ILE B CG2 1 
ATOM   5410  C  CD1 . ILE B 1 337 ? 19.316  -41.092 16.026  1.00 35.00  ? 337  ILE B CD1 1 
ATOM   5411  N  N   . GLY B 1 338 ? 18.252  -37.458 18.736  1.00 42.77  ? 338  GLY B N   1 
ATOM   5412  C  CA  . GLY B 1 338 ? 19.112  -36.307 18.924  1.00 36.50  ? 338  GLY B CA  1 
ATOM   5413  C  C   . GLY B 1 338 ? 18.335  -35.069 19.304  1.00 32.49  ? 338  GLY B C   1 
ATOM   5414  O  O   . GLY B 1 338 ? 17.427  -35.123 20.149  1.00 46.24  ? 338  GLY B O   1 
ATOM   5415  N  N   . ILE B 1 339 ? 18.693  -33.951 18.682  1.00 24.78  ? 339  ILE B N   1 
ATOM   5416  C  CA  . ILE B 1 339 ? 18.034  -32.681 18.958  1.00 34.40  ? 339  ILE B CA  1 
ATOM   5417  C  C   . ILE B 1 339 ? 17.548  -31.970 17.694  1.00 38.56  ? 339  ILE B C   1 
ATOM   5418  O  O   . ILE B 1 339 ? 17.803  -32.407 16.560  1.00 34.08  ? 339  ILE B O   1 
ATOM   5419  C  CB  . ILE B 1 339 ? 18.982  -31.730 19.682  1.00 32.16  ? 339  ILE B CB  1 
ATOM   5420  C  CG1 . ILE B 1 339 ? 20.281  -31.612 18.888  1.00 37.33  ? 339  ILE B CG1 1 
ATOM   5421  C  CG2 . ILE B 1 339 ? 19.281  -32.235 21.075  1.00 29.84  ? 339  ILE B CG2 1 
ATOM   5422  C  CD1 . ILE B 1 339 ? 21.293  -30.702 19.528  1.00 24.84  ? 339  ILE B CD1 1 
ATOM   5423  N  N   . LYS B 1 340 ? 16.832  -30.872 17.916  1.00 37.70  ? 340  LYS B N   1 
ATOM   5424  C  CA  . LYS B 1 340 ? 16.432  -29.960 16.853  1.00 36.02  ? 340  LYS B CA  1 
ATOM   5425  C  C   . LYS B 1 340 ? 16.075  -28.614 17.457  1.00 43.14  ? 340  LYS B C   1 
ATOM   5426  O  O   . LYS B 1 340 ? 15.748  -28.522 18.648  1.00 46.65  ? 340  LYS B O   1 
ATOM   5427  C  CB  . LYS B 1 340 ? 15.238  -30.507 16.087  1.00 36.09  ? 340  LYS B CB  1 
ATOM   5428  C  CG  . LYS B 1 340 ? 14.004  -30.704 16.938  1.00 30.22  ? 340  LYS B CG  1 
ATOM   5429  C  CD  . LYS B 1 340 ? 12.837  -31.115 16.048  1.00 34.34  ? 340  LYS B CD  1 
ATOM   5430  C  CE  . LYS B 1 340 ? 11.590  -31.480 16.853  1.00 28.04  ? 340  LYS B CE  1 
ATOM   5431  N  NZ  . LYS B 1 340 ? 10.497  -31.929 15.947  1.00 30.06  ? 340  LYS B NZ  1 
ATOM   5432  N  N   . GLY B 1 341 ? 16.136  -27.569 16.641  1.00 28.31  ? 341  GLY B N   1 
ATOM   5433  C  CA  . GLY B 1 341 ? 15.846  -26.235 17.130  1.00 30.14  ? 341  GLY B CA  1 
ATOM   5434  C  C   . GLY B 1 341 ? 16.093  -25.147 16.106  1.00 35.01  ? 341  GLY B C   1 
ATOM   5435  O  O   . GLY B 1 341 ? 16.250  -25.412 14.911  1.00 29.98  ? 341  GLY B O   1 
ATOM   5436  N  N   . LEU B 1 342 ? 16.141  -23.913 16.589  1.00 37.94  ? 342  LEU B N   1 
ATOM   5437  C  CA  . LEU B 1 342 ? 16.260  -22.756 15.724  1.00 36.44  ? 342  LEU B CA  1 
ATOM   5438  C  C   . LEU B 1 342 ? 17.502  -21.947 16.048  1.00 37.59  ? 342  LEU B C   1 
ATOM   5439  O  O   . LEU B 1 342 ? 17.882  -21.803 17.219  1.00 43.75  ? 342  LEU B O   1 
ATOM   5440  C  CB  . LEU B 1 342 ? 15.028  -21.871 15.901  1.00 33.07  ? 342  LEU B CB  1 
ATOM   5441  C  CG  . LEU B 1 342 ? 13.708  -22.587 15.627  1.00 36.39  ? 342  LEU B CG  1 
ATOM   5442  C  CD1 . LEU B 1 342 ? 12.515  -21.734 16.057  1.00 30.47  ? 342  LEU B CD1 1 
ATOM   5443  C  CD2 . LEU B 1 342 ? 13.605  -23.011 14.143  1.00 27.46  ? 342  LEU B CD2 1 
ATOM   5444  N  N   . VAL B 1 343 ? 18.143  -21.432 15.006  1.00 30.59  ? 343  VAL B N   1 
ATOM   5445  C  CA  . VAL B 1 343 ? 19.155  -20.407 15.196  1.00 39.59  ? 343  VAL B CA  1 
ATOM   5446  C  C   . VAL B 1 343 ? 18.498  -19.117 14.763  1.00 38.58  ? 343  VAL B C   1 
ATOM   5447  O  O   . VAL B 1 343 ? 18.094  -18.977 13.607  1.00 38.06  ? 343  VAL B O   1 
ATOM   5448  C  CB  . VAL B 1 343 ? 20.457  -20.651 14.398  1.00 38.37  ? 343  VAL B CB  1 
ATOM   5449  C  CG1 . VAL B 1 343 ? 21.448  -19.515 14.671  1.00 31.51  ? 343  VAL B CG1 1 
ATOM   5450  C  CG2 . VAL B 1 343 ? 21.091  -21.983 14.784  1.00 37.22  ? 343  VAL B CG2 1 
ATOM   5451  N  N   . THR B 1 344 ? 18.381  -18.183 15.700  1.00 45.99  ? 344  THR B N   1 
ATOM   5452  C  CA  . THR B 1 344 ? 17.536  -17.025 15.495  1.00 44.80  ? 344  THR B CA  1 
ATOM   5453  C  C   . THR B 1 344 ? 18.192  -15.700 15.891  1.00 46.85  ? 344  THR B C   1 
ATOM   5454  O  O   . THR B 1 344 ? 19.233  -15.667 16.572  1.00 42.10  ? 344  THR B O   1 
ATOM   5455  C  CB  . THR B 1 344 ? 16.222  -17.184 16.273  1.00 47.49  ? 344  THR B CB  1 
ATOM   5456  O  OG1 . THR B 1 344 ? 15.235  -16.311 15.717  1.00 69.72  ? 344  THR B OG1 1 
ATOM   5457  C  CG2 . THR B 1 344 ? 16.426  -16.860 17.768  1.00 35.20  ? 344  THR B CG2 1 
ATOM   5458  N  N   . ASP B 1 345 ? 17.553  -14.623 15.440  1.00 34.41  ? 345  ASP B N   1 
ATOM   5459  C  CA  . ASP B 1 345 ? 17.881  -13.238 15.780  1.00 37.51  ? 345  ASP B CA  1 
ATOM   5460  C  C   . ASP B 1 345 ? 17.671  -12.929 17.243  1.00 44.83  ? 345  ASP B C   1 
ATOM   5461  O  O   . ASP B 1 345 ? 16.872  -13.583 17.930  1.00 43.44  ? 345  ASP B O   1 
ATOM   5462  C  CB  . ASP B 1 345 ? 16.903  -12.313 15.055  1.00 44.18  ? 345  ASP B CB  1 
ATOM   5463  C  CG  . ASP B 1 345 ? 17.530  -11.566 13.928  1.00 48.94  ? 345  ASP B CG  1 
ATOM   5464  O  OD1 . ASP B 1 345 ? 16.765  -10.929 13.174  1.00 58.98  ? 345  ASP B OD1 1 
ATOM   5465  O  OD2 . ASP B 1 345 ? 18.771  -11.609 13.801  1.00 67.03  ? 345  ASP B OD2 1 
ATOM   5466  N  N   . ALA B 1 346 ? 18.362  -11.894 17.704  1.00 56.44  ? 346  ALA B N   1 
ATOM   5467  C  CA  . ALA B 1 346 ? 17.918  -11.176 18.882  1.00 53.04  ? 346  ALA B CA  1 
ATOM   5468  C  C   . ALA B 1 346 ? 16.424  -10.913 18.645  1.00 43.58  ? 346  ALA B C   1 
ATOM   5469  O  O   . ALA B 1 346 ? 15.569  -11.171 19.506  1.00 34.13  ? 346  ALA B O   1 
ATOM   5470  C  CB  . ALA B 1 346 ? 18.692  -9.871  19.005  1.00 31.75  ? 346  ALA B CB  1 
ATOM   5471  N  N   . SER B 1 347 ? 16.128  -10.432 17.440  1.00 36.08  ? 347  SER B N   1 
ATOM   5472  C  CA  . SER B 1 347 ? 14.767  -10.148 17.004  1.00 48.02  ? 347  SER B CA  1 
ATOM   5473  C  C   . SER B 1 347 ? 13.851  -11.352 17.171  1.00 49.83  ? 347  SER B C   1 
ATOM   5474  O  O   . SER B 1 347 ? 12.655  -11.195 17.404  1.00 50.62  ? 347  SER B O   1 
ATOM   5475  C  CB  . SER B 1 347 ? 14.762  -9.723  15.531  1.00 67.89  ? 347  SER B CB  1 
ATOM   5476  O  OG  . SER B 1 347 ? 15.686  -8.674  15.279  1.00 80.32  ? 347  SER B OG  1 
ATOM   5477  N  N   . GLY B 1 348 ? 14.415  -12.552 17.046  1.00 49.81  ? 348  GLY B N   1 
ATOM   5478  C  CA  . GLY B 1 348 ? 13.630  -13.779 17.033  1.00 37.81  ? 348  GLY B CA  1 
ATOM   5479  C  C   . GLY B 1 348 ? 13.459  -14.267 15.606  1.00 40.72  ? 348  GLY B C   1 
ATOM   5480  O  O   . GLY B 1 348 ? 12.621  -15.124 15.318  1.00 44.28  ? 348  GLY B O   1 
ATOM   5481  N  N   . PHE B 1 349 ? 14.276  -13.714 14.712  1.00 34.58  ? 349  PHE B N   1 
ATOM   5482  C  CA  . PHE B 1 349 ? 14.175  -13.965 13.280  1.00 25.29  ? 349  PHE B CA  1 
ATOM   5483  C  C   . PHE B 1 349 ? 15.274  -14.901 12.774  1.00 42.48  ? 349  PHE B C   1 
ATOM   5484  O  O   . PHE B 1 349 ? 16.462  -14.688 13.037  1.00 29.69  ? 349  PHE B O   1 
ATOM   5485  C  CB  . PHE B 1 349 ? 14.229  -12.649 12.509  1.00 36.74  ? 349  PHE B CB  1 
ATOM   5486  C  CG  . PHE B 1 349 ? 13.773  -12.773 11.089  1.00 43.67  ? 349  PHE B CG  1 
ATOM   5487  C  CD1 . PHE B 1 349 ? 12.427  -12.649 10.768  1.00 44.91  ? 349  PHE B CD1 1 
ATOM   5488  C  CD2 . PHE B 1 349 ? 14.679  -13.037 10.081  1.00 40.68  ? 349  PHE B CD2 1 
ATOM   5489  C  CE1 . PHE B 1 349 ? 11.998  -12.774 9.467   1.00 35.24  ? 349  PHE B CE1 1 
ATOM   5490  C  CE2 . PHE B 1 349 ? 14.261  -13.166 8.777   1.00 41.90  ? 349  PHE B CE2 1 
ATOM   5491  C  CZ  . PHE B 1 349 ? 12.921  -13.037 8.468   1.00 48.33  ? 349  PHE B CZ  1 
ATOM   5492  N  N   . PRO B 1 350 ? 14.879  -15.924 12.000  1.00 44.16  ? 350  PRO B N   1 
ATOM   5493  C  CA  . PRO B 1 350 ? 15.736  -17.087 11.720  1.00 33.73  ? 350  PRO B CA  1 
ATOM   5494  C  C   . PRO B 1 350 ? 16.992  -16.732 10.925  1.00 39.54  ? 350  PRO B C   1 
ATOM   5495  O  O   . PRO B 1 350 ? 16.939  -15.881 10.040  1.00 36.42  ? 350  PRO B O   1 
ATOM   5496  C  CB  . PRO B 1 350 ? 14.813  -18.006 10.918  1.00 29.55  ? 350  PRO B CB  1 
ATOM   5497  C  CG  . PRO B 1 350 ? 13.837  -17.075 10.259  1.00 40.94  ? 350  PRO B CG  1 
ATOM   5498  C  CD  . PRO B 1 350 ? 13.627  -15.946 11.218  1.00 35.73  ? 350  PRO B CD  1 
ATOM   5499  N  N   . ILE B 1 351 ? 18.113  -17.365 11.263  1.00 36.93  ? 351  ILE B N   1 
ATOM   5500  C  CA  . ILE B 1 351 ? 19.335  -17.231 10.479  1.00 24.54  ? 351  ILE B CA  1 
ATOM   5501  C  C   . ILE B 1 351 ? 19.540  -18.474 9.601   1.00 34.04  ? 351  ILE B C   1 
ATOM   5502  O  O   . ILE B 1 351 ? 19.686  -19.602 10.084  1.00 21.50  ? 351  ILE B O   1 
ATOM   5503  C  CB  . ILE B 1 351 ? 20.573  -17.010 11.348  1.00 33.46  ? 351  ILE B CB  1 
ATOM   5504  C  CG1 . ILE B 1 351 ? 20.375  -15.818 12.284  1.00 42.56  ? 351  ILE B CG1 1 
ATOM   5505  C  CG2 . ILE B 1 351 ? 21.783  -16.749 10.472  1.00 31.54  ? 351  ILE B CG2 1 
ATOM   5506  C  CD1 . ILE B 1 351 ? 21.414  -15.719 13.410  1.00 29.11  ? 351  ILE B CD1 1 
ATOM   5507  N  N   . ALA B 1 352 ? 19.544  -18.247 8.298   1.00 34.27  ? 352  ALA B N   1 
ATOM   5508  C  CA  . ALA B 1 352 ? 19.678  -19.310 7.329   1.00 28.12  ? 352  ALA B CA  1 
ATOM   5509  C  C   . ALA B 1 352 ? 21.144  -19.635 7.135   1.00 35.94  ? 352  ALA B C   1 
ATOM   5510  O  O   . ALA B 1 352 ? 21.993  -18.744 7.230   1.00 38.59  ? 352  ALA B O   1 
ATOM   5511  C  CB  . ALA B 1 352 ? 19.045  -18.880 6.009   1.00 22.08  ? 352  ALA B CB  1 
ATOM   5512  N  N   . ASP B 1 353 ? 21.439  -20.908 6.866   1.00 31.23  ? 353  ASP B N   1 
ATOM   5513  C  CA  . ASP B 1 353 ? 22.805  -21.337 6.589   1.00 25.33  ? 353  ASP B CA  1 
ATOM   5514  C  C   . ASP B 1 353 ? 23.742  -21.124 7.770   1.00 33.85  ? 353  ASP B C   1 
ATOM   5515  O  O   . ASP B 1 353 ? 24.952  -21.007 7.590   1.00 38.44  ? 353  ASP B O   1 
ATOM   5516  C  CB  . ASP B 1 353 ? 23.360  -20.577 5.388   1.00 50.36  ? 353  ASP B CB  1 
ATOM   5517  C  CG  . ASP B 1 353 ? 23.445  -21.431 4.146   1.00 72.84  ? 353  ASP B CG  1 
ATOM   5518  O  OD1 . ASP B 1 353 ? 24.548  -21.933 3.843   1.00 79.92  ? 353  ASP B OD1 1 
ATOM   5519  O  OD2 . ASP B 1 353 ? 22.408  -21.604 3.476   1.00 81.10  ? 353  ASP B OD2 1 
ATOM   5520  N  N   . ALA B 1 354 ? 23.183  -21.041 8.972   1.00 39.22  ? 354  ALA B N   1 
ATOM   5521  C  CA  . ALA B 1 354 ? 23.984  -21.025 10.191  1.00 43.68  ? 354  ALA B CA  1 
ATOM   5522  C  C   . ALA B 1 354 ? 24.537  -22.435 10.456  1.00 47.50  ? 354  ALA B C   1 
ATOM   5523  O  O   . ALA B 1 354 ? 23.989  -23.430 9.953   1.00 31.99  ? 354  ALA B O   1 
ATOM   5524  C  CB  . ALA B 1 354 ? 23.145  -20.541 11.371  1.00 35.69  ? 354  ALA B CB  1 
ATOM   5525  N  N   . ASN B 1 355 ? 25.622  -22.520 11.228  1.00 44.45  ? 355  ASN B N   1 
ATOM   5526  C  CA  . ASN B 1 355 ? 26.243  -23.811 11.542  1.00 44.57  ? 355  ASN B CA  1 
ATOM   5527  C  C   . ASN B 1 355 ? 26.057  -24.225 12.997  1.00 44.58  ? 355  ASN B C   1 
ATOM   5528  O  O   . ASN B 1 355 ? 26.237  -23.429 13.925  1.00 41.75  ? 355  ASN B O   1 
ATOM   5529  C  CB  . ASN B 1 355 ? 27.732  -23.825 11.177  1.00 51.09  ? 355  ASN B CB  1 
ATOM   5530  C  CG  . ASN B 1 355 ? 27.976  -23.998 9.678   1.00 52.76  ? 355  ASN B CG  1 
ATOM   5531  O  OD1 . ASN B 1 355 ? 28.615  -23.157 9.049   1.00 55.28  ? 355  ASN B OD1 1 
ATOM   5532  N  ND2 . ASN B 1 355 ? 27.471  -25.091 9.106   1.00 50.51  ? 355  ASN B ND2 1 
ATOM   5533  N  N   . VAL B 1 356 ? 25.686  -25.483 13.187  1.00 35.16  ? 356  VAL B N   1 
ATOM   5534  C  CA  . VAL B 1 356 ? 25.466  -25.994 14.522  1.00 32.13  ? 356  VAL B CA  1 
ATOM   5535  C  C   . VAL B 1 356 ? 26.422  -27.137 14.738  1.00 32.55  ? 356  VAL B C   1 
ATOM   5536  O  O   . VAL B 1 356 ? 26.355  -28.152 14.056  1.00 27.40  ? 356  VAL B O   1 
ATOM   5537  C  CB  . VAL B 1 356 ? 24.011  -26.466 14.730  1.00 41.87  ? 356  VAL B CB  1 
ATOM   5538  C  CG1 . VAL B 1 356 ? 23.859  -27.145 16.089  1.00 41.12  ? 356  VAL B CG1 1 
ATOM   5539  C  CG2 . VAL B 1 356 ? 23.032  -25.293 14.594  1.00 27.41  ? 356  VAL B CG2 1 
ATOM   5540  N  N   . TYR B 1 357 ? 27.312  -26.949 15.703  1.00 43.88  ? 357  TYR B N   1 
ATOM   5541  C  CA  . TYR B 1 357 ? 28.380  -27.891 16.010  1.00 39.97  ? 357  TYR B CA  1 
ATOM   5542  C  C   . TYR B 1 357 ? 28.155  -28.649 17.333  1.00 47.09  ? 357  TYR B C   1 
ATOM   5543  O  O   . TYR B 1 357 ? 27.636  -28.094 18.313  1.00 43.04  ? 357  TYR B O   1 
ATOM   5544  C  CB  . TYR B 1 357 ? 29.698  -27.131 16.125  1.00 37.18  ? 357  TYR B CB  1 
ATOM   5545  C  CG  . TYR B 1 357 ? 30.264  -26.553 14.853  1.00 36.23  ? 357  TYR B CG  1 
ATOM   5546  C  CD1 . TYR B 1 357 ? 30.078  -25.211 14.517  1.00 31.09  ? 357  TYR B CD1 1 
ATOM   5547  C  CD2 . TYR B 1 357 ? 31.036  -27.345 14.007  1.00 42.78  ? 357  TYR B CD2 1 
ATOM   5548  C  CE1 . TYR B 1 357 ? 30.629  -24.690 13.352  1.00 39.30  ? 357  TYR B CE1 1 
ATOM   5549  C  CE2 . TYR B 1 357 ? 31.588  -26.839 12.850  1.00 29.70  ? 357  TYR B CE2 1 
ATOM   5550  C  CZ  . TYR B 1 357 ? 31.381  -25.519 12.525  1.00 37.91  ? 357  TYR B CZ  1 
ATOM   5551  O  OH  . TYR B 1 357 ? 31.939  -25.039 11.372  1.00 50.36  ? 357  TYR B OH  1 
ATOM   5552  N  N   . VAL B 1 358 ? 28.568  -29.916 17.352  1.00 57.51  ? 358  VAL B N   1 
ATOM   5553  C  CA  . VAL B 1 358 ? 28.592  -30.723 18.572  1.00 46.62  ? 358  VAL B CA  1 
ATOM   5554  C  C   . VAL B 1 358 ? 30.043  -31.118 18.869  1.00 50.48  ? 358  VAL B C   1 
ATOM   5555  O  O   . VAL B 1 358 ? 30.768  -31.583 17.980  1.00 48.89  ? 358  VAL B O   1 
ATOM   5556  C  CB  . VAL B 1 358 ? 27.709  -32.000 18.446  1.00 29.79  ? 358  VAL B CB  1 
ATOM   5557  C  CG1 . VAL B 1 358 ? 27.736  -32.811 19.730  1.00 22.43  ? 358  VAL B CG1 1 
ATOM   5558  C  CG2 . VAL B 1 358 ? 26.269  -31.646 18.086  1.00 22.52  ? 358  VAL B CG2 1 
ATOM   5559  N  N   . ALA B 1 359 ? 30.466  -30.922 20.114  1.00 50.07  ? 359  ALA B N   1 
ATOM   5560  C  CA  . ALA B 1 359 ? 31.829  -31.238 20.518  1.00 49.65  ? 359  ALA B CA  1 
ATOM   5561  C  C   . ALA B 1 359 ? 32.162  -32.681 20.170  1.00 41.99  ? 359  ALA B C   1 
ATOM   5562  O  O   . ALA B 1 359 ? 31.428  -33.596 20.545  1.00 40.97  ? 359  ALA B O   1 
ATOM   5563  C  CB  . ALA B 1 359 ? 31.995  -31.010 22.007  1.00 53.43  ? 359  ALA B CB  1 
ATOM   5564  N  N   . GLY B 1 360 ? 33.265  -32.890 19.459  1.00 28.54  ? 360  GLY B N   1 
ATOM   5565  C  CA  . GLY B 1 360 ? 33.627  -34.233 19.062  1.00 27.49  ? 360  GLY B CA  1 
ATOM   5566  C  C   . GLY B 1 360 ? 32.917  -34.667 17.796  1.00 41.10  ? 360  GLY B C   1 
ATOM   5567  O  O   . GLY B 1 360 ? 33.117  -35.787 17.326  1.00 57.10  ? 360  GLY B O   1 
ATOM   5568  N  N   . LEU B 1 361 ? 32.090  -33.784 17.240  1.00 34.60  ? 361  LEU B N   1 
ATOM   5569  C  CA  . LEU B 1 361 ? 31.484  -34.016 15.931  1.00 34.19  ? 361  LEU B CA  1 
ATOM   5570  C  C   . LEU B 1 361 ? 31.530  -32.750 15.110  1.00 39.93  ? 361  LEU B C   1 
ATOM   5571  O  O   . LEU B 1 361 ? 30.642  -32.498 14.293  1.00 37.63  ? 361  LEU B O   1 
ATOM   5572  C  CB  . LEU B 1 361 ? 30.036  -34.462 16.070  1.00 26.02  ? 361  LEU B CB  1 
ATOM   5573  C  CG  . LEU B 1 361 ? 29.812  -35.801 16.766  1.00 32.63  ? 361  LEU B CG  1 
ATOM   5574  C  CD1 . LEU B 1 361 ? 28.345  -35.974 17.075  1.00 42.39  ? 361  LEU B CD1 1 
ATOM   5575  C  CD2 . LEU B 1 361 ? 30.309  -36.942 15.914  1.00 32.66  ? 361  LEU B CD2 1 
ATOM   5576  N  N   . GLU B 1 362 ? 32.572  -31.956 15.333  1.00 40.48  ? 362  GLU B N   1 
ATOM   5577  C  CA  . GLU B 1 362 ? 32.681  -30.636 14.716  1.00 39.39  ? 362  GLU B CA  1 
ATOM   5578  C  C   . GLU B 1 362 ? 32.995  -30.716 13.231  1.00 42.97  ? 362  GLU B C   1 
ATOM   5579  O  O   . GLU B 1 362 ? 32.906  -29.719 12.510  1.00 39.16  ? 362  GLU B O   1 
ATOM   5580  C  CB  . GLU B 1 362 ? 33.709  -29.754 15.445  1.00 37.33  ? 362  GLU B CB  1 
ATOM   5581  C  CG  . GLU B 1 362 ? 33.120  -28.852 16.539  1.00 57.25  ? 362  GLU B CG  1 
ATOM   5582  C  CD  . GLU B 1 362 ? 33.841  -28.983 17.887  1.00 82.72  ? 362  GLU B CD  1 
ATOM   5583  O  OE1 . GLU B 1 362 ? 34.396  -30.075 18.180  1.00 84.98  ? 362  GLU B OE1 1 
ATOM   5584  O  OE2 . GLU B 1 362 ? 33.839  -27.992 18.658  1.00 82.37  ? 362  GLU B OE2 1 
ATOM   5585  N  N   . GLU B 1 363 ? 33.338  -31.908 12.763  1.00 40.06  ? 363  GLU B N   1 
ATOM   5586  C  CA  . GLU B 1 363 ? 33.672  -32.070 11.354  1.00 37.46  ? 363  GLU B CA  1 
ATOM   5587  C  C   . GLU B 1 363 ? 32.430  -32.180 10.480  1.00 42.11  ? 363  GLU B C   1 
ATOM   5588  O  O   . GLU B 1 363 ? 32.510  -32.027 9.253   1.00 27.72  ? 363  GLU B O   1 
ATOM   5589  C  CB  . GLU B 1 363 ? 34.576  -33.284 11.155  1.00 53.27  ? 363  GLU B CB  1 
ATOM   5590  C  CG  . GLU B 1 363 ? 36.007  -33.050 11.616  1.00 76.84  ? 363  GLU B CG  1 
ATOM   5591  C  CD  . GLU B 1 363 ? 36.919  -34.206 11.266  1.00 91.11  ? 363  GLU B CD  1 
ATOM   5592  O  OE1 . GLU B 1 363 ? 36.627  -35.341 11.707  1.00 84.18  ? 363  GLU B OE1 1 
ATOM   5593  O  OE2 . GLU B 1 363 ? 37.923  -33.978 10.547  1.00 102.92 ? 363  GLU B OE2 1 
ATOM   5594  N  N   . LYS B 1 364 ? 31.295  -32.457 11.128  1.00 37.92  ? 364  LYS B N   1 
ATOM   5595  C  CA  . LYS B 1 364 ? 29.998  -32.534 10.459  1.00 35.39  ? 364  LYS B CA  1 
ATOM   5596  C  C   . LYS B 1 364 ? 28.971  -31.623 11.126  1.00 44.14  ? 364  LYS B C   1 
ATOM   5597  O  O   . LYS B 1 364 ? 28.103  -32.084 11.891  1.00 48.07  ? 364  LYS B O   1 
ATOM   5598  C  CB  . LYS B 1 364 ? 29.458  -33.966 10.438  1.00 35.22  ? 364  LYS B CB  1 
ATOM   5599  C  CG  . LYS B 1 364 ? 28.154  -34.099 9.651   1.00 26.94  ? 364  LYS B CG  1 
ATOM   5600  C  CD  . LYS B 1 364 ? 28.370  -33.571 8.250   1.00 22.62  ? 364  LYS B CD  1 
ATOM   5601  C  CE  . LYS B 1 364 ? 27.195  -33.807 7.343   1.00 27.52  ? 364  LYS B CE  1 
ATOM   5602  N  NZ  . LYS B 1 364 ? 27.318  -32.981 6.096   1.00 18.54  ? 364  LYS B NZ  1 
ATOM   5603  N  N   . PRO B 1 365 ? 29.070  -30.322 10.837  1.00 32.99  ? 365  PRO B N   1 
ATOM   5604  C  CA  . PRO B 1 365 ? 28.120  -29.309 11.289  1.00 32.46  ? 365  PRO B CA  1 
ATOM   5605  C  C   . PRO B 1 365 ? 26.812  -29.443 10.530  1.00 40.75  ? 365  PRO B C   1 
ATOM   5606  O  O   . PRO B 1 365 ? 26.806  -29.983 9.422   1.00 41.48  ? 365  PRO B O   1 
ATOM   5607  C  CB  . PRO B 1 365 ? 28.794  -27.988 10.892  1.00 42.25  ? 365  PRO B CB  1 
ATOM   5608  C  CG  . PRO B 1 365 ? 30.150  -28.340 10.386  1.00 39.21  ? 365  PRO B CG  1 
ATOM   5609  C  CD  . PRO B 1 365 ? 30.103  -29.759 9.959   1.00 38.30  ? 365  PRO B CD  1 
ATOM   5610  N  N   . MET B 1 366 ? 25.719  -28.969 11.116  1.00 39.83  ? 366  MET B N   1 
ATOM   5611  C  CA  . MET B 1 366 ? 24.453  -28.903 10.409  1.00 22.68  ? 366  MET B CA  1 
ATOM   5612  C  C   . MET B 1 366 ? 24.262  -27.477 9.921   1.00 29.73  ? 366  MET B C   1 
ATOM   5613  O  O   . MET B 1 366 ? 24.575  -26.518 10.629  1.00 34.54  ? 366  MET B O   1 
ATOM   5614  C  CB  . MET B 1 366 ? 23.301  -29.304 11.318  1.00 33.69  ? 366  MET B CB  1 
ATOM   5615  C  CG  . MET B 1 366 ? 23.385  -30.725 11.844  1.00 39.16  ? 366  MET B CG  1 
ATOM   5616  S  SD  . MET B 1 366 ? 23.189  -31.958 10.553  1.00 44.91  ? 366  MET B SD  1 
ATOM   5617  C  CE  . MET B 1 366 ? 24.881  -32.476 10.245  1.00 41.18  ? 366  MET B CE  1 
ATOM   5618  N  N   . ARG B 1 367 ? 23.762  -27.347 8.698   1.00 34.60  ? 367  ARG B N   1 
ATOM   5619  C  CA  . ARG B 1 367 ? 23.515  -26.052 8.077   1.00 33.26  ? 367  ARG B CA  1 
ATOM   5620  C  C   . ARG B 1 367 ? 22.026  -25.781 8.211   1.00 36.19  ? 367  ARG B C   1 
ATOM   5621  O  O   . ARG B 1 367 ? 21.207  -26.563 7.722   1.00 52.50  ? 367  ARG B O   1 
ATOM   5622  C  CB  . ARG B 1 367 ? 23.942  -26.080 6.595   1.00 41.66  ? 367  ARG B CB  1 
ATOM   5623  C  CG  . ARG B 1 367 ? 24.098  -24.701 5.912   1.00 57.09  ? 367  ARG B CG  1 
ATOM   5624  C  CD  . ARG B 1 367 ? 22.933  -24.349 4.977   1.00 71.68  ? 367  ARG B CD  1 
ATOM   5625  N  NE  . ARG B 1 367 ? 22.722  -25.384 3.986   1.00 81.96  ? 367  ARG B NE  1 
ATOM   5626  C  CZ  . ARG B 1 367 ? 22.893  -25.288 2.672   1.00 87.64  ? 367  ARG B CZ  1 
ATOM   5627  N  NH1 . ARG B 1 367 ? 22.657  -26.367 1.948   1.00 96.36  ? 367  ARG B NH1 1 
ATOM   5628  N  NH2 . ARG B 1 367 ? 23.275  -24.163 2.078   1.00 83.92  ? 367  ARG B NH2 1 
ATOM   5629  N  N   . THR B 1 368 ? 21.669  -24.690 8.883   1.00 28.29  ? 368  THR B N   1 
ATOM   5630  C  CA  . THR B 1 368 ? 20.261  -24.436 9.153   1.00 26.64  ? 368  THR B CA  1 
ATOM   5631  C  C   . THR B 1 368 ? 19.553  -24.157 7.857   1.00 29.69  ? 368  THR B C   1 
ATOM   5632  O  O   . THR B 1 368 ? 20.188  -23.822 6.850   1.00 18.21  ? 368  THR B O   1 
ATOM   5633  C  CB  . THR B 1 368 ? 20.016  -23.245 10.085  1.00 23.61  ? 368  THR B CB  1 
ATOM   5634  O  OG1 . THR B 1 368 ? 20.389  -22.026 9.424   1.00 25.24  ? 368  THR B OG1 1 
ATOM   5635  C  CG2 . THR B 1 368 ? 20.781  -23.429 11.397  1.00 23.20  ? 368  THR B CG2 1 
ATOM   5636  N  N   . SER B 1 369 ? 18.233  -24.316 7.900   1.00 22.63  ? 369  SER B N   1 
ATOM   5637  C  CA  . SER B 1 369 ? 17.382  -24.094 6.750   1.00 26.21  ? 369  SER B CA  1 
ATOM   5638  C  C   . SER B 1 369 ? 17.049  -22.609 6.653   1.00 35.83  ? 369  SER B C   1 
ATOM   5639  O  O   . SER B 1 369 ? 17.457  -21.819 7.503   1.00 44.32  ? 369  SER B O   1 
ATOM   5640  C  CB  . SER B 1 369 ? 16.101  -24.919 6.886   1.00 28.18  ? 369  SER B CB  1 
ATOM   5641  O  OG  . SER B 1 369 ? 15.334  -24.526 8.012   1.00 21.81  ? 369  SER B OG  1 
ATOM   5642  N  N   . LYS B 1 370 ? 16.306  -22.234 5.619   1.00 37.31  ? 370  LYS B N   1 
ATOM   5643  C  CA  . LYS B 1 370 ? 15.903  -20.840 5.424   1.00 40.15  ? 370  LYS B CA  1 
ATOM   5644  C  C   . LYS B 1 370 ? 15.132  -20.295 6.635   1.00 37.48  ? 370  LYS B C   1 
ATOM   5645  O  O   . LYS B 1 370 ? 15.099  -19.077 6.881   1.00 45.95  ? 370  LYS B O   1 
ATOM   5646  C  CB  . LYS B 1 370 ? 15.091  -20.702 4.130   1.00 17.83  ? 370  LYS B CB  1 
ATOM   5647  C  CG  . LYS B 1 370 ? 15.922  -20.916 2.871   1.00 19.13  ? 370  LYS B CG  1 
ATOM   5648  C  CD  . LYS B 1 370 ? 15.063  -21.255 1.644   1.00 28.62  ? 370  LYS B CD  1 
ATOM   5649  C  CE  . LYS B 1 370 ? 15.939  -21.533 0.406   1.00 35.80  ? 370  LYS B CE  1 
ATOM   5650  N  NZ  . LYS B 1 370 ? 15.177  -21.616 -0.898  1.00 46.68  ? 370  LYS B NZ  1 
ATOM   5651  N  N   . ARG B 1 371 ? 14.523  -21.205 7.390   1.00 27.56  ? 371  ARG B N   1 
ATOM   5652  C  CA  . ARG B 1 371 ? 13.807  -20.840 8.610   1.00 37.49  ? 371  ARG B CA  1 
ATOM   5653  C  C   . ARG B 1 371 ? 14.681  -21.056 9.852   1.00 32.86  ? 371  ARG B C   1 
ATOM   5654  O  O   . ARG B 1 371 ? 14.184  -21.098 10.970  1.00 38.07  ? 371  ARG B O   1 
ATOM   5655  C  CB  . ARG B 1 371 ? 12.515  -21.652 8.736   1.00 31.53  ? 371  ARG B CB  1 
ATOM   5656  C  CG  . ARG B 1 371 ? 11.633  -21.640 7.490   1.00 20.74  ? 371  ARG B CG  1 
ATOM   5657  C  CD  . ARG B 1 371 ? 10.203  -21.905 7.893   1.00 36.91  ? 371  ARG B CD  1 
ATOM   5658  N  NE  . ARG B 1 371 ? 9.502   -22.643 6.868   1.00 60.48  ? 371  ARG B NE  1 
ATOM   5659  C  CZ  . ARG B 1 371 ? 9.024   -23.885 6.962   1.00 73.49  ? 371  ARG B CZ  1 
ATOM   5660  N  NH1 . ARG B 1 371 ? 9.117   -24.608 8.076   1.00 60.98  ? 371  ARG B NH1 1 
ATOM   5661  N  NH2 . ARG B 1 371 ? 8.424   -24.401 5.900   1.00 77.76  ? 371  ARG B NH2 1 
ATOM   5662  N  N   . GLY B 1 372 ? 15.987  -21.191 9.642   1.00 34.07  ? 372  GLY B N   1 
ATOM   5663  C  CA  . GLY B 1 372 ? 16.921  -21.381 10.733  1.00 40.66  ? 372  GLY B CA  1 
ATOM   5664  C  C   . GLY B 1 372 ? 16.698  -22.657 11.530  1.00 38.31  ? 372  GLY B C   1 
ATOM   5665  O  O   . GLY B 1 372 ? 17.045  -22.716 12.711  1.00 35.05  ? 372  GLY B O   1 
ATOM   5666  N  N   . GLU B 1 373 ? 16.127  -23.682 10.902  1.00 28.12  ? 373  GLU B N   1 
ATOM   5667  C  CA  . GLU B 1 373 ? 15.929  -24.949 11.603  1.00 36.95  ? 373  GLU B CA  1 
ATOM   5668  C  C   . GLU B 1 373 ? 17.058  -25.923 11.356  1.00 34.45  ? 373  GLU B C   1 
ATOM   5669  O  O   . GLU B 1 373 ? 17.655  -25.957 10.282  1.00 37.91  ? 373  GLU B O   1 
ATOM   5670  C  CB  . GLU B 1 373 ? 14.608  -25.621 11.229  1.00 32.80  ? 373  GLU B CB  1 
ATOM   5671  C  CG  . GLU B 1 373 ? 13.647  -24.752 10.444  1.00 41.34  ? 373  GLU B CG  1 
ATOM   5672  C  CD  . GLU B 1 373 ? 12.679  -25.603 9.662   1.00 39.39  ? 373  GLU B CD  1 
ATOM   5673  O  OE1 . GLU B 1 373 ? 11.926  -26.357 10.303  1.00 33.54  ? 373  GLU B OE1 1 
ATOM   5674  O  OE2 . GLU B 1 373 ? 12.695  -25.553 8.416   1.00 35.10  ? 373  GLU B OE2 1 
ATOM   5675  N  N   . TYR B 1 374 ? 17.335  -26.729 12.368  1.00 33.66  ? 374  TYR B N   1 
ATOM   5676  C  CA  . TYR B 1 374 ? 18.317  -27.787 12.240  1.00 41.03  ? 374  TYR B CA  1 
ATOM   5677  C  C   . TYR B 1 374 ? 17.835  -29.026 12.988  1.00 36.02  ? 374  TYR B C   1 
ATOM   5678  O  O   . TYR B 1 374 ? 17.088  -28.938 13.958  1.00 37.30  ? 374  TYR B O   1 
ATOM   5679  C  CB  . TYR B 1 374 ? 19.674  -27.325 12.792  1.00 34.69  ? 374  TYR B CB  1 
ATOM   5680  C  CG  . TYR B 1 374 ? 19.733  -27.330 14.302  1.00 36.86  ? 374  TYR B CG  1 
ATOM   5681  C  CD1 . TYR B 1 374 ? 19.373  -26.200 15.044  1.00 33.07  ? 374  TYR B CD1 1 
ATOM   5682  C  CD2 . TYR B 1 374 ? 20.124  -28.471 14.995  1.00 41.29  ? 374  TYR B CD2 1 
ATOM   5683  C  CE1 . TYR B 1 374 ? 19.423  -26.205 16.445  1.00 35.51  ? 374  TYR B CE1 1 
ATOM   5684  C  CE2 . TYR B 1 374 ? 20.170  -28.487 16.393  1.00 38.00  ? 374  TYR B CE2 1 
ATOM   5685  C  CZ  . TYR B 1 374 ? 19.822  -27.355 17.105  1.00 33.79  ? 374  TYR B CZ  1 
ATOM   5686  O  OH  . TYR B 1 374 ? 19.871  -27.378 18.472  1.00 39.52  ? 374  TYR B OH  1 
ATOM   5687  N  N   . TRP B 1 375 ? 18.258  -30.187 12.524  1.00 40.25  ? 375  TRP B N   1 
ATOM   5688  C  CA  . TRP B 1 375 ? 18.035  -31.425 13.255  1.00 32.37  ? 375  TRP B CA  1 
ATOM   5689  C  C   . TRP B 1 375 ? 19.375  -32.095 13.353  1.00 35.45  ? 375  TRP B C   1 
ATOM   5690  O  O   . TRP B 1 375 ? 20.022  -32.329 12.327  1.00 42.82  ? 375  TRP B O   1 
ATOM   5691  C  CB  . TRP B 1 375 ? 17.081  -32.352 12.497  1.00 21.33  ? 375  TRP B CB  1 
ATOM   5692  C  CG  . TRP B 1 375 ? 15.777  -31.726 12.154  1.00 30.12  ? 375  TRP B CG  1 
ATOM   5693  C  CD1 . TRP B 1 375 ? 14.576  -31.946 12.763  1.00 33.57  ? 375  TRP B CD1 1 
ATOM   5694  C  CD2 . TRP B 1 375 ? 15.539  -30.757 11.125  1.00 27.30  ? 375  TRP B CD2 1 
ATOM   5695  N  NE1 . TRP B 1 375 ? 13.594  -31.181 12.160  1.00 39.05  ? 375  TRP B NE1 1 
ATOM   5696  C  CE2 . TRP B 1 375 ? 14.160  -30.444 11.151  1.00 34.73  ? 375  TRP B CE2 1 
ATOM   5697  C  CE3 . TRP B 1 375 ? 16.354  -30.128 10.184  1.00 28.07  ? 375  TRP B CE3 1 
ATOM   5698  C  CZ2 . TRP B 1 375 ? 13.581  -29.526 10.272  1.00 20.48  ? 375  TRP B CZ2 1 
ATOM   5699  C  CZ3 . TRP B 1 375 ? 15.780  -29.224 9.306   1.00 35.43  ? 375  TRP B CZ3 1 
ATOM   5700  C  CH2 . TRP B 1 375 ? 14.404  -28.933 9.353   1.00 23.74  ? 375  TRP B CH2 1 
ATOM   5701  N  N   . ARG B 1 376 ? 19.805  -32.395 14.573  1.00 34.75  ? 376  ARG B N   1 
ATOM   5702  C  CA  . ARG B 1 376 ? 21.063  -33.105 14.755  1.00 32.83  ? 376  ARG B CA  1 
ATOM   5703  C  C   . ARG B 1 376 ? 20.800  -34.469 15.376  1.00 37.54  ? 376  ARG B C   1 
ATOM   5704  O  O   . ARG B 1 376 ? 20.470  -34.581 16.561  1.00 31.15  ? 376  ARG B O   1 
ATOM   5705  C  CB  . ARG B 1 376 ? 22.063  -32.279 15.568  1.00 17.30  ? 376  ARG B CB  1 
ATOM   5706  C  CG  . ARG B 1 376 ? 23.403  -32.960 15.784  1.00 31.16  ? 376  ARG B CG  1 
ATOM   5707  C  CD  . ARG B 1 376 ? 24.167  -33.191 14.489  1.00 36.73  ? 376  ARG B CD  1 
ATOM   5708  N  NE  . ARG B 1 376 ? 25.434  -33.883 14.740  1.00 47.21  ? 376  ARG B NE  1 
ATOM   5709  C  CZ  . ARG B 1 376 ? 26.233  -34.376 13.798  1.00 40.22  ? 376  ARG B CZ  1 
ATOM   5710  N  NH1 . ARG B 1 376 ? 25.906  -34.261 12.527  1.00 64.38  ? 376  ARG B NH1 1 
ATOM   5711  N  NH2 . ARG B 1 376 ? 27.359  -34.985 14.125  1.00 45.07  ? 376  ARG B NH2 1 
ATOM   5712  N  N   . LEU B 1 377 ? 20.907  -35.501 14.545  1.00 40.30  ? 377  LEU B N   1 
ATOM   5713  C  CA  . LEU B 1 377 ? 20.677  -36.873 14.979  1.00 32.45  ? 377  LEU B CA  1 
ATOM   5714  C  C   . LEU B 1 377 ? 21.784  -37.215 15.933  1.00 32.12  ? 377  LEU B C   1 
ATOM   5715  O  O   . LEU B 1 377 ? 22.955  -37.014 15.609  1.00 36.60  ? 377  LEU B O   1 
ATOM   5716  C  CB  . LEU B 1 377 ? 20.719  -37.831 13.785  1.00 20.74  ? 377  LEU B CB  1 
ATOM   5717  C  CG  . LEU B 1 377 ? 19.770  -37.529 12.628  1.00 24.92  ? 377  LEU B CG  1 
ATOM   5718  C  CD1 . LEU B 1 377 ? 19.819  -38.635 11.595  1.00 14.51  ? 377  LEU B CD1 1 
ATOM   5719  C  CD2 . LEU B 1 377 ? 18.337  -37.332 13.144  1.00 21.80  ? 377  LEU B CD2 1 
ATOM   5720  N  N   . LEU B 1 378 ? 21.431  -37.729 17.106  1.00 33.96  ? 378  LEU B N   1 
ATOM   5721  C  CA  . LEU B 1 378 ? 22.446  -38.097 18.089  1.00 34.48  ? 378  LEU B CA  1 
ATOM   5722  C  C   . LEU B 1 378 ? 22.147  -39.404 18.818  1.00 33.38  ? 378  LEU B C   1 
ATOM   5723  O  O   . LEU B 1 378 ? 20.994  -39.718 19.129  1.00 43.08  ? 378  LEU B O   1 
ATOM   5724  C  CB  . LEU B 1 378 ? 22.672  -36.963 19.103  1.00 31.47  ? 378  LEU B CB  1 
ATOM   5725  C  CG  . LEU B 1 378 ? 23.332  -35.655 18.628  1.00 24.07  ? 378  LEU B CG  1 
ATOM   5726  C  CD1 . LEU B 1 378 ? 23.008  -34.520 19.581  1.00 29.13  ? 378  LEU B CD1 1 
ATOM   5727  C  CD2 . LEU B 1 378 ? 24.849  -35.784 18.438  1.00 15.06  ? 378  LEU B CD2 1 
ATOM   5728  N  N   . THR B 1 379 ? 23.209  -40.166 19.062  1.00 45.30  ? 379  THR B N   1 
ATOM   5729  C  CA  . THR B 1 379 ? 23.185  -41.322 19.948  1.00 41.97  ? 379  THR B CA  1 
ATOM   5730  C  C   . THR B 1 379 ? 22.919  -40.820 21.363  1.00 46.89  ? 379  THR B C   1 
ATOM   5731  O  O   . THR B 1 379 ? 23.281  -39.686 21.686  1.00 42.36  ? 379  THR B O   1 
ATOM   5732  C  CB  . THR B 1 379 ? 24.555  -42.002 19.920  1.00 44.26  ? 379  THR B CB  1 
ATOM   5733  O  OG1 . THR B 1 379 ? 24.739  -42.638 18.654  1.00 41.61  ? 379  THR B OG1 1 
ATOM   5734  C  CG2 . THR B 1 379 ? 24.678  -43.033 21.019  1.00 63.37  ? 379  THR B CG2 1 
ATOM   5735  N  N   . PRO B 1 380 ? 22.266  -41.637 22.209  1.00 42.52  ? 380  PRO B N   1 
ATOM   5736  C  CA  . PRO B 1 380 ? 22.097  -41.230 23.611  1.00 42.68  ? 380  PRO B CA  1 
ATOM   5737  C  C   . PRO B 1 380 ? 23.424  -40.788 24.234  1.00 42.56  ? 380  PRO B C   1 
ATOM   5738  O  O   . PRO B 1 380 ? 24.476  -41.326 23.902  1.00 29.40  ? 380  PRO B O   1 
ATOM   5739  C  CB  . PRO B 1 380 ? 21.593  -42.504 24.276  1.00 18.95  ? 380  PRO B CB  1 
ATOM   5740  C  CG  . PRO B 1 380 ? 20.826  -43.190 23.199  1.00 36.33  ? 380  PRO B CG  1 
ATOM   5741  C  CD  . PRO B 1 380 ? 21.546  -42.888 21.909  1.00 35.79  ? 380  PRO B CD  1 
ATOM   5742  N  N   . GLY B 1 381 ? 23.372  -39.798 25.117  1.00 42.96  ? 381  GLY B N   1 
ATOM   5743  C  CA  . GLY B 1 381 ? 24.575  -39.285 25.762  1.00 34.14  ? 381  GLY B CA  1 
ATOM   5744  C  C   . GLY B 1 381 ? 24.426  -37.818 26.131  1.00 38.90  ? 381  GLY B C   1 
ATOM   5745  O  O   . GLY B 1 381 ? 23.334  -37.260 26.022  1.00 45.01  ? 381  GLY B O   1 
ATOM   5746  N  N   . LEU B 1 382 ? 25.506  -37.181 26.574  1.00 36.51  ? 382  LEU B N   1 
ATOM   5747  C  CA  . LEU B 1 382 ? 25.447  -35.741 26.816  1.00 44.98  ? 382  LEU B CA  1 
ATOM   5748  C  C   . LEU B 1 382 ? 26.466  -34.992 25.981  1.00 49.33  ? 382  LEU B C   1 
ATOM   5749  O  O   . LEU B 1 382 ? 27.615  -35.429 25.825  1.00 38.44  ? 382  LEU B O   1 
ATOM   5750  C  CB  . LEU B 1 382 ? 25.596  -35.391 28.296  1.00 52.64  ? 382  LEU B CB  1 
ATOM   5751  C  CG  . LEU B 1 382 ? 26.958  -35.516 28.963  1.00 66.19  ? 382  LEU B CG  1 
ATOM   5752  C  CD1 . LEU B 1 382 ? 27.867  -34.370 28.564  1.00 72.35  ? 382  LEU B CD1 1 
ATOM   5753  C  CD2 . LEU B 1 382 ? 26.747  -35.523 30.464  1.00 78.75  ? 382  LEU B CD2 1 
ATOM   5754  N  N   . TYR B 1 383 ? 26.025  -33.852 25.455  1.00 49.47  ? 383  TYR B N   1 
ATOM   5755  C  CA  . TYR B 1 383 ? 26.790  -33.094 24.474  1.00 41.71  ? 383  TYR B CA  1 
ATOM   5756  C  C   . TYR B 1 383 ? 26.803  -31.593 24.768  1.00 48.07  ? 383  TYR B C   1 
ATOM   5757  O  O   . TYR B 1 383 ? 25.848  -31.029 25.324  1.00 55.03  ? 383  TYR B O   1 
ATOM   5758  C  CB  . TYR B 1 383 ? 26.212  -33.311 23.075  1.00 40.49  ? 383  TYR B CB  1 
ATOM   5759  C  CG  . TYR B 1 383 ? 25.991  -34.761 22.685  1.00 45.94  ? 383  TYR B CG  1 
ATOM   5760  C  CD1 . TYR B 1 383 ? 24.945  -35.502 23.226  1.00 45.17  ? 383  TYR B CD1 1 
ATOM   5761  C  CD2 . TYR B 1 383 ? 26.807  -35.377 21.747  1.00 43.69  ? 383  TYR B CD2 1 
ATOM   5762  C  CE1 . TYR B 1 383 ? 24.736  -36.822 22.859  1.00 42.23  ? 383  TYR B CE1 1 
ATOM   5763  C  CE2 . TYR B 1 383 ? 26.598  -36.696 21.369  1.00 43.40  ? 383  TYR B CE2 1 
ATOM   5764  C  CZ  . TYR B 1 383 ? 25.565  -37.413 21.930  1.00 46.65  ? 383  TYR B CZ  1 
ATOM   5765  O  OH  . TYR B 1 383 ? 25.372  -38.722 21.556  1.00 42.68  ? 383  TYR B OH  1 
ATOM   5766  N  N   . SER B 1 384 ? 27.895  -30.947 24.385  1.00 37.48  ? 384  SER B N   1 
ATOM   5767  C  CA  . SER B 1 384 ? 27.948  -29.501 24.380  1.00 39.80  ? 384  SER B CA  1 
ATOM   5768  C  C   . SER B 1 384 ? 27.754  -29.021 22.947  1.00 57.17  ? 384  SER B C   1 
ATOM   5769  O  O   . SER B 1 384 ? 28.651  -29.178 22.094  1.00 42.45  ? 384  SER B O   1 
ATOM   5770  C  CB  . SER B 1 384 ? 29.272  -29.007 24.946  1.00 39.56  ? 384  SER B CB  1 
ATOM   5771  O  OG  . SER B 1 384 ? 29.201  -28.902 26.360  1.00 74.13  ? 384  SER B OG  1 
ATOM   5772  N  N   . VAL B 1 385 ? 26.575  -28.454 22.688  1.00 52.21  ? 385  VAL B N   1 
ATOM   5773  C  CA  . VAL B 1 385 ? 26.235  -27.974 21.357  1.00 47.80  ? 385  VAL B CA  1 
ATOM   5774  C  C   . VAL B 1 385 ? 26.399  -26.458 21.260  1.00 48.69  ? 385  VAL B C   1 
ATOM   5775  O  O   . VAL B 1 385 ? 26.149  -25.739 22.233  1.00 38.49  ? 385  VAL B O   1 
ATOM   5776  C  CB  . VAL B 1 385 ? 24.799  -28.349 20.983  1.00 35.68  ? 385  VAL B CB  1 
ATOM   5777  C  CG1 . VAL B 1 385 ? 24.654  -28.334 19.476  1.00 37.43  ? 385  VAL B CG1 1 
ATOM   5778  C  CG2 . VAL B 1 385 ? 24.452  -29.728 21.536  1.00 34.62  ? 385  VAL B CG2 1 
ATOM   5779  N  N   . HIS B 1 386 ? 26.840  -25.982 20.094  1.00 36.64  ? 386  HIS B N   1 
ATOM   5780  C  CA  . HIS B 1 386 ? 26.914  -24.543 19.837  1.00 40.48  ? 386  HIS B CA  1 
ATOM   5781  C  C   . HIS B 1 386 ? 26.617  -24.197 18.372  1.00 38.18  ? 386  HIS B C   1 
ATOM   5782  O  O   . HIS B 1 386 ? 26.642  -25.065 17.506  1.00 29.44  ? 386  HIS B O   1 
ATOM   5783  C  CB  . HIS B 1 386 ? 28.232  -23.899 20.361  1.00 58.66  ? 386  HIS B CB  1 
ATOM   5784  C  CG  . HIS B 1 386 ? 29.451  -24.160 19.515  1.00 68.88  ? 386  HIS B CG  1 
ATOM   5785  N  ND1 . HIS B 1 386 ? 29.418  -24.852 18.324  1.00 77.49  ? 386  HIS B ND1 1 
ATOM   5786  C  CD2 . HIS B 1 386 ? 30.747  -23.799 19.700  1.00 66.69  ? 386  HIS B CD2 1 
ATOM   5787  C  CE1 . HIS B 1 386 ? 30.639  -24.911 17.815  1.00 53.95  ? 386  HIS B CE1 1 
ATOM   5788  N  NE2 . HIS B 1 386 ? 31.462  -24.287 18.633  1.00 41.65  ? 386  HIS B NE2 1 
ATOM   5789  N  N   . ALA B 1 387 ? 26.303  -22.930 18.121  1.00 37.47  ? 387  ALA B N   1 
ATOM   5790  C  CA  . ALA B 1 387 ? 25.993  -22.466 16.781  1.00 39.24  ? 387  ALA B CA  1 
ATOM   5791  C  C   . ALA B 1 387 ? 26.831  -21.247 16.437  1.00 49.46  ? 387  ALA B C   1 
ATOM   5792  O  O   . ALA B 1 387 ? 27.194  -20.459 17.314  1.00 57.71  ? 387  ALA B O   1 
ATOM   5793  C  CB  . ALA B 1 387 ? 24.534  -22.126 16.676  1.00 42.93  ? 387  ALA B CB  1 
ATOM   5794  N  N   . SER B 1 388 ? 27.121  -21.080 15.157  1.00 35.88  ? 388  SER B N   1 
ATOM   5795  C  CA  . SER B 1 388 ? 27.871  -19.926 14.711  1.00 42.09  ? 388  SER B CA  1 
ATOM   5796  C  C   . SER B 1 388 ? 27.364  -19.524 13.334  1.00 42.18  ? 388  SER B C   1 
ATOM   5797  O  O   . SER B 1 388 ? 26.682  -20.298 12.671  1.00 32.02  ? 388  SER B O   1 
ATOM   5798  C  CB  . SER B 1 388 ? 29.362  -20.258 14.673  1.00 38.28  ? 388  SER B CB  1 
ATOM   5799  O  OG  . SER B 1 388 ? 29.600  -21.389 13.860  1.00 47.61  ? 388  SER B OG  1 
ATOM   5800  N  N   . ALA B 1 389 ? 27.688  -18.308 12.912  1.00 48.31  ? 389  ALA B N   1 
ATOM   5801  C  CA  . ALA B 1 389 ? 27.332  -17.850 11.573  1.00 44.90  ? 389  ALA B CA  1 
ATOM   5802  C  C   . ALA B 1 389 ? 28.126  -16.614 11.192  1.00 46.31  ? 389  ALA B C   1 
ATOM   5803  O  O   . ALA B 1 389 ? 28.483  -15.814 12.052  1.00 57.26  ? 389  ALA B O   1 
ATOM   5804  C  CB  . ALA B 1 389 ? 25.841  -17.574 11.481  1.00 24.78  ? 389  ALA B CB  1 
ATOM   5805  N  N   . PHE B 1 390 ? 28.407  -16.463 9.905   1.00 47.28  ? 390  PHE B N   1 
ATOM   5806  C  CA  . PHE B 1 390 ? 29.181  -15.325 9.446   1.00 61.42  ? 390  PHE B CA  1 
ATOM   5807  C  C   . PHE B 1 390 ? 28.426  -14.055 9.779   1.00 58.44  ? 390  PHE B C   1 
ATOM   5808  O  O   . PHE B 1 390 ? 27.229  -13.960 9.528   1.00 55.57  ? 390  PHE B O   1 
ATOM   5809  C  CB  . PHE B 1 390 ? 29.420  -15.410 7.943   1.00 75.42  ? 390  PHE B CB  1 
ATOM   5810  C  CG  . PHE B 1 390 ? 30.064  -14.187 7.365   1.00 96.72  ? 390  PHE B CG  1 
ATOM   5811  C  CD1 . PHE B 1 390 ? 29.332  -13.315 6.573   1.00 102.99 ? 390  PHE B CD1 1 
ATOM   5812  C  CD2 . PHE B 1 390 ? 31.397  -13.897 7.624   1.00 104.80 ? 390  PHE B CD2 1 
ATOM   5813  C  CE1 . PHE B 1 390 ? 29.919  -12.184 6.036   1.00 107.50 ? 390  PHE B CE1 1 
ATOM   5814  C  CE2 . PHE B 1 390 ? 31.989  -12.763 7.090   1.00 109.25 ? 390  PHE B CE2 1 
ATOM   5815  C  CZ  . PHE B 1 390 ? 31.248  -11.907 6.294   1.00 110.02 ? 390  PHE B CZ  1 
ATOM   5816  N  N   . GLY B 1 391 ? 29.125  -13.084 10.354  1.00 52.18  ? 391  GLY B N   1 
ATOM   5817  C  CA  . GLY B 1 391 ? 28.496  -11.838 10.752  1.00 51.87  ? 391  GLY B CA  1 
ATOM   5818  C  C   . GLY B 1 391 ? 27.873  -11.936 12.133  1.00 53.19  ? 391  GLY B C   1 
ATOM   5819  O  O   . GLY B 1 391 ? 27.283  -10.977 12.637  1.00 44.94  ? 391  GLY B O   1 
ATOM   5820  N  N   . TYR B 1 392 ? 28.013  -13.104 12.751  1.00 60.75  ? 392  TYR B N   1 
ATOM   5821  C  CA  . TYR B 1 392 ? 27.476  -13.328 14.084  1.00 55.79  ? 392  TYR B CA  1 
ATOM   5822  C  C   . TYR B 1 392 ? 28.513  -13.875 15.048  1.00 59.59  ? 392  TYR B C   1 
ATOM   5823  O  O   . TYR B 1 392 ? 29.318  -14.740 14.703  1.00 64.11  ? 392  TYR B O   1 
ATOM   5824  C  CB  . TYR B 1 392 ? 26.287  -14.280 14.030  1.00 50.82  ? 392  TYR B CB  1 
ATOM   5825  C  CG  . TYR B 1 392 ? 25.065  -13.682 13.380  1.00 60.62  ? 392  TYR B CG  1 
ATOM   5826  C  CD1 . TYR B 1 392 ? 24.060  -13.100 14.147  1.00 66.39  ? 392  TYR B CD1 1 
ATOM   5827  C  CD2 . TYR B 1 392 ? 24.917  -13.694 11.997  1.00 49.39  ? 392  TYR B CD2 1 
ATOM   5828  C  CE1 . TYR B 1 392 ? 22.935  -12.553 13.555  1.00 62.88  ? 392  TYR B CE1 1 
ATOM   5829  C  CE2 . TYR B 1 392 ? 23.799  -13.151 11.392  1.00 50.85  ? 392  TYR B CE2 1 
ATOM   5830  C  CZ  . TYR B 1 392 ? 22.811  -12.583 12.176  1.00 63.51  ? 392  TYR B CZ  1 
ATOM   5831  O  OH  . TYR B 1 392 ? 21.696  -12.043 11.582  1.00 63.61  ? 392  TYR B OH  1 
ATOM   5832  N  N   . GLN B 1 393 ? 28.472  -13.364 16.272  1.00 66.23  ? 393  GLN B N   1 
ATOM   5833  C  CA  . GLN B 1 393 ? 29.275  -13.894 17.356  1.00 55.18  ? 393  GLN B CA  1 
ATOM   5834  C  C   . GLN B 1 393 ? 28.836  -15.327 17.656  1.00 56.29  ? 393  GLN B C   1 
ATOM   5835  O  O   . GLN B 1 393 ? 27.647  -15.605 17.876  1.00 46.27  ? 393  GLN B O   1 
ATOM   5836  C  CB  . GLN B 1 393 ? 29.151  -12.987 18.588  1.00 37.82  ? 393  GLN B CB  1 
ATOM   5837  C  CG  . GLN B 1 393 ? 29.454  -11.514 18.265  1.00 51.98  ? 393  GLN B CG  1 
ATOM   5838  C  CD  . GLN B 1 393 ? 29.509  -10.623 19.500  1.00 72.28  ? 393  GLN B CD  1 
ATOM   5839  O  OE1 . GLN B 1 393 ? 29.072  -11.017 20.585  1.00 74.34  ? 393  GLN B OE1 1 
ATOM   5840  N  NE2 . GLN B 1 393 ? 30.047  -9.413  19.338  1.00 71.48  ? 393  GLN B NE2 1 
ATOM   5841  N  N   . THR B 1 394 ? 29.804  -16.236 17.636  1.00 58.50  ? 394  THR B N   1 
ATOM   5842  C  CA  . THR B 1 394 ? 29.535  -17.641 17.895  1.00 57.57  ? 394  THR B CA  1 
ATOM   5843  C  C   . THR B 1 394 ? 28.965  -17.835 19.292  1.00 55.74  ? 394  THR B C   1 
ATOM   5844  O  O   . THR B 1 394 ? 29.645  -17.571 20.280  1.00 60.46  ? 394  THR B O   1 
ATOM   5845  C  CB  . THR B 1 394 ? 30.810  -18.478 17.769  1.00 54.91  ? 394  THR B CB  1 
ATOM   5846  O  OG1 . THR B 1 394 ? 31.344  -18.337 16.443  1.00 54.08  ? 394  THR B OG1 1 
ATOM   5847  C  CG2 . THR B 1 394 ? 30.508  -19.952 18.050  1.00 59.44  ? 394  THR B CG2 1 
ATOM   5848  N  N   . SER B 1 395 ? 27.720  -18.302 19.360  1.00 46.75  ? 395  SER B N   1 
ATOM   5849  C  CA  . SER B 1 395 ? 27.010  -18.491 20.621  1.00 42.95  ? 395  SER B CA  1 
ATOM   5850  C  C   . SER B 1 395 ? 27.838  -19.178 21.695  1.00 52.16  ? 395  SER B C   1 
ATOM   5851  O  O   . SER B 1 395 ? 28.810  -19.872 21.402  1.00 67.00  ? 395  SER B O   1 
ATOM   5852  C  CB  . SER B 1 395 ? 25.758  -19.329 20.389  1.00 41.68  ? 395  SER B CB  1 
ATOM   5853  O  OG  . SER B 1 395 ? 26.112  -20.672 20.104  1.00 47.86  ? 395  SER B OG  1 
ATOM   5854  N  N   . ALA B 1 396 ? 27.435  -19.000 22.946  1.00 42.10  ? 396  ALA B N   1 
ATOM   5855  C  CA  . ALA B 1 396 ? 28.002  -19.789 24.036  1.00 41.40  ? 396  ALA B CA  1 
ATOM   5856  C  C   . ALA B 1 396 ? 27.492  -21.223 23.913  1.00 53.52  ? 396  ALA B C   1 
ATOM   5857  O  O   . ALA B 1 396 ? 26.483  -21.466 23.246  1.00 68.59  ? 396  ALA B O   1 
ATOM   5858  C  CB  . ALA B 1 396 ? 27.608  -19.201 25.364  1.00 36.00  ? 396  ALA B CB  1 
ATOM   5859  N  N   . PRO B 1 397 ? 28.185  -22.180 24.550  1.00 41.49  ? 397  PRO B N   1 
ATOM   5860  C  CA  . PRO B 1 397 ? 27.841  -23.598 24.391  1.00 40.47  ? 397  PRO B CA  1 
ATOM   5861  C  C   . PRO B 1 397 ? 26.752  -24.052 25.342  1.00 44.07  ? 397  PRO B C   1 
ATOM   5862  O  O   . PRO B 1 397 ? 26.729  -23.635 26.489  1.00 58.97  ? 397  PRO B O   1 
ATOM   5863  C  CB  . PRO B 1 397 ? 29.153  -24.329 24.731  1.00 42.22  ? 397  PRO B CB  1 
ATOM   5864  C  CG  . PRO B 1 397 ? 30.195  -23.256 24.912  1.00 48.98  ? 397  PRO B CG  1 
ATOM   5865  C  CD  . PRO B 1 397 ? 29.440  -22.015 25.291  1.00 50.11  ? 397  PRO B CD  1 
ATOM   5866  N  N   . GLN B 1 398 ? 25.855  -24.903 24.867  1.00 59.45  ? 398  GLN B N   1 
ATOM   5867  C  CA  . GLN B 1 398 ? 24.821  -25.462 25.727  1.00 53.59  ? 398  GLN B CA  1 
ATOM   5868  C  C   . GLN B 1 398 ? 25.021  -26.969 25.869  1.00 44.36  ? 398  GLN B C   1 
ATOM   5869  O  O   . GLN B 1 398 ? 25.356  -27.675 24.906  1.00 47.63  ? 398  GLN B O   1 
ATOM   5870  C  CB  . GLN B 1 398 ? 23.420  -25.125 25.190  1.00 47.90  ? 398  GLN B CB  1 
ATOM   5871  C  CG  . GLN B 1 398 ? 23.094  -23.625 25.207  1.00 43.31  ? 398  GLN B CG  1 
ATOM   5872  C  CD  . GLN B 1 398 ? 21.780  -23.304 24.530  1.00 49.84  ? 398  GLN B CD  1 
ATOM   5873  O  OE1 . GLN B 1 398 ? 20.849  -24.106 24.563  1.00 53.37  ? 398  GLN B OE1 1 
ATOM   5874  N  NE2 . GLN B 1 398 ? 21.697  -22.127 23.908  1.00 47.06  ? 398  GLN B NE2 1 
ATOM   5875  N  N   . GLN B 1 399 ? 24.832  -27.444 27.087  1.00 39.87  ? 399  GLN B N   1 
ATOM   5876  C  CA  . GLN B 1 399 ? 24.974  -28.856 27.404  1.00 57.62  ? 399  GLN B CA  1 
ATOM   5877  C  C   . GLN B 1 399 ? 23.594  -29.506 27.399  1.00 63.79  ? 399  GLN B C   1 
ATOM   5878  O  O   . GLN B 1 399 ? 22.643  -28.951 27.950  1.00 68.49  ? 399  GLN B O   1 
ATOM   5879  C  CB  . GLN B 1 399 ? 25.633  -29.001 28.777  1.00 65.41  ? 399  GLN B CB  1 
ATOM   5880  C  CG  . GLN B 1 399 ? 25.424  -30.324 29.469  1.00 77.34  ? 399  GLN B CG  1 
ATOM   5881  C  CD  . GLN B 1 399 ? 25.677  -30.210 30.950  1.00 92.23  ? 399  GLN B CD  1 
ATOM   5882  O  OE1 . GLN B 1 399 ? 24.924  -29.552 31.661  1.00 98.31  ? 399  GLN B OE1 1 
ATOM   5883  N  NE2 . GLN B 1 399 ? 26.744  -30.838 31.424  1.00 97.14  ? 399  GLN B NE2 1 
ATOM   5884  N  N   . VAL B 1 400 ? 23.479  -30.670 26.766  1.00 56.28  ? 400  VAL B N   1 
ATOM   5885  C  CA  . VAL B 1 400 ? 22.190  -31.358 26.675  1.00 46.11  ? 400  VAL B CA  1 
ATOM   5886  C  C   . VAL B 1 400 ? 22.308  -32.862 26.889  1.00 42.30  ? 400  VAL B C   1 
ATOM   5887  O  O   . VAL B 1 400 ? 23.205  -33.518 26.359  1.00 38.88  ? 400  VAL B O   1 
ATOM   5888  C  CB  . VAL B 1 400 ? 21.499  -31.111 25.310  1.00 59.36  ? 400  VAL B CB  1 
ATOM   5889  C  CG1 . VAL B 1 400 ? 22.274  -31.781 24.160  1.00 44.59  ? 400  VAL B CG1 1 
ATOM   5890  C  CG2 . VAL B 1 400 ? 20.060  -31.618 25.353  1.00 72.14  ? 400  VAL B CG2 1 
ATOM   5891  N  N   . ARG B 1 401 ? 21.395  -33.415 27.671  1.00 46.85  ? 401  ARG B N   1 
ATOM   5892  C  CA  . ARG B 1 401 ? 21.401  -34.853 27.883  1.00 54.20  ? 401  ARG B CA  1 
ATOM   5893  C  C   . ARG B 1 401 ? 20.481  -35.525 26.881  1.00 49.94  ? 401  ARG B C   1 
ATOM   5894  O  O   . ARG B 1 401 ? 19.261  -35.533 27.049  1.00 52.54  ? 401  ARG B O   1 
ATOM   5895  C  CB  . ARG B 1 401 ? 20.984  -35.201 29.310  1.00 57.24  ? 401  ARG B CB  1 
ATOM   5896  C  CG  . ARG B 1 401 ? 20.879  -36.701 29.579  1.00 69.92  ? 401  ARG B CG  1 
ATOM   5897  C  CD  . ARG B 1 401 ? 20.744  -37.016 31.090  1.00 81.68  ? 401  ARG B CD  1 
ATOM   5898  N  NE  . ARG B 1 401 ? 19.763  -36.159 31.740  1.00 85.47  ? 401  ARG B NE  1 
ATOM   5899  C  CZ  . ARG B 1 401 ? 19.985  -35.405 32.809  1.00 92.68  ? 401  ARG B CZ  1 
ATOM   5900  N  NH1 . ARG B 1 401 ? 19.001  -34.660 33.284  1.00 103.20 ? 401  ARG B NH1 1 
ATOM   5901  N  NH2 . ARG B 1 401 ? 21.166  -35.394 33.409  1.00 92.41  ? 401  ARG B NH2 1 
ATOM   5902  N  N   . VAL B 1 402 ? 21.072  -36.074 25.826  1.00 47.03  ? 402  VAL B N   1 
ATOM   5903  C  CA  . VAL B 1 402 ? 20.297  -36.791 24.822  1.00 40.19  ? 402  VAL B CA  1 
ATOM   5904  C  C   . VAL B 1 402 ? 19.932  -38.195 25.277  1.00 56.14  ? 402  VAL B C   1 
ATOM   5905  O  O   . VAL B 1 402 ? 20.763  -39.119 25.248  1.00 33.78  ? 402  VAL B O   1 
ATOM   5906  C  CB  . VAL B 1 402 ? 21.022  -36.888 23.487  1.00 21.16  ? 402  VAL B CB  1 
ATOM   5907  C  CG1 . VAL B 1 402 ? 20.216  -37.740 22.524  1.00 21.32  ? 402  VAL B CG1 1 
ATOM   5908  C  CG2 . VAL B 1 402 ? 21.231  -35.520 22.927  1.00 20.66  ? 402  VAL B CG2 1 
ATOM   5909  N  N   . THR B 1 403 ? 18.686  -38.309 25.728  1.00 73.20  ? 403  THR B N   1 
ATOM   5910  C  CA  . THR B 1 403 ? 17.994  -39.569 25.914  1.00 70.62  ? 403  THR B CA  1 
ATOM   5911  C  C   . THR B 1 403 ? 17.025  -39.647 24.739  1.00 70.80  ? 403  THR B C   1 
ATOM   5912  O  O   . THR B 1 403 ? 16.350  -38.655 24.418  1.00 80.52  ? 403  THR B O   1 
ATOM   5913  C  CB  . THR B 1 403 ? 17.201  -39.573 27.248  1.00 70.06  ? 403  THR B CB  1 
ATOM   5914  O  OG1 . THR B 1 403 ? 16.404  -40.759 27.336  1.00 90.64  ? 403  THR B OG1 1 
ATOM   5915  C  CG2 . THR B 1 403 ? 16.277  -38.351 27.343  1.00 62.33  ? 403  THR B CG2 1 
ATOM   5916  N  N   . ASN B 1 404 ? 16.958  -40.793 24.069  1.00 44.77  ? 404  ASN B N   1 
ATOM   5917  C  CA  . ASN B 1 404 ? 16.043  -40.894 22.923  1.00 51.62  ? 404  ASN B CA  1 
ATOM   5918  C  C   . ASN B 1 404 ? 14.723  -41.556 23.296  1.00 53.87  ? 404  ASN B C   1 
ATOM   5919  O  O   . ASN B 1 404 ? 14.149  -42.306 22.509  1.00 48.75  ? 404  ASN B O   1 
ATOM   5920  C  CB  . ASN B 1 404 ? 16.697  -41.576 21.705  1.00 38.49  ? 404  ASN B CB  1 
ATOM   5921  C  CG  . ASN B 1 404 ? 17.786  -40.713 21.059  1.00 51.16  ? 404  ASN B CG  1 
ATOM   5922  O  OD1 . ASN B 1 404 ? 17.628  -39.502 20.915  1.00 49.22  ? 404  ASN B OD1 1 
ATOM   5923  N  ND2 . ASN B 1 404 ? 18.899  -41.337 20.679  1.00 62.99  ? 404  ASN B ND2 1 
ATOM   5924  N  N   . ASP B 1 405 ? 14.241  -41.258 24.502  1.00 55.36  ? 405  ASP B N   1 
ATOM   5925  C  CA  . ASP B 1 405 ? 13.031  -41.887 25.023  1.00 58.10  ? 405  ASP B CA  1 
ATOM   5926  C  C   . ASP B 1 405 ? 11.758  -41.197 24.537  1.00 53.81  ? 405  ASP B C   1 
ATOM   5927  O  O   . ASP B 1 405 ? 10.698  -41.823 24.440  1.00 52.31  ? 405  ASP B O   1 
ATOM   5928  C  CB  . ASP B 1 405 ? 13.071  -41.922 26.554  1.00 60.97  ? 405  ASP B CB  1 
ATOM   5929  C  CG  . ASP B 1 405 ? 14.176  -42.835 27.095  1.00 55.06  ? 405  ASP B CG  1 
ATOM   5930  O  OD1 . ASP B 1 405 ? 14.540  -43.791 26.378  1.00 28.58  ? 405  ASP B OD1 1 
ATOM   5931  O  OD2 . ASP B 1 405 ? 14.676  -42.601 28.233  1.00 39.49  ? 405  ASP B OD2 1 
ATOM   5932  N  N   . ASN B 1 406 ? 11.863  -39.908 24.233  1.00 39.91  ? 406  ASN B N   1 
ATOM   5933  C  CA  . ASN B 1 406 ? 10.694  -39.140 23.839  1.00 56.40  ? 406  ASN B CA  1 
ATOM   5934  C  C   . ASN B 1 406 ? 10.456  -39.152 22.333  1.00 71.17  ? 406  ASN B C   1 
ATOM   5935  O  O   . ASN B 1 406 ? 11.402  -39.214 21.546  1.00 81.28  ? 406  ASN B O   1 
ATOM   5936  C  CB  . ASN B 1 406 ? 10.799  -37.708 24.343  1.00 60.99  ? 406  ASN B CB  1 
ATOM   5937  C  CG  . ASN B 1 406 ? 9.472   -36.983 24.293  1.00 62.97  ? 406  ASN B CG  1 
ATOM   5938  O  OD1 . ASN B 1 406 ? 8.766   -36.890 25.307  1.00 64.70  ? 406  ASN B OD1 1 
ATOM   5939  N  ND2 . ASN B 1 406 ? 9.117   -36.468 23.110  1.00 32.15  ? 406  ASN B ND2 1 
ATOM   5940  N  N   . GLN B 1 407 ? 9.186   -39.074 21.938  1.00 70.95  ? 407  GLN B N   1 
ATOM   5941  C  CA  . GLN B 1 407 ? 8.799   -39.205 20.529  1.00 75.37  ? 407  GLN B CA  1 
ATOM   5942  C  C   . GLN B 1 407 ? 9.531   -38.277 19.553  1.00 62.35  ? 407  GLN B C   1 
ATOM   5943  O  O   . GLN B 1 407 ? 9.732   -38.636 18.389  1.00 61.06  ? 407  GLN B O   1 
ATOM   5944  C  CB  . GLN B 1 407 ? 7.281   -39.038 20.359  1.00 80.33  ? 407  GLN B CB  1 
ATOM   5945  C  CG  . GLN B 1 407 ? 6.501   -40.332 20.436  1.00 75.39  ? 407  GLN B CG  1 
ATOM   5946  C  CD  . GLN B 1 407 ? 5.011   -40.120 20.320  1.00 85.30  ? 407  GLN B CD  1 
ATOM   5947  O  OE1 . GLN B 1 407 ? 4.505   -39.040 20.617  1.00 87.60  ? 407  GLN B OE1 1 
ATOM   5948  N  NE2 . GLN B 1 407 ? 4.295   -41.153 19.894  1.00 93.35  ? 407  GLN B NE2 1 
ATOM   5949  N  N   . GLU B 1 408 ? 9.913   -37.088 20.017  1.00 49.72  ? 408  GLU B N   1 
ATOM   5950  C  CA  . GLU B 1 408 ? 10.533  -36.103 19.131  1.00 49.56  ? 408  GLU B CA  1 
ATOM   5951  C  C   . GLU B 1 408 ? 11.798  -35.487 19.701  1.00 48.83  ? 408  GLU B C   1 
ATOM   5952  O  O   . GLU B 1 408 ? 11.966  -35.405 20.910  1.00 58.03  ? 408  GLU B O   1 
ATOM   5953  C  CB  . GLU B 1 408 ? 9.529   -35.014 18.731  1.00 54.54  ? 408  GLU B CB  1 
ATOM   5954  C  CG  . GLU B 1 408 ? 8.399   -35.545 17.852  1.00 62.32  ? 408  GLU B CG  1 
ATOM   5955  C  CD  . GLU B 1 408 ? 7.454   -34.463 17.375  1.00 63.69  ? 408  GLU B CD  1 
ATOM   5956  O  OE1 . GLU B 1 408 ? 6.238   -34.735 17.287  1.00 46.55  ? 408  GLU B OE1 1 
ATOM   5957  O  OE2 . GLU B 1 408 ? 7.922   -33.342 17.083  1.00 78.49  ? 408  GLU B OE2 1 
ATOM   5958  N  N   . ALA B 1 409 ? 12.690  -35.060 18.812  1.00 51.04  ? 409  ALA B N   1 
ATOM   5959  C  CA  . ALA B 1 409 ? 14.013  -34.584 19.212  1.00 44.01  ? 409  ALA B CA  1 
ATOM   5960  C  C   . ALA B 1 409 ? 13.933  -33.445 20.221  1.00 44.33  ? 409  ALA B C   1 
ATOM   5961  O  O   . ALA B 1 409 ? 13.081  -32.563 20.109  1.00 38.73  ? 409  ALA B O   1 
ATOM   5962  C  CB  . ALA B 1 409 ? 14.838  -34.167 17.985  1.00 32.36  ? 409  ALA B CB  1 
ATOM   5963  N  N   . LEU B 1 410 ? 14.832  -33.474 21.200  1.00 43.41  ? 410  LEU B N   1 
ATOM   5964  C  CA  . LEU B 1 410 ? 14.904  -32.423 22.200  1.00 30.52  ? 410  LEU B CA  1 
ATOM   5965  C  C   . LEU B 1 410 ? 15.110  -31.086 21.517  1.00 28.35  ? 410  LEU B C   1 
ATOM   5966  O  O   . LEU B 1 410 ? 16.039  -30.898 20.726  1.00 27.54  ? 410  LEU B O   1 
ATOM   5967  C  CB  . LEU B 1 410 ? 16.034  -32.702 23.183  1.00 41.49  ? 410  LEU B CB  1 
ATOM   5968  C  CG  . LEU B 1 410 ? 15.694  -33.814 24.181  1.00 63.00  ? 410  LEU B CG  1 
ATOM   5969  C  CD1 . LEU B 1 410 ? 16.933  -34.516 24.741  1.00 73.82  ? 410  LEU B CD1 1 
ATOM   5970  C  CD2 . LEU B 1 410 ? 14.833  -33.279 25.312  1.00 68.54  ? 410  LEU B CD2 1 
ATOM   5971  N  N   . ARG B 1 411 ? 14.216  -30.162 21.802  1.00 31.28  ? 411  ARG B N   1 
ATOM   5972  C  CA  . ARG B 1 411 ? 14.341  -28.821 21.276  1.00 38.28  ? 411  ARG B CA  1 
ATOM   5973  C  C   . ARG B 1 411 ? 15.473  -28.069 21.968  1.00 38.45  ? 411  ARG B C   1 
ATOM   5974  O  O   . ARG B 1 411 ? 15.645  -28.155 23.189  1.00 35.17  ? 411  ARG B O   1 
ATOM   5975  C  CB  . ARG B 1 411 ? 13.040  -28.059 21.473  1.00 39.87  ? 411  ARG B CB  1 
ATOM   5976  C  CG  . ARG B 1 411 ? 13.192  -26.578 21.250  1.00 37.27  ? 411  ARG B CG  1 
ATOM   5977  C  CD  . ARG B 1 411 ? 13.223  -26.275 19.798  1.00 32.84  ? 411  ARG B CD  1 
ATOM   5978  N  NE  . ARG B 1 411 ? 11.871  -26.053 19.313  1.00 48.55  ? 411  ARG B NE  1 
ATOM   5979  C  CZ  . ARG B 1 411 ? 11.365  -24.850 19.081  1.00 48.91  ? 411  ARG B CZ  1 
ATOM   5980  N  NH1 . ARG B 1 411 ? 12.112  -23.772 19.285  1.00 43.07  ? 411  ARG B NH1 1 
ATOM   5981  N  NH2 . ARG B 1 411 ? 10.121  -24.726 18.633  1.00 45.13  ? 411  ARG B NH2 1 
ATOM   5982  N  N   . LEU B 1 412 ? 16.237  -27.322 21.180  1.00 39.69  ? 412  LEU B N   1 
ATOM   5983  C  CA  . LEU B 1 412 ? 17.342  -26.534 21.707  1.00 42.94  ? 412  LEU B CA  1 
ATOM   5984  C  C   . LEU B 1 412 ? 17.643  -25.388 20.750  1.00 36.92  ? 412  LEU B C   1 
ATOM   5985  O  O   . LEU B 1 412 ? 18.068  -25.623 19.629  1.00 37.93  ? 412  LEU B O   1 
ATOM   5986  C  CB  . LEU B 1 412 ? 18.578  -27.418 21.884  1.00 45.45  ? 412  LEU B CB  1 
ATOM   5987  C  CG  . LEU B 1 412 ? 19.826  -26.809 22.534  1.00 42.94  ? 412  LEU B CG  1 
ATOM   5988  C  CD1 . LEU B 1 412 ? 19.629  -26.663 24.019  1.00 57.18  ? 412  LEU B CD1 1 
ATOM   5989  C  CD2 . LEU B 1 412 ? 21.041  -27.664 22.263  1.00 22.18  ? 412  LEU B CD2 1 
ATOM   5990  N  N   . ASP B 1 413 ? 17.410  -24.153 21.187  1.00 31.27  ? 413  ASP B N   1 
ATOM   5991  C  CA  . ASP B 1 413 ? 17.529  -22.996 20.302  1.00 30.44  ? 413  ASP B CA  1 
ATOM   5992  C  C   . ASP B 1 413 ? 18.733  -22.084 20.604  1.00 50.68  ? 413  ASP B C   1 
ATOM   5993  O  O   . ASP B 1 413 ? 19.326  -22.117 21.699  1.00 46.52  ? 413  ASP B O   1 
ATOM   5994  C  CB  . ASP B 1 413 ? 16.261  -22.145 20.345  1.00 34.27  ? 413  ASP B CB  1 
ATOM   5995  C  CG  . ASP B 1 413 ? 15.046  -22.840 19.756  1.00 42.49  ? 413  ASP B CG  1 
ATOM   5996  O  OD1 . ASP B 1 413 ? 15.147  -24.001 19.312  1.00 49.18  ? 413  ASP B OD1 1 
ATOM   5997  O  OD2 . ASP B 1 413 ? 13.972  -22.203 19.744  1.00 50.34  ? 413  ASP B OD2 1 
ATOM   5998  N  N   . PHE B 1 414 ? 19.070  -21.247 19.624  1.00 51.29  ? 414  PHE B N   1 
ATOM   5999  C  CA  . PHE B 1 414 ? 20.171  -20.307 19.760  1.00 42.06  ? 414  PHE B CA  1 
ATOM   6000  C  C   . PHE B 1 414 ? 19.822  -18.904 19.259  1.00 51.53  ? 414  PHE B C   1 
ATOM   6001  O  O   . PHE B 1 414 ? 19.266  -18.733 18.173  1.00 46.54  ? 414  PHE B O   1 
ATOM   6002  C  CB  . PHE B 1 414 ? 21.386  -20.822 18.996  1.00 42.98  ? 414  PHE B CB  1 
ATOM   6003  C  CG  . PHE B 1 414 ? 21.848  -22.168 19.443  1.00 46.05  ? 414  PHE B CG  1 
ATOM   6004  C  CD1 . PHE B 1 414 ? 21.285  -23.321 18.920  1.00 40.79  ? 414  PHE B CD1 1 
ATOM   6005  C  CD2 . PHE B 1 414 ? 22.853  -22.285 20.389  1.00 60.39  ? 414  PHE B CD2 1 
ATOM   6006  C  CE1 . PHE B 1 414 ? 21.718  -24.568 19.338  1.00 41.93  ? 414  PHE B CE1 1 
ATOM   6007  C  CE2 . PHE B 1 414 ? 23.291  -23.526 20.811  1.00 54.98  ? 414  PHE B CE2 1 
ATOM   6008  C  CZ  . PHE B 1 414 ? 22.722  -24.669 20.285  1.00 51.84  ? 414  PHE B CZ  1 
ATOM   6009  N  N   . LYS B 1 415 ? 20.151  -17.898 20.065  1.00 52.96  ? 415  LYS B N   1 
ATOM   6010  C  CA  . LYS B 1 415 ? 20.120  -16.510 19.605  1.00 54.05  ? 415  LYS B CA  1 
ATOM   6011  C  C   . LYS B 1 415 ? 21.543  -16.004 19.485  1.00 58.12  ? 415  LYS B C   1 
ATOM   6012  O  O   . LYS B 1 415 ? 22.325  -16.068 20.443  1.00 50.24  ? 415  LYS B O   1 
ATOM   6013  C  CB  . LYS B 1 415 ? 19.341  -15.606 20.562  1.00 57.15  ? 415  LYS B CB  1 
ATOM   6014  C  CG  . LYS B 1 415 ? 17.833  -15.840 20.560  1.00 72.49  ? 415  LYS B CG  1 
ATOM   6015  C  CD  . LYS B 1 415 ? 17.061  -14.634 21.091  1.00 76.74  ? 415  LYS B CD  1 
ATOM   6016  C  CE  . LYS B 1 415 ? 15.582  -14.743 20.747  1.00 81.31  ? 415  LYS B CE  1 
ATOM   6017  N  NZ  . LYS B 1 415 ? 14.854  -13.478 21.010  1.00 81.88  ? 415  LYS B NZ  1 
ATOM   6018  N  N   . LEU B 1 416 ? 21.877  -15.508 18.301  1.00 51.77  ? 416  LEU B N   1 
ATOM   6019  C  CA  . LEU B 1 416 ? 23.227  -15.042 18.046  1.00 50.14  ? 416  LEU B CA  1 
ATOM   6020  C  C   . LEU B 1 416 ? 23.197  -13.551 17.882  1.00 50.94  ? 416  LEU B C   1 
ATOM   6021  O  O   . LEU B 1 416 ? 22.345  -13.027 17.170  1.00 60.42  ? 416  LEU B O   1 
ATOM   6022  C  CB  . LEU B 1 416 ? 23.763  -15.663 16.765  1.00 55.84  ? 416  LEU B CB  1 
ATOM   6023  C  CG  . LEU B 1 416 ? 23.728  -17.184 16.679  1.00 39.79  ? 416  LEU B CG  1 
ATOM   6024  C  CD1 . LEU B 1 416 ? 24.465  -17.638 15.404  1.00 31.84  ? 416  LEU B CD1 1 
ATOM   6025  C  CD2 . LEU B 1 416 ? 24.355  -17.762 17.936  1.00 30.10  ? 416  LEU B CD2 1 
ATOM   6026  N  N   . ALA B 1 417 ? 24.119  -12.858 18.533  1.00 47.69  ? 417  ALA B N   1 
ATOM   6027  C  CA  . ALA B 1 417 ? 24.208  -11.422 18.341  1.00 33.19  ? 417  ALA B CA  1 
ATOM   6028  C  C   . ALA B 1 417 ? 25.054  -11.150 17.121  1.00 41.61  ? 417  ALA B C   1 
ATOM   6029  O  O   . ALA B 1 417 ? 25.826  -12.009 16.677  1.00 53.35  ? 417  ALA B O   1 
ATOM   6030  C  CB  . ALA B 1 417 ? 24.802  -10.760 19.539  1.00 32.01  ? 417  ALA B CB  1 
ATOM   6031  N  N   . PRO B 1 418 ? 24.903  -9.953  16.558  1.00 37.00  ? 418  PRO B N   1 
ATOM   6032  C  CA  . PRO B 1 418 ? 25.728  -9.622  15.401  1.00 47.68  ? 418  PRO B CA  1 
ATOM   6033  C  C   . PRO B 1 418 ? 27.078  -9.147  15.899  1.00 48.77  ? 418  PRO B C   1 
ATOM   6034  O  O   . PRO B 1 418 ? 27.180  -8.645  17.020  1.00 54.86  ? 418  PRO B O   1 
ATOM   6035  C  CB  . PRO B 1 418 ? 24.957  -8.485  14.722  1.00 31.81  ? 418  PRO B CB  1 
ATOM   6036  C  CG  . PRO B 1 418 ? 23.775  -8.178  15.628  1.00 44.61  ? 418  PRO B CG  1 
ATOM   6037  C  CD  . PRO B 1 418 ? 24.023  -8.847  16.942  1.00 32.51  ? 418  PRO B CD  1 
ATOM   6038  N  N   . VAL B 1 419 ? 28.109  -9.335  15.089  1.00 36.26  ? 419  VAL B N   1 
ATOM   6039  C  CA  . VAL B 1 419 ? 29.436  -8.921  15.473  1.00 38.05  ? 419  VAL B CA  1 
ATOM   6040  C  C   . VAL B 1 419 ? 29.508  -7.384  15.477  1.00 49.49  ? 419  VAL B C   1 
ATOM   6041  O  O   . VAL B 1 419 ? 30.203  -6.773  16.300  1.00 41.77  ? 419  VAL B O   1 
ATOM   6042  C  CB  . VAL B 1 419 ? 30.475  -9.538  14.525  1.00 47.06  ? 419  VAL B CB  1 
ATOM   6043  C  CG1 . VAL B 1 419 ? 30.422  -11.053 14.611  1.00 55.63  ? 419  VAL B CG1 1 
ATOM   6044  C  CG2 . VAL B 1 419 ? 30.213  -9.102  13.097  1.00 47.01  ? 419  VAL B CG2 1 
ATOM   6045  N  N   . GLU B 1 420 ? 28.764  -6.760  14.571  1.00 48.89  ? 420  GLU B N   1 
ATOM   6046  C  CA  . GLU B 1 420 ? 28.774  -5.307  14.458  1.00 66.33  ? 420  GLU B CA  1 
ATOM   6047  C  C   . GLU B 1 420 ? 28.783  -4.620  15.831  1.00 67.91  ? 420  GLU B C   1 
ATOM   6048  O  O   . GLU B 1 420 ? 29.835  -4.189  16.320  1.00 51.99  ? 420  GLU B O   1 
ATOM   6049  C  CB  . GLU B 1 420 ? 27.583  -4.824  13.627  1.00 63.19  ? 420  GLU B CB  1 
ATOM   6050  C  CG  . GLU B 1 420 ? 27.637  -3.338  13.321  1.00 68.03  ? 420  GLU B CG  1 
ATOM   6051  C  CD  . GLU B 1 420 ? 26.264  -2.699  13.301  1.00 75.83  ? 420  GLU B CD  1 
ATOM   6052  O  OE1 . GLU B 1 420 ? 25.270  -3.457  13.304  1.00 78.50  ? 420  GLU B OE1 1 
ATOM   6053  O  OE2 . GLU B 1 420 ? 26.179  -1.448  13.283  1.00 69.65  ? 420  GLU B OE2 1 
ATOM   6054  N  N   . GLU C 1 30  ? -29.372 29.861  39.339  1.00 39.22  ? 30   GLU C N   1 
ATOM   6055  C  CA  . GLU C 1 30  ? -28.272 29.331  38.537  1.00 42.61  ? 30   GLU C CA  1 
ATOM   6056  C  C   . GLU C 1 30  ? -28.727 28.077  37.813  1.00 40.23  ? 30   GLU C C   1 
ATOM   6057  O  O   . GLU C 1 30  ? -29.294 27.167  38.417  1.00 43.51  ? 30   GLU C O   1 
ATOM   6058  C  CB  . GLU C 1 30  ? -27.048 29.021  39.418  1.00 31.00  ? 30   GLU C CB  1 
ATOM   6059  C  CG  . GLU C 1 30  ? -25.754 28.685  38.677  1.00 23.25  ? 30   GLU C CG  1 
ATOM   6060  C  CD  . GLU C 1 30  ? -24.508 28.914  39.542  1.00 55.54  ? 30   GLU C CD  1 
ATOM   6061  O  OE1 . GLU C 1 30  ? -24.630 29.032  40.782  1.00 43.63  ? 30   GLU C OE1 1 
ATOM   6062  O  OE2 . GLU C 1 30  ? -23.391 28.974  38.984  1.00 63.95  ? 30   GLU C OE2 1 
ATOM   6063  N  N   . ASP C 1 31  ? -28.486 28.034  36.513  1.00 46.05  ? 31   ASP C N   1 
ATOM   6064  C  CA  . ASP C 1 31  ? -28.873 26.881  35.719  1.00 38.29  ? 31   ASP C CA  1 
ATOM   6065  C  C   . ASP C 1 31  ? -27.680 25.983  35.410  1.00 53.45  ? 31   ASP C C   1 
ATOM   6066  O  O   . ASP C 1 31  ? -26.727 26.411  34.742  1.00 30.65  ? 31   ASP C O   1 
ATOM   6067  C  CB  . ASP C 1 31  ? -29.516 27.333  34.419  1.00 45.43  ? 31   ASP C CB  1 
ATOM   6068  C  CG  . ASP C 1 31  ? -29.813 26.177  33.495  1.00 66.23  ? 31   ASP C CG  1 
ATOM   6069  O  OD1 . ASP C 1 31  ? -30.102 26.425  32.302  1.00 72.88  ? 31   ASP C OD1 1 
ATOM   6070  O  OD2 . ASP C 1 31  ? -29.752 25.017  33.967  1.00 61.86  ? 31   ASP C OD2 1 
ATOM   6071  N  N   . GLU C 1 32  ? -27.744 24.742  35.901  1.00 62.09  ? 32   GLU C N   1 
ATOM   6072  C  CA  . GLU C 1 32  ? -26.698 23.740  35.663  1.00 61.65  ? 32   GLU C CA  1 
ATOM   6073  C  C   . GLU C 1 32  ? -27.284 22.352  35.337  1.00 50.89  ? 32   GLU C C   1 
ATOM   6074  O  O   . GLU C 1 32  ? -26.771 21.316  35.776  1.00 35.11  ? 32   GLU C O   1 
ATOM   6075  C  CB  . GLU C 1 32  ? -25.751 23.638  36.869  1.00 76.73  ? 32   GLU C CB  1 
ATOM   6076  C  CG  . GLU C 1 32  ? -24.955 24.904  37.195  1.00 70.63  ? 32   GLU C CG  1 
ATOM   6077  C  CD  . GLU C 1 32  ? -23.966 24.689  38.335  1.00 58.90  ? 32   GLU C CD  1 
ATOM   6078  O  OE1 . GLU C 1 32  ? -22.944 24.009  38.111  1.00 48.94  ? 32   GLU C OE1 1 
ATOM   6079  O  OE2 . GLU C 1 32  ? -24.208 25.196  39.456  1.00 55.30  ? 32   GLU C OE2 1 
ATOM   6080  N  N   . SER C 1 33  ? -28.352 22.342  34.550  1.00 51.46  ? 33   SER C N   1 
ATOM   6081  C  CA  . SER C 1 33  ? -29.064 21.110  34.218  1.00 52.18  ? 33   SER C CA  1 
ATOM   6082  C  C   . SER C 1 33  ? -28.289 20.166  33.283  1.00 44.57  ? 33   SER C C   1 
ATOM   6083  O  O   . SER C 1 33  ? -28.637 18.994  33.142  1.00 35.49  ? 33   SER C O   1 
ATOM   6084  C  CB  . SER C 1 33  ? -30.419 21.456  33.607  1.00 60.36  ? 33   SER C CB  1 
ATOM   6085  O  OG  . SER C 1 33  ? -30.237 22.289  32.474  1.00 67.35  ? 33   SER C OG  1 
ATOM   6086  N  N   . PHE C 1 34  ? -27.251 20.667  32.627  1.00 34.70  ? 34   PHE C N   1 
ATOM   6087  C  CA  . PHE C 1 34  ? -26.415 19.773  31.839  1.00 44.00  ? 34   PHE C CA  1 
ATOM   6088  C  C   . PHE C 1 34  ? -25.904 18.606  32.698  1.00 41.80  ? 34   PHE C C   1 
ATOM   6089  O  O   . PHE C 1 34  ? -25.482 17.584  32.155  1.00 43.08  ? 34   PHE C O   1 
ATOM   6090  C  CB  . PHE C 1 34  ? -25.261 20.519  31.122  1.00 50.35  ? 34   PHE C CB  1 
ATOM   6091  C  CG  . PHE C 1 34  ? -24.437 21.419  32.020  1.00 50.65  ? 34   PHE C CG  1 
ATOM   6092  C  CD1 . PHE C 1 34  ? -23.543 20.887  32.947  1.00 48.91  ? 34   PHE C CD1 1 
ATOM   6093  C  CD2 . PHE C 1 34  ? -24.535 22.798  31.915  1.00 46.12  ? 34   PHE C CD2 1 
ATOM   6094  C  CE1 . PHE C 1 34  ? -22.783 21.715  33.769  1.00 37.58  ? 34   PHE C CE1 1 
ATOM   6095  C  CE2 . PHE C 1 34  ? -23.774 23.632  32.734  1.00 50.43  ? 34   PHE C CE2 1 
ATOM   6096  C  CZ  . PHE C 1 34  ? -22.903 23.093  33.665  1.00 27.56  ? 34   PHE C CZ  1 
ATOM   6097  N  N   . LEU C 1 35  ? -25.971 18.760  34.027  1.00 29.96  ? 35   LEU C N   1 
ATOM   6098  C  CA  . LEU C 1 35  ? -25.453 17.762  34.978  1.00 27.23  ? 35   LEU C CA  1 
ATOM   6099  C  C   . LEU C 1 35  ? -26.505 16.695  35.218  1.00 42.28  ? 35   LEU C C   1 
ATOM   6100  O  O   . LEU C 1 35  ? -26.241 15.660  35.834  1.00 44.67  ? 35   LEU C O   1 
ATOM   6101  C  CB  . LEU C 1 35  ? -25.047 18.393  36.320  1.00 22.81  ? 35   LEU C CB  1 
ATOM   6102  C  CG  . LEU C 1 35  ? -23.984 19.497  36.363  1.00 39.77  ? 35   LEU C CG  1 
ATOM   6103  C  CD1 . LEU C 1 35  ? -23.763 19.963  37.790  1.00 35.91  ? 35   LEU C CD1 1 
ATOM   6104  C  CD2 . LEU C 1 35  ? -22.647 19.065  35.728  1.00 38.07  ? 35   LEU C CD2 1 
ATOM   6105  N  N   . GLN C 1 36  ? -27.710 16.984  34.745  1.00 54.62  ? 36   GLN C N   1 
ATOM   6106  C  CA  . GLN C 1 36  ? -28.791 16.015  34.700  1.00 69.22  ? 36   GLN C CA  1 
ATOM   6107  C  C   . GLN C 1 36  ? -28.264 14.751  34.054  1.00 76.63  ? 36   GLN C C   1 
ATOM   6108  O  O   . GLN C 1 36  ? -27.800 14.779  32.910  1.00 88.64  ? 36   GLN C O   1 
ATOM   6109  C  CB  . GLN C 1 36  ? -29.940 16.567  33.844  1.00 83.74  ? 36   GLN C CB  1 
ATOM   6110  C  CG  . GLN C 1 36  ? -31.250 15.834  33.994  1.00 74.30  ? 36   GLN C CG  1 
ATOM   6111  C  CD  . GLN C 1 36  ? -31.792 15.997  35.384  1.00 69.60  ? 36   GLN C CD  1 
ATOM   6112  O  OE1 . GLN C 1 36  ? -32.829 15.431  35.748  1.00 63.91  ? 36   GLN C OE1 1 
ATOM   6113  N  NE2 . GLN C 1 36  ? -31.087 16.787  36.182  1.00 60.33  ? 36   GLN C NE2 1 
ATOM   6114  N  N   . GLN C 1 37  ? -28.322 13.647  34.787  1.00 72.98  ? 37   GLN C N   1 
ATOM   6115  C  CA  . GLN C 1 37  ? -28.026 12.348  34.203  1.00 80.34  ? 37   GLN C CA  1 
ATOM   6116  C  C   . GLN C 1 37  ? -26.662 12.327  33.501  1.00 75.57  ? 37   GLN C C   1 
ATOM   6117  O  O   . GLN C 1 37  ? -26.624 12.293  32.268  1.00 45.55  ? 37   GLN C O   1 
ATOM   6118  C  CB  . GLN C 1 37  ? -29.131 12.001  33.194  1.00 88.06  ? 37   GLN C CB  1 
ATOM   6119  C  CG  . GLN C 1 37  ? -30.557 12.215  33.731  1.00 96.92  ? 37   GLN C CG  1 
ATOM   6120  C  CD  . GLN C 1 37  ? -31.618 12.183  32.640  1.00 92.96  ? 37   GLN C CD  1 
ATOM   6121  O  OE1 . GLN C 1 37  ? -31.566 11.361  31.721  1.00 99.81  ? 37   GLN C OE1 1 
ATOM   6122  N  NE2 . GLN C 1 37  ? -32.588 13.085  32.740  1.00 76.75  ? 37   GLN C NE2 1 
ATOM   6123  N  N   . PRO C 1 38  ? -25.547 12.330  34.281  1.00 90.52  ? 38   PRO C N   1 
ATOM   6124  C  CA  . PRO C 1 38  ? -24.158 12.442  33.781  1.00 84.68  ? 38   PRO C CA  1 
ATOM   6125  C  C   . PRO C 1 38  ? -23.750 11.356  32.768  1.00 87.20  ? 38   PRO C C   1 
ATOM   6126  O  O   . PRO C 1 38  ? -24.176 10.205  32.888  1.00 115.01 ? 38   PRO C O   1 
ATOM   6127  C  CB  . PRO C 1 38  ? -23.300 12.337  35.060  1.00 69.01  ? 38   PRO C CB  1 
ATOM   6128  C  CG  . PRO C 1 38  ? -24.212 12.675  36.183  1.00 61.04  ? 38   PRO C CG  1 
ATOM   6129  C  CD  . PRO C 1 38  ? -25.582 12.191  35.751  1.00 82.97  ? 38   PRO C CD  1 
ATOM   6130  N  N   . HIS C 1 39  ? -22.923 11.725  31.790  1.00 56.59  ? 39   HIS C N   1 
ATOM   6131  C  CA  . HIS C 1 39  ? -22.562 10.825  30.699  1.00 51.46  ? 39   HIS C CA  1 
ATOM   6132  C  C   . HIS C 1 39  ? -21.553 11.517  29.782  1.00 54.38  ? 39   HIS C C   1 
ATOM   6133  O  O   . HIS C 1 39  ? -21.488 12.748  29.742  1.00 45.95  ? 39   HIS C O   1 
ATOM   6134  C  CB  . HIS C 1 39  ? -23.813 10.423  29.901  1.00 47.81  ? 39   HIS C CB  1 
ATOM   6135  C  CG  . HIS C 1 39  ? -24.289 11.485  28.959  1.00 45.71  ? 39   HIS C CG  1 
ATOM   6136  N  ND1 . HIS C 1 39  ? -24.650 12.746  29.382  1.00 56.65  ? 39   HIS C ND1 1 
ATOM   6137  C  CD2 . HIS C 1 39  ? -24.437 11.483  27.613  1.00 51.16  ? 39   HIS C CD2 1 
ATOM   6138  C  CE1 . HIS C 1 39  ? -25.010 13.473  28.339  1.00 52.48  ? 39   HIS C CE1 1 
ATOM   6139  N  NE2 . HIS C 1 39  ? -24.884 12.734  27.253  1.00 46.81  ? 39   HIS C NE2 1 
ATOM   6140  N  N   . TYR C 1 40  ? -20.769 10.730  29.046  1.00 68.37  ? 40   TYR C N   1 
ATOM   6141  C  CA  . TYR C 1 40  ? -19.798 11.278  28.091  1.00 57.80  ? 40   TYR C CA  1 
ATOM   6142  C  C   . TYR C 1 40  ? -20.417 11.532  26.730  1.00 49.26  ? 40   TYR C C   1 
ATOM   6143  O  O   . TYR C 1 40  ? -20.960 10.622  26.099  1.00 59.94  ? 40   TYR C O   1 
ATOM   6144  C  CB  . TYR C 1 40  ? -18.600 10.343  27.941  1.00 58.50  ? 40   TYR C CB  1 
ATOM   6145  C  CG  . TYR C 1 40  ? -17.633 10.438  29.091  1.00 55.82  ? 40   TYR C CG  1 
ATOM   6146  C  CD1 . TYR C 1 40  ? -17.587 9.461   30.076  1.00 61.90  ? 40   TYR C CD1 1 
ATOM   6147  C  CD2 . TYR C 1 40  ? -16.778 11.520  29.200  1.00 42.76  ? 40   TYR C CD2 1 
ATOM   6148  C  CE1 . TYR C 1 40  ? -16.700 9.560   31.130  1.00 62.05  ? 40   TYR C CE1 1 
ATOM   6149  C  CE2 . TYR C 1 40  ? -15.890 11.628  30.242  1.00 47.40  ? 40   TYR C CE2 1 
ATOM   6150  C  CZ  . TYR C 1 40  ? -15.849 10.652  31.206  1.00 54.77  ? 40   TYR C CZ  1 
ATOM   6151  O  OH  . TYR C 1 40  ? -14.950 10.781  32.249  1.00 57.41  ? 40   TYR C OH  1 
ATOM   6152  N  N   . ALA C 1 41  ? -20.322 12.773  26.278  1.00 41.03  ? 41   ALA C N   1 
ATOM   6153  C  CA  . ALA C 1 41  ? -20.921 13.167  25.009  1.00 41.45  ? 41   ALA C CA  1 
ATOM   6154  C  C   . ALA C 1 41  ? -20.166 12.540  23.838  1.00 39.49  ? 41   ALA C C   1 
ATOM   6155  O  O   . ALA C 1 41  ? -18.942 12.652  23.755  1.00 39.11  ? 41   ALA C O   1 
ATOM   6156  C  CB  . ALA C 1 41  ? -20.950 14.695  24.890  1.00 24.23  ? 41   ALA C CB  1 
ATOM   6157  N  N   . SER C 1 42  ? -20.890 11.870  22.943  1.00 43.44  ? 42   SER C N   1 
ATOM   6158  C  CA  . SER C 1 42  ? -20.266 11.261  21.773  1.00 45.44  ? 42   SER C CA  1 
ATOM   6159  C  C   . SER C 1 42  ? -20.038 12.306  20.706  1.00 48.80  ? 42   SER C C   1 
ATOM   6160  O  O   . SER C 1 42  ? -20.583 13.411  20.778  1.00 41.26  ? 42   SER C O   1 
ATOM   6161  C  CB  . SER C 1 42  ? -21.168 10.191  21.182  1.00 46.26  ? 42   SER C CB  1 
ATOM   6162  O  OG  . SER C 1 42  ? -22.237 10.791  20.471  1.00 43.66  ? 42   SER C OG  1 
ATOM   6163  N  N   . GLN C 1 43  ? -19.252 11.943  19.699  1.00 46.30  ? 43   GLN C N   1 
ATOM   6164  C  CA  . GLN C 1 43  ? -19.050 12.829  18.561  1.00 40.73  ? 43   GLN C CA  1 
ATOM   6165  C  C   . GLN C 1 43  ? -20.409 13.340  18.082  1.00 41.10  ? 43   GLN C C   1 
ATOM   6166  O  O   . GLN C 1 43  ? -20.623 14.549  17.928  1.00 32.09  ? 43   GLN C O   1 
ATOM   6167  C  CB  . GLN C 1 43  ? -18.309 12.106  17.433  1.00 44.98  ? 43   GLN C CB  1 
ATOM   6168  C  CG  . GLN C 1 43  ? -17.909 13.010  16.265  1.00 54.64  ? 43   GLN C CG  1 
ATOM   6169  C  CD  . GLN C 1 43  ? -16.973 14.127  16.682  1.00 53.60  ? 43   GLN C CD  1 
ATOM   6170  O  OE1 . GLN C 1 43  ? -16.245 14.004  17.667  1.00 60.60  ? 43   GLN C OE1 1 
ATOM   6171  N  NE2 . GLN C 1 43  ? -16.988 15.226  15.933  1.00 56.66  ? 43   GLN C NE2 1 
ATOM   6172  N  N   . GLU C 1 44  ? -21.343 12.426  17.867  1.00 37.80  ? 44   GLU C N   1 
ATOM   6173  C  CA  . GLU C 1 44  ? -22.640 12.869  17.409  1.00 49.92  ? 44   GLU C CA  1 
ATOM   6174  C  C   . GLU C 1 44  ? -23.263 13.835  18.411  1.00 43.96  ? 44   GLU C C   1 
ATOM   6175  O  O   . GLU C 1 44  ? -23.737 14.909  18.043  1.00 54.48  ? 44   GLU C O   1 
ATOM   6176  C  CB  . GLU C 1 44  ? -23.580 11.700  17.134  1.00 57.49  ? 44   GLU C CB  1 
ATOM   6177  C  CG  . GLU C 1 44  ? -24.822 12.142  16.362  1.00 78.53  ? 44   GLU C CG  1 
ATOM   6178  C  CD  . GLU C 1 44  ? -26.027 11.254  16.605  1.00 96.22  ? 44   GLU C CD  1 
ATOM   6179  O  OE1 . GLU C 1 44  ? -25.845 10.137  17.139  1.00 104.99 ? 44   GLU C OE1 1 
ATOM   6180  O  OE2 . GLU C 1 44  ? -27.157 11.676  16.263  1.00 95.69  ? 44   GLU C OE2 1 
ATOM   6181  N  N   . GLN C 1 45  ? -23.254 13.462  19.680  1.00 40.92  ? 45   GLN C N   1 
ATOM   6182  C  CA  . GLN C 1 45  ? -23.921 14.276  20.685  1.00 44.37  ? 45   GLN C CA  1 
ATOM   6183  C  C   . GLN C 1 45  ? -23.310 15.673  20.777  1.00 45.95  ? 45   GLN C C   1 
ATOM   6184  O  O   . GLN C 1 45  ? -23.993 16.649  21.099  1.00 45.85  ? 45   GLN C O   1 
ATOM   6185  C  CB  . GLN C 1 45  ? -23.867 13.593  22.045  1.00 36.32  ? 45   GLN C CB  1 
ATOM   6186  C  CG  . GLN C 1 45  ? -24.535 12.261  22.074  1.00 41.69  ? 45   GLN C CG  1 
ATOM   6187  C  CD  . GLN C 1 45  ? -24.912 11.854  23.468  1.00 49.73  ? 45   GLN C CD  1 
ATOM   6188  O  OE1 . GLN C 1 45  ? -24.054 11.683  24.329  1.00 42.92  ? 45   GLN C OE1 1 
ATOM   6189  N  NE2 . GLN C 1 45  ? -26.210 11.702  23.707  1.00 65.90  ? 45   GLN C NE2 1 
ATOM   6190  N  N   . LEU C 1 46  ? -22.019 15.758  20.490  1.00 36.70  ? 46   LEU C N   1 
ATOM   6191  C  CA  . LEU C 1 46  ? -21.296 17.013  20.605  1.00 37.77  ? 46   LEU C CA  1 
ATOM   6192  C  C   . LEU C 1 46  ? -21.638 17.933  19.438  1.00 44.40  ? 46   LEU C C   1 
ATOM   6193  O  O   . LEU C 1 46  ? -21.854 19.132  19.619  1.00 39.65  ? 46   LEU C O   1 
ATOM   6194  C  CB  . LEU C 1 46  ? -19.789 16.743  20.659  1.00 34.14  ? 46   LEU C CB  1 
ATOM   6195  C  CG  . LEU C 1 46  ? -18.835 17.918  20.442  1.00 42.18  ? 46   LEU C CG  1 
ATOM   6196  C  CD1 . LEU C 1 46  ? -19.158 19.062  21.385  1.00 51.39  ? 46   LEU C CD1 1 
ATOM   6197  C  CD2 . LEU C 1 46  ? -17.372 17.465  20.587  1.00 30.66  ? 46   LEU C CD2 1 
ATOM   6198  N  N   . GLU C 1 47  ? -21.682 17.372  18.237  1.00 40.22  ? 47   GLU C N   1 
ATOM   6199  C  CA  . GLU C 1 47  ? -22.019 18.165  17.069  1.00 44.66  ? 47   GLU C CA  1 
ATOM   6200  C  C   . GLU C 1 47  ? -23.438 18.670  17.229  1.00 47.62  ? 47   GLU C C   1 
ATOM   6201  O  O   . GLU C 1 47  ? -23.741 19.837  16.964  1.00 45.75  ? 47   GLU C O   1 
ATOM   6202  C  CB  . GLU C 1 47  ? -21.894 17.324  15.811  1.00 47.01  ? 47   GLU C CB  1 
ATOM   6203  C  CG  . GLU C 1 47  ? -20.467 16.922  15.490  1.00 49.05  ? 47   GLU C CG  1 
ATOM   6204  C  CD  . GLU C 1 47  ? -20.396 16.033  14.260  1.00 53.86  ? 47   GLU C CD  1 
ATOM   6205  O  OE1 . GLU C 1 47  ? -21.427 15.405  13.925  1.00 39.51  ? 47   GLU C OE1 1 
ATOM   6206  O  OE2 . GLU C 1 47  ? -19.312 15.966  13.637  1.00 63.20  ? 47   GLU C OE2 1 
ATOM   6207  N  N   . ASP C 1 48  ? -24.300 17.774  17.687  1.00 50.25  ? 48   ASP C N   1 
ATOM   6208  C  CA  . ASP C 1 48  ? -25.691 18.100  17.924  1.00 54.51  ? 48   ASP C CA  1 
ATOM   6209  C  C   . ASP C 1 48  ? -25.840 19.214  18.956  1.00 51.22  ? 48   ASP C C   1 
ATOM   6210  O  O   . ASP C 1 48  ? -26.640 20.134  18.777  1.00 52.75  ? 48   ASP C O   1 
ATOM   6211  C  CB  . ASP C 1 48  ? -26.449 16.851  18.369  1.00 61.37  ? 48   ASP C CB  1 
ATOM   6212  C  CG  . ASP C 1 48  ? -26.552 15.817  17.270  1.00 65.60  ? 48   ASP C CG  1 
ATOM   6213  O  OD1 . ASP C 1 48  ? -26.393 16.189  16.092  1.00 67.58  ? 48   ASP C OD1 1 
ATOM   6214  O  OD2 . ASP C 1 48  ? -26.795 14.633  17.583  1.00 74.58  ? 48   ASP C OD2 1 
ATOM   6215  N  N   . LEU C 1 49  ? -25.060 19.149  20.028  1.00 42.78  ? 49   LEU C N   1 
ATOM   6216  C  CA  . LEU C 1 49  ? -25.202 20.142  21.083  1.00 38.16  ? 49   LEU C CA  1 
ATOM   6217  C  C   . LEU C 1 49  ? -24.699 21.517  20.681  1.00 35.65  ? 49   LEU C C   1 
ATOM   6218  O  O   . LEU C 1 49  ? -25.235 22.528  21.139  1.00 34.50  ? 49   LEU C O   1 
ATOM   6219  C  CB  . LEU C 1 49  ? -24.525 19.691  22.371  1.00 50.77  ? 49   LEU C CB  1 
ATOM   6220  C  CG  . LEU C 1 49  ? -24.924 20.540  23.584  1.00 48.47  ? 49   LEU C CG  1 
ATOM   6221  C  CD1 . LEU C 1 49  ? -24.973 19.696  24.844  1.00 69.05  ? 49   LEU C CD1 1 
ATOM   6222  C  CD2 . LEU C 1 49  ? -23.992 21.710  23.772  1.00 44.33  ? 49   LEU C CD2 1 
ATOM   6223  N  N   . PHE C 1 50  ? -23.671 21.554  19.835  1.00 41.61  ? 50   PHE C N   1 
ATOM   6224  C  CA  . PHE C 1 50  ? -23.114 22.819  19.341  1.00 37.45  ? 50   PHE C CA  1 
ATOM   6225  C  C   . PHE C 1 50  ? -24.021 23.539  18.352  1.00 42.90  ? 50   PHE C C   1 
ATOM   6226  O  O   . PHE C 1 50  ? -24.084 24.768  18.338  1.00 51.94  ? 50   PHE C O   1 
ATOM   6227  C  CB  . PHE C 1 50  ? -21.758 22.592  18.692  1.00 30.96  ? 50   PHE C CB  1 
ATOM   6228  C  CG  . PHE C 1 50  ? -20.633 22.628  19.657  1.00 33.93  ? 50   PHE C CG  1 
ATOM   6229  C  CD1 . PHE C 1 50  ? -20.881 22.547  21.013  1.00 36.59  ? 50   PHE C CD1 1 
ATOM   6230  C  CD2 . PHE C 1 50  ? -19.333 22.746  19.222  1.00 27.21  ? 50   PHE C CD2 1 
ATOM   6231  C  CE1 . PHE C 1 50  ? -19.846 22.577  21.921  1.00 33.92  ? 50   PHE C CE1 1 
ATOM   6232  C  CE2 . PHE C 1 50  ? -18.289 22.779  20.122  1.00 31.64  ? 50   PHE C CE2 1 
ATOM   6233  C  CZ  . PHE C 1 50  ? -18.547 22.688  21.476  1.00 38.76  ? 50   PHE C CZ  1 
ATOM   6234  N  N   . ALA C 1 51  ? -24.716 22.773  17.521  1.00 29.49  ? 51   ALA C N   1 
ATOM   6235  C  CA  . ALA C 1 51  ? -25.658 23.366  16.588  1.00 41.53  ? 51   ALA C CA  1 
ATOM   6236  C  C   . ALA C 1 51  ? -26.859 23.909  17.359  1.00 60.16  ? 51   ALA C C   1 
ATOM   6237  O  O   . ALA C 1 51  ? -27.407 24.960  17.016  1.00 73.48  ? 51   ALA C O   1 
ATOM   6238  C  CB  . ALA C 1 51  ? -26.096 22.350  15.547  1.00 29.57  ? 51   ALA C CB  1 
ATOM   6239  N  N   . GLY C 1 52  ? -27.259 23.194  18.408  1.00 54.71  ? 52   GLY C N   1 
ATOM   6240  C  CA  . GLY C 1 52  ? -28.385 23.605  19.223  1.00 39.70  ? 52   GLY C CA  1 
ATOM   6241  C  C   . GLY C 1 52  ? -28.120 24.958  19.844  1.00 41.52  ? 52   GLY C C   1 
ATOM   6242  O  O   . GLY C 1 52  ? -28.991 25.825  19.821  1.00 43.59  ? 52   GLY C O   1 
ATOM   6243  N  N   . LEU C 1 53  ? -26.914 25.139  20.386  1.00 39.63  ? 53   LEU C N   1 
ATOM   6244  C  CA  . LEU C 1 53  ? -26.528 26.397  21.031  1.00 50.21  ? 53   LEU C CA  1 
ATOM   6245  C  C   . LEU C 1 53  ? -26.488 27.529  20.028  1.00 47.59  ? 53   LEU C C   1 
ATOM   6246  O  O   . LEU C 1 53  ? -26.862 28.666  20.331  1.00 43.90  ? 53   LEU C O   1 
ATOM   6247  C  CB  . LEU C 1 53  ? -25.157 26.284  21.703  1.00 44.99  ? 53   LEU C CB  1 
ATOM   6248  C  CG  . LEU C 1 53  ? -25.024 25.256  22.823  1.00 46.01  ? 53   LEU C CG  1 
ATOM   6249  C  CD1 . LEU C 1 53  ? -23.728 25.430  23.569  1.00 52.26  ? 53   LEU C CD1 1 
ATOM   6250  C  CD2 . LEU C 1 53  ? -26.192 25.348  23.769  1.00 42.80  ? 53   LEU C CD2 1 
ATOM   6251  N  N   . GLU C 1 54  ? -26.023 27.202  18.830  1.00 48.58  ? 54   GLU C N   1 
ATOM   6252  C  CA  . GLU C 1 54  ? -25.936 28.174  17.754  1.00 56.08  ? 54   GLU C CA  1 
ATOM   6253  C  C   . GLU C 1 54  ? -27.302 28.754  17.400  1.00 61.73  ? 54   GLU C C   1 
ATOM   6254  O  O   . GLU C 1 54  ? -27.425 29.956  17.145  1.00 60.53  ? 54   GLU C O   1 
ATOM   6255  C  CB  . GLU C 1 54  ? -25.289 27.553  16.521  1.00 59.93  ? 54   GLU C CB  1 
ATOM   6256  C  CG  . GLU C 1 54  ? -24.716 28.597  15.575  1.00 76.56  ? 54   GLU C CG  1 
ATOM   6257  C  CD  . GLU C 1 54  ? -23.876 27.999  14.463  1.00 73.58  ? 54   GLU C CD  1 
ATOM   6258  O  OE1 . GLU C 1 54  ? -23.218 28.770  13.736  1.00 72.18  ? 54   GLU C OE1 1 
ATOM   6259  O  OE2 . GLU C 1 54  ? -23.871 26.760  14.318  1.00 69.91  ? 54   GLU C OE2 1 
ATOM   6260  N  N   . LYS C 1 55  ? -28.327 27.905  17.384  1.00 64.36  ? 55   LYS C N   1 
ATOM   6261  C  CA  . LYS C 1 55  ? -29.681 28.386  17.118  1.00 60.71  ? 55   LYS C CA  1 
ATOM   6262  C  C   . LYS C 1 55  ? -30.364 28.910  18.385  1.00 43.20  ? 55   LYS C C   1 
ATOM   6263  O  O   . LYS C 1 55  ? -31.092 29.895  18.346  1.00 43.82  ? 55   LYS C O   1 
ATOM   6264  C  CB  . LYS C 1 55  ? -30.532 27.330  16.400  1.00 56.12  ? 55   LYS C CB  1 
ATOM   6265  C  CG  . LYS C 1 55  ? -30.501 25.956  17.025  1.00 58.46  ? 55   LYS C CG  1 
ATOM   6266  C  CD  . LYS C 1 55  ? -31.407 24.993  16.261  1.00 62.26  ? 55   LYS C CD  1 
ATOM   6267  C  CE  . LYS C 1 55  ? -32.874 25.381  16.386  1.00 59.74  ? 55   LYS C CE  1 
ATOM   6268  N  NZ  . LYS C 1 55  ? -33.776 24.339  15.805  1.00 63.74  ? 55   LYS C NZ  1 
ATOM   6269  N  N   . ALA C 1 56  ? -30.103 28.272  19.513  1.00 36.47  ? 56   ALA C N   1 
ATOM   6270  C  CA  . ALA C 1 56  ? -30.683 28.728  20.765  1.00 40.79  ? 56   ALA C CA  1 
ATOM   6271  C  C   . ALA C 1 56  ? -30.154 30.106  21.137  1.00 45.54  ? 56   ALA C C   1 
ATOM   6272  O  O   . ALA C 1 56  ? -30.854 30.895  21.781  1.00 52.48  ? 56   ALA C O   1 
ATOM   6273  C  CB  . ALA C 1 56  ? -30.395 27.740  21.876  1.00 41.21  ? 56   ALA C CB  1 
ATOM   6274  N  N   . TYR C 1 57  ? -28.915 30.385  20.743  1.00 44.01  ? 57   TYR C N   1 
ATOM   6275  C  CA  . TYR C 1 57  ? -28.266 31.654  21.076  1.00 41.89  ? 57   TYR C CA  1 
ATOM   6276  C  C   . TYR C 1 57  ? -27.634 32.293  19.842  1.00 40.29  ? 57   TYR C C   1 
ATOM   6277  O  O   . TYR C 1 57  ? -26.419 32.411  19.751  1.00 39.53  ? 57   TYR C O   1 
ATOM   6278  C  CB  . TYR C 1 57  ? -27.217 31.426  22.148  1.00 38.76  ? 57   TYR C CB  1 
ATOM   6279  C  CG  . TYR C 1 57  ? -27.784 30.767  23.386  1.00 50.74  ? 57   TYR C CG  1 
ATOM   6280  C  CD1 . TYR C 1 57  ? -27.829 29.386  23.501  1.00 51.68  ? 57   TYR C CD1 1 
ATOM   6281  C  CD2 . TYR C 1 57  ? -28.285 31.528  24.436  1.00 47.55  ? 57   TYR C CD2 1 
ATOM   6282  C  CE1 . TYR C 1 57  ? -28.350 28.780  24.623  1.00 48.17  ? 57   TYR C CE1 1 
ATOM   6283  C  CE2 . TYR C 1 57  ? -28.809 30.929  25.570  1.00 35.80  ? 57   TYR C CE2 1 
ATOM   6284  C  CZ  . TYR C 1 57  ? -28.840 29.554  25.654  1.00 45.85  ? 57   TYR C CZ  1 
ATOM   6285  O  OH  . TYR C 1 57  ? -29.352 28.932  26.768  1.00 41.87  ? 57   TYR C OH  1 
ATOM   6286  N  N   . PRO C 1 58  ? -28.479 32.714  18.896  1.00 32.75  ? 58   PRO C N   1 
ATOM   6287  C  CA  . PRO C 1 58  ? -28.116 33.144  17.548  1.00 38.61  ? 58   PRO C CA  1 
ATOM   6288  C  C   . PRO C 1 58  ? -26.965 34.128  17.477  1.00 53.87  ? 58   PRO C C   1 
ATOM   6289  O  O   . PRO C 1 58  ? -26.168 34.031  16.548  1.00 67.68  ? 58   PRO C O   1 
ATOM   6290  C  CB  . PRO C 1 58  ? -29.390 33.830  17.058  1.00 48.37  ? 58   PRO C CB  1 
ATOM   6291  C  CG  . PRO C 1 58  ? -30.485 33.143  17.793  1.00 43.03  ? 58   PRO C CG  1 
ATOM   6292  C  CD  . PRO C 1 58  ? -29.932 32.807  19.131  1.00 29.62  ? 58   PRO C CD  1 
ATOM   6293  N  N   . ASN C 1 59  ? -26.881 35.064  18.415  1.00 61.90  ? 59   ASN C N   1 
ATOM   6294  C  CA  . ASN C 1 59  ? -25.908 36.151  18.286  1.00 60.66  ? 59   ASN C CA  1 
ATOM   6295  C  C   . ASN C 1 59  ? -24.627 35.921  19.083  1.00 53.00  ? 59   ASN C C   1 
ATOM   6296  O  O   . ASN C 1 59  ? -23.677 36.692  18.962  1.00 44.67  ? 59   ASN C O   1 
ATOM   6297  C  CB  . ASN C 1 59  ? -26.526 37.500  18.697  1.00 71.46  ? 59   ASN C CB  1 
ATOM   6298  C  CG  . ASN C 1 59  ? -27.844 37.803  17.981  1.00 73.80  ? 59   ASN C CG  1 
ATOM   6299  O  OD1 . ASN C 1 59  ? -28.559 36.904  17.545  1.00 68.42  ? 59   ASN C OD1 1 
ATOM   6300  N  ND2 . ASN C 1 59  ? -28.172 39.084  17.879  1.00 76.24  ? 59   ASN C ND2 1 
ATOM   6301  N  N   . GLN C 1 60  ? -24.598 34.862  19.890  1.00 47.68  ? 60   GLN C N   1 
ATOM   6302  C  CA  . GLN C 1 60  ? -23.552 34.715  20.890  1.00 41.69  ? 60   GLN C CA  1 
ATOM   6303  C  C   . GLN C 1 60  ? -22.845 33.391  20.787  1.00 38.80  ? 60   GLN C C   1 
ATOM   6304  O  O   . GLN C 1 60  ? -21.736 33.234  21.297  1.00 48.97  ? 60   GLN C O   1 
ATOM   6305  C  CB  . GLN C 1 60  ? -24.129 34.887  22.296  1.00 38.23  ? 60   GLN C CB  1 
ATOM   6306  C  CG  . GLN C 1 60  ? -25.564 35.379  22.303  1.00 57.11  ? 60   GLN C CG  1 
ATOM   6307  C  CD  . GLN C 1 60  ? -25.824 36.434  23.370  1.00 68.74  ? 60   GLN C CD  1 
ATOM   6308  O  OE1 . GLN C 1 60  ? -26.924 36.506  23.930  1.00 61.55  ? 60   GLN C OE1 1 
ATOM   6309  N  NE2 . GLN C 1 60  ? -24.812 37.261  23.656  1.00 60.65  ? 60   GLN C NE2 1 
ATOM   6310  N  N   . ALA C 1 61  ? -23.485 32.432  20.137  1.00 29.14  ? 61   ALA C N   1 
ATOM   6311  C  CA  . ALA C 1 61  ? -22.858 31.129  19.941  1.00 32.73  ? 61   ALA C CA  1 
ATOM   6312  C  C   . ALA C 1 61  ? -22.686 30.882  18.455  1.00 31.79  ? 61   ALA C C   1 
ATOM   6313  O  O   . ALA C 1 61  ? -23.631 31.020  17.689  1.00 31.09  ? 61   ALA C O   1 
ATOM   6314  C  CB  . ALA C 1 61  ? -23.684 30.017  20.584  1.00 40.95  ? 61   ALA C CB  1 
ATOM   6315  N  N   . LYS C 1 62  ? -21.468 30.540  18.050  1.00 33.43  ? 62   LYS C N   1 
ATOM   6316  C  CA  . LYS C 1 62  ? -21.172 30.279  16.645  1.00 29.18  ? 62   LYS C CA  1 
ATOM   6317  C  C   . LYS C 1 62  ? -20.216 29.090  16.489  1.00 26.96  ? 62   LYS C C   1 
ATOM   6318  O  O   . LYS C 1 62  ? -19.203 29.007  17.177  1.00 41.61  ? 62   LYS C O   1 
ATOM   6319  C  CB  . LYS C 1 62  ? -20.574 31.528  15.987  1.00 30.79  ? 62   LYS C CB  1 
ATOM   6320  C  CG  . LYS C 1 62  ? -20.241 31.344  14.508  1.00 40.03  ? 62   LYS C CG  1 
ATOM   6321  C  CD  . LYS C 1 62  ? -19.809 32.653  13.896  1.00 56.78  ? 62   LYS C CD  1 
ATOM   6322  C  CE  . LYS C 1 62  ? -19.285 32.448  12.500  1.00 72.13  ? 62   LYS C CE  1 
ATOM   6323  N  NZ  . LYS C 1 62  ? -20.292 31.750  11.668  1.00 82.89  ? 62   LYS C NZ  1 
ATOM   6324  N  N   . VAL C 1 63  ? -20.539 28.175  15.583  1.00 31.53  ? 63   VAL C N   1 
ATOM   6325  C  CA  . VAL C 1 63  ? -19.704 26.990  15.375  1.00 33.40  ? 63   VAL C CA  1 
ATOM   6326  C  C   . VAL C 1 63  ? -18.636 27.194  14.291  1.00 44.01  ? 63   VAL C C   1 
ATOM   6327  O  O   . VAL C 1 63  ? -18.903 27.739  13.210  1.00 30.23  ? 63   VAL C O   1 
ATOM   6328  C  CB  . VAL C 1 63  ? -20.549 25.742  15.044  1.00 24.67  ? 63   VAL C CB  1 
ATOM   6329  C  CG1 . VAL C 1 63  ? -19.663 24.613  14.579  1.00 17.56  ? 63   VAL C CG1 1 
ATOM   6330  C  CG2 . VAL C 1 63  ? -21.335 25.314  16.265  1.00 38.31  ? 63   VAL C CG2 1 
ATOM   6331  N  N   . HIS C 1 64  ? -17.424 26.745  14.603  1.00 45.56  ? 64   HIS C N   1 
ATOM   6332  C  CA  . HIS C 1 64  ? -16.289 26.904  13.715  1.00 28.52  ? 64   HIS C CA  1 
ATOM   6333  C  C   . HIS C 1 64  ? -15.726 25.541  13.365  1.00 32.76  ? 64   HIS C C   1 
ATOM   6334  O  O   . HIS C 1 64  ? -15.545 24.697  14.249  1.00 30.70  ? 64   HIS C O   1 
ATOM   6335  C  CB  . HIS C 1 64  ? -15.233 27.795  14.373  1.00 23.99  ? 64   HIS C CB  1 
ATOM   6336  C  CG  . HIS C 1 64  ? -15.732 29.177  14.670  1.00 41.66  ? 64   HIS C CG  1 
ATOM   6337  N  ND1 . HIS C 1 64  ? -15.698 30.197  13.744  1.00 45.38  ? 64   HIS C ND1 1 
ATOM   6338  C  CD2 . HIS C 1 64  ? -16.325 29.696  15.773  1.00 46.28  ? 64   HIS C CD2 1 
ATOM   6339  C  CE1 . HIS C 1 64  ? -16.234 31.286  14.268  1.00 40.78  ? 64   HIS C CE1 1 
ATOM   6340  N  NE2 . HIS C 1 64  ? -16.621 31.008  15.499  1.00 39.73  ? 64   HIS C NE2 1 
ATOM   6341  N  N   . PHE C 1 65  ? -15.493 25.334  12.065  1.00 36.82  ? 65   PHE C N   1 
ATOM   6342  C  CA  . PHE C 1 65  ? -14.902 24.104  11.525  1.00 38.77  ? 65   PHE C CA  1 
ATOM   6343  C  C   . PHE C 1 65  ? -13.404 24.307  11.346  1.00 36.79  ? 65   PHE C C   1 
ATOM   6344  O  O   . PHE C 1 65  ? -12.976 25.217  10.633  1.00 39.87  ? 65   PHE C O   1 
ATOM   6345  C  CB  . PHE C 1 65  ? -15.549 23.723  10.181  1.00 31.65  ? 65   PHE C CB  1 
ATOM   6346  C  CG  . PHE C 1 65  ? -14.854 22.586  9.460   1.00 33.58  ? 65   PHE C CG  1 
ATOM   6347  C  CD1 . PHE C 1 65  ? -13.854 22.844  8.540   1.00 38.12  ? 65   PHE C CD1 1 
ATOM   6348  C  CD2 . PHE C 1 65  ? -15.207 21.264  9.696   1.00 34.54  ? 65   PHE C CD2 1 
ATOM   6349  C  CE1 . PHE C 1 65  ? -13.218 21.818  7.876   1.00 42.98  ? 65   PHE C CE1 1 
ATOM   6350  C  CE2 . PHE C 1 65  ? -14.571 20.233  9.031   1.00 38.91  ? 65   PHE C CE2 1 
ATOM   6351  C  CZ  . PHE C 1 65  ? -13.576 20.511  8.126   1.00 50.56  ? 65   PHE C CZ  1 
ATOM   6352  N  N   . LEU C 1 66  ? -12.611 23.461  12.000  1.00 39.01  ? 66   LEU C N   1 
ATOM   6353  C  CA  . LEU C 1 66  ? -11.159 23.606  12.002  1.00 21.12  ? 66   LEU C CA  1 
ATOM   6354  C  C   . LEU C 1 66  ? -10.515 22.608  11.058  1.00 28.39  ? 66   LEU C C   1 
ATOM   6355  O  O   . LEU C 1 66  ? -9.456  22.867  10.488  1.00 40.60  ? 66   LEU C O   1 
ATOM   6356  C  CB  . LEU C 1 66  ? -10.612 23.420  13.412  1.00 23.18  ? 66   LEU C CB  1 
ATOM   6357  C  CG  . LEU C 1 66  ? -11.281 24.168  14.572  1.00 26.87  ? 66   LEU C CG  1 
ATOM   6358  C  CD1 . LEU C 1 66  ? -10.416 24.005  15.807  1.00 25.00  ? 66   LEU C CD1 1 
ATOM   6359  C  CD2 . LEU C 1 66  ? -11.508 25.647  14.267  1.00 13.28  ? 66   LEU C CD2 1 
ATOM   6360  N  N   . GLY C 1 67  ? -11.162 21.464  10.881  1.00 27.47  ? 67   GLY C N   1 
ATOM   6361  C  CA  . GLY C 1 67  ? -10.657 20.447  9.974   1.00 36.84  ? 67   GLY C CA  1 
ATOM   6362  C  C   . GLY C 1 67  ? -11.277 19.104  10.286  1.00 36.68  ? 67   GLY C C   1 
ATOM   6363  O  O   . GLY C 1 67  ? -12.209 19.016  11.073  1.00 49.26  ? 67   GLY C O   1 
ATOM   6364  N  N   . ARG C 1 68  ? -10.762 18.047  9.687   1.00 34.75  ? 68   ARG C N   1 
ATOM   6365  C  CA  . ARG C 1 68  ? -11.287 16.722  9.982   1.00 30.49  ? 68   ARG C CA  1 
ATOM   6366  C  C   . ARG C 1 68  ? -10.197 15.747  10.407  1.00 38.28  ? 68   ARG C C   1 
ATOM   6367  O  O   . ARG C 1 68  ? -9.031  15.890  10.035  1.00 43.68  ? 68   ARG C O   1 
ATOM   6368  C  CB  . ARG C 1 68  ? -12.056 16.168  8.787   1.00 23.34  ? 68   ARG C CB  1 
ATOM   6369  C  CG  . ARG C 1 68  ? -13.570 16.262  8.933   1.00 36.18  ? 68   ARG C CG  1 
ATOM   6370  C  CD  . ARG C 1 68  ? -14.233 16.532  7.597   1.00 39.40  ? 68   ARG C CD  1 
ATOM   6371  N  NE  . ARG C 1 68  ? -15.678 16.430  7.675   1.00 40.98  ? 68   ARG C NE  1 
ATOM   6372  C  CZ  . ARG C 1 68  ? -16.508 17.077  6.868   1.00 58.07  ? 68   ARG C CZ  1 
ATOM   6373  N  NH1 . ARG C 1 68  ? -16.028 17.874  5.928   1.00 67.19  ? 68   ARG C NH1 1 
ATOM   6374  N  NH2 . ARG C 1 68  ? -17.816 16.935  7.008   1.00 70.89  ? 68   ARG C NH2 1 
ATOM   6375  N  N   . SER C 1 69  ? -10.584 14.760  11.200  1.00 30.02  ? 69   SER C N   1 
ATOM   6376  C  CA  . SER C 1 69  ? -9.660  13.727  11.627  1.00 24.70  ? 69   SER C CA  1 
ATOM   6377  C  C   . SER C 1 69  ? -9.387  12.768  10.469  1.00 29.50  ? 69   SER C C   1 
ATOM   6378  O  O   . SER C 1 69  ? -10.094 12.784  9.466   1.00 24.33  ? 69   SER C O   1 
ATOM   6379  C  CB  . SER C 1 69  ? -10.247 12.957  12.816  1.00 25.97  ? 69   SER C CB  1 
ATOM   6380  O  OG  . SER C 1 69  ? -11.316 12.128  12.396  1.00 32.53  ? 69   SER C OG  1 
ATOM   6381  N  N   . LEU C 1 70  ? -8.356  11.941  10.613  1.00 33.23  ? 70   LEU C N   1 
ATOM   6382  C  CA  . LEU C 1 70  ? -8.115  10.860  9.668   1.00 34.33  ? 70   LEU C CA  1 
ATOM   6383  C  C   . LEU C 1 70  ? -9.431  10.185  9.291   1.00 36.59  ? 70   LEU C C   1 
ATOM   6384  O  O   . LEU C 1 70  ? -9.732  10.006  8.113   1.00 37.65  ? 70   LEU C O   1 
ATOM   6385  C  CB  . LEU C 1 70  ? -7.174  9.815   10.273  1.00 40.70  ? 70   LEU C CB  1 
ATOM   6386  C  CG  . LEU C 1 70  ? -5.708  10.205  10.492  1.00 43.95  ? 70   LEU C CG  1 
ATOM   6387  C  CD1 . LEU C 1 70  ? -4.943  9.079   11.193  1.00 45.52  ? 70   LEU C CD1 1 
ATOM   6388  C  CD2 . LEU C 1 70  ? -5.047  10.561  9.168   1.00 23.58  ? 70   LEU C CD2 1 
ATOM   6389  N  N   . GLU C 1 71  ? -10.220 9.820   10.296  1.00 34.14  ? 71   GLU C N   1 
ATOM   6390  C  CA  . GLU C 1 71  ? -11.399 9.000   10.063  1.00 32.41  ? 71   GLU C CA  1 
ATOM   6391  C  C   . GLU C 1 71  ? -12.671 9.802   9.824   1.00 39.53  ? 71   GLU C C   1 
ATOM   6392  O  O   . GLU C 1 71  ? -13.772 9.292   10.013  1.00 41.33  ? 71   GLU C O   1 
ATOM   6393  C  CB  . GLU C 1 71  ? -11.588 8.013   11.203  1.00 38.29  ? 71   GLU C CB  1 
ATOM   6394  C  CG  . GLU C 1 71  ? -10.396 7.113   11.396  1.00 39.15  ? 71   GLU C CG  1 
ATOM   6395  C  CD  . GLU C 1 71  ? -10.583 6.154   12.544  1.00 56.09  ? 71   GLU C CD  1 
ATOM   6396  O  OE1 . GLU C 1 71  ? -11.283 6.508   13.518  1.00 54.46  ? 71   GLU C OE1 1 
ATOM   6397  O  OE2 . GLU C 1 71  ? -10.028 5.040   12.476  1.00 68.02  ? 71   GLU C OE2 1 
ATOM   6398  N  N   . GLY C 1 72  ? -12.512 11.054  9.399   1.00 47.34  ? 72   GLY C N   1 
ATOM   6399  C  CA  . GLY C 1 72  ? -13.627 11.841  8.897   1.00 40.56  ? 72   GLY C CA  1 
ATOM   6400  C  C   . GLY C 1 72  ? -14.394 12.646  9.928   1.00 45.46  ? 72   GLY C C   1 
ATOM   6401  O  O   . GLY C 1 72  ? -15.295 13.412  9.569   1.00 45.85  ? 72   GLY C O   1 
ATOM   6402  N  N   . ARG C 1 73  ? -14.038 12.482  11.202  1.00 43.82  ? 73   ARG C N   1 
ATOM   6403  C  CA  . ARG C 1 73  ? -14.714 13.187  12.289  1.00 44.42  ? 73   ARG C CA  1 
ATOM   6404  C  C   . ARG C 1 73  ? -14.397 14.670  12.293  1.00 44.64  ? 73   ARG C C   1 
ATOM   6405  O  O   . ARG C 1 73  ? -13.246 15.063  12.113  1.00 50.39  ? 73   ARG C O   1 
ATOM   6406  C  CB  . ARG C 1 73  ? -14.346 12.577  13.642  1.00 40.63  ? 73   ARG C CB  1 
ATOM   6407  C  CG  . ARG C 1 73  ? -14.807 11.142  13.793  1.00 43.22  ? 73   ARG C CG  1 
ATOM   6408  C  CD  . ARG C 1 73  ? -14.405 10.571  15.131  1.00 36.35  ? 73   ARG C CD  1 
ATOM   6409  N  NE  . ARG C 1 73  ? -13.986 9.182   15.002  1.00 28.96  ? 73   ARG C NE  1 
ATOM   6410  C  CZ  . ARG C 1 73  ? -14.832 8.169   15.013  1.00 34.67  ? 73   ARG C CZ  1 
ATOM   6411  N  NH1 . ARG C 1 73  ? -14.384 6.928   14.897  1.00 39.41  ? 73   ARG C NH1 1 
ATOM   6412  N  NH2 . ARG C 1 73  ? -16.129 8.410   15.146  1.00 46.91  ? 73   ARG C NH2 1 
ATOM   6413  N  N   . ASN C 1 74  ? -15.421 15.488  12.516  1.00 50.20  ? 74   ASN C N   1 
ATOM   6414  C  CA  . ASN C 1 74  ? -15.259 16.943  12.501  1.00 47.15  ? 74   ASN C CA  1 
ATOM   6415  C  C   . ASN C 1 74  ? -14.612 17.539  13.748  1.00 40.59  ? 74   ASN C C   1 
ATOM   6416  O  O   . ASN C 1 74  ? -15.047 17.310  14.879  1.00 34.12  ? 74   ASN C O   1 
ATOM   6417  C  CB  . ASN C 1 74  ? -16.592 17.643  12.231  1.00 44.41  ? 74   ASN C CB  1 
ATOM   6418  C  CG  . ASN C 1 74  ? -16.985 17.600  10.769  1.00 51.66  ? 74   ASN C CG  1 
ATOM   6419  O  OD1 . ASN C 1 74  ? -16.151 17.766  9.883   1.00 50.90  ? 74   ASN C OD1 1 
ATOM   6420  N  ND2 . ASN C 1 74  ? -18.267 17.385  10.511  1.00 63.58  ? 74   ASN C ND2 1 
ATOM   6421  N  N   . LEU C 1 75  ? -13.565 18.317  13.516  1.00 44.10  ? 75   LEU C N   1 
ATOM   6422  C  CA  . LEU C 1 75  ? -12.946 19.100  14.568  1.00 44.64  ? 75   LEU C CA  1 
ATOM   6423  C  C   . LEU C 1 75  ? -13.651 20.459  14.641  1.00 29.75  ? 75   LEU C C   1 
ATOM   6424  O  O   . LEU C 1 75  ? -13.498 21.299  13.760  1.00 44.35  ? 75   LEU C O   1 
ATOM   6425  C  CB  . LEU C 1 75  ? -11.444 19.255  14.296  1.00 43.84  ? 75   LEU C CB  1 
ATOM   6426  C  CG  . LEU C 1 75  ? -10.538 18.042  14.551  1.00 41.97  ? 75   LEU C CG  1 
ATOM   6427  C  CD1 . LEU C 1 75  ? -11.300 16.724  14.444  1.00 51.80  ? 75   LEU C CD1 1 
ATOM   6428  C  CD2 . LEU C 1 75  ? -9.328  18.042  13.608  1.00 44.13  ? 75   LEU C CD2 1 
ATOM   6429  N  N   . LEU C 1 76  ? -14.428 20.657  15.698  1.00 23.05  ? 76   LEU C N   1 
ATOM   6430  C  CA  . LEU C 1 76  ? -15.269 21.840  15.851  1.00 30.81  ? 76   LEU C CA  1 
ATOM   6431  C  C   . LEU C 1 76  ? -14.907 22.709  17.055  1.00 35.42  ? 76   LEU C C   1 
ATOM   6432  O  O   . LEU C 1 76  ? -14.489 22.198  18.090  1.00 48.07  ? 76   LEU C O   1 
ATOM   6433  C  CB  . LEU C 1 76  ? -16.709 21.394  16.031  1.00 37.01  ? 76   LEU C CB  1 
ATOM   6434  C  CG  . LEU C 1 76  ? -17.338 20.610  14.889  1.00 40.21  ? 76   LEU C CG  1 
ATOM   6435  C  CD1 . LEU C 1 76  ? -18.697 20.076  15.340  1.00 39.31  ? 76   LEU C CD1 1 
ATOM   6436  C  CD2 . LEU C 1 76  ? -17.461 21.497  13.687  1.00 39.16  ? 76   LEU C CD2 1 
ATOM   6437  N  N   . ALA C 1 77  ? -15.098 24.021  16.930  1.00 40.12  ? 77   ALA C N   1 
ATOM   6438  C  CA  . ALA C 1 77  ? -14.880 24.921  18.062  1.00 27.47  ? 77   ALA C CA  1 
ATOM   6439  C  C   . ALA C 1 77  ? -16.037 25.854  18.141  1.00 29.45  ? 77   ALA C C   1 
ATOM   6440  O  O   . ALA C 1 77  ? -16.413 26.459  17.135  1.00 37.22  ? 77   ALA C O   1 
ATOM   6441  C  CB  . ALA C 1 77  ? -13.581 25.718  17.922  1.00 21.23  ? 77   ALA C CB  1 
ATOM   6442  N  N   . LEU C 1 78  ? -16.596 25.965  19.341  1.00 31.12  ? 78   LEU C N   1 
ATOM   6443  C  CA  . LEU C 1 78  ? -17.706 26.861  19.597  1.00 19.82  ? 78   LEU C CA  1 
ATOM   6444  C  C   . LEU C 1 78  ? -17.207 28.184  20.161  1.00 30.85  ? 78   LEU C C   1 
ATOM   6445  O  O   . LEU C 1 78  ? -16.511 28.218  21.184  1.00 29.16  ? 78   LEU C O   1 
ATOM   6446  C  CB  . LEU C 1 78  ? -18.695 26.225  20.565  1.00 22.46  ? 78   LEU C CB  1 
ATOM   6447  C  CG  . LEU C 1 78  ? -19.955 27.064  20.811  1.00 34.76  ? 78   LEU C CG  1 
ATOM   6448  C  CD1 . LEU C 1 78  ? -20.926 26.906  19.645  1.00 25.10  ? 78   LEU C CD1 1 
ATOM   6449  C  CD2 . LEU C 1 78  ? -20.619 26.667  22.132  1.00 33.37  ? 78   LEU C CD2 1 
ATOM   6450  N  N   . GLN C 1 79  ? -17.553 29.268  19.475  1.00 29.92  ? 79   GLN C N   1 
ATOM   6451  C  CA  . GLN C 1 79  ? -17.197 30.615  19.892  1.00 16.70  ? 79   GLN C CA  1 
ATOM   6452  C  C   . GLN C 1 79  ? -18.347 31.230  20.647  1.00 29.00  ? 79   GLN C C   1 
ATOM   6453  O  O   . GLN C 1 79  ? -19.520 31.087  20.266  1.00 30.96  ? 79   GLN C O   1 
ATOM   6454  C  CB  . GLN C 1 79  ? -16.914 31.476  18.667  1.00 31.39  ? 79   GLN C CB  1 
ATOM   6455  C  CG  . GLN C 1 79  ? -17.046 32.968  18.906  1.00 28.14  ? 79   GLN C CG  1 
ATOM   6456  C  CD  . GLN C 1 79  ? -16.857 33.761  17.634  1.00 28.70  ? 79   GLN C CD  1 
ATOM   6457  O  OE1 . GLN C 1 79  ? -17.081 33.248  16.541  1.00 27.27  ? 79   GLN C OE1 1 
ATOM   6458  N  NE2 . GLN C 1 79  ? -16.452 35.020  17.766  1.00 32.47  ? 79   GLN C NE2 1 
ATOM   6459  N  N   . ILE C 1 80  ? -18.006 31.933  21.713  1.00 28.34  ? 80   ILE C N   1 
ATOM   6460  C  CA  . ILE C 1 80  ? -18.989 32.620  22.518  1.00 28.19  ? 80   ILE C CA  1 
ATOM   6461  C  C   . ILE C 1 80  ? -18.510 34.035  22.682  1.00 31.92  ? 80   ILE C C   1 
ATOM   6462  O  O   . ILE C 1 80  ? -17.412 34.266  23.166  1.00 42.48  ? 80   ILE C O   1 
ATOM   6463  C  CB  . ILE C 1 80  ? -19.116 31.981  23.908  1.00 30.75  ? 80   ILE C CB  1 
ATOM   6464  C  CG1 . ILE C 1 80  ? -19.605 30.535  23.784  1.00 22.73  ? 80   ILE C CG1 1 
ATOM   6465  C  CG2 . ILE C 1 80  ? -20.054 32.811  24.805  1.00 24.59  ? 80   ILE C CG2 1 
ATOM   6466  C  CD1 . ILE C 1 80  ? -19.528 29.754  25.068  1.00 25.02  ? 80   ILE C CD1 1 
ATOM   6467  N  N   . SER C 1 81  ? -19.333 34.989  22.288  1.00 38.60  ? 81   SER C N   1 
ATOM   6468  C  CA  . SER C 1 81  ? -18.921 36.377  22.341  1.00 39.43  ? 81   SER C CA  1 
ATOM   6469  C  C   . SER C 1 81  ? -20.109 37.294  22.599  1.00 41.83  ? 81   SER C C   1 
ATOM   6470  O  O   . SER C 1 81  ? -21.260 36.871  22.515  1.00 47.19  ? 81   SER C O   1 
ATOM   6471  C  CB  . SER C 1 81  ? -18.259 36.743  21.020  1.00 32.23  ? 81   SER C CB  1 
ATOM   6472  O  OG  . SER C 1 81  ? -19.108 36.380  19.944  1.00 53.11  ? 81   SER C OG  1 
ATOM   6473  N  N   . ARG C 1 82  ? -19.832 38.554  22.916  1.00 45.45  ? 82   ARG C N   1 
ATOM   6474  C  CA  . ARG C 1 82  ? -20.895 39.546  23.006  1.00 47.81  ? 82   ARG C CA  1 
ATOM   6475  C  C   . ARG C 1 82  ? -21.647 39.593  21.672  1.00 51.62  ? 82   ARG C C   1 
ATOM   6476  O  O   . ARG C 1 82  ? -22.875 39.601  21.650  1.00 59.44  ? 82   ARG C O   1 
ATOM   6477  C  CB  . ARG C 1 82  ? -20.328 40.924  23.363  1.00 50.67  ? 82   ARG C CB  1 
ATOM   6478  C  CG  . ARG C 1 82  ? -21.394 41.983  23.638  1.00 55.59  ? 82   ARG C CG  1 
ATOM   6479  C  CD  . ARG C 1 82  ? -20.780 43.347  23.890  1.00 62.13  ? 82   ARG C CD  1 
ATOM   6480  N  NE  . ARG C 1 82  ? -21.137 43.903  25.173  1.00 64.26  ? 82   ARG C NE  1 
ATOM   6481  C  CZ  . ARG C 1 82  ? -21.042 45.175  25.554  1.00 71.78  ? 82   ARG C CZ  1 
ATOM   6482  N  NH1 . ARG C 1 82  ? -20.601 46.136  24.751  1.00 54.67  ? 82   ARG C NH1 1 
ATOM   6483  N  NH2 . ARG C 1 82  ? -21.413 45.477  26.789  1.00 82.72  ? 82   ARG C NH2 1 
ATOM   6484  N  N   . ASN C 1 83  ? -20.896 39.608  20.571  1.00 40.88  ? 83   ASN C N   1 
ATOM   6485  C  CA  . ASN C 1 83  ? -21.456 39.595  19.224  1.00 36.41  ? 83   ASN C CA  1 
ATOM   6486  C  C   . ASN C 1 83  ? -20.621 38.736  18.275  1.00 40.26  ? 83   ASN C C   1 
ATOM   6487  O  O   . ASN C 1 83  ? -19.534 39.142  17.844  1.00 39.80  ? 83   ASN C O   1 
ATOM   6488  C  CB  . ASN C 1 83  ? -21.551 41.016  18.681  1.00 53.11  ? 83   ASN C CB  1 
ATOM   6489  C  CG  . ASN C 1 83  ? -21.750 41.048  17.182  1.00 65.98  ? 83   ASN C CG  1 
ATOM   6490  O  OD1 . ASN C 1 83  ? -22.352 40.139  16.608  1.00 65.50  ? 83   ASN C OD1 1 
ATOM   6491  N  ND2 . ASN C 1 83  ? -21.239 42.095  16.536  1.00 67.74  ? 83   ASN C ND2 1 
ATOM   6492  N  N   . THR C 1 84  ? -21.144 37.562  17.932  1.00 37.94  ? 84   THR C N   1 
ATOM   6493  C  CA  . THR C 1 84  ? -20.393 36.564  17.168  1.00 23.58  ? 84   THR C CA  1 
ATOM   6494  C  C   . THR C 1 84  ? -20.025 37.013  15.756  1.00 33.89  ? 84   THR C C   1 
ATOM   6495  O  O   . THR C 1 84  ? -19.118 36.450  15.133  1.00 41.59  ? 84   THR C O   1 
ATOM   6496  C  CB  . THR C 1 84  ? -21.173 35.249  17.080  1.00 32.94  ? 84   THR C CB  1 
ATOM   6497  O  OG1 . THR C 1 84  ? -20.300 34.156  17.374  1.00 41.12  ? 84   THR C OG1 1 
ATOM   6498  C  CG2 . THR C 1 84  ? -21.786 35.068  15.710  1.00 11.49  ? 84   THR C CG2 1 
ATOM   6499  N  N   . ARG C 1 85  ? -20.725 38.026  15.250  1.00 37.70  ? 85   ARG C N   1 
ATOM   6500  C  CA  . ARG C 1 85  ? -20.450 38.538  13.909  1.00 41.32  ? 85   ARG C CA  1 
ATOM   6501  C  C   . ARG C 1 85  ? -18.990 38.957  13.772  1.00 44.33  ? 85   ARG C C   1 
ATOM   6502  O  O   . ARG C 1 85  ? -18.316 38.606  12.807  1.00 48.47  ? 85   ARG C O   1 
ATOM   6503  C  CB  . ARG C 1 85  ? -21.365 39.719  13.558  1.00 49.82  ? 85   ARG C CB  1 
ATOM   6504  C  CG  . ARG C 1 85  ? -22.839 39.378  13.458  1.00 72.34  ? 85   ARG C CG  1 
ATOM   6505  C  CD  . ARG C 1 85  ? -23.580 40.359  12.545  1.00 96.50  ? 85   ARG C CD  1 
ATOM   6506  N  NE  . ARG C 1 85  ? -23.405 40.048  11.124  1.00 105.15 ? 85   ARG C NE  1 
ATOM   6507  C  CZ  . ARG C 1 85  ? -22.500 40.615  10.329  1.00 101.78 ? 85   ARG C CZ  1 
ATOM   6508  N  NH1 . ARG C 1 85  ? -22.421 40.257  9.053   1.00 98.85  ? 85   ARG C NH1 1 
ATOM   6509  N  NH2 . ARG C 1 85  ? -21.673 41.538  10.806  1.00 98.27  ? 85   ARG C NH2 1 
ATOM   6510  N  N   . SER C 1 86  ? -18.501 39.715  14.739  1.00 42.96  ? 86   SER C N   1 
ATOM   6511  C  CA  . SER C 1 86  ? -17.133 40.180  14.680  1.00 43.46  ? 86   SER C CA  1 
ATOM   6512  C  C   . SER C 1 86  ? -16.439 39.971  16.007  1.00 61.02  ? 86   SER C C   1 
ATOM   6513  O  O   . SER C 1 86  ? -16.824 39.118  16.810  1.00 74.59  ? 86   SER C O   1 
ATOM   6514  C  CB  . SER C 1 86  ? -17.106 41.662  14.346  1.00 35.13  ? 86   SER C CB  1 
ATOM   6515  O  OG  . SER C 1 86  ? -17.664 41.875  13.078  1.00 38.03  ? 86   SER C OG  1 
ATOM   6516  N  N   . ARG C 1 87  ? -15.397 40.760  16.216  1.00 52.52  ? 87   ARG C N   1 
ATOM   6517  C  CA  . ARG C 1 87  ? -14.736 40.844  17.502  1.00 44.83  ? 87   ARG C CA  1 
ATOM   6518  C  C   . ARG C 1 87  ? -14.570 42.312  17.794  1.00 40.70  ? 87   ARG C C   1 
ATOM   6519  O  O   . ARG C 1 87  ? -13.943 43.033  17.031  1.00 34.58  ? 87   ARG C O   1 
ATOM   6520  C  CB  . ARG C 1 87  ? -13.358 40.191  17.463  1.00 20.82  ? 87   ARG C CB  1 
ATOM   6521  C  CG  . ARG C 1 87  ? -12.971 39.532  18.759  1.00 21.18  ? 87   ARG C CG  1 
ATOM   6522  C  CD  . ARG C 1 87  ? -11.560 39.055  18.716  1.00 23.09  ? 87   ARG C CD  1 
ATOM   6523  N  NE  . ARG C 1 87  ? -10.676 40.171  18.974  1.00 38.66  ? 87   ARG C NE  1 
ATOM   6524  C  CZ  . ARG C 1 87  ? -9.851  40.703  18.085  1.00 40.48  ? 87   ARG C CZ  1 
ATOM   6525  N  NH1 . ARG C 1 87  ? -9.780  40.213  16.859  1.00 44.75  ? 87   ARG C NH1 1 
ATOM   6526  N  NH2 . ARG C 1 87  ? -9.087  41.722  18.436  1.00 47.34  ? 87   ARG C NH2 1 
ATOM   6527  N  N   . ASN C 1 88  ? -15.149 42.767  18.889  1.00 45.26  ? 88   ASN C N   1 
ATOM   6528  C  CA  . ASN C 1 88  ? -15.006 44.163  19.258  1.00 38.08  ? 88   ASN C CA  1 
ATOM   6529  C  C   . ASN C 1 88  ? -13.545 44.528  19.469  1.00 35.41  ? 88   ASN C C   1 
ATOM   6530  O  O   . ASN C 1 88  ? -12.787 43.775  20.086  1.00 39.14  ? 88   ASN C O   1 
ATOM   6531  C  CB  . ASN C 1 88  ? -15.827 44.459  20.507  1.00 46.59  ? 88   ASN C CB  1 
ATOM   6532  C  CG  . ASN C 1 88  ? -17.311 44.297  20.265  1.00 54.83  ? 88   ASN C CG  1 
ATOM   6533  O  OD1 . ASN C 1 88  ? -18.000 43.559  20.971  1.00 66.22  ? 88   ASN C OD1 1 
ATOM   6534  N  ND2 . ASN C 1 88  ? -17.807 44.970  19.240  1.00 62.62  ? 88   ASN C ND2 1 
ATOM   6535  N  N   . LEU C 1 89  ? -13.149 45.681  18.941  1.00 25.29  ? 89   LEU C N   1 
ATOM   6536  C  CA  . LEU C 1 89  ? -11.775 46.146  19.074  1.00 35.53  ? 89   LEU C CA  1 
ATOM   6537  C  C   . LEU C 1 89  ? -11.260 45.953  20.519  1.00 44.53  ? 89   LEU C C   1 
ATOM   6538  O  O   . LEU C 1 89  ? -11.938 46.291  21.502  1.00 38.03  ? 89   LEU C O   1 
ATOM   6539  C  CB  . LEU C 1 89  ? -11.654 47.610  18.611  1.00 33.35  ? 89   LEU C CB  1 
ATOM   6540  C  CG  . LEU C 1 89  ? -10.242 48.161  18.383  1.00 28.81  ? 89   LEU C CG  1 
ATOM   6541  C  CD1 . LEU C 1 89  ? -9.655  47.592  17.135  1.00 18.47  ? 89   LEU C CD1 1 
ATOM   6542  C  CD2 . LEU C 1 89  ? -10.251 49.674  18.317  1.00 36.73  ? 89   LEU C CD2 1 
ATOM   6543  N  N   . LEU C 1 90  ? -10.070 45.372  20.632  1.00 45.81  ? 90   LEU C N   1 
ATOM   6544  C  CA  . LEU C 1 90  ? -9.402  45.182  21.917  1.00 43.27  ? 90   LEU C CA  1 
ATOM   6545  C  C   . LEU C 1 90  ? -10.013 44.083  22.801  1.00 45.20  ? 90   LEU C C   1 
ATOM   6546  O  O   . LEU C 1 90  ? -9.561  43.875  23.935  1.00 44.78  ? 90   LEU C O   1 
ATOM   6547  C  CB  . LEU C 1 90  ? -9.263  46.519  22.661  1.00 34.05  ? 90   LEU C CB  1 
ATOM   6548  C  CG  . LEU C 1 90  ? -8.249  47.454  21.993  1.00 31.98  ? 90   LEU C CG  1 
ATOM   6549  C  CD1 . LEU C 1 90  ? -8.177  48.839  22.654  1.00 19.59  ? 90   LEU C CD1 1 
ATOM   6550  C  CD2 . LEU C 1 90  ? -6.902  46.760  22.026  1.00 28.76  ? 90   LEU C CD2 1 
ATOM   6551  N  N   . THR C 1 91  ? -11.015 43.365  22.294  1.00 34.17  ? 91   THR C N   1 
ATOM   6552  C  CA  . THR C 1 91  ? -11.507 42.214  23.042  1.00 32.87  ? 91   THR C CA  1 
ATOM   6553  C  C   . THR C 1 91  ? -10.560 41.052  22.836  1.00 37.58  ? 91   THR C C   1 
ATOM   6554  O  O   . THR C 1 91  ? -10.294 40.665  21.707  1.00 29.33  ? 91   THR C O   1 
ATOM   6555  C  CB  . THR C 1 91  ? -12.901 41.767  22.635  1.00 23.71  ? 91   THR C CB  1 
ATOM   6556  O  OG1 . THR C 1 91  ? -13.840 42.822  22.879  1.00 29.44  ? 91   THR C OG1 1 
ATOM   6557  C  CG2 . THR C 1 91  ? -13.282 40.537  23.464  1.00 18.31  ? 91   THR C CG2 1 
ATOM   6558  N  N   . PRO C 1 92  ? -10.045 40.494  23.935  1.00 33.77  ? 92   PRO C N   1 
ATOM   6559  C  CA  . PRO C 1 92  ? -9.123  39.357  23.901  1.00 30.53  ? 92   PRO C CA  1 
ATOM   6560  C  C   . PRO C 1 92  ? -9.793  38.117  23.343  1.00 34.55  ? 92   PRO C C   1 
ATOM   6561  O  O   . PRO C 1 92  ? -10.832 37.723  23.868  1.00 31.67  ? 92   PRO C O   1 
ATOM   6562  C  CB  . PRO C 1 92  ? -8.828  39.096  25.383  1.00 35.31  ? 92   PRO C CB  1 
ATOM   6563  C  CG  . PRO C 1 92  ? -9.389  40.239  26.137  1.00 31.90  ? 92   PRO C CG  1 
ATOM   6564  C  CD  . PRO C 1 92  ? -10.442 40.860  25.303  1.00 30.66  ? 92   PRO C CD  1 
ATOM   6565  N  N   . PRO C 1 93  ? -9.199  37.495  22.309  1.00 43.67  ? 93   PRO C N   1 
ATOM   6566  C  CA  . PRO C 1 93  ? -9.620  36.144  21.922  1.00 37.63  ? 93   PRO C CA  1 
ATOM   6567  C  C   . PRO C 1 93  ? -8.857  35.116  22.753  1.00 36.48  ? 93   PRO C C   1 
ATOM   6568  O  O   . PRO C 1 93  ? -7.668  35.269  23.052  1.00 29.69  ? 93   PRO C O   1 
ATOM   6569  C  CB  . PRO C 1 93  ? -9.226  36.053  20.444  1.00 29.78  ? 93   PRO C CB  1 
ATOM   6570  C  CG  . PRO C 1 93  ? -8.166  37.144  20.233  1.00 29.57  ? 93   PRO C CG  1 
ATOM   6571  C  CD  . PRO C 1 93  ? -8.053  37.960  21.511  1.00 27.77  ? 93   PRO C CD  1 
ATOM   6572  N  N   . VAL C 1 94  ? -9.553  34.063  23.138  1.00 33.32  ? 94   VAL C N   1 
ATOM   6573  C  CA  . VAL C 1 94  ? -8.985  33.079  24.023  1.00 26.39  ? 94   VAL C CA  1 
ATOM   6574  C  C   . VAL C 1 94  ? -9.527  31.739  23.588  1.00 20.15  ? 94   VAL C C   1 
ATOM   6575  O  O   . VAL C 1 94  ? -10.586 31.672  22.968  1.00 30.66  ? 94   VAL C O   1 
ATOM   6576  C  CB  . VAL C 1 94  ? -9.434  33.359  25.484  1.00 42.36  ? 94   VAL C CB  1 
ATOM   6577  C  CG1 . VAL C 1 94  ? -8.824  32.354  26.440  1.00 59.87  ? 94   VAL C CG1 1 
ATOM   6578  C  CG2 . VAL C 1 94  ? -9.068  34.782  25.905  1.00 33.44  ? 94   VAL C CG2 1 
ATOM   6579  N  N   . LYS C 1 95  ? -8.831  30.666  23.930  1.00 16.24  ? 95   LYS C N   1 
ATOM   6580  C  CA  . LYS C 1 95  ? -9.332  29.334  23.606  1.00 26.05  ? 95   LYS C CA  1 
ATOM   6581  C  C   . LYS C 1 95  ? -9.134  28.318  24.726  1.00 31.06  ? 95   LYS C C   1 
ATOM   6582  O  O   . LYS C 1 95  ? -8.262  28.485  25.582  1.00 33.05  ? 95   LYS C O   1 
ATOM   6583  C  CB  . LYS C 1 95  ? -8.649  28.832  22.345  1.00 20.27  ? 95   LYS C CB  1 
ATOM   6584  C  CG  . LYS C 1 95  ? -7.130  28.849  22.437  1.00 20.38  ? 95   LYS C CG  1 
ATOM   6585  C  CD  . LYS C 1 95  ? -6.533  29.397  21.150  1.00 23.60  ? 95   LYS C CD  1 
ATOM   6586  C  CE  . LYS C 1 95  ? -5.247  28.676  20.772  1.00 26.23  ? 95   LYS C CE  1 
ATOM   6587  N  NZ  . LYS C 1 95  ? -4.238  28.678  21.853  1.00 39.53  ? 95   LYS C NZ  1 
ATOM   6588  N  N   . TYR C 1 96  ? -9.947  27.265  24.713  1.00 27.19  ? 96   TYR C N   1 
ATOM   6589  C  CA  . TYR C 1 96  ? -9.750  26.105  25.590  1.00 37.83  ? 96   TYR C CA  1 
ATOM   6590  C  C   . TYR C 1 96  ? -9.811  24.839  24.737  1.00 38.06  ? 96   TYR C C   1 
ATOM   6591  O  O   . TYR C 1 96  ? -10.813 24.588  24.067  1.00 30.43  ? 96   TYR C O   1 
ATOM   6592  C  CB  . TYR C 1 96  ? -10.830 26.024  26.677  1.00 25.81  ? 96   TYR C CB  1 
ATOM   6593  C  CG  . TYR C 1 96  ? -10.554 26.818  27.945  1.00 31.10  ? 96   TYR C CG  1 
ATOM   6594  C  CD1 . TYR C 1 96  ? -9.276  27.264  28.257  1.00 28.20  ? 96   TYR C CD1 1 
ATOM   6595  C  CD2 . TYR C 1 96  ? -11.582 27.103  28.849  1.00 37.34  ? 96   TYR C CD2 1 
ATOM   6596  C  CE1 . TYR C 1 96  ? -9.031  27.998  29.432  1.00 29.43  ? 96   TYR C CE1 1 
ATOM   6597  C  CE2 . TYR C 1 96  ? -11.348 27.825  30.024  1.00 41.68  ? 96   TYR C CE2 1 
ATOM   6598  C  CZ  . TYR C 1 96  ? -10.067 28.267  30.310  1.00 41.56  ? 96   TYR C CZ  1 
ATOM   6599  O  OH  . TYR C 1 96  ? -9.832  28.982  31.468  1.00 39.76  ? 96   TYR C OH  1 
ATOM   6600  N  N   . ILE C 1 97  ? -8.747  24.046  24.737  1.00 27.93  ? 97   ILE C N   1 
ATOM   6601  C  CA  . ILE C 1 97  ? -8.807  22.767  24.038  1.00 29.25  ? 97   ILE C CA  1 
ATOM   6602  C  C   . ILE C 1 97  ? -8.713  21.596  25.004  1.00 32.43  ? 97   ILE C C   1 
ATOM   6603  O  O   . ILE C 1 97  ? -8.090  21.690  26.082  1.00 29.06  ? 97   ILE C O   1 
ATOM   6604  C  CB  . ILE C 1 97  ? -7.714  22.627  22.987  1.00 36.92  ? 97   ILE C CB  1 
ATOM   6605  C  CG1 . ILE C 1 97  ? -7.804  23.768  21.976  1.00 36.25  ? 97   ILE C CG1 1 
ATOM   6606  C  CG2 . ILE C 1 97  ? -7.819  21.275  22.288  1.00 32.91  ? 97   ILE C CG2 1 
ATOM   6607  C  CD1 . ILE C 1 97  ? -7.170  25.057  22.465  1.00 42.41  ? 97   ILE C CD1 1 
ATOM   6608  N  N   . ALA C 1 98  ? -9.340  20.492  24.621  1.00 19.33  ? 98   ALA C N   1 
ATOM   6609  C  CA  . ALA C 1 98  ? -9.318  19.299  25.457  1.00 24.32  ? 98   ALA C CA  1 
ATOM   6610  C  C   . ALA C 1 98  ? -9.095  18.021  24.680  1.00 26.10  ? 98   ALA C C   1 
ATOM   6611  O  O   . ALA C 1 98  ? -9.062  18.016  23.454  1.00 35.92  ? 98   ALA C O   1 
ATOM   6612  C  CB  . ALA C 1 98  ? -10.588 19.194  26.261  1.00 14.20  ? 98   ALA C CB  1 
ATOM   6613  N  N   . ASN C 1 99  ? -8.915  16.937  25.418  1.00 38.07  ? 99   ASN C N   1 
ATOM   6614  C  CA  . ASN C 1 99  ? -8.951  15.602  24.843  1.00 28.52  ? 99   ASN C CA  1 
ATOM   6615  C  C   . ASN C 1 99  ? -8.080  15.404  23.593  1.00 42.80  ? 99   ASN C C   1 
ATOM   6616  O  O   . ASN C 1 99  ? -8.463  14.674  22.668  1.00 41.23  ? 99   ASN C O   1 
ATOM   6617  C  CB  . ASN C 1 99  ? -10.399 15.230  24.542  1.00 24.19  ? 99   ASN C CB  1 
ATOM   6618  C  CG  . ASN C 1 99  ? -10.570 13.759  24.260  1.00 44.07  ? 99   ASN C CG  1 
ATOM   6619  O  OD1 . ASN C 1 99  ? -11.123 13.376  23.229  1.00 47.39  ? 99   ASN C OD1 1 
ATOM   6620  N  ND2 . ASN C 1 99  ? -10.088 12.917  25.175  1.00 35.56  ? 99   ASN C ND2 1 
ATOM   6621  N  N   . MET C 1 100 ? -6.912  16.049  23.562  1.00 46.84  ? 100  MET C N   1 
ATOM   6622  C  CA  . MET C 1 100 ? -5.940  15.800  22.486  1.00 44.93  ? 100  MET C CA  1 
ATOM   6623  C  C   . MET C 1 100 ? -5.370  14.380  22.609  1.00 46.16  ? 100  MET C C   1 
ATOM   6624  O  O   . MET C 1 100 ? -5.101  13.718  21.601  1.00 35.73  ? 100  MET C O   1 
ATOM   6625  C  CB  . MET C 1 100 ? -4.812  16.837  22.476  1.00 41.02  ? 100  MET C CB  1 
ATOM   6626  C  CG  . MET C 1 100 ? -3.758  16.637  23.564  1.00 46.36  ? 100  MET C CG  1 
ATOM   6627  S  SD  . MET C 1 100 ? -2.483  17.893  23.447  1.00 52.07  ? 100  MET C SD  1 
ATOM   6628  C  CE  . MET C 1 100 ? -2.212  17.955  21.669  1.00 33.59  ? 100  MET C CE  1 
ATOM   6629  N  N   . HIS C 1 101 ? -5.169  13.933  23.849  1.00 40.65  ? 101  HIS C N   1 
ATOM   6630  C  CA  . HIS C 1 101 ? -5.016  12.518  24.124  1.00 28.06  ? 101  HIS C CA  1 
ATOM   6631  C  C   . HIS C 1 101 ? -6.414  11.953  24.392  1.00 43.66  ? 101  HIS C C   1 
ATOM   6632  O  O   . HIS C 1 101 ? -7.004  12.175  25.465  1.00 36.72  ? 101  HIS C O   1 
ATOM   6633  C  CB  . HIS C 1 101 ? -4.088  12.302  25.307  1.00 25.59  ? 101  HIS C CB  1 
ATOM   6634  C  CG  . HIS C 1 101 ? -2.694  12.787  25.068  1.00 42.26  ? 101  HIS C CG  1 
ATOM   6635  N  ND1 . HIS C 1 101 ? -2.173  13.892  25.702  1.00 47.92  ? 101  HIS C ND1 1 
ATOM   6636  C  CD2 . HIS C 1 101 ? -1.718  12.329  24.246  1.00 56.57  ? 101  HIS C CD2 1 
ATOM   6637  C  CE1 . HIS C 1 101 ? -0.925  14.078  25.306  1.00 54.14  ? 101  HIS C CE1 1 
ATOM   6638  N  NE2 . HIS C 1 101 ? -0.627  13.150  24.413  1.00 56.75  ? 101  HIS C NE2 1 
ATOM   6639  N  N   . GLY C 1 102 ? -6.944  11.247  23.393  1.00 39.10  ? 102  GLY C N   1 
ATOM   6640  C  CA  . GLY C 1 102 ? -8.309  10.740  23.415  1.00 31.35  ? 102  GLY C CA  1 
ATOM   6641  C  C   . GLY C 1 102 ? -8.746  9.971   24.656  1.00 33.98  ? 102  GLY C C   1 
ATOM   6642  O  O   . GLY C 1 102 ? -9.947  9.894   24.932  1.00 46.01  ? 102  GLY C O   1 
ATOM   6643  N  N   . ASP C 1 103 ? -7.793  9.409   25.405  1.00 33.58  ? 103  ASP C N   1 
ATOM   6644  C  CA  . ASP C 1 103 ? -8.106  8.665   26.632  1.00 37.16  ? 103  ASP C CA  1 
ATOM   6645  C  C   . ASP C 1 103 ? -7.997  9.521   27.880  1.00 40.14  ? 103  ASP C C   1 
ATOM   6646  O  O   . ASP C 1 103 ? -8.071  9.002   28.992  1.00 42.01  ? 103  ASP C O   1 
ATOM   6647  C  CB  . ASP C 1 103 ? -7.195  7.451   26.789  1.00 46.91  ? 103  ASP C CB  1 
ATOM   6648  C  CG  . ASP C 1 103 ? -5.724  7.803   26.650  1.00 53.47  ? 103  ASP C CG  1 
ATOM   6649  O  OD1 . ASP C 1 103 ? -4.912  6.872   26.491  1.00 65.84  ? 103  ASP C OD1 1 
ATOM   6650  O  OD2 . ASP C 1 103 ? -5.376  9.004   26.687  1.00 60.79  ? 103  ASP C OD2 1 
ATOM   6651  N  N   . GLU C 1 104 ? -7.789  10.825  27.697  1.00 38.32  ? 104  GLU C N   1 
ATOM   6652  C  CA  . GLU C 1 104 ? -7.841  11.767  28.810  1.00 23.64  ? 104  GLU C CA  1 
ATOM   6653  C  C   . GLU C 1 104 ? -9.077  12.634  28.566  1.00 42.74  ? 104  GLU C C   1 
ATOM   6654  O  O   . GLU C 1 104 ? -9.050  13.565  27.759  1.00 45.55  ? 104  GLU C O   1 
ATOM   6655  C  CB  . GLU C 1 104 ? -6.571  12.600  28.863  1.00 20.12  ? 104  GLU C CB  1 
ATOM   6656  C  CG  . GLU C 1 104 ? -5.286  11.775  28.827  1.00 47.35  ? 104  GLU C CG  1 
ATOM   6657  C  CD  . GLU C 1 104 ? -4.048  12.637  28.622  1.00 62.29  ? 104  GLU C CD  1 
ATOM   6658  O  OE1 . GLU C 1 104 ? -4.185  13.879  28.689  1.00 69.12  ? 104  GLU C OE1 1 
ATOM   6659  O  OE2 . GLU C 1 104 ? -2.943  12.091  28.385  1.00 69.01  ? 104  GLU C OE2 1 
ATOM   6660  N  N   . THR C 1 105 ? -10.158 12.316  29.278  1.00 52.42  ? 105  THR C N   1 
ATOM   6661  C  CA  . THR C 1 105 ? -11.515 12.693  28.866  1.00 44.56  ? 105  THR C CA  1 
ATOM   6662  C  C   . THR C 1 105 ? -12.243 13.733  29.725  1.00 38.79  ? 105  THR C C   1 
ATOM   6663  O  O   . THR C 1 105 ? -13.190 14.363  29.260  1.00 34.10  ? 105  THR C O   1 
ATOM   6664  C  CB  . THR C 1 105 ? -12.430 11.437  28.792  1.00 42.01  ? 105  THR C CB  1 
ATOM   6665  O  OG1 . THR C 1 105 ? -12.637 10.909  30.109  1.00 24.82  ? 105  THR C OG1 1 
ATOM   6666  C  CG2 . THR C 1 105 ? -11.806 10.361  27.894  1.00 48.58  ? 105  THR C CG2 1 
ATOM   6667  N  N   . VAL C 1 106 ? -11.841 13.899  30.977  1.00 36.45  ? 106  VAL C N   1 
ATOM   6668  C  CA  . VAL C 1 106 ? -12.540 14.837  31.845  1.00 38.53  ? 106  VAL C CA  1 
ATOM   6669  C  C   . VAL C 1 106 ? -12.578 16.266  31.287  1.00 42.51  ? 106  VAL C C   1 
ATOM   6670  O  O   . VAL C 1 106 ? -13.638 16.913  31.283  1.00 36.08  ? 106  VAL C O   1 
ATOM   6671  C  CB  . VAL C 1 106 ? -11.917 14.884  33.224  1.00 44.74  ? 106  VAL C CB  1 
ATOM   6672  C  CG1 . VAL C 1 106 ? -12.665 15.892  34.083  1.00 44.53  ? 106  VAL C CG1 1 
ATOM   6673  C  CG2 . VAL C 1 106 ? -11.948 13.508  33.837  1.00 47.61  ? 106  VAL C CG2 1 
ATOM   6674  N  N   . GLY C 1 107 ? -11.421 16.761  30.839  1.00 45.89  ? 107  GLY C N   1 
ATOM   6675  C  CA  . GLY C 1 107 ? -11.342 18.059  30.187  1.00 37.23  ? 107  GLY C CA  1 
ATOM   6676  C  C   . GLY C 1 107 ? -12.428 18.212  29.132  1.00 42.64  ? 107  GLY C C   1 
ATOM   6677  O  O   . GLY C 1 107 ? -13.150 19.214  29.096  1.00 43.71  ? 107  GLY C O   1 
ATOM   6678  N  N   . ARG C 1 108 ? -12.543 17.200  28.275  1.00 35.22  ? 108  ARG C N   1 
ATOM   6679  C  CA  . ARG C 1 108 ? -13.591 17.126  27.258  1.00 37.71  ? 108  ARG C CA  1 
ATOM   6680  C  C   . ARG C 1 108 ? -14.990 17.525  27.755  1.00 35.32  ? 108  ARG C C   1 
ATOM   6681  O  O   . ARG C 1 108 ? -15.614 18.453  27.232  1.00 36.47  ? 108  ARG C O   1 
ATOM   6682  C  CB  . ARG C 1 108 ? -13.618 15.708  26.698  1.00 34.13  ? 108  ARG C CB  1 
ATOM   6683  C  CG  . ARG C 1 108 ? -14.866 15.318  25.968  1.00 38.81  ? 108  ARG C CG  1 
ATOM   6684  C  CD  . ARG C 1 108 ? -14.657 13.933  25.371  1.00 47.04  ? 108  ARG C CD  1 
ATOM   6685  N  NE  . ARG C 1 108 ? -15.724 13.591  24.451  1.00 46.72  ? 108  ARG C NE  1 
ATOM   6686  C  CZ  . ARG C 1 108 ? -15.609 13.393  23.142  1.00 39.72  ? 108  ARG C CZ  1 
ATOM   6687  N  NH1 . ARG C 1 108 ? -16.703 13.104  22.471  1.00 37.92  ? 108  ARG C NH1 1 
ATOM   6688  N  NH2 . ARG C 1 108 ? -14.444 13.465  22.501  1.00 42.40  ? 108  ARG C NH2 1 
ATOM   6689  N  N   . GLN C 1 109 ? -15.482 16.814  28.761  1.00 39.06  ? 109  GLN C N   1 
ATOM   6690  C  CA  . GLN C 1 109 ? -16.811 17.089  29.286  1.00 41.52  ? 109  GLN C CA  1 
ATOM   6691  C  C   . GLN C 1 109 ? -16.860 18.426  29.997  1.00 30.71  ? 109  GLN C C   1 
ATOM   6692  O  O   . GLN C 1 109 ? -17.869 19.127  29.941  1.00 34.99  ? 109  GLN C O   1 
ATOM   6693  C  CB  . GLN C 1 109 ? -17.271 15.980  30.224  1.00 44.75  ? 109  GLN C CB  1 
ATOM   6694  C  CG  . GLN C 1 109 ? -17.946 14.831  29.506  1.00 49.82  ? 109  GLN C CG  1 
ATOM   6695  C  CD  . GLN C 1 109 ? -19.174 15.260  28.711  1.00 53.96  ? 109  GLN C CD  1 
ATOM   6696  O  OE1 . GLN C 1 109 ? -19.270 14.984  27.516  1.00 65.33  ? 109  GLN C OE1 1 
ATOM   6697  N  NE2 . GLN C 1 109 ? -20.120 15.927  29.372  1.00 40.83  ? 109  GLN C NE2 1 
ATOM   6698  N  N   . LEU C 1 110 ? -15.769 18.787  30.661  1.00 24.73  ? 110  LEU C N   1 
ATOM   6699  C  CA  . LEU C 1 110 ? -15.723 20.070  31.349  1.00 33.37  ? 110  LEU C CA  1 
ATOM   6700  C  C   . LEU C 1 110 ? -15.995 21.212  30.376  1.00 41.15  ? 110  LEU C C   1 
ATOM   6701  O  O   . LEU C 1 110 ? -16.737 22.145  30.692  1.00 44.19  ? 110  LEU C O   1 
ATOM   6702  C  CB  . LEU C 1 110 ? -14.390 20.272  32.073  1.00 29.22  ? 110  LEU C CB  1 
ATOM   6703  C  CG  . LEU C 1 110 ? -14.196 19.454  33.352  1.00 28.36  ? 110  LEU C CG  1 
ATOM   6704  C  CD1 . LEU C 1 110 ? -12.987 19.952  34.093  1.00 35.44  ? 110  LEU C CD1 1 
ATOM   6705  C  CD2 . LEU C 1 110 ? -15.399 19.570  34.236  1.00 28.06  ? 110  LEU C CD2 1 
ATOM   6706  N  N   . LEU C 1 111 ? -15.411 21.126  29.186  1.00 35.81  ? 111  LEU C N   1 
ATOM   6707  C  CA  . LEU C 1 111 ? -15.603 22.175  28.203  1.00 30.01  ? 111  LEU C CA  1 
ATOM   6708  C  C   . LEU C 1 111 ? -17.034 22.133  27.697  1.00 32.63  ? 111  LEU C C   1 
ATOM   6709  O  O   . LEU C 1 111 ? -17.649 23.178  27.483  1.00 46.94  ? 111  LEU C O   1 
ATOM   6710  C  CB  . LEU C 1 111 ? -14.583 22.073  27.055  1.00 43.56  ? 111  LEU C CB  1 
ATOM   6711  C  CG  . LEU C 1 111 ? -13.128 22.416  27.434  1.00 46.11  ? 111  LEU C CG  1 
ATOM   6712  C  CD1 . LEU C 1 111 ? -12.194 22.508  26.230  1.00 33.57  ? 111  LEU C CD1 1 
ATOM   6713  C  CD2 . LEU C 1 111 ? -13.060 23.704  28.225  1.00 47.88  ? 111  LEU C CD2 1 
ATOM   6714  N  N   . VAL C 1 112 ? -17.557 20.924  27.518  1.00 30.97  ? 112  VAL C N   1 
ATOM   6715  C  CA  . VAL C 1 112 ? -18.947 20.748  27.105  1.00 34.00  ? 112  VAL C CA  1 
ATOM   6716  C  C   . VAL C 1 112 ? -19.878 21.393  28.125  1.00 39.88  ? 112  VAL C C   1 
ATOM   6717  O  O   . VAL C 1 112 ? -20.839 22.078  27.759  1.00 34.44  ? 112  VAL C O   1 
ATOM   6718  C  CB  . VAL C 1 112 ? -19.304 19.260  26.944  1.00 33.89  ? 112  VAL C CB  1 
ATOM   6719  C  CG1 . VAL C 1 112 ? -20.792 19.080  26.912  1.00 18.60  ? 112  VAL C CG1 1 
ATOM   6720  C  CG2 . VAL C 1 112 ? -18.675 18.705  25.678  1.00 34.56  ? 112  VAL C CG2 1 
ATOM   6721  N  N   . TYR C 1 113 ? -19.571 21.177  29.403  1.00 37.08  ? 113  TYR C N   1 
ATOM   6722  C  CA  . TYR C 1 113 ? -20.270 21.844  30.499  1.00 41.94  ? 113  TYR C CA  1 
ATOM   6723  C  C   . TYR C 1 113 ? -20.124 23.378  30.473  1.00 49.49  ? 113  TYR C C   1 
ATOM   6724  O  O   . TYR C 1 113 ? -21.089 24.101  30.748  1.00 46.85  ? 113  TYR C O   1 
ATOM   6725  C  CB  . TYR C 1 113 ? -19.777 21.314  31.843  1.00 38.63  ? 113  TYR C CB  1 
ATOM   6726  C  CG  . TYR C 1 113 ? -20.224 19.906  32.158  1.00 49.59  ? 113  TYR C CG  1 
ATOM   6727  C  CD1 . TYR C 1 113 ? -19.606 19.169  33.165  1.00 49.12  ? 113  TYR C CD1 1 
ATOM   6728  C  CD2 . TYR C 1 113 ? -21.259 19.310  31.449  1.00 53.95  ? 113  TYR C CD2 1 
ATOM   6729  C  CE1 . TYR C 1 113 ? -20.014 17.877  33.463  1.00 46.79  ? 113  TYR C CE1 1 
ATOM   6730  C  CE2 . TYR C 1 113 ? -21.677 18.013  31.740  1.00 54.62  ? 113  TYR C CE2 1 
ATOM   6731  C  CZ  . TYR C 1 113 ? -21.054 17.302  32.749  1.00 52.55  ? 113  TYR C CZ  1 
ATOM   6732  O  OH  . TYR C 1 113 ? -21.475 16.015  33.023  1.00 51.51  ? 113  TYR C OH  1 
ATOM   6733  N  N   . MET C 1 114 ? -18.922 23.866  30.159  1.00 41.18  ? 114  MET C N   1 
ATOM   6734  C  CA  . MET C 1 114 ? -18.649 25.304  30.153  1.00 41.45  ? 114  MET C CA  1 
ATOM   6735  C  C   . MET C 1 114 ? -19.491 26.045  29.107  1.00 44.39  ? 114  MET C C   1 
ATOM   6736  O  O   . MET C 1 114 ? -20.080 27.104  29.377  1.00 45.03  ? 114  MET C O   1 
ATOM   6737  C  CB  . MET C 1 114 ? -17.162 25.563  29.906  1.00 31.79  ? 114  MET C CB  1 
ATOM   6738  C  CG  . MET C 1 114 ? -16.764 27.048  29.959  1.00 34.79  ? 114  MET C CG  1 
ATOM   6739  S  SD  . MET C 1 114 ? -17.235 27.877  31.506  1.00 55.55  ? 114  MET C SD  1 
ATOM   6740  C  CE  . MET C 1 114 ? -16.103 27.114  32.675  1.00 58.12  ? 114  MET C CE  1 
ATOM   6741  N  N   . ALA C 1 115 ? -19.532 25.486  27.909  1.00 27.48  ? 115  ALA C N   1 
ATOM   6742  C  CA  . ALA C 1 115 ? -20.330 26.051  26.835  1.00 32.05  ? 115  ALA C CA  1 
ATOM   6743  C  C   . ALA C 1 115 ? -21.742 26.360  27.322  1.00 41.64  ? 115  ALA C C   1 
ATOM   6744  O  O   . ALA C 1 115 ? -22.156 27.518  27.369  1.00 55.39  ? 115  ALA C O   1 
ATOM   6745  C  CB  . ALA C 1 115 ? -20.381 25.081  25.666  1.00 32.43  ? 115  ALA C CB  1 
ATOM   6746  N  N   . GLN C 1 116 ? -22.471 25.313  27.692  1.00 36.00  ? 116  GLN C N   1 
ATOM   6747  C  CA  . GLN C 1 116 ? -23.829 25.452  28.186  1.00 23.93  ? 116  GLN C CA  1 
ATOM   6748  C  C   . GLN C 1 116 ? -23.890 26.453  29.325  1.00 35.36  ? 116  GLN C C   1 
ATOM   6749  O  O   . GLN C 1 116 ? -24.644 27.426  29.263  1.00 47.07  ? 116  GLN C O   1 
ATOM   6750  C  CB  . GLN C 1 116 ? -24.355 24.095  28.642  1.00 19.00  ? 116  GLN C CB  1 
ATOM   6751  C  CG  . GLN C 1 116 ? -24.401 23.044  27.534  1.00 25.15  ? 116  GLN C CG  1 
ATOM   6752  C  CD  . GLN C 1 116 ? -24.735 21.650  28.042  1.00 31.93  ? 116  GLN C CD  1 
ATOM   6753  O  OE1 . GLN C 1 116 ? -25.891 21.265  28.096  1.00 39.36  ? 116  GLN C OE1 1 
ATOM   6754  N  NE2 . GLN C 1 116 ? -23.715 20.890  28.420  1.00 45.34  ? 116  GLN C NE2 1 
ATOM   6755  N  N   . TYR C 1 117 ? -23.092 26.210  30.364  1.00 34.00  ? 117  TYR C N   1 
ATOM   6756  C  CA  . TYR C 1 117 ? -23.063 27.065  31.555  1.00 33.04  ? 117  TYR C CA  1 
ATOM   6757  C  C   . TYR C 1 117 ? -22.954 28.550  31.206  1.00 33.35  ? 117  TYR C C   1 
ATOM   6758  O  O   . TYR C 1 117 ? -23.724 29.370  31.694  1.00 34.34  ? 117  TYR C O   1 
ATOM   6759  C  CB  . TYR C 1 117 ? -21.904 26.668  32.473  1.00 30.13  ? 117  TYR C CB  1 
ATOM   6760  C  CG  . TYR C 1 117 ? -21.820 27.466  33.759  1.00 34.55  ? 117  TYR C CG  1 
ATOM   6761  C  CD1 . TYR C 1 117 ? -22.561 27.101  34.872  1.00 31.30  ? 117  TYR C CD1 1 
ATOM   6762  C  CD2 . TYR C 1 117 ? -20.989 28.570  33.860  1.00 34.72  ? 117  TYR C CD2 1 
ATOM   6763  C  CE1 . TYR C 1 117 ? -22.492 27.821  36.039  1.00 31.95  ? 117  TYR C CE1 1 
ATOM   6764  C  CE2 . TYR C 1 117 ? -20.907 29.292  35.030  1.00 40.34  ? 117  TYR C CE2 1 
ATOM   6765  C  CZ  . TYR C 1 117 ? -21.664 28.915  36.117  1.00 36.11  ? 117  TYR C CZ  1 
ATOM   6766  O  OH  . TYR C 1 117 ? -21.584 29.635  37.290  1.00 39.55  ? 117  TYR C OH  1 
ATOM   6767  N  N   . LEU C 1 118 ? -21.995 28.896  30.359  1.00 37.39  ? 118  LEU C N   1 
ATOM   6768  C  CA  . LEU C 1 118 ? -21.782 30.299  30.035  1.00 49.12  ? 118  LEU C CA  1 
ATOM   6769  C  C   . LEU C 1 118 ? -23.021 30.897  29.366  1.00 52.55  ? 118  LEU C C   1 
ATOM   6770  O  O   . LEU C 1 118 ? -23.572 31.908  29.830  1.00 49.91  ? 118  LEU C O   1 
ATOM   6771  C  CB  . LEU C 1 118 ? -20.531 30.479  29.167  1.00 44.50  ? 118  LEU C CB  1 
ATOM   6772  C  CG  . LEU C 1 118 ? -19.203 30.467  29.935  1.00 48.26  ? 118  LEU C CG  1 
ATOM   6773  C  CD1 . LEU C 1 118 ? -17.994 30.541  28.987  1.00 50.11  ? 118  LEU C CD1 1 
ATOM   6774  C  CD2 . LEU C 1 118 ? -19.152 31.593  30.970  1.00 46.76  ? 118  LEU C CD2 1 
ATOM   6775  N  N   . LEU C 1 119 ? -23.459 30.249  28.288  1.00 47.97  ? 119  LEU C N   1 
ATOM   6776  C  CA  . LEU C 1 119 ? -24.605 30.710  27.512  1.00 40.63  ? 119  LEU C CA  1 
ATOM   6777  C  C   . LEU C 1 119 ? -25.861 30.801  28.367  1.00 44.26  ? 119  LEU C C   1 
ATOM   6778  O  O   . LEU C 1 119 ? -26.478 31.861  28.472  1.00 54.80  ? 119  LEU C O   1 
ATOM   6779  C  CB  . LEU C 1 119 ? -24.822 29.799  26.296  1.00 45.09  ? 119  LEU C CB  1 
ATOM   6780  C  CG  . LEU C 1 119 ? -23.843 30.052  25.136  1.00 44.81  ? 119  LEU C CG  1 
ATOM   6781  C  CD1 . LEU C 1 119 ? -23.881 28.945  24.087  1.00 40.28  ? 119  LEU C CD1 1 
ATOM   6782  C  CD2 . LEU C 1 119 ? -24.114 31.422  24.501  1.00 37.79  ? 119  LEU C CD2 1 
ATOM   6783  N  N   . GLY C 1 120 ? -26.219 29.691  29.002  1.00 42.00  ? 120  GLY C N   1 
ATOM   6784  C  CA  . GLY C 1 120 ? -27.415 29.634  29.817  1.00 28.99  ? 120  GLY C CA  1 
ATOM   6785  C  C   . GLY C 1 120 ? -27.438 30.569  31.009  1.00 28.29  ? 120  GLY C C   1 
ATOM   6786  O  O   . GLY C 1 120 ? -28.479 30.778  31.621  1.00 48.80  ? 120  GLY C O   1 
ATOM   6787  N  N   . ASN C 1 121 ? -26.296 31.136  31.360  1.00 45.49  ? 121  ASN C N   1 
ATOM   6788  C  CA  . ASN C 1 121 ? -26.225 31.912  32.592  1.00 50.99  ? 121  ASN C CA  1 
ATOM   6789  C  C   . ASN C 1 121 ? -25.752 33.349  32.398  1.00 52.02  ? 121  ASN C C   1 
ATOM   6790  O  O   . ASN C 1 121 ? -26.043 34.212  33.224  1.00 48.58  ? 121  ASN C O   1 
ATOM   6791  C  CB  . ASN C 1 121 ? -25.362 31.186  33.641  1.00 42.29  ? 121  ASN C CB  1 
ATOM   6792  C  CG  . ASN C 1 121 ? -26.072 29.991  34.260  1.00 37.02  ? 121  ASN C CG  1 
ATOM   6793  O  OD1 . ASN C 1 121 ? -26.854 30.141  35.189  1.00 42.75  ? 121  ASN C OD1 1 
ATOM   6794  N  ND2 . ASN C 1 121 ? -25.805 28.804  33.743  1.00 39.44  ? 121  ASN C ND2 1 
ATOM   6795  N  N   . HIS C 1 122 ? -25.037 33.606  31.305  1.00 38.08  ? 122  HIS C N   1 
ATOM   6796  C  CA  . HIS C 1 122 ? -24.433 34.911  31.079  1.00 29.44  ? 122  HIS C CA  1 
ATOM   6797  C  C   . HIS C 1 122 ? -25.405 36.080  31.205  1.00 44.69  ? 122  HIS C C   1 
ATOM   6798  O  O   . HIS C 1 122 ? -25.005 37.165  31.608  1.00 40.11  ? 122  HIS C O   1 
ATOM   6799  C  CB  . HIS C 1 122 ? -23.736 34.957  29.727  1.00 48.39  ? 122  HIS C CB  1 
ATOM   6800  C  CG  . HIS C 1 122 ? -24.632 35.340  28.595  1.00 54.78  ? 122  HIS C CG  1 
ATOM   6801  N  ND1 . HIS C 1 122 ? -25.377 34.418  27.893  1.00 67.63  ? 122  HIS C ND1 1 
ATOM   6802  C  CD2 . HIS C 1 122 ? -24.894 36.545  28.034  1.00 50.64  ? 122  HIS C CD2 1 
ATOM   6803  C  CE1 . HIS C 1 122 ? -26.066 35.038  26.950  1.00 70.94  ? 122  HIS C CE1 1 
ATOM   6804  N  NE2 . HIS C 1 122 ? -25.790 36.328  27.013  1.00 64.82  ? 122  HIS C NE2 1 
ATOM   6805  N  N   . GLU C 1 123 ? -26.676 35.873  30.868  1.00 52.08  ? 123  GLU C N   1 
ATOM   6806  C  CA  . GLU C 1 123 ? -27.650 36.944  31.036  1.00 53.46  ? 123  GLU C CA  1 
ATOM   6807  C  C   . GLU C 1 123 ? -28.170 37.050  32.470  1.00 56.82  ? 123  GLU C C   1 
ATOM   6808  O  O   . GLU C 1 123 ? -28.595 38.125  32.900  1.00 51.97  ? 123  GLU C O   1 
ATOM   6809  C  CB  . GLU C 1 123 ? -28.804 36.820  30.041  1.00 71.04  ? 123  GLU C CB  1 
ATOM   6810  C  CG  . GLU C 1 123 ? -28.410 37.181  28.613  1.00 88.87  ? 123  GLU C CG  1 
ATOM   6811  C  CD  . GLU C 1 123 ? -29.593 37.559  27.738  1.00 102.48 ? 123  GLU C CD  1 
ATOM   6812  O  OE1 . GLU C 1 123 ? -30.741 37.220  28.092  1.00 106.54 ? 123  GLU C OE1 1 
ATOM   6813  O  OE2 . GLU C 1 123 ? -29.370 38.199  26.689  1.00 108.66 ? 123  GLU C OE2 1 
ATOM   6814  N  N   . ARG C 1 124 ? -28.115 35.945  33.212  1.00 56.63  ? 124  ARG C N   1 
ATOM   6815  C  CA  . ARG C 1 124 ? -28.649 35.918  34.579  1.00 53.22  ? 124  ARG C CA  1 
ATOM   6816  C  C   . ARG C 1 124 ? -27.622 36.287  35.655  1.00 44.99  ? 124  ARG C C   1 
ATOM   6817  O  O   . ARG C 1 124 ? -27.952 36.951  36.629  1.00 34.67  ? 124  ARG C O   1 
ATOM   6818  C  CB  . ARG C 1 124 ? -29.265 34.548  34.904  1.00 66.11  ? 124  ARG C CB  1 
ATOM   6819  C  CG  . ARG C 1 124 ? -29.046 33.455  33.852  1.00 74.90  ? 124  ARG C CG  1 
ATOM   6820  C  CD  . ARG C 1 124 ? -29.240 32.056  34.461  1.00 79.21  ? 124  ARG C CD  1 
ATOM   6821  N  NE  . ARG C 1 124 ? -30.359 32.016  35.399  1.00 85.16  ? 124  ARG C NE  1 
ATOM   6822  C  CZ  . ARG C 1 124 ? -31.540 31.456  35.147  1.00 87.50  ? 124  ARG C CZ  1 
ATOM   6823  N  NH1 . ARG C 1 124 ? -31.767 30.860  33.986  1.00 82.61  ? 124  ARG C NH1 1 
ATOM   6824  N  NH2 . ARG C 1 124 ? -32.498 31.484  36.066  1.00 90.03  ? 124  ARG C NH2 1 
ATOM   6825  N  N   . ILE C 1 125 ? -26.385 35.827  35.479  1.00 41.33  ? 125  ILE C N   1 
ATOM   6826  C  CA  . ILE C 1 125 ? -25.313 36.088  36.430  1.00 42.42  ? 125  ILE C CA  1 
ATOM   6827  C  C   . ILE C 1 125 ? -24.371 37.187  35.927  1.00 54.58  ? 125  ILE C C   1 
ATOM   6828  O  O   . ILE C 1 125 ? -23.691 37.013  34.923  1.00 62.79  ? 125  ILE C O   1 
ATOM   6829  C  CB  . ILE C 1 125 ? -24.502 34.811  36.714  1.00 45.62  ? 125  ILE C CB  1 
ATOM   6830  C  CG1 . ILE C 1 125 ? -25.262 33.880  37.659  1.00 54.37  ? 125  ILE C CG1 1 
ATOM   6831  C  CG2 . ILE C 1 125 ? -23.180 35.161  37.349  1.00 42.61  ? 125  ILE C CG2 1 
ATOM   6832  C  CD1 . ILE C 1 125 ? -26.527 33.301  37.091  1.00 54.37  ? 125  ILE C CD1 1 
ATOM   6833  N  N   . SER C 1 126 ? -24.323 38.306  36.645  1.00 66.75  ? 126  SER C N   1 
ATOM   6834  C  CA  . SER C 1 126 ? -23.557 39.490  36.240  1.00 66.24  ? 126  SER C CA  1 
ATOM   6835  C  C   . SER C 1 126 ? -22.076 39.243  35.898  1.00 62.02  ? 126  SER C C   1 
ATOM   6836  O  O   . SER C 1 126 ? -21.600 39.676  34.851  1.00 56.98  ? 126  SER C O   1 
ATOM   6837  C  CB  . SER C 1 126 ? -23.668 40.570  37.315  1.00 68.54  ? 126  SER C CB  1 
ATOM   6838  O  OG  . SER C 1 126 ? -23.400 41.849  36.767  1.00 70.94  ? 126  SER C OG  1 
ATOM   6839  N  N   . ASP C 1 127 ? -21.353 38.568  36.788  1.00 65.70  ? 127  ASP C N   1 
ATOM   6840  C  CA  . ASP C 1 127 ? -19.964 38.185  36.524  1.00 61.77  ? 127  ASP C CA  1 
ATOM   6841  C  C   . ASP C 1 127 ? -19.815 37.597  35.129  1.00 47.70  ? 127  ASP C C   1 
ATOM   6842  O  O   . ASP C 1 127 ? -19.033 38.094  34.322  1.00 55.99  ? 127  ASP C O   1 
ATOM   6843  C  CB  . ASP C 1 127 ? -19.461 37.165  37.559  1.00 71.22  ? 127  ASP C CB  1 
ATOM   6844  C  CG  . ASP C 1 127 ? -18.992 37.818  38.845  1.00 83.47  ? 127  ASP C CG  1 
ATOM   6845  O  OD1 . ASP C 1 127 ? -18.448 38.945  38.794  1.00 79.25  ? 127  ASP C OD1 1 
ATOM   6846  O  OD2 . ASP C 1 127 ? -19.165 37.193  39.912  1.00 94.55  ? 127  ASP C OD2 1 
ATOM   6847  N  N   . LEU C 1 128 ? -20.570 36.537  34.851  1.00 38.39  ? 128  LEU C N   1 
ATOM   6848  C  CA  . LEU C 1 128 ? -20.466 35.837  33.576  1.00 36.67  ? 128  LEU C CA  1 
ATOM   6849  C  C   . LEU C 1 128 ? -20.860 36.748  32.423  1.00 45.18  ? 128  LEU C C   1 
ATOM   6850  O  O   . LEU C 1 128 ? -20.217 36.760  31.371  1.00 44.91  ? 128  LEU C O   1 
ATOM   6851  C  CB  . LEU C 1 128 ? -21.343 34.585  33.566  1.00 38.31  ? 128  LEU C CB  1 
ATOM   6852  C  CG  . LEU C 1 128 ? -21.097 33.544  34.656  1.00 37.46  ? 128  LEU C CG  1 
ATOM   6853  C  CD1 . LEU C 1 128 ? -22.111 32.427  34.559  1.00 34.31  ? 128  LEU C CD1 1 
ATOM   6854  C  CD2 . LEU C 1 128 ? -19.714 32.993  34.549  1.00 36.98  ? 128  LEU C CD2 1 
ATOM   6855  N  N   . GLY C 1 129 ? -21.931 37.505  32.617  1.00 44.19  ? 129  GLY C N   1 
ATOM   6856  C  CA  . GLY C 1 129 ? -22.391 38.412  31.585  1.00 54.16  ? 129  GLY C CA  1 
ATOM   6857  C  C   . GLY C 1 129 ? -21.294 39.396  31.241  1.00 52.27  ? 129  GLY C C   1 
ATOM   6858  O  O   . GLY C 1 129 ? -21.188 39.854  30.098  1.00 54.92  ? 129  GLY C O   1 
ATOM   6859  N  N   . GLN C 1 130 ? -20.475 39.714  32.241  1.00 30.65  ? 130  GLN C N   1 
ATOM   6860  C  CA  . GLN C 1 130 ? -19.349 40.622  32.062  1.00 43.06  ? 130  GLN C CA  1 
ATOM   6861  C  C   . GLN C 1 130 ? -18.134 39.894  31.475  1.00 37.45  ? 130  GLN C C   1 
ATOM   6862  O  O   . GLN C 1 130 ? -17.453 40.415  30.586  1.00 35.62  ? 130  GLN C O   1 
ATOM   6863  C  CB  . GLN C 1 130 ? -19.000 41.303  33.383  1.00 50.18  ? 130  GLN C CB  1 
ATOM   6864  C  CG  . GLN C 1 130 ? -18.408 42.685  33.219  1.00 54.09  ? 130  GLN C CG  1 
ATOM   6865  C  CD  . GLN C 1 130 ? -16.940 42.643  32.876  1.00 52.92  ? 130  GLN C CD  1 
ATOM   6866  O  OE1 . GLN C 1 130 ? -16.262 41.641  33.124  1.00 52.61  ? 130  GLN C OE1 1 
ATOM   6867  N  NE2 . GLN C 1 130 ? -16.430 43.736  32.314  1.00 60.50  ? 130  GLN C NE2 1 
ATOM   6868  N  N   . LEU C 1 131 ? -17.871 38.688  31.960  1.00 33.00  ? 131  LEU C N   1 
ATOM   6869  C  CA  . LEU C 1 131 ? -16.870 37.841  31.334  1.00 34.60  ? 131  LEU C CA  1 
ATOM   6870  C  C   . LEU C 1 131 ? -17.081 37.809  29.813  1.00 29.63  ? 131  LEU C C   1 
ATOM   6871  O  O   . LEU C 1 131 ? -16.165 38.106  29.031  1.00 27.10  ? 131  LEU C O   1 
ATOM   6872  C  CB  . LEU C 1 131 ? -16.943 36.429  31.915  1.00 29.22  ? 131  LEU C CB  1 
ATOM   6873  C  CG  . LEU C 1 131 ? -15.934 35.419  31.364  1.00 41.48  ? 131  LEU C CG  1 
ATOM   6874  C  CD1 . LEU C 1 131 ? -14.502 35.902  31.567  1.00 29.14  ? 131  LEU C CD1 1 
ATOM   6875  C  CD2 . LEU C 1 131 ? -16.144 34.055  32.005  1.00 38.25  ? 131  LEU C CD2 1 
ATOM   6876  N  N   . VAL C 1 132 ? -18.304 37.473  29.409  1.00 33.30  ? 132  VAL C N   1 
ATOM   6877  C  CA  . VAL C 1 132 ? -18.639 37.239  28.008  1.00 25.06  ? 132  VAL C CA  1 
ATOM   6878  C  C   . VAL C 1 132 ? -18.614 38.520  27.192  1.00 37.08  ? 132  VAL C C   1 
ATOM   6879  O  O   . VAL C 1 132 ? -18.118 38.544  26.067  1.00 50.14  ? 132  VAL C O   1 
ATOM   6880  C  CB  . VAL C 1 132 ? -20.008 36.577  27.880  1.00 23.98  ? 132  VAL C CB  1 
ATOM   6881  C  CG1 . VAL C 1 132 ? -20.435 36.514  26.429  1.00 38.33  ? 132  VAL C CG1 1 
ATOM   6882  C  CG2 . VAL C 1 132 ? -19.969 35.187  28.484  1.00 17.46  ? 132  VAL C CG2 1 
ATOM   6883  N  N   . ASN C 1 133 ? -19.149 39.591  27.761  1.00 33.10  ? 133  ASN C N   1 
ATOM   6884  C  CA  . ASN C 1 133 ? -19.097 40.895  27.115  1.00 33.23  ? 133  ASN C CA  1 
ATOM   6885  C  C   . ASN C 1 133 ? -17.682 41.322  26.720  1.00 34.27  ? 133  ASN C C   1 
ATOM   6886  O  O   . ASN C 1 133 ? -17.479 42.025  25.728  1.00 32.28  ? 133  ASN C O   1 
ATOM   6887  C  CB  . ASN C 1 133 ? -19.682 41.950  28.045  1.00 36.71  ? 133  ASN C CB  1 
ATOM   6888  C  CG  . ASN C 1 133 ? -21.175 42.015  27.978  1.00 43.49  ? 133  ASN C CG  1 
ATOM   6889  O  OD1 . ASN C 1 133 ? -21.811 41.136  27.401  1.00 51.12  ? 133  ASN C OD1 1 
ATOM   6890  N  ND2 . ASN C 1 133 ? -21.754 43.068  28.564  1.00 53.80  ? 133  ASN C ND2 1 
ATOM   6891  N  N   . SER C 1 134 ? -16.709 40.892  27.514  1.00 36.60  ? 134  SER C N   1 
ATOM   6892  C  CA  . SER C 1 134 ? -15.359 41.435  27.443  1.00 38.41  ? 134  SER C CA  1 
ATOM   6893  C  C   . SER C 1 134 ? -14.358 40.471  26.832  1.00 40.21  ? 134  SER C C   1 
ATOM   6894  O  O   . SER C 1 134 ? -13.203 40.831  26.596  1.00 42.13  ? 134  SER C O   1 
ATOM   6895  C  CB  . SER C 1 134 ? -14.883 41.804  28.848  1.00 38.12  ? 134  SER C CB  1 
ATOM   6896  O  OG  . SER C 1 134 ? -14.823 40.647  29.657  1.00 29.23  ? 134  SER C OG  1 
ATOM   6897  N  N   . THR C 1 135 ? -14.795 39.244  26.582  1.00 38.25  ? 135  THR C N   1 
ATOM   6898  C  CA  . THR C 1 135 ? -13.880 38.233  26.093  1.00 37.38  ? 135  THR C CA  1 
ATOM   6899  C  C   . THR C 1 135 ? -14.448 37.429  24.945  1.00 29.96  ? 135  THR C C   1 
ATOM   6900  O  O   . THR C 1 135 ? -15.592 36.993  24.986  1.00 42.92  ? 135  THR C O   1 
ATOM   6901  C  CB  . THR C 1 135 ? -13.523 37.262  27.204  1.00 44.06  ? 135  THR C CB  1 
ATOM   6902  O  OG1 . THR C 1 135 ? -13.588 37.942  28.467  1.00 42.06  ? 135  THR C OG1 1 
ATOM   6903  C  CG2 . THR C 1 135 ? -12.125 36.713  26.971  1.00 37.60  ? 135  THR C CG2 1 
ATOM   6904  N  N   . ASP C 1 136 ? -13.639 37.225  23.918  1.00 30.67  ? 136  ASP C N   1 
ATOM   6905  C  CA  . ASP C 1 136 ? -14.005 36.318  22.836  1.00 39.75  ? 136  ASP C CA  1 
ATOM   6906  C  C   . ASP C 1 136 ? -13.527 34.916  23.209  1.00 34.08  ? 136  ASP C C   1 
ATOM   6907  O  O   . ASP C 1 136 ? -12.331 34.678  23.351  1.00 36.39  ? 136  ASP C O   1 
ATOM   6908  C  CB  . ASP C 1 136 ? -13.354 36.769  21.533  1.00 57.24  ? 136  ASP C CB  1 
ATOM   6909  C  CG  . ASP C 1 136 ? -14.355 36.967  20.415  1.00 72.07  ? 136  ASP C CG  1 
ATOM   6910  O  OD1 . ASP C 1 136 ? -15.331 37.735  20.608  1.00 67.63  ? 136  ASP C OD1 1 
ATOM   6911  O  OD2 . ASP C 1 136 ? -14.150 36.363  19.335  1.00 81.88  ? 136  ASP C OD2 1 
ATOM   6912  N  N   . ILE C 1 137 ? -14.457 33.991  23.388  1.00 21.53  ? 137  ILE C N   1 
ATOM   6913  C  CA  . ILE C 1 137 ? -14.098 32.692  23.934  1.00 23.51  ? 137  ILE C CA  1 
ATOM   6914  C  C   . ILE C 1 137 ? -14.401 31.538  22.982  1.00 25.78  ? 137  ILE C C   1 
ATOM   6915  O  O   . ILE C 1 137 ? -15.516 31.415  22.475  1.00 36.83  ? 137  ILE C O   1 
ATOM   6916  C  CB  . ILE C 1 137 ? -14.827 32.428  25.256  1.00 32.46  ? 137  ILE C CB  1 
ATOM   6917  C  CG1 . ILE C 1 137 ? -14.606 33.583  26.234  1.00 28.67  ? 137  ILE C CG1 1 
ATOM   6918  C  CG2 . ILE C 1 137 ? -14.404 31.071  25.852  1.00 26.40  ? 137  ILE C CG2 1 
ATOM   6919  C  CD1 . ILE C 1 137 ? -15.613 33.585  27.398  1.00 17.52  ? 137  ILE C CD1 1 
ATOM   6920  N  N   . TYR C 1 138 ? -13.399 30.695  22.744  1.00 33.24  ? 138  TYR C N   1 
ATOM   6921  C  CA  . TYR C 1 138 ? -13.568 29.521  21.899  1.00 29.15  ? 138  TYR C CA  1 
ATOM   6922  C  C   . TYR C 1 138 ? -13.338 28.249  22.705  1.00 35.04  ? 138  TYR C C   1 
ATOM   6923  O  O   . TYR C 1 138 ? -12.349 28.147  23.435  1.00 31.88  ? 138  TYR C O   1 
ATOM   6924  C  CB  . TYR C 1 138 ? -12.594 29.576  20.736  1.00 23.20  ? 138  TYR C CB  1 
ATOM   6925  C  CG  . TYR C 1 138 ? -12.856 30.708  19.784  1.00 29.65  ? 138  TYR C CG  1 
ATOM   6926  C  CD1 . TYR C 1 138 ? -12.586 32.021  20.140  1.00 33.51  ? 138  TYR C CD1 1 
ATOM   6927  C  CD2 . TYR C 1 138 ? -13.353 30.466  18.523  1.00 18.61  ? 138  TYR C CD2 1 
ATOM   6928  C  CE1 . TYR C 1 138 ? -12.824 33.059  19.263  1.00 32.34  ? 138  TYR C CE1 1 
ATOM   6929  C  CE2 . TYR C 1 138 ? -13.592 31.491  17.651  1.00 23.23  ? 138  TYR C CE2 1 
ATOM   6930  C  CZ  . TYR C 1 138 ? -13.329 32.789  18.019  1.00 31.33  ? 138  TYR C CZ  1 
ATOM   6931  O  OH  . TYR C 1 138 ? -13.577 33.825  17.130  1.00 41.91  ? 138  TYR C OH  1 
ATOM   6932  N  N   . LEU C 1 139 ? -14.249 27.283  22.567  1.00 35.00  ? 139  LEU C N   1 
ATOM   6933  C  CA  . LEU C 1 139 ? -14.129 26.010  23.292  1.00 38.51  ? 139  LEU C CA  1 
ATOM   6934  C  C   . LEU C 1 139 ? -14.054 24.809  22.366  1.00 30.92  ? 139  LEU C C   1 
ATOM   6935  O  O   . LEU C 1 139 ? -14.981 24.555  21.621  1.00 27.78  ? 139  LEU C O   1 
ATOM   6936  C  CB  . LEU C 1 139 ? -15.305 25.800  24.250  1.00 31.66  ? 139  LEU C CB  1 
ATOM   6937  C  CG  . LEU C 1 139 ? -15.634 26.951  25.203  1.00 35.56  ? 139  LEU C CG  1 
ATOM   6938  C  CD1 . LEU C 1 139 ? -16.868 26.617  26.069  1.00 27.64  ? 139  LEU C CD1 1 
ATOM   6939  C  CD2 . LEU C 1 139 ? -14.412 27.326  26.045  1.00 16.99  ? 139  LEU C CD2 1 
ATOM   6940  N  N   . VAL C 1 140 ? -12.953 24.068  22.447  1.00 37.95  ? 140  VAL C N   1 
ATOM   6941  C  CA  . VAL C 1 140 ? -12.740 22.862  21.647  1.00 39.70  ? 140  VAL C CA  1 
ATOM   6942  C  C   . VAL C 1 140 ? -12.670 21.625  22.556  1.00 38.16  ? 140  VAL C C   1 
ATOM   6943  O  O   . VAL C 1 140 ? -11.585 21.223  22.975  1.00 37.71  ? 140  VAL C O   1 
ATOM   6944  C  CB  . VAL C 1 140 ? -11.414 22.963  20.850  1.00 40.32  ? 140  VAL C CB  1 
ATOM   6945  C  CG1 . VAL C 1 140 ? -11.233 21.751  19.937  1.00 21.41  ? 140  VAL C CG1 1 
ATOM   6946  C  CG2 . VAL C 1 140 ? -11.337 24.283  20.053  1.00 32.62  ? 140  VAL C CG2 1 
ATOM   6947  N  N   . PRO C 1 141 ? -13.829 21.037  22.882  1.00 39.66  ? 141  PRO C N   1 
ATOM   6948  C  CA  . PRO C 1 141 ? -13.936 19.894  23.802  1.00 45.52  ? 141  PRO C CA  1 
ATOM   6949  C  C   . PRO C 1 141 ? -13.071 18.697  23.396  1.00 41.69  ? 141  PRO C C   1 
ATOM   6950  O  O   . PRO C 1 141 ? -12.518 18.038  24.273  1.00 46.88  ? 141  PRO C O   1 
ATOM   6951  C  CB  . PRO C 1 141 ? -15.426 19.533  23.736  1.00 34.85  ? 141  PRO C CB  1 
ATOM   6952  C  CG  . PRO C 1 141 ? -16.091 20.810  23.433  1.00 37.68  ? 141  PRO C CG  1 
ATOM   6953  C  CD  . PRO C 1 141 ? -15.153 21.547  22.497  1.00 44.83  ? 141  PRO C CD  1 
ATOM   6954  N  N   . THR C 1 142 ? -12.967 18.413  22.100  1.00 30.06  ? 142  THR C N   1 
ATOM   6955  C  CA  . THR C 1 142 ? -12.019 17.398  21.638  1.00 42.58  ? 142  THR C CA  1 
ATOM   6956  C  C   . THR C 1 142 ? -11.160 17.815  20.450  1.00 36.00  ? 142  THR C C   1 
ATOM   6957  O  O   . THR C 1 142 ? -11.606 18.514  19.551  1.00 30.88  ? 142  THR C O   1 
ATOM   6958  C  CB  . THR C 1 142 ? -12.684 16.062  21.273  1.00 35.01  ? 142  THR C CB  1 
ATOM   6959  O  OG1 . THR C 1 142 ? -11.659 15.107  20.972  1.00 37.03  ? 142  THR C OG1 1 
ATOM   6960  C  CG2 . THR C 1 142 ? -13.541 16.222  20.063  1.00 27.98  ? 142  THR C CG2 1 
ATOM   6961  N  N   . MET C 1 143 ? -9.924  17.337  20.468  1.00 47.89  ? 143  MET C N   1 
ATOM   6962  C  CA  . MET C 1 143 ? -8.953  17.588  19.420  1.00 39.73  ? 143  MET C CA  1 
ATOM   6963  C  C   . MET C 1 143 ? -8.503  16.221  18.883  1.00 38.13  ? 143  MET C C   1 
ATOM   6964  O  O   . MET C 1 143 ? -7.667  16.124  17.995  1.00 28.74  ? 143  MET C O   1 
ATOM   6965  C  CB  . MET C 1 143 ? -7.777  18.357  20.019  1.00 33.69  ? 143  MET C CB  1 
ATOM   6966  C  CG  . MET C 1 143 ? -6.752  18.848  19.033  1.00 31.52  ? 143  MET C CG  1 
ATOM   6967  S  SD  . MET C 1 143 ? -5.287  19.483  19.873  1.00 51.13  ? 143  MET C SD  1 
ATOM   6968  C  CE  . MET C 1 143 ? -4.013  19.127  18.659  1.00 21.06  ? 143  MET C CE  1 
ATOM   6969  N  N   . ASN C 1 144 ? -9.070  15.156  19.431  1.00 25.44  ? 144  ASN C N   1 
ATOM   6970  C  CA  . ASN C 1 144 ? -8.743  13.831  18.947  1.00 33.23  ? 144  ASN C CA  1 
ATOM   6971  C  C   . ASN C 1 144 ? -9.907  12.852  19.050  1.00 43.40  ? 144  ASN C C   1 
ATOM   6972  O  O   . ASN C 1 144 ? -9.877  11.924  19.864  1.00 49.00  ? 144  ASN C O   1 
ATOM   6973  C  CB  . ASN C 1 144 ? -7.546  13.286  19.704  1.00 37.61  ? 144  ASN C CB  1 
ATOM   6974  C  CG  . ASN C 1 144 ? -7.144  11.936  19.213  1.00 46.76  ? 144  ASN C CG  1 
ATOM   6975  O  OD1 . ASN C 1 144 ? -7.552  11.522  18.120  1.00 44.13  ? 144  ASN C OD1 1 
ATOM   6976  N  ND2 . ASN C 1 144 ? -6.351  11.219  20.015  1.00 53.02  ? 144  ASN C ND2 1 
ATOM   6977  N  N   . PRO C 1 145 ? -10.934 13.052  18.213  1.00 32.32  ? 145  PRO C N   1 
ATOM   6978  C  CA  . PRO C 1 145 ? -12.183 12.287  18.206  1.00 21.78  ? 145  PRO C CA  1 
ATOM   6979  C  C   . PRO C 1 145 ? -11.921 10.822  17.882  1.00 30.51  ? 145  PRO C C   1 
ATOM   6980  O  O   . PRO C 1 145 ? -12.635 9.941   18.369  1.00 35.15  ? 145  PRO C O   1 
ATOM   6981  C  CB  . PRO C 1 145 ? -12.965 12.902  17.055  1.00 22.18  ? 145  PRO C CB  1 
ATOM   6982  C  CG  . PRO C 1 145 ? -12.243 14.134  16.662  1.00 31.82  ? 145  PRO C CG  1 
ATOM   6983  C  CD  . PRO C 1 145 ? -10.831 13.951  17.057  1.00 30.44  ? 145  PRO C CD  1 
ATOM   6984  N  N   . ASP C 1 146 ? -10.902 10.587  17.060  1.00 31.63  ? 146  ASP C N   1 
ATOM   6985  C  CA  . ASP C 1 146 ? -10.523 9.253   16.615  1.00 38.29  ? 146  ASP C CA  1 
ATOM   6986  C  C   . ASP C 1 146 ? -9.835  8.504   17.745  1.00 37.39  ? 146  ASP C C   1 
ATOM   6987  O  O   . ASP C 1 146 ? -10.098 7.318   17.975  1.00 40.39  ? 146  ASP C O   1 
ATOM   6988  C  CB  . ASP C 1 146 ? -9.611  9.336   15.378  1.00 48.93  ? 146  ASP C CB  1 
ATOM   6989  C  CG  . ASP C 1 146 ? -10.357 9.810   14.114  1.00 43.33  ? 146  ASP C CG  1 
ATOM   6990  O  OD1 . ASP C 1 146 ? -11.557 10.136  14.197  1.00 28.66  ? 146  ASP C OD1 1 
ATOM   6991  O  OD2 . ASP C 1 146 ? -9.741  9.849   13.029  1.00 43.78  ? 146  ASP C OD2 1 
ATOM   6992  N  N   . GLY C 1 147 ? -8.958  9.209   18.456  1.00 34.06  ? 147  GLY C N   1 
ATOM   6993  C  CA  . GLY C 1 147 ? -8.330  8.670   19.651  1.00 25.87  ? 147  GLY C CA  1 
ATOM   6994  C  C   . GLY C 1 147 ? -9.379  8.404   20.714  1.00 34.38  ? 147  GLY C C   1 
ATOM   6995  O  O   . GLY C 1 147 ? -9.351  7.366   21.382  1.00 44.62  ? 147  GLY C O   1 
ATOM   6996  N  N   . TYR C 1 148 ? -10.319 9.336   20.866  1.00 38.57  ? 148  TYR C N   1 
ATOM   6997  C  CA  . TYR C 1 148 ? -11.423 9.172   21.817  1.00 50.87  ? 148  TYR C CA  1 
ATOM   6998  C  C   . TYR C 1 148 ? -12.222 7.893   21.539  1.00 52.85  ? 148  TYR C C   1 
ATOM   6999  O  O   . TYR C 1 148 ? -12.254 6.981   22.362  1.00 47.49  ? 148  TYR C O   1 
ATOM   7000  C  CB  . TYR C 1 148 ? -12.348 10.408  21.822  1.00 44.38  ? 148  TYR C CB  1 
ATOM   7001  C  CG  . TYR C 1 148 ? -13.562 10.267  22.734  1.00 40.34  ? 148  TYR C CG  1 
ATOM   7002  C  CD1 . TYR C 1 148 ? -13.419 10.154  24.124  1.00 43.31  ? 148  TYR C CD1 1 
ATOM   7003  C  CD2 . TYR C 1 148 ? -14.845 10.243  22.206  1.00 27.47  ? 148  TYR C CD2 1 
ATOM   7004  C  CE1 . TYR C 1 148 ? -14.526 10.015  24.955  1.00 38.51  ? 148  TYR C CE1 1 
ATOM   7005  C  CE2 . TYR C 1 148 ? -15.954 10.103  23.021  1.00 28.38  ? 148  TYR C CE2 1 
ATOM   7006  C  CZ  . TYR C 1 148 ? -15.796 9.989   24.395  1.00 48.68  ? 148  TYR C CZ  1 
ATOM   7007  O  OH  . TYR C 1 148 ? -16.911 9.850   25.207  1.00 62.23  ? 148  TYR C OH  1 
ATOM   7008  N  N   . ALA C 1 149 ? -12.850 7.837   20.370  1.00 45.08  ? 149  ALA C N   1 
ATOM   7009  C  CA  . ALA C 1 149 ? -13.619 6.680   19.938  1.00 26.27  ? 149  ALA C CA  1 
ATOM   7010  C  C   . ALA C 1 149 ? -12.931 5.346   20.243  1.00 37.18  ? 149  ALA C C   1 
ATOM   7011  O  O   . ALA C 1 149 ? -13.587 4.342   20.494  1.00 33.40  ? 149  ALA C O   1 
ATOM   7012  C  CB  . ALA C 1 149 ? -13.894 6.790   18.452  1.00 23.73  ? 149  ALA C CB  1 
ATOM   7013  N  N   . LEU C 1 150 ? -11.605 5.331   20.217  1.00 49.20  ? 150  LEU C N   1 
ATOM   7014  C  CA  . LEU C 1 150 ? -10.868 4.089   20.426  1.00 52.93  ? 150  LEU C CA  1 
ATOM   7015  C  C   . LEU C 1 150 ? -10.553 3.817   21.902  1.00 62.13  ? 150  LEU C C   1 
ATOM   7016  O  O   . LEU C 1 150 ? -10.101 2.728   22.258  1.00 68.36  ? 150  LEU C O   1 
ATOM   7017  C  CB  . LEU C 1 150 ? -9.590  4.075   19.574  1.00 53.08  ? 150  LEU C CB  1 
ATOM   7018  C  CG  . LEU C 1 150 ? -9.817  3.999   18.057  1.00 47.71  ? 150  LEU C CG  1 
ATOM   7019  C  CD1 . LEU C 1 150 ? -8.682  4.652   17.272  1.00 45.95  ? 150  LEU C CD1 1 
ATOM   7020  C  CD2 . LEU C 1 150 ? -10.018 2.566   17.627  1.00 41.25  ? 150  LEU C CD2 1 
ATOM   7021  N  N   . SER C 1 151 ? -10.806 4.802   22.762  1.00 64.88  ? 151  SER C N   1 
ATOM   7022  C  CA  . SER C 1 151 ? -10.546 4.663   24.200  1.00 48.57  ? 151  SER C CA  1 
ATOM   7023  C  C   . SER C 1 151 ? -11.721 4.035   24.963  1.00 51.25  ? 151  SER C C   1 
ATOM   7024  O  O   . SER C 1 151 ? -12.849 3.980   24.470  1.00 51.53  ? 151  SER C O   1 
ATOM   7025  C  CB  . SER C 1 151 ? -10.193 6.023   24.803  1.00 32.62  ? 151  SER C CB  1 
ATOM   7026  O  OG  . SER C 1 151 ? -9.078  6.600   24.143  1.00 32.32  ? 151  SER C OG  1 
ATOM   7027  N  N   . GLN C 1 152 ? -11.458 3.571   26.179  1.00 48.19  ? 152  GLN C N   1 
ATOM   7028  C  CA  . GLN C 1 152 ? -12.475 2.843   26.935  1.00 54.37  ? 152  GLN C CA  1 
ATOM   7029  C  C   . GLN C 1 152 ? -12.857 3.549   28.227  1.00 58.43  ? 152  GLN C C   1 
ATOM   7030  O  O   . GLN C 1 152 ? -12.048 3.643   29.158  1.00 66.72  ? 152  GLN C O   1 
ATOM   7031  C  CB  . GLN C 1 152 ? -11.994 1.422   27.246  1.00 68.53  ? 152  GLN C CB  1 
ATOM   7032  C  CG  . GLN C 1 152 ? -12.942 0.619   28.119  1.00 76.36  ? 152  GLN C CG  1 
ATOM   7033  C  CD  . GLN C 1 152 ? -12.402 -0.772  28.444  1.00 85.55  ? 152  GLN C CD  1 
ATOM   7034  O  OE1 . GLN C 1 152 ? -12.912 -1.456  29.336  1.00 93.85  ? 152  GLN C OE1 1 
ATOM   7035  N  NE2 . GLN C 1 152 ? -11.363 -1.194  27.718  1.00 77.51  ? 152  GLN C NE2 1 
ATOM   7036  N  N   . GLU C 1 153 ? -14.089 4.044   28.289  1.00 46.71  ? 153  GLU C N   1 
ATOM   7037  C  CA  . GLU C 1 153 ? -14.547 4.672   29.508  1.00 48.42  ? 153  GLU C CA  1 
ATOM   7038  C  C   . GLU C 1 153 ? -14.214 3.758   30.697  1.00 62.23  ? 153  GLU C C   1 
ATOM   7039  O  O   . GLU C 1 153 ? -14.497 2.552   30.668  1.00 59.22  ? 153  GLU C O   1 
ATOM   7040  C  CB  . GLU C 1 153 ? -16.049 4.972   29.454  1.00 40.11  ? 153  GLU C CB  1 
ATOM   7041  C  CG  . GLU C 1 153 ? -16.535 5.688   30.711  1.00 53.75  ? 153  GLU C CG  1 
ATOM   7042  C  CD  . GLU C 1 153 ? -17.998 6.024   30.680  1.00 60.23  ? 153  GLU C CD  1 
ATOM   7043  O  OE1 . GLU C 1 153 ? -18.603 6.137   31.774  1.00 63.20  ? 153  GLU C OE1 1 
ATOM   7044  O  OE2 . GLU C 1 153 ? -18.536 6.173   29.562  1.00 62.79  ? 153  GLU C OE2 1 
ATOM   7045  N  N   . GLY C 1 154 ? -13.601 4.329   31.732  1.00 58.62  ? 154  GLY C N   1 
ATOM   7046  C  CA  . GLY C 1 154 ? -13.290 3.579   32.933  1.00 52.50  ? 154  GLY C CA  1 
ATOM   7047  C  C   . GLY C 1 154 ? -11.798 3.451   33.145  1.00 55.09  ? 154  GLY C C   1 
ATOM   7048  O  O   . GLY C 1 154 ? -11.332 3.288   34.270  1.00 62.73  ? 154  GLY C O   1 
ATOM   7049  N  N   . ASN C 1 155 ? -11.038 3.534   32.062  1.00 49.36  ? 155  ASN C N   1 
ATOM   7050  C  CA  . ASN C 1 155 ? -9.604  3.334   32.157  1.00 46.16  ? 155  ASN C CA  1 
ATOM   7051  C  C   . ASN C 1 155 ? -8.876  4.515   32.785  1.00 53.16  ? 155  ASN C C   1 
ATOM   7052  O  O   . ASN C 1 155 ? -8.677  5.551   32.152  1.00 64.43  ? 155  ASN C O   1 
ATOM   7053  C  CB  . ASN C 1 155 ? -9.016  2.994   30.792  1.00 43.51  ? 155  ASN C CB  1 
ATOM   7054  C  CG  . ASN C 1 155 ? -8.993  1.509   30.530  1.00 52.12  ? 155  ASN C CG  1 
ATOM   7055  O  OD1 . ASN C 1 155 ? -9.163  1.061   29.398  1.00 60.16  ? 155  ASN C OD1 1 
ATOM   7056  N  ND2 . ASN C 1 155 ? -8.786  0.735   31.578  1.00 62.72  ? 155  ASN C ND2 1 
ATOM   7057  N  N   . CYS C 1 156 ? -8.487  4.352   34.043  1.00 57.89  ? 156  CYS C N   1 
ATOM   7058  C  CA  . CYS C 1 156 ? -7.702  5.365   34.730  1.00 62.97  ? 156  CYS C CA  1 
ATOM   7059  C  C   . CYS C 1 156 ? -6.326  5.413   34.091  1.00 57.83  ? 156  CYS C C   1 
ATOM   7060  O  O   . CYS C 1 156 ? -5.704  6.472   34.003  1.00 56.93  ? 156  CYS C O   1 
ATOM   7061  C  CB  . CYS C 1 156 ? -7.608  5.052   36.230  1.00 64.68  ? 156  CYS C CB  1 
ATOM   7062  S  SG  . CYS C 1 156 ? -9.098  5.528   37.185  1.00 68.07  ? 156  CYS C SG  1 
ATOM   7063  N  N   . GLU C 1 157 ? -5.862  4.253   33.638  1.00 58.94  ? 157  GLU C N   1 
ATOM   7064  C  CA  . GLU C 1 157 ? -4.624  4.166   32.871  1.00 58.43  ? 157  GLU C CA  1 
ATOM   7065  C  C   . GLU C 1 157 ? -4.924  3.931   31.390  1.00 56.41  ? 157  GLU C C   1 
ATOM   7066  O  O   . GLU C 1 157 ? -5.920  3.298   31.026  1.00 58.63  ? 157  GLU C O   1 
ATOM   7067  C  CB  . GLU C 1 157 ? -3.691  3.067   33.412  1.00 69.42  ? 157  GLU C CB  1 
ATOM   7068  C  CG  . GLU C 1 157 ? -3.058  3.361   34.770  1.00 80.70  ? 157  GLU C CG  1 
ATOM   7069  C  CD  . GLU C 1 157 ? -3.782  2.669   35.908  1.00 96.58  ? 157  GLU C CD  1 
ATOM   7070  O  OE1 . GLU C 1 157 ? -3.420  1.511   36.231  1.00 105.31 ? 157  GLU C OE1 1 
ATOM   7071  O  OE2 . GLU C 1 157 ? -4.717  3.280   36.474  1.00 91.87  ? 157  GLU C OE2 1 
ATOM   7072  N  N   . SER C 1 158 ? -4.053  4.454   30.538  1.00 54.96  ? 158  SER C N   1 
ATOM   7073  C  CA  . SER C 1 158 ? -4.201  4.294   29.109  1.00 41.00  ? 158  SER C CA  1 
ATOM   7074  C  C   . SER C 1 158 ? -4.193  2.806   28.736  1.00 50.49  ? 158  SER C C   1 
ATOM   7075  O  O   . SER C 1 158 ? -3.807  1.945   29.528  1.00 54.06  ? 158  SER C O   1 
ATOM   7076  C  CB  . SER C 1 158 ? -3.089  5.048   28.395  1.00 33.99  ? 158  SER C CB  1 
ATOM   7077  O  OG  . SER C 1 158 ? -3.292  4.996   26.997  1.00 62.90  ? 158  SER C OG  1 
ATOM   7078  N  N   . LEU C 1 159 ? -4.627  2.500   27.524  1.00 72.40  ? 159  LEU C N   1 
ATOM   7079  C  CA  . LEU C 1 159 ? -4.672  1.116   27.071  1.00 71.46  ? 159  LEU C CA  1 
ATOM   7080  C  C   . LEU C 1 159 ? -3.283  0.614   26.696  1.00 80.22  ? 159  LEU C C   1 
ATOM   7081  O  O   . LEU C 1 159 ? -2.317  1.382   26.682  1.00 73.01  ? 159  LEU C O   1 
ATOM   7082  C  CB  . LEU C 1 159 ? -5.601  0.988   25.863  1.00 65.09  ? 159  LEU C CB  1 
ATOM   7083  C  CG  . LEU C 1 159 ? -7.086  1.260   26.090  1.00 51.52  ? 159  LEU C CG  1 
ATOM   7084  C  CD1 . LEU C 1 159 ? -7.765  1.645   24.769  1.00 40.79  ? 159  LEU C CD1 1 
ATOM   7085  C  CD2 . LEU C 1 159 ? -7.746  0.055   26.741  1.00 36.79  ? 159  LEU C CD2 1 
ATOM   7086  N  N   . PRO C 1 160 ? -3.178  -0.690  26.401  1.00 87.59  ? 160  PRO C N   1 
ATOM   7087  C  CA  . PRO C 1 160 ? -1.946  -1.258  25.852  1.00 82.55  ? 160  PRO C CA  1 
ATOM   7088  C  C   . PRO C 1 160 ? -1.612  -0.573  24.538  1.00 72.93  ? 160  PRO C C   1 
ATOM   7089  O  O   . PRO C 1 160 ? -2.528  -0.172  23.823  1.00 77.31  ? 160  PRO C O   1 
ATOM   7090  C  CB  . PRO C 1 160 ? -2.327  -2.714  25.599  1.00 92.12  ? 160  PRO C CB  1 
ATOM   7091  C  CG  . PRO C 1 160 ? -3.411  -2.992  26.582  1.00 89.66  ? 160  PRO C CG  1 
ATOM   7092  C  CD  . PRO C 1 160 ? -4.190  -1.724  26.680  1.00 86.61  ? 160  PRO C CD  1 
ATOM   7093  N  N   . ASN C 1 161 ? -0.325  -0.436  24.232  1.00 79.62  ? 161  ASN C N   1 
ATOM   7094  C  CA  . ASN C 1 161 ? 0.115   0.276   23.035  1.00 89.87  ? 161  ASN C CA  1 
ATOM   7095  C  C   . ASN C 1 161 ? -0.273  1.742   23.110  1.00 71.14  ? 161  ASN C C   1 
ATOM   7096  O  O   . ASN C 1 161 ? -0.128  2.482   22.139  1.00 83.79  ? 161  ASN C O   1 
ATOM   7097  C  CB  . ASN C 1 161 ? -0.489  -0.344  21.770  1.00 104.61 ? 161  ASN C CB  1 
ATOM   7098  C  CG  . ASN C 1 161 ? -0.226  -1.833  21.663  1.00 104.57 ? 161  ASN C CG  1 
ATOM   7099  O  OD1 . ASN C 1 161 ? -1.115  -2.605  21.296  1.00 103.17 ? 161  ASN C OD1 1 
ATOM   7100  N  ND2 . ASN C 1 161 ? 1.000   -2.246  21.987  1.00 100.25 ? 161  ASN C ND2 1 
ATOM   7101  N  N   . TYR C 1 162 ? -0.780  2.148   24.267  1.00 57.72  ? 162  TYR C N   1 
ATOM   7102  C  CA  . TYR C 1 162 ? -1.281  3.502   24.457  1.00 63.36  ? 162  TYR C CA  1 
ATOM   7103  C  C   . TYR C 1 162 ? -2.316  3.838   23.391  1.00 63.28  ? 162  TYR C C   1 
ATOM   7104  O  O   . TYR C 1 162 ? -2.467  4.994   22.967  1.00 64.73  ? 162  TYR C O   1 
ATOM   7105  C  CB  . TYR C 1 162 ? -0.135  4.512   24.465  1.00 60.00  ? 162  TYR C CB  1 
ATOM   7106  C  CG  . TYR C 1 162 ? 0.650   4.526   25.761  1.00 56.14  ? 162  TYR C CG  1 
ATOM   7107  C  CD1 . TYR C 1 162 ? 1.942   4.024   25.824  1.00 57.72  ? 162  TYR C CD1 1 
ATOM   7108  C  CD2 . TYR C 1 162 ? 0.094   5.044   26.922  1.00 53.09  ? 162  TYR C CD2 1 
ATOM   7109  C  CE1 . TYR C 1 162 ? 2.658   4.046   27.010  1.00 63.09  ? 162  TYR C CE1 1 
ATOM   7110  C  CE2 . TYR C 1 162 ? 0.800   5.074   28.103  1.00 47.61  ? 162  TYR C CE2 1 
ATOM   7111  C  CZ  . TYR C 1 162 ? 2.081   4.572   28.151  1.00 59.92  ? 162  TYR C CZ  1 
ATOM   7112  O  OH  . TYR C 1 162 ? 2.783   4.599   29.346  1.00 51.19  ? 162  TYR C OH  1 
ATOM   7113  N  N   . VAL C 1 163 ? -3.030  2.804   22.965  1.00 59.18  ? 163  VAL C N   1 
ATOM   7114  C  CA  . VAL C 1 163 ? -4.099  2.966   21.987  1.00 72.11  ? 163  VAL C CA  1 
ATOM   7115  C  C   . VAL C 1 163 ? -5.195  3.901   22.536  1.00 64.10  ? 163  VAL C C   1 
ATOM   7116  O  O   . VAL C 1 163 ? -5.539  3.845   23.726  1.00 59.21  ? 163  VAL C O   1 
ATOM   7117  C  CB  . VAL C 1 163 ? -4.657  1.578   21.538  1.00 45.43  ? 163  VAL C CB  1 
ATOM   7118  C  CG1 . VAL C 1 163 ? -6.085  1.696   20.993  1.00 40.25  ? 163  VAL C CG1 1 
ATOM   7119  C  CG2 . VAL C 1 163 ? -3.705  0.924   20.516  1.00 37.11  ? 163  VAL C CG2 1 
ATOM   7120  N  N   . GLY C 1 164 ? -5.720  4.771   21.676  1.00 41.22  ? 164  GLY C N   1 
ATOM   7121  C  CA  . GLY C 1 164 ? -6.675  5.770   22.106  1.00 35.38  ? 164  GLY C CA  1 
ATOM   7122  C  C   . GLY C 1 164 ? -6.000  7.087   22.461  1.00 30.84  ? 164  GLY C C   1 
ATOM   7123  O  O   . GLY C 1 164 ? -6.575  8.148   22.258  1.00 46.08  ? 164  GLY C O   1 
ATOM   7124  N  N   . ARG C 1 165 ? -4.781  7.025   22.987  1.00 27.06  ? 165  ARG C N   1 
ATOM   7125  C  CA  . ARG C 1 165 ? -4.046  8.236   23.328  1.00 47.31  ? 165  ARG C CA  1 
ATOM   7126  C  C   . ARG C 1 165 ? -3.697  9.020   22.043  1.00 49.20  ? 165  ARG C C   1 
ATOM   7127  O  O   . ARG C 1 165 ? -4.084  10.190  21.865  1.00 35.77  ? 165  ARG C O   1 
ATOM   7128  C  CB  . ARG C 1 165 ? -2.788  7.884   24.141  1.00 42.58  ? 165  ARG C CB  1 
ATOM   7129  C  CG  . ARG C 1 165 ? -1.924  9.079   24.558  1.00 39.43  ? 165  ARG C CG  1 
ATOM   7130  C  CD  . ARG C 1 165 ? -0.708  8.658   25.400  1.00 41.12  ? 165  ARG C CD  1 
ATOM   7131  N  NE  . ARG C 1 165 ? 0.372   9.647   25.341  1.00 34.85  ? 165  ARG C NE  1 
ATOM   7132  C  CZ  . ARG C 1 165 ? 0.580   10.611  26.242  1.00 37.62  ? 165  ARG C CZ  1 
ATOM   7133  N  NH1 . ARG C 1 165 ? -0.203  10.731  27.314  1.00 37.99  ? 165  ARG C NH1 1 
ATOM   7134  N  NH2 . ARG C 1 165 ? 1.587   11.456  26.080  1.00 29.55  ? 165  ARG C NH2 1 
ATOM   7135  N  N   . GLY C 1 166 ? -2.979  8.360   21.140  1.00 38.76  ? 166  GLY C N   1 
ATOM   7136  C  CA  . GLY C 1 166 ? -2.573  8.996   19.904  1.00 35.03  ? 166  GLY C CA  1 
ATOM   7137  C  C   . GLY C 1 166 ? -3.771  9.048   18.997  1.00 43.30  ? 166  GLY C C   1 
ATOM   7138  O  O   . GLY C 1 166 ? -4.841  8.584   19.382  1.00 56.18  ? 166  GLY C O   1 
ATOM   7139  N  N   . ASN C 1 167 ? -3.612  9.601   17.798  1.00 38.43  ? 167  ASN C N   1 
ATOM   7140  C  CA  . ASN C 1 167 ? -4.719  9.613   16.854  1.00 35.28  ? 167  ASN C CA  1 
ATOM   7141  C  C   . ASN C 1 167 ? -4.940  8.212   16.243  1.00 42.05  ? 167  ASN C C   1 
ATOM   7142  O  O   . ASN C 1 167 ? -4.606  7.203   16.873  1.00 43.26  ? 167  ASN C O   1 
ATOM   7143  C  CB  . ASN C 1 167 ? -4.540  10.714  15.798  1.00 19.47  ? 167  ASN C CB  1 
ATOM   7144  C  CG  . ASN C 1 167 ? -3.402  10.428  14.833  1.00 31.43  ? 167  ASN C CG  1 
ATOM   7145  O  OD1 . ASN C 1 167 ? -2.707  9.424   14.947  1.00 39.05  ? 167  ASN C OD1 1 
ATOM   7146  N  ND2 . ASN C 1 167 ? -3.217  11.311  13.868  1.00 26.01  ? 167  ASN C ND2 1 
ATOM   7147  N  N   . ALA C 1 168 ? -5.504  8.155   15.036  1.00 45.84  ? 168  ALA C N   1 
ATOM   7148  C  CA  . ALA C 1 168 ? -5.851  6.891   14.385  1.00 50.71  ? 168  ALA C CA  1 
ATOM   7149  C  C   . ALA C 1 168 ? -4.622  6.193   13.804  1.00 62.68  ? 168  ALA C C   1 
ATOM   7150  O  O   . ALA C 1 168 ? -4.617  4.973   13.590  1.00 62.18  ? 168  ALA C O   1 
ATOM   7151  C  CB  . ALA C 1 168 ? -6.905  7.124   13.300  1.00 49.33  ? 168  ALA C CB  1 
ATOM   7152  N  N   . ALA C 1 169 ? -3.588  6.987   13.553  1.00 54.51  ? 169  ALA C N   1 
ATOM   7153  C  CA  . ALA C 1 169 ? -2.319  6.484   13.052  1.00 47.21  ? 169  ALA C CA  1 
ATOM   7154  C  C   . ALA C 1 169 ? -1.392  6.123   14.219  1.00 46.46  ? 169  ALA C C   1 
ATOM   7155  O  O   . ALA C 1 169 ? -0.227  5.771   14.029  1.00 39.29  ? 169  ALA C O   1 
ATOM   7156  C  CB  . ALA C 1 169 ? -1.672  7.532   12.162  1.00 38.29  ? 169  ALA C CB  1 
ATOM   7157  N  N   . ASN C 1 170 ? -1.925  6.221   15.429  1.00 38.01  ? 170  ASN C N   1 
ATOM   7158  C  CA  . ASN C 1 170 ? -1.159  5.940   16.625  1.00 49.76  ? 170  ASN C CA  1 
ATOM   7159  C  C   . ASN C 1 170 ? 0.030   6.868   16.873  1.00 51.72  ? 170  ASN C C   1 
ATOM   7160  O  O   . ASN C 1 170 ? 1.020   6.463   17.482  1.00 53.13  ? 170  ASN C O   1 
ATOM   7161  C  CB  . ASN C 1 170 ? -0.718  4.482   16.637  1.00 68.98  ? 170  ASN C CB  1 
ATOM   7162  C  CG  . ASN C 1 170 ? -1.721  3.593   17.320  1.00 84.25  ? 170  ASN C CG  1 
ATOM   7163  O  OD1 . ASN C 1 170 ? -2.281  2.679   16.704  1.00 82.76  ? 170  ASN C OD1 1 
ATOM   7164  N  ND2 . ASN C 1 170 ? -1.971  3.862   18.607  1.00 85.52  ? 170  ASN C ND2 1 
ATOM   7165  N  N   . ILE C 1 171 ? -0.066  8.119   16.433  1.00 43.05  ? 171  ILE C N   1 
ATOM   7166  C  CA  . ILE C 1 171 ? 0.963   9.077   16.812  1.00 49.63  ? 171  ILE C CA  1 
ATOM   7167  C  C   . ILE C 1 171 ? 0.451   10.084  17.835  1.00 43.87  ? 171  ILE C C   1 
ATOM   7168  O  O   . ILE C 1 171 ? -0.684  10.548  17.749  1.00 45.09  ? 171  ILE C O   1 
ATOM   7169  C  CB  . ILE C 1 171 ? 1.572   9.806   15.613  1.00 44.46  ? 171  ILE C CB  1 
ATOM   7170  C  CG1 . ILE C 1 171 ? 0.807   11.091  15.339  1.00 36.76  ? 171  ILE C CG1 1 
ATOM   7171  C  CG2 . ILE C 1 171 ? 1.702   8.867   14.412  1.00 43.68  ? 171  ILE C CG2 1 
ATOM   7172  C  CD1 . ILE C 1 171 ? 1.391   12.293  16.061  1.00 39.93  ? 171  ILE C CD1 1 
ATOM   7173  N  N   . ASP C 1 172 ? 1.304   10.394  18.809  1.00 46.24  ? 172  ASP C N   1 
ATOM   7174  C  CA  . ASP C 1 172 ? 0.976   11.294  19.906  1.00 39.01  ? 172  ASP C CA  1 
ATOM   7175  C  C   . ASP C 1 172 ? 0.950   12.739  19.433  1.00 42.50  ? 172  ASP C C   1 
ATOM   7176  O  O   . ASP C 1 172 ? 1.994   13.354  19.203  1.00 45.98  ? 172  ASP C O   1 
ATOM   7177  C  CB  . ASP C 1 172 ? 2.011   11.157  21.021  1.00 30.78  ? 172  ASP C CB  1 
ATOM   7178  C  CG  . ASP C 1 172 ? 1.616   11.902  22.285  1.00 37.78  ? 172  ASP C CG  1 
ATOM   7179  O  OD1 . ASP C 1 172 ? 1.006   12.991  22.192  1.00 38.58  ? 172  ASP C OD1 1 
ATOM   7180  O  OD2 . ASP C 1 172 ? 1.918   11.393  23.385  1.00 44.80  ? 172  ASP C OD2 1 
ATOM   7181  N  N   . LEU C 1 173 ? -0.251  13.280  19.315  1.00 30.86  ? 173  LEU C N   1 
ATOM   7182  C  CA  . LEU C 1 173 ? -0.430  14.629  18.819  1.00 40.16  ? 173  LEU C CA  1 
ATOM   7183  C  C   . LEU C 1 173 ? 0.348   15.664  19.633  1.00 35.06  ? 173  LEU C C   1 
ATOM   7184  O  O   . LEU C 1 173 ? 0.641   16.755  19.131  1.00 31.24  ? 173  LEU C O   1 
ATOM   7185  C  CB  . LEU C 1 173 ? -1.926  14.970  18.768  1.00 40.44  ? 173  LEU C CB  1 
ATOM   7186  C  CG  . LEU C 1 173 ? -2.690  14.089  17.771  1.00 33.25  ? 173  LEU C CG  1 
ATOM   7187  C  CD1 . LEU C 1 173 ? -4.201  14.306  17.823  1.00 21.67  ? 173  LEU C CD1 1 
ATOM   7188  C  CD2 . LEU C 1 173 ? -2.155  14.329  16.380  1.00 34.17  ? 173  LEU C CD2 1 
ATOM   7189  N  N   . ASN C 1 174 ? 0.688   15.330  20.878  1.00 23.99  ? 174  ASN C N   1 
ATOM   7190  C  CA  . ASN C 1 174 ? 1.436   16.264  21.725  1.00 18.15  ? 174  ASN C CA  1 
ATOM   7191  C  C   . ASN C 1 174 ? 2.954   16.106  21.529  1.00 32.26  ? 174  ASN C C   1 
ATOM   7192  O  O   . ASN C 1 174 ? 3.752   16.544  22.355  1.00 44.45  ? 174  ASN C O   1 
ATOM   7193  C  CB  . ASN C 1 174 ? 1.032   16.129  23.198  1.00 20.44  ? 174  ASN C CB  1 
ATOM   7194  C  CG  . ASN C 1 174 ? 1.157   17.452  23.983  1.00 34.56  ? 174  ASN C CG  1 
ATOM   7195  O  OD1 . ASN C 1 174 ? 1.126   18.543  23.408  1.00 37.18  ? 174  ASN C OD1 1 
ATOM   7196  N  ND2 . ASN C 1 174 ? 1.288   17.346  25.305  1.00 28.16  ? 174  ASN C ND2 1 
ATOM   7197  N  N   . ARG C 1 175 ? 3.338   15.472  20.423  1.00 25.27  ? 175  ARG C N   1 
ATOM   7198  C  CA  . ARG C 1 175 ? 4.727   15.434  19.979  1.00 25.31  ? 175  ARG C CA  1 
ATOM   7199  C  C   . ARG C 1 175 ? 4.805   15.881  18.515  1.00 30.16  ? 175  ARG C C   1 
ATOM   7200  O  O   . ARG C 1 175 ? 5.885   15.921  17.922  1.00 41.10  ? 175  ARG C O   1 
ATOM   7201  C  CB  . ARG C 1 175 ? 5.311   14.018  20.100  1.00 18.54  ? 175  ARG C CB  1 
ATOM   7202  C  CG  . ARG C 1 175 ? 5.072   13.306  21.426  1.00 27.87  ? 175  ARG C CG  1 
ATOM   7203  C  CD  . ARG C 1 175 ? 6.025   13.705  22.552  1.00 28.04  ? 175  ARG C CD  1 
ATOM   7204  N  NE  . ARG C 1 175 ? 5.291   14.354  23.623  1.00 47.03  ? 175  ARG C NE  1 
ATOM   7205  C  CZ  . ARG C 1 175 ? 5.073   13.896  24.854  1.00 44.72  ? 175  ARG C CZ  1 
ATOM   7206  N  NH1 . ARG C 1 175 ? 5.551   12.743  25.287  1.00 46.73  ? 175  ARG C NH1 1 
ATOM   7207  N  NH2 . ARG C 1 175 ? 4.350   14.637  25.666  1.00 53.61  ? 175  ARG C NH2 1 
ATOM   7208  N  N   . ASP C 1 176 ? 3.657   16.228  17.934  1.00 45.05  ? 176  ASP C N   1 
ATOM   7209  C  CA  . ASP C 1 176 ? 3.543   16.429  16.479  1.00 38.78  ? 176  ASP C CA  1 
ATOM   7210  C  C   . ASP C 1 176 ? 3.617   17.888  16.019  1.00 36.68  ? 176  ASP C C   1 
ATOM   7211  O  O   . ASP C 1 176 ? 3.675   18.168  14.825  1.00 36.52  ? 176  ASP C O   1 
ATOM   7212  C  CB  . ASP C 1 176 ? 2.241   15.806  15.961  1.00 29.83  ? 176  ASP C CB  1 
ATOM   7213  C  CG  . ASP C 1 176 ? 2.309   15.453  14.487  1.00 41.31  ? 176  ASP C CG  1 
ATOM   7214  O  OD1 . ASP C 1 176 ? 3.430   15.198  13.999  1.00 46.17  ? 176  ASP C OD1 1 
ATOM   7215  O  OD2 . ASP C 1 176 ? 1.249   15.419  13.814  1.00 41.73  ? 176  ASP C OD2 1 
ATOM   7216  N  N   . PHE C 1 177 ? 3.593   18.823  16.956  1.00 35.25  ? 177  PHE C N   1 
ATOM   7217  C  CA  . PHE C 1 177 ? 3.663   20.229  16.592  1.00 29.99  ? 177  PHE C CA  1 
ATOM   7218  C  C   . PHE C 1 177 ? 5.100   20.660  16.331  1.00 31.82  ? 177  PHE C C   1 
ATOM   7219  O  O   . PHE C 1 177 ? 6.045   20.025  16.813  1.00 47.61  ? 177  PHE C O   1 
ATOM   7220  C  CB  . PHE C 1 177 ? 3.028   21.091  17.679  1.00 36.05  ? 177  PHE C CB  1 
ATOM   7221  C  CG  . PHE C 1 177 ? 1.539   20.994  17.721  1.00 37.31  ? 177  PHE C CG  1 
ATOM   7222  C  CD1 . PHE C 1 177 ? 0.915   19.866  18.246  1.00 45.22  ? 177  PHE C CD1 1 
ATOM   7223  C  CD2 . PHE C 1 177 ? 0.758   22.031  17.240  1.00 28.26  ? 177  PHE C CD2 1 
ATOM   7224  C  CE1 . PHE C 1 177 ? -0.468  19.775  18.291  1.00 45.38  ? 177  PHE C CE1 1 
ATOM   7225  C  CE2 . PHE C 1 177 ? -0.632  21.948  17.281  1.00 36.52  ? 177  PHE C CE2 1 
ATOM   7226  C  CZ  . PHE C 1 177 ? -1.243  20.817  17.805  1.00 43.83  ? 177  PHE C CZ  1 
ATOM   7227  N  N   . PRO C 1 178 ? 5.268   21.736  15.548  1.00 29.42  ? 178  PRO C N   1 
ATOM   7228  C  CA  . PRO C 1 178 ? 6.615   22.239  15.266  1.00 29.06  ? 178  PRO C CA  1 
ATOM   7229  C  C   . PRO C 1 178 ? 7.309   22.638  16.556  1.00 40.73  ? 178  PRO C C   1 
ATOM   7230  O  O   . PRO C 1 178 ? 6.707   23.272  17.424  1.00 34.24  ? 178  PRO C O   1 
ATOM   7231  C  CB  . PRO C 1 178 ? 6.363   23.473  14.400  1.00 22.54  ? 178  PRO C CB  1 
ATOM   7232  C  CG  . PRO C 1 178 ? 5.000   23.233  13.775  1.00 28.85  ? 178  PRO C CG  1 
ATOM   7233  C  CD  . PRO C 1 178 ? 4.222   22.480  14.816  1.00 31.03  ? 178  PRO C CD  1 
ATOM   7234  N  N   . ASP C 1 179 ? 8.575   22.264  16.675  1.00 45.21  ? 179  ASP C N   1 
ATOM   7235  C  CA  . ASP C 1 179 ? 9.366   22.595  17.847  1.00 44.31  ? 179  ASP C CA  1 
ATOM   7236  C  C   . ASP C 1 179 ? 10.152  23.898  17.630  1.00 44.09  ? 179  ASP C C   1 
ATOM   7237  O  O   . ASP C 1 179 ? 10.775  24.095  16.581  1.00 36.86  ? 179  ASP C O   1 
ATOM   7238  C  CB  . ASP C 1 179 ? 10.322  21.440  18.163  1.00 45.03  ? 179  ASP C CB  1 
ATOM   7239  C  CG  . ASP C 1 179 ? 10.959  21.563  19.544  1.00 57.80  ? 179  ASP C CG  1 
ATOM   7240  O  OD1 . ASP C 1 179 ? 10.249  21.949  20.504  1.00 55.61  ? 179  ASP C OD1 1 
ATOM   7241  O  OD2 . ASP C 1 179 ? 12.167  21.254  19.669  1.00 52.22  ? 179  ASP C OD2 1 
ATOM   7242  N  N   . ARG C 1 180 ? 10.118  24.785  18.621  1.00 37.27  ? 180  ARG C N   1 
ATOM   7243  C  CA  . ARG C 1 180 ? 10.901  26.015  18.570  1.00 43.55  ? 180  ARG C CA  1 
ATOM   7244  C  C   . ARG C 1 180 ? 12.387  25.721  18.353  1.00 51.49  ? 180  ARG C C   1 
ATOM   7245  O  O   . ARG C 1 180 ? 13.092  26.484  17.691  1.00 50.24  ? 180  ARG C O   1 
ATOM   7246  C  CB  . ARG C 1 180 ? 10.722  26.794  19.862  1.00 42.94  ? 180  ARG C CB  1 
ATOM   7247  C  CG  . ARG C 1 180 ? 11.038  25.954  21.092  1.00 50.85  ? 180  ARG C CG  1 
ATOM   7248  C  CD  . ARG C 1 180 ? 10.608  26.627  22.384  1.00 49.31  ? 180  ARG C CD  1 
ATOM   7249  N  NE  . ARG C 1 180 ? 11.169  25.933  23.531  1.00 56.45  ? 180  ARG C NE  1 
ATOM   7250  C  CZ  . ARG C 1 180 ? 12.331  26.251  24.092  1.00 47.90  ? 180  ARG C CZ  1 
ATOM   7251  N  NH1 . ARG C 1 180 ? 13.042  27.264  23.619  1.00 34.51  ? 180  ARG C NH1 1 
ATOM   7252  N  NH2 . ARG C 1 180 ? 12.779  25.559  25.134  1.00 40.66  ? 180  ARG C NH2 1 
ATOM   7253  N  N   . LEU C 1 181 ? 12.858  24.614  18.916  1.00 46.90  ? 181  LEU C N   1 
ATOM   7254  C  CA  . LEU C 1 181 ? 14.248  24.202  18.749  1.00 45.22  ? 181  LEU C CA  1 
ATOM   7255  C  C   . LEU C 1 181 ? 14.445  23.306  17.515  1.00 48.15  ? 181  LEU C C   1 
ATOM   7256  O  O   . LEU C 1 181 ? 15.339  22.474  17.496  1.00 56.15  ? 181  LEU C O   1 
ATOM   7257  C  CB  . LEU C 1 181 ? 14.744  23.484  20.006  1.00 26.23  ? 181  LEU C CB  1 
ATOM   7258  C  CG  . LEU C 1 181 ? 14.262  24.100  21.319  1.00 45.44  ? 181  LEU C CG  1 
ATOM   7259  C  CD1 . LEU C 1 181 ? 14.537  23.186  22.507  1.00 49.01  ? 181  LEU C CD1 1 
ATOM   7260  C  CD2 . LEU C 1 181 ? 14.882  25.470  21.532  1.00 65.99  ? 181  LEU C CD2 1 
ATOM   7261  N  N   . GLU C 1 182 ? 13.582  23.450  16.511  1.00 69.58  ? 182  GLU C N   1 
ATOM   7262  C  CA  . GLU C 1 182 ? 13.817  22.880  15.170  1.00 80.22  ? 182  GLU C CA  1 
ATOM   7263  C  C   . GLU C 1 182 ? 13.980  21.345  15.056  1.00 94.50  ? 182  GLU C C   1 
ATOM   7264  O  O   . GLU C 1 182 ? 14.063  20.628  16.061  1.00 92.48  ? 182  GLU C O   1 
ATOM   7265  C  CB  . GLU C 1 182 ? 15.030  23.565  14.528  1.00 65.84  ? 182  GLU C CB  1 
ATOM   7266  C  CG  . GLU C 1 182 ? 14.950  23.685  13.029  1.00 77.04  ? 182  GLU C CG  1 
ATOM   7267  C  CD  . GLU C 1 182 ? 13.994  24.778  12.604  1.00 98.21  ? 182  GLU C CD  1 
ATOM   7268  O  OE1 . GLU C 1 182 ? 13.348  25.371  13.503  1.00 97.05  ? 182  GLU C OE1 1 
ATOM   7269  O  OE2 . GLU C 1 182 ? 13.893  25.047  11.379  1.00 96.27  ? 182  GLU C OE2 1 
ATOM   7270  N  N   . GLN C 1 183 ? 14.026  20.867  13.809  1.00 92.17  ? 183  GLN C N   1 
ATOM   7271  C  CA  . GLN C 1 183 ? 14.266  19.456  13.486  1.00 86.29  ? 183  GLN C CA  1 
ATOM   7272  C  C   . GLN C 1 183 ? 14.553  19.277  11.992  1.00 91.62  ? 183  GLN C C   1 
ATOM   7273  O  O   . GLN C 1 183 ? 13.657  18.960  11.201  1.00 89.37  ? 183  GLN C O   1 
ATOM   7274  C  CB  . GLN C 1 183 ? 13.078  18.579  13.903  1.00 70.71  ? 183  GLN C CB  1 
ATOM   7275  C  CG  . GLN C 1 183 ? 13.145  17.126  13.416  1.00 64.89  ? 183  GLN C CG  1 
ATOM   7276  C  CD  . GLN C 1 183 ? 13.960  16.218  14.331  1.00 80.85  ? 183  GLN C CD  1 
ATOM   7277  O  OE1 . GLN C 1 183 ? 14.508  16.660  15.348  1.00 74.90  ? 183  GLN C OE1 1 
ATOM   7278  N  NE2 . GLN C 1 183 ? 14.037  14.935  13.971  1.00 81.12  ? 183  GLN C NE2 1 
ATOM   7279  N  N   . LEU C 1 189 ? 5.987   29.677  7.815   1.00 92.26  ? 189  LEU C N   1 
ATOM   7280  C  CA  . LEU C 1 189 ? 6.934   28.627  7.455   1.00 97.89  ? 189  LEU C CA  1 
ATOM   7281  C  C   . LEU C 1 189 ? 6.565   27.295  8.101   1.00 101.65 ? 189  LEU C C   1 
ATOM   7282  O  O   . LEU C 1 189 ? 7.236   26.282  7.888   1.00 97.56  ? 189  LEU C O   1 
ATOM   7283  C  CB  . LEU C 1 189 ? 8.344   29.011  7.886   1.00 91.23  ? 189  LEU C CB  1 
ATOM   7284  C  CG  . LEU C 1 189 ? 8.500   29.124  9.400   1.00 78.63  ? 189  LEU C CG  1 
ATOM   7285  C  CD1 . LEU C 1 189 ? 9.943   28.840  9.819   1.00 80.69  ? 189  LEU C CD1 1 
ATOM   7286  C  CD2 . LEU C 1 189 ? 8.038   30.497  9.877   1.00 78.91  ? 189  LEU C CD2 1 
ATOM   7287  N  N   . ARG C 1 190 ? 5.510   27.305  8.907   1.00 98.38  ? 190  ARG C N   1 
ATOM   7288  C  CA  . ARG C 1 190 ? 5.009   26.078  9.505   1.00 85.01  ? 190  ARG C CA  1 
ATOM   7289  C  C   . ARG C 1 190 ? 4.122   25.355  8.488   1.00 76.24  ? 190  ARG C C   1 
ATOM   7290  O  O   . ARG C 1 190 ? 3.050   25.852  8.125   1.00 60.30  ? 190  ARG C O   1 
ATOM   7291  C  CB  . ARG C 1 190 ? 4.274   26.368  10.827  1.00 70.11  ? 190  ARG C CB  1 
ATOM   7292  C  CG  . ARG C 1 190 ? 3.315   27.555  10.796  1.00 54.86  ? 190  ARG C CG  1 
ATOM   7293  C  CD  . ARG C 1 190 ? 3.748   28.687  11.731  1.00 48.49  ? 190  ARG C CD  1 
ATOM   7294  N  NE  . ARG C 1 190 ? 4.562   29.691  11.041  1.00 70.86  ? 190  ARG C NE  1 
ATOM   7295  C  CZ  . ARG C 1 190 ? 4.817   30.918  11.502  1.00 61.69  ? 190  ARG C CZ  1 
ATOM   7296  N  NH1 . ARG C 1 190 ? 4.314   31.316  12.663  1.00 38.30  ? 190  ARG C NH1 1 
ATOM   7297  N  NH2 . ARG C 1 190 ? 5.574   31.758  10.795  1.00 55.07  ? 190  ARG C NH2 1 
ATOM   7298  N  N   . ALA C 1 191 ? 4.592   24.198  8.014   1.00 79.54  ? 191  ALA C N   1 
ATOM   7299  C  CA  . ALA C 1 191 ? 3.918   23.449  6.947   1.00 89.13  ? 191  ALA C CA  1 
ATOM   7300  C  C   . ALA C 1 191 ? 4.175   21.934  6.990   1.00 96.19  ? 191  ALA C C   1 
ATOM   7301  O  O   . ALA C 1 191 ? 3.931   21.276  8.006   1.00 100.96 ? 191  ALA C O   1 
ATOM   7302  C  CB  . ALA C 1 191 ? 4.308   24.010  5.577   1.00 86.75  ? 191  ALA C CB  1 
ATOM   7303  N  N   . GLN C 1 192 ? 4.647   21.391  5.868   1.00 98.74  ? 192  GLN C N   1 
ATOM   7304  C  CA  . GLN C 1 192 ? 4.979   19.962  5.745   1.00 101.47 ? 192  GLN C CA  1 
ATOM   7305  C  C   . GLN C 1 192 ? 3.804   18.985  5.942   1.00 94.21  ? 192  GLN C C   1 
ATOM   7306  O  O   . GLN C 1 192 ? 2.685   19.216  5.458   1.00 101.14 ? 192  GLN C O   1 
ATOM   7307  C  CB  . GLN C 1 192 ? 6.146   19.592  6.673   1.00 102.96 ? 192  GLN C CB  1 
ATOM   7308  C  CG  . GLN C 1 192 ? 7.537   19.962  6.143   1.00 88.25  ? 192  GLN C CG  1 
ATOM   7309  C  CD  . GLN C 1 192 ? 8.084   18.938  5.165   1.00 67.68  ? 192  GLN C CD  1 
ATOM   7310  O  OE1 . GLN C 1 192 ? 9.198   18.439  5.325   1.00 62.22  ? 192  GLN C OE1 1 
ATOM   7311  N  NE2 . GLN C 1 192 ? 7.295   18.610  4.154   1.00 69.94  ? 192  GLN C NE2 1 
ATOM   7312  N  N   . SER C 1 193 ? 4.069   17.881  6.636   1.00 73.70  ? 193  SER C N   1 
ATOM   7313  C  CA  . SER C 1 193 ? 3.052   16.852  6.814   1.00 69.85  ? 193  SER C CA  1 
ATOM   7314  C  C   . SER C 1 193 ? 2.922   16.323  8.238   1.00 59.94  ? 193  SER C C   1 
ATOM   7315  O  O   . SER C 1 193 ? 3.443   15.254  8.587   1.00 44.00  ? 193  SER C O   1 
ATOM   7316  C  CB  . SER C 1 193 ? 3.238   15.700  5.826   1.00 80.61  ? 193  SER C CB  1 
ATOM   7317  O  OG  . SER C 1 193 ? 2.270   15.786  4.788   1.00 90.36  ? 193  SER C OG  1 
ATOM   7318  N  N   . ARG C 1 194 ? 2.196   17.093  9.040   1.00 47.44  ? 194  ARG C N   1 
ATOM   7319  C  CA  . ARG C 1 194 ? 1.760   16.675  10.354  1.00 43.81  ? 194  ARG C CA  1 
ATOM   7320  C  C   . ARG C 1 194 ? 0.464   15.877  10.247  1.00 37.65  ? 194  ARG C C   1 
ATOM   7321  O  O   . ARG C 1 194 ? -0.135  15.796  9.179   1.00 40.80  ? 194  ARG C O   1 
ATOM   7322  C  CB  . ARG C 1 194 ? 1.501   17.917  11.197  1.00 46.36  ? 194  ARG C CB  1 
ATOM   7323  C  CG  . ARG C 1 194 ? 2.535   18.994  10.997  1.00 54.89  ? 194  ARG C CG  1 
ATOM   7324  C  CD  . ARG C 1 194 ? 3.770   18.710  11.817  1.00 68.65  ? 194  ARG C CD  1 
ATOM   7325  N  NE  . ARG C 1 194 ? 4.770   19.756  11.656  1.00 84.41  ? 194  ARG C NE  1 
ATOM   7326  C  CZ  . ARG C 1 194 ? 5.727   20.014  12.540  1.00 99.10  ? 194  ARG C CZ  1 
ATOM   7327  N  NH1 . ARG C 1 194 ? 5.813   19.307  13.661  1.00 100.50 ? 194  ARG C NH1 1 
ATOM   7328  N  NH2 . ARG C 1 194 ? 6.597   20.984  12.302  1.00 107.30 ? 194  ARG C NH2 1 
ATOM   7329  N  N   . GLN C 1 195 ? 0.022   15.303  11.361  1.00 40.35  ? 195  GLN C N   1 
ATOM   7330  C  CA  . GLN C 1 195 ? -1.320  14.739  11.440  1.00 42.83  ? 195  GLN C CA  1 
ATOM   7331  C  C   . GLN C 1 195 ? -2.411  15.775  11.066  1.00 44.18  ? 195  GLN C C   1 
ATOM   7332  O  O   . GLN C 1 195 ? -2.249  16.982  11.288  1.00 42.69  ? 195  GLN C O   1 
ATOM   7333  C  CB  . GLN C 1 195 ? -1.559  14.188  12.852  1.00 46.33  ? 195  GLN C CB  1 
ATOM   7334  C  CG  . GLN C 1 195 ? -0.581  13.097  13.238  1.00 42.01  ? 195  GLN C CG  1 
ATOM   7335  C  CD  . GLN C 1 195 ? -0.496  12.008  12.186  1.00 43.97  ? 195  GLN C CD  1 
ATOM   7336  O  OE1 . GLN C 1 195 ? -1.465  11.289  11.924  1.00 54.63  ? 195  GLN C OE1 1 
ATOM   7337  N  NE2 . GLN C 1 195 ? 0.667   11.882  11.576  1.00 31.18  ? 195  GLN C NE2 1 
ATOM   7338  N  N   . PRO C 1 196 ? -3.532  15.299  10.511  1.00 36.50  ? 196  PRO C N   1 
ATOM   7339  C  CA  . PRO C 1 196 ? -4.651  16.168  10.114  1.00 22.88  ? 196  PRO C CA  1 
ATOM   7340  C  C   . PRO C 1 196 ? -5.083  17.082  11.241  1.00 32.98  ? 196  PRO C C   1 
ATOM   7341  O  O   . PRO C 1 196 ? -5.450  18.242  11.031  1.00 34.14  ? 196  PRO C O   1 
ATOM   7342  C  CB  . PRO C 1 196 ? -5.786  15.181  9.864   1.00 25.16  ? 196  PRO C CB  1 
ATOM   7343  C  CG  . PRO C 1 196 ? -5.106  13.870  9.592   1.00 36.96  ? 196  PRO C CG  1 
ATOM   7344  C  CD  . PRO C 1 196 ? -3.835  13.866  10.358  1.00 20.03  ? 196  PRO C CD  1 
ATOM   7345  N  N   . GLU C 1 197 ? -5.063  16.527  12.446  1.00 25.41  ? 197  GLU C N   1 
ATOM   7346  C  CA  . GLU C 1 197 ? -5.555  17.229  13.609  1.00 26.78  ? 197  GLU C CA  1 
ATOM   7347  C  C   . GLU C 1 197 ? -4.585  18.335  14.004  1.00 32.18  ? 197  GLU C C   1 
ATOM   7348  O  O   . GLU C 1 197 ? -4.989  19.453  14.325  1.00 26.20  ? 197  GLU C O   1 
ATOM   7349  C  CB  . GLU C 1 197 ? -5.739  16.242  14.767  1.00 27.97  ? 197  GLU C CB  1 
ATOM   7350  C  CG  . GLU C 1 197 ? -6.807  15.188  14.511  1.00 26.60  ? 197  GLU C CG  1 
ATOM   7351  C  CD  . GLU C 1 197 ? -6.262  13.916  13.891  1.00 37.51  ? 197  GLU C CD  1 
ATOM   7352  O  OE1 . GLU C 1 197 ? -7.049  12.951  13.747  1.00 47.11  ? 197  GLU C OE1 1 
ATOM   7353  O  OE2 . GLU C 1 197 ? -5.050  13.873  13.564  1.00 34.68  ? 197  GLU C OE2 1 
ATOM   7354  N  N   . THR C 1 198 ? -3.300  18.002  13.981  1.00 30.48  ? 198  THR C N   1 
ATOM   7355  C  CA  . THR C 1 198 ? -2.266  18.942  14.334  1.00 24.87  ? 198  THR C CA  1 
ATOM   7356  C  C   . THR C 1 198 ? -2.363  20.098  13.360  1.00 30.17  ? 198  THR C C   1 
ATOM   7357  O  O   . THR C 1 198 ? -2.541  21.256  13.752  1.00 30.89  ? 198  THR C O   1 
ATOM   7358  C  CB  . THR C 1 198 ? -0.895  18.276  14.236  1.00 39.05  ? 198  THR C CB  1 
ATOM   7359  O  OG1 . THR C 1 198 ? -0.937  17.031  14.939  1.00 41.21  ? 198  THR C OG1 1 
ATOM   7360  C  CG2 . THR C 1 198 ? 0.185   19.162  14.858  1.00 43.46  ? 198  THR C CG2 1 
ATOM   7361  N  N   . ALA C 1 199 ? -2.274  19.772  12.076  1.00 39.05  ? 199  ALA C N   1 
ATOM   7362  C  CA  . ALA C 1 199 ? -2.331  20.786  11.028  1.00 33.78  ? 199  ALA C CA  1 
ATOM   7363  C  C   . ALA C 1 199 ? -3.566  21.694  11.198  1.00 39.91  ? 199  ALA C C   1 
ATOM   7364  O  O   . ALA C 1 199 ? -3.486  22.924  11.045  1.00 37.55  ? 199  ALA C O   1 
ATOM   7365  C  CB  . ALA C 1 199 ? -2.297  20.126  9.647   1.00 20.99  ? 199  ALA C CB  1 
ATOM   7366  N  N   . ALA C 1 200 ? -4.703  21.091  11.536  1.00 21.07  ? 200  ALA C N   1 
ATOM   7367  C  CA  . ALA C 1 200 ? -5.913  21.869  11.749  1.00 24.40  ? 200  ALA C CA  1 
ATOM   7368  C  C   . ALA C 1 200 ? -5.662  22.918  12.828  1.00 36.93  ? 200  ALA C C   1 
ATOM   7369  O  O   . ALA C 1 200 ? -5.957  24.107  12.655  1.00 49.50  ? 200  ALA C O   1 
ATOM   7370  C  CB  . ALA C 1 200 ? -7.083  20.966  12.141  1.00 17.88  ? 200  ALA C CB  1 
ATOM   7371  N  N   . LEU C 1 201 ? -5.105  22.479  13.947  1.00 21.00  ? 201  LEU C N   1 
ATOM   7372  C  CA  . LEU C 1 201 ? -4.913  23.382  15.059  1.00 31.80  ? 201  LEU C CA  1 
ATOM   7373  C  C   . LEU C 1 201 ? -3.812  24.410  14.833  1.00 36.73  ? 201  LEU C C   1 
ATOM   7374  O  O   . LEU C 1 201 ? -3.973  25.588  15.176  1.00 23.30  ? 201  LEU C O   1 
ATOM   7375  C  CB  . LEU C 1 201 ? -4.705  22.607  16.356  1.00 31.11  ? 201  LEU C CB  1 
ATOM   7376  C  CG  . LEU C 1 201 ? -6.096  22.482  16.981  1.00 36.16  ? 201  LEU C CG  1 
ATOM   7377  C  CD1 . LEU C 1 201 ? -6.857  21.298  16.384  1.00 35.67  ? 201  LEU C CD1 1 
ATOM   7378  C  CD2 . LEU C 1 201 ? -6.026  22.392  18.474  1.00 47.17  ? 201  LEU C CD2 1 
ATOM   7379  N  N   . VAL C 1 202 ? -2.700  23.972  14.255  1.00 26.76  ? 202  VAL C N   1 
ATOM   7380  C  CA  . VAL C 1 202 ? -1.655  24.917  13.905  1.00 29.71  ? 202  VAL C CA  1 
ATOM   7381  C  C   . VAL C 1 202 ? -2.294  26.064  13.121  1.00 36.96  ? 202  VAL C C   1 
ATOM   7382  O  O   . VAL C 1 202 ? -2.159  27.238  13.491  1.00 34.62  ? 202  VAL C O   1 
ATOM   7383  C  CB  . VAL C 1 202 ? -0.527  24.267  13.073  1.00 24.60  ? 202  VAL C CB  1 
ATOM   7384  C  CG1 . VAL C 1 202 ? 0.306   25.331  12.419  1.00 16.90  ? 202  VAL C CG1 1 
ATOM   7385  C  CG2 . VAL C 1 202 ? 0.362   23.393  13.948  1.00 17.36  ? 202  VAL C CG2 1 
ATOM   7386  N  N   . ASN C 1 203 ? -3.018  25.716  12.056  1.00 23.24  ? 203  ASN C N   1 
ATOM   7387  C  CA  . ASN C 1 203 ? -3.606  26.729  11.179  1.00 29.67  ? 203  ASN C CA  1 
ATOM   7388  C  C   . ASN C 1 203 ? -4.404  27.729  11.976  1.00 18.15  ? 203  ASN C C   1 
ATOM   7389  O  O   . ASN C 1 203 ? -4.257  28.933  11.839  1.00 29.93  ? 203  ASN C O   1 
ATOM   7390  C  CB  . ASN C 1 203 ? -4.519  26.082  10.146  1.00 27.92  ? 203  ASN C CB  1 
ATOM   7391  C  CG  . ASN C 1 203 ? -3.788  25.695  8.874   1.00 50.15  ? 203  ASN C CG  1 
ATOM   7392  O  OD1 . ASN C 1 203 ? -2.555  25.657  8.833   1.00 50.00  ? 203  ASN C OD1 1 
ATOM   7393  N  ND2 . ASN C 1 203 ? -4.552  25.402  7.823   1.00 60.43  ? 203  ASN C ND2 1 
ATOM   7394  N  N   . TRP C 1 204 ? -5.258  27.189  12.821  1.00 26.95  ? 204  TRP C N   1 
ATOM   7395  C  CA  . TRP C 1 204 ? -6.157  27.966  13.637  1.00 18.76  ? 204  TRP C CA  1 
ATOM   7396  C  C   . TRP C 1 204 ? -5.361  28.900  14.527  1.00 28.71  ? 204  TRP C C   1 
ATOM   7397  O  O   . TRP C 1 204 ? -5.615  30.114  14.572  1.00 33.68  ? 204  TRP C O   1 
ATOM   7398  C  CB  . TRP C 1 204 ? -6.961  26.995  14.490  1.00 23.29  ? 204  TRP C CB  1 
ATOM   7399  C  CG  . TRP C 1 204 ? -8.138  27.605  15.144  1.00 33.16  ? 204  TRP C CG  1 
ATOM   7400  C  CD1 . TRP C 1 204 ? -9.020  28.483  14.588  1.00 34.93  ? 204  TRP C CD1 1 
ATOM   7401  C  CD2 . TRP C 1 204 ? -8.583  27.378  16.488  1.00 22.94  ? 204  TRP C CD2 1 
ATOM   7402  N  NE1 . TRP C 1 204 ? -9.987  28.824  15.505  1.00 36.61  ? 204  TRP C NE1 1 
ATOM   7403  C  CE2 . TRP C 1 204 ? -9.740  28.156  16.680  1.00 27.82  ? 204  TRP C CE2 1 
ATOM   7404  C  CE3 . TRP C 1 204 ? -8.110  26.601  17.546  1.00 12.10  ? 204  TRP C CE3 1 
ATOM   7405  C  CZ2 . TRP C 1 204 ? -10.437 28.169  17.885  1.00 16.27  ? 204  TRP C CZ2 1 
ATOM   7406  C  CZ3 . TRP C 1 204 ? -8.800  26.617  18.742  1.00 28.19  ? 204  TRP C CZ3 1 
ATOM   7407  C  CH2 . TRP C 1 204 ? -9.951  27.396  18.902  1.00 24.18  ? 204  TRP C CH2 1 
ATOM   7408  N  N   . ILE C 1 205 ? -4.390  28.322  15.230  1.00 23.00  ? 205  ILE C N   1 
ATOM   7409  C  CA  . ILE C 1 205 ? -3.636  29.039  16.253  1.00 32.84  ? 205  ILE C CA  1 
ATOM   7410  C  C   . ILE C 1 205 ? -2.977  30.312  15.703  1.00 41.32  ? 205  ILE C C   1 
ATOM   7411  O  O   . ILE C 1 205 ? -2.911  31.340  16.379  1.00 45.47  ? 205  ILE C O   1 
ATOM   7412  C  CB  . ILE C 1 205 ? -2.590  28.109  16.902  1.00 32.04  ? 205  ILE C CB  1 
ATOM   7413  C  CG1 . ILE C 1 205 ? -3.295  26.985  17.681  1.00 36.10  ? 205  ILE C CG1 1 
ATOM   7414  C  CG2 . ILE C 1 205 ? -1.652  28.895  17.796  1.00 37.29  ? 205  ILE C CG2 1 
ATOM   7415  C  CD1 . ILE C 1 205 ? -2.379  25.836  18.093  1.00 29.69  ? 205  ILE C CD1 1 
ATOM   7416  N  N   . VAL C 1 206 ? -2.511  30.236  14.465  1.00 29.85  ? 206  VAL C N   1 
ATOM   7417  C  CA  . VAL C 1 206 ? -1.839  31.358  13.835  1.00 36.79  ? 206  VAL C CA  1 
ATOM   7418  C  C   . VAL C 1 206 ? -2.837  32.214  13.069  1.00 29.17  ? 206  VAL C C   1 
ATOM   7419  O  O   . VAL C 1 206 ? -2.478  33.212  12.454  1.00 29.97  ? 206  VAL C O   1 
ATOM   7420  C  CB  . VAL C 1 206 ? -0.744  30.865  12.859  1.00 32.10  ? 206  VAL C CB  1 
ATOM   7421  C  CG1 . VAL C 1 206 ? 0.354   30.119  13.614  1.00 24.89  ? 206  VAL C CG1 1 
ATOM   7422  C  CG2 . VAL C 1 206 ? -1.364  29.968  11.806  1.00 36.47  ? 206  VAL C CG2 1 
ATOM   7423  N  N   . SER C 1 207 ? -4.098  31.819  13.105  1.00 32.80  ? 207  SER C N   1 
ATOM   7424  C  CA  . SER C 1 207 ? -5.100  32.477  12.284  1.00 30.80  ? 207  SER C CA  1 
ATOM   7425  C  C   . SER C 1 207 ? -5.704  33.660  13.023  1.00 29.78  ? 207  SER C C   1 
ATOM   7426  O  O   . SER C 1 207 ? -6.348  34.512  12.420  1.00 37.17  ? 207  SER C O   1 
ATOM   7427  C  CB  . SER C 1 207 ? -6.204  31.498  11.883  1.00 17.65  ? 207  SER C CB  1 
ATOM   7428  O  OG  . SER C 1 207 ? -7.204  31.430  12.880  1.00 31.29  ? 207  SER C OG  1 
ATOM   7429  N  N   . LYS C 1 208 ? -5.499  33.701  14.334  1.00 29.75  ? 208  LYS C N   1 
ATOM   7430  C  CA  . LYS C 1 208 ? -6.070  34.751  15.178  1.00 33.77  ? 208  LYS C CA  1 
ATOM   7431  C  C   . LYS C 1 208 ? -5.116  35.112  16.307  1.00 20.95  ? 208  LYS C C   1 
ATOM   7432  O  O   . LYS C 1 208 ? -4.401  34.266  16.808  1.00 41.48  ? 208  LYS C O   1 
ATOM   7433  C  CB  . LYS C 1 208 ? -7.428  34.321  15.752  1.00 41.59  ? 208  LYS C CB  1 
ATOM   7434  C  CG  . LYS C 1 208 ? -8.501  34.103  14.697  1.00 40.81  ? 208  LYS C CG  1 
ATOM   7435  C  CD  . LYS C 1 208 ? -9.855  33.762  15.296  1.00 30.85  ? 208  LYS C CD  1 
ATOM   7436  C  CE  . LYS C 1 208 ? -10.943 33.871  14.214  1.00 44.27  ? 208  LYS C CE  1 
ATOM   7437  N  NZ  . LYS C 1 208 ? -12.292 33.467  14.685  1.00 45.47  ? 208  LYS C NZ  1 
ATOM   7438  N  N   . PRO C 1 209 ? -5.114  36.378  16.714  1.00 20.37  ? 209  PRO C N   1 
ATOM   7439  C  CA  . PRO C 1 209 ? -4.236  36.880  17.772  1.00 23.48  ? 209  PRO C CA  1 
ATOM   7440  C  C   . PRO C 1 209 ? -4.586  36.359  19.179  1.00 33.44  ? 209  PRO C C   1 
ATOM   7441  O  O   . PRO C 1 209 ? -4.722  37.166  20.101  1.00 33.45  ? 209  PRO C O   1 
ATOM   7442  C  CB  . PRO C 1 209 ? -4.475  38.389  17.724  1.00 18.79  ? 209  PRO C CB  1 
ATOM   7443  C  CG  . PRO C 1 209 ? -5.875  38.516  17.257  1.00 26.36  ? 209  PRO C CG  1 
ATOM   7444  C  CD  . PRO C 1 209 ? -6.051  37.411  16.239  1.00 24.06  ? 209  PRO C CD  1 
ATOM   7445  N  N   . PHE C 1 210 ? -4.693  35.045  19.353  1.00 29.70  ? 210  PHE C N   1 
ATOM   7446  C  CA  . PHE C 1 210 ? -5.063  34.493  20.651  1.00 27.73  ? 210  PHE C CA  1 
ATOM   7447  C  C   . PHE C 1 210 ? -4.166  35.002  21.761  1.00 30.45  ? 210  PHE C C   1 
ATOM   7448  O  O   . PHE C 1 210 ? -2.940  35.009  21.633  1.00 35.43  ? 210  PHE C O   1 
ATOM   7449  C  CB  . PHE C 1 210 ? -5.071  32.962  20.629  1.00 20.71  ? 210  PHE C CB  1 
ATOM   7450  C  CG  . PHE C 1 210 ? -6.233  32.375  19.861  1.00 28.36  ? 210  PHE C CG  1 
ATOM   7451  C  CD1 . PHE C 1 210 ? -6.040  31.792  18.606  1.00 28.25  ? 210  PHE C CD1 1 
ATOM   7452  C  CD2 . PHE C 1 210 ? -7.523  32.427  20.382  1.00 32.48  ? 210  PHE C CD2 1 
ATOM   7453  C  CE1 . PHE C 1 210 ? -7.108  31.260  17.892  1.00 18.60  ? 210  PHE C CE1 1 
ATOM   7454  C  CE2 . PHE C 1 210 ? -8.594  31.900  19.674  1.00 39.83  ? 210  PHE C CE2 1 
ATOM   7455  C  CZ  . PHE C 1 210 ? -8.386  31.317  18.422  1.00 31.34  ? 210  PHE C CZ  1 
ATOM   7456  N  N   . VAL C 1 211 ? -4.800  35.410  22.855  1.00 22.91  ? 211  VAL C N   1 
ATOM   7457  C  CA  . VAL C 1 211 ? -4.113  36.072  23.953  1.00 29.63  ? 211  VAL C CA  1 
ATOM   7458  C  C   . VAL C 1 211 ? -3.723  35.073  25.034  1.00 30.70  ? 211  VAL C C   1 
ATOM   7459  O  O   . VAL C 1 211 ? -2.629  35.135  25.592  1.00 38.33  ? 211  VAL C O   1 
ATOM   7460  C  CB  . VAL C 1 211 ? -4.983  37.208  24.573  1.00 20.04  ? 211  VAL C CB  1 
ATOM   7461  C  CG1 . VAL C 1 211 ? -4.380  37.717  25.882  1.00 22.43  ? 211  VAL C CG1 1 
ATOM   7462  C  CG2 . VAL C 1 211 ? -5.151  38.349  23.580  1.00 24.41  ? 211  VAL C CG2 1 
ATOM   7463  N  N   . LEU C 1 212 ? -4.634  34.153  25.319  1.00 29.26  ? 212  LEU C N   1 
ATOM   7464  C  CA  . LEU C 1 212 ? -4.495  33.209  26.428  1.00 26.33  ? 212  LEU C CA  1 
ATOM   7465  C  C   . LEU C 1 212 ? -5.167  31.897  26.041  1.00 17.67  ? 212  LEU C C   1 
ATOM   7466  O  O   . LEU C 1 212 ? -6.150  31.894  25.304  1.00 36.15  ? 212  LEU C O   1 
ATOM   7467  C  CB  . LEU C 1 212 ? -5.146  33.781  27.708  1.00 37.13  ? 212  LEU C CB  1 
ATOM   7468  C  CG  . LEU C 1 212 ? -5.323  32.940  28.994  1.00 36.50  ? 212  LEU C CG  1 
ATOM   7469  C  CD1 . LEU C 1 212 ? -3.970  32.473  29.525  1.00 45.58  ? 212  LEU C CD1 1 
ATOM   7470  C  CD2 . LEU C 1 212 ? -6.096  33.703  30.087  1.00 21.87  ? 212  LEU C CD2 1 
ATOM   7471  N  N   . SER C 1 213 ? -4.638  30.784  26.533  1.00 19.66  ? 213  SER C N   1 
ATOM   7472  C  CA  . SER C 1 213 ? -5.147  29.477  26.141  1.00 15.53  ? 213  SER C CA  1 
ATOM   7473  C  C   . SER C 1 213 ? -4.785  28.420  27.161  1.00 25.89  ? 213  SER C C   1 
ATOM   7474  O  O   . SER C 1 213 ? -3.859  28.595  27.946  1.00 30.17  ? 213  SER C O   1 
ATOM   7475  C  CB  . SER C 1 213 ? -4.569  29.077  24.787  1.00 20.39  ? 213  SER C CB  1 
ATOM   7476  O  OG  . SER C 1 213 ? -4.857  27.722  24.511  1.00 31.17  ? 213  SER C OG  1 
ATOM   7477  N  N   . ALA C 1 214 ? -5.508  27.310  27.131  1.00 28.78  ? 214  ALA C N   1 
ATOM   7478  C  CA  . ALA C 1 214 ? -5.203  26.178  27.993  1.00 28.25  ? 214  ALA C CA  1 
ATOM   7479  C  C   . ALA C 1 214 ? -5.693  24.878  27.356  1.00 20.54  ? 214  ALA C C   1 
ATOM   7480  O  O   . ALA C 1 214 ? -6.790  24.835  26.800  1.00 25.59  ? 214  ALA C O   1 
ATOM   7481  C  CB  . ALA C 1 214 ? -5.846  26.379  29.369  1.00 31.99  ? 214  ALA C CB  1 
ATOM   7482  N  N   . ASN C 1 215 ? -4.885  23.823  27.412  1.00 31.18  ? 215  ASN C N   1 
ATOM   7483  C  CA  . ASN C 1 215 ? -5.362  22.523  26.958  1.00 29.68  ? 215  ASN C CA  1 
ATOM   7484  C  C   . ASN C 1 215 ? -5.263  21.457  28.042  1.00 42.92  ? 215  ASN C C   1 
ATOM   7485  O  O   . ASN C 1 215 ? -4.289  21.414  28.801  1.00 41.63  ? 215  ASN C O   1 
ATOM   7486  C  CB  . ASN C 1 215 ? -4.715  22.092  25.641  1.00 33.43  ? 215  ASN C CB  1 
ATOM   7487  C  CG  . ASN C 1 215 ? -3.287  21.679  25.792  1.00 26.64  ? 215  ASN C CG  1 
ATOM   7488  O  OD1 . ASN C 1 215 ? -2.969  20.486  25.767  1.00 43.75  ? 215  ASN C OD1 1 
ATOM   7489  N  ND2 . ASN C 1 215 ? -2.405  22.652  25.907  1.00 21.19  ? 215  ASN C ND2 1 
ATOM   7490  N  N   . PHE C 1 216 ? -6.291  20.614  28.113  1.00 33.24  ? 216  PHE C N   1 
ATOM   7491  C  CA  . PHE C 1 216 ? -6.516  19.791  29.292  1.00 17.92  ? 216  PHE C CA  1 
ATOM   7492  C  C   . PHE C 1 216 ? -6.156  18.335  29.089  1.00 23.92  ? 216  PHE C C   1 
ATOM   7493  O  O   . PHE C 1 216 ? -6.470  17.735  28.067  1.00 34.26  ? 216  PHE C O   1 
ATOM   7494  C  CB  . PHE C 1 216 ? -7.971  19.932  29.724  1.00 30.02  ? 216  PHE C CB  1 
ATOM   7495  C  CG  . PHE C 1 216 ? -8.357  21.339  30.029  1.00 33.09  ? 216  PHE C CG  1 
ATOM   7496  C  CD1 . PHE C 1 216 ? -8.846  22.166  29.032  1.00 40.15  ? 216  PHE C CD1 1 
ATOM   7497  C  CD2 . PHE C 1 216 ? -8.192  21.857  31.309  1.00 36.45  ? 216  PHE C CD2 1 
ATOM   7498  C  CE1 . PHE C 1 216 ? -9.187  23.496  29.306  1.00 28.73  ? 216  PHE C CE1 1 
ATOM   7499  C  CE2 . PHE C 1 216 ? -8.537  23.181  31.595  1.00 35.78  ? 216  PHE C CE2 1 
ATOM   7500  C  CZ  . PHE C 1 216 ? -9.034  24.000  30.586  1.00 24.12  ? 216  PHE C CZ  1 
ATOM   7501  N  N   . HIS C 1 217 ? -5.499  17.773  30.085  1.00 19.76  ? 217  HIS C N   1 
ATOM   7502  C  CA  . HIS C 1 217 ? -4.996  16.420  29.999  1.00 27.95  ? 217  HIS C CA  1 
ATOM   7503  C  C   . HIS C 1 217 ? -5.424  15.688  31.234  1.00 27.92  ? 217  HIS C C   1 
ATOM   7504  O  O   . HIS C 1 217 ? -6.034  16.280  32.110  1.00 36.66  ? 217  HIS C O   1 
ATOM   7505  C  CB  . HIS C 1 217 ? -3.473  16.445  29.932  1.00 35.65  ? 217  HIS C CB  1 
ATOM   7506  C  CG  . HIS C 1 217 ? -2.946  16.954  28.630  1.00 28.20  ? 217  HIS C CG  1 
ATOM   7507  N  ND1 . HIS C 1 217 ? -2.440  16.124  27.654  1.00 34.37  ? 217  HIS C ND1 1 
ATOM   7508  C  CD2 . HIS C 1 217 ? -2.879  18.208  28.128  1.00 36.16  ? 217  HIS C CD2 1 
ATOM   7509  C  CE1 . HIS C 1 217 ? -2.069  16.849  26.612  1.00 42.17  ? 217  HIS C CE1 1 
ATOM   7510  N  NE2 . HIS C 1 217 ? -2.325  18.118  26.873  1.00 34.53  ? 217  HIS C NE2 1 
ATOM   7511  N  N   . GLY C 1 218 ? -5.095  14.404  31.310  1.00 39.31  ? 218  GLY C N   1 
ATOM   7512  C  CA  . GLY C 1 218 ? -5.396  13.603  32.485  1.00 31.46  ? 218  GLY C CA  1 
ATOM   7513  C  C   . GLY C 1 218 ? -4.243  12.685  32.825  1.00 32.35  ? 218  GLY C C   1 
ATOM   7514  O  O   . GLY C 1 218 ? -3.364  12.452  31.992  1.00 38.56  ? 218  GLY C O   1 
ATOM   7515  N  N   . GLY C 1 219 ? -4.250  12.168  34.050  1.00 32.66  ? 219  GLY C N   1 
ATOM   7516  C  CA  . GLY C 1 219 ? -3.230  11.242  34.512  1.00 35.60  ? 219  GLY C CA  1 
ATOM   7517  C  C   . GLY C 1 219 ? -2.541  11.808  35.734  1.00 50.78  ? 219  GLY C C   1 
ATOM   7518  O  O   . GLY C 1 219 ? -1.820  11.115  36.468  1.00 55.67  ? 219  GLY C O   1 
ATOM   7519  N  N   . ALA C 1 220 ? -2.774  13.095  35.949  1.00 45.97  ? 220  ALA C N   1 
ATOM   7520  C  CA  . ALA C 1 220 ? -2.221  13.783  37.097  1.00 52.44  ? 220  ALA C CA  1 
ATOM   7521  C  C   . ALA C 1 220 ? -3.033  15.039  37.352  1.00 35.06  ? 220  ALA C C   1 
ATOM   7522  O  O   . ALA C 1 220 ? -3.800  15.463  36.492  1.00 27.41  ? 220  ALA C O   1 
ATOM   7523  C  CB  . ALA C 1 220 ? -0.751  14.119  36.859  1.00 51.54  ? 220  ALA C CB  1 
ATOM   7524  N  N   . VAL C 1 221 ? -2.867  15.614  38.539  1.00 35.08  ? 221  VAL C N   1 
ATOM   7525  C  CA  . VAL C 1 221 ? -3.552  16.850  38.897  1.00 45.31  ? 221  VAL C CA  1 
ATOM   7526  C  C   . VAL C 1 221 ? -2.568  17.983  39.155  1.00 47.72  ? 221  VAL C C   1 
ATOM   7527  O  O   . VAL C 1 221 ? -2.040  18.110  40.262  1.00 43.36  ? 221  VAL C O   1 
ATOM   7528  C  CB  . VAL C 1 221 ? -4.397  16.660  40.144  1.00 39.75  ? 221  VAL C CB  1 
ATOM   7529  C  CG1 . VAL C 1 221 ? -5.418  17.788  40.255  1.00 33.26  ? 221  VAL C CG1 1 
ATOM   7530  C  CG2 . VAL C 1 221 ? -5.071  15.303  40.093  1.00 37.60  ? 221  VAL C CG2 1 
ATOM   7531  N  N   . VAL C 1 222 ? -2.331  18.808  38.134  1.00 42.22  ? 222  VAL C N   1 
ATOM   7532  C  CA  . VAL C 1 222 ? -1.326  19.861  38.234  1.00 40.43  ? 222  VAL C CA  1 
ATOM   7533  C  C   . VAL C 1 222 ? -1.456  20.908  37.128  1.00 47.17  ? 222  VAL C C   1 
ATOM   7534  O  O   . VAL C 1 222 ? -1.970  20.625  36.044  1.00 53.80  ? 222  VAL C O   1 
ATOM   7535  C  CB  . VAL C 1 222 ? 0.073   19.262  38.152  1.00 39.70  ? 222  VAL C CB  1 
ATOM   7536  C  CG1 . VAL C 1 222 ? 0.317   18.745  36.756  1.00 28.84  ? 222  VAL C CG1 1 
ATOM   7537  C  CG2 . VAL C 1 222 ? 1.116   20.293  38.534  1.00 49.27  ? 222  VAL C CG2 1 
ATOM   7538  N  N   . ALA C 1 223 ? -0.984  22.118  37.414  1.00 36.13  ? 223  ALA C N   1 
ATOM   7539  C  CA  . ALA C 1 223 ? -0.968  23.200  36.435  1.00 33.00  ? 223  ALA C CA  1 
ATOM   7540  C  C   . ALA C 1 223 ? 0.440   23.375  35.845  1.00 41.98  ? 223  ALA C C   1 
ATOM   7541  O  O   . ALA C 1 223 ? 1.351   23.874  36.516  1.00 42.11  ? 223  ALA C O   1 
ATOM   7542  C  CB  . ALA C 1 223 ? -1.461  24.503  37.071  1.00 21.89  ? 223  ALA C CB  1 
ATOM   7543  N  N   . SER C 1 224 ? 0.608   22.963  34.590  1.00 36.78  ? 224  SER C N   1 
ATOM   7544  C  CA  . SER C 1 224 ? 1.917   22.972  33.934  1.00 31.12  ? 224  SER C CA  1 
ATOM   7545  C  C   . SER C 1 224 ? 2.032   24.107  32.905  1.00 29.98  ? 224  SER C C   1 
ATOM   7546  O  O   . SER C 1 224 ? 1.054   24.473  32.259  1.00 31.50  ? 224  SER C O   1 
ATOM   7547  C  CB  . SER C 1 224 ? 2.187   21.615  33.280  1.00 32.96  ? 224  SER C CB  1 
ATOM   7548  O  OG  . SER C 1 224 ? 3.508   21.547  32.778  1.00 45.01  ? 224  SER C OG  1 
ATOM   7549  N  N   . TYR C 1 225 ? 3.229   24.666  32.767  1.00 28.97  ? 225  TYR C N   1 
ATOM   7550  C  CA  . TYR C 1 225 ? 3.446   25.836  31.933  1.00 19.05  ? 225  TYR C CA  1 
ATOM   7551  C  C   . TYR C 1 225 ? 4.795   25.689  31.228  1.00 29.56  ? 225  TYR C C   1 
ATOM   7552  O  O   . TYR C 1 225 ? 5.594   24.827  31.611  1.00 30.12  ? 225  TYR C O   1 
ATOM   7553  C  CB  . TYR C 1 225 ? 3.385   27.120  32.787  1.00 34.21  ? 225  TYR C CB  1 
ATOM   7554  C  CG  . TYR C 1 225 ? 4.300   27.129  34.009  1.00 25.89  ? 225  TYR C CG  1 
ATOM   7555  C  CD1 . TYR C 1 225 ? 3.905   26.559  35.206  1.00 27.71  ? 225  TYR C CD1 1 
ATOM   7556  C  CD2 . TYR C 1 225 ? 5.558   27.714  33.955  1.00 38.38  ? 225  TYR C CD2 1 
ATOM   7557  C  CE1 . TYR C 1 225 ? 4.736   26.562  36.307  1.00 33.44  ? 225  TYR C CE1 1 
ATOM   7558  C  CE2 . TYR C 1 225 ? 6.401   27.723  35.055  1.00 44.66  ? 225  TYR C CE2 1 
ATOM   7559  C  CZ  . TYR C 1 225 ? 5.983   27.150  36.227  1.00 43.88  ? 225  TYR C CZ  1 
ATOM   7560  O  OH  . TYR C 1 225 ? 6.823   27.158  37.318  1.00 51.93  ? 225  TYR C OH  1 
ATOM   7561  N  N   . PRO C 1 226 ? 5.045   26.511  30.183  1.00 29.85  ? 226  PRO C N   1 
ATOM   7562  C  CA  . PRO C 1 226 ? 6.261   26.473  29.342  1.00 35.88  ? 226  PRO C CA  1 
ATOM   7563  C  C   . PRO C 1 226 ? 7.570   26.797  30.074  1.00 35.95  ? 226  PRO C C   1 
ATOM   7564  O  O   . PRO C 1 226 ? 7.551   27.500  31.100  1.00 35.82  ? 226  PRO C O   1 
ATOM   7565  C  CB  . PRO C 1 226 ? 5.989   27.552  28.281  1.00 37.24  ? 226  PRO C CB  1 
ATOM   7566  C  CG  . PRO C 1 226 ? 4.509   27.651  28.216  1.00 35.92  ? 226  PRO C CG  1 
ATOM   7567  C  CD  . PRO C 1 226 ? 4.029   27.422  29.627  1.00 25.85  ? 226  PRO C CD  1 
ATOM   7568  N  N   . TYR C 1 227 ? 8.699   26.300  29.558  1.00 30.13  ? 227  TYR C N   1 
ATOM   7569  C  CA  . TYR C 1 227 ? 8.762   25.449  28.372  1.00 30.39  ? 227  TYR C CA  1 
ATOM   7570  C  C   . TYR C 1 227 ? 8.705   23.981  28.774  1.00 39.03  ? 227  TYR C C   1 
ATOM   7571  O  O   . TYR C 1 227 ? 9.086   23.632  29.900  1.00 36.48  ? 227  TYR C O   1 
ATOM   7572  C  CB  . TYR C 1 227 ? 10.096  25.644  27.648  1.00 34.94  ? 227  TYR C CB  1 
ATOM   7573  C  CG  . TYR C 1 227 ? 10.276  26.959  26.953  1.00 32.81  ? 227  TYR C CG  1 
ATOM   7574  C  CD1 . TYR C 1 227 ? 9.579   27.251  25.799  1.00 30.48  ? 227  TYR C CD1 1 
ATOM   7575  C  CD2 . TYR C 1 227 ? 11.178  27.899  27.430  1.00 40.78  ? 227  TYR C CD2 1 
ATOM   7576  C  CE1 . TYR C 1 227 ? 9.755   28.458  25.151  1.00 32.31  ? 227  TYR C CE1 1 
ATOM   7577  C  CE2 . TYR C 1 227 ? 11.368  29.112  26.783  1.00 31.32  ? 227  TYR C CE2 1 
ATOM   7578  C  CZ  . TYR C 1 227 ? 10.652  29.381  25.649  1.00 37.94  ? 227  TYR C CZ  1 
ATOM   7579  O  OH  . TYR C 1 227 ? 10.823  30.572  24.995  1.00 45.27  ? 227  TYR C OH  1 
ATOM   7580  N  N   . ASP C 1 228 ? 8.288   23.127  27.835  1.00 37.15  ? 228  ASP C N   1 
ATOM   7581  C  CA  . ASP C 1 228 ? 8.247   21.677  28.037  1.00 25.87  ? 228  ASP C CA  1 
ATOM   7582  C  C   . ASP C 1 228 ? 9.575   20.992  27.702  1.00 35.86  ? 228  ASP C C   1 
ATOM   7583  O  O   . ASP C 1 228 ? 9.756   19.813  28.023  1.00 44.51  ? 228  ASP C O   1 
ATOM   7584  C  CB  . ASP C 1 228 ? 7.135   21.032  27.201  1.00 26.31  ? 228  ASP C CB  1 
ATOM   7585  C  CG  . ASP C 1 228 ? 5.743   21.245  27.786  1.00 47.89  ? 228  ASP C CG  1 
ATOM   7586  O  OD1 . ASP C 1 228 ? 5.630   21.635  28.973  1.00 50.26  ? 228  ASP C OD1 1 
ATOM   7587  O  OD2 . ASP C 1 228 ? 4.750   21.012  27.051  1.00 53.01  ? 228  ASP C OD2 1 
ATOM   7588  N  N   . ASN C 1 229 ? 10.487  21.706  27.039  1.00 34.03  ? 229  ASN C N   1 
ATOM   7589  C  CA  . ASN C 1 229 ? 11.817  21.154  26.741  1.00 44.84  ? 229  ASN C CA  1 
ATOM   7590  C  C   . ASN C 1 229 ? 12.885  22.234  26.726  1.00 49.16  ? 229  ASN C C   1 
ATOM   7591  O  O   . ASN C 1 229 ? 12.591  23.401  27.009  1.00 39.19  ? 229  ASN C O   1 
ATOM   7592  C  CB  . ASN C 1 229 ? 11.837  20.406  25.402  1.00 38.48  ? 229  ASN C CB  1 
ATOM   7593  C  CG  . ASN C 1 229 ? 11.688  21.337  24.224  1.00 40.39  ? 229  ASN C CG  1 
ATOM   7594  O  OD1 . ASN C 1 229 ? 11.716  22.565  24.385  1.00 32.12  ? 229  ASN C OD1 1 
ATOM   7595  N  ND2 . ASN C 1 229 ? 11.522  20.767  23.026  1.00 35.71  ? 229  ASN C ND2 1 
ATOM   7596  N  N   . SER C 1 230 ? 14.110  21.838  26.359  1.00 54.98  ? 230  SER C N   1 
ATOM   7597  C  CA  . SER C 1 230 ? 15.279  22.724  26.374  1.00 36.69  ? 230  SER C CA  1 
ATOM   7598  C  C   . SER C 1 230 ? 16.409  22.210  25.476  1.00 39.01  ? 230  SER C C   1 
ATOM   7599  O  O   . SER C 1 230 ? 16.416  21.036  25.091  1.00 43.37  ? 230  SER C O   1 
ATOM   7600  C  CB  . SER C 1 230 ? 15.813  22.828  27.799  1.00 34.14  ? 230  SER C CB  1 
ATOM   7601  O  OG  . SER C 1 230 ? 16.488  21.630  28.152  1.00 47.50  ? 230  SER C OG  1 
ATOM   7602  N  N   . LEU C 1 231 ? 17.374  23.085  25.170  1.00 47.84  ? 231  LEU C N   1 
ATOM   7603  C  CA  . LEU C 1 231 ? 18.581  22.704  24.410  1.00 55.14  ? 231  LEU C CA  1 
ATOM   7604  C  C   . LEU C 1 231 ? 19.416  21.610  25.076  1.00 59.96  ? 231  LEU C C   1 
ATOM   7605  O  O   . LEU C 1 231 ? 20.077  20.825  24.392  1.00 62.29  ? 231  LEU C O   1 
ATOM   7606  C  CB  . LEU C 1 231 ? 19.490  23.913  24.165  1.00 53.50  ? 231  LEU C CB  1 
ATOM   7607  C  CG  . LEU C 1 231 ? 19.224  24.815  22.956  1.00 56.76  ? 231  LEU C CG  1 
ATOM   7608  C  CD1 . LEU C 1 231 ? 20.096  26.075  23.047  1.00 50.13  ? 231  LEU C CD1 1 
ATOM   7609  C  CD2 . LEU C 1 231 ? 19.449  24.068  21.628  1.00 51.51  ? 231  LEU C CD2 1 
ATOM   7610  N  N   . ALA C 1 232 ? 19.409  21.600  26.408  1.00 57.90  ? 232  ALA C N   1 
ATOM   7611  C  CA  . ALA C 1 232 ? 20.097  20.589  27.209  1.00 54.22  ? 232  ALA C CA  1 
ATOM   7612  C  C   . ALA C 1 232 ? 19.487  19.206  26.960  1.00 61.00  ? 232  ALA C C   1 
ATOM   7613  O  O   . ALA C 1 232 ? 20.175  18.179  27.032  1.00 49.13  ? 232  ALA C O   1 
ATOM   7614  C  CB  . ALA C 1 232 ? 20.000  20.952  28.695  1.00 36.41  ? 232  ALA C CB  1 
ATOM   7615  N  N   . HIS C 1 233 ? 18.190  19.212  26.654  1.00 64.22  ? 233  HIS C N   1 
ATOM   7616  C  CA  . HIS C 1 233 ? 17.400  17.997  26.494  1.00 58.96  ? 233  HIS C CA  1 
ATOM   7617  C  C   . HIS C 1 233 ? 17.520  17.059  27.703  1.00 60.43  ? 233  HIS C C   1 
ATOM   7618  O  O   . HIS C 1 233 ? 17.825  15.876  27.552  1.00 60.29  ? 233  HIS C O   1 
ATOM   7619  C  CB  . HIS C 1 233 ? 17.734  17.287  25.175  1.00 43.13  ? 233  HIS C CB  1 
ATOM   7620  C  CG  . HIS C 1 233 ? 17.167  17.972  23.965  1.00 51.54  ? 233  HIS C CG  1 
ATOM   7621  N  ND1 . HIS C 1 233 ? 17.955  18.637  23.049  1.00 63.45  ? 233  HIS C ND1 1 
ATOM   7622  C  CD2 . HIS C 1 233 ? 15.891  18.104  23.527  1.00 51.98  ? 233  HIS C CD2 1 
ATOM   7623  C  CE1 . HIS C 1 233 ? 17.191  19.147  22.097  1.00 59.36  ? 233  HIS C CE1 1 
ATOM   7624  N  NE2 . HIS C 1 233 ? 15.933  18.839  22.363  1.00 51.42  ? 233  HIS C NE2 1 
ATOM   7625  N  N   . ASN C 1 234 ? 17.269  17.608  28.894  1.00 62.56  ? 234  ASN C N   1 
ATOM   7626  C  CA  . ASN C 1 234 ? 17.285  16.838  30.139  1.00 64.07  ? 234  ASN C CA  1 
ATOM   7627  C  C   . ASN C 1 234 ? 16.016  16.003  30.256  1.00 59.34  ? 234  ASN C C   1 
ATOM   7628  O  O   . ASN C 1 234 ? 14.925  16.483  29.937  1.00 53.29  ? 234  ASN C O   1 
ATOM   7629  C  CB  . ASN C 1 234 ? 17.409  17.763  31.368  1.00 56.68  ? 234  ASN C CB  1 
ATOM   7630  C  CG  . ASN C 1 234 ? 18.710  18.582  31.383  1.00 56.72  ? 234  ASN C CG  1 
ATOM   7631  O  OD1 . ASN C 1 234 ? 19.761  18.122  30.933  1.00 47.15  ? 234  ASN C OD1 1 
ATOM   7632  N  ND2 . ASN C 1 234 ? 18.635  19.801  31.922  1.00 47.73  ? 234  ASN C ND2 1 
ATOM   7633  N  N   . GLU C 1 235 ? 16.153  14.759  30.712  1.00 57.95  ? 235  GLU C N   1 
ATOM   7634  C  CA  . GLU C 1 235 ? 14.983  13.929  30.963  1.00 58.38  ? 235  GLU C CA  1 
ATOM   7635  C  C   . GLU C 1 235 ? 13.946  14.694  31.804  1.00 59.60  ? 235  GLU C C   1 
ATOM   7636  O  O   . GLU C 1 235 ? 12.784  14.808  31.414  1.00 36.58  ? 235  GLU C O   1 
ATOM   7637  C  CB  . GLU C 1 235 ? 15.379  12.620  31.655  1.00 54.62  ? 235  GLU C CB  1 
ATOM   7638  C  CG  . GLU C 1 235 ? 14.195  11.720  32.004  1.00 67.88  ? 235  GLU C CG  1 
ATOM   7639  C  CD  . GLU C 1 235 ? 14.600  10.473  32.792  1.00 88.32  ? 235  GLU C CD  1 
ATOM   7640  O  OE1 . GLU C 1 235 ? 13.943  9.421   32.619  1.00 100.64 ? 235  GLU C OE1 1 
ATOM   7641  O  OE2 . GLU C 1 235 ? 15.570  10.534  33.588  1.00 82.48  ? 235  GLU C OE2 1 
ATOM   7642  N  N   . CYS C 1 236 ? 14.385  15.246  32.935  1.00 64.14  ? 236  CYS C N   1 
ATOM   7643  C  CA  . CYS C 1 236 ? 13.456  15.752  33.934  1.00 59.74  ? 236  CYS C CA  1 
ATOM   7644  C  C   . CYS C 1 236 ? 14.088  16.660  34.979  1.00 57.48  ? 236  CYS C C   1 
ATOM   7645  O  O   . CYS C 1 236 ? 15.300  16.872  35.004  1.00 58.18  ? 236  CYS C O   1 
ATOM   7646  C  CB  . CYS C 1 236 ? 12.912  14.569  34.718  1.00 72.62  ? 236  CYS C CB  1 
ATOM   7647  S  SG  . CYS C 1 236 ? 14.125  14.032  35.974  1.00 62.99  ? 236  CYS C SG  1 
ATOM   7648  N  N   . CYS C 1 237 ? 13.230  17.151  35.871  1.00 58.89  ? 237  CYS C N   1 
ATOM   7649  C  CA  . CYS C 1 237 ? 13.634  17.776  37.122  1.00 44.84  ? 237  CYS C CA  1 
ATOM   7650  C  C   . CYS C 1 237 ? 14.590  18.943  36.902  1.00 45.65  ? 237  CYS C C   1 
ATOM   7651  O  O   . CYS C 1 237 ? 15.430  19.247  37.756  1.00 52.94  ? 237  CYS C O   1 
ATOM   7652  C  CB  . CYS C 1 237 ? 14.275  16.726  38.031  1.00 57.91  ? 237  CYS C CB  1 
ATOM   7653  S  SG  . CYS C 1 237 ? 13.711  15.047  37.692  1.00 70.79  ? 237  CYS C SG  1 
ATOM   7654  N  N   . GLU C 1 238 ? 14.479  19.593  35.750  1.00 45.23  ? 238  GLU C N   1 
ATOM   7655  C  CA  . GLU C 1 238 ? 15.276  20.788  35.482  1.00 42.88  ? 238  GLU C CA  1 
ATOM   7656  C  C   . GLU C 1 238 ? 14.437  21.825  34.759  1.00 50.95  ? 238  GLU C C   1 
ATOM   7657  O  O   . GLU C 1 238 ? 13.944  21.584  33.653  1.00 42.44  ? 238  GLU C O   1 
ATOM   7658  C  CB  . GLU C 1 238 ? 16.522  20.451  34.674  1.00 55.50  ? 238  GLU C CB  1 
ATOM   7659  C  CG  . GLU C 1 238 ? 17.811  20.896  35.336  1.00 71.65  ? 238  GLU C CG  1 
ATOM   7660  C  CD  . GLU C 1 238 ? 18.975  19.999  34.980  1.00 89.25  ? 238  GLU C CD  1 
ATOM   7661  O  OE1 . GLU C 1 238 ? 20.134  20.411  35.223  1.00 100.66 ? 238  GLU C OE1 1 
ATOM   7662  O  OE2 . GLU C 1 238 ? 18.729  18.883  34.457  1.00 85.17  ? 238  GLU C OE2 1 
ATOM   7663  N  N   . GLU C 1 239 ? 14.268  22.972  35.412  1.00 63.76  ? 239  GLU C N   1 
ATOM   7664  C  CA  . GLU C 1 239 ? 13.415  24.043  34.914  1.00 55.99  ? 239  GLU C CA  1 
ATOM   7665  C  C   . GLU C 1 239 ? 13.936  24.605  33.604  1.00 45.86  ? 239  GLU C C   1 
ATOM   7666  O  O   . GLU C 1 239 ? 15.073  25.048  33.536  1.00 60.93  ? 239  GLU C O   1 
ATOM   7667  C  CB  . GLU C 1 239 ? 13.312  25.178  35.951  1.00 66.83  ? 239  GLU C CB  1 
ATOM   7668  C  CG  . GLU C 1 239 ? 12.350  24.920  37.115  1.00 76.02  ? 239  GLU C CG  1 
ATOM   7669  C  CD  . GLU C 1 239 ? 12.214  26.120  38.045  1.00 87.93  ? 239  GLU C CD  1 
ATOM   7670  O  OE1 . GLU C 1 239 ? 11.114  26.321  38.617  1.00 85.50  ? 239  GLU C OE1 1 
ATOM   7671  O  OE2 . GLU C 1 239 ? 13.208  26.869  38.199  1.00 90.23  ? 239  GLU C OE2 1 
ATOM   7672  N  N   . SER C 1 240 ? 13.109  24.573  32.561  1.00 40.69  ? 240  SER C N   1 
ATOM   7673  C  CA  . SER C 1 240 ? 13.391  25.313  31.336  1.00 24.08  ? 240  SER C CA  1 
ATOM   7674  C  C   . SER C 1 240 ? 12.439  26.488  31.246  1.00 46.45  ? 240  SER C C   1 
ATOM   7675  O  O   . SER C 1 240 ? 11.426  26.422  30.547  1.00 53.67  ? 240  SER C O   1 
ATOM   7676  C  CB  . SER C 1 240 ? 13.225  24.436  30.098  1.00 26.30  ? 240  SER C CB  1 
ATOM   7677  O  OG  . SER C 1 240 ? 13.527  25.162  28.913  1.00 24.08  ? 240  SER C OG  1 
ATOM   7678  N  N   . LEU C 1 241 ? 12.764  27.570  31.945  1.00 54.90  ? 241  LEU C N   1 
ATOM   7679  C  CA  . LEU C 1 241 ? 11.814  28.668  32.136  1.00 43.98  ? 241  LEU C CA  1 
ATOM   7680  C  C   . LEU C 1 241 ? 11.659  29.601  30.939  1.00 38.73  ? 241  LEU C C   1 
ATOM   7681  O  O   . LEU C 1 241 ? 12.524  29.672  30.059  1.00 43.49  ? 241  LEU C O   1 
ATOM   7682  C  CB  . LEU C 1 241 ? 12.159  29.460  33.403  1.00 41.54  ? 241  LEU C CB  1 
ATOM   7683  C  CG  . LEU C 1 241 ? 12.051  28.643  34.700  1.00 44.78  ? 241  LEU C CG  1 
ATOM   7684  C  CD1 . LEU C 1 241 ? 12.453  29.481  35.936  1.00 32.28  ? 241  LEU C CD1 1 
ATOM   7685  C  CD2 . LEU C 1 241 ? 10.639  28.042  34.854  1.00 22.48  ? 241  LEU C CD2 1 
ATOM   7686  N  N   . THR C 1 242 ? 10.540  30.316  30.940  1.00 51.03  ? 242  THR C N   1 
ATOM   7687  C  CA  . THR C 1 242 ? 10.149  31.205  29.854  1.00 48.11  ? 242  THR C CA  1 
ATOM   7688  C  C   . THR C 1 242 ? 10.402  32.674  30.229  1.00 47.54  ? 242  THR C C   1 
ATOM   7689  O  O   . THR C 1 242 ? 10.344  33.037  31.412  1.00 45.90  ? 242  THR C O   1 
ATOM   7690  C  CB  . THR C 1 242 ? 8.643   30.979  29.519  1.00 49.84  ? 242  THR C CB  1 
ATOM   7691  O  OG1 . THR C 1 242 ? 8.509   30.216  28.304  1.00 44.25  ? 242  THR C OG1 1 
ATOM   7692  C  CG2 . THR C 1 242 ? 7.909   32.291  29.370  1.00 44.84  ? 242  THR C CG2 1 
ATOM   7693  N  N   . PRO C 1 243 ? 10.686  33.531  29.226  1.00 44.60  ? 243  PRO C N   1 
ATOM   7694  C  CA  . PRO C 1 243 ? 10.845  34.959  29.540  1.00 39.01  ? 243  PRO C CA  1 
ATOM   7695  C  C   . PRO C 1 243 ? 9.661   35.487  30.363  1.00 39.58  ? 243  PRO C C   1 
ATOM   7696  O  O   . PRO C 1 243 ? 9.803   36.396  31.180  1.00 36.10  ? 243  PRO C O   1 
ATOM   7697  C  CB  . PRO C 1 243 ? 10.867  35.631  28.158  1.00 28.04  ? 243  PRO C CB  1 
ATOM   7698  C  CG  . PRO C 1 243 ? 11.300  34.566  27.206  1.00 42.21  ? 243  PRO C CG  1 
ATOM   7699  C  CD  . PRO C 1 243 ? 10.781  33.260  27.777  1.00 49.73  ? 243  PRO C CD  1 
ATOM   7700  N  N   . ASP C 1 244 ? 8.487   34.911  30.138  1.00 44.08  ? 244  ASP C N   1 
ATOM   7701  C  CA  . ASP C 1 244 ? 7.285   35.339  30.833  1.00 40.06  ? 244  ASP C CA  1 
ATOM   7702  C  C   . ASP C 1 244 ? 6.966   34.377  31.963  1.00 41.35  ? 244  ASP C C   1 
ATOM   7703  O  O   . ASP C 1 244 ? 5.800   34.067  32.222  1.00 38.94  ? 244  ASP C O   1 
ATOM   7704  C  CB  . ASP C 1 244 ? 6.110   35.424  29.853  1.00 32.56  ? 244  ASP C CB  1 
ATOM   7705  C  CG  . ASP C 1 244 ? 6.067   36.746  29.104  1.00 49.14  ? 244  ASP C CG  1 
ATOM   7706  O  OD1 . ASP C 1 244 ? 5.673   37.757  29.729  1.00 54.63  ? 244  ASP C OD1 1 
ATOM   7707  O  OD2 . ASP C 1 244 ? 6.424   36.775  27.900  1.00 48.19  ? 244  ASP C OD2 1 
ATOM   7708  N  N   . ASP C 1 245 ? 8.001   33.903  32.644  1.00 31.45  ? 245  ASP C N   1 
ATOM   7709  C  CA  . ASP C 1 245 ? 7.770   32.950  33.726  1.00 37.84  ? 245  ASP C CA  1 
ATOM   7710  C  C   . ASP C 1 245 ? 6.866   33.463  34.851  1.00 42.84  ? 245  ASP C C   1 
ATOM   7711  O  O   . ASP C 1 245 ? 5.982   32.743  35.310  1.00 41.74  ? 245  ASP C O   1 
ATOM   7712  C  CB  . ASP C 1 245 ? 9.077   32.448  34.320  1.00 35.32  ? 245  ASP C CB  1 
ATOM   7713  C  CG  . ASP C 1 245 ? 8.898   31.138  35.056  1.00 53.85  ? 245  ASP C CG  1 
ATOM   7714  O  OD1 . ASP C 1 245 ? 8.385   30.184  34.425  1.00 63.09  ? 245  ASP C OD1 1 
ATOM   7715  O  OD2 . ASP C 1 245 ? 9.252   31.065  36.256  1.00 57.75  ? 245  ASP C OD2 1 
ATOM   7716  N  N   . ARG C 1 246 ? 7.103   34.688  35.312  1.00 38.00  ? 246  ARG C N   1 
ATOM   7717  C  CA  . ARG C 1 246 ? 6.223   35.287  36.307  1.00 39.12  ? 246  ARG C CA  1 
ATOM   7718  C  C   . ARG C 1 246 ? 4.743   35.177  35.884  1.00 42.00  ? 246  ARG C C   1 
ATOM   7719  O  O   . ARG C 1 246 ? 3.916   34.621  36.613  1.00 49.58  ? 246  ARG C O   1 
ATOM   7720  C  CB  . ARG C 1 246 ? 6.585   36.752  36.547  1.00 36.55  ? 246  ARG C CB  1 
ATOM   7721  C  CG  . ARG C 1 246 ? 8.027   37.008  36.893  1.00 44.93  ? 246  ARG C CG  1 
ATOM   7722  C  CD  . ARG C 1 246 ? 8.354   38.494  36.743  1.00 63.83  ? 246  ARG C CD  1 
ATOM   7723  N  NE  . ARG C 1 246 ? 8.304   39.215  38.008  1.00 74.20  ? 246  ARG C NE  1 
ATOM   7724  C  CZ  . ARG C 1 246 ? 8.368   40.539  38.120  1.00 88.04  ? 246  ARG C CZ  1 
ATOM   7725  N  NH1 . ARG C 1 246 ? 8.476   41.300  37.039  1.00 88.71  ? 246  ARG C NH1 1 
ATOM   7726  N  NH2 . ARG C 1 246 ? 8.317   41.101  39.319  1.00 97.77  ? 246  ARG C NH2 1 
ATOM   7727  N  N   . VAL C 1 247 ? 4.402   35.708  34.713  1.00 31.47  ? 247  VAL C N   1 
ATOM   7728  C  CA  . VAL C 1 247 ? 3.015   35.619  34.242  1.00 36.20  ? 247  VAL C CA  1 
ATOM   7729  C  C   . VAL C 1 247 ? 2.516   34.176  34.165  1.00 36.04  ? 247  VAL C C   1 
ATOM   7730  O  O   . VAL C 1 247 ? 1.404   33.872  34.607  1.00 40.78  ? 247  VAL C O   1 
ATOM   7731  C  CB  . VAL C 1 247 ? 2.828   36.278  32.878  1.00 38.07  ? 247  VAL C CB  1 
ATOM   7732  C  CG1 . VAL C 1 247 ? 1.497   35.870  32.287  1.00 37.17  ? 247  VAL C CG1 1 
ATOM   7733  C  CG2 . VAL C 1 247 ? 2.915   37.787  33.021  1.00 40.87  ? 247  VAL C CG2 1 
ATOM   7734  N  N   . PHE C 1 248 ? 3.343   33.290  33.612  1.00 40.83  ? 248  PHE C N   1 
ATOM   7735  C  CA  . PHE C 1 248 ? 3.003   31.868  33.538  1.00 36.46  ? 248  PHE C CA  1 
ATOM   7736  C  C   . PHE C 1 248 ? 2.784   31.224  34.898  1.00 34.73  ? 248  PHE C C   1 
ATOM   7737  O  O   . PHE C 1 248 ? 1.886   30.398  35.060  1.00 36.24  ? 248  PHE C O   1 
ATOM   7738  C  CB  . PHE C 1 248 ? 4.051   31.093  32.754  1.00 28.58  ? 248  PHE C CB  1 
ATOM   7739  C  CG  . PHE C 1 248 ? 3.758   31.036  31.297  1.00 38.87  ? 248  PHE C CG  1 
ATOM   7740  C  CD1 . PHE C 1 248 ? 2.621   30.383  30.844  1.00 41.76  ? 248  PHE C CD1 1 
ATOM   7741  C  CD2 . PHE C 1 248 ? 4.596   31.649  30.370  1.00 31.70  ? 248  PHE C CD2 1 
ATOM   7742  C  CE1 . PHE C 1 248 ? 2.323   30.321  29.486  1.00 40.74  ? 248  PHE C CE1 1 
ATOM   7743  C  CE2 . PHE C 1 248 ? 4.306   31.588  29.008  1.00 26.19  ? 248  PHE C CE2 1 
ATOM   7744  C  CZ  . PHE C 1 248 ? 3.164   30.922  28.569  1.00 23.12  ? 248  PHE C CZ  1 
ATOM   7745  N  N   . LYS C 1 249 ? 3.610   31.600  35.868  1.00 22.73  ? 249  LYS C N   1 
ATOM   7746  C  CA  . LYS C 1 249 ? 3.413   31.160  37.242  1.00 28.66  ? 249  LYS C CA  1 
ATOM   7747  C  C   . LYS C 1 249 ? 2.112   31.722  37.842  1.00 37.36  ? 249  LYS C C   1 
ATOM   7748  O  O   . LYS C 1 249 ? 1.381   31.007  38.533  1.00 39.46  ? 249  LYS C O   1 
ATOM   7749  C  CB  . LYS C 1 249 ? 4.627   31.525  38.114  1.00 31.01  ? 249  LYS C CB  1 
ATOM   7750  C  CG  . LYS C 1 249 ? 5.616   30.376  38.284  1.00 29.67  ? 249  LYS C CG  1 
ATOM   7751  C  CD  . LYS C 1 249 ? 6.994   30.833  38.757  1.00 37.46  ? 249  LYS C CD  1 
ATOM   7752  C  CE  . LYS C 1 249 ? 7.926   29.628  38.924  1.00 45.03  ? 249  LYS C CE  1 
ATOM   7753  N  NZ  . LYS C 1 249 ? 9.381   29.958  38.969  1.00 48.71  ? 249  LYS C NZ  1 
ATOM   7754  N  N   . GLN C 1 250 ? 1.818   32.994  37.576  1.00 32.73  ? 250  GLN C N   1 
ATOM   7755  C  CA  . GLN C 1 250 ? 0.554   33.567  38.027  1.00 35.84  ? 250  GLN C CA  1 
ATOM   7756  C  C   . GLN C 1 250 ? -0.643  32.815  37.434  1.00 37.93  ? 250  GLN C C   1 
ATOM   7757  O  O   . GLN C 1 250 ? -1.568  32.461  38.164  1.00 34.36  ? 250  GLN C O   1 
ATOM   7758  C  CB  . GLN C 1 250 ? 0.474   35.058  37.707  1.00 34.75  ? 250  GLN C CB  1 
ATOM   7759  C  CG  . GLN C 1 250 ? -0.820  35.705  38.173  1.00 34.82  ? 250  GLN C CG  1 
ATOM   7760  C  CD  . GLN C 1 250 ? -0.720  37.223  38.282  1.00 47.26  ? 250  GLN C CD  1 
ATOM   7761  O  OE1 . GLN C 1 250 ? 0.286   37.766  38.745  1.00 56.20  ? 250  GLN C OE1 1 
ATOM   7762  N  NE2 . GLN C 1 250 ? -1.775  37.913  37.864  1.00 48.90  ? 250  GLN C NE2 1 
ATOM   7763  N  N   . LEU C 1 251 ? -0.612  32.574  36.120  1.00 30.35  ? 251  LEU C N   1 
ATOM   7764  C  CA  . LEU C 1 251 ? -1.647  31.799  35.423  1.00 31.59  ? 251  LEU C CA  1 
ATOM   7765  C  C   . LEU C 1 251 ? -1.864  30.412  36.056  1.00 34.99  ? 251  LEU C C   1 
ATOM   7766  O  O   . LEU C 1 251 ? -2.969  30.063  36.480  1.00 43.67  ? 251  LEU C O   1 
ATOM   7767  C  CB  . LEU C 1 251 ? -1.266  31.632  33.947  1.00 41.23  ? 251  LEU C CB  1 
ATOM   7768  C  CG  . LEU C 1 251 ? -1.698  32.632  32.857  1.00 47.09  ? 251  LEU C CG  1 
ATOM   7769  C  CD1 . LEU C 1 251 ? -2.415  33.890  33.373  1.00 34.39  ? 251  LEU C CD1 1 
ATOM   7770  C  CD2 . LEU C 1 251 ? -0.569  32.973  31.877  1.00 33.87  ? 251  LEU C CD2 1 
ATOM   7771  N  N   . ALA C 1 252 ? -0.801  29.622  36.104  1.00 32.31  ? 252  ALA C N   1 
ATOM   7772  C  CA  . ALA C 1 252 ? -0.854  28.288  36.681  1.00 38.18  ? 252  ALA C CA  1 
ATOM   7773  C  C   . ALA C 1 252 ? -1.421  28.327  38.096  1.00 45.81  ? 252  ALA C C   1 
ATOM   7774  O  O   . ALA C 1 252 ? -2.209  27.457  38.485  1.00 42.98  ? 252  ALA C O   1 
ATOM   7775  C  CB  . ALA C 1 252 ? 0.548   27.667  36.685  1.00 36.98  ? 252  ALA C CB  1 
ATOM   7776  N  N   . HIS C 1 253 ? -0.998  29.325  38.872  1.00 39.10  ? 253  HIS C N   1 
ATOM   7777  C  CA  . HIS C 1 253 ? -1.485  29.467  40.241  1.00 35.32  ? 253  HIS C CA  1 
ATOM   7778  C  C   . HIS C 1 253 ? -2.951  29.854  40.271  1.00 43.65  ? 253  HIS C C   1 
ATOM   7779  O  O   . HIS C 1 253 ? -3.696  29.391  41.134  1.00 49.97  ? 253  HIS C O   1 
ATOM   7780  C  CB  . HIS C 1 253 ? -0.654  30.468  41.048  1.00 33.34  ? 253  HIS C CB  1 
ATOM   7781  C  CG  . HIS C 1 253 ? 0.487   29.837  41.784  1.00 42.03  ? 253  HIS C CG  1 
ATOM   7782  N  ND1 . HIS C 1 253 ? 1.808   30.127  41.509  1.00 36.20  ? 253  HIS C ND1 1 
ATOM   7783  C  CD2 . HIS C 1 253 ? 0.504   28.902  42.763  1.00 42.97  ? 253  HIS C CD2 1 
ATOM   7784  C  CE1 . HIS C 1 253 ? 2.588   29.412  42.298  1.00 41.53  ? 253  HIS C CE1 1 
ATOM   7785  N  NE2 . HIS C 1 253 ? 1.822   28.659  43.068  1.00 55.44  ? 253  HIS C NE2 1 
ATOM   7786  N  N   . THR C 1 254 ? -3.362  30.697  39.325  1.00 37.92  ? 254  THR C N   1 
ATOM   7787  C  CA  . THR C 1 254 ? -4.754  31.106  39.245  1.00 34.56  ? 254  THR C CA  1 
ATOM   7788  C  C   . THR C 1 254 ? -5.614  29.862  39.184  1.00 37.70  ? 254  THR C C   1 
ATOM   7789  O  O   . THR C 1 254 ? -6.624  29.767  39.892  1.00 45.79  ? 254  THR C O   1 
ATOM   7790  C  CB  . THR C 1 254 ? -5.059  31.989  38.011  1.00 36.20  ? 254  THR C CB  1 
ATOM   7791  O  OG1 . THR C 1 254 ? -4.127  33.072  37.936  1.00 40.33  ? 254  THR C OG1 1 
ATOM   7792  C  CG2 . THR C 1 254 ? -6.458  32.561  38.118  1.00 30.95  ? 254  THR C CG2 1 
ATOM   7793  N  N   . TYR C 1 255 ? -5.214  28.903  38.347  1.00 29.58  ? 255  TYR C N   1 
ATOM   7794  C  CA  . TYR C 1 255 ? -5.981  27.671  38.228  1.00 31.43  ? 255  TYR C CA  1 
ATOM   7795  C  C   . TYR C 1 255 ? -5.880  26.755  39.450  1.00 30.13  ? 255  TYR C C   1 
ATOM   7796  O  O   . TYR C 1 255 ? -6.888  26.257  39.957  1.00 37.16  ? 255  TYR C O   1 
ATOM   7797  C  CB  . TYR C 1 255 ? -5.590  26.895  36.991  1.00 17.44  ? 255  TYR C CB  1 
ATOM   7798  C  CG  . TYR C 1 255 ? -6.663  25.896  36.624  1.00 37.79  ? 255  TYR C CG  1 
ATOM   7799  C  CD1 . TYR C 1 255 ? -6.780  24.690  37.301  1.00 45.24  ? 255  TYR C CD1 1 
ATOM   7800  C  CD2 . TYR C 1 255 ? -7.579  26.170  35.616  1.00 31.46  ? 255  TYR C CD2 1 
ATOM   7801  C  CE1 . TYR C 1 255 ? -7.770  23.777  36.970  1.00 46.74  ? 255  TYR C CE1 1 
ATOM   7802  C  CE2 . TYR C 1 255 ? -8.567  25.265  35.285  1.00 37.75  ? 255  TYR C CE2 1 
ATOM   7803  C  CZ  . TYR C 1 255 ? -8.657  24.069  35.962  1.00 34.16  ? 255  TYR C CZ  1 
ATOM   7804  O  OH  . TYR C 1 255 ? -9.645  23.172  35.626  1.00 36.71  ? 255  TYR C OH  1 
ATOM   7805  N  N   . SER C 1 256 ? -4.660  26.528  39.912  1.00 32.17  ? 256  SER C N   1 
ATOM   7806  C  CA  . SER C 1 256 ? -4.447  25.619  41.022  1.00 37.12  ? 256  SER C CA  1 
ATOM   7807  C  C   . SER C 1 256 ? -5.032  26.179  42.314  1.00 46.84  ? 256  SER C C   1 
ATOM   7808  O  O   . SER C 1 256 ? -5.761  25.482  43.024  1.00 47.77  ? 256  SER C O   1 
ATOM   7809  C  CB  . SER C 1 256 ? -2.961  25.324  41.191  1.00 31.44  ? 256  SER C CB  1 
ATOM   7810  O  OG  . SER C 1 256 ? -2.759  24.312  42.160  1.00 50.03  ? 256  SER C OG  1 
ATOM   7811  N  N   . ASP C 1 257 ? -4.717  27.438  42.610  1.00 45.62  ? 257  ASP C N   1 
ATOM   7812  C  CA  . ASP C 1 257 ? -5.175  28.084  43.843  1.00 42.75  ? 257  ASP C CA  1 
ATOM   7813  C  C   . ASP C 1 257 ? -6.683  27.988  44.006  1.00 46.26  ? 257  ASP C C   1 
ATOM   7814  O  O   . ASP C 1 257 ? -7.183  27.927  45.127  1.00 55.09  ? 257  ASP C O   1 
ATOM   7815  C  CB  . ASP C 1 257 ? -4.775  29.560  43.878  1.00 40.91  ? 257  ASP C CB  1 
ATOM   7816  C  CG  . ASP C 1 257 ? -3.308  29.769  44.195  1.00 59.83  ? 257  ASP C CG  1 
ATOM   7817  O  OD1 . ASP C 1 257 ? -2.576  28.780  44.440  1.00 69.45  ? 257  ASP C OD1 1 
ATOM   7818  O  OD2 . ASP C 1 257 ? -2.890  30.946  44.207  1.00 68.97  ? 257  ASP C OD2 1 
ATOM   7819  N  N   . ASN C 1 258 ? -7.398  27.993  42.883  1.00 40.04  ? 258  ASN C N   1 
ATOM   7820  C  CA  . ASN C 1 258 ? -8.854  27.881  42.885  1.00 37.72  ? 258  ASN C CA  1 
ATOM   7821  C  C   . ASN C 1 258 ? -9.385  26.461  42.726  1.00 34.54  ? 258  ASN C C   1 
ATOM   7822  O  O   . ASN C 1 258 ? -10.573 26.269  42.505  1.00 39.46  ? 258  ASN C O   1 
ATOM   7823  C  CB  . ASN C 1 258 ? -9.444  28.766  41.790  1.00 37.02  ? 258  ASN C CB  1 
ATOM   7824  C  CG  . ASN C 1 258 ? -9.471  30.230  42.182  1.00 51.43  ? 258  ASN C CG  1 
ATOM   7825  O  OD1 . ASN C 1 258 ? -10.305 30.659  42.998  1.00 52.29  ? 258  ASN C OD1 1 
ATOM   7826  N  ND2 . ASN C 1 258 ? -8.553  31.007  41.616  1.00 44.48  ? 258  ASN C ND2 1 
ATOM   7827  N  N   . HIS C 1 259 ? -8.508  25.472  42.831  1.00 44.81  ? 259  HIS C N   1 
ATOM   7828  C  CA  . HIS C 1 259 ? -8.892  24.080  42.644  1.00 48.03  ? 259  HIS C CA  1 
ATOM   7829  C  C   . HIS C 1 259 ? -8.548  23.318  43.908  1.00 49.62  ? 259  HIS C C   1 
ATOM   7830  O  O   . HIS C 1 259 ? -7.388  22.986  44.145  1.00 54.36  ? 259  HIS C O   1 
ATOM   7831  C  CB  . HIS C 1 259 ? -8.148  23.490  41.443  1.00 59.23  ? 259  HIS C CB  1 
ATOM   7832  C  CG  . HIS C 1 259 ? -8.582  22.103  41.076  1.00 55.18  ? 259  HIS C CG  1 
ATOM   7833  N  ND1 . HIS C 1 259 ? -8.443  21.029  41.927  1.00 53.10  ? 259  HIS C ND1 1 
ATOM   7834  C  CD2 . HIS C 1 259 ? -9.131  21.618  39.937  1.00 43.19  ? 259  HIS C CD2 1 
ATOM   7835  C  CE1 . HIS C 1 259 ? -8.901  19.940  41.331  1.00 45.50  ? 259  HIS C CE1 1 
ATOM   7836  N  NE2 . HIS C 1 259 ? -9.324  20.270  40.126  1.00 36.85  ? 259  HIS C NE2 1 
ATOM   7837  N  N   . PRO C 1 260 ? -9.568  23.022  44.714  1.00 58.30  ? 260  PRO C N   1 
ATOM   7838  C  CA  . PRO C 1 260 ? -9.469  22.496  46.083  1.00 60.82  ? 260  PRO C CA  1 
ATOM   7839  C  C   . PRO C 1 260 ? -8.480  21.346  46.246  1.00 56.29  ? 260  PRO C C   1 
ATOM   7840  O  O   . PRO C 1 260 ? -7.971  21.145  47.366  1.00 53.21  ? 260  PRO C O   1 
ATOM   7841  C  CB  . PRO C 1 260 ? -10.888 21.993  46.366  1.00 59.70  ? 260  PRO C CB  1 
ATOM   7842  C  CG  . PRO C 1 260 ? -11.759 22.792  45.453  1.00 62.79  ? 260  PRO C CG  1 
ATOM   7843  C  CD  . PRO C 1 260 ? -10.952 23.014  44.213  1.00 54.37  ? 260  PRO C CD  1 
ATOM   7844  N  N   . ILE C 1 261 ? -8.227  20.609  45.161  1.00 49.64  ? 261  ILE C N   1 
ATOM   7845  C  CA  . ILE C 1 261 ? -7.395  19.414  45.228  1.00 55.15  ? 261  ILE C CA  1 
ATOM   7846  C  C   . ILE C 1 261 ? -6.047  19.663  44.592  1.00 46.00  ? 261  ILE C C   1 
ATOM   7847  O  O   . ILE C 1 261 ? -5.008  19.269  45.117  1.00 46.98  ? 261  ILE C O   1 
ATOM   7848  C  CB  . ILE C 1 261 ? -8.063  18.220  44.535  1.00 54.85  ? 261  ILE C CB  1 
ATOM   7849  C  CG1 . ILE C 1 261 ? -9.280  17.760  45.342  1.00 53.10  ? 261  ILE C CG1 1 
ATOM   7850  C  CG2 . ILE C 1 261 ? -7.065  17.080  44.379  1.00 49.79  ? 261  ILE C CG2 1 
ATOM   7851  C  CD1 . ILE C 1 261 ? -10.113 16.726  44.632  1.00 63.90  ? 261  ILE C CD1 1 
ATOM   7852  N  N   . MET C 1 262 ? -6.064  20.332  43.454  1.00 37.83  ? 262  MET C N   1 
ATOM   7853  C  CA  . MET C 1 262 ? -4.821  20.644  42.768  1.00 48.65  ? 262  MET C CA  1 
ATOM   7854  C  C   . MET C 1 262 ? -3.905  21.496  43.650  1.00 48.87  ? 262  MET C C   1 
ATOM   7855  O  O   . MET C 1 262 ? -2.682  21.342  43.627  1.00 54.45  ? 262  MET C O   1 
ATOM   7856  C  CB  . MET C 1 262 ? -5.120  21.353  41.449  1.00 32.34  ? 262  MET C CB  1 
ATOM   7857  C  CG  . MET C 1 262 ? -3.909  21.668  40.603  1.00 18.25  ? 262  MET C CG  1 
ATOM   7858  S  SD  . MET C 1 262 ? -4.426  22.429  39.042  1.00 37.65  ? 262  MET C SD  1 
ATOM   7859  C  CE  . MET C 1 262 ? -5.350  21.079  38.289  1.00 22.35  ? 262  MET C CE  1 
ATOM   7860  N  N   . ARG C 1 263 ? -4.518  22.383  44.423  1.00 49.10  ? 263  ARG C N   1 
ATOM   7861  C  CA  . ARG C 1 263 ? -3.827  23.322  45.306  1.00 46.47  ? 263  ARG C CA  1 
ATOM   7862  C  C   . ARG C 1 263 ? -2.928  22.628  46.327  1.00 49.96  ? 263  ARG C C   1 
ATOM   7863  O  O   . ARG C 1 263 ? -2.050  23.255  46.923  1.00 58.01  ? 263  ARG C O   1 
ATOM   7864  C  CB  . ARG C 1 263 ? -4.881  24.163  46.032  1.00 59.08  ? 263  ARG C CB  1 
ATOM   7865  C  CG  . ARG C 1 263 ? -4.371  25.258  46.953  1.00 71.12  ? 263  ARG C CG  1 
ATOM   7866  C  CD  . ARG C 1 263 ? -5.552  26.070  47.506  1.00 78.29  ? 263  ARG C CD  1 
ATOM   7867  N  NE  . ARG C 1 263 ? -6.527  25.231  48.204  1.00 76.97  ? 263  ARG C NE  1 
ATOM   7868  C  CZ  . ARG C 1 263 ? -7.843  25.390  48.128  1.00 67.41  ? 263  ARG C CZ  1 
ATOM   7869  N  NH1 . ARG C 1 263 ? -8.352  26.356  47.381  1.00 60.22  ? 263  ARG C NH1 1 
ATOM   7870  N  NH2 . ARG C 1 263 ? -8.652  24.582  48.796  1.00 66.62  ? 263  ARG C NH2 1 
ATOM   7871  N  N   . LYS C 1 264 ? -3.145  21.332  46.530  1.00 60.26  ? 264  LYS C N   1 
ATOM   7872  C  CA  . LYS C 1 264 ? -2.414  20.584  47.561  1.00 69.36  ? 264  LYS C CA  1 
ATOM   7873  C  C   . LYS C 1 264 ? -1.007  20.175  47.131  1.00 61.94  ? 264  LYS C C   1 
ATOM   7874  O  O   . LYS C 1 264 ? -0.042  20.382  47.864  1.00 61.21  ? 264  LYS C O   1 
ATOM   7875  C  CB  . LYS C 1 264 ? -3.219  19.361  48.019  1.00 67.46  ? 264  LYS C CB  1 
ATOM   7876  C  CG  . LYS C 1 264 ? -4.621  19.720  48.514  1.00 68.40  ? 264  LYS C CG  1 
ATOM   7877  C  CD  . LYS C 1 264 ? -5.383  18.511  49.042  1.00 74.21  ? 264  LYS C CD  1 
ATOM   7878  C  CE  . LYS C 1 264 ? -6.636  18.953  49.786  1.00 83.60  ? 264  LYS C CE  1 
ATOM   7879  N  NZ  . LYS C 1 264 ? -6.321  19.863  50.939  1.00 95.56  ? 264  LYS C NZ  1 
ATOM   7880  N  N   . GLY C 1 265 ? -0.897  19.582  45.949  1.00 59.11  ? 265  GLY C N   1 
ATOM   7881  C  CA  . GLY C 1 265 ? 0.397   19.274  45.366  1.00 46.87  ? 265  GLY C CA  1 
ATOM   7882  C  C   . GLY C 1 265 ? 0.867   17.841  45.527  1.00 50.09  ? 265  GLY C C   1 
ATOM   7883  O  O   . GLY C 1 265 ? 1.944   17.486  45.041  1.00 54.50  ? 265  GLY C O   1 
ATOM   7884  N  N   . ASN C 1 266 ? 0.063   17.016  46.195  1.00 42.57  ? 266  ASN C N   1 
ATOM   7885  C  CA  . ASN C 1 266 ? 0.452   15.643  46.493  1.00 54.04  ? 266  ASN C CA  1 
ATOM   7886  C  C   . ASN C 1 266 ? -0.507  14.581  45.937  1.00 57.51  ? 266  ASN C C   1 
ATOM   7887  O  O   . ASN C 1 266 ? -0.756  13.545  46.572  1.00 55.21  ? 266  ASN C O   1 
ATOM   7888  C  CB  . ASN C 1 266 ? 0.607   15.473  47.999  1.00 58.10  ? 266  ASN C CB  1 
ATOM   7889  C  CG  . ASN C 1 266 ? -0.586  16.007  48.764  1.00 77.28  ? 266  ASN C CG  1 
ATOM   7890  O  OD1 . ASN C 1 266 ? -1.557  16.482  48.165  1.00 80.67  ? 266  ASN C OD1 1 
ATOM   7891  N  ND2 . ASN C 1 266 ? -0.521  15.940  50.095  1.00 75.02  ? 266  ASN C ND2 1 
ATOM   7892  N  N   . ASN C 1 267 ? -1.022  14.842  44.740  1.00 50.60  ? 267  ASN C N   1 
ATOM   7893  C  CA  . ASN C 1 267 ? -1.991  13.961  44.090  1.00 48.65  ? 267  ASN C CA  1 
ATOM   7894  C  C   . ASN C 1 267 ? -1.321  12.936  43.176  1.00 45.73  ? 267  ASN C C   1 
ATOM   7895  O  O   . ASN C 1 267 ? -0.188  13.136  42.747  1.00 40.88  ? 267  ASN C O   1 
ATOM   7896  C  CB  . ASN C 1 267 ? -2.995  14.793  43.288  1.00 51.15  ? 267  ASN C CB  1 
ATOM   7897  C  CG  . ASN C 1 267 ? -3.402  16.071  44.009  1.00 54.47  ? 267  ASN C CG  1 
ATOM   7898  O  OD1 . ASN C 1 267 ? -3.912  16.031  45.130  1.00 43.12  ? 267  ASN C OD1 1 
ATOM   7899  N  ND2 . ASN C 1 267 ? -3.163  17.215  43.368  1.00 53.11  ? 267  ASN C ND2 1 
ATOM   7900  N  N   . CYS C 1 268 ? -2.037  11.849  42.891  1.00 52.04  ? 268  CYS C N   1 
ATOM   7901  C  CA  . CYS C 1 268 ? -1.558  10.740  42.052  1.00 55.63  ? 268  CYS C CA  1 
ATOM   7902  C  C   . CYS C 1 268 ? -0.086  10.359  42.252  1.00 61.21  ? 268  CYS C C   1 
ATOM   7903  O  O   . CYS C 1 268 ? 0.624   10.080  41.287  1.00 63.07  ? 268  CYS C O   1 
ATOM   7904  C  CB  . CYS C 1 268 ? -1.843  10.990  40.557  1.00 43.53  ? 268  CYS C CB  1 
ATOM   7905  S  SG  . CYS C 1 268 ? -2.809  12.482  40.179  1.00 67.50  ? 268  CYS C SG  1 
ATOM   7906  N  N   . ASN C 1 269 ? 0.367   10.332  43.500  1.00 69.45  ? 269  ASN C N   1 
ATOM   7907  C  CA  . ASN C 1 269 ? 1.762   9.987   43.794  1.00 75.21  ? 269  ASN C CA  1 
ATOM   7908  C  C   . ASN C 1 269 ? 2.757   11.050  43.312  1.00 72.86  ? 269  ASN C C   1 
ATOM   7909  O  O   . ASN C 1 269 ? 3.977   10.847  43.363  1.00 69.92  ? 269  ASN C O   1 
ATOM   7910  C  CB  . ASN C 1 269 ? 2.125   8.618   43.201  1.00 74.18  ? 269  ASN C CB  1 
ATOM   7911  C  CG  . ASN C 1 269 ? 1.442   7.465   43.921  1.00 83.95  ? 269  ASN C CG  1 
ATOM   7912  O  OD1 . ASN C 1 269 ? 1.273   6.383   43.354  1.00 87.74  ? 269  ASN C OD1 1 
ATOM   7913  N  ND2 . ASN C 1 269 ? 1.047   7.689   45.177  1.00 85.56  ? 269  ASN C ND2 1 
ATOM   7914  N  N   . ASP C 1 270 ? 2.228   12.181  42.847  1.00 68.96  ? 270  ASP C N   1 
ATOM   7915  C  CA  . ASP C 1 270 ? 3.054   13.295  42.388  1.00 59.19  ? 270  ASP C CA  1 
ATOM   7916  C  C   . ASP C 1 270 ? 3.244   14.328  43.480  1.00 67.19  ? 270  ASP C C   1 
ATOM   7917  O  O   . ASP C 1 270 ? 2.373   14.516  44.338  1.00 61.05  ? 270  ASP C O   1 
ATOM   7918  C  CB  . ASP C 1 270 ? 2.414   13.984  41.184  1.00 55.73  ? 270  ASP C CB  1 
ATOM   7919  C  CG  . ASP C 1 270 ? 2.216   13.049  40.014  1.00 57.52  ? 270  ASP C CG  1 
ATOM   7920  O  OD1 . ASP C 1 270 ? 2.977   12.067  39.918  1.00 69.66  ? 270  ASP C OD1 1 
ATOM   7921  O  OD2 . ASP C 1 270 ? 1.304   13.292  39.191  1.00 58.97  ? 270  ASP C OD2 1 
ATOM   7922  N  N   . SER C 1 271 ? 4.387   15.005  43.425  1.00 71.29  ? 271  SER C N   1 
ATOM   7923  C  CA  . SER C 1 271 ? 4.674   16.109  44.332  1.00 65.75  ? 271  SER C CA  1 
ATOM   7924  C  C   . SER C 1 271 ? 4.944   17.394  43.536  1.00 61.84  ? 271  SER C C   1 
ATOM   7925  O  O   . SER C 1 271 ? 5.997   17.553  42.918  1.00 68.41  ? 271  SER C O   1 
ATOM   7926  C  CB  . SER C 1 271 ? 5.848   15.757  45.248  1.00 50.48  ? 271  SER C CB  1 
ATOM   7927  O  OG  . SER C 1 271 ? 6.198   16.845  46.078  1.00 49.91  ? 271  SER C OG  1 
ATOM   7928  N  N   . PHE C 1 272 ? 3.970   18.296  43.546  1.00 52.42  ? 272  PHE C N   1 
ATOM   7929  C  CA  . PHE C 1 272 ? 4.072   19.558  42.828  1.00 41.87  ? 272  PHE C CA  1 
ATOM   7930  C  C   . PHE C 1 272 ? 3.764   20.699  43.766  1.00 40.22  ? 272  PHE C C   1 
ATOM   7931  O  O   . PHE C 1 272 ? 2.622   20.863  44.195  1.00 43.44  ? 272  PHE C O   1 
ATOM   7932  C  CB  . PHE C 1 272 ? 3.088   19.589  41.660  1.00 38.24  ? 272  PHE C CB  1 
ATOM   7933  C  CG  . PHE C 1 272 ? 3.428   18.622  40.572  1.00 49.63  ? 272  PHE C CG  1 
ATOM   7934  C  CD1 . PHE C 1 272 ? 2.553   17.604  40.226  1.00 50.64  ? 272  PHE C CD1 1 
ATOM   7935  C  CD2 . PHE C 1 272 ? 4.638   18.715  39.911  1.00 34.92  ? 272  PHE C CD2 1 
ATOM   7936  C  CE1 . PHE C 1 272 ? 2.872   16.711  39.223  1.00 39.06  ? 272  PHE C CE1 1 
ATOM   7937  C  CE2 . PHE C 1 272 ? 4.960   17.826  38.913  1.00 37.19  ? 272  PHE C CE2 1 
ATOM   7938  C  CZ  . PHE C 1 272 ? 4.079   16.821  38.568  1.00 38.16  ? 272  PHE C CZ  1 
ATOM   7939  N  N   . SER C 1 273 ? 4.784   21.485  44.084  1.00 50.73  ? 273  SER C N   1 
ATOM   7940  C  CA  . SER C 1 273 ? 4.635   22.594  45.019  1.00 56.83  ? 273  SER C CA  1 
ATOM   7941  C  C   . SER C 1 273 ? 3.639   23.612  44.504  1.00 58.60  ? 273  SER C C   1 
ATOM   7942  O  O   . SER C 1 273 ? 3.798   24.131  43.403  1.00 53.79  ? 273  SER C O   1 
ATOM   7943  C  CB  . SER C 1 273 ? 5.972   23.283  45.257  1.00 62.54  ? 273  SER C CB  1 
ATOM   7944  O  OG  . SER C 1 273 ? 5.797   24.415  46.091  1.00 68.10  ? 273  SER C OG  1 
ATOM   7945  N  N   . GLY C 1 274 ? 2.616   23.895  45.309  1.00 54.25  ? 274  GLY C N   1 
ATOM   7946  C  CA  . GLY C 1 274 ? 1.544   24.791  44.910  1.00 44.53  ? 274  GLY C CA  1 
ATOM   7947  C  C   . GLY C 1 274 ? 0.634   24.198  43.846  1.00 49.69  ? 274  GLY C C   1 
ATOM   7948  O  O   . GLY C 1 274 ? -0.251  24.885  43.330  1.00 50.35  ? 274  GLY C O   1 
ATOM   7949  N  N   . GLY C 1 275 ? 0.863   22.927  43.515  1.00 38.35  ? 275  GLY C N   1 
ATOM   7950  C  CA  . GLY C 1 275 ? 0.063   22.213  42.543  1.00 26.86  ? 275  GLY C CA  1 
ATOM   7951  C  C   . GLY C 1 275 ? 0.387   22.638  41.122  1.00 47.02  ? 275  GLY C C   1 
ATOM   7952  O  O   . GLY C 1 275 ? -0.362  22.371  40.174  1.00 46.96  ? 275  GLY C O   1 
ATOM   7953  N  N   . ILE C 1 276 ? 1.513   23.313  40.961  1.00 53.09  ? 276  ILE C N   1 
ATOM   7954  C  CA  . ILE C 1 276 ? 1.925   23.739  39.634  1.00 53.97  ? 276  ILE C CA  1 
ATOM   7955  C  C   . ILE C 1 276 ? 3.327   23.236  39.353  1.00 42.93  ? 276  ILE C C   1 
ATOM   7956  O  O   . ILE C 1 276 ? 4.055   22.856  40.264  1.00 50.63  ? 276  ILE C O   1 
ATOM   7957  C  CB  . ILE C 1 276 ? 1.897   25.265  39.493  1.00 49.62  ? 276  ILE C CB  1 
ATOM   7958  C  CG1 . ILE C 1 276 ? 3.032   25.887  40.306  1.00 43.52  ? 276  ILE C CG1 1 
ATOM   7959  C  CG2 . ILE C 1 276 ? 0.543   25.815  39.931  1.00 42.52  ? 276  ILE C CG2 1 
ATOM   7960  C  CD1 . ILE C 1 276 ? 3.218   27.350  40.027  1.00 43.76  ? 276  ILE C CD1 1 
ATOM   7961  N  N   . THR C 1 277 ? 3.700   23.221  38.085  1.00 38.47  ? 277  THR C N   1 
ATOM   7962  C  CA  . THR C 1 277 ? 5.020   22.768  37.723  1.00 41.10  ? 277  THR C CA  1 
ATOM   7963  C  C   . THR C 1 277 ? 5.396   23.299  36.352  1.00 45.99  ? 277  THR C C   1 
ATOM   7964  O  O   . THR C 1 277 ? 4.534   23.697  35.568  1.00 46.88  ? 277  THR C O   1 
ATOM   7965  C  CB  . THR C 1 277 ? 5.103   21.231  37.718  1.00 38.89  ? 277  THR C CB  1 
ATOM   7966  O  OG1 . THR C 1 277 ? 6.467   20.833  37.552  1.00 44.57  ? 277  THR C OG1 1 
ATOM   7967  C  CG2 . THR C 1 277 ? 4.271   20.636  36.585  1.00 24.14  ? 277  THR C CG2 1 
ATOM   7968  N  N   . ASN C 1 278 ? 6.698   23.322  36.093  1.00 47.17  ? 278  ASN C N   1 
ATOM   7969  C  CA  . ASN C 1 278 ? 7.244   23.593  34.768  1.00 41.09  ? 278  ASN C CA  1 
ATOM   7970  C  C   . ASN C 1 278 ? 7.262   22.289  33.961  1.00 50.97  ? 278  ASN C C   1 
ATOM   7971  O  O   . ASN C 1 278 ? 7.650   21.233  34.485  1.00 63.58  ? 278  ASN C O   1 
ATOM   7972  C  CB  . ASN C 1 278 ? 8.660   24.192  34.893  1.00 39.60  ? 278  ASN C CB  1 
ATOM   7973  C  CG  . ASN C 1 278 ? 9.364   24.355  33.548  1.00 48.75  ? 278  ASN C CG  1 
ATOM   7974  O  OD1 . ASN C 1 278 ? 10.462  23.821  33.348  1.00 49.69  ? 278  ASN C OD1 1 
ATOM   7975  N  ND2 . ASN C 1 278 ? 8.740   25.104  32.625  1.00 32.96  ? 278  ASN C ND2 1 
ATOM   7976  N  N   . GLY C 1 279 ? 6.815   22.351  32.706  1.00 29.72  ? 279  GLY C N   1 
ATOM   7977  C  CA  . GLY C 1 279 ? 6.765   21.161  31.881  1.00 25.84  ? 279  GLY C CA  1 
ATOM   7978  C  C   . GLY C 1 279 ? 8.067   20.383  31.986  1.00 45.35  ? 279  GLY C C   1 
ATOM   7979  O  O   . GLY C 1 279 ? 8.086   19.235  32.462  1.00 42.55  ? 279  GLY C O   1 
ATOM   7980  N  N   . ALA C 1 280 ? 9.159   21.027  31.571  1.00 38.56  ? 280  ALA C N   1 
ATOM   7981  C  CA  . ALA C 1 280 ? 10.454  20.370  31.473  1.00 35.16  ? 280  ALA C CA  1 
ATOM   7982  C  C   . ALA C 1 280 ? 10.870  19.800  32.816  1.00 37.46  ? 280  ALA C C   1 
ATOM   7983  O  O   . ALA C 1 280 ? 11.435  18.703  32.890  1.00 46.23  ? 280  ALA C O   1 
ATOM   7984  C  CB  . ALA C 1 280 ? 11.498  21.338  30.956  1.00 29.99  ? 280  ALA C CB  1 
ATOM   7985  N  N   . HIS C 1 281 ? 10.589  20.548  33.877  1.00 36.25  ? 281  HIS C N   1 
ATOM   7986  C  CA  . HIS C 1 281 ? 10.983  20.124  35.213  1.00 37.68  ? 281  HIS C CA  1 
ATOM   7987  C  C   . HIS C 1 281 ? 10.288  18.828  35.623  1.00 33.61  ? 281  HIS C C   1 
ATOM   7988  O  O   . HIS C 1 281 ? 10.878  17.972  36.268  1.00 40.90  ? 281  HIS C O   1 
ATOM   7989  C  CB  . HIS C 1 281 ? 10.731  21.214  36.252  1.00 33.51  ? 281  HIS C CB  1 
ATOM   7990  C  CG  . HIS C 1 281 ? 11.378  20.929  37.569  1.00 47.31  ? 281  HIS C CG  1 
ATOM   7991  N  ND1 . HIS C 1 281 ? 10.713  20.310  38.606  1.00 48.24  ? 281  HIS C ND1 1 
ATOM   7992  C  CD2 . HIS C 1 281 ? 12.644  21.132  38.002  1.00 52.39  ? 281  HIS C CD2 1 
ATOM   7993  C  CE1 . HIS C 1 281 ? 11.535  20.162  39.629  1.00 45.62  ? 281  HIS C CE1 1 
ATOM   7994  N  NE2 . HIS C 1 281 ? 12.713  20.654  39.289  1.00 62.34  ? 281  HIS C NE2 1 
ATOM   7995  N  N   . TRP C 1 282 ? 9.023   18.695  35.260  1.00 40.32  ? 282  TRP C N   1 
ATOM   7996  C  CA  . TRP C 1 282 ? 8.338   17.426  35.413  1.00 44.48  ? 282  TRP C CA  1 
ATOM   7997  C  C   . TRP C 1 282 ? 9.090   16.390  34.573  1.00 42.76  ? 282  TRP C C   1 
ATOM   7998  O  O   . TRP C 1 282 ? 9.751   15.485  35.092  1.00 33.73  ? 282  TRP C O   1 
ATOM   7999  C  CB  . TRP C 1 282 ? 6.908   17.567  34.908  1.00 43.10  ? 282  TRP C CB  1 
ATOM   8000  C  CG  . TRP C 1 282 ? 6.068   16.352  35.127  1.00 50.92  ? 282  TRP C CG  1 
ATOM   8001  C  CD1 . TRP C 1 282 ? 6.461   15.173  35.690  1.00 48.39  ? 282  TRP C CD1 1 
ATOM   8002  C  CD2 . TRP C 1 282 ? 4.684   16.196  34.795  1.00 49.59  ? 282  TRP C CD2 1 
ATOM   8003  N  NE1 . TRP C 1 282 ? 5.407   14.288  35.723  1.00 43.45  ? 282  TRP C NE1 1 
ATOM   8004  C  CE2 . TRP C 1 282 ? 4.305   14.894  35.185  1.00 41.58  ? 282  TRP C CE2 1 
ATOM   8005  C  CE3 . TRP C 1 282 ? 3.727   17.033  34.211  1.00 45.11  ? 282  TRP C CE3 1 
ATOM   8006  C  CZ2 . TRP C 1 282 ? 3.015   14.407  35.004  1.00 36.80  ? 282  TRP C CZ2 1 
ATOM   8007  C  CZ3 . TRP C 1 282 ? 2.438   16.545  34.033  1.00 43.24  ? 282  TRP C CZ3 1 
ATOM   8008  C  CH2 . TRP C 1 282 ? 2.095   15.244  34.430  1.00 30.65  ? 282  TRP C CH2 1 
ATOM   8009  N  N   . TYR C 1 283 ? 8.961   16.532  33.262  1.00 43.44  ? 283  TYR C N   1 
ATOM   8010  C  CA  . TYR C 1 283 ? 9.813   15.822  32.329  1.00 47.51  ? 283  TYR C CA  1 
ATOM   8011  C  C   . TYR C 1 283 ? 9.702   16.535  31.005  1.00 44.21  ? 283  TYR C C   1 
ATOM   8012  O  O   . TYR C 1 283 ? 8.660   17.104  30.698  1.00 38.62  ? 283  TYR C O   1 
ATOM   8013  C  CB  . TYR C 1 283 ? 9.410   14.358  32.193  1.00 36.19  ? 283  TYR C CB  1 
ATOM   8014  C  CG  . TYR C 1 283 ? 7.967   14.131  31.813  1.00 39.84  ? 283  TYR C CG  1 
ATOM   8015  C  CD1 . TYR C 1 283 ? 7.565   14.147  30.489  1.00 43.14  ? 283  TYR C CD1 1 
ATOM   8016  C  CD2 . TYR C 1 283 ? 7.014   13.861  32.786  1.00 50.55  ? 283  TYR C CD2 1 
ATOM   8017  C  CE1 . TYR C 1 283 ? 6.244   13.922  30.139  1.00 41.35  ? 283  TYR C CE1 1 
ATOM   8018  C  CE2 . TYR C 1 283 ? 5.698   13.631  32.451  1.00 52.08  ? 283  TYR C CE2 1 
ATOM   8019  C  CZ  . TYR C 1 283 ? 5.319   13.664  31.121  1.00 53.24  ? 283  TYR C CZ  1 
ATOM   8020  O  OH  . TYR C 1 283 ? 4.007   13.440  30.785  1.00 59.85  ? 283  TYR C OH  1 
ATOM   8021  N  N   . GLU C 1 284 ? 10.787  16.521  30.239  1.00 51.27  ? 284  GLU C N   1 
ATOM   8022  C  CA  . GLU C 1 284 ? 10.818  17.157  28.920  1.00 50.28  ? 284  GLU C CA  1 
ATOM   8023  C  C   . GLU C 1 284 ? 10.103  16.366  27.826  1.00 41.78  ? 284  GLU C C   1 
ATOM   8024  O  O   . GLU C 1 284 ? 10.093  15.129  27.813  1.00 46.92  ? 284  GLU C O   1 
ATOM   8025  C  CB  . GLU C 1 284 ? 12.261  17.465  28.481  1.00 48.97  ? 284  GLU C CB  1 
ATOM   8026  C  CG  . GLU C 1 284 ? 12.966  18.503  29.355  1.00 55.71  ? 284  GLU C CG  1 
ATOM   8027  C  CD  . GLU C 1 284 ? 14.235  19.047  28.722  1.00 50.41  ? 284  GLU C CD  1 
ATOM   8028  O  OE1 . GLU C 1 284 ? 14.999  19.741  29.433  1.00 40.53  ? 284  GLU C OE1 1 
ATOM   8029  O  OE2 . GLU C 1 284 ? 14.462  18.779  27.520  1.00 52.28  ? 284  GLU C OE2 1 
ATOM   8030  N  N   . LEU C 1 285 ? 9.499   17.105  26.908  1.00 30.00  ? 285  LEU C N   1 
ATOM   8031  C  CA  . LEU C 1 285 ? 8.876   16.508  25.746  1.00 39.21  ? 285  LEU C CA  1 
ATOM   8032  C  C   . LEU C 1 285 ? 8.993   17.538  24.633  1.00 39.44  ? 285  LEU C C   1 
ATOM   8033  O  O   . LEU C 1 285 ? 9.128   18.731  24.908  1.00 33.04  ? 285  LEU C O   1 
ATOM   8034  C  CB  . LEU C 1 285 ? 7.411   16.148  26.050  1.00 37.19  ? 285  LEU C CB  1 
ATOM   8035  C  CG  . LEU C 1 285 ? 6.424   17.287  26.327  1.00 34.26  ? 285  LEU C CG  1 
ATOM   8036  C  CD1 . LEU C 1 285 ? 5.665   17.652  25.057  1.00 32.37  ? 285  LEU C CD1 1 
ATOM   8037  C  CD2 . LEU C 1 285 ? 5.433   16.929  27.414  1.00 31.12  ? 285  LEU C CD2 1 
ATOM   8038  N  N   . SER C 1 286 ? 8.965   17.085  23.383  1.00 40.57  ? 286  SER C N   1 
ATOM   8039  C  CA  . SER C 1 286 ? 9.143   17.990  22.252  1.00 40.10  ? 286  SER C CA  1 
ATOM   8040  C  C   . SER C 1 286 ? 8.050   17.815  21.227  1.00 36.61  ? 286  SER C C   1 
ATOM   8041  O  O   . SER C 1 286 ? 7.538   16.706  21.047  1.00 44.97  ? 286  SER C O   1 
ATOM   8042  C  CB  . SER C 1 286 ? 10.508  17.784  21.596  1.00 47.94  ? 286  SER C CB  1 
ATOM   8043  O  OG  . SER C 1 286 ? 11.551  17.886  22.553  1.00 52.92  ? 286  SER C OG  1 
ATOM   8044  N  N   . GLY C 1 287 ? 7.701   18.921  20.564  1.00 33.45  ? 287  GLY C N   1 
ATOM   8045  C  CA  . GLY C 1 287 ? 6.609   18.962  19.596  1.00 26.61  ? 287  GLY C CA  1 
ATOM   8046  C  C   . GLY C 1 287 ? 5.222   19.181  20.190  1.00 25.32  ? 287  GLY C C   1 
ATOM   8047  O  O   . GLY C 1 287 ? 4.202   18.955  19.531  1.00 25.70  ? 287  GLY C O   1 
ATOM   8048  N  N   . GLY C 1 288 ? 5.187   19.631  21.443  1.00 35.64  ? 288  GLY C N   1 
ATOM   8049  C  CA  . GLY C 1 288 ? 3.941   19.908  22.145  1.00 38.12  ? 288  GLY C CA  1 
ATOM   8050  C  C   . GLY C 1 288 ? 3.183   21.121  21.629  1.00 37.26  ? 288  GLY C C   1 
ATOM   8051  O  O   . GLY C 1 288 ? 3.738   21.990  20.938  1.00 25.42  ? 288  GLY C O   1 
ATOM   8052  N  N   . MET C 1 289 ? 1.899   21.179  21.959  1.00 35.65  ? 289  MET C N   1 
ATOM   8053  C  CA  . MET C 1 289 ? 1.072   22.259  21.464  1.00 35.28  ? 289  MET C CA  1 
ATOM   8054  C  C   . MET C 1 289 ? 1.351   23.476  22.318  1.00 28.69  ? 289  MET C C   1 
ATOM   8055  O  O   . MET C 1 289 ? 1.417   24.599  21.827  1.00 30.67  ? 289  MET C O   1 
ATOM   8056  C  CB  . MET C 1 289 ? -0.415  21.880  21.506  1.00 24.69  ? 289  MET C CB  1 
ATOM   8057  C  CG  . MET C 1 289 ? -1.352  22.893  20.816  1.00 26.69  ? 289  MET C CG  1 
ATOM   8058  S  SD  . MET C 1 289 ? -3.062  22.280  20.635  1.00 50.90  ? 289  MET C SD  1 
ATOM   8059  C  CE  . MET C 1 289 ? -3.463  21.962  22.359  1.00 30.48  ? 289  MET C CE  1 
ATOM   8060  N  N   . GLN C 1 290 ? 1.524   23.239  23.609  1.00 25.39  ? 290  GLN C N   1 
ATOM   8061  C  CA  . GLN C 1 290 ? 1.681   24.327  24.555  1.00 22.92  ? 290  GLN C CA  1 
ATOM   8062  C  C   . GLN C 1 290 ? 2.745   25.295  24.061  1.00 29.22  ? 290  GLN C C   1 
ATOM   8063  O  O   . GLN C 1 290 ? 2.450   26.442  23.717  1.00 30.76  ? 290  GLN C O   1 
ATOM   8064  C  CB  . GLN C 1 290 ? 2.094   23.775  25.914  1.00 35.30  ? 290  GLN C CB  1 
ATOM   8065  C  CG  . GLN C 1 290 ? 2.378   24.860  26.944  1.00 36.05  ? 290  GLN C CG  1 
ATOM   8066  C  CD  . GLN C 1 290 ? 3.008   24.313  28.207  1.00 36.44  ? 290  GLN C CD  1 
ATOM   8067  O  OE1 . GLN C 1 290 ? 2.307   23.991  29.168  1.00 44.48  ? 290  GLN C OE1 1 
ATOM   8068  N  NE2 . GLN C 1 290 ? 4.338   24.199  28.211  1.00 16.75  ? 290  GLN C NE2 1 
ATOM   8069  N  N   . ASP C 1 291 ? 3.985   24.814  24.024  1.00 28.99  ? 291  ASP C N   1 
ATOM   8070  C  CA  . ASP C 1 291 ? 5.129   25.640  23.663  1.00 21.07  ? 291  ASP C CA  1 
ATOM   8071  C  C   . ASP C 1 291 ? 4.985   26.218  22.240  1.00 34.48  ? 291  ASP C C   1 
ATOM   8072  O  O   . ASP C 1 291 ? 5.478   27.307  21.936  1.00 30.12  ? 291  ASP C O   1 
ATOM   8073  C  CB  . ASP C 1 291 ? 6.426   24.825  23.817  1.00 32.54  ? 291  ASP C CB  1 
ATOM   8074  C  CG  . ASP C 1 291 ? 6.829   24.608  25.277  1.00 51.27  ? 291  ASP C CG  1 
ATOM   8075  O  OD1 . ASP C 1 291 ? 6.035   24.934  26.182  1.00 56.86  ? 291  ASP C OD1 1 
ATOM   8076  O  OD2 . ASP C 1 291 ? 7.953   24.120  25.524  1.00 56.15  ? 291  ASP C OD2 1 
ATOM   8077  N  N   . PHE C 1 292 ? 4.301   25.487  21.364  1.00 39.73  ? 292  PHE C N   1 
ATOM   8078  C  CA  . PHE C 1 292 ? 4.041   25.977  20.009  1.00 24.85  ? 292  PHE C CA  1 
ATOM   8079  C  C   . PHE C 1 292 ? 3.265   27.311  19.993  1.00 25.60  ? 292  PHE C C   1 
ATOM   8080  O  O   . PHE C 1 292 ? 3.575   28.209  19.209  1.00 45.08  ? 292  PHE C O   1 
ATOM   8081  C  CB  . PHE C 1 292 ? 3.291   24.938  19.189  1.00 14.80  ? 292  PHE C CB  1 
ATOM   8082  C  CG  . PHE C 1 292 ? 2.844   25.452  17.866  1.00 26.94  ? 292  PHE C CG  1 
ATOM   8083  C  CD1 . PHE C 1 292 ? 3.691   25.390  16.766  1.00 33.66  ? 292  PHE C CD1 1 
ATOM   8084  C  CD2 . PHE C 1 292 ? 1.593   26.038  17.717  1.00 25.16  ? 292  PHE C CD2 1 
ATOM   8085  C  CE1 . PHE C 1 292 ? 3.292   25.872  15.527  1.00 25.46  ? 292  PHE C CE1 1 
ATOM   8086  C  CE2 . PHE C 1 292 ? 1.188   26.531  16.494  1.00 32.09  ? 292  PHE C CE2 1 
ATOM   8087  C  CZ  . PHE C 1 292 ? 2.041   26.446  15.392  1.00 33.83  ? 292  PHE C CZ  1 
ATOM   8088  N  N   . ASN C 1 293 ? 2.252   27.431  20.844  1.00 24.52  ? 293  ASN C N   1 
ATOM   8089  C  CA  . ASN C 1 293 ? 1.538   28.690  21.023  1.00 34.06  ? 293  ASN C CA  1 
ATOM   8090  C  C   . ASN C 1 293 ? 2.432   29.873  21.385  1.00 33.76  ? 293  ASN C C   1 
ATOM   8091  O  O   . ASN C 1 293 ? 2.358   30.947  20.770  1.00 27.48  ? 293  ASN C O   1 
ATOM   8092  C  CB  . ASN C 1 293 ? 0.472   28.528  22.102  1.00 36.81  ? 293  ASN C CB  1 
ATOM   8093  C  CG  . ASN C 1 293 ? -0.796  27.892  21.566  1.00 38.71  ? 293  ASN C CG  1 
ATOM   8094  O  OD1 . ASN C 1 293 ? -1.695  28.585  21.063  1.00 29.01  ? 293  ASN C OD1 1 
ATOM   8095  N  ND2 . ASN C 1 293 ? -0.871  26.564  21.655  1.00 25.35  ? 293  ASN C ND2 1 
ATOM   8096  N  N   . TYR C 1 294 ? 3.267   29.671  22.397  1.00 37.90  ? 294  TYR C N   1 
ATOM   8097  C  CA  . TYR C 1 294 ? 4.136   30.729  22.916  1.00 46.97  ? 294  TYR C CA  1 
ATOM   8098  C  C   . TYR C 1 294 ? 5.243   31.118  21.953  1.00 41.74  ? 294  TYR C C   1 
ATOM   8099  O  O   . TYR C 1 294 ? 5.608   32.294  21.858  1.00 28.82  ? 294  TYR C O   1 
ATOM   8100  C  CB  . TYR C 1 294 ? 4.782   30.289  24.224  1.00 37.39  ? 294  TYR C CB  1 
ATOM   8101  C  CG  . TYR C 1 294 ? 5.586   31.370  24.895  1.00 28.50  ? 294  TYR C CG  1 
ATOM   8102  C  CD1 . TYR C 1 294 ? 4.982   32.533  25.343  1.00 30.58  ? 294  TYR C CD1 1 
ATOM   8103  C  CD2 . TYR C 1 294 ? 6.939   31.222  25.105  1.00 31.41  ? 294  TYR C CD2 1 
ATOM   8104  C  CE1 . TYR C 1 294 ? 5.714   33.528  25.975  1.00 32.64  ? 294  TYR C CE1 1 
ATOM   8105  C  CE2 . TYR C 1 294 ? 7.675   32.211  25.740  1.00 33.20  ? 294  TYR C CE2 1 
ATOM   8106  C  CZ  . TYR C 1 294 ? 7.059   33.357  26.173  1.00 31.30  ? 294  TYR C CZ  1 
ATOM   8107  O  OH  . TYR C 1 294 ? 7.795   34.336  26.807  1.00 38.03  ? 294  TYR C OH  1 
ATOM   8108  N  N   . ALA C 1 295 ? 5.782   30.117  21.261  1.00 34.28  ? 295  ALA C N   1 
ATOM   8109  C  CA  . ALA C 1 295 ? 6.933   30.311  20.386  1.00 31.42  ? 295  ALA C CA  1 
ATOM   8110  C  C   . ALA C 1 295 ? 6.580   30.813  18.978  1.00 25.42  ? 295  ALA C C   1 
ATOM   8111  O  O   . ALA C 1 295 ? 7.411   31.438  18.304  1.00 32.97  ? 295  ALA C O   1 
ATOM   8112  C  CB  . ALA C 1 295 ? 7.730   29.025  20.298  1.00 29.88  ? 295  ALA C CB  1 
ATOM   8113  N  N   . PHE C 1 296 ? 5.353   30.538  18.543  1.00 27.30  ? 296  PHE C N   1 
ATOM   8114  C  CA  . PHE C 1 296 ? 4.959   30.801  17.161  1.00 34.32  ? 296  PHE C CA  1 
ATOM   8115  C  C   . PHE C 1 296 ? 3.769   31.749  17.087  1.00 36.29  ? 296  PHE C C   1 
ATOM   8116  O  O   . PHE C 1 296 ? 3.297   32.087  15.992  1.00 33.61  ? 296  PHE C O   1 
ATOM   8117  C  CB  . PHE C 1 296 ? 4.674   29.487  16.411  1.00 34.40  ? 296  PHE C CB  1 
ATOM   8118  C  CG  . PHE C 1 296 ? 5.883   28.599  16.271  1.00 48.01  ? 296  PHE C CG  1 
ATOM   8119  C  CD1 . PHE C 1 296 ? 6.261   27.752  17.301  1.00 46.66  ? 296  PHE C CD1 1 
ATOM   8120  C  CD2 . PHE C 1 296 ? 6.655   28.620  15.114  1.00 49.66  ? 296  PHE C CD2 1 
ATOM   8121  C  CE1 . PHE C 1 296 ? 7.386   26.937  17.181  1.00 40.84  ? 296  PHE C CE1 1 
ATOM   8122  C  CE2 . PHE C 1 296 ? 7.776   27.798  14.984  1.00 43.87  ? 296  PHE C CE2 1 
ATOM   8123  C  CZ  . PHE C 1 296 ? 8.140   26.960  16.019  1.00 43.47  ? 296  PHE C CZ  1 
ATOM   8124  N  N   . SER C 1 297 ? 3.295   32.182  18.252  1.00 33.72  ? 297  SER C N   1 
ATOM   8125  C  CA  . SER C 1 297 ? 2.252   33.204  18.313  1.00 21.54  ? 297  SER C CA  1 
ATOM   8126  C  C   . SER C 1 297 ? 2.382   34.059  19.573  1.00 19.86  ? 297  SER C C   1 
ATOM   8127  O  O   . SER C 1 297 ? 3.360   33.951  20.311  1.00 39.14  ? 297  SER C O   1 
ATOM   8128  C  CB  . SER C 1 297 ? 0.865   32.551  18.250  1.00 31.69  ? 297  SER C CB  1 
ATOM   8129  O  OG  . SER C 1 297 ? 0.442   32.077  19.520  1.00 31.02  ? 297  SER C OG  1 
ATOM   8130  N  N   . ASN C 1 298 ? 1.392   34.907  19.811  1.00 14.76  ? 298  ASN C N   1 
ATOM   8131  C  CA  . ASN C 1 298 ? 1.330   35.687  21.037  1.00 22.55  ? 298  ASN C CA  1 
ATOM   8132  C  C   . ASN C 1 298 ? 0.802   34.851  22.197  1.00 28.66  ? 298  ASN C C   1 
ATOM   8133  O  O   . ASN C 1 298 ? 0.972   35.196  23.368  1.00 30.88  ? 298  ASN C O   1 
ATOM   8134  C  CB  . ASN C 1 298 ? 0.398   36.894  20.861  1.00 18.08  ? 298  ASN C CB  1 
ATOM   8135  C  CG  . ASN C 1 298 ? 0.914   37.907  19.858  1.00 25.58  ? 298  ASN C CG  1 
ATOM   8136  O  OD1 . ASN C 1 298 ? 2.119   38.049  19.663  1.00 32.61  ? 298  ASN C OD1 1 
ATOM   8137  N  ND2 . ASN C 1 298 ? -0.008  38.631  19.222  1.00 30.81  ? 298  ASN C ND2 1 
ATOM   8138  N  N   . CYS C 1 299 ? 0.138   33.756  21.867  1.00 19.68  ? 299  CYS C N   1 
ATOM   8139  C  CA  . CYS C 1 299 ? -0.634  33.020  22.859  1.00 16.40  ? 299  CYS C CA  1 
ATOM   8140  C  C   . CYS C 1 299 ? 0.209   32.456  24.012  1.00 25.75  ? 299  CYS C C   1 
ATOM   8141  O  O   . CYS C 1 299 ? 1.314   31.948  23.818  1.00 29.02  ? 299  CYS C O   1 
ATOM   8142  C  CB  . CYS C 1 299 ? -1.422  31.896  22.192  1.00 11.64  ? 299  CYS C CB  1 
ATOM   8143  S  SG  . CYS C 1 299 ? -2.863  31.357  23.095  1.00 22.33  ? 299  CYS C SG  1 
ATOM   8144  N  N   . PHE C 1 300 ? -0.351  32.556  25.215  1.00 22.32  ? 300  PHE C N   1 
ATOM   8145  C  CA  . PHE C 1 300 ? 0.210   31.994  26.433  1.00 17.99  ? 300  PHE C CA  1 
ATOM   8146  C  C   . PHE C 1 300 ? -0.626  30.778  26.860  1.00 32.94  ? 300  PHE C C   1 
ATOM   8147  O  O   . PHE C 1 300 ? -1.666  30.925  27.531  1.00 31.71  ? 300  PHE C O   1 
ATOM   8148  C  CB  . PHE C 1 300 ? 0.168   33.050  27.534  1.00 36.86  ? 300  PHE C CB  1 
ATOM   8149  C  CG  . PHE C 1 300 ? 1.166   34.155  27.357  1.00 39.36  ? 300  PHE C CG  1 
ATOM   8150  C  CD1 . PHE C 1 300 ? 1.743   34.758  28.461  1.00 30.61  ? 300  PHE C CD1 1 
ATOM   8151  C  CD2 . PHE C 1 300 ? 1.539   34.583  26.089  1.00 45.85  ? 300  PHE C CD2 1 
ATOM   8152  C  CE1 . PHE C 1 300 ? 2.671   35.780  28.313  1.00 34.48  ? 300  PHE C CE1 1 
ATOM   8153  C  CE2 . PHE C 1 300 ? 2.474   35.603  25.926  1.00 43.52  ? 300  PHE C CE2 1 
ATOM   8154  C  CZ  . PHE C 1 300 ? 3.039   36.200  27.039  1.00 34.54  ? 300  PHE C CZ  1 
ATOM   8155  N  N   . GLU C 1 301 ? -0.195  29.583  26.461  1.00 22.67  ? 301  GLU C N   1 
ATOM   8156  C  CA  . GLU C 1 301 ? -0.971  28.369  26.727  1.00 23.59  ? 301  GLU C CA  1 
ATOM   8157  C  C   . GLU C 1 301 ? -0.451  27.589  27.941  1.00 30.82  ? 301  GLU C C   1 
ATOM   8158  O  O   . GLU C 1 301 ? 0.753   27.339  28.073  1.00 32.70  ? 301  GLU C O   1 
ATOM   8159  C  CB  . GLU C 1 301 ? -1.037  27.461  25.483  1.00 32.31  ? 301  GLU C CB  1 
ATOM   8160  C  CG  . GLU C 1 301 ? -1.580  26.058  25.761  1.00 40.10  ? 301  GLU C CG  1 
ATOM   8161  C  CD  . GLU C 1 301 ? -2.132  25.373  24.521  1.00 39.27  ? 301  GLU C CD  1 
ATOM   8162  O  OE1 . GLU C 1 301 ? -3.021  25.944  23.867  1.00 43.03  ? 301  GLU C OE1 1 
ATOM   8163  O  OE2 . GLU C 1 301 ? -1.687  24.253  24.208  1.00 44.71  ? 301  GLU C OE2 1 
ATOM   8164  N  N   . LEU C 1 302 ? -1.358  27.224  28.840  1.00 33.24  ? 302  LEU C N   1 
ATOM   8165  C  CA  . LEU C 1 302 ? -0.994  26.335  29.937  1.00 41.94  ? 302  LEU C CA  1 
ATOM   8166  C  C   . LEU C 1 302 ? -1.420  24.924  29.582  1.00 40.12  ? 302  LEU C C   1 
ATOM   8167  O  O   . LEU C 1 302 ? -2.371  24.733  28.822  1.00 38.60  ? 302  LEU C O   1 
ATOM   8168  C  CB  . LEU C 1 302 ? -1.666  26.743  31.252  1.00 35.43  ? 302  LEU C CB  1 
ATOM   8169  C  CG  . LEU C 1 302 ? -1.323  28.071  31.921  1.00 35.37  ? 302  LEU C CG  1 
ATOM   8170  C  CD1 . LEU C 1 302 ? -2.034  28.158  33.269  1.00 39.65  ? 302  LEU C CD1 1 
ATOM   8171  C  CD2 . LEU C 1 302 ? 0.173   28.204  32.102  1.00 37.16  ? 302  LEU C CD2 1 
ATOM   8172  N  N   . THR C 1 303 ? -0.709  23.944  30.130  1.00 39.55  ? 303  THR C N   1 
ATOM   8173  C  CA  . THR C 1 303 ? -1.148  22.549  30.087  1.00 50.89  ? 303  THR C CA  1 
ATOM   8174  C  C   . THR C 1 303 ? -1.740  22.193  31.449  1.00 52.39  ? 303  THR C C   1 
ATOM   8175  O  O   . THR C 1 303 ? -1.061  22.301  32.477  1.00 46.01  ? 303  THR C O   1 
ATOM   8176  C  CB  . THR C 1 303 ? 0.020   21.573  29.786  1.00 51.92  ? 303  THR C CB  1 
ATOM   8177  O  OG1 . THR C 1 303 ? 0.771   22.030  28.649  1.00 52.79  ? 303  THR C OG1 1 
ATOM   8178  C  CG2 . THR C 1 303 ? -0.513  20.176  29.513  1.00 38.04  ? 303  THR C CG2 1 
ATOM   8179  N  N   . ILE C 1 304 ? -3.002  21.770  31.465  1.00 52.77  ? 304  ILE C N   1 
ATOM   8180  C  CA  . ILE C 1 304 ? -3.650  21.441  32.733  1.00 46.94  ? 304  ILE C CA  1 
ATOM   8181  C  C   . ILE C 1 304 ? -4.110  19.988  32.879  1.00 45.59  ? 304  ILE C C   1 
ATOM   8182  O  O   . ILE C 1 304 ? -4.867  19.461  32.060  1.00 37.90  ? 304  ILE C O   1 
ATOM   8183  C  CB  . ILE C 1 304 ? -4.773  22.417  33.048  1.00 40.91  ? 304  ILE C CB  1 
ATOM   8184  C  CG1 . ILE C 1 304 ? -4.180  23.831  33.163  1.00 34.92  ? 304  ILE C CG1 1 
ATOM   8185  C  CG2 . ILE C 1 304 ? -5.474  22.008  34.344  1.00 42.80  ? 304  ILE C CG2 1 
ATOM   8186  C  CD1 . ILE C 1 304 ? -5.201  24.944  33.189  1.00 50.15  ? 304  ILE C CD1 1 
ATOM   8187  N  N   . GLU C 1 305 ? -3.613  19.352  33.934  1.00 39.81  ? 305  GLU C N   1 
ATOM   8188  C  CA  . GLU C 1 305 ? -3.921  17.966  34.237  1.00 30.31  ? 305  GLU C CA  1 
ATOM   8189  C  C   . GLU C 1 305 ? -5.037  17.944  35.258  1.00 41.81  ? 305  GLU C C   1 
ATOM   8190  O  O   . GLU C 1 305 ? -4.904  18.501  36.353  1.00 50.67  ? 305  GLU C O   1 
ATOM   8191  C  CB  . GLU C 1 305 ? -2.682  17.286  34.794  1.00 23.36  ? 305  GLU C CB  1 
ATOM   8192  C  CG  . GLU C 1 305 ? -1.509  17.322  33.843  1.00 18.01  ? 305  GLU C CG  1 
ATOM   8193  C  CD  . GLU C 1 305 ? -1.607  16.255  32.753  1.00 43.86  ? 305  GLU C CD  1 
ATOM   8194  O  OE1 . GLU C 1 305 ? -0.682  16.187  31.916  1.00 50.20  ? 305  GLU C OE1 1 
ATOM   8195  O  OE2 . GLU C 1 305 ? -2.593  15.478  32.729  1.00 41.54  ? 305  GLU C OE2 1 
ATOM   8196  N  N   . LEU C 1 306 ? -6.139  17.298  34.896  1.00 40.47  ? 306  LEU C N   1 
ATOM   8197  C  CA  . LEU C 1 306 ? -7.381  17.413  35.653  1.00 40.01  ? 306  LEU C CA  1 
ATOM   8198  C  C   . LEU C 1 306 ? -7.637  16.278  36.654  1.00 42.87  ? 306  LEU C C   1 
ATOM   8199  O  O   . LEU C 1 306 ? -8.066  16.533  37.781  1.00 49.55  ? 306  LEU C O   1 
ATOM   8200  C  CB  . LEU C 1 306 ? -8.561  17.554  34.686  1.00 45.79  ? 306  LEU C CB  1 
ATOM   8201  C  CG  . LEU C 1 306 ? -8.567  18.786  33.778  1.00 42.54  ? 306  LEU C CG  1 
ATOM   8202  C  CD1 . LEU C 1 306 ? -9.691  18.690  32.757  1.00 32.11  ? 306  LEU C CD1 1 
ATOM   8203  C  CD2 . LEU C 1 306 ? -8.680  20.069  34.597  1.00 33.14  ? 306  LEU C CD2 1 
ATOM   8204  N  N   . SER C 1 307 ? -7.378  15.036  36.248  1.00 47.53  ? 307  SER C N   1 
ATOM   8205  C  CA  . SER C 1 307 ? -7.647  13.872  37.101  1.00 41.77  ? 307  SER C CA  1 
ATOM   8206  C  C   . SER C 1 307 ? -6.472  12.899  37.184  1.00 40.50  ? 307  SER C C   1 
ATOM   8207  O  O   . SER C 1 307 ? -5.611  12.866  36.302  1.00 48.40  ? 307  SER C O   1 
ATOM   8208  C  CB  . SER C 1 307 ? -8.885  13.137  36.586  1.00 47.93  ? 307  SER C CB  1 
ATOM   8209  O  OG  . SER C 1 307 ? -8.874  13.077  35.167  1.00 48.39  ? 307  SER C OG  1 
ATOM   8210  N  N   . CYS C 1 308 ? -6.429  12.113  38.253  1.00 48.50  ? 308  CYS C N   1 
ATOM   8211  C  CA  . CYS C 1 308 ? -5.467  11.022  38.336  1.00 46.67  ? 308  CYS C CA  1 
ATOM   8212  C  C   . CYS C 1 308 ? -5.937  9.951   37.371  1.00 50.97  ? 308  CYS C C   1 
ATOM   8213  O  O   . CYS C 1 308 ? -5.145  9.351   36.645  1.00 56.40  ? 308  CYS C O   1 
ATOM   8214  C  CB  . CYS C 1 308 ? -5.410  10.445  39.748  1.00 42.44  ? 308  CYS C CB  1 
ATOM   8215  S  SG  . CYS C 1 308 ? -4.322  11.317  40.871  1.00 64.87  ? 308  CYS C SG  1 
ATOM   8216  N  N   . CYS C 1 309 ? -7.248  9.729   37.369  1.00 42.80  ? 309  CYS C N   1 
ATOM   8217  C  CA  . CYS C 1 309 ? -7.872  8.771   36.474  1.00 36.40  ? 309  CYS C CA  1 
ATOM   8218  C  C   . CYS C 1 309 ? -8.051  9.420   35.117  1.00 48.14  ? 309  CYS C C   1 
ATOM   8219  O  O   . CYS C 1 309 ? -8.731  10.441  35.019  1.00 34.08  ? 309  CYS C O   1 
ATOM   8220  C  CB  . CYS C 1 309 ? -9.228  8.367   37.043  1.00 28.01  ? 309  CYS C CB  1 
ATOM   8221  S  SG  . CYS C 1 309 ? -10.041 7.032   36.179  1.00 54.43  ? 309  CYS C SG  1 
ATOM   8222  N  N   . LYS C 1 310 ? -7.435  8.839   34.084  1.00 55.10  ? 310  LYS C N   1 
ATOM   8223  C  CA  . LYS C 1 310 ? -7.456  9.426   32.741  1.00 50.69  ? 310  LYS C CA  1 
ATOM   8224  C  C   . LYS C 1 310 ? -8.868  9.476   32.173  1.00 54.34  ? 310  LYS C C   1 
ATOM   8225  O  O   . LYS C 1 310 ? -9.300  10.519  31.656  1.00 54.62  ? 310  LYS C O   1 
ATOM   8226  C  CB  . LYS C 1 310 ? -6.527  8.669   31.779  1.00 54.87  ? 310  LYS C CB  1 
ATOM   8227  C  CG  . LYS C 1 310 ? -5.036  8.980   31.941  1.00 49.79  ? 310  LYS C CG  1 
ATOM   8228  C  CD  . LYS C 1 310 ? -4.188  8.199   30.938  1.00 43.18  ? 310  LYS C CD  1 
ATOM   8229  C  CE  . LYS C 1 310 ? -2.769  8.741   30.855  1.00 47.36  ? 310  LYS C CE  1 
ATOM   8230  N  NZ  . LYS C 1 310 ? -2.021  8.130   29.715  1.00 62.50  ? 310  LYS C NZ  1 
ATOM   8231  N  N   . TYR C 1 311 ? -9.575  8.348   32.281  1.00 50.42  ? 311  TYR C N   1 
ATOM   8232  C  CA  . TYR C 1 311 ? -10.939 8.206   31.774  1.00 48.15  ? 311  TYR C CA  1 
ATOM   8233  C  C   . TYR C 1 311 ? -11.864 7.693   32.870  1.00 47.24  ? 311  TYR C C   1 
ATOM   8234  O  O   . TYR C 1 311 ? -12.154 6.503   32.934  1.00 49.18  ? 311  TYR C O   1 
ATOM   8235  C  CB  . TYR C 1 311 ? -10.959 7.221   30.604  1.00 47.57  ? 311  TYR C CB  1 
ATOM   8236  C  CG  . TYR C 1 311 ? -12.121 7.383   29.633  1.00 44.23  ? 311  TYR C CG  1 
ATOM   8237  C  CD1 . TYR C 1 311 ? -11.965 7.085   28.288  1.00 34.78  ? 311  TYR C CD1 1 
ATOM   8238  C  CD2 . TYR C 1 311 ? -13.369 7.827   30.060  1.00 44.07  ? 311  TYR C CD2 1 
ATOM   8239  C  CE1 . TYR C 1 311 ? -13.012 7.219   27.395  1.00 46.41  ? 311  TYR C CE1 1 
ATOM   8240  C  CE2 . TYR C 1 311 ? -14.425 7.968   29.166  1.00 38.68  ? 311  TYR C CE2 1 
ATOM   8241  C  CZ  . TYR C 1 311 ? -14.239 7.663   27.834  1.00 41.55  ? 311  TYR C CZ  1 
ATOM   8242  O  OH  . TYR C 1 311 ? -15.272 7.801   26.926  1.00 35.69  ? 311  TYR C OH  1 
ATOM   8243  N  N   . PRO C 1 312 ? -12.336 8.591   33.742  1.00 55.01  ? 312  PRO C N   1 
ATOM   8244  C  CA  . PRO C 1 312 ? -13.174 8.157   34.862  1.00 56.53  ? 312  PRO C CA  1 
ATOM   8245  C  C   . PRO C 1 312 ? -14.599 7.919   34.396  1.00 62.45  ? 312  PRO C C   1 
ATOM   8246  O  O   . PRO C 1 312 ? -14.875 8.043   33.211  1.00 67.25  ? 312  PRO C O   1 
ATOM   8247  C  CB  . PRO C 1 312 ? -13.125 9.347   35.838  1.00 49.65  ? 312  PRO C CB  1 
ATOM   8248  C  CG  . PRO C 1 312 ? -12.189 10.361  35.214  1.00 63.69  ? 312  PRO C CG  1 
ATOM   8249  C  CD  . PRO C 1 312 ? -12.124 10.043  33.752  1.00 58.26  ? 312  PRO C CD  1 
ATOM   8250  N  N   . ALA C 1 313 ? -15.485 7.575   35.323  1.00 62.23  ? 313  ALA C N   1 
ATOM   8251  C  CA  . ALA C 1 313 ? -16.878 7.313   34.994  1.00 65.12  ? 313  ALA C CA  1 
ATOM   8252  C  C   . ALA C 1 313 ? -17.762 8.558   35.149  1.00 58.06  ? 313  ALA C C   1 
ATOM   8253  O  O   . ALA C 1 313 ? -17.466 9.451   35.951  1.00 53.86  ? 313  ALA C O   1 
ATOM   8254  C  CB  . ALA C 1 313 ? -17.407 6.175   35.848  1.00 69.30  ? 313  ALA C CB  1 
ATOM   8255  N  N   . ALA C 1 314 ? -18.855 8.591   34.386  1.00 47.79  ? 314  ALA C N   1 
ATOM   8256  C  CA  . ALA C 1 314 ? -19.782 9.723   34.354  1.00 44.30  ? 314  ALA C CA  1 
ATOM   8257  C  C   . ALA C 1 314 ? -20.127 10.326  35.723  1.00 48.17  ? 314  ALA C C   1 
ATOM   8258  O  O   . ALA C 1 314 ? -20.122 11.547  35.903  1.00 45.46  ? 314  ALA C O   1 
ATOM   8259  C  CB  . ALA C 1 314 ? -21.060 9.314   33.631  1.00 47.79  ? 314  ALA C CB  1 
ATOM   8260  N  N   . SER C 1 315 ? -20.446 9.465   36.680  1.00 48.80  ? 315  SER C N   1 
ATOM   8261  C  CA  . SER C 1 315 ? -20.902 9.918   37.988  1.00 48.40  ? 315  SER C CA  1 
ATOM   8262  C  C   . SER C 1 315 ? -19.870 10.846  38.604  1.00 43.16  ? 315  SER C C   1 
ATOM   8263  O  O   . SER C 1 315 ? -20.178 11.717  39.415  1.00 40.48  ? 315  SER C O   1 
ATOM   8264  C  CB  . SER C 1 315 ? -21.133 8.717   38.891  1.00 42.28  ? 315  SER C CB  1 
ATOM   8265  O  OG  . SER C 1 315 ? -19.944 7.954   39.002  1.00 47.24  ? 315  SER C OG  1 
ATOM   8266  N  N   . THR C 1 316 ? -18.631 10.647  38.197  1.00 38.10  ? 316  THR C N   1 
ATOM   8267  C  CA  . THR C 1 316 ? -17.544 11.502  38.623  1.00 42.20  ? 316  THR C CA  1 
ATOM   8268  C  C   . THR C 1 316 ? -17.690 12.920  38.085  1.00 45.01  ? 316  THR C C   1 
ATOM   8269  O  O   . THR C 1 316 ? -17.440 13.890  38.803  1.00 51.47  ? 316  THR C O   1 
ATOM   8270  C  CB  . THR C 1 316 ? -16.214 10.892  38.175  1.00 50.18  ? 316  THR C CB  1 
ATOM   8271  O  OG1 . THR C 1 316 ? -15.727 10.035  39.221  1.00 52.19  ? 316  THR C OG1 1 
ATOM   8272  C  CG2 . THR C 1 316 ? -15.189 11.960  37.848  1.00 55.21  ? 316  THR C CG2 1 
ATOM   8273  N  N   . LEU C 1 317 ? -18.117 13.022  36.829  1.00 38.14  ? 317  LEU C N   1 
ATOM   8274  C  CA  . LEU C 1 317 ? -18.235 14.296  36.107  1.00 44.26  ? 317  LEU C CA  1 
ATOM   8275  C  C   . LEU C 1 317 ? -18.836 15.498  36.861  1.00 43.10  ? 317  LEU C C   1 
ATOM   8276  O  O   . LEU C 1 317 ? -18.286 16.600  36.798  1.00 38.67  ? 317  LEU C O   1 
ATOM   8277  C  CB  . LEU C 1 317 ? -18.999 14.094  34.791  1.00 33.67  ? 317  LEU C CB  1 
ATOM   8278  C  CG  . LEU C 1 317 ? -18.499 12.989  33.860  1.00 36.86  ? 317  LEU C CG  1 
ATOM   8279  C  CD1 . LEU C 1 317 ? -19.466 12.815  32.715  1.00 59.01  ? 317  LEU C CD1 1 
ATOM   8280  C  CD2 . LEU C 1 317 ? -17.101 13.278  33.333  1.00 33.56  ? 317  LEU C CD2 1 
ATOM   8281  N  N   . PRO C 1 318 ? -19.978 15.307  37.542  1.00 43.54  ? 318  PRO C N   1 
ATOM   8282  C  CA  . PRO C 1 318 ? -20.562 16.432  38.287  1.00 47.41  ? 318  PRO C CA  1 
ATOM   8283  C  C   . PRO C 1 318 ? -19.637 17.030  39.377  1.00 55.28  ? 318  PRO C C   1 
ATOM   8284  O  O   . PRO C 1 318 ? -19.596 18.262  39.515  1.00 50.43  ? 318  PRO C O   1 
ATOM   8285  C  CB  . PRO C 1 318 ? -21.825 15.821  38.901  1.00 48.54  ? 318  PRO C CB  1 
ATOM   8286  C  CG  . PRO C 1 318 ? -22.187 14.715  37.982  1.00 49.97  ? 318  PRO C CG  1 
ATOM   8287  C  CD  . PRO C 1 318 ? -20.871 14.136  37.525  1.00 50.98  ? 318  PRO C CD  1 
ATOM   8288  N  N   . GLN C 1 319 ? -18.922 16.188  40.130  1.00 44.89  ? 319  GLN C N   1 
ATOM   8289  C  CA  . GLN C 1 319 ? -17.907 16.662  41.083  1.00 40.74  ? 319  GLN C CA  1 
ATOM   8290  C  C   . GLN C 1 319 ? -16.794 17.441  40.391  1.00 41.64  ? 319  GLN C C   1 
ATOM   8291  O  O   . GLN C 1 319 ? -16.434 18.546  40.811  1.00 36.18  ? 319  GLN C O   1 
ATOM   8292  C  CB  . GLN C 1 319 ? -17.266 15.492  41.819  1.00 62.97  ? 319  GLN C CB  1 
ATOM   8293  C  CG  . GLN C 1 319 ? -17.913 15.141  43.144  1.00 79.38  ? 319  GLN C CG  1 
ATOM   8294  C  CD  . GLN C 1 319 ? -18.624 13.800  43.107  1.00 98.13  ? 319  GLN C CD  1 
ATOM   8295  O  OE1 . GLN C 1 319 ? -18.655 13.070  44.102  1.00 105.84 ? 319  GLN C OE1 1 
ATOM   8296  N  NE2 . GLN C 1 319 ? -19.195 13.465  41.952  1.00 98.70  ? 319  GLN C NE2 1 
ATOM   8297  N  N   . GLU C 1 320 ? -16.236 16.845  39.338  1.00 46.98  ? 320  GLU C N   1 
ATOM   8298  C  CA  . GLU C 1 320 ? -15.187 17.494  38.542  1.00 52.23  ? 320  GLU C CA  1 
ATOM   8299  C  C   . GLU C 1 320 ? -15.589 18.907  38.110  1.00 42.17  ? 320  GLU C C   1 
ATOM   8300  O  O   . GLU C 1 320 ? -14.783 19.844  38.161  1.00 51.18  ? 320  GLU C O   1 
ATOM   8301  C  CB  . GLU C 1 320 ? -14.825 16.654  37.305  1.00 46.92  ? 320  GLU C CB  1 
ATOM   8302  C  CG  . GLU C 1 320 ? -14.346 15.232  37.600  1.00 55.68  ? 320  GLU C CG  1 
ATOM   8303  C  CD  . GLU C 1 320 ? -13.021 15.171  38.346  1.00 61.62  ? 320  GLU C CD  1 
ATOM   8304  O  OE1 . GLU C 1 320 ? -12.475 16.243  38.698  1.00 62.15  ? 320  GLU C OE1 1 
ATOM   8305  O  OE2 . GLU C 1 320 ? -12.529 14.042  38.582  1.00 58.35  ? 320  GLU C OE2 1 
ATOM   8306  N  N   . TRP C 1 321 ? -16.837 19.053  37.683  1.00 34.82  ? 321  TRP C N   1 
ATOM   8307  C  CA  . TRP C 1 321 ? -17.360 20.364  37.328  1.00 42.88  ? 321  TRP C CA  1 
ATOM   8308  C  C   . TRP C 1 321 ? -17.231 21.383  38.465  1.00 55.94  ? 321  TRP C C   1 
ATOM   8309  O  O   . TRP C 1 321 ? -16.759 22.509  38.253  1.00 43.74  ? 321  TRP C O   1 
ATOM   8310  C  CB  . TRP C 1 321 ? -18.824 20.268  36.917  1.00 39.72  ? 321  TRP C CB  1 
ATOM   8311  C  CG  . TRP C 1 321 ? -19.447 21.609  36.836  1.00 49.40  ? 321  TRP C CG  1 
ATOM   8312  C  CD1 . TRP C 1 321 ? -20.389 22.122  37.674  1.00 44.31  ? 321  TRP C CD1 1 
ATOM   8313  C  CD2 . TRP C 1 321 ? -19.141 22.644  35.885  1.00 61.04  ? 321  TRP C CD2 1 
ATOM   8314  N  NE1 . TRP C 1 321 ? -20.707 23.406  37.296  1.00 51.90  ? 321  TRP C NE1 1 
ATOM   8315  C  CE2 . TRP C 1 321 ? -19.956 23.750  36.201  1.00 56.87  ? 321  TRP C CE2 1 
ATOM   8316  C  CE3 . TRP C 1 321 ? -18.265 22.737  34.791  1.00 56.50  ? 321  TRP C CE3 1 
ATOM   8317  C  CZ2 . TRP C 1 321 ? -19.923 24.941  35.463  1.00 51.43  ? 321  TRP C CZ2 1 
ATOM   8318  C  CZ3 . TRP C 1 321 ? -18.231 23.920  34.059  1.00 45.17  ? 321  TRP C CZ3 1 
ATOM   8319  C  CH2 . TRP C 1 321 ? -19.054 25.006  34.399  1.00 41.14  ? 321  TRP C CH2 1 
ATOM   8320  N  N   . GLN C 1 322 ? -17.655 20.982  39.666  1.00 60.29  ? 322  GLN C N   1 
ATOM   8321  C  CA  . GLN C 1 322 ? -17.736 21.900  40.804  1.00 56.76  ? 322  GLN C CA  1 
ATOM   8322  C  C   . GLN C 1 322 ? -16.360 22.389  41.243  1.00 56.09  ? 322  GLN C C   1 
ATOM   8323  O  O   . GLN C 1 322 ? -16.202 23.536  41.674  1.00 56.39  ? 322  GLN C O   1 
ATOM   8324  C  CB  . GLN C 1 322 ? -18.479 21.255  41.980  1.00 55.89  ? 322  GLN C CB  1 
ATOM   8325  C  CG  . GLN C 1 322 ? -19.647 22.096  42.510  1.00 66.61  ? 322  GLN C CG  1 
ATOM   8326  C  CD  . GLN C 1 322 ? -20.779 22.248  41.490  1.00 72.97  ? 322  GLN C CD  1 
ATOM   8327  O  OE1 . GLN C 1 322 ? -21.293 23.349  41.255  1.00 71.80  ? 322  GLN C OE1 1 
ATOM   8328  N  NE2 . GLN C 1 322 ? -21.168 21.135  40.879  1.00 68.77  ? 322  GLN C NE2 1 
ATOM   8329  N  N   . ARG C 1 323 ? -15.371 21.510  41.123  1.00 46.66  ? 323  ARG C N   1 
ATOM   8330  C  CA  . ARG C 1 323 ? -13.991 21.831  41.459  1.00 38.12  ? 323  ARG C CA  1 
ATOM   8331  C  C   . ARG C 1 323 ? -13.322 22.750  40.421  1.00 51.05  ? 323  ARG C C   1 
ATOM   8332  O  O   . ARG C 1 323 ? -12.657 23.742  40.772  1.00 45.92  ? 323  ARG C O   1 
ATOM   8333  C  CB  . ARG C 1 323 ? -13.203 20.532  41.569  1.00 43.24  ? 323  ARG C CB  1 
ATOM   8334  C  CG  . ARG C 1 323 ? -13.824 19.525  42.522  1.00 44.65  ? 323  ARG C CG  1 
ATOM   8335  C  CD  . ARG C 1 323 ? -13.128 18.195  42.386  1.00 54.51  ? 323  ARG C CD  1 
ATOM   8336  N  NE  . ARG C 1 323 ? -13.482 17.264  43.449  1.00 57.74  ? 323  ARG C NE  1 
ATOM   8337  C  CZ  . ARG C 1 323 ? -13.072 16.001  43.480  1.00 78.36  ? 323  ARG C CZ  1 
ATOM   8338  N  NH1 . ARG C 1 323 ? -12.301 15.534  42.504  1.00 76.71  ? 323  ARG C NH1 1 
ATOM   8339  N  NH2 . ARG C 1 323 ? -13.425 15.206  44.484  1.00 92.74  ? 323  ARG C NH2 1 
ATOM   8340  N  N   . ASN C 1 324 ? -13.493 22.418  39.143  1.00 38.94  ? 324  ASN C N   1 
ATOM   8341  C  CA  . ASN C 1 324 ? -12.835 23.168  38.081  1.00 39.06  ? 324  ASN C CA  1 
ATOM   8342  C  C   . ASN C 1 324 ? -13.550 24.472  37.710  1.00 41.11  ? 324  ASN C C   1 
ATOM   8343  O  O   . ASN C 1 324 ? -12.964 25.366  37.087  1.00 38.52  ? 324  ASN C O   1 
ATOM   8344  C  CB  . ASN C 1 324 ? -12.660 22.280  36.852  1.00 38.00  ? 324  ASN C CB  1 
ATOM   8345  C  CG  . ASN C 1 324 ? -11.732 21.122  37.107  1.00 40.66  ? 324  ASN C CG  1 
ATOM   8346  O  OD1 . ASN C 1 324 ? -10.559 21.157  36.738  1.00 46.05  ? 324  ASN C OD1 1 
ATOM   8347  N  ND2 . ASN C 1 324 ? -12.245 20.092  37.763  1.00 44.25  ? 324  ASN C ND2 1 
ATOM   8348  N  N   . LYS C 1 325 ? -14.817 24.564  38.103  1.00 37.84  ? 325  LYS C N   1 
ATOM   8349  C  CA  . LYS C 1 325 ? -15.675 25.702  37.782  1.00 37.28  ? 325  LYS C CA  1 
ATOM   8350  C  C   . LYS C 1 325 ? -15.016 27.062  38.051  1.00 37.62  ? 325  LYS C C   1 
ATOM   8351  O  O   . LYS C 1 325 ? -14.863 27.890  37.152  1.00 44.52  ? 325  LYS C O   1 
ATOM   8352  C  CB  . LYS C 1 325 ? -16.958 25.579  38.592  1.00 40.63  ? 325  LYS C CB  1 
ATOM   8353  C  CG  . LYS C 1 325 ? -18.089 26.477  38.146  1.00 43.19  ? 325  LYS C CG  1 
ATOM   8354  C  CD  . LYS C 1 325 ? -19.273 26.268  39.061  1.00 40.98  ? 325  LYS C CD  1 
ATOM   8355  C  CE  . LYS C 1 325 ? -20.418 27.168  38.720  1.00 49.33  ? 325  LYS C CE  1 
ATOM   8356  N  NZ  . LYS C 1 325 ? -21.522 26.888  39.670  1.00 62.11  ? 325  LYS C NZ  1 
ATOM   8357  N  N   . ALA C 1 326 ? -14.628 27.283  39.301  1.00 45.91  ? 326  ALA C N   1 
ATOM   8358  C  CA  . ALA C 1 326 ? -13.950 28.520  39.696  1.00 58.08  ? 326  ALA C CA  1 
ATOM   8359  C  C   . ALA C 1 326 ? -12.607 28.754  38.972  1.00 51.93  ? 326  ALA C C   1 
ATOM   8360  O  O   . ALA C 1 326 ? -12.280 29.899  38.639  1.00 36.96  ? 326  ALA C O   1 
ATOM   8361  C  CB  . ALA C 1 326 ? -13.768 28.575  41.246  1.00 34.71  ? 326  ALA C CB  1 
ATOM   8362  N  N   . SER C 1 327 ? -11.841 27.679  38.745  1.00 45.65  ? 327  SER C N   1 
ATOM   8363  C  CA  . SER C 1 327 ? -10.497 27.778  38.157  1.00 32.99  ? 327  SER C CA  1 
ATOM   8364  C  C   . SER C 1 327 ? -10.591 28.065  36.667  1.00 32.28  ? 327  SER C C   1 
ATOM   8365  O  O   . SER C 1 327 ? -9.706  28.696  36.087  1.00 43.83  ? 327  SER C O   1 
ATOM   8366  C  CB  . SER C 1 327 ? -9.681  26.490  38.363  1.00 28.90  ? 327  SER C CB  1 
ATOM   8367  O  OG  . SER C 1 327 ? -9.727  26.004  39.693  1.00 39.12  ? 327  SER C OG  1 
ATOM   8368  N  N   . LEU C 1 328 ? -11.664 27.586  36.045  1.00 31.65  ? 328  LEU C N   1 
ATOM   8369  C  CA  . LEU C 1 328 ? -11.864 27.780  34.615  1.00 37.12  ? 328  LEU C CA  1 
ATOM   8370  C  C   . LEU C 1 328 ? -12.289 29.208  34.320  1.00 39.02  ? 328  LEU C C   1 
ATOM   8371  O  O   . LEU C 1 328 ? -11.917 29.777  33.294  1.00 38.29  ? 328  LEU C O   1 
ATOM   8372  C  CB  . LEU C 1 328 ? -12.912 26.802  34.080  1.00 25.97  ? 328  LEU C CB  1 
ATOM   8373  C  CG  . LEU C 1 328 ? -12.407 25.387  33.808  1.00 22.79  ? 328  LEU C CG  1 
ATOM   8374  C  CD1 . LEU C 1 328 ? -13.514 24.349  33.933  1.00 24.98  ? 328  LEU C CD1 1 
ATOM   8375  C  CD2 . LEU C 1 328 ? -11.753 25.328  32.430  1.00 22.71  ? 328  LEU C CD2 1 
ATOM   8376  N  N   . LEU C 1 329 ? -13.079 29.772  35.227  1.00 30.14  ? 329  LEU C N   1 
ATOM   8377  C  CA  . LEU C 1 329 ? -13.553 31.139  35.083  1.00 42.76  ? 329  LEU C CA  1 
ATOM   8378  C  C   . LEU C 1 329 ? -12.426 32.120  35.390  1.00 41.97  ? 329  LEU C C   1 
ATOM   8379  O  O   . LEU C 1 329 ? -12.181 33.054  34.623  1.00 53.43  ? 329  LEU C O   1 
ATOM   8380  C  CB  . LEU C 1 329 ? -14.743 31.402  36.018  1.00 49.31  ? 329  LEU C CB  1 
ATOM   8381  C  CG  . LEU C 1 329 ? -16.135 31.026  35.511  1.00 48.31  ? 329  LEU C CG  1 
ATOM   8382  C  CD1 . LEU C 1 329 ? -16.060 30.421  34.095  1.00 48.87  ? 329  LEU C CD1 1 
ATOM   8383  C  CD2 . LEU C 1 329 ? -16.825 30.085  36.495  1.00 45.88  ? 329  LEU C CD2 1 
ATOM   8384  N  N   . GLN C 1 330 ? -11.741 31.894  36.510  1.00 25.79  ? 330  GLN C N   1 
ATOM   8385  C  CA  . GLN C 1 330 ? -10.697 32.802  36.986  1.00 39.76  ? 330  GLN C CA  1 
ATOM   8386  C  C   . GLN C 1 330 ? -9.460  32.826  36.087  1.00 43.73  ? 330  GLN C C   1 
ATOM   8387  O  O   . GLN C 1 330 ? -8.804  33.858  35.956  1.00 49.41  ? 330  GLN C O   1 
ATOM   8388  C  CB  . GLN C 1 330 ? -10.303 32.485  38.442  1.00 57.23  ? 330  GLN C CB  1 
ATOM   8389  C  CG  . GLN C 1 330 ? -11.406 32.759  39.480  1.00 55.33  ? 330  GLN C CG  1 
ATOM   8390  C  CD  . GLN C 1 330 ? -11.864 34.223  39.512  1.00 57.46  ? 330  GLN C CD  1 
ATOM   8391  O  OE1 . GLN C 1 330 ? -11.104 35.122  39.875  1.00 48.54  ? 330  GLN C OE1 1 
ATOM   8392  N  NE2 . GLN C 1 330 ? -13.119 34.459  39.136  1.00 70.34  ? 330  GLN C NE2 1 
ATOM   8393  N  N   . LEU C 1 331 ? -9.142  31.691  35.468  1.00 36.81  ? 331  LEU C N   1 
ATOM   8394  C  CA  . LEU C 1 331 ? -8.085  31.655  34.458  1.00 26.77  ? 331  LEU C CA  1 
ATOM   8395  C  C   . LEU C 1 331 ? -8.465  32.563  33.289  1.00 24.91  ? 331  LEU C C   1 
ATOM   8396  O  O   . LEU C 1 331 ? -7.735  33.484  32.946  1.00 29.30  ? 331  LEU C O   1 
ATOM   8397  C  CB  . LEU C 1 331 ? -7.839  30.227  33.968  1.00 15.37  ? 331  LEU C CB  1 
ATOM   8398  C  CG  . LEU C 1 331 ? -6.539  30.011  33.183  1.00 28.88  ? 331  LEU C CG  1 
ATOM   8399  C  CD1 . LEU C 1 331 ? -6.295  28.540  32.921  1.00 27.14  ? 331  LEU C CD1 1 
ATOM   8400  C  CD2 . LEU C 1 331 ? -6.547  30.765  31.868  1.00 59.56  ? 331  LEU C CD2 1 
ATOM   8401  N  N   . LEU C 1 332 ? -9.610  32.290  32.678  1.00 21.52  ? 332  LEU C N   1 
ATOM   8402  C  CA  . LEU C 1 332 ? -10.114 33.128  31.608  1.00 27.55  ? 332  LEU C CA  1 
ATOM   8403  C  C   . LEU C 1 332 ? -9.910  34.610  31.905  1.00 29.30  ? 332  LEU C C   1 
ATOM   8404  O  O   . LEU C 1 332 ? -9.384  35.351  31.081  1.00 30.63  ? 332  LEU C O   1 
ATOM   8405  C  CB  . LEU C 1 332 ? -11.599 32.836  31.387  1.00 41.49  ? 332  LEU C CB  1 
ATOM   8406  C  CG  . LEU C 1 332 ? -11.862 31.474  30.746  1.00 42.92  ? 332  LEU C CG  1 
ATOM   8407  C  CD1 . LEU C 1 332 ? -13.335 31.289  30.398  1.00 31.32  ? 332  LEU C CD1 1 
ATOM   8408  C  CD2 . LEU C 1 332 ? -11.010 31.340  29.507  1.00 40.53  ? 332  LEU C CD2 1 
ATOM   8409  N  N   . ARG C 1 333 ? -10.323 35.034  33.092  1.00 35.48  ? 333  ARG C N   1 
ATOM   8410  C  CA  . ARG C 1 333 ? -10.261 36.440  33.479  1.00 29.90  ? 333  ARG C CA  1 
ATOM   8411  C  C   . ARG C 1 333 ? -8.853  36.957  33.516  1.00 26.71  ? 333  ARG C C   1 
ATOM   8412  O  O   . ARG C 1 333 ? -8.646  38.164  33.529  1.00 57.04  ? 333  ARG C O   1 
ATOM   8413  C  CB  . ARG C 1 333 ? -10.904 36.668  34.851  1.00 31.05  ? 333  ARG C CB  1 
ATOM   8414  C  CG  . ARG C 1 333 ? -12.421 36.487  34.852  1.00 51.99  ? 333  ARG C CG  1 
ATOM   8415  C  CD  . ARG C 1 333 ? -13.093 37.505  35.761  1.00 59.36  ? 333  ARG C CD  1 
ATOM   8416  N  NE  . ARG C 1 333 ? -14.531 37.419  35.641  1.00 56.85  ? 333  ARG C NE  1 
ATOM   8417  C  CZ  . ARG C 1 333 ? -15.338 38.338  35.126  1.00 61.75  ? 333  ARG C CZ  1 
ATOM   8418  N  NH1 . ARG C 1 333 ? -14.904 39.507  34.670  1.00 56.93  ? 333  ARG C NH1 1 
ATOM   8419  N  NH2 . ARG C 1 333 ? -16.621 38.063  35.083  1.00 66.67  ? 333  ARG C NH2 1 
ATOM   8420  N  N   . GLN C 1 334 ? -7.881  36.055  33.560  1.00 27.81  ? 334  GLN C N   1 
ATOM   8421  C  CA  . GLN C 1 334 ? -6.475  36.463  33.531  1.00 23.58  ? 334  GLN C CA  1 
ATOM   8422  C  C   . GLN C 1 334 ? -6.104  37.024  32.153  1.00 29.50  ? 334  GLN C C   1 
ATOM   8423  O  O   . GLN C 1 334 ? -5.061  37.657  31.991  1.00 39.18  ? 334  GLN C O   1 
ATOM   8424  C  CB  . GLN C 1 334 ? -5.553  35.287  33.885  1.00 35.60  ? 334  GLN C CB  1 
ATOM   8425  C  CG  . GLN C 1 334 ? -5.511  34.900  35.369  1.00 28.75  ? 334  GLN C CG  1 
ATOM   8426  C  CD  . GLN C 1 334 ? -4.698  35.861  36.203  1.00 35.12  ? 334  GLN C CD  1 
ATOM   8427  O  OE1 . GLN C 1 334 ? -3.480  35.939  36.076  1.00 48.81  ? 334  GLN C OE1 1 
ATOM   8428  N  NE2 . GLN C 1 334 ? -5.370  36.599  37.069  1.00 39.45  ? 334  GLN C NE2 1 
ATOM   8429  N  N   . ALA C 1 335 ? -6.961  36.787  31.163  1.00 25.47  ? 335  ALA C N   1 
ATOM   8430  C  CA  . ALA C 1 335 ? -6.728  37.305  29.828  1.00 32.89  ? 335  ALA C CA  1 
ATOM   8431  C  C   . ALA C 1 335 ? -6.943  38.811  29.843  1.00 37.51  ? 335  ALA C C   1 
ATOM   8432  O  O   . ALA C 1 335 ? -6.940  39.471  28.802  1.00 40.15  ? 335  ALA C O   1 
ATOM   8433  C  CB  . ALA C 1 335 ? -7.660  36.646  28.833  1.00 33.41  ? 335  ALA C CB  1 
ATOM   8434  N  N   . HIS C 1 336 ? -7.124  39.363  31.034  1.00 24.66  ? 336  HIS C N   1 
ATOM   8435  C  CA  . HIS C 1 336 ? -7.393  40.785  31.144  1.00 30.77  ? 336  HIS C CA  1 
ATOM   8436  C  C   . HIS C 1 336 ? -6.319  41.534  31.910  1.00 40.82  ? 336  HIS C C   1 
ATOM   8437  O  O   . HIS C 1 336 ? -6.330  42.770  31.930  1.00 38.74  ? 336  HIS C O   1 
ATOM   8438  C  CB  . HIS C 1 336 ? -8.781  41.041  31.738  1.00 32.52  ? 336  HIS C CB  1 
ATOM   8439  C  CG  . HIS C 1 336 ? -9.899  40.519  30.885  1.00 49.53  ? 336  HIS C CG  1 
ATOM   8440  N  ND1 . HIS C 1 336 ? -10.319 41.157  29.735  1.00 45.95  ? 336  HIS C ND1 1 
ATOM   8441  C  CD2 . HIS C 1 336 ? -10.668 39.409  31.003  1.00 48.13  ? 336  HIS C CD2 1 
ATOM   8442  C  CE1 . HIS C 1 336 ? -11.301 40.464  29.185  1.00 48.73  ? 336  HIS C CE1 1 
ATOM   8443  N  NE2 . HIS C 1 336 ? -11.534 39.401  29.936  1.00 53.73  ? 336  HIS C NE2 1 
ATOM   8444  N  N   . ILE C 1 337 ? -5.386  40.796  32.518  1.00 36.34  ? 337  ILE C N   1 
ATOM   8445  C  CA  . ILE C 1 337 ? -4.267  41.422  33.225  1.00 31.47  ? 337  ILE C CA  1 
ATOM   8446  C  C   . ILE C 1 337 ? -3.324  42.147  32.281  1.00 33.79  ? 337  ILE C C   1 
ATOM   8447  O  O   . ILE C 1 337 ? -3.382  41.972  31.063  1.00 42.70  ? 337  ILE C O   1 
ATOM   8448  C  CB  . ILE C 1 337 ? -3.440  40.420  34.056  1.00 42.21  ? 337  ILE C CB  1 
ATOM   8449  C  CG1 . ILE C 1 337 ? -2.789  39.369  33.161  1.00 38.14  ? 337  ILE C CG1 1 
ATOM   8450  C  CG2 . ILE C 1 337 ? -4.297  39.772  35.135  1.00 48.76  ? 337  ILE C CG2 1 
ATOM   8451  C  CD1 . ILE C 1 337 ? -2.035  38.334  33.968  1.00 36.44  ? 337  ILE C CD1 1 
ATOM   8452  N  N   . GLY C 1 338 ? -2.457  42.970  32.858  1.00 38.62  ? 338  GLY C N   1 
ATOM   8453  C  CA  . GLY C 1 338 ? -1.484  43.707  32.075  1.00 42.94  ? 338  GLY C CA  1 
ATOM   8454  C  C   . GLY C 1 338 ? -2.068  44.903  31.347  1.00 34.49  ? 338  GLY C C   1 
ATOM   8455  O  O   . GLY C 1 338 ? -2.789  45.722  31.934  1.00 41.78  ? 338  GLY C O   1 
ATOM   8456  N  N   . ILE C 1 339 ? -1.748  45.008  30.063  1.00 26.17  ? 339  ILE C N   1 
ATOM   8457  C  CA  . ILE C 1 339 ? -2.190  46.142  29.266  1.00 36.74  ? 339  ILE C CA  1 
ATOM   8458  C  C   . ILE C 1 339 ? -2.640  45.716  27.887  1.00 34.08  ? 339  ILE C C   1 
ATOM   8459  O  O   . ILE C 1 339 ? -2.599  44.541  27.533  1.00 37.54  ? 339  ILE C O   1 
ATOM   8460  C  CB  . ILE C 1 339 ? -1.075  47.189  29.087  1.00 42.10  ? 339  ILE C CB  1 
ATOM   8461  C  CG1 . ILE C 1 339 ? 0.156   46.552  28.418  1.00 39.22  ? 339  ILE C CG1 1 
ATOM   8462  C  CG2 . ILE C 1 339 ? -0.745  47.872  30.436  1.00 29.61  ? 339  ILE C CG2 1 
ATOM   8463  C  CD1 . ILE C 1 339 ? 1.311   47.517  28.193  1.00 25.58  ? 339  ILE C CD1 1 
ATOM   8464  N  N   . LYS C 1 340 ? -3.086  46.691  27.113  1.00 24.78  ? 340  LYS C N   1 
ATOM   8465  C  CA  . LYS C 1 340 ? -3.502  46.454  25.741  1.00 29.18  ? 340  LYS C CA  1 
ATOM   8466  C  C   . LYS C 1 340 ? -3.647  47.819  25.105  1.00 43.56  ? 340  LYS C C   1 
ATOM   8467  O  O   . LYS C 1 340 ? -3.838  48.826  25.802  1.00 28.72  ? 340  LYS C O   1 
ATOM   8468  C  CB  . LYS C 1 340 ? -4.830  45.700  25.666  1.00 35.84  ? 340  LYS C CB  1 
ATOM   8469  C  CG  . LYS C 1 340 ? -6.020  46.441  26.309  1.00 37.36  ? 340  LYS C CG  1 
ATOM   8470  C  CD  . LYS C 1 340 ? -7.320  45.708  26.052  1.00 29.91  ? 340  LYS C CD  1 
ATOM   8471  C  CE  . LYS C 1 340 ? -8.414  46.144  27.014  1.00 26.24  ? 340  LYS C CE  1 
ATOM   8472  N  NZ  . LYS C 1 340 ? -9.723  45.411  26.754  1.00 35.10  ? 340  LYS C NZ  1 
ATOM   8473  N  N   . GLY C 1 341 ? -3.530  47.863  23.784  1.00 34.89  ? 341  GLY C N   1 
ATOM   8474  C  CA  . GLY C 1 341 ? -3.600  49.133  23.100  1.00 26.57  ? 341  GLY C CA  1 
ATOM   8475  C  C   . GLY C 1 341 ? -3.442  48.997  21.609  1.00 30.39  ? 341  GLY C C   1 
ATOM   8476  O  O   . GLY C 1 341 ? -3.506  47.899  21.045  1.00 23.40  ? 341  GLY C O   1 
ATOM   8477  N  N   . LEU C 1 342 ? -3.229  50.135  20.965  1.00 36.93  ? 342  LEU C N   1 
ATOM   8478  C  CA  . LEU C 1 342 ? -3.086  50.166  19.524  1.00 39.34  ? 342  LEU C CA  1 
ATOM   8479  C  C   . LEU C 1 342 ? -1.746  50.745  19.112  1.00 35.78  ? 342  LEU C C   1 
ATOM   8480  O  O   . LEU C 1 342 ? -1.239  51.685  19.719  1.00 34.60  ? 342  LEU C O   1 
ATOM   8481  C  CB  . LEU C 1 342 ? -4.213  50.988  18.909  1.00 27.85  ? 342  LEU C CB  1 
ATOM   8482  C  CG  . LEU C 1 342 ? -5.627  50.471  19.176  1.00 26.21  ? 342  LEU C CG  1 
ATOM   8483  C  CD1 . LEU C 1 342 ? -6.673  51.443  18.664  1.00 20.12  ? 342  LEU C CD1 1 
ATOM   8484  C  CD2 . LEU C 1 342 ? -5.830  49.080  18.580  1.00 20.54  ? 342  LEU C CD2 1 
ATOM   8485  N  N   . VAL C 1 343 ? -1.165  50.160  18.082  1.00 30.47  ? 343  VAL C N   1 
ATOM   8486  C  CA  . VAL C 1 343 ? -0.059  50.794  17.420  1.00 38.21  ? 343  VAL C CA  1 
ATOM   8487  C  C   . VAL C 1 343 ? -0.646  51.369  16.147  1.00 32.73  ? 343  VAL C C   1 
ATOM   8488  O  O   . VAL C 1 343 ? -1.247  50.650  15.356  1.00 30.00  ? 343  VAL C O   1 
ATOM   8489  C  CB  . VAL C 1 343 ? 1.053   49.809  17.089  1.00 35.55  ? 343  VAL C CB  1 
ATOM   8490  C  CG1 . VAL C 1 343 ? 2.118   50.518  16.280  1.00 24.54  ? 343  VAL C CG1 1 
ATOM   8491  C  CG2 . VAL C 1 343 ? 1.633   49.216  18.368  1.00 29.48  ? 343  VAL C CG2 1 
ATOM   8492  N  N   . THR C 1 344 ? -0.481  52.671  15.959  1.00 43.78  ? 344  THR C N   1 
ATOM   8493  C  CA  . THR C 1 344 ? -1.210  53.354  14.911  1.00 47.21  ? 344  THR C CA  1 
ATOM   8494  C  C   . THR C 1 344 ? -0.320  54.302  14.103  1.00 46.28  ? 344  THR C C   1 
ATOM   8495  O  O   . THR C 1 344 ? 0.809   54.614  14.502  1.00 38.65  ? 344  THR C O   1 
ATOM   8496  C  CB  . THR C 1 344 ? -2.455  54.078  15.494  1.00 45.90  ? 344  THR C CB  1 
ATOM   8497  O  OG1 . THR C 1 344 ? -3.395  54.349  14.452  1.00 62.73  ? 344  THR C OG1 1 
ATOM   8498  C  CG2 . THR C 1 344 ? -2.066  55.367  16.188  1.00 34.03  ? 344  THR C CG2 1 
ATOM   8499  N  N   . ASP C 1 345 ? -0.842  54.709  12.947  1.00 41.37  ? 345  ASP C N   1 
ATOM   8500  C  CA  . ASP C 1 345 ? -0.228  55.657  12.014  1.00 42.14  ? 345  ASP C CA  1 
ATOM   8501  C  C   . ASP C 1 345 ? -0.142  57.071  12.570  1.00 45.65  ? 345  ASP C C   1 
ATOM   8502  O  O   . ASP C 1 345 ? -0.600  57.359  13.673  1.00 30.43  ? 345  ASP C O   1 
ATOM   8503  C  CB  . ASP C 1 345 ? -1.134  55.792  10.779  1.00 38.50  ? 345  ASP C CB  1 
ATOM   8504  C  CG  . ASP C 1 345 ? -0.745  54.888  9.647   1.00 44.75  ? 345  ASP C CG  1 
ATOM   8505  O  OD1 . ASP C 1 345 ? -1.463  54.890  8.627   1.00 55.84  ? 345  ASP C OD1 1 
ATOM   8506  O  OD2 . ASP C 1 345 ? 0.270   54.186  9.764   1.00 62.89  ? 345  ASP C OD2 1 
ATOM   8507  N  N   . ALA C 1 346 ? 0.411   57.964  11.756  1.00 58.48  ? 346  ALA C N   1 
ATOM   8508  C  CA  . ALA C 1 346 ? 0.120   59.378  11.893  1.00 59.63  ? 346  ALA C CA  1 
ATOM   8509  C  C   . ALA C 1 346 ? -1.334  59.507  11.461  1.00 82.40  ? 346  ALA C C   1 
ATOM   8510  O  O   . ALA C 1 346 ? -2.132  60.199  12.100  1.00 98.86  ? 346  ALA C O   1 
ATOM   8511  C  CB  . ALA C 1 346 ? 1.027   60.206  10.982  1.00 37.20  ? 346  ALA C CB  1 
ATOM   8512  N  N   . SER C 1 347 ? -1.669  58.787  10.388  1.00 79.23  ? 347  SER C N   1 
ATOM   8513  C  CA  . SER C 1 347 ? -3.033  58.707  9.851   1.00 71.82  ? 347  SER C CA  1 
ATOM   8514  C  C   . SER C 1 347 ? -4.080  58.232  10.859  1.00 69.84  ? 347  SER C C   1 
ATOM   8515  O  O   . SER C 1 347 ? -5.283  58.310  10.584  1.00 71.68  ? 347  SER C O   1 
ATOM   8516  C  CB  . SER C 1 347 ? -3.068  57.769  8.636   1.00 62.58  ? 347  SER C CB  1 
ATOM   8517  O  OG  . SER C 1 347 ? -3.246  58.486  7.423   1.00 64.47  ? 347  SER C OG  1 
ATOM   8518  N  N   . GLY C 1 348 ? -3.632  57.738  12.013  1.00 54.53  ? 348  GLY C N   1 
ATOM   8519  C  CA  . GLY C 1 348 ? -4.533  57.110  12.964  1.00 43.37  ? 348  GLY C CA  1 
ATOM   8520  C  C   . GLY C 1 348 ? -4.990  55.774  12.410  1.00 41.37  ? 348  GLY C C   1 
ATOM   8521  O  O   . GLY C 1 348 ? -6.051  55.256  12.764  1.00 54.67  ? 348  GLY C O   1 
ATOM   8522  N  N   . PHE C 1 349 ? -4.174  55.222  11.524  1.00 20.08  ? 349  PHE C N   1 
ATOM   8523  C  CA  . PHE C 1 349 ? -4.421  53.908  10.969  1.00 35.52  ? 349  PHE C CA  1 
ATOM   8524  C  C   . PHE C 1 349 ? -3.497  52.822  11.555  1.00 38.03  ? 349  PHE C C   1 
ATOM   8525  O  O   . PHE C 1 349 ? -2.268  52.956  11.590  1.00 29.34  ? 349  PHE C O   1 
ATOM   8526  C  CB  . PHE C 1 349 ? -4.311  53.933  9.443   1.00 24.79  ? 349  PHE C CB  1 
ATOM   8527  C  CG  . PHE C 1 349 ? -4.967  52.761  8.787   1.00 28.28  ? 349  PHE C CG  1 
ATOM   8528  C  CD1 . PHE C 1 349 ? -6.291  52.834  8.376   1.00 21.83  ? 349  PHE C CD1 1 
ATOM   8529  C  CD2 . PHE C 1 349 ? -4.277  51.566  8.619   1.00 29.77  ? 349  PHE C CD2 1 
ATOM   8530  C  CE1 . PHE C 1 349 ? -6.910  51.747  7.798   1.00 27.07  ? 349  PHE C CE1 1 
ATOM   8531  C  CE2 . PHE C 1 349 ? -4.889  50.466  8.034   1.00 25.11  ? 349  PHE C CE2 1 
ATOM   8532  C  CZ  . PHE C 1 349 ? -6.206  50.554  7.626   1.00 26.14  ? 349  PHE C CZ  1 
ATOM   8533  N  N   . PRO C 1 350 ? -4.099  51.714  11.979  1.00 34.03  ? 350  PRO C N   1 
ATOM   8534  C  CA  . PRO C 1 350 ? -3.420  50.623  12.675  1.00 36.44  ? 350  PRO C CA  1 
ATOM   8535  C  C   . PRO C 1 350 ? -2.236  50.092  11.893  1.00 42.52  ? 350  PRO C C   1 
ATOM   8536  O  O   . PRO C 1 350 ? -2.319  49.942  10.672  1.00 28.80  ? 350  PRO C O   1 
ATOM   8537  C  CB  . PRO C 1 350 ? -4.499  49.534  12.753  1.00 32.60  ? 350  PRO C CB  1 
ATOM   8538  C  CG  . PRO C 1 350 ? -5.430  49.841  11.657  1.00 34.49  ? 350  PRO C CG  1 
ATOM   8539  C  CD  . PRO C 1 350 ? -5.461  51.340  11.576  1.00 34.61  ? 350  PRO C CD  1 
ATOM   8540  N  N   . ILE C 1 351 ? -1.147  49.803  12.602  1.00 44.82  ? 351  ILE C N   1 
ATOM   8541  C  CA  . ILE C 1 351 ? 0.004   49.146  12.000  1.00 30.89  ? 351  ILE C CA  1 
ATOM   8542  C  C   . ILE C 1 351 ? -0.008  47.681  12.391  1.00 35.93  ? 351  ILE C C   1 
ATOM   8543  O  O   . ILE C 1 351 ? 0.091   47.343  13.568  1.00 35.98  ? 351  ILE C O   1 
ATOM   8544  C  CB  . ILE C 1 351 ? 1.333   49.755  12.467  1.00 39.20  ? 351  ILE C CB  1 
ATOM   8545  C  CG1 . ILE C 1 351 ? 1.350   51.273  12.256  1.00 38.40  ? 351  ILE C CG1 1 
ATOM   8546  C  CG2 . ILE C 1 351 ? 2.504   49.097  11.733  1.00 33.59  ? 351  ILE C CG2 1 
ATOM   8547  C  CD1 . ILE C 1 351 ? 2.574   51.955  12.876  1.00 33.66  ? 351  ILE C CD1 1 
ATOM   8548  N  N   . ALA C 1 352 ? -0.142  46.811  11.399  1.00 33.23  ? 352  ALA C N   1 
ATOM   8549  C  CA  . ALA C 1 352 ? -0.166  45.378  11.641  1.00 32.23  ? 352  ALA C CA  1 
ATOM   8550  C  C   . ALA C 1 352 ? 1.257   44.841  11.809  1.00 45.34  ? 352  ALA C C   1 
ATOM   8551  O  O   . ALA C 1 352 ? 2.214   45.376  11.224  1.00 47.60  ? 352  ALA C O   1 
ATOM   8552  C  CB  . ALA C 1 352 ? -0.894  44.659  10.488  1.00 19.68  ? 352  ALA C CB  1 
ATOM   8553  N  N   . ASP C 1 353 ? 1.396   43.788  12.614  1.00 46.44  ? 353  ASP C N   1 
ATOM   8554  C  CA  . ASP C 1 353 ? 2.684   43.110  12.774  1.00 44.01  ? 353  ASP C CA  1 
ATOM   8555  C  C   . ASP C 1 353 ? 3.765   43.971  13.410  1.00 37.02  ? 353  ASP C C   1 
ATOM   8556  O  O   . ASP C 1 353 ? 4.950   43.676  13.284  1.00 45.47  ? 353  ASP C O   1 
ATOM   8557  C  CB  . ASP C 1 353 ? 3.192   42.592  11.432  1.00 45.85  ? 353  ASP C CB  1 
ATOM   8558  C  CG  . ASP C 1 353 ? 3.158   41.097  11.355  1.00 68.32  ? 353  ASP C CG  1 
ATOM   8559  O  OD1 . ASP C 1 353 ? 4.178   40.458  11.695  1.00 76.20  ? 353  ASP C OD1 1 
ATOM   8560  O  OD2 . ASP C 1 353 ? 2.098   40.563  10.973  1.00 83.10  ? 353  ASP C OD2 1 
ATOM   8561  N  N   . ALA C 1 354 ? 3.351   45.043  14.068  1.00 38.25  ? 354  ALA C N   1 
ATOM   8562  C  CA  . ALA C 1 354 ? 4.255   45.865  14.852  1.00 39.82  ? 354  ALA C CA  1 
ATOM   8563  C  C   . ALA C 1 354 ? 4.731   45.069  16.060  1.00 42.38  ? 354  ALA C C   1 
ATOM   8564  O  O   . ALA C 1 354 ? 4.115   44.087  16.459  1.00 41.56  ? 354  ALA C O   1 
ATOM   8565  C  CB  . ALA C 1 354 ? 3.550   47.143  15.299  1.00 32.31  ? 354  ALA C CB  1 
ATOM   8566  N  N   . ASN C 1 355 ? 5.833   45.489  16.652  1.00 40.62  ? 355  ASN C N   1 
ATOM   8567  C  CA  . ASN C 1 355 ? 6.280   44.842  17.860  1.00 42.02  ? 355  ASN C CA  1 
ATOM   8568  C  C   . ASN C 1 355 ? 6.142   45.761  19.058  1.00 43.88  ? 355  ASN C C   1 
ATOM   8569  O  O   . ASN C 1 355 ? 6.525   46.934  19.001  1.00 47.07  ? 355  ASN C O   1 
ATOM   8570  C  CB  . ASN C 1 355 ? 7.713   44.338  17.704  1.00 48.14  ? 355  ASN C CB  1 
ATOM   8571  C  CG  . ASN C 1 355 ? 7.786   43.054  16.906  1.00 47.45  ? 355  ASN C CG  1 
ATOM   8572  O  OD1 . ASN C 1 355 ? 8.380   43.012  15.829  1.00 55.36  ? 355  ASN C OD1 1 
ATOM   8573  N  ND2 . ASN C 1 355 ? 7.162   42.001  17.424  1.00 39.24  ? 355  ASN C ND2 1 
ATOM   8574  N  N   . VAL C 1 356 ? 5.563   45.224  20.131  1.00 29.31  ? 356  VAL C N   1 
ATOM   8575  C  CA  . VAL C 1 356 ? 5.518   45.910  21.416  1.00 32.17  ? 356  VAL C CA  1 
ATOM   8576  C  C   . VAL C 1 356 ? 6.436   45.246  22.458  1.00 39.58  ? 356  VAL C C   1 
ATOM   8577  O  O   . VAL C 1 356 ? 6.226   44.087  22.845  1.00 45.42  ? 356  VAL C O   1 
ATOM   8578  C  CB  . VAL C 1 356 ? 4.083   45.976  21.958  1.00 45.25  ? 356  VAL C CB  1 
ATOM   8579  C  CG1 . VAL C 1 356 ? 4.073   46.579  23.371  1.00 43.27  ? 356  VAL C CG1 1 
ATOM   8580  C  CG2 . VAL C 1 356 ? 3.189   46.770  20.997  1.00 37.57  ? 356  VAL C CG2 1 
ATOM   8581  N  N   . TYR C 1 357 ? 7.452   45.987  22.904  1.00 39.43  ? 357  TYR C N   1 
ATOM   8582  C  CA  . TYR C 1 357 ? 8.428   45.482  23.868  1.00 39.43  ? 357  TYR C CA  1 
ATOM   8583  C  C   . TYR C 1 357 ? 8.237   46.051  25.279  1.00 47.31  ? 357  TYR C C   1 
ATOM   8584  O  O   . TYR C 1 357 ? 7.904   47.236  25.447  1.00 33.94  ? 357  TYR C O   1 
ATOM   8585  C  CB  . TYR C 1 357 ? 9.857   45.817  23.426  1.00 39.15  ? 357  TYR C CB  1 
ATOM   8586  C  CG  . TYR C 1 357 ? 10.396  45.080  22.208  1.00 45.84  ? 357  TYR C CG  1 
ATOM   8587  C  CD1 . TYR C 1 357 ? 10.389  45.674  20.944  1.00 45.55  ? 357  TYR C CD1 1 
ATOM   8588  C  CD2 . TYR C 1 357 ? 10.959  43.812  22.327  1.00 43.28  ? 357  TYR C CD2 1 
ATOM   8589  C  CE1 . TYR C 1 357 ? 10.913  45.017  19.830  1.00 37.03  ? 357  TYR C CE1 1 
ATOM   8590  C  CE2 . TYR C 1 357 ? 11.481  43.149  21.219  1.00 33.79  ? 357  TYR C CE2 1 
ATOM   8591  C  CZ  . TYR C 1 357 ? 11.452  43.755  19.979  1.00 35.26  ? 357  TYR C CZ  1 
ATOM   8592  O  OH  . TYR C 1 357 ? 11.964  43.082  18.897  1.00 47.84  ? 357  TYR C OH  1 
ATOM   8593  N  N   . VAL C 1 358 ? 8.484   45.199  26.280  1.00 57.60  ? 358  VAL C N   1 
ATOM   8594  C  CA  . VAL C 1 358 ? 8.587   45.606  27.685  1.00 49.66  ? 358  VAL C CA  1 
ATOM   8595  C  C   . VAL C 1 358 ? 10.023  45.392  28.210  1.00 50.71  ? 358  VAL C C   1 
ATOM   8596  O  O   . VAL C 1 358 ? 10.602  44.316  28.029  1.00 48.50  ? 358  VAL C O   1 
ATOM   8597  C  CB  . VAL C 1 358 ? 7.603   44.803  28.569  1.00 39.57  ? 358  VAL C CB  1 
ATOM   8598  C  CG1 . VAL C 1 358 ? 7.793   45.138  30.062  1.00 36.94  ? 358  VAL C CG1 1 
ATOM   8599  C  CG2 . VAL C 1 358 ? 6.162   45.041  28.124  1.00 32.05  ? 358  VAL C CG2 1 
ATOM   8600  N  N   . ALA C 1 359 ? 10.595  46.414  28.850  1.00 53.52  ? 359  ALA C N   1 
ATOM   8601  C  CA  . ALA C 1 359 ? 11.940  46.310  29.453  1.00 55.10  ? 359  ALA C CA  1 
ATOM   8602  C  C   . ALA C 1 359 ? 12.072  45.110  30.383  1.00 42.08  ? 359  ALA C C   1 
ATOM   8603  O  O   . ALA C 1 359 ? 11.390  45.023  31.405  1.00 41.30  ? 359  ALA C O   1 
ATOM   8604  C  CB  . ALA C 1 359 ? 12.306  47.587  30.208  1.00 48.51  ? 359  ALA C CB  1 
ATOM   8605  N  N   . GLY C 1 360 ? 12.957  44.188  30.026  1.00 38.20  ? 360  GLY C N   1 
ATOM   8606  C  CA  . GLY C 1 360 ? 13.163  43.000  30.826  1.00 33.41  ? 360  GLY C CA  1 
ATOM   8607  C  C   . GLY C 1 360 ? 12.343  41.836  30.316  1.00 38.48  ? 360  GLY C C   1 
ATOM   8608  O  O   . GLY C 1 360 ? 12.413  40.725  30.847  1.00 54.99  ? 360  GLY C O   1 
ATOM   8609  N  N   . LEU C 1 361 ? 11.557  42.096  29.279  1.00 35.95  ? 361  LEU C N   1 
ATOM   8610  C  CA  . LEU C 1 361 ? 10.759  41.061  28.632  1.00 40.26  ? 361  LEU C CA  1 
ATOM   8611  C  C   . LEU C 1 361 ? 10.847  41.241  27.116  1.00 47.00  ? 361  LEU C C   1 
ATOM   8612  O  O   . LEU C 1 361 ? 9.936   40.866  26.369  1.00 35.58  ? 361  LEU C O   1 
ATOM   8613  C  CB  . LEU C 1 361 ? 9.305   41.141  29.101  1.00 30.24  ? 361  LEU C CB  1 
ATOM   8614  C  CG  . LEU C 1 361 ? 9.075   40.927  30.598  1.00 34.05  ? 361  LEU C CG  1 
ATOM   8615  C  CD1 . LEU C 1 361 ? 7.661   41.289  30.943  1.00 36.86  ? 361  LEU C CD1 1 
ATOM   8616  C  CD2 . LEU C 1 361 ? 9.365   39.492  31.001  1.00 33.26  ? 361  LEU C CD2 1 
ATOM   8617  N  N   . GLU C 1 362 ? 11.961  41.822  26.679  1.00 51.34  ? 362  GLU C N   1 
ATOM   8618  C  CA  . GLU C 1 362 ? 12.177  42.157  25.275  1.00 43.16  ? 362  GLU C CA  1 
ATOM   8619  C  C   . GLU C 1 362 ? 12.339  40.931  24.386  1.00 45.90  ? 362  GLU C C   1 
ATOM   8620  O  O   . GLU C 1 362 ? 12.184  41.019  23.169  1.00 40.39  ? 362  GLU C O   1 
ATOM   8621  C  CB  . GLU C 1 362 ? 13.381  43.090  25.130  1.00 39.52  ? 362  GLU C CB  1 
ATOM   8622  C  CG  . GLU C 1 362 ? 13.005  44.561  25.110  1.00 61.01  ? 362  GLU C CG  1 
ATOM   8623  C  CD  . GLU C 1 362 ? 13.869  45.402  26.027  1.00 82.31  ? 362  GLU C CD  1 
ATOM   8624  O  OE1 . GLU C 1 362 ? 14.342  44.868  27.059  1.00 87.34  ? 362  GLU C OE1 1 
ATOM   8625  O  OE2 . GLU C 1 362 ? 14.060  46.599  25.721  1.00 83.78  ? 362  GLU C OE2 1 
ATOM   8626  N  N   . GLU C 1 363 ? 12.630  39.785  24.994  1.00 48.83  ? 363  GLU C N   1 
ATOM   8627  C  CA  . GLU C 1 363 ? 12.788  38.553  24.231  1.00 41.44  ? 363  GLU C CA  1 
ATOM   8628  C  C   . GLU C 1 363 ? 11.453  38.021  23.754  1.00 31.71  ? 363  GLU C C   1 
ATOM   8629  O  O   . GLU C 1 363 ? 11.412  37.203  22.847  1.00 39.34  ? 363  GLU C O   1 
ATOM   8630  C  CB  . GLU C 1 363 ? 13.543  37.489  25.039  1.00 57.74  ? 363  GLU C CB  1 
ATOM   8631  C  CG  . GLU C 1 363 ? 15.050  37.728  25.092  1.00 74.72  ? 363  GLU C CG  1 
ATOM   8632  C  CD  . GLU C 1 363 ? 15.796  36.668  25.877  1.00 85.04  ? 363  GLU C CD  1 
ATOM   8633  O  OE1 . GLU C 1 363 ? 15.482  36.465  27.069  1.00 76.84  ? 363  GLU C OE1 1 
ATOM   8634  O  OE2 . GLU C 1 363 ? 16.710  36.047  25.300  1.00 95.69  ? 363  GLU C OE2 1 
ATOM   8635  N  N   . LYS C 1 364 ? 10.363  38.480  24.367  1.00 38.89  ? 364  LYS C N   1 
ATOM   8636  C  CA  . LYS C 1 364 ? 9.025   38.038  23.968  1.00 36.54  ? 364  LYS C CA  1 
ATOM   8637  C  C   . LYS C 1 364 ? 8.089   39.215  23.660  1.00 36.63  ? 364  LYS C C   1 
ATOM   8638  O  O   . LYS C 1 364 ? 7.171   39.520  24.421  1.00 52.32  ? 364  LYS C O   1 
ATOM   8639  C  CB  . LYS C 1 364 ? 8.420   37.114  25.030  1.00 41.78  ? 364  LYS C CB  1 
ATOM   8640  C  CG  . LYS C 1 364 ? 7.044   36.575  24.671  1.00 37.13  ? 364  LYS C CG  1 
ATOM   8641  C  CD  . LYS C 1 364 ? 7.059   35.916  23.315  1.00 31.31  ? 364  LYS C CD  1 
ATOM   8642  C  CE  . LYS C 1 364 ? 5.718   35.237  23.028  1.00 34.49  ? 364  LYS C CE  1 
ATOM   8643  N  NZ  . LYS C 1 364 ? 5.566   34.864  21.597  1.00 25.34  ? 364  LYS C NZ  1 
ATOM   8644  N  N   . PRO C 1 365 ? 8.328   39.881  22.526  1.00 44.54  ? 365  PRO C N   1 
ATOM   8645  C  CA  . PRO C 1 365 ? 7.521   41.013  22.054  1.00 41.20  ? 365  PRO C CA  1 
ATOM   8646  C  C   . PRO C 1 365 ? 6.141   40.534  21.617  1.00 47.95  ? 365  PRO C C   1 
ATOM   8647  O  O   . PRO C 1 365 ? 5.973   39.348  21.300  1.00 50.43  ? 365  PRO C O   1 
ATOM   8648  C  CB  . PRO C 1 365 ? 8.289   41.517  20.818  1.00 52.26  ? 365  PRO C CB  1 
ATOM   8649  C  CG  . PRO C 1 365 ? 9.550   40.676  20.701  1.00 50.20  ? 365  PRO C CG  1 
ATOM   8650  C  CD  . PRO C 1 365 ? 9.335   39.452  21.539  1.00 56.51  ? 365  PRO C CD  1 
ATOM   8651  N  N   . MET C 1 366 ? 5.169   41.440  21.598  1.00 42.65  ? 366  MET C N   1 
ATOM   8652  C  CA  . MET C 1 366 ? 3.844   41.125  21.064  1.00 34.00  ? 366  MET C CA  1 
ATOM   8653  C  C   . MET C 1 366 ? 3.733   41.611  19.619  1.00 29.63  ? 366  MET C C   1 
ATOM   8654  O  O   . MET C 1 366 ? 4.106   42.738  19.314  1.00 45.22  ? 366  MET C O   1 
ATOM   8655  C  CB  . MET C 1 366 ? 2.738   41.750  21.930  1.00 38.02  ? 366  MET C CB  1 
ATOM   8656  C  CG  . MET C 1 366 ? 2.568   41.130  23.337  1.00 34.44  ? 366  MET C CG  1 
ATOM   8657  S  SD  . MET C 1 366 ? 2.221   39.334  23.368  1.00 40.52  ? 366  MET C SD  1 
ATOM   8658  C  CE  . MET C 1 366 ? 3.815   38.675  23.854  1.00 33.13  ? 366  MET C CE  1 
ATOM   8659  N  N   . ARG C 1 367 ? 3.245   40.754  18.728  1.00 26.02  ? 367  ARG C N   1 
ATOM   8660  C  CA  . ARG C 1 367 ? 3.020   41.153  17.341  1.00 34.89  ? 367  ARG C CA  1 
ATOM   8661  C  C   . ARG C 1 367 ? 1.567   41.612  17.159  1.00 41.84  ? 367  ARG C C   1 
ATOM   8662  O  O   . ARG C 1 367 ? 0.637   40.812  17.288  1.00 55.45  ? 367  ARG C O   1 
ATOM   8663  C  CB  . ARG C 1 367 ? 3.361   40.005  16.384  1.00 44.15  ? 367  ARG C CB  1 
ATOM   8664  C  CG  . ARG C 1 367 ? 3.496   40.402  14.893  1.00 51.75  ? 367  ARG C CG  1 
ATOM   8665  C  CD  . ARG C 1 367 ? 2.268   39.995  14.038  1.00 74.04  ? 367  ARG C CD  1 
ATOM   8666  N  NE  . ARG C 1 367 ? 1.898   38.594  14.206  1.00 83.07  ? 367  ARG C NE  1 
ATOM   8667  C  CZ  . ARG C 1 367 ? 2.027   37.607  13.320  1.00 86.38  ? 367  ARG C CZ  1 
ATOM   8668  N  NH1 . ARG C 1 367 ? 1.642   36.398  13.681  1.00 93.50  ? 367  ARG C NH1 1 
ATOM   8669  N  NH2 . ARG C 1 367 ? 2.518   37.793  12.103  1.00 86.21  ? 367  ARG C NH2 1 
ATOM   8670  N  N   . THR C 1 368 ? 1.370   42.901  16.882  1.00 25.91  ? 368  THR C N   1 
ATOM   8671  C  CA  . THR C 1 368 ? 0.021   43.443  16.775  1.00 25.16  ? 368  THR C CA  1 
ATOM   8672  C  C   . THR C 1 368 ? -0.780  42.731  15.700  1.00 27.30  ? 368  THR C C   1 
ATOM   8673  O  O   . THR C 1 368 ? -0.225  42.192  14.737  1.00 22.73  ? 368  THR C O   1 
ATOM   8674  C  CB  . THR C 1 368 ? 0.004   44.951  16.448  1.00 21.74  ? 368  THR C CB  1 
ATOM   8675  O  OG1 . THR C 1 368 ? 0.526   45.163  15.129  1.00 25.99  ? 368  THR C OG1 1 
ATOM   8676  C  CG2 . THR C 1 368 ? 0.809   45.738  17.474  1.00 21.15  ? 368  THR C CG2 1 
ATOM   8677  N  N   . SER C 1 369 ? -2.093  42.746  15.880  1.00 25.04  ? 369  SER C N   1 
ATOM   8678  C  CA  . SER C 1 369 ? -3.018  42.176  14.918  1.00 31.71  ? 369  SER C CA  1 
ATOM   8679  C  C   . SER C 1 369 ? -3.170  43.082  13.696  1.00 37.51  ? 369  SER C C   1 
ATOM   8680  O  O   . SER C 1 369 ? -2.542  44.141  13.607  1.00 45.17  ? 369  SER C O   1 
ATOM   8681  C  CB  . SER C 1 369 ? -4.374  41.994  15.577  1.00 28.58  ? 369  SER C CB  1 
ATOM   8682  O  OG  . SER C 1 369 ? -4.899  43.257  15.923  1.00 35.57  ? 369  SER C OG  1 
ATOM   8683  N  N   . LYS C 1 370 ? -4.002  42.650  12.752  1.00 32.32  ? 370  LYS C N   1 
ATOM   8684  C  CA  . LYS C 1 370 ? -4.273  43.415  11.544  1.00 28.70  ? 370  LYS C CA  1 
ATOM   8685  C  C   . LYS C 1 370 ? -4.840  44.801  11.872  1.00 34.66  ? 370  LYS C C   1 
ATOM   8686  O  O   . LYS C 1 370 ? -4.719  45.744  11.082  1.00 48.11  ? 370  LYS C O   1 
ATOM   8687  C  CB  . LYS C 1 370 ? -5.227  42.632  10.643  1.00 23.08  ? 370  LYS C CB  1 
ATOM   8688  C  CG  . LYS C 1 370 ? -4.596  41.371  10.056  1.00 30.89  ? 370  LYS C CG  1 
ATOM   8689  C  CD  . LYS C 1 370 ? -5.588  40.487  9.264   1.00 28.97  ? 370  LYS C CD  1 
ATOM   8690  C  CE  . LYS C 1 370 ? -4.894  39.172  8.859   1.00 30.72  ? 370  LYS C CE  1 
ATOM   8691  N  NZ  . LYS C 1 370 ? -5.765  38.173  8.175   1.00 38.70  ? 370  LYS C NZ  1 
ATOM   8692  N  N   . ARG C 1 371 ? -5.449  44.923  13.049  1.00 26.55  ? 371  ARG C N   1 
ATOM   8693  C  CA  . ARG C 1 371 ? -6.025  46.191  13.476  1.00 33.28  ? 371  ARG C CA  1 
ATOM   8694  C  C   . ARG C 1 371 ? -5.059  46.913  14.430  1.00 36.82  ? 371  ARG C C   1 
ATOM   8695  O  O   . ARG C 1 371 ? -5.404  47.931  15.038  1.00 39.42  ? 371  ARG C O   1 
ATOM   8696  C  CB  . ARG C 1 371 ? -7.436  45.993  14.066  1.00 32.01  ? 371  ARG C CB  1 
ATOM   8697  C  CG  . ARG C 1 371 ? -8.298  45.020  13.220  1.00 34.93  ? 371  ARG C CG  1 
ATOM   8698  C  CD  . ARG C 1 371 ? -9.837  45.246  13.272  1.00 49.81  ? 371  ARG C CD  1 
ATOM   8699  N  NE  . ARG C 1 371 ? -10.425 44.926  14.568  1.00 61.78  ? 371  ARG C NE  1 
ATOM   8700  C  CZ  . ARG C 1 371 ? -11.205 43.887  14.880  1.00 69.80  ? 371  ARG C CZ  1 
ATOM   8701  N  NH1 . ARG C 1 371 ? -11.618 43.784  16.133  1.00 57.47  ? 371  ARG C NH1 1 
ATOM   8702  N  NH2 . ARG C 1 371 ? -11.579 42.966  13.992  1.00 79.52  ? 371  ARG C NH2 1 
ATOM   8703  N  N   . GLY C 1 372 ? -3.834  46.398  14.514  1.00 31.72  ? 372  GLY C N   1 
ATOM   8704  C  CA  . GLY C 1 372 ? -2.776  47.022  15.291  1.00 36.96  ? 372  GLY C CA  1 
ATOM   8705  C  C   . GLY C 1 372 ? -2.983  46.855  16.786  1.00 35.97  ? 372  GLY C C   1 
ATOM   8706  O  O   . GLY C 1 372 ? -2.455  47.629  17.594  1.00 32.31  ? 372  GLY C O   1 
ATOM   8707  N  N   . GLU C 1 373 ? -3.757  45.842  17.163  1.00 27.84  ? 373  GLU C N   1 
ATOM   8708  C  CA  . GLU C 1 373 ? -4.045  45.627  18.566  1.00 32.67  ? 373  GLU C CA  1 
ATOM   8709  C  C   . GLU C 1 373 ? -3.037  44.694  19.174  1.00 35.99  ? 373  GLU C C   1 
ATOM   8710  O  O   . GLU C 1 373 ? -2.527  43.790  18.510  1.00 39.00  ? 373  GLU C O   1 
ATOM   8711  C  CB  . GLU C 1 373 ? -5.419  45.014  18.766  1.00 30.83  ? 373  GLU C CB  1 
ATOM   8712  C  CG  . GLU C 1 373 ? -6.318  45.100  17.578  1.00 36.05  ? 373  GLU C CG  1 
ATOM   8713  C  CD  . GLU C 1 373 ? -7.489  44.170  17.712  1.00 37.24  ? 373  GLU C CD  1 
ATOM   8714  O  OE1 . GLU C 1 373 ? -8.324  44.437  18.603  1.00 30.94  ? 373  GLU C OE1 1 
ATOM   8715  O  OE2 . GLU C 1 373 ? -7.564  43.172  16.948  1.00 32.78  ? 373  GLU C OE2 1 
ATOM   8716  N  N   . TYR C 1 374 ? -2.788  44.909  20.458  1.00 34.40  ? 374  TYR C N   1 
ATOM   8717  C  CA  . TYR C 1 374 ? -1.927  44.044  21.229  1.00 37.07  ? 374  TYR C CA  1 
ATOM   8718  C  C   . TYR C 1 374 ? -2.458  43.920  22.648  1.00 44.74  ? 374  TYR C C   1 
ATOM   8719  O  O   . TYR C 1 374 ? -3.037  44.866  23.199  1.00 41.61  ? 374  TYR C O   1 
ATOM   8720  C  CB  . TYR C 1 374 ? -0.512  44.605  21.273  1.00 26.80  ? 374  TYR C CB  1 
ATOM   8721  C  CG  . TYR C 1 374 ? -0.303  45.722  22.277  1.00 33.51  ? 374  TYR C CG  1 
ATOM   8722  C  CD1 . TYR C 1 374 ? -0.462  47.058  21.909  1.00 27.21  ? 374  TYR C CD1 1 
ATOM   8723  C  CD2 . TYR C 1 374 ? 0.074   45.444  23.592  1.00 39.45  ? 374  TYR C CD2 1 
ATOM   8724  C  CE1 . TYR C 1 374 ? -0.266  48.076  22.810  1.00 31.57  ? 374  TYR C CE1 1 
ATOM   8725  C  CE2 . TYR C 1 374 ? 0.278   46.470  24.509  1.00 31.59  ? 374  TYR C CE2 1 
ATOM   8726  C  CZ  . TYR C 1 374 ? 0.101   47.777  24.108  1.00 32.83  ? 374  TYR C CZ  1 
ATOM   8727  O  OH  . TYR C 1 374 ? 0.293   48.789  25.005  1.00 32.91  ? 374  TYR C OH  1 
ATOM   8728  N  N   . TRP C 1 375 ? -2.261  42.742  23.229  1.00 38.92  ? 375  TRP C N   1 
ATOM   8729  C  CA  . TRP C 1 375 ? -2.485  42.549  24.643  1.00 26.66  ? 375  TRP C CA  1 
ATOM   8730  C  C   . TRP C 1 375 ? -1.214  41.992  25.222  1.00 29.99  ? 375  TRP C C   1 
ATOM   8731  O  O   . TRP C 1 375 ? -0.722  40.965  24.760  1.00 34.17  ? 375  TRP C O   1 
ATOM   8732  C  CB  . TRP C 1 375 ? -3.606  41.559  24.881  1.00 23.45  ? 375  TRP C CB  1 
ATOM   8733  C  CG  . TRP C 1 375 ? -4.866  41.875  24.128  1.00 23.74  ? 375  TRP C CG  1 
ATOM   8734  C  CD1 . TRP C 1 375 ? -6.034  42.381  24.637  1.00 29.51  ? 375  TRP C CD1 1 
ATOM   8735  C  CD2 . TRP C 1 375 ? -5.089  41.688  22.734  1.00 27.99  ? 375  TRP C CD2 1 
ATOM   8736  N  NE1 . TRP C 1 375 ? -6.972  42.514  23.642  1.00 20.55  ? 375  TRP C NE1 1 
ATOM   8737  C  CE2 . TRP C 1 375 ? -6.418  42.092  22.463  1.00 32.78  ? 375  TRP C CE2 1 
ATOM   8738  C  CE3 . TRP C 1 375 ? -4.300  41.214  21.682  1.00 29.04  ? 375  TRP C CE3 1 
ATOM   8739  C  CZ2 . TRP C 1 375 ? -6.968  42.041  21.180  1.00 26.28  ? 375  TRP C CZ2 1 
ATOM   8740  C  CZ3 . TRP C 1 375 ? -4.845  41.166  20.414  1.00 24.01  ? 375  TRP C CZ3 1 
ATOM   8741  C  CH2 . TRP C 1 375 ? -6.170  41.575  20.173  1.00 20.59  ? 375  TRP C CH2 1 
ATOM   8742  N  N   . ARG C 1 376 ? -0.682  42.675  26.231  1.00 37.18  ? 376  ARG C N   1 
ATOM   8743  C  CA  . ARG C 1 376 ? 0.468   42.179  26.969  1.00 31.40  ? 376  ARG C CA  1 
ATOM   8744  C  C   . ARG C 1 376 ? 0.049   41.820  28.391  1.00 36.99  ? 376  ARG C C   1 
ATOM   8745  O  O   . ARG C 1 376 ? -0.292  42.698  29.191  1.00 30.59  ? 376  ARG C O   1 
ATOM   8746  C  CB  . ARG C 1 376 ? 1.584   43.221  26.972  1.00 36.01  ? 376  ARG C CB  1 
ATOM   8747  C  CG  . ARG C 1 376 ? 2.873   42.773  27.638  1.00 43.53  ? 376  ARG C CG  1 
ATOM   8748  C  CD  . ARG C 1 376 ? 3.559   41.613  26.926  1.00 38.80  ? 376  ARG C CD  1 
ATOM   8749  N  NE  . ARG C 1 376 ? 4.703   41.141  27.704  1.00 47.09  ? 376  ARG C NE  1 
ATOM   8750  C  CZ  . ARG C 1 376 ? 5.354   40.007  27.476  1.00 50.97  ? 376  ARG C CZ  1 
ATOM   8751  N  NH1 . ARG C 1 376 ? 4.981   39.214  26.485  1.00 59.46  ? 376  ARG C NH1 1 
ATOM   8752  N  NH2 . ARG C 1 376 ? 6.384   39.672  28.237  1.00 59.22  ? 376  ARG C NH2 1 
ATOM   8753  N  N   . LEU C 1 377 ? 0.035   40.518  28.681  1.00 33.74  ? 377  LEU C N   1 
ATOM   8754  C  CA  . LEU C 1 377 ? -0.283  40.041  30.016  1.00 33.55  ? 377  LEU C CA  1 
ATOM   8755  C  C   . LEU C 1 377 ? 0.875   40.392  30.935  1.00 36.17  ? 377  LEU C C   1 
ATOM   8756  O  O   . LEU C 1 377 ? 2.027   40.142  30.604  1.00 39.33  ? 377  LEU C O   1 
ATOM   8757  C  CB  . LEU C 1 377 ? -0.515  38.531  30.014  1.00 30.05  ? 377  LEU C CB  1 
ATOM   8758  C  CG  . LEU C 1 377 ? -1.564  38.002  29.031  1.00 36.25  ? 377  LEU C CG  1 
ATOM   8759  C  CD1 . LEU C 1 377 ? -1.861  36.522  29.317  1.00 21.41  ? 377  LEU C CD1 1 
ATOM   8760  C  CD2 . LEU C 1 377 ? -2.856  38.843  29.035  1.00 25.58  ? 377  LEU C CD2 1 
ATOM   8761  N  N   . LEU C 1 378 ? 0.574   40.980  32.087  1.00 41.73  ? 378  LEU C N   1 
ATOM   8762  C  CA  . LEU C 1 378 ? 1.623   41.384  33.011  1.00 35.60  ? 378  LEU C CA  1 
ATOM   8763  C  C   . LEU C 1 378 ? 1.231   41.145  34.473  1.00 33.89  ? 378  LEU C C   1 
ATOM   8764  O  O   . LEU C 1 378 ? 0.089   41.350  34.880  1.00 38.30  ? 378  LEU C O   1 
ATOM   8765  C  CB  . LEU C 1 378 ? 1.972   42.863  32.804  1.00 30.60  ? 378  LEU C CB  1 
ATOM   8766  C  CG  . LEU C 1 378 ? 2.709   43.323  31.549  1.00 25.90  ? 378  LEU C CG  1 
ATOM   8767  C  CD1 . LEU C 1 378 ? 2.794   44.853  31.510  1.00 26.85  ? 378  LEU C CD1 1 
ATOM   8768  C  CD2 . LEU C 1 378 ? 4.096   42.719  31.507  1.00 26.11  ? 378  LEU C CD2 1 
ATOM   8769  N  N   . THR C 1 379 ? 2.202   40.694  35.249  1.00 41.93  ? 379  THR C N   1 
ATOM   8770  C  CA  . THR C 1 379 ? 2.122   40.696  36.701  1.00 47.90  ? 379  THR C CA  1 
ATOM   8771  C  C   . THR C 1 379 ? 2.061   42.144  37.193  1.00 54.10  ? 379  THR C C   1 
ATOM   8772  O  O   . THR C 1 379 ? 2.545   43.061  36.514  1.00 44.37  ? 379  THR C O   1 
ATOM   8773  C  CB  . THR C 1 379 ? 3.387   40.030  37.272  1.00 54.78  ? 379  THR C CB  1 
ATOM   8774  O  OG1 . THR C 1 379 ? 3.305   38.620  37.048  1.00 60.95  ? 379  THR C OG1 1 
ATOM   8775  C  CG2 . THR C 1 379 ? 3.560   40.306  38.760  1.00 61.54  ? 379  THR C CG2 1 
ATOM   8776  N  N   . PRO C 1 380 ? 1.459   42.364  38.369  1.00 44.36  ? 380  PRO C N   1 
ATOM   8777  C  CA  . PRO C 1 380 ? 1.505   43.713  38.939  1.00 36.12  ? 380  PRO C CA  1 
ATOM   8778  C  C   . PRO C 1 380 ? 2.955   44.260  39.035  1.00 49.86  ? 380  PRO C C   1 
ATOM   8779  O  O   . PRO C 1 380 ? 3.923   43.495  39.181  1.00 37.25  ? 380  PRO C O   1 
ATOM   8780  C  CB  . PRO C 1 380 ? 0.886   43.509  40.323  1.00 39.43  ? 380  PRO C CB  1 
ATOM   8781  C  CG  . PRO C 1 380 ? -0.074  42.347  40.123  1.00 37.70  ? 380  PRO C CG  1 
ATOM   8782  C  CD  . PRO C 1 380 ? 0.638   41.436  39.173  1.00 37.72  ? 380  PRO C CD  1 
ATOM   8783  N  N   . GLY C 1 381 ? 3.092   45.583  38.941  1.00 49.14  ? 381  GLY C N   1 
ATOM   8784  C  CA  . GLY C 1 381 ? 4.392   46.238  38.891  1.00 40.73  ? 381  GLY C CA  1 
ATOM   8785  C  C   . GLY C 1 381 ? 4.389   47.404  37.909  1.00 48.14  ? 381  GLY C C   1 
ATOM   8786  O  O   . GLY C 1 381 ? 3.361   47.688  37.282  1.00 53.83  ? 381  GLY C O   1 
ATOM   8787  N  N   . LEU C 1 382 ? 5.518   48.097  37.767  1.00 40.13  ? 382  LEU C N   1 
ATOM   8788  C  CA  . LEU C 1 382 ? 5.575   49.205  36.813  1.00 40.33  ? 382  LEU C CA  1 
ATOM   8789  C  C   . LEU C 1 382 ? 6.571   48.910  35.708  1.00 46.28  ? 382  LEU C C   1 
ATOM   8790  O  O   . LEU C 1 382 ? 7.640   48.356  35.976  1.00 43.29  ? 382  LEU C O   1 
ATOM   8791  C  CB  . LEU C 1 382 ? 5.901   50.529  37.507  1.00 51.93  ? 382  LEU C CB  1 
ATOM   8792  C  CG  . LEU C 1 382 ? 7.298   50.777  38.083  1.00 69.59  ? 382  LEU C CG  1 
ATOM   8793  C  CD1 . LEU C 1 382 ? 8.335   51.057  36.995  1.00 79.87  ? 382  LEU C CD1 1 
ATOM   8794  C  CD2 . LEU C 1 382 ? 7.234   51.940  39.044  1.00 80.90  ? 382  LEU C CD2 1 
ATOM   8795  N  N   . TYR C 1 383 ? 6.224   49.294  34.477  1.00 47.69  ? 383  TYR C N   1 
ATOM   8796  C  CA  . TYR C 1 383 ? 6.990   48.896  33.291  1.00 39.75  ? 383  TYR C CA  1 
ATOM   8797  C  C   . TYR C 1 383 ? 7.213   50.036  32.297  1.00 43.80  ? 383  TYR C C   1 
ATOM   8798  O  O   . TYR C 1 383 ? 6.406   50.960  32.204  1.00 54.30  ? 383  TYR C O   1 
ATOM   8799  C  CB  . TYR C 1 383 ? 6.271   47.763  32.559  1.00 43.42  ? 383  TYR C CB  1 
ATOM   8800  C  CG  . TYR C 1 383 ? 5.855   46.584  33.427  1.00 54.61  ? 383  TYR C CG  1 
ATOM   8801  C  CD1 . TYR C 1 383 ? 4.774   46.673  34.306  1.00 49.71  ? 383  TYR C CD1 1 
ATOM   8802  C  CD2 . TYR C 1 383 ? 6.526   45.369  33.343  1.00 54.08  ? 383  TYR C CD2 1 
ATOM   8803  C  CE1 . TYR C 1 383 ? 4.398   45.587  35.091  1.00 47.60  ? 383  TYR C CE1 1 
ATOM   8804  C  CE2 . TYR C 1 383 ? 6.149   44.281  34.116  1.00 45.49  ? 383  TYR C CE2 1 
ATOM   8805  C  CZ  . TYR C 1 383 ? 5.093   44.393  34.983  1.00 47.78  ? 383  TYR C CZ  1 
ATOM   8806  O  OH  . TYR C 1 383 ? 4.750   43.297  35.734  1.00 42.08  ? 383  TYR C OH  1 
ATOM   8807  N  N   . SER C 1 384 ? 8.306   49.953  31.544  1.00 46.46  ? 384  SER C N   1 
ATOM   8808  C  CA  . SER C 1 384 ? 8.547   50.862  30.419  1.00 49.80  ? 384  SER C CA  1 
ATOM   8809  C  C   . SER C 1 384 ? 8.301   50.134  29.101  1.00 56.22  ? 384  SER C C   1 
ATOM   8810  O  O   . SER C 1 384 ? 9.140   49.355  28.630  1.00 45.97  ? 384  SER C O   1 
ATOM   8811  C  CB  . SER C 1 384 ? 9.967   51.434  30.450  1.00 46.52  ? 384  SER C CB  1 
ATOM   8812  O  OG  . SER C 1 384 ? 10.039  52.586  31.280  1.00 76.01  ? 384  SER C OG  1 
ATOM   8813  N  N   . VAL C 1 385 ? 7.138   50.387  28.517  1.00 52.23  ? 385  VAL C N   1 
ATOM   8814  C  CA  . VAL C 1 385 ? 6.737   49.725  27.289  1.00 45.45  ? 385  VAL C CA  1 
ATOM   8815  C  C   . VAL C 1 385 ? 7.098   50.602  26.089  1.00 44.61  ? 385  VAL C C   1 
ATOM   8816  O  O   . VAL C 1 385 ? 7.023   51.831  26.167  1.00 48.69  ? 385  VAL C O   1 
ATOM   8817  C  CB  . VAL C 1 385 ? 5.215   49.489  27.303  1.00 41.46  ? 385  VAL C CB  1 
ATOM   8818  C  CG1 . VAL C 1 385 ? 4.815   48.438  26.283  1.00 41.62  ? 385  VAL C CG1 1 
ATOM   8819  C  CG2 . VAL C 1 385 ? 4.762   49.088  28.688  1.00 39.35  ? 385  VAL C CG2 1 
ATOM   8820  N  N   . HIS C 1 386 ? 7.504   49.981  24.987  1.00 32.10  ? 386  HIS C N   1 
ATOM   8821  C  CA  . HIS C 1 386 ? 7.674   50.715  23.730  1.00 36.86  ? 386  HIS C CA  1 
ATOM   8822  C  C   . HIS C 1 386 ? 7.350   49.844  22.518  1.00 40.86  ? 386  HIS C C   1 
ATOM   8823  O  O   . HIS C 1 386 ? 7.354   48.616  22.610  1.00 33.18  ? 386  HIS C O   1 
ATOM   8824  C  CB  . HIS C 1 386 ? 9.074   51.348  23.604  1.00 52.11  ? 386  HIS C CB  1 
ATOM   8825  C  CG  . HIS C 1 386 ? 10.170  50.380  23.255  1.00 68.66  ? 386  HIS C CG  1 
ATOM   8826  N  ND1 . HIS C 1 386 ? 9.975   49.017  23.165  1.00 82.18  ? 386  HIS C ND1 1 
ATOM   8827  C  CD2 . HIS C 1 386 ? 11.481  50.589  22.983  1.00 64.38  ? 386  HIS C CD2 1 
ATOM   8828  C  CE1 . HIS C 1 386 ? 11.117  48.430  22.846  1.00 59.77  ? 386  HIS C CE1 1 
ATOM   8829  N  NE2 . HIS C 1 386 ? 12.043  49.361  22.728  1.00 51.01  ? 386  HIS C NE2 1 
ATOM   8830  N  N   . ALA C 1 387 ? 7.064   50.487  21.388  1.00 44.27  ? 387  ALA C N   1 
ATOM   8831  C  CA  . ALA C 1 387 ? 6.701   49.773  20.166  1.00 40.41  ? 387  ALA C CA  1 
ATOM   8832  C  C   . ALA C 1 387 ? 7.670   50.097  19.041  1.00 48.06  ? 387  ALA C C   1 
ATOM   8833  O  O   . ALA C 1 387 ? 8.294   51.166  19.007  1.00 50.08  ? 387  ALA C O   1 
ATOM   8834  C  CB  . ALA C 1 387 ? 5.273   50.103  19.749  1.00 40.69  ? 387  ALA C CB  1 
ATOM   8835  N  N   . SER C 1 388 ? 7.805   49.162  18.115  1.00 37.83  ? 388  SER C N   1 
ATOM   8836  C  CA  . SER C 1 388 ? 8.607   49.422  16.936  1.00 45.48  ? 388  SER C CA  1 
ATOM   8837  C  C   . SER C 1 388 ? 8.022   48.667  15.758  1.00 42.19  ? 388  SER C C   1 
ATOM   8838  O  O   . SER C 1 388 ? 7.283   47.702  15.933  1.00 34.53  ? 388  SER C O   1 
ATOM   8839  C  CB  . SER C 1 388 ? 10.068  49.034  17.178  1.00 40.94  ? 388  SER C CB  1 
ATOM   8840  O  OG  . SER C 1 388 ? 10.175  47.693  17.616  1.00 41.16  ? 388  SER C OG  1 
ATOM   8841  N  N   . ALA C 1 389 ? 8.350   49.121  14.558  1.00 51.56  ? 389  ALA C N   1 
ATOM   8842  C  CA  . ALA C 1 389 ? 7.949   48.431  13.343  1.00 45.84  ? 389  ALA C CA  1 
ATOM   8843  C  C   . ALA C 1 389 ? 8.904   48.807  12.213  1.00 44.18  ? 389  ALA C C   1 
ATOM   8844  O  O   . ALA C 1 389 ? 9.420   49.930  12.173  1.00 54.65  ? 389  ALA C O   1 
ATOM   8845  C  CB  . ALA C 1 389 ? 6.514   48.786  12.987  1.00 21.93  ? 389  ALA C CB  1 
ATOM   8846  N  N   . PHE C 1 390 ? 9.155   47.861  11.315  1.00 41.72  ? 390  PHE C N   1 
ATOM   8847  C  CA  . PHE C 1 390 ? 9.936   48.126  10.113  1.00 59.85  ? 390  PHE C CA  1 
ATOM   8848  C  C   . PHE C 1 390 ? 9.341   49.311  9.348   1.00 58.04  ? 390  PHE C C   1 
ATOM   8849  O  O   . PHE C 1 390 ? 8.124   49.374  9.140   1.00 55.44  ? 390  PHE C O   1 
ATOM   8850  C  CB  . PHE C 1 390 ? 9.968   46.878  9.226   1.00 74.97  ? 390  PHE C CB  1 
ATOM   8851  C  CG  . PHE C 1 390 ? 10.656  47.085  7.908   1.00 94.02  ? 390  PHE C CG  1 
ATOM   8852  C  CD1 . PHE C 1 390 ? 9.923   47.176  6.733   1.00 103.28 ? 390  PHE C CD1 1 
ATOM   8853  C  CD2 . PHE C 1 390 ? 12.033  47.188  7.843   1.00 102.16 ? 390  PHE C CD2 1 
ATOM   8854  C  CE1 . PHE C 1 390 ? 10.552  47.370  5.516   1.00 108.27 ? 390  PHE C CE1 1 
ATOM   8855  C  CE2 . PHE C 1 390 ? 12.668  47.380  6.632   1.00 111.26 ? 390  PHE C CE2 1 
ATOM   8856  C  CZ  . PHE C 1 390 ? 11.925  47.473  5.464   1.00 112.30 ? 390  PHE C CZ  1 
ATOM   8857  N  N   . GLY C 1 391 ? 10.198  50.248  8.946   1.00 44.31  ? 391  GLY C N   1 
ATOM   8858  C  CA  . GLY C 1 391 ? 9.750   51.440  8.242   1.00 54.22  ? 391  GLY C CA  1 
ATOM   8859  C  C   . GLY C 1 391 ? 9.247   52.545  9.164   1.00 55.54  ? 391  GLY C C   1 
ATOM   8860  O  O   . GLY C 1 391 ? 8.883   53.639  8.707   1.00 42.70  ? 391  GLY C O   1 
ATOM   8861  N  N   . TYR C 1 392 ? 9.238   52.261  10.467  1.00 59.62  ? 392  TYR C N   1 
ATOM   8862  C  CA  . TYR C 1 392 ? 8.783   53.224  11.470  1.00 58.12  ? 392  TYR C CA  1 
ATOM   8863  C  C   . TYR C 1 392 ? 9.844   53.493  12.519  1.00 57.48  ? 392  TYR C C   1 
ATOM   8864  O  O   . TYR C 1 392 ? 10.531  52.577  12.971  1.00 68.36  ? 392  TYR C O   1 
ATOM   8865  C  CB  . TYR C 1 392 ? 7.507   52.736  12.157  1.00 55.41  ? 392  TYR C CB  1 
ATOM   8866  C  CG  . TYR C 1 392 ? 6.303   52.744  11.249  1.00 61.51  ? 392  TYR C CG  1 
ATOM   8867  C  CD1 . TYR C 1 392 ? 5.394   53.796  11.281  1.00 65.62  ? 392  TYR C CD1 1 
ATOM   8868  C  CD2 . TYR C 1 392 ? 6.083   51.712  10.344  1.00 48.47  ? 392  TYR C CD2 1 
ATOM   8869  C  CE1 . TYR C 1 392 ? 4.296   53.815  10.447  1.00 60.53  ? 392  TYR C CE1 1 
ATOM   8870  C  CE2 . TYR C 1 392 ? 4.986   51.722  9.505   1.00 54.61  ? 392  TYR C CE2 1 
ATOM   8871  C  CZ  . TYR C 1 392 ? 4.096   52.775  9.560   1.00 62.55  ? 392  TYR C CZ  1 
ATOM   8872  O  OH  . TYR C 1 392 ? 2.999   52.779  8.726   1.00 59.88  ? 392  TYR C OH  1 
ATOM   8873  N  N   . GLN C 1 393 ? 9.974   54.757  12.898  1.00 54.67  ? 393  GLN C N   1 
ATOM   8874  C  CA  . GLN C 1 393 ? 10.864  55.126  13.975  1.00 50.97  ? 393  GLN C CA  1 
ATOM   8875  C  C   . GLN C 1 393 ? 10.282  54.535  15.237  1.00 59.84  ? 393  GLN C C   1 
ATOM   8876  O  O   . GLN C 1 393 ? 9.080   54.666  15.503  1.00 59.68  ? 393  GLN C O   1 
ATOM   8877  C  CB  . GLN C 1 393 ? 10.967  56.640  14.090  1.00 43.61  ? 393  GLN C CB  1 
ATOM   8878  C  CG  . GLN C 1 393 ? 11.356  57.294  12.795  1.00 54.31  ? 393  GLN C CG  1 
ATOM   8879  C  CD  . GLN C 1 393 ? 11.589  58.778  12.934  1.00 66.98  ? 393  GLN C CD  1 
ATOM   8880  O  OE1 . GLN C 1 393 ? 11.131  59.401  13.889  1.00 62.82  ? 393  GLN C OE1 1 
ATOM   8881  N  NE2 . GLN C 1 393 ? 12.301  59.358  11.969  1.00 74.32  ? 393  GLN C NE2 1 
ATOM   8882  N  N   . THR C 1 394 ? 11.136  53.860  15.999  1.00 65.46  ? 394  THR C N   1 
ATOM   8883  C  CA  . THR C 1 394 ? 10.711  53.156  17.200  1.00 64.51  ? 394  THR C CA  1 
ATOM   8884  C  C   . THR C 1 394 ? 10.277  54.154  18.254  1.00 60.81  ? 394  THR C C   1 
ATOM   8885  O  O   . THR C 1 394 ? 11.076  54.979  18.696  1.00 65.55  ? 394  THR C O   1 
ATOM   8886  C  CB  . THR C 1 394 ? 11.848  52.285  17.751  1.00 61.00  ? 394  THR C CB  1 
ATOM   8887  O  OG1 . THR C 1 394 ? 12.194  51.297  16.769  1.00 51.55  ? 394  THR C OG1 1 
ATOM   8888  C  CG2 . THR C 1 394 ? 11.435  51.609  19.068  1.00 60.26  ? 394  THR C CG2 1 
ATOM   8889  N  N   . SER C 1 395 ? 9.008   54.074  18.646  1.00 53.76  ? 395  SER C N   1 
ATOM   8890  C  CA  . SER C 1 395 ? 8.419   55.020  19.593  1.00 51.16  ? 395  SER C CA  1 
ATOM   8891  C  C   . SER C 1 395 ? 9.323   55.340  20.784  1.00 62.34  ? 395  SER C C   1 
ATOM   8892  O  O   . SER C 1 395 ? 10.238  54.573  21.117  1.00 66.45  ? 395  SER C O   1 
ATOM   8893  C  CB  . SER C 1 395 ? 7.120   54.453  20.145  1.00 41.38  ? 395  SER C CB  1 
ATOM   8894  O  OG  . SER C 1 395 ? 7.405   53.518  21.177  1.00 39.33  ? 395  SER C OG  1 
ATOM   8895  N  N   . ALA C 1 396 ? 9.052   56.475  21.426  1.00 53.87  ? 396  ALA C N   1 
ATOM   8896  C  CA  . ALA C 1 396 ? 9.600   56.752  22.743  1.00 43.27  ? 396  ALA C CA  1 
ATOM   8897  C  C   . ALA C 1 396 ? 8.915   55.813  23.733  1.00 55.29  ? 396  ALA C C   1 
ATOM   8898  O  O   . ALA C 1 396 ? 7.781   55.375  23.503  1.00 61.69  ? 396  ALA C O   1 
ATOM   8899  C  CB  . ALA C 1 396 ? 9.345   58.188  23.116  1.00 34.96  ? 396  ALA C CB  1 
ATOM   8900  N  N   . PRO C 1 397 ? 9.596   55.496  24.842  1.00 52.31  ? 397  PRO C N   1 
ATOM   8901  C  CA  . PRO C 1 397 ? 9.051   54.554  25.827  1.00 44.03  ? 397  PRO C CA  1 
ATOM   8902  C  C   . PRO C 1 397 ? 7.977   55.197  26.708  1.00 45.12  ? 397  PRO C C   1 
ATOM   8903  O  O   . PRO C 1 397 ? 8.028   56.404  26.975  1.00 49.38  ? 397  PRO C O   1 
ATOM   8904  C  CB  . PRO C 1 397 ? 10.280  54.195  26.679  1.00 49.71  ? 397  PRO C CB  1 
ATOM   8905  C  CG  . PRO C 1 397 ? 11.470  54.881  26.016  1.00 49.17  ? 397  PRO C CG  1 
ATOM   8906  C  CD  . PRO C 1 397 ? 10.903  56.024  25.258  1.00 52.06  ? 397  PRO C CD  1 
ATOM   8907  N  N   . GLN C 1 398 ? 7.014   54.398  27.155  1.00 55.36  ? 398  GLN C N   1 
ATOM   8908  C  CA  . GLN C 1 398 ? 6.017   54.877  28.115  1.00 56.86  ? 398  GLN C CA  1 
ATOM   8909  C  C   . GLN C 1 398 ? 6.039   54.038  29.382  1.00 49.10  ? 398  GLN C C   1 
ATOM   8910  O  O   . GLN C 1 398 ? 6.145   52.810  29.340  1.00 49.76  ? 398  GLN C O   1 
ATOM   8911  C  CB  . GLN C 1 398 ? 4.605   54.888  27.508  1.00 50.72  ? 398  GLN C CB  1 
ATOM   8912  C  CG  . GLN C 1 398 ? 4.412   55.890  26.373  1.00 34.19  ? 398  GLN C CG  1 
ATOM   8913  C  CD  . GLN C 1 398 ? 3.145   55.641  25.582  1.00 53.67  ? 398  GLN C CD  1 
ATOM   8914  O  OE1 . GLN C 1 398 ? 2.072   55.433  26.146  1.00 58.18  ? 398  GLN C OE1 1 
ATOM   8915  N  NE2 . GLN C 1 398 ? 3.262   55.665  24.260  1.00 57.92  ? 398  GLN C NE2 1 
ATOM   8916  N  N   . GLN C 1 399 ? 5.937   54.719  30.510  1.00 65.58  ? 399  GLN C N   1 
ATOM   8917  C  CA  . GLN C 1 399 ? 5.942   54.065  31.805  1.00 68.10  ? 399  GLN C CA  1 
ATOM   8918  C  C   . GLN C 1 399 ? 4.505   53.842  32.281  1.00 70.41  ? 399  GLN C C   1 
ATOM   8919  O  O   . GLN C 1 399 ? 3.666   54.738  32.210  1.00 75.65  ? 399  GLN C O   1 
ATOM   8920  C  CB  . GLN C 1 399 ? 6.732   54.927  32.793  1.00 72.28  ? 399  GLN C CB  1 
ATOM   8921  C  CG  . GLN C 1 399 ? 6.490   54.630  34.262  1.00 87.39  ? 399  GLN C CG  1 
ATOM   8922  C  CD  . GLN C 1 399 ? 6.877   55.808  35.168  1.00 106.29 ? 399  GLN C CD  1 
ATOM   8923  O  OE1 . GLN C 1 399 ? 6.201   56.845  35.183  1.00 117.61 ? 399  GLN C OE1 1 
ATOM   8924  N  NE2 . GLN C 1 399 ? 7.961   55.648  35.928  1.00 102.76 ? 399  GLN C NE2 1 
ATOM   8925  N  N   . VAL C 1 400 ? 4.216   52.636  32.752  1.00 55.11  ? 400  VAL C N   1 
ATOM   8926  C  CA  . VAL C 1 400 ? 2.875   52.332  33.222  1.00 47.52  ? 400  VAL C CA  1 
ATOM   8927  C  C   . VAL C 1 400 ? 2.897   51.521  34.512  1.00 50.70  ? 400  VAL C C   1 
ATOM   8928  O  O   . VAL C 1 400 ? 3.691   50.588  34.673  1.00 47.28  ? 400  VAL C O   1 
ATOM   8929  C  CB  . VAL C 1 400 ? 2.075   51.567  32.169  1.00 48.17  ? 400  VAL C CB  1 
ATOM   8930  C  CG1 . VAL C 1 400 ? 2.630   50.167  32.018  1.00 51.26  ? 400  VAL C CG1 1 
ATOM   8931  C  CG2 . VAL C 1 400 ? 0.602   51.520  32.547  1.00 60.85  ? 400  VAL C CG2 1 
ATOM   8932  N  N   . ARG C 1 401 ? 2.027   51.890  35.442  1.00 51.12  ? 401  ARG C N   1 
ATOM   8933  C  CA  . ARG C 1 401 ? 1.912   51.133  36.669  1.00 55.40  ? 401  ARG C CA  1 
ATOM   8934  C  C   . ARG C 1 401 ? 0.821   50.105  36.468  1.00 50.71  ? 401  ARG C C   1 
ATOM   8935  O  O   . ARG C 1 401 ? -0.367  50.448  36.432  1.00 48.67  ? 401  ARG C O   1 
ATOM   8936  C  CB  . ARG C 1 401 ? 1.601   52.042  37.863  1.00 59.99  ? 401  ARG C CB  1 
ATOM   8937  C  CG  . ARG C 1 401 ? 1.446   51.300  39.203  1.00 63.15  ? 401  ARG C CG  1 
ATOM   8938  C  CD  . ARG C 1 401 ? 1.444   52.276  40.388  1.00 77.75  ? 401  ARG C CD  1 
ATOM   8939  N  NE  . ARG C 1 401 ? 0.604   53.440  40.117  1.00 93.46  ? 401  ARG C NE  1 
ATOM   8940  C  CZ  . ARG C 1 401 ? 0.972   54.715  40.241  1.00 98.90  ? 401  ARG C CZ  1 
ATOM   8941  N  NH1 . ARG C 1 401 ? 0.094   55.664  39.945  1.00 106.74 ? 401  ARG C NH1 1 
ATOM   8942  N  NH2 . ARG C 1 401 ? 2.191   55.050  40.657  1.00 89.03  ? 401  ARG C NH2 1 
ATOM   8943  N  N   . VAL C 1 402 ? 1.234   48.848  36.314  1.00 46.10  ? 402  VAL C N   1 
ATOM   8944  C  CA  . VAL C 1 402 ? 0.288   47.743  36.221  1.00 43.59  ? 402  VAL C CA  1 
ATOM   8945  C  C   . VAL C 1 402 ? -0.187  47.260  37.589  1.00 57.13  ? 402  VAL C C   1 
ATOM   8946  O  O   . VAL C 1 402 ? 0.536   46.553  38.306  1.00 36.10  ? 402  VAL C O   1 
ATOM   8947  C  CB  . VAL C 1 402 ? 0.848   46.531  35.446  1.00 37.54  ? 402  VAL C CB  1 
ATOM   8948  C  CG1 . VAL C 1 402 ? -0.155  45.370  35.499  1.00 35.32  ? 402  VAL C CG1 1 
ATOM   8949  C  CG2 . VAL C 1 402 ? 1.160   46.909  33.999  1.00 32.05  ? 402  VAL C CG2 1 
ATOM   8950  N  N   . THR C 1 403 ? -1.400  47.687  37.937  1.00 70.74  ? 403  THR C N   1 
ATOM   8951  C  CA  . THR C 1 403 ? -2.197  47.086  38.989  1.00 66.21  ? 403  THR C CA  1 
ATOM   8952  C  C   . THR C 1 403 ? -3.246  46.253  38.265  1.00 73.89  ? 403  THR C C   1 
ATOM   8953  O  O   . THR C 1 403 ? -3.833  46.710  37.282  1.00 77.25  ? 403  THR C O   1 
ATOM   8954  C  CB  . THR C 1 403 ? -2.899  48.161  39.845  1.00 72.01  ? 403  THR C CB  1 
ATOM   8955  O  OG1 . THR C 1 403 ? -3.736  47.531  40.823  1.00 89.82  ? 403  THR C OG1 1 
ATOM   8956  C  CG2 . THR C 1 403 ? -3.760  49.091  38.973  1.00 65.80  ? 403  THR C CG2 1 
ATOM   8957  N  N   . ASN C 1 404 ? -3.455  45.020  38.710  1.00 80.20  ? 404  ASN C N   1 
ATOM   8958  C  CA  . ASN C 1 404 ? -4.541  44.210  38.174  1.00 66.40  ? 404  ASN C CA  1 
ATOM   8959  C  C   . ASN C 1 404 ? -5.711  44.262  39.153  1.00 75.90  ? 404  ASN C C   1 
ATOM   8960  O  O   . ASN C 1 404 ? -6.045  43.275  39.819  1.00 83.22  ? 404  ASN C O   1 
ATOM   8961  C  CB  . ASN C 1 404 ? -4.087  42.771  37.906  1.00 51.26  ? 404  ASN C CB  1 
ATOM   8962  C  CG  . ASN C 1 404 ? -3.008  42.688  36.844  1.00 40.96  ? 404  ASN C CG  1 
ATOM   8963  O  OD1 . ASN C 1 404 ? -3.082  43.365  35.816  1.00 45.76  ? 404  ASN C OD1 1 
ATOM   8964  N  ND2 . ASN C 1 404 ? -2.001  41.845  37.082  1.00 34.87  ? 404  ASN C ND2 1 
ATOM   8965  N  N   . ASP C 1 405 ? -6.303  45.449  39.247  1.00 77.54  ? 405  ASP C N   1 
ATOM   8966  C  CA  . ASP C 1 405 ? -7.448  45.709  40.112  1.00 84.04  ? 405  ASP C CA  1 
ATOM   8967  C  C   . ASP C 1 405 ? -8.589  46.252  39.249  1.00 60.86  ? 405  ASP C C   1 
ATOM   8968  O  O   . ASP C 1 405 ? -9.700  46.467  39.722  1.00 65.46  ? 405  ASP C O   1 
ATOM   8969  C  CB  . ASP C 1 405 ? -7.065  46.712  41.211  1.00 117.10 ? 405  ASP C CB  1 
ATOM   8970  C  CG  . ASP C 1 405 ? -7.982  46.641  42.431  1.00 130.88 ? 405  ASP C CG  1 
ATOM   8971  O  OD1 . ASP C 1 405 ? -8.983  45.893  42.399  1.00 138.96 ? 405  ASP C OD1 1 
ATOM   8972  O  OD2 . ASP C 1 405 ? -7.697  47.339  43.429  1.00 125.58 ? 405  ASP C OD2 1 
ATOM   8973  N  N   . ASN C 1 406 ? -8.293  46.453  37.969  1.00 61.00  ? 406  ASN C N   1 
ATOM   8974  C  CA  . ASN C 1 406 ? -9.270  46.883  36.979  1.00 41.91  ? 406  ASN C CA  1 
ATOM   8975  C  C   . ASN C 1 406 ? -9.792  45.637  36.240  1.00 57.80  ? 406  ASN C C   1 
ATOM   8976  O  O   . ASN C 1 406 ? -9.020  44.698  36.002  1.00 48.64  ? 406  ASN C O   1 
ATOM   8977  C  CB  . ASN C 1 406 ? -8.590  47.847  35.996  1.00 70.21  ? 406  ASN C CB  1 
ATOM   8978  C  CG  . ASN C 1 406 ? -9.536  48.911  35.442  1.00 93.46  ? 406  ASN C CG  1 
ATOM   8979  O  OD1 . ASN C 1 406 ? -10.329 49.509  36.181  1.00 98.87  ? 406  ASN C OD1 1 
ATOM   8980  N  ND2 . ASN C 1 406 ? -9.432  49.169  34.133  1.00 81.51  ? 406  ASN C ND2 1 
ATOM   8981  N  N   . GLN C 1 407 ? -11.089 45.622  35.897  1.00 75.07  ? 407  GLN C N   1 
ATOM   8982  C  CA  . GLN C 1 407 ? -11.714 44.507  35.159  1.00 73.28  ? 407  GLN C CA  1 
ATOM   8983  C  C   . GLN C 1 407 ? -11.080 44.264  33.787  1.00 63.51  ? 407  GLN C C   1 
ATOM   8984  O  O   . GLN C 1 407 ? -11.123 43.145  33.265  1.00 60.26  ? 407  GLN C O   1 
ATOM   8985  C  CB  . GLN C 1 407 ? -13.228 44.725  34.979  1.00 79.76  ? 407  GLN C CB  1 
ATOM   8986  C  CG  . GLN C 1 407 ? -14.127 44.040  36.015  1.00 74.75  ? 407  GLN C CG  1 
ATOM   8987  C  CD  . GLN C 1 407 ? -15.606 44.315  35.771  1.00 89.00  ? 407  GLN C CD  1 
ATOM   8988  O  OE1 . GLN C 1 407 ? -15.964 45.247  35.047  1.00 92.47  ? 407  GLN C OE1 1 
ATOM   8989  N  NE2 . GLN C 1 407 ? -16.471 43.504  36.374  1.00 96.97  ? 407  GLN C NE2 1 
ATOM   8990  N  N   . GLU C 1 408 ? -10.504 45.312  33.202  1.00 57.87  ? 408  GLU C N   1 
ATOM   8991  C  CA  . GLU C 1 408 ? -9.838  45.177  31.910  1.00 53.93  ? 408  GLU C CA  1 
ATOM   8992  C  C   . GLU C 1 408 ? -8.445  45.823  31.841  1.00 53.98  ? 408  GLU C C   1 
ATOM   8993  O  O   . GLU C 1 408 ? -8.151  46.817  32.528  1.00 52.11  ? 408  GLU C O   1 
ATOM   8994  C  CB  . GLU C 1 408 ? -10.753 45.652  30.777  1.00 53.76  ? 408  GLU C CB  1 
ATOM   8995  C  CG  . GLU C 1 408 ? -12.000 44.779  30.638  1.00 63.31  ? 408  GLU C CG  1 
ATOM   8996  C  CD  . GLU C 1 408 ? -12.885 45.174  29.476  1.00 69.44  ? 408  GLU C CD  1 
ATOM   8997  O  OE1 . GLU C 1 408 ? -14.130 45.075  29.614  1.00 52.34  ? 408  GLU C OE1 1 
ATOM   8998  O  OE2 . GLU C 1 408 ? -12.335 45.580  28.426  1.00 85.01  ? 408  GLU C OE2 1 
ATOM   8999  N  N   . ALA C 1 409 ? -7.591  45.223  31.012  1.00 44.85  ? 409  ALA C N   1 
ATOM   9000  C  CA  . ALA C 1 409 ? -6.205  45.642  30.883  1.00 31.30  ? 409  ALA C CA  1 
ATOM   9001  C  C   . ALA C 1 409 ? -6.075  47.142  30.636  1.00 45.96  ? 409  ALA C C   1 
ATOM   9002  O  O   . ALA C 1 409 ? -6.887  47.762  29.944  1.00 47.43  ? 409  ALA C O   1 
ATOM   9003  C  CB  . ALA C 1 409 ? -5.520  44.866  29.796  1.00 31.60  ? 409  ALA C CB  1 
ATOM   9004  N  N   . LEU C 1 410 ? -5.040  47.725  31.218  1.00 52.23  ? 410  LEU C N   1 
ATOM   9005  C  CA  . LEU C 1 410 ? -4.814  49.150  31.089  1.00 38.83  ? 410  LEU C CA  1 
ATOM   9006  C  C   . LEU C 1 410 ? -4.553  49.536  29.645  1.00 32.01  ? 410  LEU C C   1 
ATOM   9007  O  O   . LEU C 1 410 ? -3.624  49.031  29.015  1.00 25.45  ? 410  LEU C O   1 
ATOM   9008  C  CB  . LEU C 1 410 ? -3.650  49.570  31.970  1.00 47.82  ? 410  LEU C CB  1 
ATOM   9009  C  CG  . LEU C 1 410 ? -4.040  49.720  33.438  1.00 67.07  ? 410  LEU C CG  1 
ATOM   9010  C  CD1 . LEU C 1 410 ? -2.841  49.495  34.357  1.00 80.99  ? 410  LEU C CD1 1 
ATOM   9011  C  CD2 . LEU C 1 410 ? -4.665  51.091  33.663  1.00 68.22  ? 410  LEU C CD2 1 
ATOM   9012  N  N   . ARG C 1 411 ? -5.390  50.423  29.121  1.00 32.86  ? 411  ARG C N   1 
ATOM   9013  C  CA  . ARG C 1 411 ? -5.181  50.920  27.775  1.00 44.48  ? 411  ARG C CA  1 
ATOM   9014  C  C   . ARG C 1 411 ? -3.847  51.667  27.674  1.00 45.35  ? 411  ARG C C   1 
ATOM   9015  O  O   . ARG C 1 411 ? -3.438  52.344  28.618  1.00 41.72  ? 411  ARG C O   1 
ATOM   9016  C  CB  . ARG C 1 411 ? -6.339  51.812  27.336  1.00 31.71  ? 411  ARG C CB  1 
ATOM   9017  C  CG  . ARG C 1 411 ? -6.106  52.456  25.978  1.00 36.48  ? 411  ARG C CG  1 
ATOM   9018  C  CD  . ARG C 1 411 ? -6.179  51.440  24.847  1.00 36.86  ? 411  ARG C CD  1 
ATOM   9019  N  NE  . ARG C 1 411 ? -7.523  51.411  24.291  1.00 44.50  ? 411  ARG C NE  1 
ATOM   9020  C  CZ  . ARG C 1 411 ? -7.876  52.079  23.208  1.00 36.68  ? 411  ARG C CZ  1 
ATOM   9021  N  NH1 . ARG C 1 411 ? -6.967  52.790  22.570  1.00 28.62  ? 411  ARG C NH1 1 
ATOM   9022  N  NH2 . ARG C 1 411 ? -9.122  52.020  22.762  1.00 32.59  ? 411  ARG C NH2 1 
ATOM   9023  N  N   . LEU C 1 412 ? -3.172  51.516  26.532  1.00 44.92  ? 412  LEU C N   1 
ATOM   9024  C  CA  . LEU C 1 412 ? -1.889  52.174  26.260  1.00 48.12  ? 412  LEU C CA  1 
ATOM   9025  C  C   . LEU C 1 412 ? -1.586  52.075  24.757  1.00 49.92  ? 412  LEU C C   1 
ATOM   9026  O  O   . LEU C 1 412 ? -1.359  50.982  24.217  1.00 42.13  ? 412  LEU C O   1 
ATOM   9027  C  CB  . LEU C 1 412 ? -0.746  51.554  27.090  1.00 45.76  ? 412  LEU C CB  1 
ATOM   9028  C  CG  . LEU C 1 412 ? 0.611   52.282  27.155  1.00 53.88  ? 412  LEU C CG  1 
ATOM   9029  C  CD1 . LEU C 1 412 ? 0.502   53.523  28.034  1.00 61.29  ? 412  LEU C CD1 1 
ATOM   9030  C  CD2 . LEU C 1 412 ? 1.744   51.383  27.658  1.00 34.18  ? 412  LEU C CD2 1 
ATOM   9031  N  N   . ASP C 1 413 ? -1.597  53.223  24.088  1.00 39.99  ? 413  ASP C N   1 
ATOM   9032  C  CA  . ASP C 1 413 ? -1.487  53.256  22.646  1.00 28.09  ? 413  ASP C CA  1 
ATOM   9033  C  C   . ASP C 1 413 ? -0.187  53.903  22.185  1.00 46.20  ? 413  ASP C C   1 
ATOM   9034  O  O   . ASP C 1 413 ? 0.471   54.633  22.939  1.00 41.70  ? 413  ASP C O   1 
ATOM   9035  C  CB  . ASP C 1 413 ? -2.654  54.026  22.038  1.00 36.51  ? 413  ASP C CB  1 
ATOM   9036  C  CG  . ASP C 1 413 ? -3.999  53.354  22.254  1.00 46.77  ? 413  ASP C CG  1 
ATOM   9037  O  OD1 . ASP C 1 413 ? -4.061  52.222  22.782  1.00 54.89  ? 413  ASP C OD1 1 
ATOM   9038  O  OD2 . ASP C 1 413 ? -5.013  53.979  21.880  1.00 52.38  ? 413  ASP C OD2 1 
ATOM   9039  N  N   . PHE C 1 414 ? 0.152   53.646  20.922  1.00 50.68  ? 414  PHE C N   1 
ATOM   9040  C  CA  . PHE C 1 414 ? 1.364   54.176  20.325  1.00 47.66  ? 414  PHE C CA  1 
ATOM   9041  C  C   . PHE C 1 414 ? 1.120   54.735  18.924  1.00 50.66  ? 414  PHE C C   1 
ATOM   9042  O  O   . PHE C 1 414 ? 0.459   54.114  18.092  1.00 52.07  ? 414  PHE C O   1 
ATOM   9043  C  CB  . PHE C 1 414 ? 2.455   53.101  20.276  1.00 49.43  ? 414  PHE C CB  1 
ATOM   9044  C  CG  . PHE C 1 414 ? 2.826   52.549  21.622  1.00 45.75  ? 414  PHE C CG  1 
ATOM   9045  C  CD1 . PHE C 1 414 ? 2.084   51.528  22.200  1.00 43.77  ? 414  PHE C CD1 1 
ATOM   9046  C  CD2 . PHE C 1 414 ? 3.921   53.049  22.310  1.00 53.87  ? 414  PHE C CD2 1 
ATOM   9047  C  CE1 . PHE C 1 414 ? 2.429   51.013  23.441  1.00 44.39  ? 414  PHE C CE1 1 
ATOM   9048  C  CE2 . PHE C 1 414 ? 4.272   52.543  23.558  1.00 52.75  ? 414  PHE C CE2 1 
ATOM   9049  C  CZ  . PHE C 1 414 ? 3.525   51.522  24.122  1.00 53.83  ? 414  PHE C CZ  1 
ATOM   9050  N  N   . LYS C 1 415 ? 1.651   55.928  18.682  1.00 45.69  ? 415  LYS C N   1 
ATOM   9051  C  CA  . LYS C 1 415 ? 1.716   56.470  17.343  1.00 50.73  ? 415  LYS C CA  1 
ATOM   9052  C  C   . LYS C 1 415 ? 3.175   56.437  16.874  1.00 59.69  ? 415  LYS C C   1 
ATOM   9053  O  O   . LYS C 1 415 ? 4.093   56.874  17.587  1.00 51.10  ? 415  LYS C O   1 
ATOM   9054  C  CB  . LYS C 1 415 ? 1.141   57.883  17.294  1.00 45.93  ? 415  LYS C CB  1 
ATOM   9055  C  CG  . LYS C 1 415 ? -0.356  57.938  17.481  1.00 61.56  ? 415  LYS C CG  1 
ATOM   9056  C  CD  . LYS C 1 415 ? -0.943  59.175  16.828  1.00 76.10  ? 415  LYS C CD  1 
ATOM   9057  C  CE  . LYS C 1 415 ? -2.456  59.069  16.697  1.00 83.95  ? 415  LYS C CE  1 
ATOM   9058  N  NZ  . LYS C 1 415 ? -3.020  60.202  15.905  1.00 88.46  ? 415  LYS C NZ  1 
ATOM   9059  N  N   . LEU C 1 416 ? 3.384   55.897  15.678  1.00 51.33  ? 416  LEU C N   1 
ATOM   9060  C  CA  . LEU C 1 416 ? 4.720   55.766  15.141  1.00 48.76  ? 416  LEU C CA  1 
ATOM   9061  C  C   . LEU C 1 416 ? 4.846   56.600  13.881  1.00 49.43  ? 416  LEU C C   1 
ATOM   9062  O  O   . LEU C 1 416 ? 3.988   56.543  13.008  1.00 49.44  ? 416  LEU C O   1 
ATOM   9063  C  CB  . LEU C 1 416 ? 5.030   54.294  14.829  1.00 49.94  ? 416  LEU C CB  1 
ATOM   9064  C  CG  . LEU C 1 416 ? 4.890   53.278  15.963  1.00 31.63  ? 416  LEU C CG  1 
ATOM   9065  C  CD1 . LEU C 1 416 ? 5.404   51.928  15.528  1.00 25.80  ? 416  LEU C CD1 1 
ATOM   9066  C  CD2 . LEU C 1 416 ? 5.636   53.750  17.181  1.00 32.10  ? 416  LEU C CD2 1 
ATOM   9067  N  N   . ALA C 1 417 ? 5.919   57.375  13.786  1.00 54.77  ? 417  ALA C N   1 
ATOM   9068  C  CA  . ALA C 1 417 ? 6.187   58.124  12.568  1.00 42.86  ? 417  ALA C CA  1 
ATOM   9069  C  C   . ALA C 1 417 ? 7.011   57.237  11.645  1.00 40.26  ? 417  ALA C C   1 
ATOM   9070  O  O   . ALA C 1 417 ? 7.655   56.297  12.115  1.00 55.12  ? 417  ALA C O   1 
ATOM   9071  C  CB  . ALA C 1 417 ? 6.921   59.420  12.893  1.00 29.71  ? 417  ALA C CB  1 
ATOM   9072  N  N   . PRO C 1 418 ? 6.972   57.507  10.327  1.00 40.84  ? 418  PRO C N   1 
ATOM   9073  C  CA  . PRO C 1 418 ? 7.800   56.766  9.365   1.00 39.31  ? 418  PRO C CA  1 
ATOM   9074  C  C   . PRO C 1 418 ? 9.249   57.223  9.386   1.00 38.97  ? 418  PRO C C   1 
ATOM   9075  O  O   . PRO C 1 418 ? 9.558   58.252  9.988   1.00 63.79  ? 418  PRO C O   1 
ATOM   9076  C  CB  . PRO C 1 418 ? 7.166   57.117  8.012   1.00 54.40  ? 418  PRO C CB  1 
ATOM   9077  C  CG  . PRO C 1 418 ? 5.784   57.602  8.334   1.00 55.06  ? 418  PRO C CG  1 
ATOM   9078  C  CD  . PRO C 1 418 ? 5.937   58.306  9.651   1.00 55.13  ? 418  PRO C CD  1 
ATOM   9079  N  N   . VAL C 1 419 ? 10.133  56.467  8.744   1.00 42.99  ? 419  VAL C N   1 
ATOM   9080  C  CA  . VAL C 1 419 ? 11.520  56.903  8.577   1.00 46.09  ? 419  VAL C CA  1 
ATOM   9081  C  C   . VAL C 1 419 ? 11.582  58.025  7.544   1.00 47.46  ? 419  VAL C C   1 
ATOM   9082  O  O   . VAL C 1 419 ? 12.611  58.689  7.389   1.00 68.02  ? 419  VAL C O   1 
ATOM   9083  C  CB  . VAL C 1 419 ? 12.444  55.746  8.114   1.00 56.38  ? 419  VAL C CB  1 
ATOM   9084  C  CG1 . VAL C 1 419 ? 12.943  54.920  9.295   1.00 33.98  ? 419  VAL C CG1 1 
ATOM   9085  C  CG2 . VAL C 1 419 ? 11.732  54.865  7.095   1.00 74.33  ? 419  VAL C CG2 1 
ATOM   9086  N  N   . THR D 1 27  ? 16.763  42.033  -26.489 1.00 112.40 ? 27   THR D N   1 
ATOM   9087  C  CA  . THR D 1 27  ? 16.157  42.124  -25.159 1.00 112.74 ? 27   THR D CA  1 
ATOM   9088  C  C   . THR D 1 27  ? 15.602  40.782  -24.628 1.00 88.50  ? 27   THR D C   1 
ATOM   9089  O  O   . THR D 1 27  ? 16.118  39.710  -24.951 1.00 73.02  ? 27   THR D O   1 
ATOM   9090  C  CB  . THR D 1 27  ? 15.079  43.240  -25.089 1.00 91.06  ? 27   THR D CB  1 
ATOM   9091  O  OG1 . THR D 1 27  ? 13.946  42.880  -25.892 1.00 99.36  ? 27   THR D OG1 1 
ATOM   9092  C  CG2 . THR D 1 27  ? 15.658  44.579  -25.570 1.00 67.76  ? 27   THR D CG2 1 
ATOM   9093  N  N   . ILE D 1 28  ? 14.551  40.846  -23.817 1.00 88.96  ? 28   ILE D N   1 
ATOM   9094  C  CA  . ILE D 1 28  ? 14.159  39.699  -22.987 1.00 95.96  ? 28   ILE D CA  1 
ATOM   9095  C  C   . ILE D 1 28  ? 13.102  38.762  -23.593 1.00 97.27  ? 28   ILE D C   1 
ATOM   9096  O  O   . ILE D 1 28  ? 12.237  39.192  -24.357 1.00 112.69 ? 28   ILE D O   1 
ATOM   9097  C  CB  . ILE D 1 28  ? 13.726  40.156  -21.571 1.00 64.81  ? 28   ILE D CB  1 
ATOM   9098  C  CG1 . ILE D 1 28  ? 14.508  41.415  -21.180 1.00 43.14  ? 28   ILE D CG1 1 
ATOM   9099  C  CG2 . ILE D 1 28  ? 13.957  39.038  -20.572 1.00 45.27  ? 28   ILE D CG2 1 
ATOM   9100  C  CD1 . ILE D 1 28  ? 14.236  41.939  -19.816 1.00 41.99  ? 28   ILE D CD1 1 
ATOM   9101  N  N   . LYS D 1 29  ? 13.189  37.481  -23.236 1.00 71.02  ? 29   LYS D N   1 
ATOM   9102  C  CA  . LYS D 1 29  ? 12.300  36.452  -23.770 1.00 54.76  ? 29   LYS D CA  1 
ATOM   9103  C  C   . LYS D 1 29  ? 11.855  35.517  -22.657 1.00 63.05  ? 29   LYS D C   1 
ATOM   9104  O  O   . LYS D 1 29  ? 12.687  34.894  -21.993 1.00 80.31  ? 29   LYS D O   1 
ATOM   9105  C  CB  . LYS D 1 29  ? 13.006  35.642  -24.867 1.00 74.94  ? 29   LYS D CB  1 
ATOM   9106  C  CG  . LYS D 1 29  ? 13.453  36.448  -26.098 1.00 81.64  ? 29   LYS D CG  1 
ATOM   9107  C  CD  . LYS D 1 29  ? 12.530  36.226  -27.300 1.00 86.48  ? 29   LYS D CD  1 
ATOM   9108  C  CE  . LYS D 1 29  ? 13.239  36.526  -28.629 1.00 96.17  ? 29   LYS D CE  1 
ATOM   9109  N  NZ  . LYS D 1 29  ? 12.389  36.217  -29.823 1.00 93.70  ? 29   LYS D NZ  1 
ATOM   9110  N  N   . GLU D 1 30  ? 10.541  35.416  -22.472 1.00 69.82  ? 30   GLU D N   1 
ATOM   9111  C  CA  . GLU D 1 30  ? 9.937   34.671  -21.369 1.00 69.38  ? 30   GLU D CA  1 
ATOM   9112  C  C   . GLU D 1 30  ? 10.588  33.328  -21.104 1.00 64.54  ? 30   GLU D C   1 
ATOM   9113  O  O   . GLU D 1 30  ? 10.890  32.579  -22.034 1.00 62.14  ? 30   GLU D O   1 
ATOM   9114  C  CB  . GLU D 1 30  ? 8.462   34.425  -21.662 1.00 75.79  ? 30   GLU D CB  1 
ATOM   9115  C  CG  . GLU D 1 30  ? 7.698   35.670  -22.015 1.00 79.91  ? 30   GLU D CG  1 
ATOM   9116  C  CD  . GLU D 1 30  ? 6.467   35.361  -22.820 1.00 78.97  ? 30   GLU D CD  1 
ATOM   9117  O  OE1 . GLU D 1 30  ? 6.612   35.057  -24.020 1.00 79.15  ? 30   GLU D OE1 1 
ATOM   9118  O  OE2 . GLU D 1 30  ? 5.357   35.419  -22.253 1.00 81.31  ? 30   GLU D OE2 1 
ATOM   9119  N  N   . ASP D 1 31  ? 10.787  33.021  -19.829 1.00 51.08  ? 31   ASP D N   1 
ATOM   9120  C  CA  . ASP D 1 31  ? 11.199  31.684  -19.444 1.00 53.76  ? 31   ASP D CA  1 
ATOM   9121  C  C   . ASP D 1 31  ? 9.975   30.791  -19.395 1.00 63.02  ? 31   ASP D C   1 
ATOM   9122  O  O   . ASP D 1 31  ? 9.190   30.858  -18.447 1.00 78.09  ? 31   ASP D O   1 
ATOM   9123  C  CB  . ASP D 1 31  ? 11.850  31.685  -18.065 1.00 66.18  ? 31   ASP D CB  1 
ATOM   9124  C  CG  . ASP D 1 31  ? 11.940  30.289  -17.468 1.00 68.58  ? 31   ASP D CG  1 
ATOM   9125  O  OD1 . ASP D 1 31  ? 11.782  30.154  -16.231 1.00 76.29  ? 31   ASP D OD1 1 
ATOM   9126  O  OD2 . ASP D 1 31  ? 12.153  29.327  -18.246 1.00 34.48  ? 31   ASP D OD2 1 
ATOM   9127  N  N   . GLU D 1 32  ? 9.800   29.953  -20.405 1.00 51.65  ? 32   GLU D N   1 
ATOM   9128  C  CA  . GLU D 1 32  ? 8.705   28.995  -20.370 1.00 55.11  ? 32   GLU D CA  1 
ATOM   9129  C  C   . GLU D 1 32  ? 9.263   27.573  -20.412 1.00 50.02  ? 32   GLU D C   1 
ATOM   9130  O  O   . GLU D 1 32  ? 8.734   26.683  -21.079 1.00 48.99  ? 32   GLU D O   1 
ATOM   9131  C  CB  . GLU D 1 32  ? 7.683   29.297  -21.469 1.00 48.42  ? 32   GLU D CB  1 
ATOM   9132  C  CG  . GLU D 1 32  ? 7.148   30.720  -21.348 1.00 57.18  ? 32   GLU D CG  1 
ATOM   9133  C  CD  . GLU D 1 32  ? 6.270   31.131  -22.501 1.00 53.40  ? 32   GLU D CD  1 
ATOM   9134  O  OE1 . GLU D 1 32  ? 5.169   30.572  -22.616 1.00 52.42  ? 32   GLU D OE1 1 
ATOM   9135  O  OE2 . GLU D 1 32  ? 6.671   32.021  -23.279 1.00 53.27  ? 32   GLU D OE2 1 
ATOM   9136  N  N   . SER D 1 33  ? 10.340  27.386  -19.656 1.00 42.52  ? 33   SER D N   1 
ATOM   9137  C  CA  . SER D 1 33  ? 11.063  26.131  -19.586 1.00 47.78  ? 33   SER D CA  1 
ATOM   9138  C  C   . SER D 1 33  ? 10.211  25.027  -18.990 1.00 46.56  ? 33   SER D C   1 
ATOM   9139  O  O   . SER D 1 33  ? 10.616  23.865  -18.963 1.00 52.31  ? 33   SER D O   1 
ATOM   9140  C  CB  . SER D 1 33  ? 12.295  26.325  -18.712 1.00 45.06  ? 33   SER D CB  1 
ATOM   9141  O  OG  . SER D 1 33  ? 11.910  26.969  -17.511 1.00 43.58  ? 33   SER D OG  1 
ATOM   9142  N  N   . PHE D 1 34  ? 9.034   25.391  -18.498 1.00 48.09  ? 34   PHE D N   1 
ATOM   9143  C  CA  . PHE D 1 34  ? 8.155   24.424  -17.844 1.00 52.21  ? 34   PHE D CA  1 
ATOM   9144  C  C   . PHE D 1 34  ? 7.378   23.544  -18.831 1.00 45.98  ? 34   PHE D C   1 
ATOM   9145  O  O   . PHE D 1 34  ? 6.674   22.616  -18.423 1.00 47.29  ? 34   PHE D O   1 
ATOM   9146  C  CB  . PHE D 1 34  ? 7.203   25.133  -16.878 1.00 49.88  ? 34   PHE D CB  1 
ATOM   9147  C  CG  . PHE D 1 34  ? 6.565   26.364  -17.450 1.00 54.25  ? 34   PHE D CG  1 
ATOM   9148  C  CD1 . PHE D 1 34  ? 5.309   26.303  -18.035 1.00 56.87  ? 34   PHE D CD1 1 
ATOM   9149  C  CD2 . PHE D 1 34  ? 7.215   27.587  -17.398 1.00 49.05  ? 34   PHE D CD2 1 
ATOM   9150  C  CE1 . PHE D 1 34  ? 4.711   27.440  -18.557 1.00 45.81  ? 34   PHE D CE1 1 
ATOM   9151  C  CE2 . PHE D 1 34  ? 6.619   28.723  -17.918 1.00 50.20  ? 34   PHE D CE2 1 
ATOM   9152  C  CZ  . PHE D 1 34  ? 5.365   28.648  -18.496 1.00 42.87  ? 34   PHE D CZ  1 
ATOM   9153  N  N   . LEU D 1 35  ? 7.536   23.826  -20.122 1.00 52.47  ? 35   LEU D N   1 
ATOM   9154  C  CA  . LEU D 1 35  ? 6.817   23.118  -21.180 1.00 48.59  ? 35   LEU D CA  1 
ATOM   9155  C  C   . LEU D 1 35  ? 7.524   21.838  -21.664 1.00 53.61  ? 35   LEU D C   1 
ATOM   9156  O  O   . LEU D 1 35  ? 6.918   21.009  -22.352 1.00 54.22  ? 35   LEU D O   1 
ATOM   9157  C  CB  . LEU D 1 35  ? 6.605   24.051  -22.376 1.00 53.41  ? 35   LEU D CB  1 
ATOM   9158  C  CG  . LEU D 1 35  ? 6.132   25.484  -22.106 1.00 62.39  ? 35   LEU D CG  1 
ATOM   9159  C  CD1 . LEU D 1 35  ? 6.329   26.385  -23.347 1.00 50.89  ? 35   LEU D CD1 1 
ATOM   9160  C  CD2 . LEU D 1 35  ? 4.670   25.520  -21.595 1.00 55.02  ? 35   LEU D CD2 1 
ATOM   9161  N  N   . GLN D 1 36  ? 8.801   21.682  -21.323 1.00 47.42  ? 36   GLN D N   1 
ATOM   9162  C  CA  . GLN D 1 36  ? 9.570   20.522  -21.775 1.00 55.09  ? 36   GLN D CA  1 
ATOM   9163  C  C   . GLN D 1 36  ? 9.055   19.206  -21.185 1.00 59.01  ? 36   GLN D C   1 
ATOM   9164  O  O   . GLN D 1 36  ? 8.788   19.095  -19.976 1.00 50.84  ? 36   GLN D O   1 
ATOM   9165  C  CB  . GLN D 1 36  ? 11.056  20.690  -21.449 1.00 72.95  ? 36   GLN D CB  1 
ATOM   9166  C  CG  . GLN D 1 36  ? 11.984  19.782  -22.256 1.00 88.31  ? 36   GLN D CG  1 
ATOM   9167  C  CD  . GLN D 1 36  ? 12.534  20.470  -23.495 1.00 88.71  ? 36   GLN D CD  1 
ATOM   9168  O  OE1 . GLN D 1 36  ? 13.032  19.824  -24.417 1.00 60.27  ? 36   GLN D OE1 1 
ATOM   9169  N  NE2 . GLN D 1 36  ? 12.446  21.795  -23.518 1.00 107.20 ? 36   GLN D NE2 1 
ATOM   9170  N  N   . GLN D 1 37  ? 8.940   18.207  -22.053 1.00 60.10  ? 37   GLN D N   1 
ATOM   9171  C  CA  . GLN D 1 37  ? 8.459   16.898  -21.652 1.00 70.52  ? 37   GLN D CA  1 
ATOM   9172  C  C   . GLN D 1 37  ? 7.131   17.075  -20.958 1.00 64.87  ? 37   GLN D C   1 
ATOM   9173  O  O   . GLN D 1 37  ? 7.039   16.889  -19.742 1.00 75.48  ? 37   GLN D O   1 
ATOM   9174  C  CB  . GLN D 1 37  ? 9.457   16.235  -20.712 1.00 81.11  ? 37   GLN D CB  1 
ATOM   9175  C  CG  . GLN D 1 37  ? 10.872  16.271  -21.237 1.00 97.17  ? 37   GLN D CG  1 
ATOM   9176  C  CD  . GLN D 1 37  ? 11.855  15.650  -20.275 1.00 106.00 ? 37   GLN D CD  1 
ATOM   9177  O  OE1 . GLN D 1 37  ? 11.467  14.902  -19.373 1.00 107.97 ? 37   GLN D OE1 1 
ATOM   9178  N  NE2 . GLN D 1 37  ? 13.140  15.953  -20.460 1.00 108.47 ? 37   GLN D NE2 1 
ATOM   9179  N  N   . PRO D 1 38  ? 6.095   17.443  -21.734 1.00 55.28  ? 38   PRO D N   1 
ATOM   9180  C  CA  . PRO D 1 38  ? 4.756   17.675  -21.183 1.00 44.97  ? 38   PRO D CA  1 
ATOM   9181  C  C   . PRO D 1 38  ? 4.336   16.438  -20.428 1.00 43.30  ? 38   PRO D C   1 
ATOM   9182  O  O   . PRO D 1 38  ? 4.660   15.322  -20.835 1.00 57.41  ? 38   PRO D O   1 
ATOM   9183  C  CB  . PRO D 1 38  ? 3.868   17.826  -22.427 1.00 36.02  ? 38   PRO D CB  1 
ATOM   9184  C  CG  . PRO D 1 38  ? 4.785   18.085  -23.559 1.00 34.19  ? 38   PRO D CG  1 
ATOM   9185  C  CD  . PRO D 1 38  ? 6.093   17.422  -23.206 1.00 43.66  ? 38   PRO D CD  1 
ATOM   9186  N  N   . HIS D 1 39  ? 3.616   16.623  -19.338 1.00 52.37  ? 39   HIS D N   1 
ATOM   9187  C  CA  . HIS D 1 39  ? 3.156   15.487  -18.564 1.00 56.39  ? 39   HIS D CA  1 
ATOM   9188  C  C   . HIS D 1 39  ? 2.252   15.992  -17.459 1.00 53.20  ? 39   HIS D C   1 
ATOM   9189  O  O   . HIS D 1 39  ? 2.320   17.159  -17.078 1.00 47.45  ? 39   HIS D O   1 
ATOM   9190  C  CB  . HIS D 1 39  ? 4.348   14.725  -17.974 1.00 57.36  ? 39   HIS D CB  1 
ATOM   9191  C  CG  . HIS D 1 39  ? 5.009   15.431  -16.832 1.00 49.68  ? 39   HIS D CG  1 
ATOM   9192  N  ND1 . HIS D 1 39  ? 5.529   16.701  -16.945 1.00 57.10  ? 39   HIS D ND1 1 
ATOM   9193  C  CD2 . HIS D 1 39  ? 5.240   15.039  -15.557 1.00 50.82  ? 39   HIS D CD2 1 
ATOM   9194  C  CE1 . HIS D 1 39  ? 6.045   17.067  -15.784 1.00 55.91  ? 39   HIS D CE1 1 
ATOM   9195  N  NE2 . HIS D 1 39  ? 5.886   16.076  -14.927 1.00 50.93  ? 39   HIS D NE2 1 
ATOM   9196  N  N   . TYR D 1 40  ? 1.396   15.115  -16.949 1.00 61.61  ? 40   TYR D N   1 
ATOM   9197  C  CA  . TYR D 1 40  ? 0.515   15.492  -15.857 1.00 53.09  ? 40   TYR D CA  1 
ATOM   9198  C  C   . TYR D 1 40  ? 1.221   15.313  -14.513 1.00 44.38  ? 40   TYR D C   1 
ATOM   9199  O  O   . TYR D 1 40  ? 1.724   14.236  -14.193 1.00 52.61  ? 40   TYR D O   1 
ATOM   9200  C  CB  . TYR D 1 40  ? -0.809  14.712  -15.914 1.00 52.53  ? 40   TYR D CB  1 
ATOM   9201  C  CG  . TYR D 1 40  ? -1.771  15.219  -16.974 1.00 50.72  ? 40   TYR D CG  1 
ATOM   9202  C  CD1 . TYR D 1 40  ? -2.012  14.493  -18.134 1.00 65.35  ? 40   TYR D CD1 1 
ATOM   9203  C  CD2 . TYR D 1 40  ? -2.429  16.427  -16.820 1.00 42.99  ? 40   TYR D CD2 1 
ATOM   9204  C  CE1 . TYR D 1 40  ? -2.888  14.956  -19.109 1.00 64.78  ? 40   TYR D CE1 1 
ATOM   9205  C  CE2 . TYR D 1 40  ? -3.305  16.896  -17.788 1.00 49.88  ? 40   TYR D CE2 1 
ATOM   9206  C  CZ  . TYR D 1 40  ? -3.527  16.156  -18.928 1.00 50.76  ? 40   TYR D CZ  1 
ATOM   9207  O  OH  . TYR D 1 40  ? -4.391  16.608  -19.890 1.00 46.66  ? 40   TYR D OH  1 
ATOM   9208  N  N   . ALA D 1 41  ? 1.262   16.393  -13.744 1.00 39.00  ? 41   ALA D N   1 
ATOM   9209  C  CA  . ALA D 1 41  ? 1.862   16.400  -12.411 1.00 44.70  ? 41   ALA D CA  1 
ATOM   9210  C  C   . ALA D 1 41  ? 1.045   15.586  -11.423 1.00 33.44  ? 41   ALA D C   1 
ATOM   9211  O  O   . ALA D 1 41  ? -0.095  15.908  -11.160 1.00 40.23  ? 41   ALA D O   1 
ATOM   9212  C  CB  . ALA D 1 41  ? 1.983   17.830  -11.905 1.00 41.71  ? 41   ALA D CB  1 
ATOM   9213  N  N   . SER D 1 42  ? 1.627   14.538  -10.865 1.00 40.41  ? 42   SER D N   1 
ATOM   9214  C  CA  . SER D 1 42  ? 0.897   13.721  -9.916  1.00 42.55  ? 42   SER D CA  1 
ATOM   9215  C  C   . SER D 1 42  ? 0.752   14.502  -8.632  1.00 44.26  ? 42   SER D C   1 
ATOM   9216  O  O   . SER D 1 42  ? 1.280   15.606  -8.521  1.00 49.16  ? 42   SER D O   1 
ATOM   9217  C  CB  . SER D 1 42  ? 1.681   12.465  -9.608  1.00 38.04  ? 42   SER D CB  1 
ATOM   9218  O  OG  . SER D 1 42  ? 2.797   12.819  -8.816  1.00 42.90  ? 42   SER D OG  1 
ATOM   9219  N  N   . GLN D 1 43  ? 0.057   13.913  -7.658  1.00 36.35  ? 43   GLN D N   1 
ATOM   9220  C  CA  . GLN D 1 43  ? -0.047  14.491  -6.320  1.00 31.60  ? 43   GLN D CA  1 
ATOM   9221  C  C   . GLN D 1 43  ? 1.327   14.712  -5.694  1.00 46.86  ? 43   GLN D C   1 
ATOM   9222  O  O   . GLN D 1 43  ? 1.606   15.788  -5.155  1.00 47.08  ? 43   GLN D O   1 
ATOM   9223  C  CB  . GLN D 1 43  ? -0.880  13.603  -5.401  1.00 41.34  ? 43   GLN D CB  1 
ATOM   9224  C  CG  . GLN D 1 43  ? -1.091  14.202  -4.006  1.00 56.96  ? 43   GLN D CG  1 
ATOM   9225  C  CD  . GLN D 1 43  ? -1.905  15.493  -4.024  1.00 59.71  ? 43   GLN D CD  1 
ATOM   9226  O  OE1 . GLN D 1 43  ? -2.761  15.701  -4.893  1.00 65.45  ? 43   GLN D OE1 1 
ATOM   9227  N  NE2 . GLN D 1 43  ? -1.642  16.366  -3.059  1.00 61.21  ? 43   GLN D NE2 1 
ATOM   9228  N  N   . GLU D 1 44  ? 2.189   13.699  -5.756  1.00 47.88  ? 44   GLU D N   1 
ATOM   9229  C  CA  . GLU D 1 44  ? 3.534   13.883  -5.238  1.00 53.04  ? 44   GLU D CA  1 
ATOM   9230  C  C   . GLU D 1 44  ? 4.232   15.015  -5.991  1.00 51.95  ? 44   GLU D C   1 
ATOM   9231  O  O   . GLU D 1 44  ? 4.774   15.936  -5.381  1.00 60.87  ? 44   GLU D O   1 
ATOM   9232  C  CB  . GLU D 1 44  ? 4.372   12.601  -5.301  1.00 52.92  ? 44   GLU D CB  1 
ATOM   9233  C  CG  . GLU D 1 44  ? 5.693   12.735  -4.537  1.00 72.02  ? 44   GLU D CG  1 
ATOM   9234  C  CD  . GLU D 1 44  ? 6.775   11.795  -5.034  1.00 95.72  ? 44   GLU D CD  1 
ATOM   9235  O  OE1 . GLU D 1 44  ? 6.470   10.930  -5.886  1.00 107.09 ? 44   GLU D OE1 1 
ATOM   9236  O  OE2 . GLU D 1 44  ? 7.933   11.926  -4.572  1.00 97.35  ? 44   GLU D OE2 1 
ATOM   9237  N  N   . GLN D 1 45  ? 4.207   14.957  -7.316  1.00 40.47  ? 45   GLN D N   1 
ATOM   9238  C  CA  . GLN D 1 45  ? 4.962   15.920  -8.102  1.00 44.42  ? 45   GLN D CA  1 
ATOM   9239  C  C   . GLN D 1 45  ? 4.511   17.348  -7.804  1.00 43.75  ? 45   GLN D C   1 
ATOM   9240  O  O   . GLN D 1 45  ? 5.301   18.294  -7.874  1.00 44.84  ? 45   GLN D O   1 
ATOM   9241  C  CB  . GLN D 1 45  ? 4.848   15.608  -9.597  1.00 46.19  ? 45   GLN D CB  1 
ATOM   9242  C  CG  . GLN D 1 45  ? 5.493   14.289  -9.990  1.00 50.21  ? 45   GLN D CG  1 
ATOM   9243  C  CD  . GLN D 1 45  ? 5.729   14.176  -11.482 1.00 55.01  ? 45   GLN D CD  1 
ATOM   9244  O  OE1 . GLN D 1 45  ? 4.785   14.086  -12.263 1.00 44.25  ? 45   GLN D OE1 1 
ATOM   9245  N  NE2 . GLN D 1 45  ? 6.998   14.169  -11.885 1.00 62.23  ? 45   GLN D NE2 1 
ATOM   9246  N  N   . LEU D 1 46  ? 3.239   17.495  -7.464  1.00 39.10  ? 46   LEU D N   1 
ATOM   9247  C  CA  . LEU D 1 46  ? 2.659   18.812  -7.218  1.00 47.06  ? 46   LEU D CA  1 
ATOM   9248  C  C   . LEU D 1 46  ? 3.170   19.401  -5.922  1.00 47.29  ? 46   LEU D C   1 
ATOM   9249  O  O   . LEU D 1 46  ? 3.572   20.568  -5.873  1.00 40.56  ? 46   LEU D O   1 
ATOM   9250  C  CB  . LEU D 1 46  ? 1.129   18.719  -7.165  1.00 42.06  ? 46   LEU D CB  1 
ATOM   9251  C  CG  . LEU D 1 46  ? 0.336   19.944  -6.700  1.00 42.26  ? 46   LEU D CG  1 
ATOM   9252  C  CD1 . LEU D 1 46  ? 0.806   21.224  -7.390  1.00 53.56  ? 46   LEU D CD1 1 
ATOM   9253  C  CD2 . LEU D 1 46  ? -1.174  19.721  -6.911  1.00 25.42  ? 46   LEU D CD2 1 
ATOM   9254  N  N   . GLU D 1 47  ? 3.133   18.583  -4.874  1.00 43.85  ? 47   GLU D N   1 
ATOM   9255  C  CA  . GLU D 1 47  ? 3.586   18.995  -3.563  1.00 47.19  ? 47   GLU D CA  1 
ATOM   9256  C  C   . GLU D 1 47  ? 5.071   19.321  -3.634  1.00 44.83  ? 47   GLU D C   1 
ATOM   9257  O  O   . GLU D 1 47  ? 5.527   20.350  -3.136  1.00 48.73  ? 47   GLU D O   1 
ATOM   9258  C  CB  . GLU D 1 47  ? 3.325   17.879  -2.546  1.00 55.67  ? 47   GLU D CB  1 
ATOM   9259  C  CG  . GLU D 1 47  ? 1.854   17.585  -2.287  1.00 48.01  ? 47   GLU D CG  1 
ATOM   9260  C  CD  . GLU D 1 47  ? 1.675   16.377  -1.407  1.00 48.88  ? 47   GLU D CD  1 
ATOM   9261  O  OE1 . GLU D 1 47  ? 2.554   15.494  -1.460  1.00 56.60  ? 47   GLU D OE1 1 
ATOM   9262  O  OE2 . GLU D 1 47  ? 0.667   16.304  -0.670  1.00 54.34  ? 47   GLU D OE2 1 
ATOM   9263  N  N   . ASP D 1 48  ? 5.825   18.435  -4.264  1.00 49.52  ? 48   ASP D N   1 
ATOM   9264  C  CA  . ASP D 1 48  ? 7.246   18.661  -4.450  1.00 54.50  ? 48   ASP D CA  1 
ATOM   9265  C  C   . ASP D 1 48  ? 7.487   20.010  -5.149  1.00 52.57  ? 48   ASP D C   1 
ATOM   9266  O  O   . ASP D 1 48  ? 8.264   20.829  -4.672  1.00 51.70  ? 48   ASP D O   1 
ATOM   9267  C  CB  . ASP D 1 48  ? 7.875   17.497  -5.222  1.00 59.95  ? 48   ASP D CB  1 
ATOM   9268  C  CG  . ASP D 1 48  ? 7.886   16.191  -4.418  1.00 68.86  ? 48   ASP D CG  1 
ATOM   9269  O  OD1 . ASP D 1 48  ? 7.873   16.244  -3.171  1.00 59.71  ? 48   ASP D OD1 1 
ATOM   9270  O  OD2 . ASP D 1 48  ? 7.918   15.106  -5.039  1.00 80.84  ? 48   ASP D OD2 1 
ATOM   9271  N  N   . LEU D 1 49  ? 6.796   20.263  -6.254  1.00 46.03  ? 49   LEU D N   1 
ATOM   9272  C  CA  . LEU D 1 49  ? 7.009   21.503  -6.992  1.00 38.71  ? 49   LEU D CA  1 
ATOM   9273  C  C   . LEU D 1 49  ? 6.701   22.739  -6.159  1.00 34.49  ? 49   LEU D C   1 
ATOM   9274  O  O   . LEU D 1 49  ? 7.388   23.753  -6.269  1.00 32.27  ? 49   LEU D O   1 
ATOM   9275  C  CB  . LEU D 1 49  ? 6.181   21.525  -8.276  1.00 45.75  ? 49   LEU D CB  1 
ATOM   9276  C  CG  . LEU D 1 49  ? 6.613   22.596  -9.286  1.00 47.13  ? 49   LEU D CG  1 
ATOM   9277  C  CD1 . LEU D 1 49  ? 6.496   22.078  -10.711 1.00 64.09  ? 49   LEU D CD1 1 
ATOM   9278  C  CD2 . LEU D 1 49  ? 5.834   23.883  -9.134  1.00 45.33  ? 49   LEU D CD2 1 
ATOM   9279  N  N   . PHE D 1 50  ? 5.656   22.654  -5.338  1.00 42.32  ? 50   PHE D N   1 
ATOM   9280  C  CA  . PHE D 1 50  ? 5.209   23.793  -4.532  1.00 41.22  ? 50   PHE D CA  1 
ATOM   9281  C  C   . PHE D 1 50  ? 6.169   24.108  -3.393  1.00 46.07  ? 50   PHE D C   1 
ATOM   9282  O  O   . PHE D 1 50  ? 6.296   25.259  -2.968  1.00 58.90  ? 50   PHE D O   1 
ATOM   9283  C  CB  . PHE D 1 50  ? 3.814   23.539  -3.969  1.00 41.00  ? 50   PHE D CB  1 
ATOM   9284  C  CG  . PHE D 1 50  ? 2.700   24.013  -4.864  1.00 41.16  ? 50   PHE D CG  1 
ATOM   9285  C  CD1 . PHE D 1 50  ? 2.950   24.344  -6.183  1.00 35.62  ? 50   PHE D CD1 1 
ATOM   9286  C  CD2 . PHE D 1 50  ? 1.399   24.126  -4.378  1.00 25.64  ? 50   PHE D CD2 1 
ATOM   9287  C  CE1 . PHE D 1 50  ? 1.919   24.780  -7.002  1.00 39.78  ? 50   PHE D CE1 1 
ATOM   9288  C  CE2 . PHE D 1 50  ? 0.377   24.551  -5.181  1.00 18.05  ? 50   PHE D CE2 1 
ATOM   9289  C  CZ  . PHE D 1 50  ? 0.627   24.879  -6.497  1.00 36.75  ? 50   PHE D CZ  1 
ATOM   9290  N  N   . ALA D 1 51  ? 6.829   23.075  -2.888  1.00 38.26  ? 51   ALA D N   1 
ATOM   9291  C  CA  . ALA D 1 51  ? 7.856   23.269  -1.883  1.00 45.67  ? 51   ALA D CA  1 
ATOM   9292  C  C   . ALA D 1 51  ? 9.104   23.899  -2.528  1.00 62.04  ? 51   ALA D C   1 
ATOM   9293  O  O   . ALA D 1 51  ? 9.779   24.739  -1.925  1.00 72.13  ? 51   ALA D O   1 
ATOM   9294  C  CB  . ALA D 1 51  ? 8.195   21.940  -1.215  1.00 33.59  ? 51   ALA D CB  1 
ATOM   9295  N  N   . GLY D 1 52  ? 9.399   23.497  -3.761  1.00 57.22  ? 52   GLY D N   1 
ATOM   9296  C  CA  . GLY D 1 52  ? 10.564  23.996  -4.470  1.00 47.77  ? 52   GLY D CA  1 
ATOM   9297  C  C   . GLY D 1 52  ? 10.488  25.484  -4.739  1.00 48.65  ? 52   GLY D C   1 
ATOM   9298  O  O   . GLY D 1 52  ? 11.482  26.205  -4.592  1.00 46.04  ? 52   GLY D O   1 
ATOM   9299  N  N   . LEU D 1 53  ? 9.308   25.948  -5.135  1.00 43.01  ? 53   LEU D N   1 
ATOM   9300  C  CA  . LEU D 1 53  ? 9.095   27.365  -5.389  1.00 42.79  ? 53   LEU D CA  1 
ATOM   9301  C  C   . LEU D 1 53  ? 9.186   28.173  -4.112  1.00 48.80  ? 53   LEU D C   1 
ATOM   9302  O  O   . LEU D 1 53  ? 9.718   29.276  -4.114  1.00 60.81  ? 53   LEU D O   1 
ATOM   9303  C  CB  . LEU D 1 53  ? 7.736   27.599  -6.023  1.00 38.16  ? 53   LEU D CB  1 
ATOM   9304  C  CG  . LEU D 1 53  ? 7.519   26.854  -7.330  1.00 43.13  ? 53   LEU D CG  1 
ATOM   9305  C  CD1 . LEU D 1 53  ? 6.174   27.215  -7.938  1.00 59.98  ? 53   LEU D CD1 1 
ATOM   9306  C  CD2 . LEU D 1 53  ? 8.645   27.154  -8.278  1.00 25.74  ? 53   LEU D CD2 1 
ATOM   9307  N  N   . GLU D 1 54  ? 8.656   27.627  -3.026  1.00 42.09  ? 54   GLU D N   1 
ATOM   9308  C  CA  . GLU D 1 54  ? 8.696   28.309  -1.738  1.00 58.78  ? 54   GLU D CA  1 
ATOM   9309  C  C   . GLU D 1 54  ? 10.141  28.599  -1.303  1.00 61.98  ? 54   GLU D C   1 
ATOM   9310  O  O   . GLU D 1 54  ? 10.444  29.677  -0.775  1.00 54.76  ? 54   GLU D O   1 
ATOM   9311  C  CB  . GLU D 1 54  ? 7.961   27.488  -0.674  1.00 65.40  ? 54   GLU D CB  1 
ATOM   9312  C  CG  . GLU D 1 54  ? 7.517   28.292  0.535   1.00 74.83  ? 54   GLU D CG  1 
ATOM   9313  C  CD  . GLU D 1 54  ? 6.581   27.516  1.449   1.00 77.57  ? 54   GLU D CD  1 
ATOM   9314  O  OE1 . GLU D 1 54  ? 6.026   28.129  2.390   1.00 76.63  ? 54   GLU D OE1 1 
ATOM   9315  O  OE2 . GLU D 1 54  ? 6.398   26.297  1.222   1.00 76.87  ? 54   GLU D OE2 1 
ATOM   9316  N  N   . LYS D 1 55  ? 11.038  27.645  -1.527  1.00 61.69  ? 55   LYS D N   1 
ATOM   9317  C  CA  . LYS D 1 55  ? 12.438  27.868  -1.185  1.00 58.29  ? 55   LYS D CA  1 
ATOM   9318  C  C   . LYS D 1 55  ? 13.175  28.591  -2.315  1.00 53.17  ? 55   LYS D C   1 
ATOM   9319  O  O   . LYS D 1 55  ? 14.033  29.430  -2.063  1.00 42.95  ? 55   LYS D O   1 
ATOM   9320  C  CB  . LYS D 1 55  ? 13.142  26.567  -0.789  1.00 50.41  ? 55   LYS D CB  1 
ATOM   9321  C  CG  . LYS D 1 55  ? 12.969  25.419  -1.764  1.00 58.21  ? 55   LYS D CG  1 
ATOM   9322  C  CD  . LYS D 1 55  ? 13.749  24.174  -1.305  1.00 61.58  ? 55   LYS D CD  1 
ATOM   9323  C  CE  . LYS D 1 55  ? 15.258  24.343  -1.474  1.00 61.96  ? 55   LYS D CE  1 
ATOM   9324  N  NZ  . LYS D 1 55  ? 16.016  23.125  -1.056  1.00 60.92  ? 55   LYS D NZ  1 
ATOM   9325  N  N   . ALA D 1 56  ? 12.827  28.290  -3.561  1.00 46.09  ? 56   ALA D N   1 
ATOM   9326  C  CA  . ALA D 1 56  ? 13.434  29.001  -4.679  1.00 44.11  ? 56   ALA D CA  1 
ATOM   9327  C  C   . ALA D 1 56  ? 13.046  30.481  -4.621  1.00 44.69  ? 56   ALA D C   1 
ATOM   9328  O  O   . ALA D 1 56  ? 13.821  31.355  -5.002  1.00 43.68  ? 56   ALA D O   1 
ATOM   9329  C  CB  . ALA D 1 56  ? 13.024  28.378  -6.006  1.00 34.17  ? 56   ALA D CB  1 
ATOM   9330  N  N   . TYR D 1 57  ? 11.846  30.753  -4.118  1.00 40.57  ? 57   TYR D N   1 
ATOM   9331  C  CA  . TYR D 1 57  ? 11.328  32.115  -4.058  1.00 43.78  ? 57   TYR D CA  1 
ATOM   9332  C  C   . TYR D 1 57  ? 10.779  32.443  -2.674  1.00 47.46  ? 57   TYR D C   1 
ATOM   9333  O  O   . TYR D 1 57  ? 9.571   32.642  -2.507  1.00 54.58  ? 57   TYR D O   1 
ATOM   9334  C  CB  . TYR D 1 57  ? 10.231  32.304  -5.102  1.00 36.46  ? 57   TYR D CB  1 
ATOM   9335  C  CG  . TYR D 1 57  ? 10.665  31.971  -6.516  1.00 55.21  ? 57   TYR D CG  1 
ATOM   9336  C  CD1 . TYR D 1 57  ? 10.602  30.667  -6.991  1.00 56.24  ? 57   TYR D CD1 1 
ATOM   9337  C  CD2 . TYR D 1 57  ? 11.133  32.963  -7.381  1.00 52.00  ? 57   TYR D CD2 1 
ATOM   9338  C  CE1 . TYR D 1 57  ? 10.990  30.354  -8.292  1.00 49.28  ? 57   TYR D CE1 1 
ATOM   9339  C  CE2 . TYR D 1 57  ? 11.519  32.659  -8.690  1.00 43.79  ? 57   TYR D CE2 1 
ATOM   9340  C  CZ  . TYR D 1 57  ? 11.442  31.352  -9.134  1.00 47.42  ? 57   TYR D CZ  1 
ATOM   9341  O  OH  . TYR D 1 57  ? 11.816  31.025  -10.419 1.00 46.80  ? 57   TYR D OH  1 
ATOM   9342  N  N   . PRO D 1 58  ? 11.673  32.516  -1.684  1.00 39.30  ? 58   PRO D N   1 
ATOM   9343  C  CA  . PRO D 1 58  ? 11.345  32.627  -0.261  1.00 33.04  ? 58   PRO D CA  1 
ATOM   9344  C  C   . PRO D 1 58  ? 10.335  33.716  0.080   1.00 55.12  ? 58   PRO D C   1 
ATOM   9345  O  O   . PRO D 1 58  ? 9.531   33.503  0.980   1.00 79.21  ? 58   PRO D O   1 
ATOM   9346  C  CB  . PRO D 1 58  ? 12.691  32.965  0.384   1.00 38.36  ? 58   PRO D CB  1 
ATOM   9347  C  CG  . PRO D 1 58  ? 13.715  32.405  -0.571  1.00 44.33  ? 58   PRO D CG  1 
ATOM   9348  C  CD  . PRO D 1 58  ? 13.126  32.561  -1.936  1.00 41.22  ? 58   PRO D CD  1 
ATOM   9349  N  N   . ASN D 1 59  ? 10.366  34.858  -0.594  1.00 55.82  ? 59   ASN D N   1 
ATOM   9350  C  CA  . ASN D 1 59  ? 9.546   35.993  -0.153  1.00 60.56  ? 59   ASN D CA  1 
ATOM   9351  C  C   . ASN D 1 59  ? 8.244   36.166  -0.944  1.00 52.36  ? 59   ASN D C   1 
ATOM   9352  O  O   . ASN D 1 59  ? 7.401   37.011  -0.622  1.00 39.90  ? 59   ASN D O   1 
ATOM   9353  C  CB  . ASN D 1 59  ? 10.358  37.295  -0.207  1.00 71.01  ? 59   ASN D CB  1 
ATOM   9354  C  CG  . ASN D 1 59  ? 11.696  37.191  0.510   1.00 79.08  ? 59   ASN D CG  1 
ATOM   9355  O  OD1 . ASN D 1 59  ? 12.300  36.120  0.587   1.00 75.66  ? 59   ASN D OD1 1 
ATOM   9356  N  ND2 . ASN D 1 59  ? 12.172  38.317  1.031   1.00 85.20  ? 59   ASN D ND2 1 
ATOM   9357  N  N   . GLN D 1 60  ? 8.077   35.368  -1.983  1.00 37.44  ? 60   GLN D N   1 
ATOM   9358  C  CA  . GLN D 1 60  ? 6.979   35.599  -2.899  1.00 44.74  ? 60   GLN D CA  1 
ATOM   9359  C  C   . GLN D 1 60  ? 6.184   34.341  -3.165  1.00 43.08  ? 60   GLN D C   1 
ATOM   9360  O  O   . GLN D 1 60  ? 5.108   34.396  -3.746  1.00 43.05  ? 60   GLN D O   1 
ATOM   9361  C  CB  . GLN D 1 60  ? 7.523   36.148  -4.205  1.00 45.12  ? 60   GLN D CB  1 
ATOM   9362  C  CG  . GLN D 1 60  ? 9.008   36.388  -4.154  1.00 60.75  ? 60   GLN D CG  1 
ATOM   9363  C  CD  . GLN D 1 60  ? 9.408   37.657  -4.868  1.00 68.16  ? 60   GLN D CD  1 
ATOM   9364  O  OE1 . GLN D 1 60  ? 10.554  37.802  -5.297  1.00 64.76  ? 60   GLN D OE1 1 
ATOM   9365  N  NE2 . GLN D 1 60  ? 8.464   38.589  -5.001  1.00 60.87  ? 60   GLN D NE2 1 
ATOM   9366  N  N   . ALA D 1 61  ? 6.720   33.203  -2.749  1.00 36.17  ? 61   ALA D N   1 
ATOM   9367  C  CA  . ALA D 1 61  ? 6.002   31.955  -2.881  1.00 28.89  ? 61   ALA D CA  1 
ATOM   9368  C  C   . ALA D 1 61  ? 5.788   31.386  -1.504  1.00 21.26  ? 61   ALA D C   1 
ATOM   9369  O  O   . ALA D 1 61  ? 6.746   31.170  -0.765  1.00 27.73  ? 61   ALA D O   1 
ATOM   9370  C  CB  . ALA D 1 61  ? 6.781   30.983  -3.730  1.00 39.07  ? 61   ALA D CB  1 
ATOM   9371  N  N   . LYS D 1 62  ? 4.527   31.150  -1.161  1.00 24.13  ? 62   LYS D N   1 
ATOM   9372  C  CA  . LYS D 1 62  ? 4.175   30.495  0.091   1.00 21.93  ? 62   LYS D CA  1 
ATOM   9373  C  C   . LYS D 1 62  ? 3.134   29.400  -0.137  1.00 24.57  ? 62   LYS D C   1 
ATOM   9374  O  O   . LYS D 1 62  ? 2.199   29.588  -0.906  1.00 38.13  ? 62   LYS D O   1 
ATOM   9375  C  CB  . LYS D 1 62  ? 3.662   31.522  1.092   1.00 30.73  ? 62   LYS D CB  1 
ATOM   9376  C  CG  . LYS D 1 62  ? 3.373   30.971  2.485   1.00 43.35  ? 62   LYS D CG  1 
ATOM   9377  C  CD  . LYS D 1 62  ? 3.068   32.109  3.457   1.00 61.75  ? 62   LYS D CD  1 
ATOM   9378  C  CE  . LYS D 1 62  ? 2.549   31.596  4.795   1.00 73.05  ? 62   LYS D CE  1 
ATOM   9379  N  NZ  . LYS D 1 62  ? 3.485   30.617  5.420   1.00 83.90  ? 62   LYS D NZ  1 
ATOM   9380  N  N   . VAL D 1 63  ? 3.319   28.251  0.511   1.00 31.82  ? 63   VAL D N   1 
ATOM   9381  C  CA  . VAL D 1 63  ? 2.349   27.162  0.439   1.00 32.14  ? 63   VAL D CA  1 
ATOM   9382  C  C   . VAL D 1 63  ? 1.345   27.204  1.601   1.00 46.18  ? 63   VAL D C   1 
ATOM   9383  O  O   . VAL D 1 63  ? 1.712   27.498  2.749   1.00 47.39  ? 63   VAL D O   1 
ATOM   9384  C  CB  . VAL D 1 63  ? 3.038   25.796  0.431   1.00 31.56  ? 63   VAL D CB  1 
ATOM   9385  C  CG1 . VAL D 1 63  ? 2.007   24.691  0.614   1.00 31.55  ? 63   VAL D CG1 1 
ATOM   9386  C  CG2 . VAL D 1 63  ? 3.809   25.610  -0.858  1.00 34.95  ? 63   VAL D CG2 1 
ATOM   9387  N  N   . HIS D 1 64  ? 0.085   26.903  1.285   1.00 40.08  ? 64   HIS D N   1 
ATOM   9388  C  CA  . HIS D 1 64  ? -1.009  26.978  2.243   1.00 29.97  ? 64   HIS D CA  1 
ATOM   9389  C  C   . HIS D 1 64  ? -1.758  25.674  2.283   1.00 33.80  ? 64   HIS D C   1 
ATOM   9390  O  O   . HIS D 1 64  ? -2.122  25.128  1.244   1.00 38.62  ? 64   HIS D O   1 
ATOM   9391  C  CB  . HIS D 1 64  ? -1.952  28.127  1.885   1.00 17.38  ? 64   HIS D CB  1 
ATOM   9392  C  CG  . HIS D 1 64  ? -1.292  29.466  1.965   1.00 35.92  ? 64   HIS D CG  1 
ATOM   9393  N  ND1 . HIS D 1 64  ? -1.254  30.210  3.125   1.00 43.46  ? 64   HIS D ND1 1 
ATOM   9394  C  CD2 . HIS D 1 64  ? -0.594  30.170  1.042   1.00 39.62  ? 64   HIS D CD2 1 
ATOM   9395  C  CE1 . HIS D 1 64  ? -0.586  31.329  2.903   1.00 49.25  ? 64   HIS D CE1 1 
ATOM   9396  N  NE2 . HIS D 1 64  ? -0.175  31.329  1.647   1.00 41.94  ? 64   HIS D NE2 1 
ATOM   9397  N  N   . PHE D 1 65  ? -1.981  25.172  3.492   1.00 33.70  ? 65   PHE D N   1 
ATOM   9398  C  CA  . PHE D 1 65  ? -2.709  23.926  3.673   1.00 36.41  ? 65   PHE D CA  1 
ATOM   9399  C  C   . PHE D 1 65  ? -4.173  24.234  3.969   1.00 35.92  ? 65   PHE D C   1 
ATOM   9400  O  O   . PHE D 1 65  ? -4.474  24.963  4.907   1.00 45.88  ? 65   PHE D O   1 
ATOM   9401  C  CB  . PHE D 1 65  ? -2.085  23.111  4.804   1.00 28.86  ? 65   PHE D CB  1 
ATOM   9402  C  CG  . PHE D 1 65  ? -2.912  21.935  5.230   1.00 40.81  ? 65   PHE D CG  1 
ATOM   9403  C  CD1 . PHE D 1 65  ? -3.875  22.074  6.226   1.00 46.11  ? 65   PHE D CD1 1 
ATOM   9404  C  CD2 . PHE D 1 65  ? -2.724  20.688  4.647   1.00 44.03  ? 65   PHE D CD2 1 
ATOM   9405  C  CE1 . PHE D 1 65  ? -4.639  20.992  6.636   1.00 54.77  ? 65   PHE D CE1 1 
ATOM   9406  C  CE2 . PHE D 1 65  ? -3.488  19.595  5.050   1.00 57.07  ? 65   PHE D CE2 1 
ATOM   9407  C  CZ  . PHE D 1 65  ? -4.446  19.747  6.049   1.00 62.91  ? 65   PHE D CZ  1 
ATOM   9408  N  N   . LEU D 1 66  ? -5.073  23.676  3.163   1.00 38.20  ? 66   LEU D N   1 
ATOM   9409  C  CA  . LEU D 1 66  ? -6.506  23.964  3.242   1.00 31.12  ? 66   LEU D CA  1 
ATOM   9410  C  C   . LEU D 1 66  ? -7.262  22.847  3.930   1.00 31.73  ? 66   LEU D C   1 
ATOM   9411  O  O   . LEU D 1 66  ? -8.291  23.061  4.565   1.00 32.80  ? 66   LEU D O   1 
ATOM   9412  C  CB  . LEU D 1 66  ? -7.077  24.109  1.833   1.00 20.52  ? 66   LEU D CB  1 
ATOM   9413  C  CG  . LEU D 1 66  ? -6.449  25.177  0.953   1.00 24.58  ? 66   LEU D CG  1 
ATOM   9414  C  CD1 . LEU D 1 66  ? -7.323  25.361  -0.264  1.00 22.37  ? 66   LEU D CD1 1 
ATOM   9415  C  CD2 . LEU D 1 66  ? -6.284  26.484  1.728   1.00 23.80  ? 66   LEU D CD2 1 
ATOM   9416  N  N   . GLY D 1 67  ? -6.759  21.637  3.758   1.00 35.79  ? 67   GLY D N   1 
ATOM   9417  C  CA  . GLY D 1 67  ? -7.407  20.474  4.312   1.00 39.02  ? 67   GLY D CA  1 
ATOM   9418  C  C   . GLY D 1 67  ? -6.862  19.206  3.698   1.00 37.68  ? 67   GLY D C   1 
ATOM   9419  O  O   . GLY D 1 67  ? -5.823  19.207  3.031   1.00 35.26  ? 67   GLY D O   1 
ATOM   9420  N  N   . ARG D 1 68  ? -7.572  18.112  3.936   1.00 43.49  ? 68   ARG D N   1 
ATOM   9421  C  CA  . ARG D 1 68  ? -7.206  16.831  3.355   1.00 40.08  ? 68   ARG D CA  1 
ATOM   9422  C  C   . ARG D 1 68  ? -8.422  16.116  2.762   1.00 47.41  ? 68   ARG D C   1 
ATOM   9423  O  O   . ARG D 1 68  ? -9.536  16.203  3.301   1.00 43.18  ? 68   ARG D O   1 
ATOM   9424  C  CB  . ARG D 1 68  ? -6.509  15.956  4.389   1.00 28.15  ? 68   ARG D CB  1 
ATOM   9425  C  CG  . ARG D 1 68  ? -4.998  15.925  4.226   1.00 38.32  ? 68   ARG D CG  1 
ATOM   9426  C  CD  . ARG D 1 68  ? -4.305  15.678  5.556   1.00 43.54  ? 68   ARG D CD  1 
ATOM   9427  N  NE  . ARG D 1 68  ? -2.883  15.442  5.397   1.00 40.30  ? 68   ARG D NE  1 
ATOM   9428  C  CZ  . ARG D 1 68  ? -1.969  15.818  6.284   1.00 67.00  ? 68   ARG D CZ  1 
ATOM   9429  N  NH1 . ARG D 1 68  ? -2.343  16.454  7.388   1.00 70.58  ? 68   ARG D NH1 1 
ATOM   9430  N  NH2 . ARG D 1 68  ? -0.680  15.560  6.067   1.00 82.70  ? 68   ARG D NH2 1 
ATOM   9431  N  N   . SER D 1 69  ? -8.191  15.434  1.637   1.00 45.61  ? 69   SER D N   1 
ATOM   9432  C  CA  . SER D 1 69  ? -9.199  14.616  0.970   1.00 26.47  ? 69   SER D CA  1 
ATOM   9433  C  C   . SER D 1 69  ? -9.535  13.414  1.845   1.00 38.51  ? 69   SER D C   1 
ATOM   9434  O  O   . SER D 1 69  ? -8.816  13.101  2.802   1.00 29.43  ? 69   SER D O   1 
ATOM   9435  C  CB  . SER D 1 69  ? -8.667  14.107  -0.369  1.00 25.76  ? 69   SER D CB  1 
ATOM   9436  O  OG  . SER D 1 69  ? -7.779  13.011  -0.175  1.00 27.76  ? 69   SER D OG  1 
ATOM   9437  N  N   . LEU D 1 70  ? -10.632 12.741  1.511   1.00 48.83  ? 70   LEU D N   1 
ATOM   9438  C  CA  . LEU D 1 70  ? -11.011 11.516  2.202   1.00 45.12  ? 70   LEU D CA  1 
ATOM   9439  C  C   . LEU D 1 70  ? -9.786  10.613  2.346   1.00 45.73  ? 70   LEU D C   1 
ATOM   9440  O  O   . LEU D 1 70  ? -9.507  10.113  3.436   1.00 50.21  ? 70   LEU D O   1 
ATOM   9441  C  CB  . LEU D 1 70  ? -12.109 10.776  1.428   1.00 47.38  ? 70   LEU D CB  1 
ATOM   9442  C  CG  . LEU D 1 70  ? -13.507 11.380  1.344   1.00 38.86  ? 70   LEU D CG  1 
ATOM   9443  C  CD1 . LEU D 1 70  ? -14.361 10.584  0.365   1.00 39.59  ? 70   LEU D CD1 1 
ATOM   9444  C  CD2 . LEU D 1 70  ? -14.136 11.396  2.709   1.00 28.68  ? 70   LEU D CD2 1 
ATOM   9445  N  N   . GLU D 1 71  ? -9.049  10.420  1.251   1.00 39.06  ? 71   GLU D N   1 
ATOM   9446  C  CA  . GLU D 1 71  ? -8.002  9.405   1.230   1.00 37.62  ? 71   GLU D CA  1 
ATOM   9447  C  C   . GLU D 1 71  ? -6.648  9.943   1.646   1.00 45.18  ? 71   GLU D C   1 
ATOM   9448  O  O   . GLU D 1 71  ? -5.624  9.327   1.349   1.00 54.42  ? 71   GLU D O   1 
ATOM   9449  C  CB  . GLU D 1 71  ? -7.926  8.731   -0.139  1.00 42.99  ? 71   GLU D CB  1 
ATOM   9450  C  CG  . GLU D 1 71  ? -9.219  8.016   -0.521  1.00 46.48  ? 71   GLU D CG  1 
ATOM   9451  C  CD  . GLU D 1 71  ? -9.149  7.353   -1.886  1.00 59.10  ? 71   GLU D CD  1 
ATOM   9452  O  OE1 . GLU D 1 71  ? -8.432  7.873   -2.774  1.00 64.29  ? 71   GLU D OE1 1 
ATOM   9453  O  OE2 . GLU D 1 71  ? -9.819  6.313   -2.070  1.00 59.07  ? 71   GLU D OE2 1 
ATOM   9454  N  N   . GLY D 1 72  ? -6.647  11.092  2.325   1.00 43.28  ? 72   GLY D N   1 
ATOM   9455  C  CA  . GLY D 1 72  ? -5.446  11.617  2.961   1.00 33.63  ? 72   GLY D CA  1 
ATOM   9456  C  C   . GLY D 1 72  ? -4.626  12.612  2.158   1.00 44.63  ? 72   GLY D C   1 
ATOM   9457  O  O   . GLY D 1 72  ? -3.688  13.211  2.683   1.00 47.41  ? 72   GLY D O   1 
ATOM   9458  N  N   . ARG D 1 73  ? -4.978  12.800  0.886   1.00 49.42  ? 73   ARG D N   1 
ATOM   9459  C  CA  . ARG D 1 73  ? -4.234  13.698  0.003   1.00 40.39  ? 73   ARG D CA  1 
ATOM   9460  C  C   . ARG D 1 73  ? -4.377  15.183  0.371   1.00 44.23  ? 73   ARG D C   1 
ATOM   9461  O  O   . ARG D 1 73  ? -5.483  15.683  0.567   1.00 46.98  ? 73   ARG D O   1 
ATOM   9462  C  CB  . ARG D 1 73  ? -4.677  13.477  -1.436  1.00 39.04  ? 73   ARG D CB  1 
ATOM   9463  C  CG  . ARG D 1 73  ? -4.525  12.058  -1.896  1.00 39.24  ? 73   ARG D CG  1 
ATOM   9464  C  CD  . ARG D 1 73  ? -4.861  11.896  -3.378  1.00 37.28  ? 73   ARG D CD  1 
ATOM   9465  N  NE  . ARG D 1 73  ? -5.423  10.570  -3.634  1.00 34.57  ? 73   ARG D NE  1 
ATOM   9466  C  CZ  . ARG D 1 73  ? -4.714  9.517   -4.022  1.00 33.95  ? 73   ARG D CZ  1 
ATOM   9467  N  NH1 . ARG D 1 73  ? -5.317  8.354   -4.218  1.00 30.82  ? 73   ARG D NH1 1 
ATOM   9468  N  NH2 . ARG D 1 73  ? -3.403  9.630   -4.221  1.00 44.37  ? 73   ARG D NH2 1 
ATOM   9469  N  N   . ASN D 1 74  ? -3.256  15.889  0.447   1.00 46.34  ? 74   ASN D N   1 
ATOM   9470  C  CA  . ASN D 1 74  ? -3.267  17.286  0.856   1.00 38.21  ? 74   ASN D CA  1 
ATOM   9471  C  C   . ASN D 1 74  ? -3.893  18.175  -0.177  1.00 37.42  ? 74   ASN D C   1 
ATOM   9472  O  O   . ASN D 1 74  ? -3.546  18.100  -1.349  1.00 46.79  ? 74   ASN D O   1 
ATOM   9473  C  CB  . ASN D 1 74  ? -1.855  17.782  1.148   1.00 33.49  ? 74   ASN D CB  1 
ATOM   9474  C  CG  . ASN D 1 74  ? -1.375  17.373  2.514   1.00 51.78  ? 74   ASN D CG  1 
ATOM   9475  O  OD1 . ASN D 1 74  ? -2.152  17.335  3.471   1.00 57.48  ? 74   ASN D OD1 1 
ATOM   9476  N  ND2 . ASN D 1 74  ? -0.083  17.067  2.623   1.00 65.09  ? 74   ASN D ND2 1 
ATOM   9477  N  N   . LEU D 1 75  ? -4.818  19.022  0.263   1.00 41.78  ? 75   LEU D N   1 
ATOM   9478  C  CA  . LEU D 1 75  ? -5.332  20.111  -0.572  1.00 34.01  ? 75   LEU D CA  1 
ATOM   9479  C  C   . LEU D 1 75  ? -4.493  21.366  -0.312  1.00 28.81  ? 75   LEU D C   1 
ATOM   9480  O  O   . LEU D 1 75  ? -4.508  21.924  0.785   1.00 37.10  ? 75   LEU D O   1 
ATOM   9481  C  CB  . LEU D 1 75  ? -6.806  20.376  -0.268  1.00 40.44  ? 75   LEU D CB  1 
ATOM   9482  C  CG  . LEU D 1 75  ? -7.852  19.407  -0.825  1.00 32.98  ? 75   LEU D CG  1 
ATOM   9483  C  CD1 . LEU D 1 75  ? -7.259  18.045  -1.133  1.00 47.19  ? 75   LEU D CD1 1 
ATOM   9484  C  CD2 . LEU D 1 75  ? -9.008  19.280  0.141   1.00 37.57  ? 75   LEU D CD2 1 
ATOM   9485  N  N   . LEU D 1 76  ? -3.751  21.796  -1.323  1.00 39.64  ? 76   LEU D N   1 
ATOM   9486  C  CA  . LEU D 1 76  ? -2.745  22.842  -1.161  1.00 33.77  ? 76   LEU D CA  1 
ATOM   9487  C  C   . LEU D 1 76  ? -2.994  24.038  -2.075  1.00 31.66  ? 76   LEU D C   1 
ATOM   9488  O  O   . LEU D 1 76  ? -3.486  23.885  -3.194  1.00 46.58  ? 76   LEU D O   1 
ATOM   9489  C  CB  . LEU D 1 76  ? -1.365  22.266  -1.494  1.00 36.08  ? 76   LEU D CB  1 
ATOM   9490  C  CG  . LEU D 1 76  ? -0.740  21.185  -0.606  1.00 49.42  ? 76   LEU D CG  1 
ATOM   9491  C  CD1 . LEU D 1 76  ? 0.486   20.584  -1.287  1.00 44.44  ? 76   LEU D CD1 1 
ATOM   9492  C  CD2 . LEU D 1 76  ? -0.376  21.737  0.780   1.00 52.81  ? 76   LEU D CD2 1 
ATOM   9493  N  N   . ALA D 1 77  ? -2.617  25.225  -1.613  1.00 42.43  ? 77   ALA D N   1 
ATOM   9494  C  CA  . ALA D 1 77  ? -2.702  26.440  -2.426  1.00 33.52  ? 77   ALA D CA  1 
ATOM   9495  C  C   . ALA D 1 77  ? -1.392  27.204  -2.365  1.00 30.56  ? 77   ALA D C   1 
ATOM   9496  O  O   . ALA D 1 77  ? -0.883  27.479  -1.282  1.00 41.88  ? 77   ALA D O   1 
ATOM   9497  C  CB  . ALA D 1 77  ? -3.837  27.327  -1.942  1.00 31.36  ? 77   ALA D CB  1 
ATOM   9498  N  N   . LEU D 1 78  ? -0.848  27.552  -3.524  1.00 33.89  ? 78   LEU D N   1 
ATOM   9499  C  CA  . LEU D 1 78  ? 0.365   28.350  -3.562  1.00 22.15  ? 78   LEU D CA  1 
ATOM   9500  C  C   . LEU D 1 78  ? 0.013   29.826  -3.681  1.00 30.96  ? 78   LEU D C   1 
ATOM   9501  O  O   . LEU D 1 78  ? -0.661  30.240  -4.630  1.00 30.92  ? 78   LEU D O   1 
ATOM   9502  C  CB  . LEU D 1 78  ? 1.248   27.927  -4.726  1.00 20.74  ? 78   LEU D CB  1 
ATOM   9503  C  CG  . LEU D 1 78  ? 2.629   28.591  -4.830  1.00 36.69  ? 78   LEU D CG  1 
ATOM   9504  C  CD1 . LEU D 1 78  ? 3.589   28.146  -3.724  1.00 23.30  ? 78   LEU D CD1 1 
ATOM   9505  C  CD2 . LEU D 1 78  ? 3.241   28.321  -6.202  1.00 30.01  ? 78   LEU D CD2 1 
ATOM   9506  N  N   . GLN D 1 79  ? 0.453   30.608  -2.701  1.00 20.68  ? 79   GLN D N   1 
ATOM   9507  C  CA  . GLN D 1 79  ? 0.292   32.051  -2.722  1.00 22.93  ? 79   GLN D CA  1 
ATOM   9508  C  C   . GLN D 1 79  ? 1.510   32.697  -3.367  1.00 36.76  ? 79   GLN D C   1 
ATOM   9509  O  O   . GLN D 1 79  ? 2.641   32.293  -3.121  1.00 41.12  ? 79   GLN D O   1 
ATOM   9510  C  CB  . GLN D 1 79  ? 0.126   32.587  -1.303  1.00 27.26  ? 79   GLN D CB  1 
ATOM   9511  C  CG  . GLN D 1 79  ? 0.440   34.055  -1.159  1.00 27.44  ? 79   GLN D CG  1 
ATOM   9512  C  CD  . GLN D 1 79  ? 0.327   34.535  0.279   1.00 39.75  ? 79   GLN D CD  1 
ATOM   9513  O  OE1 . GLN D 1 79  ? 0.429   33.742  1.225   1.00 35.05  ? 79   GLN D OE1 1 
ATOM   9514  N  NE2 . GLN D 1 79  ? 0.119   35.844  0.455   1.00 38.84  ? 79   GLN D NE2 1 
ATOM   9515  N  N   . ILE D 1 80  ? 1.266   33.699  -4.204  1.00 46.61  ? 80   ILE D N   1 
ATOM   9516  C  CA  . ILE D 1 80  ? 2.326   34.488  -4.832  1.00 36.48  ? 80   ILE D CA  1 
ATOM   9517  C  C   . ILE D 1 80  ? 2.015   35.956  -4.596  1.00 39.69  ? 80   ILE D C   1 
ATOM   9518  O  O   . ILE D 1 80  ? 0.918   36.432  -4.925  1.00 50.35  ? 80   ILE D O   1 
ATOM   9519  C  CB  . ILE D 1 80  ? 2.384   34.276  -6.364  1.00 29.62  ? 80   ILE D CB  1 
ATOM   9520  C  CG1 . ILE D 1 80  ? 2.681   32.818  -6.715  1.00 25.82  ? 80   ILE D CG1 1 
ATOM   9521  C  CG2 . ILE D 1 80  ? 3.419   35.206  -6.989  1.00 24.74  ? 80   ILE D CG2 1 
ATOM   9522  C  CD1 . ILE D 1 80  ? 2.347   32.485  -8.160  1.00 22.08  ? 80   ILE D CD1 1 
ATOM   9523  N  N   . SER D 1 81  ? 2.974   36.683  -4.039  1.00 41.04  ? 81   SER D N   1 
ATOM   9524  C  CA  . SER D 1 81  ? 2.714   38.059  -3.664  1.00 42.77  ? 81   SER D CA  1 
ATOM   9525  C  C   . SER D 1 81  ? 3.985   38.874  -3.700  1.00 42.19  ? 81   SER D C   1 
ATOM   9526  O  O   . SER D 1 81  ? 5.072   38.319  -3.806  1.00 49.36  ? 81   SER D O   1 
ATOM   9527  C  CB  . SER D 1 81  ? 2.113   38.105  -2.261  1.00 40.65  ? 81   SER D CB  1 
ATOM   9528  O  OG  . SER D 1 81  ? 3.037   37.577  -1.325  1.00 54.32  ? 81   SER D OG  1 
ATOM   9529  N  N   . ARG D 1 82  ? 3.839   40.192  -3.622  1.00 45.36  ? 82   ARG D N   1 
ATOM   9530  C  CA  . ARG D 1 82  ? 4.979   41.084  -3.485  1.00 51.16  ? 82   ARG D CA  1 
ATOM   9531  C  C   . ARG D 1 82  ? 5.735   40.698  -2.214  1.00 55.94  ? 82   ARG D C   1 
ATOM   9532  O  O   . ARG D 1 82  ? 6.969   40.651  -2.185  1.00 59.02  ? 82   ARG D O   1 
ATOM   9533  C  CB  . ARG D 1 82  ? 4.504   42.541  -3.415  1.00 48.61  ? 82   ARG D CB  1 
ATOM   9534  C  CG  . ARG D 1 82  ? 5.603   43.574  -3.234  1.00 55.88  ? 82   ARG D CG  1 
ATOM   9535  C  CD  . ARG D 1 82  ? 5.543   44.666  -4.310  1.00 66.54  ? 82   ARG D CD  1 
ATOM   9536  N  NE  . ARG D 1 82  ? 5.263   45.990  -3.762  1.00 73.17  ? 82   ARG D NE  1 
ATOM   9537  C  CZ  . ARG D 1 82  ? 5.539   47.151  -4.361  1.00 81.70  ? 82   ARG D CZ  1 
ATOM   9538  N  NH1 . ARG D 1 82  ? 5.231   48.284  -3.749  1.00 75.57  ? 82   ARG D NH1 1 
ATOM   9539  N  NH2 . ARG D 1 82  ? 6.120   47.199  -5.554  1.00 86.43  ? 82   ARG D NH2 1 
ATOM   9540  N  N   . ASN D 1 83  ? 4.974   40.397  -1.168  1.00 36.85  ? 83   ASN D N   1 
ATOM   9541  C  CA  . ASN D 1 83  ? 5.545   39.997  0.102   1.00 39.40  ? 83   ASN D CA  1 
ATOM   9542  C  C   . ASN D 1 83  ? 4.633   39.003  0.798   1.00 41.77  ? 83   ASN D C   1 
ATOM   9543  O  O   . ASN D 1 83  ? 3.621   39.372  1.394   1.00 43.15  ? 83   ASN D O   1 
ATOM   9544  C  CB  . ASN D 1 83  ? 5.760   41.215  0.998   1.00 58.15  ? 83   ASN D CB  1 
ATOM   9545  C  CG  . ASN D 1 83  ? 6.028   40.836  2.442   1.00 70.35  ? 83   ASN D CG  1 
ATOM   9546  O  OD1 . ASN D 1 83  ? 6.605   39.780  2.724   1.00 71.95  ? 83   ASN D OD1 1 
ATOM   9547  N  ND2 . ASN D 1 83  ? 5.610   41.700  3.370   1.00 71.01  ? 83   ASN D ND2 1 
ATOM   9548  N  N   . THR D 1 84  ? 5.007   37.736  0.733   1.00 47.66  ? 84   THR D N   1 
ATOM   9549  C  CA  . THR D 1 84  ? 4.168   36.664  1.249   1.00 35.70  ? 84   THR D CA  1 
ATOM   9550  C  C   . THR D 1 84  ? 3.855   36.780  2.745   1.00 32.09  ? 84   THR D C   1 
ATOM   9551  O  O   . THR D 1 84  ? 2.897   36.167  3.227   1.00 37.65  ? 84   THR D O   1 
ATOM   9552  C  CB  . THR D 1 84  ? 4.786   35.285  0.916   1.00 39.67  ? 84   THR D CB  1 
ATOM   9553  O  OG1 . THR D 1 84  ? 3.821   34.478  0.234   1.00 48.18  ? 84   THR D OG1 1 
ATOM   9554  C  CG2 . THR D 1 84  ? 5.276   34.570  2.176   1.00 26.95  ? 84   THR D CG2 1 
ATOM   9555  N  N   . ARG D 1 85  ? 4.646   37.569  3.470   1.00 37.69  ? 85   ARG D N   1 
ATOM   9556  C  CA  . ARG D 1 85  ? 4.468   37.689  4.919   1.00 42.31  ? 85   ARG D CA  1 
ATOM   9557  C  C   . ARG D 1 85  ? 3.081   38.205  5.253   1.00 45.03  ? 85   ARG D C   1 
ATOM   9558  O  O   . ARG D 1 85  ? 2.378   37.627  6.073   1.00 53.43  ? 85   ARG D O   1 
ATOM   9559  C  CB  . ARG D 1 85  ? 5.533   38.598  5.555   1.00 55.96  ? 85   ARG D CB  1 
ATOM   9560  C  CG  . ARG D 1 85  ? 6.946   38.040  5.535   1.00 71.30  ? 85   ARG D CG  1 
ATOM   9561  C  CD  . ARG D 1 85  ? 7.785   38.659  6.642   1.00 94.54  ? 85   ARG D CD  1 
ATOM   9562  N  NE  . ARG D 1 85  ? 7.588   38.023  7.948   1.00 102.30 ? 85   ARG D NE  1 
ATOM   9563  C  CZ  . ARG D 1 85  ? 6.756   38.462  8.893   1.00 99.01  ? 85   ARG D CZ  1 
ATOM   9564  N  NH1 . ARG D 1 85  ? 6.663   37.813  10.048  1.00 91.94  ? 85   ARG D NH1 1 
ATOM   9565  N  NH2 . ARG D 1 85  ? 6.015   39.543  8.690   1.00 96.90  ? 85   ARG D NH2 1 
ATOM   9566  N  N   . SER D 1 86  ? 2.677   39.292  4.611   1.00 46.43  ? 86   SER D N   1 
ATOM   9567  C  CA  . SER D 1 86  ? 1.362   39.848  4.868   1.00 36.28  ? 86   SER D CA  1 
ATOM   9568  C  C   . SER D 1 86  ? 0.650   40.057  3.562   1.00 53.91  ? 86   SER D C   1 
ATOM   9569  O  O   . SER D 1 86  ? 0.918   39.370  2.577   1.00 67.08  ? 86   SER D O   1 
ATOM   9570  C  CB  . SER D 1 86  ? 1.494   41.190  5.577   1.00 43.79  ? 86   SER D CB  1 
ATOM   9571  O  OG  . SER D 1 86  ? 2.044   41.037  6.875   1.00 56.14  ? 86   SER D OG  1 
ATOM   9572  N  N   . ARG D 1 87  ? -0.266  41.017  3.575   1.00 54.23  ? 87   ARG D N   1 
ATOM   9573  C  CA  . ARG D 1 87  ? -0.924  41.500  2.367   1.00 48.70  ? 87   ARG D CA  1 
ATOM   9574  C  C   . ARG D 1 87  ? -0.974  43.010  2.440   1.00 41.78  ? 87   ARG D C   1 
ATOM   9575  O  O   . ARG D 1 87  ? -1.533  43.568  3.376   1.00 34.04  ? 87   ARG D O   1 
ATOM   9576  C  CB  . ARG D 1 87  ? -2.347  40.969  2.256   1.00 17.22  ? 87   ARG D CB  1 
ATOM   9577  C  CG  . ARG D 1 87  ? -2.803  40.826  0.840   1.00 19.48  ? 87   ARG D CG  1 
ATOM   9578  C  CD  . ARG D 1 87  ? -4.286  40.554  0.756   1.00 31.29  ? 87   ARG D CD  1 
ATOM   9579  N  NE  . ARG D 1 87  ? -5.023  41.810  0.746   1.00 48.42  ? 87   ARG D NE  1 
ATOM   9580  C  CZ  . ARG D 1 87  ? -5.726  42.286  1.768   1.00 48.79  ? 87   ARG D CZ  1 
ATOM   9581  N  NH1 . ARG D 1 87  ? -5.817  41.610  2.908   1.00 54.94  ? 87   ARG D NH1 1 
ATOM   9582  N  NH2 . ARG D 1 87  ? -6.345  43.448  1.636   1.00 47.04  ? 87   ARG D NH2 1 
ATOM   9583  N  N   . ASN D 1 88  ? -0.386  43.676  1.458   1.00 52.30  ? 88   ASN D N   1 
ATOM   9584  C  CA  . ASN D 1 88  ? -0.360  45.130  1.470   1.00 45.32  ? 88   ASN D CA  1 
ATOM   9585  C  C   . ASN D 1 88  ? -1.767  45.691  1.440   1.00 39.18  ? 88   ASN D C   1 
ATOM   9586  O  O   . ASN D 1 88  ? -2.651  45.152  0.775   1.00 36.81  ? 88   ASN D O   1 
ATOM   9587  C  CB  . ASN D 1 88  ? 0.504   45.676  0.332   1.00 47.83  ? 88   ASN D CB  1 
ATOM   9588  C  CG  . ASN D 1 88  ? 1.967   45.309  0.497   1.00 55.98  ? 88   ASN D CG  1 
ATOM   9589  O  OD1 . ASN D 1 88  ? 2.554   44.636  -0.352  1.00 67.89  ? 88   ASN D OD1 1 
ATOM   9590  N  ND2 . ASN D 1 88  ? 2.556   45.727  1.612   1.00 59.23  ? 88   ASN D ND2 1 
ATOM   9591  N  N   . LEU D 1 89  ? -1.974  46.750  2.205   1.00 22.92  ? 89   LEU D N   1 
ATOM   9592  C  CA  . LEU D 1 89  ? -3.259  47.392  2.257   1.00 28.62  ? 89   LEU D CA  1 
ATOM   9593  C  C   . LEU D 1 89  ? -3.766  47.645  0.850   1.00 38.94  ? 89   LEU D C   1 
ATOM   9594  O  O   . LEU D 1 89  ? -3.049  48.183  -0.003  1.00 41.99  ? 89   LEU D O   1 
ATOM   9595  C  CB  . LEU D 1 89  ? -3.165  48.708  3.019   1.00 30.23  ? 89   LEU D CB  1 
ATOM   9596  C  CG  . LEU D 1 89  ? -4.503  49.259  3.501   1.00 34.57  ? 89   LEU D CG  1 
ATOM   9597  C  CD1 . LEU D 1 89  ? -5.084  48.368  4.593   1.00 23.75  ? 89   LEU D CD1 1 
ATOM   9598  C  CD2 . LEU D 1 89  ? -4.323  50.675  3.998   1.00 36.49  ? 89   LEU D CD2 1 
ATOM   9599  N  N   . LEU D 1 90  ? -5.007  47.238  0.615   1.00 44.67  ? 90   LEU D N   1 
ATOM   9600  C  CA  . LEU D 1 90  ? -5.706  47.484  -0.647  1.00 43.58  ? 90   LEU D CA  1 
ATOM   9601  C  C   . LEU D 1 90  ? -5.247  46.609  -1.809  1.00 38.06  ? 90   LEU D C   1 
ATOM   9602  O  O   . LEU D 1 90  ? -5.734  46.756  -2.924  1.00 33.53  ? 90   LEU D O   1 
ATOM   9603  C  CB  . LEU D 1 90  ? -5.698  48.975  -1.015  1.00 32.66  ? 90   LEU D CB  1 
ATOM   9604  C  CG  . LEU D 1 90  ? -6.633  49.780  -0.102  1.00 39.31  ? 90   LEU D CG  1 
ATOM   9605  C  CD1 . LEU D 1 90  ? -6.550  51.284  -0.356  1.00 25.78  ? 90   LEU D CD1 1 
ATOM   9606  C  CD2 . LEU D 1 90  ? -8.072  49.290  -0.238  1.00 25.52  ? 90   LEU D CD2 1 
ATOM   9607  N  N   . THR D 1 91  ? -4.332  45.683  -1.544  1.00 39.98  ? 91   THR D N   1 
ATOM   9608  C  CA  . THR D 1 91  ? -3.999  44.677  -2.554  1.00 45.09  ? 91   THR D CA  1 
ATOM   9609  C  C   . THR D 1 91  ? -5.106  43.621  -2.602  1.00 37.05  ? 91   THR D C   1 
ATOM   9610  O  O   . THR D 1 91  ? -5.473  43.019  -1.583  1.00 25.75  ? 91   THR D O   1 
ATOM   9611  C  CB  . THR D 1 91  ? -2.600  43.989  -2.328  1.00 42.82  ? 91   THR D CB  1 
ATOM   9612  O  OG1 . THR D 1 91  ? -1.534  44.944  -2.469  1.00 25.43  ? 91   THR D OG1 1 
ATOM   9613  C  CG2 . THR D 1 91  ? -2.387  42.831  -3.331  1.00 25.86  ? 91   THR D CG2 1 
ATOM   9614  N  N   . PRO D 1 92  ? -5.639  43.395  -3.799  1.00 28.43  ? 92   PRO D N   1 
ATOM   9615  C  CA  . PRO D 1 92  ? -6.692  42.406  -4.028  1.00 33.40  ? 92   PRO D CA  1 
ATOM   9616  C  C   . PRO D 1 92  ? -6.180  40.980  -3.897  1.00 41.21  ? 92   PRO D C   1 
ATOM   9617  O  O   . PRO D 1 92  ? -5.283  40.588  -4.658  1.00 31.71  ? 92   PRO D O   1 
ATOM   9618  C  CB  . PRO D 1 92  ? -7.091  42.643  -5.491  1.00 33.01  ? 92   PRO D CB  1 
ATOM   9619  C  CG  . PRO D 1 92  ? -6.359  43.887  -5.936  1.00 29.70  ? 92   PRO D CG  1 
ATOM   9620  C  CD  . PRO D 1 92  ? -5.180  44.025  -5.047  1.00 30.12  ? 92   PRO D CD  1 
ATOM   9621  N  N   . PRO D 1 93  ? -6.745  40.209  -2.955  1.00 40.15  ? 93   PRO D N   1 
ATOM   9622  C  CA  . PRO D 1 93  ? -6.489  38.769  -2.958  1.00 37.27  ? 93   PRO D CA  1 
ATOM   9623  C  C   . PRO D 1 93  ? -7.390  38.113  -4.011  1.00 38.93  ? 93   PRO D C   1 
ATOM   9624  O  O   . PRO D 1 93  ? -8.554  38.484  -4.181  1.00 33.54  ? 93   PRO D O   1 
ATOM   9625  C  CB  . PRO D 1 93  ? -6.865  38.340  -1.537  1.00 26.62  ? 93   PRO D CB  1 
ATOM   9626  C  CG  . PRO D 1 93  ? -7.899  39.350  -1.087  1.00 28.53  ? 93   PRO D CG  1 
ATOM   9627  C  CD  . PRO D 1 93  ? -7.742  40.600  -1.944  1.00 24.88  ? 93   PRO D CD  1 
ATOM   9628  N  N   . VAL D 1 94  ? -6.838  37.160  -4.741  1.00 29.83  ? 94   VAL D N   1 
ATOM   9629  C  CA  . VAL D 1 94  ? -7.568  36.514  -5.814  1.00 19.77  ? 94   VAL D CA  1 
ATOM   9630  C  C   . VAL D 1 94  ? -7.196  35.040  -5.812  1.00 31.42  ? 94   VAL D C   1 
ATOM   9631  O  O   . VAL D 1 94  ? -6.154  34.666  -5.256  1.00 41.69  ? 94   VAL D O   1 
ATOM   9632  C  CB  . VAL D 1 94  ? -7.173  37.123  -7.146  1.00 34.74  ? 94   VAL D CB  1 
ATOM   9633  C  CG1 . VAL D 1 94  ? -7.969  36.507  -8.286  1.00 56.65  ? 94   VAL D CG1 1 
ATOM   9634  C  CG2 . VAL D 1 94  ? -7.386  38.610  -7.095  1.00 40.15  ? 94   VAL D CG2 1 
ATOM   9635  N  N   . LYS D 1 95  ? -8.038  34.199  -6.416  1.00 17.89  ? 95   LYS D N   1 
ATOM   9636  C  CA  . LYS D 1 95  ? -7.756  32.767  -6.462  1.00 23.97  ? 95   LYS D CA  1 
ATOM   9637  C  C   . LYS D 1 95  ? -8.126  32.121  -7.780  1.00 32.38  ? 95   LYS D C   1 
ATOM   9638  O  O   . LYS D 1 95  ? -9.015  32.589  -8.489  1.00 31.22  ? 95   LYS D O   1 
ATOM   9639  C  CB  . LYS D 1 95  ? -8.474  32.037  -5.335  1.00 15.77  ? 95   LYS D CB  1 
ATOM   9640  C  CG  . LYS D 1 95  ? -9.965  32.262  -5.320  1.00 14.77  ? 95   LYS D CG  1 
ATOM   9641  C  CD  . LYS D 1 95  ? -10.420 32.474  -3.892  1.00 25.80  ? 95   LYS D CD  1 
ATOM   9642  C  CE  . LYS D 1 95  ? -11.791 31.858  -3.621  1.00 33.87  ? 95   LYS D CE  1 
ATOM   9643  N  NZ  . LYS D 1 95  ? -12.817 32.297  -4.599  1.00 42.07  ? 95   LYS D NZ  1 
ATOM   9644  N  N   . TYR D 1 96  ? -7.423  31.038  -8.090  1.00 33.70  ? 96   TYR D N   1 
ATOM   9645  C  CA  . TYR D 1 96  ? -7.751  30.155  -9.206  1.00 37.01  ? 96   TYR D CA  1 
ATOM   9646  C  C   . TYR D 1 96  ? -7.825  28.715  -8.680  1.00 43.14  ? 96   TYR D C   1 
ATOM   9647  O  O   . TYR D 1 96  ? -6.850  28.194  -8.110  1.00 34.23  ? 96   TYR D O   1 
ATOM   9648  C  CB  . TYR D 1 96  ? -6.679  30.222  -10.307 1.00 28.51  ? 96   TYR D CB  1 
ATOM   9649  C  CG  . TYR D 1 96  ? -6.850  31.334  -11.321 1.00 27.48  ? 96   TYR D CG  1 
ATOM   9650  C  CD1 . TYR D 1 96  ? -8.082  31.920  -11.538 1.00 31.66  ? 96   TYR D CD1 1 
ATOM   9651  C  CD2 . TYR D 1 96  ? -5.778  31.777  -12.075 1.00 32.16  ? 96   TYR D CD2 1 
ATOM   9652  C  CE1 . TYR D 1 96  ? -8.241  32.923  -12.456 1.00 22.04  ? 96   TYR D CE1 1 
ATOM   9653  C  CE2 . TYR D 1 96  ? -5.931  32.779  -13.000 1.00 44.01  ? 96   TYR D CE2 1 
ATOM   9654  C  CZ  . TYR D 1 96  ? -7.170  33.348  -13.184 1.00 40.69  ? 96   TYR D CZ  1 
ATOM   9655  O  OH  . TYR D 1 96  ? -7.339  34.352  -14.108 1.00 52.53  ? 96   TYR D OH  1 
ATOM   9656  N  N   . ILE D 1 97  ? -8.973  28.066  -8.854  1.00 34.71  ? 97   ILE D N   1 
ATOM   9657  C  CA  . ILE D 1 97  ? -9.069  26.660  -8.483  1.00 26.91  ? 97   ILE D CA  1 
ATOM   9658  C  C   . ILE D 1 97  ? -9.273  25.846  -9.731  1.00 27.13  ? 97   ILE D C   1 
ATOM   9659  O  O   . ILE D 1 97  ? -9.831  26.340  -10.712 1.00 26.93  ? 97   ILE D O   1 
ATOM   9660  C  CB  . ILE D 1 97  ? -10.225 26.366  -7.518  1.00 29.23  ? 97   ILE D CB  1 
ATOM   9661  C  CG1 . ILE D 1 97  ? -10.094 27.179  -6.220  1.00 30.24  ? 97   ILE D CG1 1 
ATOM   9662  C  CG2 . ILE D 1 97  ? -10.243 24.884  -7.193  1.00 24.95  ? 97   ILE D CG2 1 
ATOM   9663  C  CD1 . ILE D 1 97  ? -10.597 28.602  -6.296  1.00 28.70  ? 97   ILE D CD1 1 
ATOM   9664  N  N   . ALA D 1 98  ? -8.814  24.601  -9.706  1.00 28.12  ? 98   ALA D N   1 
ATOM   9665  C  CA  . ALA D 1 98  ? -9.046  23.702  -10.832 1.00 27.95  ? 98   ALA D CA  1 
ATOM   9666  C  C   . ALA D 1 98  ? -9.296  22.254  -10.404 1.00 38.86  ? 98   ALA D C   1 
ATOM   9667  O  O   . ALA D 1 98  ? -9.179  21.898  -9.220  1.00 42.65  ? 98   ALA D O   1 
ATOM   9668  C  CB  . ALA D 1 98  ? -7.885  23.774  -11.825 1.00 23.49  ? 98   ALA D CB  1 
ATOM   9669  N  N   . ASN D 1 99  ? -9.653  21.434  -11.389 1.00 39.72  ? 99   ASN D N   1 
ATOM   9670  C  CA  . ASN D 1 99  ? -9.737  19.993  -11.205 1.00 26.49  ? 99   ASN D CA  1 
ATOM   9671  C  C   . ASN D 1 99  ? -10.681 19.556  -10.061 1.00 44.19  ? 99   ASN D C   1 
ATOM   9672  O  O   . ASN D 1 99  ? -10.448 18.532  -9.410  1.00 44.02  ? 99   ASN D O   1 
ATOM   9673  C  CB  . ASN D 1 99  ? -8.315  19.428  -11.020 1.00 28.55  ? 99   ASN D CB  1 
ATOM   9674  C  CG  . ASN D 1 99  ? -8.241  17.914  -11.231 1.00 39.33  ? 99   ASN D CG  1 
ATOM   9675  O  OD1 . ASN D 1 99  ? -7.545  17.219  -10.491 1.00 35.52  ? 99   ASN D OD1 1 
ATOM   9676  N  ND2 . ASN D 1 99  ? -8.961  17.402  -12.238 1.00 27.16  ? 99   ASN D ND2 1 
ATOM   9677  N  N   . MET D 1 100 ? -11.749 20.324  -9.820  1.00 48.48  ? 100  MET D N   1 
ATOM   9678  C  CA  . MET D 1 100 ? -12.753 19.913  -8.830  1.00 43.01  ? 100  MET D CA  1 
ATOM   9679  C  C   . MET D 1 100 ? -13.498 18.671  -9.313  1.00 43.06  ? 100  MET D C   1 
ATOM   9680  O  O   . MET D 1 100 ? -13.906 17.832  -8.506  1.00 42.59  ? 100  MET D O   1 
ATOM   9681  C  CB  . MET D 1 100 ? -13.729 21.039  -8.476  1.00 39.05  ? 100  MET D CB  1 
ATOM   9682  C  CG  . MET D 1 100 ? -14.895 21.191  -9.399  1.00 47.69  ? 100  MET D CG  1 
ATOM   9683  S  SD  . MET D 1 100 ? -16.002 22.486  -8.811  1.00 38.74  ? 100  MET D SD  1 
ATOM   9684  C  CE  . MET D 1 100 ? -16.215 22.038  -7.113  1.00 21.65  ? 100  MET D CE  1 
ATOM   9685  N  N   . HIS D 1 101 ? -13.670 18.559  -10.631 1.00 39.53  ? 101  HIS D N   1 
ATOM   9686  C  CA  . HIS D 1 101 ? -14.008 17.276  -11.249 1.00 31.00  ? 101  HIS D CA  1 
ATOM   9687  C  C   . HIS D 1 101 ? -12.699 16.620  -11.693 1.00 36.02  ? 101  HIS D C   1 
ATOM   9688  O  O   . HIS D 1 101 ? -12.013 17.097  -12.603 1.00 26.81  ? 101  HIS D O   1 
ATOM   9689  C  CB  . HIS D 1 101 ? -14.999 17.436  -12.407 1.00 20.66  ? 101  HIS D CB  1 
ATOM   9690  C  CG  . HIS D 1 101 ? -16.307 18.058  -12.006 1.00 39.39  ? 101  HIS D CG  1 
ATOM   9691  N  ND1 . HIS D 1 101 ? -16.666 19.346  -12.357 1.00 40.46  ? 101  HIS D ND1 1 
ATOM   9692  C  CD2 . HIS D 1 101 ? -17.338 17.567  -11.279 1.00 51.46  ? 101  HIS D CD2 1 
ATOM   9693  C  CE1 . HIS D 1 101 ? -17.860 19.618  -11.860 1.00 45.22  ? 101  HIS D CE1 1 
ATOM   9694  N  NE2 . HIS D 1 101 ? -18.291 18.555  -11.204 1.00 52.63  ? 101  HIS D NE2 1 
ATOM   9695  N  N   . GLY D 1 102 ? -12.353 15.532  -11.014 1.00 35.22  ? 102  GLY D N   1 
ATOM   9696  C  CA  . GLY D 1 102 ? -11.030 14.949  -11.117 1.00 31.91  ? 102  GLY D CA  1 
ATOM   9697  C  C   . GLY D 1 102 ? -10.661 14.545  -12.518 1.00 30.53  ? 102  GLY D C   1 
ATOM   9698  O  O   . GLY D 1 102 ? -9.482  14.480  -12.871 1.00 46.81  ? 102  GLY D O   1 
ATOM   9699  N  N   . ASP D 1 103 ? -11.674 14.274  -13.329 1.00 43.02  ? 103  ASP D N   1 
ATOM   9700  C  CA  . ASP D 1 103 ? -11.443 13.875  -14.717 1.00 43.05  ? 103  ASP D CA  1 
ATOM   9701  C  C   . ASP D 1 103 ? -11.333 15.048  -15.694 1.00 32.97  ? 103  ASP D C   1 
ATOM   9702  O  O   . ASP D 1 103 ? -11.183 14.837  -16.889 1.00 46.20  ? 103  ASP D O   1 
ATOM   9703  C  CB  . ASP D 1 103 ? -12.522 12.892  -15.174 1.00 44.38  ? 103  ASP D CB  1 
ATOM   9704  C  CG  . ASP D 1 103 ? -13.927 13.370  -14.857 1.00 46.41  ? 103  ASP D CG  1 
ATOM   9705  O  OD1 . ASP D 1 103 ? -14.864 12.556  -14.957 1.00 63.01  ? 103  ASP D OD1 1 
ATOM   9706  O  OD2 . ASP D 1 103 ? -14.108 14.554  -14.516 1.00 48.51  ? 103  ASP D OD2 1 
ATOM   9707  N  N   . GLU D 1 104 ? -11.419 16.275  -15.186 1.00 32.92  ? 104  GLU D N   1 
ATOM   9708  C  CA  . GLU D 1 104 ? -11.313 17.464  -16.017 1.00 20.95  ? 104  GLU D CA  1 
ATOM   9709  C  C   . GLU D 1 104 ? -10.000 18.125  -15.661 1.00 35.41  ? 104  GLU D C   1 
ATOM   9710  O  O   . GLU D 1 104 ? -9.936  18.892  -14.699 1.00 43.33  ? 104  GLU D O   1 
ATOM   9711  C  CB  . GLU D 1 104 ? -12.473 18.407  -15.726 1.00 31.27  ? 104  GLU D CB  1 
ATOM   9712  C  CG  . GLU D 1 104 ? -13.869 17.774  -15.832 1.00 41.64  ? 104  GLU D CG  1 
ATOM   9713  C  CD  . GLU D 1 104 ? -14.954 18.743  -15.416 1.00 53.75  ? 104  GLU D CD  1 
ATOM   9714  O  OE1 . GLU D 1 104 ? -14.639 19.933  -15.219 1.00 54.72  ? 104  GLU D OE1 1 
ATOM   9715  O  OE2 . GLU D 1 104 ? -16.119 18.332  -15.272 1.00 69.58  ? 104  GLU D OE2 1 
ATOM   9716  N  N   . THR D 1 105 ? -8.959  17.837  -16.446 1.00 38.25  ? 105  THR D N   1 
ATOM   9717  C  CA  . THR D 1 105 ? -7.567  17.976  -15.985 1.00 46.96  ? 105  THR D CA  1 
ATOM   9718  C  C   . THR D 1 105 ? -6.720  19.112  -16.581 1.00 36.93  ? 105  THR D C   1 
ATOM   9719  O  O   . THR D 1 105 ? -5.681  19.481  -16.037 1.00 19.72  ? 105  THR D O   1 
ATOM   9720  C  CB  . THR D 1 105 ? -6.789  16.677  -16.222 1.00 41.24  ? 105  THR D CB  1 
ATOM   9721  O  OG1 . THR D 1 105 ? -6.692  16.444  -17.632 1.00 34.10  ? 105  THR D OG1 1 
ATOM   9722  C  CG2 . THR D 1 105 ? -7.497  15.514  -15.560 1.00 50.24  ? 105  THR D CG2 1 
ATOM   9723  N  N   . VAL D 1 106 ? -7.139  19.649  -17.710 1.00 32.68  ? 106  VAL D N   1 
ATOM   9724  C  CA  . VAL D 1 106 ? -6.369  20.717  -18.306 1.00 39.55  ? 106  VAL D CA  1 
ATOM   9725  C  C   . VAL D 1 106 ? -6.135  21.853  -17.292 1.00 27.90  ? 106  VAL D C   1 
ATOM   9726  O  O   . VAL D 1 106 ? -5.000  22.188  -16.980 1.00 31.57  ? 106  VAL D O   1 
ATOM   9727  C  CB  . VAL D 1 106 ? -7.026  21.213  -19.616 1.00 46.03  ? 106  VAL D CB  1 
ATOM   9728  C  CG1 . VAL D 1 106 ? -6.225  22.341  -20.220 1.00 44.79  ? 106  VAL D CG1 1 
ATOM   9729  C  CG2 . VAL D 1 106 ? -7.125  20.071  -20.603 1.00 38.51  ? 106  VAL D CG2 1 
ATOM   9730  N  N   . GLY D 1 107 ? -7.208  22.428  -16.766 1.00 44.43  ? 107  GLY D N   1 
ATOM   9731  C  CA  . GLY D 1 107 ? -7.080  23.519  -15.817 1.00 36.30  ? 107  GLY D CA  1 
ATOM   9732  C  C   . GLY D 1 107 ? -6.023  23.240  -14.777 1.00 31.73  ? 107  GLY D C   1 
ATOM   9733  O  O   . GLY D 1 107 ? -5.287  24.147  -14.397 1.00 40.39  ? 107  GLY D O   1 
ATOM   9734  N  N   . ARG D 1 108 ? -5.950  21.983  -14.331 1.00 37.01  ? 108  ARG D N   1 
ATOM   9735  C  CA  . ARG D 1 108 ? -4.965  21.527  -13.334 1.00 34.12  ? 108  ARG D CA  1 
ATOM   9736  C  C   . ARG D 1 108 ? -3.533  21.887  -13.699 1.00 32.47  ? 108  ARG D C   1 
ATOM   9737  O  O   . ARG D 1 108 ? -2.832  22.511  -12.910 1.00 33.24  ? 108  ARG D O   1 
ATOM   9738  C  CB  . ARG D 1 108 ? -5.052  20.002  -13.115 1.00 35.45  ? 108  ARG D CB  1 
ATOM   9739  C  CG  . ARG D 1 108 ? -3.751  19.387  -12.565 1.00 36.04  ? 108  ARG D CG  1 
ATOM   9740  C  CD  . ARG D 1 108 ? -3.730  17.843  -12.558 1.00 43.23  ? 108  ARG D CD  1 
ATOM   9741  N  NE  . ARG D 1 108 ? -4.307  17.322  -11.335 1.00 47.02  ? 108  ARG D NE  1 
ATOM   9742  C  CZ  . ARG D 1 108 ? -3.661  16.735  -10.331 1.00 37.09  ? 108  ARG D CZ  1 
ATOM   9743  N  NH1 . ARG D 1 108 ? -2.362  16.516  -10.363 1.00 32.89  ? 108  ARG D NH1 1 
ATOM   9744  N  NH2 . ARG D 1 108 ? -4.352  16.349  -9.275  1.00 34.05  ? 108  ARG D NH2 1 
ATOM   9745  N  N   . GLN D 1 109 ? -3.107  21.475  -14.893 1.00 45.37  ? 109  GLN D N   1 
ATOM   9746  C  CA  . GLN D 1 109 ? -1.756  21.739  -15.395 1.00 44.75  ? 109  GLN D CA  1 
ATOM   9747  C  C   . GLN D 1 109 ? -1.525  23.201  -15.738 1.00 31.79  ? 109  GLN D C   1 
ATOM   9748  O  O   . GLN D 1 109 ? -0.430  23.716  -15.560 1.00 35.12  ? 109  GLN D O   1 
ATOM   9749  C  CB  . GLN D 1 109 ? -1.460  20.878  -16.622 1.00 46.73  ? 109  GLN D CB  1 
ATOM   9750  C  CG  . GLN D 1 109 ? -0.950  19.509  -16.272 1.00 49.64  ? 109  GLN D CG  1 
ATOM   9751  C  CD  . GLN D 1 109 ? 0.283   19.575  -15.401 1.00 55.53  ? 109  GLN D CD  1 
ATOM   9752  O  OE1 . GLN D 1 109 ? 0.317   19.001  -14.313 1.00 65.71  ? 109  GLN D OE1 1 
ATOM   9753  N  NE2 . GLN D 1 109 ? 1.308   20.285  -15.873 1.00 50.14  ? 109  GLN D NE2 1 
ATOM   9754  N  N   . LEU D 1 110 ? -2.553  23.862  -16.250 1.00 28.60  ? 110  LEU D N   1 
ATOM   9755  C  CA  . LEU D 1 110 ? -2.471  25.289  -16.526 1.00 35.42  ? 110  LEU D CA  1 
ATOM   9756  C  C   . LEU D 1 110 ? -2.088  26.096  -15.289 1.00 36.60  ? 110  LEU D C   1 
ATOM   9757  O  O   . LEU D 1 110 ? -1.338  27.061  -15.379 1.00 33.42  ? 110  LEU D O   1 
ATOM   9758  C  CB  . LEU D 1 110 ? -3.793  25.809  -17.090 1.00 36.15  ? 110  LEU D CB  1 
ATOM   9759  C  CG  . LEU D 1 110 ? -4.109  25.403  -18.528 1.00 41.83  ? 110  LEU D CG  1 
ATOM   9760  C  CD1 . LEU D 1 110 ? -5.336  26.158  -19.020 1.00 44.48  ? 110  LEU D CD1 1 
ATOM   9761  C  CD2 . LEU D 1 110 ? -2.912  25.658  -19.435 1.00 27.58  ? 110  LEU D CD2 1 
ATOM   9762  N  N   . LEU D 1 111 ? -2.608  25.710  -14.132 1.00 41.27  ? 111  LEU D N   1 
ATOM   9763  C  CA  . LEU D 1 111 ? -2.304  26.440  -12.903 1.00 28.45  ? 111  LEU D CA  1 
ATOM   9764  C  C   . LEU D 1 111 ? -0.879  26.157  -12.461 1.00 30.79  ? 111  LEU D C   1 
ATOM   9765  O  O   . LEU D 1 111 ? -0.160  27.055  -12.034 1.00 45.14  ? 111  LEU D O   1 
ATOM   9766  C  CB  . LEU D 1 111 ? -3.308  26.094  -11.805 1.00 32.80  ? 111  LEU D CB  1 
ATOM   9767  C  CG  . LEU D 1 111 ? -4.696  26.668  -12.073 1.00 34.68  ? 111  LEU D CG  1 
ATOM   9768  C  CD1 . LEU D 1 111 ? -5.541  26.528  -10.823 1.00 37.12  ? 111  LEU D CD1 1 
ATOM   9769  C  CD2 . LEU D 1 111 ? -4.600  28.132  -12.520 1.00 33.00  ? 111  LEU D CD2 1 
ATOM   9770  N  N   . VAL D 1 112 ? -0.483  24.892  -12.573 1.00 45.53  ? 112  VAL D N   1 
ATOM   9771  C  CA  . VAL D 1 112 ? 0.894   24.469  -12.346 1.00 37.26  ? 112  VAL D CA  1 
ATOM   9772  C  C   . VAL D 1 112 ? 1.840   25.301  -13.236 1.00 41.58  ? 112  VAL D C   1 
ATOM   9773  O  O   . VAL D 1 112 ? 2.845   25.842  -12.768 1.00 38.90  ? 112  VAL D O   1 
ATOM   9774  C  CB  . VAL D 1 112 ? 1.055   22.935  -12.618 1.00 33.81  ? 112  VAL D CB  1 
ATOM   9775  C  CG1 . VAL D 1 112 ? 2.482   22.576  -12.876 1.00 19.23  ? 112  VAL D CG1 1 
ATOM   9776  C  CG2 . VAL D 1 112 ? 0.528   22.121  -11.453 1.00 34.39  ? 112  VAL D CG2 1 
ATOM   9777  N  N   . TYR D 1 113 ? 1.496   25.420  -14.517 1.00 33.73  ? 113  TYR D N   1 
ATOM   9778  C  CA  . TYR D 1 113 ? 2.259   26.249  -15.438 1.00 35.67  ? 113  TYR D CA  1 
ATOM   9779  C  C   . TYR D 1 113 ? 2.289   27.701  -14.975 1.00 44.47  ? 113  TYR D C   1 
ATOM   9780  O  O   . TYR D 1 113 ? 3.327   28.372  -15.056 1.00 42.34  ? 113  TYR D O   1 
ATOM   9781  C  CB  . TYR D 1 113 ? 1.669   26.163  -16.842 1.00 26.59  ? 113  TYR D CB  1 
ATOM   9782  C  CG  . TYR D 1 113 ? 1.906   24.822  -17.514 1.00 47.74  ? 113  TYR D CG  1 
ATOM   9783  C  CD1 . TYR D 1 113 ? 1.138   24.417  -18.600 1.00 52.16  ? 113  TYR D CD1 1 
ATOM   9784  C  CD2 . TYR D 1 113 ? 2.910   23.960  -17.068 1.00 51.95  ? 113  TYR D CD2 1 
ATOM   9785  C  CE1 . TYR D 1 113 ? 1.355   23.189  -19.218 1.00 51.40  ? 113  TYR D CE1 1 
ATOM   9786  C  CE2 . TYR D 1 113 ? 3.133   22.730  -17.680 1.00 48.12  ? 113  TYR D CE2 1 
ATOM   9787  C  CZ  . TYR D 1 113 ? 2.351   22.350  -18.752 1.00 51.49  ? 113  TYR D CZ  1 
ATOM   9788  O  OH  . TYR D 1 113 ? 2.569   21.131  -19.363 1.00 55.24  ? 113  TYR D OH  1 
ATOM   9789  N  N   . MET D 1 114 ? 1.148   28.171  -14.472 1.00 37.47  ? 114  MET D N   1 
ATOM   9790  C  CA  . MET D 1 114 ? 0.994   29.569  -14.097 1.00 40.75  ? 114  MET D CA  1 
ATOM   9791  C  C   . MET D 1 114 ? 1.910   29.909  -12.941 1.00 43.29  ? 114  MET D C   1 
ATOM   9792  O  O   . MET D 1 114 ? 2.608   30.922  -12.974 1.00 51.34  ? 114  MET D O   1 
ATOM   9793  C  CB  . MET D 1 114 ? -0.462  29.901  -13.734 1.00 32.61  ? 114  MET D CB  1 
ATOM   9794  C  CG  . MET D 1 114 ? -0.696  31.365  -13.318 1.00 30.40  ? 114  MET D CG  1 
ATOM   9795  S  SD  . MET D 1 114 ? -0.188  32.613  -14.538 1.00 42.10  ? 114  MET D SD  1 
ATOM   9796  C  CE  . MET D 1 114 ? -1.321  32.240  -15.867 1.00 69.48  ? 114  MET D CE  1 
ATOM   9797  N  N   . ALA D 1 115 ? 1.904   29.062  -11.920 1.00 25.75  ? 115  ALA D N   1 
ATOM   9798  C  CA  . ALA D 1 115 ? 2.773   29.264  -10.765 1.00 26.95  ? 115  ALA D CA  1 
ATOM   9799  C  C   . ALA D 1 115 ? 4.248   29.492  -11.156 1.00 30.14  ? 115  ALA D C   1 
ATOM   9800  O  O   . ALA D 1 115 ? 4.833   30.532  -10.865 1.00 37.77  ? 115  ALA D O   1 
ATOM   9801  C  CB  . ALA D 1 115 ? 2.647   28.082  -9.827  1.00 39.83  ? 115  ALA D CB  1 
ATOM   9802  N  N   . GLN D 1 116 ? 4.838   28.513  -11.829 1.00 41.02  ? 116  GLN D N   1 
ATOM   9803  C  CA  . GLN D 1 116 ? 6.182   28.659  -12.373 1.00 30.23  ? 116  GLN D CA  1 
ATOM   9804  C  C   . GLN D 1 116 ? 6.300   29.934  -13.198 1.00 38.31  ? 116  GLN D C   1 
ATOM   9805  O  O   . GLN D 1 116 ? 7.091   30.817  -12.864 1.00 47.40  ? 116  GLN D O   1 
ATOM   9806  C  CB  . GLN D 1 116 ? 6.533   27.448  -13.231 1.00 23.62  ? 116  GLN D CB  1 
ATOM   9807  C  CG  . GLN D 1 116 ? 6.406   26.122  -12.491 1.00 35.13  ? 116  GLN D CG  1 
ATOM   9808  C  CD  . GLN D 1 116 ? 6.473   24.917  -13.423 1.00 41.74  ? 116  GLN D CD  1 
ATOM   9809  O  OE1 . GLN D 1 116 ? 7.549   24.396  -13.698 1.00 44.95  ? 116  GLN D OE1 1 
ATOM   9810  N  NE2 . GLN D 1 116 ? 5.317   24.471  -13.913 1.00 40.37  ? 116  GLN D NE2 1 
ATOM   9811  N  N   . TYR D 1 117 ? 5.510   30.027  -14.270 1.00 35.82  ? 117  TYR D N   1 
ATOM   9812  C  CA  . TYR D 1 117 ? 5.539   31.184  -15.181 1.00 32.67  ? 117  TYR D CA  1 
ATOM   9813  C  C   . TYR D 1 117 ? 5.688   32.517  -14.448 1.00 41.12  ? 117  TYR D C   1 
ATOM   9814  O  O   . TYR D 1 117 ? 6.623   33.280  -14.696 1.00 47.91  ? 117  TYR D O   1 
ATOM   9815  C  CB  . TYR D 1 117 ? 4.273   31.217  -16.045 1.00 26.61  ? 117  TYR D CB  1 
ATOM   9816  C  CG  . TYR D 1 117 ? 4.291   32.297  -17.102 1.00 41.45  ? 117  TYR D CG  1 
ATOM   9817  C  CD1 . TYR D 1 117 ? 5.058   32.159  -18.271 1.00 47.53  ? 117  TYR D CD1 1 
ATOM   9818  C  CD2 . TYR D 1 117 ? 3.546   33.460  -16.941 1.00 38.61  ? 117  TYR D CD2 1 
ATOM   9819  C  CE1 . TYR D 1 117 ? 5.075   33.164  -19.252 1.00 45.44  ? 117  TYR D CE1 1 
ATOM   9820  C  CE2 . TYR D 1 117 ? 3.555   34.463  -17.911 1.00 39.91  ? 117  TYR D CE2 1 
ATOM   9821  C  CZ  . TYR D 1 117 ? 4.316   34.313  -19.057 1.00 45.19  ? 117  TYR D CZ  1 
ATOM   9822  O  OH  . TYR D 1 117 ? 4.311   35.323  -19.991 1.00 40.34  ? 117  TYR D OH  1 
ATOM   9823  N  N   . LEU D 1 118 ? 4.758   32.781  -13.538 1.00 48.12  ? 118  LEU D N   1 
ATOM   9824  C  CA  . LEU D 1 118 ? 4.740   34.030  -12.790 1.00 48.75  ? 118  LEU D CA  1 
ATOM   9825  C  C   . LEU D 1 118 ? 6.033   34.220  -12.032 1.00 40.41  ? 118  LEU D C   1 
ATOM   9826  O  O   . LEU D 1 118 ? 6.715   35.227  -12.207 1.00 42.89  ? 118  LEU D O   1 
ATOM   9827  C  CB  . LEU D 1 118 ? 3.529   34.088  -11.843 1.00 44.19  ? 118  LEU D CB  1 
ATOM   9828  C  CG  . LEU D 1 118 ? 2.212   34.432  -12.553 1.00 44.57  ? 118  LEU D CG  1 
ATOM   9829  C  CD1 . LEU D 1 118 ? 1.019   34.427  -11.603 1.00 53.84  ? 118  LEU D CD1 1 
ATOM   9830  C  CD2 . LEU D 1 118 ? 2.342   35.783  -13.234 1.00 42.49  ? 118  LEU D CD2 1 
ATOM   9831  N  N   . LEU D 1 119 ? 6.373   33.243  -11.203 1.00 32.90  ? 119  LEU D N   1 
ATOM   9832  C  CA  . LEU D 1 119 ? 7.558   33.355  -10.366 1.00 46.35  ? 119  LEU D CA  1 
ATOM   9833  C  C   . LEU D 1 119 ? 8.833   33.534  -11.189 1.00 58.33  ? 119  LEU D C   1 
ATOM   9834  O  O   . LEU D 1 119 ? 9.616   34.461  -10.947 1.00 54.63  ? 119  LEU D O   1 
ATOM   9835  C  CB  . LEU D 1 119 ? 7.678   32.147  -9.446  1.00 39.96  ? 119  LEU D CB  1 
ATOM   9836  C  CG  . LEU D 1 119 ? 6.774   32.264  -8.226  1.00 41.99  ? 119  LEU D CG  1 
ATOM   9837  C  CD1 . LEU D 1 119 ? 6.835   30.993  -7.390  1.00 43.45  ? 119  LEU D CD1 1 
ATOM   9838  C  CD2 . LEU D 1 119 ? 7.195   33.481  -7.424  1.00 26.80  ? 119  LEU D CD2 1 
ATOM   9839  N  N   . GLY D 1 120 ? 9.035   32.652  -12.167 1.00 52.64  ? 120  GLY D N   1 
ATOM   9840  C  CA  . GLY D 1 120 ? 10.235  32.679  -12.981 1.00 33.37  ? 120  GLY D CA  1 
ATOM   9841  C  C   . GLY D 1 120 ? 10.324  33.879  -13.909 1.00 38.12  ? 120  GLY D C   1 
ATOM   9842  O  O   . GLY D 1 120 ? 11.387  34.182  -14.442 1.00 47.21  ? 120  GLY D O   1 
ATOM   9843  N  N   . ASN D 1 121 ? 9.209   34.570  -14.116 1.00 47.39  ? 121  ASN D N   1 
ATOM   9844  C  CA  . ASN D 1 121 ? 9.189   35.679  -15.069 1.00 54.05  ? 121  ASN D CA  1 
ATOM   9845  C  C   . ASN D 1 121 ? 8.887   37.054  -14.470 1.00 50.47  ? 121  ASN D C   1 
ATOM   9846  O  O   . ASN D 1 121 ? 9.185   38.081  -15.081 1.00 48.24  ? 121  ASN D O   1 
ATOM   9847  C  CB  . ASN D 1 121 ? 8.218   35.386  -16.219 1.00 49.23  ? 121  ASN D CB  1 
ATOM   9848  C  CG  . ASN D 1 121 ? 8.749   34.333  -17.174 1.00 56.53  ? 121  ASN D CG  1 
ATOM   9849  O  OD1 . ASN D 1 121 ? 9.504   34.639  -18.115 1.00 53.17  ? 121  ASN D OD1 1 
ATOM   9850  N  ND2 . ASN D 1 121 ? 8.352   33.080  -16.945 1.00 56.22  ? 121  ASN D ND2 1 
ATOM   9851  N  N   . HIS D 1 122 ? 8.312   37.075  -13.273 1.00 36.61  ? 122  HIS D N   1 
ATOM   9852  C  CA  . HIS D 1 122 ? 7.880   38.337  -12.686 1.00 43.08  ? 122  HIS D CA  1 
ATOM   9853  C  C   . HIS D 1 122 ? 8.985   39.415  -12.589 1.00 54.55  ? 122  HIS D C   1 
ATOM   9854  O  O   . HIS D 1 122 ? 8.702   40.605  -12.761 1.00 53.42  ? 122  HIS D O   1 
ATOM   9855  C  CB  . HIS D 1 122 ? 7.185   38.103  -11.340 1.00 55.93  ? 122  HIS D CB  1 
ATOM   9856  C  CG  . HIS D 1 122 ? 8.120   38.031  -10.175 1.00 61.32  ? 122  HIS D CG  1 
ATOM   9857  N  ND1 . HIS D 1 122 ? 8.697   36.853  -9.753  1.00 66.65  ? 122  HIS D ND1 1 
ATOM   9858  C  CD2 . HIS D 1 122 ? 8.569   38.994  -9.336  1.00 53.21  ? 122  HIS D CD2 1 
ATOM   9859  C  CE1 . HIS D 1 122 ? 9.469   37.095  -8.708  1.00 67.40  ? 122  HIS D CE1 1 
ATOM   9860  N  NE2 . HIS D 1 122 ? 9.411   38.386  -8.438  1.00 63.24  ? 122  HIS D NE2 1 
ATOM   9861  N  N   . GLU D 1 123 ? 10.234  39.013  -12.341 1.00 56.80  ? 123  GLU D N   1 
ATOM   9862  C  CA  . GLU D 1 123 ? 11.334  39.988  -12.261 1.00 57.51  ? 123  GLU D CA  1 
ATOM   9863  C  C   . GLU D 1 123 ? 11.886  40.402  -13.633 1.00 56.02  ? 123  GLU D C   1 
ATOM   9864  O  O   . GLU D 1 123 ? 12.499  41.465  -13.772 1.00 46.20  ? 123  GLU D O   1 
ATOM   9865  C  CB  . GLU D 1 123 ? 12.468  39.488  -11.355 1.00 72.21  ? 123  GLU D CB  1 
ATOM   9866  C  CG  . GLU D 1 123 ? 12.109  39.453  -9.871  1.00 89.06  ? 123  GLU D CG  1 
ATOM   9867  C  CD  . GLU D 1 123 ? 13.323  39.423  -8.957  1.00 104.26 ? 123  GLU D CD  1 
ATOM   9868  O  OE1 . GLU D 1 123 ? 14.408  38.987  -9.399  1.00 109.56 ? 123  GLU D OE1 1 
ATOM   9869  O  OE2 . GLU D 1 123 ? 13.187  39.838  -7.786  1.00 112.03 ? 123  GLU D OE2 1 
ATOM   9870  N  N   . ARG D 1 124 ? 11.656  39.569  -14.643 1.00 55.22  ? 124  ARG D N   1 
ATOM   9871  C  CA  . ARG D 1 124 ? 12.183  39.835  -15.974 1.00 51.13  ? 124  ARG D CA  1 
ATOM   9872  C  C   . ARG D 1 124 ? 11.205  40.636  -16.834 1.00 53.96  ? 124  ARG D C   1 
ATOM   9873  O  O   . ARG D 1 124 ? 11.603  41.556  -17.549 1.00 58.45  ? 124  ARG D O   1 
ATOM   9874  C  CB  . ARG D 1 124 ? 12.569  38.529  -16.687 1.00 68.26  ? 124  ARG D CB  1 
ATOM   9875  C  CG  . ARG D 1 124 ? 12.226  37.231  -15.954 1.00 73.96  ? 124  ARG D CG  1 
ATOM   9876  C  CD  . ARG D 1 124 ? 12.266  36.033  -16.914 1.00 79.56  ? 124  ARG D CD  1 
ATOM   9877  N  NE  . ARG D 1 124 ? 13.327  36.149  -17.919 1.00 83.28  ? 124  ARG D NE  1 
ATOM   9878  C  CZ  . ARG D 1 124 ? 14.481  35.490  -17.884 1.00 85.22  ? 124  ARG D CZ  1 
ATOM   9879  N  NH1 . ARG D 1 124 ? 14.747  34.646  -16.894 1.00 88.96  ? 124  ARG D NH1 1 
ATOM   9880  N  NH2 . ARG D 1 124 ? 15.367  35.669  -18.850 1.00 82.15  ? 124  ARG D NH2 1 
ATOM   9881  N  N   . ILE D 1 125 ? 9.926   40.280  -16.767 1.00 45.45  ? 125  ILE D N   1 
ATOM   9882  C  CA  . ILE D 1 125 ? 8.904   40.926  -17.589 1.00 48.35  ? 125  ILE D CA  1 
ATOM   9883  C  C   . ILE D 1 125 ? 8.079   41.923  -16.776 1.00 56.38  ? 125  ILE D C   1 
ATOM   9884  O  O   . ILE D 1 125 ? 7.390   41.557  -15.818 1.00 62.30  ? 125  ILE D O   1 
ATOM   9885  C  CB  . ILE D 1 125 ? 7.957   39.890  -18.254 1.00 54.32  ? 125  ILE D CB  1 
ATOM   9886  C  CG1 . ILE D 1 125 ? 8.603   39.267  -19.509 1.00 54.60  ? 125  ILE D CG1 1 
ATOM   9887  C  CG2 . ILE D 1 125 ? 6.626   40.548  -18.610 1.00 44.44  ? 125  ILE D CG2 1 
ATOM   9888  C  CD1 . ILE D 1 125 ? 9.731   38.279  -19.253 1.00 55.88  ? 125  ILE D CD1 1 
ATOM   9889  N  N   . SER D 1 126 ? 8.151   43.183  -17.182 1.00 65.42  ? 126  SER D N   1 
ATOM   9890  C  CA  . SER D 1 126 ? 7.544   44.288  -16.449 1.00 68.33  ? 126  SER D CA  1 
ATOM   9891  C  C   . SER D 1 126 ? 6.068   44.056  -16.105 1.00 67.16  ? 126  SER D C   1 
ATOM   9892  O  O   . SER D 1 126 ? 5.661   44.178  -14.943 1.00 57.38  ? 126  SER D O   1 
ATOM   9893  C  CB  . SER D 1 126 ? 7.709   45.579  -17.261 1.00 69.21  ? 126  SER D CB  1 
ATOM   9894  O  OG  . SER D 1 126 ? 7.614   46.728  -16.438 1.00 77.98  ? 126  SER D OG  1 
ATOM   9895  N  N   . ASP D 1 127 ? 5.272   43.731  -17.119 1.00 66.41  ? 127  ASP D N   1 
ATOM   9896  C  CA  . ASP D 1 127 ? 3.847   43.505  -16.919 1.00 62.20  ? 127  ASP D CA  1 
ATOM   9897  C  C   . ASP D 1 127 ? 3.600   42.605  -15.725 1.00 50.84  ? 127  ASP D C   1 
ATOM   9898  O  O   . ASP D 1 127 ? 2.863   42.966  -14.816 1.00 62.79  ? 127  ASP D O   1 
ATOM   9899  C  CB  . ASP D 1 127 ? 3.221   42.884  -18.168 1.00 73.03  ? 127  ASP D CB  1 
ATOM   9900  C  CG  . ASP D 1 127 ? 2.908   43.911  -19.228 1.00 88.76  ? 127  ASP D CG  1 
ATOM   9901  O  OD1 . ASP D 1 127 ? 2.582   45.066  -18.870 1.00 92.61  ? 127  ASP D OD1 1 
ATOM   9902  O  OD2 . ASP D 1 127 ? 2.987   43.565  -20.423 1.00 96.06  ? 127  ASP D OD2 1 
ATOM   9903  N  N   . LEU D 1 128 ? 4.221   41.432  -15.740 1.00 45.07  ? 128  LEU D N   1 
ATOM   9904  C  CA  . LEU D 1 128 ? 4.008   40.431  -14.703 1.00 38.18  ? 128  LEU D CA  1 
ATOM   9905  C  C   . LEU D 1 128 ? 4.505   40.939  -13.363 1.00 46.31  ? 128  LEU D C   1 
ATOM   9906  O  O   . LEU D 1 128 ? 3.857   40.746  -12.337 1.00 43.68  ? 128  LEU D O   1 
ATOM   9907  C  CB  . LEU D 1 128 ? 4.716   39.123  -15.067 1.00 44.77  ? 128  LEU D CB  1 
ATOM   9908  C  CG  . LEU D 1 128 ? 4.354   38.472  -16.409 1.00 45.95  ? 128  LEU D CG  1 
ATOM   9909  C  CD1 . LEU D 1 128 ? 5.310   37.316  -16.787 1.00 43.33  ? 128  LEU D CD1 1 
ATOM   9910  C  CD2 . LEU D 1 128 ? 2.919   38.003  -16.369 1.00 44.17  ? 128  LEU D CD2 1 
ATOM   9911  N  N   . GLY D 1 129 ? 5.662   41.594  -13.377 1.00 53.54  ? 129  GLY D N   1 
ATOM   9912  C  CA  . GLY D 1 129 ? 6.234   42.135  -12.155 1.00 56.23  ? 129  GLY D CA  1 
ATOM   9913  C  C   . GLY D 1 129 ? 5.267   43.096  -11.501 1.00 46.83  ? 129  GLY D C   1 
ATOM   9914  O  O   . GLY D 1 129 ? 5.187   43.198  -10.276 1.00 47.90  ? 129  GLY D O   1 
ATOM   9915  N  N   . GLN D 1 130 ? 4.520   43.800  -12.337 1.00 29.47  ? 130  GLN D N   1 
ATOM   9916  C  CA  . GLN D 1 130 ? 3.494   44.715  -11.864 1.00 42.08  ? 130  GLN D CA  1 
ATOM   9917  C  C   . GLN D 1 130 ? 2.197   43.978  -11.461 1.00 33.71  ? 130  GLN D C   1 
ATOM   9918  O  O   . GLN D 1 130 ? 1.557   44.324  -10.475 1.00 39.17  ? 130  GLN D O   1 
ATOM   9919  C  CB  . GLN D 1 130 ? 3.225   45.772  -12.932 1.00 50.86  ? 130  GLN D CB  1 
ATOM   9920  C  CG  . GLN D 1 130 ? 2.840   47.122  -12.374 1.00 57.40  ? 130  GLN D CG  1 
ATOM   9921  C  CD  . GLN D 1 130 ? 1.391   47.183  -11.977 1.00 50.82  ? 130  GLN D CD  1 
ATOM   9922  O  OE1 . GLN D 1 130 ? 0.601   46.331  -12.363 1.00 49.65  ? 130  GLN D OE1 1 
ATOM   9923  N  NE2 . GLN D 1 130 ? 1.030   48.199  -11.203 1.00 57.81  ? 130  GLN D NE2 1 
ATOM   9924  N  N   . LEU D 1 131 ? 1.819   42.954  -12.215 1.00 35.85  ? 131  LEU D N   1 
ATOM   9925  C  CA  . LEU D 1 131 ? 0.700   42.101  -11.835 1.00 35.59  ? 131  LEU D CA  1 
ATOM   9926  C  C   . LEU D 1 131 ? 0.912   41.537  -10.429 1.00 29.14  ? 131  LEU D C   1 
ATOM   9927  O  O   . LEU D 1 131 ? 0.026   41.601  -9.580  1.00 35.43  ? 131  LEU D O   1 
ATOM   9928  C  CB  . LEU D 1 131 ? 0.543   40.950  -12.836 1.00 37.99  ? 131  LEU D CB  1 
ATOM   9929  C  CG  . LEU D 1 131 ? -0.553  39.926  -12.513 1.00 44.85  ? 131  LEU D CG  1 
ATOM   9930  C  CD1 . LEU D 1 131 ? -1.932  40.567  -12.601 1.00 39.82  ? 131  LEU D CD1 1 
ATOM   9931  C  CD2 . LEU D 1 131 ? -0.476  38.723  -13.432 1.00 30.79  ? 131  LEU D CD2 1 
ATOM   9932  N  N   . VAL D 1 132 ? 2.103   41.001  -10.193 1.00 34.96  ? 132  VAL D N   1 
ATOM   9933  C  CA  . VAL D 1 132 ? 2.461   40.397  -8.913  1.00 37.13  ? 132  VAL D CA  1 
ATOM   9934  C  C   . VAL D 1 132 ? 2.588   41.397  -7.759  1.00 41.84  ? 132  VAL D C   1 
ATOM   9935  O  O   . VAL D 1 132 ? 2.171   41.114  -6.631  1.00 56.74  ? 132  VAL D O   1 
ATOM   9936  C  CB  . VAL D 1 132 ? 3.785   39.608  -9.012  1.00 32.84  ? 132  VAL D CB  1 
ATOM   9937  C  CG1 . VAL D 1 132 ? 4.218   39.151  -7.619  1.00 45.11  ? 132  VAL D CG1 1 
ATOM   9938  C  CG2 . VAL D 1 132 ? 3.629   38.427  -9.935  1.00 20.62  ? 132  VAL D CG2 1 
ATOM   9939  N  N   . ASN D 1 133 ? 3.186   42.551  -8.040  1.00 41.91  ? 133  ASN D N   1 
ATOM   9940  C  CA  . ASN D 1 133 ? 3.340   43.606  -7.044  1.00 41.03  ? 133  ASN D CA  1 
ATOM   9941  C  C   . ASN D 1 133 ? 1.997   44.087  -6.519  1.00 42.64  ? 133  ASN D C   1 
ATOM   9942  O  O   . ASN D 1 133 ? 1.899   44.523  -5.374  1.00 49.80  ? 133  ASN D O   1 
ATOM   9943  C  CB  . ASN D 1 133 ? 4.079   44.812  -7.641  1.00 48.43  ? 133  ASN D CB  1 
ATOM   9944  C  CG  . ASN D 1 133 ? 5.588   44.708  -7.512  1.00 55.17  ? 133  ASN D CG  1 
ATOM   9945  O  OD1 . ASN D 1 133 ? 6.127   43.670  -7.101  1.00 55.39  ? 133  ASN D OD1 1 
ATOM   9946  N  ND2 . ASN D 1 133 ? 6.283   45.807  -7.854  1.00 62.90  ? 133  ASN D ND2 1 
ATOM   9947  N  N   . SER D 1 134 ? 0.966   44.008  -7.360  1.00 41.29  ? 134  SER D N   1 
ATOM   9948  C  CA  . SER D 1 134 ? -0.309  44.664  -7.079  1.00 38.47  ? 134  SER D CA  1 
ATOM   9949  C  C   . SER D 1 134 ? -1.413  43.688  -6.743  1.00 34.77  ? 134  SER D C   1 
ATOM   9950  O  O   . SER D 1 134 ? -2.541  44.096  -6.478  1.00 46.73  ? 134  SER D O   1 
ATOM   9951  C  CB  . SER D 1 134 ? -0.745  45.472  -8.295  1.00 43.29  ? 134  SER D CB  1 
ATOM   9952  O  OG  . SER D 1 134 ? -0.812  44.621  -9.431  1.00 49.37  ? 134  SER D OG  1 
ATOM   9953  N  N   . THR D 1 135 ? -1.106  42.401  -6.769  1.00 24.82  ? 135  THR D N   1 
ATOM   9954  C  CA  . THR D 1 135 ? -2.156  41.419  -6.576  1.00 42.34  ? 135  THR D CA  1 
ATOM   9955  C  C   . THR D 1 135 ? -1.685  40.254  -5.733  1.00 30.14  ? 135  THR D C   1 
ATOM   9956  O  O   . THR D 1 135 ? -0.556  39.763  -5.884  1.00 28.44  ? 135  THR D O   1 
ATOM   9957  C  CB  . THR D 1 135 ? -2.710  40.891  -7.923  1.00 50.24  ? 135  THR D CB  1 
ATOM   9958  O  OG1 . THR D 1 135 ? -2.729  41.952  -8.889  1.00 33.91  ? 135  THR D OG1 1 
ATOM   9959  C  CG2 . THR D 1 135 ? -4.122  40.323  -7.741  1.00 33.98  ? 135  THR D CG2 1 
ATOM   9960  N  N   . ASP D 1 136 ? -2.564  39.825  -4.837  1.00 32.51  ? 136  ASP D N   1 
ATOM   9961  C  CA  . ASP D 1 136 ? -2.307  38.660  -4.007  1.00 40.41  ? 136  ASP D CA  1 
ATOM   9962  C  C   . ASP D 1 136 ? -2.955  37.463  -4.670  1.00 40.01  ? 136  ASP D C   1 
ATOM   9963  O  O   . ASP D 1 136 ? -4.187  37.369  -4.745  1.00 26.53  ? 136  ASP D O   1 
ATOM   9964  C  CB  . ASP D 1 136 ? -2.883  38.854  -2.619  1.00 48.92  ? 136  ASP D CB  1 
ATOM   9965  C  CG  . ASP D 1 136 ? -1.862  38.656  -1.546  1.00 66.29  ? 136  ASP D CG  1 
ATOM   9966  O  OD1 . ASP D 1 136 ? -0.815  39.344  -1.599  1.00 61.02  ? 136  ASP D OD1 1 
ATOM   9967  O  OD2 . ASP D 1 136 ? -2.116  37.815  -0.650  1.00 79.62  ? 136  ASP D OD2 1 
ATOM   9968  N  N   . ILE D 1 137 ? -2.115  36.556  -5.166  1.00 34.74  ? 137  ILE D N   1 
ATOM   9969  C  CA  . ILE D 1 137 ? -2.593  35.463  -6.010  1.00 32.28  ? 137  ILE D CA  1 
ATOM   9970  C  C   . ILE D 1 137 ? -2.432  34.065  -5.414  1.00 32.94  ? 137  ILE D C   1 
ATOM   9971  O  O   . ILE D 1 137 ? -1.353  33.680  -4.963  1.00 34.07  ? 137  ILE D O   1 
ATOM   9972  C  CB  . ILE D 1 137 ? -1.939  35.481  -7.399  1.00 30.78  ? 137  ILE D CB  1 
ATOM   9973  C  CG1 . ILE D 1 137 ? -2.136  36.848  -8.070  1.00 37.35  ? 137  ILE D CG1 1 
ATOM   9974  C  CG2 . ILE D 1 137 ? -2.530  34.373  -8.256  1.00 24.26  ? 137  ILE D CG2 1 
ATOM   9975  C  CD1 . ILE D 1 137 ? -1.100  37.159  -9.164  1.00 28.29  ? 137  ILE D CD1 1 
ATOM   9976  N  N   . TYR D 1 138 ? -3.529  33.316  -5.437  1.00 37.29  ? 138  TYR D N   1 
ATOM   9977  C  CA  . TYR D 1 138 ? -3.578  31.972  -4.885  1.00 29.91  ? 138  TYR D CA  1 
ATOM   9978  C  C   . TYR D 1 138 ? -3.944  30.955  -5.976  1.00 32.41  ? 138  TYR D C   1 
ATOM   9979  O  O   . TYR D 1 138 ? -4.949  31.099  -6.666  1.00 35.90  ? 138  TYR D O   1 
ATOM   9980  C  CB  . TYR D 1 138 ? -4.590  31.933  -3.738  1.00 28.52  ? 138  TYR D CB  1 
ATOM   9981  C  CG  . TYR D 1 138 ? -4.163  32.696  -2.491  1.00 33.87  ? 138  TYR D CG  1 
ATOM   9982  C  CD1 . TYR D 1 138 ? -4.338  34.072  -2.397  1.00 31.95  ? 138  TYR D CD1 1 
ATOM   9983  C  CD2 . TYR D 1 138 ? -3.602  32.030  -1.398  1.00 30.60  ? 138  TYR D CD2 1 
ATOM   9984  C  CE1 . TYR D 1 138 ? -3.958  34.769  -1.256  1.00 30.55  ? 138  TYR D CE1 1 
ATOM   9985  C  CE2 . TYR D 1 138 ? -3.224  32.718  -0.243  1.00 33.97  ? 138  TYR D CE2 1 
ATOM   9986  C  CZ  . TYR D 1 138 ? -3.405  34.085  -0.182  1.00 35.45  ? 138  TYR D CZ  1 
ATOM   9987  O  OH  . TYR D 1 138 ? -3.026  34.762  0.956   1.00 32.38  ? 138  TYR D OH  1 
ATOM   9988  N  N   . LEU D 1 139 ? -3.118  29.932  -6.143  1.00 32.47  ? 139  LEU D N   1 
ATOM   9989  C  CA  . LEU D 1 139 ? -3.341  28.957  -7.202  1.00 27.28  ? 139  LEU D CA  1 
ATOM   9990  C  C   . LEU D 1 139 ? -3.564  27.585  -6.619  1.00 33.84  ? 139  LEU D C   1 
ATOM   9991  O  O   . LEU D 1 139 ? -2.690  27.043  -5.930  1.00 32.71  ? 139  LEU D O   1 
ATOM   9992  C  CB  . LEU D 1 139 ? -2.143  28.903  -8.142  1.00 16.37  ? 139  LEU D CB  1 
ATOM   9993  C  CG  . LEU D 1 139 ? -1.706  30.227  -8.771  1.00 30.71  ? 139  LEU D CG  1 
ATOM   9994  C  CD1 . LEU D 1 139 ? -0.583  30.027  -9.823  1.00 20.92  ? 139  LEU D CD1 1 
ATOM   9995  C  CD2 . LEU D 1 139 ? -2.920  30.931  -9.390  1.00 29.96  ? 139  LEU D CD2 1 
ATOM   9996  N  N   . VAL D 1 140 ? -4.731  27.022  -6.907  1.00 38.81  ? 140  VAL D N   1 
ATOM   9997  C  CA  . VAL D 1 140 ? -5.090  25.693  -6.418  1.00 41.01  ? 140  VAL D CA  1 
ATOM   9998  C  C   . VAL D 1 140 ? -5.313  24.737  -7.573  1.00 35.50  ? 140  VAL D C   1 
ATOM   9999  O  O   . VAL D 1 140 ? -6.447  24.508  -7.989  1.00 36.81  ? 140  VAL D O   1 
ATOM   10000 C  CB  . VAL D 1 140 ? -6.367  25.735  -5.569  1.00 42.11  ? 140  VAL D CB  1 
ATOM   10001 C  CG1 . VAL D 1 140 ? -6.657  24.356  -4.969  1.00 27.20  ? 140  VAL D CG1 1 
ATOM   10002 C  CG2 . VAL D 1 140 ? -6.236  26.797  -4.481  1.00 39.16  ? 140  VAL D CG2 1 
ATOM   10003 N  N   . PRO D 1 141 ? -4.219  24.175  -8.097  1.00 40.89  ? 141  PRO D N   1 
ATOM   10004 C  CA  . PRO D 1 141 ? -4.238  23.263  -9.247  1.00 37.29  ? 141  PRO D CA  1 
ATOM   10005 C  C   . PRO D 1 141 ? -5.284  22.157  -9.118  1.00 38.58  ? 141  PRO D C   1 
ATOM   10006 O  O   . PRO D 1 141 ? -6.007  21.870  -10.082 1.00 40.95  ? 141  PRO D O   1 
ATOM   10007 C  CB  . PRO D 1 141 ? -2.838  22.675  -9.238  1.00 28.30  ? 141  PRO D CB  1 
ATOM   10008 C  CG  . PRO D 1 141 ? -1.997  23.764  -8.646  1.00 43.40  ? 141  PRO D CG  1 
ATOM   10009 C  CD  . PRO D 1 141 ? -2.855  24.406  -7.595  1.00 43.36  ? 141  PRO D CD  1 
ATOM   10010 N  N   . THR D 1 142 ? -5.377  21.534  -7.951  1.00 27.28  ? 142  THR D N   1 
ATOM   10011 C  CA  . THR D 1 142 ? -6.453  20.575  -7.762  1.00 42.17  ? 142  THR D CA  1 
ATOM   10012 C  C   . THR D 1 142 ? -7.244  20.754  -6.485  1.00 41.14  ? 142  THR D C   1 
ATOM   10013 O  O   . THR D 1 142 ? -6.725  21.167  -5.439  1.00 29.01  ? 142  THR D O   1 
ATOM   10014 C  CB  . THR D 1 142 ? -5.989  19.103  -7.857  1.00 39.28  ? 142  THR D CB  1 
ATOM   10015 O  OG1 . THR D 1 142 ? -7.128  18.240  -7.698  1.00 37.54  ? 142  THR D OG1 1 
ATOM   10016 C  CG2 . THR D 1 142 ? -4.989  18.793  -6.783  1.00 24.23  ? 142  THR D CG2 1 
ATOM   10017 N  N   . MET D 1 143 ? -8.512  20.394  -6.595  1.00 47.55  ? 143  MET D N   1 
ATOM   10018 C  CA  . MET D 1 143 ? -9.455  20.468  -5.503  1.00 35.09  ? 143  MET D CA  1 
ATOM   10019 C  C   . MET D 1 143 ? -10.071 19.065  -5.318  1.00 35.33  ? 143  MET D C   1 
ATOM   10020 O  O   . MET D 1 143 ? -10.876 18.819  -4.423  1.00 28.01  ? 143  MET D O   1 
ATOM   10021 C  CB  . MET D 1 143 ? -10.508 21.496  -5.878  1.00 27.08  ? 143  MET D CB  1 
ATOM   10022 C  CG  . MET D 1 143 ? -11.435 21.853  -4.785  1.00 33.12  ? 143  MET D CG  1 
ATOM   10023 S  SD  . MET D 1 143 ? -12.821 22.728  -5.500  1.00 36.50  ? 143  MET D SD  1 
ATOM   10024 C  CE  . MET D 1 143 ? -14.074 22.287  -4.281  1.00 26.80  ? 143  MET D CE  1 
ATOM   10025 N  N   . ASN D 1 144 ? -9.678  18.134  -6.170  1.00 16.91  ? 144  ASN D N   1 
ATOM   10026 C  CA  . ASN D 1 144 ? -10.137 16.775  -6.008  1.00 32.70  ? 144  ASN D CA  1 
ATOM   10027 C  C   . ASN D 1 144 ? -9.075  15.759  -6.427  1.00 43.91  ? 144  ASN D C   1 
ATOM   10028 O  O   . ASN D 1 144 ? -9.162  15.159  -7.501  1.00 46.38  ? 144  ASN D O   1 
ATOM   10029 C  CB  . ASN D 1 144 ? -11.427 16.574  -6.786  1.00 33.92  ? 144  ASN D CB  1 
ATOM   10030 C  CG  . ASN D 1 144 ? -11.976 15.194  -6.640  1.00 36.85  ? 144  ASN D CG  1 
ATOM   10031 O  OD1 . ASN D 1 144 ? -11.603 14.449  -5.726  1.00 37.55  ? 144  ASN D OD1 1 
ATOM   10032 N  ND2 . ASN D 1 144 ? -12.878 14.834  -7.537  1.00 42.83  ? 144  ASN D ND2 1 
ATOM   10033 N  N   . PRO D 1 145 ? -8.073  15.560  -5.559  1.00 37.90  ? 145  PRO D N   1 
ATOM   10034 C  CA  . PRO D 1 145 ? -6.951  14.640  -5.771  1.00 29.84  ? 145  PRO D CA  1 
ATOM   10035 C  C   . PRO D 1 145 ? -7.424  13.190  -5.848  1.00 35.45  ? 145  PRO D C   1 
ATOM   10036 O  O   . PRO D 1 145 ? -6.881  12.392  -6.599  1.00 41.91  ? 145  PRO D O   1 
ATOM   10037 C  CB  . PRO D 1 145 ? -6.108  14.809  -4.498  1.00 22.70  ? 145  PRO D CB  1 
ATOM   10038 C  CG  . PRO D 1 145 ? -6.721  15.944  -3.731  1.00 38.85  ? 145  PRO D CG  1 
ATOM   10039 C  CD  . PRO D 1 145 ? -8.131  16.048  -4.170  1.00 35.74  ? 145  PRO D CD  1 
ATOM   10040 N  N   . ASP D 1 146 ? -8.427  12.855  -5.047  1.00 43.56  ? 146  ASP D N   1 
ATOM   10041 C  CA  . ASP D 1 146 ? -8.904  11.489  -4.967  1.00 42.08  ? 146  ASP D CA  1 
ATOM   10042 C  C   . ASP D 1 146 ? -9.676  11.162  -6.219  1.00 37.39  ? 146  ASP D C   1 
ATOM   10043 O  O   . ASP D 1 146 ? -9.544  10.068  -6.772  1.00 43.43  ? 146  ASP D O   1 
ATOM   10044 C  CB  . ASP D 1 146 ? -9.764  11.299  -3.721  1.00 48.02  ? 146  ASP D CB  1 
ATOM   10045 C  CG  . ASP D 1 146 ? -8.958  11.427  -2.439  1.00 45.12  ? 146  ASP D CG  1 
ATOM   10046 O  OD1 . ASP D 1 146 ? -7.764  11.779  -2.546  1.00 33.63  ? 146  ASP D OD1 1 
ATOM   10047 O  OD2 . ASP D 1 146 ? -9.504  11.179  -1.333  1.00 44.85  ? 146  ASP D OD2 1 
ATOM   10048 N  N   . GLY D 1 147 ? -10.483 12.118  -6.658  1.00 25.09  ? 147  GLY D N   1 
ATOM   10049 C  CA  . GLY D 1 147 ? -11.140 12.019  -7.947  1.00 28.78  ? 147  GLY D CA  1 
ATOM   10050 C  C   . GLY D 1 147 ? -10.111 11.875  -9.058  1.00 36.42  ? 147  GLY D C   1 
ATOM   10051 O  O   . GLY D 1 147 ? -10.223 10.977  -9.898  1.00 40.63  ? 147  GLY D O   1 
ATOM   10052 N  N   . TYR D 1 148 ? -9.098  12.745  -9.061  1.00 36.22  ? 148  TYR D N   1 
ATOM   10053 C  CA  . TYR D 1 148 ? -8.074  12.737  -10.113 1.00 49.28  ? 148  TYR D CA  1 
ATOM   10054 C  C   . TYR D 1 148 ? -7.393  11.379  -10.223 1.00 55.52  ? 148  TYR D C   1 
ATOM   10055 O  O   . TYR D 1 148 ? -7.336  10.784  -11.303 1.00 48.49  ? 148  TYR D O   1 
ATOM   10056 C  CB  . TYR D 1 148 ? -7.025  13.831  -9.875  1.00 44.08  ? 148  TYR D CB  1 
ATOM   10057 C  CG  . TYR D 1 148 ? -5.819  13.784  -10.811 1.00 42.65  ? 148  TYR D CG  1 
ATOM   10058 C  CD1 . TYR D 1 148 ? -5.943  14.101  -12.163 1.00 43.93  ? 148  TYR D CD1 1 
ATOM   10059 C  CD2 . TYR D 1 148 ? -4.549  13.456  -10.332 1.00 31.33  ? 148  TYR D CD2 1 
ATOM   10060 C  CE1 . TYR D 1 148 ? -4.841  14.073  -13.014 1.00 32.09  ? 148  TYR D CE1 1 
ATOM   10061 C  CE2 . TYR D 1 148 ? -3.449  13.433  -11.178 1.00 27.96  ? 148  TYR D CE2 1 
ATOM   10062 C  CZ  . TYR D 1 148 ? -3.607  13.740  -12.514 1.00 34.35  ? 148  TYR D CZ  1 
ATOM   10063 O  OH  . TYR D 1 148 ? -2.527  13.703  -13.357 1.00 55.62  ? 148  TYR D OH  1 
ATOM   10064 N  N   . ALA D 1 149 ? -6.884  10.895  -9.095  1.00 50.33  ? 149  ALA D N   1 
ATOM   10065 C  CA  . ALA D 1 149 ? -6.213  9.604   -9.033  1.00 39.09  ? 149  ALA D CA  1 
ATOM   10066 C  C   . ALA D 1 149 ? -7.068  8.462   -9.637  1.00 41.24  ? 149  ALA D C   1 
ATOM   10067 O  O   . ALA D 1 149 ? -6.547  7.483   -10.175 1.00 37.96  ? 149  ALA D O   1 
ATOM   10068 C  CB  . ALA D 1 149 ? -5.814  9.296   -7.587  1.00 24.30  ? 149  ALA D CB  1 
ATOM   10069 N  N   . LEU D 1 150 ? -8.386  8.592   -9.560  1.00 50.80  ? 150  LEU D N   1 
ATOM   10070 C  CA  . LEU D 1 150 ? -9.261  7.543   -10.067 1.00 53.64  ? 150  LEU D CA  1 
ATOM   10071 C  C   . LEU D 1 150 ? -9.590  7.717   -11.562 1.00 57.99  ? 150  LEU D C   1 
ATOM   10072 O  O   . LEU D 1 150 ? -10.185 6.838   -12.186 1.00 61.21  ? 150  LEU D O   1 
ATOM   10073 C  CB  . LEU D 1 150 ? -10.528 7.446   -9.202  1.00 45.86  ? 150  LEU D CB  1 
ATOM   10074 C  CG  . LEU D 1 150 ? -10.296 6.883   -7.786  1.00 52.50  ? 150  LEU D CG  1 
ATOM   10075 C  CD1 . LEU D 1 150 ? -11.268 7.447   -6.739  1.00 43.96  ? 150  LEU D CD1 1 
ATOM   10076 C  CD2 . LEU D 1 150 ? -10.308 5.349   -7.785  1.00 45.05  ? 150  LEU D CD2 1 
ATOM   10077 N  N   . SER D 1 151 ? -9.176  8.839   -12.138 1.00 55.77  ? 151  SER D N   1 
ATOM   10078 C  CA  . SER D 1 151 ? -9.465  9.126   -13.542 1.00 51.67  ? 151  SER D CA  1 
ATOM   10079 C  C   . SER D 1 151 ? -8.379  8.594   -14.476 1.00 51.55  ? 151  SER D C   1 
ATOM   10080 O  O   . SER D 1 151 ? -7.273  8.278   -14.046 1.00 47.72  ? 151  SER D O   1 
ATOM   10081 C  CB  . SER D 1 151 ? -9.644  10.633  -13.752 1.00 45.16  ? 151  SER D CB  1 
ATOM   10082 O  OG  . SER D 1 151 ? -10.711 11.135  -12.961 1.00 43.76  ? 151  SER D OG  1 
ATOM   10083 N  N   . GLN D 1 152 ? -8.698  8.511   -15.763 1.00 48.94  ? 152  GLN D N   1 
ATOM   10084 C  CA  . GLN D 1 152 ? -7.771  7.945   -16.736 1.00 52.08  ? 152  GLN D CA  1 
ATOM   10085 C  C   . GLN D 1 152 ? -7.350  8.924   -17.832 1.00 55.91  ? 152  GLN D C   1 
ATOM   10086 O  O   . GLN D 1 152 ? -8.171  9.361   -18.641 1.00 54.27  ? 152  GLN D O   1 
ATOM   10087 C  CB  . GLN D 1 152 ? -8.380  6.702   -17.374 1.00 65.59  ? 152  GLN D CB  1 
ATOM   10088 C  CG  . GLN D 1 152 ? -7.512  6.069   -18.437 1.00 73.64  ? 152  GLN D CG  1 
ATOM   10089 C  CD  . GLN D 1 152 ? -8.222  4.938   -19.138 1.00 81.91  ? 152  GLN D CD  1 
ATOM   10090 O  OE1 . GLN D 1 152 ? -7.884  4.587   -20.269 1.00 94.26  ? 152  GLN D OE1 1 
ATOM   10091 N  NE2 . GLN D 1 152 ? -9.225  4.365   -18.474 1.00 72.32  ? 152  GLN D NE2 1 
ATOM   10092 N  N   . GLU D 1 153 ? -6.062  9.256   -17.858 1.00 53.01  ? 153  GLU D N   1 
ATOM   10093 C  CA  . GLU D 1 153 ? -5.541  10.141  -18.890 1.00 55.40  ? 153  GLU D CA  1 
ATOM   10094 C  C   . GLU D 1 153 ? -6.006  9.642   -20.250 1.00 54.17  ? 153  GLU D C   1 
ATOM   10095 O  O   . GLU D 1 153 ? -5.937  8.446   -20.545 1.00 48.26  ? 153  GLU D O   1 
ATOM   10096 C  CB  . GLU D 1 153 ? -4.005  10.227  -18.841 1.00 46.84  ? 153  GLU D CB  1 
ATOM   10097 C  CG  . GLU D 1 153 ? -3.403  11.169  -19.889 1.00 47.19  ? 153  GLU D CG  1 
ATOM   10098 C  CD  . GLU D 1 153 ? -1.890  11.279  -19.788 1.00 56.03  ? 153  GLU D CD  1 
ATOM   10099 O  OE1 . GLU D 1 153 ? -1.242  11.565  -20.817 1.00 57.53  ? 153  GLU D OE1 1 
ATOM   10100 O  OE2 . GLU D 1 153 ? -1.347  11.075  -18.684 1.00 52.62  ? 153  GLU D OE2 1 
ATOM   10101 N  N   . GLY D 1 154 ? -6.502  10.561  -21.067 1.00 51.73  ? 154  GLY D N   1 
ATOM   10102 C  CA  . GLY D 1 154 ? -6.946  10.211  -22.401 1.00 53.86  ? 154  GLY D CA  1 
ATOM   10103 C  C   . GLY D 1 154 ? -8.443  10.337  -22.575 1.00 57.20  ? 154  GLY D C   1 
ATOM   10104 O  O   . GLY D 1 154 ? -8.925  10.662  -23.662 1.00 60.72  ? 154  GLY D O   1 
ATOM   10105 N  N   . ASN D 1 155 ? -9.183  10.085  -21.499 1.00 55.79  ? 155  ASN D N   1 
ATOM   10106 C  CA  . ASN D 1 155 ? -10.641 10.114  -21.562 1.00 43.63  ? 155  ASN D CA  1 
ATOM   10107 C  C   . ASN D 1 155 ? -11.174 11.504  -21.809 1.00 49.42  ? 155  ASN D C   1 
ATOM   10108 O  O   . ASN D 1 155 ? -11.214 12.333  -20.904 1.00 60.91  ? 155  ASN D O   1 
ATOM   10109 C  CB  . ASN D 1 155 ? -11.270 9.512   -20.303 1.00 42.42  ? 155  ASN D CB  1 
ATOM   10110 C  CG  . ASN D 1 155 ? -11.541 8.022   -20.445 1.00 52.97  ? 155  ASN D CG  1 
ATOM   10111 O  OD1 . ASN D 1 155 ? -11.493 7.272   -19.475 1.00 56.19  ? 155  ASN D OD1 1 
ATOM   10112 N  ND2 . ASN D 1 155 ? -11.827 7.590   -21.662 1.00 67.56  ? 155  ASN D ND2 1 
ATOM   10113 N  N   . CYS D 1 156 ? -11.565 11.756  -23.050 1.00 50.66  ? 156  CYS D N   1 
ATOM   10114 C  CA  . CYS D 1 156 ? -12.241 12.995  -23.386 1.00 58.35  ? 156  CYS D CA  1 
ATOM   10115 C  C   . CYS D 1 156 ? -13.605 12.992  -22.734 1.00 54.88  ? 156  CYS D C   1 
ATOM   10116 O  O   . CYS D 1 156 ? -14.109 14.049  -22.353 1.00 59.26  ? 156  CYS D O   1 
ATOM   10117 C  CB  . CYS D 1 156 ? -12.362 13.167  -24.902 1.00 67.71  ? 156  CYS D CB  1 
ATOM   10118 S  SG  . CYS D 1 156 ? -10.829 13.751  -25.678 1.00 72.83  ? 156  CYS D SG  1 
ATOM   10119 N  N   . GLU D 1 157 ? -14.187 11.796  -22.602 1.00 54.46  ? 157  GLU D N   1 
ATOM   10120 C  CA  . GLU D 1 157 ? -15.419 11.596  -21.826 1.00 59.23  ? 157  GLU D CA  1 
ATOM   10121 C  C   . GLU D 1 157 ? -15.174 10.928  -20.467 1.00 55.41  ? 157  GLU D C   1 
ATOM   10122 O  O   . GLU D 1 157 ? -14.284 10.086  -20.319 1.00 49.54  ? 157  GLU D O   1 
ATOM   10123 C  CB  . GLU D 1 157 ? -16.461 10.799  -22.614 1.00 67.59  ? 157  GLU D CB  1 
ATOM   10124 C  CG  . GLU D 1 157 ? -17.087 11.566  -23.762 1.00 82.66  ? 157  GLU D CG  1 
ATOM   10125 C  CD  . GLU D 1 157 ? -16.501 11.174  -25.093 1.00 97.45  ? 157  GLU D CD  1 
ATOM   10126 O  OE1 . GLU D 1 157 ? -17.008 10.202  -25.697 1.00 108.24 ? 157  GLU D OE1 1 
ATOM   10127 O  OE2 . GLU D 1 157 ? -15.532 11.834  -25.529 1.00 94.21  ? 157  GLU D OE2 1 
ATOM   10128 N  N   . SER D 1 158 ? -15.981 11.310  -19.480 1.00 57.56  ? 158  SER D N   1 
ATOM   10129 C  CA  . SER D 1 158 ? -15.841 10.783  -18.135 1.00 45.67  ? 158  SER D CA  1 
ATOM   10130 C  C   . SER D 1 158 ? -16.036 9.276   -18.122 1.00 51.36  ? 158  SER D C   1 
ATOM   10131 O  O   . SER D 1 158 ? -16.705 8.702   -18.990 1.00 45.24  ? 158  SER D O   1 
ATOM   10132 C  CB  . SER D 1 158 ? -16.822 11.462  -17.182 1.00 43.45  ? 158  SER D CB  1 
ATOM   10133 O  OG  . SER D 1 158 ? -16.624 11.023  -15.853 1.00 58.37  ? 158  SER D OG  1 
ATOM   10134 N  N   . LEU D 1 159 ? -15.423 8.643   -17.129 1.00 67.58  ? 159  LEU D N   1 
ATOM   10135 C  CA  . LEU D 1 159 ? -15.515 7.200   -16.961 1.00 75.63  ? 159  LEU D CA  1 
ATOM   10136 C  C   . LEU D 1 159 ? -16.954 6.770   -16.671 1.00 71.17  ? 159  LEU D C   1 
ATOM   10137 O  O   . LEU D 1 159 ? -17.703 7.500   -16.014 1.00 51.10  ? 159  LEU D O   1 
ATOM   10138 C  CB  . LEU D 1 159 ? -14.561 6.734   -15.850 1.00 74.45  ? 159  LEU D CB  1 
ATOM   10139 C  CG  . LEU D 1 159 ? -13.063 6.714   -16.188 1.00 60.12  ? 159  LEU D CG  1 
ATOM   10140 C  CD1 . LEU D 1 159 ? -12.197 6.410   -14.967 1.00 58.17  ? 159  LEU D CD1 1 
ATOM   10141 C  CD2 . LEU D 1 159 ? -12.764 5.717   -17.293 1.00 41.43  ? 159  LEU D CD2 1 
ATOM   10142 N  N   . PRO D 1 160 ? -17.324 5.575   -17.158 1.00 85.80  ? 160  PRO D N   1 
ATOM   10143 C  CA  . PRO D 1 160 ? -18.601 4.855   -17.112 1.00 102.48 ? 160  PRO D CA  1 
ATOM   10144 C  C   . PRO D 1 160 ? -19.640 5.334   -16.095 1.00 96.03  ? 160  PRO D C   1 
ATOM   10145 O  O   . PRO D 1 160 ? -20.789 5.640   -16.448 1.00 98.92  ? 160  PRO D O   1 
ATOM   10146 C  CB  . PRO D 1 160 ? -18.157 3.430   -16.796 1.00 111.38 ? 160  PRO D CB  1 
ATOM   10147 C  CG  . PRO D 1 160 ? -16.700 3.340   -17.319 1.00 95.62  ? 160  PRO D CG  1 
ATOM   10148 C  CD  . PRO D 1 160 ? -16.289 4.730   -17.771 1.00 90.84  ? 160  PRO D CD  1 
ATOM   10149 N  N   . ASN D 1 161 ? -19.261 5.371   -14.830 1.00 73.81  ? 161  ASN D N   1 
ATOM   10150 C  CA  . ASN D 1 161 ? -20.217 5.760   -13.804 1.00 45.62  ? 161  ASN D CA  1 
ATOM   10151 C  C   . ASN D 1 161 ? -19.878 7.153   -13.327 1.00 36.36  ? 161  ASN D C   1 
ATOM   10152 O  O   . ASN D 1 161 ? -20.314 7.596   -12.259 1.00 50.61  ? 161  ASN D O   1 
ATOM   10153 C  CB  . ASN D 1 161 ? -20.195 4.742   -12.671 1.00 57.05  ? 161  ASN D CB  1 
ATOM   10154 C  CG  . ASN D 1 161 ? -20.610 3.359   -13.146 1.00 87.07  ? 161  ASN D CG  1 
ATOM   10155 O  OD1 . ASN D 1 161 ? -19.967 2.353   -12.840 1.00 100.08 ? 161  ASN D OD1 1 
ATOM   10156 N  ND2 . ASN D 1 161 ? -21.691 3.311   -13.924 1.00 91.26  ? 161  ASN D ND2 1 
ATOM   10157 N  N   . TYR D 1 162 ? -19.106 7.851   -14.153 1.00 37.35  ? 162  TYR D N   1 
ATOM   10158 C  CA  . TYR D 1 162 ? -18.645 9.187   -13.822 1.00 49.09  ? 162  TYR D CA  1 
ATOM   10159 C  C   . TYR D 1 162 ? -17.655 9.112   -12.688 1.00 54.95  ? 162  TYR D C   1 
ATOM   10160 O  O   . TYR D 1 162 ? -17.389 10.106  -12.009 1.00 46.79  ? 162  TYR D O   1 
ATOM   10161 C  CB  . TYR D 1 162 ? -19.819 10.068  -13.444 1.00 27.51  ? 162  TYR D CB  1 
ATOM   10162 C  CG  . TYR D 1 162 ? -20.518 10.596  -14.648 1.00 44.04  ? 162  TYR D CG  1 
ATOM   10163 C  CD1 . TYR D 1 162 ? -21.761 10.112  -15.028 1.00 60.21  ? 162  TYR D CD1 1 
ATOM   10164 C  CD2 . TYR D 1 162 ? -19.918 11.570  -15.430 1.00 51.33  ? 162  TYR D CD2 1 
ATOM   10165 C  CE1 . TYR D 1 162 ? -22.397 10.607  -16.151 1.00 68.69  ? 162  TYR D CE1 1 
ATOM   10166 C  CE2 . TYR D 1 162 ? -20.543 12.070  -16.544 1.00 58.40  ? 162  TYR D CE2 1 
ATOM   10167 C  CZ  . TYR D 1 162 ? -21.782 11.586  -16.904 1.00 64.10  ? 162  TYR D CZ  1 
ATOM   10168 O  OH  . TYR D 1 162 ? -22.394 12.094  -18.028 1.00 79.64  ? 162  TYR D OH  1 
ATOM   10169 N  N   . VAL D 1 163 ? -17.127 7.908   -12.494 1.00 60.20  ? 163  VAL D N   1 
ATOM   10170 C  CA  . VAL D 1 163 ? -16.051 7.669   -11.553 1.00 64.51  ? 163  VAL D CA  1 
ATOM   10171 C  C   . VAL D 1 163 ? -14.860 8.556   -11.915 1.00 57.49  ? 163  VAL D C   1 
ATOM   10172 O  O   . VAL D 1 163 ? -14.464 8.639   -13.085 1.00 51.41  ? 163  VAL D O   1 
ATOM   10173 C  CB  . VAL D 1 163 ? -15.629 6.177   -11.566 1.00 49.36  ? 163  VAL D CB  1 
ATOM   10174 C  CG1 . VAL D 1 163 ? -14.190 6.010   -11.076 1.00 45.62  ? 163  VAL D CG1 1 
ATOM   10175 C  CG2 . VAL D 1 163 ? -16.599 5.332   -10.738 1.00 36.73  ? 163  VAL D CG2 1 
ATOM   10176 N  N   . GLY D 1 164 ? -14.303 9.221   -10.902 1.00 42.91  ? 164  GLY D N   1 
ATOM   10177 C  CA  . GLY D 1 164 ? -13.201 10.148  -11.085 1.00 34.52  ? 164  GLY D CA  1 
ATOM   10178 C  C   . GLY D 1 164 ? -13.691 11.580  -11.134 1.00 30.93  ? 164  GLY D C   1 
ATOM   10179 O  O   . GLY D 1 164 ? -12.950 12.513  -10.813 1.00 42.49  ? 164  GLY D O   1 
ATOM   10180 N  N   . ARG D 1 165 ? -14.941 11.757  -11.557 1.00 33.14  ? 165  ARG D N   1 
ATOM   10181 C  CA  . ARG D 1 165 ? -15.572 13.076  -11.555 1.00 50.02  ? 165  ARG D CA  1 
ATOM   10182 C  C   . ARG D 1 165 ? -15.854 13.551  -10.125 1.00 51.97  ? 165  ARG D C   1 
ATOM   10183 O  O   . ARG D 1 165 ? -15.414 14.638  -9.718  1.00 47.55  ? 165  ARG D O   1 
ATOM   10184 C  CB  . ARG D 1 165 ? -16.864 13.058  -12.370 1.00 39.63  ? 165  ARG D CB  1 
ATOM   10185 C  CG  . ARG D 1 165 ? -17.590 14.391  -12.375 1.00 42.87  ? 165  ARG D CG  1 
ATOM   10186 C  CD  . ARG D 1 165 ? -18.800 14.383  -13.328 1.00 38.51  ? 165  ARG D CD  1 
ATOM   10187 N  NE  . ARG D 1 165 ? -19.770 15.429  -12.990 1.00 27.41  ? 165  ARG D NE  1 
ATOM   10188 C  CZ  . ARG D 1 165 ? -19.842 16.632  -13.568 1.00 36.40  ? 165  ARG D CZ  1 
ATOM   10189 N  NH1 . ARG D 1 165 ? -19.017 16.988  -14.555 1.00 23.96  ? 165  ARG D NH1 1 
ATOM   10190 N  NH2 . ARG D 1 165 ? -20.765 17.492  -13.160 1.00 38.42  ? 165  ARG D NH2 1 
ATOM   10191 N  N   . GLY D 1 166 ? -16.587 12.724  -9.374  1.00 38.60  ? 166  GLY D N   1 
ATOM   10192 C  CA  . GLY D 1 166 ? -16.856 12.984  -7.970  1.00 38.72  ? 166  GLY D CA  1 
ATOM   10193 C  C   . GLY D 1 166 ? -15.672 12.601  -7.101  1.00 40.08  ? 166  GLY D C   1 
ATOM   10194 O  O   . GLY D 1 166 ? -14.695 12.038  -7.601  1.00 47.65  ? 166  GLY D O   1 
ATOM   10195 N  N   . ASN D 1 167 ? -15.741 12.908  -5.806  1.00 34.40  ? 167  ASN D N   1 
ATOM   10196 C  CA  . ASN D 1 167 ? -14.637 12.564  -4.915  1.00 33.68  ? 167  ASN D CA  1 
ATOM   10197 C  C   . ASN D 1 167 ? -14.614 11.053  -4.647  1.00 41.27  ? 167  ASN D C   1 
ATOM   10198 O  O   . ASN D 1 167 ? -15.148 10.272  -5.445  1.00 47.45  ? 167  ASN D O   1 
ATOM   10199 C  CB  . ASN D 1 167 ? -14.648 13.411  -3.632  1.00 28.38  ? 167  ASN D CB  1 
ATOM   10200 C  CG  . ASN D 1 167 ? -15.720 12.995  -2.659  1.00 27.78  ? 167  ASN D CG  1 
ATOM   10201 O  OD1 . ASN D 1 167 ? -16.555 12.156  -2.970  1.00 36.56  ? 167  ASN D OD1 1 
ATOM   10202 N  ND2 . ASN D 1 167 ? -15.702 13.586  -1.464  1.00 22.02  ? 167  ASN D ND2 1 
ATOM   10203 N  N   . ALA D 1 168 ? -13.988 10.632  -3.554  1.00 46.24  ? 168  ALA D N   1 
ATOM   10204 C  CA  . ALA D 1 168 ? -13.811 9.203   -3.286  1.00 48.22  ? 168  ALA D CA  1 
ATOM   10205 C  C   . ALA D 1 168 ? -15.104 8.524   -2.831  1.00 65.47  ? 168  ALA D C   1 
ATOM   10206 O  O   . ALA D 1 168 ? -15.224 7.298   -2.894  1.00 74.89  ? 168  ALA D O   1 
ATOM   10207 C  CB  . ALA D 1 168 ? -12.706 8.980   -2.264  1.00 51.22  ? 168  ALA D CB  1 
ATOM   10208 N  N   . ALA D 1 169 ? -16.060 9.321   -2.360  1.00 62.35  ? 169  ALA D N   1 
ATOM   10209 C  CA  . ALA D 1 169 ? -17.379 8.816   -1.985  1.00 40.24  ? 169  ALA D CA  1 
ATOM   10210 C  C   . ALA D 1 169 ? -18.333 8.938   -3.173  1.00 42.27  ? 169  ALA D C   1 
ATOM   10211 O  O   . ALA D 1 169 ? -19.532 8.692   -3.051  1.00 37.31  ? 169  ALA D O   1 
ATOM   10212 C  CB  . ALA D 1 169 ? -17.920 9.573   -0.792  1.00 25.50  ? 169  ALA D CB  1 
ATOM   10213 N  N   . ASN D 1 170 ? -17.783 9.325   -4.321  1.00 43.13  ? 170  ASN D N   1 
ATOM   10214 C  CA  . ASN D 1 170 ? -18.551 9.438   -5.552  1.00 51.53  ? 170  ASN D CA  1 
ATOM   10215 C  C   . ASN D 1 170 ? -19.628 10.517  -5.530  1.00 54.43  ? 170  ASN D C   1 
ATOM   10216 O  O   . ASN D 1 170 ? -20.635 10.396  -6.231  1.00 61.45  ? 170  ASN D O   1 
ATOM   10217 C  CB  . ASN D 1 170 ? -19.174 8.090   -5.925  1.00 64.11  ? 170  ASN D CB  1 
ATOM   10218 C  CG  . ASN D 1 170 ? -18.305 7.293   -6.872  1.00 79.55  ? 170  ASN D CG  1 
ATOM   10219 O  OD1 . ASN D 1 170 ? -17.860 6.187   -6.553  1.00 79.33  ? 170  ASN D OD1 1 
ATOM   10220 N  ND2 . ASN D 1 170 ? -18.053 7.855   -8.050  1.00 85.19  ? 170  ASN D ND2 1 
ATOM   10221 N  N   . ILE D 1 171 ? -19.435 11.569  -4.738  1.00 37.19  ? 171  ILE D N   1 
ATOM   10222 C  CA  . ILE D 1 171 ? -20.378 12.687  -4.819  1.00 50.84  ? 171  ILE D CA  1 
ATOM   10223 C  C   . ILE D 1 171 ? -19.754 13.863  -5.572  1.00 39.30  ? 171  ILE D C   1 
ATOM   10224 O  O   . ILE D 1 171 ? -18.562 14.129  -5.460  1.00 35.17  ? 171  ILE D O   1 
ATOM   10225 C  CB  . ILE D 1 171 ? -20.941 13.157  -3.435  1.00 50.44  ? 171  ILE D CB  1 
ATOM   10226 C  CG1 . ILE D 1 171 ? -20.030 14.209  -2.811  1.00 39.60  ? 171  ILE D CG1 1 
ATOM   10227 C  CG2 . ILE D 1 171 ? -21.222 11.986  -2.502  1.00 36.28  ? 171  ILE D CG2 1 
ATOM   10228 C  CD1 . ILE D 1 171 ? -20.411 15.607  -3.186  1.00 43.74  ? 171  ILE D CD1 1 
ATOM   10229 N  N   . ASP D 1 172 ? -20.582 14.551  -6.343  1.00 42.03  ? 172  ASP D N   1 
ATOM   10230 C  CA  . ASP D 1 172 ? -20.134 15.622  -7.214  1.00 34.75  ? 172  ASP D CA  1 
ATOM   10231 C  C   . ASP D 1 172 ? -19.947 16.922  -6.444  1.00 31.90  ? 172  ASP D C   1 
ATOM   10232 O  O   . ASP D 1 172 ? -20.906 17.600  -6.095  1.00 43.26  ? 172  ASP D O   1 
ATOM   10233 C  CB  . ASP D 1 172 ? -21.144 15.804  -8.338  1.00 34.46  ? 172  ASP D CB  1 
ATOM   10234 C  CG  . ASP D 1 172 ? -20.766 16.900  -9.297  1.00 38.53  ? 172  ASP D CG  1 
ATOM   10235 O  OD1 . ASP D 1 172 ? -20.083 17.866  -8.901  1.00 41.92  ? 172  ASP D OD1 1 
ATOM   10236 O  OD2 . ASP D 1 172 ? -21.180 16.798  -10.466 1.00 44.95  ? 172  ASP D OD2 1 
ATOM   10237 N  N   . LEU D 1 173 ? -18.694 17.270  -6.202  1.00 28.93  ? 173  LEU D N   1 
ATOM   10238 C  CA  . LEU D 1 173 ? -18.354 18.411  -5.370  1.00 44.92  ? 173  LEU D CA  1 
ATOM   10239 C  C   . LEU D 1 173 ? -18.969 19.731  -5.873  1.00 35.02  ? 173  LEU D C   1 
ATOM   10240 O  O   . LEU D 1 173 ? -19.111 20.686  -5.108  1.00 29.63  ? 173  LEU D O   1 
ATOM   10241 C  CB  . LEU D 1 173 ? -16.820 18.518  -5.221  1.00 42.95  ? 173  LEU D CB  1 
ATOM   10242 C  CG  . LEU D 1 173 ? -16.086 17.381  -4.490  1.00 30.48  ? 173  LEU D CG  1 
ATOM   10243 C  CD1 . LEU D 1 173 ? -14.599 17.611  -4.522  1.00 16.26  ? 173  LEU D CD1 1 
ATOM   10244 C  CD2 . LEU D 1 173 ? -16.577 17.230  -3.045  1.00 37.48  ? 173  LEU D CD2 1 
ATOM   10245 N  N   . ASN D 1 174 ? -19.334 19.789  -7.147  1.00 22.01  ? 174  ASN D N   1 
ATOM   10246 C  CA  . ASN D 1 174 ? -19.979 20.987  -7.666  1.00 19.02  ? 174  ASN D CA  1 
ATOM   10247 C  C   . ASN D 1 174 ? -21.479 20.967  -7.406  1.00 30.74  ? 174  ASN D C   1 
ATOM   10248 O  O   . ASN D 1 174 ? -22.240 21.740  -7.988  1.00 44.38  ? 174  ASN D O   1 
ATOM   10249 C  CB  . ASN D 1 174 ? -19.696 21.186  -9.150  1.00 17.99  ? 174  ASN D CB  1 
ATOM   10250 C  CG  . ASN D 1 174 ? -19.675 22.656  -9.536  1.00 35.38  ? 174  ASN D CG  1 
ATOM   10251 O  OD1 . ASN D 1 174 ? -19.534 23.544  -8.693  1.00 39.08  ? 174  ASN D OD1 1 
ATOM   10252 N  ND2 . ASN D 1 174 ? -19.816 22.918  -10.818 1.00 39.58  ? 174  ASN D ND2 1 
ATOM   10253 N  N   . ARG D 1 175 ? -21.896 20.059  -6.531  1.00 29.42  ? 175  ARG D N   1 
ATOM   10254 C  CA  . ARG D 1 175 ? -23.266 20.031  -6.027  1.00 37.62  ? 175  ARG D CA  1 
ATOM   10255 C  C   . ARG D 1 175 ? -23.308 20.094  -4.498  1.00 31.40  ? 175  ARG D C   1 
ATOM   10256 O  O   . ARG D 1 175 ? -24.380 20.087  -3.906  1.00 40.02  ? 175  ARG D O   1 
ATOM   10257 C  CB  . ARG D 1 175 ? -23.974 18.756  -6.470  1.00 21.55  ? 175  ARG D CB  1 
ATOM   10258 C  CG  . ARG D 1 175 ? -24.006 18.554  -7.948  1.00 28.98  ? 175  ARG D CG  1 
ATOM   10259 C  CD  . ARG D 1 175 ? -24.439 19.807  -8.700  1.00 34.72  ? 175  ARG D CD  1 
ATOM   10260 N  NE  . ARG D 1 175 ? -24.681 19.434  -10.084 1.00 48.49  ? 175  ARG D NE  1 
ATOM   10261 C  CZ  . ARG D 1 175 ? -23.950 19.754  -11.148 1.00 48.49  ? 175  ARG D CZ  1 
ATOM   10262 N  NH1 . ARG D 1 175 ? -24.324 19.274  -12.323 1.00 49.64  ? 175  ARG D NH1 1 
ATOM   10263 N  NH2 . ARG D 1 175 ? -22.884 20.538  -11.067 1.00 56.50  ? 175  ARG D NH2 1 
ATOM   10264 N  N   . ASP D 1 176 ? -22.137 20.173  -3.876  1.00 29.97  ? 176  ASP D N   1 
ATOM   10265 C  CA  . ASP D 1 176 ? -22.006 19.953  -2.442  1.00 31.60  ? 176  ASP D CA  1 
ATOM   10266 C  C   . ASP D 1 176 ? -21.888 21.249  -1.637  1.00 34.25  ? 176  ASP D C   1 
ATOM   10267 O  O   . ASP D 1 176 ? -21.905 21.219  -0.400  1.00 33.12  ? 176  ASP D O   1 
ATOM   10268 C  CB  . ASP D 1 176 ? -20.804 19.027  -2.158  1.00 36.95  ? 176  ASP D CB  1 
ATOM   10269 C  CG  . ASP D 1 176 ? -20.849 18.393  -0.758  1.00 50.65  ? 176  ASP D CG  1 
ATOM   10270 O  OD1 . ASP D 1 176 ? -21.962 18.047  -0.275  1.00 46.93  ? 176  ASP D OD1 1 
ATOM   10271 O  OD2 . ASP D 1 176 ? -19.761 18.224  -0.144  1.00 48.25  ? 176  ASP D OD2 1 
ATOM   10272 N  N   . PHE D 1 177 ? -21.775 22.388  -2.320  1.00 29.89  ? 177  PHE D N   1 
ATOM   10273 C  CA  . PHE D 1 177 ? -21.642 23.661  -1.606  1.00 28.78  ? 177  PHE D CA  1 
ATOM   10274 C  C   . PHE D 1 177 ? -22.997 24.176  -1.129  1.00 32.80  ? 177  PHE D C   1 
ATOM   10275 O  O   . PHE D 1 177 ? -24.018 23.851  -1.736  1.00 47.76  ? 177  PHE D O   1 
ATOM   10276 C  CB  . PHE D 1 177 ? -20.925 24.710  -2.467  1.00 31.03  ? 177  PHE D CB  1 
ATOM   10277 C  CG  . PHE D 1 177 ? -19.435 24.499  -2.567  1.00 36.29  ? 177  PHE D CG  1 
ATOM   10278 C  CD1 . PHE D 1 177 ? -18.916 23.535  -3.417  1.00 44.55  ? 177  PHE D CD1 1 
ATOM   10279 C  CD2 . PHE D 1 177 ? -18.556 25.254  -1.806  1.00 31.62  ? 177  PHE D CD2 1 
ATOM   10280 C  CE1 . PHE D 1 177 ? -17.554 23.329  -3.512  1.00 36.57  ? 177  PHE D CE1 1 
ATOM   10281 C  CE2 . PHE D 1 177 ? -17.187 25.047  -1.893  1.00 35.81  ? 177  PHE D CE2 1 
ATOM   10282 C  CZ  . PHE D 1 177 ? -16.692 24.085  -2.752  1.00 33.65  ? 177  PHE D CZ  1 
ATOM   10283 N  N   . PRO D 1 178 ? -23.016 24.962  -0.028  1.00 31.68  ? 178  PRO D N   1 
ATOM   10284 C  CA  . PRO D 1 178 ? -24.281 25.583  0.400   1.00 34.85  ? 178  PRO D CA  1 
ATOM   10285 C  C   . PRO D 1 178 ? -24.931 26.406  -0.723  1.00 42.72  ? 178  PRO D C   1 
ATOM   10286 O  O   . PRO D 1 178 ? -24.252 27.114  -1.480  1.00 30.64  ? 178  PRO D O   1 
ATOM   10287 C  CB  . PRO D 1 178 ? -23.866 26.472  1.577   1.00 24.01  ? 178  PRO D CB  1 
ATOM   10288 C  CG  . PRO D 1 178 ? -22.608 25.797  2.140   1.00 19.31  ? 178  PRO D CG  1 
ATOM   10289 C  CD  . PRO D 1 178 ? -21.916 25.200  0.933   1.00 30.03  ? 178  PRO D CD  1 
ATOM   10290 N  N   . ASP D 1 179 ? -26.250 26.280  -0.835  1.00 43.87  ? 179  ASP D N   1 
ATOM   10291 C  CA  . ASP D 1 179 ? -26.995 26.950  -1.879  1.00 38.71  ? 179  ASP D CA  1 
ATOM   10292 C  C   . ASP D 1 179 ? -27.641 28.185  -1.281  1.00 41.77  ? 179  ASP D C   1 
ATOM   10293 O  O   . ASP D 1 179 ? -28.159 28.155  -0.165  1.00 37.83  ? 179  ASP D O   1 
ATOM   10294 C  CB  . ASP D 1 179 ? -28.056 26.008  -2.466  1.00 50.29  ? 179  ASP D CB  1 
ATOM   10295 C  CG  . ASP D 1 179 ? -28.646 26.519  -3.772  1.00 55.15  ? 179  ASP D CG  1 
ATOM   10296 O  OD1 . ASP D 1 179 ? -27.876 27.015  -4.627  1.00 58.37  ? 179  ASP D OD1 1 
ATOM   10297 O  OD2 . ASP D 1 179 ? -29.882 26.416  -3.944  1.00 53.37  ? 179  ASP D OD2 1 
ATOM   10298 N  N   . ARG D 1 180 ? -27.585 29.280  -2.026  1.00 43.29  ? 180  ARG D N   1 
ATOM   10299 C  CA  . ARG D 1 180 ? -28.205 30.522  -1.608  1.00 43.95  ? 180  ARG D CA  1 
ATOM   10300 C  C   . ARG D 1 180 ? -29.708 30.313  -1.438  1.00 47.74  ? 180  ARG D C   1 
ATOM   10301 O  O   . ARG D 1 180 ? -30.337 30.911  -0.564  1.00 45.26  ? 180  ARG D O   1 
ATOM   10302 C  CB  . ARG D 1 180 ? -27.948 31.584  -2.673  1.00 54.72  ? 180  ARG D CB  1 
ATOM   10303 C  CG  . ARG D 1 180 ? -28.346 31.125  -4.076  1.00 52.54  ? 180  ARG D CG  1 
ATOM   10304 C  CD  . ARG D 1 180 ? -27.813 32.063  -5.139  1.00 54.38  ? 180  ARG D CD  1 
ATOM   10305 N  NE  . ARG D 1 180 ? -28.400 31.775  -6.445  1.00 62.03  ? 180  ARG D NE  1 
ATOM   10306 C  CZ  . ARG D 1 180 ? -29.523 32.329  -6.888  1.00 47.36  ? 180  ARG D CZ  1 
ATOM   10307 N  NH1 . ARG D 1 180 ? -30.175 33.200  -6.122  1.00 42.03  ? 180  ARG D NH1 1 
ATOM   10308 N  NH2 . ARG D 1 180 ? -29.991 32.013  -8.090  1.00 26.29  ? 180  ARG D NH2 1 
ATOM   10309 N  N   . LEU D 1 181 ? -30.284 29.463  -2.283  1.00 29.13  ? 181  LEU D N   1 
ATOM   10310 C  CA  . LEU D 1 181 ? -31.713 29.190  -2.215  1.00 31.18  ? 181  LEU D CA  1 
ATOM   10311 C  C   . LEU D 1 181 ? -32.016 28.139  -1.149  1.00 42.11  ? 181  LEU D C   1 
ATOM   10312 O  O   . LEU D 1 181 ? -32.880 28.341  -0.291  1.00 44.30  ? 181  LEU D O   1 
ATOM   10313 C  CB  . LEU D 1 181 ? -32.224 28.721  -3.574  1.00 30.57  ? 181  LEU D CB  1 
ATOM   10314 C  CG  . LEU D 1 181 ? -31.687 29.550  -4.733  1.00 31.68  ? 181  LEU D CG  1 
ATOM   10315 C  CD1 . LEU D 1 181 ? -32.055 28.893  -6.037  1.00 29.38  ? 181  LEU D CD1 1 
ATOM   10316 C  CD2 . LEU D 1 181 ? -32.209 30.971  -4.661  1.00 31.95  ? 181  LEU D CD2 1 
ATOM   10317 N  N   . ALA D 1 191 ? -18.601 22.721  8.041   1.00 79.50  ? 191  ALA D N   1 
ATOM   10318 C  CA  . ALA D 1 191 ? -18.856 21.395  7.497   1.00 69.57  ? 191  ALA D CA  1 
ATOM   10319 C  C   . ALA D 1 191 ? -20.274 20.952  7.795   1.00 82.45  ? 191  ALA D C   1 
ATOM   10320 O  O   . ALA D 1 191 ? -21.115 21.749  8.223   1.00 76.04  ? 191  ALA D O   1 
ATOM   10321 C  CB  . ALA D 1 191 ? -17.875 20.383  8.061   1.00 56.47  ? 191  ALA D CB  1 
ATOM   10322 N  N   . GLN D 1 192 ? -20.506 19.662  7.573   1.00 87.52  ? 192  GLN D N   1 
ATOM   10323 C  CA  . GLN D 1 192 ? -21.798 19.019  7.749   1.00 107.93 ? 192  GLN D CA  1 
ATOM   10324 C  C   . GLN D 1 192 ? -21.577 17.615  7.221   1.00 98.69  ? 192  GLN D C   1 
ATOM   10325 O  O   . GLN D 1 192 ? -20.494 17.055  7.392   1.00 109.06 ? 192  GLN D O   1 
ATOM   10326 C  CB  . GLN D 1 192 ? -22.871 19.729  6.916   1.00 132.09 ? 192  GLN D CB  1 
ATOM   10327 C  CG  . GLN D 1 192 ? -24.297 19.220  7.129   1.00 138.54 ? 192  GLN D CG  1 
ATOM   10328 C  CD  . GLN D 1 192 ? -25.202 19.508  5.942   1.00 136.36 ? 192  GLN D CD  1 
ATOM   10329 O  OE1 . GLN D 1 192 ? -25.654 20.638  5.745   1.00 132.58 ? 192  GLN D OE1 1 
ATOM   10330 N  NE2 . GLN D 1 192 ? -25.467 18.482  5.141   1.00 137.00 ? 192  GLN D NE2 1 
ATOM   10331 N  N   . SER D 1 193 ? -22.585 17.045  6.568   1.00 71.71  ? 193  SER D N   1 
ATOM   10332 C  CA  . SER D 1 193 ? -22.337 15.883  5.740   1.00 54.04  ? 193  SER D CA  1 
ATOM   10333 C  C   . SER D 1 193 ? -21.894 16.412  4.379   1.00 40.93  ? 193  SER D C   1 
ATOM   10334 O  O   . SER D 1 193 ? -22.250 15.856  3.340   1.00 42.70  ? 193  SER D O   1 
ATOM   10335 C  CB  . SER D 1 193 ? -23.572 14.980  5.636   1.00 54.76  ? 193  SER D CB  1 
ATOM   10336 O  OG  . SER D 1 193 ? -23.204 13.603  5.661   1.00 42.69  ? 193  SER D OG  1 
ATOM   10337 N  N   . ARG D 1 194 ? -21.136 17.513  4.396   1.00 36.31  ? 194  ARG D N   1 
ATOM   10338 C  CA  . ARG D 1 194 ? -20.426 17.993  3.204   1.00 42.96  ? 194  ARG D CA  1 
ATOM   10339 C  C   . ARG D 1 194 ? -19.056 17.336  3.124   1.00 50.91  ? 194  ARG D C   1 
ATOM   10340 O  O   . ARG D 1 194 ? -18.453 17.008  4.145   1.00 54.18  ? 194  ARG D O   1 
ATOM   10341 C  CB  . ARG D 1 194 ? -20.235 19.515  3.212   1.00 29.19  ? 194  ARG D CB  1 
ATOM   10342 C  CG  . ARG D 1 194 ? -21.515 20.288  3.303   1.00 34.53  ? 194  ARG D CG  1 
ATOM   10343 C  CD  . ARG D 1 194 ? -21.335 21.740  2.901   1.00 44.85  ? 194  ARG D CD  1 
ATOM   10344 N  NE  . ARG D 1 194 ? -22.469 22.535  3.358   1.00 55.85  ? 194  ARG D NE  1 
ATOM   10345 C  CZ  . ARG D 1 194 ? -23.694 22.446  2.847   1.00 57.33  ? 194  ARG D CZ  1 
ATOM   10346 N  NH1 . ARG D 1 194 ? -23.942 21.604  1.856   1.00 44.58  ? 194  ARG D NH1 1 
ATOM   10347 N  NH2 . ARG D 1 194 ? -24.674 23.196  3.331   1.00 65.47  ? 194  ARG D NH2 1 
ATOM   10348 N  N   . GLN D 1 195 ? -18.557 17.171  1.907   1.00 44.77  ? 195  GLN D N   1 
ATOM   10349 C  CA  . GLN D 1 195 ? -17.298 16.482  1.698   1.00 34.93  ? 195  GLN D CA  1 
ATOM   10350 C  C   . GLN D 1 195 ? -16.126 17.265  2.256   1.00 32.98  ? 195  GLN D C   1 
ATOM   10351 O  O   . GLN D 1 195 ? -16.156 18.492  2.322   1.00 29.07  ? 195  GLN D O   1 
ATOM   10352 C  CB  . GLN D 1 195 ? -17.090 16.187  0.221   1.00 34.61  ? 195  GLN D CB  1 
ATOM   10353 C  CG  . GLN D 1 195 ? -18.190 15.325  -0.348  1.00 44.51  ? 195  GLN D CG  1 
ATOM   10354 C  CD  . GLN D 1 195 ? -18.364 13.994  0.399   1.00 49.74  ? 195  GLN D CD  1 
ATOM   10355 O  OE1 . GLN D 1 195 ? -17.525 13.092  0.296   1.00 53.73  ? 195  GLN D OE1 1 
ATOM   10356 N  NE2 . GLN D 1 195 ? -19.463 13.867  1.142   1.00 31.36  ? 195  GLN D NE2 1 
ATOM   10357 N  N   . PRO D 1 196 ? -15.088 16.538  2.679   1.00 39.50  ? 196  PRO D N   1 
ATOM   10358 C  CA  . PRO D 1 196 ? -13.855 17.104  3.236   1.00 36.18  ? 196  PRO D CA  1 
ATOM   10359 C  C   . PRO D 1 196 ? -13.298 18.214  2.340   1.00 37.53  ? 196  PRO D C   1 
ATOM   10360 O  O   . PRO D 1 196 ? -12.728 19.210  2.812   1.00 41.98  ? 196  PRO D O   1 
ATOM   10361 C  CB  . PRO D 1 196 ? -12.888 15.913  3.207   1.00 28.80  ? 196  PRO D CB  1 
ATOM   10362 C  CG  . PRO D 1 196 ? -13.756 14.705  3.224   1.00 32.82  ? 196  PRO D CG  1 
ATOM   10363 C  CD  . PRO D 1 196 ? -15.036 15.066  2.564   1.00 26.95  ? 196  PRO D CD  1 
ATOM   10364 N  N   . GLU D 1 197 ? -13.447 18.022  1.037   1.00 21.97  ? 197  GLU D N   1 
ATOM   10365 C  CA  . GLU D 1 197 ? -12.871 18.944  0.091   1.00 25.93  ? 197  GLU D CA  1 
ATOM   10366 C  C   . GLU D 1 197 ? -13.726 20.192  0.026   1.00 29.60  ? 197  GLU D C   1 
ATOM   10367 O  O   . GLU D 1 197 ? -13.214 21.309  -0.036  1.00 28.84  ? 197  GLU D O   1 
ATOM   10368 C  CB  . GLU D 1 197 ? -12.749 18.269  -1.258  1.00 21.81  ? 197  GLU D CB  1 
ATOM   10369 C  CG  . GLU D 1 197 ? -11.771 17.089  -1.214  1.00 26.56  ? 197  GLU D CG  1 
ATOM   10370 C  CD  . GLU D 1 197 ? -12.422 15.761  -0.832  1.00 36.38  ? 197  GLU D CD  1 
ATOM   10371 O  OE1 . GLU D 1 197 ? -11.730 14.718  -0.898  1.00 36.25  ? 197  GLU D OE1 1 
ATOM   10372 O  OE2 . GLU D 1 197 ? -13.628 15.748  -0.487  1.00 45.42  ? 197  GLU D OE2 1 
ATOM   10373 N  N   . THR D 1 198 ? -15.037 19.994  0.083   1.00 32.34  ? 198  THR D N   1 
ATOM   10374 C  CA  . THR D 1 198 ? -15.979 21.109  0.100   1.00 36.08  ? 198  THR D CA  1 
ATOM   10375 C  C   . THR D 1 198 ? -15.800 21.940  1.368   1.00 33.97  ? 198  THR D C   1 
ATOM   10376 O  O   . THR D 1 198 ? -15.678 23.171  1.319   1.00 34.39  ? 198  THR D O   1 
ATOM   10377 C  CB  . THR D 1 198 ? -17.434 20.612  0.031   1.00 42.61  ? 198  THR D CB  1 
ATOM   10378 O  OG1 . THR D 1 198 ? -17.592 19.718  -1.082  1.00 46.46  ? 198  THR D OG1 1 
ATOM   10379 C  CG2 . THR D 1 198 ? -18.370 21.778  -0.136  1.00 30.70  ? 198  THR D CG2 1 
ATOM   10380 N  N   . ALA D 1 199 ? -15.775 21.249  2.499   1.00 18.34  ? 199  ALA D N   1 
ATOM   10381 C  CA  . ALA D 1 199 ? -15.618 21.902  3.778   1.00 20.35  ? 199  ALA D CA  1 
ATOM   10382 C  C   . ALA D 1 199 ? -14.336 22.716  3.820   1.00 33.71  ? 199  ALA D C   1 
ATOM   10383 O  O   . ALA D 1 199 ? -14.320 23.841  4.340   1.00 30.68  ? 199  ALA D O   1 
ATOM   10384 C  CB  . ALA D 1 199 ? -15.632 20.878  4.893   1.00 16.04  ? 199  ALA D CB  1 
ATOM   10385 N  N   . ALA D 1 200 ? -13.262 22.145  3.271   1.00 31.84  ? 200  ALA D N   1 
ATOM   10386 C  CA  . ALA D 1 200 ? -11.960 22.819  3.248   1.00 28.60  ? 200  ALA D CA  1 
ATOM   10387 C  C   . ALA D 1 200 ? -12.069 24.138  2.493   1.00 34.39  ? 200  ALA D C   1 
ATOM   10388 O  O   . ALA D 1 200 ? -11.661 25.197  2.988   1.00 30.39  ? 200  ALA D O   1 
ATOM   10389 C  CB  . ALA D 1 200 ? -10.935 21.942  2.607   1.00 22.48  ? 200  ALA D CB  1 
ATOM   10390 N  N   . LEU D 1 201 ? -12.651 24.066  1.302   1.00 17.55  ? 201  LEU D N   1 
ATOM   10391 C  CA  . LEU D 1 201 ? -12.790 25.249  0.490   1.00 27.11  ? 201  LEU D CA  1 
ATOM   10392 C  C   . LEU D 1 201 ? -13.745 26.301  1.056   1.00 34.29  ? 201  LEU D C   1 
ATOM   10393 O  O   . LEU D 1 201 ? -13.398 27.480  1.102   1.00 35.25  ? 201  LEU D O   1 
ATOM   10394 C  CB  . LEU D 1 201 ? -13.126 24.872  -0.951  1.00 26.30  ? 201  LEU D CB  1 
ATOM   10395 C  CG  . LEU D 1 201 ? -11.799 24.786  -1.702  1.00 28.90  ? 201  LEU D CG  1 
ATOM   10396 C  CD1 . LEU D 1 201 ? -11.163 23.417  -1.516  1.00 28.92  ? 201  LEU D CD1 1 
ATOM   10397 C  CD2 . LEU D 1 201 ? -11.961 25.138  -3.168  1.00 45.52  ? 201  LEU D CD2 1 
ATOM   10398 N  N   . VAL D 1 202 ? -14.938 25.889  1.480   1.00 22.84  ? 202  VAL D N   1 
ATOM   10399 C  CA  . VAL D 1 202 ? -15.870 26.821  2.098   1.00 18.96  ? 202  VAL D CA  1 
ATOM   10400 C  C   . VAL D 1 202 ? -15.127 27.674  3.147   1.00 37.96  ? 202  VAL D C   1 
ATOM   10401 O  O   . VAL D 1 202 ? -15.087 28.911  3.055   1.00 31.61  ? 202  VAL D O   1 
ATOM   10402 C  CB  . VAL D 1 202 ? -17.062 26.071  2.745   1.00 26.03  ? 202  VAL D CB  1 
ATOM   10403 C  CG1 . VAL D 1 202 ? -17.839 26.968  3.699   1.00 10.73  ? 202  VAL D CG1 1 
ATOM   10404 C  CG2 . VAL D 1 202 ? -17.984 25.513  1.685   1.00 14.94  ? 202  VAL D CG2 1 
ATOM   10405 N  N   . ASN D 1 203 ? -14.528 27.005  4.129   1.00 23.52  ? 203  ASN D N   1 
ATOM   10406 C  CA  . ASN D 1 203 ? -13.726 27.672  5.146   1.00 22.09  ? 203  ASN D CA  1 
ATOM   10407 C  C   . ASN D 1 203 ? -12.789 28.709  4.576   1.00 22.44  ? 203  ASN D C   1 
ATOM   10408 O  O   . ASN D 1 203 ? -12.754 29.856  5.016   1.00 34.43  ? 203  ASN D O   1 
ATOM   10409 C  CB  . ASN D 1 203 ? -12.871 26.657  5.890   1.00 27.86  ? 203  ASN D CB  1 
ATOM   10410 C  CG  . ASN D 1 203 ? -13.617 25.983  6.983   1.00 41.35  ? 203  ASN D CG  1 
ATOM   10411 O  OD1 . ASN D 1 203 ? -14.853 25.965  6.985   1.00 46.58  ? 203  ASN D OD1 1 
ATOM   10412 N  ND2 . ASN D 1 203 ? -12.882 25.414  7.931   1.00 52.95  ? 203  ASN D ND2 1 
ATOM   10413 N  N   . TRP D 1 204 ? -12.001 28.278  3.607   1.00 24.08  ? 204  TRP D N   1 
ATOM   10414 C  CA  . TRP D 1 204 ? -11.011 29.136  2.993   1.00 23.23  ? 204  TRP D CA  1 
ATOM   10415 C  C   . TRP D 1 204 ? -11.687 30.357  2.375   1.00 37.21  ? 204  TRP D C   1 
ATOM   10416 O  O   . TRP D 1 204 ? -11.297 31.499  2.648   1.00 40.29  ? 204  TRP D O   1 
ATOM   10417 C  CB  . TRP D 1 204 ? -10.239 28.341  1.944   1.00 20.97  ? 204  TRP D CB  1 
ATOM   10418 C  CG  . TRP D 1 204 ? -9.005  29.009  1.434   1.00 25.10  ? 204  TRP D CG  1 
ATOM   10419 C  CD1 . TRP D 1 204 ? -8.017  29.598  2.173   1.00 25.59  ? 204  TRP D CD1 1 
ATOM   10420 C  CD2 . TRP D 1 204 ? -8.609  29.137  0.062   1.00 29.67  ? 204  TRP D CD2 1 
ATOM   10421 N  NE1 . TRP D 1 204 ? -7.032  30.089  1.347   1.00 29.74  ? 204  TRP D NE1 1 
ATOM   10422 C  CE2 . TRP D 1 204 ? -7.374  29.823  0.045   1.00 27.05  ? 204  TRP D CE2 1 
ATOM   10423 C  CE3 . TRP D 1 204 ? -9.183  28.744  -1.154  1.00 17.93  ? 204  TRP D CE3 1 
ATOM   10424 C  CZ2 . TRP D 1 204 ? -6.705  30.122  -1.134  1.00 17.88  ? 204  TRP D CZ2 1 
ATOM   10425 C  CZ3 . TRP D 1 204 ? -8.508  29.039  -2.329  1.00 24.01  ? 204  TRP D CZ3 1 
ATOM   10426 C  CH2 . TRP D 1 204 ? -7.283  29.720  -2.308  1.00 25.04  ? 204  TRP D CH2 1 
ATOM   10427 N  N   . ILE D 1 205 ? -12.716 30.114  1.564   1.00 30.03  ? 205  ILE D N   1 
ATOM   10428 C  CA  . ILE D 1 205 ? -13.328 31.177  0.778   1.00 31.28  ? 205  ILE D CA  1 
ATOM   10429 C  C   . ILE D 1 205 ? -13.828 32.311  1.681   1.00 44.86  ? 205  ILE D C   1 
ATOM   10430 O  O   . ILE D 1 205 ? -13.753 33.491  1.312   1.00 51.08  ? 205  ILE D O   1 
ATOM   10431 C  CB  . ILE D 1 205 ? -14.491 30.635  -0.095  1.00 27.78  ? 205  ILE D CB  1 
ATOM   10432 C  CG1 . ILE D 1 205 ? -13.984 29.655  -1.147  1.00 23.13  ? 205  ILE D CG1 1 
ATOM   10433 C  CG2 . ILE D 1 205 ? -15.245 31.776  -0.755  1.00 33.46  ? 205  ILE D CG2 1 
ATOM   10434 C  CD1 . ILE D 1 205 ? -15.101 28.915  -1.858  1.00 24.81  ? 205  ILE D CD1 1 
ATOM   10435 N  N   . VAL D 1 206 ? -14.335 31.942  2.859   1.00 37.19  ? 206  VAL D N   1 
ATOM   10436 C  CA  . VAL D 1 206 ? -14.897 32.907  3.806   1.00 35.62  ? 206  VAL D CA  1 
ATOM   10437 C  C   . VAL D 1 206 ? -13.812 33.399  4.753   1.00 31.69  ? 206  VAL D C   1 
ATOM   10438 O  O   . VAL D 1 206 ? -14.052 34.268  5.598   1.00 33.59  ? 206  VAL D O   1 
ATOM   10439 C  CB  . VAL D 1 206 ? -16.041 32.280  4.644   1.00 28.38  ? 206  VAL D CB  1 
ATOM   10440 C  CG1 . VAL D 1 206 ? -17.181 31.857  3.753   1.00 13.91  ? 206  VAL D CG1 1 
ATOM   10441 C  CG2 . VAL D 1 206 ? -15.523 31.076  5.425   1.00 33.63  ? 206  VAL D CG2 1 
ATOM   10442 N  N   . SER D 1 207 ? -12.613 32.846  4.601   1.00 29.15  ? 207  SER D N   1 
ATOM   10443 C  CA  . SER D 1 207 ? -11.509 33.162  5.507   1.00 29.03  ? 207  SER D CA  1 
ATOM   10444 C  C   . SER D 1 207 ? -10.757 34.420  5.095   1.00 29.33  ? 207  SER D C   1 
ATOM   10445 O  O   . SER D 1 207 ? -10.035 35.010  5.899   1.00 43.52  ? 207  SER D O   1 
ATOM   10446 C  CB  . SER D 1 207 ? -10.534 31.976  5.621   1.00 21.12  ? 207  SER D CB  1 
ATOM   10447 O  OG  . SER D 1 207 ? -9.503  32.055  4.649   1.00 30.77  ? 207  SER D OG  1 
ATOM   10448 N  N   . LYS D 1 208 ? -10.915 34.819  3.839   1.00 29.59  ? 208  LYS D N   1 
ATOM   10449 C  CA  . LYS D 1 208 ? -10.237 36.001  3.323   1.00 34.25  ? 208  LYS D CA  1 
ATOM   10450 C  C   . LYS D 1 208 ? -11.164 36.724  2.379   1.00 32.18  ? 208  LYS D C   1 
ATOM   10451 O  O   . LYS D 1 208 ? -12.020 36.107  1.751   1.00 49.55  ? 208  LYS D O   1 
ATOM   10452 C  CB  . LYS D 1 208 ? -8.941  35.621  2.601   1.00 34.67  ? 208  LYS D CB  1 
ATOM   10453 C  CG  . LYS D 1 208 ? -7.923  34.942  3.504   1.00 40.64  ? 208  LYS D CG  1 
ATOM   10454 C  CD  . LYS D 1 208 ? -6.607  34.639  2.788   1.00 45.16  ? 208  LYS D CD  1 
ATOM   10455 C  CE  . LYS D 1 208 ? -5.507  34.331  3.812   1.00 45.00  ? 208  LYS D CE  1 
ATOM   10456 N  NZ  . LYS D 1 208 ? -4.181  34.040  3.192   1.00 53.76  ? 208  LYS D NZ  1 
ATOM   10457 N  N   . PRO D 1 209 ? -10.994 38.040  2.274   1.00 22.12  ? 209  PRO D N   1 
ATOM   10458 C  CA  . PRO D 1 209 ? -11.817 38.924  1.449   1.00 19.05  ? 209  PRO D CA  1 
ATOM   10459 C  C   . PRO D 1 209 ? -11.496 38.812  -0.044  1.00 30.79  ? 209  PRO D C   1 
ATOM   10460 O  O   . PRO D 1 209 ? -11.262 39.832  -0.697  1.00 38.70  ? 209  PRO D O   1 
ATOM   10461 C  CB  . PRO D 1 209 ? -11.423 40.300  1.951   1.00 12.76  ? 209  PRO D CB  1 
ATOM   10462 C  CG  . PRO D 1 209 ? -10.008 40.125  2.320   1.00 31.20  ? 209  PRO D CG  1 
ATOM   10463 C  CD  . PRO D 1 209 ? -9.919  38.772  2.950   1.00 17.92  ? 209  PRO D CD  1 
ATOM   10464 N  N   . PHE D 1 210 ? -11.503 37.597  -0.577  1.00 21.24  ? 210  PHE D N   1 
ATOM   10465 C  CA  . PHE D 1 210 ? -11.234 37.407  -1.992  1.00 28.78  ? 210  PHE D CA  1 
ATOM   10466 C  C   . PHE D 1 210 ? -12.095 38.309  -2.876  1.00 34.43  ? 210  PHE D C   1 
ATOM   10467 O  O   . PHE D 1 210 ? -13.320 38.439  -2.687  1.00 38.23  ? 210  PHE D O   1 
ATOM   10468 C  CB  . PHE D 1 210 ? -11.412 35.947  -2.385  1.00 18.11  ? 210  PHE D CB  1 
ATOM   10469 C  CG  . PHE D 1 210 ? -10.336 35.051  -1.863  1.00 15.59  ? 210  PHE D CG  1 
ATOM   10470 C  CD1 . PHE D 1 210 ? -10.585 34.196  -0.808  1.00 14.57  ? 210  PHE D CD1 1 
ATOM   10471 C  CD2 . PHE D 1 210 ? -9.074  35.069  -2.432  1.00 23.53  ? 210  PHE D CD2 1 
ATOM   10472 C  CE1 . PHE D 1 210 ? -9.604  33.354  -0.332  1.00 26.11  ? 210  PHE D CE1 1 
ATOM   10473 C  CE2 . PHE D 1 210 ? -8.075  34.229  -1.963  1.00 33.21  ? 210  PHE D CE2 1 
ATOM   10474 C  CZ  . PHE D 1 210 ? -8.346  33.369  -0.905  1.00 35.55  ? 210  PHE D CZ  1 
ATOM   10475 N  N   . VAL D 1 211 ? -11.426 38.924  -3.847  1.00 24.83  ? 211  VAL D N   1 
ATOM   10476 C  CA  . VAL D 1 211 ? -12.037 39.894  -4.740  1.00 25.54  ? 211  VAL D CA  1 
ATOM   10477 C  C   . VAL D 1 211 ? -12.576 39.233  -5.997  1.00 28.54  ? 211  VAL D C   1 
ATOM   10478 O  O   . VAL D 1 211 ? -13.736 39.443  -6.380  1.00 35.84  ? 211  VAL D O   1 
ATOM   10479 C  CB  . VAL D 1 211 ? -11.027 40.982  -5.127  1.00 19.65  ? 211  VAL D CB  1 
ATOM   10480 C  CG1 . VAL D 1 211 ? -11.617 41.912  -6.169  1.00 20.19  ? 211  VAL D CG1 1 
ATOM   10481 C  CG2 . VAL D 1 211 ? -10.613 41.759  -3.881  1.00 21.88  ? 211  VAL D CG2 1 
ATOM   10482 N  N   . LEU D 1 212 ? -11.727 38.427  -6.628  1.00 17.86  ? 212  LEU D N   1 
ATOM   10483 C  CA  . LEU D 1 212 ? -12.055 37.804  -7.909  1.00 21.54  ? 212  LEU D CA  1 
ATOM   10484 C  C   . LEU D 1 212 ? -11.584 36.365  -7.917  1.00 20.01  ? 212  LEU D C   1 
ATOM   10485 O  O   . LEU D 1 212 ? -10.635 36.021  -7.233  1.00 39.65  ? 212  LEU D O   1 
ATOM   10486 C  CB  . LEU D 1 212 ? -11.406 38.589  -9.047  1.00 18.83  ? 212  LEU D CB  1 
ATOM   10487 C  CG  . LEU D 1 212 ? -11.414 38.045  -10.475 1.00 29.41  ? 212  LEU D CG  1 
ATOM   10488 C  CD1 . LEU D 1 212 ? -12.833 37.813  -10.958 1.00 41.16  ? 212  LEU D CD1 1 
ATOM   10489 C  CD2 . LEU D 1 212 ? -10.678 39.002  -11.417 1.00 25.07  ? 212  LEU D CD2 1 
ATOM   10490 N  N   . SER D 1 213 ? -12.253 35.520  -8.687  1.00 26.41  ? 213  SER D N   1 
ATOM   10491 C  CA  . SER D 1 213 ? -11.969 34.088  -8.663  1.00 26.02  ? 213  SER D CA  1 
ATOM   10492 C  C   . SER D 1 213 ? -12.423 33.406  -9.950  1.00 37.99  ? 213  SER D C   1 
ATOM   10493 O  O   . SER D 1 213 ? -13.293 33.923  -10.677 1.00 39.36  ? 213  SER D O   1 
ATOM   10494 C  CB  . SER D 1 213 ? -12.682 33.442  -7.469  1.00 27.10  ? 213  SER D CB  1 
ATOM   10495 O  OG  . SER D 1 213 ? -12.448 32.044  -7.423  1.00 44.48  ? 213  SER D OG  1 
ATOM   10496 N  N   . ALA D 1 214 ? -11.835 32.244  -10.233 1.00 34.70  ? 214  ALA D N   1 
ATOM   10497 C  CA  . ALA D 1 214 ? -12.291 31.404  -11.345 1.00 33.09  ? 214  ALA D CA  1 
ATOM   10498 C  C   . ALA D 1 214 ? -11.975 29.949  -11.052 1.00 25.99  ? 214  ALA D C   1 
ATOM   10499 O  O   . ALA D 1 214 ? -10.937 29.652  -10.454 1.00 30.09  ? 214  ALA D O   1 
ATOM   10500 C  CB  . ALA D 1 214 ? -11.637 31.833  -12.636 1.00 26.45  ? 214  ALA D CB  1 
ATOM   10501 N  N   . ASN D 1 215 ? -12.877 29.044  -11.424 1.00 34.46  ? 215  ASN D N   1 
ATOM   10502 C  CA  . ASN D 1 215 ? -12.549 27.620  -11.355 1.00 36.99  ? 215  ASN D CA  1 
ATOM   10503 C  C   . ASN D 1 215 ? -12.760 26.946  -12.684 1.00 32.17  ? 215  ASN D C   1 
ATOM   10504 O  O   . ASN D 1 215 ? -13.665 27.289  -13.425 1.00 37.64  ? 215  ASN D O   1 
ATOM   10505 C  CB  . ASN D 1 215 ? -13.218 26.872  -10.183 1.00 38.84  ? 215  ASN D CB  1 
ATOM   10506 C  CG  . ASN D 1 215 ? -14.704 26.674  -10.363 1.00 37.84  ? 215  ASN D CG  1 
ATOM   10507 O  OD1 . ASN D 1 215 ? -15.180 25.543  -10.539 1.00 39.08  ? 215  ASN D OD1 1 
ATOM   10508 N  ND2 . ASN D 1 215 ? -15.454 27.762  -10.268 1.00 35.41  ? 215  ASN D ND2 1 
ATOM   10509 N  N   . PHE D 1 216 ? -11.889 26.000  -12.983 1.00 26.39  ? 216  PHE D N   1 
ATOM   10510 C  CA  . PHE D 1 216 ? -11.755 25.495  -14.329 1.00 11.63  ? 216  PHE D CA  1 
ATOM   10511 C  C   . PHE D 1 216 ? -12.304 24.089  -14.451 1.00 31.17  ? 216  PHE D C   1 
ATOM   10512 O  O   . PHE D 1 216 ? -12.132 23.248  -13.564 1.00 27.78  ? 216  PHE D O   1 
ATOM   10513 C  CB  . PHE D 1 216 ? -10.285 25.556  -14.751 1.00 26.91  ? 216  PHE D CB  1 
ATOM   10514 C  CG  . PHE D 1 216 ? -9.708  26.938  -14.673 1.00 25.48  ? 216  PHE D CG  1 
ATOM   10515 C  CD1 . PHE D 1 216 ? -9.191  27.417  -13.486 1.00 29.80  ? 216  PHE D CD1 1 
ATOM   10516 C  CD2 . PHE D 1 216 ? -9.737  27.774  -15.776 1.00 25.53  ? 216  PHE D CD2 1 
ATOM   10517 C  CE1 . PHE D 1 216 ? -8.692  28.701  -13.398 1.00 26.07  ? 216  PHE D CE1 1 
ATOM   10518 C  CE2 . PHE D 1 216 ? -9.249  29.053  -15.697 1.00 32.26  ? 216  PHE D CE2 1 
ATOM   10519 C  CZ  . PHE D 1 216 ? -8.718  29.518  -14.503 1.00 30.61  ? 216  PHE D CZ  1 
ATOM   10520 N  N   . HIS D 1 217 ? -12.968 23.845  -15.571 1.00 32.13  ? 217  HIS D N   1 
ATOM   10521 C  CA  . HIS D 1 217 ? -13.611 22.575  -15.828 1.00 36.01  ? 217  HIS D CA  1 
ATOM   10522 C  C   . HIS D 1 217 ? -13.281 22.124  -17.240 1.00 37.08  ? 217  HIS D C   1 
ATOM   10523 O  O   . HIS D 1 217 ? -12.590 22.826  -17.977 1.00 35.04  ? 217  HIS D O   1 
ATOM   10524 C  CB  . HIS D 1 217 ? -15.130 22.711  -15.650 1.00 30.73  ? 217  HIS D CB  1 
ATOM   10525 C  CG  . HIS D 1 217 ? -15.546 22.979  -14.237 1.00 30.82  ? 217  HIS D CG  1 
ATOM   10526 N  ND1 . HIS D 1 217 ? -16.214 22.051  -13.469 1.00 33.42  ? 217  HIS D ND1 1 
ATOM   10527 C  CD2 . HIS D 1 217 ? -15.376 24.065  -13.446 1.00 35.16  ? 217  HIS D CD2 1 
ATOM   10528 C  CE1 . HIS D 1 217 ? -16.438 22.548  -12.268 1.00 34.46  ? 217  HIS D CE1 1 
ATOM   10529 N  NE2 . HIS D 1 217 ? -15.941 23.771  -12.227 1.00 32.59  ? 217  HIS D NE2 1 
ATOM   10530 N  N   . GLY D 1 218 ? -13.789 20.950  -17.607 1.00 39.70  ? 218  GLY D N   1 
ATOM   10531 C  CA  . GLY D 1 218 ? -13.562 20.378  -18.915 1.00 30.71  ? 218  GLY D CA  1 
ATOM   10532 C  C   . GLY D 1 218 ? -14.849 19.787  -19.446 1.00 30.23  ? 218  GLY D C   1 
ATOM   10533 O  O   . GLY D 1 218 ? -15.791 19.540  -18.692 1.00 31.96  ? 218  GLY D O   1 
ATOM   10534 N  N   . GLY D 1 219 ? -14.899 19.581  -20.758 1.00 29.58  ? 219  GLY D N   1 
ATOM   10535 C  CA  . GLY D 1 219 ? -16.074 19.028  -21.396 1.00 33.77  ? 219  GLY D CA  1 
ATOM   10536 C  C   . GLY D 1 219 ? -16.611 19.955  -22.461 1.00 49.83  ? 219  GLY D C   1 
ATOM   10537 O  O   . GLY D 1 219 ? -17.412 19.558  -23.306 1.00 64.12  ? 219  GLY D O   1 
ATOM   10538 N  N   . ALA D 1 220 ? -16.155 21.200  -22.433 1.00 45.74  ? 220  ALA D N   1 
ATOM   10539 C  CA  . ALA D 1 220 ? -16.670 22.213  -23.347 1.00 50.01  ? 220  ALA D CA  1 
ATOM   10540 C  C   . ALA D 1 220 ? -15.767 23.426  -23.278 1.00 47.34  ? 220  ALA D C   1 
ATOM   10541 O  O   . ALA D 1 220 ? -14.891 23.497  -22.417 1.00 49.00  ? 220  ALA D O   1 
ATOM   10542 C  CB  . ALA D 1 220 ? -18.090 22.593  -22.967 1.00 47.93  ? 220  ALA D CB  1 
ATOM   10543 N  N   . VAL D 1 221 ? -15.977 24.385  -24.170 1.00 40.60  ? 221  VAL D N   1 
ATOM   10544 C  CA  . VAL D 1 221 ? -15.111 25.551  -24.215 1.00 45.12  ? 221  VAL D CA  1 
ATOM   10545 C  C   . VAL D 1 221 ? -15.924 26.836  -24.146 1.00 47.70  ? 221  VAL D C   1 
ATOM   10546 O  O   . VAL D 1 221 ? -16.458 27.285  -25.160 1.00 48.39  ? 221  VAL D O   1 
ATOM   10547 C  CB  . VAL D 1 221 ? -14.259 25.533  -25.490 1.00 41.46  ? 221  VAL D CB  1 
ATOM   10548 C  CG1 . VAL D 1 221 ? -13.098 26.504  -25.364 1.00 37.23  ? 221  VAL D CG1 1 
ATOM   10549 C  CG2 . VAL D 1 221 ? -13.741 24.134  -25.728 1.00 34.37  ? 221  VAL D CG2 1 
ATOM   10550 N  N   . VAL D 1 222 ? -16.002 27.427  -22.953 1.00 42.46  ? 222  VAL D N   1 
ATOM   10551 C  CA  . VAL D 1 222 ? -16.879 28.576  -22.699 1.00 39.04  ? 222  VAL D CA  1 
ATOM   10552 C  C   . VAL D 1 222 ? -16.626 29.259  -21.333 1.00 49.85  ? 222  VAL D C   1 
ATOM   10553 O  O   . VAL D 1 222 ? -16.162 28.627  -20.369 1.00 50.53  ? 222  VAL D O   1 
ATOM   10554 C  CB  . VAL D 1 222 ? -18.352 28.136  -22.742 1.00 39.88  ? 222  VAL D CB  1 
ATOM   10555 C  CG1 . VAL D 1 222 ? -18.653 27.220  -21.559 1.00 35.72  ? 222  VAL D CG1 1 
ATOM   10556 C  CG2 . VAL D 1 222 ? -19.288 29.346  -22.740 1.00 44.01  ? 222  VAL D CG2 1 
ATOM   10557 N  N   . ALA D 1 223 ? -16.944 30.551  -21.257 1.00 41.30  ? 223  ALA D N   1 
ATOM   10558 C  CA  . ALA D 1 223 ? -16.838 31.304  -20.008 1.00 38.64  ? 223  ALA D CA  1 
ATOM   10559 C  C   . ALA D 1 223 ? -18.210 31.459  -19.349 1.00 43.13  ? 223  ALA D C   1 
ATOM   10560 O  O   . ALA D 1 223 ? -19.052 32.220  -19.838 1.00 44.15  ? 223  ALA D O   1 
ATOM   10561 C  CB  . ALA D 1 223 ? -16.210 32.679  -20.260 1.00 26.03  ? 223  ALA D CB  1 
ATOM   10562 N  N   . SER D 1 224 ? -18.414 30.759  -18.229 1.00 35.76  ? 224  SER D N   1 
ATOM   10563 C  CA  . SER D 1 224 ? -19.710 30.707  -17.524 1.00 26.03  ? 224  SER D CA  1 
ATOM   10564 C  C   . SER D 1 224 ? -19.699 31.511  -16.212 1.00 28.71  ? 224  SER D C   1 
ATOM   10565 O  O   . SER D 1 224 ? -18.715 31.497  -15.453 1.00 27.80  ? 224  SER D O   1 
ATOM   10566 C  CB  . SER D 1 224 ? -20.079 29.239  -17.246 1.00 30.89  ? 224  SER D CB  1 
ATOM   10567 O  OG  . SER D 1 224 ? -21.324 29.108  -16.600 1.00 48.35  ? 224  SER D OG  1 
ATOM   10568 N  N   . TYR D 1 225 ? -20.802 32.203  -15.948 1.00 28.63  ? 225  TYR D N   1 
ATOM   10569 C  CA  . TYR D 1 225 ? -20.920 33.104  -14.803 1.00 17.73  ? 225  TYR D CA  1 
ATOM   10570 C  C   . TYR D 1 225 ? -22.286 32.951  -14.128 1.00 25.52  ? 225  TYR D C   1 
ATOM   10571 O  O   . TYR D 1 225 ? -23.239 32.469  -14.741 1.00 32.72  ? 225  TYR D O   1 
ATOM   10572 C  CB  . TYR D 1 225 ? -20.736 34.554  -15.259 1.00 28.43  ? 225  TYR D CB  1 
ATOM   10573 C  CG  . TYR D 1 225 ? -21.672 34.968  -16.401 1.00 27.12  ? 225  TYR D CG  1 
ATOM   10574 C  CD1 . TYR D 1 225 ? -21.321 34.756  -17.734 1.00 31.28  ? 225  TYR D CD1 1 
ATOM   10575 C  CD2 . TYR D 1 225 ? -22.901 35.567  -16.145 1.00 33.27  ? 225  TYR D CD2 1 
ATOM   10576 C  CE1 . TYR D 1 225 ? -22.168 35.119  -18.770 1.00 39.03  ? 225  TYR D CE1 1 
ATOM   10577 C  CE2 . TYR D 1 225 ? -23.746 35.948  -17.179 1.00 45.02  ? 225  TYR D CE2 1 
ATOM   10578 C  CZ  . TYR D 1 225 ? -23.378 35.717  -18.488 1.00 47.78  ? 225  TYR D CZ  1 
ATOM   10579 O  OH  . TYR D 1 225 ? -24.226 36.088  -19.512 1.00 53.02  ? 225  TYR D OH  1 
ATOM   10580 N  N   . PRO D 1 226 ? -22.387 33.371  -12.860 1.00 23.17  ? 226  PRO D N   1 
ATOM   10581 C  CA  . PRO D 1 226 ? -23.610 33.284  -12.038 1.00 30.28  ? 226  PRO D CA  1 
ATOM   10582 C  C   . PRO D 1 226 ? -24.856 33.924  -12.665 1.00 36.00  ? 226  PRO D C   1 
ATOM   10583 O  O   . PRO D 1 226 ? -24.719 34.856  -13.470 1.00 41.01  ? 226  PRO D O   1 
ATOM   10584 C  CB  . PRO D 1 226 ? -23.227 34.044  -10.760 1.00 34.44  ? 226  PRO D CB  1 
ATOM   10585 C  CG  . PRO D 1 226 ? -21.728 33.929  -10.687 1.00 35.93  ? 226  PRO D CG  1 
ATOM   10586 C  CD  . PRO D 1 226 ? -21.228 33.871  -12.098 1.00 20.37  ? 226  PRO D CD  1 
ATOM   10587 N  N   . TYR D 1 227 ? -26.050 33.448  -12.300 1.00 27.65  ? 227  TYR D N   1 
ATOM   10588 C  CA  . TYR D 1 227 ? -26.213 32.337  -11.363 1.00 30.06  ? 227  TYR D CA  1 
ATOM   10589 C  C   . TYR D 1 227 ? -26.310 31.043  -12.136 1.00 33.29  ? 227  TYR D C   1 
ATOM   10590 O  O   . TYR D 1 227 ? -26.573 31.053  -13.342 1.00 30.94  ? 227  TYR D O   1 
ATOM   10591 C  CB  . TYR D 1 227 ? -27.506 32.465  -10.549 1.00 37.08  ? 227  TYR D CB  1 
ATOM   10592 C  CG  . TYR D 1 227 ? -27.541 33.570  -9.533  1.00 30.71  ? 227  TYR D CG  1 
ATOM   10593 C  CD1 . TYR D 1 227 ? -26.748 33.520  -8.388  1.00 30.31  ? 227  TYR D CD1 1 
ATOM   10594 C  CD2 . TYR D 1 227 ? -28.394 34.645  -9.696  1.00 32.71  ? 227  TYR D CD2 1 
ATOM   10595 C  CE1 . TYR D 1 227 ? -26.794 34.534  -7.436  1.00 27.05  ? 227  TYR D CE1 1 
ATOM   10596 C  CE2 . TYR D 1 227 ? -28.445 35.664  -8.761  1.00 39.68  ? 227  TYR D CE2 1 
ATOM   10597 C  CZ  . TYR D 1 227 ? -27.652 35.607  -7.635  1.00 40.56  ? 227  TYR D CZ  1 
ATOM   10598 O  OH  . TYR D 1 227 ? -27.728 36.643  -6.729  1.00 44.47  ? 227  TYR D OH  1 
ATOM   10599 N  N   . ASP D 1 228 ? -26.111 29.932  -11.430 1.00 31.35  ? 228  ASP D N   1 
ATOM   10600 C  CA  . ASP D 1 228 ? -26.221 28.593  -12.011 1.00 31.65  ? 228  ASP D CA  1 
ATOM   10601 C  C   . ASP D 1 228 ? -27.625 28.004  -11.787 1.00 34.79  ? 228  ASP D C   1 
ATOM   10602 O  O   . ASP D 1 228 ? -27.983 26.974  -12.361 1.00 35.54  ? 228  ASP D O   1 
ATOM   10603 C  CB  . ASP D 1 228 ? -25.165 27.639  -11.418 1.00 34.23  ? 228  ASP D CB  1 
ATOM   10604 C  CG  . ASP D 1 228 ? -23.778 27.814  -12.035 1.00 44.86  ? 228  ASP D CG  1 
ATOM   10605 O  OD1 . ASP D 1 228 ? -23.624 28.460  -13.098 1.00 47.35  ? 228  ASP D OD1 1 
ATOM   10606 O  OD2 . ASP D 1 228 ? -22.822 27.274  -11.447 1.00 56.29  ? 228  ASP D OD2 1 
ATOM   10607 N  N   . ASN D 1 229 ? -28.416 28.638  -10.932 1.00 31.21  ? 229  ASN D N   1 
ATOM   10608 C  CA  . ASN D 1 229 ? -29.785 28.186  -10.742 1.00 35.46  ? 229  ASN D CA  1 
ATOM   10609 C  C   . ASN D 1 229 ? -30.732 29.339  -10.465 1.00 44.80  ? 229  ASN D C   1 
ATOM   10610 O  O   . ASN D 1 229 ? -30.341 30.507  -10.557 1.00 30.10  ? 229  ASN D O   1 
ATOM   10611 C  CB  . ASN D 1 229 ? -29.895 27.104  -9.659  1.00 41.32  ? 229  ASN D CB  1 
ATOM   10612 C  CG  . ASN D 1 229 ? -29.450 27.583  -8.278  1.00 42.74  ? 229  ASN D CG  1 
ATOM   10613 O  OD1 . ASN D 1 229 ? -29.179 28.772  -8.055  1.00 39.75  ? 229  ASN D OD1 1 
ATOM   10614 N  ND2 . ASN D 1 229 ? -29.369 26.645  -7.342  1.00 27.82  ? 229  ASN D ND2 1 
ATOM   10615 N  N   . SER D 1 230 ? -31.979 29.001  -10.138 1.00 48.40  ? 230  SER D N   1 
ATOM   10616 C  CA  . SER D 1 230 ? -33.005 30.006  -9.883  1.00 32.44  ? 230  SER D CA  1 
ATOM   10617 C  C   . SER D 1 230 ? -34.174 29.437  -9.085  1.00 35.24  ? 230  SER D C   1 
ATOM   10618 O  O   . SER D 1 230 ? -34.280 28.227  -8.899  1.00 37.41  ? 230  SER D O   1 
ATOM   10619 C  CB  . SER D 1 230 ? -33.520 30.544  -11.206 1.00 29.30  ? 230  SER D CB  1 
ATOM   10620 O  OG  . SER D 1 230 ? -34.278 29.559  -11.873 1.00 39.81  ? 230  SER D OG  1 
ATOM   10621 N  N   . LEU D 1 231 ? -35.068 30.305  -8.624  1.00 41.15  ? 231  LEU D N   1 
ATOM   10622 C  CA  . LEU D 1 231 ? -36.225 29.827  -7.874  1.00 48.16  ? 231  LEU D CA  1 
ATOM   10623 C  C   . LEU D 1 231 ? -37.178 29.052  -8.782  1.00 58.19  ? 231  LEU D C   1 
ATOM   10624 O  O   . LEU D 1 231 ? -37.879 28.138  -8.337  1.00 60.72  ? 231  LEU D O   1 
ATOM   10625 C  CB  . LEU D 1 231 ? -36.960 30.984  -7.200  1.00 51.44  ? 231  LEU D CB  1 
ATOM   10626 C  CG  . LEU D 1 231 ? -36.531 31.428  -5.799  1.00 45.59  ? 231  LEU D CG  1 
ATOM   10627 C  CD1 . LEU D 1 231 ? -37.189 32.763  -5.426  1.00 47.66  ? 231  LEU D CD1 1 
ATOM   10628 C  CD2 . LEU D 1 231 ? -36.867 30.367  -4.772  1.00 50.49  ? 231  LEU D CD2 1 
ATOM   10629 N  N   . ALA D 1 232 ? -37.201 29.420  -10.058 1.00 49.77  ? 232  ALA D N   1 
ATOM   10630 C  CA  . ALA D 1 232 ? -38.030 28.718  -11.024 1.00 44.80  ? 232  ALA D CA  1 
ATOM   10631 C  C   . ALA D 1 232 ? -37.527 27.286  -11.249 1.00 50.76  ? 232  ALA D C   1 
ATOM   10632 O  O   . ALA D 1 232 ? -38.269 26.431  -11.719 1.00 52.99  ? 232  ALA D O   1 
ATOM   10633 C  CB  . ALA D 1 232 ? -38.082 29.487  -12.333 1.00 26.68  ? 232  ALA D CB  1 
ATOM   10634 N  N   . HIS D 1 233 ? -36.266 27.034  -10.909 1.00 53.16  ? 233  HIS D N   1 
ATOM   10635 C  CA  . HIS D 1 233 ? -35.632 25.728  -11.131 1.00 49.43  ? 233  HIS D CA  1 
ATOM   10636 C  C   . HIS D 1 233 ? -35.857 25.168  -12.546 1.00 56.06  ? 233  HIS D C   1 
ATOM   10637 O  O   . HIS D 1 233 ? -36.327 24.048  -12.724 1.00 61.81  ? 233  HIS D O   1 
ATOM   10638 C  CB  . HIS D 1 233 ? -36.057 24.717  -10.057 1.00 35.76  ? 233  HIS D CB  1 
ATOM   10639 C  CG  . HIS D 1 233 ? -35.475 24.992  -8.699  1.00 47.83  ? 233  HIS D CG  1 
ATOM   10640 N  ND1 . HIS D 1 233 ? -36.222 25.489  -7.651  1.00 56.59  ? 233  HIS D ND1 1 
ATOM   10641 C  CD2 . HIS D 1 233 ? -34.215 24.848  -8.224  1.00 49.43  ? 233  HIS D CD2 1 
ATOM   10642 C  CE1 . HIS D 1 233 ? -35.448 25.633  -6.588  1.00 53.40  ? 233  HIS D CE1 1 
ATOM   10643 N  NE2 . HIS D 1 233 ? -34.226 25.251  -6.909  1.00 52.41  ? 233  HIS D NE2 1 
ATOM   10644 N  N   . ASN D 1 234 ? -35.504 25.954  -13.553 1.00 59.46  ? 234  ASN D N   1 
ATOM   10645 C  CA  . ASN D 1 234 ? -35.649 25.526  -14.937 1.00 58.82  ? 234  ASN D CA  1 
ATOM   10646 C  C   . ASN D 1 234 ? -34.489 24.636  -15.358 1.00 47.02  ? 234  ASN D C   1 
ATOM   10647 O  O   . ASN D 1 234 ? -33.361 24.839  -14.928 1.00 49.03  ? 234  ASN D O   1 
ATOM   10648 C  CB  . ASN D 1 234 ? -35.766 26.750  -15.847 1.00 51.31  ? 234  ASN D CB  1 
ATOM   10649 C  CG  . ASN D 1 234 ? -36.824 27.724  -15.354 1.00 52.01  ? 234  ASN D CG  1 
ATOM   10650 O  OD1 . ASN D 1 234 ? -37.840 27.307  -14.795 1.00 52.52  ? 234  ASN D OD1 1 
ATOM   10651 N  ND2 . ASN D 1 234 ? -36.586 29.020  -15.536 1.00 49.73  ? 234  ASN D ND2 1 
ATOM   10652 N  N   . GLU D 1 235 ? -34.776 23.639  -16.183 1.00 52.68  ? 235  GLU D N   1 
ATOM   10653 C  CA  . GLU D 1 235 ? -33.756 22.715  -16.657 1.00 50.79  ? 235  GLU D CA  1 
ATOM   10654 C  C   . GLU D 1 235 ? -32.650 23.485  -17.356 1.00 59.79  ? 235  GLU D C   1 
ATOM   10655 O  O   . GLU D 1 235 ? -31.466 23.267  -17.091 1.00 56.03  ? 235  GLU D O   1 
ATOM   10656 C  CB  . GLU D 1 235 ? -34.357 21.676  -17.618 1.00 56.37  ? 235  GLU D CB  1 
ATOM   10657 C  CG  . GLU D 1 235 ? -33.332 20.684  -18.171 1.00 70.03  ? 235  GLU D CG  1 
ATOM   10658 C  CD  . GLU D 1 235 ? -33.891 19.775  -19.247 1.00 77.47  ? 235  GLU D CD  1 
ATOM   10659 O  OE1 . GLU D 1 235 ? -33.398 18.636  -19.391 1.00 87.20  ? 235  GLU D OE1 1 
ATOM   10660 O  OE2 . GLU D 1 235 ? -34.823 20.201  -19.951 1.00 73.14  ? 235  GLU D OE2 1 
ATOM   10661 N  N   . CYS D 1 236 ? -33.035 24.404  -18.237 1.00 58.55  ? 236  CYS D N   1 
ATOM   10662 C  CA  . CYS D 1 236 ? -32.050 25.102  -19.046 1.00 60.56  ? 236  CYS D CA  1 
ATOM   10663 C  C   . CYS D 1 236 ? -32.610 26.316  -19.775 1.00 51.47  ? 236  CYS D C   1 
ATOM   10664 O  O   . CYS D 1 236 ? -33.762 26.690  -19.604 1.00 60.35  ? 236  CYS D O   1 
ATOM   10665 C  CB  . CYS D 1 236 ? -31.492 24.142  -20.094 1.00 67.25  ? 236  CYS D CB  1 
ATOM   10666 S  SG  . CYS D 1 236 ? -32.531 24.028  -21.592 1.00 70.28  ? 236  CYS D SG  1 
ATOM   10667 N  N   . CYS D 1 237 ? -31.756 26.917  -20.592 1.00 49.69  ? 237  CYS D N   1 
ATOM   10668 C  CA  . CYS D 1 237 ? -32.148 27.875  -21.619 1.00 45.06  ? 237  CYS D CA  1 
ATOM   10669 C  C   . CYS D 1 237 ? -32.864 29.106  -21.096 1.00 44.43  ? 237  CYS D C   1 
ATOM   10670 O  O   . CYS D 1 237 ? -33.541 29.802  -21.859 1.00 38.30  ? 237  CYS D O   1 
ATOM   10671 C  CB  . CYS D 1 237 ? -32.988 27.180  -22.682 1.00 42.57  ? 237  CYS D CB  1 
ATOM   10672 S  SG  . CYS D 1 237 ? -32.405 25.505  -22.991 1.00 55.43  ? 237  CYS D SG  1 
ATOM   10673 N  N   . GLU D 1 238 ? -32.688 29.382  -19.806 1.00 40.87  ? 238  GLU D N   1 
ATOM   10674 C  CA  . GLU D 1 238 ? -33.295 30.552  -19.185 1.00 39.92  ? 238  GLU D CA  1 
ATOM   10675 C  C   . GLU D 1 238 ? -32.333 31.266  -18.237 1.00 46.04  ? 238  GLU D C   1 
ATOM   10676 O  O   . GLU D 1 238 ? -31.966 30.726  -17.192 1.00 53.54  ? 238  GLU D O   1 
ATOM   10677 C  CB  . GLU D 1 238 ? -34.567 30.149  -18.443 1.00 51.54  ? 238  GLU D CB  1 
ATOM   10678 C  CG  . GLU D 1 238 ? -35.809 30.856  -18.926 1.00 70.84  ? 238  GLU D CG  1 
ATOM   10679 C  CD  . GLU D 1 238 ? -37.062 30.051  -18.663 1.00 81.58  ? 238  GLU D CD  1 
ATOM   10680 O  OE1 . GLU D 1 238 ? -38.147 30.663  -18.586 1.00 91.93  ? 238  GLU D OE1 1 
ATOM   10681 O  OE2 . GLU D 1 238 ? -36.960 28.809  -18.536 1.00 75.84  ? 238  GLU D OE2 1 
ATOM   10682 N  N   . GLU D 1 239 ? -31.938 32.485  -18.601 1.00 58.20  ? 239  GLU D N   1 
ATOM   10683 C  CA  . GLU D 1 239 ? -30.995 33.277  -17.801 1.00 55.59  ? 239  GLU D CA  1 
ATOM   10684 C  C   . GLU D 1 239 ? -31.429 33.525  -16.344 1.00 47.52  ? 239  GLU D C   1 
ATOM   10685 O  O   . GLU D 1 239 ? -32.482 34.099  -16.091 1.00 49.60  ? 239  GLU D O   1 
ATOM   10686 C  CB  . GLU D 1 239 ? -30.718 34.620  -18.476 1.00 59.94  ? 239  GLU D CB  1 
ATOM   10687 C  CG  . GLU D 1 239 ? -29.798 34.551  -19.679 1.00 73.91  ? 239  GLU D CG  1 
ATOM   10688 C  CD  . GLU D 1 239 ? -29.534 35.928  -20.278 1.00 89.82  ? 239  GLU D CD  1 
ATOM   10689 O  OE1 . GLU D 1 239 ? -28.430 36.143  -20.830 1.00 89.12  ? 239  GLU D OE1 1 
ATOM   10690 O  OE2 . GLU D 1 239 ? -30.429 36.800  -20.188 1.00 93.03  ? 239  GLU D OE2 1 
ATOM   10691 N  N   . SER D 1 240 ? -30.604 33.095  -15.392 1.00 37.11  ? 240  SER D N   1 
ATOM   10692 C  CA  . SER D 1 240 ? -30.798 33.464  -13.996 1.00 26.88  ? 240  SER D CA  1 
ATOM   10693 C  C   . SER D 1 240 ? -29.722 34.468  -13.588 1.00 41.62  ? 240  SER D C   1 
ATOM   10694 O  O   . SER D 1 240 ? -28.723 34.119  -12.947 1.00 40.40  ? 240  SER D O   1 
ATOM   10695 C  CB  . SER D 1 240 ? -30.749 32.235  -13.095 1.00 31.90  ? 240  SER D CB  1 
ATOM   10696 O  OG  . SER D 1 240 ? -31.059 32.578  -11.751 1.00 38.61  ? 240  SER D OG  1 
ATOM   10697 N  N   . LEU D 1 241 ? -29.933 35.725  -13.958 1.00 50.96  ? 241  LEU D N   1 
ATOM   10698 C  CA  . LEU D 1 241 ? -28.865 36.721  -13.895 1.00 39.71  ? 241  LEU D CA  1 
ATOM   10699 C  C   . LEU D 1 241 ? -28.585 37.277  -12.492 1.00 32.73  ? 241  LEU D C   1 
ATOM   10700 O  O   . LEU D 1 241 ? -29.415 37.202  -11.591 1.00 27.85  ? 241  LEU D O   1 
ATOM   10701 C  CB  . LEU D 1 241 ? -29.128 37.835  -14.927 1.00 32.57  ? 241  LEU D CB  1 
ATOM   10702 C  CG  . LEU D 1 241 ? -29.150 37.369  -16.398 1.00 38.64  ? 241  LEU D CG  1 
ATOM   10703 C  CD1 . LEU D 1 241 ? -29.416 38.510  -17.405 1.00 30.36  ? 241  LEU D CD1 1 
ATOM   10704 C  CD2 . LEU D 1 241 ? -27.855 36.616  -16.773 1.00 24.83  ? 241  LEU D CD2 1 
ATOM   10705 N  N   . THR D 1 242 ? -27.394 37.836  -12.335 1.00 54.40  ? 242  THR D N   1 
ATOM   10706 C  CA  . THR D 1 242 ? -26.905 38.340  -11.060 1.00 42.82  ? 242  THR D CA  1 
ATOM   10707 C  C   . THR D 1 242 ? -27.023 39.870  -11.037 1.00 48.30  ? 242  THR D C   1 
ATOM   10708 O  O   . THR D 1 242 ? -27.028 40.501  -12.102 1.00 45.63  ? 242  THR D O   1 
ATOM   10709 C  CB  . THR D 1 242 ? -25.433 37.923  -10.892 1.00 37.41  ? 242  THR D CB  1 
ATOM   10710 O  OG1 . THR D 1 242 ? -25.347 36.758  -10.060 1.00 33.49  ? 242  THR D OG1 1 
ATOM   10711 C  CG2 . THR D 1 242 ? -24.624 39.031  -10.292 1.00 32.09  ? 242  THR D CG2 1 
ATOM   10712 N  N   . PRO D 1 243 ? -27.132 40.474  -9.833  1.00 46.61  ? 243  PRO D N   1 
ATOM   10713 C  CA  . PRO D 1 243 ? -27.185 41.944  -9.746  1.00 35.37  ? 243  PRO D CA  1 
ATOM   10714 C  C   . PRO D 1 243 ? -25.962 42.565  -10.407 1.00 35.71  ? 243  PRO D C   1 
ATOM   10715 O  O   . PRO D 1 243 ? -26.036 43.679  -10.928 1.00 31.77  ? 243  PRO D O   1 
ATOM   10716 C  CB  . PRO D 1 243 ? -27.147 42.218  -8.239  1.00 26.77  ? 243  PRO D CB  1 
ATOM   10717 C  CG  . PRO D 1 243 ? -27.664 40.981  -7.605  1.00 38.42  ? 243  PRO D CG  1 
ATOM   10718 C  CD  . PRO D 1 243 ? -27.251 39.834  -8.508  1.00 47.75  ? 243  PRO D CD  1 
ATOM   10719 N  N   . ASP D 1 244 ? -24.846 41.838  -10.378 1.00 34.72  ? 244  ASP D N   1 
ATOM   10720 C  CA  . ASP D 1 244 ? -23.612 42.288  -11.018 1.00 37.50  ? 244  ASP D CA  1 
ATOM   10721 C  C   . ASP D 1 244 ? -23.400 41.661  -12.411 1.00 44.04  ? 244  ASP D C   1 
ATOM   10722 O  O   . ASP D 1 244 ? -22.262 41.350  -12.788 1.00 53.13  ? 244  ASP D O   1 
ATOM   10723 C  CB  . ASP D 1 244 ? -22.408 41.984  -10.120 1.00 41.24  ? 244  ASP D CB  1 
ATOM   10724 C  CG  . ASP D 1 244 ? -22.185 43.043  -9.032  1.00 51.78  ? 244  ASP D CG  1 
ATOM   10725 O  OD1 . ASP D 1 244 ? -21.604 44.113  -9.330  1.00 59.05  ? 244  ASP D OD1 1 
ATOM   10726 O  OD2 . ASP D 1 244 ? -22.564 42.791  -7.869  1.00 51.07  ? 244  ASP D OD2 1 
ATOM   10727 N  N   . ASP D 1 245 ? -24.475 41.487  -13.181 1.00 32.95  ? 245  ASP D N   1 
ATOM   10728 C  CA  . ASP D 1 245 ? -24.350 40.859  -14.496 1.00 39.22  ? 245  ASP D CA  1 
ATOM   10729 C  C   . ASP D 1 245 ? -23.427 41.585  -15.461 1.00 41.97  ? 245  ASP D C   1 
ATOM   10730 O  O   . ASP D 1 245 ? -22.698 40.950  -16.222 1.00 48.36  ? 245  ASP D O   1 
ATOM   10731 C  CB  . ASP D 1 245 ? -25.696 40.672  -15.173 1.00 36.80  ? 245  ASP D CB  1 
ATOM   10732 C  CG  . ASP D 1 245 ? -25.650 39.576  -16.216 1.00 52.85  ? 245  ASP D CG  1 
ATOM   10733 O  OD1 . ASP D 1 245 ? -25.136 38.473  -15.894 1.00 60.25  ? 245  ASP D OD1 1 
ATOM   10734 O  OD2 . ASP D 1 245 ? -26.111 39.814  -17.349 1.00 59.74  ? 245  ASP D OD2 1 
ATOM   10735 N  N   . ARG D 1 246 ? -23.474 42.910  -15.453 1.00 33.48  ? 246  ARG D N   1 
ATOM   10736 C  CA  . ARG D 1 246 ? -22.561 43.677  -16.285 1.00 38.66  ? 246  ARG D CA  1 
ATOM   10737 C  C   . ARG D 1 246 ? -21.127 43.223  -16.065 1.00 40.79  ? 246  ARG D C   1 
ATOM   10738 O  O   . ARG D 1 246 ? -20.458 42.753  -16.988 1.00 45.99  ? 246  ARG D O   1 
ATOM   10739 C  CB  . ARG D 1 246 ? -22.698 45.161  -15.972 1.00 42.23  ? 246  ARG D CB  1 
ATOM   10740 C  CG  . ARG D 1 246 ? -24.120 45.670  -16.181 1.00 51.96  ? 246  ARG D CG  1 
ATOM   10741 C  CD  . ARG D 1 246 ? -24.288 47.100  -15.704 1.00 62.84  ? 246  ARG D CD  1 
ATOM   10742 N  NE  . ARG D 1 246 ? -24.169 48.071  -16.786 1.00 77.70  ? 246  ARG D NE  1 
ATOM   10743 C  CZ  . ARG D 1 246 ? -24.124 49.386  -16.598 1.00 91.75  ? 246  ARG D CZ  1 
ATOM   10744 N  NH1 . ARG D 1 246 ? -24.176 49.881  -15.370 1.00 92.93  ? 246  ARG D NH1 1 
ATOM   10745 N  NH2 . ARG D 1 246 ? -24.023 50.208  -17.634 1.00 103.93 ? 246  ARG D NH2 1 
ATOM   10746 N  N   . VAL D 1 247 ? -20.659 43.351  -14.832 1.00 30.03  ? 247  VAL D N   1 
ATOM   10747 C  CA  . VAL D 1 247 ? -19.285 43.010  -14.524 1.00 33.34  ? 247  VAL D CA  1 
ATOM   10748 C  C   . VAL D 1 247 ? -18.996 41.547  -14.801 1.00 26.54  ? 247  VAL D C   1 
ATOM   10749 O  O   . VAL D 1 247 ? -17.939 41.216  -15.321 1.00 36.17  ? 247  VAL D O   1 
ATOM   10750 C  CB  . VAL D 1 247 ? -18.939 43.333  -13.071 1.00 45.47  ? 247  VAL D CB  1 
ATOM   10751 C  CG1 . VAL D 1 247 ? -17.699 42.555  -12.632 1.00 33.56  ? 247  VAL D CG1 1 
ATOM   10752 C  CG2 . VAL D 1 247 ? -18.736 44.835  -12.910 1.00 37.44  ? 247  VAL D CG2 1 
ATOM   10753 N  N   . PHE D 1 248 ? -19.925 40.663  -14.466 1.00 32.50  ? 248  PHE D N   1 
ATOM   10754 C  CA  . PHE D 1 248 ? -19.704 39.243  -14.756 1.00 33.96  ? 248  PHE D CA  1 
ATOM   10755 C  C   . PHE D 1 248 ? -19.528 39.009  -16.246 1.00 32.23  ? 248  PHE D C   1 
ATOM   10756 O  O   . PHE D 1 248 ? -18.675 38.237  -16.662 1.00 35.56  ? 248  PHE D O   1 
ATOM   10757 C  CB  . PHE D 1 248 ? -20.829 38.357  -14.212 1.00 28.04  ? 248  PHE D CB  1 
ATOM   10758 C  CG  . PHE D 1 248 ? -20.556 37.836  -12.839 1.00 34.51  ? 248  PHE D CG  1 
ATOM   10759 C  CD1 . PHE D 1 248 ? -19.545 36.917  -12.630 1.00 37.22  ? 248  PHE D CD1 1 
ATOM   10760 C  CD2 . PHE D 1 248 ? -21.284 38.291  -11.750 1.00 27.79  ? 248  PHE D CD2 1 
ATOM   10761 C  CE1 . PHE D 1 248 ? -19.272 36.453  -11.358 1.00 40.43  ? 248  PHE D CE1 1 
ATOM   10762 C  CE2 . PHE D 1 248 ? -21.015 37.831  -10.478 1.00 27.55  ? 248  PHE D CE2 1 
ATOM   10763 C  CZ  . PHE D 1 248 ? -20.014 36.910  -10.279 1.00 19.13  ? 248  PHE D CZ  1 
ATOM   10764 N  N   . LYS D 1 249 ? -20.340 39.686  -17.047 1.00 29.68  ? 249  LYS D N   1 
ATOM   10765 C  CA  . LYS D 1 249 ? -20.227 39.598  -18.493 1.00 31.82  ? 249  LYS D CA  1 
ATOM   10766 C  C   . LYS D 1 249 ? -18.868 40.124  -18.981 1.00 39.32  ? 249  LYS D C   1 
ATOM   10767 O  O   . LYS D 1 249 ? -18.223 39.510  -19.841 1.00 41.52  ? 249  LYS D O   1 
ATOM   10768 C  CB  . LYS D 1 249 ? -21.409 40.300  -19.176 1.00 35.84  ? 249  LYS D CB  1 
ATOM   10769 C  CG  . LYS D 1 249 ? -22.610 39.378  -19.381 1.00 35.13  ? 249  LYS D CG  1 
ATOM   10770 C  CD  . LYS D 1 249 ? -23.834 40.088  -19.948 1.00 27.23  ? 249  LYS D CD  1 
ATOM   10771 C  CE  . LYS D 1 249 ? -24.904 39.069  -20.319 1.00 32.37  ? 249  LYS D CE  1 
ATOM   10772 N  NZ  . LYS D 1 249 ? -26.258 39.661  -20.373 1.00 40.15  ? 249  LYS D NZ  1 
ATOM   10773 N  N   . GLN D 1 250 ? -18.414 41.241  -18.422 1.00 29.77  ? 250  GLN D N   1 
ATOM   10774 C  CA  . GLN D 1 250 ? -17.087 41.731  -18.763 1.00 32.25  ? 250  GLN D CA  1 
ATOM   10775 C  C   . GLN D 1 250 ? -15.999 40.707  -18.433 1.00 33.92  ? 250  GLN D C   1 
ATOM   10776 O  O   . GLN D 1 250 ? -15.102 40.470  -19.246 1.00 33.91  ? 250  GLN D O   1 
ATOM   10777 C  CB  . GLN D 1 250 ? -16.800 43.046  -18.059 1.00 35.36  ? 250  GLN D CB  1 
ATOM   10778 C  CG  . GLN D 1 250 ? -15.454 43.643  -18.422 1.00 34.02  ? 250  GLN D CG  1 
ATOM   10779 C  CD  . GLN D 1 250 ? -15.403 45.137  -18.136 1.00 53.83  ? 250  GLN D CD  1 
ATOM   10780 O  OE1 . GLN D 1 250 ? -16.359 45.869  -18.411 1.00 61.81  ? 250  GLN D OE1 1 
ATOM   10781 N  NE2 . GLN D 1 250 ? -14.285 45.596  -17.583 1.00 57.98  ? 250  GLN D NE2 1 
ATOM   10782 N  N   . LEU D 1 251 ? -16.073 40.106  -17.244 1.00 25.46  ? 251  LEU D N   1 
ATOM   10783 C  CA  . LEU D 1 251 ? -15.091 39.095  -16.832 1.00 30.37  ? 251  LEU D CA  1 
ATOM   10784 C  C   . LEU D 1 251 ? -15.046 37.909  -17.798 1.00 37.15  ? 251  LEU D C   1 
ATOM   10785 O  O   . LEU D 1 251 ? -13.987 37.567  -18.341 1.00 39.02  ? 251  LEU D O   1 
ATOM   10786 C  CB  . LEU D 1 251 ? -15.383 38.597  -15.414 1.00 36.63  ? 251  LEU D CB  1 
ATOM   10787 C  CG  . LEU D 1 251 ? -15.310 39.654  -14.301 1.00 44.44  ? 251  LEU D CG  1 
ATOM   10788 C  CD1 . LEU D 1 251 ? -15.784 39.122  -12.937 1.00 38.78  ? 251  LEU D CD1 1 
ATOM   10789 C  CD2 . LEU D 1 251 ? -13.921 40.283  -14.206 1.00 25.92  ? 251  LEU D CD2 1 
ATOM   10790 N  N   . ALA D 1 252 ? -16.206 37.292  -18.011 1.00 39.87  ? 252  ALA D N   1 
ATOM   10791 C  CA  . ALA D 1 252 ? -16.327 36.168  -18.924 1.00 41.43  ? 252  ALA D CA  1 
ATOM   10792 C  C   . ALA D 1 252 ? -15.792 36.537  -20.303 1.00 48.88  ? 252  ALA D C   1 
ATOM   10793 O  O   . ALA D 1 252 ? -15.083 35.753  -20.937 1.00 52.85  ? 252  ALA D O   1 
ATOM   10794 C  CB  . ALA D 1 252 ? -17.773 35.713  -19.013 1.00 34.18  ? 252  ALA D CB  1 
ATOM   10795 N  N   . HIS D 1 253 ? -16.126 37.733  -20.769 1.00 41.59  ? 253  HIS D N   1 
ATOM   10796 C  CA  . HIS D 1 253 ? -15.629 38.179  -22.065 1.00 36.02  ? 253  HIS D CA  1 
ATOM   10797 C  C   . HIS D 1 253 ? -14.129 38.360  -22.047 1.00 35.51  ? 253  HIS D C   1 
ATOM   10798 O  O   . HIS D 1 253 ? -13.451 38.074  -23.032 1.00 37.15  ? 253  HIS D O   1 
ATOM   10799 C  CB  . HIS D 1 253 ? -16.286 39.487  -22.495 1.00 32.87  ? 253  HIS D CB  1 
ATOM   10800 C  CG  . HIS D 1 253 ? -17.476 39.290  -23.372 1.00 42.06  ? 253  HIS D CG  1 
ATOM   10801 N  ND1 . HIS D 1 253 ? -18.747 39.668  -22.997 1.00 43.74  ? 253  HIS D ND1 1 
ATOM   10802 C  CD2 . HIS D 1 253 ? -17.597 38.719  -24.595 1.00 48.57  ? 253  HIS D CD2 1 
ATOM   10803 C  CE1 . HIS D 1 253 ? -19.599 39.359  -23.959 1.00 49.45  ? 253  HIS D CE1 1 
ATOM   10804 N  NE2 . HIS D 1 253 ? -18.927 38.782  -24.940 1.00 60.76  ? 253  HIS D NE2 1 
ATOM   10805 N  N   . THR D 1 254 ? -13.609 38.847  -20.927 1.00 28.56  ? 254  THR D N   1 
ATOM   10806 C  CA  . THR D 1 254 ? -12.188 39.121  -20.856 1.00 35.19  ? 254  THR D CA  1 
ATOM   10807 C  C   . THR D 1 254 ? -11.430 37.834  -21.147 1.00 30.38  ? 254  THR D C   1 
ATOM   10808 O  O   . THR D 1 254 ? -10.401 37.826  -21.840 1.00 38.00  ? 254  THR D O   1 
ATOM   10809 C  CB  . THR D 1 254 ? -11.776 39.664  -19.486 1.00 41.42  ? 254  THR D CB  1 
ATOM   10810 O  OG1 . THR D 1 254 ? -12.521 40.855  -19.190 1.00 35.50  ? 254  THR D OG1 1 
ATOM   10811 C  CG2 . THR D 1 254 ? -10.291 39.983  -19.492 1.00 30.77  ? 254  THR D CG2 1 
ATOM   10812 N  N   . TYR D 1 255 ? -11.958 36.734  -20.637 1.00 23.61  ? 255  TYR D N   1 
ATOM   10813 C  CA  . TYR D 1 255 ? -11.292 35.462  -20.841 1.00 33.94  ? 255  TYR D CA  1 
ATOM   10814 C  C   . TYR D 1 255 ? -11.516 34.941  -22.246 1.00 25.78  ? 255  TYR D C   1 
ATOM   10815 O  O   . TYR D 1 255 ? -10.564 34.582  -22.933 1.00 35.93  ? 255  TYR D O   1 
ATOM   10816 C  CB  . TYR D 1 255 ? -11.757 34.420  -19.820 1.00 34.37  ? 255  TYR D CB  1 
ATOM   10817 C  CG  . TYR D 1 255 ? -10.812 33.250  -19.731 1.00 33.44  ? 255  TYR D CG  1 
ATOM   10818 C  CD1 . TYR D 1 255 ? -10.810 32.263  -20.702 1.00 43.98  ? 255  TYR D CD1 1 
ATOM   10819 C  CD2 . TYR D 1 255 ? -9.904  33.147  -18.688 1.00 27.24  ? 255  TYR D CD2 1 
ATOM   10820 C  CE1 . TYR D 1 255 ? -9.940  31.190  -20.628 1.00 48.53  ? 255  TYR D CE1 1 
ATOM   10821 C  CE2 . TYR D 1 255 ? -9.031  32.083  -18.601 1.00 36.84  ? 255  TYR D CE2 1 
ATOM   10822 C  CZ  . TYR D 1 255 ? -9.050  31.106  -19.573 1.00 41.33  ? 255  TYR D CZ  1 
ATOM   10823 O  OH  . TYR D 1 255 ? -8.172  30.047  -19.484 1.00 40.90  ? 255  TYR D OH  1 
ATOM   10824 N  N   . SER D 1 256 ? -12.780 34.897  -22.657 1.00 27.96  ? 256  SER D N   1 
ATOM   10825 C  CA  . SER D 1 256 ? -13.152 34.338  -23.946 1.00 38.16  ? 256  SER D CA  1 
ATOM   10826 C  C   . SER D 1 256 ? -12.554 35.147  -25.112 1.00 48.92  ? 256  SER D C   1 
ATOM   10827 O  O   . SER D 1 256 ? -11.952 34.578  -26.028 1.00 40.61  ? 256  SER D O   1 
ATOM   10828 C  CB  . SER D 1 256 ? -14.674 34.260  -24.059 1.00 36.69  ? 256  SER D CB  1 
ATOM   10829 O  OG  . SER D 1 256 ? -15.059 33.625  -25.264 1.00 50.57  ? 256  SER D OG  1 
ATOM   10830 N  N   . ASP D 1 257 ? -12.722 36.470  -25.069 1.00 46.79  ? 257  ASP D N   1 
ATOM   10831 C  CA  . ASP D 1 257 ? -12.157 37.367  -26.083 1.00 36.04  ? 257  ASP D CA  1 
ATOM   10832 C  C   . ASP D 1 257 ? -10.655 37.141  -26.262 1.00 43.61  ? 257  ASP D C   1 
ATOM   10833 O  O   . ASP D 1 257 ? -10.116 37.312  -27.349 1.00 47.48  ? 257  ASP D O   1 
ATOM   10834 C  CB  . ASP D 1 257 ? -12.389 38.833  -25.705 1.00 41.86  ? 257  ASP D CB  1 
ATOM   10835 C  CG  . ASP D 1 257 ? -13.849 39.247  -25.788 1.00 59.89  ? 257  ASP D CG  1 
ATOM   10836 O  OD1 . ASP D 1 257 ? -14.690 38.434  -26.239 1.00 61.94  ? 257  ASP D OD1 1 
ATOM   10837 O  OD2 . ASP D 1 257 ? -14.150 40.400  -25.402 1.00 68.22  ? 257  ASP D OD2 1 
ATOM   10838 N  N   . ASN D 1 258 ? -9.978  36.771  -25.179 1.00 50.07  ? 258  ASN D N   1 
ATOM   10839 C  CA  . ASN D 1 258 ? -8.540  36.538  -25.226 1.00 47.29  ? 258  ASN D CA  1 
ATOM   10840 C  C   . ASN D 1 258 ? -8.174  35.099  -25.566 1.00 45.65  ? 258  ASN D C   1 
ATOM   10841 O  O   . ASN D 1 258 ? -6.997  34.730  -25.553 1.00 44.00  ? 258  ASN D O   1 
ATOM   10842 C  CB  . ASN D 1 258 ? -7.897  36.956  -23.903 1.00 39.89  ? 258  ASN D CB  1 
ATOM   10843 C  CG  . ASN D 1 258 ? -7.635  38.444  -23.840 1.00 51.03  ? 258  ASN D CG  1 
ATOM   10844 O  OD1 . ASN D 1 258 ? -6.632  38.939  -24.387 1.00 49.42  ? 258  ASN D OD1 1 
ATOM   10845 N  ND2 . ASN D 1 258 ? -8.554  39.179  -23.206 1.00 33.85  ? 258  ASN D ND2 1 
ATOM   10846 N  N   . HIS D 1 259 ? -9.191  34.295  -25.873 1.00 54.05  ? 259  HIS D N   1 
ATOM   10847 C  CA  . HIS D 1 259 ? -9.011  32.867  -26.139 1.00 54.30  ? 259  HIS D CA  1 
ATOM   10848 C  C   . HIS D 1 259 ? -9.447  32.535  -27.574 1.00 51.92  ? 259  HIS D C   1 
ATOM   10849 O  O   . HIS D 1 259 ? -10.640 32.479  -27.881 1.00 41.30  ? 259  HIS D O   1 
ATOM   10850 C  CB  . HIS D 1 259 ? -9.795  32.044  -25.113 1.00 49.82  ? 259  HIS D CB  1 
ATOM   10851 C  CG  . HIS D 1 259 ? -9.495  30.576  -25.145 1.00 50.10  ? 259  HIS D CG  1 
ATOM   10852 N  ND1 . HIS D 1 259 ? -9.761  29.783  -26.241 1.00 44.89  ? 259  HIS D ND1 1 
ATOM   10853 C  CD2 . HIS D 1 259 ? -8.988  29.750  -24.199 1.00 46.04  ? 259  HIS D CD2 1 
ATOM   10854 C  CE1 . HIS D 1 259 ? -9.409  28.538  -25.978 1.00 36.03  ? 259  HIS D CE1 1 
ATOM   10855 N  NE2 . HIS D 1 259 ? -8.945  28.488  -24.743 1.00 36.74  ? 259  HIS D NE2 1 
ATOM   10856 N  N   . PRO D 1 260 ? -8.461  32.306  -28.454 1.00 60.03  ? 260  PRO D N   1 
ATOM   10857 C  CA  . PRO D 1 260 ? -8.618  32.193  -29.911 1.00 60.51  ? 260  PRO D CA  1 
ATOM   10858 C  C   . PRO D 1 260 ? -9.725  31.248  -30.339 1.00 50.59  ? 260  PRO D C   1 
ATOM   10859 O  O   . PRO D 1 260 ? -10.263 31.409  -31.437 1.00 47.12  ? 260  PRO D O   1 
ATOM   10860 C  CB  . PRO D 1 260 ? -7.269  31.626  -30.363 1.00 58.51  ? 260  PRO D CB  1 
ATOM   10861 C  CG  . PRO D 1 260 ? -6.317  32.058  -29.327 1.00 65.59  ? 260  PRO D CG  1 
ATOM   10862 C  CD  . PRO D 1 260 ? -7.072  32.059  -28.030 1.00 52.48  ? 260  PRO D CD  1 
ATOM   10863 N  N   . ILE D 1 261 ? -10.048 30.278  -29.490 1.00 46.96  ? 261  ILE D N   1 
ATOM   10864 C  CA  . ILE D 1 261 ? -11.008 29.243  -29.842 1.00 55.50  ? 261  ILE D CA  1 
ATOM   10865 C  C   . ILE D 1 261 ? -12.331 29.462  -29.128 1.00 49.53  ? 261  ILE D C   1 
ATOM   10866 O  O   . ILE D 1 261 ? -13.406 29.363  -29.746 1.00 53.28  ? 261  ILE D O   1 
ATOM   10867 C  CB  . ILE D 1 261 ? -10.467 27.839  -29.516 1.00 54.07  ? 261  ILE D CB  1 
ATOM   10868 C  CG1 . ILE D 1 261 ? -9.364  27.456  -30.498 1.00 47.68  ? 261  ILE D CG1 1 
ATOM   10869 C  CG2 . ILE D 1 261 ? -11.570 26.808  -29.582 1.00 48.38  ? 261  ILE D CG2 1 
ATOM   10870 C  CD1 . ILE D 1 261 ? -8.689  26.143  -30.148 1.00 59.72  ? 261  ILE D CD1 1 
ATOM   10871 N  N   . MET D 1 262 ? -12.251 29.772  -27.836 1.00 27.76  ? 262  MET D N   1 
ATOM   10872 C  CA  . MET D 1 262 ? -13.445 30.057  -27.043 1.00 44.27  ? 262  MET D CA  1 
ATOM   10873 C  C   . MET D 1 262 ? -14.252 31.208  -27.647 1.00 53.83  ? 262  MET D C   1 
ATOM   10874 O  O   . MET D 1 262 ? -15.487 31.148  -27.733 1.00 49.85  ? 262  MET D O   1 
ATOM   10875 C  CB  . MET D 1 262 ? -13.058 30.399  -25.606 1.00 35.39  ? 262  MET D CB  1 
ATOM   10876 C  CG  . MET D 1 262 ? -14.233 30.586  -24.688 1.00 20.72  ? 262  MET D CG  1 
ATOM   10877 S  SD  . MET D 1 262 ? -13.667 30.682  -22.984 1.00 38.87  ? 262  MET D SD  1 
ATOM   10878 C  CE  . MET D 1 262 ? -12.773 29.145  -22.842 1.00 24.78  ? 262  MET D CE  1 
ATOM   10879 N  N   . ARG D 1 263 ? -13.526 32.248  -28.057 1.00 56.34  ? 263  ARG D N   1 
ATOM   10880 C  CA  . ARG D 1 263 ? -14.074 33.445  -28.699 1.00 54.28  ? 263  ARG D CA  1 
ATOM   10881 C  C   . ARG D 1 263 ? -15.055 33.145  -29.834 1.00 53.09  ? 263  ARG D C   1 
ATOM   10882 O  O   . ARG D 1 263 ? -15.844 34.004  -30.228 1.00 56.68  ? 263  ARG D O   1 
ATOM   10883 C  CB  . ARG D 1 263 ? -12.910 34.285  -29.239 1.00 56.64  ? 263  ARG D CB  1 
ATOM   10884 C  CG  . ARG D 1 263 ? -13.290 35.601  -29.887 1.00 71.90  ? 263  ARG D CG  1 
ATOM   10885 C  CD  . ARG D 1 263 ? -12.027 36.398  -30.227 1.00 85.16  ? 263  ARG D CD  1 
ATOM   10886 N  NE  . ARG D 1 263 ? -11.147 35.695  -31.165 1.00 82.98  ? 263  ARG D NE  1 
ATOM   10887 C  CZ  . ARG D 1 263 ? -9.822  35.624  -31.046 1.00 72.38  ? 263  ARG D CZ  1 
ATOM   10888 N  NH1 . ARG D 1 263 ? -9.196  36.204  -30.025 1.00 57.47  ? 263  ARG D NH1 1 
ATOM   10889 N  NH2 . ARG D 1 263 ? -9.120  34.964  -31.953 1.00 67.04  ? 263  ARG D NH2 1 
ATOM   10890 N  N   . LYS D 1 264 ? -15.002 31.924  -30.355 1.00 59.96  ? 264  LYS D N   1 
ATOM   10891 C  CA  . LYS D 1 264 ? -15.778 31.563  -31.531 1.00 64.71  ? 264  LYS D CA  1 
ATOM   10892 C  C   . LYS D 1 264 ? -17.230 31.216  -31.197 1.00 62.40  ? 264  LYS D C   1 
ATOM   10893 O  O   . LYS D 1 264 ? -18.162 31.694  -31.849 1.00 65.63  ? 264  LYS D O   1 
ATOM   10894 C  CB  . LYS D 1 264 ? -15.089 30.420  -32.272 1.00 62.97  ? 264  LYS D CB  1 
ATOM   10895 C  CG  . LYS D 1 264 ? -13.685 30.768  -32.714 1.00 60.05  ? 264  LYS D CG  1 
ATOM   10896 C  CD  . LYS D 1 264 ? -13.090 29.670  -33.564 1.00 72.15  ? 264  LYS D CD  1 
ATOM   10897 C  CE  . LYS D 1 264 ? -11.776 30.113  -34.163 1.00 78.29  ? 264  LYS D CE  1 
ATOM   10898 N  NZ  . LYS D 1 264 ? -11.957 31.342  -34.985 1.00 95.58  ? 264  LYS D NZ  1 
ATOM   10899 N  N   . GLY D 1 265 ? -17.422 30.386  -30.180 1.00 63.45  ? 265  GLY D N   1 
ATOM   10900 C  CA  . GLY D 1 265 ? -18.756 30.113  -29.678 1.00 47.00  ? 265  GLY D CA  1 
ATOM   10901 C  C   . GLY D 1 265 ? -19.402 28.863  -30.226 1.00 48.38  ? 265  GLY D C   1 
ATOM   10902 O  O   . GLY D 1 265 ? -20.534 28.564  -29.872 1.00 59.85  ? 265  GLY D O   1 
ATOM   10903 N  N   . ASN D 1 266 ? -18.697 28.126  -31.078 1.00 44.99  ? 266  ASN D N   1 
ATOM   10904 C  CA  . ASN D 1 266 ? -19.267 26.929  -31.692 1.00 49.37  ? 266  ASN D CA  1 
ATOM   10905 C  C   . ASN D 1 266 ? -18.447 25.658  -31.458 1.00 56.07  ? 266  ASN D C   1 
ATOM   10906 O  O   . ASN D 1 266 ? -18.307 24.829  -32.359 1.00 63.07  ? 266  ASN D O   1 
ATOM   10907 C  CB  . ASN D 1 266 ? -19.454 27.157  -33.188 1.00 50.22  ? 266  ASN D CB  1 
ATOM   10908 C  CG  . ASN D 1 266 ? -18.194 27.669  -33.857 1.00 72.64  ? 266  ASN D CG  1 
ATOM   10909 O  OD1 . ASN D 1 266 ? -17.142 27.759  -33.221 1.00 78.03  ? 266  ASN D OD1 1 
ATOM   10910 N  ND2 . ASN D 1 266 ? -18.290 28.009  -35.144 1.00 70.59  ? 266  ASN D ND2 1 
ATOM   10911 N  N   . ASN D 1 267 ? -17.925 25.497  -30.245 1.00 42.53  ? 267  ASN D N   1 
ATOM   10912 C  CA  . ASN D 1 267 ? -17.041 24.378  -29.942 1.00 40.65  ? 267  ASN D CA  1 
ATOM   10913 C  C   . ASN D 1 267 ? -17.795 23.209  -29.333 1.00 44.22  ? 267  ASN D C   1 
ATOM   10914 O  O   . ASN D 1 267 ? -18.894 23.383  -28.820 1.00 40.34  ? 267  ASN D O   1 
ATOM   10915 C  CB  . ASN D 1 267 ? -15.933 24.833  -29.001 1.00 44.91  ? 267  ASN D CB  1 
ATOM   10916 C  CG  . ASN D 1 267 ? -15.402 26.199  -29.363 1.00 50.53  ? 267  ASN D CG  1 
ATOM   10917 O  OD1 . ASN D 1 267 ? -14.848 26.387  -30.442 1.00 48.73  ? 267  ASN D OD1 1 
ATOM   10918 N  ND2 . ASN D 1 267 ? -15.579 27.167  -28.466 1.00 47.42  ? 267  ASN D ND2 1 
ATOM   10919 N  N   . CYS D 1 268 ? -17.194 22.023  -29.402 1.00 52.22  ? 268  CYS D N   1 
ATOM   10920 C  CA  . CYS D 1 268 ? -17.761 20.782  -28.862 1.00 52.60  ? 268  CYS D CA  1 
ATOM   10921 C  C   . CYS D 1 268 ? -19.257 20.586  -29.122 1.00 63.78  ? 268  CYS D C   1 
ATOM   10922 O  O   . CYS D 1 268 ? -19.971 20.064  -28.263 1.00 58.16  ? 268  CYS D O   1 
ATOM   10923 C  CB  . CYS D 1 268 ? -17.479 20.669  -27.365 1.00 42.30  ? 268  CYS D CB  1 
ATOM   10924 S  SG  . CYS D 1 268 ? -16.297 21.878  -26.723 1.00 74.83  ? 268  CYS D SG  1 
ATOM   10925 N  N   . ASN D 1 269 ? -19.720 20.981  -30.307 1.00 70.10  ? 269  ASN D N   1 
ATOM   10926 C  CA  . ASN D 1 269 ? -21.140 20.893  -30.647 1.00 70.29  ? 269  ASN D CA  1 
ATOM   10927 C  C   . ASN D 1 269 ? -22.006 21.900  -29.875 1.00 67.35  ? 269  ASN D C   1 
ATOM   10928 O  O   . ASN D 1 269 ? -23.237 21.878  -29.978 1.00 58.18  ? 269  ASN D O   1 
ATOM   10929 C  CB  . ASN D 1 269 ? -21.669 19.468  -30.432 1.00 73.48  ? 269  ASN D CB  1 
ATOM   10930 C  CG  . ASN D 1 269 ? -21.126 18.479  -31.447 1.00 78.76  ? 269  ASN D CG  1 
ATOM   10931 O  OD1 . ASN D 1 269 ? -21.084 17.267  -31.205 1.00 77.09  ? 269  ASN D OD1 1 
ATOM   10932 N  ND2 . ASN D 1 269 ? -20.707 18.993  -32.594 1.00 82.50  ? 269  ASN D ND2 1 
ATOM   10933 N  N   . ASP D 1 270 ? -21.364 22.778  -29.104 1.00 62.22  ? 270  ASP D N   1 
ATOM   10934 C  CA  . ASP D 1 270 ? -22.084 23.790  -28.327 1.00 59.58  ? 270  ASP D CA  1 
ATOM   10935 C  C   . ASP D 1 270 ? -22.222 25.097  -29.114 1.00 65.33  ? 270  ASP D C   1 
ATOM   10936 O  O   . ASP D 1 270 ? -21.384 25.404  -29.970 1.00 63.00  ? 270  ASP D O   1 
ATOM   10937 C  CB  . ASP D 1 270 ? -21.375 24.071  -26.989 1.00 56.45  ? 270  ASP D CB  1 
ATOM   10938 C  CG  . ASP D 1 270 ? -21.261 22.837  -26.097 1.00 54.50  ? 270  ASP D CG  1 
ATOM   10939 O  OD1 . ASP D 1 270 ? -22.059 21.892  -26.236 1.00 60.55  ? 270  ASP D OD1 1 
ATOM   10940 O  OD2 . ASP D 1 270 ? -20.363 22.818  -25.240 1.00 51.57  ? 270  ASP D OD2 1 
ATOM   10941 N  N   . SER D 1 271 ? -23.279 25.858  -28.824 1.00 62.39  ? 271  SER D N   1 
ATOM   10942 C  CA  . SER D 1 271 ? -23.431 27.202  -29.383 1.00 58.53  ? 271  SER D CA  1 
ATOM   10943 C  C   . SER D 1 271 ? -23.521 28.267  -28.281 1.00 57.12  ? 271  SER D C   1 
ATOM   10944 O  O   . SER D 1 271 ? -24.580 28.455  -27.685 1.00 66.35  ? 271  SER D O   1 
ATOM   10945 C  CB  . SER D 1 271 ? -24.647 27.278  -30.312 1.00 49.19  ? 271  SER D CB  1 
ATOM   10946 O  OG  . SER D 1 271 ? -24.749 28.562  -30.919 1.00 47.28  ? 271  SER D OG  1 
ATOM   10947 N  N   . PHE D 1 272 ? -22.403 28.951  -28.021 1.00 51.40  ? 272  PHE D N   1 
ATOM   10948 C  CA  . PHE D 1 272 ? -22.308 29.980  -26.977 1.00 41.33  ? 272  PHE D CA  1 
ATOM   10949 C  C   . PHE D 1 272 ? -21.867 31.318  -27.562 1.00 38.80  ? 272  PHE D C   1 
ATOM   10950 O  O   . PHE D 1 272 ? -20.676 31.524  -27.816 1.00 47.89  ? 272  PHE D O   1 
ATOM   10951 C  CB  . PHE D 1 272 ? -21.293 29.573  -25.892 1.00 39.78  ? 272  PHE D CB  1 
ATOM   10952 C  CG  . PHE D 1 272 ? -21.727 28.407  -25.042 1.00 46.69  ? 272  PHE D CG  1 
ATOM   10953 C  CD1 . PHE D 1 272 ? -20.994 27.220  -25.038 1.00 44.39  ? 272  PHE D CD1 1 
ATOM   10954 C  CD2 . PHE D 1 272 ? -22.860 28.501  -24.235 1.00 39.81  ? 272  PHE D CD2 1 
ATOM   10955 C  CE1 . PHE D 1 272 ? -21.388 26.138  -24.248 1.00 34.74  ? 272  PHE D CE1 1 
ATOM   10956 C  CE2 . PHE D 1 272 ? -23.273 27.431  -23.441 1.00 31.56  ? 272  PHE D CE2 1 
ATOM   10957 C  CZ  . PHE D 1 272 ? -22.539 26.247  -23.443 1.00 30.67  ? 272  PHE D CZ  1 
ATOM   10958 N  N   . SER D 1 273 ? -22.818 32.225  -27.760 1.00 45.13  ? 273  SER D N   1 
ATOM   10959 C  CA  . SER D 1 273 ? -22.529 33.551  -28.309 1.00 57.85  ? 273  SER D CA  1 
ATOM   10960 C  C   . SER D 1 273 ? -21.369 34.247  -27.576 1.00 59.23  ? 273  SER D C   1 
ATOM   10961 O  O   . SER D 1 273 ? -21.392 34.396  -26.351 1.00 52.13  ? 273  SER D O   1 
ATOM   10962 C  CB  . SER D 1 273 ? -23.794 34.421  -28.297 1.00 58.48  ? 273  SER D CB  1 
ATOM   10963 O  OG  . SER D 1 273 ? -23.543 35.726  -28.784 1.00 59.44  ? 273  SER D OG  1 
ATOM   10964 N  N   . GLY D 1 274 ? -20.352 34.649  -28.338 1.00 58.21  ? 274  GLY D N   1 
ATOM   10965 C  CA  . GLY D 1 274 ? -19.179 35.297  -27.781 1.00 50.09  ? 274  GLY D CA  1 
ATOM   10966 C  C   . GLY D 1 274 ? -18.323 34.363  -26.942 1.00 59.60  ? 274  GLY D C   1 
ATOM   10967 O  O   . GLY D 1 274 ? -17.321 34.790  -26.350 1.00 56.34  ? 274  GLY D O   1 
ATOM   10968 N  N   . GLY D 1 275 ? -18.717 33.088  -26.890 1.00 53.34  ? 275  GLY D N   1 
ATOM   10969 C  CA  . GLY D 1 275 ? -17.970 32.075  -26.163 1.00 40.48  ? 275  GLY D CA  1 
ATOM   10970 C  C   . GLY D 1 275 ? -18.220 32.144  -24.673 1.00 44.78  ? 275  GLY D C   1 
ATOM   10971 O  O   . GLY D 1 275 ? -17.452 31.586  -23.887 1.00 45.29  ? 275  GLY D O   1 
ATOM   10972 N  N   . ILE D 1 276 ? -19.287 32.843  -24.279 1.00 45.88  ? 276  ILE D N   1 
ATOM   10973 C  CA  . ILE D 1 276 ? -19.671 32.898  -22.872 1.00 48.10  ? 276  ILE D CA  1 
ATOM   10974 C  C   . ILE D 1 276 ? -21.130 32.515  -22.694 1.00 38.24  ? 276  ILE D C   1 
ATOM   10975 O  O   . ILE D 1 276 ? -21.863 32.366  -23.659 1.00 36.49  ? 276  ILE D O   1 
ATOM   10976 C  CB  . ILE D 1 276 ? -19.464 34.287  -22.246 1.00 46.66  ? 276  ILE D CB  1 
ATOM   10977 C  CG1 . ILE D 1 276 ? -20.524 35.249  -22.760 1.00 38.38  ? 276  ILE D CG1 1 
ATOM   10978 C  CG2 . ILE D 1 276 ? -18.045 34.803  -22.504 1.00 49.91  ? 276  ILE D CG2 1 
ATOM   10979 C  CD1 . ILE D 1 276 ? -20.459 36.596  -22.101 1.00 36.42  ? 276  ILE D CD1 1 
ATOM   10980 N  N   . THR D 1 277 ? -21.543 32.351  -21.444 1.00 38.69  ? 277  THR D N   1 
ATOM   10981 C  CA  . THR D 1 277 ? -22.897 31.915  -21.150 1.00 47.08  ? 277  THR D CA  1 
ATOM   10982 C  C   . THR D 1 277 ? -23.181 32.061  -19.670 1.00 54.81  ? 277  THR D C   1 
ATOM   10983 O  O   . THR D 1 277 ? -22.260 32.083  -18.846 1.00 58.97  ? 277  THR D O   1 
ATOM   10984 C  CB  . THR D 1 277 ? -23.150 30.432  -21.570 1.00 43.75  ? 277  THR D CB  1 
ATOM   10985 O  OG1 . THR D 1 277 ? -24.537 30.104  -21.387 1.00 43.61  ? 277  THR D OG1 1 
ATOM   10986 C  CG2 . THR D 1 277 ? -22.287 29.467  -20.747 1.00 33.19  ? 277  THR D CG2 1 
ATOM   10987 N  N   . ASN D 1 278 ? -24.466 32.175  -19.349 1.00 57.05  ? 278  ASN D N   1 
ATOM   10988 C  CA  . ASN D 1 278 ? -24.950 32.145  -17.976 1.00 38.19  ? 278  ASN D CA  1 
ATOM   10989 C  C   . ASN D 1 278 ? -25.099 30.688  -17.547 1.00 44.62  ? 278  ASN D C   1 
ATOM   10990 O  O   . ASN D 1 278 ? -25.618 29.862  -18.307 1.00 60.25  ? 278  ASN D O   1 
ATOM   10991 C  CB  . ASN D 1 278 ? -26.284 32.899  -17.890 1.00 26.32  ? 278  ASN D CB  1 
ATOM   10992 C  CG  . ASN D 1 278 ? -26.982 32.722  -16.556 1.00 39.00  ? 278  ASN D CG  1 
ATOM   10993 O  OD1 . ASN D 1 278 ? -28.153 32.345  -16.511 1.00 46.09  ? 278  ASN D OD1 1 
ATOM   10994 N  ND2 . ASN D 1 278 ? -26.274 33.002  -15.463 1.00 34.93  ? 278  ASN D ND2 1 
ATOM   10995 N  N   . GLY D 1 279 ? -24.616 30.361  -16.353 1.00 27.15  ? 279  GLY D N   1 
ATOM   10996 C  CA  . GLY D 1 279 ? -24.738 29.004  -15.852 1.00 25.23  ? 279  GLY D CA  1 
ATOM   10997 C  C   . GLY D 1 279 ? -26.120 28.422  -16.115 1.00 41.73  ? 279  GLY D C   1 
ATOM   10998 O  O   . GLY D 1 279 ? -26.252 27.434  -16.841 1.00 37.30  ? 279  GLY D O   1 
ATOM   10999 N  N   . ALA D 1 280 ? -27.150 29.052  -15.547 1.00 36.92  ? 280  ALA D N   1 
ATOM   11000 C  CA  . ALA D 1 280 ? -28.518 28.522  -15.622 1.00 32.60  ? 280  ALA D CA  1 
ATOM   11001 C  C   . ALA D 1 280 ? -28.981 28.388  -17.058 1.00 34.89  ? 280  ALA D C   1 
ATOM   11002 O  O   . ALA D 1 280 ? -29.525 27.362  -17.458 1.00 39.83  ? 280  ALA D O   1 
ATOM   11003 C  CB  . ALA D 1 280 ? -29.488 29.400  -14.833 1.00 29.26  ? 280  ALA D CB  1 
ATOM   11004 N  N   . HIS D 1 281 ? -28.767 29.434  -17.840 1.00 37.39  ? 281  HIS D N   1 
ATOM   11005 C  CA  . HIS D 1 281 ? -29.180 29.392  -19.226 1.00 31.08  ? 281  HIS D CA  1 
ATOM   11006 C  C   . HIS D 1 281 ? -28.612 28.156  -19.908 1.00 35.42  ? 281  HIS D C   1 
ATOM   11007 O  O   . HIS D 1 281 ? -29.316 27.484  -20.628 1.00 37.69  ? 281  HIS D O   1 
ATOM   11008 C  CB  . HIS D 1 281 ? -28.749 30.645  -19.970 1.00 37.60  ? 281  HIS D CB  1 
ATOM   11009 C  CG  . HIS D 1 281 ? -29.407 30.796  -21.303 1.00 51.86  ? 281  HIS D CG  1 
ATOM   11010 N  ND1 . HIS D 1 281 ? -28.782 30.460  -22.487 1.00 52.13  ? 281  HIS D ND1 1 
ATOM   11011 C  CD2 . HIS D 1 281 ? -30.646 31.231  -21.638 1.00 55.89  ? 281  HIS D CD2 1 
ATOM   11012 C  CE1 . HIS D 1 281 ? -29.604 30.694  -23.495 1.00 51.74  ? 281  HIS D CE1 1 
ATOM   11013 N  NE2 . HIS D 1 281 ? -30.743 31.158  -23.007 1.00 64.12  ? 281  HIS D NE2 1 
ATOM   11014 N  N   . TRP D 1 282 ? -27.337 27.856  -19.690 1.00 42.25  ? 282  TRP D N   1 
ATOM   11015 C  CA  . TRP D 1 282 ? -26.798 26.595  -20.181 1.00 39.78  ? 282  TRP D CA  1 
ATOM   11016 C  C   . TRP D 1 282 ? -27.680 25.470  -19.635 1.00 47.29  ? 282  TRP D C   1 
ATOM   11017 O  O   . TRP D 1 282 ? -28.502 24.899  -20.357 1.00 50.12  ? 282  TRP D O   1 
ATOM   11018 C  CB  . TRP D 1 282 ? -25.354 26.422  -19.727 1.00 37.71  ? 282  TRP D CB  1 
ATOM   11019 C  CG  . TRP D 1 282 ? -24.674 25.199  -20.292 1.00 53.56  ? 282  TRP D CG  1 
ATOM   11020 C  CD1 . TRP D 1 282 ? -25.202 24.277  -21.166 1.00 49.38  ? 282  TRP D CD1 1 
ATOM   11021 C  CD2 . TRP D 1 282 ? -23.338 24.768  -20.019 1.00 44.28  ? 282  TRP D CD2 1 
ATOM   11022 N  NE1 . TRP D 1 282 ? -24.271 23.302  -21.445 1.00 39.48  ? 282  TRP D NE1 1 
ATOM   11023 C  CE2 . TRP D 1 282 ? -23.120 23.585  -20.755 1.00 44.24  ? 282  TRP D CE2 1 
ATOM   11024 C  CE3 . TRP D 1 282 ? -22.299 25.276  -19.232 1.00 40.98  ? 282  TRP D CE3 1 
ATOM   11025 C  CZ2 . TRP D 1 282 ? -21.903 22.904  -20.723 1.00 38.74  ? 282  TRP D CZ2 1 
ATOM   11026 C  CZ3 . TRP D 1 282 ? -21.097 24.598  -19.205 1.00 35.66  ? 282  TRP D CZ3 1 
ATOM   11027 C  CH2 . TRP D 1 282 ? -20.909 23.424  -19.942 1.00 26.89  ? 282  TRP D CH2 1 
ATOM   11028 N  N   . TYR D 1 283 ? -27.499 25.158  -18.354 1.00 41.31  ? 283  TYR D N   1 
ATOM   11029 C  CA  . TYR D 1 283 ? -28.420 24.290  -17.619 1.00 45.28  ? 283  TYR D CA  1 
ATOM   11030 C  C   . TYR D 1 283 ? -28.266 24.593  -16.143 1.00 49.98  ? 283  TYR D C   1 
ATOM   11031 O  O   . TYR D 1 283 ? -27.182 24.978  -15.697 1.00 45.20  ? 283  TYR D O   1 
ATOM   11032 C  CB  . TYR D 1 283 ? -28.176 22.794  -17.900 1.00 42.13  ? 283  TYR D CB  1 
ATOM   11033 C  CG  . TYR D 1 283 ? -26.754 22.306  -17.665 1.00 47.56  ? 283  TYR D CG  1 
ATOM   11034 C  CD1 . TYR D 1 283 ? -26.335 21.889  -16.407 1.00 45.08  ? 283  TYR D CD1 1 
ATOM   11035 C  CD2 . TYR D 1 283 ? -25.837 22.242  -18.713 1.00 49.51  ? 283  TYR D CD2 1 
ATOM   11036 C  CE1 . TYR D 1 283 ? -25.038 21.445  -16.202 1.00 39.87  ? 283  TYR D CE1 1 
ATOM   11037 C  CE2 . TYR D 1 283 ? -24.548 21.802  -18.514 1.00 39.82  ? 283  TYR D CE2 1 
ATOM   11038 C  CZ  . TYR D 1 283 ? -24.159 21.403  -17.265 1.00 45.59  ? 283  TYR D CZ  1 
ATOM   11039 O  OH  . TYR D 1 283 ? -22.880 20.959  -17.087 1.00 56.60  ? 283  TYR D OH  1 
ATOM   11040 N  N   . GLU D 1 284 ? -29.347 24.441  -15.383 1.00 51.66  ? 284  GLU D N   1 
ATOM   11041 C  CA  . GLU D 1 284 ? -29.297 24.769  -13.960 1.00 51.33  ? 284  GLU D CA  1 
ATOM   11042 C  C   . GLU D 1 284 ? -28.681 23.654  -13.099 1.00 44.72  ? 284  GLU D C   1 
ATOM   11043 O  O   . GLU D 1 284 ? -28.870 22.460  -13.356 1.00 47.98  ? 284  GLU D O   1 
ATOM   11044 C  CB  . GLU D 1 284 ? -30.686 25.160  -13.438 1.00 46.09  ? 284  GLU D CB  1 
ATOM   11045 C  CG  . GLU D 1 284 ? -31.170 26.530  -13.892 1.00 43.50  ? 284  GLU D CG  1 
ATOM   11046 C  CD  . GLU D 1 284 ? -32.391 26.998  -13.110 1.00 46.28  ? 284  GLU D CD  1 
ATOM   11047 O  OE1 . GLU D 1 284 ? -33.120 27.884  -13.600 1.00 31.66  ? 284  GLU D OE1 1 
ATOM   11048 O  OE2 . GLU D 1 284 ? -32.624 26.479  -11.996 1.00 58.45  ? 284  GLU D OE2 1 
ATOM   11049 N  N   . LEU D 1 285 ? -27.942 24.057  -12.074 1.00 27.03  ? 285  LEU D N   1 
ATOM   11050 C  CA  . LEU D 1 285 ? -27.398 23.109  -11.111 1.00 39.05  ? 285  LEU D CA  1 
ATOM   11051 C  C   . LEU D 1 285 ? -27.352 23.788  -9.759  1.00 44.21  ? 285  LEU D C   1 
ATOM   11052 O  O   . LEU D 1 285 ? -27.280 25.015  -9.673  1.00 46.15  ? 285  LEU D O   1 
ATOM   11053 C  CB  . LEU D 1 285 ? -25.998 22.625  -11.517 1.00 36.15  ? 285  LEU D CB  1 
ATOM   11054 C  CG  . LEU D 1 285 ? -24.877 23.662  -11.493 1.00 36.69  ? 285  LEU D CG  1 
ATOM   11055 C  CD1 . LEU D 1 285 ? -24.174 23.650  -10.148 1.00 25.99  ? 285  LEU D CD1 1 
ATOM   11056 C  CD2 . LEU D 1 285 ? -23.904 23.404  -12.642 1.00 28.57  ? 285  LEU D CD2 1 
ATOM   11057 N  N   . SER D 1 286 ? -27.397 22.991  -8.700  1.00 47.38  ? 286  SER D N   1 
ATOM   11058 C  CA  . SER D 1 286 ? -27.408 23.552  -7.364  1.00 45.35  ? 286  SER D CA  1 
ATOM   11059 C  C   . SER D 1 286 ? -26.266 23.001  -6.510  1.00 43.95  ? 286  SER D C   1 
ATOM   11060 O  O   . SER D 1 286 ? -25.789 21.886  -6.729  1.00 51.83  ? 286  SER D O   1 
ATOM   11061 C  CB  . SER D 1 286 ? -28.772 23.319  -6.725  1.00 41.49  ? 286  SER D CB  1 
ATOM   11062 O  OG  . SER D 1 286 ? -29.785 23.896  -7.537  1.00 43.05  ? 286  SER D OG  1 
ATOM   11063 N  N   . GLY D 1 287 ? -25.802 23.803  -5.559  1.00 35.72  ? 287  GLY D N   1 
ATOM   11064 C  CA  . GLY D 1 287 ? -24.689 23.400  -4.719  1.00 24.66  ? 287  GLY D CA  1 
ATOM   11065 C  C   . GLY D 1 287 ? -23.322 23.695  -5.312  1.00 30.61  ? 287  GLY D C   1 
ATOM   11066 O  O   . GLY D 1 287 ? -22.306 23.207  -4.805  1.00 34.60  ? 287  GLY D O   1 
ATOM   11067 N  N   . GLY D 1 288 ? -23.284 24.502  -6.373  1.00 30.99  ? 288  GLY D N   1 
ATOM   11068 C  CA  . GLY D 1 288 ? -22.031 24.839  -7.026  1.00 35.68  ? 288  GLY D CA  1 
ATOM   11069 C  C   . GLY D 1 288 ? -21.149 25.781  -6.222  1.00 34.95  ? 288  GLY D C   1 
ATOM   11070 O  O   . GLY D 1 288 ? -21.634 26.550  -5.394  1.00 22.02  ? 288  GLY D O   1 
ATOM   11071 N  N   . MET D 1 289 ? -19.846 25.727  -6.482  1.00 35.05  ? 289  MET D N   1 
ATOM   11072 C  CA  . MET D 1 289 ? -18.895 26.583  -5.787  1.00 28.96  ? 289  MET D CA  1 
ATOM   11073 C  C   . MET D 1 289 ? -19.016 28.010  -6.297  1.00 34.23  ? 289  MET D C   1 
ATOM   11074 O  O   . MET D 1 289 ? -18.890 28.971  -5.528  1.00 35.78  ? 289  MET D O   1 
ATOM   11075 C  CB  . MET D 1 289 ? -17.470 26.065  -5.987  1.00 19.42  ? 289  MET D CB  1 
ATOM   11076 C  CG  . MET D 1 289 ? -16.378 26.827  -5.208  1.00 28.39  ? 289  MET D CG  1 
ATOM   11077 S  SD  . MET D 1 289 ? -14.733 26.056  -5.325  1.00 40.07  ? 289  MET D SD  1 
ATOM   11078 C  CE  . MET D 1 289 ? -14.586 25.889  -7.097  1.00 28.93  ? 289  MET D CE  1 
ATOM   11079 N  N   . GLN D 1 290 ? -19.271 28.145  -7.597  1.00 23.48  ? 290  GLN D N   1 
ATOM   11080 C  CA  . GLN D 1 290 ? -19.322 29.465  -8.220  1.00 32.20  ? 290  GLN D CA  1 
ATOM   11081 C  C   . GLN D 1 290 ? -20.282 30.379  -7.469  1.00 33.19  ? 290  GLN D C   1 
ATOM   11082 O  O   . GLN D 1 290 ? -19.894 31.412  -6.916  1.00 31.05  ? 290  GLN D O   1 
ATOM   11083 C  CB  . GLN D 1 290 ? -19.759 29.348  -9.683  1.00 38.00  ? 290  GLN D CB  1 
ATOM   11084 C  CG  . GLN D 1 290 ? -19.642 30.625  -10.516 1.00 18.60  ? 290  GLN D CG  1 
ATOM   11085 C  CD  . GLN D 1 290 ? -20.538 30.594  -11.747 1.00 24.58  ? 290  GLN D CD  1 
ATOM   11086 O  OE1 . GLN D 1 290 ? -20.062 30.493  -12.872 1.00 42.77  ? 290  GLN D OE1 1 
ATOM   11087 N  NE2 . GLN D 1 290 ? -21.844 30.673  -11.533 1.00 14.53  ? 290  GLN D NE2 1 
ATOM   11088 N  N   . ASP D 1 291 ? -21.548 29.990  -7.449  1.00 37.03  ? 291  ASP D N   1 
ATOM   11089 C  CA  . ASP D 1 291 ? -22.565 30.837  -6.847  1.00 36.82  ? 291  ASP D CA  1 
ATOM   11090 C  C   . ASP D 1 291 ? -22.340 30.963  -5.347  1.00 36.36  ? 291  ASP D C   1 
ATOM   11091 O  O   . ASP D 1 291 ? -22.835 31.902  -4.708  1.00 40.70  ? 291  ASP D O   1 
ATOM   11092 C  CB  . ASP D 1 291 ? -23.972 30.323  -7.174  1.00 43.29  ? 291  ASP D CB  1 
ATOM   11093 C  CG  . ASP D 1 291 ? -24.347 30.533  -8.644  1.00 52.14  ? 291  ASP D CG  1 
ATOM   11094 O  OD1 . ASP D 1 291 ? -23.528 31.107  -9.398  1.00 52.69  ? 291  ASP D OD1 1 
ATOM   11095 O  OD2 . ASP D 1 291 ? -25.461 30.130  -9.043  1.00 50.66  ? 291  ASP D OD2 1 
ATOM   11096 N  N   . PHE D 1 292 ? -21.568 30.035  -4.789  1.00 33.79  ? 292  PHE D N   1 
ATOM   11097 C  CA  . PHE D 1 292 ? -21.321 30.061  -3.355  1.00 19.32  ? 292  PHE D CA  1 
ATOM   11098 C  C   . PHE D 1 292 ? -20.463 31.257  -3.004  1.00 14.39  ? 292  PHE D C   1 
ATOM   11099 O  O   . PHE D 1 292 ? -20.746 31.970  -2.052  1.00 31.53  ? 292  PHE D O   1 
ATOM   11100 C  CB  . PHE D 1 292 ? -20.668 28.775  -2.873  1.00 13.08  ? 292  PHE D CB  1 
ATOM   11101 C  CG  . PHE D 1 292 ? -20.196 28.850  -1.452  1.00 18.02  ? 292  PHE D CG  1 
ATOM   11102 C  CD1 . PHE D 1 292 ? -21.082 28.659  -0.402  1.00 25.33  ? 292  PHE D CD1 1 
ATOM   11103 C  CD2 . PHE D 1 292 ? -18.881 29.136  -1.165  1.00 14.87  ? 292  PHE D CD2 1 
ATOM   11104 C  CE1 . PHE D 1 292 ? -20.671 28.749  0.906   1.00 25.59  ? 292  PHE D CE1 1 
ATOM   11105 C  CE2 . PHE D 1 292 ? -18.456 29.229  0.140   1.00 33.33  ? 292  PHE D CE2 1 
ATOM   11106 C  CZ  . PHE D 1 292 ? -19.352 29.032  1.182   1.00 36.82  ? 292  PHE D CZ  1 
ATOM   11107 N  N   . ASN D 1 293 ? -19.414 31.469  -3.784  1.00 21.84  ? 293  ASN D N   1 
ATOM   11108 C  CA  . ASN D 1 293 ? -18.569 32.649  -3.636  1.00 31.36  ? 293  ASN D CA  1 
ATOM   11109 C  C   . ASN D 1 293 ? -19.370 33.947  -3.647  1.00 28.77  ? 293  ASN D C   1 
ATOM   11110 O  O   . ASN D 1 293 ? -19.201 34.797  -2.781  1.00 36.17  ? 293  ASN D O   1 
ATOM   11111 C  CB  . ASN D 1 293 ? -17.527 32.702  -4.753  1.00 29.59  ? 293  ASN D CB  1 
ATOM   11112 C  CG  . ASN D 1 293 ? -16.300 31.869  -4.448  1.00 27.18  ? 293  ASN D CG  1 
ATOM   11113 O  OD1 . ASN D 1 293 ? -15.311 32.394  -3.949  1.00 26.86  ? 293  ASN D OD1 1 
ATOM   11114 N  ND2 . ASN D 1 293 ? -16.346 30.573  -4.759  1.00 26.26  ? 293  ASN D ND2 1 
ATOM   11115 N  N   . TYR D 1 294 ? -20.244 34.099  -4.630  1.00 20.80  ? 294  TYR D N   1 
ATOM   11116 C  CA  . TYR D 1 294 ? -20.964 35.356  -4.806  1.00 41.94  ? 294  TYR D CA  1 
ATOM   11117 C  C   . TYR D 1 294 ? -21.990 35.590  -3.718  1.00 42.56  ? 294  TYR D C   1 
ATOM   11118 O  O   . TYR D 1 294 ? -22.175 36.721  -3.259  1.00 34.57  ? 294  TYR D O   1 
ATOM   11119 C  CB  . TYR D 1 294 ? -21.672 35.398  -6.162  1.00 44.43  ? 294  TYR D CB  1 
ATOM   11120 C  CG  . TYR D 1 294 ? -22.338 36.736  -6.454  1.00 39.96  ? 294  TYR D CG  1 
ATOM   11121 C  CD1 . TYR D 1 294 ? -21.577 37.891  -6.649  1.00 39.35  ? 294  TYR D CD1 1 
ATOM   11122 C  CD2 . TYR D 1 294 ? -23.724 36.841  -6.549  1.00 29.27  ? 294  TYR D CD2 1 
ATOM   11123 C  CE1 . TYR D 1 294 ? -22.184 39.110  -6.920  1.00 38.48  ? 294  TYR D CE1 1 
ATOM   11124 C  CE2 . TYR D 1 294 ? -24.336 38.049  -6.806  1.00 22.21  ? 294  TYR D CE2 1 
ATOM   11125 C  CZ  . TYR D 1 294 ? -23.565 39.181  -6.994  1.00 38.12  ? 294  TYR D CZ  1 
ATOM   11126 O  OH  . TYR D 1 294 ? -24.180 40.389  -7.255  1.00 41.28  ? 294  TYR D OH  1 
ATOM   11127 N  N   . ALA D 1 295 ? -22.662 34.515  -3.318  1.00 37.37  ? 295  ALA D N   1 
ATOM   11128 C  CA  . ALA D 1 295 ? -23.777 34.610  -2.382  1.00 32.22  ? 295  ALA D CA  1 
ATOM   11129 C  C   . ALA D 1 295 ? -23.364 34.627  -0.892  1.00 25.57  ? 295  ALA D C   1 
ATOM   11130 O  O   . ALA D 1 295 ? -24.137 35.038  -0.022  1.00 25.30  ? 295  ALA D O   1 
ATOM   11131 C  CB  . ALA D 1 295 ? -24.767 33.493  -2.653  1.00 23.09  ? 295  ALA D CB  1 
ATOM   11132 N  N   . PHE D 1 296 ? -22.147 34.198  -0.597  1.00 26.81  ? 296  PHE D N   1 
ATOM   11133 C  CA  . PHE D 1 296 ? -21.736 34.070  0.799   1.00 32.55  ? 296  PHE D CA  1 
ATOM   11134 C  C   . PHE D 1 296 ? -20.449 34.820  1.100   1.00 36.50  ? 296  PHE D C   1 
ATOM   11135 O  O   . PHE D 1 296 ? -19.928 34.739  2.218   1.00 25.18  ? 296  PHE D O   1 
ATOM   11136 C  CB  . PHE D 1 296 ? -21.598 32.597  1.184   1.00 35.84  ? 296  PHE D CB  1 
ATOM   11137 C  CG  . PHE D 1 296 ? -22.889 31.830  1.104   1.00 46.63  ? 296  PHE D CG  1 
ATOM   11138 C  CD1 . PHE D 1 296 ? -23.381 31.399  -0.117  1.00 44.21  ? 296  PHE D CD1 1 
ATOM   11139 C  CD2 . PHE D 1 296 ? -23.617 31.543  2.252   1.00 47.55  ? 296  PHE D CD2 1 
ATOM   11140 C  CE1 . PHE D 1 296 ? -24.571 30.696  -0.191  1.00 40.34  ? 296  PHE D CE1 1 
ATOM   11141 C  CE2 . PHE D 1 296 ? -24.808 30.838  2.187   1.00 34.99  ? 296  PHE D CE2 1 
ATOM   11142 C  CZ  . PHE D 1 296 ? -25.286 30.416  0.962   1.00 44.05  ? 296  PHE D CZ  1 
ATOM   11143 N  N   . SER D 1 297 ? -19.954 35.551  0.097   1.00 33.89  ? 297  SER D N   1 
ATOM   11144 C  CA  . SER D 1 297 ? -18.775 36.403  0.258   1.00 23.35  ? 297  SER D CA  1 
ATOM   11145 C  C   . SER D 1 297 ? -18.767 37.580  -0.730  1.00 21.17  ? 297  SER D C   1 
ATOM   11146 O  O   . SER D 1 297 ? -19.766 37.854  -1.390  1.00 33.86  ? 297  SER D O   1 
ATOM   11147 C  CB  . SER D 1 297 ? -17.494 35.576  0.098   1.00 24.56  ? 297  SER D CB  1 
ATOM   11148 O  OG  . SER D 1 297 ? -17.223 35.307  -1.265  1.00 22.08  ? 297  SER D OG  1 
ATOM   11149 N  N   . ASN D 1 298 ? -17.636 38.266  -0.831  1.00 10.99  ? 298  ASN D N   1 
ATOM   11150 C  CA  . ASN D 1 298 ? -17.479 39.348  -1.790  1.00 30.81  ? 298  ASN D CA  1 
ATOM   11151 C  C   . ASN D 1 298 ? -17.053 38.838  -3.161  1.00 33.10  ? 298  ASN D C   1 
ATOM   11152 O  O   . ASN D 1 298 ? -17.086 39.567  -4.169  1.00 27.50  ? 298  ASN D O   1 
ATOM   11153 C  CB  . ASN D 1 298 ? -16.419 40.338  -1.308  1.00 28.76  ? 298  ASN D CB  1 
ATOM   11154 C  CG  . ASN D 1 298 ? -16.862 41.118  -0.105  1.00 30.74  ? 298  ASN D CG  1 
ATOM   11155 O  OD1 . ASN D 1 298 ? -18.066 41.237  0.156   1.00 32.52  ? 298  ASN D OD1 1 
ATOM   11156 N  ND2 . ASN D 1 298 ? -15.890 41.660  0.650   1.00 21.30  ? 298  ASN D ND2 1 
ATOM   11157 N  N   . CYS D 1 299 ? -16.639 37.580  -3.181  1.00 21.29  ? 299  CYS D N   1 
ATOM   11158 C  CA  . CYS D 1 299 ? -15.921 37.056  -4.318  1.00 23.91  ? 299  CYS D CA  1 
ATOM   11159 C  C   . CYS D 1 299 ? -16.783 36.919  -5.569  1.00 27.78  ? 299  CYS D C   1 
ATOM   11160 O  O   . CYS D 1 299 ? -17.931 36.483  -5.488  1.00 38.24  ? 299  CYS D O   1 
ATOM   11161 C  CB  . CYS D 1 299 ? -15.288 35.724  -3.971  1.00 9.36   ? 299  CYS D CB  1 
ATOM   11162 S  SG  . CYS D 1 299 ? -13.929 35.423  -5.046  1.00 28.51  ? 299  CYS D SG  1 
ATOM   11163 N  N   . PHE D 1 300 ? -16.215 37.304  -6.716  1.00 29.48  ? 300  PHE D N   1 
ATOM   11164 C  CA  . PHE D 1 300 ? -16.831 37.089  -8.028  1.00 26.98  ? 300  PHE D CA  1 
ATOM   11165 C  C   . PHE D 1 300 ? -16.131 35.954  -8.786  1.00 31.25  ? 300  PHE D C   1 
ATOM   11166 O  O   . PHE D 1 300 ? -15.113 36.168  -9.458  1.00 32.74  ? 300  PHE D O   1 
ATOM   11167 C  CB  . PHE D 1 300 ? -16.762 38.357  -8.875  1.00 32.11  ? 300  PHE D CB  1 
ATOM   11168 C  CG  . PHE D 1 300 ? -17.617 39.480  -8.373  1.00 41.33  ? 300  PHE D CG  1 
ATOM   11169 C  CD1 . PHE D 1 300 ? -18.149 40.405  -9.264  1.00 33.99  ? 300  PHE D CD1 1 
ATOM   11170 C  CD2 . PHE D 1 300 ? -17.886 39.625  -7.018  1.00 47.09  ? 300  PHE D CD2 1 
ATOM   11171 C  CE1 . PHE D 1 300 ? -18.941 41.462  -8.815  1.00 35.72  ? 300  PHE D CE1 1 
ATOM   11172 C  CE2 . PHE D 1 300 ? -18.679 40.672  -6.563  1.00 50.29  ? 300  PHE D CE2 1 
ATOM   11173 C  CZ  . PHE D 1 300 ? -19.208 41.596  -7.468  1.00 39.52  ? 300  PHE D CZ  1 
ATOM   11174 N  N   . GLU D 1 301 ? -16.681 34.751  -8.683  1.00 22.90  ? 301  GLU D N   1 
ATOM   11175 C  CA  . GLU D 1 301 ? -16.103 33.597  -9.335  1.00 11.87  ? 301  GLU D CA  1 
ATOM   11176 C  C   . GLU D 1 301 ? -16.792 33.309  -10.669 1.00 28.01  ? 301  GLU D C   1 
ATOM   11177 O  O   . GLU D 1 301 ? -18.022 33.250  -10.752 1.00 26.75  ? 301  GLU D O   1 
ATOM   11178 C  CB  . GLU D 1 301 ? -16.187 32.385  -8.403  1.00 21.39  ? 301  GLU D CB  1 
ATOM   11179 C  CG  . GLU D 1 301 ? -15.685 31.081  -9.004  1.00 33.89  ? 301  GLU D CG  1 
ATOM   11180 C  CD  . GLU D 1 301 ? -15.357 30.024  -7.945  1.00 44.18  ? 301  GLU D CD  1 
ATOM   11181 O  OE1 . GLU D 1 301 ? -14.406 30.226  -7.153  1.00 49.55  ? 301  GLU D OE1 1 
ATOM   11182 O  OE2 . GLU D 1 301 ? -16.039 28.979  -7.905  1.00 47.79  ? 301  GLU D OE2 1 
ATOM   11183 N  N   . LEU D 1 302 ? -15.991 33.156  -11.719 1.00 34.98  ? 302  LEU D N   1 
ATOM   11184 C  CA  . LEU D 1 302 ? -16.467 32.601  -12.979 1.00 34.68  ? 302  LEU D CA  1 
ATOM   11185 C  C   . LEU D 1 302 ? -16.205 31.105  -13.001 1.00 38.78  ? 302  LEU D C   1 
ATOM   11186 O  O   . LEU D 1 302 ? -15.307 30.617  -12.308 1.00 40.85  ? 302  LEU D O   1 
ATOM   11187 C  CB  . LEU D 1 302 ? -15.690 33.193  -14.142 1.00 33.23  ? 302  LEU D CB  1 
ATOM   11188 C  CG  . LEU D 1 302 ? -15.829 34.670  -14.419 1.00 34.86  ? 302  LEU D CG  1 
ATOM   11189 C  CD1 . LEU D 1 302 ? -15.138 34.948  -15.731 1.00 36.01  ? 302  LEU D CD1 1 
ATOM   11190 C  CD2 . LEU D 1 302 ? -17.314 35.015  -14.492 1.00 42.12  ? 302  LEU D CD2 1 
ATOM   11191 N  N   . THR D 1 303 ? -16.969 30.384  -13.818 1.00 35.04  ? 303  THR D N   1 
ATOM   11192 C  CA  . THR D 1 303 ? -16.676 28.984  -14.107 1.00 41.21  ? 303  THR D CA  1 
ATOM   11193 C  C   . THR D 1 303 ? -16.103 28.924  -15.522 1.00 46.32  ? 303  THR D C   1 
ATOM   11194 O  O   . THR D 1 303 ? -16.686 29.480  -16.453 1.00 51.31  ? 303  THR D O   1 
ATOM   11195 C  CB  . THR D 1 303 ? -17.935 28.095  -14.021 1.00 42.80  ? 303  THR D CB  1 
ATOM   11196 O  OG1 . THR D 1 303 ? -18.662 28.391  -12.825 1.00 44.88  ? 303  THR D OG1 1 
ATOM   11197 C  CG2 . THR D 1 303 ? -17.548 26.631  -14.023 1.00 34.56  ? 303  THR D CG2 1 
ATOM   11198 N  N   . ILE D 1 304 ? -14.958 28.269  -15.690 1.00 51.21  ? 304  ILE D N   1 
ATOM   11199 C  CA  . ILE D 1 304 ? -14.295 28.248  -16.994 1.00 53.93  ? 304  ILE D CA  1 
ATOM   11200 C  C   . ILE D 1 304 ? -14.005 26.854  -17.567 1.00 49.30  ? 304  ILE D C   1 
ATOM   11201 O  O   . ILE D 1 304 ? -13.234 26.066  -17.019 1.00 29.08  ? 304  ILE D O   1 
ATOM   11202 C  CB  . ILE D 1 304 ? -13.022 29.125  -17.012 1.00 42.67  ? 304  ILE D CB  1 
ATOM   11203 C  CG1 . ILE D 1 304 ? -13.400 30.578  -16.728 1.00 36.56  ? 304  ILE D CG1 1 
ATOM   11204 C  CG2 . ILE D 1 304 ? -12.321 29.022  -18.367 1.00 36.61  ? 304  ILE D CG2 1 
ATOM   11205 C  CD1 . ILE D 1 304 ? -12.233 31.465  -16.461 1.00 47.36  ? 304  ILE D CD1 1 
ATOM   11206 N  N   . GLU D 1 305 ? -14.634 26.576  -18.699 1.00 39.96  ? 305  GLU D N   1 
ATOM   11207 C  CA  . GLU D 1 305 ? -14.468 25.310  -19.370 1.00 36.89  ? 305  GLU D CA  1 
ATOM   11208 C  C   . GLU D 1 305 ? -13.320 25.436  -20.374 1.00 42.93  ? 305  GLU D C   1 
ATOM   11209 O  O   . GLU D 1 305 ? -13.356 26.300  -21.240 1.00 51.84  ? 305  GLU D O   1 
ATOM   11210 C  CB  . GLU D 1 305 ? -15.780 24.970  -20.071 1.00 28.77  ? 305  GLU D CB  1 
ATOM   11211 C  CG  . GLU D 1 305 ? -16.981 24.858  -19.128 1.00 23.89  ? 305  GLU D CG  1 
ATOM   11212 C  CD  . GLU D 1 305 ? -17.023 23.537  -18.352 1.00 39.78  ? 305  GLU D CD  1 
ATOM   11213 O  OE1 . GLU D 1 305 ? -17.873 23.424  -17.442 1.00 38.98  ? 305  GLU D OE1 1 
ATOM   11214 O  OE2 . GLU D 1 305 ? -16.209 22.622  -18.633 1.00 36.31  ? 305  GLU D OE2 1 
ATOM   11215 N  N   . LEU D 1 306 ? -12.309 24.576  -20.275 1.00 36.80  ? 306  LEU D N   1 
ATOM   11216 C  CA  . LEU D 1 306 ? -11.088 24.764  -21.073 1.00 39.01  ? 306  LEU D CA  1 
ATOM   11217 C  C   . LEU D 1 306 ? -10.969 23.941  -22.359 1.00 40.92  ? 306  LEU D C   1 
ATOM   11218 O  O   . LEU D 1 306 ? -10.451 24.425  -23.366 1.00 41.05  ? 306  LEU D O   1 
ATOM   11219 C  CB  . LEU D 1 306 ? -9.854  24.551  -20.202 1.00 37.16  ? 306  LEU D CB  1 
ATOM   11220 C  CG  . LEU D 1 306 ? -9.798  25.494  -18.996 1.00 45.40  ? 306  LEU D CG  1 
ATOM   11221 C  CD1 . LEU D 1 306 ? -8.763  25.072  -17.964 1.00 35.83  ? 306  LEU D CD1 1 
ATOM   11222 C  CD2 . LEU D 1 306 ? -9.549  26.914  -19.470 1.00 40.17  ? 306  LEU D CD2 1 
ATOM   11223 N  N   . SER D 1 307 ? -11.451 22.703  -22.322 1.00 45.01  ? 307  SER D N   1 
ATOM   11224 C  CA  . SER D 1 307 ? -11.318 21.802  -23.458 1.00 37.80  ? 307  SER D CA  1 
ATOM   11225 C  C   . SER D 1 307 ? -12.574 20.955  -23.721 1.00 41.10  ? 307  SER D C   1 
ATOM   11226 O  O   . SER D 1 307 ? -13.392 20.726  -22.830 1.00 47.64  ? 307  SER D O   1 
ATOM   11227 C  CB  . SER D 1 307 ? -10.115 20.891  -23.230 1.00 37.66  ? 307  SER D CB  1 
ATOM   11228 O  OG  . SER D 1 307 ? -10.291 20.145  -22.043 1.00 38.47  ? 307  SER D OG  1 
ATOM   11229 N  N   . CYS D 1 308 ? -12.723 20.496  -24.959 1.00 51.17  ? 308  CYS D N   1 
ATOM   11230 C  CA  . CYS D 1 308 ? -13.790 19.560  -25.299 1.00 49.96  ? 308  CYS D CA  1 
ATOM   11231 C  C   . CYS D 1 308 ? -13.504 18.210  -24.670 1.00 47.40  ? 308  CYS D C   1 
ATOM   11232 O  O   . CYS D 1 308 ? -14.410 17.524  -24.188 1.00 50.92  ? 308  CYS D O   1 
ATOM   11233 C  CB  . CYS D 1 308 ? -13.912 19.409  -26.815 1.00 36.97  ? 308  CYS D CB  1 
ATOM   11234 S  SG  . CYS D 1 308 ? -14.854 20.717  -27.573 1.00 51.54  ? 308  CYS D SG  1 
ATOM   11235 N  N   . CYS D 1 309 ? -12.229 17.838  -24.695 1.00 41.72  ? 309  CYS D N   1 
ATOM   11236 C  CA  . CYS D 1 309 ? -11.757 16.603  -24.088 1.00 40.66  ? 309  CYS D CA  1 
ATOM   11237 C  C   . CYS D 1 309 ? -11.440 16.851  -22.626 1.00 46.76  ? 309  CYS D C   1 
ATOM   11238 O  O   . CYS D 1 309 ? -10.539 17.631  -22.304 1.00 32.60  ? 309  CYS D O   1 
ATOM   11239 C  CB  . CYS D 1 309 ? -10.503 16.102  -24.811 1.00 37.47  ? 309  CYS D CB  1 
ATOM   11240 S  SG  . CYS D 1 309 ? -9.791  14.578  -24.113 1.00 57.88  ? 309  CYS D SG  1 
ATOM   11241 N  N   . LYS D 1 310 ? -12.181 16.185  -21.744 1.00 51.98  ? 310  LYS D N   1 
ATOM   11242 C  CA  . LYS D 1 310 ? -12.049 16.414  -20.304 1.00 48.26  ? 310  LYS D CA  1 
ATOM   11243 C  C   . LYS D 1 310 ? -10.643 16.125  -19.826 1.00 52.59  ? 310  LYS D C   1 
ATOM   11244 O  O   . LYS D 1 310 ? -10.091 16.894  -19.044 1.00 59.08  ? 310  LYS D O   1 
ATOM   11245 C  CB  . LYS D 1 310 ? -13.043 15.559  -19.511 1.00 54.25  ? 310  LYS D CB  1 
ATOM   11246 C  CG  . LYS D 1 310 ? -14.480 16.065  -19.538 1.00 48.61  ? 310  LYS D CG  1 
ATOM   11247 C  CD  . LYS D 1 310 ? -15.395 15.135  -18.771 1.00 43.01  ? 310  LYS D CD  1 
ATOM   11248 C  CE  . LYS D 1 310 ? -16.783 15.724  -18.671 1.00 48.67  ? 310  LYS D CE  1 
ATOM   11249 N  NZ  . LYS D 1 310 ? -17.638 14.960  -17.717 1.00 63.01  ? 310  LYS D NZ  1 
ATOM   11250 N  N   . TYR D 1 311 ? -10.081 15.010  -20.300 1.00 51.11  ? 311  TYR D N   1 
ATOM   11251 C  CA  . TYR D 1 311 ? -8.743  14.562  -19.922 1.00 50.23  ? 311  TYR D CA  1 
ATOM   11252 C  C   . TYR D 1 311 ? -7.907  14.267  -21.172 1.00 57.02  ? 311  TYR D C   1 
ATOM   11253 O  O   . TYR D 1 311 ? -7.799  13.116  -21.609 1.00 60.40  ? 311  TYR D O   1 
ATOM   11254 C  CB  . TYR D 1 311 ? -8.831  13.302  -19.053 1.00 54.61  ? 311  TYR D CB  1 
ATOM   11255 C  CG  . TYR D 1 311 ? -7.645  13.054  -18.128 1.00 46.99  ? 311  TYR D CG  1 
ATOM   11256 C  CD1 . TYR D 1 311 ? -7.817  12.352  -16.936 1.00 39.61  ? 311  TYR D CD1 1 
ATOM   11257 C  CD2 . TYR D 1 311 ? -6.368  13.516  -18.441 1.00 39.76  ? 311  TYR D CD2 1 
ATOM   11258 C  CE1 . TYR D 1 311 ? -6.758  12.115  -16.079 1.00 42.13  ? 311  TYR D CE1 1 
ATOM   11259 C  CE2 . TYR D 1 311 ? -5.300  13.289  -17.578 1.00 44.89  ? 311  TYR D CE2 1 
ATOM   11260 C  CZ  . TYR D 1 311 ? -5.507  12.584  -16.399 1.00 43.61  ? 311  TYR D CZ  1 
ATOM   11261 O  OH  . TYR D 1 311 ? -4.475  12.341  -15.528 1.00 46.93  ? 311  TYR D OH  1 
ATOM   11262 N  N   . PRO D 1 312 ? -7.318  15.313  -21.760 1.00 54.63  ? 312  PRO D N   1 
ATOM   11263 C  CA  . PRO D 1 312 ? -6.478  15.145  -22.947 1.00 47.56  ? 312  PRO D CA  1 
ATOM   11264 C  C   . PRO D 1 312 ? -5.090  14.613  -22.589 1.00 65.51  ? 312  PRO D C   1 
ATOM   11265 O  O   . PRO D 1 312 ? -4.751  14.450  -21.412 1.00 65.77  ? 312  PRO D O   1 
ATOM   11266 C  CB  . PRO D 1 312 ? -6.354  16.570  -23.497 1.00 44.53  ? 312  PRO D CB  1 
ATOM   11267 C  CG  . PRO D 1 312 ? -7.297  17.419  -22.676 1.00 57.85  ? 312  PRO D CG  1 
ATOM   11268 C  CD  . PRO D 1 312 ? -7.462  16.724  -21.378 1.00 53.63  ? 312  PRO D CD  1 
ATOM   11269 N  N   . ALA D 1 313 ? -4.290  14.348  -23.614 1.00 66.51  ? 313  ALA D N   1 
ATOM   11270 C  CA  . ALA D 1 313 ? -2.951  13.836  -23.418 1.00 58.17  ? 313  ALA D CA  1 
ATOM   11271 C  C   . ALA D 1 313 ? -1.987  14.989  -23.216 1.00 54.46  ? 313  ALA D C   1 
ATOM   11272 O  O   . ALA D 1 313 ? -2.229  16.100  -23.693 1.00 53.28  ? 313  ALA D O   1 
ATOM   11273 C  CB  . ALA D 1 313 ? -2.532  12.998  -24.608 1.00 61.02  ? 313  ALA D CB  1 
ATOM   11274 N  N   . ALA D 1 314 ? -0.888  14.710  -22.516 1.00 53.19  ? 314  ALA D N   1 
ATOM   11275 C  CA  . ALA D 1 314 ? 0.144   15.704  -22.218 1.00 49.29  ? 314  ALA D CA  1 
ATOM   11276 C  C   . ALA D 1 314 ? 0.516   16.591  -23.409 1.00 58.54  ? 314  ALA D C   1 
ATOM   11277 O  O   . ALA D 1 314 ? 0.521   17.813  -23.287 1.00 60.20  ? 314  ALA D O   1 
ATOM   11278 C  CB  . ALA D 1 314 ? 1.388   15.020  -21.671 1.00 49.63  ? 314  ALA D CB  1 
ATOM   11279 N  N   . SER D 1 315 ? 0.822   15.972  -24.552 1.00 56.52  ? 315  SER D N   1 
ATOM   11280 C  CA  . SER D 1 315 ? 1.322   16.684  -25.731 1.00 45.73  ? 315  SER D CA  1 
ATOM   11281 C  C   . SER D 1 315 ? 0.428   17.851  -26.092 1.00 42.84  ? 315  SER D C   1 
ATOM   11282 O  O   . SER D 1 315 ? 0.834   18.795  -26.775 1.00 47.68  ? 315  SER D O   1 
ATOM   11283 C  CB  . SER D 1 315 ? 1.423   15.731  -26.916 1.00 46.46  ? 315  SER D CB  1 
ATOM   11284 O  OG  . SER D 1 315 ? 0.156   15.195  -27.236 1.00 45.45  ? 315  SER D OG  1 
ATOM   11285 N  N   . THR D 1 316 ? -0.803  17.770  -25.618 1.00 44.28  ? 316  THR D N   1 
ATOM   11286 C  CA  . THR D 1 316 ? -1.788  18.805  -25.840 1.00 45.13  ? 316  THR D CA  1 
ATOM   11287 C  C   . THR D 1 316 ? -1.495  20.012  -24.946 1.00 44.44  ? 316  THR D C   1 
ATOM   11288 O  O   . THR D 1 316 ? -1.763  21.160  -25.314 1.00 48.31  ? 316  THR D O   1 
ATOM   11289 C  CB  . THR D 1 316 ? -3.186  18.237  -25.573 1.00 40.46  ? 316  THR D CB  1 
ATOM   11290 O  OG1 . THR D 1 316 ? -3.726  17.745  -26.806 1.00 42.05  ? 316  THR D OG1 1 
ATOM   11291 C  CG2 . THR D 1 316 ? -4.111  19.294  -25.004 1.00 57.89  ? 316  THR D CG2 1 
ATOM   11292 N  N   . LEU D 1 317 ? -0.905  19.739  -23.792 1.00 25.99  ? 317  LEU D N   1 
ATOM   11293 C  CA  . LEU D 1 317 ? -0.733  20.741  -22.755 1.00 38.12  ? 317  LEU D CA  1 
ATOM   11294 C  C   . LEU D 1 317 ? -0.019  22.015  -23.196 1.00 38.02  ? 317  LEU D C   1 
ATOM   11295 O  O   . LEU D 1 317 ? -0.463  23.114  -22.881 1.00 43.99  ? 317  LEU D O   1 
ATOM   11296 C  CB  . LEU D 1 317 ? -0.032  20.136  -21.536 1.00 34.47  ? 317  LEU D CB  1 
ATOM   11297 C  CG  . LEU D 1 317 ? -0.649  18.858  -20.962 1.00 37.55  ? 317  LEU D CG  1 
ATOM   11298 C  CD1 . LEU D 1 317 ? 0.291   18.283  -19.930 1.00 52.78  ? 317  LEU D CD1 1 
ATOM   11299 C  CD2 . LEU D 1 317 ? -2.044  19.094  -20.383 1.00 26.07  ? 317  LEU D CD2 1 
ATOM   11300 N  N   . PRO D 1 318 ? 1.101   21.886  -23.913 1.00 41.24  ? 318  PRO D N   1 
ATOM   11301 C  CA  . PRO D 1 318 ? 1.777   23.113  -24.371 1.00 47.98  ? 318  PRO D CA  1 
ATOM   11302 C  C   . PRO D 1 318 ? 0.889   24.064  -25.223 1.00 51.07  ? 318  PRO D C   1 
ATOM   11303 O  O   . PRO D 1 318 ? 0.882   25.269  -24.968 1.00 44.77  ? 318  PRO D O   1 
ATOM   11304 C  CB  . PRO D 1 318 ? 2.968   22.574  -25.177 1.00 47.35  ? 318  PRO D CB  1 
ATOM   11305 C  CG  . PRO D 1 318 ? 3.220   21.202  -24.611 1.00 44.42  ? 318  PRO D CG  1 
ATOM   11306 C  CD  . PRO D 1 318 ? 1.848   20.671  -24.276 1.00 47.80  ? 318  PRO D CD  1 
ATOM   11307 N  N   . GLN D 1 319 ? 0.161   23.541  -26.206 1.00 40.03  ? 319  GLN D N   1 
ATOM   11308 C  CA  . GLN D 1 319 ? -0.815  24.350  -26.926 1.00 43.73  ? 319  GLN D CA  1 
ATOM   11309 C  C   . GLN D 1 319 ? -1.780  25.033  -25.963 1.00 42.66  ? 319  GLN D C   1 
ATOM   11310 O  O   . GLN D 1 319 ? -1.956  26.263  -25.989 1.00 32.99  ? 319  GLN D O   1 
ATOM   11311 C  CB  . GLN D 1 319 ? -1.626  23.486  -27.895 1.00 63.32  ? 319  GLN D CB  1 
ATOM   11312 C  CG  . GLN D 1 319 ? -1.080  23.437  -29.309 1.00 79.45  ? 319  GLN D CG  1 
ATOM   11313 C  CD  . GLN D 1 319 ? -0.477  22.084  -29.643 1.00 100.03 ? 319  GLN D CD  1 
ATOM   11314 O  OE1 . GLN D 1 319 ? -0.485  21.653  -30.799 1.00 106.50 ? 319  GLN D OE1 1 
ATOM   11315 N  NE2 . GLN D 1 319 ? 0.040   21.398  -28.622 1.00 99.48  ? 319  GLN D NE2 1 
ATOM   11316 N  N   . GLU D 1 320 ? -2.418  24.224  -25.122 1.00 41.64  ? 320  GLU D N   1 
ATOM   11317 C  CA  . GLU D 1 320 ? -3.411  24.740  -24.193 1.00 41.61  ? 320  GLU D CA  1 
ATOM   11318 C  C   . GLU D 1 320 ? -2.839  25.945  -23.454 1.00 35.87  ? 320  GLU D C   1 
ATOM   11319 O  O   . GLU D 1 320 ? -3.511  26.960  -23.301 1.00 47.46  ? 320  GLU D O   1 
ATOM   11320 C  CB  . GLU D 1 320 ? -3.862  23.650  -23.222 1.00 45.27  ? 320  GLU D CB  1 
ATOM   11321 C  CG  . GLU D 1 320 ? -4.553  22.457  -23.880 1.00 50.57  ? 320  GLU D CG  1 
ATOM   11322 C  CD  . GLU D 1 320 ? -5.913  22.793  -24.477 1.00 53.58  ? 320  GLU D CD  1 
ATOM   11323 O  OE1 . GLU D 1 320 ? -6.314  23.975  -24.448 1.00 45.00  ? 320  GLU D OE1 1 
ATOM   11324 O  OE2 . GLU D 1 320 ? -6.586  21.866  -24.980 1.00 58.80  ? 320  GLU D OE2 1 
ATOM   11325 N  N   . TRP D 1 321 ? -1.581  25.838  -23.037 1.00 32.73  ? 321  TRP D N   1 
ATOM   11326 C  CA  . TRP D 1 321 ? -0.916  26.930  -22.344 1.00 44.01  ? 321  TRP D CA  1 
ATOM   11327 C  C   . TRP D 1 321 ? -0.874  28.219  -23.163 1.00 55.33  ? 321  TRP D C   1 
ATOM   11328 O  O   . TRP D 1 321 ? -1.098  29.302  -22.623 1.00 48.59  ? 321  TRP D O   1 
ATOM   11329 C  CB  . TRP D 1 321 ? 0.508   26.556  -21.930 1.00 47.53  ? 321  TRP D CB  1 
ATOM   11330 C  CG  . TRP D 1 321 ? 1.309   27.776  -21.531 1.00 57.98  ? 321  TRP D CG  1 
ATOM   11331 C  CD1 . TRP D 1 321 ? 2.277   28.404  -22.271 1.00 50.17  ? 321  TRP D CD1 1 
ATOM   11332 C  CD2 . TRP D 1 321 ? 1.178   28.536  -20.317 1.00 63.09  ? 321  TRP D CD2 1 
ATOM   11333 N  NE1 . TRP D 1 321 ? 2.764   29.495  -21.582 1.00 46.46  ? 321  TRP D NE1 1 
ATOM   11334 C  CE2 . TRP D 1 321 ? 2.108   29.595  -20.382 1.00 46.27  ? 321  TRP D CE2 1 
ATOM   11335 C  CE3 . TRP D 1 321 ? 0.368   28.419  -19.180 1.00 63.81  ? 321  TRP D CE3 1 
ATOM   11336 C  CZ2 . TRP D 1 321 ? 2.252   30.528  -19.356 1.00 32.85  ? 321  TRP D CZ2 1 
ATOM   11337 C  CZ3 . TRP D 1 321 ? 0.517   29.352  -18.155 1.00 48.86  ? 321  TRP D CZ3 1 
ATOM   11338 C  CH2 . TRP D 1 321 ? 1.456   30.390  -18.254 1.00 36.06  ? 321  TRP D CH2 1 
ATOM   11339 N  N   . GLN D 1 322 ? -0.573  28.109  -24.454 1.00 56.75  ? 322  GLN D N   1 
ATOM   11340 C  CA  . GLN D 1 322 ? -0.406  29.300  -25.284 1.00 57.44  ? 322  GLN D CA  1 
ATOM   11341 C  C   . GLN D 1 322 ? -1.749  29.995  -25.530 1.00 55.15  ? 322  GLN D C   1 
ATOM   11342 O  O   . GLN D 1 322 ? -1.811  31.213  -25.728 1.00 52.40  ? 322  GLN D O   1 
ATOM   11343 C  CB  . GLN D 1 322 ? 0.289   28.956  -26.606 1.00 54.56  ? 322  GLN D CB  1 
ATOM   11344 C  CG  . GLN D 1 322 ? 1.518   29.822  -26.906 1.00 59.92  ? 322  GLN D CG  1 
ATOM   11345 C  CD  . GLN D 1 322 ? 2.700   29.547  -25.970 1.00 67.66  ? 322  GLN D CD  1 
ATOM   11346 O  OE1 . GLN D 1 322 ? 3.363   30.474  -25.501 1.00 65.72  ? 322  GLN D OE1 1 
ATOM   11347 N  NE2 . GLN D 1 322 ? 2.968   28.271  -25.701 1.00 63.18  ? 322  GLN D NE2 1 
ATOM   11348 N  N   . ARG D 1 323 ? -2.824  29.217  -25.496 1.00 42.32  ? 323  ARG D N   1 
ATOM   11349 C  CA  . ARG D 1 323 ? -4.162  29.760  -25.715 1.00 48.38  ? 323  ARG D CA  1 
ATOM   11350 C  C   . ARG D 1 323 ? -4.723  30.485  -24.481 1.00 52.30  ? 323  ARG D C   1 
ATOM   11351 O  O   . ARG D 1 323 ? -5.282  31.592  -24.573 1.00 45.77  ? 323  ARG D O   1 
ATOM   11352 C  CB  . ARG D 1 323 ? -5.111  28.635  -26.119 1.00 42.50  ? 323  ARG D CB  1 
ATOM   11353 C  CG  . ARG D 1 323 ? -4.640  27.843  -27.321 1.00 41.63  ? 323  ARG D CG  1 
ATOM   11354 C  CD  . ARG D 1 323 ? -5.502  26.617  -27.510 1.00 43.33  ? 323  ARG D CD  1 
ATOM   11355 N  NE  . ARG D 1 323 ? -5.284  25.985  -28.803 1.00 53.00  ? 323  ARG D NE  1 
ATOM   11356 C  CZ  . ARG D 1 323 ? -5.890  24.866  -29.191 1.00 74.63  ? 323  ARG D CZ  1 
ATOM   11357 N  NH1 . ARG D 1 323 ? -6.748  24.254  -28.386 1.00 71.51  ? 323  ARG D NH1 1 
ATOM   11358 N  NH2 . ARG D 1 323 ? -5.640  24.355  -30.384 1.00 92.88  ? 323  ARG D NH2 1 
ATOM   11359 N  N   . ASN D 1 324 ? -4.573  29.853  -23.324 1.00 41.30  ? 324  ASN D N   1 
ATOM   11360 C  CA  . ASN D 1 324 ? -5.145  30.386  -22.098 1.00 39.42  ? 324  ASN D CA  1 
ATOM   11361 C  C   . ASN D 1 324 ? -4.265  31.438  -21.416 1.00 30.81  ? 324  ASN D C   1 
ATOM   11362 O  O   . ASN D 1 324 ? -4.734  32.203  -20.580 1.00 39.48  ? 324  ASN D O   1 
ATOM   11363 C  CB  . ASN D 1 324 ? -5.474  29.236  -21.148 1.00 41.44  ? 324  ASN D CB  1 
ATOM   11364 C  CG  . ASN D 1 324 ? -6.508  28.283  -21.728 1.00 37.25  ? 324  ASN D CG  1 
ATOM   11365 O  OD1 . ASN D 1 324 ? -7.678  28.351  -21.380 1.00 41.58  ? 324  ASN D OD1 1 
ATOM   11366 N  ND2 . ASN D 1 324 ? -6.078  27.396  -22.624 1.00 38.99  ? 324  ASN D ND2 1 
ATOM   11367 N  N   . LYS D 1 325 ? -2.996  31.483  -21.808 1.00 35.80  ? 325  LYS D N   1 
ATOM   11368 C  CA  . LYS D 1 325 ? -2.003  32.375  -21.212 1.00 40.23  ? 325  LYS D CA  1 
ATOM   11369 C  C   . LYS D 1 325 ? -2.542  33.782  -21.067 1.00 39.38  ? 325  LYS D C   1 
ATOM   11370 O  O   . LYS D 1 325 ? -2.650  34.307  -19.959 1.00 43.98  ? 325  LYS D O   1 
ATOM   11371 C  CB  . LYS D 1 325 ? -0.746  32.394  -22.082 1.00 42.51  ? 325  LYS D CB  1 
ATOM   11372 C  CG  . LYS D 1 325 ? 0.489   33.019  -21.455 1.00 37.37  ? 325  LYS D CG  1 
ATOM   11373 C  CD  . LYS D 1 325 ? 1.600   32.990  -22.491 1.00 46.08  ? 325  LYS D CD  1 
ATOM   11374 C  CE  . LYS D 1 325 ? 2.925   33.449  -21.948 1.00 53.87  ? 325  LYS D CE  1 
ATOM   11375 N  NZ  . LYS D 1 325 ? 3.965   33.306  -23.011 1.00 65.18  ? 325  LYS D NZ  1 
ATOM   11376 N  N   . ALA D 1 326 ? -2.886  34.390  -22.194 1.00 38.01  ? 326  ALA D N   1 
ATOM   11377 C  CA  . ALA D 1 326 ? -3.383  35.759  -22.183 1.00 48.34  ? 326  ALA D CA  1 
ATOM   11378 C  C   . ALA D 1 326 ? -4.657  35.905  -21.348 1.00 51.53  ? 326  ALA D C   1 
ATOM   11379 O  O   . ALA D 1 326 ? -4.816  36.891  -20.621 1.00 37.55  ? 326  ALA D O   1 
ATOM   11380 C  CB  . ALA D 1 326 ? -3.607  36.252  -23.602 1.00 33.49  ? 326  ALA D CB  1 
ATOM   11381 N  N   . SER D 1 327 ? -5.545  34.912  -21.451 1.00 50.09  ? 327  SER D N   1 
ATOM   11382 C  CA  . SER D 1 327 ? -6.865  34.955  -20.816 1.00 33.54  ? 327  SER D CA  1 
ATOM   11383 C  C   . SER D 1 327 ? -6.750  34.884  -19.305 1.00 34.76  ? 327  SER D C   1 
ATOM   11384 O  O   . SER D 1 327 ? -7.474  35.562  -18.580 1.00 46.78  ? 327  SER D O   1 
ATOM   11385 C  CB  . SER D 1 327 ? -7.755  33.817  -21.324 1.00 24.59  ? 327  SER D CB  1 
ATOM   11386 O  OG  . SER D 1 327 ? -7.957  33.899  -22.726 1.00 34.93  ? 327  SER D OG  1 
ATOM   11387 N  N   . LEU D 1 328 ? -5.829  34.057  -18.833 1.00 32.94  ? 328  LEU D N   1 
ATOM   11388 C  CA  . LEU D 1 328 ? -5.552  33.914  -17.408 1.00 23.71  ? 328  LEU D CA  1 
ATOM   11389 C  C   . LEU D 1 328 ? -4.904  35.164  -16.785 1.00 32.37  ? 328  LEU D C   1 
ATOM   11390 O  O   . LEU D 1 328 ? -5.138  35.487  -15.619 1.00 29.20  ? 328  LEU D O   1 
ATOM   11391 C  CB  . LEU D 1 328 ? -4.631  32.722  -17.208 1.00 25.39  ? 328  LEU D CB  1 
ATOM   11392 C  CG  . LEU D 1 328 ? -5.232  31.343  -17.439 1.00 22.72  ? 328  LEU D CG  1 
ATOM   11393 C  CD1 . LEU D 1 328 ? -4.112  30.357  -17.670 1.00 24.09  ? 328  LEU D CD1 1 
ATOM   11394 C  CD2 . LEU D 1 328 ? -6.072  30.926  -16.240 1.00 24.39  ? 328  LEU D CD2 1 
ATOM   11395 N  N   . LEU D 1 329 ? -4.062  35.845  -17.556 1.00 36.94  ? 329  LEU D N   1 
ATOM   11396 C  CA  . LEU D 1 329 ? -3.414  37.056  -17.080 1.00 35.72  ? 329  LEU D CA  1 
ATOM   11397 C  C   . LEU D 1 329 ? -4.396  38.208  -17.094 1.00 34.30  ? 329  LEU D C   1 
ATOM   11398 O  O   . LEU D 1 329 ? -4.494  38.960  -16.130 1.00 43.36  ? 329  LEU D O   1 
ATOM   11399 C  CB  . LEU D 1 329 ? -2.209  37.398  -17.947 1.00 46.81  ? 329  LEU D CB  1 
ATOM   11400 C  CG  . LEU D 1 329 ? -0.849  36.763  -17.630 1.00 48.39  ? 329  LEU D CG  1 
ATOM   11401 C  CD1 . LEU D 1 329 ? -0.917  35.837  -16.419 1.00 43.97  ? 329  LEU D CD1 1 
ATOM   11402 C  CD2 . LEU D 1 329 ? -0.293  36.032  -18.854 1.00 46.41  ? 329  LEU D CD2 1 
ATOM   11403 N  N   . GLN D 1 330 ? -5.128  38.334  -18.198 1.00 39.14  ? 330  GLN D N   1 
ATOM   11404 C  CA  . GLN D 1 330 ? -6.059  39.446  -18.386 1.00 45.91  ? 330  GLN D CA  1 
ATOM   11405 C  C   . GLN D 1 330 ? -7.272  39.378  -17.452 1.00 43.97  ? 330  GLN D C   1 
ATOM   11406 O  O   . GLN D 1 330 ? -7.776  40.407  -16.988 1.00 51.05  ? 330  GLN D O   1 
ATOM   11407 C  CB  . GLN D 1 330 ? -6.495  39.539  -19.853 1.00 58.38  ? 330  GLN D CB  1 
ATOM   11408 C  CG  . GLN D 1 330 ? -5.373  39.992  -20.802 1.00 65.25  ? 330  GLN D CG  1 
ATOM   11409 C  CD  . GLN D 1 330 ? -4.741  41.327  -20.394 1.00 62.33  ? 330  GLN D CD  1 
ATOM   11410 O  OE1 . GLN D 1 330 ? -5.387  42.379  -20.439 1.00 61.50  ? 330  GLN D OE1 1 
ATOM   11411 N  NE2 . GLN D 1 330 ? -3.476  41.281  -19.992 1.00 58.47  ? 330  GLN D NE2 1 
ATOM   11412 N  N   . LEU D 1 331 ? -7.734  38.167  -17.172 1.00 25.60  ? 331  LEU D N   1 
ATOM   11413 C  CA  . LEU D 1 331 ? -8.784  37.988  -16.188 1.00 22.85  ? 331  LEU D CA  1 
ATOM   11414 C  C   . LEU D 1 331 ? -8.294  38.463  -14.834 1.00 30.42  ? 331  LEU D C   1 
ATOM   11415 O  O   . LEU D 1 331 ? -9.006  39.189  -14.129 1.00 29.33  ? 331  LEU D O   1 
ATOM   11416 C  CB  . LEU D 1 331 ? -9.167  36.523  -16.082 1.00 23.41  ? 331  LEU D CB  1 
ATOM   11417 C  CG  . LEU D 1 331 ? -10.414 36.219  -15.257 1.00 31.46  ? 331  LEU D CG  1 
ATOM   11418 C  CD1 . LEU D 1 331 ? -10.695 34.749  -15.370 1.00 28.29  ? 331  LEU D CD1 1 
ATOM   11419 C  CD2 . LEU D 1 331 ? -10.240 36.596  -13.803 1.00 55.80  ? 331  LEU D CD2 1 
ATOM   11420 N  N   . LEU D 1 332 ? -7.087  38.025  -14.465 1.00 31.06  ? 332  LEU D N   1 
ATOM   11421 C  CA  . LEU D 1 332 ? -6.448  38.451  -13.216 1.00 38.07  ? 332  LEU D CA  1 
ATOM   11422 C  C   . LEU D 1 332 ? -6.429  39.966  -13.079 1.00 36.10  ? 332  LEU D C   1 
ATOM   11423 O  O   . LEU D 1 332 ? -6.759  40.508  -12.013 1.00 32.69  ? 332  LEU D O   1 
ATOM   11424 C  CB  . LEU D 1 332 ? -5.024  37.907  -13.113 1.00 41.71  ? 332  LEU D CB  1 
ATOM   11425 C  CG  . LEU D 1 332 ? -4.987  36.414  -12.820 1.00 43.06  ? 332  LEU D CG  1 
ATOM   11426 C  CD1 . LEU D 1 332 ? -3.557  35.895  -12.756 1.00 28.94  ? 332  LEU D CD1 1 
ATOM   11427 C  CD2 . LEU D 1 332 ? -5.747  36.148  -11.520 1.00 39.68  ? 332  LEU D CD2 1 
ATOM   11428 N  N   . ARG D 1 333 ? -6.051  40.644  -14.164 1.00 30.53  ? 333  ARG D N   1 
ATOM   11429 C  CA  . ARG D 1 333 ? -5.974  42.099  -14.165 1.00 28.36  ? 333  ARG D CA  1 
ATOM   11430 C  C   . ARG D 1 333 ? -7.338  42.773  -14.044 1.00 30.76  ? 333  ARG D C   1 
ATOM   11431 O  O   . ARG D 1 333 ? -7.425  43.975  -13.772 1.00 50.70  ? 333  ARG D O   1 
ATOM   11432 C  CB  . ARG D 1 333 ? -5.227  42.589  -15.392 1.00 27.75  ? 333  ARG D CB  1 
ATOM   11433 C  CG  . ARG D 1 333 ? -3.856  41.958  -15.514 1.00 42.95  ? 333  ARG D CG  1 
ATOM   11434 C  CD  . ARG D 1 333 ? -2.880  42.795  -16.340 1.00 60.30  ? 333  ARG D CD  1 
ATOM   11435 N  NE  . ARG D 1 333 ? -2.276  43.870  -15.567 1.00 60.00  ? 333  ARG D NE  1 
ATOM   11436 C  CZ  . ARG D 1 333 ? -0.992  43.988  -15.229 1.00 63.80  ? 333  ARG D CZ  1 
ATOM   11437 N  NH1 . ARG D 1 333 ? -0.639  45.038  -14.518 1.00 63.69  ? 333  ARG D NH1 1 
ATOM   11438 N  NH2 . ARG D 1 333 ? -0.068  43.102  -15.586 1.00 64.53  ? 333  ARG D NH2 1 
ATOM   11439 N  N   . GLN D 1 334 ? -8.399  41.994  -14.236 1.00 30.76  ? 334  GLN D N   1 
ATOM   11440 C  CA  . GLN D 1 334 ? -9.756  42.472  -13.994 1.00 31.62  ? 334  GLN D CA  1 
ATOM   11441 C  C   . GLN D 1 334 ? -10.040 42.661  -12.492 1.00 39.27  ? 334  GLN D C   1 
ATOM   11442 O  O   . GLN D 1 334 ? -11.024 43.298  -12.114 1.00 43.80  ? 334  GLN D O   1 
ATOM   11443 C  CB  . GLN D 1 334 ? -10.775 41.508  -14.593 1.00 28.91  ? 334  GLN D CB  1 
ATOM   11444 C  CG  . GLN D 1 334 ? -10.895 41.592  -16.081 1.00 36.30  ? 334  GLN D CG  1 
ATOM   11445 C  CD  . GLN D 1 334 ? -11.545 42.888  -16.531 1.00 47.68  ? 334  GLN D CD  1 
ATOM   11446 O  OE1 . GLN D 1 334 ? -12.739 43.114  -16.309 1.00 56.23  ? 334  GLN D OE1 1 
ATOM   11447 N  NE2 . GLN D 1 334 ? -10.760 43.748  -17.172 1.00 41.40  ? 334  GLN D NE2 1 
ATOM   11448 N  N   . ALA D 1 335 ? -9.181  42.108  -11.640 1.00 28.10  ? 335  ALA D N   1 
ATOM   11449 C  CA  . ALA D 1 335 ? -9.333  42.278  -10.195 1.00 38.77  ? 335  ALA D CA  1 
ATOM   11450 C  C   . ALA D 1 335 ? -8.960  43.698  -9.790  1.00 42.35  ? 335  ALA D C   1 
ATOM   11451 O  O   . ALA D 1 335 ? -8.849  44.012  -8.599  1.00 40.81  ? 335  ALA D O   1 
ATOM   11452 C  CB  . ALA D 1 335 ? -8.470  41.262  -9.430  1.00 28.03  ? 335  ALA D CB  1 
ATOM   11453 N  N   . HIS D 1 336 ? -8.763  44.559  -10.784 1.00 30.73  ? 336  HIS D N   1 
ATOM   11454 C  CA  . HIS D 1 336 ? -8.353  45.925  -10.506 1.00 34.75  ? 336  HIS D CA  1 
ATOM   11455 C  C   . HIS D 1 336 ? -9.365  46.965  -10.997 1.00 40.56  ? 336  HIS D C   1 
ATOM   11456 O  O   . HIS D 1 336 ? -9.183  48.166  -10.773 1.00 34.42  ? 336  HIS D O   1 
ATOM   11457 C  CB  . HIS D 1 336 ? -6.950  46.171  -11.067 1.00 37.34  ? 336  HIS D CB  1 
ATOM   11458 C  CG  . HIS D 1 336 ? -5.905  45.304  -10.434 1.00 44.45  ? 336  HIS D CG  1 
ATOM   11459 N  ND1 . HIS D 1 336 ? -5.363  45.576  -9.195  1.00 43.60  ? 336  HIS D ND1 1 
ATOM   11460 C  CD2 . HIS D 1 336 ? -5.326  44.154  -10.856 1.00 39.56  ? 336  HIS D CD2 1 
ATOM   11461 C  CE1 . HIS D 1 336 ? -4.483  44.640  -8.886  1.00 42.73  ? 336  HIS D CE1 1 
ATOM   11462 N  NE2 . HIS D 1 336 ? -4.444  43.764  -9.876  1.00 51.31  ? 336  HIS D NE2 1 
ATOM   11463 N  N   . ILE D 1 337 ? -10.442 46.494  -11.633 1.00 32.66  ? 337  ILE D N   1 
ATOM   11464 C  CA  . ILE D 1 337 ? -11.461 47.389  -12.161 1.00 30.93  ? 337  ILE D CA  1 
ATOM   11465 C  C   . ILE D 1 337 ? -12.314 47.939  -11.042 1.00 34.76  ? 337  ILE D C   1 
ATOM   11466 O  O   . ILE D 1 337 ? -12.272 47.443  -9.918  1.00 48.87  ? 337  ILE D O   1 
ATOM   11467 C  CB  . ILE D 1 337 ? -12.380 46.726  -13.242 1.00 48.80  ? 337  ILE D CB  1 
ATOM   11468 C  CG1 . ILE D 1 337 ? -13.171 45.554  -12.654 1.00 50.54  ? 337  ILE D CG1 1 
ATOM   11469 C  CG2 . ILE D 1 337 ? -11.579 46.297  -14.485 1.00 40.56  ? 337  ILE D CG2 1 
ATOM   11470 C  CD1 . ILE D 1 337 ? -14.130 44.896  -13.659 1.00 39.71  ? 337  ILE D CD1 1 
ATOM   11471 N  N   . GLY D 1 338 ? -13.082 48.978  -11.354 1.00 42.65  ? 338  GLY D N   1 
ATOM   11472 C  CA  . GLY D 1 338 ? -13.984 49.563  -10.386 1.00 37.20  ? 338  GLY D CA  1 
ATOM   11473 C  C   . GLY D 1 338 ? -13.248 50.475  -9.444  1.00 22.92  ? 338  GLY D C   1 
ATOM   11474 O  O   . GLY D 1 338 ? -12.456 51.322  -9.857  1.00 41.35  ? 338  GLY D O   1 
ATOM   11475 N  N   . ILE D 1 339 ? -13.518 50.316  -8.165  1.00 22.65  ? 339  ILE D N   1 
ATOM   11476 C  CA  . ILE D 1 339 ? -12.906 51.191  -7.187  1.00 35.01  ? 339  ILE D CA  1 
ATOM   11477 C  C   . ILE D 1 339 ? -12.427 50.386  -6.002  1.00 36.81  ? 339  ILE D C   1 
ATOM   11478 O  O   . ILE D 1 339 ? -12.689 49.186  -5.895  1.00 44.00  ? 339  ILE D O   1 
ATOM   11479 C  CB  . ILE D 1 339 ? -13.908 52.228  -6.673  1.00 33.85  ? 339  ILE D CB  1 
ATOM   11480 C  CG1 . ILE D 1 339 ? -15.202 51.511  -6.256  1.00 36.30  ? 339  ILE D CG1 1 
ATOM   11481 C  CG2 . ILE D 1 339 ? -14.152 53.310  -7.734  1.00 25.91  ? 339  ILE D CG2 1 
ATOM   11482 C  CD1 . ILE D 1 339 ? -16.173 52.363  -5.489  1.00 28.77  ? 339  ILE D CD1 1 
ATOM   11483 N  N   . LYS D 1 340 ? -11.712 51.050  -5.113  1.00 28.48  ? 340  LYS D N   1 
ATOM   11484 C  CA  . LYS D 1 340 ? -11.369 50.447  -3.843  1.00 33.52  ? 340  LYS D CA  1 
ATOM   11485 C  C   . LYS D 1 340 ? -11.071 51.572  -2.864  1.00 46.82  ? 340  LYS D C   1 
ATOM   11486 O  O   . LYS D 1 340 ? -10.850 52.725  -3.285  1.00 42.98  ? 340  LYS D O   1 
ATOM   11487 C  CB  . LYS D 1 340 ? -10.167 49.527  -4.000  1.00 33.75  ? 340  LYS D CB  1 
ATOM   11488 C  CG  . LYS D 1 340 ? -8.917  50.224  -4.496  1.00 33.90  ? 340  LYS D CG  1 
ATOM   11489 C  CD  . LYS D 1 340 ? -7.711  49.302  -4.391  1.00 22.69  ? 340  LYS D CD  1 
ATOM   11490 C  CE  . LYS D 1 340 ? -6.585  49.785  -5.274  1.00 25.93  ? 340  LYS D CE  1 
ATOM   11491 N  NZ  . LYS D 1 340 ? -5.416  48.859  -5.217  1.00 31.89  ? 340  LYS D NZ  1 
ATOM   11492 N  N   . GLY D 1 341 ? -11.076 51.255  -1.568  1.00 30.24  ? 341  GLY D N   1 
ATOM   11493 C  CA  . GLY D 1 341 ? -10.830 52.275  -0.565  1.00 32.57  ? 341  GLY D CA  1 
ATOM   11494 C  C   . GLY D 1 341 ? -11.014 51.830  0.865   1.00 35.00  ? 341  GLY D C   1 
ATOM   11495 O  O   . GLY D 1 341 ? -11.012 50.636  1.165   1.00 30.84  ? 341  GLY D O   1 
ATOM   11496 N  N   . LEU D 1 342 ? -11.181 52.803  1.755   1.00 40.36  ? 342  LEU D N   1 
ATOM   11497 C  CA  . LEU D 1 342 ? -11.307 52.509  3.169   1.00 38.15  ? 342  LEU D CA  1 
ATOM   11498 C  C   . LEU D 1 342 ? -12.594 53.088  3.762   1.00 33.65  ? 342  LEU D C   1 
ATOM   11499 O  O   . LEU D 1 342 ? -13.042 54.162  3.386   1.00 41.73  ? 342  LEU D O   1 
ATOM   11500 C  CB  . LEU D 1 342 ? -10.072 53.024  3.916   1.00 29.95  ? 342  LEU D CB  1 
ATOM   11501 C  CG  . LEU D 1 342 ? -8.739  52.540  3.348   1.00 23.87  ? 342  LEU D CG  1 
ATOM   11502 C  CD1 . LEU D 1 342 ? -7.616  53.332  3.963   1.00 21.36  ? 342  LEU D CD1 1 
ATOM   11503 C  CD2 . LEU D 1 342 ? -8.550  51.031  3.570   1.00 20.32  ? 342  LEU D CD2 1 
ATOM   11504 N  N   . VAL D 1 343 ? -13.193 52.350  4.682   1.00 36.01  ? 343  VAL D N   1 
ATOM   11505 C  CA  . VAL D 1 343 ? -14.211 52.903  5.547   1.00 30.86  ? 343  VAL D CA  1 
ATOM   11506 C  C   . VAL D 1 343 ? -13.552 53.013  6.899   1.00 33.17  ? 343  VAL D C   1 
ATOM   11507 O  O   . VAL D 1 343 ? -13.139 52.009  7.487   1.00 38.10  ? 343  VAL D O   1 
ATOM   11508 C  CB  . VAL D 1 343 ? -15.445 51.993  5.642   1.00 36.38  ? 343  VAL D CB  1 
ATOM   11509 C  CG1 . VAL D 1 343 ? -16.419 52.528  6.669   1.00 26.07  ? 343  VAL D CG1 1 
ATOM   11510 C  CG2 . VAL D 1 343 ? -16.121 51.882  4.284   1.00 33.84  ? 343  VAL D CG2 1 
ATOM   11511 N  N   . THR D 1 344 ? -13.450 54.236  7.398   1.00 47.89  ? 344  THR D N   1 
ATOM   11512 C  CA  . THR D 1 344 ? -12.584 54.496  8.532   1.00 49.48  ? 344  THR D CA  1 
ATOM   11513 C  C   . THR D 1 344 ? -13.271 55.306  9.625   1.00 51.35  ? 344  THR D C   1 
ATOM   11514 O  O   . THR D 1 344 ? -14.320 55.922  9.389   1.00 45.10  ? 344  THR D O   1 
ATOM   11515 C  CB  . THR D 1 344 ? -11.304 55.231  8.062   1.00 58.61  ? 344  THR D CB  1 
ATOM   11516 O  OG1 . THR D 1 344 ? -10.296 55.161  9.080   1.00 74.37  ? 344  THR D OG1 1 
ATOM   11517 C  CG2 . THR D 1 344 ? -11.612 56.703  7.707   1.00 41.17  ? 344  THR D CG2 1 
ATOM   11518 N  N   . ASP D 1 345 ? -12.663 55.277  10.815  1.00 64.84  ? 345  ASP D N   1 
ATOM   11519 C  CA  . ASP D 1 345 ? -13.074 56.066  11.976  1.00 52.84  ? 345  ASP D CA  1 
ATOM   11520 C  C   . ASP D 1 345 ? -12.965 57.531  11.635  1.00 60.95  ? 345  ASP D C   1 
ATOM   11521 O  O   . ASP D 1 345 ? -12.371 57.898  10.621  1.00 52.40  ? 345  ASP D O   1 
ATOM   11522 C  CB  . ASP D 1 345 ? -12.120 55.809  13.153  1.00 40.66  ? 345  ASP D CB  1 
ATOM   11523 C  CG  . ASP D 1 345 ? -12.840 55.393  14.427  1.00 59.87  ? 345  ASP D CG  1 
ATOM   11524 O  OD1 . ASP D 1 345 ? -12.159 54.938  15.367  1.00 75.47  ? 345  ASP D OD1 1 
ATOM   11525 O  OD2 . ASP D 1 345 ? -14.079 55.510  14.501  1.00 64.77  ? 345  ASP D OD2 1 
ATOM   11526 N  N   . ALA D 1 346 ? -13.540 58.371  12.489  1.00 75.85  ? 346  ALA D N   1 
ATOM   11527 C  CA  . ALA D 1 346 ? -13.167 59.767  12.502  1.00 58.28  ? 346  ALA D CA  1 
ATOM   11528 C  C   . ALA D 1 346 ? -11.705 59.700  12.905  1.00 53.33  ? 346  ALA D C   1 
ATOM   11529 O  O   . ALA D 1 346 ? -10.867 60.407  12.352  1.00 52.12  ? 346  ALA D O   1 
ATOM   11530 C  CB  . ALA D 1 346 ? -13.988 60.531  13.524  1.00 58.75  ? 346  ALA D CB  1 
ATOM   11531 N  N   . SER D 1 347 ? -11.403 58.794  13.840  1.00 67.24  ? 347  SER D N   1 
ATOM   11532 C  CA  . SER D 1 347 ? -10.031 58.542  14.286  1.00 76.16  ? 347  SER D CA  1 
ATOM   11533 C  C   . SER D 1 347 ? -9.094  58.305  13.091  1.00 73.49  ? 347  SER D C   1 
ATOM   11534 O  O   . SER D 1 347 ? -7.873  58.442  13.204  1.00 57.98  ? 347  SER D O   1 
ATOM   11535 C  CB  . SER D 1 347 ? -9.977  57.327  15.239  1.00 74.23  ? 347  SER D CB  1 
ATOM   11536 O  OG  . SER D 1 347 ? -10.547 57.589  16.518  1.00 74.58  ? 347  SER D OG  1 
ATOM   11537 N  N   . GLY D 1 348 ? -9.675  57.962  11.944  1.00 58.76  ? 348  GLY D N   1 
ATOM   11538 C  CA  . GLY D 1 348 ? -8.909  57.436  10.830  1.00 33.62  ? 348  GLY D CA  1 
ATOM   11539 C  C   . GLY D 1 348 ? -8.652  55.945  11.048  1.00 54.13  ? 348  GLY D C   1 
ATOM   11540 O  O   . GLY D 1 348 ? -7.769  55.352  10.419  1.00 61.41  ? 348  GLY D O   1 
ATOM   11541 N  N   . PHE D 1 349 ? -9.428  55.331  11.943  1.00 44.17  ? 349  PHE D N   1 
ATOM   11542 C  CA  . PHE D 1 349 ? -9.248  53.917  12.256  1.00 39.16  ? 349  PHE D CA  1 
ATOM   11543 C  C   . PHE D 1 349 ? -10.299 53.014  11.610  1.00 35.69  ? 349  PHE D C   1 
ATOM   11544 O  O   . PHE D 1 349 ? -11.495 53.207  11.810  1.00 25.79  ? 349  PHE D O   1 
ATOM   11545 C  CB  . PHE D 1 349 ? -9.215  53.663  13.765  1.00 28.07  ? 349  PHE D CB  1 
ATOM   11546 C  CG  . PHE D 1 349 ? -8.765  52.281  14.110  1.00 30.52  ? 349  PHE D CG  1 
ATOM   11547 C  CD1 . PHE D 1 349 ? -7.446  52.035  14.424  1.00 22.27  ? 349  PHE D CD1 1 
ATOM   11548 C  CD2 . PHE D 1 349 ? -9.649  51.210  14.048  1.00 26.44  ? 349  PHE D CD2 1 
ATOM   11549 C  CE1 . PHE D 1 349 ? -7.018  50.747  14.718  1.00 47.17  ? 349  PHE D CE1 1 
ATOM   11550 C  CE2 . PHE D 1 349 ? -9.225  49.927  14.340  1.00 30.46  ? 349  PHE D CE2 1 
ATOM   11551 C  CZ  . PHE D 1 349 ? -7.905  49.694  14.673  1.00 21.14  ? 349  PHE D CZ  1 
ATOM   11552 N  N   . PRO D 1 350 ? -9.838  51.986  10.880  1.00 37.67  ? 350  PRO D N   1 
ATOM   11553 C  CA  . PRO D 1 350 ? -10.666 51.158  9.996   1.00 41.49  ? 350  PRO D CA  1 
ATOM   11554 C  C   . PRO D 1 350 ? -11.888 50.572  10.689  1.00 43.70  ? 350  PRO D C   1 
ATOM   11555 O  O   . PRO D 1 350 ? -11.825 50.158  11.860  1.00 37.75  ? 350  PRO D O   1 
ATOM   11556 C  CB  . PRO D 1 350 ? -9.712  50.020  9.578   1.00 36.94  ? 350  PRO D CB  1 
ATOM   11557 C  CG  . PRO D 1 350 ? -8.709  49.944  10.668  1.00 36.99  ? 350  PRO D CG  1 
ATOM   11558 C  CD  . PRO D 1 350 ? -8.507  51.392  11.076  1.00 39.21  ? 350  PRO D CD  1 
ATOM   11559 N  N   . ILE D 1 351 ? -12.993 50.539  9.949   1.00 42.09  ? 351  ILE D N   1 
ATOM   11560 C  CA  . ILE D 1 351 ? -14.199 49.853  10.395  1.00 34.63  ? 351  ILE D CA  1 
ATOM   11561 C  C   . ILE D 1 351 ? -14.358 48.533  9.644   1.00 38.58  ? 351  ILE D C   1 
ATOM   11562 O  O   . ILE D 1 351 ? -14.393 48.498  8.406   1.00 34.69  ? 351  ILE D O   1 
ATOM   11563 C  CB  . ILE D 1 351 ? -15.450 50.710  10.178  1.00 35.28  ? 351  ILE D CB  1 
ATOM   11564 C  CG1 . ILE D 1 351 ? -15.255 52.105  10.774  1.00 34.56  ? 351  ILE D CG1 1 
ATOM   11565 C  CG2 . ILE D 1 351 ? -16.638 50.039  10.818  1.00 33.22  ? 351  ILE D CG2 1 
ATOM   11566 C  CD1 . ILE D 1 351 ? -16.324 53.084  10.378  1.00 35.05  ? 351  ILE D CD1 1 
ATOM   11567 N  N   . ALA D 1 352 ? -14.444 47.448  10.402  1.00 38.47  ? 352  ALA D N   1 
ATOM   11568 C  CA  . ALA D 1 352 ? -14.540 46.111  9.821   1.00 39.89  ? 352  ALA D CA  1 
ATOM   11569 C  C   . ALA D 1 352 ? -15.987 45.757  9.583   1.00 37.60  ? 352  ALA D C   1 
ATOM   11570 O  O   . ALA D 1 352 ? -16.848 46.142  10.358  1.00 40.80  ? 352  ALA D O   1 
ATOM   11571 C  CB  . ALA D 1 352 ? -13.892 45.072  10.752  1.00 28.23  ? 352  ALA D CB  1 
ATOM   11572 N  N   . ASP D 1 353 ? -16.256 45.014  8.517   1.00 37.76  ? 353  ASP D N   1 
ATOM   11573 C  CA  . ASP D 1 353 ? -17.611 44.553  8.254   1.00 36.01  ? 353  ASP D CA  1 
ATOM   11574 C  C   . ASP D 1 353 ? -18.589 45.694  7.978   1.00 35.95  ? 353  ASP D C   1 
ATOM   11575 O  O   . ASP D 1 353 ? -19.798 45.524  8.106   1.00 45.08  ? 353  ASP D O   1 
ATOM   11576 C  CB  . ASP D 1 353 ? -18.119 43.722  9.429   1.00 51.73  ? 353  ASP D CB  1 
ATOM   11577 C  CG  . ASP D 1 353 ? -18.192 42.247  9.108   1.00 71.49  ? 353  ASP D CG  1 
ATOM   11578 O  OD1 . ASP D 1 353 ? -19.288 41.771  8.733   1.00 76.79  ? 353  ASP D OD1 1 
ATOM   11579 O  OD2 . ASP D 1 353 ? -17.149 41.570  9.222   1.00 80.92  ? 353  ASP D OD2 1 
ATOM   11580 N  N   . ALA D 1 354 ? -18.073 46.860  7.617   1.00 30.65  ? 354  ALA D N   1 
ATOM   11581 C  CA  . ALA D 1 354 ? -18.933 47.923  7.128   1.00 40.42  ? 354  ALA D CA  1 
ATOM   11582 C  C   . ALA D 1 354 ? -19.513 47.511  5.771   1.00 46.01  ? 354  ALA D C   1 
ATOM   11583 O  O   . ALA D 1 354 ? -18.995 46.606  5.111   1.00 42.11  ? 354  ALA D O   1 
ATOM   11584 C  CB  . ALA D 1 354 ? -18.147 49.219  6.995   1.00 42.81  ? 354  ALA D CB  1 
ATOM   11585 N  N   . ASN D 1 355 ? -20.583 48.175  5.346   1.00 40.00  ? 355  ASN D N   1 
ATOM   11586 C  CA  . ASN D 1 355 ? -21.155 47.894  4.031   1.00 43.74  ? 355  ASN D CA  1 
ATOM   11587 C  C   . ASN D 1 355 ? -20.997 49.051  3.049   1.00 50.75  ? 355  ASN D C   1 
ATOM   11588 O  O   . ASN D 1 355 ? -21.318 50.201  3.367   1.00 52.22  ? 355  ASN D O   1 
ATOM   11589 C  CB  . ASN D 1 355 ? -22.628 47.495  4.139   1.00 52.16  ? 355  ASN D CB  1 
ATOM   11590 C  CG  . ASN D 1 355 ? -22.808 46.070  4.620   1.00 55.92  ? 355  ASN D CG  1 
ATOM   11591 O  OD1 . ASN D 1 355 ? -23.423 45.819  5.660   1.00 58.82  ? 355  ASN D OD1 1 
ATOM   11592 N  ND2 . ASN D 1 355 ? -22.265 45.124  3.866   1.00 62.76  ? 355  ASN D ND2 1 
ATOM   11593 N  N   . VAL D 1 356 ? -20.497 48.735  1.857   1.00 43.48  ? 356  VAL D N   1 
ATOM   11594 C  CA  . VAL D 1 356 ? -20.350 49.722  0.797   1.00 44.51  ? 356  VAL D CA  1 
ATOM   11595 C  C   . VAL D 1 356 ? -21.340 49.464  -0.348  1.00 43.88  ? 356  VAL D C   1 
ATOM   11596 O  O   . VAL D 1 356 ? -21.272 48.432  -1.034  1.00 36.25  ? 356  VAL D O   1 
ATOM   11597 C  CB  . VAL D 1 356 ? -18.911 49.735  0.278   1.00 45.88  ? 356  VAL D CB  1 
ATOM   11598 C  CG1 . VAL D 1 356 ? -18.777 50.687  -0.899  1.00 41.53  ? 356  VAL D CG1 1 
ATOM   11599 C  CG2 . VAL D 1 356 ? -17.966 50.119  1.414   1.00 35.77  ? 356  VAL D CG2 1 
ATOM   11600 N  N   . TYR D 1 357 ? -22.265 50.402  -0.541  1.00 41.48  ? 357  TYR D N   1 
ATOM   11601 C  CA  . TYR D 1 357 ? -23.325 50.233  -1.537  1.00 44.39  ? 357  TYR D CA  1 
ATOM   11602 C  C   . TYR D 1 357 ? -23.129 51.079  -2.799  1.00 45.61  ? 357  TYR D C   1 
ATOM   11603 O  O   . TYR D 1 357 ? -22.654 52.210  -2.724  1.00 48.24  ? 357  TYR D O   1 
ATOM   11604 C  CB  . TYR D 1 357 ? -24.672 50.611  -0.938  1.00 39.41  ? 357  TYR D CB  1 
ATOM   11605 C  CG  . TYR D 1 357 ? -25.232 49.668  0.095   1.00 45.14  ? 357  TYR D CG  1 
ATOM   11606 C  CD1 . TYR D 1 357 ? -25.004 49.875  1.459   1.00 40.91  ? 357  TYR D CD1 1 
ATOM   11607 C  CD2 . TYR D 1 357 ? -26.033 48.596  -0.289  1.00 49.27  ? 357  TYR D CD2 1 
ATOM   11608 C  CE1 . TYR D 1 357 ? -25.538 49.019  2.412   1.00 41.56  ? 357  TYR D CE1 1 
ATOM   11609 C  CE2 . TYR D 1 357 ? -26.570 47.736  0.654   1.00 44.39  ? 357  TYR D CE2 1 
ATOM   11610 C  CZ  . TYR D 1 357 ? -26.315 47.949  2.000   1.00 43.05  ? 357  TYR D CZ  1 
ATOM   11611 O  OH  . TYR D 1 357 ? -26.855 47.092  2.925   1.00 57.53  ? 357  TYR D OH  1 
ATOM   11612 N  N   . VAL D 1 358 ? -23.526 50.536  -3.949  1.00 54.70  ? 358  VAL D N   1 
ATOM   11613 C  CA  . VAL D 1 358 ? -23.581 51.298  -5.205  1.00 49.85  ? 358  VAL D CA  1 
ATOM   11614 C  C   . VAL D 1 358 ? -25.028 51.383  -5.714  1.00 54.60  ? 358  VAL D C   1 
ATOM   11615 O  O   . VAL D 1 358 ? -25.709 50.356  -5.842  1.00 53.88  ? 358  VAL D O   1 
ATOM   11616 C  CB  . VAL D 1 358 ? -22.705 50.652  -6.314  1.00 36.01  ? 358  VAL D CB  1 
ATOM   11617 C  CG1 . VAL D 1 358 ? -22.834 51.416  -7.606  1.00 35.04  ? 358  VAL D CG1 1 
ATOM   11618 C  CG2 . VAL D 1 358 ? -21.246 50.586  -5.891  1.00 35.55  ? 358  VAL D CG2 1 
ATOM   11619 N  N   . ALA D 1 359 ? -25.499 52.599  -5.994  1.00 49.86  ? 359  ALA D N   1 
ATOM   11620 C  CA  . ALA D 1 359 ? -26.867 52.798  -6.467  1.00 47.03  ? 359  ALA D CA  1 
ATOM   11621 C  C   . ALA D 1 359 ? -27.177 51.870  -7.625  1.00 37.45  ? 359  ALA D C   1 
ATOM   11622 O  O   . ALA D 1 359 ? -26.500 51.895  -8.653  1.00 44.29  ? 359  ALA D O   1 
ATOM   11623 C  CB  . ALA D 1 359 ? -27.079 54.235  -6.890  1.00 55.51  ? 359  ALA D CB  1 
ATOM   11624 N  N   . GLY D 1 360 ? -28.201 51.046  -7.462  1.00 36.29  ? 360  GLY D N   1 
ATOM   11625 C  CA  . GLY D 1 360 ? -28.607 50.146  -8.524  1.00 32.59  ? 360  GLY D CA  1 
ATOM   11626 C  C   . GLY D 1 360 ? -27.933 48.808  -8.369  1.00 36.25  ? 360  GLY D C   1 
ATOM   11627 O  O   . GLY D 1 360 ? -28.183 47.889  -9.137  1.00 56.57  ? 360  GLY D O   1 
ATOM   11628 N  N   . LEU D 1 361 ? -27.065 48.708  -7.372  1.00 34.21  ? 361  LEU D N   1 
ATOM   11629 C  CA  . LEU D 1 361 ? -26.354 47.469  -7.074  1.00 41.70  ? 361  LEU D CA  1 
ATOM   11630 C  C   . LEU D 1 361 ? -26.386 47.212  -5.565  1.00 44.72  ? 361  LEU D C   1 
ATOM   11631 O  O   . LEU D 1 361 ? -25.551 46.490  -5.017  1.00 34.66  ? 361  LEU D O   1 
ATOM   11632 C  CB  . LEU D 1 361 ? -24.907 47.539  -7.574  1.00 31.50  ? 361  LEU D CB  1 
ATOM   11633 C  CG  . LEU D 1 361 ? -24.679 47.610  -9.084  1.00 32.72  ? 361  LEU D CG  1 
ATOM   11634 C  CD1 . LEU D 1 361 ? -23.211 47.888  -9.388  1.00 33.30  ? 361  LEU D CD1 1 
ATOM   11635 C  CD2 . LEU D 1 361 ? -25.108 46.323  -9.744  1.00 34.04  ? 361  LEU D CD2 1 
ATOM   11636 N  N   . GLU D 1 362 ? -27.371 47.808  -4.903  1.00 52.39  ? 362  GLU D N   1 
ATOM   11637 C  CA  . GLU D 1 362 ? -27.462 47.761  -3.450  1.00 43.89  ? 362  GLU D CA  1 
ATOM   11638 C  C   . GLU D 1 362 ? -27.826 46.381  -2.927  1.00 49.70  ? 362  GLU D C   1 
ATOM   11639 O  O   . GLU D 1 362 ? -27.775 46.141  -1.721  1.00 51.47  ? 362  GLU D O   1 
ATOM   11640 C  CB  . GLU D 1 362 ? -28.471 48.787  -2.942  1.00 45.76  ? 362  GLU D CB  1 
ATOM   11641 C  CG  . GLU D 1 362 ? -27.890 50.169  -2.722  1.00 60.43  ? 362  GLU D CG  1 
ATOM   11642 C  CD  . GLU D 1 362 ? -28.749 51.263  -3.338  1.00 83.86  ? 362  GLU D CD  1 
ATOM   11643 O  OE1 . GLU D 1 362 ? -29.388 50.996  -4.385  1.00 86.50  ? 362  GLU D OE1 1 
ATOM   11644 O  OE2 . GLU D 1 362 ? -28.779 52.387  -2.782  1.00 85.26  ? 362  GLU D OE2 1 
ATOM   11645 N  N   . GLU D 1 363 ? -28.200 45.471  -3.819  1.00 46.55  ? 363  GLU D N   1 
ATOM   11646 C  CA  . GLU D 1 363 ? -28.492 44.111  -3.375  1.00 40.88  ? 363  GLU D CA  1 
ATOM   11647 C  C   . GLU D 1 363 ? -27.211 43.335  -3.133  1.00 42.01  ? 363  GLU D C   1 
ATOM   11648 O  O   . GLU D 1 363 ? -27.223 42.278  -2.489  1.00 46.08  ? 363  GLU D O   1 
ATOM   11649 C  CB  . GLU D 1 363 ? -29.382 43.374  -4.372  1.00 48.63  ? 363  GLU D CB  1 
ATOM   11650 C  CG  . GLU D 1 363 ? -30.838 43.768  -4.290  1.00 73.22  ? 363  GLU D CG  1 
ATOM   11651 C  CD  . GLU D 1 363 ? -31.720 42.921  -5.187  1.00 91.08  ? 363  GLU D CD  1 
ATOM   11652 O  OE1 . GLU D 1 363 ? -31.423 42.833  -6.401  1.00 91.99  ? 363  GLU D OE1 1 
ATOM   11653 O  OE2 . GLU D 1 363 ? -32.714 42.348  -4.681  1.00 97.88  ? 363  GLU D OE2 1 
ATOM   11654 N  N   . LYS D 1 364 ? -26.103 43.863  -3.651  1.00 35.05  ? 364  LYS D N   1 
ATOM   11655 C  CA  . LYS D 1 364 ? -24.796 43.234  -3.460  1.00 35.40  ? 364  LYS D CA  1 
ATOM   11656 C  C   . LYS D 1 364 ? -23.787 44.248  -2.936  1.00 44.14  ? 364  LYS D C   1 
ATOM   11657 O  O   . LYS D 1 364 ? -22.950 44.763  -3.685  1.00 56.89  ? 364  LYS D O   1 
ATOM   11658 C  CB  . LYS D 1 364 ? -24.291 42.589  -4.758  1.00 40.51  ? 364  LYS D CB  1 
ATOM   11659 C  CG  . LYS D 1 364 ? -22.964 41.836  -4.616  1.00 39.37  ? 364  LYS D CG  1 
ATOM   11660 C  CD  . LYS D 1 364 ? -23.045 40.817  -3.487  1.00 37.98  ? 364  LYS D CD  1 
ATOM   11661 C  CE  . LYS D 1 364 ? -21.798 39.965  -3.402  1.00 31.89  ? 364  LYS D CE  1 
ATOM   11662 N  NZ  . LYS D 1 364 ? -21.909 39.095  -2.208  1.00 23.58  ? 364  LYS D NZ  1 
ATOM   11663 N  N   . PRO D 1 365 ? -23.874 44.544  -1.636  1.00 44.43  ? 365  PRO D N   1 
ATOM   11664 C  CA  . PRO D 1 365 ? -22.925 45.404  -0.927  1.00 43.89  ? 365  PRO D CA  1 
ATOM   11665 C  C   . PRO D 1 365 ? -21.601 44.680  -0.737  1.00 42.89  ? 365  PRO D C   1 
ATOM   11666 O  O   . PRO D 1 365 ? -21.566 43.452  -0.755  1.00 45.14  ? 365  PRO D O   1 
ATOM   11667 C  CB  . PRO D 1 365 ? -23.575 45.592  0.455   1.00 50.49  ? 365  PRO D CB  1 
ATOM   11668 C  CG  . PRO D 1 365 ? -24.915 44.912  0.392   1.00 47.28  ? 365  PRO D CG  1 
ATOM   11669 C  CD  . PRO D 1 365 ? -24.868 43.945  -0.733  1.00 49.88  ? 365  PRO D CD  1 
ATOM   11670 N  N   . MET D 1 366 ? -20.524 45.431  -0.544  1.00 43.53  ? 366  MET D N   1 
ATOM   11671 C  CA  . MET D 1 366 ? -19.249 44.834  -0.161  1.00 31.32  ? 366  MET D CA  1 
ATOM   11672 C  C   . MET D 1 366 ? -19.063 44.977  1.347   1.00 37.39  ? 366  MET D C   1 
ATOM   11673 O  O   . MET D 1 366 ? -19.363 46.032  1.941   1.00 37.82  ? 366  MET D O   1 
ATOM   11674 C  CB  . MET D 1 366 ? -18.083 45.487  -0.914  1.00 41.66  ? 366  MET D CB  1 
ATOM   11675 C  CG  . MET D 1 366 ? -18.113 45.301  -2.442  1.00 32.41  ? 366  MET D CG  1 
ATOM   11676 S  SD  . MET D 1 366 ? -17.962 43.566  -2.921  1.00 50.05  ? 366  MET D SD  1 
ATOM   11677 C  CE  . MET D 1 366 ? -19.646 43.127  -3.343  1.00 40.99  ? 366  MET D CE  1 
ATOM   11678 N  N   . ARG D 1 367 ? -18.586 43.904  1.967   1.00 33.20  ? 367  ARG D N   1 
ATOM   11679 C  CA  . ARG D 1 367 ? -18.296 43.907  3.390   1.00 32.92  ? 367  ARG D CA  1 
ATOM   11680 C  C   . ARG D 1 367 ? -16.798 44.103  3.596   1.00 33.09  ? 367  ARG D C   1 
ATOM   11681 O  O   . ARG D 1 367 ? -15.986 43.300  3.151   1.00 58.26  ? 367  ARG D O   1 
ATOM   11682 C  CB  . ARG D 1 367 ? -18.786 42.605  4.010   1.00 46.38  ? 367  ARG D CB  1 
ATOM   11683 C  CG  . ARG D 1 367 ? -18.492 42.456  5.476   1.00 62.00  ? 367  ARG D CG  1 
ATOM   11684 C  CD  . ARG D 1 367 ? -17.277 41.559  5.669   1.00 70.23  ? 367  ARG D CD  1 
ATOM   11685 N  NE  . ARG D 1 367 ? -17.523 40.619  6.741   1.00 79.95  ? 367  ARG D NE  1 
ATOM   11686 C  CZ  . ARG D 1 367 ? -17.545 39.295  6.650   1.00 88.25  ? 367  ARG D CZ  1 
ATOM   11687 N  NH1 . ARG D 1 367 ? -17.294 38.658  5.511   1.00 97.83  ? 367  ARG D NH1 1 
ATOM   11688 N  NH2 . ARG D 1 367 ? -17.809 38.603  7.745   1.00 82.74  ? 367  ARG D NH2 1 
ATOM   11689 N  N   . THR D 1 368 ? -16.427 45.194  4.244   1.00 29.21  ? 368  THR D N   1 
ATOM   11690 C  CA  . THR D 1 368 ? -15.025 45.534  4.375   1.00 26.88  ? 368  THR D CA  1 
ATOM   11691 C  C   . THR D 1 368 ? -14.293 44.534  5.245   1.00 22.21  ? 368  THR D C   1 
ATOM   11692 O  O   . THR D 1 368 ? -14.866 43.918  6.127   1.00 19.75  ? 368  THR D O   1 
ATOM   11693 C  CB  . THR D 1 368 ? -14.844 46.901  5.000   1.00 21.11  ? 368  THR D CB  1 
ATOM   11694 O  OG1 . THR D 1 368 ? -15.207 46.836  6.392   1.00 30.50  ? 368  THR D OG1 1 
ATOM   11695 C  CG2 . THR D 1 368 ? -15.717 47.910  4.266   1.00 29.11  ? 368  THR D CG2 1 
ATOM   11696 N  N   . SER D 1 369 ? -13.003 44.406  4.980   1.00 26.83  ? 369  SER D N   1 
ATOM   11697 C  CA  . SER D 1 369 ? -12.122 43.550  5.738   1.00 28.15  ? 369  SER D CA  1 
ATOM   11698 C  C   . SER D 1 369 ? -11.835 44.128  7.126   1.00 38.36  ? 369  SER D C   1 
ATOM   11699 O  O   . SER D 1 369 ? -12.298 45.223  7.477   1.00 42.42  ? 369  SER D O   1 
ATOM   11700 C  CB  . SER D 1 369 ? -10.809 43.419  4.982   1.00 28.99  ? 369  SER D CB  1 
ATOM   11701 O  OG  . SER D 1 369 ? -10.101 44.655  5.020   1.00 28.31  ? 369  SER D OG  1 
ATOM   11702 N  N   . LYS D 1 370 ? -11.049 43.387  7.905   1.00 35.93  ? 370  LYS D N   1 
ATOM   11703 C  CA  . LYS D 1 370 ? -10.655 43.812  9.250   1.00 36.78  ? 370  LYS D CA  1 
ATOM   11704 C  C   . LYS D 1 370 ? -9.929  45.168  9.243   1.00 37.80  ? 370  LYS D C   1 
ATOM   11705 O  O   . LYS D 1 370 ? -9.947  45.899  10.227  1.00 53.07  ? 370  LYS D O   1 
ATOM   11706 C  CB  . LYS D 1 370 ? -9.785  42.742  9.923   1.00 27.20  ? 370  LYS D CB  1 
ATOM   11707 C  CG  . LYS D 1 370 ? -10.548 41.488  10.345  1.00 24.01  ? 370  LYS D CG  1 
ATOM   11708 C  CD  . LYS D 1 370 ? -9.614  40.313  10.632  1.00 20.95  ? 370  LYS D CD  1 
ATOM   11709 C  CE  . LYS D 1 370 ? -10.392 39.002  10.733  1.00 26.52  ? 370  LYS D CE  1 
ATOM   11710 N  NZ  . LYS D 1 370 ? -9.591  37.892  11.329  1.00 38.45  ? 370  LYS D NZ  1 
ATOM   11711 N  N   . ARG D 1 371 ? -9.287  45.503  8.134   1.00 28.48  ? 371  ARG D N   1 
ATOM   11712 C  CA  . ARG D 1 371 ? -8.630  46.789  8.016   1.00 29.06  ? 371  ARG D CA  1 
ATOM   11713 C  C   . ARG D 1 371 ? -9.557  47.784  7.301   1.00 38.77  ? 371  ARG D C   1 
ATOM   11714 O  O   . ARG D 1 371 ? -9.125  48.837  6.820   1.00 39.43  ? 371  ARG D O   1 
ATOM   11715 C  CB  . ARG D 1 371 ? -7.329  46.632  7.241   1.00 32.96  ? 371  ARG D CB  1 
ATOM   11716 C  CG  . ARG D 1 371 ? -6.422  45.524  7.718   1.00 23.93  ? 371  ARG D CG  1 
ATOM   11717 C  CD  . ARG D 1 371 ? -5.001  45.817  7.256   1.00 37.74  ? 371  ARG D CD  1 
ATOM   11718 N  NE  . ARG D 1 371 ? -4.282  44.590  7.013   1.00 50.66  ? 371  ARG D NE  1 
ATOM   11719 C  CZ  . ARG D 1 371 ? -3.748  44.199  5.865   1.00 61.33  ? 371  ARG D CZ  1 
ATOM   11720 N  NH1 . ARG D 1 371 ? -3.793  44.955  4.781   1.00 55.92  ? 371  ARG D NH1 1 
ATOM   11721 N  NH2 . ARG D 1 371 ? -3.143  43.024  5.831   1.00 73.16  ? 371  ARG D NH2 1 
ATOM   11722 N  N   . GLY D 1 372 ? -10.839 47.440  7.221   1.00 43.07  ? 372  GLY D N   1 
ATOM   11723 C  CA  . GLY D 1 372 ? -11.820 48.328  6.620   1.00 49.72  ? 372  GLY D CA  1 
ATOM   11724 C  C   . GLY D 1 372 ? -11.618 48.579  5.135   1.00 40.68  ? 372  GLY D C   1 
ATOM   11725 O  O   . GLY D 1 372 ? -12.005 49.639  4.627   1.00 29.61  ? 372  GLY D O   1 
ATOM   11726 N  N   . GLU D 1 373 ? -11.031 47.608  4.435   1.00 31.52  ? 373  GLU D N   1 
ATOM   11727 C  CA  . GLU D 1 373 ? -10.829 47.748  2.997   1.00 35.73  ? 373  GLU D CA  1 
ATOM   11728 C  C   . GLU D 1 373 ? -11.966 47.109  2.217   1.00 42.39  ? 373  GLU D C   1 
ATOM   11729 O  O   . GLU D 1 373 ? -12.608 46.164  2.685   1.00 39.98  ? 373  GLU D O   1 
ATOM   11730 C  CB  . GLU D 1 373 ? -9.513  47.131  2.540   1.00 28.47  ? 373  GLU D CB  1 
ATOM   11731 C  CG  . GLU D 1 373 ? -8.549  46.816  3.644   1.00 39.14  ? 373  GLU D CG  1 
ATOM   11732 C  CD  . GLU D 1 373 ? -7.563  45.761  3.225   1.00 38.27  ? 373  GLU D CD  1 
ATOM   11733 O  OE1 . GLU D 1 373 ? -6.738  46.041  2.326   1.00 37.01  ? 373  GLU D OE1 1 
ATOM   11734 O  OE2 . GLU D 1 373 ? -7.627  44.644  3.787   1.00 42.93  ? 373  GLU D OE2 1 
ATOM   11735 N  N   . TYR D 1 374 ? -12.204 47.639  1.020   1.00 45.75  ? 374  TYR D N   1 
ATOM   11736 C  CA  . TYR D 1 374 ? -13.203 47.098  0.114   1.00 42.29  ? 374  TYR D CA  1 
ATOM   11737 C  C   . TYR D 1 374 ? -12.731 47.309  -1.312  1.00 36.31  ? 374  TYR D C   1 
ATOM   11738 O  O   . TYR D 1 374 ? -12.057 48.285  -1.618  1.00 32.39  ? 374  TYR D O   1 
ATOM   11739 C  CB  . TYR D 1 374 ? -14.546 47.804  0.308   1.00 35.78  ? 374  TYR D CB  1 
ATOM   11740 C  CG  . TYR D 1 374 ? -14.593 49.157  -0.356  1.00 33.60  ? 374  TYR D CG  1 
ATOM   11741 C  CD1 . TYR D 1 374 ? -14.282 50.300  0.353   1.00 28.36  ? 374  TYR D CD1 1 
ATOM   11742 C  CD2 . TYR D 1 374 ? -14.923 49.282  -1.703  1.00 45.05  ? 374  TYR D CD2 1 
ATOM   11743 C  CE1 . TYR D 1 374 ? -14.309 51.547  -0.249  1.00 39.60  ? 374  TYR D CE1 1 
ATOM   11744 C  CE2 . TYR D 1 374 ? -14.949 50.518  -2.319  1.00 45.50  ? 374  TYR D CE2 1 
ATOM   11745 C  CZ  . TYR D 1 374 ? -14.638 51.654  -1.583  1.00 45.24  ? 374  TYR D CZ  1 
ATOM   11746 O  OH  . TYR D 1 374 ? -14.651 52.900  -2.177  1.00 40.27  ? 374  TYR D OH  1 
ATOM   11747 N  N   . TRP D 1 375 ? -13.090 46.378  -2.180  1.00 37.29  ? 375  TRP D N   1 
ATOM   11748 C  CA  . TRP D 1 375 ? -12.913 46.566  -3.604  1.00 34.89  ? 375  TRP D CA  1 
ATOM   11749 C  C   . TRP D 1 375 ? -14.285 46.364  -4.229  1.00 39.86  ? 375  TRP D C   1 
ATOM   11750 O  O   . TRP D 1 375 ? -14.955 45.358  -3.968  1.00 42.99  ? 375  TRP D O   1 
ATOM   11751 C  CB  . TRP D 1 375 ? -11.903 45.562  -4.191  1.00 23.13  ? 375  TRP D CB  1 
ATOM   11752 C  CG  . TRP D 1 375 ? -10.609 45.496  -3.451  1.00 21.61  ? 375  TRP D CG  1 
ATOM   11753 C  CD1 . TRP D 1 375 ? -9.404  46.004  -3.851  1.00 30.74  ? 375  TRP D CD1 1 
ATOM   11754 C  CD2 . TRP D 1 375 ? -10.386 44.892  -2.173  1.00 25.54  ? 375  TRP D CD2 1 
ATOM   11755 N  NE1 . TRP D 1 375 ? -8.440  45.754  -2.891  1.00 29.22  ? 375  TRP D NE1 1 
ATOM   11756 C  CE2 . TRP D 1 375 ? -9.022  45.066  -1.857  1.00 35.11  ? 375  TRP D CE2 1 
ATOM   11757 C  CE3 . TRP D 1 375 ? -11.208 44.224  -1.260  1.00 28.20  ? 375  TRP D CE3 1 
ATOM   11758 C  CZ2 . TRP D 1 375 ? -8.467  44.594  -0.668  1.00 32.11  ? 375  TRP D CZ2 1 
ATOM   11759 C  CZ3 . TRP D 1 375 ? -10.647 43.746  -0.082  1.00 25.45  ? 375  TRP D CZ3 1 
ATOM   11760 C  CH2 . TRP D 1 375 ? -9.295  43.932  0.199   1.00 18.50  ? 375  TRP D CH2 1 
ATOM   11761 N  N   . ARG D 1 376 ? -14.719 47.328  -5.031  1.00 38.82  ? 376  ARG D N   1 
ATOM   11762 C  CA  . ARG D 1 376 ? -15.937 47.147  -5.803  1.00 32.01  ? 376  ARG D CA  1 
ATOM   11763 C  C   . ARG D 1 376 ? -15.634 47.105  -7.296  1.00 41.68  ? 376  ARG D C   1 
ATOM   11764 O  O   . ARG D 1 376 ? -15.369 48.139  -7.937  1.00 37.63  ? 376  ARG D O   1 
ATOM   11765 C  CB  . ARG D 1 376 ? -16.951 48.241  -5.484  1.00 34.99  ? 376  ARG D CB  1 
ATOM   11766 C  CG  . ARG D 1 376 ? -18.301 48.080  -6.190  1.00 41.26  ? 376  ARG D CG  1 
ATOM   11767 C  CD  . ARG D 1 376 ? -19.061 46.825  -5.758  1.00 37.54  ? 376  ARG D CD  1 
ATOM   11768 N  NE  . ARG D 1 376 ? -20.277 46.655  -6.547  1.00 40.64  ? 376  ARG D NE  1 
ATOM   11769 C  CZ  . ARG D 1 376 ? -21.023 45.553  -6.577  1.00 47.80  ? 376  ARG D CZ  1 
ATOM   11770 N  NH1 . ARG D 1 376 ? -20.696 44.489  -5.860  1.00 61.80  ? 376  ARG D NH1 1 
ATOM   11771 N  NH2 . ARG D 1 376 ? -22.109 45.519  -7.334  1.00 58.45  ? 376  ARG D NH2 1 
ATOM   11772 N  N   . LEU D 1 377 ? -15.660 45.893  -7.839  1.00 28.88  ? 377  LEU D N   1 
ATOM   11773 C  CA  . LEU D 1 377 ? -15.554 45.716  -9.271  1.00 27.79  ? 377  LEU D CA  1 
ATOM   11774 C  C   . LEU D 1 377 ? -16.697 46.442  -9.999  1.00 34.64  ? 377  LEU D C   1 
ATOM   11775 O  O   . LEU D 1 377 ? -17.877 46.231  -9.709  1.00 34.13  ? 377  LEU D O   1 
ATOM   11776 C  CB  . LEU D 1 377 ? -15.562 44.227  -9.611  1.00 28.22  ? 377  LEU D CB  1 
ATOM   11777 C  CG  . LEU D 1 377 ? -14.513 43.385  -8.885  1.00 24.04  ? 377  LEU D CG  1 
ATOM   11778 C  CD1 . LEU D 1 377 ? -14.462 41.968  -9.435  1.00 18.21  ? 377  LEU D CD1 1 
ATOM   11779 C  CD2 . LEU D 1 377 ? -13.174 44.049  -9.016  1.00 23.44  ? 377  LEU D CD2 1 
ATOM   11780 N  N   . LEU D 1 378 ? -16.343 47.290  -10.959 1.00 45.18  ? 378  LEU D N   1 
ATOM   11781 C  CA  . LEU D 1 378 ? -17.342 48.077  -11.684 1.00 44.21  ? 378  LEU D CA  1 
ATOM   11782 C  C   . LEU D 1 378 ? -17.082 48.193  -13.182 1.00 32.20  ? 378  LEU D C   1 
ATOM   11783 O  O   . LEU D 1 378 ? -15.945 48.351  -13.624 1.00 48.16  ? 378  LEU D O   1 
ATOM   11784 C  CB  . LEU D 1 378 ? -17.452 49.482  -11.086 1.00 36.79  ? 378  LEU D CB  1 
ATOM   11785 C  CG  . LEU D 1 378 ? -18.081 49.564  -9.704  1.00 25.15  ? 378  LEU D CG  1 
ATOM   11786 C  CD1 . LEU D 1 378 ? -18.097 51.001  -9.259  1.00 30.57  ? 378  LEU D CD1 1 
ATOM   11787 C  CD2 . LEU D 1 378 ? -19.482 49.011  -9.732  1.00 25.06  ? 378  LEU D CD2 1 
ATOM   11788 N  N   . THR D 1 379 ? -18.158 48.116  -13.952 1.00 37.77  ? 379  THR D N   1 
ATOM   11789 C  CA  . THR D 1 379 ? -18.122 48.411  -15.373 1.00 40.58  ? 379  THR D CA  1 
ATOM   11790 C  C   . THR D 1 379 ? -17.900 49.910  -15.577 1.00 44.55  ? 379  THR D C   1 
ATOM   11791 O  O   . THR D 1 379 ? -18.332 50.718  -14.758 1.00 34.01  ? 379  THR D O   1 
ATOM   11792 C  CB  . THR D 1 379 ? -19.448 48.014  -15.993 1.00 51.12  ? 379  THR D CB  1 
ATOM   11793 O  OG1 . THR D 1 379 ? -19.549 46.583  -15.993 1.00 61.95  ? 379  THR D OG1 1 
ATOM   11794 C  CG2 . THR D 1 379 ? -19.564 48.542  -17.411 1.00 64.95  ? 379  THR D CG2 1 
ATOM   11795 N  N   . PRO D 1 380 ? -17.199 50.295  -16.655 1.00 43.62  ? 380  PRO D N   1 
ATOM   11796 C  CA  . PRO D 1 380 ? -17.095 51.737  -16.915 1.00 45.90  ? 380  PRO D CA  1 
ATOM   11797 C  C   . PRO D 1 380 ? -18.461 52.442  -16.792 1.00 54.77  ? 380  PRO D C   1 
ATOM   11798 O  O   . PRO D 1 380 ? -19.497 51.841  -17.093 1.00 52.70  ? 380  PRO D O   1 
ATOM   11799 C  CB  . PRO D 1 380 ? -16.577 51.794  -18.355 1.00 31.30  ? 380  PRO D CB  1 
ATOM   11800 C  CG  . PRO D 1 380 ? -15.793 50.541  -18.514 1.00 38.54  ? 380  PRO D CG  1 
ATOM   11801 C  CD  . PRO D 1 380 ? -16.443 49.496  -17.639 1.00 41.29  ? 380  PRO D CD  1 
ATOM   11802 N  N   . GLY D 1 381 ? -18.457 53.699  -16.348 1.00 51.86  ? 381  GLY D N   1 
ATOM   11803 C  CA  . GLY D 1 381 ? -19.687 54.446  -16.118 1.00 42.80  ? 381  GLY D CA  1 
ATOM   11804 C  C   . GLY D 1 381 ? -19.584 55.284  -14.856 1.00 42.93  ? 381  GLY D C   1 
ATOM   11805 O  O   . GLY D 1 381 ? -18.530 55.326  -14.226 1.00 49.70  ? 381  GLY D O   1 
ATOM   11806 N  N   . LEU D 1 382 ? -20.661 55.957  -14.472 1.00 35.23  ? 382  LEU D N   1 
ATOM   11807 C  CA  . LEU D 1 382 ? -20.598 56.771  -13.266 1.00 48.26  ? 382  LEU D CA  1 
ATOM   11808 C  C   . LEU D 1 382 ? -21.568 56.293  -12.184 1.00 49.04  ? 382  LEU D C   1 
ATOM   11809 O  O   . LEU D 1 382 ? -22.694 55.879  -12.473 1.00 35.92  ? 382  LEU D O   1 
ATOM   11810 C  CB  . LEU D 1 382 ? -20.763 58.269  -13.582 1.00 54.86  ? 382  LEU D CB  1 
ATOM   11811 C  CG  . LEU D 1 382 ? -22.130 58.835  -13.956 1.00 68.61  ? 382  LEU D CG  1 
ATOM   11812 C  CD1 . LEU D 1 382 ? -23.033 58.965  -12.736 1.00 74.16  ? 382  LEU D CD1 1 
ATOM   11813 C  CD2 . LEU D 1 382 ? -21.942 60.188  -14.616 1.00 80.36  ? 382  LEU D CD2 1 
ATOM   11814 N  N   . TYR D 1 383 ? -21.115 56.362  -10.934 1.00 47.21  ? 383  TYR D N   1 
ATOM   11815 C  CA  . TYR D 1 383 ? -21.831 55.755  -9.823  1.00 42.77  ? 383  TYR D CA  1 
ATOM   11816 C  C   . TYR D 1 383 ? -21.914 56.651  -8.587  1.00 48.13  ? 383  TYR D C   1 
ATOM   11817 O  O   . TYR D 1 383 ? -21.044 57.497  -8.340  1.00 52.05  ? 383  TYR D O   1 
ATOM   11818 C  CB  . TYR D 1 383 ? -21.153 54.432  -9.432  1.00 44.58  ? 383  TYR D CB  1 
ATOM   11819 C  CG  . TYR D 1 383 ? -20.948 53.489  -10.593 1.00 48.59  ? 383  TYR D CG  1 
ATOM   11820 C  CD1 . TYR D 1 383 ? -19.868 53.644  -11.457 1.00 47.55  ? 383  TYR D CD1 1 
ATOM   11821 C  CD2 . TYR D 1 383 ? -21.837 52.446  -10.830 1.00 48.71  ? 383  TYR D CD2 1 
ATOM   11822 C  CE1 . TYR D 1 383 ? -19.677 52.787  -12.533 1.00 49.11  ? 383  TYR D CE1 1 
ATOM   11823 C  CE2 . TYR D 1 383 ? -21.655 51.578  -11.894 1.00 51.77  ? 383  TYR D CE2 1 
ATOM   11824 C  CZ  . TYR D 1 383 ? -20.574 51.752  -12.742 1.00 57.86  ? 383  TYR D CZ  1 
ATOM   11825 O  OH  . TYR D 1 383 ? -20.406 50.882  -13.797 1.00 57.50  ? 383  TYR D OH  1 
ATOM   11826 N  N   . SER D 1 384 ? -22.974 56.446  -7.811  1.00 49.94  ? 384  SER D N   1 
ATOM   11827 C  CA  . SER D 1 384 ? -23.098 57.058  -6.499  1.00 48.02  ? 384  SER D CA  1 
ATOM   11828 C  C   . SER D 1 384 ? -22.868 55.989  -5.437  1.00 53.45  ? 384  SER D C   1 
ATOM   11829 O  O   . SER D 1 384 ? -23.742 55.168  -5.142  1.00 39.78  ? 384  SER D O   1 
ATOM   11830 C  CB  . SER D 1 384 ? -24.458 57.740  -6.322  1.00 45.34  ? 384  SER D CB  1 
ATOM   11831 O  OG  . SER D 1 384 ? -24.410 59.081  -6.788  1.00 73.61  ? 384  SER D OG  1 
ATOM   11832 N  N   . VAL D 1 385 ? -21.672 56.009  -4.869  1.00 55.34  ? 385  VAL D N   1 
ATOM   11833 C  CA  . VAL D 1 385 ? -21.307 55.054  -3.844  1.00 50.42  ? 385  VAL D CA  1 
ATOM   11834 C  C   . VAL D 1 385 ? -21.496 55.630  -2.432  1.00 50.29  ? 385  VAL D C   1 
ATOM   11835 O  O   . VAL D 1 385 ? -21.227 56.812  -2.200  1.00 50.50  ? 385  VAL D O   1 
ATOM   11836 C  CB  . VAL D 1 385 ? -19.850 54.637  -4.029  1.00 41.44  ? 385  VAL D CB  1 
ATOM   11837 C  CG1 . VAL D 1 385 ? -19.614 53.280  -3.399  1.00 35.11  ? 385  VAL D CG1 1 
ATOM   11838 C  CG2 . VAL D 1 385 ? -19.498 54.617  -5.520  1.00 37.74  ? 385  VAL D CG2 1 
ATOM   11839 N  N   . HIS D 1 386 ? -21.965 54.798  -1.498  1.00 39.85  ? 386  HIS D N   1 
ATOM   11840 C  CA  . HIS D 1 386 ? -22.014 55.164  -0.071  1.00 36.00  ? 386  HIS D CA  1 
ATOM   11841 C  C   . HIS D 1 386 ? -21.742 53.976  0.858   1.00 38.18  ? 386  HIS D C   1 
ATOM   11842 O  O   . HIS D 1 386 ? -21.841 52.798  0.467   1.00 33.22  ? 386  HIS D O   1 
ATOM   11843 C  CB  . HIS D 1 386 ? -23.327 55.870  0.317   1.00 49.29  ? 386  HIS D CB  1 
ATOM   11844 C  CG  . HIS D 1 386 ? -24.511 54.958  0.447   1.00 61.60  ? 386  HIS D CG  1 
ATOM   11845 N  ND1 . HIS D 1 386 ? -24.417 53.585  0.394   1.00 77.65  ? 386  HIS D ND1 1 
ATOM   11846 C  CD2 . HIS D 1 386 ? -25.824 55.235  0.632   1.00 65.41  ? 386  HIS D CD2 1 
ATOM   11847 C  CE1 . HIS D 1 386 ? -25.620 53.054  0.534   1.00 59.42  ? 386  HIS D CE1 1 
ATOM   11848 N  NE2 . HIS D 1 386 ? -26.491 54.034  0.676   1.00 52.07  ? 386  HIS D NE2 1 
ATOM   11849 N  N   . ALA D 1 387 ? -21.389 54.292  2.094   1.00 35.80  ? 387  ALA D N   1 
ATOM   11850 C  CA  . ALA D 1 387 ? -21.031 53.259  3.042   1.00 41.13  ? 387  ALA D CA  1 
ATOM   11851 C  C   . ALA D 1 387 ? -21.845 53.412  4.297   1.00 46.60  ? 387  ALA D C   1 
ATOM   11852 O  O   . ALA D 1 387 ? -22.254 54.523  4.663   1.00 50.02  ? 387  ALA D O   1 
ATOM   11853 C  CB  . ALA D 1 387 ? -19.542 53.317  3.369   1.00 46.83  ? 387  ALA D CB  1 
ATOM   11854 N  N   . SER D 1 388 ? -22.070 52.286  4.959   1.00 33.08  ? 388  SER D N   1 
ATOM   11855 C  CA  . SER D 1 388 ? -22.814 52.282  6.199   1.00 45.41  ? 388  SER D CA  1 
ATOM   11856 C  C   . SER D 1 388 ? -22.291 51.168  7.101   1.00 47.34  ? 388  SER D C   1 
ATOM   11857 O  O   . SER D 1 388 ? -21.648 50.222  6.628   1.00 35.64  ? 388  SER D O   1 
ATOM   11858 C  CB  . SER D 1 388 ? -24.315 52.118  5.923   1.00 42.53  ? 388  SER D CB  1 
ATOM   11859 O  OG  . SER D 1 388 ? -24.579 50.875  5.294   1.00 50.57  ? 388  SER D OG  1 
ATOM   11860 N  N   . ALA D 1 389 ? -22.568 51.294  8.397   1.00 54.38  ? 389  ALA D N   1 
ATOM   11861 C  CA  . ALA D 1 389 ? -22.157 50.301  9.380   1.00 45.79  ? 389  ALA D CA  1 
ATOM   11862 C  C   . ALA D 1 389 ? -22.954 50.468  10.678  1.00 49.31  ? 389  ALA D C   1 
ATOM   11863 O  O   . ALA D 1 389 ? -23.325 51.590  11.048  1.00 58.68  ? 389  ALA D O   1 
ATOM   11864 C  CB  . ALA D 1 389 ? -20.681 50.428  9.640   1.00 28.76  ? 389  ALA D CB  1 
ATOM   11865 N  N   . PHE D 1 390 ? -23.225 49.358  11.361  1.00 43.42  ? 390  PHE D N   1 
ATOM   11866 C  CA  . PHE D 1 390 ? -23.999 49.400  12.603  1.00 63.26  ? 390  PHE D CA  1 
ATOM   11867 C  C   . PHE D 1 390 ? -23.291 50.263  13.651  1.00 60.03  ? 390  PHE D C   1 
ATOM   11868 O  O   . PHE D 1 390 ? -22.101 50.088  13.901  1.00 55.21  ? 390  PHE D O   1 
ATOM   11869 C  CB  . PHE D 1 390 ? -24.241 47.984  13.137  1.00 75.32  ? 390  PHE D CB  1 
ATOM   11870 C  CG  . PHE D 1 390 ? -24.872 47.948  14.502  1.00 95.81  ? 390  PHE D CG  1 
ATOM   11871 C  CD1 . PHE D 1 390 ? -24.125 47.591  15.617  1.00 102.15 ? 390  PHE D CD1 1 
ATOM   11872 C  CD2 . PHE D 1 390 ? -26.209 48.277  14.674  1.00 104.26 ? 390  PHE D CD2 1 
ATOM   11873 C  CE1 . PHE D 1 390 ? -24.699 47.558  16.882  1.00 106.38 ? 390  PHE D CE1 1 
ATOM   11874 C  CE2 . PHE D 1 390 ? -26.790 48.247  15.937  1.00 110.04 ? 390  PHE D CE2 1 
ATOM   11875 C  CZ  . PHE D 1 390 ? -26.033 47.887  17.042  1.00 109.35 ? 390  PHE D CZ  1 
ATOM   11876 N  N   . GLY D 1 391 ? -24.022 51.198  14.254  1.00 53.71  ? 391  GLY D N   1 
ATOM   11877 C  CA  . GLY D 1 391 ? -23.437 52.103  15.230  1.00 52.12  ? 391  GLY D CA  1 
ATOM   11878 C  C   . GLY D 1 391 ? -22.816 53.335  14.594  1.00 51.34  ? 391  GLY D C   1 
ATOM   11879 O  O   . GLY D 1 391 ? -22.192 54.155  15.270  1.00 42.55  ? 391  GLY D O   1 
ATOM   11880 N  N   . TYR D 1 392 ? -22.982 53.458  13.281  1.00 59.62  ? 392  TYR D N   1 
ATOM   11881 C  CA  . TYR D 1 392 ? -22.469 54.609  12.549  1.00 56.73  ? 392  TYR D CA  1 
ATOM   11882 C  C   . TYR D 1 392 ? -23.529 55.187  11.641  1.00 62.16  ? 392  TYR D C   1 
ATOM   11883 O  O   . TYR D 1 392 ? -24.318 54.454  11.035  1.00 67.19  ? 392  TYR D O   1 
ATOM   11884 C  CB  . TYR D 1 392 ? -21.259 54.230  11.698  1.00 52.51  ? 392  TYR D CB  1 
ATOM   11885 C  CG  . TYR D 1 392 ? -20.039 53.884  12.499  1.00 61.93  ? 392  TYR D CG  1 
ATOM   11886 C  CD1 . TYR D 1 392 ? -19.051 54.837  12.737  1.00 62.69  ? 392  TYR D CD1 1 
ATOM   11887 C  CD2 . TYR D 1 392 ? -19.865 52.601  13.023  1.00 55.17  ? 392  TYR D CD2 1 
ATOM   11888 C  CE1 . TYR D 1 392 ? -17.914 54.521  13.475  1.00 63.07  ? 392  TYR D CE1 1 
ATOM   11889 C  CE2 . TYR D 1 392 ? -18.733 52.275  13.769  1.00 54.77  ? 392  TYR D CE2 1 
ATOM   11890 C  CZ  . TYR D 1 392 ? -17.764 53.236  13.990  1.00 63.22  ? 392  TYR D CZ  1 
ATOM   11891 O  OH  . TYR D 1 392 ? -16.644 52.918  14.725  1.00 60.30  ? 392  TYR D OH  1 
ATOM   11892 N  N   . GLN D 1 393 ? -23.533 56.511  11.548  1.00 68.58  ? 393  GLN D N   1 
ATOM   11893 C  CA  . GLN D 1 393 ? -24.404 57.213  10.626  1.00 55.69  ? 393  GLN D CA  1 
ATOM   11894 C  C   . GLN D 1 393 ? -23.925 56.926  9.202   1.00 59.01  ? 393  GLN D C   1 
ATOM   11895 O  O   . GLN D 1 393 ? -22.732 57.037  8.905   1.00 58.76  ? 393  GLN D O   1 
ATOM   11896 C  CB  . GLN D 1 393 ? -24.402 58.709  10.944  1.00 42.47  ? 393  GLN D CB  1 
ATOM   11897 C  CG  . GLN D 1 393 ? -24.691 59.009  12.418  1.00 49.95  ? 393  GLN D CG  1 
ATOM   11898 C  CD  . GLN D 1 393 ? -24.764 60.495  12.709  1.00 66.62  ? 393  GLN D CD  1 
ATOM   11899 O  OE1 . GLN D 1 393 ? -24.269 61.308  11.935  1.00 74.22  ? 393  GLN D OE1 1 
ATOM   11900 N  NE2 . GLN D 1 393 ? -25.380 60.856  13.827  1.00 68.14  ? 393  GLN D NE2 1 
ATOM   11901 N  N   . THR D 1 394 ? -24.856 56.527  8.338   1.00 63.05  ? 394  THR D N   1 
ATOM   11902 C  CA  . THR D 1 394 ? -24.540 56.159  6.958   1.00 59.55  ? 394  THR D CA  1 
ATOM   11903 C  C   . THR D 1 394 ? -24.039 57.360  6.174   1.00 58.82  ? 394  THR D C   1 
ATOM   11904 O  O   . THR D 1 394 ? -24.750 58.358  6.023   1.00 59.91  ? 394  THR D O   1 
ATOM   11905 C  CB  . THR D 1 394 ? -25.767 55.583  6.243   1.00 57.86  ? 394  THR D CB  1 
ATOM   11906 O  OG1 . THR D 1 394 ? -26.245 54.443  6.972   1.00 62.10  ? 394  THR D OG1 1 
ATOM   11907 C  CG2 . THR D 1 394 ? -25.411 55.166  4.823   1.00 57.45  ? 394  THR D CG2 1 
ATOM   11908 N  N   . SER D 1 395 ? -22.813 57.247  5.671   1.00 57.38  ? 395  SER D N   1 
ATOM   11909 C  CA  . SER D 1 395 ? -22.124 58.356  5.018   1.00 50.16  ? 395  SER D CA  1 
ATOM   11910 C  C   . SER D 1 395 ? -22.966 58.998  3.934   1.00 57.37  ? 395  SER D C   1 
ATOM   11911 O  O   . SER D 1 395 ? -23.903 58.394  3.418   1.00 59.64  ? 395  SER D O   1 
ATOM   11912 C  CB  . SER D 1 395 ? -20.851 57.858  4.362   1.00 44.74  ? 395  SER D CB  1 
ATOM   11913 O  OG  . SER D 1 395 ? -21.185 57.017  3.268   1.00 53.63  ? 395  SER D OG  1 
ATOM   11914 N  N   . ALA D 1 396 ? -22.610 60.226  3.580   1.00 58.21  ? 396  ALA D N   1 
ATOM   11915 C  CA  . ALA D 1 396 ? -23.191 60.872  2.417   1.00 50.56  ? 396  ALA D CA  1 
ATOM   11916 C  C   . ALA D 1 396 ? -22.686 60.122  1.186   1.00 57.37  ? 396  ALA D C   1 
ATOM   11917 O  O   . ALA D 1 396 ? -21.661 59.436  1.253   1.00 67.87  ? 396  ALA D O   1 
ATOM   11918 C  CB  . ALA D 1 396 ? -22.776 62.326  2.368   1.00 38.24  ? 396  ALA D CB  1 
ATOM   11919 N  N   . PRO D 1 397 ? -23.408 60.240  0.059   1.00 50.47  ? 397  PRO D N   1 
ATOM   11920 C  CA  . PRO D 1 397 ? -23.027 59.579  -1.194  1.00 43.45  ? 397  PRO D CA  1 
ATOM   11921 C  C   . PRO D 1 397 ? -21.902 60.302  -1.917  1.00 41.59  ? 397  PRO D C   1 
ATOM   11922 O  O   . PRO D 1 397 ? -21.913 61.530  -1.961  1.00 58.31  ? 397  PRO D O   1 
ATOM   11923 C  CB  . PRO D 1 397 ? -24.305 59.669  -2.052  1.00 41.94  ? 397  PRO D CB  1 
ATOM   11924 C  CG  . PRO D 1 397 ? -25.377 60.176  -1.145  1.00 53.21  ? 397  PRO D CG  1 
ATOM   11925 C  CD  . PRO D 1 397 ? -24.686 60.951  -0.071  1.00 58.04  ? 397  PRO D CD  1 
ATOM   11926 N  N   . GLN D 1 398 ? -20.957 59.557  -2.481  1.00 46.45  ? 398  GLN D N   1 
ATOM   11927 C  CA  . GLN D 1 398 ? -19.975 60.133  -3.400  1.00 48.14  ? 398  GLN D CA  1 
ATOM   11928 C  C   . GLN D 1 398 ? -20.189 59.633  -4.830  1.00 46.07  ? 398  GLN D C   1 
ATOM   11929 O  O   . GLN D 1 398 ? -20.424 58.448  -5.072  1.00 51.58  ? 398  GLN D O   1 
ATOM   11930 C  CB  . GLN D 1 398 ? -18.539 59.855  -2.937  1.00 42.14  ? 398  GLN D CB  1 
ATOM   11931 C  CG  . GLN D 1 398 ? -18.210 60.466  -1.587  1.00 36.79  ? 398  GLN D CG  1 
ATOM   11932 C  CD  . GLN D 1 398 ? -16.869 60.014  -1.004  1.00 49.23  ? 398  GLN D CD  1 
ATOM   11933 O  OE1 . GLN D 1 398 ? -15.838 60.019  -1.683  1.00 49.45  ? 398  GLN D OE1 1 
ATOM   11934 N  NE2 . GLN D 1 398 ? -16.880 59.647  0.278   1.00 54.76  ? 398  GLN D NE2 1 
ATOM   11935 N  N   . GLN D 1 399 ? -20.109 60.553  -5.776  1.00 54.21  ? 399  GLN D N   1 
ATOM   11936 C  CA  . GLN D 1 399 ? -20.238 60.225  -7.182  1.00 55.34  ? 399  GLN D CA  1 
ATOM   11937 C  C   . GLN D 1 399 ? -18.853 60.022  -7.768  1.00 65.53  ? 399  GLN D C   1 
ATOM   11938 O  O   . GLN D 1 399 ? -17.935 60.802  -7.490  1.00 76.49  ? 399  GLN D O   1 
ATOM   11939 C  CB  . GLN D 1 399 ? -20.949 61.365  -7.891  1.00 64.00  ? 399  GLN D CB  1 
ATOM   11940 C  CG  . GLN D 1 399 ? -20.688 61.450  -9.368  1.00 82.59  ? 399  GLN D CG  1 
ATOM   11941 C  CD  . GLN D 1 399 ? -20.975 62.841  -9.895  1.00 99.91  ? 399  GLN D CD  1 
ATOM   11942 O  OE1 . GLN D 1 399 ? -20.238 63.790  -9.615  1.00 104.65 ? 399  GLN D OE1 1 
ATOM   11943 N  NE2 . GLN D 1 399 ? -22.063 62.975  -10.646 1.00 104.15 ? 399  GLN D NE2 1 
ATOM   11944 N  N   . VAL D 1 400 ? -18.692 58.970  -8.567  1.00 60.62  ? 400  VAL D N   1 
ATOM   11945 C  CA  . VAL D 1 400 ? -17.393 58.675  -9.173  1.00 52.44  ? 400  VAL D CA  1 
ATOM   11946 C  C   . VAL D 1 400 ? -17.518 58.214  -10.629 1.00 49.18  ? 400  VAL D C   1 
ATOM   11947 O  O   . VAL D 1 400 ? -18.396 57.424  -10.974 1.00 42.42  ? 400  VAL D O   1 
ATOM   11948 C  CB  . VAL D 1 400 ? -16.613 57.621  -8.355  1.00 50.80  ? 400  VAL D CB  1 
ATOM   11949 C  CG1 . VAL D 1 400 ? -17.287 56.273  -8.458  1.00 54.11  ? 400  VAL D CG1 1 
ATOM   11950 C  CG2 . VAL D 1 400 ? -15.184 57.529  -8.850  1.00 66.40  ? 400  VAL D CG2 1 
ATOM   11951 N  N   . ARG D 1 401 ? -16.640 58.721  -11.483 1.00 51.01  ? 401  ARG D N   1 
ATOM   11952 C  CA  . ARG D 1 401 ? -16.603 58.279  -12.865 1.00 53.33  ? 401  ARG D CA  1 
ATOM   11953 C  C   . ARG D 1 401 ? -15.605 57.130  -13.028 1.00 54.56  ? 401  ARG D C   1 
ATOM   11954 O  O   . ARG D 1 401 ? -14.388 57.347  -13.007 1.00 62.01  ? 401  ARG D O   1 
ATOM   11955 C  CB  . ARG D 1 401 ? -16.233 59.446  -13.786 1.00 62.86  ? 401  ARG D CB  1 
ATOM   11956 C  CG  . ARG D 1 401 ? -16.123 59.074  -15.268 1.00 69.60  ? 401  ARG D CG  1 
ATOM   11957 C  CD  . ARG D 1 401 ? -16.076 60.320  -16.153 1.00 80.63  ? 401  ARG D CD  1 
ATOM   11958 N  NE  . ARG D 1 401 ? -15.087 61.284  -15.688 1.00 88.83  ? 401  ARG D NE  1 
ATOM   11959 C  CZ  . ARG D 1 401 ? -15.291 62.590  -15.538 1.00 92.53  ? 401  ARG D CZ  1 
ATOM   11960 N  NH1 . ARG D 1 401 ? -14.299 63.346  -15.097 1.00 101.02 ? 401  ARG D NH1 1 
ATOM   11961 N  NH2 . ARG D 1 401 ? -16.462 63.144  -15.822 1.00 86.67  ? 401  ARG D NH2 1 
ATOM   11962 N  N   . VAL D 1 402 ? -16.121 55.909  -13.178 1.00 51.36  ? 402  VAL D N   1 
ATOM   11963 C  CA  . VAL D 1 402 ? -15.269 54.733  -13.392 1.00 40.85  ? 402  VAL D CA  1 
ATOM   11964 C  C   . VAL D 1 402 ? -14.855 54.584  -14.843 1.00 52.79  ? 402  VAL D C   1 
ATOM   11965 O  O   . VAL D 1 402 ? -15.618 54.113  -15.692 1.00 41.51  ? 402  VAL D O   1 
ATOM   11966 C  CB  . VAL D 1 402 ? -15.941 53.410  -12.985 1.00 30.70  ? 402  VAL D CB  1 
ATOM   11967 C  CG1 . VAL D 1 402 ? -15.050 52.251  -13.370 1.00 26.06  ? 402  VAL D CG1 1 
ATOM   11968 C  CG2 . VAL D 1 402 ? -16.225 53.385  -11.497 1.00 41.05  ? 402  VAL D CG2 1 
ATOM   11969 N  N   . THR D 1 403 ? -13.640 55.016  -15.124 1.00 71.40  ? 403  THR D N   1 
ATOM   11970 C  CA  . THR D 1 403 ? -12.971 54.645  -16.349 1.00 74.21  ? 403  THR D CA  1 
ATOM   11971 C  C   . THR D 1 403 ? -11.963 53.609  -15.899 1.00 72.16  ? 403  THR D C   1 
ATOM   11972 O  O   . THR D 1 403 ? -11.375 53.731  -14.823 1.00 78.33  ? 403  THR D O   1 
ATOM   11973 C  CB  . THR D 1 403 ? -12.212 55.828  -16.952 1.00 73.24  ? 403  THR D CB  1 
ATOM   11974 O  OG1 . THR D 1 403 ? -11.411 55.372  -18.050 1.00 87.18  ? 403  THR D OG1 1 
ATOM   11975 C  CG2 . THR D 1 403 ? -11.302 56.460  -15.898 1.00 64.93  ? 403  THR D CG2 1 
ATOM   11976 N  N   . ASN D 1 404 ? -11.754 52.576  -16.693 1.00 45.99  ? 404  ASN D N   1 
ATOM   11977 C  CA  . ASN D 1 404 ? -10.761 51.613  -16.284 1.00 45.32  ? 404  ASN D CA  1 
ATOM   11978 C  C   . ASN D 1 404 ? -9.487  51.786  -17.085 1.00 47.64  ? 404  ASN D C   1 
ATOM   11979 O  O   . ASN D 1 404 ? -9.034  50.861  -17.761 1.00 48.68  ? 404  ASN D O   1 
ATOM   11980 C  CB  . ASN D 1 404 ? -11.313 50.183  -16.323 1.00 52.81  ? 404  ASN D CB  1 
ATOM   11981 C  CG  . ASN D 1 404 ? -12.364 49.930  -15.226 1.00 63.37  ? 404  ASN D CG  1 
ATOM   11982 O  OD1 . ASN D 1 404 ? -12.112 50.163  -14.038 1.00 56.56  ? 404  ASN D OD1 1 
ATOM   11983 N  ND2 . ASN D 1 404 ? -13.548 49.458  -15.629 1.00 59.08  ? 404  ASN D ND2 1 
ATOM   11984 N  N   . ASP D 1 405 ? -8.920  52.993  -17.000 1.00 68.85  ? 405  ASP D N   1 
ATOM   11985 C  CA  . ASP D 1 405 ? -7.634  53.313  -17.630 1.00 87.11  ? 405  ASP D CA  1 
ATOM   11986 C  C   . ASP D 1 405 ? -6.463  53.000  -16.708 1.00 84.23  ? 405  ASP D C   1 
ATOM   11987 O  O   . ASP D 1 405 ? -5.583  52.204  -17.050 1.00 67.69  ? 405  ASP D O   1 
ATOM   11988 C  CB  . ASP D 1 405 ? -7.572  54.789  -18.026 1.00 101.26 ? 405  ASP D CB  1 
ATOM   11989 C  CG  . ASP D 1 405 ? -6.190  55.206  -18.513 1.00 109.19 ? 405  ASP D CG  1 
ATOM   11990 O  OD1 . ASP D 1 405 ? -5.312  54.327  -18.672 1.00 99.55  ? 405  ASP D OD1 1 
ATOM   11991 O  OD2 . ASP D 1 405 ? -5.981  56.418  -18.741 1.00 116.39 ? 405  ASP D OD2 1 
ATOM   11992 N  N   . ASN D 1 406 ? -6.444  53.634  -15.539 1.00 88.78  ? 406  ASN D N   1 
ATOM   11993 C  CA  . ASN D 1 406 ? -5.356  53.390  -14.604 1.00 89.43  ? 406  ASN D CA  1 
ATOM   11994 C  C   . ASN D 1 406 ? -5.242  51.919  -14.240 1.00 90.76  ? 406  ASN D C   1 
ATOM   11995 O  O   . ASN D 1 406 ? -6.243  51.220  -14.084 1.00 94.43  ? 406  ASN D O   1 
ATOM   11996 C  CB  . ASN D 1 406 ? -5.481  54.230  -13.337 1.00 82.83  ? 406  ASN D CB  1 
ATOM   11997 C  CG  . ASN D 1 406 ? -4.142  54.430  -12.650 1.00 80.12  ? 406  ASN D CG  1 
ATOM   11998 O  OD1 . ASN D 1 406 ? -3.510  55.474  -12.806 1.00 94.27  ? 406  ASN D OD1 1 
ATOM   11999 N  ND2 . ASN D 1 406 ? -3.691  53.421  -11.905 1.00 62.93  ? 406  ASN D ND2 1 
ATOM   12000 N  N   . GLN D 1 407 ? -4.003  51.464  -14.109 1.00 81.33  ? 407  GLN D N   1 
ATOM   12001 C  CA  . GLN D 1 407 ? -3.693  50.079  -13.767 1.00 70.36  ? 407  GLN D CA  1 
ATOM   12002 C  C   . GLN D 1 407 ? -4.385  49.597  -12.507 1.00 59.64  ? 407  GLN D C   1 
ATOM   12003 O  O   . GLN D 1 407 ? -4.533  48.391  -12.306 1.00 61.55  ? 407  GLN D O   1 
ATOM   12004 C  CB  . GLN D 1 407 ? -2.190  49.918  -13.582 1.00 74.55  ? 407  GLN D CB  1 
ATOM   12005 C  CG  . GLN D 1 407 ? -1.422  49.616  -14.855 1.00 76.89  ? 407  GLN D CG  1 
ATOM   12006 C  CD  . GLN D 1 407 ? 0.085   49.665  -14.635 1.00 93.18  ? 407  GLN D CD  1 
ATOM   12007 O  OE1 . GLN D 1 407 ? 0.577   50.380  -13.752 1.00 94.47  ? 407  GLN D OE1 1 
ATOM   12008 N  NE2 . GLN D 1 407 ? 0.826   48.904  -15.437 1.00 99.47  ? 407  GLN D NE2 1 
ATOM   12009 N  N   . GLU D 1 408 ? -4.788  50.523  -11.644 1.00 48.19  ? 408  GLU D N   1 
ATOM   12010 C  CA  . GLU D 1 408 ? -5.450  50.117  -10.415 1.00 51.34  ? 408  GLU D CA  1 
ATOM   12011 C  C   . GLU D 1 408 ? -6.747  50.860  -10.130 1.00 52.81  ? 408  GLU D C   1 
ATOM   12012 O  O   . GLU D 1 408 ? -6.912  52.023  -10.503 1.00 55.87  ? 408  GLU D O   1 
ATOM   12013 C  CB  . GLU D 1 408 ? -4.481  50.186  -9.236  1.00 50.79  ? 408  GLU D CB  1 
ATOM   12014 C  CG  . GLU D 1 408 ? -3.416  49.125  -9.330  1.00 57.61  ? 408  GLU D CG  1 
ATOM   12015 C  CD  . GLU D 1 408 ? -2.449  49.170  -8.182  1.00 67.17  ? 408  GLU D CD  1 
ATOM   12016 O  OE1 . GLU D 1 408 ? -1.222  49.071  -8.422  1.00 52.98  ? 408  GLU D OE1 1 
ATOM   12017 O  OE2 . GLU D 1 408 ? -2.918  49.313  -7.037  1.00 84.99  ? 408  GLU D OE2 1 
ATOM   12018 N  N   . ALA D 1 409 ? -7.667  50.158  -9.474  1.00 53.26  ? 409  ALA D N   1 
ATOM   12019 C  CA  . ALA D 1 409 ? -8.978  50.701  -9.138  1.00 45.91  ? 409  ALA D CA  1 
ATOM   12020 C  C   . ALA D 1 409 ? -8.899  52.098  -8.505  1.00 54.27  ? 409  ALA D C   1 
ATOM   12021 O  O   . ALA D 1 409 ? -8.001  52.396  -7.702  1.00 46.29  ? 409  ALA D O   1 
ATOM   12022 C  CB  . ALA D 1 409 ? -9.728  49.729  -8.221  1.00 36.61  ? 409  ALA D CB  1 
ATOM   12023 N  N   . LEU D 1 410 ? -9.845  52.952  -8.883  1.00 55.25  ? 410  LEU D N   1 
ATOM   12024 C  CA  . LEU D 1 410 ? -9.939  54.296  -8.330  1.00 34.67  ? 410  LEU D CA  1 
ATOM   12025 C  C   . LEU D 1 410 ? -10.125 54.272  -6.819  1.00 27.72  ? 410  LEU D C   1 
ATOM   12026 O  O   . LEU D 1 410 ? -11.073 53.690  -6.302  1.00 28.56  ? 410  LEU D O   1 
ATOM   12027 C  CB  . LEU D 1 410 ? -11.091 55.055  -8.989  1.00 45.18  ? 410  LEU D CB  1 
ATOM   12028 C  CG  . LEU D 1 410 ? -10.779 55.564  -10.400 1.00 65.09  ? 410  LEU D CG  1 
ATOM   12029 C  CD1 . LEU D 1 410 ? -12.024 55.681  -11.291 1.00 75.26  ? 410  LEU D CD1 1 
ATOM   12030 C  CD2 . LEU D 1 410 ? -10.050 56.893  -10.311 1.00 67.37  ? 410  LEU D CD2 1 
ATOM   12031 N  N   . ARG D 1 411 ? -9.207  54.904  -6.107  1.00 34.94  ? 411  ARG D N   1 
ATOM   12032 C  CA  . ARG D 1 411 ? -9.348  54.992  -4.663  1.00 44.13  ? 411  ARG D CA  1 
ATOM   12033 C  C   . ARG D 1 411 ? -10.529 55.881  -4.294  1.00 39.87  ? 411  ARG D C   1 
ATOM   12034 O  O   . ARG D 1 411 ? -10.779 56.890  -4.953  1.00 38.14  ? 411  ARG D O   1 
ATOM   12035 C  CB  . ARG D 1 411 ? -8.077  55.540  -4.028  1.00 37.20  ? 411  ARG D CB  1 
ATOM   12036 C  CG  . ARG D 1 411 ? -8.263  55.843  -2.567  1.00 37.92  ? 411  ARG D CG  1 
ATOM   12037 C  CD  . ARG D 1 411 ? -8.227  54.567  -1.744  1.00 35.40  ? 411  ARG D CD  1 
ATOM   12038 N  NE  . ARG D 1 411 ? -6.874  54.314  -1.270  1.00 42.74  ? 411  ARG D NE  1 
ATOM   12039 C  CZ  . ARG D 1 411 ? -6.446  54.635  -0.055  1.00 40.46  ? 411  ARG D CZ  1 
ATOM   12040 N  NH1 . ARG D 1 411 ? -7.278  55.191  0.804   1.00 36.51  ? 411  ARG D NH1 1 
ATOM   12041 N  NH2 . ARG D 1 411 ? -5.191  54.394  0.304   1.00 38.88  ? 411  ARG D NH2 1 
ATOM   12042 N  N   . LEU D 1 412 ? -11.242 55.499  -3.238  1.00 46.14  ? 412  LEU D N   1 
ATOM   12043 C  CA  . LEU D 1 412 ? -12.403 56.248  -2.739  1.00 46.09  ? 412  LEU D CA  1 
ATOM   12044 C  C   . LEU D 1 412 ? -12.701 55.826  -1.299  1.00 48.16  ? 412  LEU D C   1 
ATOM   12045 O  O   . LEU D 1 412 ? -13.093 54.675  -1.045  1.00 45.16  ? 412  LEU D O   1 
ATOM   12046 C  CB  . LEU D 1 412 ? -13.630 55.991  -3.619  1.00 40.30  ? 412  LEU D CB  1 
ATOM   12047 C  CG  . LEU D 1 412 ? -14.893 56.790  -3.314  1.00 44.10  ? 412  LEU D CG  1 
ATOM   12048 C  CD1 . LEU D 1 412 ? -14.731 58.232  -3.777  1.00 60.51  ? 412  LEU D CD1 1 
ATOM   12049 C  CD2 . LEU D 1 412 ? -16.083 56.141  -3.986  1.00 28.27  ? 412  LEU D CD2 1 
ATOM   12050 N  N   . ASP D 1 413 ? -12.500 56.741  -0.356  1.00 37.80  ? 413  ASP D N   1 
ATOM   12051 C  CA  . ASP D 1 413 ? -12.589 56.372  1.050   1.00 39.13  ? 413  ASP D CA  1 
ATOM   12052 C  C   . ASP D 1 413 ? -13.817 56.958  1.726   1.00 51.23  ? 413  ASP D C   1 
ATOM   12053 O  O   . ASP D 1 413 ? -14.464 57.860  1.189   1.00 56.87  ? 413  ASP D O   1 
ATOM   12054 C  CB  . ASP D 1 413 ? -11.353 56.840  1.810   1.00 38.57  ? 413  ASP D CB  1 
ATOM   12055 C  CG  . ASP D 1 413 ? -10.105 56.091  1.426   1.00 40.18  ? 413  ASP D CG  1 
ATOM   12056 O  OD1 . ASP D 1 413 ? -10.173 55.145  0.609   1.00 42.10  ? 413  ASP D OD1 1 
ATOM   12057 O  OD2 . ASP D 1 413 ? -9.040  56.463  1.963   1.00 49.00  ? 413  ASP D OD2 1 
ATOM   12058 N  N   . PHE D 1 414 ? -14.104 56.462  2.926   1.00 48.95  ? 414  PHE D N   1 
ATOM   12059 C  CA  . PHE D 1 414 ? -15.221 56.958  3.709   1.00 47.77  ? 414  PHE D CA  1 
ATOM   12060 C  C   . PHE D 1 414 ? -14.892 57.108  5.186   1.00 52.32  ? 414  PHE D C   1 
ATOM   12061 O  O   . PHE D 1 414 ? -14.325 56.202  5.803   1.00 53.81  ? 414  PHE D O   1 
ATOM   12062 C  CB  . PHE D 1 414 ? -16.403 56.017  3.567   1.00 50.19  ? 414  PHE D CB  1 
ATOM   12063 C  CG  . PHE D 1 414 ? -16.884 55.870  2.165   1.00 46.77  ? 414  PHE D CG  1 
ATOM   12064 C  CD1 . PHE D 1 414 ? -16.334 54.923  1.333   1.00 45.45  ? 414  PHE D CD1 1 
ATOM   12065 C  CD2 . PHE D 1 414 ? -17.897 56.679  1.681   1.00 58.46  ? 414  PHE D CD2 1 
ATOM   12066 C  CE1 . PHE D 1 414 ? -16.784 54.781  0.043   1.00 49.85  ? 414  PHE D CE1 1 
ATOM   12067 C  CE2 . PHE D 1 414 ? -18.347 56.547  0.389   1.00 56.79  ? 414  PHE D CE2 1 
ATOM   12068 C  CZ  . PHE D 1 414 ? -17.791 55.599  -0.432  1.00 54.30  ? 414  PHE D CZ  1 
ATOM   12069 N  N   . LYS D 1 415 ? -15.260 58.256  5.744   1.00 39.38  ? 415  LYS D N   1 
ATOM   12070 C  CA  . LYS D 1 415 ? -15.227 58.436  7.181   1.00 43.98  ? 415  LYS D CA  1 
ATOM   12071 C  C   . LYS D 1 415 ? -16.661 58.436  7.686   1.00 52.73  ? 415  LYS D C   1 
ATOM   12072 O  O   . LYS D 1 415 ? -17.527 59.104  7.119   1.00 53.56  ? 415  LYS D O   1 
ATOM   12073 C  CB  . LYS D 1 415 ? -14.515 59.737  7.561   1.00 52.99  ? 415  LYS D CB  1 
ATOM   12074 C  CG  . LYS D 1 415 ? -13.018 59.727  7.281   1.00 68.28  ? 415  LYS D CG  1 
ATOM   12075 C  CD  . LYS D 1 415 ? -12.270 60.722  8.164   1.00 77.34  ? 415  LYS D CD  1 
ATOM   12076 C  CE  . LYS D 1 415 ? -10.771 60.422  8.187   1.00 84.25  ? 415  LYS D CE  1 
ATOM   12077 N  NZ  . LYS D 1 415 ? -10.038 61.236  9.208   1.00 86.27  ? 415  LYS D NZ  1 
ATOM   12078 N  N   . LEU D 1 416 ? -16.917 57.674  8.743   1.00 44.86  ? 416  LEU D N   1 
ATOM   12079 C  CA  . LEU D 1 416 ? -18.256 57.587  9.299   1.00 44.74  ? 416  LEU D CA  1 
ATOM   12080 C  C   . LEU D 1 416 ? -18.262 58.042  10.757  1.00 50.32  ? 416  LEU D C   1 
ATOM   12081 O  O   . LEU D 1 416 ? -17.375 57.686  11.528  1.00 52.22  ? 416  LEU D O   1 
ATOM   12082 C  CB  . LEU D 1 416 ? -18.787 56.149  9.204   1.00 53.83  ? 416  LEU D CB  1 
ATOM   12083 C  CG  . LEU D 1 416 ? -18.715 55.375  7.879   1.00 43.16  ? 416  LEU D CG  1 
ATOM   12084 C  CD1 . LEU D 1 416 ? -19.378 54.007  8.020   1.00 37.28  ? 416  LEU D CD1 1 
ATOM   12085 C  CD2 . LEU D 1 416 ? -19.349 56.157  6.745   1.00 39.62  ? 416  LEU D CD2 1 
ATOM   12086 N  N   . ALA D 1 417 ? -19.269 58.825  11.137  1.00 57.69  ? 417  ALA D N   1 
ATOM   12087 C  CA  . ALA D 1 417 ? -19.425 59.255  12.530  1.00 46.61  ? 417  ALA D CA  1 
ATOM   12088 C  C   . ALA D 1 417 ? -20.236 58.224  13.307  1.00 47.39  ? 417  ALA D C   1 
ATOM   12089 O  O   . ALA D 1 417 ? -21.110 57.567  12.738  1.00 55.04  ? 417  ALA D O   1 
ATOM   12090 C  CB  . ALA D 1 417 ? -20.096 60.621  12.596  1.00 37.09  ? 417  ALA D CB  1 
ATOM   12091 N  N   . PRO D 1 418 ? -19.953 58.076  14.615  1.00 70.53  ? 418  PRO D N   1 
ATOM   12092 C  CA  . PRO D 1 418 ? -20.664 57.049  15.377  1.00 57.99  ? 418  PRO D CA  1 
ATOM   12093 C  C   . PRO D 1 418 ? -22.002 57.629  15.745  1.00 49.11  ? 418  PRO D C   1 
ATOM   12094 O  O   . PRO D 1 418 ? -22.129 58.849  15.764  1.00 46.59  ? 418  PRO D O   1 
ATOM   12095 C  CB  . PRO D 1 418 ? -19.818 56.924  16.633  1.00 46.49  ? 418  PRO D CB  1 
ATOM   12096 C  CG  . PRO D 1 418 ? -19.372 58.336  16.875  1.00 47.28  ? 418  PRO D CG  1 
ATOM   12097 C  CD  . PRO D 1 418 ? -19.161 58.953  15.499  1.00 59.40  ? 418  PRO D CD  1 
ATOM   12098 N  N   . VAL D 1 419 ? -22.986 56.785  16.023  1.00 69.74  ? 419  VAL D N   1 
ATOM   12099 C  CA  . VAL D 1 419 ? -24.278 57.295  16.450  1.00 74.00  ? 419  VAL D CA  1 
ATOM   12100 C  C   . VAL D 1 419 ? -24.240 57.754  17.920  1.00 70.86  ? 419  VAL D C   1 
ATOM   12101 O  O   . VAL D 1 419 ? -23.471 57.227  18.730  1.00 61.91  ? 419  VAL D O   1 
ATOM   12102 C  CB  . VAL D 1 419 ? -25.409 56.283  16.185  1.00 66.60  ? 419  VAL D CB  1 
ATOM   12103 C  CG1 . VAL D 1 419 ? -25.069 54.920  16.779  1.00 51.81  ? 419  VAL D CG1 1 
ATOM   12104 C  CG2 . VAL D 1 419 ? -26.735 56.828  16.707  1.00 42.42  ? 419  VAL D CG2 1 
ATOM   12105 N  N   . GLU D 1 420 ? -25.052 58.760  18.236  1.00 72.25  ? 420  GLU D N   1 
ATOM   12106 C  CA  . GLU D 1 420 ? -25.048 59.393  19.549  1.00 63.10  ? 420  GLU D CA  1 
ATOM   12107 C  C   . GLU D 1 420 ? -23.716 60.082  19.816  1.00 53.79  ? 420  GLU D C   1 
ATOM   12108 O  O   . GLU D 1 420 ? -23.666 61.302  19.989  1.00 59.58  ? 420  GLU D O   1 
ATOM   12109 C  CB  . GLU D 1 420 ? -25.373 58.383  20.655  1.00 63.91  ? 420  GLU D CB  1 
ATOM   12110 C  CG  . GLU D 1 420 ? -25.648 59.013  22.013  1.00 70.35  ? 420  GLU D CG  1 
ATOM   12111 C  CD  . GLU D 1 420 ? -24.420 59.054  22.900  1.00 77.69  ? 420  GLU D CD  1 
ATOM   12112 O  OE1 . GLU D 1 420 ? -24.237 60.059  23.626  1.00 71.72  ? 420  GLU D OE1 1 
ATOM   12113 O  OE2 . GLU D 1 420 ? -23.641 58.076  22.867  1.00 80.02  ? 420  GLU D OE2 1 
HETATM 12114 C  C1  . NAG E 2 .   ? 28.116  -3.838  -3.798  1.00 55.32  ? 501  NAG A C1  1 
HETATM 12115 C  C2  . NAG E 2 .   ? 28.286  -2.432  -3.225  1.00 67.95  ? 501  NAG A C2  1 
HETATM 12116 C  C3  . NAG E 2 .   ? 29.725  -2.116  -2.834  1.00 79.93  ? 501  NAG A C3  1 
HETATM 12117 C  C4  . NAG E 2 .   ? 30.360  -3.296  -2.101  1.00 73.40  ? 501  NAG A C4  1 
HETATM 12118 C  C5  . NAG E 2 .   ? 30.102  -4.591  -2.857  1.00 59.12  ? 501  NAG A C5  1 
HETATM 12119 C  C6  . NAG E 2 .   ? 30.655  -5.778  -2.092  1.00 76.10  ? 501  NAG A C6  1 
HETATM 12120 C  C7  . NAG E 2 .   ? 28.242  -1.059  -5.324  1.00 67.71  ? 501  NAG A C7  1 
HETATM 12121 C  C8  . NAG E 2 .   ? 29.107  -2.017  -6.102  1.00 71.95  ? 501  NAG A C8  1 
HETATM 12122 N  N2  . NAG E 2 .   ? 27.750  -1.424  -4.133  1.00 73.78  ? 501  NAG A N2  1 
HETATM 12123 O  O3  . NAG E 2 .   ? 29.730  -0.962  -2.015  1.00 89.80  ? 501  NAG A O3  1 
HETATM 12124 O  O4  . NAG E 2 .   ? 31.753  -3.104  -1.959  1.00 76.08  ? 501  NAG A O4  1 
HETATM 12125 O  O5  . NAG E 2 .   ? 28.719  -4.796  -2.973  1.00 39.80  ? 501  NAG A O5  1 
HETATM 12126 O  O6  . NAG E 2 .   ? 29.787  -6.019  -1.005  1.00 77.28  ? 501  NAG A O6  1 
HETATM 12127 O  O7  . NAG E 2 .   ? 27.986  0.046   -5.802  1.00 46.04  ? 501  NAG A O7  1 
HETATM 12128 ZN ZN  . ZN  F 3 .   ? 8.313   -16.656 -30.205 1.00 42.65  ? 999  ZN  A ZN  1 
HETATM 12129 C  C8  . GEM G 4 .   ? 3.703   -15.206 -29.745 1.00 57.00  ? 601  GEM A C8  1 
HETATM 12130 S  S7  . GEM G 4 .   ? 4.045   -14.832 -28.048 1.00 57.42  ? 601  GEM A S7  1 
HETATM 12131 C  C6  . GEM G 4 .   ? 3.822   -13.076 -28.052 1.00 51.59  ? 601  GEM A C6  1 
HETATM 12132 C  C5  . GEM G 4 .   ? 2.471   -12.629 -28.606 1.00 34.21  ? 601  GEM A C5  1 
HETATM 12133 N  N3  . GEM G 4 .   ? 1.451   -13.028 -27.649 1.00 36.03  ? 601  GEM A N3  1 
HETATM 12134 C  C1  . GEM G 4 .   ? 0.134   -12.985 -27.820 1.00 43.13  ? 601  GEM A C1  1 
HETATM 12135 N  N4  . GEM G 4 .   ? -0.681  -13.385 -26.852 1.00 32.44  ? 601  GEM A N4  1 
HETATM 12136 N  N2  . GEM G 4 .   ? -0.375  -12.545 -28.966 1.00 48.23  ? 601  GEM A N2  1 
HETATM 12137 C  C9  . GEM G 4 .   ? 3.606   -16.704 -29.861 1.00 64.36  ? 601  GEM A C9  1 
HETATM 12138 O  O14 . GEM G 4 .   ? 3.870   -17.392 -28.850 1.00 32.86  ? 601  GEM A O14 1 
HETATM 12139 O  O15 . GEM G 4 .   ? 3.259   -17.208 -30.950 1.00 65.33  ? 601  GEM A O15 1 
HETATM 12140 C  C10 . GEM G 4 .   ? 4.739   -14.619 -30.718 1.00 45.92  ? 601  GEM A C10 1 
HETATM 12141 C  C11 . GEM G 4 .   ? 6.143   -15.209 -30.669 1.00 54.16  ? 601  GEM A C11 1 
HETATM 12142 O  O12 . GEM G 4 .   ? 7.105   -14.405 -30.603 1.00 39.20  ? 601  GEM A O12 1 
HETATM 12143 O  O13 . GEM G 4 .   ? 6.303   -16.455 -30.733 1.00 33.28  ? 601  GEM A O13 1 
HETATM 12144 C  C1  . GOL H 5 .   ? 13.206  -7.853  11.393  1.00 36.97  ? 801  GOL A C1  1 
HETATM 12145 O  O1  . GOL H 5 .   ? 13.183  -6.741  12.258  1.00 40.50  ? 801  GOL A O1  1 
HETATM 12146 C  C2  . GOL H 5 .   ? 14.537  -7.860  10.662  1.00 35.00  ? 801  GOL A C2  1 
HETATM 12147 O  O2  . GOL H 5 .   ? 14.523  -6.841  9.680   1.00 40.75  ? 801  GOL A O2  1 
HETATM 12148 C  C3  . GOL H 5 .   ? 14.770  -9.229  10.027  1.00 30.10  ? 801  GOL A C3  1 
HETATM 12149 O  O3  . GOL H 5 .   ? 16.151  -9.390  9.744   1.00 38.14  ? 801  GOL A O3  1 
HETATM 12150 C  C1  . GOL I 5 .   ? -11.765 -4.628  -36.819 1.00 64.17  ? 802  GOL A C1  1 
HETATM 12151 O  O1  . GOL I 5 .   ? -10.956 -4.659  -35.662 1.00 67.89  ? 802  GOL A O1  1 
HETATM 12152 C  C2  . GOL I 5 .   ? -11.953 -6.048  -37.349 1.00 58.05  ? 802  GOL A C2  1 
HETATM 12153 O  O2  . GOL I 5 .   ? -13.335 -6.345  -37.397 1.00 54.64  ? 802  GOL A O2  1 
HETATM 12154 C  C3  . GOL I 5 .   ? -11.253 -7.036  -36.417 1.00 53.08  ? 802  GOL A C3  1 
HETATM 12155 O  O3  . GOL I 5 .   ? -11.098 -8.276  -37.074 1.00 53.83  ? 802  GOL A O3  1 
HETATM 12156 C  C1  . GOL J 5 .   ? 19.393  6.024   -14.433 1.00 56.16  ? 803  GOL A C1  1 
HETATM 12157 O  O1  . GOL J 5 .   ? 20.465  6.937   -14.279 1.00 58.39  ? 803  GOL A O1  1 
HETATM 12158 C  C2  . GOL J 5 .   ? 18.078  6.773   -14.658 1.00 59.50  ? 803  GOL A C2  1 
HETATM 12159 O  O2  . GOL J 5 .   ? 18.107  8.044   -14.032 1.00 40.51  ? 803  GOL A O2  1 
HETATM 12160 C  C3  . GOL J 5 .   ? 16.891  5.954   -14.140 1.00 61.28  ? 803  GOL A C3  1 
HETATM 12161 O  O3  . GOL J 5 .   ? 15.680  6.515   -14.612 1.00 49.13  ? 803  GOL A O3  1 
HETATM 12162 C  C1  . NAG K 2 .   ? -2.434  -35.877 13.977  1.00 61.83  ? 501  NAG B C1  1 
HETATM 12163 C  C2  . NAG K 2 .   ? -2.540  -36.400 15.416  1.00 67.46  ? 501  NAG B C2  1 
HETATM 12164 C  C3  . NAG K 2 .   ? -3.917  -36.242 16.062  1.00 72.75  ? 501  NAG B C3  1 
HETATM 12165 C  C4  . NAG K 2 .   ? -4.659  -34.989 15.607  1.00 83.06  ? 501  NAG B C4  1 
HETATM 12166 C  C5  . NAG K 2 .   ? -4.472  -34.694 14.127  1.00 67.09  ? 501  NAG B C5  1 
HETATM 12167 C  C6  . NAG K 2 .   ? -5.003  -33.307 13.816  1.00 68.00  ? 501  NAG B C6  1 
HETATM 12168 C  C7  . NAG K 2 .   ? -2.887  -38.858 15.328  1.00 57.07  ? 501  NAG B C7  1 
HETATM 12169 C  C8  . NAG K 2 .   ? -3.711  -38.949 14.072  1.00 44.15  ? 501  NAG B C8  1 
HETATM 12170 N  N2  . NAG K 2 .   ? -2.096  -37.789 15.468  1.00 65.76  ? 501  NAG B N2  1 
HETATM 12171 O  O3  . NAG K 2 .   ? -3.756  -36.165 17.463  1.00 66.43  ? 501  NAG B O3  1 
HETATM 12172 O  O4  . NAG K 2 .   ? -6.041  -35.142 15.866  1.00 97.70  ? 501  NAG B O4  1 
HETATM 12173 O  O5  . NAG K 2 .   ? -3.106  -34.655 13.804  1.00 63.17  ? 501  NAG B O5  1 
HETATM 12174 O  O6  . NAG K 2 .   ? -3.898  -32.435 13.731  1.00 61.62  ? 501  NAG B O6  1 
HETATM 12175 O  O7  . NAG K 2 .   ? -2.939  -39.757 16.169  1.00 51.83  ? 501  NAG B O7  1 
HETATM 12176 ZN ZN  . ZN  L 3 .   ? 22.149  -52.081 -6.384  1.00 38.83  ? 999  ZN  B ZN  1 
HETATM 12177 C  C8  . GEM M 4 .   ? 26.475  -51.566 -4.442  1.00 23.26  ? 601  GEM B C8  1 
HETATM 12178 S  S7  . GEM M 4 .   ? 25.611  -50.415 -3.433  1.00 36.43  ? 601  GEM B S7  1 
HETATM 12179 C  C6  . GEM M 4 .   ? 25.527  -51.317 -1.917  1.00 57.34  ? 601  GEM B C6  1 
HETATM 12180 C  C5  . GEM M 4 .   ? 26.901  -51.819 -1.481  1.00 47.09  ? 601  GEM B C5  1 
HETATM 12181 N  N3  . GEM M 4 .   ? 27.703  -50.678 -1.055  1.00 41.08  ? 601  GEM B N3  1 
HETATM 12182 C  C1  . GEM M 4 .   ? 29.034  -50.668 -0.972  1.00 22.82  ? 601  GEM B C1  1 
HETATM 12183 N  N4  . GEM M 4 .   ? 29.683  -49.584 -0.579  1.00 22.60  ? 601  GEM B N4  1 
HETATM 12184 N  N2  . GEM M 4 .   ? 29.717  -51.754 -1.304  1.00 22.95  ? 601  GEM B N2  1 
HETATM 12185 C  C9  . GEM M 4 .   ? 26.433  -50.974 -5.802  1.00 40.89  ? 601  GEM B C9  1 
HETATM 12186 O  O14 . GEM M 4 .   ? 25.830  -49.883 -5.934  1.00 31.92  ? 601  GEM B O14 1 
HETATM 12187 O  O15 . GEM M 4 .   ? 26.978  -51.600 -6.740  1.00 47.47  ? 601  GEM B O15 1 
HETATM 12188 C  C10 . GEM M 4 .   ? 25.733  -52.891 -4.475  1.00 23.54  ? 601  GEM B C10 1 
HETATM 12189 C  C11 . GEM M 4 .   ? 24.349  -52.678 -5.041  1.00 34.92  ? 601  GEM B C11 1 
HETATM 12190 O  O12 . GEM M 4 .   ? 23.410  -52.675 -4.214  1.00 32.88  ? 601  GEM B O12 1 
HETATM 12191 O  O13 . GEM M 4 .   ? 24.200  -52.503 -6.286  1.00 24.91  ? 601  GEM B O13 1 
HETATM 12192 C  C1  . NAG N 2 .   ? -23.202 42.986  28.532  1.00 69.57  ? 501  NAG C C1  1 
HETATM 12193 C  C2  . NAG N 2 .   ? -23.817 43.554  29.824  1.00 61.43  ? 501  NAG C C2  1 
HETATM 12194 C  C3  . NAG N 2 .   ? -25.262 44.061  29.695  1.00 71.71  ? 501  NAG C C3  1 
HETATM 12195 C  C4  . NAG N 2 .   ? -25.363 44.826  28.393  1.00 64.64  ? 501  NAG C C4  1 
HETATM 12196 C  C5  . NAG N 2 .   ? -25.146 43.787  27.312  1.00 59.71  ? 501  NAG C C5  1 
HETATM 12197 C  C6  . NAG N 2 .   ? -25.576 44.304  25.945  1.00 58.28  ? 501  NAG C C6  1 
HETATM 12198 C  C7  . NAG N 2 .   ? -24.458 41.476  31.052  1.00 100.01 ? 501  NAG C C7  1 
HETATM 12199 C  C8  . NAG N 2 .   ? -25.185 40.877  29.877  1.00 105.70 ? 501  NAG C C8  1 
HETATM 12200 N  N2  . NAG N 2 .   ? -23.671 42.549  30.866  1.00 74.18  ? 501  NAG C N2  1 
HETATM 12201 O  O3  . NAG N 2 .   ? -25.681 44.895  30.761  1.00 72.24  ? 501  NAG C O3  1 
HETATM 12202 O  O4  . NAG N 2 .   ? -26.616 45.462  28.282  1.00 67.23  ? 501  NAG C O4  1 
HETATM 12203 O  O5  . NAG N 2 .   ? -23.775 43.436  27.307  1.00 74.69  ? 501  NAG C O5  1 
HETATM 12204 O  O6  . NAG N 2 .   ? -24.726 45.356  25.539  1.00 68.82  ? 501  NAG C O6  1 
HETATM 12205 O  O7  . NAG N 2 .   ? -24.590 40.952  32.161  1.00 104.83 ? 501  NAG C O7  1 
HETATM 12206 ZN ZN  . ZN  O 3 .   ? -2.356  13.980  27.833  1.00 42.41  ? 999  ZN  C ZN  1 
HETATM 12207 C  C8  . GEM P 4 .   ? 2.162   15.121  28.949  1.00 38.10  ? 601  GEM C C8  1 
HETATM 12208 S  S7  . GEM P 4 .   ? 1.681   16.775  28.570  1.00 44.10  ? 601  GEM C S7  1 
HETATM 12209 C  C6  . GEM P 4 .   ? 1.914   17.563  30.138  1.00 48.73  ? 601  GEM C C6  1 
HETATM 12210 C  C5  . GEM P 4 .   ? 3.046   18.581  30.051  1.00 47.28  ? 601  GEM C C5  1 
HETATM 12211 N  N3  . GEM P 4 .   ? 4.176   17.794  30.517  1.00 54.00  ? 601  GEM C N3  1 
HETATM 12212 C  C1  . GEM P 4 .   ? 5.470   18.082  30.427  1.00 46.28  ? 601  GEM C C1  1 
HETATM 12213 N  N4  . GEM P 4 .   ? 6.389   17.250  30.912  1.00 46.77  ? 601  GEM C N4  1 
HETATM 12214 N  N2  . GEM P 4 .   ? 5.842   19.206  29.847  1.00 37.61  ? 601  GEM C N2  1 
HETATM 12215 C  C9  . GEM P 4 .   ? 2.225   14.358  27.661  1.00 35.97  ? 601  GEM C C9  1 
HETATM 12216 O  O14 . GEM P 4 .   ? 1.506   14.725  26.705  1.00 41.75  ? 601  GEM C O14 1 
HETATM 12217 O  O15 . GEM P 4 .   ? 3.000   13.384  27.587  1.00 58.94  ? 601  GEM C O15 1 
HETATM 12218 C  C10 . GEM P 4 .   ? 1.197   14.469  29.938  1.00 36.19  ? 601  GEM C C10 1 
HETATM 12219 C  C11 . GEM P 4 .   ? -0.182  14.238  29.369  1.00 46.56  ? 601  GEM C C11 1 
HETATM 12220 O  O12 . GEM P 4 .   ? -1.160  14.650  30.030  1.00 59.01  ? 601  GEM C O12 1 
HETATM 12221 O  O13 . GEM P 4 .   ? -0.320  13.633  28.285  1.00 38.13  ? 601  GEM C O13 1 
HETATM 12222 C  C1  . GOL Q 5 .   ? 0.658   9.771   30.985  1.00 63.91  ? 804  GOL C C1  1 
HETATM 12223 O  O1  . GOL Q 5 .   ? -0.017  10.796  30.271  1.00 52.23  ? 804  GOL C O1  1 
HETATM 12224 C  C2  . GOL Q 5 .   ? 1.264   10.368  32.254  1.00 69.76  ? 804  GOL C C2  1 
HETATM 12225 O  O2  . GOL Q 5 .   ? 1.183   9.477   33.359  1.00 44.93  ? 804  GOL C O2  1 
HETATM 12226 C  C3  . GOL Q 5 .   ? 0.532   11.678  32.540  1.00 65.37  ? 804  GOL C C3  1 
HETATM 12227 O  O3  . GOL Q 5 .   ? 1.363   12.531  33.291  1.00 63.37  ? 804  GOL C O3  1 
HETATM 12228 C  C1  . NAG R 2 .   ? 7.725   45.636  -7.873  1.00 78.45  ? 501  NAG D C1  1 
HETATM 12229 C  C2  . NAG R 2 .   ? 8.040   46.831  -8.784  1.00 88.99  ? 501  NAG D C2  1 
HETATM 12230 C  C3  . NAG R 2 .   ? 9.521   47.193  -8.853  1.00 91.92  ? 501  NAG D C3  1 
HETATM 12231 C  C4  . NAG R 2 .   ? 10.120  47.243  -7.460  1.00 110.34 ? 501  NAG D C4  1 
HETATM 12232 C  C5  . NAG R 2 .   ? 9.744   46.003  -6.641  1.00 102.36 ? 501  NAG D C5  1 
HETATM 12233 C  C6  . NAG R 2 .   ? 10.246  46.152  -5.210  1.00 114.37 ? 501  NAG D C6  1 
HETATM 12234 C  C7  . NAG R 2 .   ? 8.022   45.731  -11.019 1.00 117.60 ? 501  NAG D C7  1 
HETATM 12235 C  C8  . NAG R 2 .   ? 8.948   44.635  -10.564 1.00 115.64 ? 501  NAG D C8  1 
HETATM 12236 N  N2  . NAG R 2 .   ? 7.519   46.588  -10.120 1.00 107.30 ? 501  NAG D N2  1 
HETATM 12237 O  O3  . NAG R 2 .   ? 9.705   48.445  -9.482  1.00 81.54  ? 501  NAG D O3  1 
HETATM 12238 O  O4  . NAG R 2 .   ? 11.527  47.365  -7.592  1.00 121.05 ? 501  NAG D O4  1 
HETATM 12239 O  O5  . NAG R 2 .   ? 8.348   45.766  -6.607  1.00 83.47  ? 501  NAG D O5  1 
HETATM 12240 O  O6  . NAG R 2 .   ? 10.051  47.480  -4.767  1.00 119.90 ? 501  NAG D O6  1 
HETATM 12241 O  O7  . NAG R 2 .   ? 7.730   45.811  -12.213 1.00 125.32 ? 501  NAG D O7  1 
HETATM 12242 ZN ZN  . ZN  S 3 .   ? -16.454 20.128  -14.356 1.00 33.83  ? 999  ZN  D ZN  1 
HETATM 12243 C  C8  . GEM T 4 .   ? -20.862 21.979  -15.053 1.00 41.98  ? 601  GEM D C8  1 
HETATM 12244 S  S7  . GEM T 4 .   ? -20.164 23.485  -14.413 1.00 42.13  ? 601  GEM D S7  1 
HETATM 12245 C  C6  . GEM T 4 .   ? -20.419 24.739  -15.624 1.00 38.81  ? 601  GEM D C6  1 
HETATM 12246 C  C5  . GEM T 4 .   ? -21.365 25.791  -15.057 1.00 38.18  ? 601  GEM D C5  1 
HETATM 12247 N  N3  . GEM T 4 .   ? -22.608 25.293  -15.624 1.00 55.95  ? 601  GEM D N3  1 
HETATM 12248 C  C1  . GEM T 4 .   ? -23.884 25.459  -15.281 1.00 50.40  ? 601  GEM D C1  1 
HETATM 12249 N  N4  . GEM T 4 .   ? -24.798 24.858  -16.023 1.00 47.12  ? 601  GEM D N4  1 
HETATM 12250 N  N2  . GEM T 4 .   ? -24.264 26.186  -14.234 1.00 29.67  ? 601  GEM D N2  1 
HETATM 12251 C  C9  . GEM T 4 .   ? -21.120 20.977  -13.944 1.00 27.80  ? 601  GEM D C9  1 
HETATM 12252 O  O14 . GEM T 4 .   ? -20.891 21.272  -12.753 1.00 41.90  ? 601  GEM D O14 1 
HETATM 12253 O  O15 . GEM T 4 .   ? -21.569 19.856  -14.254 1.00 68.13  ? 601  GEM D O15 1 
HETATM 12254 C  C10 . GEM T 4 .   ? -19.988 21.328  -16.129 1.00 28.12  ? 601  GEM D C10 1 
HETATM 12255 C  C11 . GEM T 4 .   ? -18.648 20.790  -15.669 1.00 38.28  ? 601  GEM D C11 1 
HETATM 12256 O  O12 . GEM T 4 .   ? -17.671 21.079  -16.411 1.00 40.97  ? 601  GEM D O12 1 
HETATM 12257 O  O13 . GEM T 4 .   ? -18.549 20.076  -14.634 1.00 27.81  ? 601  GEM D O13 1 
HETATM 12258 O  O   . HOH U 6 .   ? 27.915  -28.917 -28.439 1.00 38.09  ? 1001 HOH A O   1 
HETATM 12259 O  O   . HOH U 6 .   ? 15.168  -18.482 -2.508  1.00 17.00  ? 1002 HOH A O   1 
HETATM 12260 O  O   . HOH U 6 .   ? 11.738  -17.003 -25.163 1.00 28.12  ? 1003 HOH A O   1 
HETATM 12261 O  O   . HOH U 6 .   ? -2.221  -19.566 -18.415 1.00 42.82  ? 1004 HOH A O   1 
HETATM 12262 O  O   . HOH U 6 .   ? -4.929  -25.468 -15.110 1.00 24.39  ? 1005 HOH A O   1 
HETATM 12263 O  O   . HOH U 6 .   ? 3.966   -14.804 -24.529 1.00 28.93  ? 1006 HOH A O   1 
HETATM 12264 O  O   . HOH U 6 .   ? 6.643   5.461   -12.392 1.00 34.98  ? 1007 HOH A O   1 
HETATM 12265 O  O   . HOH U 6 .   ? -3.657  0.352   -17.314 1.00 60.09  ? 1008 HOH A O   1 
HETATM 12266 O  O   . HOH U 6 .   ? 11.087  -10.265 -41.817 1.00 51.55  ? 1009 HOH A O   1 
HETATM 12267 O  O   . HOH U 6 .   ? -3.141  1.034   11.871  1.00 39.76  ? 1010 HOH A O   1 
HETATM 12268 O  O   . HOH U 6 .   ? 31.821  -12.248 -2.752  1.00 30.59  ? 1011 HOH A O   1 
HETATM 12269 O  O   . HOH U 6 .   ? -1.323  -18.405 -22.712 1.00 30.28  ? 1012 HOH A O   1 
HETATM 12270 O  O   . HOH U 6 .   ? 0.773   -37.829 -17.399 1.00 33.24  ? 1013 HOH A O   1 
HETATM 12271 O  O   . HOH U 6 .   ? 3.299   -12.576 -17.120 1.00 20.14  ? 1014 HOH A O   1 
HETATM 12272 O  O   . HOH U 6 .   ? 6.731   8.426   -12.448 1.00 26.00  ? 1015 HOH A O   1 
HETATM 12273 O  O   . HOH U 6 .   ? 8.423   7.260   -30.377 1.00 35.77  ? 1016 HOH A O   1 
HETATM 12274 O  O   . HOH U 6 .   ? -2.697  -19.259 -30.697 1.00 17.82  ? 1017 HOH A O   1 
HETATM 12275 O  O   . HOH U 6 .   ? -1.225  -16.850 -34.764 1.00 32.90  ? 1018 HOH A O   1 
HETATM 12276 O  O   . HOH U 6 .   ? 2.079   -18.543 -35.450 1.00 35.57  ? 1019 HOH A O   1 
HETATM 12277 O  O   . HOH U 6 .   ? 1.855   -21.564 -34.092 1.00 45.36  ? 1020 HOH A O   1 
HETATM 12278 O  O   . HOH U 6 .   ? 2.937   -16.015 -34.753 1.00 33.99  ? 1021 HOH A O   1 
HETATM 12279 O  O   . HOH U 6 .   ? 20.613  0.929   -24.686 1.00 26.22  ? 1022 HOH A O   1 
HETATM 12280 O  O   . HOH U 6 .   ? 8.603   -4.552  -4.599  1.00 35.35  ? 1023 HOH A O   1 
HETATM 12281 O  O   . HOH U 6 .   ? 9.985   2.304   -3.773  1.00 57.01  ? 1024 HOH A O   1 
HETATM 12282 O  O   . HOH U 6 .   ? 4.044   -20.352 7.701   1.00 34.13  ? 1025 HOH A O   1 
HETATM 12283 O  O   . HOH U 6 .   ? 14.027  2.146   -7.860  1.00 62.86  ? 1026 HOH A O   1 
HETATM 12284 O  O   . HOH U 6 .   ? 17.563  -18.496 -2.512  1.00 41.89  ? 1027 HOH A O   1 
HETATM 12285 O  O   . HOH U 6 .   ? -1.619  -0.931  11.491  1.00 28.89  ? 1028 HOH A O   1 
HETATM 12286 O  O   . HOH U 6 .   ? 18.230  -6.421  -0.500  1.00 40.62  ? 1029 HOH A O   1 
HETATM 12287 O  O   . HOH U 6 .   ? -0.987  -13.478 -35.760 1.00 29.88  ? 1030 HOH A O   1 
HETATM 12288 O  O   . HOH U 6 .   ? 6.507   -10.817 -6.185  1.00 33.51  ? 1031 HOH A O   1 
HETATM 12289 O  O   . HOH U 6 .   ? -17.015 -11.366 -26.710 1.00 25.29  ? 1032 HOH A O   1 
HETATM 12290 O  O   . HOH U 6 .   ? -17.373 -17.031 -25.616 1.00 53.96  ? 1033 HOH A O   1 
HETATM 12291 O  O   . HOH U 6 .   ? -17.080 -14.441 -26.420 1.00 34.93  ? 1034 HOH A O   1 
HETATM 12292 O  O   . HOH U 6 .   ? -2.284  3.581   -17.464 1.00 25.63  ? 1035 HOH A O   1 
HETATM 12293 O  O   . HOH U 6 .   ? 7.597   8.584   -20.707 1.00 46.15  ? 1036 HOH A O   1 
HETATM 12294 O  O   . HOH U 6 .   ? 8.297   11.811  -22.242 1.00 57.64  ? 1037 HOH A O   1 
HETATM 12295 O  O   . HOH U 6 .   ? 5.393   -2.030  -33.954 1.00 48.46  ? 1038 HOH A O   1 
HETATM 12296 O  O   . HOH U 6 .   ? 6.482   -12.676 -1.800  1.00 49.45  ? 1039 HOH A O   1 
HETATM 12297 O  O   . HOH U 6 .   ? 19.891  2.289   -32.977 1.00 23.99  ? 1040 HOH A O   1 
HETATM 12298 O  O   . HOH U 6 .   ? 11.597  -4.541  -4.524  1.00 37.33  ? 1041 HOH A O   1 
HETATM 12299 O  O   . HOH U 6 .   ? 9.121   -18.945 17.425  1.00 64.68  ? 1042 HOH A O   1 
HETATM 12300 O  O   . HOH U 6 .   ? 7.001   -19.657 16.173  1.00 41.08  ? 1043 HOH A O   1 
HETATM 12301 O  O   . HOH U 6 .   ? -5.358  0.674   -5.836  1.00 28.32  ? 1044 HOH A O   1 
HETATM 12302 O  O   . HOH U 6 .   ? -1.189  -8.053  -3.500  1.00 28.98  ? 1045 HOH A O   1 
HETATM 12303 O  O   . HOH U 6 .   ? -9.492  -7.817  5.249   1.00 18.33  ? 1046 HOH A O   1 
HETATM 12304 O  O   . HOH U 6 .   ? -8.931  -5.442  6.100   1.00 31.67  ? 1047 HOH A O   1 
HETATM 12305 O  O   . HOH U 6 .   ? -1.569  -20.176 14.337  1.00 38.73  ? 1048 HOH A O   1 
HETATM 12306 O  O   . HOH U 6 .   ? 37.136  -12.808 -33.476 1.00 64.58  ? 1049 HOH A O   1 
HETATM 12307 O  O   . HOH U 6 .   ? 3.045   -31.228 -24.699 1.00 27.56  ? 1050 HOH A O   1 
HETATM 12308 O  O   . HOH V 6 .   ? 4.118   -31.517 10.813  1.00 27.84  ? 1001 HOH B O   1 
HETATM 12309 O  O   . HOH V 6 .   ? 10.939  -27.783 3.126   1.00 16.60  ? 1002 HOH B O   1 
HETATM 12310 O  O   . HOH V 6 .   ? -0.455  -47.785 18.028  1.00 40.69  ? 1003 HOH B O   1 
HETATM 12311 O  O   . HOH V 6 .   ? -4.875  -45.918 0.759   1.00 38.95  ? 1004 HOH B O   1 
HETATM 12312 O  O   . HOH V 6 .   ? 10.192  -54.689 -16.538 1.00 35.21  ? 1005 HOH B O   1 
HETATM 12313 O  O   . HOH V 6 .   ? 20.786  -44.337 -24.967 1.00 23.99  ? 1006 HOH B O   1 
HETATM 12314 O  O   . HOH V 6 .   ? 34.430  -36.411 2.440   1.00 33.27  ? 1007 HOH B O   1 
HETATM 12315 O  O   . HOH V 6 .   ? 31.229  -38.625 -2.195  1.00 39.07  ? 1008 HOH B O   1 
HETATM 12316 O  O   . HOH V 6 .   ? 20.312  -28.879 1.245   1.00 33.23  ? 1009 HOH B O   1 
HETATM 12317 O  O   . HOH V 6 .   ? 19.042  -26.675 3.056   1.00 57.88  ? 1010 HOH B O   1 
HETATM 12318 O  O   . HOH V 6 .   ? 25.901  -46.571 18.202  1.00 28.16  ? 1011 HOH B O   1 
HETATM 12319 O  O   . HOH V 6 .   ? 20.603  -49.265 17.561  1.00 31.54  ? 1012 HOH B O   1 
HETATM 12320 O  O   . HOH V 6 .   ? 22.025  -60.024 7.083   1.00 34.63  ? 1013 HOH B O   1 
HETATM 12321 O  O   . HOH V 6 .   ? 30.473  -59.993 -0.938  1.00 32.16  ? 1014 HOH B O   1 
HETATM 12322 O  O   . HOH V 6 .   ? 23.993  -45.275 -1.895  1.00 39.77  ? 1015 HOH B O   1 
HETATM 12323 O  O   . HOH V 6 .   ? 21.922  -34.930 12.306  1.00 37.34  ? 1016 HOH B O   1 
HETATM 12324 O  O   . HOH V 6 .   ? 5.891   -46.231 13.729  1.00 35.58  ? 1017 HOH B O   1 
HETATM 12325 O  O   . HOH V 6 .   ? 11.516  -34.659 16.250  1.00 29.12  ? 1018 HOH B O   1 
HETATM 12326 O  O   . HOH V 6 .   ? 26.501  -30.698 13.888  1.00 21.05  ? 1019 HOH B O   1 
HETATM 12327 O  O   . HOH V 6 .   ? 19.329  -28.287 9.549   1.00 41.08  ? 1020 HOH B O   1 
HETATM 12328 O  O   . HOH V 6 .   ? 20.816  -19.235 23.098  1.00 62.48  ? 1021 HOH B O   1 
HETATM 12329 O  O   . HOH V 6 .   ? 6.225   -42.678 19.516  1.00 32.36  ? 1022 HOH B O   1 
HETATM 12330 O  O   . HOH V 6 .   ? 28.011  -46.619 -25.927 1.00 38.04  ? 1023 HOH B O   1 
HETATM 12331 O  O   . HOH V 6 .   ? -4.121  -58.505 2.169   1.00 28.07  ? 1024 HOH B O   1 
HETATM 12332 O  O   . HOH V 6 .   ? 9.526   -43.129 -7.993  1.00 30.30  ? 1025 HOH B O   1 
HETATM 12333 O  O   . HOH V 6 .   ? 13.339  -36.755 27.181  1.00 35.02  ? 1026 HOH B O   1 
HETATM 12334 O  O   . HOH V 6 .   ? 8.145   -42.281 -22.671 1.00 30.78  ? 1027 HOH B O   1 
HETATM 12335 O  O   . HOH V 6 .   ? 16.870  -58.446 -14.519 1.00 15.89  ? 1028 HOH B O   1 
HETATM 12336 O  O   . HOH V 6 .   ? 27.426  -48.843 -24.807 1.00 33.62  ? 1029 HOH B O   1 
HETATM 12337 O  O   . HOH V 6 .   ? 22.782  -27.758 -10.470 1.00 26.49  ? 1030 HOH B O   1 
HETATM 12338 O  O   . HOH V 6 .   ? 37.108  -47.495 -4.482  1.00 39.14  ? 1031 HOH B O   1 
HETATM 12339 O  O   . HOH V 6 .   ? 36.209  -58.528 4.940   1.00 34.72  ? 1032 HOH B O   1 
HETATM 12340 O  O   . HOH V 6 .   ? 8.032   -39.587 -22.511 1.00 48.49  ? 1033 HOH B O   1 
HETATM 12341 O  O   . HOH V 6 .   ? 3.107   -43.455 19.363  1.00 63.32  ? 1034 HOH B O   1 
HETATM 12342 O  O   . HOH V 6 .   ? 25.211  -70.735 -2.445  1.00 41.70  ? 1035 HOH B O   1 
HETATM 12343 O  O   . HOH V 6 .   ? 24.034  -40.855 -21.552 1.00 30.14  ? 1036 HOH B O   1 
HETATM 12344 O  O   . HOH V 6 .   ? -7.246  -33.342 4.629   1.00 61.74  ? 1037 HOH B O   1 
HETATM 12345 O  O   . HOH V 6 .   ? 15.624  -56.342 -4.454  1.00 33.57  ? 1038 HOH B O   1 
HETATM 12346 O  O   . HOH V 6 .   ? 10.004  -31.979 -3.539  1.00 60.67  ? 1039 HOH B O   1 
HETATM 12347 O  O   . HOH V 6 .   ? 43.291  -52.781 -2.878  1.00 16.17  ? 1040 HOH B O   1 
HETATM 12348 O  O   . HOH V 6 .   ? 31.811  -52.925 8.602   1.00 23.10  ? 1041 HOH B O   1 
HETATM 12349 O  O   . HOH V 6 .   ? 32.620  -38.832 19.118  1.00 34.68  ? 1042 HOH B O   1 
HETATM 12350 O  O   . HOH V 6 .   ? 33.858  -47.407 -7.966  1.00 20.49  ? 1043 HOH B O   1 
HETATM 12351 O  O   . HOH V 6 .   ? 33.239  -50.734 -7.304  1.00 22.23  ? 1044 HOH B O   1 
HETATM 12352 O  O   . HOH V 6 .   ? 33.009  -49.679 -9.650  1.00 45.54  ? 1045 HOH B O   1 
HETATM 12353 O  O   . HOH V 6 .   ? 3.005   -37.938 -14.001 1.00 56.08  ? 1046 HOH B O   1 
HETATM 12354 O  O   . HOH V 6 .   ? 32.362  -34.496 6.656   1.00 30.78  ? 1047 HOH B O   1 
HETATM 12355 O  O   . HOH V 6 .   ? 32.036  -36.197 4.447   1.00 25.30  ? 1048 HOH B O   1 
HETATM 12356 O  O   . HOH V 6 .   ? 24.907  -45.599 -25.058 1.00 47.17  ? 1049 HOH B O   1 
HETATM 12357 O  O   . HOH V 6 .   ? -10.052 -37.449 1.822   1.00 37.03  ? 1050 HOH B O   1 
HETATM 12358 O  O   . HOH V 6 .   ? 6.692   -49.858 -16.785 1.00 31.24  ? 1051 HOH B O   1 
HETATM 12359 O  O   . HOH V 6 .   ? 18.394  -43.869 20.557  1.00 48.74  ? 1052 HOH B O   1 
HETATM 12360 O  O   . HOH V 6 .   ? 22.709  -13.044 22.343  1.00 34.23  ? 1053 HOH B O   1 
HETATM 12361 O  O   . HOH V 6 .   ? 25.576  -7.276  19.736  1.00 37.76  ? 1054 HOH B O   1 
HETATM 12362 O  O   . HOH W 6 .   ? -29.848 23.763  38.254  1.00 25.65  ? 1001 HOH C O   1 
HETATM 12363 O  O   . HOH W 6 .   ? -9.827  37.593  14.823  1.00 20.36  ? 1002 HOH C O   1 
HETATM 12364 O  O   . HOH W 6 .   ? -6.434  15.300  27.771  1.00 44.73  ? 1003 HOH C O   1 
HETATM 12365 O  O   . HOH W 6 .   ? -9.457  16.086  28.185  1.00 35.61  ? 1004 HOH C O   1 
HETATM 12366 O  O   . HOH W 6 .   ? -16.591 6.542   23.895  1.00 27.93  ? 1005 HOH C O   1 
HETATM 12367 O  O   . HOH W 6 .   ? -28.084 18.959  26.922  1.00 33.38  ? 1006 HOH C O   1 
HETATM 12368 O  O   . HOH W 6 .   ? -12.375 43.598  26.234  1.00 28.34  ? 1007 HOH C O   1 
HETATM 12369 O  O   . HOH W 6 .   ? -15.626 36.476  15.076  1.00 26.98  ? 1008 HOH C O   1 
HETATM 12370 O  O   . HOH W 6 .   ? -2.769  12.088  20.684  1.00 19.74  ? 1009 HOH C O   1 
HETATM 12371 O  O   . HOH W 6 .   ? -1.038  38.414  23.768  1.00 17.93  ? 1010 HOH C O   1 
HETATM 12372 O  O   . HOH W 6 .   ? -1.755  41.056  19.558  1.00 24.84  ? 1011 HOH C O   1 
HETATM 12373 O  O   . HOH W 6 .   ? -3.156  47.534  9.346   1.00 28.89  ? 1012 HOH C O   1 
HETATM 12374 O  O   . HOH W 6 .   ? 9.540   44.597  13.878  1.00 48.78  ? 1013 HOH C O   1 
HETATM 12375 O  O   . HOH W 6 .   ? -2.664  38.328  20.839  1.00 27.04  ? 1014 HOH C O   1 
HETATM 12376 O  O   . HOH W 6 .   ? -7.129  10.226  13.859  1.00 19.49  ? 1015 HOH C O   1 
HETATM 12377 O  O   . HOH W 6 .   ? -9.756  2.852   37.925  1.00 49.61  ? 1016 HOH C O   1 
HETATM 12378 O  O   . HOH W 6 .   ? -0.449  0.993   29.457  1.00 40.70  ? 1017 HOH C O   1 
HETATM 12379 O  O   . HOH W 6 .   ? 14.173  20.073  20.243  1.00 34.17  ? 1018 HOH C O   1 
HETATM 12380 O  O   . HOH W 6 .   ? -15.359 31.843  39.619  1.00 42.01  ? 1019 HOH C O   1 
HETATM 12381 O  O   . HOH W 6 .   ? -16.160 35.181  36.335  1.00 22.44  ? 1020 HOH C O   1 
HETATM 12382 O  O   . HOH W 6 .   ? -4.492  41.759  41.494  1.00 33.68  ? 1021 HOH C O   1 
HETATM 12383 O  O   . HOH W 6 .   ? -9.849  53.619  20.890  1.00 34.46  ? 1022 HOH C O   1 
HETATM 12384 O  O   . HOH W 6 .   ? -0.572  3.667   44.294  1.00 58.76  ? 1023 HOH C O   1 
HETATM 12385 O  O   . HOH W 6 .   ? -30.149 48.754  29.452  1.00 42.93  ? 1024 HOH C O   1 
HETATM 12386 O  O   . HOH W 6 .   ? -24.383 14.977  24.995  1.00 40.46  ? 1025 HOH C O   1 
HETATM 12387 O  O   . HOH W 6 .   ? -16.093 45.809  15.849  1.00 29.93  ? 1026 HOH C O   1 
HETATM 12388 O  O   . HOH W 6 .   ? -12.779 46.750  24.746  1.00 32.68  ? 1027 HOH C O   1 
HETATM 12389 O  O   . HOH W 6 .   ? -23.683 37.867  9.518   1.00 36.09  ? 1028 HOH C O   1 
HETATM 12390 O  O   . HOH W 6 .   ? -18.032 2.856   31.577  1.00 55.96  ? 1029 HOH C O   1 
HETATM 12391 O  O   . HOH W 6 .   ? -8.016  1.537   33.811  1.00 96.93  ? 1030 HOH C O   1 
HETATM 12392 O  O   . HOH W 6 .   ? -12.467 11.523  38.168  1.00 28.44  ? 1031 HOH C O   1 
HETATM 12393 O  O   . HOH W 6 .   ? 6.828   34.667  17.118  1.00 49.33  ? 1032 HOH C O   1 
HETATM 12394 O  O   . HOH W 6 .   ? 6.582   33.554  14.731  1.00 33.39  ? 1033 HOH C O   1 
HETATM 12395 O  O   . HOH W 6 .   ? 6.292   22.814  19.829  1.00 26.35  ? 1034 HOH C O   1 
HETATM 12396 O  O   . HOH W 6 .   ? 17.448  25.898  9.860   1.00 27.48  ? 1035 HOH C O   1 
HETATM 12397 O  O   . HOH W 6 .   ? 1.625   21.199  3.007   1.00 29.79  ? 1036 HOH C O   1 
HETATM 12398 O  O   . HOH W 6 .   ? -2.230  32.063  19.315  1.00 29.47  ? 1037 HOH C O   1 
HETATM 12399 O  O   . HOH W 6 .   ? -9.312  15.284  40.523  1.00 47.12  ? 1038 HOH C O   1 
HETATM 12400 O  O   . HOH W 6 .   ? 7.904   15.611  41.369  1.00 41.23  ? 1039 HOH C O   1 
HETATM 12401 O  O   . HOH W 6 .   ? 6.323   24.634  42.036  1.00 36.95  ? 1040 HOH C O   1 
HETATM 12402 O  O   . HOH W 6 .   ? 9.128   14.426  23.430  1.00 42.84  ? 1041 HOH C O   1 
HETATM 12403 O  O   . HOH W 6 .   ? -21.164 6.439   34.939  1.00 38.98  ? 1042 HOH C O   1 
HETATM 12404 O  O   . HOH W 6 .   ? -3.722  42.242  28.601  1.00 36.31  ? 1043 HOH C O   1 
HETATM 12405 O  O   . HOH W 6 .   ? 6.323   59.779  22.922  1.00 67.67  ? 1044 HOH C O   1 
HETATM 12406 O  O   . HOH W 6 .   ? 3.918   57.571  21.688  1.00 46.68  ? 1045 HOH C O   1 
HETATM 12407 O  O   . HOH W 6 .   ? -9.461  54.241  17.770  1.00 31.06  ? 1046 HOH C O   1 
HETATM 12408 O  O   . HOH W 6 .   ? -15.714 4.545   22.902  1.00 24.49  ? 1047 HOH C O   1 
HETATM 12409 O  O   . HOH W 6 .   ? 13.967  16.939  19.781  1.00 76.23  ? 1048 HOH C O   1 
HETATM 12410 O  O   . HOH W 6 .   ? -31.224 51.412  30.133  1.00 29.22  ? 1049 HOH C O   1 
HETATM 12411 O  O   . HOH W 6 .   ? 0.521   20.367  7.037   1.00 17.70  ? 1050 HOH C O   1 
HETATM 12412 O  O   . HOH W 6 .   ? -28.164 45.899  29.973  1.00 43.94  ? 1051 HOH C O   1 
HETATM 12413 O  O   . HOH X 6 .   ? -10.283 19.551  5.751   1.00 37.18  ? 1001 HOH D O   1 
HETATM 12414 O  O   . HOH X 6 .   ? 4.141   19.279  -17.847 1.00 27.21  ? 1002 HOH D O   1 
HETATM 12415 O  O   . HOH X 6 .   ? -4.628  27.855  4.948   1.00 55.06  ? 1003 HOH D O   1 
HETATM 12416 O  O   . HOH X 6 .   ? 6.682   41.456  7.093   1.00 39.90  ? 1004 HOH D O   1 
HETATM 12417 O  O   . HOH X 6 .   ? 0.475   36.365  3.937   1.00 39.83  ? 1005 HOH D O   1 
HETATM 12418 O  O   . HOH X 6 .   ? -16.768 7.317   -20.858 1.00 36.54  ? 1006 HOH D O   1 
HETATM 12419 O  O   . HOH X 6 .   ? -15.240 37.012  3.060   1.00 48.55  ? 1007 HOH D O   1 
HETATM 12420 O  O   . HOH X 6 .   ? -14.478 44.086  -0.410  1.00 28.16  ? 1008 HOH D O   1 
HETATM 12421 O  O   . HOH X 6 .   ? -25.557 26.311  -7.925  1.00 36.22  ? 1009 HOH D O   1 
HETATM 12422 O  O   . HOH X 6 .   ? -6.916  12.033  -26.079 1.00 24.29  ? 1010 HOH D O   1 
HETATM 12423 O  O   . HOH X 6 .   ? -0.330  10.336  -3.692  1.00 34.75  ? 1011 HOH D O   1 
HETATM 12424 O  O   . HOH X 6 .   ? 12.875  17.446  -25.969 1.00 36.48  ? 1012 HOH D O   1 
HETATM 12425 O  O   . HOH X 6 .   ? -9.497  25.338  4.647   1.00 29.17  ? 1013 HOH D O   1 
HETATM 12426 O  O   . HOH X 6 .   ? -12.775 23.294  -10.452 1.00 30.47  ? 1014 HOH D O   1 
HETATM 12427 O  O   . HOH X 6 .   ? -31.676 31.564  1.728   1.00 37.70  ? 1015 HOH D O   1 
HETATM 12428 O  O   . HOH X 6 .   ? -31.266 28.354  2.434   1.00 25.45  ? 1016 HOH D O   1 
HETATM 12429 O  O   . HOH X 6 .   ? -28.858 28.621  3.060   1.00 30.52  ? 1017 HOH D O   1 
HETATM 12430 O  O   . HOH X 6 .   ? -24.858 53.039  -16.034 1.00 47.03  ? 1018 HOH D O   1 
HETATM 12431 O  O   . HOH X 6 .   ? -20.134 33.876  -32.189 1.00 35.75  ? 1019 HOH D O   1 
HETATM 12432 O  O   . HOH X 6 .   ? -16.989 28.752  -27.173 1.00 48.89  ? 1020 HOH D O   1 
HETATM 12433 O  O   . HOH X 6 .   ? -20.934 14.213  -32.389 1.00 39.80  ? 1021 HOH D O   1 
HETATM 12434 O  O   . HOH X 6 .   ? -24.572 20.725  -23.001 1.00 36.09  ? 1022 HOH D O   1 
HETATM 12435 O  O   . HOH X 6 .   ? -26.726 19.603  -21.344 1.00 30.53  ? 1023 HOH D O   1 
HETATM 12436 O  O   . HOH X 6 .   ? -26.885 16.993  -21.253 1.00 22.88  ? 1024 HOH D O   1 
HETATM 12437 O  O   . HOH X 6 .   ? -7.468  41.824  6.204   1.00 20.13  ? 1025 HOH D O   1 
HETATM 12438 O  O   . HOH X 6 .   ? -0.072  11.542  6.498   1.00 40.41  ? 1026 HOH D O   1 
HETATM 12439 O  O   . HOH X 6 .   ? 10.149  31.715  -24.530 1.00 30.58  ? 1027 HOH D O   1 
HETATM 12440 O  O   . HOH X 6 .   ? 14.310  24.747  -5.443  1.00 41.52  ? 1028 HOH D O   1 
HETATM 12441 O  O   . HOH X 6 .   ? -4.783  30.720  2.470   1.00 30.96  ? 1029 HOH D O   1 
HETATM 12442 O  O   . HOH X 6 .   ? -11.596 6.571   1.170   1.00 34.29  ? 1030 HOH D O   1 
HETATM 12443 O  O   . HOH X 6 .   ? -14.005 6.421   1.327   1.00 27.19  ? 1031 HOH D O   1 
HETATM 12444 O  O   . HOH X 6 .   ? -5.841  5.989   -5.130  1.00 31.12  ? 1032 HOH D O   1 
HETATM 12445 O  O   . HOH X 6 .   ? -2.998  50.702  -4.936  1.00 34.74  ? 1033 HOH D O   1 
HETATM 12446 O  O   . HOH X 6 .   ? -13.005 20.026  -13.009 1.00 15.19  ? 1034 HOH D O   1 
HETATM 12447 O  O   . HOH X 6 .   ? -10.319 21.633  -16.695 1.00 42.84  ? 1035 HOH D O   1 
HETATM 12448 O  O   . HOH X 6 .   ? 5.571   22.482  -15.613 1.00 44.96  ? 1036 HOH D O   1 
HETATM 12449 O  O   . HOH X 6 .   ? 10.295  41.598  -7.011  1.00 51.59  ? 1037 HOH D O   1 
HETATM 12450 O  O   . HOH X 6 .   ? -0.313  41.087  -17.341 1.00 30.45  ? 1038 HOH D O   1 
HETATM 12451 O  O   . HOH X 6 .   ? -12.980 37.286  6.051   1.00 46.21  ? 1039 HOH D O   1 
HETATM 12452 O  O   . HOH X 6 .   ? -20.912 41.021  -0.920  1.00 32.08  ? 1040 HOH D O   1 
HETATM 12453 O  O   . HOH X 6 .   ? -36.791 32.896  -10.220 1.00 24.29  ? 1041 HOH D O   1 
HETATM 12454 O  O   . HOH X 6 .   ? -30.750 21.864  -15.256 1.00 36.72  ? 1042 HOH D O   1 
HETATM 12455 O  O   . HOH X 6 .   ? -23.310 14.066  -30.959 1.00 26.92  ? 1043 HOH D O   1 
HETATM 12456 O  O   . HOH X 6 .   ? -7.386  21.053  -28.981 1.00 42.31  ? 1044 HOH D O   1 
HETATM 12457 O  O   . HOH X 6 .   ? -7.026  19.013  -25.046 1.00 84.19  ? 1045 HOH D O   1 
HETATM 12458 O  O   . HOH X 6 .   ? -2.713  33.364  -24.626 1.00 26.51  ? 1046 HOH D O   1 
HETATM 12459 O  O   . HOH X 6 .   ? -16.332 61.796  7.028   1.00 32.02  ? 1047 HOH D O   1 
HETATM 12460 O  O   . HOH X 6 .   ? -16.658 58.390  13.993  1.00 35.04  ? 1048 HOH D O   1 
HETATM 12461 O  O   . HOH X 6 .   ? -21.035 61.039  5.588   1.00 35.37  ? 1049 HOH D O   1 
HETATM 12462 O  O   . HOH X 6 .   ? -14.677 60.876  -5.901  1.00 27.39  ? 1050 HOH D O   1 
HETATM 12463 O  O   . HOH X 6 .   ? -14.123 60.216  -10.555 1.00 31.68  ? 1051 HOH D O   1 
HETATM 12464 O  O   . HOH X 6 .   ? 14.615  17.097  -29.013 1.00 35.29  ? 1052 HOH D O   1 
HETATM 12465 O  O   . HOH X 6 .   ? 15.613  14.403  -29.243 1.00 21.76  ? 1053 HOH D O   1 
HETATM 12466 O  O   . HOH X 6 .   ? 16.638  13.999  -31.477 1.00 53.69  ? 1054 HOH D O   1 
HETATM 12467 O  O   . HOH X 6 .   ? -33.584 30.760  3.216   1.00 45.26  ? 1055 HOH D O   1 
HETATM 12468 O  O   . HOH X 6 .   ? -33.796 28.362  3.920   1.00 43.88  ? 1056 HOH D 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   . LYS A 29  ? 0.5460 0.4451 1.0655 -0.2594 0.2803  -0.0799 29   LYS A N   
2     C  CA  . LYS A 29  ? 0.9112 0.7854 1.3831 -0.2359 0.2651  -0.0615 29   LYS A CA  
3     C  C   . LYS A 29  ? 1.0749 0.9815 1.5205 -0.2146 0.2436  -0.0605 29   LYS A C   
4     O  O   . LYS A 29  ? 0.9780 0.9262 1.4435 -0.2147 0.2302  -0.0821 29   LYS A O   
5     C  CB  . LYS A 29  ? 1.0707 0.9000 1.5142 -0.2327 0.2884  -0.0267 29   LYS A CB  
6     C  CG  . LYS A 29  ? 1.1066 0.8975 1.5158 -0.2163 0.2774  -0.0133 29   LYS A CG  
7     C  CD  . LYS A 29  ? 1.1128 0.8715 1.4853 -0.2051 0.2951  0.0235  29   LYS A CD  
8     C  CE  . LYS A 29  ? 0.9782 0.6981 1.3232 -0.1906 0.2870  0.0356  29   LYS A CE  
9     N  NZ  . LYS A 29  ? 0.8490 0.5503 1.1514 -0.1722 0.2953  0.0698  29   LYS A NZ  
10    N  N   . GLU A 30  ? 1.2079 1.0949 1.6097 -0.1961 0.2412  -0.0356 30   GLU A N   
11    C  CA  . GLU A 30  ? 1.1346 1.0424 1.5072 -0.1748 0.2194  -0.0343 30   GLU A CA  
12    C  C   . GLU A 30  ? 0.8238 0.7738 1.2025 -0.1721 0.2190  -0.0399 30   GLU A C   
13    O  O   . GLU A 30  ? 0.6050 0.5623 0.9898 -0.1799 0.2406  -0.0297 30   GLU A O   
14    C  CB  . GLU A 30  ? 1.1624 1.0407 1.4900 -0.1581 0.2208  -0.0061 30   GLU A CB  
15    C  CG  . GLU A 30  ? 1.3034 1.1386 1.6228 -0.1584 0.2236  0.0026  30   GLU A CG  
16    C  CD  . GLU A 30  ? 1.4553 1.2635 1.7346 -0.1434 0.2309  0.0331  30   GLU A CD  
17    O  OE1 . GLU A 30  ? 1.3406 1.1435 1.6119 -0.1455 0.2524  0.0532  30   GLU A OE1 
18    O  OE2 . GLU A 30  ? 1.5767 1.3707 1.8325 -0.1290 0.2155  0.0370  30   GLU A OE2 
19    N  N   . ASP A 31  ? 0.6175 0.5939 0.9930 -0.1600 0.1949  -0.0557 31   ASP A N   
20    C  CA  . ASP A 31  ? 0.5257 0.5386 0.9013 -0.1528 0.1919  -0.0603 31   ASP A CA  
21    C  C   . ASP A 31  ? 0.7566 0.7614 1.0882 -0.1337 0.1867  -0.0413 31   ASP A C   
22    O  O   . ASP A 31  ? 0.7875 0.7950 1.1009 -0.1188 0.1653  -0.0463 31   ASP A O   
23    C  CB  . ASP A 31  ? 0.4064 0.4515 0.8032 -0.1488 0.1694  -0.0876 31   ASP A CB  
24    C  CG  . ASP A 31  ? 0.5569 0.6346 0.9477 -0.1360 0.1621  -0.0920 31   ASP A CG  
25    O  OD1 . ASP A 31  ? 0.5427 0.6439 0.9437 -0.1277 0.1422  -0.1108 31   ASP A OD1 
26    O  OD2 . ASP A 31  ? 0.5587 0.6382 0.9333 -0.1331 0.1762  -0.0766 31   ASP A OD2 
27    N  N   . GLU A 32  ? 0.7614 0.7566 1.0761 -0.1344 0.2071  -0.0196 32   GLU A N   
28    C  CA  . GLU A 32  ? 0.6484 0.6403 0.9227 -0.1173 0.2040  -0.0026 32   GLU A CA  
29    C  C   . GLU A 32  ? 0.7675 0.7918 1.0413 -0.1148 0.2130  -0.0032 32   GLU A C   
30    O  O   . GLU A 32  ? 0.7195 0.7407 0.9671 -0.1089 0.2256  0.0157  32   GLU A O   
31    C  CB  . GLU A 32  ? 0.5674 0.5248 0.8162 -0.1160 0.2192  0.0244  32   GLU A CB  
32    C  CG  . GLU A 32  ? 0.6896 0.6127 0.9338 -0.1155 0.2115  0.0275  32   GLU A CG  
33    C  CD  . GLU A 32  ? 0.8915 0.7810 1.1115 -0.1124 0.2281  0.0554  32   GLU A CD  
34    O  OE1 . GLU A 32  ? 0.7133 0.5941 0.8993 -0.0960 0.2193  0.0686  32   GLU A OE1 
35    O  OE2 . GLU A 32  ? 1.0062 0.8783 1.2416 -0.1261 0.2505  0.0641  32   GLU A OE2 
36    N  N   . SER A 33  ? 0.6345 0.6912 0.9368 -0.1181 0.2064  -0.0252 33   SER A N   
37    C  CA  . SER A 33  ? 0.6416 0.7314 0.9488 -0.1164 0.2158  -0.0289 33   SER A CA  
38    C  C   . SER A 33  ? 0.7221 0.8166 0.9921 -0.0976 0.2067  -0.0221 33   SER A C   
39    O  O   . SER A 33  ? 0.4809 0.5930 0.7408 -0.0946 0.2196  -0.0161 33   SER A O   
40    C  CB  . SER A 33  ? 0.5002 0.6248 0.8456 -0.1204 0.2067  -0.0557 33   SER A CB  
41    O  OG  . SER A 33  ? 0.6366 0.7651 0.9749 -0.1061 0.1799  -0.0690 33   SER A OG  
42    N  N   . PHE A 34  ? 0.6632 0.7427 0.9136 -0.0856 0.1852  -0.0238 34   PHE A N   
43    C  CA  . PHE A 34  ? 0.5249 0.6081 0.7433 -0.0690 0.1746  -0.0207 34   PHE A CA  
44    C  C   . PHE A 34  ? 0.6347 0.7134 0.8226 -0.0649 0.1903  0.0003  34   PHE A C   
45    O  O   . PHE A 34  ? 0.9163 1.0012 1.0777 -0.0521 0.1832  0.0019  34   PHE A O   
46    C  CB  . PHE A 34  ? 0.5602 0.6234 0.7629 -0.0593 0.1521  -0.0234 34   PHE A CB  
47    C  CG  . PHE A 34  ? 0.5546 0.5851 0.7496 -0.0637 0.1529  -0.0103 34   PHE A CG  
48    C  CD1 . PHE A 34  ? 0.5342 0.5458 0.6989 -0.0582 0.1592  0.0103  34   PHE A CD1 
49    C  CD2 . PHE A 34  ? 0.6418 0.6619 0.8595 -0.0717 0.1463  -0.0200 34   PHE A CD2 
50    C  CE1 . PHE A 34  ? 0.6186 0.6001 0.7770 -0.0604 0.1599  0.0220  34   PHE A CE1 
51    C  CE2 . PHE A 34  ? 0.5270 0.5164 0.7380 -0.0750 0.1473  -0.0096 34   PHE A CE2 
52    C  CZ  . PHE A 34  ? 0.5062 0.4754 0.6881 -0.0691 0.1543  0.0117  34   PHE A CZ  
53    N  N   . LEU A 35  ? 0.7105 0.7789 0.9022 -0.0757 0.2120  0.0159  35   LEU A N   
54    C  CA  . LEU A 35  ? 0.9448 1.0083 1.1058 -0.0709 0.2285  0.0385  35   LEU A CA  
55    C  C   . LEU A 35  ? 1.1047 1.1969 1.2713 -0.0746 0.2482  0.0386  35   LEU A C   
56    O  O   . LEU A 35  ? 1.2889 1.3838 1.4271 -0.0683 0.2612  0.0556  35   LEU A O   
57    C  CB  . LEU A 35  ? 1.0066 1.0367 1.1633 -0.0782 0.2428  0.0597  35   LEU A CB  
58    C  CG  . LEU A 35  ? 0.9979 0.9987 1.1569 -0.0780 0.2275  0.0582  35   LEU A CG  
59    C  CD1 . LEU A 35  ? 0.9919 0.9607 1.1569 -0.0887 0.2459  0.0755  35   LEU A CD1 
60    C  CD2 . LEU A 35  ? 0.9313 0.9249 1.0563 -0.0606 0.2090  0.0631  35   LEU A CD2 
61    N  N   . GLN A 36  ? 0.9728 1.0887 1.1754 -0.0839 0.2505  0.0196  36   GLN A N   
62    C  CA  . GLN A 36  ? 0.8272 0.9702 1.0422 -0.0909 0.2727  0.0196  36   GLN A CA  
63    C  C   . GLN A 36  ? 0.7246 0.8954 0.9179 -0.0766 0.2703  0.0144  36   GLN A C   
64    O  O   . GLN A 36  ? 0.7671 0.9664 0.9724 -0.0801 0.2854  0.0090  36   GLN A O   
65    C  CB  . GLN A 36  ? 0.8989 1.0625 1.1630 -0.1049 0.2743  -0.0017 36   GLN A CB  
66    C  CG  . GLN A 36  ? 1.1490 1.3391 1.4346 -0.1167 0.3008  -0.0018 36   GLN A CG  
67    C  CD  . GLN A 36  ? 1.3641 1.5325 1.6622 -0.1352 0.3257  0.0151  36   GLN A CD  
68    O  OE1 . GLN A 36  ? 1.1739 1.3608 1.4988 -0.1497 0.3485  0.0133  36   GLN A OE1 
69    N  NE2 . GLN A 36  ? 1.5276 1.6559 1.8077 -0.1350 0.3226  0.0311  36   GLN A NE2 
70    N  N   . GLN A 37  ? 0.6587 0.8217 0.8210 -0.0612 0.2520  0.0149  37   GLN A N   
71    C  CA  . GLN A 37  ? 0.7321 0.9201 0.8778 -0.0477 0.2450  0.0038  37   GLN A CA  
72    C  C   . GLN A 37  ? 0.8870 1.0599 0.9959 -0.0334 0.2280  0.0091  37   GLN A C   
73    O  O   . GLN A 37  ? 0.8166 0.9897 0.9259 -0.0256 0.2071  -0.0068 37   GLN A O   
74    C  CB  . GLN A 37  ? 0.7649 0.9734 0.9417 -0.0467 0.2313  -0.0233 37   GLN A CB  
75    C  CG  . GLN A 37  ? 0.6012 0.7911 0.7968 -0.0488 0.2108  -0.0330 37   GLN A CG  
76    C  CD  . GLN A 37  ? 0.6901 0.8716 0.8676 -0.0344 0.1867  -0.0423 37   GLN A CD  
77    O  OE1 . GLN A 37  ? 0.8259 0.9852 0.9761 -0.0293 0.1792  -0.0309 37   GLN A OE1 
78    N  NE2 . GLN A 37  ? 0.6386 0.8374 0.8324 -0.0278 0.1750  -0.0631 37   GLN A NE2 
79    N  N   . PRO A 38  ? 0.7934 0.9536 0.8707 -0.0298 0.2374  0.0318  38   PRO A N   
80    C  CA  . PRO A 38  ? 0.7479 0.8953 0.7923 -0.0170 0.2218  0.0378  38   PRO A CA  
81    C  C   . PRO A 38  ? 0.7476 0.9183 0.7762 -0.0048 0.2100  0.0212  38   PRO A C   
82    O  O   . PRO A 38  ? 0.8876 1.0833 0.9060 -0.0011 0.2217  0.0191  38   PRO A O   
83    C  CB  . PRO A 38  ? 0.8093 0.9473 0.8245 -0.0143 0.2389  0.0656  38   PRO A CB  
84    C  CG  . PRO A 38  ? 0.9123 1.0448 0.9503 -0.0292 0.2625  0.0761  38   PRO A CG  
85    C  CD  . PRO A 38  ? 0.8544 1.0129 0.9254 -0.0366 0.2642  0.0534  38   PRO A CD  
86    N  N   . HIS A 39  ? 0.6492 0.8107 0.6759 0.0011  0.1879  0.0089  39   HIS A N   
87    C  CA  . HIS A 39  ? 0.6156 0.7941 0.6306 0.0113  0.1758  -0.0090 39   HIS A CA  
88    C  C   . HIS A 39  ? 0.6016 0.7615 0.6143 0.0154  0.1534  -0.0169 39   HIS A C   
89    O  O   . HIS A 39  ? 0.4569 0.5945 0.4841 0.0100  0.1464  -0.0136 39   HIS A O   
90    C  CB  . HIS A 39  ? 0.5067 0.7072 0.5462 0.0099  0.1789  -0.0294 39   HIS A CB  
91    C  CG  . HIS A 39  ? 0.4345 0.6248 0.5055 0.0059  0.1661  -0.0436 39   HIS A CG  
92    N  ND1 . HIS A 39  ? 0.6341 0.8104 0.7282 -0.0045 0.1684  -0.0373 39   HIS A ND1 
93    C  CD2 . HIS A 39  ? 0.4883 0.6808 0.5702 0.0118  0.1512  -0.0639 39   HIS A CD2 
94    C  CE1 . HIS A 39  ? 0.6553 0.8283 0.7722 -0.0040 0.1542  -0.0532 39   HIS A CE1 
95    N  NE2 . HIS A 39  ? 0.5333 0.7146 0.6428 0.0063  0.1441  -0.0682 39   HIS A NE2 
96    N  N   . TYR A 40  ? 0.6747 0.8438 0.6693 0.0245  0.1430  -0.0281 40   TYR A N   
97    C  CA  . TYR A 40  ? 0.6566 0.8089 0.6503 0.0273  0.1236  -0.0367 40   TYR A CA  
98    C  C   . TYR A 40  ? 0.5597 0.7102 0.5774 0.0269  0.1141  -0.0576 40   TYR A C   
99    O  O   . TYR A 40  ? 0.6846 0.8533 0.7064 0.0307  0.1169  -0.0726 40   TYR A O   
100   C  CB  . TYR A 40  ? 0.7064 0.8682 0.6715 0.0359  0.1164  -0.0395 40   TYR A CB  
101   C  CG  . TYR A 40  ? 0.7239 0.8806 0.6657 0.0387  0.1192  -0.0177 40   TYR A CG  
102   C  CD1 . TYR A 40  ? 0.7696 0.9462 0.6863 0.0447  0.1305  -0.0067 40   TYR A CD1 
103   C  CD2 . TYR A 40  ? 0.6270 0.7596 0.5712 0.0366  0.1109  -0.0075 40   TYR A CD2 
104   C  CE1 . TYR A 40  ? 0.7273 0.8988 0.6217 0.0498  0.1328  0.0147  40   TYR A CE1 
105   C  CE2 . TYR A 40  ? 0.5899 0.7175 0.5139 0.0411  0.1135  0.0125  40   TYR A CE2 
106   C  CZ  . TYR A 40  ? 0.5834 0.7299 0.4825 0.0481  0.1241  0.0240  40   TYR A CZ  
107   O  OH  . TYR A 40  ? 0.4848 0.6255 0.3631 0.0548  0.1263  0.0454  40   TYR A OH  
108   N  N   . ALA A 41  ? 0.5396 0.6681 0.5721 0.0236  0.1034  -0.0582 41   ALA A N   
109   C  CA  . ALA A 41  ? 0.5181 0.6428 0.5712 0.0254  0.0938  -0.0756 41   ALA A CA  
110   C  C   . ALA A 41  ? 0.4796 0.6009 0.5215 0.0325  0.0823  -0.0899 41   ALA A C   
111   O  O   . ALA A 41  ? 0.2964 0.4052 0.3234 0.0332  0.0742  -0.0861 41   ALA A O   
112   C  CB  . ALA A 41  ? 0.4142 0.5182 0.4842 0.0205  0.0863  -0.0714 41   ALA A CB  
113   N  N   . SER A 42  ? 0.5794 0.7122 0.6303 0.0376  0.0825  -0.1072 42   SER A N   
114   C  CA  . SER A 42  ? 0.5385 0.6659 0.5819 0.0436  0.0736  -0.1229 42   SER A CA  
115   C  C   . SER A 42  ? 0.5232 0.6240 0.5770 0.0444  0.0607  -0.1261 42   SER A C   
116   O  O   . SER A 42  ? 0.6435 0.7341 0.7105 0.0416  0.0581  -0.1183 42   SER A O   
117   C  CB  . SER A 42  ? 0.4920 0.6383 0.5424 0.0499  0.0792  -0.1407 42   SER A CB  
118   O  OG  . SER A 42  ? 0.4934 0.6376 0.5687 0.0526  0.0779  -0.1472 42   SER A OG  
119   N  N   . GLN A 43  ? 0.4339 0.5235 0.4815 0.0481  0.0532  -0.1380 43   GLN A N   
120   C  CA  . GLN A 43  ? 0.3544 0.4177 0.4106 0.0501  0.0429  -0.1412 43   GLN A CA  
121   C  C   . GLN A 43  ? 0.4666 0.5302 0.5441 0.0552  0.0426  -0.1450 43   GLN A C   
122   O  O   . GLN A 43  ? 0.3761 0.4262 0.4621 0.0546  0.0367  -0.1377 43   GLN A O   
123   C  CB  . GLN A 43  ? 0.5202 0.5723 0.5700 0.0533  0.0385  -0.1562 43   GLN A CB  
124   C  CG  . GLN A 43  ? 0.6042 0.6257 0.6592 0.0551  0.0296  -0.1568 43   GLN A CG  
125   C  CD  . GLN A 43  ? 0.7119 0.7192 0.7602 0.0487  0.0242  -0.1415 43   GLN A CD  
126   O  OE1 . GLN A 43  ? 0.7409 0.7579 0.7776 0.0431  0.0257  -0.1337 43   GLN A OE1 
127   N  NE2 . GLN A 43  ? 0.7695 0.7540 0.8241 0.0508  0.0179  -0.1372 43   GLN A NE2 
128   N  N   . GLU A 44  ? 0.5329 0.6142 0.6192 0.0611  0.0487  -0.1574 44   GLU A N   
129   C  CA  . GLU A 44  ? 0.5500 0.6365 0.6585 0.0674  0.0480  -0.1622 44   GLU A CA  
130   C  C   . GLU A 44  ? 0.4893 0.5868 0.6099 0.0606  0.0509  -0.1499 44   GLU A C   
131   O  O   . GLU A 44  ? 0.5438 0.6353 0.6792 0.0628  0.0443  -0.1487 44   GLU A O   
132   C  CB  . GLU A 44  ? 0.5850 0.6928 0.7022 0.0750  0.0555  -0.1779 44   GLU A CB  
133   C  CG  . GLU A 44  ? 0.8639 0.9765 1.0052 0.0847  0.0526  -0.1851 44   GLU A CG  
134   C  CD  . GLU A 44  ? 1.1092 1.2543 1.2651 0.0890  0.0633  -0.1959 44   GLU A CD  
135   O  OE1 . GLU A 44  ? 1.1864 1.3482 1.3312 0.0855  0.0736  -0.1990 44   GLU A OE1 
136   O  OE2 . GLU A 44  ? 1.1460 1.3020 1.3245 0.0966  0.0615  -0.2016 44   GLU A OE2 
137   N  N   . GLN A 45  ? 0.4795 0.5928 0.5933 0.0525  0.0612  -0.1412 45   GLN A N   
138   C  CA  . GLN A 45  ? 0.4474 0.5695 0.5739 0.0443  0.0668  -0.1301 45   GLN A CA  
139   C  C   . GLN A 45  ? 0.4368 0.5358 0.5621 0.0396  0.0576  -0.1192 45   GLN A C   
140   O  O   . GLN A 45  ? 0.5090 0.6105 0.6516 0.0353  0.0572  -0.1160 45   GLN A O   
141   C  CB  . GLN A 45  ? 0.4343 0.5729 0.5500 0.0373  0.0813  -0.1204 45   GLN A CB  
142   C  CG  . GLN A 45  ? 0.5363 0.7031 0.6573 0.0410  0.0929  -0.1309 45   GLN A CG  
143   C  CD  . GLN A 45  ? 0.5577 0.7431 0.6757 0.0332  0.1099  -0.1193 45   GLN A CD  
144   O  OE1 . GLN A 45  ? 0.5956 0.7777 0.6901 0.0305  0.1145  -0.1071 45   GLN A OE1 
145   N  NE2 . GLN A 45  ? 0.5740 0.7797 0.7159 0.0299  0.1198  -0.1226 45   GLN A NE2 
146   N  N   . LEU A 46  ? 0.3485 0.4269 0.4545 0.0403  0.0504  -0.1152 46   LEU A N   
147   C  CA  . LEU A 46  ? 0.4884 0.5445 0.5908 0.0367  0.0420  -0.1054 46   LEU A CA  
148   C  C   . LEU A 46  ? 0.4354 0.4782 0.5494 0.0430  0.0305  -0.1116 46   LEU A C   
149   O  O   . LEU A 46  ? 0.2931 0.3313 0.4168 0.0402  0.0264  -0.1071 46   LEU A O   
150   C  CB  . LEU A 46  ? 0.5022 0.5442 0.5817 0.0356  0.0388  -0.0999 46   LEU A CB  
151   C  CG  . LEU A 46  ? 0.4524 0.4706 0.5266 0.0336  0.0296  -0.0921 46   LEU A CG  
152   C  CD1 . LEU A 46  ? 0.5651 0.5818 0.6471 0.0271  0.0321  -0.0808 46   LEU A CD1 
153   C  CD2 . LEU A 46  ? 0.2667 0.2772 0.3210 0.0323  0.0276  -0.0885 46   LEU A CD2 
154   N  N   . GLU A 47  ? 0.4364 0.4726 0.5484 0.0520  0.0257  -0.1222 47   GLU A N   
155   C  CA  . GLU A 47  ? 0.5310 0.5541 0.6511 0.0609  0.0157  -0.1270 47   GLU A CA  
156   C  C   . GLU A 47  ? 0.6107 0.6541 0.7542 0.0635  0.0156  -0.1313 47   GLU A C   
157   O  O   . GLU A 47  ? 0.6183 0.6565 0.7694 0.0658  0.0074  -0.1294 47   GLU A O   
158   C  CB  . GLU A 47  ? 0.3855 0.3984 0.5010 0.0709  0.0138  -0.1380 47   GLU A CB  
159   C  CG  . GLU A 47  ? 0.3843 0.3764 0.4801 0.0675  0.0128  -0.1363 47   GLU A CG  
160   C  CD  . GLU A 47  ? 0.5726 0.5554 0.6662 0.0751  0.0136  -0.1495 47   GLU A CD  
161   O  OE1 . GLU A 47  ? 0.7434 0.7406 0.8482 0.0826  0.0171  -0.1600 47   GLU A OE1 
162   O  OE2 . GLU A 47  ? 0.6025 0.5637 0.6844 0.0733  0.0114  -0.1503 47   GLU A OE2 
163   N  N   . ASP A 48  ? 0.5625 0.6314 0.7174 0.0630  0.0251  -0.1379 48   ASP A N   
164   C  CA  . ASP A 48  ? 0.6120 0.7061 0.7928 0.0641  0.0269  -0.1440 48   ASP A CA  
165   C  C   . ASP A 48  ? 0.5373 0.6347 0.7274 0.0528  0.0272  -0.1357 48   ASP A C   
166   O  O   . ASP A 48  ? 0.4947 0.6010 0.7033 0.0552  0.0205  -0.1405 48   ASP A O   
167   C  CB  . ASP A 48  ? 0.6100 0.7319 0.8000 0.0635  0.0399  -0.1515 48   ASP A CB  
168   C  CG  . ASP A 48  ? 0.7996 0.9220 0.9874 0.0769  0.0390  -0.1643 48   ASP A CG  
169   O  OD1 . ASP A 48  ? 0.8142 0.9182 1.0004 0.0882  0.0282  -0.1683 48   ASP A OD1 
170   O  OD2 . ASP A 48  ? 0.8819 1.0224 1.0693 0.0766  0.0499  -0.1704 48   ASP A OD2 
171   N  N   . LEU A 49  ? 0.3969 0.4872 0.5744 0.0412  0.0346  -0.1240 49   LEU A N   
172   C  CA  . LEU A 49  ? 0.4715 0.5623 0.6586 0.0299  0.0371  -0.1166 49   LEU A CA  
173   C  C   . LEU A 49  ? 0.4719 0.5419 0.6550 0.0314  0.0238  -0.1137 49   LEU A C   
174   O  O   . LEU A 49  ? 0.4927 0.5683 0.6922 0.0263  0.0212  -0.1155 49   LEU A O   
175   C  CB  . LEU A 49  ? 0.5412 0.6282 0.7149 0.0191  0.0497  -0.1033 49   LEU A CB  
176   C  CG  . LEU A 49  ? 0.5128 0.6005 0.7004 0.0066  0.0560  -0.0966 49   LEU A CG  
177   C  CD1 . LEU A 49  ? 0.7683 0.8663 0.9542 -0.0024 0.0745  -0.0873 49   LEU A CD1 
178   C  CD2 . LEU A 49  ? 0.3744 0.4356 0.5497 0.0041  0.0481  -0.0877 49   LEU A CD2 
179   N  N   . PHE A 50  ? 0.3048 0.3519 0.4665 0.0378  0.0162  -0.1103 50   PHE A N   
180   C  CA  . PHE A 50  ? 0.3246 0.3509 0.4787 0.0405  0.0046  -0.1069 50   PHE A CA  
181   C  C   . PHE A 50  ? 0.4643 0.4965 0.6313 0.0513  -0.0065 -0.1163 50   PHE A C   
182   O  O   . PHE A 50  ? 0.7281 0.7545 0.8969 0.0516  -0.0147 -0.1155 50   PHE A O   
183   C  CB  . PHE A 50  ? 0.4799 0.4822 0.6096 0.0440  0.0012  -0.1012 50   PHE A CB  
184   C  CG  . PHE A 50  ? 0.4237 0.4153 0.5390 0.0346  0.0061  -0.0896 50   PHE A CG  
185   C  CD1 . PHE A 50  ? 0.3942 0.3955 0.5163 0.0249  0.0151  -0.0836 50   PHE A CD1 
186   C  CD2 . PHE A 50  ? 0.2563 0.2282 0.3522 0.0359  0.0025  -0.0846 50   PHE A CD2 
187   C  CE1 . PHE A 50  ? 0.3937 0.3842 0.5018 0.0188  0.0196  -0.0718 50   PHE A CE1 
188   C  CE2 . PHE A 50  ? 0.2944 0.2595 0.3782 0.0292  0.0062  -0.0744 50   PHE A CE2 
189   C  CZ  . PHE A 50  ? 0.4113 0.3852 0.5002 0.0217  0.0143  -0.0675 50   PHE A CZ  
190   N  N   . ALA A 51  ? 0.4291 0.4735 0.6040 0.0615  -0.0069 -0.1256 51   ALA A N   
191   C  CA  . ALA A 51  ? 0.4938 0.5480 0.6823 0.0742  -0.0173 -0.1344 51   ALA A CA  
192   C  C   . ALA A 51  ? 0.5747 0.6583 0.7905 0.0682  -0.0168 -0.1416 51   ALA A C   
193   O  O   . ALA A 51  ? 0.6362 0.7263 0.8611 0.0739  -0.0276 -0.1464 51   ALA A O   
194   C  CB  . ALA A 51  ? 0.3105 0.3696 0.5015 0.0879  -0.0168 -0.1427 51   ALA A CB  
195   N  N   . GLY A 52  ? 0.5750 0.6769 0.8037 0.0564  -0.0036 -0.1425 52   GLY A N   
196   C  CA  . GLY A 52  ? 0.5511 0.6819 0.8092 0.0481  0.0000  -0.1504 52   GLY A CA  
197   C  C   . GLY A 52  ? 0.5051 0.6275 0.7654 0.0381  -0.0043 -0.1471 52   GLY A C   
198   O  O   . GLY A 52  ? 0.3004 0.4414 0.5820 0.0377  -0.0112 -0.1572 52   GLY A O   
199   N  N   . LEU A 53  ? 0.4975 0.5929 0.7361 0.0304  -0.0004 -0.1340 53   LEU A N   
200   C  CA  . LEU A 53  ? 0.5655 0.6483 0.8030 0.0214  -0.0033 -0.1301 53   LEU A CA  
201   C  C   . LEU A 53  ? 0.5143 0.5922 0.7479 0.0326  -0.0206 -0.1356 53   LEU A C   
202   O  O   . LEU A 53  ? 0.5732 0.6574 0.8189 0.0278  -0.0260 -0.1417 53   LEU A O   
203   C  CB  . LEU A 53  ? 0.4718 0.5261 0.6838 0.0155  0.0029  -0.1146 53   LEU A CB  
204   C  CG  . LEU A 53  ? 0.6047 0.6599 0.8216 0.0005  0.0194  -0.1066 53   LEU A CG  
205   C  CD1 . LEU A 53  ? 0.5114 0.5950 0.7527 -0.0054 0.0311  -0.1134 53   LEU A CD1 
206   C  CD2 . LEU A 53  ? 0.7495 0.7850 0.9395 0.0003  0.0258  -0.0921 53   LEU A CD2 
207   N  N   . GLU A 54  ? 0.4792 0.5457 0.6954 0.0477  -0.0286 -0.1338 54   GLU A N   
208   C  CA  . GLU A 54  ? 0.6594 0.7167 0.8653 0.0605  -0.0437 -0.1354 54   GLU A CA  
209   C  C   . GLU A 54  ? 0.7149 0.8030 0.9450 0.0680  -0.0533 -0.1499 54   GLU A C   
210   O  O   . GLU A 54  ? 0.6213 0.7123 0.8516 0.0717  -0.0645 -0.1543 54   GLU A O   
211   C  CB  . GLU A 54  ? 0.7831 0.8193 0.9664 0.0744  -0.0472 -0.1293 54   GLU A CB  
212   C  CG  . GLU A 54  ? 0.9082 0.9233 1.0712 0.0847  -0.0587 -0.1242 54   GLU A CG  
213   C  CD  . GLU A 54  ? 0.9246 0.9121 1.0644 0.0936  -0.0579 -0.1160 54   GLU A CD  
214   O  OE1 . GLU A 54  ? 1.0035 0.9704 1.1245 0.1010  -0.0647 -0.1097 54   GLU A OE1 
215   O  OE2 . GLU A 54  ? 0.7827 0.7694 0.9233 0.0927  -0.0498 -0.1166 54   GLU A OE2 
216   N  N   . LYS A 55  ? 0.7078 0.8218 0.9587 0.0706  -0.0488 -0.1585 55   LYS A N   
217   C  CA  . LYS A 55  ? 0.6402 0.7897 0.9184 0.0777  -0.0572 -0.1740 55   LYS A CA  
218   C  C   . LYS A 55  ? 0.4768 0.6507 0.7841 0.0589  -0.0508 -0.1832 55   LYS A C   
219   O  O   . LYS A 55  ? 0.3814 0.5778 0.7070 0.0597  -0.0607 -0.1957 55   LYS A O   
220   C  CB  . LYS A 55  ? 0.5493 0.7179 0.8390 0.0908  -0.0557 -0.1805 55   LYS A CB  
221   C  CG  . LYS A 55  ? 0.5274 0.6979 0.8210 0.0810  -0.0385 -0.1778 55   LYS A CG  
222   C  CD  . LYS A 55  ? 0.6392 0.8319 0.9466 0.0957  -0.0380 -0.1872 55   LYS A CD  
223   C  CE  . LYS A 55  ? 0.6674 0.9048 1.0112 0.0987  -0.0432 -0.2039 55   LYS A CE  
224   N  NZ  . LYS A 55  ? 0.6065 0.8697 0.9673 0.1132  -0.0416 -0.2142 55   LYS A NZ  
225   N  N   . ALA A 56  ? 0.3045 0.4737 0.6158 0.0421  -0.0339 -0.1773 56   ALA A N   
226   C  CA  . ALA A 56  ? 0.3959 0.5783 0.7313 0.0222  -0.0248 -0.1827 56   ALA A CA  
227   C  C   . ALA A 56  ? 0.4166 0.5837 0.7453 0.0169  -0.0332 -0.1830 56   ALA A C   
228   O  O   . ALA A 56  ? 0.3910 0.5780 0.7453 0.0072  -0.0349 -0.1961 56   ALA A O   
229   C  CB  . ALA A 56  ? 0.2182 0.3888 0.5497 0.0071  -0.0044 -0.1709 56   ALA A CB  
230   N  N   . TYR A 57  ? 0.3454 0.4784 0.6410 0.0228  -0.0381 -0.1700 57   TYR A N   
231   C  CA  . TYR A 57  ? 0.4032 0.5190 0.6891 0.0181  -0.0443 -0.1691 57   TYR A CA  
232   C  C   . TYR A 57  ? 0.3845 0.4855 0.6438 0.0359  -0.0602 -0.1656 57   TYR A C   
233   O  O   . TYR A 57  ? 0.5577 0.6279 0.7896 0.0372  -0.0591 -0.1523 57   TYR A O   
234   C  CB  . TYR A 57  ? 0.2757 0.3619 0.5475 0.0044  -0.0308 -0.1545 57   TYR A CB  
235   C  CG  . TYR A 57  ? 0.4913 0.5864 0.7848 -0.0130 -0.0129 -0.1541 57   TYR A CG  
236   C  CD1 . TYR A 57  ? 0.6460 0.7439 0.9370 -0.0137 -0.0005 -0.1460 57   TYR A CD1 
237   C  CD2 . TYR A 57  ? 0.3479 0.4477 0.6638 -0.0290 -0.0071 -0.1619 57   TYR A CD2 
238   C  CE1 . TYR A 57  ? 0.5992 0.7048 0.9076 -0.0291 0.0177  -0.1437 57   TYR A CE1 
239   C  CE2 . TYR A 57  ? 0.3704 0.4751 0.7060 -0.0456 0.0117  -0.1598 57   TYR A CE2 
240   C  CZ  . TYR A 57  ? 0.5496 0.6573 0.8804 -0.0452 0.0244  -0.1496 57   TYR A CZ  
241   O  OH  . TYR A 57  ? 0.4384 0.5506 0.7863 -0.0611 0.0445  -0.1456 57   TYR A OH  
242   N  N   . PRO A 58  ? 0.3920 0.5162 0.6597 0.0502  -0.0745 -0.1774 58   PRO A N   
243   C  CA  . PRO A 58  ? 0.4006 0.5132 0.6429 0.0707  -0.0889 -0.1730 58   PRO A CA  
244   C  C   . PRO A 58  ? 0.5459 0.6292 0.7609 0.0700  -0.0927 -0.1641 58   PRO A C   
245   O  O   . PRO A 58  ? 0.7203 0.7787 0.9071 0.0814  -0.0953 -0.1518 58   PRO A O   
246   C  CB  . PRO A 58  ? 0.3572 0.5070 0.6199 0.0817  -0.1033 -0.1905 58   PRO A CB  
247   C  CG  . PRO A 58  ? 0.2747 0.4568 0.5740 0.0711  -0.0949 -0.2024 58   PRO A CG  
248   C  CD  . PRO A 58  ? 0.2630 0.4289 0.5671 0.0477  -0.0771 -0.1960 58   PRO A CD  
249   N  N   . ASN A 59  ? 0.5732 0.6586 0.7971 0.0568  -0.0920 -0.1707 59   ASN A N   
250   C  CA  . ASN A 59  ? 0.7534 0.8159 0.9529 0.0583  -0.0973 -0.1653 59   ASN A CA  
251   C  C   . ASN A 59  ? 0.5990 0.6288 0.7832 0.0459  -0.0846 -0.1512 59   ASN A C   
252   O  O   . ASN A 59  ? 0.3430 0.3521 0.5054 0.0480  -0.0875 -0.1451 59   ASN A O   
253   C  CB  . ASN A 59  ? 0.8105 0.8941 1.0251 0.0546  -0.1068 -0.1829 59   ASN A CB  
254   C  CG  . ASN A 59  ? 0.8644 0.9855 1.0950 0.0682  -0.1212 -0.1984 59   ASN A CG  
255   O  OD1 . ASN A 59  ? 0.8291 0.9656 1.0706 0.0756  -0.1207 -0.1988 59   ASN A OD1 
256   N  ND2 . ASN A 59  ? 0.8817 1.0199 1.1141 0.0723  -0.1343 -0.2124 59   ASN A ND2 
257   N  N   . GLN A 60  ? 0.4161 0.4430 0.6111 0.0342  -0.0706 -0.1457 60   GLN A N   
258   C  CA  . GLN A 60  ? 0.4399 0.4412 0.6245 0.0225  -0.0587 -0.1337 60   GLN A CA  
259   C  C   . GLN A 60  ? 0.4553 0.4426 0.6262 0.0235  -0.0494 -0.1194 60   GLN A C   
260   O  O   . GLN A 60  ? 0.5531 0.5183 0.7081 0.0191  -0.0426 -0.1075 60   GLN A O   
261   C  CB  . GLN A 60  ? 0.4646 0.4736 0.6746 0.0049  -0.0489 -0.1408 60   GLN A CB  
262   C  CG  . GLN A 60  ? 0.6943 0.7372 0.9351 0.0025  -0.0545 -0.1603 60   GLN A CG  
263   C  CD  . GLN A 60  ? 0.7676 0.8132 1.0279 -0.0122 -0.0518 -0.1721 60   GLN A CD  
264   O  OE1 . GLN A 60  ? 0.6622 0.7336 0.9544 -0.0217 -0.0498 -0.1874 60   GLN A OE1 
265   N  NE2 . GLN A 60  ? 0.6775 0.6967 0.9203 -0.0146 -0.0511 -0.1662 60   GLN A NE2 
266   N  N   . ALA A 61  ? 0.3500 0.3521 0.5278 0.0300  -0.0494 -0.1217 61   ALA A N   
267   C  CA  . ALA A 61  ? 0.4076 0.3985 0.5720 0.0322  -0.0419 -0.1111 61   ALA A CA  
268   C  C   . ALA A 61  ? 0.4106 0.3955 0.5595 0.0485  -0.0509 -0.1100 61   ALA A C   
269   O  O   . ALA A 61  ? 0.4078 0.4094 0.5664 0.0589  -0.0593 -0.1190 61   ALA A O   
270   C  CB  . ALA A 61  ? 0.4843 0.4941 0.6679 0.0254  -0.0311 -0.1141 61   ALA A CB  
271   N  N   . LYS A 62  ? 0.4146 0.3755 0.5404 0.0507  -0.0486 -0.0990 62   LYS A N   
272   C  CA  . LYS A 62  ? 0.3655 0.3139 0.4753 0.0643  -0.0540 -0.0962 62   LYS A CA  
273   C  C   . LYS A 62  ? 0.3491 0.2829 0.4466 0.0615  -0.0455 -0.0888 62   LYS A C   
274   O  O   . LYS A 62  ? 0.5891 0.5131 0.6787 0.0521  -0.0394 -0.0817 62   LYS A O   
275   C  CB  . LYS A 62  ? 0.3782 0.3098 0.4697 0.0711  -0.0624 -0.0919 62   LYS A CB  
276   C  CG  . LYS A 62  ? 0.3922 0.3062 0.4658 0.0848  -0.0661 -0.0868 62   LYS A CG  
277   C  CD  . LYS A 62  ? 0.7073 0.6081 0.7630 0.0925  -0.0739 -0.0824 62   LYS A CD  
278   C  CE  . LYS A 62  ? 0.9134 0.7914 0.9494 0.1048  -0.0746 -0.0746 62   LYS A CE  
279   N  NZ  . LYS A 62  ? 1.0473 0.9329 1.0915 0.1175  -0.0774 -0.0792 62   LYS A NZ  
280   N  N   . VAL A 63  ? 0.4321 0.3657 0.5288 0.0702  -0.0454 -0.0915 63   VAL A N   
281   C  CA  . VAL A 63  ? 0.3712 0.2933 0.4578 0.0677  -0.0380 -0.0879 63   VAL A CA  
282   C  C   . VAL A 63  ? 0.4730 0.3685 0.5400 0.0734  -0.0406 -0.0821 63   VAL A C   
283   O  O   . VAL A 63  ? 0.5717 0.4586 0.6340 0.0853  -0.0472 -0.0823 63   VAL A O   
284   C  CB  . VAL A 63  ? 0.3958 0.3311 0.4931 0.0730  -0.0345 -0.0960 63   VAL A CB  
285   C  CG1 . VAL A 63  ? 0.3120 0.2334 0.3971 0.0718  -0.0286 -0.0947 63   VAL A CG1 
286   C  CG2 . VAL A 63  ? 0.5459 0.5081 0.6623 0.0649  -0.0282 -0.1008 63   VAL A CG2 
287   N  N   . HIS A 64  ? 0.5026 0.3863 0.5586 0.0653  -0.0349 -0.0767 64   HIS A N   
288   C  CA  . HIS A 64  ? 0.3977 0.2639 0.4370 0.0648  -0.0354 -0.0696 64   HIS A CA  
289   C  C   . HIS A 64  ? 0.4465 0.3095 0.4839 0.0615  -0.0289 -0.0727 64   HIS A C   
290   O  O   . HIS A 64  ? 0.3355 0.2084 0.3766 0.0548  -0.0234 -0.0756 64   HIS A O   
291   C  CB  . HIS A 64  ? 0.3262 0.1896 0.3561 0.0561  -0.0353 -0.0605 64   HIS A CB  
292   C  CG  . HIS A 64  ? 0.5342 0.3997 0.5653 0.0588  -0.0415 -0.0596 64   HIS A CG  
293   N  ND1 . HIS A 64  ? 0.5914 0.4458 0.6112 0.0663  -0.0475 -0.0563 64   HIS A ND1 
294   C  CD2 . HIS A 64  ? 0.5237 0.3995 0.5662 0.0555  -0.0420 -0.0630 64   HIS A CD2 
295   C  CE1 . HIS A 64  ? 0.5653 0.4252 0.5893 0.0681  -0.0527 -0.0590 64   HIS A CE1 
296   N  NE2 . HIS A 64  ? 0.5743 0.4468 0.6134 0.0607  -0.0492 -0.0635 64   HIS A NE2 
297   N  N   . PHE A 65  ? 0.4911 0.3385 0.5220 0.0671  -0.0291 -0.0729 65   PHE A N   
298   C  CA  . PHE A 65  ? 0.4824 0.3231 0.5120 0.0638  -0.0229 -0.0780 65   PHE A CA  
299   C  C   . PHE A 65  ? 0.5047 0.3354 0.5236 0.0545  -0.0199 -0.0714 65   PHE A C   
300   O  O   . PHE A 65  ? 0.5564 0.3727 0.5659 0.0561  -0.0215 -0.0635 65   PHE A O   
301   C  CB  . PHE A 65  ? 0.4749 0.3008 0.5053 0.0752  -0.0232 -0.0826 65   PHE A CB  
302   C  CG  . PHE A 65  ? 0.5299 0.3422 0.5584 0.0716  -0.0164 -0.0885 65   PHE A CG  
303   C  CD1 . PHE A 65  ? 0.5985 0.3882 0.6171 0.0685  -0.0134 -0.0827 65   PHE A CD1 
304   C  CD2 . PHE A 65  ? 0.6177 0.4397 0.6549 0.0713  -0.0122 -0.1015 65   PHE A CD2 
305   C  CE1 . PHE A 65  ? 0.7168 0.4930 0.7367 0.0639  -0.0063 -0.0904 65   PHE A CE1 
306   C  CE2 . PHE A 65  ? 0.7192 0.5290 0.7558 0.0677  -0.0062 -0.1099 65   PHE A CE2 
307   C  CZ  . PHE A 65  ? 0.8123 0.5988 0.8415 0.0634  -0.0033 -0.1047 65   PHE A CZ  
308   N  N   . LEU A 66  ? 0.4685 0.3078 0.4887 0.0457  -0.0154 -0.0754 66   LEU A N   
309   C  CA  . LEU A 66  ? 0.3324 0.1669 0.3460 0.0370  -0.0126 -0.0715 66   LEU A CA  
310   C  C   . LEU A 66  ? 0.5097 0.3327 0.5243 0.0339  -0.0073 -0.0805 66   LEU A C   
311   O  O   . LEU A 66  ? 0.6982 0.5092 0.7089 0.0284  -0.0040 -0.0783 66   LEU A O   
312   C  CB  . LEU A 66  ? 0.3193 0.1708 0.3333 0.0305  -0.0118 -0.0712 66   LEU A CB  
313   C  CG  . LEU A 66  ? 0.3455 0.2072 0.3611 0.0321  -0.0149 -0.0644 66   LEU A CG  
314   C  CD1 . LEU A 66  ? 0.3727 0.2441 0.3859 0.0266  -0.0126 -0.0624 66   LEU A CD1 
315   C  CD2 . LEU A 66  ? 0.3154 0.1692 0.3263 0.0343  -0.0191 -0.0552 66   LEU A CD2 
316   N  N   . GLY A 67  ? 0.4125 0.2393 0.4335 0.0372  -0.0055 -0.0922 67   GLY A N   
317   C  CA  . GLY A 67  ? 0.5497 0.3648 0.5733 0.0343  -0.0002 -0.1036 67   GLY A CA  
318   C  C   . GLY A 67  ? 0.5803 0.4098 0.6097 0.0359  0.0016  -0.1188 67   GLY A C   
319   O  O   . GLY A 67  ? 0.5312 0.3769 0.5626 0.0406  -0.0004 -0.1191 67   GLY A O   
320   N  N   . ARG A 68  ? 0.5729 0.3969 0.6050 0.0314  0.0063  -0.1330 68   ARG A N   
321   C  CA  . ARG A 68  ? 0.4688 0.3072 0.5046 0.0333  0.0087  -0.1500 68   ARG A CA  
322   C  C   . ARG A 68  ? 0.5708 0.4240 0.6046 0.0226  0.0108  -0.1637 68   ARG A C   
323   O  O   . ARG A 68  ? 0.5108 0.3555 0.5445 0.0137  0.0119  -0.1642 68   ARG A O   
324   C  CB  . ARG A 68  ? 0.3872 0.2068 0.4294 0.0413  0.0119  -0.1584 68   ARG A CB  
325   C  CG  . ARG A 68  ? 0.3765 0.2018 0.4228 0.0548  0.0096  -0.1561 68   ARG A CG  
326   C  CD  . ARG A 68  ? 0.5594 0.3582 0.6098 0.0652  0.0111  -0.1570 68   ARG A CD  
327   N  NE  . ARG A 68  ? 0.6600 0.4678 0.7171 0.0794  0.0090  -0.1592 68   ARG A NE  
328   C  CZ  . ARG A 68  ? 0.8119 0.6046 0.8704 0.0924  0.0057  -0.1513 68   ARG A CZ  
329   N  NH1 . ARG A 68  ? 0.8955 0.6609 0.9463 0.0934  0.0048  -0.1394 68   ARG A NH1 
330   N  NH2 . ARG A 68  ? 0.9771 0.7835 1.0445 0.1055  0.0036  -0.1559 68   ARG A NH2 
331   N  N   . SER A 69  ? 0.5292 0.4111 0.5625 0.0236  0.0112  -0.1726 69   SER A N   
332   C  CA  . SER A 69  ? 0.2448 0.1502 0.2754 0.0155  0.0117  -0.1853 69   SER A CA  
333   C  C   . SER A 69  ? 0.4958 0.3888 0.5331 0.0122  0.0161  -0.2070 69   SER A C   
334   O  O   . SER A 69  ? 0.3951 0.2604 0.4383 0.0176  0.0194  -0.2104 69   SER A O   
335   C  CB  . SER A 69  ? 0.3029 0.2425 0.3279 0.0196  0.0115  -0.1858 69   SER A CB  
336   O  OG  . SER A 69  ? 0.4136 0.3559 0.4429 0.0259  0.0154  -0.1991 69   SER A OG  
337   N  N   . LEU A 70  ? 0.5490 0.4629 0.5855 0.0039  0.0160  -0.2222 70   LEU A N   
338   C  CA  . LEU A 70  ? 0.5773 0.4825 0.6216 -0.0011 0.0204  -0.2465 70   LEU A CA  
339   C  C   . LEU A 70  ? 0.5926 0.4912 0.6398 0.0091  0.0242  -0.2560 70   LEU A C   
340   O  O   . LEU A 70  ? 0.6187 0.4880 0.6743 0.0100  0.0294  -0.2674 70   LEU A O   
341   C  CB  . LEU A 70  ? 0.4953 0.4363 0.5372 -0.0090 0.0181  -0.2639 70   LEU A CB  
342   C  CG  . LEU A 70  ? 0.5335 0.4824 0.5774 -0.0205 0.0149  -0.2626 70   LEU A CG  
343   C  CD1 . LEU A 70  ? 0.5839 0.5760 0.6239 -0.0250 0.0107  -0.2796 70   LEU A CD1 
344   C  CD2 . LEU A 70  ? 0.4895 0.4026 0.5466 -0.0304 0.0205  -0.2708 70   LEU A CD2 
345   N  N   . GLU A 71  ? 0.4544 0.3798 0.4951 0.0172  0.0227  -0.2508 71   GLU A N   
346   C  CA  . GLU A 71  ? 0.5101 0.4392 0.5540 0.0265  0.0268  -0.2628 71   GLU A CA  
347   C  C   . GLU A 71  ? 0.5598 0.4716 0.6084 0.0383  0.0273  -0.2484 71   GLU A C   
348   O  O   . GLU A 71  ? 0.4925 0.4166 0.5437 0.0475  0.0300  -0.2534 71   GLU A O   
349   C  CB  . GLU A 71  ? 0.5850 0.5573 0.6194 0.0279  0.0267  -0.2692 71   GLU A CB  
350   C  CG  . GLU A 71  ? 0.4847 0.4784 0.5141 0.0183  0.0249  -0.2862 71   GLU A CG  
351   C  CD  . GLU A 71  ? 0.7020 0.7393 0.7184 0.0219  0.0248  -0.2910 71   GLU A CD  
352   O  OE1 . GLU A 71  ? 0.7649 0.8174 0.7732 0.0274  0.0247  -0.2714 71   GLU A OE1 
353   O  OE2 . GLU A 71  ? 0.7097 0.7659 0.7236 0.0190  0.0253  -0.3145 71   GLU A OE2 
354   N  N   . GLY A 72  ? 0.5832 0.4693 0.6330 0.0381  0.0247  -0.2314 72   GLY A N   
355   C  CA  . GLY A 72  ? 0.5086 0.3749 0.5633 0.0498  0.0240  -0.2198 72   GLY A CA  
356   C  C   . GLY A 72  ? 0.5599 0.4451 0.6127 0.0543  0.0200  -0.2019 72   GLY A C   
357   O  O   . GLY A 72  ? 0.6942 0.5676 0.7519 0.0637  0.0179  -0.1927 72   GLY A O   
358   N  N   . ARG A 73  ? 0.5443 0.4588 0.5904 0.0479  0.0189  -0.1973 73   ARG A N   
359   C  CA  . ARG A 73  ? 0.5236 0.4549 0.5692 0.0505  0.0170  -0.1815 73   ARG A CA  
360   C  C   . ARG A 73  ? 0.6055 0.5188 0.6497 0.0488  0.0119  -0.1639 73   ARG A C   
361   O  O   . ARG A 73  ? 0.6459 0.5472 0.6845 0.0416  0.0101  -0.1604 73   ARG A O   
362   C  CB  . ARG A 73  ? 0.5368 0.5011 0.5739 0.0451  0.0189  -0.1802 73   ARG A CB  
363   C  CG  . ARG A 73  ? 0.4742 0.4589 0.5098 0.0471  0.0240  -0.1985 73   ARG A CG  
364   C  CD  . ARG A 73  ? 0.5374 0.5555 0.5615 0.0442  0.0264  -0.1942 73   ARG A CD  
365   N  NE  . ARG A 73  ? 0.5946 0.6315 0.6122 0.0438  0.0293  -0.2135 73   ARG A NE  
366   C  CZ  . ARG A 73  ? 0.5158 0.5719 0.5338 0.0495  0.0354  -0.2244 73   ARG A CZ  
367   N  NH1 . ARG A 73  ? 0.4748 0.5485 0.4855 0.0491  0.0375  -0.2436 73   ARG A NH1 
368   N  NH2 . ARG A 73  ? 0.6718 0.7316 0.6981 0.0556  0.0395  -0.2172 73   ARG A NH2 
369   N  N   . ASN A 74  ? 0.5736 0.4872 0.6237 0.0554  0.0097  -0.1543 74   ASN A N   
370   C  CA  . ASN A 74  ? 0.4849 0.3832 0.5334 0.0552  0.0045  -0.1394 74   ASN A CA  
371   C  C   . ASN A 74  ? 0.5071 0.4183 0.5491 0.0468  0.0034  -0.1278 74   ASN A C   
372   O  O   . ASN A 74  ? 0.4428 0.3774 0.4854 0.0450  0.0061  -0.1254 74   ASN A O   
373   C  CB  . ASN A 74  ? 0.4638 0.3624 0.5220 0.0653  0.0016  -0.1355 74   ASN A CB  
374   C  CG  . ASN A 74  ? 0.6407 0.5161 0.7026 0.0765  0.0005  -0.1413 74   ASN A CG  
375   O  OD1 . ASN A 74  ? 0.6678 0.5166 0.7235 0.0756  0.0010  -0.1418 74   ASN A OD1 
376   N  ND2 . ASN A 74  ? 0.7555 0.6410 0.8285 0.0874  -0.0004 -0.1454 74   ASN A ND2 
377   N  N   . LEU A 75  ? 0.5433 0.4382 0.5789 0.0421  0.0005  -0.1203 75   LEU A N   
378   C  CA  . LEU A 75  ? 0.4452 0.3478 0.4754 0.0363  -0.0011 -0.1081 75   LEU A CA  
379   C  C   . LEU A 75  ? 0.4333 0.3269 0.4669 0.0402  -0.0051 -0.0977 75   LEU A C   
380   O  O   . LEU A 75  ? 0.6184 0.4906 0.6502 0.0435  -0.0083 -0.0950 75   LEU A O   
381   C  CB  . LEU A 75  ? 0.5305 0.4237 0.5534 0.0293  -0.0017 -0.1071 75   LEU A CB  
382   C  CG  . LEU A 75  ? 0.4826 0.3922 0.5015 0.0234  0.0006  -0.1168 75   LEU A CG  
383   C  CD1 . LEU A 75  ? 0.6631 0.5872 0.6849 0.0265  0.0040  -0.1302 75   LEU A CD1 
384   C  CD2 . LEU A 75  ? 0.5216 0.4153 0.5402 0.0175  0.0008  -0.1231 75   LEU A CD2 
385   N  N   . LEU A 76  ? 0.4534 0.3636 0.4918 0.0398  -0.0043 -0.0925 76   LEU A N   
386   C  CA  . LEU A 76  ? 0.4479 0.3553 0.4934 0.0434  -0.0082 -0.0869 76   LEU A CA  
387   C  C   . LEU A 76  ? 0.4851 0.3962 0.5289 0.0374  -0.0082 -0.0763 76   LEU A C   
388   O  O   . LEU A 76  ? 0.4417 0.3648 0.4821 0.0322  -0.0035 -0.0723 76   LEU A O   
389   C  CB  . LEU A 76  ? 0.3466 0.2712 0.4055 0.0480  -0.0063 -0.0933 76   LEU A CB  
390   C  CG  . LEU A 76  ? 0.5630 0.4857 0.6271 0.0566  -0.0062 -0.1046 76   LEU A CG  
391   C  CD1 . LEU A 76  ? 0.5673 0.5146 0.6456 0.0593  -0.0021 -0.1110 76   LEU A CD1 
392   C  CD2 . LEU A 76  ? 0.6567 0.5585 0.7206 0.0657  -0.0129 -0.1037 76   LEU A CD2 
393   N  N   . ALA A 77  ? 0.5152 0.4159 0.5605 0.0393  -0.0134 -0.0718 77   ALA A N   
394   C  CA  . ALA A 77  ? 0.4633 0.3654 0.5090 0.0343  -0.0133 -0.0636 77   ALA A CA  
395   C  C   . ALA A 77  ? 0.4879 0.3948 0.5460 0.0366  -0.0169 -0.0656 77   ALA A C   
396   O  O   . ALA A 77  ? 0.5046 0.4038 0.5630 0.0435  -0.0236 -0.0687 77   ALA A O   
397   C  CB  . ALA A 77  ? 0.3645 0.2500 0.3985 0.0329  -0.0161 -0.0573 77   ALA A CB  
398   N  N   . LEU A 78  ? 0.4822 0.4020 0.5503 0.0309  -0.0122 -0.0640 78   LEU A N   
399   C  CA  . LEU A 78  ? 0.3045 0.2316 0.3875 0.0307  -0.0153 -0.0680 78   LEU A CA  
400   C  C   . LEU A 78  ? 0.2916 0.2070 0.3708 0.0272  -0.0180 -0.0629 78   LEU A C   
401   O  O   . LEU A 78  ? 0.3673 0.2791 0.4432 0.0207  -0.0120 -0.0555 78   LEU A O   
402   C  CB  . LEU A 78  ? 0.2957 0.2423 0.3950 0.0246  -0.0069 -0.0701 78   LEU A CB  
403   C  CG  . LEU A 78  ? 0.3894 0.3492 0.5097 0.0233  -0.0097 -0.0781 78   LEU A CG  
404   C  CD1 . LEU A 78  ? 0.2043 0.1749 0.3326 0.0337  -0.0169 -0.0886 78   LEU A CD1 
405   C  CD2 . LEU A 78  ? 0.3154 0.2905 0.4521 0.0132  0.0017  -0.0777 78   LEU A CD2 
406   N  N   . GLN A 79  ? 0.2787 0.1885 0.3573 0.0327  -0.0269 -0.0668 79   GLN A N   
407   C  CA  . GLN A 79  ? 0.3238 0.2259 0.4010 0.0301  -0.0303 -0.0654 79   GLN A CA  
408   C  C   . GLN A 79  ? 0.3281 0.2447 0.4257 0.0252  -0.0305 -0.0732 79   GLN A C   
409   O  O   . GLN A 79  ? 0.3070 0.2398 0.4182 0.0288  -0.0343 -0.0822 79   GLN A O   
410   C  CB  . GLN A 79  ? 0.2925 0.1831 0.3569 0.0391  -0.0396 -0.0661 79   GLN A CB  
411   C  CG  . GLN A 79  ? 0.2546 0.1432 0.3196 0.0386  -0.0449 -0.0690 79   GLN A CG  
412   C  CD  . GLN A 79  ? 0.3732 0.2539 0.4243 0.0496  -0.0540 -0.0697 79   GLN A CD  
413   O  OE1 . GLN A 79  ? 0.3281 0.2080 0.3746 0.0585  -0.0572 -0.0698 79   GLN A OE1 
414   N  NE2 . GLN A 79  ? 0.3075 0.1815 0.3506 0.0498  -0.0576 -0.0697 79   GLN A NE2 
415   N  N   . ILE A 80  ? 0.4635 0.3740 0.5641 0.0171  -0.0262 -0.0705 80   ILE A N   
416   C  CA  . ILE A 80  ? 0.3607 0.2812 0.4815 0.0100  -0.0255 -0.0791 80   ILE A CA  
417   C  C   . ILE A 80  ? 0.4817 0.3900 0.5964 0.0100  -0.0309 -0.0811 80   ILE A C   
418   O  O   . ILE A 80  ? 0.5884 0.4793 0.6895 0.0087  -0.0273 -0.0721 80   ILE A O   
419   C  CB  . ILE A 80  ? 0.3592 0.2808 0.4913 -0.0013 -0.0118 -0.0738 80   ILE A CB  
420   C  CG1 . ILE A 80  ? 0.3068 0.2424 0.4433 -0.0010 -0.0054 -0.0720 80   ILE A CG1 
421   C  CG2 . ILE A 80  ? 0.3448 0.2731 0.4998 -0.0108 -0.0094 -0.0835 80   ILE A CG2 
422   C  CD1 . ILE A 80  ? 0.2883 0.2226 0.4272 -0.0094 0.0094  -0.0622 80   ILE A CD1 
423   N  N   . SER A 81  ? 0.5448 0.4643 0.6694 0.0121  -0.0399 -0.0938 81   SER A N   
424   C  CA  . SER A 81  ? 0.4383 0.3486 0.5555 0.0133  -0.0460 -0.0981 81   SER A CA  
425   C  C   . SER A 81  ? 0.5194 0.4480 0.6575 0.0098  -0.0521 -0.1154 81   SER A C   
426   O  O   . SER A 81  ? 0.6550 0.6054 0.8122 0.0088  -0.0536 -0.1240 81   SER A O   
427   C  CB  . SER A 81  ? 0.3874 0.2899 0.4808 0.0264  -0.0553 -0.0941 81   SER A CB  
428   O  OG  . SER A 81  ? 0.6615 0.5794 0.7577 0.0358  -0.0634 -0.0997 81   SER A OG  
429   N  N   . ARG A 82  ? 0.6004 0.5223 0.7358 0.0081  -0.0557 -0.1220 82   ARG A N   
430   C  CA  . ARG A 82  ? 0.6008 0.5422 0.7547 0.0055  -0.0636 -0.1415 82   ARG A CA  
431   C  C   . ARG A 82  ? 0.6590 0.6221 0.8099 0.0192  -0.0772 -0.1479 82   ARG A C   
432   O  O   . ARG A 82  ? 0.7166 0.7062 0.8904 0.0178  -0.0815 -0.1613 82   ARG A O   
433   C  CB  . ARG A 82  ? 0.6382 0.5679 0.7831 0.0049  -0.0672 -0.1479 82   ARG A CB  
434   C  CG  . ARG A 82  ? 0.6177 0.5693 0.7789 0.0032  -0.0774 -0.1708 82   ARG A CG  
435   C  CD  . ARG A 82  ? 0.7594 0.7008 0.9369 -0.0114 -0.0696 -0.1810 82   ARG A CD  
436   N  NE  . ARG A 82  ? 0.8326 0.7709 0.9974 -0.0066 -0.0781 -0.1919 82   ARG A NE  
437   C  CZ  . ARG A 82  ? 0.9579 0.8929 1.1376 -0.0170 -0.0756 -0.2080 82   ARG A CZ  
438   N  NH1 . ARG A 82  ? 0.8819 0.8156 1.0464 -0.0105 -0.0841 -0.2180 82   ARG A NH1 
439   N  NH2 . ARG A 82  ? 1.0102 0.9426 1.2198 -0.0340 -0.0639 -0.2144 82   ARG A NH2 
440   N  N   . ASN A 83  ? 0.5281 0.4796 0.6510 0.0329  -0.0831 -0.1376 83   ASN A N   
441   C  CA  . ASN A 83  ? 0.4748 0.4409 0.5898 0.0489  -0.0951 -0.1400 83   ASN A CA  
442   C  C   . ASN A 83  ? 0.3872 0.3350 0.4797 0.0582  -0.0924 -0.1230 83   ASN A C   
443   O  O   . ASN A 83  ? 0.5401 0.4674 0.6081 0.0630  -0.0920 -0.1131 83   ASN A O   
444   C  CB  . ASN A 83  ? 0.7155 0.6880 0.8172 0.0588  -0.1081 -0.1489 83   ASN A CB  
445   C  CG  . ASN A 83  ? 0.8772 0.8546 0.9594 0.0790  -0.1190 -0.1443 83   ASN A CG  
446   O  OD1 . ASN A 83  ? 0.8790 0.8667 0.9687 0.0856  -0.1205 -0.1428 83   ASN A OD1 
447   N  ND2 . ASN A 83  ? 0.9116 0.8808 0.9678 0.0897  -0.1259 -0.1417 83   ASN A ND2 
448   N  N   . THR A 84  ? 0.4984 0.4545 0.6004 0.0606  -0.0900 -0.1210 84   THR A N   
449   C  CA  . THR A 84  ? 0.4642 0.4024 0.5489 0.0668  -0.0854 -0.1070 84   THR A CA  
450   C  C   . THR A 84  ? 0.3868 0.3139 0.4465 0.0836  -0.0936 -0.1009 84   THR A C   
451   O  O   . THR A 84  ? 0.4800 0.3863 0.5226 0.0870  -0.0887 -0.0890 84   THR A O   
452   C  CB  . THR A 84  ? 0.4011 0.3522 0.5025 0.0661  -0.0808 -0.1086 84   THR A CB  
453   O  OG1 . THR A 84  ? 0.5717 0.5058 0.6656 0.0595  -0.0697 -0.0974 84   THR A OG1 
454   C  CG2 . THR A 84  ? 0.3523 0.3109 0.4494 0.0833  -0.0896 -0.1103 84   THR A CG2 
455   N  N   . ARG A 85  ? 0.3322 0.2729 0.3891 0.0940  -0.1055 -0.1089 85   ARG A N   
456   C  CA  . ARG A 85  ? 0.4853 0.4142 0.5155 0.1112  -0.1123 -0.1011 85   ARG A CA  
457   C  C   . ARG A 85  ? 0.5599 0.4603 0.5647 0.1087  -0.1060 -0.0885 85   ARG A C   
458   O  O   . ARG A 85  ? 0.7066 0.5861 0.6930 0.1154  -0.1020 -0.0760 85   ARG A O   
459   C  CB  . ARG A 85  ? 0.7447 0.6963 0.7741 0.1235  -0.1269 -0.1124 85   ARG A CB  
460   C  CG  . ARG A 85  ? 0.9603 0.9434 1.0139 0.1300  -0.1349 -0.1251 85   ARG A CG  
461   C  CD  . ARG A 85  ? 1.2033 1.2051 1.2463 0.1501  -0.1508 -0.1311 85   ARG A CD  
462   N  NE  . ARG A 85  ? 1.3436 1.3282 1.3618 0.1705  -0.1530 -0.1165 85   ARG A NE  
463   C  CZ  . ARG A 85  ? 1.3078 1.2666 1.2925 0.1797  -0.1522 -0.1024 85   ARG A CZ  
464   N  NH1 . ARG A 85  ? 1.2567 1.1981 1.2215 0.1977  -0.1525 -0.0888 85   ARG A NH1 
465   N  NH2 . ARG A 85  ? 1.2589 1.2083 1.2306 0.1711  -0.1500 -0.1018 85   ARG A NH2 
466   N  N   . SER A 86  ? 0.7317 0.6314 0.7369 0.0989  -0.1044 -0.0925 86   SER A N   
467   C  CA  . SER A 86  ? 0.6835 0.5599 0.6672 0.0963  -0.0981 -0.0820 86   SER A CA  
468   C  C   . SER A 86  ? 0.7626 0.6330 0.7581 0.0795  -0.0883 -0.0820 86   SER A C   
469   O  O   . SER A 86  ? 0.9707 0.8483 0.9867 0.0701  -0.0835 -0.0849 86   SER A O   
470   C  CB  . SER A 86  ? 0.6210 0.5000 0.5864 0.1054  -0.1062 -0.0857 86   SER A CB  
471   O  OG  . SER A 86  ? 0.6791 0.5620 0.6288 0.1236  -0.1151 -0.0829 86   SER A OG  
472   N  N   . ARG A 87  ? 0.7104 0.5675 0.6916 0.0771  -0.0848 -0.0778 87   ARG A N   
473   C  CA  . ARG A 87  ? 0.5905 0.4422 0.5814 0.0642  -0.0768 -0.0785 87   ARG A CA  
474   C  C   . ARG A 87  ? 0.5684 0.4212 0.5521 0.0656  -0.0808 -0.0865 87   ARG A C   
475   O  O   . ARG A 87  ? 0.4472 0.2920 0.4085 0.0737  -0.0826 -0.0819 87   ARG A O   
476   C  CB  . ARG A 87  ? 0.3052 0.1418 0.2861 0.0599  -0.0670 -0.0640 87   ARG A CB  
477   C  CG  . ARG A 87  ? 0.3439 0.1873 0.3403 0.0468  -0.0586 -0.0594 87   ARG A CG  
478   C  CD  . ARG A 87  ? 0.3537 0.1938 0.3391 0.0427  -0.0510 -0.0464 87   ARG A CD  
479   N  NE  . ARG A 87  ? 0.5622 0.3957 0.5385 0.0430  -0.0495 -0.0462 87   ARG A NE  
480   C  CZ  . ARG A 87  ? 0.5763 0.4006 0.5337 0.0490  -0.0503 -0.0435 87   ARG A CZ  
481   N  NH1 . ARG A 87  ? 0.7262 0.5445 0.6709 0.0551  -0.0519 -0.0395 87   ARG A NH1 
482   N  NH2 . ARG A 87  ? 0.6769 0.4960 0.6279 0.0494  -0.0482 -0.0447 87   ARG A NH2 
483   N  N   . ASN A 88  ? 0.6138 0.4760 0.6164 0.0575  -0.0816 -0.0991 88   ASN A N   
484   C  CA  . ASN A 88  ? 0.4610 0.3242 0.4583 0.0581  -0.0852 -0.1097 88   ASN A CA  
485   C  C   . ASN A 88  ? 0.5607 0.4045 0.5417 0.0574  -0.0772 -0.1002 88   ASN A C   
486   O  O   . ASN A 88  ? 0.6121 0.4440 0.5979 0.0506  -0.0674 -0.0906 88   ASN A O   
487   C  CB  . ASN A 88  ? 0.6084 0.4813 0.6324 0.0468  -0.0847 -0.1253 88   ASN A CB  
488   C  CG  . ASN A 88  ? 0.8187 0.7156 0.8619 0.0468  -0.0927 -0.1371 88   ASN A CG  
489   O  OD1 . ASN A 88  ? 0.9398 0.8421 1.0070 0.0366  -0.0871 -0.1393 88   ASN A OD1 
490   N  ND2 . ASN A 88  ? 0.8811 0.7942 0.9137 0.0593  -0.1054 -0.1444 88   ASN A ND2 
491   N  N   . LEU A 89  ? 0.4575 0.3003 0.4187 0.0655  -0.0814 -0.1033 89   LEU A N   
492   C  CA  . LEU A 89  ? 0.4439 0.2713 0.3900 0.0658  -0.0738 -0.0957 89   LEU A CA  
493   C  C   . LEU A 89  ? 0.5169 0.3354 0.4807 0.0547  -0.0648 -0.0968 89   LEU A C   
494   O  O   . LEU A 89  ? 0.5453 0.3682 0.5274 0.0481  -0.0658 -0.1095 89   LEU A O   
495   C  CB  . LEU A 89  ? 0.4315 0.2629 0.3588 0.0742  -0.0794 -0.1045 89   LEU A CB  
496   C  CG  . LEU A 89  ? 0.4122 0.2304 0.3178 0.0781  -0.0718 -0.0946 89   LEU A CG  
497   C  CD1 . LEU A 89  ? 0.2727 0.0850 0.1593 0.0853  -0.0700 -0.0785 89   LEU A CD1 
498   C  CD2 . LEU A 89  ? 0.5658 0.3892 0.4568 0.0844  -0.0759 -0.1067 89   LEU A CD2 
499   N  N   . LEU A 90  ? 0.4859 0.2985 0.4458 0.0521  -0.0560 -0.0808 90   LEU A N   
500   C  CA  . LEU A 90  ? 0.5478 0.3589 0.5207 0.0442  -0.0475 -0.0761 90   LEU A CA  
501   C  C   . LEU A 90  ? 0.5332 0.3500 0.5287 0.0354  -0.0440 -0.0741 90   LEU A C   
502   O  O   . LEU A 90  ? 0.4700 0.2827 0.4763 0.0301  -0.0365 -0.0713 90   LEU A O   
503   C  CB  . LEU A 90  ? 0.5049 0.3093 0.4777 0.0451  -0.0470 -0.0887 90   LEU A CB  
504   C  CG  . LEU A 90  ? 0.5466 0.3441 0.4962 0.0534  -0.0459 -0.0874 90   LEU A CG  
505   C  CD1 . LEU A 90  ? 0.2736 0.0655 0.2220 0.0552  -0.0456 -0.1025 90   LEU A CD1 
506   C  CD2 . LEU A 90  ? 0.4670 0.2630 0.4125 0.0522  -0.0373 -0.0700 90   LEU A CD2 
507   N  N   . THR A 91  ? 0.4022 0.2267 0.4037 0.0350  -0.0485 -0.0755 91   THR A N   
508   C  CA  . THR A 91  ? 0.5253 0.3551 0.5444 0.0276  -0.0432 -0.0706 91   THR A CA  
509   C  C   . THR A 91  ? 0.5336 0.3659 0.5443 0.0276  -0.0379 -0.0545 91   THR A C   
510   O  O   . THR A 91  ? 0.3567 0.1909 0.3541 0.0324  -0.0412 -0.0500 91   THR A O   
511   C  CB  . THR A 91  ? 0.3909 0.2293 0.4216 0.0272  -0.0493 -0.0798 91   THR A CB  
512   O  OG1 . THR A 91  ? 0.3212 0.1613 0.3637 0.0249  -0.0543 -0.0986 91   THR A OG1 
513   C  CG2 . THR A 91  ? 0.1811 0.0239 0.2271 0.0200  -0.0418 -0.0732 91   THR A CG2 
514   N  N   . PRO A 92  ? 0.4781 0.3093 0.4962 0.0227  -0.0292 -0.0469 92   PRO A N   
515   C  CA  . PRO A 92  ? 0.4335 0.2687 0.4451 0.0225  -0.0241 -0.0346 92   PRO A CA  
516   C  C   . PRO A 92  ? 0.5502 0.3939 0.5657 0.0212  -0.0250 -0.0326 92   PRO A C   
517   O  O   . PRO A 92  ? 0.4918 0.3369 0.5212 0.0174  -0.0230 -0.0356 92   PRO A O   
518   C  CB  . PRO A 92  ? 0.3709 0.2000 0.3907 0.0195  -0.0154 -0.0299 92   PRO A CB  
519   C  CG  . PRO A 92  ? 0.3884 0.2075 0.4171 0.0178  -0.0151 -0.0391 92   PRO A CG  
520   C  CD  . PRO A 92  ? 0.3156 0.1391 0.3485 0.0175  -0.0234 -0.0512 92   PRO A CD  
521   N  N   . PRO A 93  ? 0.5451 0.3930 0.5492 0.0238  -0.0270 -0.0283 93   PRO A N   
522   C  CA  . PRO A 93  ? 0.5181 0.3726 0.5255 0.0226  -0.0263 -0.0264 93   PRO A CA  
523   C  C   . PRO A 93  ? 0.5526 0.4092 0.5614 0.0201  -0.0191 -0.0194 93   PRO A C   
524   O  O   . PRO A 93  ? 0.4382 0.2929 0.4404 0.0210  -0.0162 -0.0147 93   PRO A O   
525   C  CB  . PRO A 93  ? 0.1884 0.0425 0.1829 0.0261  -0.0298 -0.0252 93   PRO A CB  
526   C  CG  . PRO A 93  ? 0.3037 0.1511 0.2865 0.0285  -0.0302 -0.0240 93   PRO A CG  
527   C  CD  . PRO A 93  ? 0.3111 0.1559 0.2997 0.0272  -0.0280 -0.0255 93   PRO A CD  
528   N  N   . VAL A 94  ? 0.4038 0.2633 0.4209 0.0180  -0.0161 -0.0191 94   VAL A N   
529   C  CA  . VAL A 94  ? 0.2897 0.1487 0.3062 0.0175  -0.0095 -0.0122 94   VAL A CA  
530   C  C   . VAL A 94  ? 0.4325 0.2966 0.4508 0.0172  -0.0090 -0.0137 94   VAL A C   
531   O  O   . VAL A 94  ? 0.5143 0.3813 0.5386 0.0169  -0.0123 -0.0202 94   VAL A O   
532   C  CB  . VAL A 94  ? 0.4087 0.2593 0.4341 0.0153  -0.0029 -0.0092 94   VAL A CB  
533   C  CG1 . VAL A 94  ? 0.7849 0.6320 0.8063 0.0174  0.0041  0.0009  94   VAL A CG1 
534   C  CG2 . VAL A 94  ? 0.4270 0.2707 0.4528 0.0156  -0.0036 -0.0108 94   VAL A CG2 
535   N  N   . LYS A 95  ? 0.3767 0.2413 0.3899 0.0187  -0.0052 -0.0087 95   LYS A N   
536   C  CA  . LYS A 95  ? 0.4285 0.2963 0.4427 0.0192  -0.0039 -0.0115 95   LYS A CA  
537   C  C   . LYS A 95  ? 0.4672 0.3441 0.4786 0.0199  0.0027  -0.0036 95   LYS A C   
538   O  O   . LYS A 95  ? 0.3764 0.2523 0.3817 0.0227  0.0050  0.0046  95   LYS A O   
539   C  CB  . LYS A 95  ? 0.3186 0.1911 0.3263 0.0202  -0.0082 -0.0165 95   LYS A CB  
540   C  CG  . LYS A 95  ? 0.3462 0.2188 0.3459 0.0218  -0.0081 -0.0132 95   LYS A CG  
541   C  CD  . LYS A 95  ? 0.3725 0.2453 0.3684 0.0202  -0.0119 -0.0159 95   LYS A CD  
542   C  CE  . LYS A 95  ? 0.3921 0.2659 0.3842 0.0200  -0.0113 -0.0183 95   LYS A CE  
543   N  NZ  . LYS A 95  ? 0.5485 0.4306 0.5387 0.0226  -0.0095 -0.0128 95   LYS A NZ  
544   N  N   . TYR A 96  ? 0.4670 0.3547 0.4823 0.0183  0.0061  -0.0056 96   TYR A N   
545   C  CA  . TYR A 96  ? 0.5170 0.4177 0.5260 0.0199  0.0123  0.0013  96   TYR A CA  
546   C  C   . TYR A 96  ? 0.4929 0.4086 0.4983 0.0206  0.0100  -0.0070 96   TYR A C   
547   O  O   . TYR A 96  ? 0.3555 0.2731 0.3683 0.0189  0.0089  -0.0158 96   TYR A O   
548   C  CB  . TYR A 96  ? 0.4212 0.3222 0.4379 0.0167  0.0212  0.0068  96   TYR A CB  
549   C  CG  . TYR A 96  ? 0.4518 0.3391 0.4687 0.0168  0.0271  0.0182  96   TYR A CG  
550   C  CD1 . TYR A 96  ? 0.3400 0.2216 0.3471 0.0223  0.0250  0.0253  96   TYR A CD1 
551   C  CD2 . TYR A 96  ? 0.4673 0.3476 0.4959 0.0113  0.0357  0.0214  96   TYR A CD2 
552   C  CE1 . TYR A 96  ? 0.3182 0.1853 0.3256 0.0240  0.0311  0.0359  96   TYR A CE1 
553   C  CE2 . TYR A 96  ? 0.4915 0.3554 0.5210 0.0112  0.0425  0.0316  96   TYR A CE2 
554   C  CZ  . TYR A 96  ? 0.5316 0.3879 0.5497 0.0183  0.0400  0.0391  96   TYR A CZ  
555   O  OH  . TYR A 96  ? 0.5822 0.4201 0.6011 0.0199  0.0471  0.0493  96   TYR A OH  
556   N  N   . ILE A 97  ? 0.4578 0.3852 0.4526 0.0237  0.0091  -0.0058 97   ILE A N   
557   C  CA  . ILE A 97  ? 0.5175 0.4601 0.5095 0.0238  0.0079  -0.0155 97   ILE A CA  
558   C  C   . ILE A 97  ? 0.4777 0.4393 0.4604 0.0272  0.0135  -0.0097 97   ILE A C   
559   O  O   . ILE A 97  ? 0.3789 0.3424 0.3539 0.0310  0.0163  0.0025  97   ILE A O   
560   C  CB  . ILE A 97  ? 0.4628 0.4067 0.4519 0.0233  0.0015  -0.0245 97   ILE A CB  
561   C  CG1 . ILE A 97  ? 0.4582 0.3820 0.4537 0.0209  -0.0027 -0.0288 97   ILE A CG1 
562   C  CG2 . ILE A 97  ? 0.3570 0.3150 0.3448 0.0227  0.0013  -0.0366 97   ILE A CG2 
563   C  CD1 . ILE A 97  ? 0.4747 0.3871 0.4691 0.0214  -0.0043 -0.0214 97   ILE A CD1 
564   N  N   . ALA A 98  ? 0.3839 0.3590 0.3661 0.0269  0.0156  -0.0180 98   ALA A N   
565   C  CA  . ALA A 98  ? 0.2341 0.2300 0.2049 0.0308  0.0212  -0.0136 98   ALA A CA  
566   C  C   . ALA A 98  ? 0.4267 0.4412 0.3928 0.0316  0.0183  -0.0287 98   ALA A C   
567   O  O   . ALA A 98  ? 0.5424 0.5506 0.5161 0.0284  0.0133  -0.0424 98   ALA A O   
568   C  CB  . ALA A 98  ? 0.2297 0.2250 0.2048 0.0294  0.0312  -0.0062 98   ALA A CB  
569   N  N   . ASN A 99  ? 0.4682 0.5049 0.4209 0.0363  0.0220  -0.0261 99   ASN A N   
570   C  CA  . ASN A 99  ? 0.3821 0.4394 0.3299 0.0372  0.0210  -0.0416 99   ASN A CA  
571   C  C   . ASN A 99  ? 0.5675 0.6266 0.5187 0.0344  0.0122  -0.0586 99   ASN A C   
572   O  O   . ASN A 99  ? 0.6259 0.6889 0.5815 0.0322  0.0115  -0.0753 99   ASN A O   
573   C  CB  . ASN A 99  ? 0.4415 0.4974 0.3984 0.0349  0.0269  -0.0490 99   ASN A CB  
574   C  CG  . ASN A 99  ? 0.4825 0.5624 0.4314 0.0375  0.0288  -0.0629 99   ASN A CG  
575   O  OD1 . ASN A 99  ? 0.4279 0.5061 0.3856 0.0355  0.0272  -0.0796 99   ASN A OD1 
576   N  ND2 . ASN A 99  ? 0.5105 0.6130 0.4415 0.0432  0.0323  -0.0561 99   ASN A ND2 
577   N  N   . MET A 100 ? 0.5423 0.5983 0.4927 0.0343  0.0063  -0.0550 100  MET A N   
578   C  CA  . MET A 100 ? 0.4802 0.5392 0.4357 0.0299  -0.0005 -0.0712 100  MET A CA  
579   C  C   . MET A 100 ? 0.5051 0.5956 0.4507 0.0326  -0.0024 -0.0837 100  MET A C   
580   O  O   . MET A 100 ? 0.5609 0.6564 0.5122 0.0278  -0.0050 -0.1033 100  MET A O   
581   C  CB  . MET A 100 ? 0.5135 0.5644 0.4723 0.0287  -0.0052 -0.0650 100  MET A CB  
582   C  CG  . MET A 100 ? 0.5949 0.6697 0.5428 0.0354  -0.0082 -0.0578 100  MET A CG  
583   S  SD  . MET A 100 ? 0.5778 0.6431 0.5334 0.0337  -0.0131 -0.0531 100  MET A SD  
584   C  CE  . MET A 100 ? 0.4092 0.4614 0.3798 0.0217  -0.0152 -0.0736 100  MET A CE  
585   N  N   . HIS A 101 ? 0.4638 0.5754 0.3940 0.0407  -0.0007 -0.0723 101  HIS A N   
586   C  CA  . HIS A 101 ? 0.3540 0.4982 0.2713 0.0454  -0.0013 -0.0826 101  HIS A CA  
587   C  C   . HIS A 101 ? 0.5099 0.6533 0.4229 0.0471  0.0077  -0.0805 101  HIS A C   
588   O  O   . HIS A 101 ? 0.3523 0.4921 0.2577 0.0518  0.0150  -0.0612 101  HIS A O   
589   C  CB  . HIS A 101 ? 0.2287 0.3981 0.1290 0.0555  -0.0043 -0.0707 101  HIS A CB  
590   C  CG  . HIS A 101 ? 0.4727 0.6470 0.3794 0.0545  -0.0130 -0.0737 101  HIS A CG  
591   N  ND1 . HIS A 101 ? 0.6095 0.7704 0.5174 0.0581  -0.0135 -0.0555 101  HIS A ND1 
592   C  CD2 . HIS A 101 ? 0.6296 0.8212 0.5439 0.0494  -0.0208 -0.0942 101  HIS A CD2 
593   C  CE1 . HIS A 101 ? 0.6536 0.8252 0.5690 0.0563  -0.0213 -0.0640 101  HIS A CE1 
594   N  NE2 . HIS A 101 ? 0.6244 0.8151 0.5446 0.0503  -0.0257 -0.0874 101  HIS A NE2 
595   N  N   . GLY A 102 ? 0.4307 0.5761 0.3505 0.0428  0.0081  -0.1008 102  GLY A N   
596   C  CA  . GLY A 102 ? 0.3282 0.4741 0.2479 0.0439  0.0164  -0.1031 102  GLY A CA  
597   C  C   . GLY A 102 ? 0.4022 0.5701 0.3030 0.0519  0.0244  -0.0902 102  GLY A C   
598   O  O   . GLY A 102 ? 0.6072 0.7699 0.5105 0.0521  0.0338  -0.0833 102  GLY A O   
599   N  N   . ASP A 103 ? 0.5266 0.7207 0.4087 0.0590  0.0211  -0.0867 103  ASP A N   
600   C  CA  . ASP A 103 ? 0.5284 0.7436 0.3884 0.0684  0.0293  -0.0723 103  ASP A CA  
601   C  C   . ASP A 103 ? 0.4584 0.6595 0.3120 0.0728  0.0349  -0.0427 103  ASP A C   
602   O  O   . ASP A 103 ? 0.5990 0.8116 0.4342 0.0807  0.0438  -0.0263 103  ASP A O   
603   C  CB  . ASP A 103 ? 0.5817 0.8353 0.4216 0.0763  0.0230  -0.0834 103  ASP A CB  
604   C  CG  . ASP A 103 ? 0.6031 0.8636 0.4461 0.0761  0.0099  -0.0896 103  ASP A CG  
605   O  OD1 . ASP A 103 ? 0.6912 0.9838 0.5252 0.0795  0.0023  -0.1068 103  ASP A OD1 
606   O  OD2 . ASP A 103 ? 0.7236 0.9600 0.5789 0.0726  0.0073  -0.0785 103  ASP A OD2 
607   N  N   . GLU A 104 ? 0.4314 0.6066 0.2996 0.0681  0.0304  -0.0359 104  GLU A N   
608   C  CA  . GLU A 104 ? 0.4129 0.5689 0.2791 0.0709  0.0362  -0.0103 104  GLU A CA  
609   C  C   . GLU A 104 ? 0.5615 0.6890 0.4472 0.0618  0.0437  -0.0069 104  GLU A C   
610   O  O   . GLU A 104 ? 0.5785 0.6846 0.4824 0.0547  0.0380  -0.0132 104  GLU A O   
611   C  CB  . GLU A 104 ? 0.3278 0.4766 0.1972 0.0726  0.0264  -0.0062 104  GLU A CB  
612   C  CG  . GLU A 104 ? 0.5539 0.7351 0.4081 0.0814  0.0170  -0.0125 104  GLU A CG  
613   C  CD  . GLU A 104 ? 0.6669 0.8425 0.5303 0.0810  0.0071  -0.0133 104  GLU A CD  
614   O  OE1 . GLU A 104 ? 0.7717 0.9171 0.6485 0.0759  0.0089  -0.0048 104  GLU A OE1 
615   O  OE2 . GLU A 104 ? 0.8179 1.0210 0.6760 0.0854  -0.0024 -0.0238 104  GLU A OE2 
616   N  N   . THR A 105 ? 0.5691 0.6982 0.4506 0.0623  0.0567  0.0032  105  THR A N   
617   C  CA  . THR A 105 ? 0.4245 0.5396 0.3254 0.0537  0.0638  -0.0014 105  THR A CA  
618   C  C   . THR A 105 ? 0.3914 0.4827 0.3032 0.0490  0.0735  0.0166  105  THR A C   
619   O  O   . THR A 105 ? 0.3653 0.4430 0.2983 0.0411  0.0749  0.0102  105  THR A O   
620   C  CB  . THR A 105 ? 0.5874 0.7259 0.4811 0.0555  0.0726  -0.0091 105  THR A CB  
621   O  OG1 . THR A 105 ? 0.4429 0.5949 0.3142 0.0630  0.0835  0.0098  105  THR A OG1 
622   C  CG2 . THR A 105 ? 0.6477 0.8070 0.5357 0.0581  0.0630  -0.0322 105  THR A CG2 
623   N  N   . VAL A 106 ? 0.4373 0.5239 0.3355 0.0543  0.0803  0.0383  106  VAL A N   
624   C  CA  . VAL A 106 ? 0.4116 0.4745 0.3207 0.0488  0.0919  0.0547  106  VAL A CA  
625   C  C   . VAL A 106 ? 0.5106 0.5483 0.4433 0.0406  0.0843  0.0481  106  VAL A C   
626   O  O   . VAL A 106 ? 0.5750 0.6013 0.5277 0.0316  0.0899  0.0453  106  VAL A O   
627   C  CB  . VAL A 106 ? 0.5941 0.6509 0.4834 0.0575  0.1002  0.0802  106  VAL A CB  
628   C  CG1 . VAL A 106 ? 0.5460 0.5748 0.4489 0.0502  0.1138  0.0958  106  VAL A CG1 
629   C  CG2 . VAL A 106 ? 0.5746 0.6576 0.4375 0.0672  0.1081  0.0880  106  VAL A CG2 
630   N  N   . GLY A 107 ? 0.6325 0.6641 0.5630 0.0437  0.0714  0.0448  107  GLY A N   
631   C  CA  . GLY A 107 ? 0.4436 0.4531 0.3923 0.0374  0.0638  0.0386  107  GLY A CA  
632   C  C   . GLY A 107 ? 0.5091 0.5183 0.4769 0.0298  0.0613  0.0214  107  GLY A C   
633   O  O   . GLY A 107 ? 0.5126 0.5055 0.4981 0.0232  0.0620  0.0199  107  GLY A O   
634   N  N   . ARG A 108 ? 0.5020 0.5301 0.4659 0.0316  0.0581  0.0076  108  ARG A N   
635   C  CA  . ARG A 108 ? 0.4691 0.4992 0.4494 0.0271  0.0566  -0.0085 108  ARG A CA  
636   C  C   . ARG A 108 ? 0.3731 0.3989 0.3692 0.0211  0.0671  -0.0037 108  ARG A C   
637   O  O   . ARG A 108 ? 0.5053 0.5185 0.5199 0.0163  0.0635  -0.0093 108  ARG A O   
638   C  CB  . ARG A 108 ? 0.3590 0.4122 0.3310 0.0307  0.0568  -0.0213 108  ARG A CB  
639   C  CG  . ARG A 108 ? 0.4592 0.5177 0.4475 0.0280  0.0602  -0.0341 108  ARG A CG  
640   C  CD  . ARG A 108 ? 0.5894 0.6707 0.5696 0.0321  0.0622  -0.0474 108  ARG A CD  
641   N  NE  . ARG A 108 ? 0.6179 0.6955 0.5995 0.0336  0.0511  -0.0646 108  ARG A NE  
642   C  CZ  . ARG A 108 ? 0.4911 0.5669 0.4856 0.0340  0.0486  -0.0810 108  ARG A CZ  
643   N  NH1 . ARG A 108 ? 0.4629 0.5443 0.4713 0.0338  0.0552  -0.0844 108  ARG A NH1 
644   N  NH2 . ARG A 108 ? 0.4688 0.5370 0.4627 0.0349  0.0398  -0.0943 108  ARG A NH2 
645   N  N   . GLN A 109 ? 0.4256 0.4630 0.4146 0.0215  0.0804  0.0064  109  GLN A N   
646   C  CA  . GLN A 109 ? 0.5708 0.6076 0.5771 0.0142  0.0928  0.0098  109  GLN A CA  
647   C  C   . GLN A 109 ? 0.4771 0.4905 0.4954 0.0079  0.0955  0.0200  109  GLN A C   
648   O  O   . GLN A 109 ? 0.5089 0.5188 0.5503 -0.0001 0.0988  0.0143  109  GLN A O   
649   C  CB  . GLN A 109 ? 0.5813 0.6355 0.5756 0.0157  0.1089  0.0196  109  GLN A CB  
650   C  CG  . GLN A 109 ? 0.5250 0.6037 0.5218 0.0173  0.1110  0.0044  109  GLN A CG  
651   C  CD  . GLN A 109 ? 0.5956 0.6742 0.6209 0.0117  0.1075  -0.0116 109  GLN A CD  
652   O  OE1 . GLN A 109 ? 0.7326 0.8159 0.7623 0.0153  0.0966  -0.0285 109  GLN A OE1 
653   N  NE2 . GLN A 109 ? 0.4582 0.5316 0.5037 0.0030  0.1167  -0.0069 109  GLN A NE2 
654   N  N   . LEU A 110 ? 0.3133 0.3123 0.3173 0.0117  0.0939  0.0336  110  LEU A N   
655   C  CA  . LEU A 110 ? 0.4152 0.3898 0.4300 0.0065  0.0963  0.0422  110  LEU A CA  
656   C  C   . LEU A 110 ? 0.5606 0.5247 0.5945 0.0018  0.0840  0.0275  110  LEU A C   
657   O  O   . LEU A 110 ? 0.5599 0.5111 0.6119 -0.0059 0.0874  0.0269  110  LEU A O   
658   C  CB  . LEU A 110 ? 0.4418 0.4037 0.4371 0.0141  0.0953  0.0581  110  LEU A CB  
659   C  CG  . LEU A 110 ? 0.5042 0.4699 0.4804 0.0198  0.1095  0.0781  110  LEU A CG  
660   C  CD1 . LEU A 110 ? 0.6477 0.5993 0.6076 0.0289  0.1068  0.0931  110  LEU A CD1 
661   C  CD2 . LEU A 110 ? 0.3317 0.2882 0.3211 0.0106  0.1277  0.0869  110  LEU A CD2 
662   N  N   . LEU A 111 ? 0.3812 0.3509 0.4108 0.0065  0.0703  0.0154  111  LEU A N   
663   C  CA  . LEU A 111 ? 0.2449 0.2050 0.2885 0.0042  0.0590  0.0030  111  LEU A CA  
664   C  C   . LEU A 111 ? 0.3914 0.3624 0.4552 -0.0002 0.0601  -0.0097 111  LEU A C   
665   O  O   . LEU A 111 ? 0.5979 0.5623 0.6782 -0.0040 0.0552  -0.0169 111  LEU A O   
666   C  CB  . LEU A 111 ? 0.5558 0.5157 0.5881 0.0104  0.0461  -0.0043 111  LEU A CB  
667   C  CG  . LEU A 111 ? 0.5481 0.4967 0.5663 0.0142  0.0422  0.0052  111  LEU A CG  
668   C  CD1 . LEU A 111 ? 0.4847 0.4336 0.4961 0.0179  0.0306  -0.0040 111  LEU A CD1 
669   C  CD2 . LEU A 111 ? 0.5070 0.4357 0.5346 0.0103  0.0429  0.0105  111  LEU A CD2 
670   N  N   . VAL A 112 ? 0.4916 0.4821 0.5543 0.0011  0.0662  -0.0132 112  VAL A N   
671   C  CA  . VAL A 112 ? 0.3913 0.3960 0.4745 -0.0020 0.0687  -0.0252 112  VAL A CA  
672   C  C   . VAL A 112 ? 0.4632 0.4654 0.5652 -0.0119 0.0794  -0.0204 112  VAL A C   
673   O  O   . VAL A 112 ? 0.5214 0.5262 0.6457 -0.0162 0.0757  -0.0309 112  VAL A O   
674   C  CB  . VAL A 112 ? 0.4591 0.4860 0.5363 0.0015  0.0755  -0.0292 112  VAL A CB  
675   C  CG1 . VAL A 112 ? 0.1848 0.2289 0.2850 -0.0033 0.0837  -0.0372 112  VAL A CG1 
676   C  CG2 . VAL A 112 ? 0.4751 0.5045 0.5422 0.0097  0.0637  -0.0408 112  VAL A CG2 
677   N  N   . TYR A 113 ? 0.4457 0.4426 0.5386 -0.0150 0.0926  -0.0045 113  TYR A N   
678   C  CA  . TYR A 113 ? 0.5057 0.4937 0.6152 -0.0257 0.1051  0.0024  113  TYR A CA  
679   C  C   . TYR A 113 ? 0.4828 0.4507 0.6045 -0.0300 0.0969  -0.0013 113  TYR A C   
680   O  O   . TYR A 113 ? 0.4820 0.4513 0.6287 -0.0393 0.0998  -0.0095 113  TYR A O   
681   C  CB  . TYR A 113 ? 0.4930 0.4725 0.5846 -0.0254 0.1204  0.0235  113  TYR A CB  
682   C  CG  . TYR A 113 ? 0.6233 0.6240 0.7048 -0.0231 0.1328  0.0283  113  TYR A CG  
683   C  CD1 . TYR A 113 ? 0.6778 0.6758 0.7333 -0.0171 0.1428  0.0473  113  TYR A CD1 
684   C  CD2 . TYR A 113 ? 0.6892 0.7141 0.7864 -0.0255 0.1348  0.0140  113  TYR A CD2 
685   C  CE1 . TYR A 113 ? 0.5872 0.6063 0.6309 -0.0142 0.1545  0.0518  113  TYR A CE1 
686   C  CE2 . TYR A 113 ? 0.5695 0.6151 0.6569 -0.0232 0.1471  0.0176  113  TYR A CE2 
687   C  CZ  . TYR A 113 ? 0.5703 0.6129 0.6301 -0.0177 0.1569  0.0364  113  TYR A CZ  
688   O  OH  . TYR A 113 ? 0.6429 0.7076 0.6904 -0.0145 0.1692  0.0398  113  TYR A OH  
689   N  N   . MET A 114 ? 0.3549 0.3061 0.4595 -0.0235 0.0870  0.0036  114  MET A N   
690   C  CA  . MET A 114 ? 0.4629 0.3957 0.5761 -0.0264 0.0793  -0.0003 114  MET A CA  
691   C  C   . MET A 114 ? 0.4592 0.4020 0.5923 -0.0284 0.0680  -0.0194 114  MET A C   
692   O  O   . MET A 114 ? 0.5298 0.4693 0.6831 -0.0364 0.0691  -0.0264 114  MET A O   
693   C  CB  . MET A 114 ? 0.3957 0.3136 0.4869 -0.0176 0.0698  0.0064  114  MET A CB  
694   C  CG  . MET A 114 ? 0.3693 0.2685 0.4664 -0.0192 0.0618  0.0021  114  MET A CG  
695   S  SD  . MET A 114 ? 0.5128 0.3906 0.6238 -0.0291 0.0753  0.0095  114  MET A SD  
696   C  CE  . MET A 114 ? 0.8062 0.6755 0.8938 -0.0226 0.0880  0.0333  114  MET A CE  
697   N  N   . ALA A 115 ? 0.3312 0.2864 0.4586 -0.0206 0.0575  -0.0281 115  ALA A N   
698   C  CA  . ALA A 115 ? 0.3679 0.3332 0.5104 -0.0187 0.0460  -0.0445 115  ALA A CA  
699   C  C   . ALA A 115 ? 0.4701 0.4507 0.6414 -0.0279 0.0526  -0.0536 115  ALA A C   
700   O  O   . ALA A 115 ? 0.5497 0.5291 0.7370 -0.0320 0.0469  -0.0628 115  ALA A O   
701   C  CB  . ALA A 115 ? 0.4032 0.3811 0.5374 -0.0093 0.0396  -0.0507 115  ALA A CB  
702   N  N   . GLN A 116 ? 0.4287 0.4261 0.6071 -0.0313 0.0648  -0.0521 116  GLN A N   
703   C  CA  . GLN A 116 ? 0.3279 0.3430 0.5360 -0.0416 0.0738  -0.0606 116  GLN A CA  
704   C  C   . GLN A 116 ? 0.3858 0.3853 0.6066 -0.0541 0.0821  -0.0567 116  GLN A C   
705   O  O   . GLN A 116 ? 0.4555 0.4629 0.7018 -0.0614 0.0790  -0.0703 116  GLN A O   
706   C  CB  . GLN A 116 ? 0.2141 0.2463 0.4227 -0.0435 0.0891  -0.0556 116  GLN A CB  
707   C  CG  . GLN A 116 ? 0.2721 0.3218 0.4721 -0.0319 0.0825  -0.0627 116  GLN A CG  
708   C  CD  . GLN A 116 ? 0.3926 0.4573 0.5864 -0.0327 0.0985  -0.0560 116  GLN A CD  
709   O  OE1 . GLN A 116 ? 0.3339 0.4210 0.5490 -0.0385 0.1089  -0.0624 116  GLN A OE1 
710   N  NE2 . GLN A 116 ? 0.3690 0.4237 0.5336 -0.0269 0.1006  -0.0436 116  GLN A NE2 
711   N  N   . TYR A 117 ? 0.2861 0.2638 0.4894 -0.0559 0.0924  -0.0390 117  TYR A N   
712   C  CA  . TYR A 117 ? 0.2666 0.2237 0.4795 -0.0670 0.1028  -0.0329 117  TYR A CA  
713   C  C   . TYR A 117 ? 0.3721 0.3194 0.5958 -0.0689 0.0896  -0.0456 117  TYR A C   
714   O  O   . TYR A 117 ? 0.4625 0.4125 0.7129 -0.0806 0.0934  -0.0567 117  TYR A O   
715   C  CB  . TYR A 117 ? 0.3235 0.2565 0.5097 -0.0628 0.1116  -0.0108 117  TYR A CB  
716   C  CG  . TYR A 117 ? 0.2864 0.1940 0.4813 -0.0728 0.1246  -0.0025 117  TYR A CG  
717   C  CD1 . TYR A 117 ? 0.3888 0.2948 0.5976 -0.0845 0.1459  0.0051  117  TYR A CD1 
718   C  CD2 . TYR A 117 ? 0.3819 0.2659 0.5715 -0.0708 0.1168  -0.0025 117  TYR A CD2 
719   C  CE1 . TYR A 117 ? 0.4621 0.3408 0.6799 -0.0941 0.1595  0.0129  117  TYR A CE1 
720   C  CE2 . TYR A 117 ? 0.4603 0.3182 0.6587 -0.0795 0.1293  0.0040  117  TYR A CE2 
721   C  CZ  . TYR A 117 ? 0.5042 0.3583 0.7170 -0.0913 0.1509  0.0118  117  TYR A CZ  
722   O  OH  . TYR A 117 ? 0.4280 0.2527 0.6506 -0.1004 0.1649  0.0184  117  TYR A OH  
723   N  N   . LEU A 118 ? 0.3257 0.2625 0.5285 -0.0576 0.0747  -0.0448 118  LEU A N   
724   C  CA  . LEU A 118 ? 0.3981 0.3265 0.6060 -0.0572 0.0617  -0.0561 118  LEU A CA  
725   C  C   . LEU A 118 ? 0.4900 0.4430 0.7234 -0.0602 0.0527  -0.0772 118  LEU A C   
726   O  O   . LEU A 118 ? 0.6102 0.5635 0.8644 -0.0692 0.0524  -0.0890 118  LEU A O   
727   C  CB  . LEU A 118 ? 0.4414 0.3594 0.6223 -0.0438 0.0476  -0.0520 118  LEU A CB  
728   C  CG  . LEU A 118 ? 0.5137 0.4070 0.6734 -0.0409 0.0536  -0.0347 118  LEU A CG  
729   C  CD1 . LEU A 118 ? 0.6042 0.4915 0.7402 -0.0289 0.0406  -0.0320 118  LEU A CD1 
730   C  CD2 . LEU A 118 ? 0.5510 0.4243 0.7219 -0.0494 0.0599  -0.0351 118  LEU A CD2 
731   N  N   . LEU A 119 ? 0.4664 0.4408 0.6985 -0.0518 0.0451  -0.0829 119  LEU A N   
732   C  CA  . LEU A 119 ? 0.5226 0.5225 0.7768 -0.0508 0.0345  -0.1023 119  LEU A CA  
733   C  C   . LEU A 119 ? 0.4935 0.5114 0.7825 -0.0659 0.0455  -0.1129 119  LEU A C   
734   O  O   . LEU A 119 ? 0.5180 0.5444 0.8278 -0.0718 0.0394  -0.1285 119  LEU A O   
735   C  CB  . LEU A 119 ? 0.5361 0.5539 0.7832 -0.0379 0.0265  -0.1051 119  LEU A CB  
736   C  CG  . LEU A 119 ? 0.4775 0.4817 0.6984 -0.0234 0.0113  -0.1023 119  LEU A CG  
737   C  CD1 . LEU A 119 ? 0.4914 0.5078 0.7046 -0.0112 0.0064  -0.1037 119  LEU A CD1 
738   C  CD2 . LEU A 119 ? 0.3014 0.3069 0.5282 -0.0207 -0.0029 -0.1146 119  LEU A CD2 
739   N  N   . GLY A 120 ? 0.4479 0.4729 0.7434 -0.0725 0.0623  -0.1050 120  GLY A N   
740   C  CA  . GLY A 120 ? 0.3809 0.4258 0.7114 -0.0878 0.0755  -0.1146 120  GLY A CA  
741   C  C   . GLY A 120 ? 0.4204 0.4459 0.7660 -0.1045 0.0877  -0.1138 120  GLY A C   
742   O  O   . GLY A 120 ? 0.4124 0.4529 0.7909 -0.1197 0.0989  -0.1242 120  GLY A O   
743   N  N   . ASN A 121 ? 0.4162 0.4083 0.7396 -0.1020 0.0863  -0.1025 121  ASN A N   
744   C  CA  . ASN A 121 ? 0.4599 0.4286 0.7959 -0.1163 0.0984  -0.1013 121  ASN A CA  
745   C  C   . ASN A 121 ? 0.4692 0.4235 0.8039 -0.1150 0.0845  -0.1124 121  ASN A C   
746   O  O   . ASN A 121 ? 0.4825 0.4244 0.8370 -0.1286 0.0924  -0.1199 121  ASN A O   
747   C  CB  . ASN A 121 ? 0.5135 0.4523 0.8281 -0.1170 0.1162  -0.0755 121  ASN A CB  
748   C  CG  . ASN A 121 ? 0.5696 0.5204 0.8940 -0.1249 0.1364  -0.0665 121  ASN A CG  
749   O  OD1 . ASN A 121 ? 0.5460 0.4944 0.8964 -0.1417 0.1539  -0.0687 121  ASN A OD1 
750   N  ND2 . ASN A 121 ? 0.6375 0.6013 0.9414 -0.1134 0.1350  -0.0569 121  ASN A ND2 
751   N  N   . HIS A 122 ? 0.2679 0.2238 0.5800 -0.0990 0.0651  -0.1140 122  HIS A N   
752   C  CA  . HIS A 122 ? 0.4613 0.4027 0.7652 -0.0950 0.0521  -0.1219 122  HIS A CA  
753   C  C   . HIS A 122 ? 0.5391 0.4948 0.8740 -0.1059 0.0468  -0.1472 122  HIS A C   
754   O  O   . HIS A 122 ? 0.5588 0.4964 0.8929 -0.1089 0.0441  -0.1534 122  HIS A O   
755   C  CB  . HIS A 122 ? 0.6500 0.5953 0.9262 -0.0762 0.0330  -0.1202 122  HIS A CB  
756   C  CG  . HIS A 122 ? 0.7217 0.6978 1.0096 -0.0701 0.0162  -0.1396 122  HIS A CG  
757   N  ND1 . HIS A 122 ? 0.7721 0.7743 1.0657 -0.0642 0.0131  -0.1420 122  HIS A ND1 
758   C  CD2 . HIS A 122 ? 0.6072 0.5931 0.9014 -0.0675 0.0015  -0.1573 122  HIS A CD2 
759   C  CE1 . HIS A 122 ? 0.7615 0.7877 1.0647 -0.0573 -0.0029 -0.1594 122  HIS A CE1 
760   N  NE2 . HIS A 122 ? 0.6337 0.6515 0.9366 -0.0591 -0.0105 -0.1688 122  HIS A NE2 
761   N  N   . GLU A 123 ? 0.5042 0.4945 0.8673 -0.1114 0.0449  -0.1633 123  GLU A N   
762   C  CA  . GLU A 123 ? 0.5921 0.6006 0.9880 -0.1231 0.0402  -0.1894 123  GLU A CA  
763   C  C   . GLU A 123 ? 0.5441 0.5420 0.9707 -0.1461 0.0622  -0.1924 123  GLU A C   
764   O  O   . GLU A 123 ? 0.4370 0.4380 0.8885 -0.1584 0.0614  -0.2128 123  GLU A O   
765   C  CB  . GLU A 123 ? 0.7498 0.8043 1.1651 -0.1176 0.0260  -0.2085 123  GLU A CB  
766   C  CG  . GLU A 123 ? 1.0060 1.0693 1.3944 -0.0954 0.0029  -0.2097 123  GLU A CG  
767   C  CD  . GLU A 123 ? 1.1912 1.2990 1.6012 -0.0893 -0.0135 -0.2329 123  GLU A CD  
768   O  OE1 . GLU A 123 ? 1.2383 1.3754 1.6832 -0.1002 -0.0067 -0.2453 123  GLU A OE1 
769   O  OE2 . GLU A 123 ? 1.2781 1.3926 1.6702 -0.0730 -0.0331 -0.2384 123  GLU A OE2 
770   N  N   . ARG A 124 ? 0.5345 0.5193 0.9583 -0.1517 0.0825  -0.1724 124  ARG A N   
771   C  CA  . ARG A 124 ? 0.5463 0.5189 0.9979 -0.1734 0.1067  -0.1716 124  ARG A CA  
772   C  C   . ARG A 124 ? 0.5027 0.4266 0.9376 -0.1767 0.1194  -0.1551 124  ARG A C   
773   O  O   . ARG A 124 ? 0.5104 0.4175 0.9694 -0.1938 0.1326  -0.1632 124  ARG A O   
774   C  CB  . ARG A 124 ? 0.7561 0.7412 1.2146 -0.1785 0.1248  -0.1582 124  ARG A CB  
775   C  CG  . ARG A 124 ? 0.8272 0.8318 1.2611 -0.1598 0.1148  -0.1478 124  ARG A CG  
776   C  CD  . ARG A 124 ? 0.8501 0.8553 1.2816 -0.1641 0.1366  -0.1290 124  ARG A CD  
777   N  NE  . ARG A 124 ? 0.9140 0.9286 1.3842 -0.1864 0.1579  -0.1365 124  ARG A NE  
778   C  CZ  . ARG A 124 ? 0.9912 1.0446 1.4898 -0.1931 0.1629  -0.1485 124  ARG A CZ  
779   N  NH1 . ARG A 124 ? 1.0177 1.1030 1.5094 -0.1778 0.1478  -0.1542 124  ARG A NH1 
780   N  NH2 . ARG A 124 ? 0.9199 0.9800 1.4551 -0.2153 0.1842  -0.1551 124  ARG A NH2 
781   N  N   . ILE A 125 ? 0.4138 0.3157 0.8091 -0.1600 0.1159  -0.1325 125  ILE A N   
782   C  CA  . ILE A 125 ? 0.5232 0.3805 0.9000 -0.1593 0.1271  -0.1145 125  ILE A CA  
783   C  C   . ILE A 125 ? 0.6593 0.5018 1.0161 -0.1475 0.1094  -0.1201 125  ILE A C   
784   O  O   . ILE A 125 ? 0.7114 0.5614 1.0408 -0.1303 0.0934  -0.1145 125  ILE A O   
785   C  CB  . ILE A 125 ? 0.5574 0.3989 0.9047 -0.1497 0.1392  -0.0834 125  ILE A CB  
786   C  CG1 . ILE A 125 ? 0.6172 0.4584 0.9831 -0.1644 0.1644  -0.0737 125  ILE A CG1 
787   C  CG2 . ILE A 125 ? 0.5760 0.3772 0.8968 -0.1410 0.1423  -0.0658 125  ILE A CG2 
788   C  CD1 . ILE A 125 ? 0.6408 0.5246 1.0331 -0.1722 0.1637  -0.0892 125  ILE A CD1 
789   N  N   . SER A 126 ? 0.8685 0.6891 1.2398 -0.1574 0.1140  -0.1313 126  SER A N   
790   C  CA  . SER A 126 ? 0.8138 0.6223 1.1712 -0.1486 0.0987  -0.1412 126  SER A CA  
791   C  C   . SER A 126 ? 0.6895 0.4790 1.0058 -0.1287 0.0923  -0.1193 126  SER A C   
792   O  O   . SER A 126 ? 0.5046 0.3081 0.8026 -0.1153 0.0732  -0.1244 126  SER A O   
793   C  CB  . SER A 126 ? 0.7609 0.5417 1.1397 -0.1632 0.1101  -0.1533 126  SER A CB  
794   O  OG  . SER A 126 ? 0.7844 0.5708 1.1631 -0.1595 0.0927  -0.1759 126  SER A OG  
795   N  N   . ASP A 127 ? 0.7530 0.5117 1.0554 -0.1265 0.1085  -0.0951 127  ASP A N   
796   C  CA  . ASP A 127 ? 0.8063 0.5514 1.0722 -0.1081 0.1036  -0.0738 127  ASP A CA  
797   C  C   . ASP A 127 ? 0.7140 0.4887 0.9613 -0.0951 0.0860  -0.0733 127  ASP A C   
798   O  O   . ASP A 127 ? 0.7777 0.5532 1.0056 -0.0829 0.0712  -0.0755 127  ASP A O   
799   C  CB  . ASP A 127 ? 0.9768 0.6992 1.2313 -0.1065 0.1233  -0.0460 127  ASP A CB  
800   C  CG  . ASP A 127 ? 1.1040 0.7855 1.3623 -0.1104 0.1387  -0.0388 127  ASP A CG  
801   O  OD1 . ASP A 127 ? 1.0998 0.7670 1.3541 -0.1057 0.1308  -0.0480 127  ASP A OD1 
802   O  OD2 . ASP A 127 ? 1.1889 0.8516 1.4533 -0.1173 0.1597  -0.0231 127  ASP A OD2 
803   N  N   . LEU A 128 ? 0.6610 0.4586 0.9147 -0.0980 0.0891  -0.0703 128  LEU A N   
804   C  CA  . LEU A 128 ? 0.5158 0.3401 0.7548 -0.0866 0.0748  -0.0702 128  LEU A CA  
805   C  C   . LEU A 128 ? 0.5948 0.4396 0.8391 -0.0831 0.0550  -0.0921 128  LEU A C   
806   O  O   . LEU A 128 ? 0.5668 0.4158 0.7890 -0.0696 0.0409  -0.0903 128  LEU A O   
807   C  CB  . LEU A 128 ? 0.5356 0.3813 0.7865 -0.0923 0.0838  -0.0669 128  LEU A CB  
808   C  CG  . LEU A 128 ? 0.5507 0.3816 0.7939 -0.0946 0.1040  -0.0440 128  LEU A CG  
809   C  CD1 . LEU A 128 ? 0.5676 0.4242 0.8250 -0.1012 0.1129  -0.0445 128  LEU A CD1 
810   C  CD2 . LEU A 128 ? 0.4645 0.2834 0.6726 -0.0787 0.1005  -0.0243 128  LEU A CD2 
811   N  N   . GLY A 129 ? 0.5973 0.4557 0.8712 -0.0951 0.0544  -0.1129 129  GLY A N   
812   C  CA  . GLY A 129 ? 0.5658 0.4453 0.8449 -0.0910 0.0355  -0.1346 129  GLY A CA  
813   C  C   . GLY A 129 ? 0.5834 0.4445 0.8378 -0.0800 0.0254  -0.1330 129  GLY A C   
814   O  O   . GLY A 129 ? 0.6553 0.5297 0.8950 -0.0682 0.0088  -0.1389 129  GLY A O   
815   N  N   . GLN A 130 ? 0.3913 0.2210 0.6406 -0.0833 0.0364  -0.1241 130  GLN A N   
816   C  CA  . GLN A 130 ? 0.5396 0.3515 0.7689 -0.0741 0.0290  -0.1243 130  GLN A CA  
817   C  C   . GLN A 130 ? 0.4804 0.2862 0.6779 -0.0590 0.0251  -0.1041 130  GLN A C   
818   O  O   . GLN A 130 ? 0.4760 0.2825 0.6544 -0.0482 0.0132  -0.1060 130  GLN A O   
819   C  CB  . GLN A 130 ? 0.5999 0.3804 0.8379 -0.0823 0.0427  -0.1236 130  GLN A CB  
820   C  CG  . GLN A 130 ? 0.7160 0.4863 0.9467 -0.0777 0.0337  -0.1373 130  GLN A CG  
821   C  CD  . GLN A 130 ? 0.6993 0.4587 0.8978 -0.0611 0.0293  -0.1208 130  GLN A CD  
822   O  OE1 . GLN A 130 ? 0.8437 0.5972 1.0276 -0.0548 0.0356  -0.0987 130  GLN A OE1 
823   N  NE2 . GLN A 130 ? 0.6806 0.4427 0.8683 -0.0537 0.0188  -0.1314 130  GLN A NE2 
824   N  N   . LEU A 131 ? 0.4131 0.2144 0.6053 -0.0588 0.0359  -0.0853 131  LEU A N   
825   C  CA  . LEU A 131 ? 0.4952 0.2959 0.6605 -0.0459 0.0323  -0.0683 131  LEU A CA  
826   C  C   . LEU A 131 ? 0.3929 0.2168 0.5495 -0.0378 0.0165  -0.0758 131  LEU A C   
827   O  O   . LEU A 131 ? 0.3791 0.2004 0.5150 -0.0274 0.0076  -0.0724 131  LEU A O   
828   C  CB  . LEU A 131 ? 0.4414 0.2411 0.6049 -0.0476 0.0453  -0.0506 131  LEU A CB  
829   C  CG  . LEU A 131 ? 0.4988 0.3016 0.6365 -0.0353 0.0417  -0.0352 131  LEU A CG  
830   C  CD1 . LEU A 131 ? 0.4041 0.1861 0.5245 -0.0272 0.0419  -0.0256 131  LEU A CD1 
831   C  CD2 . LEU A 131 ? 0.4293 0.2380 0.5659 -0.0370 0.0532  -0.0214 131  LEU A CD2 
832   N  N   . VAL A 132 ? 0.3868 0.2330 0.5605 -0.0427 0.0140  -0.0860 132  VAL A N   
833   C  CA  . VAL A 132 ? 0.4754 0.3429 0.6424 -0.0339 0.0004  -0.0920 132  VAL A CA  
834   C  C   . VAL A 132 ? 0.6115 0.4828 0.7719 -0.0273 -0.0142 -0.1052 132  VAL A C   
835   O  O   . VAL A 132 ? 0.7144 0.5889 0.8555 -0.0157 -0.0241 -0.1022 132  VAL A O   
836   C  CB  . VAL A 132 ? 0.4455 0.3383 0.6354 -0.0398 0.0016  -0.1012 132  VAL A CB  
837   C  CG1 . VAL A 132 ? 0.5577 0.4710 0.7417 -0.0287 -0.0133 -0.1087 132  VAL A CG1 
838   C  CG2 . VAL A 132 ? 0.3546 0.2467 0.5458 -0.0438 0.0156  -0.0870 132  VAL A CG2 
839   N  N   . ASN A 133 ? 0.5382 0.4090 0.7146 -0.0348 -0.0149 -0.1202 133  ASN A N   
840   C  CA  . ASN A 133 ? 0.4291 0.3050 0.5988 -0.0286 -0.0283 -0.1343 133  ASN A CA  
841   C  C   . ASN A 133 ? 0.4820 0.3387 0.6229 -0.0185 -0.0310 -0.1239 133  ASN A C   
842   O  O   . ASN A 133 ? 0.5599 0.4227 0.6845 -0.0082 -0.0428 -0.1282 133  ASN A O   
843   C  CB  . ASN A 133 ? 0.5896 0.4660 0.7826 -0.0404 -0.0261 -0.1530 133  ASN A CB  
844   C  CG  . ASN A 133 ? 0.5790 0.4853 0.8001 -0.0474 -0.0308 -0.1716 133  ASN A CG  
845   O  OD1 . ASN A 133 ? 0.4803 0.4059 0.7050 -0.0438 -0.0337 -0.1688 133  ASN A OD1 
846   N  ND2 . ASN A 133 ? 0.6790 0.5907 0.9216 -0.0575 -0.0316 -0.1923 133  ASN A ND2 
847   N  N   . SER A 134 ? 0.4075 0.2420 0.5419 -0.0206 -0.0195 -0.1095 134  SER A N   
848   C  CA  . SER A 134 ? 0.4810 0.3050 0.5947 -0.0124 -0.0199 -0.1000 134  SER A CA  
849   C  C   . SER A 134 ? 0.5199 0.3458 0.6131 -0.0040 -0.0191 -0.0807 134  SER A C   
850   O  O   . SER A 134 ? 0.5293 0.3510 0.6055 0.0025  -0.0201 -0.0731 134  SER A O   
851   C  CB  . SER A 134 ? 0.5100 0.3152 0.6318 -0.0186 -0.0080 -0.0971 134  SER A CB  
852   O  OG  . SER A 134 ? 0.4797 0.2769 0.6108 -0.0249 0.0048  -0.0852 134  SER A OG  
853   N  N   . THR A 135 ? 0.5752 0.4084 0.6714 -0.0050 -0.0170 -0.0746 135  THR A N   
854   C  CA  . THR A 135 ? 0.5424 0.3789 0.6218 0.0011  -0.0159 -0.0590 135  THR A CA  
855   C  C   . THR A 135 ? 0.4059 0.2545 0.4832 0.0048  -0.0224 -0.0612 135  THR A C   
856   O  O   . THR A 135 ? 0.5703 0.4246 0.6631 0.0009  -0.0232 -0.0708 135  THR A O   
857   C  CB  . THR A 135 ? 0.6262 0.4554 0.7079 -0.0027 -0.0036 -0.0462 135  THR A CB  
858   O  OG1 . THR A 135 ? 0.4629 0.2771 0.5545 -0.0081 0.0049  -0.0466 135  THR A OG1 
859   C  CG2 . THR A 135 ? 0.5343 0.3655 0.5966 0.0041  -0.0032 -0.0328 135  THR A CG2 
860   N  N   . ASP A 136 ? 0.4745 0.3265 0.5339 0.0118  -0.0263 -0.0532 136  ASP A N   
861   C  CA  . ASP A 136 ? 0.4705 0.3304 0.5261 0.0164  -0.0313 -0.0538 136  ASP A CA  
862   C  C   . ASP A 136 ? 0.5019 0.3641 0.5549 0.0147  -0.0241 -0.0439 136  ASP A C   
863   O  O   . ASP A 136 ? 0.3787 0.2398 0.4186 0.0161  -0.0219 -0.0349 136  ASP A O   
864   C  CB  . ASP A 136 ? 0.6680 0.5267 0.7054 0.0242  -0.0388 -0.0520 136  ASP A CB  
865   C  CG  . ASP A 136 ? 0.8372 0.6989 0.8750 0.0312  -0.0476 -0.0609 136  ASP A CG  
866   O  OD1 . ASP A 136 ? 0.7868 0.6506 0.8347 0.0320  -0.0529 -0.0741 136  ASP A OD1 
867   O  OD2 . ASP A 136 ? 1.0433 0.9049 1.0710 0.0364  -0.0493 -0.0561 136  ASP A OD2 
868   N  N   . ILE A 137 ? 0.2991 0.1649 0.3648 0.0116  -0.0204 -0.0475 137  ILE A N   
869   C  CA  . ILE A 137 ? 0.1859 0.0512 0.2498 0.0095  -0.0122 -0.0395 137  ILE A CA  
870   C  C   . ILE A 137 ? 0.3955 0.2680 0.4565 0.0136  -0.0142 -0.0417 137  ILE A C   
871   O  O   . ILE A 137 ? 0.4031 0.2859 0.4740 0.0151  -0.0179 -0.0501 137  ILE A O   
872   C  CB  . ILE A 137 ? 0.3185 0.1835 0.3975 0.0017  -0.0027 -0.0388 137  ILE A CB  
873   C  CG1 . ILE A 137 ? 0.3531 0.2029 0.4343 -0.0019 0.0012  -0.0364 137  ILE A CG1 
874   C  CG2 . ILE A 137 ? 0.3666 0.2374 0.4412 0.0012  0.0057  -0.0292 137  ILE A CG2 
875   C  CD1 . ILE A 137 ? 0.2684 0.1179 0.3691 -0.0116 0.0109  -0.0381 137  ILE A CD1 
876   N  N   . TYR A 138 ? 0.4603 0.3330 0.5089 0.0153  -0.0119 -0.0344 138  TYR A N   
877   C  CA  . TYR A 138 ? 0.3536 0.2320 0.3992 0.0185  -0.0123 -0.0373 138  TYR A CA  
878   C  C   . TYR A 138 ? 0.4085 0.2965 0.4525 0.0159  -0.0043 -0.0318 138  TYR A C   
879   O  O   . TYR A 138 ? 0.3195 0.2046 0.3548 0.0154  -0.0008 -0.0236 138  TYR A O   
880   C  CB  . TYR A 138 ? 0.4201 0.2977 0.4523 0.0218  -0.0174 -0.0352 138  TYR A CB  
881   C  CG  . TYR A 138 ? 0.4225 0.2979 0.4519 0.0252  -0.0249 -0.0375 138  TYR A CG  
882   C  CD1 . TYR A 138 ? 0.3424 0.2141 0.3681 0.0244  -0.0271 -0.0348 138  TYR A CD1 
883   C  CD2 . TYR A 138 ? 0.3800 0.2549 0.4089 0.0308  -0.0297 -0.0425 138  TYR A CD2 
884   C  CE1 . TYR A 138 ? 0.4171 0.2847 0.4371 0.0290  -0.0339 -0.0374 138  TYR A CE1 
885   C  CE2 . TYR A 138 ? 0.3223 0.1918 0.3453 0.0361  -0.0365 -0.0437 138  TYR A CE2 
886   C  CZ  . TYR A 138 ? 0.4383 0.3042 0.4560 0.0352  -0.0387 -0.0413 138  TYR A CZ  
887   O  OH  . TYR A 138 ? 0.5368 0.3956 0.5458 0.0420  -0.0454 -0.0430 138  TYR A OH  
888   N  N   . LEU A 139 ? 0.4587 0.3600 0.5105 0.0157  -0.0016 -0.0367 139  LEU A N   
889   C  CA  . LEU A 139 ? 0.4290 0.3424 0.4783 0.0140  0.0066  -0.0324 139  LEU A CA  
890   C  C   . LEU A 139 ? 0.4891 0.4111 0.5328 0.0178  0.0051  -0.0389 139  LEU A C   
891   O  O   . LEU A 139 ? 0.4056 0.3315 0.4567 0.0205  0.0021  -0.0481 139  LEU A O   
892   C  CB  . LEU A 139 ? 0.2571 0.1806 0.3209 0.0092  0.0144  -0.0323 139  LEU A CB  
893   C  CG  . LEU A 139 ? 0.3665 0.2810 0.4405 0.0036  0.0172  -0.0291 139  LEU A CG  
894   C  CD1 . LEU A 139 ? 0.2479 0.1740 0.3388 -0.0030 0.0271  -0.0300 139  LEU A CD1 
895   C  CD2 . LEU A 139 ? 0.3292 0.2302 0.3911 0.0037  0.0203  -0.0171 139  LEU A CD2 
896   N  N   . VAL A 140 ? 0.5011 0.4266 0.5322 0.0185  0.0069  -0.0351 140  VAL A N   
897   C  CA  . VAL A 140 ? 0.4796 0.4140 0.5052 0.0208  0.0062  -0.0428 140  VAL A CA  
898   C  C   . VAL A 140 ? 0.5296 0.4823 0.5491 0.0206  0.0137  -0.0393 140  VAL A C   
899   O  O   . VAL A 140 ? 0.5837 0.5417 0.5914 0.0215  0.0142  -0.0342 140  VAL A O   
900   C  CB  . VAL A 140 ? 0.4855 0.4112 0.5018 0.0215  0.0010  -0.0445 140  VAL A CB  
901   C  CG1 . VAL A 140 ? 0.2477 0.1792 0.2618 0.0226  0.0002  -0.0560 140  VAL A CG1 
902   C  CG2 . VAL A 140 ? 0.5558 0.4624 0.5743 0.0220  -0.0047 -0.0440 140  VAL A CG2 
903   N  N   . PRO A 141 ? 0.4938 0.4584 0.5211 0.0201  0.0197  -0.0419 141  PRO A N   
904   C  CA  . PRO A 141 ? 0.5529 0.5359 0.5732 0.0206  0.0284  -0.0382 141  PRO A CA  
905   C  C   . PRO A 141 ? 0.5101 0.5052 0.5162 0.0239  0.0264  -0.0440 141  PRO A C   
906   O  O   . PRO A 141 ? 0.5482 0.5558 0.5414 0.0258  0.0306  -0.0366 141  PRO A O   
907   C  CB  . PRO A 141 ? 0.4142 0.4079 0.4484 0.0199  0.0335  -0.0457 141  PRO A CB  
908   C  CG  . PRO A 141 ? 0.4635 0.4447 0.5134 0.0178  0.0290  -0.0476 141  PRO A CG  
909   C  CD  . PRO A 141 ? 0.5663 0.5295 0.6100 0.0198  0.0188  -0.0487 141  PRO A CD  
910   N  N   . THR A 142 ? 0.4959 0.4875 0.5044 0.0250  0.0203  -0.0576 142  THR A N   
911   C  CA  . THR A 142 ? 0.5241 0.5261 0.5222 0.0264  0.0178  -0.0664 142  THR A CA  
912   C  C   . THR A 142 ? 0.5785 0.5644 0.5787 0.0249  0.0103  -0.0743 142  THR A C   
913   O  O   . THR A 142 ? 0.4934 0.4611 0.5026 0.0248  0.0073  -0.0768 142  THR A O   
914   C  CB  . THR A 142 ? 0.4553 0.4745 0.4531 0.0287  0.0220  -0.0792 142  THR A CB  
915   O  OG1 . THR A 142 ? 0.5663 0.5959 0.5544 0.0291  0.0189  -0.0898 142  THR A OG1 
916   C  CG2 . THR A 142 ? 0.4261 0.4345 0.4381 0.0299  0.0206  -0.0902 142  THR A CG2 
917   N  N   . MET A 143 ? 0.6761 0.6706 0.6676 0.0239  0.0077  -0.0782 143  MET A N   
918   C  CA  . MET A 143 ? 0.5370 0.5191 0.5306 0.0206  0.0025  -0.0859 143  MET A CA  
919   C  C   . MET A 143 ? 0.5789 0.5759 0.5700 0.0194  0.0024  -0.1030 143  MET A C   
920   O  O   . MET A 143 ? 0.4914 0.4808 0.4858 0.0151  -0.0003 -0.1133 143  MET A O   
921   C  CB  . MET A 143 ? 0.4024 0.3841 0.3911 0.0194  -0.0004 -0.0753 143  MET A CB  
922   C  CG  . MET A 143 ? 0.4972 0.4655 0.4896 0.0151  -0.0042 -0.0804 143  MET A CG  
923   S  SD  . MET A 143 ? 0.5246 0.5027 0.5115 0.0151  -0.0070 -0.0705 143  MET A SD  
924   C  CE  . MET A 143 ? 0.3667 0.3463 0.3593 0.0078  -0.0095 -0.0865 143  MET A CE  
925   N  N   . ASN A 144 ? 0.4309 0.4492 0.4163 0.0227  0.0061  -0.1066 144  ASN A N   
926   C  CA  . ASN A 144 ? 0.4380 0.4738 0.4201 0.0222  0.0062  -0.1246 144  ASN A CA  
927   C  C   . ASN A 144 ? 0.5990 0.6470 0.5804 0.0265  0.0120  -0.1312 144  ASN A C   
928   O  O   . ASN A 144 ? 0.4790 0.5527 0.4489 0.0299  0.0152  -0.1304 144  ASN A O   
929   C  CB  . ASN A 144 ? 0.4411 0.5027 0.4113 0.0226  0.0033  -0.1242 144  ASN A CB  
930   C  CG  . ASN A 144 ? 0.5737 0.6554 0.5413 0.0211  0.0019  -0.1462 144  ASN A CG  
931   O  OD1 . ASN A 144 ? 0.6234 0.6950 0.5994 0.0187  0.0036  -0.1623 144  ASN A OD1 
932   N  ND2 . ASN A 144 ? 0.5854 0.6964 0.5415 0.0233  -0.0014 -0.1477 144  ASN A ND2 
933   N  N   . PRO A 145 ? 0.5423 0.5725 0.5354 0.0274  0.0137  -0.1377 145  PRO A N   
934   C  CA  . PRO A 145 ? 0.4279 0.4686 0.4241 0.0320  0.0195  -0.1458 145  PRO A CA  
935   C  C   . PRO A 145 ? 0.4673 0.5281 0.4569 0.0327  0.0209  -0.1652 145  PRO A C   
936   O  O   . PRO A 145 ? 0.5822 0.6660 0.5652 0.0366  0.0265  -0.1684 145  PRO A O   
937   C  CB  . PRO A 145 ? 0.3692 0.3837 0.3802 0.0339  0.0184  -0.1509 145  PRO A CB  
938   C  CG  . PRO A 145 ? 0.4070 0.3973 0.4203 0.0303  0.0129  -0.1414 145  PRO A CG  
939   C  CD  . PRO A 145 ? 0.3608 0.3607 0.3643 0.0251  0.0101  -0.1389 145  PRO A CD  
940   N  N   . ASP A 146 ? 0.4126 0.4646 0.4045 0.0282  0.0166  -0.1790 146  ASP A N   
941   C  CA  . ASP A 146 ? 0.4790 0.5476 0.4674 0.0274  0.0173  -0.2015 146  ASP A CA  
942   C  C   . ASP A 146 ? 0.4817 0.5856 0.4532 0.0287  0.0163  -0.1987 146  ASP A C   
943   O  O   . ASP A 146 ? 0.6183 0.7477 0.5809 0.0322  0.0192  -0.2111 146  ASP A O   
944   C  CB  . ASP A 146 ? 0.5361 0.5852 0.5335 0.0202  0.0137  -0.2165 146  ASP A CB  
945   C  CG  . ASP A 146 ? 0.5080 0.5209 0.5195 0.0213  0.0160  -0.2200 146  ASP A CG  
946   O  OD1 . ASP A 146 ? 0.4502 0.4541 0.4655 0.0279  0.0182  -0.2090 146  ASP A OD1 
947   O  OD2 . ASP A 146 ? 0.4446 0.4382 0.4638 0.0159  0.0161  -0.2337 146  ASP A OD2 
948   N  N   . GLY A 147 ? 0.3714 0.4769 0.3374 0.0271  0.0122  -0.1821 147  GLY A N   
949   C  CA  . GLY A 147 ? 0.4258 0.5631 0.3744 0.0307  0.0105  -0.1759 147  GLY A CA  
950   C  C   . GLY A 147 ? 0.4080 0.5605 0.3452 0.0380  0.0181  -0.1631 147  GLY A C   
951   O  O   . GLY A 147 ? 0.5025 0.6853 0.4237 0.0431  0.0201  -0.1674 147  GLY A O   
952   N  N   . TYR A 148 ? 0.3956 0.5278 0.3415 0.0382  0.0229  -0.1482 148  TYR A N   
953   C  CA  . TYR A 148 ? 0.5869 0.7299 0.5265 0.0429  0.0322  -0.1350 148  TYR A CA  
954   C  C   . TYR A 148 ? 0.6374 0.7985 0.5749 0.0462  0.0383  -0.1519 148  TYR A C   
955   O  O   . TYR A 148 ? 0.4611 0.6497 0.3817 0.0512  0.0437  -0.1503 148  TYR A O   
956   C  CB  . TYR A 148 ? 0.5293 0.6470 0.4841 0.0405  0.0351  -0.1213 148  TYR A CB  
957   C  CG  . TYR A 148 ? 0.5399 0.6671 0.4946 0.0429  0.0462  -0.1106 148  TYR A CG  
958   C  CD1 . TYR A 148 ? 0.5816 0.7209 0.5218 0.0452  0.0527  -0.0916 148  TYR A CD1 
959   C  CD2 . TYR A 148 ? 0.4627 0.5865 0.4327 0.0431  0.0510  -0.1189 148  TYR A CD2 
960   C  CE1 . TYR A 148 ? 0.3807 0.5274 0.3222 0.0457  0.0650  -0.0812 148  TYR A CE1 
961   C  CE2 . TYR A 148 ? 0.4512 0.5861 0.4242 0.0439  0.0622  -0.1100 148  TYR A CE2 
962   C  CZ  . TYR A 148 ? 0.5104 0.6560 0.4692 0.0442  0.0698  -0.0912 148  TYR A CZ  
963   O  OH  . TYR A 148 ? 0.7614 0.9167 0.7242 0.0434  0.0830  -0.0820 148  TYR A OH  
964   N  N   . ALA A 149 ? 0.6299 0.7752 0.5838 0.0446  0.0379  -0.1677 149  ALA A N   
965   C  CA  . ALA A 149 ? 0.5237 0.6832 0.4786 0.0484  0.0434  -0.1869 149  ALA A CA  
966   C  C   . ALA A 149 ? 0.3524 0.5434 0.2886 0.0510  0.0430  -0.2011 149  ALA A C   
967   O  O   . ALA A 149 ? 0.4728 0.6855 0.4020 0.0559  0.0502  -0.2102 149  ALA A O   
968   C  CB  . ALA A 149 ? 0.2740 0.4084 0.2475 0.0470  0.0404  -0.2044 149  ALA A CB  
969   N  N   . LEU A 150 ? 0.4366 0.6327 0.3653 0.0481  0.0345  -0.2043 150  LEU A N   
970   C  CA  . LEU A 150 ? 0.6250 0.8544 0.5366 0.0507  0.0320  -0.2203 150  LEU A CA  
971   C  C   . LEU A 150 ? 0.7052 0.9634 0.5923 0.0577  0.0341  -0.2013 150  LEU A C   
972   O  O   . LEU A 150 ? 0.7602 1.0515 0.6289 0.0626  0.0324  -0.2120 150  LEU A O   
973   C  CB  . LEU A 150 ? 0.5519 0.7773 0.4702 0.0439  0.0217  -0.2380 150  LEU A CB  
974   C  CG  . LEU A 150 ? 0.5942 0.7941 0.5329 0.0380  0.0216  -0.2611 150  LEU A CG  
975   C  CD1 . LEU A 150 ? 0.5190 0.6985 0.4702 0.0287  0.0142  -0.2660 150  LEU A CD1 
976   C  CD2 . LEU A 150 ? 0.5470 0.7686 0.4812 0.0400  0.0239  -0.2902 150  LEU A CD2 
977   N  N   . SER A 151 ? 0.6684 0.9137 0.5548 0.0587  0.0382  -0.1735 151  SER A N   
978   C  CA  . SER A 151 ? 0.6055 0.8710 0.4690 0.0660  0.0420  -0.1513 151  SER A CA  
979   C  C   . SER A 151 ? 0.6842 0.9646 0.5361 0.0716  0.0563  -0.1422 151  SER A C   
980   O  O   . SER A 151 ? 0.7261 0.9965 0.5929 0.0689  0.0636  -0.1481 151  SER A O   
981   C  CB  . SER A 151 ? 0.5210 0.7633 0.3893 0.0640  0.0399  -0.1261 151  SER A CB  
982   O  OG  . SER A 151 ? 0.4208 0.6549 0.2970 0.0597  0.0278  -0.1336 151  SER A OG  
983   N  N   . GLN A 152 ? 0.6037 0.9089 0.4291 0.0802  0.0607  -0.1273 152  GLN A N   
984   C  CA  . GLN A 152 ? 0.5151 0.8373 0.3260 0.0857  0.0759  -0.1176 152  GLN A CA  
985   C  C   . GLN A 152 ? 0.5696 0.8814 0.3723 0.0879  0.0867  -0.0837 152  GLN A C   
986   O  O   . GLN A 152 ? 0.6446 0.9649 0.4260 0.0953  0.0849  -0.0662 152  GLN A O   
987   C  CB  . GLN A 152 ? 0.8715 1.2347 0.6537 0.0955  0.0753  -0.1295 152  GLN A CB  
988   C  CG  . GLN A 152 ? 0.9329 1.3165 0.6949 0.1026  0.0924  -0.1173 152  GLN A CG  
989   C  CD  . GLN A 152 ? 0.9382 1.3644 0.6680 0.1139  0.0910  -0.1283 152  GLN A CD  
990   O  OE1 . GLN A 152 ? 1.1122 1.5586 0.8176 0.1222  0.1042  -0.1144 152  GLN A OE1 
991   N  NE2 . GLN A 152 ? 0.8804 1.3213 0.6098 0.1141  0.0754  -0.1539 152  GLN A NE2 
992   N  N   . GLU A 153 ? 0.5604 0.8543 0.3808 0.0819  0.0984  -0.0751 153  GLU A N   
993   C  CA  . GLU A 153 ? 0.6126 0.8943 0.4289 0.0816  0.1113  -0.0449 153  GLU A CA  
994   C  C   . GLU A 153 ? 0.6895 0.9968 0.4704 0.0930  0.1204  -0.0284 153  GLU A C   
995   O  O   . GLU A 153 ? 0.7212 1.0574 0.4862 0.0986  0.1261  -0.0392 153  GLU A O   
996   C  CB  . GLU A 153 ? 0.5334 0.8045 0.3726 0.0737  0.1249  -0.0437 153  GLU A CB  
997   C  CG  . GLU A 153 ? 0.6388 0.8960 0.4778 0.0709  0.1401  -0.0145 153  GLU A CG  
998   C  CD  . GLU A 153 ? 0.6956 0.9482 0.5600 0.0621  0.1538  -0.0161 153  GLU A CD  
999   O  OE1 . GLU A 153 ? 0.7124 0.9612 0.5750 0.0592  0.1710  0.0049  153  GLU A OE1 
1000  O  OE2 . GLU A 153 ? 0.6041 0.8570 0.4908 0.0583  0.1479  -0.0385 153  GLU A OE2 
1001  N  N   . GLY A 154 ? 0.7050 1.0015 0.4726 0.0975  0.1221  -0.0019 154  GLY A N   
1002  C  CA  . GLY A 154 ? 0.5961 0.9133 0.3277 0.1105  0.1310  0.0183  154  GLY A CA  
1003  C  C   . GLY A 154 ? 0.6720 1.0035 0.3822 0.1220  0.1153  0.0196  154  GLY A C   
1004  O  O   . GLY A 154 ? 0.7990 1.1369 0.4824 0.1340  0.1199  0.0436  154  GLY A O   
1005  N  N   . ASN A 155 ? 0.6198 0.9564 0.3430 0.1185  0.0971  -0.0062 155  ASN A N   
1006  C  CA  . ASN A 155 ? 0.6420 0.9967 0.3501 0.1279  0.0810  -0.0096 155  ASN A CA  
1007  C  C   . ASN A 155 ? 0.7876 1.1182 0.4992 0.1302  0.0763  0.0130  155  ASN A C   
1008  O  O   . ASN A 155 ? 0.8547 1.1616 0.5923 0.1206  0.0673  0.0057  155  ASN A O   
1009  C  CB  . ASN A 155 ? 0.6117 0.9780 0.3359 0.1213  0.0648  -0.0452 155  ASN A CB  
1010  C  CG  . ASN A 155 ? 0.7152 1.1236 0.4188 0.1285  0.0623  -0.0671 155  ASN A CG  
1011  O  OD1 . ASN A 155 ? 0.6727 1.0880 0.3903 0.1213  0.0568  -0.0975 155  ASN A OD1 
1012  N  ND2 . ASN A 155 ? 0.9310 1.3673 0.5997 0.1436  0.0668  -0.0514 155  ASN A ND2 
1013  N  N   . CYS A 156 ? 0.7071 1.0433 0.3916 0.1440  0.0829  0.0407  156  CYS A N   
1014  C  CA  . CYS A 156 ? 0.7908 1.1074 0.4757 0.1493  0.0782  0.0615  156  CYS A CA  
1015  C  C   . CYS A 156 ? 0.7652 1.1004 0.4550 0.1520  0.0567  0.0420  156  CYS A C   
1016  O  O   . CYS A 156 ? 0.8326 1.1463 0.5415 0.1473  0.0489  0.0436  156  CYS A O   
1017  C  CB  . CYS A 156 ? 0.8634 1.1853 0.5147 0.1667  0.0894  0.0945  156  CYS A CB  
1018  S  SG  . CYS A 156 ? 0.7832 1.0713 0.4356 0.1605  0.1174  0.1232  156  CYS A SG  
1019  N  N   . GLU A 157 ? 0.7433 1.1203 0.4167 0.1590  0.0477  0.0222  157  GLU A N   
1020  C  CA  . GLU A 157 ? 0.7506 1.1506 0.4318 0.1590  0.0279  -0.0019 157  GLU A CA  
1021  C  C   . GLU A 157 ? 0.6972 1.0971 0.4037 0.1425  0.0221  -0.0372 157  GLU A C   
1022  O  O   . GLU A 157 ? 0.7651 1.1684 0.4710 0.1378  0.0305  -0.0482 157  GLU A O   
1023  C  CB  . GLU A 157 ? 0.8385 1.2880 0.4871 0.1776  0.0197  -0.0041 157  GLU A CB  
1024  C  CG  . GLU A 157 ? 1.0544 1.5060 0.6789 0.1969  0.0209  0.0291  157  GLU A CG  
1025  C  CD  . GLU A 157 ? 1.2349 1.6935 0.8240 0.2112  0.0371  0.0551  157  GLU A CD  
1026  O  OE1 . GLU A 157 ? 1.2917 1.7941 0.8510 0.2254  0.0330  0.0490  157  GLU A OE1 
1027  O  OE2 . GLU A 157 ? 1.2138 1.6348 0.8049 0.2080  0.0544  0.0812  157  GLU A OE2 
1028  N  N   . SER A 158 ? 0.6895 1.0850 0.4185 0.1343  0.0088  -0.0543 158  SER A N   
1029  C  CA  . SER A 158 ? 0.5898 0.9800 0.3437 0.1188  0.0037  -0.0862 158  SER A CA  
1030  C  C   . SER A 158 ? 0.5108 0.9410 0.2516 0.1217  -0.0001 -0.1133 158  SER A C   
1031  O  O   . SER A 158 ? 0.6228 1.0887 0.3346 0.1363  -0.0012 -0.1081 158  SER A O   
1032  C  CB  . SER A 158 ? 0.6388 1.0193 0.4162 0.1105  -0.0088 -0.0972 158  SER A CB  
1033  O  OG  . SER A 158 ? 0.8202 1.1879 0.6222 0.0952  -0.0114 -0.1248 158  SER A OG  
1034  N  N   . LEU A 159 ? 0.4214 0.8452 0.1828 0.1087  -0.0020 -0.1424 159  LEU A N   
1035  C  CA  . LEU A 159 ? 0.3980 0.8541 0.1504 0.1095  -0.0036 -0.1713 159  LEU A CA  
1036  C  C   . LEU A 159 ? 0.8621 1.3499 0.6190 0.1076  -0.0193 -0.1997 159  LEU A C   
1037  O  O   . LEU A 159 ? 0.7856 1.2678 0.5565 0.1038  -0.0283 -0.1979 159  LEU A O   
1038  C  CB  . LEU A 159 ? 1.2318 1.6618 1.0057 0.0971  0.0039  -0.1890 159  LEU A CB  
1039  C  CG  . LEU A 159 ? 1.1687 1.5788 0.9407 0.0978  0.0201  -0.1734 159  LEU A CG  
1040  C  CD1 . LEU A 159 ? 1.0990 1.4811 0.8991 0.0855  0.0231  -0.1934 159  LEU A CD1 
1041  C  CD2 . LEU A 159 ? 1.0586 1.5035 0.8001 0.1099  0.0284  -0.1713 159  LEU A CD2 
1042  N  N   . PRO A 160 ? 0.9906 1.5137 0.7369 0.1096  -0.0222 -0.2277 160  PRO A N   
1043  C  CA  . PRO A 160 ? 0.9068 1.4610 0.6620 0.1047  -0.0365 -0.2615 160  PRO A CA  
1044  C  C   . PRO A 160 ? 0.8677 1.3890 0.6606 0.0860  -0.0404 -0.2773 160  PRO A C   
1045  O  O   . PRO A 160 ? 0.9830 1.4626 0.7942 0.0760  -0.0317 -0.2768 160  PRO A O   
1046  C  CB  . PRO A 160 ? 0.5045 1.0843 0.2491 0.1055  -0.0336 -0.2903 160  PRO A CB  
1047  C  CG  . PRO A 160 ? 0.5579 1.1446 0.2715 0.1202  -0.0217 -0.2640 160  PRO A CG  
1048  C  CD  . PRO A 160 ? 0.7732 1.3134 0.4964 0.1178  -0.0117 -0.2288 160  PRO A CD  
1049  N  N   . ASN A 161 ? 0.7751 1.3162 0.5792 0.0821  -0.0530 -0.2909 161  ASN A N   
1050  C  CA  . ASN A 161 ? 0.8245 1.3358 0.6634 0.0642  -0.0556 -0.3043 161  ASN A CA  
1051  C  C   . ASN A 161 ? 0.6440 1.1107 0.4945 0.0615  -0.0507 -0.2730 161  ASN A C   
1052  O  O   . ASN A 161 ? 0.4746 0.9157 0.3511 0.0483  -0.0521 -0.2792 161  ASN A O   
1053  C  CB  . ASN A 161 ? 0.8490 1.3380 0.7066 0.0502  -0.0496 -0.3331 161  ASN A CB  
1054  C  CG  . ASN A 161 ? 0.9950 1.5266 0.8454 0.0505  -0.0548 -0.3695 161  ASN A CG  
1055  O  OD1 . ASN A 161 ? 1.1012 1.6288 0.9470 0.0505  -0.0476 -0.3837 161  ASN A OD1 
1056  N  ND2 . ASN A 161 ? 1.0552 1.6301 0.9052 0.0512  -0.0676 -0.3861 161  ASN A ND2 
1057  N  N   . TYR A 162 ? 0.6807 1.1389 0.5115 0.0740  -0.0444 -0.2398 162  TYR A N   
1058  C  CA  . TYR A 162 ? 0.9185 1.3308 0.7595 0.0711  -0.0374 -0.2121 162  TYR A CA  
1059  C  C   . TYR A 162 ? 0.9644 1.3367 0.8249 0.0585  -0.0290 -0.2215 162  TYR A C   
1060  O  O   . TYR A 162 ? 0.8825 1.2175 0.7633 0.0493  -0.0273 -0.2149 162  TYR A O   
1061  C  CB  . TYR A 162 ? 0.8130 1.2189 0.6689 0.0676  -0.0449 -0.2049 162  TYR A CB  
1062  C  CG  . TYR A 162 ? 0.7556 1.1896 0.5909 0.0839  -0.0503 -0.1838 162  TYR A CG  
1063  C  CD1 . TYR A 162 ? 0.5545 1.0355 0.3850 0.0897  -0.0627 -0.1990 162  TYR A CD1 
1064  C  CD2 . TYR A 162 ? 0.9655 1.3798 0.7866 0.0943  -0.0429 -0.1493 162  TYR A CD2 
1065  C  CE1 . TYR A 162 ? 0.5912 1.0989 0.4018 0.1075  -0.0681 -0.1787 162  TYR A CE1 
1066  C  CE2 . TYR A 162 ? 1.0235 1.4602 0.8248 0.1111  -0.0468 -0.1285 162  TYR A CE2 
1067  C  CZ  . TYR A 162 ? 0.7629 1.2466 0.5582 0.1187  -0.0598 -0.1425 162  TYR A CZ  
1068  O  OH  . TYR A 162 ? 0.8390 1.3455 0.6138 0.1380  -0.0642 -0.1209 162  TYR A OH  
1069  N  N   . VAL A 163 ? 0.6991 1.0811 0.5524 0.0596  -0.0239 -0.2370 163  VAL A N   
1070  C  CA  . VAL A 163 ? 0.7105 1.0579 0.5795 0.0515  -0.0153 -0.2444 163  VAL A CA  
1071  C  C   . VAL A 163 ? 0.6632 0.9819 0.5297 0.0556  -0.0056 -0.2137 163  VAL A C   
1072  O  O   . VAL A 163 ? 0.5773 0.9101 0.4231 0.0662  -0.0008 -0.1930 163  VAL A O   
1073  C  CB  . VAL A 163 ? 0.5727 0.9398 0.4352 0.0527  -0.0119 -0.2705 163  VAL A CB  
1074  C  CG1 . VAL A 163 ? 0.4482 0.7829 0.3210 0.0504  -0.0008 -0.2687 163  VAL A CG1 
1075  C  CG2 . VAL A 163 ? 0.4441 0.8253 0.3202 0.0431  -0.0199 -0.3067 163  VAL A CG2 
1076  N  N   . GLY A 164 ? 0.5701 0.8484 0.4581 0.0469  -0.0025 -0.2110 164  GLY A N   
1077  C  CA  . GLY A 164 ? 0.5567 0.8070 0.4476 0.0486  0.0051  -0.1852 164  GLY A CA  
1078  C  C   . GLY A 164 ? 0.4641 0.6961 0.3605 0.0470  0.0011  -0.1647 164  GLY A C   
1079  O  O   . GLY A 164 ? 0.4545 0.6544 0.3631 0.0434  0.0045  -0.1518 164  GLY A O   
1080  N  N   . ARG A 165 ? 0.5555 0.8106 0.4428 0.0505  -0.0066 -0.1627 165  ARG A N   
1081  C  CA  . ARG A 165 ? 0.4981 0.7397 0.3905 0.0501  -0.0107 -0.1451 165  ARG A CA  
1082  C  C   . ARG A 165 ? 0.4707 0.6851 0.3868 0.0379  -0.0140 -0.1570 165  ARG A C   
1083  O  O   . ARG A 165 ? 0.6206 0.8034 0.5467 0.0347  -0.0115 -0.1429 165  ARG A O   
1084  C  CB  . ARG A 165 ? 0.5174 0.7950 0.3951 0.0587  -0.0186 -0.1424 165  ARG A CB  
1085  C  CG  . ARG A 165 ? 0.5230 0.7898 0.4064 0.0598  -0.0230 -0.1257 165  ARG A CG  
1086  C  CD  . ARG A 165 ? 0.4411 0.7468 0.3098 0.0710  -0.0313 -0.1226 165  ARG A CD  
1087  N  NE  . ARG A 165 ? 0.2931 0.5947 0.1747 0.0689  -0.0378 -0.1189 165  ARG A NE  
1088  C  CZ  . ARG A 165 ? 0.3739 0.6635 0.2512 0.0769  -0.0366 -0.0939 165  ARG A CZ  
1089  N  NH1 . ARG A 165 ? 0.3885 0.6670 0.2494 0.0865  -0.0286 -0.0699 165  ARG A NH1 
1090  N  NH2 . ARG A 165 ? 0.4747 0.7632 0.3650 0.0750  -0.0424 -0.0933 165  ARG A NH2 
1091  N  N   . GLY A 166 ? 0.4156 0.6421 0.3404 0.0308  -0.0189 -0.1832 166  GLY A N   
1092  C  CA  . GLY A 166 ? 0.3497 0.5496 0.2963 0.0186  -0.0201 -0.1947 166  GLY A CA  
1093  C  C   . GLY A 166 ? 0.4078 0.5776 0.3636 0.0145  -0.0132 -0.2018 166  GLY A C   
1094  O  O   . GLY A 166 ? 0.5065 0.6801 0.4534 0.0208  -0.0081 -0.1987 166  GLY A O   
1095  N  N   . ASN A 167 ? 0.4661 0.6063 0.4397 0.0049  -0.0123 -0.2104 167  ASN A N   
1096  C  CA  . ASN A 167 ? 0.4046 0.5144 0.3870 0.0032  -0.0062 -0.2161 167  ASN A CA  
1097  C  C   . ASN A 167 ? 0.5167 0.6393 0.5006 0.0015  -0.0045 -0.2434 167  ASN A C   
1098  O  O   . ASN A 167 ? 0.5593 0.7186 0.5327 0.0041  -0.0075 -0.2547 167  ASN A O   
1099  C  CB  . ASN A 167 ? 0.3866 0.4568 0.3843 -0.0040 -0.0046 -0.2123 167  ASN A CB  
1100  C  CG  . ASN A 167 ? 0.4739 0.5410 0.4843 -0.0156 -0.0058 -0.2321 167  ASN A CG  
1101  O  OD1 . ASN A 167 ? 0.4885 0.5843 0.4989 -0.0191 -0.0087 -0.2519 167  ASN A OD1 
1102  N  ND2 . ASN A 167 ? 0.4019 0.4347 0.4235 -0.0218 -0.0030 -0.2271 167  ASN A ND2 
1103  N  N   . ALA A 168 ? 0.5525 0.6454 0.5485 -0.0017 0.0004  -0.2541 168  ALA A N   
1104  C  CA  . ALA A 168 ? 0.6071 0.7077 0.6055 -0.0024 0.0033  -0.2806 168  ALA A CA  
1105  C  C   . ALA A 168 ? 0.7816 0.8951 0.7882 -0.0131 0.0000  -0.3062 168  ALA A C   
1106  O  O   . ALA A 168 ? 0.8393 0.9722 0.8448 -0.0139 0.0005  -0.3309 168  ALA A O   
1107  C  CB  . ALA A 168 ? 0.5877 0.6509 0.5973 -0.0007 0.0099  -0.2838 168  ALA A CB  
1108  N  N   . ALA A 169 ? 0.7864 0.8905 0.8023 -0.0219 -0.0028 -0.3016 169  ALA A N   
1109  C  CA  . ALA A 169 ? 0.5845 0.7044 0.6115 -0.0339 -0.0058 -0.3259 169  ALA A CA  
1110  C  C   . ALA A 169 ? 0.5807 0.7498 0.5964 -0.0308 -0.0148 -0.3247 169  ALA A C   
1111  O  O   . ALA A 169 ? 0.5149 0.7068 0.5398 -0.0398 -0.0194 -0.3435 169  ALA A O   
1112  C  CB  . ALA A 169 ? 0.3653 0.4502 0.4102 -0.0457 -0.0024 -0.3231 169  ALA A CB  
1113  N  N   . ASN A 170 ? 0.5205 0.7062 0.5169 -0.0177 -0.0169 -0.3026 170  ASN A N   
1114  C  CA  . ASN A 170 ? 0.5207 0.7510 0.5022 -0.0106 -0.0248 -0.2969 170  ASN A CA  
1115  C  C   . ASN A 170 ? 0.5076 0.7430 0.4967 -0.0148 -0.0303 -0.2871 170  ASN A C   
1116  O  O   . ASN A 170 ? 0.6179 0.8940 0.6018 -0.0121 -0.0382 -0.2932 170  ASN A O   
1117  C  CB  . ASN A 170 ? 0.7926 1.0652 0.7688 -0.0108 -0.0295 -0.3261 170  ASN A CB  
1118  C  CG  . ASN A 170 ? 0.8820 1.1742 0.8363 0.0020  -0.0271 -0.3237 170  ASN A CG  
1119  O  OD1 . ASN A 170 ? 0.9525 1.2458 0.9079 0.0005  -0.0234 -0.3457 170  ASN A OD1 
1120  N  ND2 . ASN A 170 ? 0.8834 1.1901 0.8178 0.0146  -0.0281 -0.2969 170  ASN A ND2 
1121  N  N   . ILE A 171 ? 0.4004 0.5973 0.4013 -0.0203 -0.0263 -0.2725 171  ILE A N   
1122  C  CA  . ILE A 171 ? 0.5793 0.7818 0.5848 -0.0218 -0.0305 -0.2593 171  ILE A CA  
1123  C  C   . ILE A 171 ? 0.4296 0.6217 0.4215 -0.0101 -0.0300 -0.2268 171  ILE A C   
1124  O  O   . ILE A 171 ? 0.3167 0.4820 0.3034 -0.0059 -0.0244 -0.2136 171  ILE A O   
1125  C  CB  . ILE A 171 ? 0.5418 0.7164 0.5701 -0.0369 -0.0269 -0.2667 171  ILE A CB  
1126  C  CG1 . ILE A 171 ? 0.4964 0.6230 0.5262 -0.0363 -0.0201 -0.2447 171  ILE A CG1 
1127  C  CG2 . ILE A 171 ? 0.5112 0.6842 0.5552 -0.0500 -0.0239 -0.2990 171  ILE A CG2 
1128  C  CD1 . ILE A 171 ? 0.6224 0.7467 0.6494 -0.0320 -0.0223 -0.2205 171  ILE A CD1 
1129  N  N   . ASP A 172 ? 0.5625 0.7777 0.5500 -0.0048 -0.0358 -0.2154 172  ASP A N   
1130  C  CA  . ASP A 172 ? 0.5527 0.7615 0.5270 0.0068  -0.0354 -0.1858 172  ASP A CA  
1131  C  C   . ASP A 172 ? 0.5437 0.7138 0.5291 0.0016  -0.0314 -0.1713 172  ASP A C   
1132  O  O   . ASP A 172 ? 0.5984 0.7704 0.5948 -0.0035 -0.0337 -0.1723 172  ASP A O   
1133  C  CB  . ASP A 172 ? 0.4906 0.7405 0.4546 0.0170  -0.0432 -0.1801 172  ASP A CB  
1134  C  CG  . ASP A 172 ? 0.5589 0.8015 0.5074 0.0306  -0.0416 -0.1493 172  ASP A CG  
1135  O  OD1 . ASP A 172 ? 0.6052 0.8104 0.5578 0.0286  -0.0358 -0.1332 172  ASP A OD1 
1136  O  OD2 . ASP A 172 ? 0.4541 0.7287 0.3863 0.0435  -0.0459 -0.1416 172  ASP A OD2 
1137  N  N   . LEU A 173 ? 0.4856 0.6229 0.4682 0.0033  -0.0255 -0.1586 173  LEU A N   
1138  C  CA  . LEU A 173 ? 0.4689 0.5697 0.4602 -0.0009 -0.0220 -0.1465 173  LEU A CA  
1139  C  C   . LEU A 173 ? 0.3961 0.5010 0.3854 0.0038  -0.0246 -0.1292 173  LEU A C   
1140  O  O   . LEU A 173 ? 0.3730 0.4565 0.3712 -0.0011 -0.0230 -0.1241 173  LEU A O   
1141  C  CB  . LEU A 173 ? 0.4095 0.4822 0.3971 0.0025  -0.0167 -0.1362 173  LEU A CB  
1142  C  CG  . LEU A 173 ? 0.3783 0.4411 0.3707 -0.0015 -0.0133 -0.1532 173  LEU A CG  
1143  C  CD1 . LEU A 173 ? 0.2554 0.2983 0.2446 0.0040  -0.0089 -0.1426 173  LEU A CD1 
1144  C  CD2 . LEU A 173 ? 0.5107 0.5518 0.5179 -0.0124 -0.0115 -0.1669 173  LEU A CD2 
1145  N  N   . ASN A 174 ? 0.3451 0.4773 0.3219 0.0144  -0.0282 -0.1200 174  ASN A N   
1146  C  CA  . ASN A 174 ? 0.1766 0.3130 0.1515 0.0208  -0.0305 -0.1039 174  ASN A CA  
1147  C  C   . ASN A 174 ? 0.3424 0.5075 0.3267 0.0177  -0.0364 -0.1168 174  ASN A C   
1148  O  O   . ASN A 174 ? 0.5428 0.7243 0.5246 0.0258  -0.0400 -0.1067 174  ASN A O   
1149  C  CB  . ASN A 174 ? 0.2580 0.4067 0.2152 0.0350  -0.0304 -0.0854 174  ASN A CB  
1150  C  CG  . ASN A 174 ? 0.4256 0.5573 0.3814 0.0413  -0.0288 -0.0641 174  ASN A CG  
1151  O  OD1 . ASN A 174 ? 0.4829 0.5892 0.4495 0.0351  -0.0269 -0.0619 174  ASN A OD1 
1152  N  ND2 . ASN A 174 ? 0.3997 0.5446 0.3413 0.0545  -0.0289 -0.0480 174  ASN A ND2 
1153  N  N   . ARG A 175 ? 0.2385 0.4106 0.2347 0.0061  -0.0370 -0.1400 175  ARG A N   
1154  C  CA  . ARG A 175 ? 0.3997 0.5934 0.4119 -0.0017 -0.0406 -0.1550 175  ARG A CA  
1155  C  C   . ARG A 175 ? 0.4252 0.5891 0.4552 -0.0179 -0.0343 -0.1662 175  ARG A C   
1156  O  O   . ARG A 175 ? 0.4969 0.6735 0.5433 -0.0278 -0.0346 -0.1799 175  ARG A O   
1157  C  CB  . ARG A 175 ? 0.1944 0.4333 0.2068 -0.0015 -0.0476 -0.1763 175  ARG A CB  
1158  C  CG  . ARG A 175 ? 0.3953 0.6652 0.3870 0.0158  -0.0534 -0.1655 175  ARG A CG  
1159  C  CD  . ARG A 175 ? 0.3990 0.6728 0.3845 0.0286  -0.0557 -0.1423 175  ARG A CD  
1160  N  NE  . ARG A 175 ? 0.5084 0.8167 0.4741 0.0457  -0.0615 -0.1343 175  ARG A NE  
1161  C  CZ  . ARG A 175 ? 0.4920 0.7899 0.4370 0.0592  -0.0582 -0.1116 175  ARG A CZ  
1162  N  NH1 . ARG A 175 ? 0.5460 0.8784 0.4723 0.0749  -0.0633 -0.1058 175  ARG A NH1 
1163  N  NH2 . ARG A 175 ? 0.6181 0.8734 0.5610 0.0574  -0.0498 -0.0948 175  ARG A NH2 
1164  N  N   . ASP A 176 ? 0.5724 0.6971 0.5994 -0.0202 -0.0280 -0.1597 176  ASP A N   
1165  C  CA  . ASP A 176 ? 0.5348 0.6301 0.5753 -0.0338 -0.0214 -0.1711 176  ASP A CA  
1166  C  C   . ASP A 176 ? 0.4807 0.5423 0.5256 -0.0369 -0.0158 -0.1568 176  ASP A C   
1167  O  O   . ASP A 176 ? 0.4794 0.5142 0.5337 -0.0472 -0.0092 -0.1631 176  ASP A O   
1168  C  CB  . ASP A 176 ? 0.5041 0.5796 0.5395 -0.0336 -0.0181 -0.1769 176  ASP A CB  
1169  C  CG  . ASP A 176 ? 0.5714 0.6241 0.6211 -0.0469 -0.0117 -0.1943 176  ASP A CG  
1170  O  OD1 . ASP A 176 ? 0.4719 0.5397 0.5359 -0.0578 -0.0113 -0.2110 176  ASP A OD1 
1171  O  OD2 . ASP A 176 ? 0.7185 0.7383 0.7658 -0.0461 -0.0067 -0.1916 176  ASP A OD2 
1172  N  N   . PHE A 177 ? 0.5164 0.5784 0.5534 -0.0276 -0.0179 -0.1375 177  PHE A N   
1173  C  CA  . PHE A 177 ? 0.3093 0.3423 0.3480 -0.0290 -0.0132 -0.1240 177  PHE A CA  
1174  C  C   . PHE A 177 ? 0.3463 0.3943 0.3985 -0.0364 -0.0120 -0.1298 177  PHE A C   
1175  O  O   . PHE A 177 ? 0.5272 0.6126 0.5854 -0.0360 -0.0170 -0.1392 177  PHE A O   
1176  C  CB  . PHE A 177 ? 0.2809 0.3061 0.3065 -0.0164 -0.0152 -0.1028 177  PHE A CB  
1177  C  CG  . PHE A 177 ? 0.4118 0.4154 0.4276 -0.0115 -0.0141 -0.0962 177  PHE A CG  
1178  C  CD1 . PHE A 177 ? 0.5105 0.5303 0.5195 -0.0067 -0.0166 -0.0999 177  PHE A CD1 
1179  C  CD2 . PHE A 177 ? 0.2979 0.2680 0.3116 -0.0113 -0.0106 -0.0869 177  PHE A CD2 
1180  C  CE1 . PHE A 177 ? 0.3821 0.3853 0.3849 -0.0028 -0.0147 -0.0948 177  PHE A CE1 
1181  C  CE2 . PHE A 177 ? 0.3751 0.3299 0.3828 -0.0068 -0.0101 -0.0826 177  PHE A CE2 
1182  C  CZ  . PHE A 177 ? 0.4434 0.4148 0.4469 -0.0030 -0.0117 -0.0866 177  PHE A CZ  
1183  N  N   . PRO A 178 ? 0.3475 0.3686 0.4047 -0.0428 -0.0049 -0.1247 178  PRO A N   
1184  C  CA  . PRO A 178 ? 0.2957 0.3297 0.3662 -0.0498 -0.0018 -0.1283 178  PRO A CA  
1185  C  C   . PRO A 178 ? 0.4923 0.5562 0.5606 -0.0387 -0.0082 -0.1195 178  PRO A C   
1186  O  O   . PRO A 178 ? 0.3081 0.3637 0.3627 -0.0262 -0.0111 -0.1031 178  PRO A O   
1187  C  CB  . PRO A 178 ? 0.3764 0.3706 0.4441 -0.0533 0.0070  -0.1171 178  PRO A CB  
1188  C  CG  . PRO A 178 ? 0.2856 0.2477 0.3443 -0.0526 0.0090  -0.1157 178  PRO A CG  
1189  C  CD  . PRO A 178 ? 0.3913 0.3697 0.4412 -0.0429 0.0007  -0.1155 178  PRO A CD  
1190  N  N   . ASP A 179 ? 0.5215 0.6206 0.6047 -0.0431 -0.0101 -0.1313 179  ASP A N   
1191  C  CA  . ASP A 179 ? 0.4221 0.5530 0.5049 -0.0312 -0.0165 -0.1245 179  ASP A CA  
1192  C  C   . ASP A 179 ? 0.4958 0.6215 0.5873 -0.0334 -0.0105 -0.1184 179  ASP A C   
1193  O  O   . ASP A 179 ? 0.4719 0.5930 0.5783 -0.0479 -0.0028 -0.1283 179  ASP A O   
1194  C  CB  . ASP A 179 ? 0.4990 0.6793 0.5927 -0.0318 -0.0240 -0.1421 179  ASP A CB  
1195  C  CG  . ASP A 179 ? 0.6825 0.8965 0.7713 -0.0145 -0.0324 -0.1329 179  ASP A CG  
1196  O  OD1 . ASP A 179 ? 0.7237 0.9234 0.7941 0.0000  -0.0345 -0.1141 179  ASP A OD1 
1197  O  OD2 . ASP A 179 ? 0.6924 0.9472 0.7966 -0.0151 -0.0364 -0.1446 179  ASP A OD2 
1198  N  N   . ARG A 180 ? 0.5312 0.6565 0.6135 -0.0192 -0.0130 -0.1021 180  ARG A N   
1199  C  CA  . ARG A 180 ? 0.5566 0.6780 0.6454 -0.0190 -0.0073 -0.0960 180  ARG A CA  
1200  C  C   . ARG A 180 ? 0.5491 0.7111 0.6604 -0.0258 -0.0072 -0.1111 180  ARG A C   
1201  O  O   . ARG A 180 ? 0.5551 0.7143 0.6783 -0.0341 0.0011  -0.1132 180  ARG A O   
1202  C  CB  . ARG A 180 ? 0.4841 0.6019 0.5601 -0.0011 -0.0110 -0.0783 180  ARG A CB  
1203  C  CG  . ARG A 180 ? 0.4686 0.6219 0.5425 0.0126  -0.0206 -0.0776 180  ARG A CG  
1204  C  CD  . ARG A 180 ? 0.5410 0.6811 0.5997 0.0299  -0.0226 -0.0587 180  ARG A CD  
1205  N  NE  . ARG A 180 ? 0.6308 0.8059 0.6869 0.0447  -0.0308 -0.0563 180  ARG A NE  
1206  C  CZ  . ARG A 180 ? 0.4756 0.6803 0.5405 0.0548  -0.0337 -0.0560 180  ARG A CZ  
1207  N  NH1 . ARG A 180 ? 0.4363 0.6398 0.5142 0.0504  -0.0282 -0.0586 180  ARG A NH1 
1208  N  NH2 . ARG A 180 ? 0.2830 0.5192 0.3429 0.0705  -0.0418 -0.0526 180  ARG A NH2 
1209  N  N   . LEU A 181 ? 0.4649 0.6671 0.5825 -0.0225 -0.0161 -0.1225 181  LEU A N   
1210  C  CA  . LEU A 181 ? 0.4575 0.7047 0.5990 -0.0287 -0.0174 -0.1394 181  LEU A CA  
1211  C  C   . LEU A 181 ? 0.4896 0.7410 0.6501 -0.0512 -0.0118 -0.1618 181  LEU A C   
1212  O  O   . LEU A 181 ? 0.6311 0.9257 0.8126 -0.0579 -0.0151 -0.1810 181  LEU A O   
1213  C  CB  . LEU A 181 ? 0.4447 0.7387 0.5844 -0.0123 -0.0306 -0.1414 181  LEU A CB  
1214  C  CG  . LEU A 181 ? 0.4650 0.7509 0.5867 0.0101  -0.0343 -0.1185 181  LEU A CG  
1215  C  CD1 . LEU A 181 ? 0.6521 0.9736 0.7638 0.0284  -0.0467 -0.1161 181  LEU A CD1 
1216  C  CD2 . LEU A 181 ? 0.3136 0.6055 0.4471 0.0137  -0.0295 -0.1136 181  LEU A CD2 
1217  N  N   . GLU A 182 ? 0.6069 0.8135 0.7609 -0.0624 -0.0031 -0.1597 182  GLU A N   
1218  C  CA  . GLU A 182 ? 0.5907 0.7901 0.7619 -0.0840 0.0053  -0.1786 182  GLU A CA  
1219  C  C   . GLU A 182 ? 0.5624 0.7933 0.7415 -0.0884 -0.0030 -0.2001 182  GLU A C   
1220  O  O   . GLU A 182 ? 0.6659 0.9364 0.8686 -0.0985 -0.0042 -0.2209 182  GLU A O   
1221  C  CB  . GLU A 182 ? 0.6620 0.8764 0.8581 -0.0978 0.0151  -0.1874 182  GLU A CB  
1222  C  CG  . GLU A 182 ? 0.7040 0.9017 0.9181 -0.1217 0.0276  -0.2041 182  GLU A CG  
1223  C  CD  . GLU A 182 ? 0.7400 0.8795 0.9422 -0.1275 0.0418  -0.1886 182  GLU A CD  
1224  O  OE1 . GLU A 182 ? 0.7225 0.8388 0.9355 -0.1455 0.0537  -0.1986 182  GLU A OE1 
1225  O  OE2 . GLU A 182 ? 0.7218 0.8388 0.9035 -0.1137 0.0414  -0.1668 182  GLU A OE2 
1226  N  N   . ALA A 191 ? 0.8226 0.6638 0.9077 -0.0989 0.0566  -0.1310 191  ALA A N   
1227  C  CA  . ALA A 191 ? 0.9323 0.7432 1.0258 -0.1104 0.0683  -0.1404 191  ALA A CA  
1228  C  C   . ALA A 191 ? 1.0128 0.8263 1.1095 -0.1096 0.0630  -0.1561 191  ALA A C   
1229  O  O   . ALA A 191 ? 1.1103 0.9294 1.2243 -0.1230 0.0678  -0.1765 191  ALA A O   
1230  C  CB  . ALA A 191 ? 1.0538 0.8754 1.1692 -0.1296 0.0793  -0.1531 191  ALA A CB  
1231  N  N   . GLN A 192 ? 0.9633 0.7727 1.0439 -0.0939 0.0539  -0.1469 192  GLN A N   
1232  C  CA  . GLN A 192 ? 0.8677 0.6851 0.9473 -0.0887 0.0471  -0.1585 192  GLN A CA  
1233  C  C   . GLN A 192 ? 0.9274 0.7543 1.0233 -0.1006 0.0498  -0.1843 192  GLN A C   
1234  O  O   . GLN A 192 ? 0.8552 0.7018 0.9683 -0.1150 0.0532  -0.1994 192  GLN A O   
1235  C  CB  . GLN A 192 ? 0.7184 0.5027 0.7829 -0.0751 0.0469  -0.1457 192  GLN A CB  
1236  C  CG  . GLN A 192 ? 0.7942 0.5837 0.8428 -0.0605 0.0394  -0.1246 192  GLN A CG  
1237  C  CD  . GLN A 192 ? 0.7380 0.5630 0.7874 -0.0607 0.0317  -0.1237 192  GLN A CD  
1238  O  OE1 . GLN A 192 ? 0.7727 0.6294 0.8260 -0.0604 0.0249  -0.1339 192  GLN A OE1 
1239  N  NE2 . GLN A 192 ? 0.6136 0.4358 0.6583 -0.0595 0.0332  -0.1102 192  GLN A NE2 
1240  N  N   . SER A 193 ? 0.9745 0.7896 1.0656 -0.0938 0.0478  -0.1902 193  SER A N   
1241  C  CA  . SER A 193 ? 0.8998 0.7291 1.0022 -0.1007 0.0473  -0.2156 193  SER A CA  
1242  C  C   . SER A 193 ? 0.8275 0.7073 0.9272 -0.0956 0.0346  -0.2236 193  SER A C   
1243  O  O   . SER A 193 ? 0.8679 0.7751 0.9788 -0.1039 0.0325  -0.2466 193  SER A O   
1244  C  CB  . SER A 193 ? 0.9161 0.7398 1.0397 -0.1205 0.0578  -0.2348 193  SER A CB  
1245  O  OG  . SER A 193 ? 0.9317 0.7536 1.0646 -0.1257 0.0597  -0.2589 193  SER A OG  
1246  N  N   . ARG A 194 ? 0.5641 0.4558 0.6486 -0.0819 0.0265  -0.2048 194  ARG A N   
1247  C  CA  . ARG A 194 ? 0.4871 0.4201 0.5648 -0.0741 0.0159  -0.2080 194  ARG A CA  
1248  C  C   . ARG A 194 ? 0.6994 0.6251 0.7688 -0.0651 0.0145  -0.2118 194  ARG A C   
1249  O  O   . ARG A 194 ? 0.7077 0.6034 0.7816 -0.0674 0.0211  -0.2195 194  ARG A O   
1250  C  CB  . ARG A 194 ? 0.2736 0.2171 0.3392 -0.0636 0.0100  -0.1852 194  ARG A CB  
1251  C  CG  . ARG A 194 ? 0.4981 0.4274 0.5673 -0.0682 0.0145  -0.1733 194  ARG A CG  
1252  C  CD  . ARG A 194 ? 0.7797 0.7474 0.8538 -0.0699 0.0093  -0.1744 194  ARG A CD  
1253  N  NE  . ARG A 194 ? 0.6731 0.6301 0.7511 -0.0739 0.0141  -0.1633 194  ARG A NE  
1254  C  CZ  . ARG A 194 ? 0.7732 0.7598 0.8606 -0.0779 0.0123  -0.1666 194  ARG A CZ  
1255  N  NH1 . ARG A 194 ? 0.8566 0.8854 0.9496 -0.0777 0.0047  -0.1801 194  ARG A NH1 
1256  N  NH2 . ARG A 194 ? 0.8896 0.8659 0.9806 -0.0813 0.0180  -0.1568 194  ARG A NH2 
1257  N  N   . GLN A 195 ? 0.5552 0.5073 0.6128 -0.0542 0.0069  -0.2053 195  GLN A N   
1258  C  CA  . GLN A 195 ? 0.4442 0.3910 0.4936 -0.0445 0.0063  -0.2055 195  GLN A CA  
1259  C  C   . GLN A 195 ? 0.5093 0.4215 0.5526 -0.0363 0.0087  -0.1858 195  GLN A C   
1260  O  O   . GLN A 195 ? 0.3930 0.2986 0.4319 -0.0338 0.0074  -0.1678 195  GLN A O   
1261  C  CB  . GLN A 195 ? 0.4431 0.4285 0.4813 -0.0360 -0.0007 -0.2033 195  GLN A CB  
1262  C  CG  . GLN A 195 ? 0.4985 0.5233 0.5399 -0.0414 -0.0049 -0.2225 195  GLN A CG  
1263  C  CD  . GLN A 195 ? 0.5464 0.5694 0.5981 -0.0497 -0.0014 -0.2502 195  GLN A CD  
1264  O  OE1 . GLN A 195 ? 0.6415 0.6550 0.6898 -0.0449 0.0012  -0.2567 195  GLN A OE1 
1265  N  NE2 . GLN A 195 ? 0.3672 0.4010 0.4329 -0.0626 -0.0009 -0.2679 195  GLN A NE2 
1266  N  N   . PRO A 196 ? 0.5017 0.3933 0.5453 -0.0315 0.0121  -0.1907 196  PRO A N   
1267  C  CA  . PRO A 196 ? 0.3467 0.2084 0.3857 -0.0221 0.0136  -0.1753 196  PRO A CA  
1268  C  C   . PRO A 196 ? 0.3797 0.2543 0.4097 -0.0149 0.0081  -0.1559 196  PRO A C   
1269  O  O   . PRO A 196 ? 0.4287 0.2843 0.4554 -0.0117 0.0080  -0.1406 196  PRO A O   
1270  C  CB  . PRO A 196 ? 0.2892 0.1515 0.3286 -0.0148 0.0145  -0.1860 196  PRO A CB  
1271  C  CG  . PRO A 196 ? 0.4920 0.3665 0.5386 -0.0233 0.0169  -0.2096 196  PRO A CG  
1272  C  CD  . PRO A 196 ? 0.3921 0.2955 0.4393 -0.0324 0.0133  -0.2123 196  PRO A CD  
1273  N  N   . GLU A 197 ? 0.4255 0.3326 0.4508 -0.0121 0.0040  -0.1569 197  GLU A N   
1274  C  CA  . GLU A 197 ? 0.4357 0.3536 0.4533 -0.0049 0.0005  -0.1397 197  GLU A CA  
1275  C  C   . GLU A 197 ? 0.3416 0.2589 0.3575 -0.0080 -0.0015 -0.1275 197  GLU A C   
1276  O  O   . GLU A 197 ? 0.3512 0.2576 0.3635 -0.0035 -0.0026 -0.1123 197  GLU A O   
1277  C  CB  . GLU A 197 ? 0.4469 0.3986 0.4585 -0.0015 -0.0014 -0.1432 197  GLU A CB  
1278  C  CG  . GLU A 197 ? 0.3768 0.3326 0.3893 0.0028  0.0013  -0.1547 197  GLU A CG  
1279  C  CD  . GLU A 197 ? 0.5415 0.5051 0.5583 -0.0028 0.0028  -0.1777 197  GLU A CD  
1280  O  OE1 . GLU A 197 ? 0.5813 0.5483 0.5990 0.0009  0.0054  -0.1895 197  GLU A OE1 
1281  O  OE2 . GLU A 197 ? 0.3139 0.2818 0.3344 -0.0111 0.0016  -0.1850 197  GLU A OE2 
1282  N  N   . THR A 198 ? 0.3511 0.2819 0.3709 -0.0157 -0.0017 -0.1358 198  THR A N   
1283  C  CA  . THR A 198 ? 0.3585 0.2916 0.3787 -0.0188 -0.0029 -0.1266 198  THR A CA  
1284  C  C   . THR A 198 ? 0.4484 0.3470 0.4703 -0.0205 0.0010  -0.1187 198  THR A C   
1285  O  O   . THR A 198 ? 0.5590 0.4488 0.5757 -0.0161 -0.0002 -0.1036 198  THR A O   
1286  C  CB  . THR A 198 ? 0.4738 0.4291 0.5017 -0.0278 -0.0034 -0.1410 198  THR A CB  
1287  O  OG1 . THR A 198 ? 0.3728 0.3596 0.3982 -0.0259 -0.0069 -0.1528 198  THR A OG1 
1288  C  CG2 . THR A 198 ? 0.4115 0.3784 0.4400 -0.0285 -0.0054 -0.1310 198  THR A CG2 
1289  N  N   . ALA A 199 ? 0.4523 0.3304 0.4807 -0.0267 0.0064  -0.1290 199  ALA A N   
1290  C  CA  . ALA A 199 ? 0.3997 0.2436 0.4277 -0.0275 0.0116  -0.1207 199  ALA A CA  
1291  C  C   . ALA A 199 ? 0.4713 0.3056 0.4909 -0.0157 0.0089  -0.1026 199  ALA A C   
1292  O  O   . ALA A 199 ? 0.5045 0.3295 0.5193 -0.0137 0.0095  -0.0888 199  ALA A O   
1293  C  CB  . ALA A 199 ? 0.2723 0.0960 0.3081 -0.0325 0.0188  -0.1317 199  ALA A CB  
1294  N  N   . ALA A 200 ? 0.3814 0.2201 0.3996 -0.0084 0.0060  -0.1044 200  ALA A N   
1295  C  CA  . ALA A 200 ? 0.3058 0.1400 0.3190 0.0016  0.0026  -0.0909 200  ALA A CA  
1296  C  C   . ALA A 200 ? 0.4180 0.2621 0.4259 0.0033  -0.0012 -0.0787 200  ALA A C   
1297  O  O   . ALA A 200 ? 0.5852 0.4212 0.5886 0.0072  -0.0026 -0.0666 200  ALA A O   
1298  C  CB  . ALA A 200 ? 0.3804 0.2237 0.3954 0.0076  0.0006  -0.0979 200  ALA A CB  
1299  N  N   . LEU A 201 ? 0.3230 0.1846 0.3303 0.0008  -0.0031 -0.0831 201  LEU A N   
1300  C  CA  . LEU A 201 ? 0.4256 0.2947 0.4285 0.0034  -0.0059 -0.0722 201  LEU A CA  
1301  C  C   . LEU A 201 ? 0.5085 0.3715 0.5103 -0.0002 -0.0046 -0.0662 201  LEU A C   
1302  O  O   . LEU A 201 ? 0.4687 0.3292 0.4667 0.0033  -0.0060 -0.0546 201  LEU A O   
1303  C  CB  . LEU A 201 ? 0.4107 0.3083 0.4129 0.0038  -0.0074 -0.0731 201  LEU A CB  
1304  C  CG  . LEU A 201 ? 0.4962 0.3978 0.4974 0.0098  -0.0080 -0.0692 201  LEU A CG  
1305  C  CD1 . LEU A 201 ? 0.3179 0.2250 0.3218 0.0102  -0.0065 -0.0811 201  LEU A CD1 
1306  C  CD2 . LEU A 201 ? 0.6911 0.6106 0.6883 0.0124  -0.0084 -0.0601 201  LEU A CD2 
1307  N  N   . VAL A 202 ? 0.3814 0.2449 0.3876 -0.0080 -0.0014 -0.0750 202  VAL A N   
1308  C  CA  . VAL A 202 ? 0.4565 0.3130 0.4632 -0.0124 0.0016  -0.0709 202  VAL A CA  
1309  C  C   . VAL A 202 ? 0.5372 0.3754 0.5378 -0.0077 0.0035  -0.0582 202  VAL A C   
1310  O  O   . VAL A 202 ? 0.5361 0.3735 0.5314 -0.0048 0.0027  -0.0484 202  VAL A O   
1311  C  CB  . VAL A 202 ? 0.3820 0.2406 0.3978 -0.0231 0.0067  -0.0831 202  VAL A CB  
1312  C  CG1 . VAL A 202 ? 0.2701 0.1145 0.2864 -0.0282 0.0126  -0.0778 202  VAL A CG1 
1313  C  CG2 . VAL A 202 ? 0.3496 0.2432 0.3718 -0.0265 0.0034  -0.0927 202  VAL A CG2 
1314  N  N   . ASN A 203 ? 0.3894 0.2136 0.3896 -0.0061 0.0057  -0.0595 203  ASN A N   
1315  C  CA  . ASN A 203 ? 0.3966 0.2026 0.3883 -0.0006 0.0069  -0.0496 203  ASN A CA  
1316  C  C   . ASN A 203 ? 0.3663 0.1802 0.3514 0.0074  0.0003  -0.0404 203  ASN A C   
1317  O  O   . ASN A 203 ? 0.4451 0.2513 0.4213 0.0107  0.0001  -0.0323 203  ASN A O   
1318  C  CB  . ASN A 203 ? 0.4135 0.2048 0.4060 0.0027  0.0085  -0.0537 203  ASN A CB  
1319  C  CG  . ASN A 203 ? 0.7071 0.4775 0.7025 -0.0042 0.0177  -0.0588 203  ASN A CG  
1320  O  OD1 . ASN A 203 ? 0.7084 0.4800 0.7090 -0.0140 0.0229  -0.0631 203  ASN A OD1 
1321  N  ND2 . ASN A 203 ? 0.8696 0.6193 0.8627 0.0008  0.0205  -0.0591 203  ASN A ND2 
1322  N  N   . TRP A 204 ? 0.3306 0.1590 0.3201 0.0100  -0.0045 -0.0431 204  TRP A N   
1323  C  CA  . TRP A 204 ? 0.2962 0.1320 0.2831 0.0158  -0.0100 -0.0370 204  TRP A CA  
1324  C  C   . TRP A 204 ? 0.3718 0.2143 0.3558 0.0145  -0.0105 -0.0312 204  TRP A C   
1325  O  O   . TRP A 204 ? 0.5212 0.3602 0.4989 0.0177  -0.0126 -0.0256 204  TRP A O   
1326  C  CB  . TRP A 204 ? 0.3439 0.1915 0.3377 0.0174  -0.0123 -0.0420 204  TRP A CB  
1327  C  CG  . TRP A 204 ? 0.4857 0.3384 0.4805 0.0221  -0.0166 -0.0383 204  TRP A CG  
1328  C  CD1 . TRP A 204 ? 0.4274 0.2735 0.4195 0.0274  -0.0203 -0.0360 204  TRP A CD1 
1329  C  CD2 . TRP A 204 ? 0.4948 0.3587 0.4943 0.0219  -0.0171 -0.0377 204  TRP A CD2 
1330  N  NE1 . TRP A 204 ? 0.5436 0.3983 0.5410 0.0294  -0.0237 -0.0358 204  TRP A NE1 
1331  C  CE2 . TRP A 204 ? 0.4280 0.2925 0.4303 0.0255  -0.0207 -0.0362 204  TRP A CE2 
1332  C  CE3 . TRP A 204 ? 0.2885 0.1598 0.2893 0.0196  -0.0144 -0.0388 204  TRP A CE3 
1333  C  CZ2 . TRP A 204 ? 0.3318 0.2034 0.3408 0.0251  -0.0203 -0.0357 204  TRP A CZ2 
1334  C  CZ3 . TRP A 204 ? 0.3651 0.2410 0.3694 0.0207  -0.0136 -0.0362 204  TRP A CZ3 
1335  C  CH2 . TRP A 204 ? 0.3857 0.2615 0.3953 0.0224  -0.0158 -0.0346 204  TRP A CH2 
1336  N  N   . ILE A 205 ? 0.4103 0.2613 0.3983 0.0105  -0.0088 -0.0340 205  ILE A N   
1337  C  CA  . ILE A 205 ? 0.5490 0.4057 0.5355 0.0107  -0.0092 -0.0291 205  ILE A CA  
1338  C  C   . ILE A 205 ? 0.6059 0.4542 0.5863 0.0105  -0.0070 -0.0243 205  ILE A C   
1339  O  O   . ILE A 205 ? 0.7469 0.5969 0.7236 0.0134  -0.0084 -0.0193 205  ILE A O   
1340  C  CB  . ILE A 205 ? 0.3858 0.2508 0.3767 0.0079  -0.0080 -0.0348 205  ILE A CB  
1341  C  CG1 . ILE A 205 ? 0.3851 0.2602 0.3779 0.0098  -0.0097 -0.0385 205  ILE A CG1 
1342  C  CG2 . ILE A 205 ? 0.3962 0.2645 0.3858 0.0103  -0.0080 -0.0293 205  ILE A CG2 
1343  C  CD1 . ILE A 205 ? 0.3184 0.2168 0.3139 0.0072  -0.0096 -0.0439 205  ILE A CD1 
1344  N  N   . VAL A 206 ? 0.4428 0.2799 0.4218 0.0070  -0.0025 -0.0264 206  VAL A N   
1345  C  CA  . VAL A 206 ? 0.4484 0.2742 0.4201 0.0066  0.0017  -0.0218 206  VAL A CA  
1346  C  C   . VAL A 206 ? 0.4819 0.2947 0.4421 0.0125  0.0001  -0.0168 206  VAL A C   
1347  O  O   . VAL A 206 ? 0.5254 0.3264 0.4758 0.0141  0.0034  -0.0124 206  VAL A O   
1348  C  CB  . VAL A 206 ? 0.4476 0.2641 0.4238 -0.0015 0.0097  -0.0264 206  VAL A CB  
1349  C  CG1 . VAL A 206 ? 0.3407 0.1712 0.3282 -0.0074 0.0100  -0.0340 206  VAL A CG1 
1350  C  CG2 . VAL A 206 ? 0.4568 0.2617 0.4346 -0.0034 0.0121  -0.0307 206  VAL A CG2 
1351  N  N   . SER A 207 ? 0.5428 0.3574 0.5039 0.0167  -0.0050 -0.0182 207  SER A N   
1352  C  CA  . SER A 207 ? 0.4529 0.2546 0.4038 0.0238  -0.0078 -0.0153 207  SER A CA  
1353  C  C   . SER A 207 ? 0.3773 0.1845 0.3230 0.0290  -0.0141 -0.0132 207  SER A C   
1354  O  O   . SER A 207 ? 0.4542 0.2499 0.3887 0.0360  -0.0169 -0.0110 207  SER A O   
1355  C  CB  . SER A 207 ? 0.4378 0.2376 0.3938 0.0267  -0.0104 -0.0192 207  SER A CB  
1356  O  OG  . SER A 207 ? 0.4643 0.2792 0.4274 0.0291  -0.0171 -0.0219 207  SER A OG  
1357  N  N   . LYS A 208 ? 0.3771 0.1998 0.3306 0.0263  -0.0161 -0.0144 208  LYS A N   
1358  C  CA  . LYS A 208 ? 0.3955 0.2225 0.3472 0.0296  -0.0210 -0.0143 208  LYS A CA  
1359  C  C   . LYS A 208 ? 0.3530 0.1878 0.3081 0.0263  -0.0183 -0.0130 208  LYS A C   
1360  O  O   . LYS A 208 ? 0.6103 0.4520 0.5721 0.0224  -0.0149 -0.0128 208  LYS A O   
1361  C  CB  . LYS A 208 ? 0.5315 0.3672 0.4932 0.0311  -0.0265 -0.0181 208  LYS A CB  
1362  C  CG  . LYS A 208 ? 0.5363 0.3652 0.4965 0.0363  -0.0300 -0.0205 208  LYS A CG  
1363  C  CD  . LYS A 208 ? 0.4987 0.3365 0.4706 0.0385  -0.0353 -0.0256 208  LYS A CD  
1364  C  CE  . LYS A 208 ? 0.6886 0.5179 0.6573 0.0473  -0.0402 -0.0284 208  LYS A CE  
1365  N  NZ  . LYS A 208 ? 0.7492 0.5875 0.7315 0.0512  -0.0456 -0.0355 208  LYS A NZ  
1366  N  N   . PRO A 209 ? 0.3841 0.2167 0.3345 0.0292  -0.0202 -0.0128 209  PRO A N   
1367  C  CA  . PRO A 209 ? 0.2919 0.1287 0.2447 0.0279  -0.0173 -0.0117 209  PRO A CA  
1368  C  C   . PRO A 209 ? 0.4655 0.3120 0.4302 0.0262  -0.0183 -0.0123 209  PRO A C   
1369  O  O   . PRO A 209 ? 0.4576 0.3031 0.4246 0.0275  -0.0193 -0.0134 209  PRO A O   
1370  C  CB  . PRO A 209 ? 0.2478 0.0758 0.1909 0.0326  -0.0195 -0.0129 209  PRO A CB  
1371  C  CG  . PRO A 209 ? 0.2186 0.0437 0.1606 0.0362  -0.0264 -0.0165 209  PRO A CG  
1372  C  CD  . PRO A 209 ? 0.2592 0.0832 0.2011 0.0353  -0.0257 -0.0148 209  PRO A CD  
1373  N  N   . PHE A 210 ? 0.4081 0.2613 0.3797 0.0236  -0.0171 -0.0118 210  PHE A N   
1374  C  CA  . PHE A 210 ? 0.4090 0.2677 0.3893 0.0229  -0.0162 -0.0109 210  PHE A CA  
1375  C  C   . PHE A 210 ? 0.4063 0.2639 0.3872 0.0245  -0.0129 -0.0076 210  PHE A C   
1376  O  O   . PHE A 210 ? 0.5900 0.4476 0.5675 0.0256  -0.0107 -0.0061 210  PHE A O   
1377  C  CB  . PHE A 210 ? 0.2674 0.1314 0.2519 0.0213  -0.0148 -0.0109 210  PHE A CB  
1378  C  CG  . PHE A 210 ? 0.3128 0.1773 0.2997 0.0208  -0.0174 -0.0146 210  PHE A CG  
1379  C  CD1 . PHE A 210 ? 0.3522 0.2143 0.3358 0.0202  -0.0176 -0.0169 210  PHE A CD1 
1380  C  CD2 . PHE A 210 ? 0.2785 0.1442 0.2723 0.0211  -0.0189 -0.0164 210  PHE A CD2 
1381  C  CE1 . PHE A 210 ? 0.2226 0.0835 0.2086 0.0214  -0.0199 -0.0205 210  PHE A CE1 
1382  C  CE2 . PHE A 210 ? 0.4375 0.3041 0.4350 0.0220  -0.0215 -0.0207 210  PHE A CE2 
1383  C  CZ  . PHE A 210 ? 0.2842 0.1483 0.2771 0.0229  -0.0223 -0.0225 210  PHE A CZ  
1384  N  N   . VAL A 211 ? 0.3240 0.1791 0.3104 0.0249  -0.0120 -0.0070 211  VAL A N   
1385  C  CA  . VAL A 211 ? 0.4581 0.3084 0.4453 0.0276  -0.0085 -0.0040 211  VAL A CA  
1386  C  C   . VAL A 211 ? 0.4437 0.2949 0.4343 0.0300  -0.0042 0.0026  211  VAL A C   
1387  O  O   . VAL A 211 ? 0.5226 0.3733 0.5114 0.0348  -0.0018 0.0070  211  VAL A O   
1388  C  CB  . VAL A 211 ? 0.3907 0.2329 0.3827 0.0271  -0.0088 -0.0075 211  VAL A CB  
1389  C  CG1 . VAL A 211 ? 0.3581 0.1922 0.3529 0.0303  -0.0034 -0.0039 211  VAL A CG1 
1390  C  CG2 . VAL A 211 ? 0.2395 0.0790 0.2250 0.0279  -0.0137 -0.0137 211  VAL A CG2 
1391  N  N   . LEU A 212 ? 0.4423 0.2945 0.4376 0.0280  -0.0031 0.0039  212  LEU A N   
1392  C  CA  . LEU A 212 ? 0.2983 0.1488 0.2945 0.0316  0.0015  0.0120  212  LEU A CA  
1393  C  C   . LEU A 212 ? 0.3439 0.1998 0.3407 0.0298  0.0008  0.0112  212  LEU A C   
1394  O  O   . LEU A 212 ? 0.5147 0.3731 0.5146 0.0251  -0.0021 0.0043  212  LEU A O   
1395  C  CB  . LEU A 212 ? 0.3805 0.2190 0.3828 0.0317  0.0074  0.0162  212  LEU A CB  
1396  C  CG  . LEU A 212 ? 0.3723 0.2041 0.3755 0.0351  0.0145  0.0273  212  LEU A CG  
1397  C  CD1 . LEU A 212 ? 0.4718 0.3082 0.4662 0.0450  0.0148  0.0373  212  LEU A CD1 
1398  C  CD2 . LEU A 212 ? 0.4202 0.2354 0.4310 0.0338  0.0217  0.0304  212  LEU A CD2 
1399  N  N   . SER A 213 ? 0.3964 0.2543 0.3897 0.0351  0.0030  0.0186  213  SER A N   
1400  C  CA  . SER A 213 ? 0.3508 0.2226 0.3430 0.0327  0.0027  0.0160  213  SER A CA  
1401  C  C   . SER A 213 ? 0.3921 0.2775 0.3783 0.0377  0.0067  0.0253  213  SER A C   
1402  O  O   . SER A 213 ? 0.4072 0.2949 0.3886 0.0446  0.0080  0.0335  213  SER A O   
1403  C  CB  . SER A 213 ? 0.3521 0.2327 0.3422 0.0306  -0.0027 0.0070  213  SER A CB  
1404  O  OG  . SER A 213 ? 0.5102 0.4050 0.4990 0.0290  -0.0027 0.0032  213  SER A OG  
1405  N  N   . ALA A 214 ? 0.4669 0.3625 0.4521 0.0357  0.0088  0.0242  214  ALA A N   
1406  C  CA  . ALA A 214 ? 0.4226 0.3340 0.3988 0.0414  0.0124  0.0326  214  ALA A CA  
1407  C  C   . ALA A 214 ? 0.2998 0.2288 0.2738 0.0386  0.0108  0.0239  214  ALA A C   
1408  O  O   . ALA A 214 ? 0.3437 0.2679 0.3251 0.0326  0.0106  0.0157  214  ALA A O   
1409  C  CB  . ALA A 214 ? 0.3861 0.2866 0.3624 0.0428  0.0218  0.0452  214  ALA A CB  
1410  N  N   . ASN A 215 ? 0.4354 0.3862 0.3998 0.0438  0.0090  0.0244  215  ASN A N   
1411  C  CA  . ASN A 215 ? 0.5345 0.5032 0.4955 0.0420  0.0090  0.0162  215  ASN A CA  
1412  C  C   . ASN A 215 ? 0.6036 0.5906 0.5509 0.0497  0.0139  0.0262  215  ASN A C   
1413  O  O   . ASN A 215 ? 0.4432 0.4376 0.3812 0.0584  0.0136  0.0368  215  ASN A O   
1414  C  CB  . ASN A 215 ? 0.4605 0.4391 0.4246 0.0379  0.0018  -0.0003 215  ASN A CB  
1415  C  CG  . ASN A 215 ? 0.4411 0.4412 0.3991 0.0425  -0.0031 -0.0024 215  ASN A CG  
1416  O  OD1 . ASN A 215 ? 0.6080 0.6306 0.5610 0.0433  -0.0052 -0.0109 215  ASN A OD1 
1417  N  ND2 . ASN A 215 ? 0.4276 0.4233 0.3870 0.0457  -0.0052 0.0036  215  ASN A ND2 
1418  N  N   . PHE A 216 ? 0.4943 0.4887 0.4398 0.0475  0.0188  0.0236  216  PHE A N   
1419  C  CA  . PHE A 216 ? 0.2316 0.2377 0.1638 0.0540  0.0267  0.0361  216  PHE A CA  
1420  C  C   . PHE A 216 ? 0.3855 0.4219 0.3055 0.0583  0.0236  0.0277  216  PHE A C   
1421  O  O   . PHE A 216 ? 0.3650 0.4097 0.2904 0.0528  0.0197  0.0105  216  PHE A O   
1422  C  CB  . PHE A 216 ? 0.2900 0.2833 0.2295 0.0484  0.0372  0.0409  216  PHE A CB  
1423  C  CG  . PHE A 216 ? 0.4605 0.4261 0.4133 0.0434  0.0400  0.0465  216  PHE A CG  
1424  C  CD1 . PHE A 216 ? 0.4759 0.4293 0.4446 0.0356  0.0348  0.0340  216  PHE A CD1 
1425  C  CD2 . PHE A 216 ? 0.5229 0.4745 0.4718 0.0475  0.0477  0.0641  216  PHE A CD2 
1426  C  CE1 . PHE A 216 ? 0.4376 0.3685 0.4177 0.0315  0.0364  0.0372  216  PHE A CE1 
1427  C  CE2 . PHE A 216 ? 0.4507 0.3767 0.4129 0.0423  0.0503  0.0667  216  PHE A CE2 
1428  C  CZ  . PHE A 216 ? 0.3341 0.2515 0.3118 0.0341  0.0442  0.0525  216  PHE A CZ  
1429  N  N   . HIS A 217 ? 0.3435 0.3960 0.2461 0.0691  0.0254  0.0400  217  HIS A N   
1430  C  CA  . HIS A 217 ? 0.3777 0.4633 0.2656 0.0754  0.0217  0.0328  217  HIS A CA  
1431  C  C   . HIS A 217 ? 0.4302 0.5249 0.2987 0.0849  0.0319  0.0508  217  HIS A C   
1432  O  O   . HIS A 217 ? 0.3908 0.4638 0.2587 0.0862  0.0418  0.0693  217  HIS A O   
1433  C  CB  . HIS A 217 ? 0.4126 0.5162 0.2968 0.0818  0.0107  0.0285  217  HIS A CB  
1434  C  CG  . HIS A 217 ? 0.4531 0.5505 0.3552 0.0720  0.0022  0.0106  217  HIS A CG  
1435  N  ND1 . HIS A 217 ? 0.3625 0.4808 0.2681 0.0674  -0.0050 -0.0107 217  HIS A ND1 
1436  C  CD2 . HIS A 217 ? 0.4016 0.4733 0.3184 0.0657  0.0010  0.0108  217  HIS A CD2 
1437  C  CE1 . HIS A 217 ? 0.4137 0.5177 0.3354 0.0585  -0.0094 -0.0212 217  HIS A CE1 
1438  N  NE2 . HIS A 217 ? 0.3427 0.4194 0.2703 0.0579  -0.0061 -0.0081 217  HIS A NE2 
1439  N  N   . GLY A 218 ? 0.4282 0.5545 0.2802 0.0915  0.0300  0.0449  218  GLY A N   
1440  C  CA  . GLY A 218 ? 0.4669 0.6052 0.2962 0.1023  0.0398  0.0626  218  GLY A CA  
1441  C  C   . GLY A 218 ? 0.5333 0.7071 0.3420 0.1164  0.0309  0.0617  218  GLY A C   
1442  O  O   . GLY A 218 ? 0.6444 0.8364 0.4597 0.1147  0.0178  0.0425  218  GLY A O   
1443  N  N   . GLY A 219 ? 0.4730 0.6573 0.2569 0.1307  0.0382  0.0823  219  GLY A N   
1444  C  CA  . GLY A 219 ? 0.4700 0.6917 0.2314 0.1469  0.0293  0.0829  219  GLY A CA  
1445  C  C   . GLY A 219 ? 0.6945 0.9056 0.4415 0.1630  0.0333  0.1117  219  GLY A C   
1446  O  O   . GLY A 219 ? 0.7977 1.0348 0.5183 0.1813  0.0318  0.1237  219  GLY A O   
1447  N  N   . ALA A 220 ? 0.5492 0.7212 0.3129 0.1570  0.0387  0.1229  220  ALA A N   
1448  C  CA  . ALA A 220 ? 0.6355 0.7906 0.3883 0.1717  0.0439  0.1501  220  ALA A CA  
1449  C  C   . ALA A 220 ? 0.5802 0.6873 0.3517 0.1601  0.0560  0.1608  220  ALA A C   
1450  O  O   . ALA A 220 ? 0.5677 0.6603 0.3592 0.1422  0.0586  0.1467  220  ALA A O   
1451  C  CB  . ALA A 220 ? 0.6325 0.8058 0.3876 0.1824  0.0283  0.1452  220  ALA A CB  
1452  N  N   . VAL A 221 ? 0.6308 0.7141 0.3959 0.1712  0.0633  0.1850  221  VAL A N   
1453  C  CA  . VAL A 221 ? 0.5971 0.6345 0.3795 0.1611  0.0756  0.1953  221  VAL A CA  
1454  C  C   . VAL A 221 ? 0.6712 0.6913 0.4623 0.1684  0.0696  0.2006  221  VAL A C   
1455  O  O   . VAL A 221 ? 0.7183 0.7308 0.4938 0.1862  0.0742  0.2228  221  VAL A O   
1456  C  CB  . VAL A 221 ? 0.5437 0.5600 0.3106 0.1661  0.0963  0.2223  221  VAL A CB  
1457  C  CG1 . VAL A 221 ? 0.5614 0.5348 0.3522 0.1489  0.1094  0.2246  221  VAL A CG1 
1458  C  CG2 . VAL A 221 ? 0.5588 0.6022 0.3076 0.1664  0.1020  0.2212  221  VAL A CG2 
1459  N  N   . VAL A 222 ? 0.6329 0.6462 0.4482 0.1557  0.0600  0.1808  222  VAL A N   
1460  C  CA  . VAL A 222 ? 0.6823 0.6859 0.5064 0.1625  0.0528  0.1817  222  VAL A CA  
1461  C  C   . VAL A 222 ? 0.6259 0.6166 0.4766 0.1453  0.0460  0.1605  222  VAL A C   
1462  O  O   . VAL A 222 ? 0.6553 0.6565 0.5157 0.1312  0.0412  0.1413  222  VAL A O   
1463  C  CB  . VAL A 222 ? 0.7004 0.7440 0.5113 0.1800  0.0386  0.1792  222  VAL A CB  
1464  C  CG1 . VAL A 222 ? 0.6298 0.7072 0.4496 0.1692  0.0248  0.1510  222  VAL A CG1 
1465  C  CG2 . VAL A 222 ? 0.6190 0.6534 0.4362 0.1918  0.0338  0.1857  222  VAL A CG2 
1466  N  N   . ALA A 223 ? 0.4818 0.4496 0.3428 0.1479  0.0458  0.1645  223  ALA A N   
1467  C  CA  . ALA A 223 ? 0.5283 0.4836 0.4113 0.1343  0.0399  0.1469  223  ALA A CA  
1468  C  C   . ALA A 223 ? 0.6302 0.6092 0.5162 0.1417  0.0264  0.1371  223  ALA A C   
1469  O  O   . ALA A 223 ? 0.4016 0.3787 0.2837 0.1566  0.0257  0.1482  223  ALA A O   
1470  C  CB  . ALA A 223 ? 0.4864 0.3998 0.3802 0.1304  0.0501  0.1556  223  ALA A CB  
1471  N  N   . SER A 224 ? 0.5381 0.5392 0.4321 0.1314  0.0166  0.1162  224  SER A N   
1472  C  CA  . SER A 224 ? 0.3092 0.3386 0.2080 0.1352  0.0045  0.1038  224  SER A CA  
1473  C  C   . SER A 224 ? 0.3928 0.4085 0.3108 0.1221  0.0011  0.0887  224  SER A C   
1474  O  O   . SER A 224 ? 0.4855 0.4841 0.4118 0.1074  0.0034  0.0798  224  SER A O   
1475  C  CB  . SER A 224 ? 0.4932 0.5607 0.3858 0.1334  -0.0031 0.0904  224  SER A CB  
1476  O  OG  . SER A 224 ? 0.6994 0.7976 0.5988 0.1359  -0.0143 0.0769  224  SER A OG  
1477  N  N   . TYR A 225 ? 0.4931 0.5186 0.4176 0.1283  -0.0045 0.0857  225  TYR A N   
1478  C  CA  . TYR A 225 ? 0.3657 0.3776 0.3061 0.1180  -0.0062 0.0740  225  TYR A CA  
1479  C  C   . TYR A 225 ? 0.3965 0.4409 0.3444 0.1192  -0.0151 0.0612  225  TYR A C   
1480  O  O   . TYR A 225 ? 0.5265 0.6028 0.4682 0.1310  -0.0203 0.0632  225  TYR A O   
1481  C  CB  . TYR A 225 ? 0.4661 0.4478 0.4093 0.1244  0.0000  0.0856  225  TYR A CB  
1482  C  CG  . TYR A 225 ? 0.3491 0.3399 0.2844 0.1449  0.0004  0.1007  225  TYR A CG  
1483  C  CD1 . TYR A 225 ? 0.4567 0.4402 0.3773 0.1565  0.0067  0.1193  225  TYR A CD1 
1484  C  CD2 . TYR A 225 ? 0.3716 0.3782 0.3141 0.1535  -0.0048 0.0971  225  TYR A CD2 
1485  C  CE1 . TYR A 225 ? 0.5760 0.5659 0.4877 0.1777  0.0073  0.1350  225  TYR A CE1 
1486  C  CE2 . TYR A 225 ? 0.5954 0.6113 0.5310 0.1746  -0.0050 0.1110  225  TYR A CE2 
1487  C  CZ  . TYR A 225 ? 0.6706 0.6771 0.5900 0.1873  0.0008  0.1305  225  TYR A CZ  
1488  O  OH  . TYR A 225 ? 0.7331 0.7472 0.6440 0.2106  0.0009  0.1463  225  TYR A OH  
1489  N  N   . PRO A 226 ? 0.2997 0.3375 0.2611 0.1073  -0.0164 0.0481  226  PRO A N   
1490  C  CA  . PRO A 226 ? 0.3730 0.4384 0.3457 0.1046  -0.0225 0.0342  226  PRO A CA  
1491  C  C   . PRO A 226 ? 0.4282 0.5145 0.4030 0.1210  -0.0254 0.0403  226  PRO A C   
1492  O  O   . PRO A 226 ? 0.4727 0.5418 0.4418 0.1339  -0.0214 0.0555  226  PRO A O   
1493  C  CB  . PRO A 226 ? 0.4655 0.5063 0.4487 0.0909  -0.0192 0.0259  226  PRO A CB  
1494  C  CG  . PRO A 226 ? 0.5759 0.5860 0.5535 0.0833  -0.0147 0.0294  226  PRO A CG  
1495  C  CD  . PRO A 226 ? 0.4169 0.4200 0.3831 0.0949  -0.0114 0.0455  226  PRO A CD  
1496  N  N   . TYR A 227 ? 0.3380 0.4616 0.3223 0.1207  -0.0320 0.0277  227  TYR A N   
1497  C  CA  . TYR A 227 ? 0.2689 0.4123 0.2604 0.1057  -0.0358 0.0092  227  TYR A CA  
1498  C  C   . TYR A 227 ? 0.3546 0.5273 0.3352 0.1121  -0.0415 0.0081  227  TYR A C   
1499  O  O   . TYR A 227 ? 0.2728 0.4589 0.2414 0.1303  -0.0438 0.0215  227  TYR A O   
1500  C  CB  . TYR A 227 ? 0.4494 0.6210 0.4593 0.1007  -0.0391 -0.0058 227  TYR A CB  
1501  C  CG  . TYR A 227 ? 0.4124 0.5601 0.4333 0.0917  -0.0329 -0.0083 227  TYR A CG  
1502  C  CD1 . TYR A 227 ? 0.2140 0.3327 0.2365 0.0748  -0.0278 -0.0142 227  TYR A CD1 
1503  C  CD2 . TYR A 227 ? 0.4018 0.5584 0.4308 0.1012  -0.0321 -0.0051 227  TYR A CD2 
1504  C  CE1 . TYR A 227 ? 0.1764 0.2752 0.2060 0.0678  -0.0221 -0.0159 227  TYR A CE1 
1505  C  CE2 . TYR A 227 ? 0.3853 0.5223 0.4227 0.0934  -0.0258 -0.0078 227  TYR A CE2 
1506  C  CZ  . TYR A 227 ? 0.4140 0.5222 0.4506 0.0767  -0.0208 -0.0129 227  TYR A CZ  
1507  O  OH  . TYR A 227 ? 0.5134 0.6030 0.5552 0.0702  -0.0144 -0.0147 227  TYR A OH  
1508  N  N   . ASP A 228 ? 0.4417 0.6240 0.4256 0.0981  -0.0435 -0.0078 228  ASP A N   
1509  C  CA  . ASP A 228 ? 0.2986 0.5103 0.2723 0.1020  -0.0489 -0.0131 228  ASP A CA  
1510  C  C   . ASP A 228 ? 0.3469 0.6079 0.3320 0.1025  -0.0579 -0.0308 228  ASP A C   
1511  O  O   . ASP A 228 ? 0.4372 0.7321 0.4141 0.1088  -0.0644 -0.0369 228  ASP A O   
1512  C  CB  . ASP A 228 ? 0.4169 0.6114 0.3886 0.0868  -0.0456 -0.0226 228  ASP A CB  
1513  C  CG  . ASP A 228 ? 0.6235 0.7836 0.5806 0.0898  -0.0385 -0.0056 228  ASP A CG  
1514  O  OD1 . ASP A 228 ? 0.6320 0.7845 0.5781 0.1041  -0.0360 0.0135  228  ASP A OD1 
1515  O  OD2 . ASP A 228 ? 0.5944 0.7350 0.5521 0.0780  -0.0348 -0.0118 228  ASP A OD2 
1516  N  N   . ASN A 229 ? 0.3467 0.6137 0.3513 0.0956  -0.0579 -0.0401 229  ASN A N   
1517  C  CA  . ASN A 229 ? 0.4743 0.7898 0.4949 0.0938  -0.0656 -0.0592 229  ASN A CA  
1518  C  C   . ASN A 229 ? 0.4547 0.7802 0.4929 0.0963  -0.0650 -0.0596 229  ASN A C   
1519  O  O   . ASN A 229 ? 0.3058 0.5978 0.3425 0.0993  -0.0583 -0.0455 229  ASN A O   
1520  C  CB  . ASN A 229 ? 0.3170 0.6388 0.3503 0.0720  -0.0653 -0.0835 229  ASN A CB  
1521  C  CG  . ASN A 229 ? 0.3752 0.6640 0.4242 0.0532  -0.0564 -0.0894 229  ASN A CG  
1522  O  OD1 . ASN A 229 ? 0.3003 0.5616 0.3497 0.0557  -0.0507 -0.0761 229  ASN A OD1 
1523  N  ND2 . ASN A 229 ? 0.3450 0.6356 0.4063 0.0346  -0.0546 -0.1096 229  ASN A ND2 
1524  N  N   . SER A 230 ? 0.4062 0.7796 0.4618 0.0951  -0.0717 -0.0772 230  SER A N   
1525  C  CA  . SER A 230 ? 0.3492 0.7386 0.4242 0.0973  -0.0709 -0.0798 230  SER A CA  
1526  C  C   . SER A 230 ? 0.2165 0.6477 0.3185 0.0819  -0.0739 -0.1070 230  SER A C   
1527  O  O   . SER A 230 ? 0.2752 0.7274 0.3798 0.0723  -0.0785 -0.1241 230  SER A O   
1528  C  CB  . SER A 230 ? 0.2300 0.6425 0.2965 0.1249  -0.0772 -0.0642 230  SER A CB  
1529  O  OG  . SER A 230 ? 0.3023 0.7666 0.3659 0.1361  -0.0891 -0.0726 230  SER A OG  
1530  N  N   . LEU A 231 ? 0.2648 0.7078 0.3878 0.0789  -0.0703 -0.1117 231  LEU A N   
1531  C  CA  . LEU A 231 ? 0.4633 0.9527 0.6162 0.0656  -0.0726 -0.1374 231  LEU A CA  
1532  C  C   . LEU A 231 ? 0.5412 1.0950 0.6978 0.0806  -0.0875 -0.1481 231  LEU A C   
1533  O  O   . LEU A 231 ? 0.5625 1.1573 0.7391 0.0677  -0.0922 -0.1738 231  LEU A O   
1534  C  CB  . LEU A 231 ? 0.4425 0.9332 0.6162 0.0621  -0.0647 -0.1376 231  LEU A CB  
1535  C  CG  . LEU A 231 ? 0.3713 0.8208 0.5547 0.0393  -0.0497 -0.1402 231  LEU A CG  
1536  C  CD1 . LEU A 231 ? 0.3786 0.8312 0.5751 0.0441  -0.0429 -0.1347 231  LEU A CD1 
1537  C  CD2 . LEU A 231 ? 0.3035 0.7670 0.5090 0.0128  -0.0458 -0.1656 231  LEU A CD2 
1538  N  N   . ALA A 232 ? 0.4839 1.0468 0.6214 0.1084  -0.0946 -0.1287 232  ALA A N   
1539  C  CA  . ALA A 232 ? 0.4552 1.0780 0.5905 0.1270  -0.1095 -0.1352 232  ALA A CA  
1540  C  C   . ALA A 232 ? 0.5206 1.1537 0.6428 0.1203  -0.1156 -0.1469 232  ALA A C   
1541  O  O   . ALA A 232 ? 0.4558 1.1458 0.5845 0.1244  -0.1276 -0.1653 232  ALA A O   
1542  C  CB  . ALA A 232 ? 0.2587 0.8788 0.3715 0.1598  -0.1138 -0.1076 232  ALA A CB  
1543  N  N   . HIS A 233 ? 0.5902 1.1700 0.6946 0.1101  -0.1073 -0.1375 233  HIS A N   
1544  C  CA  . HIS A 233 ? 0.5242 1.1061 0.6124 0.1056  -0.1111 -0.1453 233  HIS A CA  
1545  C  C   . HIS A 233 ? 0.4801 1.1034 0.5467 0.1316  -0.1238 -0.1384 233  HIS A C   
1546  O  O   . HIS A 233 ? 0.4942 1.1642 0.5632 0.1306  -0.1338 -0.1591 233  HIS A O   
1547  C  CB  . HIS A 233 ? 0.3525 0.9529 0.4645 0.0789  -0.1109 -0.1782 233  HIS A CB  
1548  C  CG  . HIS A 233 ? 0.3927 0.9417 0.5174 0.0541  -0.0966 -0.1810 233  HIS A CG  
1549  N  ND1 . HIS A 233 ? 0.5273 1.0789 0.6809 0.0386  -0.0900 -0.1924 233  HIS A ND1 
1550  C  CD2 . HIS A 233 ? 0.4138 0.9077 0.5249 0.0442  -0.0873 -0.1720 233  HIS A CD2 
1551  C  CE1 . HIS A 233 ? 0.5589 1.0579 0.7140 0.0205  -0.0772 -0.1895 233  HIS A CE1 
1552  N  NE2 . HIS A 233 ? 0.4457 0.9097 0.5757 0.0241  -0.0761 -0.1776 233  HIS A NE2 
1553  N  N   . ASN A 234 ? 0.5319 1.1365 0.5768 0.1553  -0.1228 -0.1089 234  ASN A N   
1554  C  CA  . ASN A 234 ? 0.5341 1.1674 0.5524 0.1830  -0.1322 -0.0950 234  ASN A CA  
1555  C  C   . ASN A 234 ? 0.4684 1.0780 0.4589 0.1814  -0.1292 -0.0880 234  ASN A C   
1556  O  O   . ASN A 234 ? 0.4311 0.9876 0.4176 0.1664  -0.1178 -0.0813 234  ASN A O   
1557  C  CB  . ASN A 234 ? 0.5484 1.1636 0.5548 0.2083  -0.1297 -0.0648 234  ASN A CB  
1558  C  CG  . ASN A 234 ? 0.5291 1.1655 0.5639 0.2104  -0.1313 -0.0715 234  ASN A CG  
1559  O  OD1 . ASN A 234 ? 0.4598 1.1519 0.5174 0.2067  -0.1406 -0.0956 234  ASN A OD1 
1560  N  ND2 . ASN A 234 ? 0.4129 1.0065 0.4474 0.2162  -0.1217 -0.0514 234  ASN A ND2 
1561  N  N   . GLU A 235 ? 0.6106 1.2619 0.5818 0.1972  -0.1393 -0.0903 235  GLU A N   
1562  C  CA  . GLU A 235 ? 0.6281 1.2612 0.5717 0.1971  -0.1358 -0.0837 235  GLU A CA  
1563  C  C   . GLU A 235 ? 0.6373 1.2126 0.5578 0.2071  -0.1235 -0.0488 235  GLU A C   
1564  O  O   . GLU A 235 ? 0.5449 1.0777 0.4584 0.1932  -0.1134 -0.0449 235  GLU A O   
1565  C  CB  . GLU A 235 ? 0.5694 1.2607 0.4924 0.2164  -0.1489 -0.0894 235  GLU A CB  
1566  C  CG  . GLU A 235 ? 0.6822 1.3581 0.5736 0.2192  -0.1443 -0.0807 235  GLU A CG  
1567  C  CD  . GLU A 235 ? 0.8823 1.6165 0.7483 0.2426  -0.1570 -0.0825 235  GLU A CD  
1568  O  OE1 . GLU A 235 ? 1.1135 1.8592 0.9646 0.2374  -0.1578 -0.0945 235  GLU A OE1 
1569  O  OE2 . GLU A 235 ? 0.6848 1.4549 0.5451 0.2673  -0.1665 -0.0724 235  GLU A OE2 
1570  N  N   . CYS A 236 ? 0.6730 1.2468 0.5835 0.2312  -0.1239 -0.0244 236  CYS A N   
1571  C  CA  . CYS A 236 ? 0.6274 1.1497 0.5152 0.2426  -0.1121 0.0087  236  CYS A CA  
1572  C  C   . CYS A 236 ? 0.6410 1.1581 0.5262 0.2666  -0.1118 0.0318  236  CYS A C   
1573  O  O   . CYS A 236 ? 0.6615 1.2159 0.5637 0.2750  -0.1210 0.0223  236  CYS A O   
1574  C  CB  . CYS A 236 ? 0.7132 1.2432 0.5671 0.2556  -0.1117 0.0209  236  CYS A CB  
1575  S  SG  . CYS A 236 ? 0.7323 1.3100 0.5590 0.2954  -0.1222 0.0402  236  CYS A SG  
1576  N  N   . CYS A 237 ? 0.6232 1.0932 0.4880 0.2775  -0.1003 0.0617  237  CYS A N   
1577  C  CA  . CYS A 237 ? 0.4568 0.9182 0.3101 0.3054  -0.0985 0.0887  237  CYS A CA  
1578  C  C   . CYS A 237 ? 0.4233 0.8849 0.3036 0.3060  -0.1003 0.0831  237  CYS A C   
1579  O  O   . CYS A 237 ? 0.4674 0.9448 0.3444 0.3315  -0.1044 0.0964  237  CYS A O   
1580  C  CB  . CYS A 237 ? 0.5592 1.0725 0.3893 0.3347  -0.1098 0.0965  237  CYS A CB  
1581  S  SG  . CYS A 237 ? 0.7235 1.2653 0.5272 0.3315  -0.1136 0.0884  237  CYS A SG  
1582  N  N   . GLU A 238 ? 0.4431 0.8877 0.3493 0.2789  -0.0968 0.0639  238  GLU A N   
1583  C  CA  . GLU A 238 ? 0.4767 0.9170 0.4080 0.2771  -0.0960 0.0587  238  GLU A CA  
1584  C  C   . GLU A 238 ? 0.5739 0.9593 0.5179 0.2523  -0.0837 0.0560  238  GLU A C   
1585  O  O   . GLU A 238 ? 0.5459 0.9278 0.5006 0.2272  -0.0828 0.0371  238  GLU A O   
1586  C  CB  . GLU A 238 ? 0.5737 1.0755 0.5296 0.2726  -0.1088 0.0309  238  GLU A CB  
1587  C  CG  . GLU A 238 ? 0.7286 1.2642 0.6948 0.2966  -0.1157 0.0351  238  GLU A CG  
1588  C  CD  . GLU A 238 ? 0.8838 1.4949 0.8656 0.2998  -0.1314 0.0105  238  GLU A CD  
1589  O  OE1 . GLU A 238 ? 0.9374 1.5840 0.9365 0.3141  -0.1377 0.0064  238  GLU A OE1 
1590  O  OE2 . GLU A 238 ? 0.8405 1.4770 0.8183 0.2881  -0.1374 -0.0061 238  GLU A OE2 
1591  N  N   . GLU A 239 ? 0.6640 1.0071 0.6060 0.2608  -0.0745 0.0748  239  GLU A N   
1592  C  CA  . GLU A 239 ? 0.5829 0.8742 0.5345 0.2411  -0.0633 0.0741  239  GLU A CA  
1593  C  C   . GLU A 239 ? 0.5530 0.8552 0.5316 0.2201  -0.0647 0.0501  239  GLU A C   
1594  O  O   . GLU A 239 ? 0.5599 0.8941 0.5553 0.2263  -0.0697 0.0412  239  GLU A O   
1595  C  CB  . GLU A 239 ? 0.7161 0.9675 0.6630 0.2566  -0.0544 0.0957  239  GLU A CB  
1596  C  CG  . GLU A 239 ? 0.9325 1.1505 0.8541 0.2690  -0.0467 0.1210  239  GLU A CG  
1597  C  CD  . GLU A 239 ? 1.0824 1.2563 1.0023 0.2817  -0.0365 0.1400  239  GLU A CD  
1598  O  OE1 . GLU A 239 ? 1.1077 1.2367 1.0154 0.2790  -0.0254 0.1553  239  GLU A OE1 
1599  O  OE2 . GLU A 239 ? 1.0578 1.2425 0.9901 0.2937  -0.0389 0.1384  239  GLU A OE2 
1600  N  N   . SER A 240 ? 0.4761 0.7517 0.4586 0.1957  -0.0594 0.0403  240  SER A N   
1601  C  CA  . SER A 240 ? 0.2792 0.5520 0.2836 0.1750  -0.0572 0.0218  240  SER A CA  
1602  C  C   . SER A 240 ? 0.3861 0.6030 0.3887 0.1653  -0.0463 0.0301  240  SER A C   
1603  O  O   . SER A 240 ? 0.3901 0.5826 0.3915 0.1471  -0.0423 0.0243  240  SER A O   
1604  C  CB  . SER A 240 ? 0.2700 0.5631 0.2814 0.1548  -0.0610 0.0008  240  SER A CB  
1605  O  OG  . SER A 240 ? 0.3702 0.6524 0.4005 0.1344  -0.0563 -0.0139 240  SER A OG  
1606  N  N   . LEU A 241 ? 0.4460 0.6441 0.4485 0.1786  -0.0418 0.0426  241  LEU A N   
1607  C  CA  . LEU A 241 ? 0.3140 0.4602 0.3121 0.1734  -0.0321 0.0518  241  LEU A CA  
1608  C  C   . LEU A 241 ? 0.4173 0.5458 0.4281 0.1533  -0.0276 0.0384  241  LEU A C   
1609  O  O   . LEU A 241 ? 0.4201 0.5742 0.4456 0.1439  -0.0301 0.0231  241  LEU A O   
1610  C  CB  . LEU A 241 ? 0.3151 0.4448 0.3090 0.1944  -0.0282 0.0684  241  LEU A CB  
1611  C  CG  . LEU A 241 ? 0.4651 0.6041 0.4422 0.2159  -0.0306 0.0860  241  LEU A CG  
1612  C  CD1 . LEU A 241 ? 0.4071 0.5300 0.3813 0.2388  -0.0262 0.1025  241  LEU A CD1 
1613  C  CD2 . LEU A 241 ? 0.3260 0.4382 0.2868 0.2084  -0.0261 0.0949  241  LEU A CD2 
1614  N  N   . THR A 242 ? 0.6288 0.7133 0.6335 0.1470  -0.0205 0.0446  242  THR A N   
1615  C  CA  . THR A 242 ? 0.4562 0.5191 0.4675 0.1294  -0.0161 0.0345  242  THR A CA  
1616  C  C   . THR A 242 ? 0.5597 0.6021 0.5748 0.1361  -0.0105 0.0382  242  THR A C   
1617  O  O   . THR A 242 ? 0.5960 0.6263 0.6059 0.1521  -0.0083 0.0505  242  THR A O   
1618  C  CB  . THR A 242 ? 0.5351 0.5672 0.5367 0.1178  -0.0134 0.0368  242  THR A CB  
1619  O  OG1 . THR A 242 ? 0.6341 0.6805 0.6388 0.1030  -0.0166 0.0245  242  THR A OG1 
1620  C  CG2 . THR A 242 ? 0.3683 0.3628 0.3697 0.1112  -0.0073 0.0371  242  THR A CG2 
1621  N  N   . PRO A 243 ? 0.4189 0.4567 0.4422 0.1247  -0.0073 0.0275  243  PRO A N   
1622  C  CA  . PRO A 243 ? 0.4066 0.4242 0.4317 0.1309  -0.0016 0.0296  243  PRO A CA  
1623  C  C   . PRO A 243 ? 0.4333 0.4107 0.4476 0.1344  0.0023  0.0396  243  PRO A C   
1624  O  O   . PRO A 243 ? 0.4733 0.4348 0.4875 0.1460  0.0063  0.0451  243  PRO A O   
1625  C  CB  . PRO A 243 ? 0.3501 0.3628 0.3801 0.1146  0.0020  0.0176  243  PRO A CB  
1626  C  CG  . PRO A 243 ? 0.4731 0.5137 0.5098 0.1031  -0.0017 0.0086  243  PRO A CG  
1627  C  CD  . PRO A 243 ? 0.4758 0.5235 0.5057 0.1064  -0.0076 0.0140  243  PRO A CD  
1628  N  N   . ASP A 244 ? 0.4198 0.3814 0.4268 0.1239  0.0017  0.0407  244  ASP A N   
1629  C  CA  . ASP A 244 ? 0.4346 0.3604 0.4344 0.1238  0.0059  0.0480  244  ASP A CA  
1630  C  C   . ASP A 244 ? 0.4782 0.4022 0.4709 0.1341  0.0062  0.0618  244  ASP A C   
1631  O  O   . ASP A 244 ? 0.5990 0.5019 0.5862 0.1285  0.0090  0.0666  244  ASP A O   
1632  C  CB  . ASP A 244 ? 0.4699 0.3793 0.4672 0.1067  0.0058  0.0407  244  ASP A CB  
1633  C  CG  . ASP A 244 ? 0.6700 0.5636 0.6691 0.1004  0.0084  0.0318  244  ASP A CG  
1634  O  OD1 . ASP A 244 ? 0.8146 0.6842 0.8127 0.1045  0.0124  0.0335  244  ASP A OD1 
1635  O  OD2 . ASP A 244 ? 0.6123 0.5171 0.6135 0.0916  0.0073  0.0232  244  ASP A OD2 
1636  N  N   . ASP A 245 ? 0.4334 0.3802 0.4261 0.1498  0.0039  0.0688  245  ASP A N   
1637  C  CA  . ASP A 245 ? 0.5746 0.5234 0.5575 0.1615  0.0042  0.0836  245  ASP A CA  
1638  C  C   . ASP A 245 ? 0.5893 0.4978 0.5663 0.1663  0.0130  0.0965  245  ASP A C   
1639  O  O   . ASP A 245 ? 0.6052 0.5038 0.5736 0.1649  0.0160  0.1058  245  ASP A O   
1640  C  CB  . ASP A 245 ? 0.4633 0.4447 0.4462 0.1810  -0.0003 0.0895  245  ASP A CB  
1641  C  CG  . ASP A 245 ? 0.6510 0.6446 0.6207 0.1914  -0.0022 0.1027  245  ASP A CG  
1642  O  OD1 . ASP A 245 ? 0.8060 0.8134 0.7715 0.1803  -0.0059 0.0975  245  ASP A OD1 
1643  O  OD2 . ASP A 245 ? 0.7188 0.7069 0.6814 0.2111  0.0006  0.1185  245  ASP A OD2 
1644  N  N   . ARG A 246 ? 0.4689 0.3548 0.4512 0.1720  0.0182  0.0966  246  ARG A N   
1645  C  CA  . ARG A 246 ? 0.5696 0.4148 0.5493 0.1747  0.0277  0.1063  246  ARG A CA  
1646  C  C   . ARG A 246 ? 0.6272 0.4530 0.6060 0.1559  0.0303  0.1024  246  ARG A C   
1647  O  O   . ARG A 246 ? 0.6875 0.4988 0.6605 0.1561  0.0359  0.1139  246  ARG A O   
1648  C  CB  . ARG A 246 ? 0.4248 0.2483 0.4125 0.1788  0.0322  0.1004  246  ARG A CB  
1649  C  CG  . ARG A 246 ? 0.6103 0.4542 0.6016 0.1972  0.0300  0.1021  246  ARG A CG  
1650  C  CD  . ARG A 246 ? 0.8577 0.6847 0.8574 0.1978  0.0339  0.0913  246  ARG A CD  
1651  N  NE  . ARG A 246 ? 1.0602 0.8541 1.0602 0.2122  0.0428  0.1007  246  ARG A NE  
1652  C  CZ  . ARG A 246 ? 1.2350 1.0082 1.2406 0.2116  0.0485  0.0912  246  ARG A CZ  
1653  N  NH1 . ARG A 246 ? 1.2789 1.0602 1.2891 0.1998  0.0456  0.0739  246  ARG A NH1 
1654  N  NH2 . ARG A 246 ? 1.3098 1.0528 1.3157 0.2235  0.0575  0.0992  246  ARG A NH2 
1655  N  N   . VAL A 247 ? 0.4729 0.2998 0.4576 0.1404  0.0268  0.0865  247  VAL A N   
1656  C  CA  . VAL A 247 ? 0.5665 0.3806 0.5516 0.1226  0.0284  0.0803  247  VAL A CA  
1657  C  C   . VAL A 247 ? 0.5005 0.3284 0.4792 0.1207  0.0262  0.0873  247  VAL A C   
1658  O  O   . VAL A 247 ? 0.4845 0.2968 0.4618 0.1146  0.0315  0.0923  247  VAL A O   
1659  C  CB  . VAL A 247 ? 0.5128 0.3330 0.5021 0.1081  0.0236  0.0629  247  VAL A CB  
1660  C  CG1 . VAL A 247 ? 0.3198 0.1369 0.3092 0.0924  0.0229  0.0572  247  VAL A CG1 
1661  C  CG2 . VAL A 247 ? 0.4309 0.2355 0.4243 0.1071  0.0271  0.0549  247  VAL A CG2 
1662  N  N   . PHE A 248 ? 0.5877 0.4486 0.5631 0.1246  0.0191  0.0858  248  PHE A N   
1663  C  CA  . PHE A 248 ? 0.5531 0.4327 0.5214 0.1219  0.0166  0.0889  248  PHE A CA  
1664  C  C   . PHE A 248 ? 0.5334 0.4039 0.4923 0.1328  0.0234  0.1071  248  PHE A C   
1665  O  O   . PHE A 248 ? 0.5271 0.3912 0.4817 0.1262  0.0274  0.1112  248  PHE A O   
1666  C  CB  . PHE A 248 ? 0.3704 0.2886 0.3385 0.1239  0.0078  0.0816  248  PHE A CB  
1667  C  CG  . PHE A 248 ? 0.4284 0.3542 0.4020 0.1076  0.0032  0.0656  248  PHE A CG  
1668  C  CD1 . PHE A 248 ? 0.4846 0.4043 0.4559 0.0966  0.0039  0.0627  248  PHE A CD1 
1669  C  CD2 . PHE A 248 ? 0.3489 0.2861 0.3302 0.1037  -0.0005 0.0543  248  PHE A CD2 
1670  C  CE1 . PHE A 248 ? 0.5535 0.4771 0.5293 0.0835  0.0003  0.0491  248  PHE A CE1 
1671  C  CE2 . PHE A 248 ? 0.4151 0.3549 0.4003 0.0894  -0.0030 0.0416  248  PHE A CE2 
1672  C  CZ  . PHE A 248 ? 0.2766 0.2087 0.2587 0.0800  -0.0029 0.0393  248  PHE A CZ  
1673  N  N   . LYS A 249 ? 0.5219 0.3907 0.4775 0.1502  0.0256  0.1187  249  LYS A N   
1674  C  CA  . LYS A 249 ? 0.4229 0.2786 0.3676 0.1635  0.0337  0.1391  249  LYS A CA  
1675  C  C   . LYS A 249 ? 0.5457 0.3603 0.4938 0.1542  0.0457  0.1442  249  LYS A C   
1676  O  O   . LYS A 249 ? 0.5710 0.3758 0.5105 0.1559  0.0537  0.1582  249  LYS A O   
1677  C  CB  . LYS A 249 ? 0.4090 0.2673 0.3508 0.1854  0.0339  0.1499  249  LYS A CB  
1678  C  CG  . LYS A 249 ? 0.4536 0.3517 0.3840 0.2014  0.0263  0.1572  249  LYS A CG  
1679  C  CD  . LYS A 249 ? 0.4488 0.3597 0.3804 0.2231  0.0231  0.1627  249  LYS A CD  
1680  C  CE  . LYS A 249 ? 0.4336 0.3926 0.3558 0.2373  0.0129  0.1656  249  LYS A CE  
1681  N  NZ  . LYS A 249 ? 0.6499 0.6366 0.5804 0.2527  0.0054  0.1610  249  LYS A NZ  
1682  N  N   . GLN A 250 ? 0.5672 0.3597 0.5280 0.1439  0.0472  0.1321  250  GLN A N   
1683  C  CA  . GLN A 250 ? 0.5942 0.3516 0.5625 0.1325  0.0575  0.1320  250  GLN A CA  
1684  C  C   . GLN A 250 ? 0.5430 0.3066 0.5126 0.1161  0.0573  0.1263  250  GLN A C   
1685  O  O   . GLN A 250 ? 0.5506 0.2964 0.5208 0.1109  0.0674  0.1344  250  GLN A O   
1686  C  CB  . GLN A 250 ? 0.4975 0.2413 0.4784 0.1240  0.0581  0.1154  250  GLN A CB  
1687  C  CG  . GLN A 250 ? 0.6120 0.3262 0.6032 0.1109  0.0684  0.1114  250  GLN A CG  
1688  C  CD  . GLN A 250 ? 0.7078 0.4054 0.7092 0.1077  0.0703  0.0985  250  GLN A CD  
1689  O  OE1 . GLN A 250 ? 0.8994 0.5931 0.8989 0.1209  0.0705  0.1012  250  GLN A OE1 
1690  N  NE2 . GLN A 250 ? 0.6285 0.3173 0.6411 0.0913  0.0714  0.0841  250  GLN A NE2 
1691  N  N   . LEU A 251 ? 0.4484 0.2373 0.4191 0.1082  0.0467  0.1123  251  LEU A N   
1692  C  CA  . LEU A 251 ? 0.4590 0.2575 0.4309 0.0949  0.0454  0.1060  251  LEU A CA  
1693  C  C   . LEU A 251 ? 0.4504 0.2606 0.4102 0.1005  0.0501  0.1203  251  LEU A C   
1694  O  O   . LEU A 251 ? 0.6232 0.4221 0.5845 0.0932  0.0586  0.1249  251  LEU A O   
1695  C  CB  . LEU A 251 ? 0.5817 0.4045 0.5553 0.0885  0.0337  0.0902  251  LEU A CB  
1696  C  CG  . LEU A 251 ? 0.6225 0.4346 0.6055 0.0818  0.0301  0.0761  251  LEU A CG  
1697  C  CD1 . LEU A 251 ? 0.6058 0.4388 0.5886 0.0772  0.0204  0.0638  251  LEU A CD1 
1698  C  CD2 . LEU A 251 ? 0.3897 0.1850 0.3824 0.0685  0.0352  0.0683  251  LEU A CD2 
1699  N  N   . ALA A 252 ? 0.5299 0.3653 0.4781 0.1136  0.0445  0.1264  252  ALA A N   
1700  C  CA  . ALA A 252 ? 0.6143 0.4652 0.5474 0.1218  0.0478  0.1401  252  ALA A CA  
1701  C  C   . ALA A 252 ? 0.6427 0.4654 0.5703 0.1276  0.0626  0.1602  252  ALA A C   
1702  O  O   . ALA A 252 ? 0.7013 0.5257 0.6207 0.1257  0.0701  0.1693  252  ALA A O   
1703  C  CB  . ALA A 252 ? 0.5391 0.4221 0.4614 0.1377  0.0387  0.1432  252  ALA A CB  
1704  N  N   . HIS A 253 ? 0.5178 0.3137 0.4499 0.1348  0.0680  0.1671  253  HIS A N   
1705  C  CA  . HIS A 253 ? 0.5479 0.3118 0.4757 0.1408  0.0838  0.1871  253  HIS A CA  
1706  C  C   . HIS A 253 ? 0.6435 0.3816 0.5850 0.1216  0.0944  0.1819  253  HIS A C   
1707  O  O   . HIS A 253 ? 0.6788 0.4008 0.6158 0.1206  0.1085  0.1969  253  HIS A O   
1708  C  CB  . HIS A 253 ? 0.5291 0.2697 0.4590 0.1546  0.0870  0.1946  253  HIS A CB  
1709  C  CG  . HIS A 253 ? 0.6988 0.4536 0.6107 0.1795  0.0855  0.2132  253  HIS A CG  
1710  N  ND1 . HIS A 253 ? 0.6435 0.4150 0.5557 0.1938  0.0753  0.2095  253  HIS A ND1 
1711  C  CD2 . HIS A 253 ? 0.7463 0.5032 0.6389 0.1936  0.0928  0.2357  253  HIS A CD2 
1712  C  CE1 . HIS A 253 ? 0.5883 0.3732 0.4833 0.2162  0.0752  0.2281  253  HIS A CE1 
1713  N  NE2 . HIS A 253 ? 0.8251 0.6008 0.7064 0.2171  0.0857  0.2449  253  HIS A NE2 
1714  N  N   . THR A 254 ? 0.4688 0.2046 0.4273 0.1065  0.0881  0.1608  254  THR A N   
1715  C  CA  . THR A 254 ? 0.5053 0.2240 0.4795 0.0876  0.0955  0.1519  254  THR A CA  
1716  C  C   . THR A 254 ? 0.5647 0.2988 0.5338 0.0810  0.1004  0.1565  254  THR A C   
1717  O  O   . THR A 254 ? 0.6260 0.3421 0.6020 0.0722  0.1143  0.1625  254  THR A O   
1718  C  CB  . THR A 254 ? 0.4519 0.1772 0.4408 0.0747  0.0843  0.1277  254  THR A CB  
1719  O  OG1 . THR A 254 ? 0.5232 0.2374 0.5160 0.0805  0.0802  0.1217  254  THR A OG1 
1720  C  CG2 . THR A 254 ? 0.4024 0.1130 0.4087 0.0569  0.0913  0.1180  254  THR A CG2 
1721  N  N   . TYR A 255 ? 0.5418 0.3099 0.5001 0.0845  0.0897  0.1525  255  TYR A N   
1722  C  CA  . TYR A 255 ? 0.5553 0.3413 0.5078 0.0792  0.0935  0.1546  255  TYR A CA  
1723  C  C   . TYR A 255 ? 0.6000 0.3832 0.5337 0.0915  0.1058  0.1791  255  TYR A C   
1724  O  O   . TYR A 255 ? 0.6316 0.4061 0.5659 0.0849  0.1197  0.1877  255  TYR A O   
1725  C  CB  . TYR A 255 ? 0.4955 0.3172 0.4426 0.0791  0.0786  0.1408  255  TYR A CB  
1726  C  CG  . TYR A 255 ? 0.5729 0.4113 0.5198 0.0701  0.0815  0.1359  255  TYR A CG  
1727  C  CD1 . TYR A 255 ? 0.6957 0.5474 0.6254 0.0775  0.0891  0.1504  255  TYR A CD1 
1728  C  CD2 . TYR A 255 ? 0.4176 0.2595 0.3808 0.0557  0.0768  0.1172  255  TYR A CD2 
1729  C  CE1 . TYR A 255 ? 0.6689 0.5371 0.5985 0.0697  0.0926  0.1451  255  TYR A CE1 
1730  C  CE2 . TYR A 255 ? 0.4936 0.3515 0.4580 0.0486  0.0798  0.1121  255  TYR A CE2 
1731  C  CZ  . TYR A 255 ? 0.5889 0.4599 0.5369 0.0552  0.0880  0.1256  255  TYR A CZ  
1732  O  OH  . TYR A 255 ? 0.4893 0.3774 0.4384 0.0488  0.0918  0.1198  255  TYR A OH  
1733  N  N   . SER A 256 ? 0.6023 0.3945 0.5193 0.1102  0.1012  0.1908  256  SER A N   
1734  C  CA  . SER A 256 ? 0.5882 0.3819 0.4832 0.1253  0.1110  0.2150  256  SER A CA  
1735  C  C   . SER A 256 ? 0.7407 0.4918 0.6389 0.1252  0.1307  0.2335  256  SER A C   
1736  O  O   . SER A 256 ? 0.7983 0.5418 0.6875 0.1245  0.1457  0.2493  256  SER A O   
1737  C  CB  . SER A 256 ? 0.6060 0.4216 0.4839 0.1470  0.1000  0.2221  256  SER A CB  
1738  O  OG  . SER A 256 ? 0.8137 0.6368 0.6668 0.1638  0.1075  0.2452  256  SER A OG  
1739  N  N   . ASP A 257 ? 0.7683 0.4908 0.6796 0.1255  0.1316  0.2310  257  ASP A N   
1740  C  CA  . ASP A 257 ? 0.6803 0.3583 0.5971 0.1251  0.1507  0.2465  257  ASP A CA  
1741  C  C   . ASP A 257 ? 0.7096 0.3742 0.6396 0.1044  0.1656  0.2444  257  ASP A C   
1742  O  O   . ASP A 257 ? 0.7781 0.4164 0.7041 0.1049  0.1852  0.2641  257  ASP A O   
1743  C  CB  . ASP A 257 ? 0.6075 0.2587 0.5416 0.1237  0.1481  0.2360  257  ASP A CB  
1744  C  CG  . ASP A 257 ? 0.8955 0.5510 0.8169 0.1472  0.1398  0.2446  257  ASP A CG  
1745  O  OD1 . ASP A 257 ? 0.9982 0.6816 0.8985 0.1639  0.1337  0.2563  257  ASP A OD1 
1746  O  OD2 . ASP A 257 ? 0.9824 0.6155 0.9153 0.1496  0.1392  0.2385  257  ASP A OD2 
1747  N  N   . ASN A 258 ? 0.6808 0.3643 0.6271 0.0866  0.1567  0.2209  258  ASN A N   
1748  C  CA  . ASN A 258 ? 0.6762 0.3539 0.6392 0.0665  0.1685  0.2148  258  ASN A CA  
1749  C  C   . ASN A 258 ? 0.7247 0.4295 0.6739 0.0660  0.1730  0.2220  258  ASN A C   
1750  O  O   . ASN A 258 ? 0.7464 0.4536 0.7099 0.0496  0.1816  0.2150  258  ASN A O   
1751  C  CB  . ASN A 258 ? 0.5724 0.2566 0.5606 0.0490  0.1572  0.1859  258  ASN A CB  
1752  C  CG  . ASN A 258 ? 0.7367 0.3872 0.7442 0.0427  0.1607  0.1781  258  ASN A CG  
1753  O  OD1 . ASN A 258 ? 0.7594 0.3833 0.7831 0.0305  0.1769  0.1798  258  ASN A OD1 
1754  N  ND2 . ASN A 258 ? 0.6804 0.3322 0.6868 0.0504  0.1465  0.1686  258  ASN A ND2 
1755  N  N   . HIS A 259 ? 0.8287 0.5561 0.7508 0.0843  0.1670  0.2346  259  HIS A N   
1756  C  CA  . HIS A 259 ? 0.7834 0.5403 0.6892 0.0861  0.1695  0.2398  259  HIS A CA  
1757  C  C   . HIS A 259 ? 0.7737 0.5203 0.6533 0.1027  0.1849  0.2708  259  HIS A C   
1758  O  O   . HIS A 259 ? 0.8901 0.6433 0.7486 0.1235  0.1780  0.2832  259  HIS A O   
1759  C  CB  . HIS A 259 ? 0.7611 0.5592 0.6567 0.0932  0.1479  0.2248  259  HIS A CB  
1760  C  CG  . HIS A 259 ? 0.8036 0.6341 0.6872 0.0917  0.1485  0.2225  259  HIS A CG  
1761  N  ND1 . HIS A 259 ? 0.7782 0.6161 0.6368 0.1031  0.1605  0.2441  259  HIS A ND1 
1762  C  CD2 . HIS A 259 ? 0.7525 0.6096 0.6447 0.0814  0.1390  0.2010  259  HIS A CD2 
1763  C  CE1 . HIS A 259 ? 0.6775 0.5468 0.5302 0.0992  0.1582  0.2346  259  HIS A CE1 
1764  N  NE2 . HIS A 259 ? 0.6664 0.5469 0.5400 0.0861  0.1453  0.2083  259  HIS A NE2 
1765  N  N   . PRO A 260 ? 0.8793 0.6104 0.7599 0.0941  0.2064  0.2840  260  PRO A N   
1766  C  CA  . PRO A 260 ? 0.8858 0.5968 0.7429 0.1079  0.2262  0.3168  260  PRO A CA  
1767  C  C   . PRO A 260 ? 0.8078 0.5495 0.6276 0.1327  0.2187  0.3323  260  PRO A C   
1768  O  O   . PRO A 260 ? 0.8785 0.6033 0.6752 0.1508  0.2300  0.3604  260  PRO A O   
1769  C  CB  . PRO A 260 ? 0.8181 0.5242 0.6842 0.0902  0.2472  0.3203  260  PRO A CB  
1770  C  CG  . PRO A 260 ? 0.8807 0.5876 0.7839 0.0659  0.2413  0.2907  260  PRO A CG  
1771  C  CD  . PRO A 260 ? 0.7767 0.5115 0.6817 0.0704  0.2134  0.2677  260  PRO A CD  
1772  N  N   . ILE A 261 ? 0.8259 0.6121 0.6399 0.1338  0.2002  0.3140  261  ILE A N   
1773  C  CA  . ILE A 261 ? 0.9074 0.7293 0.6873 0.1552  0.1923  0.3243  261  ILE A CA  
1774  C  C   . ILE A 261 ? 0.7536 0.5990 0.5291 0.1692  0.1680  0.3126  261  ILE A C   
1775  O  O   . ILE A 261 ? 0.7329 0.5913 0.4829 0.1928  0.1634  0.3287  261  ILE A O   
1776  C  CB  . ILE A 261 ? 0.9091 0.7681 0.6825 0.1472  0.1916  0.3125  261  ILE A CB  
1777  C  CG1 . ILE A 261 ? 0.7711 0.6132 0.5402 0.1394  0.2182  0.3307  261  ILE A CG1 
1778  C  CG2 . ILE A 261 ? 0.8136 0.7173 0.5564 0.1675  0.1768  0.3129  261  ILE A CG2 
1779  C  CD1 . ILE A 261 ? 0.8225 0.6980 0.5910 0.1288  0.2196  0.3166  261  ILE A CD1 
1780  N  N   . MET A 262 ? 0.6821 0.5342 0.4831 0.1548  0.1531  0.2848  262  MET A N   
1781  C  CA  . MET A 262 ? 0.6930 0.5630 0.4969 0.1633  0.1320  0.2710  262  MET A CA  
1782  C  C   . MET A 262 ? 0.7011 0.5437 0.5028 0.1786  0.1340  0.2873  262  MET A C   
1783  O  O   . MET A 262 ? 0.8236 0.6865 0.6124 0.1974  0.1218  0.2905  262  MET A O   
1784  C  CB  . MET A 262 ? 0.5956 0.4681 0.4285 0.1429  0.1204  0.2411  262  MET A CB  
1785  C  CG  . MET A 262 ? 0.4641 0.3587 0.3014 0.1483  0.0996  0.2242  262  MET A CG  
1786  S  SD  . MET A 262 ? 0.7691 0.6652 0.6358 0.1246  0.0891  0.1922  262  MET A SD  
1787  C  CE  . MET A 262 ? 0.4606 0.3840 0.3215 0.1156  0.0913  0.1833  262  MET A CE  
1788  N  N   . ARG A 263 ? 0.7675 0.5650 0.5833 0.1704  0.1498  0.2964  263  ARG A N   
1789  C  CA  . ARG A 263 ? 0.7495 0.5135 0.5647 0.1840  0.1555  0.3127  263  ARG A CA  
1790  C  C   . ARG A 263 ? 0.7582 0.5304 0.5414 0.2132  0.1577  0.3402  263  ARG A C   
1791  O  O   . ARG A 263 ? 0.9637 0.7208 0.7438 0.2303  0.1559  0.3506  263  ARG A O   
1792  C  CB  . ARG A 263 ? 0.8129 0.5271 0.6447 0.1695  0.1772  0.3210  263  ARG A CB  
1793  C  CG  . ARG A 263 ? 0.9792 0.6513 0.8153 0.1800  0.1852  0.3345  263  ARG A CG  
1794  C  CD  . ARG A 263 ? 1.1848 0.8107 1.0440 0.1597  0.2052  0.3344  263  ARG A CD  
1795  N  NE  . ARG A 263 ? 1.2729 0.8882 1.1231 0.1534  0.2264  0.3525  263  ARG A NE  
1796  C  CZ  . ARG A 263 ? 1.1256 0.7329 0.9968 0.1282  0.2375  0.3415  263  ARG A CZ  
1797  N  NH1 . ARG A 263 ? 0.9662 0.5754 0.8673 0.1079  0.2283  0.3126  263  ARG A NH1 
1798  N  NH2 . ARG A 263 ? 1.0889 0.6882 0.9509 0.1239  0.2582  0.3597  263  ARG A NH2 
1799  N  N   . LYS A 264 ? 0.9256 0.7228 0.6842 0.2203  0.1616  0.3516  264  LYS A N   
1800  C  CA  . LYS A 264 ? 1.0681 0.8727 0.7923 0.2493  0.1659  0.3807  264  LYS A CA  
1801  C  C   . LYS A 264 ? 0.9769 0.8273 0.6873 0.2708  0.1428  0.3742  264  LYS A C   
1802  O  O   . LYS A 264 ? 0.9861 0.8319 0.6833 0.2953  0.1408  0.3916  264  LYS A O   
1803  C  CB  . LYS A 264 ? 1.0244 0.8386 0.7254 0.2492  0.1804  0.3964  264  LYS A CB  
1804  C  CG  . LYS A 264 ? 1.0312 0.8013 0.7463 0.2289  0.2057  0.4052  264  LYS A CG  
1805  C  CD  . LYS A 264 ? 1.1334 0.9116 0.8229 0.2317  0.2230  0.4249  264  LYS A CD  
1806  C  CE  . LYS A 264 ? 1.2194 0.9496 0.9232 0.2136  0.2514  0.4381  264  LYS A CE  
1807  N  NZ  . LYS A 264 ? 1.3341 1.0119 1.0397 0.2236  0.2652  0.4608  264  LYS A NZ  
1808  N  N   . GLY A 265 ? 0.8727 0.7679 0.5869 0.2618  0.1260  0.3488  265  GLY A N   
1809  C  CA  . GLY A 265 ? 0.7589 0.6977 0.4700 0.2755  0.1033  0.3349  265  GLY A CA  
1810  C  C   . GLY A 265 ? 0.8101 0.7965 0.4899 0.2948  0.0955  0.3414  265  GLY A C   
1811  O  O   . GLY A 265 ? 0.8202 0.8479 0.4972 0.3070  0.0763  0.3292  265  GLY A O   
1812  N  N   . ASN A 266 ? 0.8328 0.8156 0.4897 0.2972  0.1104  0.3593  266  ASN A N   
1813  C  CA  . ASN A 266 ? 0.8367 0.8638 0.4587 0.3180  0.1051  0.3685  266  ASN A CA  
1814  C  C   . ASN A 266 ? 0.8636 0.9147 0.4785 0.3031  0.1081  0.3559  266  ASN A C   
1815  O  O   . ASN A 266 ? 0.9475 1.0157 0.5301 0.3167  0.1157  0.3728  266  ASN A O   
1816  C  CB  . ASN A 266 ? 0.9286 0.9335 0.5190 0.3445  0.1207  0.4086  266  ASN A CB  
1817  C  CG  . ASN A 266 ? 1.1062 1.0523 0.7015 0.3316  0.1484  0.4293  266  ASN A CG  
1818  O  OD1 . ASN A 266 ? 1.1156 1.0411 0.7384 0.3029  0.1549  0.4125  266  ASN A OD1 
1819  N  ND2 . ASN A 266 ? 1.1293 1.0483 0.6985 0.3531  0.1652  0.4658  266  ASN A ND2 
1820  N  N   . ASN A 267 ? 0.7038 0.7570 0.3478 0.2764  0.1023  0.3262  267  ASN A N   
1821  C  CA  . ASN A 267 ? 0.7084 0.7787 0.3513 0.2600  0.1065  0.3120  267  ASN A CA  
1822  C  C   . ASN A 267 ? 0.6995 0.8276 0.3335 0.2642  0.0866  0.2877  267  ASN A C   
1823  O  O   . ASN A 267 ? 0.6916 0.8438 0.3325 0.2714  0.0679  0.2739  267  ASN A O   
1824  C  CB  . ASN A 267 ? 0.7898 0.8311 0.4689 0.2303  0.1111  0.2930  267  ASN A CB  
1825  C  CG  . ASN A 267 ? 0.8561 0.8421 0.5510 0.2245  0.1266  0.3101  267  ASN A CG  
1826  O  OD1 . ASN A 267 ? 0.8632 0.8225 0.5432 0.2313  0.1462  0.3378  267  ASN A OD1 
1827  N  ND2 . ASN A 267 ? 0.7668 0.7351 0.4915 0.2117  0.1186  0.2934  267  ASN A ND2 
1828  N  N   . CYS A 268 ? 0.7917 0.9424 0.4115 0.2595  0.0915  0.2818  268  CYS A N   
1829  C  CA  . CYS A 268 ? 0.8176 1.0223 0.4293 0.2611  0.0747  0.2559  268  CYS A CA  
1830  C  C   . CYS A 268 ? 0.8783 1.1242 0.4723 0.2851  0.0564  0.2553  268  CYS A C   
1831  O  O   . CYS A 268 ? 0.8337 1.1162 0.4389 0.2809  0.0375  0.2262  268  CYS A O   
1832  C  CB  . CYS A 268 ? 0.6486 0.8564 0.2950 0.2360  0.0640  0.2201  268  CYS A CB  
1833  S  SG  . CYS A 268 ? 0.9055 1.0562 0.5899 0.2109  0.0748  0.2182  268  CYS A SG  
1834  N  N   . ASN A 269 ? 0.9225 1.1625 0.4899 0.3101  0.0624  0.2870  269  ASN A N   
1835  C  CA  . ASN A 269 ? 1.0075 1.2870 0.5579 0.3363  0.0451  0.2894  269  ASN A CA  
1836  C  C   . ASN A 269 ? 0.9718 1.2462 0.5520 0.3343  0.0308  0.2770  269  ASN A C   
1837  O  O   . ASN A 269 ? 0.8999 1.2095 0.4729 0.3543  0.0150  0.2752  269  ASN A O   
1838  C  CB  . ASN A 269 ? 1.0163 1.3596 0.5499 0.3421  0.0295  0.2662  269  ASN A CB  
1839  C  CG  . ASN A 269 ? 1.0827 1.4404 0.5761 0.3548  0.0422  0.2843  269  ASN A CG  
1840  O  OD1 . ASN A 269 ? 1.0586 1.4582 0.5409 0.3522  0.0352  0.2634  269  ASN A OD1 
1841  N  ND2 . ASN A 269 ? 1.1269 1.4492 0.5982 0.3685  0.0618  0.3231  269  ASN A ND2 
1842  N  N   . ASP A 270 ? 0.9106 1.1434 0.5239 0.3109  0.0365  0.2683  270  ASP A N   
1843  C  CA  . ASP A 270 ? 0.8492 1.0740 0.4914 0.3068  0.0252  0.2562  270  ASP A CA  
1844  C  C   . ASP A 270 ? 0.9628 1.1459 0.6029 0.3212  0.0355  0.2856  270  ASP A C   
1845  O  O   . ASP A 270 ? 0.9957 1.1402 0.6233 0.3233  0.0550  0.3115  270  ASP A O   
1846  C  CB  . ASP A 270 ? 0.7149 0.9175 0.3922 0.2756  0.0253  0.2310  270  ASP A CB  
1847  C  CG  . ASP A 270 ? 0.7736 1.0125 0.4562 0.2607  0.0155  0.2003  270  ASP A CG  
1848  O  OD1 . ASP A 270 ? 0.8523 1.1408 0.5231 0.2721  0.0012  0.1881  270  ASP A OD1 
1849  O  OD2 . ASP A 270 ? 0.7651 0.9835 0.4647 0.2380  0.0219  0.1874  270  ASP A OD2 
1850  N  N   . SER A 271 ? 0.8676 1.0585 0.5213 0.3307  0.0233  0.2809  271  SER A N   
1851  C  CA  . SER A 271 ? 0.8142 0.9639 0.4711 0.3433  0.0321  0.3045  271  SER A CA  
1852  C  C   . SER A 271 ? 0.8960 1.0257 0.5893 0.3266  0.0268  0.2855  271  SER A C   
1853  O  O   . SER A 271 ? 0.9843 1.1458 0.6905 0.3314  0.0104  0.2688  271  SER A O   
1854  C  CB  . SER A 271 ? 0.8697 1.0463 0.5028 0.3787  0.0244  0.3236  271  SER A CB  
1855  O  OG  . SER A 271 ? 0.9257 1.0610 0.5641 0.3916  0.0326  0.3446  271  SER A OG  
1856  N  N   . PHE A 272 ? 0.8377 0.9168 0.5477 0.3068  0.0411  0.2876  272  PHE A N   
1857  C  CA  . PHE A 272 ? 0.6508 0.7085 0.3935 0.2893  0.0376  0.2694  272  PHE A CA  
1858  C  C   . PHE A 272 ? 0.6583 0.6602 0.4078 0.2924  0.0527  0.2891  272  PHE A C   
1859  O  O   . PHE A 272 ? 0.6647 0.6270 0.4172 0.2787  0.0688  0.2973  272  PHE A O   
1860  C  CB  . PHE A 272 ? 0.5693 0.6226 0.3303 0.2591  0.0381  0.2458  272  PHE A CB  
1861  C  CG  . PHE A 272 ? 0.6922 0.7954 0.4545 0.2524  0.0225  0.2203  272  PHE A CG  
1862  C  CD1 . PHE A 272 ? 0.7276 0.8431 0.4817 0.2410  0.0255  0.2127  272  PHE A CD1 
1863  C  CD2 . PHE A 272 ? 0.6155 0.7529 0.3893 0.2564  0.0057  0.2025  272  PHE A CD2 
1864  C  CE1 . PHE A 272 ? 0.5548 0.7136 0.3116 0.2340  0.0119  0.1871  272  PHE A CE1 
1865  C  CE2 . PHE A 272 ? 0.5690 0.7503 0.3467 0.2481  -0.0074 0.1771  272  PHE A CE2 
1866  C  CZ  . PHE A 272 ? 0.5230 0.7137 0.2918 0.2370  -0.0044 0.1693  272  PHE A CZ  
1867  N  N   . SER A 273 ? 0.8207 0.8207 0.5739 0.3102  0.0476  0.2953  273  SER A N   
1868  C  CA  . SER A 273 ? 0.8735 0.8211 0.6327 0.3162  0.0614  0.3132  273  SER A CA  
1869  C  C   . SER A 273 ? 0.9284 0.8349 0.7129 0.2875  0.0705  0.2999  273  SER A C   
1870  O  O   . SER A 273 ? 0.9131 0.8289 0.7200 0.2714  0.0605  0.2747  273  SER A O   
1871  C  CB  . SER A 273 ? 0.8522 0.8103 0.6184 0.3364  0.0515  0.3132  273  SER A CB  
1872  O  OG  . SER A 273 ? 0.8823 0.7881 0.6578 0.3399  0.0645  0.3257  273  SER A OG  
1873  N  N   . GLY A 274 ? 0.8354 0.6975 0.6163 0.2816  0.0899  0.3170  274  GLY A N   
1874  C  CA  . GLY A 274 ? 0.7985 0.6222 0.6034 0.2557  0.0993  0.3052  274  GLY A CA  
1875  C  C   . GLY A 274 ? 0.7860 0.6285 0.5992 0.2312  0.0954  0.2847  274  GLY A C   
1876  O  O   . GLY A 274 ? 0.6667 0.4863 0.5006 0.2088  0.1001  0.2710  274  GLY A O   
1877  N  N   . GLY A 275 ? 0.6726 0.5586 0.4697 0.2366  0.0861  0.2815  275  GLY A N   
1878  C  CA  . GLY A 275 ? 0.6102 0.5160 0.4124 0.2165  0.0829  0.2633  275  GLY A CA  
1879  C  C   . GLY A 275 ? 0.6261 0.5513 0.4496 0.2016  0.0672  0.2333  275  GLY A C   
1880  O  O   . GLY A 275 ? 0.6567 0.5885 0.4898 0.1828  0.0656  0.2165  275  GLY A O   
1881  N  N   . ILE A 276 ? 0.6433 0.5772 0.4742 0.2105  0.0564  0.2272  276  ILE A N   
1882  C  CA  . ILE A 276 ? 0.6518 0.6051 0.5012 0.1977  0.0425  0.2006  276  ILE A CA  
1883  C  C   . ILE A 276 ? 0.6354 0.6326 0.4791 0.2130  0.0276  0.1947  276  ILE A C   
1884  O  O   . ILE A 276 ? 0.6873 0.6954 0.5151 0.2357  0.0273  0.2119  276  ILE A O   
1885  C  CB  . ILE A 276 ? 0.6037 0.5245 0.4740 0.1893  0.0446  0.1938  276  ILE A CB  
1886  C  CG1 . ILE A 276 ? 0.6071 0.5207 0.4743 0.2103  0.0447  0.2070  276  ILE A CG1 
1887  C  CG2 . ILE A 276 ? 0.6888 0.5677 0.5669 0.1749  0.0591  0.1984  276  ILE A CG2 
1888  C  CD1 . ILE A 276 ? 0.5800 0.4668 0.4667 0.2038  0.0456  0.1981  276  ILE A CD1 
1889  N  N   . THR A 277 ? 0.5682 0.5908 0.4256 0.2007  0.0157  0.1704  277  THR A N   
1890  C  CA  . THR A 277 ? 0.5686 0.6356 0.4263 0.2111  0.0015  0.1601  277  THR A CA  
1891  C  C   . THR A 277 ? 0.6249 0.7030 0.5046 0.1940  -0.0072 0.1344  277  THR A C   
1892  O  O   . THR A 277 ? 0.7709 0.8315 0.6610 0.1742  -0.0045 0.1226  277  THR A O   
1893  C  CB  . THR A 277 ? 0.5518 0.6602 0.3918 0.2179  -0.0048 0.1582  277  THR A CB  
1894  O  OG1 . THR A 277 ? 0.6201 0.7734 0.4623 0.2296  -0.0188 0.1482  277  THR A OG1 
1895  C  CG2 . THR A 277 ? 0.4234 0.5374 0.2692 0.1961  -0.0057 0.1391  277  THR A CG2 
1896  N  N   . ASN A 278 ? 0.6083 0.7168 0.4953 0.2027  -0.0172 0.1264  278  ASN A N   
1897  C  CA  . ASN A 278 ? 0.4002 0.5249 0.3073 0.1876  -0.0248 0.1025  278  ASN A CA  
1898  C  C   . ASN A 278 ? 0.6102 0.7704 0.5147 0.1792  -0.0323 0.0861  278  ASN A C   
1899  O  O   . ASN A 278 ? 0.7703 0.9634 0.6603 0.1930  -0.0376 0.0901  278  ASN A O   
1900  C  CB  . ASN A 278 ? 0.2817 0.4290 0.1985 0.2007  -0.0314 0.1005  278  ASN A CB  
1901  C  CG  . ASN A 278 ? 0.4630 0.6342 0.4002 0.1862  -0.0386 0.0762  278  ASN A CG  
1902  O  OD1 . ASN A 278 ? 0.5679 0.7832 0.5105 0.1930  -0.0480 0.0664  278  ASN A OD1 
1903  N  ND2 . ASN A 278 ? 0.3260 0.4692 0.2753 0.1663  -0.0339 0.0663  278  ASN A ND2 
1904  N  N   . GLY A 279 ? 0.4207 0.5740 0.3380 0.1577  -0.0326 0.0678  279  GLY A N   
1905  C  CA  . GLY A 279 ? 0.3934 0.5767 0.3103 0.1485  -0.0387 0.0499  279  GLY A CA  
1906  C  C   . GLY A 279 ? 0.5089 0.7442 0.4261 0.1594  -0.0500 0.0404  279  GLY A C   
1907  O  O   . GLY A 279 ? 0.3871 0.6515 0.2882 0.1698  -0.0543 0.0422  279  GLY A O   
1908  N  N   . ALA A 280 ? 0.4027 0.6520 0.3385 0.1572  -0.0547 0.0299  280  ALA A N   
1909  C  CA  . ALA A 280 ? 0.3723 0.6742 0.3144 0.1657  -0.0659 0.0176  280  ALA A CA  
1910  C  C   . ALA A 280 ? 0.4735 0.8009 0.3951 0.1923  -0.0706 0.0345  280  ALA A C   
1911  O  O   . ALA A 280 ? 0.5547 0.9270 0.4696 0.1991  -0.0798 0.0250  280  ALA A O   
1912  C  CB  . ALA A 280 ? 0.4010 0.7082 0.3658 0.1625  -0.0673 0.0096  280  ALA A CB  
1913  N  N   . HIS A 281 ? 0.5111 0.8097 0.4227 0.2080  -0.0640 0.0592  281  HIS A N   
1914  C  CA  . HIS A 281 ? 0.3902 0.7065 0.2807 0.2358  -0.0666 0.0794  281  HIS A CA  
1915  C  C   . HIS A 281 ? 0.4170 0.7430 0.2823 0.2405  -0.0661 0.0858  281  HIS A C   
1916  O  O   . HIS A 281 ? 0.5113 0.8763 0.3601 0.2604  -0.0737 0.0909  281  HIS A O   
1917  C  CB  . HIS A 281 ? 0.4947 0.7687 0.3792 0.2497  -0.0568 0.1052  281  HIS A CB  
1918  C  CG  . HIS A 281 ? 0.5941 0.8865 0.4596 0.2808  -0.0597 0.1262  281  HIS A CG  
1919  N  ND1 . HIS A 281 ? 0.6261 0.9057 0.4634 0.2950  -0.0534 0.1491  281  HIS A ND1 
1920  C  CD2 . HIS A 281 ? 0.6593 0.9838 0.5295 0.3017  -0.0681 0.1281  281  HIS A CD2 
1921  C  CE1 . HIS A 281 ? 0.5410 0.8416 0.3647 0.3241  -0.0577 0.1656  281  HIS A CE1 
1922  N  NE2 . HIS A 281 ? 0.6353 0.9645 0.4791 0.3293  -0.0674 0.1527  281  HIS A NE2 
1923  N  N   . TRP A 282 ? 0.4041 0.6970 0.2659 0.2234  -0.0570 0.0856  282  TRP A N   
1924  C  CA  . TRP A 282 ? 0.4848 0.7914 0.3260 0.2242  -0.0564 0.0863  282  TRP A CA  
1925  C  C   . TRP A 282 ? 0.5201 0.8823 0.3668 0.2206  -0.0702 0.0594  282  TRP A C   
1926  O  O   . TRP A 282 ? 0.4932 0.8997 0.3255 0.2394  -0.0794 0.0606  282  TRP A O   
1927  C  CB  . TRP A 282 ? 0.4188 0.6854 0.2623 0.2034  -0.0454 0.0844  282  TRP A CB  
1928  C  CG  . TRP A 282 ? 0.6167 0.8935 0.4385 0.2053  -0.0422 0.0875  282  TRP A CG  
1929  C  CD1 . TRP A 282 ? 0.4761 0.7933 0.2752 0.2230  -0.0481 0.0914  282  TRP A CD1 
1930  C  CD2 . TRP A 282 ? 0.6521 0.9009 0.4722 0.1899  -0.0320 0.0867  282  TRP A CD2 
1931  N  NE1 . TRP A 282 ? 0.5126 0.8273 0.2949 0.2190  -0.0413 0.0933  282  TRP A NE1 
1932  C  CE2 . TRP A 282 ? 0.5810 0.8542 0.3770 0.1986  -0.0312 0.0904  282  TRP A CE2 
1933  C  CE3 . TRP A 282 ? 0.5648 0.7726 0.4012 0.1705  -0.0238 0.0829  282  TRP A CE3 
1934  C  CZ2 . TRP A 282 ? 0.3539 0.6117 0.1434 0.1878  -0.0216 0.0898  282  TRP A CZ2 
1935  C  CZ3 . TRP A 282 ? 0.5040 0.6977 0.3348 0.1605  -0.0154 0.0823  282  TRP A CZ3 
1936  C  CH2 . TRP A 282 ? 0.5007 0.7192 0.3089 0.1689  -0.0139 0.0856  282  TRP A CH2 
1937  N  N   . TYR A 283 ? 0.4406 0.7999 0.3086 0.1964  -0.0714 0.0347  283  TYR A N   
1938  C  CA  . TYR A 283 ? 0.4737 0.8798 0.3556 0.1880  -0.0832 0.0052  283  TYR A CA  
1939  C  C   . TYR A 283 ? 0.4855 0.8692 0.3951 0.1619  -0.0801 -0.0143 283  TYR A C   
1940  O  O   . TYR A 283 ? 0.3723 0.7110 0.2834 0.1490  -0.0702 -0.0091 283  TYR A O   
1941  C  CB  . TYR A 283 ? 0.4492 0.8843 0.3140 0.1884  -0.0870 -0.0055 283  TYR A CB  
1942  C  CG  . TYR A 283 ? 0.5746 0.9721 0.4327 0.1739  -0.0760 -0.0039 283  TYR A CG  
1943  C  CD1 . TYR A 283 ? 0.5646 0.9505 0.4416 0.1500  -0.0745 -0.0273 283  TYR A CD1 
1944  C  CD2 . TYR A 283 ? 0.5585 0.9321 0.3923 0.1845  -0.0662 0.0211  283  TYR A CD2 
1945  C  CE1 . TYR A 283 ? 0.5027 0.8570 0.3747 0.1388  -0.0651 -0.0263 283  TYR A CE1 
1946  C  CE2 . TYR A 283 ? 0.5612 0.9047 0.3917 0.1713  -0.0561 0.0214  283  TYR A CE2 
1947  C  CZ  . TYR A 283 ? 0.5595 0.8947 0.4091 0.1493  -0.0563 -0.0026 283  TYR A CZ  
1948  O  OH  . TYR A 283 ? 0.5932 0.9009 0.4401 0.1383  -0.0468 -0.0025 283  TYR A OH  
1949  N  N   . GLU A 284 ? 0.5142 0.9300 0.4458 0.1546  -0.0882 -0.0362 284  GLU A N   
1950  C  CA  . GLU A 284 ? 0.4750 0.8697 0.4323 0.1310  -0.0841 -0.0529 284  GLU A CA  
1951  C  C   . GLU A 284 ? 0.4592 0.8472 0.4200 0.1115  -0.0820 -0.0725 284  GLU A C   
1952  O  O   . GLU A 284 ? 0.4560 0.8739 0.4070 0.1136  -0.0874 -0.0840 284  GLU A O   
1953  C  CB  . GLU A 284 ? 0.3560 0.7852 0.3381 0.1282  -0.0909 -0.0693 284  GLU A CB  
1954  C  CG  . GLU A 284 ? 0.4093 0.8326 0.3940 0.1437  -0.0899 -0.0509 284  GLU A CG  
1955  C  CD  . GLU A 284 ? 0.5009 0.9502 0.5143 0.1365  -0.0932 -0.0676 284  GLU A CD  
1956  O  OE1 . GLU A 284 ? 0.4539 0.9096 0.4714 0.1513  -0.0942 -0.0561 284  GLU A OE1 
1957  O  OE2 . GLU A 284 ? 0.5837 1.0465 0.6164 0.1160  -0.0939 -0.0923 284  GLU A OE2 
1958  N  N   . LEU A 285 ? 0.3376 0.6852 0.3114 0.0936  -0.0738 -0.0759 285  LEU A N   
1959  C  CA  . LEU A 285 ? 0.4106 0.7472 0.3907 0.0751  -0.0709 -0.0946 285  LEU A CA  
1960  C  C   . LEU A 285 ? 0.4129 0.7193 0.4144 0.0576  -0.0647 -0.1012 285  LEU A C   
1961  O  O   . LEU A 285 ? 0.3995 0.6836 0.4041 0.0609  -0.0607 -0.0864 285  LEU A O   
1962  C  CB  . LEU A 285 ? 0.4251 0.7329 0.3855 0.0774  -0.0647 -0.0821 285  LEU A CB  
1963  C  CG  . LEU A 285 ? 0.3229 0.5796 0.2799 0.0764  -0.0550 -0.0614 285  LEU A CG  
1964  C  CD1 . LEU A 285 ? 0.1817 0.4072 0.1530 0.0572  -0.0496 -0.0735 285  LEU A CD1 
1965  C  CD2 . LEU A 285 ? 0.2590 0.5032 0.1937 0.0872  -0.0503 -0.0429 285  LEU A CD2 
1966  N  N   . SER A 286 ? 0.4803 0.7856 0.4959 0.0396  -0.0632 -0.1234 286  SER A N   
1967  C  CA  . SER A 286 ? 0.4454 0.7211 0.4793 0.0233  -0.0560 -0.1286 286  SER A CA  
1968  C  C   . SER A 286 ? 0.4445 0.6811 0.4771 0.0108  -0.0487 -0.1326 286  SER A C   
1969  O  O   . SER A 286 ? 0.5428 0.7859 0.5685 0.0095  -0.0502 -0.1424 286  SER A O   
1970  C  CB  . SER A 286 ? 0.3810 0.6892 0.4388 0.0121  -0.0588 -0.1511 286  SER A CB  
1971  O  OG  . SER A 286 ? 0.5199 0.8657 0.5801 0.0256  -0.0660 -0.1467 286  SER A OG  
1972  N  N   . GLY A 287 ? 0.3387 0.5357 0.3769 0.0035  -0.0411 -0.1246 287  GLY A N   
1973  C  CA  . GLY A 287 ? 0.2046 0.3639 0.2432 -0.0073 -0.0343 -0.1280 287  GLY A CA  
1974  C  C   . GLY A 287 ? 0.3449 0.4781 0.3661 0.0015  -0.0323 -0.1110 287  GLY A C   
1975  O  O   . GLY A 287 ? 0.4589 0.5694 0.4779 -0.0038 -0.0287 -0.1149 287  GLY A O   
1976  N  N   . GLY A 288 ? 0.3386 0.4746 0.3487 0.0150  -0.0342 -0.0925 288  GLY A N   
1977  C  CA  . GLY A 288 ? 0.3952 0.5078 0.3912 0.0223  -0.0312 -0.0764 288  GLY A CA  
1978  C  C   . GLY A 288 ? 0.4038 0.4756 0.4022 0.0179  -0.0255 -0.0673 288  GLY A C   
1979  O  O   . GLY A 288 ? 0.3649 0.4260 0.3721 0.0131  -0.0237 -0.0674 288  GLY A O   
1980  N  N   . MET A 289 ? 0.5288 0.5799 0.5193 0.0201  -0.0226 -0.0595 289  MET A N   
1981  C  CA  . MET A 289 ? 0.4986 0.5147 0.4906 0.0174  -0.0185 -0.0518 289  MET A CA  
1982  C  C   . MET A 289 ? 0.4479 0.4552 0.4374 0.0244  -0.0178 -0.0365 289  MET A C   
1983  O  O   . MET A 289 ? 0.4552 0.4418 0.4486 0.0213  -0.0157 -0.0339 289  MET A O   
1984  C  CB  . MET A 289 ? 0.4221 0.4245 0.4088 0.0182  -0.0161 -0.0495 289  MET A CB  
1985  C  CG  . MET A 289 ? 0.3437 0.3143 0.3325 0.0161  -0.0133 -0.0439 289  MET A CG  
1986  S  SD  . MET A 289 ? 0.5481 0.5102 0.5355 0.0158  -0.0111 -0.0472 289  MET A SD  
1987  C  CE  . MET A 289 ? 0.3905 0.3697 0.3688 0.0238  -0.0092 -0.0356 289  MET A CE  
1988  N  N   . GLN A 290 ? 0.3323 0.3549 0.3144 0.0346  -0.0190 -0.0264 290  GLN A N   
1989  C  CA  . GLN A 290 ? 0.3003 0.3128 0.2798 0.0427  -0.0174 -0.0117 290  GLN A CA  
1990  C  C   . GLN A 290 ? 0.3343 0.3470 0.3224 0.0406  -0.0182 -0.0149 290  GLN A C   
1991  O  O   . GLN A 290 ? 0.2949 0.2842 0.2854 0.0384  -0.0154 -0.0114 290  GLN A O   
1992  C  CB  . GLN A 290 ? 0.2521 0.2851 0.2222 0.0555  -0.0186 -0.0012 290  GLN A CB  
1993  C  CG  . GLN A 290 ? 0.2745 0.2940 0.2420 0.0651  -0.0158 0.0145  290  GLN A CG  
1994  C  CD  . GLN A 290 ? 0.4006 0.4423 0.3587 0.0800  -0.0173 0.0253  290  GLN A CD  
1995  O  OE1 . GLN A 290 ? 0.5116 0.5492 0.4587 0.0870  -0.0135 0.0375  290  GLN A OE1 
1996  N  NE2 . GLN A 290 ? 0.2368 0.3030 0.1994 0.0856  -0.0225 0.0213  290  GLN A NE2 
1997  N  N   . ASP A 291 ? 0.5041 0.5459 0.4972 0.0414  -0.0219 -0.0226 291  ASP A N   
1998  C  CA  . ASP A 291 ? 0.4562 0.5030 0.4591 0.0398  -0.0217 -0.0257 291  ASP A CA  
1999  C  C   . ASP A 291 ? 0.4627 0.4889 0.4729 0.0265  -0.0178 -0.0343 291  ASP A C   
2000  O  O   . ASP A 291 ? 0.4299 0.4487 0.4455 0.0247  -0.0149 -0.0334 291  ASP A O   
2001  C  CB  . ASP A 291 ? 0.4902 0.5777 0.4998 0.0430  -0.0268 -0.0342 291  ASP A CB  
2002  C  CG  . ASP A 291 ? 0.6425 0.7491 0.6435 0.0603  -0.0304 -0.0218 291  ASP A CG  
2003  O  OD1 . ASP A 291 ? 0.6651 0.7507 0.6548 0.0684  -0.0276 -0.0066 291  ASP A OD1 
2004  O  OD2 . ASP A 291 ? 0.6021 0.7447 0.6080 0.0662  -0.0357 -0.0274 291  ASP A OD2 
2005  N  N   . PHE A 292 ? 0.3741 0.3906 0.3836 0.0184  -0.0170 -0.0419 292  PHE A N   
2006  C  CA  . PHE A 292 ? 0.2580 0.2524 0.2725 0.0075  -0.0127 -0.0483 292  PHE A CA  
2007  C  C   . PHE A 292 ? 0.2952 0.2583 0.3034 0.0101  -0.0098 -0.0375 292  PHE A C   
2008  O  O   . PHE A 292 ? 0.4764 0.4259 0.4869 0.0060  -0.0060 -0.0375 292  PHE A O   
2009  C  CB  . PHE A 292 ? 0.1512 0.1409 0.1666 0.0000  -0.0123 -0.0591 292  PHE A CB  
2010  C  CG  . PHE A 292 ? 0.2007 0.1608 0.2178 -0.0079 -0.0073 -0.0616 292  PHE A CG  
2011  C  CD1 . PHE A 292 ? 0.3258 0.2853 0.3527 -0.0183 -0.0029 -0.0715 292  PHE A CD1 
2012  C  CD2 . PHE A 292 ? 0.2036 0.1367 0.2126 -0.0045 -0.0065 -0.0538 292  PHE A CD2 
2013  C  CE1 . PHE A 292 ? 0.3793 0.3085 0.4055 -0.0243 0.0031  -0.0714 292  PHE A CE1 
2014  C  CE2 . PHE A 292 ? 0.4292 0.3360 0.4376 -0.0092 -0.0024 -0.0548 292  PHE A CE2 
2015  C  CZ  . PHE A 292 ? 0.4411 0.3441 0.4567 -0.0185 0.0028  -0.0624 292  PHE A CZ  
2016  N  N   . ASN A 293 ? 0.3261 0.2793 0.3265 0.0168  -0.0111 -0.0288 293  ASN A N   
2017  C  CA  . ASN A 293 ? 0.4533 0.3819 0.4491 0.0199  -0.0094 -0.0202 293  ASN A CA  
2018  C  C   . ASN A 293 ? 0.4240 0.3520 0.4211 0.0235  -0.0077 -0.0157 293  ASN A C   
2019  O  O   . ASN A 293 ? 0.4566 0.3673 0.4523 0.0213  -0.0052 -0.0153 293  ASN A O   
2020  C  CB  . ASN A 293 ? 0.4015 0.3255 0.3922 0.0261  -0.0102 -0.0122 293  ASN A CB  
2021  C  CG  . ASN A 293 ? 0.4748 0.3898 0.4644 0.0224  -0.0103 -0.0161 293  ASN A CG  
2022  O  OD1 . ASN A 293 ? 0.3065 0.2022 0.2954 0.0216  -0.0099 -0.0149 293  ASN A OD1 
2023  N  ND2 . ASN A 293 ? 0.4912 0.4226 0.4809 0.0209  -0.0113 -0.0219 293  ASN A ND2 
2024  N  N   . TYR A 294 ? 0.3575 0.3056 0.3566 0.0304  -0.0091 -0.0122 294  TYR A N   
2025  C  CA  . TYR A 294 ? 0.5711 0.5193 0.5719 0.0364  -0.0074 -0.0073 294  TYR A CA  
2026  C  C   . TYR A 294 ? 0.4744 0.4290 0.4823 0.0298  -0.0045 -0.0146 294  TYR A C   
2027  O  O   . TYR A 294 ? 0.3732 0.3147 0.3799 0.0303  -0.0010 -0.0126 294  TYR A O   
2028  C  CB  . TYR A 294 ? 0.5021 0.4712 0.5030 0.0477  -0.0097 -0.0010 294  TYR A CB  
2029  C  CG  . TYR A 294 ? 0.5019 0.4702 0.5049 0.0564  -0.0077 0.0046  294  TYR A CG  
2030  C  CD1 . TYR A 294 ? 0.4740 0.4154 0.4725 0.0599  -0.0046 0.0108  294  TYR A CD1 
2031  C  CD2 . TYR A 294 ? 0.3939 0.3901 0.4045 0.0617  -0.0090 0.0021  294  TYR A CD2 
2032  C  CE1 . TYR A 294 ? 0.5256 0.4653 0.5261 0.0686  -0.0023 0.0145  294  TYR A CE1 
2033  C  CE2 . TYR A 294 ? 0.3513 0.3477 0.3646 0.0712  -0.0069 0.0067  294  TYR A CE2 
2034  C  CZ  . TYR A 294 ? 0.5093 0.4760 0.5169 0.0748  -0.0032 0.0130  294  TYR A CZ  
2035  O  OH  . TYR A 294 ? 0.4151 0.3810 0.4256 0.0848  -0.0005 0.0162  294  TYR A OH  
2036  N  N   . ALA A 295 ? 0.5439 0.5191 0.5594 0.0231  -0.0054 -0.0240 295  ALA A N   
2037  C  CA  . ALA A 295 ? 0.4201 0.4070 0.4462 0.0155  -0.0014 -0.0320 295  ALA A CA  
2038  C  C   . ALA A 295 ? 0.4053 0.3677 0.4299 0.0045  0.0046  -0.0354 295  ALA A C   
2039  O  O   . ALA A 295 ? 0.5211 0.4850 0.5518 -0.0012 0.0106  -0.0384 295  ALA A O   
2040  C  CB  . ALA A 295 ? 0.2658 0.2869 0.3031 0.0118  -0.0046 -0.0428 295  ALA A CB  
2041  N  N   . PHE A 296 ? 0.2941 0.2347 0.3106 0.0024  0.0037  -0.0343 296  PHE A N   
2042  C  CA  . PHE A 296 ? 0.3464 0.2634 0.3602 -0.0059 0.0092  -0.0364 296  PHE A CA  
2043  C  C   . PHE A 296 ? 0.5048 0.3939 0.5053 -0.0003 0.0084  -0.0282 296  PHE A C   
2044  O  O   . PHE A 296 ? 0.4136 0.2813 0.4084 -0.0038 0.0112  -0.0281 296  PHE A O   
2045  C  CB  . PHE A 296 ? 0.5031 0.4213 0.5220 -0.0141 0.0091  -0.0460 296  PHE A CB  
2046  C  CG  . PHE A 296 ? 0.6664 0.6137 0.7002 -0.0217 0.0098  -0.0579 296  PHE A CG  
2047  C  CD1 . PHE A 296 ? 0.5714 0.5490 0.6092 -0.0168 0.0029  -0.0617 296  PHE A CD1 
2048  C  CD2 . PHE A 296 ? 0.6909 0.6363 0.7348 -0.0337 0.0178  -0.0655 296  PHE A CD2 
2049  C  CE1 . PHE A 296 ? 0.4831 0.4920 0.5352 -0.0231 0.0021  -0.0747 296  PHE A CE1 
2050  C  CE2 . PHE A 296 ? 0.5320 0.5074 0.5930 -0.0422 0.0183  -0.0792 296  PHE A CE2 
2051  C  CZ  . PHE A 296 ? 0.4675 0.4763 0.5327 -0.0366 0.0096  -0.0846 296  PHE A CZ  
2052  N  N   . SER A 297 ? 0.4142 0.3038 0.4102 0.0088  0.0046  -0.0217 297  SER A N   
2053  C  CA  . SER A 297 ? 0.2434 0.1107 0.2292 0.0137  0.0033  -0.0161 297  SER A CA  
2054  C  C   . SER A 297 ? 0.3637 0.2340 0.3484 0.0219  0.0017  -0.0109 297  SER A C   
2055  O  O   . SER A 297 ? 0.5035 0.3915 0.4942 0.0249  0.0022  -0.0103 297  SER A O   
2056  C  CB  . SER A 297 ? 0.3280 0.1868 0.3113 0.0140  -0.0008 -0.0169 297  SER A CB  
2057  O  OG  . SER A 297 ? 0.2812 0.1497 0.2667 0.0187  -0.0044 -0.0142 297  SER A OG  
2058  N  N   . ASN A 298 ? 0.3162 0.1736 0.2940 0.0252  -0.0001 -0.0079 298  ASN A N   
2059  C  CA  . ASN A 298 ? 0.2361 0.0943 0.2133 0.0313  -0.0008 -0.0043 298  ASN A CA  
2060  C  C   . ASN A 298 ? 0.3917 0.2550 0.3731 0.0340  -0.0032 -0.0012 298  ASN A C   
2061  O  O   . ASN A 298 ? 0.3688 0.2319 0.3518 0.0399  -0.0022 0.0030  298  ASN A O   
2062  C  CB  . ASN A 298 ? 0.2221 0.0730 0.1913 0.0309  -0.0021 -0.0047 298  ASN A CB  
2063  C  CG  . ASN A 298 ? 0.3155 0.1582 0.2767 0.0313  0.0012  -0.0058 298  ASN A CG  
2064  O  OD1 . ASN A 298 ? 0.4479 0.2903 0.4115 0.0329  0.0058  -0.0059 298  ASN A OD1 
2065  N  ND2 . ASN A 298 ? 0.3810 0.2161 0.3328 0.0311  -0.0009 -0.0069 298  ASN A ND2 
2066  N  N   . CYS A 299 ? 0.2165 0.0826 0.1992 0.0304  -0.0052 -0.0029 299  CYS A N   
2067  C  CA  . CYS A 299 ? 0.2666 0.1346 0.2511 0.0323  -0.0062 0.0004  299  CYS A CA  
2068  C  C   . CYS A 299 ? 0.4292 0.3071 0.4160 0.0394  -0.0053 0.0063  299  CYS A C   
2069  O  O   . CYS A 299 ? 0.4924 0.3883 0.4810 0.0397  -0.0058 0.0045  299  CYS A O   
2070  C  CB  . CYS A 299 ? 0.2266 0.0963 0.2118 0.0277  -0.0081 -0.0035 299  CYS A CB  
2071  S  SG  . CYS A 299 ? 0.4719 0.3410 0.4593 0.0285  -0.0077 -0.0001 299  CYS A SG  
2072  N  N   . PHE A 300 ? 0.3705 0.2417 0.3572 0.0440  -0.0035 0.0132  300  PHE A N   
2073  C  CA  . PHE A 300 ? 0.3666 0.2492 0.3524 0.0517  -0.0019 0.0218  300  PHE A CA  
2074  C  C   . PHE A 300 ? 0.3988 0.2873 0.3823 0.0508  -0.0011 0.0252  300  PHE A C   
2075  O  O   . PHE A 300 ? 0.3216 0.1966 0.3058 0.0505  0.0026  0.0300  300  PHE A O   
2076  C  CB  . PHE A 300 ? 0.5298 0.3963 0.5161 0.0585  0.0021  0.0289  300  PHE A CB  
2077  C  CG  . PHE A 300 ? 0.5515 0.4155 0.5393 0.0621  0.0022  0.0264  300  PHE A CG  
2078  C  CD1 . PHE A 300 ? 0.4300 0.2876 0.4185 0.0714  0.0058  0.0329  300  PHE A CD1 
2079  C  CD2 . PHE A 300 ? 0.6306 0.4981 0.6186 0.0566  0.0001  0.0178  300  PHE A CD2 
2080  C  CE1 . PHE A 300 ? 0.5285 0.3854 0.5186 0.0754  0.0066  0.0296  300  PHE A CE1 
2081  C  CE2 . PHE A 300 ? 0.6242 0.4907 0.6130 0.0600  0.0017  0.0156  300  PHE A CE2 
2082  C  CZ  . PHE A 300 ? 0.5192 0.3811 0.5094 0.0696  0.0046  0.0208  300  PHE A CZ  
2083  N  N   . GLU A 301 ? 0.4324 0.3422 0.4141 0.0498  -0.0038 0.0216  301  GLU A N   
2084  C  CA  . GLU A 301 ? 0.2657 0.1840 0.2437 0.0494  -0.0027 0.0237  301  GLU A CA  
2085  C  C   . GLU A 301 ? 0.3909 0.3246 0.3619 0.0597  -0.0012 0.0344  301  GLU A C   
2086  O  O   . GLU A 301 ? 0.4481 0.4006 0.4176 0.0658  -0.0045 0.0345  301  GLU A O   
2087  C  CB  . GLU A 301 ? 0.3524 0.2837 0.3316 0.0425  -0.0063 0.0117  301  GLU A CB  
2088  C  CG  . GLU A 301 ? 0.4309 0.3747 0.4057 0.0425  -0.0052 0.0115  301  GLU A CG  
2089  C  CD  . GLU A 301 ? 0.5536 0.5022 0.5315 0.0348  -0.0076 -0.0021 301  GLU A CD  
2090  O  OE1 . GLU A 301 ? 0.6718 0.6028 0.6543 0.0295  -0.0073 -0.0066 301  GLU A OE1 
2091  O  OE2 . GLU A 301 ? 0.5559 0.5260 0.5317 0.0347  -0.0100 -0.0091 301  GLU A OE2 
2092  N  N   . LEU A 302 ? 0.4915 0.4183 0.4581 0.0619  0.0042  0.0437  302  LEU A N   
2093  C  CA  . LEU A 302 ? 0.4924 0.4343 0.4484 0.0723  0.0065  0.0552  302  LEU A CA  
2094  C  C   . LEU A 302 ? 0.4139 0.3766 0.3643 0.0697  0.0052  0.0497  302  LEU A C   
2095  O  O   . LEU A 302 ? 0.4789 0.4366 0.4343 0.0600  0.0054  0.0404  302  LEU A O   
2096  C  CB  . LEU A 302 ? 0.4973 0.4179 0.4506 0.0763  0.0159  0.0705  302  LEU A CB  
2097  C  CG  . LEU A 302 ? 0.5371 0.4351 0.4946 0.0812  0.0193  0.0777  302  LEU A CG  
2098  C  CD1 . LEU A 302 ? 0.4872 0.3650 0.4414 0.0849  0.0303  0.0933  302  LEU A CD1 
2099  C  CD2 . LEU A 302 ? 0.4402 0.3538 0.3942 0.0930  0.0142  0.0803  302  LEU A CD2 
2100  N  N   . THR A 303 ? 0.4740 0.4609 0.4133 0.0795  0.0037  0.0552  303  THR A N   
2101  C  CA  . THR A 303 ? 0.5405 0.5482 0.4709 0.0795  0.0038  0.0519  303  THR A CA  
2102  C  C   . THR A 303 ? 0.6287 0.6300 0.5469 0.0875  0.0130  0.0705  303  THR A C   
2103  O  O   . THR A 303 ? 0.6007 0.6026 0.5101 0.1001  0.0150  0.0854  303  THR A O   
2104  C  CB  . THR A 303 ? 0.6239 0.6682 0.5484 0.0855  -0.0047 0.0437  303  THR A CB  
2105  O  OG1 . THR A 303 ? 0.6365 0.6850 0.5738 0.0786  -0.0114 0.0289  303  THR A OG1 
2106  C  CG2 . THR A 303 ? 0.5014 0.5670 0.4183 0.0832  -0.0053 0.0349  303  THR A CG2 
2107  N  N   . ILE A 304 ? 0.7096 0.7043 0.6275 0.0809  0.0197  0.0704  304  ILE A N   
2108  C  CA  . ILE A 304 ? 0.6857 0.6726 0.5930 0.0868  0.0311  0.0887  304  ILE A CA  
2109  C  C   . ILE A 304 ? 0.7282 0.7382 0.6218 0.0891  0.0344  0.0888  304  ILE A C   
2110  O  O   . ILE A 304 ? 0.5476 0.5638 0.4472 0.0796  0.0341  0.0752  304  ILE A O   
2111  C  CB  . ILE A 304 ? 0.5249 0.4792 0.4449 0.0777  0.0405  0.0935  304  ILE A CB  
2112  C  CG1 . ILE A 304 ? 0.4855 0.4174 0.4146 0.0786  0.0386  0.0960  304  ILE A CG1 
2113  C  CG2 . ILE A 304 ? 0.6185 0.5644 0.5286 0.0819  0.0546  0.1122  304  ILE A CG2 
2114  C  CD1 . ILE A 304 ? 0.6731 0.5774 0.6186 0.0671  0.0438  0.0923  304  ILE A CD1 
2115  N  N   . GLU A 305 ? 0.6077 0.6308 0.4819 0.1033  0.0377  0.1048  305  GLU A N   
2116  C  CA  . GLU A 305 ? 0.5642 0.6118 0.4205 0.1087  0.0414  0.1075  305  GLU A CA  
2117  C  C   . GLU A 305 ? 0.5874 0.6146 0.4388 0.1077  0.0584  0.1259  305  GLU A C   
2118  O  O   . GLU A 305 ? 0.7167 0.7228 0.5633 0.1148  0.0666  0.1460  305  GLU A O   
2119  C  CB  . GLU A 305 ? 0.4561 0.5331 0.2919 0.1265  0.0347  0.1146  305  GLU A CB  
2120  C  CG  . GLU A 305 ? 0.3702 0.4712 0.2133 0.1270  0.0186  0.0959  305  GLU A CG  
2121  C  CD  . GLU A 305 ? 0.5135 0.6417 0.3587 0.1188  0.0116  0.0720  305  GLU A CD  
2122  O  OE1 . GLU A 305 ? 0.4839 0.6320 0.3369 0.1168  -0.0001 0.0547  305  GLU A OE1 
2123  O  OE2 . GLU A 305 ? 0.6027 0.7319 0.4432 0.1139  0.0185  0.0697  305  GLU A OE2 
2124  N  N   . LEU A 306 ? 0.4782 0.5111 0.3316 0.0990  0.0647  0.1187  306  LEU A N   
2125  C  CA  . LEU A 306 ? 0.6361 0.6490 0.4916 0.0937  0.0821  0.1327  306  LEU A CA  
2126  C  C   . LEU A 306 ? 0.6620 0.6896 0.4922 0.1042  0.0939  0.1501  306  LEU A C   
2127  O  O   . LEU A 306 ? 0.7394 0.7461 0.5639 0.1068  0.1092  0.1719  306  LEU A O   
2128  C  CB  . LEU A 306 ? 0.5826 0.5905 0.4597 0.0771  0.0840  0.1154  306  LEU A CB  
2129  C  CG  . LEU A 306 ? 0.6049 0.5941 0.5051 0.0675  0.0747  0.1018  306  LEU A CG  
2130  C  CD1 . LEU A 306 ? 0.6227 0.6138 0.5415 0.0548  0.0730  0.0826  306  LEU A CD1 
2131  C  CD2 . LEU A 306 ? 0.5899 0.5468 0.4990 0.0657  0.0824  0.1159  306  LEU A CD2 
2132  N  N   . SER A 307 ? 0.6111 0.6736 0.4256 0.1100  0.0876  0.1404  307  SER A N   
2133  C  CA  . SER A 307 ? 0.4992 0.5795 0.2873 0.1204  0.0986  0.1552  307  SER A CA  
2134  C  C   . SER A 307 ? 0.6617 0.7785 0.4248 0.1371  0.0867  0.1532  307  SER A C   
2135  O  O   . SER A 307 ? 0.7686 0.9029 0.5390 0.1365  0.0698  0.1332  307  SER A O   
2136  C  CB  . SER A 307 ? 0.5433 0.6343 0.3369 0.1095  0.1069  0.1435  307  SER A CB  
2137  O  OG  . SER A 307 ? 0.6792 0.7867 0.4868 0.1016  0.0929  0.1146  307  SER A OG  
2138  N  N   . CYS A 308 ? 0.6999 0.8287 0.4337 0.1522  0.0960  0.1741  308  CYS A N   
2139  C  CA  . CYS A 308 ? 0.5965 0.7666 0.3030 0.1693  0.0857  0.1718  308  CYS A CA  
2140  C  C   . CYS A 308 ? 0.6412 0.8431 0.3468 0.1623  0.0812  0.1464  308  CYS A C   
2141  O  O   . CYS A 308 ? 0.6581 0.8931 0.3599 0.1663  0.0653  0.1261  308  CYS A O   
2142  C  CB  . CYS A 308 ? 0.5781 0.7505 0.2509 0.1884  0.0987  0.2033  308  CYS A CB  
2143  S  SG  . CYS A 308 ? 0.8992 1.0420 0.5668 0.2039  0.1002  0.2322  308  CYS A SG  
2144  N  N   . CYS A 309 ? 0.6480 0.8404 0.3587 0.1516  0.0960  0.1465  309  CYS A N   
2145  C  CA  . CYS A 309 ? 0.5621 0.7798 0.2761 0.1438  0.0934  0.1211  309  CYS A CA  
2146  C  C   . CYS A 309 ? 0.6857 0.8904 0.4344 0.1261  0.0838  0.0946  309  CYS A C   
2147  O  O   . CYS A 309 ? 0.5634 0.7367 0.3354 0.1134  0.0909  0.0972  309  CYS A O   
2148  C  CB  . CYS A 309 ? 0.5343 0.7509 0.2394 0.1410  0.1138  0.1318  309  CYS A CB  
2149  S  SG  . CYS A 309 ? 0.9573 1.2069 0.6647 0.1341  0.1118  0.1005  309  CYS A SG  
2150  N  N   . LYS A 310 ? 0.7030 0.9321 0.4547 0.1255  0.0679  0.0690  310  LYS A N   
2151  C  CA  . LYS A 310 ? 0.6563 0.8724 0.4379 0.1107  0.0587  0.0452  310  LYS A CA  
2152  C  C   . LYS A 310 ? 0.6351 0.8371 0.4341 0.0980  0.0690  0.0372  310  LYS A C   
2153  O  O   . LYS A 310 ? 0.6848 0.8587 0.5085 0.0870  0.0692  0.0347  310  LYS A O   
2154  C  CB  . LYS A 310 ? 0.6747 0.9211 0.4551 0.1116  0.0431  0.0182  310  LYS A CB  
2155  C  CG  . LYS A 310 ? 0.6670 0.9299 0.4377 0.1222  0.0305  0.0214  310  LYS A CG  
2156  C  CD  . LYS A 310 ? 0.6022 0.8954 0.3771 0.1198  0.0155  -0.0087 310  LYS A CD  
2157  C  CE  . LYS A 310 ? 0.6812 0.9798 0.4627 0.1233  0.0024  -0.0096 310  LYS A CE  
2158  N  NZ  . LYS A 310 ? 0.7390 1.0640 0.5312 0.1175  -0.0114 -0.0405 310  LYS A NZ  
2159  N  N   . TYR A 311 ? 0.7090 0.9329 0.4946 0.1007  0.0774  0.0328  311  TYR A N   
2160  C  CA  . TYR A 311 ? 0.7322 0.9497 0.5341 0.0905  0.0874  0.0233  311  TYR A CA  
2161  C  C   . TYR A 311 ? 0.6754 0.8975 0.4625 0.0941  0.1070  0.0430  311  TYR A C   
2162  O  O   . TYR A 311 ? 0.6937 0.9436 0.4634 0.0995  0.1124  0.0368  311  TYR A O   
2163  C  CB  . TYR A 311 ? 0.6842 0.9257 0.4881 0.0889  0.0800  -0.0067 311  TYR A CB  
2164  C  CG  . TYR A 311 ? 0.5830 0.8124 0.4130 0.0779  0.0838  -0.0229 311  TYR A CG  
2165  C  CD1 . TYR A 311 ? 0.5900 0.8243 0.4324 0.0739  0.0736  -0.0509 311  TYR A CD1 
2166  C  CD2 . TYR A 311 ? 0.6214 0.8344 0.4645 0.0719  0.0977  -0.0107 311  TYR A CD2 
2167  C  CE1 . TYR A 311 ? 0.5172 0.7402 0.3825 0.0665  0.0766  -0.0649 311  TYR A CE1 
2168  C  CE2 . TYR A 311 ? 0.6118 0.8174 0.4798 0.0636  0.0999  -0.0262 311  TYR A CE2 
2169  C  CZ  . TYR A 311 ? 0.5518 0.7622 0.4296 0.0621  0.0890  -0.0526 311  TYR A CZ  
2170  O  OH  . TYR A 311 ? 0.5085 0.7114 0.4097 0.0566  0.0908  -0.0671 311  TYR A OH  
2171  N  N   . PRO A 312 ? 0.7139 0.9086 0.5080 0.0904  0.1188  0.0661  312  PRO A N   
2172  C  CA  . PRO A 312 ? 0.6006 0.7968 0.3815 0.0925  0.1400  0.0869  312  PRO A CA  
2173  C  C   . PRO A 312 ? 0.7822 0.9816 0.5832 0.0811  0.1510  0.0742  312  PRO A C   
2174  O  O   . PRO A 312 ? 0.8449 1.0446 0.6683 0.0737  0.1410  0.0501  312  PRO A O   
2175  C  CB  . PRO A 312 ? 0.5698 0.7311 0.3571 0.0902  0.1480  0.1125  312  PRO A CB  
2176  C  CG  . PRO A 312 ? 0.7843 0.9302 0.5845 0.0894  0.1290  0.1047  312  PRO A CG  
2177  C  CD  . PRO A 312 ? 0.7476 0.9090 0.5612 0.0843  0.1139  0.0738  312  PRO A CD  
2178  N  N   . ALA A 313 ? 0.8206 1.0227 0.6137 0.0805  0.1720  0.0907  313  ALA A N   
2179  C  CA  . ALA A 313 ? 0.8018 1.0108 0.6150 0.0702  0.1846  0.0797  313  ALA A CA  
2180  C  C   . ALA A 313 ? 0.6632 0.8423 0.5107 0.0555  0.1916  0.0846  313  ALA A C   
2181  O  O   . ALA A 313 ? 0.6996 0.8521 0.5487 0.0538  0.1944  0.1036  313  ALA A O   
2182  C  CB  . ALA A 313 ? 0.7599 0.9905 0.5488 0.0759  0.2055  0.0934  313  ALA A CB  
2183  N  N   . ALA A 314 ? 0.5766 0.7619 0.4517 0.0456  0.1942  0.0664  314  ALA A N   
2184  C  CA  . ALA A 314 ? 0.6448 0.8083 0.5555 0.0316  0.1985  0.0655  314  ALA A CA  
2185  C  C   . ALA A 314 ? 0.6751 0.8173 0.5875 0.0252  0.2179  0.0922  314  ALA A C   
2186  O  O   . ALA A 314 ? 0.7543 0.8689 0.6848 0.0178  0.2150  0.0973  314  ALA A O   
2187  C  CB  . ALA A 314 ? 0.6520 0.8339 0.5881 0.0246  0.2030  0.0449  314  ALA A CB  
2188  N  N   . SER A 315 ? 0.6472 0.8013 0.5404 0.0281  0.2385  0.1088  315  SER A N   
2189  C  CA  . SER A 315 ? 0.6900 0.8225 0.5854 0.0210  0.2611  0.1347  315  SER A CA  
2190  C  C   . SER A 315 ? 0.6121 0.7120 0.4980 0.0251  0.2553  0.1532  315  SER A C   
2191  O  O   . SER A 315 ? 0.6633 0.7353 0.5614 0.0164  0.2695  0.1697  315  SER A O   
2192  C  CB  . SER A 315 ? 0.6722 0.8227 0.5383 0.0276  0.2835  0.1531  315  SER A CB  
2193  O  OG  . SER A 315 ? 0.6559 0.8170 0.4797 0.0463  0.2757  0.1634  315  SER A OG  
2194  N  N   . THR A 316 ? 0.4866 0.5908 0.3519 0.0383  0.2349  0.1491  316  THR A N   
2195  C  CA  . THR A 316 ? 0.5096 0.5875 0.3657 0.0447  0.2261  0.1633  316  THR A CA  
2196  C  C   . THR A 316 ? 0.6210 0.6735 0.5117 0.0324  0.2160  0.1516  316  THR A C   
2197  O  O   . THR A 316 ? 0.6997 0.7218 0.5945 0.0308  0.2189  0.1663  316  THR A O   
2198  C  CB  . THR A 316 ? 0.5365 0.6330 0.3649 0.0613  0.2060  0.1577  316  THR A CB  
2199  O  OG1 . THR A 316 ? 0.6768 0.7857 0.4671 0.0763  0.2159  0.1794  316  THR A OG1 
2200  C  CG2 . THR A 316 ? 0.6341 0.7084 0.4683 0.0639  0.1891  0.1578  316  THR A CG2 
2201  N  N   . LEU A 317 ? 0.5170 0.5819 0.4319 0.0246  0.2046  0.1252  317  LEU A N   
2202  C  CA  . LEU A 317 ? 0.4781 0.5250 0.4220 0.0157  0.1908  0.1104  317  LEU A CA  
2203  C  C   . LEU A 317 ? 0.5116 0.5293 0.4795 0.0029  0.2024  0.1198  317  LEU A C   
2204  O  O   . LEU A 317 ? 0.5729 0.5674 0.5495 0.0015  0.1924  0.1194  317  LEU A O   
2205  C  CB  . LEU A 317 ? 0.4008 0.4677 0.3658 0.0105  0.1809  0.0830  317  LEU A CB  
2206  C  CG  . LEU A 317 ? 0.5347 0.6283 0.4815 0.0210  0.1691  0.0686  317  LEU A CG  
2207  C  CD1 . LEU A 317 ? 0.7233 0.8323 0.6942 0.0155  0.1640  0.0438  317  LEU A CD1 
2208  C  CD2 . LEU A 317 ? 0.4211 0.5087 0.3525 0.0301  0.1496  0.0659  317  LEU A CD2 
2209  N  N   . PRO A 318 ? 0.4926 0.5118 0.4730 -0.0072 0.2239  0.1265  318  PRO A N   
2210  C  CA  . PRO A 318 ? 0.5015 0.4931 0.5075 -0.0212 0.2359  0.1330  318  PRO A CA  
2211  C  C   . PRO A 318 ? 0.7042 0.6626 0.6936 -0.0154 0.2404  0.1565  318  PRO A C   
2212  O  O   . PRO A 318 ? 0.8045 0.7374 0.8133 -0.0228 0.2367  0.1537  318  PRO A O   
2213  C  CB  . PRO A 318 ? 0.5321 0.5354 0.5484 -0.0313 0.2609  0.1389  318  PRO A CB  
2214  C  CG  . PRO A 318 ? 0.5145 0.5553 0.5277 -0.0267 0.2546  0.1215  318  PRO A CG  
2215  C  CD  . PRO A 318 ? 0.5296 0.5780 0.5091 -0.0090 0.2368  0.1221  318  PRO A CD  
2216  N  N   . GLN A 319 ? 0.6498 0.6095 0.6036 -0.0013 0.2477  0.1783  319  GLN A N   
2217  C  CA  . GLN A 319 ? 0.6917 0.6226 0.6253 0.0092  0.2496  0.2015  319  GLN A CA  
2218  C  C   . GLN A 319 ? 0.6855 0.6084 0.6181 0.0169  0.2249  0.1915  319  GLN A C   
2219  O  O   . GLN A 319 ? 0.5639 0.4557 0.5037 0.0160  0.2246  0.1988  319  GLN A O   
2220  C  CB  . GLN A 319 ? 0.8444 0.7866 0.7365 0.0268  0.2585  0.2249  319  GLN A CB  
2221  C  CG  . GLN A 319 ? 1.0403 0.9659 0.9242 0.0237  0.2887  0.2517  319  GLN A CG  
2222  C  CD  . GLN A 319 ? 1.2976 1.2552 1.1695 0.0235  0.3021  0.2523  319  GLN A CD  
2223  O  OE1 . GLN A 319 ? 1.4055 1.3609 1.2510 0.0312  0.3221  0.2779  319  GLN A OE1 
2224  N  NE2 . GLN A 319 ? 1.2484 1.2358 1.1385 0.0160  0.2915  0.2246  319  GLN A NE2 
2225  N  N   . GLU A 320 ? 0.6933 0.6439 0.6167 0.0245  0.2054  0.1748  320  GLU A N   
2226  C  CA  . GLU A 320 ? 0.5310 0.4782 0.4545 0.0305  0.1829  0.1635  320  GLU A CA  
2227  C  C   . GLU A 320 ? 0.5573 0.4835 0.5137 0.0167  0.1777  0.1496  320  GLU A C   
2228  O  O   . GLU A 320 ? 0.6789 0.5857 0.6375 0.0196  0.1683  0.1503  320  GLU A O   
2229  C  CB  . GLU A 320 ? 0.5259 0.5058 0.4408 0.0365  0.1654  0.1440  320  GLU A CB  
2230  C  CG  . GLU A 320 ? 0.8106 0.8168 0.6922 0.0506  0.1681  0.1535  320  GLU A CG  
2231  C  CD  . GLU A 320 ? 0.8965 0.8967 0.7505 0.0673  0.1649  0.1734  320  GLU A CD  
2232  O  OE1 . GLU A 320 ? 0.8470 0.8200 0.7080 0.0679  0.1627  0.1816  320  GLU A OE1 
2233  O  OE2 . GLU A 320 ? 0.8823 0.9071 0.7075 0.0809  0.1642  0.1800  320  GLU A OE2 
2234  N  N   . TRP A 321 ? 0.4483 0.3806 0.4306 0.0022  0.1838  0.1362  321  TRP A N   
2235  C  CA  . TRP A 321 ? 0.6259 0.5422 0.6397 -0.0105 0.1786  0.1217  321  TRP A CA  
2236  C  C   . TRP A 321 ? 0.7068 0.5875 0.7277 -0.0152 0.1902  0.1364  321  TRP A C   
2237  O  O   . TRP A 321 ? 0.6662 0.5288 0.6957 -0.0158 0.1796  0.1303  321  TRP A O   
2238  C  CB  . TRP A 321 ? 0.6509 0.5838 0.6928 -0.0243 0.1835  0.1045  321  TRP A CB  
2239  C  CG  . TRP A 321 ? 0.6262 0.5426 0.7002 -0.0378 0.1818  0.0926  321  TRP A CG  
2240  C  CD1 . TRP A 321 ? 0.4705 0.3741 0.5677 -0.0521 0.1991  0.0956  321  TRP A CD1 
2241  C  CD2 . TRP A 321 ? 0.7581 0.6693 0.8436 -0.0379 0.1621  0.0757  321  TRP A CD2 
2242  N  NE1 . TRP A 321 ? 0.5224 0.4155 0.6455 -0.0612 0.1902  0.0795  321  TRP A NE1 
2243  C  CE2 . TRP A 321 ? 0.6573 0.5549 0.7723 -0.0519 0.1674  0.0680  321  TRP A CE2 
2244  C  CE3 . TRP A 321 ? 0.7338 0.6508 0.8076 -0.0280 0.1413  0.0662  321  TRP A CE3 
2245  C  CZ2 . TRP A 321 ? 0.4950 0.3863 0.6254 -0.0547 0.1516  0.0511  321  TRP A CZ2 
2246  C  CZ3 . TRP A 321 ? 0.5619 0.4705 0.6510 -0.0312 0.1272  0.0514  321  TRP A CZ3 
2247  C  CH2 . TRP A 321 ? 0.4014 0.2981 0.5171 -0.0436 0.1319  0.0441  321  TRP A CH2 
2248  N  N   . GLN A 322 ? 0.6870 0.5566 0.7037 -0.0183 0.2130  0.1558  322  GLN A N   
2249  C  CA  . GLN A 322 ? 0.7514 0.5837 0.7772 -0.0242 0.2272  0.1697  322  GLN A CA  
2250  C  C   . GLN A 322 ? 0.7721 0.5822 0.7763 -0.0088 0.2198  0.1839  322  GLN A C   
2251  O  O   . GLN A 322 ? 0.7829 0.5627 0.8000 -0.0130 0.2218  0.1851  322  GLN A O   
2252  C  CB  . GLN A 322 ? 0.7187 0.5419 0.7425 -0.0301 0.2555  0.1898  322  GLN A CB  
2253  C  CG  . GLN A 322 ? 0.8272 0.6309 0.8878 -0.0516 0.2711  0.1832  322  GLN A CG  
2254  C  CD  . GLN A 322 ? 0.9003 0.7327 0.9924 -0.0661 0.2642  0.1552  322  GLN A CD  
2255  O  OE1 . GLN A 322 ? 0.9311 0.7562 1.0549 -0.0796 0.2598  0.1371  322  GLN A OE1 
2256  N  NE2 . GLN A 322 ? 0.8239 0.6909 0.9073 -0.0624 0.2628  0.1507  322  GLN A NE2 
2257  N  N   . ARG A 323 ? 0.6311 0.4584 0.6040 0.0090  0.2110  0.1930  323  ARG A N   
2258  C  CA  . ARG A 323 ? 0.6297 0.4429 0.5823 0.0255  0.2021  0.2051  323  ARG A CA  
2259  C  C   . ARG A 323 ? 0.6961 0.5095 0.6606 0.0254  0.1799  0.1848  323  ARG A C   
2260  O  O   . ARG A 323 ? 0.7138 0.5016 0.6820 0.0285  0.1777  0.1886  323  ARG A O   
2261  C  CB  . ARG A 323 ? 0.5467 0.3846 0.4639 0.0445  0.1981  0.2180  323  ARG A CB  
2262  C  CG  . ARG A 323 ? 0.7393 0.5817 0.6405 0.0462  0.2194  0.2377  323  ARG A CG  
2263  C  CD  . ARG A 323 ? 0.7845 0.6591 0.6509 0.0644  0.2128  0.2452  323  ARG A CD  
2264  N  NE  . ARG A 323 ? 0.7938 0.6668 0.6368 0.0714  0.2345  0.2712  323  ARG A NE  
2265  C  CZ  . ARG A 323 ? 1.0689 0.9726 0.8804 0.0860  0.2331  0.2786  323  ARG A CZ  
2266  N  NH1 . ARG A 323 ? 0.9951 0.9324 0.7983 0.0935  0.2110  0.2600  323  ARG A NH1 
2267  N  NH2 . ARG A 323 ? 1.2977 1.1985 1.0861 0.0929  0.2543  0.3039  323  ARG A NH2 
2268  N  N   . ASN A 324 ? 0.5456 0.3871 0.5155 0.0224  0.1644  0.1637  324  ASN A N   
2269  C  CA  . ASN A 324 ? 0.4597 0.3042 0.4359 0.0239  0.1440  0.1465  324  ASN A CA  
2270  C  C   . ASN A 324 ? 0.5878 0.4166 0.5938 0.0092  0.1417  0.1301  324  ASN A C   
2271  O  O   . ASN A 324 ? 0.6558 0.4787 0.6673 0.0104  0.1279  0.1191  324  ASN A O   
2272  C  CB  . ASN A 324 ? 0.5691 0.4470 0.5376 0.0275  0.1294  0.1317  324  ASN A CB  
2273  C  CG  . ASN A 324 ? 0.6821 0.5793 0.6209 0.0431  0.1278  0.1439  324  ASN A CG  
2274  O  OD1 . ASN A 324 ? 0.7349 0.6383 0.6619 0.0536  0.1148  0.1429  324  ASN A OD1 
2275  N  ND2 . ASN A 324 ? 0.6912 0.6002 0.6177 0.0449  0.1411  0.1549  324  ASN A ND2 
2276  N  N   . LYS A 325 ? 0.5378 0.3620 0.5631 -0.0045 0.1555  0.1279  325  LYS A N   
2277  C  CA  . LYS A 325 ? 0.5799 0.3946 0.6357 -0.0194 0.1538  0.1101  325  LYS A CA  
2278  C  C   . LYS A 325 ? 0.5406 0.3283 0.6019 -0.0183 0.1481  0.1082  325  LYS A C   
2279  O  O   . LYS A 325 ? 0.5827 0.3745 0.6532 -0.0201 0.1326  0.0905  325  LYS A O   
2280  C  CB  . LYS A 325 ? 0.5781 0.3866 0.6536 -0.0340 0.1744  0.1134  325  LYS A CB  
2281  C  CG  . LYS A 325 ? 0.4008 0.2118 0.5108 -0.0506 0.1723  0.0911  325  LYS A CG  
2282  C  CD  . LYS A 325 ? 0.5692 0.3718 0.6983 -0.0651 0.1957  0.0973  325  LYS A CD  
2283  C  CE  . LYS A 325 ? 0.7202 0.5315 0.8864 -0.0824 0.1945  0.0737  325  LYS A CE  
2284  N  NZ  . LYS A 325 ? 0.7899 0.5969 0.9762 -0.0979 0.2192  0.0795  325  LYS A NZ  
2285  N  N   . ALA A 326 ? 0.5613 0.3211 0.6159 -0.0147 0.1615  0.1268  326  ALA A N   
2286  C  CA  . ALA A 326 ? 0.6443 0.3756 0.7035 -0.0125 0.1590  0.1264  326  ALA A CA  
2287  C  C   . ALA A 326 ? 0.7696 0.5080 0.8116 0.0023  0.1405  0.1241  326  ALA A C   
2288  O  O   . ALA A 326 ? 0.6704 0.3997 0.7215 0.0010  0.1304  0.1111  326  ALA A O   
2289  C  CB  . ALA A 326 ? 0.5756 0.2741 0.6295 -0.0097 0.1793  0.1492  326  ALA A CB  
2290  N  N   . SER A 327 ? 0.7405 0.4966 0.7579 0.0160  0.1365  0.1359  327  SER A N   
2291  C  CA  . SER A 327 ? 0.5545 0.3218 0.5569 0.0293  0.1200  0.1335  327  SER A CA  
2292  C  C   . SER A 327 ? 0.3858 0.1725 0.3971 0.0238  0.1026  0.1104  327  SER A C   
2293  O  O   . SER A 327 ? 0.5120 0.2992 0.5200 0.0295  0.0906  0.1039  327  SER A O   
2294  C  CB  . SER A 327 ? 0.5033 0.2902 0.4794 0.0440  0.1198  0.1489  327  SER A CB  
2295  O  OG  . SER A 327 ? 0.5917 0.3622 0.5573 0.0495  0.1375  0.1721  327  SER A OG  
2296  N  N   . LEU A 328 ? 0.3492 0.1518 0.3713 0.0135  0.1023  0.0988  328  LEU A N   
2297  C  CA  . LEU A 328 ? 0.4645 0.2836 0.4940 0.0096  0.0870  0.0787  328  LEU A CA  
2298  C  C   . LEU A 328 ? 0.5055 0.3098 0.5548 0.0008  0.0831  0.0644  328  LEU A C   
2299  O  O   . LEU A 328 ? 0.5167 0.3250 0.5668 0.0021  0.0697  0.0520  328  LEU A O   
2300  C  CB  . LEU A 328 ? 0.5097 0.3521 0.5432 0.0042  0.0880  0.0715  328  LEU A CB  
2301  C  CG  . LEU A 328 ? 0.3771 0.2418 0.3910 0.0125  0.0882  0.0786  328  LEU A CG  
2302  C  CD1 . LEU A 328 ? 0.2905 0.1696 0.3115 0.0055  0.0979  0.0766  328  LEU A CD1 
2303  C  CD2 . LEU A 328 ? 0.2977 0.1789 0.3034 0.0181  0.0721  0.0670  328  LEU A CD2 
2304  N  N   . LEU A 329 ? 0.5034 0.2909 0.5685 -0.0085 0.0953  0.0659  329  LEU A N   
2305  C  CA  . LEU A 329 ? 0.6304 0.4045 0.7146 -0.0169 0.0921  0.0512  329  LEU A CA  
2306  C  C   . LEU A 329 ? 0.5799 0.3332 0.6564 -0.0092 0.0886  0.0547  329  LEU A C   
2307  O  O   . LEU A 329 ? 0.6967 0.4508 0.7753 -0.0083 0.0766  0.0414  329  LEU A O   
2308  C  CB  . LEU A 329 ? 0.7055 0.4679 0.8116 -0.0306 0.1076  0.0503  329  LEU A CB  
2309  C  CG  . LEU A 329 ? 0.6384 0.4224 0.7638 -0.0423 0.1086  0.0371  329  LEU A CG  
2310  C  CD1 . LEU A 329 ? 0.4948 0.3069 0.6124 -0.0364 0.0930  0.0273  329  LEU A CD1 
2311  C  CD2 . LEU A 329 ? 0.5712 0.3541 0.7009 -0.0487 0.1286  0.0507  329  LEU A CD2 
2312  N  N   . GLN A 330 ? 0.4333 0.1684 0.5001 -0.0025 0.0998  0.0731  330  GLN A N   
2313  C  CA  . GLN A 330 ? 0.5935 0.3078 0.6543 0.0062  0.0986  0.0774  330  GLN A CA  
2314  C  C   . GLN A 330 ? 0.6007 0.3304 0.6465 0.0175  0.0829  0.0739  330  GLN A C   
2315  O  O   . GLN A 330 ? 0.6899 0.4119 0.7372 0.0203  0.0768  0.0661  330  GLN A O   
2316  C  CB  . GLN A 330 ? 0.7603 0.4534 0.8115 0.0141  0.1139  0.1004  330  GLN A CB  
2317  C  CG  . GLN A 330 ? 0.7831 0.4518 0.8517 0.0018  0.1318  0.1034  330  GLN A CG  
2318  C  CD  . GLN A 330 ? 0.8072 0.4586 0.8979 -0.0091 0.1304  0.0841  330  GLN A CD  
2319  O  OE1 . GLN A 330 ? 0.8152 0.4458 0.9044 -0.0027 0.1298  0.0841  330  GLN A OE1 
2320  N  NE2 . GLN A 330 ? 0.8953 0.5575 1.0071 -0.0251 0.1295  0.0666  330  GLN A NE2 
2321  N  N   . LEU A 331 ? 0.5424 0.2962 0.5745 0.0232  0.0773  0.0783  331  LEU A N   
2322  C  CA  . LEU A 331 ? 0.4258 0.1960 0.4463 0.0316  0.0635  0.0736  331  LEU A CA  
2323  C  C   . LEU A 331 ? 0.3931 0.1675 0.4234 0.0241  0.0529  0.0542  331  LEU A C   
2324  O  O   . LEU A 331 ? 0.4546 0.2327 0.4820 0.0278  0.0454  0.0474  331  LEU A O   
2325  C  CB  . LEU A 331 ? 0.3859 0.1821 0.3930 0.0363  0.0601  0.0785  331  LEU A CB  
2326  C  CG  . LEU A 331 ? 0.5530 0.3676 0.5491 0.0442  0.0479  0.0744  331  LEU A CG  
2327  C  CD1 . LEU A 331 ? 0.4229 0.2626 0.4073 0.0480  0.0461  0.0779  331  LEU A CD1 
2328  C  CD2 . LEU A 331 ? 0.8489 0.6665 0.8526 0.0377  0.0376  0.0570  331  LEU A CD2 
2329  N  N   . LEU A 332 ? 0.3404 0.1220 0.3822 0.0140  0.0527  0.0445  332  LEU A N   
2330  C  CA  . LEU A 332 ? 0.5095 0.2973 0.5592 0.0089  0.0422  0.0268  332  LEU A CA  
2331  C  C   . LEU A 332 ? 0.4475 0.2263 0.5037 0.0077  0.0413  0.0194  332  LEU A C   
2332  O  O   . LEU A 332 ? 0.5018 0.2902 0.5533 0.0103  0.0318  0.0110  332  LEU A O   
2333  C  CB  . LEU A 332 ? 0.6063 0.4040 0.6704 -0.0007 0.0430  0.0174  332  LEU A CB  
2334  C  CG  . LEU A 332 ? 0.5467 0.3658 0.6037 0.0012  0.0409  0.0194  332  LEU A CG  
2335  C  CD1 . LEU A 332 ? 0.4557 0.2862 0.5281 -0.0073 0.0445  0.0119  332  LEU A CD1 
2336  C  CD2 . LEU A 332 ? 0.3643 0.1934 0.4108 0.0069  0.0283  0.0128  332  LEU A CD2 
2337  N  N   . ARG A 333 ? 0.5257 0.2840 0.5919 0.0038  0.0522  0.0232  333  ARG A N   
2338  C  CA  . ARG A 333 ? 0.4154 0.1616 0.4895 0.0021  0.0525  0.0144  333  ARG A CA  
2339  C  C   . ARG A 333 ? 0.4288 0.1733 0.4892 0.0131  0.0496  0.0194  333  ARG A C   
2340  O  O   . ARG A 333 ? 0.7245 0.4620 0.7882 0.0133  0.0476  0.0107  333  ARG A O   
2341  C  CB  . ARG A 333 ? 0.3769 0.0983 0.4672 -0.0059 0.0667  0.0164  333  ARG A CB  
2342  C  CG  . ARG A 333 ? 0.6243 0.3484 0.7305 -0.0185 0.0714  0.0114  333  ARG A CG  
2343  C  CD  . ARG A 333 ? 0.8361 0.5399 0.9655 -0.0316 0.0828  0.0038  333  ARG A CD  
2344  N  NE  . ARG A 333 ? 0.8567 0.5674 0.9994 -0.0373 0.0733  -0.0191 333  ARG A NE  
2345  C  CZ  . ARG A 333 ? 0.8845 0.6029 1.0491 -0.0504 0.0716  -0.0368 333  ARG A CZ  
2346  N  NH1 . ARG A 333 ? 0.8101 0.5356 0.9823 -0.0523 0.0612  -0.0569 333  ARG A NH1 
2347  N  NH2 . ARG A 333 ? 0.8387 0.5669 1.0176 -0.0601 0.0799  -0.0352 333  ARG A NH2 
2348  N  N   . GLN A 334 ? 0.4354 0.1872 0.4809 0.0223  0.0490  0.0323  334  GLN A N   
2349  C  CA  . GLN A 334 ? 0.3360 0.0909 0.3697 0.0327  0.0452  0.0360  334  GLN A CA  
2350  C  C   . GLN A 334 ? 0.5339 0.3075 0.5628 0.0318  0.0330  0.0236  334  GLN A C   
2351  O  O   . GLN A 334 ? 0.6776 0.4528 0.7001 0.0377  0.0301  0.0226  334  GLN A O   
2352  C  CB  . GLN A 334 ? 0.5501 0.3097 0.5709 0.0430  0.0474  0.0524  334  GLN A CB  
2353  C  CG  . GLN A 334 ? 0.4996 0.2377 0.5195 0.0492  0.0602  0.0694  334  GLN A CG  
2354  C  CD  . GLN A 334 ? 0.5908 0.3114 0.6114 0.0570  0.0646  0.0718  334  GLN A CD  
2355  O  OE1 . GLN A 334 ? 0.6846 0.4138 0.6966 0.0677  0.0596  0.0743  334  GLN A OE1 
2356  N  NE2 . GLN A 334 ? 0.5185 0.2140 0.5510 0.0514  0.0743  0.0703  334  GLN A NE2 
2357  N  N   . ALA A 335 ? 0.3630 0.1494 0.3948 0.0250  0.0267  0.0150  335  ALA A N   
2358  C  CA  . ALA A 335 ? 0.4356 0.2354 0.4622 0.0244  0.0166  0.0050  335  ALA A CA  
2359  C  C   . ALA A 335 ? 0.5090 0.3001 0.5409 0.0226  0.0149  -0.0054 335  ALA A C   
2360  O  O   . ALA A 335 ? 0.5198 0.3187 0.5470 0.0225  0.0071  -0.0138 335  ALA A O   
2361  C  CB  . ALA A 335 ? 0.3314 0.1446 0.3596 0.0197  0.0108  -0.0004 335  ALA A CB  
2362  N  N   . HIS A 336 ? 0.4335 0.2064 0.4746 0.0215  0.0227  -0.0050 336  HIS A N   
2363  C  CA  . HIS A 336 ? 0.5240 0.2874 0.5714 0.0193  0.0213  -0.0175 336  HIS A CA  
2364  C  C   . HIS A 336 ? 0.5466 0.2955 0.5904 0.0261  0.0261  -0.0149 336  HIS A C   
2365  O  O   . HIS A 336 ? 0.3264 0.0670 0.3735 0.0256  0.0248  -0.0263 336  HIS A O   
2366  C  CB  . HIS A 336 ? 0.4849 0.2381 0.5507 0.0099  0.0255  -0.0259 336  HIS A CB  
2367  C  CG  . HIS A 336 ? 0.6552 0.4240 0.7264 0.0042  0.0193  -0.0321 336  HIS A CG  
2368  N  ND1 . HIS A 336 ? 0.6766 0.4584 0.7452 0.0043  0.0079  -0.0442 336  HIS A ND1 
2369  C  CD2 . HIS A 336 ? 0.5483 0.3208 0.6264 -0.0006 0.0231  -0.0275 336  HIS A CD2 
2370  C  CE1 . HIS A 336 ? 0.5820 0.3750 0.6569 0.0004  0.0045  -0.0472 336  HIS A CE1 
2371  N  NE2 . HIS A 336 ? 0.5644 0.3526 0.6458 -0.0032 0.0137  -0.0379 336  HIS A NE2 
2372  N  N   . ILE A 337 ? 0.4738 0.2962 0.5748 0.0121  0.0336  0.0020  337  ILE A N   
2373  C  CA  . ILE A 337 ? 0.4305 0.2477 0.5366 0.0140  0.0331  0.0007  337  ILE A CA  
2374  C  C   . ILE A 337 ? 0.3758 0.1990 0.4805 0.0148  0.0317  -0.0045 337  ILE A C   
2375  O  O   . ILE A 337 ? 0.5261 0.3567 0.6244 0.0140  0.0309  -0.0058 337  ILE A O   
2376  C  CB  . ILE A 337 ? 0.5548 0.3667 0.6591 0.0176  0.0325  0.0065  337  ILE A CB  
2377  C  CG1 . ILE A 337 ? 0.5608 0.3804 0.6573 0.0199  0.0302  0.0079  337  ILE A CG1 
2378  C  CG2 . ILE A 337 ? 0.4958 0.2990 0.6004 0.0169  0.0348  0.0131  337  ILE A CG2 
2379  C  CD1 . ILE A 337 ? 0.5239 0.3383 0.6173 0.0242  0.0288  0.0132  337  ILE A CD1 
2380  N  N   . GLY A 338 ? 0.4621 0.2806 0.5725 0.0168  0.0315  -0.0074 338  GLY A N   
2381  C  CA  . GLY A 338 ? 0.5430 0.3659 0.6532 0.0181  0.0312  -0.0121 338  GLY A CA  
2382  C  C   . GLY A 338 ? 0.3322 0.1572 0.4417 0.0161  0.0320  -0.0180 338  GLY A C   
2383  O  O   . GLY A 338 ? 0.3583 0.1780 0.4722 0.0151  0.0319  -0.0212 338  GLY A O   
2384  N  N   . ILE A 339 ? 0.2687 0.1000 0.3722 0.0155  0.0324  -0.0195 339  ILE A N   
2385  C  CA  . ILE A 339 ? 0.4538 0.2859 0.5541 0.0146  0.0331  -0.0250 339  ILE A CA  
2386  C  C   . ILE A 339 ? 0.4724 0.3094 0.5623 0.0126  0.0327  -0.0236 339  ILE A C   
2387  O  O   . ILE A 339 ? 0.4466 0.2866 0.5322 0.0119  0.0315  -0.0189 339  ILE A O   
2388  C  CB  . ILE A 339 ? 0.4135 0.2445 0.5155 0.0173  0.0348  -0.0297 339  ILE A CB  
2389  C  CG1 . ILE A 339 ? 0.4651 0.3002 0.5653 0.0176  0.0356  -0.0265 339  ILE A CG1 
2390  C  CG2 . ILE A 339 ? 0.3132 0.1375 0.4243 0.0207  0.0342  -0.0333 339  ILE A CG2 
2391  C  CD1 . ILE A 339 ? 0.3648 0.1995 0.4674 0.0202  0.0384  -0.0310 339  ILE A CD1 
2392  N  N   . LYS A 340 ? 0.3858 0.2219 0.4707 0.0122  0.0331  -0.0283 340  LYS A N   
2393  C  CA  . LYS A 340 ? 0.4298 0.2676 0.5030 0.0110  0.0322  -0.0276 340  LYS A CA  
2394  C  C   . LYS A 340 ? 0.5332 0.3677 0.6014 0.0120  0.0333  -0.0335 340  LYS A C   
2395  O  O   . LYS A 340 ? 0.3626 0.1944 0.4370 0.0136  0.0337  -0.0387 340  LYS A O   
2396  C  CB  . LYS A 340 ? 0.5164 0.3558 0.5867 0.0099  0.0296  -0.0259 340  LYS A CB  
2397  C  CG  . LYS A 340 ? 0.3822 0.2199 0.4583 0.0095  0.0290  -0.0303 340  LYS A CG  
2398  C  CD  . LYS A 340 ? 0.3169 0.1568 0.3895 0.0087  0.0268  -0.0288 340  LYS A CD  
2399  C  CE  . LYS A 340 ? 0.2413 0.0797 0.3226 0.0075  0.0261  -0.0331 340  LYS A CE  
2400  N  NZ  . LYS A 340 ? 0.3131 0.1539 0.3935 0.0068  0.0250  -0.0310 340  LYS A NZ  
2401  N  N   . GLY A 341 ? 0.3213 0.1542 0.3771 0.0115  0.0333  -0.0328 341  GLY A N   
2402  C  CA  . GLY A 341 ? 0.2563 0.0843 0.3043 0.0131  0.0348  -0.0380 341  GLY A CA  
2403  C  C   . GLY A 341 ? 0.3694 0.1924 0.4018 0.0124  0.0351  -0.0359 341  GLY A C   
2404  O  O   . GLY A 341 ? 0.2692 0.0924 0.2958 0.0104  0.0330  -0.0308 341  GLY A O   
2405  N  N   . LEU A 342 ? 0.5051 0.3222 0.5298 0.0144  0.0377  -0.0403 342  LEU A N   
2406  C  CA  . LEU A 342 ? 0.5193 0.3278 0.5269 0.0139  0.0384  -0.0385 342  LEU A CA  
2407  C  C   . LEU A 342 ? 0.5496 0.3529 0.5556 0.0139  0.0448  -0.0390 342  LEU A C   
2408  O  O   . LEU A 342 ? 0.5977 0.4021 0.6094 0.0175  0.0483  -0.0448 342  LEU A O   
2409  C  CB  . LEU A 342 ? 0.4598 0.2632 0.4552 0.0174  0.0356  -0.0437 342  LEU A CB  
2410  C  CG  . LEU A 342 ? 0.4490 0.2573 0.4470 0.0179  0.0295  -0.0448 342  LEU A CG  
2411  C  CD1 . LEU A 342 ? 0.4599 0.2637 0.4482 0.0224  0.0266  -0.0519 342  LEU A CD1 
2412  C  CD2 . LEU A 342 ? 0.4186 0.2268 0.4103 0.0158  0.0259  -0.0385 342  LEU A CD2 
2413  N  N   . VAL A 343 ? 0.4423 0.2393 0.4406 0.0100  0.0461  -0.0333 343  VAL A N   
2414  C  CA  . VAL A 343 ? 0.4647 0.2534 0.4589 0.0089  0.0527  -0.0332 343  VAL A CA  
2415  C  C   . VAL A 343 ? 0.5546 0.3295 0.5271 0.0096  0.0525  -0.0333 343  VAL A C   
2416  O  O   . VAL A 343 ? 0.4542 0.2229 0.4152 0.0069  0.0478  -0.0283 343  VAL A O   
2417  C  CB  . VAL A 343 ? 0.5186 0.3071 0.5198 0.0024  0.0542  -0.0263 343  VAL A CB  
2418  C  CG1 . VAL A 343 ? 0.2254 0.0161 0.2226 -0.0013 0.0616  -0.0236 343  VAL A CG1 
2419  C  CG2 . VAL A 343 ? 0.4151 0.2165 0.4364 0.0034  0.0534  -0.0269 343  VAL A CG2 
2420  N  N   . THR A 344 ? 0.7281 0.5035 0.6936 0.0142  0.0572  -0.0386 344  THR A N   
2421  C  CA  . THR A 344 ? 0.7463 0.5137 0.6899 0.0169  0.0563  -0.0392 344  THR A CA  
2422  C  C   . THR A 344 ? 0.7322 0.5065 0.6647 0.0159  0.0644  -0.0359 344  THR A C   
2423  O  O   . THR A 344 ? 0.6436 0.4325 0.5875 0.0150  0.0711  -0.0356 344  THR A O   
2424  C  CB  . THR A 344 ? 0.7452 0.5110 0.6873 0.0254  0.0522  -0.0499 344  THR A CB  
2425  O  OG1 . THR A 344 ? 1.0087 0.7643 0.9289 0.0285  0.0488  -0.0505 344  THR A OG1 
2426  C  CG2 . THR A 344 ? 0.5388 0.3166 0.4868 0.0311  0.0573  -0.0572 344  THR A CG2 
2427  N  N   . ASP A 345 ? 0.5989 0.3629 0.5086 0.0166  0.0635  -0.0330 345  ASP A N   
2428  C  CA  . ASP A 345 ? 0.5643 0.3326 0.4581 0.0172  0.0709  -0.0300 345  ASP A CA  
2429  C  C   . ASP A 345 ? 0.7021 0.4832 0.5987 0.0264  0.0747  -0.0398 345  ASP A C   
2430  O  O   . ASP A 345 ? 0.5112 0.2944 0.4201 0.0324  0.0701  -0.0496 345  ASP A O   
2431  C  CB  . ASP A 345 ? 0.4804 0.2321 0.3473 0.0203  0.0665  -0.0285 345  ASP A CB  
2432  C  CG  . ASP A 345 ? 0.5333 0.2743 0.3858 0.0115  0.0683  -0.0160 345  ASP A CG  
2433  O  OD1 . ASP A 345 ? 0.8558 0.5800 0.6855 0.0138  0.0635  -0.0137 345  ASP A OD1 
2434  O  OD2 . ASP A 345 ? 0.4813 0.2306 0.3458 0.0025  0.0740  -0.0088 345  ASP A OD2 
2435  N  N   . ALA A 346 ? 0.8921 0.6810 0.7760 0.0274  0.0828  -0.0369 346  ALA A N   
2436  C  CA  . ALA A 346 ? 0.9080 0.7045 0.7835 0.0385  0.0851  -0.0463 346  ALA A CA  
2437  C  C   . ALA A 346 ? 0.7942 0.5750 0.6490 0.0452  0.0775  -0.0508 346  ALA A C   
2438  O  O   . ALA A 346 ? 0.7970 0.5794 0.6507 0.0552  0.0735  -0.0626 346  ALA A O   
2439  C  CB  . ALA A 346 ? 0.8878 0.6976 0.7531 0.0378  0.0965  -0.0407 346  ALA A CB  
2440  N  N   . SER A 347 ? 0.5005 0.2659 0.3392 0.0399  0.0747  -0.0420 347  SER A N   
2441  C  CA  . SER A 347 ? 0.5775 0.3267 0.3989 0.0460  0.0655  -0.0461 347  SER A CA  
2442  C  C   . SER A 347 ? 0.6284 0.3762 0.4681 0.0486  0.0564  -0.0554 347  SER A C   
2443  O  O   . SER A 347 ? 0.6742 0.4126 0.5049 0.0541  0.0481  -0.0610 347  SER A O   
2444  C  CB  . SER A 347 ? 0.7820 0.5135 0.5860 0.0392  0.0630  -0.0345 347  SER A CB  
2445  O  OG  . SER A 347 ? 0.8734 0.6041 0.6599 0.0349  0.0715  -0.0240 347  SER A OG  
2446  N  N   . GLY A 348 ? 0.7002 0.4579 0.5654 0.0445  0.0582  -0.0567 348  GLY A N   
2447  C  CA  . GLY A 348 ? 0.7174 0.4737 0.6008 0.0451  0.0509  -0.0632 348  GLY A CA  
2448  C  C   . GLY A 348 ? 0.5158 0.2597 0.3960 0.0399  0.0449  -0.0569 348  GLY A C   
2449  O  O   . GLY A 348 ? 0.6355 0.3757 0.5195 0.0427  0.0373  -0.0621 348  GLY A O   
2450  N  N   . PHE A 349 ? 0.3806 0.1197 0.2544 0.0323  0.0482  -0.0455 349  PHE A N   
2451  C  CA  . PHE A 349 ? 0.4356 0.1606 0.3015 0.0282  0.0421  -0.0392 349  PHE A CA  
2452  C  C   . PHE A 349 ? 0.5582 0.2852 0.4410 0.0193  0.0432  -0.0321 349  PHE A C   
2453  O  O   . PHE A 349 ? 0.5777 0.3123 0.4672 0.0131  0.0503  -0.0263 349  PHE A O   
2454  C  CB  . PHE A 349 ? 0.4076 0.1195 0.2460 0.0273  0.0428  -0.0317 349  PHE A CB  
2455  C  CG  . PHE A 349 ? 0.6465 0.3414 0.4742 0.0247  0.0352  -0.0263 349  PHE A CG  
2456  C  CD1 . PHE A 349 ? 0.7994 0.4835 0.6127 0.0327  0.0264  -0.0317 349  PHE A CD1 
2457  C  CD2 . PHE A 349 ? 0.6744 0.3645 0.5076 0.0150  0.0360  -0.0168 349  PHE A CD2 
2458  C  CE1 . PHE A 349 ? 0.6825 0.3509 0.4854 0.0319  0.0186  -0.0276 349  PHE A CE1 
2459  C  CE2 . PHE A 349 ? 0.5294 0.2025 0.3523 0.0136  0.0277  -0.0127 349  PHE A CE2 
2460  C  CZ  . PHE A 349 ? 0.5767 0.2388 0.3838 0.0225  0.0191  -0.0182 349  PHE A CZ  
2461  N  N   . PRO A 350 ? 0.5692 0.2950 0.4588 0.0186  0.0360  -0.0319 350  PRO A N   
2462  C  CA  . PRO A 350 ? 0.5292 0.2666 0.4373 0.0120  0.0359  -0.0264 350  PRO A CA  
2463  C  C   . PRO A 350 ? 0.5653 0.2921 0.4704 0.0038  0.0391  -0.0177 350  PRO A C   
2464  O  O   . PRO A 350 ? 0.5972 0.3069 0.4836 0.0016  0.0365  -0.0126 350  PRO A O   
2465  C  CB  . PRO A 350 ? 0.4972 0.2406 0.4048 0.0137  0.0269  -0.0259 350  PRO A CB  
2466  C  CG  . PRO A 350 ? 0.5510 0.2809 0.4364 0.0192  0.0220  -0.0283 350  PRO A CG  
2467  C  CD  . PRO A 350 ? 0.5172 0.2422 0.3965 0.0237  0.0271  -0.0344 350  PRO A CD  
2468  N  N   . ILE A 351 ? 0.5298 0.2664 0.4537 -0.0010 0.0441  -0.0158 351  ILE A N   
2469  C  CA  . ILE A 351 ? 0.5227 0.2557 0.4493 -0.0104 0.0459  -0.0071 351  ILE A CA  
2470  C  C   . ILE A 351 ? 0.5601 0.3029 0.4971 -0.0118 0.0390  -0.0053 351  ILE A C   
2471  O  O   . ILE A 351 ? 0.4823 0.2414 0.4370 -0.0093 0.0386  -0.0085 351  ILE A O   
2472  C  CB  . ILE A 351 ? 0.5717 0.3230 0.5131 -0.0143 0.0551  -0.0057 351  ILE A CB  
2473  C  CG1 . ILE A 351 ? 0.5298 0.2889 0.4625 -0.0098 0.0623  -0.0091 351  ILE A CG1 
2474  C  CG2 . ILE A 351 ? 0.3609 0.1117 0.3036 -0.0253 0.0572  0.0038  351  ILE A CG2 
2475  C  CD1 . ILE A 351 ? 0.3920 0.1722 0.3402 -0.0111 0.0714  -0.0098 351  ILE A CD1 
2476  N  N   . ALA A 352 ? 0.5527 0.2851 0.4774 -0.0154 0.0333  -0.0001 352  ALA A N   
2477  C  CA  . ALA A 352 ? 0.4655 0.2055 0.3966 -0.0153 0.0257  0.0008  352  ALA A CA  
2478  C  C   . ALA A 352 ? 0.5293 0.2732 0.4749 -0.0231 0.0278  0.0053  352  ALA A C   
2479  O  O   . ALA A 352 ? 0.5774 0.3137 0.5226 -0.0309 0.0337  0.0101  352  ALA A O   
2480  C  CB  . ALA A 352 ? 0.3874 0.1128 0.2979 -0.0141 0.0171  0.0027  352  ALA A CB  
2481  N  N   . ASP A 353 ? 0.5028 0.2588 0.4617 -0.0214 0.0232  0.0041  353  ASP A N   
2482  C  CA  . ASP A 353 ? 0.4926 0.2532 0.4670 -0.0277 0.0239  0.0073  353  ASP A CA  
2483  C  C   . ASP A 353 ? 0.4346 0.2030 0.4256 -0.0312 0.0335  0.0071  353  ASP A C   
2484  O  O   . ASP A 353 ? 0.3740 0.1441 0.3767 -0.0389 0.0355  0.0106  353  ASP A O   
2485  C  CB  . ASP A 353 ? 0.6647 0.4103 0.6289 -0.0361 0.0198  0.0134  353  ASP A CB  
2486  C  CG  . ASP A 353 ? 0.9984 0.7431 0.9621 -0.0343 0.0090  0.0133  353  ASP A CG  
2487  O  OD1 . ASP A 353 ? 1.1198 0.8697 1.0981 -0.0386 0.0073  0.0148  353  ASP A OD1 
2488  O  OD2 . ASP A 353 ? 1.1141 0.8528 1.0629 -0.0284 0.0019  0.0115  353  ASP A OD2 
2489  N  N   . ALA A 354 ? 0.5166 0.2892 0.5091 -0.0258 0.0389  0.0025  354  ALA A N   
2490  C  CA  . ALA A 354 ? 0.5894 0.3694 0.5982 -0.0267 0.0468  0.0005  354  ALA A CA  
2491  C  C   . ALA A 354 ? 0.5558 0.3495 0.5836 -0.0236 0.0439  -0.0016 354  ALA A C   
2492  O  O   . ALA A 354 ? 0.3780 0.1764 0.4049 -0.0193 0.0369  -0.0022 354  ALA A O   
2493  C  CB  . ALA A 354 ? 0.4701 0.2498 0.4750 -0.0199 0.0514  -0.0055 354  ALA A CB  
2494  N  N   . ASN A 355 ? 0.4867 0.2862 0.5309 -0.0257 0.0494  -0.0027 355  ASN A N   
2495  C  CA  . ASN A 355 ? 0.5166 0.3266 0.5781 -0.0215 0.0468  -0.0052 355  ASN A CA  
2496  C  C   . ASN A 355 ? 0.5749 0.3910 0.6446 -0.0133 0.0508  -0.0117 355  ASN A C   
2497  O  O   . ASN A 355 ? 0.7105 0.5370 0.7809 -0.0121 0.0576  -0.0144 355  ASN A O   
2498  C  CB  . ASN A 355 ? 0.6081 0.4287 0.6839 -0.0283 0.0476  -0.0022 355  ASN A CB  
2499  C  CG  . ASN A 355 ? 0.7324 0.5419 0.8044 -0.0349 0.0399  0.0027  355  ASN A CG  
2500  O  OD1 . ASN A 355 ? 0.8138 0.6243 0.8846 -0.0445 0.0409  0.0074  355  ASN A OD1 
2501  N  ND2 . ASN A 355 ? 0.7042 0.5163 0.7736 -0.0276 0.0320  0.0014  355  ASN A ND2 
2502  N  N   . VAL A 356 ? 0.4699 0.2933 0.5450 -0.0069 0.0463  -0.0135 356  VAL A N   
2503  C  CA  . VAL A 356 ? 0.5018 0.3303 0.5850 0.0004  0.0484  -0.0190 356  VAL A CA  
2504  C  C   . VAL A 356 ? 0.5257 0.3603 0.6245 0.0036  0.0462  -0.0195 356  VAL A C   
2505  O  O   . VAL A 356 ? 0.5408 0.3788 0.6407 0.0042  0.0404  -0.0164 356  VAL A O   
2506  C  CB  . VAL A 356 ? 0.5952 0.4258 0.6704 0.0038  0.0453  -0.0199 356  VAL A CB  
2507  C  CG1 . VAL A 356 ? 0.5448 0.3796 0.6296 0.0096  0.0459  -0.0243 356  VAL A CG1 
2508  C  CG2 . VAL A 356 ? 0.3615 0.1854 0.4215 0.0025  0.0472  -0.0211 356  VAL A CG2 
2509  N  N   . TYR A 357 ? 0.4533 0.2917 0.5634 0.0069  0.0507  -0.0240 357  TYR A N   
2510  C  CA  . TYR A 357 ? 0.3967 0.2443 0.5218 0.0109  0.0486  -0.0251 357  TYR A CA  
2511  C  C   . TYR A 357 ? 0.5408 0.3865 0.6716 0.0208  0.0483  -0.0305 357  TYR A C   
2512  O  O   . TYR A 357 ? 0.3413 0.1877 0.4695 0.0244  0.0521  -0.0355 357  TYR A O   
2513  C  CB  . TYR A 357 ? 0.4438 0.3126 0.5798 0.0075  0.0531  -0.0255 357  TYR A CB  
2514  C  CG  . TYR A 357 ? 0.5164 0.3887 0.6521 -0.0031 0.0521  -0.0196 357  TYR A CG  
2515  C  CD1 . TYR A 357 ? 0.5745 0.4473 0.7006 -0.0112 0.0570  -0.0163 357  TYR A CD1 
2516  C  CD2 . TYR A 357 ? 0.4282 0.3028 0.5730 -0.0050 0.0461  -0.0174 357  TYR A CD2 
2517  C  CE1 . TYR A 357 ? 0.5830 0.4568 0.7088 -0.0219 0.0557  -0.0105 357  TYR A CE1 
2518  C  CE2 . TYR A 357 ? 0.4096 0.2862 0.5550 -0.0151 0.0442  -0.0127 357  TYR A CE2 
2519  C  CZ  . TYR A 357 ? 0.4853 0.3608 0.6214 -0.0241 0.0490  -0.0090 357  TYR A CZ  
2520  O  OH  . TYR A 357 ? 0.5487 0.4237 0.6852 -0.0350 0.0466  -0.0038 357  TYR A OH  
2521  N  N   . VAL A 358 ? 0.6863 0.5333 0.8238 0.0246  0.0432  -0.0291 358  VAL A N   
2522  C  CA  . VAL A 358 ? 0.5751 0.4234 0.7185 0.0327  0.0417  -0.0326 358  VAL A CA  
2523  C  C   . VAL A 358 ? 0.6133 0.4673 0.7707 0.0400  0.0409  -0.0361 358  VAL A C   
2524  O  O   . VAL A 358 ? 0.6089 0.4660 0.7705 0.0384  0.0368  -0.0326 358  VAL A O   
2525  C  CB  . VAL A 358 ? 0.4553 0.3007 0.5928 0.0316  0.0363  -0.0274 358  VAL A CB  
2526  C  CG1 . VAL A 358 ? 0.4394 0.2818 0.5820 0.0391  0.0343  -0.0301 358  VAL A CG1 
2527  C  CG2 . VAL A 358 ? 0.4166 0.2600 0.5424 0.0262  0.0371  -0.0253 358  VAL A CG2 
2528  N  N   . ALA A 359 ? 0.5934 0.4573 0.7577 0.0469  0.0438  -0.0426 359  ALA A N   
2529  C  CA  . ALA A 359 ? 0.6392 0.5192 0.8172 0.0534  0.0425  -0.0461 359  ALA A CA  
2530  C  C   . ALA A 359 ? 0.5018 0.3721 0.6822 0.0585  0.0351  -0.0432 359  ALA A C   
2531  O  O   . ALA A 359 ? 0.5411 0.3965 0.7154 0.0624  0.0317  -0.0419 359  ALA A O   
2532  C  CB  . ALA A 359 ? 0.6005 0.4873 0.7829 0.0632  0.0451  -0.0544 359  ALA A CB  
2533  N  N   . GLY A 360 ? 0.4326 0.3152 0.6210 0.0564  0.0323  -0.0413 360  GLY A N   
2534  C  CA  . GLY A 360 ? 0.3424 0.2177 0.5324 0.0620  0.0248  -0.0388 360  GLY A CA  
2535  C  C   . GLY A 360 ? 0.4480 0.3095 0.6280 0.0553  0.0213  -0.0315 360  GLY A C   
2536  O  O   . GLY A 360 ? 0.6577 0.5150 0.8362 0.0583  0.0150  -0.0284 360  GLY A O   
2537  N  N   . LEU A 361 ? 0.4221 0.2785 0.5935 0.0462  0.0250  -0.0289 361  LEU A N   
2538  C  CA  . LEU A 361 ? 0.4620 0.3146 0.6227 0.0378  0.0215  -0.0223 361  LEU A CA  
2539  C  C   . LEU A 361 ? 0.6034 0.4555 0.7628 0.0289  0.0247  -0.0217 361  LEU A C   
2540  O  O   . LEU A 361 ? 0.5004 0.3498 0.6480 0.0219  0.0238  -0.0173 361  LEU A O   
2541  C  CB  . LEU A 361 ? 0.3123 0.1608 0.4596 0.0354  0.0217  -0.0184 361  LEU A CB  
2542  C  CG  . LEU A 361 ? 0.4843 0.3288 0.6304 0.0419  0.0189  -0.0173 361  LEU A CG  
2543  C  CD1 . LEU A 361 ? 0.4831 0.3234 0.6192 0.0385  0.0208  -0.0147 361  LEU A CD1 
2544  C  CD2 . LEU A 361 ? 0.3755 0.2186 0.5204 0.0453  0.0124  -0.0138 361  LEU A CD2 
2545  N  N   . GLU A 362 ? 0.5676 0.4394 0.7385 0.0262  0.0283  -0.0248 362  GLU A N   
2546  C  CA  . GLU A 362 ? 0.4919 0.3716 0.6616 0.0152  0.0324  -0.0229 362  GLU A CA  
2547  C  C   . GLU A 362 ? 0.5188 0.3956 0.6873 0.0074  0.0266  -0.0185 362  GLU A C   
2548  O  O   . GLU A 362 ? 0.5010 0.3778 0.6649 -0.0026 0.0287  -0.0155 362  GLU A O   
2549  C  CB  . GLU A 362 ? 0.5382 0.4422 0.7216 0.0145  0.0387  -0.0270 362  GLU A CB  
2550  C  CG  . GLU A 362 ? 0.7436 0.6501 0.9221 0.0166  0.0466  -0.0303 362  GLU A CG  
2551  C  CD  . GLU A 362 ? 0.9845 0.9067 1.1748 0.0267  0.0493  -0.0374 362  GLU A CD  
2552  O  OE1 . GLU A 362 ? 1.0100 0.9332 1.2086 0.0347  0.0439  -0.0397 362  GLU A OE1 
2553  O  OE2 . GLU A 362 ? 0.9952 0.9280 1.1852 0.0276  0.0565  -0.0409 362  GLU A OE2 
2554  N  N   . GLU A 363 ? 0.4463 0.3194 0.6179 0.0123  0.0189  -0.0181 363  GLU A N   
2555  C  CA  . GLU A 363 ? 0.4532 0.3218 0.6228 0.0064  0.0118  -0.0150 363  GLU A CA  
2556  C  C   . GLU A 363 ? 0.4758 0.3223 0.6265 0.0050  0.0089  -0.0109 363  GLU A C   
2557  O  O   . GLU A 363 ? 0.4769 0.3166 0.6217 -0.0014 0.0040  -0.0083 363  GLU A O   
2558  C  CB  . GLU A 363 ? 0.6072 0.4813 0.7864 0.0134  0.0038  -0.0170 363  GLU A CB  
2559  C  CG  . GLU A 363 ? 0.8696 0.7685 1.0692 0.0125  0.0047  -0.0213 363  GLU A CG  
2560  C  CD  . GLU A 363 ? 1.0300 0.9343 1.2386 0.0204  -0.0043 -0.0239 363  GLU A CD  
2561  O  OE1 . GLU A 363 ? 1.0244 0.9202 1.2281 0.0322  -0.0070 -0.0246 363  GLU A OE1 
2562  O  OE2 . GLU A 363 ? 1.1467 1.0638 1.3673 0.0146  -0.0089 -0.0254 363  GLU A OE2 
2563  N  N   . LYS A 364 ? 0.4000 0.2442 0.5416 0.0103  0.0117  -0.0105 364  LYS A N   
2564  C  CA  . LYS A 364 ? 0.4441 0.2867 0.5690 0.0085  0.0101  -0.0071 364  LYS A CA  
2565  C  C   . LYS A 364 ? 0.4917 0.3345 0.6094 0.0062  0.0172  -0.0076 364  LYS A C   
2566  O  O   . LYS A 364 ? 0.5625 0.4074 0.6765 0.0102  0.0193  -0.0081 364  LYS A O   
2567  C  CB  . LYS A 364 ? 0.4581 0.3021 0.5773 0.0152  0.0059  -0.0056 364  LYS A CB  
2568  C  CG  . LYS A 364 ? 0.3737 0.2162 0.4769 0.0140  0.0041  -0.0029 364  LYS A CG  
2569  C  CD  . LYS A 364 ? 0.4028 0.2409 0.4992 0.0094  -0.0010 -0.0017 364  LYS A CD  
2570  C  CE  . LYS A 364 ? 0.4093 0.2450 0.4898 0.0108  -0.0051 0.0000  364  LYS A CE  
2571  N  NZ  . LYS A 364 ? 0.3820 0.2112 0.4543 0.0061  -0.0096 0.0005  364  LYS A NZ  
2572  N  N   . PRO A 365 ? 0.4725 0.3118 0.5877 -0.0009 0.0205  -0.0072 365  PRO A N   
2573  C  CA  . PRO A 365 ? 0.4672 0.3047 0.5726 -0.0027 0.0263  -0.0077 365  PRO A CA  
2574  C  C   . PRO A 365 ? 0.5413 0.3773 0.6307 -0.0021 0.0226  -0.0056 365  PRO A C   
2575  O  O   . PRO A 365 ? 0.4957 0.3301 0.5799 -0.0023 0.0159  -0.0033 365  PRO A O   
2576  C  CB  . PRO A 365 ? 0.5769 0.4090 0.6826 -0.0118 0.0297  -0.0064 365  PRO A CB  
2577  C  CG  . PRO A 365 ? 0.5924 0.4249 0.7108 -0.0160 0.0258  -0.0054 365  PRO A CG  
2578  C  CD  . PRO A 365 ? 0.5983 0.4337 0.7181 -0.0086 0.0181  -0.0056 365  PRO A CD  
2579  N  N   . MET A 366 ? 0.5321 0.3680 0.6139 -0.0008 0.0265  -0.0071 366  MET A N   
2580  C  CA  . MET A 366 ? 0.4232 0.2569 0.4900 -0.0005 0.0234  -0.0059 366  MET A CA  
2581  C  C   . MET A 366 ? 0.4437 0.2696 0.4995 -0.0053 0.0251  -0.0051 366  MET A C   
2582  O  O   . MET A 366 ? 0.5532 0.3766 0.6114 -0.0076 0.0311  -0.0065 366  MET A O   
2583  C  CB  . MET A 366 ? 0.5560 0.3932 0.6215 0.0031  0.0259  -0.0082 366  MET A CB  
2584  C  CG  . MET A 366 ? 0.5508 0.3930 0.6239 0.0071  0.0241  -0.0078 366  MET A CG  
2585  S  SD  . MET A 366 ? 0.4197 0.2618 0.4859 0.0084  0.0168  -0.0043 366  MET A SD  
2586  C  CE  . MET A 366 ? 0.5860 0.4289 0.6642 0.0096  0.0141  -0.0033 366  MET A CE  
2587  N  N   . ARG A 367 ? 0.4148 0.2352 0.4576 -0.0065 0.0195  -0.0030 367  ARG A N   
2588  C  CA  . ARG A 367 ? 0.4540 0.2639 0.4831 -0.0108 0.0199  -0.0016 367  ARG A CA  
2589  C  C   . ARG A 367 ? 0.4525 0.2603 0.4681 -0.0072 0.0197  -0.0036 367  ARG A C   
2590  O  O   . ARG A 367 ? 0.7135 0.5239 0.7243 -0.0035 0.0147  -0.0041 367  ARG A O   
2591  C  CB  . ARG A 367 ? 0.5980 0.4001 0.6206 -0.0143 0.0123  0.0016  367  ARG A CB  
2592  C  CG  . ARG A 367 ? 0.7595 0.5476 0.7659 -0.0192 0.0112  0.0040  367  ARG A CG  
2593  C  CD  . ARG A 367 ? 0.9470 0.7295 0.9364 -0.0146 0.0041  0.0032  367  ARG A CD  
2594  N  NE  . ARG A 367 ? 1.1423 0.9098 1.1190 -0.0188 -0.0027 0.0062  367  ARG A NE  
2595  C  CZ  . ARG A 367 ? 1.2481 1.0112 1.2205 -0.0173 -0.0122 0.0065  367  ARG A CZ  
2596  N  NH1 . ARG A 367 ? 1.3256 1.0986 1.3044 -0.0113 -0.0158 0.0044  367  ARG A NH1 
2597  N  NH2 . ARG A 367 ? 1.2405 0.9870 1.2007 -0.0219 -0.0184 0.0092  367  ARG A NH2 
2598  N  N   . THR A 368 ? 0.3018 0.1049 0.3119 -0.0082 0.0251  -0.0051 368  THR A N   
2599  C  CA  . THR A 368 ? 0.3970 0.1983 0.3957 -0.0044 0.0244  -0.0078 368  THR A CA  
2600  C  C   . THR A 368 ? 0.4708 0.2629 0.4519 -0.0039 0.0174  -0.0062 368  THR A C   
2601  O  O   . THR A 368 ? 0.4665 0.2489 0.4400 -0.0077 0.0142  -0.0029 368  THR A O   
2602  C  CB  . THR A 368 ? 0.3502 0.1459 0.3442 -0.0045 0.0307  -0.0104 368  THR A CB  
2603  O  OG1 . THR A 368 ? 0.3525 0.1347 0.3345 -0.0094 0.0321  -0.0070 368  THR A OG1 
2604  C  CG2 . THR A 368 ? 0.2994 0.1026 0.3098 -0.0038 0.0371  -0.0132 368  THR A CG2 
2605  N  N   . SER A 369 ? 0.4046 0.1992 0.3799 0.0007  0.0146  -0.0089 369  SER A N   
2606  C  CA  . SER A 369 ? 0.2940 0.0798 0.2522 0.0030  0.0075  -0.0087 369  SER A CA  
2607  C  C   . SER A 369 ? 0.5381 0.3086 0.4788 0.0020  0.0082  -0.0086 369  SER A C   
2608  O  O   . SER A 369 ? 0.6674 0.4348 0.6097 -0.0005 0.0148  -0.0087 369  SER A O   
2609  C  CB  . SER A 369 ? 0.2544 0.0483 0.2143 0.0079  0.0052  -0.0119 369  SER A CB  
2610  O  OG  . SER A 369 ? 0.3252 0.1190 0.2836 0.0096  0.0086  -0.0155 369  SER A OG  
2611  N  N   . LYS A 370 ? 0.5000 0.2595 0.4231 0.0046  0.0012  -0.0085 370  LYS A N   
2612  C  CA  . LYS A 370 ? 0.5339 0.2760 0.4373 0.0049  0.0007  -0.0083 370  LYS A CA  
2613  C  C   . LYS A 370 ? 0.4207 0.1657 0.3245 0.0081  0.0059  -0.0126 370  LYS A C   
2614  O  O   . LYS A 370 ? 0.6929 0.4247 0.5843 0.0075  0.0089  -0.0123 370  LYS A O   
2615  C  CB  . LYS A 370 ? 0.4719 0.2019 0.3561 0.0094  -0.0091 -0.0087 370  LYS A CB  
2616  C  CG  . LYS A 370 ? 0.5001 0.2208 0.3790 0.0062  -0.0154 -0.0048 370  LYS A CG  
2617  C  CD  . LYS A 370 ? 0.4992 0.2122 0.3634 0.0127  -0.0262 -0.0067 370  LYS A CD  
2618  C  CE  . LYS A 370 ? 0.5002 0.2039 0.3610 0.0096  -0.0333 -0.0036 370  LYS A CE  
2619  N  NZ  . LYS A 370 ? 0.6556 0.3448 0.4967 0.0162  -0.0449 -0.0055 370  LYS A NZ  
2620  N  N   . ARG A 371 ? 0.3205 0.0815 0.2386 0.0112  0.0067  -0.0166 371  ARG A N   
2621  C  CA  . ARG A 371 ? 0.4542 0.2189 0.3753 0.0142  0.0103  -0.0217 371  ARG A CA  
2622  C  C   . ARG A 371 ? 0.4048 0.1786 0.3434 0.0112  0.0182  -0.0224 371  ARG A C   
2623  O  O   . ARG A 371 ? 0.5445 0.3239 0.4902 0.0136  0.0209  -0.0273 371  ARG A O   
2624  C  CB  . ARG A 371 ? 0.5120 0.2863 0.4377 0.0190  0.0055  -0.0262 371  ARG A CB  
2625  C  CG  . ARG A 371 ? 0.4882 0.2554 0.3991 0.0228  -0.0030 -0.0257 371  ARG A CG  
2626  C  CD  . ARG A 371 ? 0.5598 0.3303 0.4683 0.0290  -0.0079 -0.0315 371  ARG A CD  
2627  N  NE  . ARG A 371 ? 0.6545 0.4417 0.5831 0.0287  -0.0068 -0.0338 371  ARG A NE  
2628  C  CZ  . ARG A 371 ? 0.8424 0.6358 0.7748 0.0311  -0.0109 -0.0344 371  ARG A CZ  
2629  N  NH1 . ARG A 371 ? 0.8380 0.6443 0.7893 0.0295  -0.0080 -0.0361 371  ARG A NH1 
2630  N  NH2 . ARG A 371 ? 1.0283 0.8140 0.9458 0.0352  -0.0178 -0.0336 371  ARG A NH2 
2631  N  N   . GLY A 372 ? 0.4448 0.2193 0.3904 0.0064  0.0212  -0.0180 372  GLY A N   
2632  C  CA  . GLY A 372 ? 0.5577 0.3387 0.5186 0.0043  0.0284  -0.0188 372  GLY A CA  
2633  C  C   . GLY A 372 ? 0.3986 0.1950 0.3782 0.0061  0.0287  -0.0213 372  GLY A C   
2634  O  O   . GLY A 372 ? 0.3460 0.1471 0.3371 0.0065  0.0335  -0.0241 372  GLY A O   
2635  N  N   . GLU A 373 ? 0.3527 0.1552 0.3346 0.0073  0.0235  -0.0204 373  GLU A N   
2636  C  CA  . GLU A 373 ? 0.5100 0.3244 0.5083 0.0082  0.0238  -0.0216 373  GLU A CA  
2637  C  C   . GLU A 373 ? 0.5530 0.3728 0.5626 0.0063  0.0248  -0.0179 373  GLU A C   
2638  O  O   . GLU A 373 ? 0.5681 0.3843 0.5726 0.0044  0.0225  -0.0143 373  GLU A O   
2639  C  CB  . GLU A 373 ? 0.4804 0.2982 0.4766 0.0104  0.0187  -0.0223 373  GLU A CB  
2640  C  CG  . GLU A 373 ? 0.5844 0.3942 0.5637 0.0129  0.0143  -0.0241 373  GLU A CG  
2641  C  CD  . GLU A 373 ? 0.5706 0.3842 0.5491 0.0154  0.0091  -0.0246 373  GLU A CD  
2642  O  OE1 . GLU A 373 ? 0.3724 0.1934 0.3625 0.0160  0.0099  -0.0275 373  GLU A OE1 
2643  O  OE2 . GLU A 373 ? 0.5217 0.3299 0.4883 0.0168  0.0040  -0.0224 373  GLU A OE2 
2644  N  N   . TYR A 374 ? 0.4313 0.2584 0.4558 0.0069  0.0273  -0.0191 374  TYR A N   
2645  C  CA  . TYR A 374 ? 0.4611 0.2933 0.4963 0.0064  0.0272  -0.0161 374  TYR A CA  
2646  C  C   . TYR A 374 ? 0.5723 0.4102 0.6188 0.0081  0.0275  -0.0170 374  TYR A C   
2647  O  O   . TYR A 374 ? 0.4345 0.2724 0.4847 0.0089  0.0292  -0.0207 374  TYR A O   
2648  C  CB  . TYR A 374 ? 0.3842 0.2153 0.4265 0.0051  0.0314  -0.0162 374  TYR A CB  
2649  C  CG  . TYR A 374 ? 0.4600 0.2931 0.5124 0.0071  0.0355  -0.0204 374  TYR A CG  
2650  C  CD1 . TYR A 374 ? 0.3165 0.1450 0.3640 0.0079  0.0388  -0.0248 374  TYR A CD1 
2651  C  CD2 . TYR A 374 ? 0.4411 0.2787 0.5064 0.0089  0.0355  -0.0205 374  TYR A CD2 
2652  C  CE1 . TYR A 374 ? 0.4607 0.2900 0.5168 0.0108  0.0414  -0.0299 374  TYR A CE1 
2653  C  CE2 . TYR A 374 ? 0.4432 0.2804 0.5167 0.0114  0.0380  -0.0248 374  TYR A CE2 
2654  C  CZ  . TYR A 374 ? 0.4289 0.2624 0.4981 0.0124  0.0408  -0.0299 374  TYR A CZ  
2655  O  OH  . TYR A 374 ? 0.4556 0.2880 0.5324 0.0158  0.0422  -0.0354 374  TYR A OH  
2656  N  N   . TRP A 375 ? 0.4564 0.2974 0.5075 0.0087  0.0255  -0.0136 375  TRP A N   
2657  C  CA  . TRP A 375 ? 0.2492 0.0930 0.3105 0.0099  0.0263  -0.0132 375  TRP A CA  
2658  C  C   . TRP A 375 ? 0.4453 0.2900 0.5140 0.0108  0.0264  -0.0108 375  TRP A C   
2659  O  O   . TRP A 375 ? 0.5047 0.3497 0.5698 0.0108  0.0234  -0.0080 375  TRP A O   
2660  C  CB  . TRP A 375 ? 0.3054 0.1503 0.3629 0.0106  0.0236  -0.0110 375  TRP A CB  
2661  C  CG  . TRP A 375 ? 0.3373 0.1812 0.3865 0.0104  0.0222  -0.0133 375  TRP A CG  
2662  C  CD1 . TRP A 375 ? 0.3235 0.1678 0.3766 0.0102  0.0230  -0.0159 375  TRP A CD1 
2663  C  CD2 . TRP A 375 ? 0.3927 0.2338 0.4283 0.0106  0.0189  -0.0136 375  TRP A CD2 
2664  N  NE1 . TRP A 375 ? 0.2873 0.1302 0.3304 0.0108  0.0203  -0.0182 375  TRP A NE1 
2665  C  CE2 . TRP A 375 ? 0.4155 0.2557 0.4467 0.0113  0.0177  -0.0166 375  TRP A CE2 
2666  C  CE3 . TRP A 375 ? 0.2606 0.0981 0.2874 0.0101  0.0163  -0.0117 375  TRP A CE3 
2667  C  CZ2 . TRP A 375 ? 0.3330 0.1688 0.3500 0.0125  0.0138  -0.0178 375  TRP A CZ2 
2668  C  CZ3 . TRP A 375 ? 0.2632 0.0951 0.2757 0.0106  0.0127  -0.0125 375  TRP A CZ3 
2669  C  CH2 . TRP A 375 ? 0.2874 0.1182 0.2943 0.0122  0.0114  -0.0154 375  TRP A CH2 
2670  N  N   . ARG A 376 ? 0.3794 0.2235 0.4584 0.0121  0.0289  -0.0124 376  ARG A N   
2671  C  CA  . ARG A 376 ? 0.2914 0.1356 0.3777 0.0140  0.0283  -0.0106 376  ARG A CA  
2672  C  C   . ARG A 376 ? 0.4523 0.2941 0.5441 0.0162  0.0280  -0.0087 376  ARG A C   
2673  O  O   . ARG A 376 ? 0.3165 0.1549 0.4144 0.0171  0.0298  -0.0112 376  ARG A O   
2674  C  CB  . ARG A 376 ? 0.3491 0.1926 0.4418 0.0147  0.0311  -0.0141 376  ARG A CB  
2675  C  CG  . ARG A 376 ? 0.4677 0.3114 0.5696 0.0176  0.0301  -0.0133 376  ARG A CG  
2676  C  CD  . ARG A 376 ? 0.4419 0.2874 0.5419 0.0167  0.0267  -0.0100 376  ARG A CD  
2677  N  NE  . ARG A 376 ? 0.5366 0.3819 0.6459 0.0202  0.0249  -0.0099 376  ARG A NE  
2678  C  CZ  . ARG A 376 ? 0.6025 0.4485 0.7129 0.0206  0.0207  -0.0076 376  ARG A CZ  
2679  N  NH1 . ARG A 376 ? 0.8826 0.7288 0.9846 0.0175  0.0176  -0.0053 376  ARG A NH1 
2680  N  NH2 . ARG A 376 ? 0.6881 0.5337 0.8075 0.0249  0.0187  -0.0084 376  ARG A NH2 
2681  N  N   . LEU A 377 ? 0.4136 0.2555 0.5024 0.0172  0.0254  -0.0045 377  LEU A N   
2682  C  CA  . LEU A 377 ? 0.3968 0.2343 0.4887 0.0194  0.0255  -0.0014 377  LEU A CA  
2683  C  C   . LEU A 377 ? 0.3398 0.1734 0.4397 0.0226  0.0255  -0.0022 377  LEU A C   
2684  O  O   . LEU A 377 ? 0.5174 0.3531 0.6195 0.0242  0.0238  -0.0028 377  LEU A O   
2685  C  CB  . LEU A 377 ? 0.3108 0.1483 0.3958 0.0209  0.0227  0.0032  377  LEU A CB  
2686  C  CG  . LEU A 377 ? 0.3958 0.2361 0.4715 0.0191  0.0217  0.0036  377  LEU A CG  
2687  C  CD1 . LEU A 377 ? 0.3921 0.2304 0.4612 0.0220  0.0192  0.0079  377  LEU A CD1 
2688  C  CD2 . LEU A 377 ? 0.3642 0.2042 0.4414 0.0168  0.0248  0.0018  377  LEU A CD2 
2689  N  N   . LEU A 378 ? 0.4827 0.3097 0.5874 0.0238  0.0269  -0.0024 378  LEU A N   
2690  C  CA  . LEU A 378 ? 0.4359 0.2572 0.5472 0.0281  0.0261  -0.0038 378  LEU A CA  
2691  C  C   . LEU A 378 ? 0.2550 0.0653 0.3671 0.0306  0.0258  0.0001  378  LEU A C   
2692  O  O   . LEU A 378 ? 0.4239 0.2297 0.5353 0.0279  0.0275  0.0019  378  LEU A O   
2693  C  CB  . LEU A 378 ? 0.3652 0.1867 0.4820 0.0284  0.0278  -0.0104 378  LEU A CB  
2694  C  CG  . LEU A 378 ? 0.3082 0.1375 0.4252 0.0274  0.0289  -0.0141 378  LEU A CG  
2695  C  CD1 . LEU A 378 ? 0.3394 0.1675 0.4596 0.0281  0.0313  -0.0207 378  LEU A CD1 
2696  C  CD2 . LEU A 378 ? 0.3156 0.1471 0.4369 0.0309  0.0270  -0.0138 378  LEU A CD2 
2697  N  N   . THR A 379 ? 0.4832 0.2883 0.5968 0.0361  0.0233  0.0014  379  THR A N   
2698  C  CA  . THR A 379 ? 0.5381 0.3295 0.6521 0.0398  0.0226  0.0045  379  THR A CA  
2699  C  C   . THR A 379 ? 0.5949 0.3796 0.7153 0.0400  0.0231  -0.0010 379  THR A C   
2700  O  O   . THR A 379 ? 0.4875 0.2790 0.6119 0.0399  0.0235  -0.0075 379  THR A O   
2701  C  CB  . THR A 379 ? 0.6724 0.4606 0.7861 0.0471  0.0188  0.0056  379  THR A CB  
2702  O  OG1 . THR A 379 ? 0.7880 0.5798 0.8946 0.0476  0.0174  0.0107  379  THR A OG1 
2703  C  CG2 . THR A 379 ? 0.8771 0.6486 0.9908 0.0528  0.0171  0.0075  379  THR A CG2 
2704  N  N   . PRO A 380 ? 0.5402 0.3105 0.6612 0.0403  0.0230  0.0015  380  PRO A N   
2705  C  CA  . PRO A 380 ? 0.5851 0.3458 0.7118 0.0420  0.0218  -0.0045 380  PRO A CA  
2706  C  C   . PRO A 380 ? 0.6215 0.3823 0.7513 0.0499  0.0188  -0.0106 380  PRO A C   
2707  O  O   . PRO A 380 ? 0.4158 0.1775 0.5438 0.0554  0.0166  -0.0083 380  PRO A O   
2708  C  CB  . PRO A 380 ? 0.4722 0.2138 0.5977 0.0421  0.0211  0.0011  380  PRO A CB  
2709  C  CG  . PRO A 380 ? 0.5455 0.2910 0.6663 0.0368  0.0245  0.0090  380  PRO A CG  
2710  C  CD  . PRO A 380 ? 0.4575 0.2188 0.5739 0.0384  0.0244  0.0097  380  PRO A CD  
2711  N  N   . GLY A 381 ? 0.5548 0.3150 0.6893 0.0514  0.0184  -0.0188 381  GLY A N   
2712  C  CA  . GLY A 381 ? 0.5142 0.2767 0.6524 0.0596  0.0163  -0.0259 381  GLY A CA  
2713  C  C   . GLY A 381 ? 0.5663 0.3381 0.7076 0.0584  0.0186  -0.0342 381  GLY A C   
2714  O  O   . GLY A 381 ? 0.6391 0.4131 0.7792 0.0517  0.0208  -0.0347 381  GLY A O   
2715  N  N   . LEU A 382 ? 0.4986 0.2762 0.6438 0.0659  0.0183  -0.0412 382  LEU A N   
2716  C  CA  . LEU A 382 ? 0.5376 0.3237 0.6842 0.0658  0.0214  -0.0490 382  LEU A CA  
2717  C  C   . LEU A 382 ? 0.5213 0.3230 0.6704 0.0667  0.0249  -0.0499 382  LEU A C   
2718  O  O   . LEU A 382 ? 0.3755 0.1807 0.5289 0.0726  0.0235  -0.0497 382  LEU A O   
2719  C  CB  . LEU A 382 ? 0.6836 0.4611 0.8328 0.0747  0.0186  -0.0589 382  LEU A CB  
2720  C  CG  . LEU A 382 ? 0.9193 0.6975 1.0730 0.0877  0.0162  -0.0653 382  LEU A CG  
2721  C  CD1 . LEU A 382 ? 1.0716 0.8691 1.2297 0.0912  0.0212  -0.0703 382  LEU A CD1 
2722  C  CD2 . LEU A 382 ? 1.0224 0.7875 1.1763 0.0958  0.0119  -0.0744 382  LEU A CD2 
2723  N  N   . TYR A 383 ? 0.5901 0.4003 0.7365 0.0611  0.0292  -0.0511 383  TYR A N   
2724  C  CA  . TYR A 383 ? 0.4408 0.2636 0.5889 0.0597  0.0331  -0.0506 383  TYR A CA  
2725  C  C   . TYR A 383 ? 0.4951 0.3247 0.6424 0.0611  0.0384  -0.0578 383  TYR A C   
2726  O  O   . TYR A 383 ? 0.5982 0.4239 0.7409 0.0608  0.0389  -0.0621 383  TYR A O   
2727  C  CB  . TYR A 383 ? 0.4641 0.2896 0.6067 0.0500  0.0334  -0.0418 383  TYR A CB  
2728  C  CG  . TYR A 383 ? 0.5723 0.3920 0.7134 0.0487  0.0293  -0.0346 383  TYR A CG  
2729  C  CD1 . TYR A 383 ? 0.5744 0.3848 0.7123 0.0468  0.0276  -0.0325 383  TYR A CD1 
2730  C  CD2 . TYR A 383 ? 0.5545 0.3778 0.6972 0.0496  0.0273  -0.0301 383  TYR A CD2 
2731  C  CE1 . TYR A 383 ? 0.5779 0.3823 0.7135 0.0460  0.0251  -0.0256 383  TYR A CE1 
2732  C  CE2 . TYR A 383 ? 0.5376 0.3552 0.6770 0.0495  0.0239  -0.0237 383  TYR A CE2 
2733  C  CZ  . TYR A 383 ? 0.6182 0.4263 0.7535 0.0478  0.0234  -0.0211 383  TYR A CZ  
2734  O  OH  . TYR A 383 ? 0.4625 0.2641 0.5936 0.0481  0.0212  -0.0144 383  TYR A OH  
2735  N  N   . SER A 384 ? 0.6016 0.4416 0.7536 0.0633  0.0424  -0.0594 384  SER A N   
2736  C  CA  . SER A 384 ? 0.5604 0.4077 0.7104 0.0640  0.0491  -0.0646 384  SER A CA  
2737  C  C   . SER A 384 ? 0.5976 0.4456 0.7419 0.0537  0.0515  -0.0575 384  SER A C   
2738  O  O   . SER A 384 ? 0.3775 0.2315 0.5269 0.0509  0.0516  -0.0533 384  SER A O   
2739  C  CB  . SER A 384 ? 0.4281 0.2938 0.5883 0.0724  0.0529  -0.0710 384  SER A CB  
2740  O  OG  . SER A 384 ? 0.9096 0.7747 1.0711 0.0834  0.0523  -0.0805 384  SER A OG  
2741  N  N   . VAL A 385 ? 0.6451 0.4882 0.7785 0.0476  0.0522  -0.0560 385  VAL A N   
2742  C  CA  . VAL A 385 ? 0.6015 0.4435 0.7270 0.0384  0.0534  -0.0494 385  VAL A CA  
2743  C  C   . VAL A 385 ? 0.5422 0.3900 0.6622 0.0375  0.0601  -0.0524 385  VAL A C   
2744  O  O   . VAL A 385 ? 0.5204 0.3717 0.6373 0.0426  0.0629  -0.0591 385  VAL A O   
2745  C  CB  . VAL A 385 ? 0.4186 0.2560 0.5347 0.0325  0.0495  -0.0452 385  VAL A CB  
2746  C  CG1 . VAL A 385 ? 0.3197 0.1575 0.4283 0.0248  0.0488  -0.0379 385  VAL A CG1 
2747  C  CG2 . VAL A 385 ? 0.4002 0.2352 0.5213 0.0340  0.0444  -0.0433 385  VAL A CG2 
2748  N  N   . HIS A 386 ? 0.3738 0.2284 0.4917 0.0294  0.0620  -0.0460 386  HIS A N   
2749  C  CA  . HIS A 386 ? 0.3345 0.1986 0.4442 0.0246  0.0681  -0.0449 386  HIS A CA  
2750  C  C   . HIS A 386 ? 0.4144 0.2715 0.5149 0.0146  0.0669  -0.0368 386  HIS A C   
2751  O  O   . HIS A 386 ? 0.3488 0.1986 0.4521 0.0113  0.0617  -0.0322 386  HIS A O   
2752  C  CB  . HIS A 386 ? 0.7036 0.5917 0.8234 0.0261  0.0744  -0.0469 386  HIS A CB  
2753  C  CG  . HIS A 386 ? 0.8314 0.7312 0.9618 0.0193  0.0744  -0.0411 386  HIS A CG  
2754  N  ND1 . HIS A 386 ? 0.9938 0.8823 1.1242 0.0134  0.0684  -0.0351 386  HIS A ND1 
2755  C  CD2 . HIS A 386 ? 0.8565 0.7798 0.9987 0.0176  0.0794  -0.0411 386  HIS A CD2 
2756  C  CE1 . HIS A 386 ? 0.7275 0.6305 0.8692 0.0083  0.0690  -0.0319 386  HIS A CE1 
2757  N  NE2 . HIS A 386 ? 0.6569 0.5818 0.8067 0.0101  0.0758  -0.0353 386  HIS A NE2 
2758  N  N   . ALA A 387 ? 0.4473 0.3058 0.5354 0.0105  0.0714  -0.0351 387  ALA A N   
2759  C  CA  . ALA A 387 ? 0.4530 0.3010 0.5291 0.0019  0.0696  -0.0279 387  ALA A CA  
2760  C  C   . ALA A 387 ? 0.5448 0.4049 0.6182 -0.0058 0.0761  -0.0228 387  ALA A C   
2761  O  O   . ALA A 387 ? 0.5431 0.4181 0.6173 -0.0035 0.0834  -0.0255 387  ALA A O   
2762  C  CB  . ALA A 387 ? 0.4912 0.3229 0.5507 0.0040  0.0671  -0.0297 387  ALA A CB  
2763  N  N   . SER A 388 ? 0.3229 0.1767 0.3931 -0.0149 0.0734  -0.0154 388  SER A N   
2764  C  CA  . SER A 388 ? 0.4216 0.2837 0.4883 -0.0243 0.0792  -0.0091 388  SER A CA  
2765  C  C   . SER A 388 ? 0.5692 0.4117 0.6203 -0.0323 0.0744  -0.0019 388  SER A C   
2766  O  O   . SER A 388 ? 0.4746 0.3006 0.5213 -0.0305 0.0661  -0.0021 388  SER A O   
2767  C  CB  . SER A 388 ? 0.4702 0.3524 0.5574 -0.0288 0.0814  -0.0076 388  SER A CB  
2768  O  OG  . SER A 388 ? 0.5407 0.4157 0.6367 -0.0300 0.0729  -0.0066 388  SER A OG  
2769  N  N   . ALA A 389 ? 0.6258 0.4702 0.6680 -0.0406 0.0798  0.0044  389  ALA A N   
2770  C  CA  . ALA A 389 ? 0.5222 0.3466 0.5477 -0.0484 0.0754  0.0117  389  ALA A CA  
2771  C  C   . ALA A 389 ? 0.6000 0.4319 0.6218 -0.0596 0.0831  0.0199  389  ALA A C   
2772  O  O   . ALA A 389 ? 0.7490 0.5977 0.7714 -0.0585 0.0930  0.0193  389  ALA A O   
2773  C  CB  . ALA A 389 ? 0.4070 0.2122 0.4107 -0.0415 0.0720  0.0093  389  ALA A CB  
2774  N  N   . PHE A 390 ? 0.6150 0.4343 0.6328 -0.0704 0.0786  0.0274  390  PHE A N   
2775  C  CA  . PHE A 390 ? 0.8046 0.6268 0.8175 -0.0832 0.0851  0.0368  390  PHE A CA  
2776  C  C   . PHE A 390 ? 0.7915 0.6069 0.7806 -0.0806 0.0917  0.0395  390  PHE A C   
2777  O  O   . PHE A 390 ? 0.8188 0.6139 0.7884 -0.0733 0.0863  0.0373  390  PHE A O   
2778  C  CB  . PHE A 390 ? 0.9992 0.8008 1.0074 -0.0938 0.0762  0.0437  390  PHE A CB  
2779  C  CG  . PHE A 390 ? 1.2571 1.0561 1.2583 -0.1086 0.0817  0.0547  390  PHE A CG  
2780  C  CD1 . PHE A 390 ? 1.3978 1.1701 1.3719 -0.1118 0.0790  0.0614  390  PHE A CD1 
2781  C  CD2 . PHE A 390 ? 1.3647 1.1880 1.3863 -0.1195 0.0893  0.0586  390  PHE A CD2 
2782  C  CE1 . PHE A 390 ? 1.4541 1.2215 1.4203 -0.1262 0.0842  0.0727  390  PHE A CE1 
2783  C  CE2 . PHE A 390 ? 1.4436 1.2648 1.4594 -0.1347 0.0950  0.0697  390  PHE A CE2 
2784  C  CZ  . PHE A 390 ? 1.4440 1.2359 1.4314 -0.1384 0.0926  0.0773  390  PHE A CZ  
2785  N  N   . GLY A 391 ? 0.7141 0.5480 0.7046 -0.0858 0.1036  0.0438  391  GLY A N   
2786  C  CA  . GLY A 391 ? 0.7233 0.5523 0.6902 -0.0827 0.1105  0.0467  391  GLY A CA  
2787  C  C   . GLY A 391 ? 0.6732 0.5133 0.6392 -0.0672 0.1135  0.0359  391  GLY A C   
2788  O  O   . GLY A 391 ? 0.5709 0.4070 0.5168 -0.0612 0.1178  0.0356  391  GLY A O   
2789  N  N   . TYR A 392 ? 0.7155 0.5685 0.7027 -0.0603 0.1106  0.0270  392  TYR A N   
2790  C  CA  . TYR A 392 ? 0.7274 0.5902 0.7165 -0.0459 0.1124  0.0161  392  TYR A CA  
2791  C  C   . TYR A 392 ? 0.6743 0.5654 0.6883 -0.0430 0.1177  0.0107  392  TYR A C   
2792  O  O   . TYR A 392 ? 0.7120 0.6104 0.7456 -0.0483 0.1148  0.0117  392  TYR A O   
2793  C  CB  . TYR A 392 ? 0.7257 0.5694 0.7113 -0.0371 0.1014  0.0089  392  TYR A CB  
2794  C  CG  . TYR A 392 ? 0.8598 0.6788 0.8195 -0.0358 0.0964  0.0112  392  TYR A CG  
2795  C  CD1 . TYR A 392 ? 0.9753 0.7911 0.9190 -0.0257 0.0978  0.0054  392  TYR A CD1 
2796  C  CD2 . TYR A 392 ? 0.6958 0.4946 0.6465 -0.0437 0.0896  0.0185  392  TYR A CD2 
2797  C  CE1 . TYR A 392 ? 0.9304 0.7244 0.8501 -0.0234 0.0927  0.0069  392  TYR A CE1 
2798  C  CE2 . TYR A 392 ? 0.7988 0.5749 0.7249 -0.0411 0.0844  0.0200  392  TYR A CE2 
2799  C  CZ  . TYR A 392 ? 0.9484 0.7227 0.8593 -0.0309 0.0861  0.0142  392  TYR A CZ  
2800  O  OH  . TYR A 392 ? 0.9970 0.7497 0.8834 -0.0273 0.0802  0.0151  392  TYR A OH  
2801  N  N   . GLN A 393 ? 0.8046 0.7116 0.8171 -0.0335 0.1248  0.0044  393  GLN A N   
2802  C  CA  . GLN A 393 ? 0.7379 0.6707 0.7721 -0.0271 0.1287  -0.0030 393  GLN A CA  
2803  C  C   . GLN A 393 ? 0.7392 0.6623 0.7843 -0.0185 0.1186  -0.0117 393  GLN A C   
2804  O  O   . GLN A 393 ? 0.6241 0.5292 0.6578 -0.0111 0.1126  -0.0167 393  GLN A O   
2805  C  CB  . GLN A 393 ? 0.4780 0.4279 0.5048 -0.0174 0.1378  -0.0085 393  GLN A CB  
2806  C  CG  . GLN A 393 ? 0.6857 0.6429 0.6971 -0.0251 0.1485  0.0011  393  GLN A CG  
2807  C  CD  . GLN A 393 ? 0.8935 0.8705 0.8972 -0.0143 0.1581  -0.0045 393  GLN A CD  
2808  O  OE1 . GLN A 393 ? 0.8826 0.8606 0.8864 0.0001  0.1550  -0.0164 393  GLN A OE1 
2809  N  NE2 . GLN A 393 ? 0.8806 0.8731 0.8769 -0.0214 0.1699  0.0043  393  GLN A NE2 
2810  N  N   . THR A 394 ? 0.7528 0.6883 0.8202 -0.0200 0.1166  -0.0130 394  THR A N   
2811  C  CA  . THR A 394 ? 0.7401 0.6666 0.8181 -0.0127 0.1075  -0.0195 394  THR A CA  
2812  C  C   . THR A 394 ? 0.6925 0.6206 0.7688 0.0014  0.1076  -0.0302 394  THR A C   
2813  O  O   . THR A 394 ? 0.7386 0.6872 0.8206 0.0075  0.1143  -0.0351 394  THR A O   
2814  C  CB  . THR A 394 ? 0.6406 0.5837 0.7425 -0.0150 0.1063  -0.0197 394  THR A CB  
2815  O  OG1 . THR A 394 ? 0.6020 0.5444 0.7067 -0.0288 0.1057  -0.0104 394  THR A OG1 
2816  C  CG2 . THR A 394 ? 0.7397 0.6705 0.8495 -0.0076 0.0967  -0.0251 394  THR A CG2 
2817  N  N   . SER A 395 ? 0.5868 0.4935 0.6555 0.0066  0.0999  -0.0341 395  SER A N   
2818  C  CA  . SER A 395 ? 0.6057 0.5101 0.6722 0.0190  0.0985  -0.0445 395  SER A CA  
2819  C  C   . SER A 395 ? 0.6939 0.6140 0.7785 0.0274  0.0991  -0.0517 395  SER A C   
2820  O  O   . SER A 395 ? 0.6489 0.5770 0.7491 0.0246  0.0977  -0.0493 395  SER A O   
2821  C  CB  . SER A 395 ? 0.5451 0.4257 0.6065 0.0214  0.0894  -0.0469 395  SER A CB  
2822  O  OG  . SER A 395 ? 0.5228 0.3998 0.5991 0.0214  0.0837  -0.0466 395  SER A OG  
2823  N  N   . ALA A 396 ? 0.6099 0.5333 0.6915 0.0386  0.1002  -0.0612 396  ALA A N   
2824  C  CA  . ALA A 396 ? 0.5179 0.4495 0.6140 0.0490  0.0982  -0.0697 396  ALA A CA  
2825  C  C   . ALA A 396 ? 0.6947 0.6055 0.7969 0.0498  0.0885  -0.0704 396  ALA A C   
2826  O  O   . ALA A 396 ? 0.8157 0.7070 0.9088 0.0454  0.0839  -0.0675 396  ALA A O   
2827  C  CB  . ALA A 396 ? 0.3828 0.3185 0.4717 0.0612  0.1000  -0.0804 396  ALA A CB  
2828  N  N   . PRO A 397 ? 0.6157 0.5314 0.7329 0.0558  0.0855  -0.0741 397  PRO A N   
2829  C  CA  . PRO A 397 ? 0.5001 0.3969 0.6230 0.0564  0.0770  -0.0732 397  PRO A CA  
2830  C  C   . PRO A 397 ? 0.5559 0.4345 0.6737 0.0638  0.0718  -0.0808 397  PRO A C   
2831  O  O   . PRO A 397 ? 0.5680 0.4514 0.6829 0.0724  0.0734  -0.0895 397  PRO A O   
2832  C  CB  . PRO A 397 ? 0.5684 0.4787 0.7078 0.0618  0.0761  -0.0752 397  PRO A CB  
2833  C  CG  . PRO A 397 ? 0.6614 0.6006 0.8054 0.0629  0.0846  -0.0769 397  PRO A CG  
2834  C  CD  . PRO A 397 ? 0.6951 0.6349 0.8243 0.0631  0.0898  -0.0792 397  PRO A CD  
2835  N  N   . GLN A 398 ? 0.6350 0.4934 0.7521 0.0604  0.0656  -0.0775 398  GLN A N   
2836  C  CA  . GLN A 398 ? 0.6476 0.4898 0.7629 0.0649  0.0598  -0.0832 398  GLN A CA  
2837  C  C   . GLN A 398 ? 0.6224 0.4601 0.7474 0.0642  0.0532  -0.0790 398  GLN A C   
2838  O  O   . GLN A 398 ? 0.6115 0.4496 0.7400 0.0583  0.0521  -0.0708 398  GLN A O   
2839  C  CB  . GLN A 398 ? 0.6156 0.4500 0.7194 0.0567  0.0572  -0.0795 398  GLN A CB  
2840  C  CG  . GLN A 398 ? 0.4418 0.2779 0.5329 0.0593  0.0627  -0.0848 398  GLN A CG  
2841  C  CD  . GLN A 398 ? 0.6051 0.4340 0.6842 0.0519  0.0598  -0.0809 398  GLN A CD  
2842  O  OE1 . GLN A 398 ? 0.6700 0.4943 0.7503 0.0491  0.0533  -0.0805 398  GLN A OE1 
2843  N  NE2 . GLN A 398 ? 0.6840 0.5125 0.7519 0.0493  0.0648  -0.0784 398  GLN A NE2 
2844  N  N   . GLN A 399 ? 0.7100 0.5425 0.8383 0.0709  0.0487  -0.0853 399  GLN A N   
2845  C  CA  . GLN A 399 ? 0.7192 0.5441 0.8544 0.0714  0.0425  -0.0820 399  GLN A CA  
2846  C  C   . GLN A 399 ? 0.7724 0.5861 0.9042 0.0641  0.0374  -0.0782 399  GLN A C   
2847  O  O   . GLN A 399 ? 0.8735 0.6826 1.0010 0.0646  0.0360  -0.0838 399  GLN A O   
2848  C  CB  . GLN A 399 ? 0.7781 0.6024 0.9189 0.0842  0.0403  -0.0916 399  GLN A CB  
2849  C  CG  . GLN A 399 ? 1.0337 0.8435 1.1779 0.0856  0.0326  -0.0904 399  GLN A CG  
2850  C  CD  . GLN A 399 ? 1.2418 1.0461 1.3876 0.0982  0.0288  -0.1020 399  GLN A CD  
2851  O  OE1 . GLN A 399 ? 1.3221 1.1213 1.4635 0.1000  0.0271  -0.1091 399  GLN A OE1 
2852  N  NE2 . GLN A 399 ? 1.3091 1.1147 1.4610 0.1080  0.0267  -0.1047 399  GLN A NE2 
2853  N  N   . VAL A 400 ? 0.7000 0.5102 0.8340 0.0581  0.0349  -0.0692 400  VAL A N   
2854  C  CA  . VAL A 400 ? 0.5992 0.4017 0.7316 0.0515  0.0315  -0.0651 400  VAL A CA  
2855  C  C   . VAL A 400 ? 0.5754 0.3694 0.7127 0.0519  0.0277  -0.0598 400  VAL A C   
2856  O  O   . VAL A 400 ? 0.5556 0.3527 0.6948 0.0530  0.0280  -0.0548 400  VAL A O   
2857  C  CB  . VAL A 400 ? 0.6802 0.4894 0.8067 0.0425  0.0339  -0.0582 400  VAL A CB  
2858  C  CG1 . VAL A 400 ? 0.6903 0.5052 0.8175 0.0396  0.0349  -0.0497 400  VAL A CG1 
2859  C  CG2 . VAL A 400 ? 0.8777 0.6813 1.0037 0.0372  0.0311  -0.0563 400  VAL A CG2 
2860  N  N   . ARG A 401 ? 0.7081 0.4900 0.8472 0.0511  0.0239  -0.0612 401  ARG A N   
2861  C  CA  . ARG A 401 ? 0.7513 0.5218 0.8933 0.0509  0.0208  -0.0554 401  ARG A CA  
2862  C  C   . ARG A 401 ? 0.4739 0.2463 0.6141 0.0418  0.0223  -0.0464 401  ARG A C   
2863  O  O   . ARG A 401 ? 0.5252 0.2947 0.6661 0.0368  0.0219  -0.0473 401  ARG A O   
2864  C  CB  . ARG A 401 ? 0.7090 0.4623 0.8543 0.0554  0.0156  -0.0618 401  ARG A CB  
2865  C  CG  . ARG A 401 ? 0.8106 0.5481 0.9578 0.0541  0.0125  -0.0551 401  ARG A CG  
2866  C  CD  . ARG A 401 ? 1.0188 0.7379 1.1693 0.0545  0.0076  -0.0607 401  ARG A CD  
2867  N  NE  . ARG A 401 ? 1.1925 0.9053 1.3435 0.0651  0.0035  -0.0715 401  ARG A NE  
2868  C  CZ  . ARG A 401 ? 1.2928 1.0016 1.4446 0.0682  0.0004  -0.0823 401  ARG A CZ  
2869  N  NH1 . ARG A 401 ? 1.3869 1.0965 1.5401 0.0611  0.0005  -0.0846 401  ARG A NH1 
2870  N  NH2 . ARG A 401 ? 1.2333 0.9375 1.3845 0.0800  -0.0032 -0.0920 401  ARG A NH2 
2871  N  N   . VAL A 402 ? 0.4817 0.2597 0.6200 0.0405  0.0238  -0.0385 402  VAL A N   
2872  C  CA  . VAL A 402 ? 0.5692 0.3499 0.7048 0.0337  0.0253  -0.0305 402  VAL A CA  
2873  C  C   . VAL A 402 ? 0.7139 0.4803 0.8513 0.0331  0.0236  -0.0251 402  VAL A C   
2874  O  O   . VAL A 402 ? 0.4181 0.1792 0.5542 0.0369  0.0225  -0.0203 402  VAL A O   
2875  C  CB  . VAL A 402 ? 0.3175 0.1100 0.4487 0.0326  0.0271  -0.0248 402  VAL A CB  
2876  C  CG1 . VAL A 402 ? 0.2640 0.0575 0.3917 0.0276  0.0281  -0.0174 402  VAL A CG1 
2877  C  CG2 . VAL A 402 ? 0.3336 0.1380 0.4621 0.0314  0.0293  -0.0287 402  VAL A CG2 
2878  N  N   . THR A 403 ? 0.9231 0.6822 1.0635 0.0285  0.0233  -0.0260 403  THR A N   
2879  C  CA  . THR A 403 ? 0.9512 0.6975 1.0934 0.0253  0.0233  -0.0192 403  THR A CA  
2880  C  C   . THR A 403 ? 0.9599 0.7167 1.1000 0.0190  0.0269  -0.0141 403  THR A C   
2881  O  O   . THR A 403 ? 1.0433 0.8100 1.1838 0.0159  0.0277  -0.0185 403  THR A O   
2882  C  CB  . THR A 403 ? 0.9217 0.6515 1.0706 0.0234  0.0203  -0.0239 403  THR A CB  
2883  O  OG1 . THR A 403 ? 1.0853 0.8036 1.2365 0.0179  0.0215  -0.0161 403  THR A OG1 
2884  C  CG2 . THR A 403 ? 0.8099 0.5473 0.9620 0.0203  0.0200  -0.0323 403  THR A CG2 
2885  N  N   . ASN A 404 ? 0.9305 0.6851 1.0672 0.0183  0.0287  -0.0052 404  ASN A N   
2886  C  CA  . ASN A 404 ? 0.9426 0.7066 1.0767 0.0137  0.0319  -0.0007 404  ASN A CA  
2887  C  C   . ASN A 404 ? 0.9227 0.6748 1.0621 0.0082  0.0336  0.0035  404  ASN A C   
2888  O  O   . ASN A 404 ? 0.5980 0.3471 0.7346 0.0067  0.0364  0.0121  404  ASN A O   
2889  C  CB  . ASN A 404 ? 0.8640 0.6348 0.9898 0.0168  0.0329  0.0059  404  ASN A CB  
2890  C  CG  . ASN A 404 ? 0.5834 0.3676 0.7053 0.0199  0.0315  0.0016  404  ASN A CG  
2891  O  OD1 . ASN A 404 ? 0.4992 0.2925 0.6214 0.0180  0.0316  -0.0040 404  ASN A OD1 
2892  N  ND2 . ASN A 404 ? 0.2871 0.0713 0.4053 0.0246  0.0300  0.0045  404  ASN A ND2 
2893  N  N   . ASP A 405 ? 1.0767 0.8216 1.2242 0.0051  0.0317  -0.0027 405  ASP A N   
2894  C  CA  . ASP A 405 ? 1.2335 0.9653 1.3890 -0.0017 0.0326  0.0000  405  ASP A CA  
2895  C  C   . ASP A 405 ? 0.9454 0.6878 1.1057 -0.0075 0.0341  -0.0036 405  ASP A C   
2896  O  O   . ASP A 405 ? 0.7068 0.4467 0.8712 -0.0136 0.0373  0.0021  405  ASP A O   
2897  C  CB  . ASP A 405 ? 1.4200 1.1337 1.5821 -0.0015 0.0281  -0.0053 405  ASP A CB  
2898  C  CG  . ASP A 405 ? 1.5610 1.2559 1.7313 -0.0093 0.0285  -0.0002 405  ASP A CG  
2899  O  OD1 . ASP A 405 ? 1.4572 1.1564 1.6313 -0.0164 0.0325  0.0044  405  ASP A OD1 
2900  O  OD2 . ASP A 405 ? 1.7343 1.4090 1.9072 -0.0085 0.0247  -0.0009 405  ASP A OD2 
2901  N  N   . ASN A 406 ? 0.7370 0.4908 0.8965 -0.0056 0.0319  -0.0129 406  ASN A N   
2902  C  CA  . ASN A 406 ? 0.8333 0.5963 0.9964 -0.0099 0.0323  -0.0176 406  ASN A CA  
2903  C  C   . ASN A 406 ? 0.7427 0.5205 0.8979 -0.0092 0.0352  -0.0137 406  ASN A C   
2904  O  O   . ASN A 406 ? 0.3733 0.1569 0.5194 -0.0048 0.0363  -0.0090 406  ASN A O   
2905  C  CB  . ASN A 406 ? 0.9920 0.7590 1.1562 -0.0079 0.0284  -0.0292 406  ASN A CB  
2906  C  CG  . ASN A 406 ? 1.0376 0.8135 1.2043 -0.0114 0.0280  -0.0344 406  ASN A CG  
2907  O  OD1 . ASN A 406 ? 0.9089 0.6792 1.0859 -0.0178 0.0279  -0.0352 406  ASN A OD1 
2908  N  ND2 . ASN A 406 ? 1.0989 0.8880 1.2562 -0.0077 0.0276  -0.0378 406  ASN A ND2 
2909  N  N   . GLN A 407 ? 0.8847 0.6680 1.0441 -0.0134 0.0356  -0.0166 407  GLN A N   
2910  C  CA  . GLN A 407 ? 0.9002 0.6942 1.0534 -0.0133 0.0380  -0.0129 407  GLN A CA  
2911  C  C   . GLN A 407 ? 0.8211 0.6274 0.9614 -0.0074 0.0365  -0.0151 407  GLN A C   
2912  O  O   . GLN A 407 ? 0.8441 0.6564 0.9760 -0.0053 0.0378  -0.0102 407  GLN A O   
2913  C  CB  . GLN A 407 ? 0.9897 0.7857 1.1514 -0.0191 0.0381  -0.0171 407  GLN A CB  
2914  C  CG  . GLN A 407 ? 0.9683 0.7554 1.1406 -0.0268 0.0420  -0.0099 407  GLN A CG  
2915  C  CD  . GLN A 407 ? 1.1566 0.9472 1.3399 -0.0340 0.0419  -0.0149 407  GLN A CD  
2916  O  OE1 . GLN A 407 ? 1.1842 0.9790 1.3705 -0.0337 0.0377  -0.0257 407  GLN A OE1 
2917  N  NE2 . GLN A 407 ? 1.2862 1.0754 1.4757 -0.0410 0.0468  -0.0070 407  GLN A NE2 
2918  N  N   . GLU A 408 ? 0.7437 0.5524 0.8818 -0.0050 0.0336  -0.0223 408  GLU A N   
2919  C  CA  . GLU A 408 ? 0.6555 0.4741 0.7815 -0.0010 0.0324  -0.0238 408  GLU A CA  
2920  C  C   . GLU A 408 ? 0.7454 0.5631 0.8682 0.0024  0.0315  -0.0255 408  GLU A C   
2921  O  O   . GLU A 408 ? 0.8192 0.6297 0.9486 0.0026  0.0305  -0.0297 408  GLU A O   
2922  C  CB  . GLU A 408 ? 0.5965 0.4210 0.7192 -0.0014 0.0302  -0.0304 408  GLU A CB  
2923  C  CG  . GLU A 408 ? 0.7741 0.6013 0.8982 -0.0035 0.0310  -0.0284 408  GLU A CG  
2924  C  CD  . GLU A 408 ? 0.8593 0.6923 0.9781 -0.0025 0.0279  -0.0350 408  GLU A CD  
2925  O  OE1 . GLU A 408 ? 0.6567 0.4894 0.7834 -0.0054 0.0277  -0.0382 408  GLU A OE1 
2926  O  OE2 . GLU A 408 ? 1.0624 0.8992 1.1693 0.0010  0.0257  -0.0370 408  GLU A OE2 
2927  N  N   . ALA A 409 ? 0.7228 0.5469 0.8359 0.0050  0.0317  -0.0225 409  ALA A N   
2928  C  CA  . ALA A 409 ? 0.4706 0.2949 0.5813 0.0078  0.0316  -0.0235 409  ALA A CA  
2929  C  C   . ALA A 409 ? 0.6413 0.4636 0.7534 0.0087  0.0306  -0.0314 409  ALA A C   
2930  O  O   . ALA A 409 ? 0.5651 0.3894 0.6743 0.0079  0.0294  -0.0361 409  ALA A O   
2931  C  CB  . ALA A 409 ? 0.4207 0.2523 0.5211 0.0091  0.0314  -0.0204 409  ALA A CB  
2932  N  N   . LEU A 410 ? 0.6456 0.4632 0.7615 0.0114  0.0306  -0.0334 410  LEU A N   
2933  C  CA  . LEU A 410 ? 0.4788 0.2932 0.5954 0.0137  0.0296  -0.0415 410  LEU A CA  
2934  C  C   . LEU A 410 ? 0.4640 0.2849 0.5703 0.0146  0.0306  -0.0437 410  LEU A C   
2935  O  O   . LEU A 410 ? 0.4112 0.2367 0.5120 0.0150  0.0324  -0.0396 410  LEU A O   
2936  C  CB  . LEU A 410 ? 0.6025 0.4108 0.7241 0.0176  0.0295  -0.0428 410  LEU A CB  
2937  C  CG  . LEU A 410 ? 0.8374 0.6341 0.9682 0.0174  0.0273  -0.0433 410  LEU A CG  
2938  C  CD1 . LEU A 410 ? 1.0157 0.8060 1.1494 0.0216  0.0269  -0.0411 410  LEU A CD1 
2939  C  CD2 . LEU A 410 ? 0.8815 0.6716 1.0160 0.0181  0.0244  -0.0528 410  LEU A CD2 
2940  N  N   . ARG A 411 ? 0.5113 0.3312 0.6147 0.0150  0.0292  -0.0504 411  ARG A N   
2941  C  CA  . ARG A 411 ? 0.5115 0.3345 0.6030 0.0163  0.0301  -0.0526 411  ARG A CA  
2942  C  C   . ARG A 411 ? 0.5235 0.3447 0.6132 0.0203  0.0325  -0.0559 411  ARG A C   
2943  O  O   . ARG A 411 ? 0.5272 0.3439 0.6241 0.0235  0.0318  -0.0608 411  ARG A O   
2944  C  CB  . ARG A 411 ? 0.3280 0.1495 0.4159 0.0168  0.0272  -0.0595 411  ARG A CB  
2945  C  CG  . ARG A 411 ? 0.4453 0.2671 0.5189 0.0193  0.0282  -0.0620 411  ARG A CG  
2946  C  CD  . ARG A 411 ? 0.3615 0.1866 0.4245 0.0170  0.0287  -0.0553 411  ARG A CD  
2947  N  NE  . ARG A 411 ? 0.4723 0.2976 0.5300 0.0170  0.0249  -0.0582 411  ARG A NE  
2948  C  CZ  . ARG A 411 ? 0.5979 0.4201 0.6423 0.0198  0.0235  -0.0623 411  ARG A CZ  
2949  N  NH1 . ARG A 411 ? 0.5948 0.4129 0.6293 0.0224  0.0266  -0.0633 411  ARG A NH1 
2950  N  NH2 . ARG A 411 ? 0.5978 0.4204 0.6383 0.0206  0.0192  -0.0655 411  ARG A NH2 
2951  N  N   . LEU A 412 ? 0.5007 0.3245 0.5807 0.0205  0.0353  -0.0536 412  LEU A N   
2952  C  CA  . LEU A 412 ? 0.5068 0.3296 0.5856 0.0242  0.0390  -0.0564 412  LEU A CA  
2953  C  C   . LEU A 412 ? 0.5508 0.3739 0.6168 0.0229  0.0420  -0.0539 412  LEU A C   
2954  O  O   . LEU A 412 ? 0.4787 0.3040 0.5424 0.0193  0.0424  -0.0468 412  LEU A O   
2955  C  CB  . LEU A 412 ? 0.5489 0.3733 0.6376 0.0248  0.0401  -0.0527 412  LEU A CB  
2956  C  CG  . LEU A 412 ? 0.6335 0.4581 0.7246 0.0299  0.0439  -0.0567 412  LEU A CG  
2957  C  CD1 . LEU A 412 ? 0.7830 0.6036 0.8774 0.0364  0.0429  -0.0663 412  LEU A CD1 
2958  C  CD2 . LEU A 412 ? 0.3910 0.2182 0.4910 0.0301  0.0443  -0.0520 412  LEU A CD2 
2959  N  N   . ASP A 413 ? 0.6557 0.4752 0.7123 0.0264  0.0438  -0.0599 413  ASP A N   
2960  C  CA  . ASP A 413 ? 0.5356 0.3516 0.5773 0.0254  0.0466  -0.0576 413  ASP A CA  
2961  C  C   . ASP A 413 ? 0.5299 0.3442 0.5693 0.0285  0.0534  -0.0599 413  ASP A C   
2962  O  O   . ASP A 413 ? 0.5766 0.3940 0.6252 0.0333  0.0556  -0.0650 413  ASP A O   
2963  C  CB  . ASP A 413 ? 0.5238 0.3357 0.5529 0.0278  0.0441  -0.0628 413  ASP A CB  
2964  C  CG  . ASP A 413 ? 0.5265 0.3405 0.5575 0.0250  0.0379  -0.0612 413  ASP A CG  
2965  O  OD1 . ASP A 413 ? 0.5659 0.3843 0.6053 0.0210  0.0364  -0.0553 413  ASP A OD1 
2966  O  OD2 . ASP A 413 ? 0.6016 0.4130 0.6251 0.0276  0.0347  -0.0666 413  ASP A OD2 
2967  N  N   . PHE A 414 ? 0.6078 0.4165 0.6345 0.0264  0.0567  -0.0565 414  PHE A N   
2968  C  CA  . PHE A 414 ? 0.5446 0.3545 0.5683 0.0281  0.0644  -0.0574 414  PHE A CA  
2969  C  C   . PHE A 414 ? 0.6966 0.5049 0.7003 0.0270  0.0670  -0.0553 414  PHE A C   
2970  O  O   . PHE A 414 ? 0.7008 0.4984 0.6933 0.0230  0.0636  -0.0507 414  PHE A O   
2971  C  CB  . PHE A 414 ? 0.5926 0.4078 0.6255 0.0214  0.0660  -0.0490 414  PHE A CB  
2972  C  CG  . PHE A 414 ? 0.6684 0.4857 0.7193 0.0236  0.0637  -0.0506 414  PHE A CG  
2973  C  CD1 . PHE A 414 ? 0.6573 0.4768 0.7131 0.0197  0.0572  -0.0453 414  PHE A CD1 
2974  C  CD2 . PHE A 414 ? 0.7261 0.5567 0.7885 0.0281  0.0674  -0.0544 414  PHE A CD2 
2975  C  CE1 . PHE A 414 ? 0.6874 0.5129 0.7577 0.0210  0.0549  -0.0447 414  PHE A CE1 
2976  C  CE2 . PHE A 414 ? 0.6926 0.5232 0.7700 0.0312  0.0645  -0.0558 414  PHE A CE2 
2977  C  CZ  . PHE A 414 ? 0.7172 0.5455 0.7979 0.0267  0.0582  -0.0500 414  PHE A CZ  
2978  N  N   . LYS A 415 ? 0.6570 0.4758 0.6551 0.0315  0.0728  -0.0591 415  LYS A N   
2979  C  CA  . LYS A 415 ? 0.7078 0.5280 0.6870 0.0297  0.0776  -0.0546 415  LYS A CA  
2980  C  C   . LYS A 415 ? 0.7095 0.5452 0.6935 0.0242  0.0861  -0.0475 415  LYS A C   
2981  O  O   . LYS A 415 ? 0.5688 0.4199 0.5662 0.0278  0.0903  -0.0513 415  LYS A O   
2982  C  CB  . LYS A 415 ? 0.6717 0.4930 0.6377 0.0390  0.0784  -0.0633 415  LYS A CB  
2983  C  CG  . LYS A 415 ? 0.9044 0.7113 0.8642 0.0432  0.0698  -0.0700 415  LYS A CG  
2984  C  CD  . LYS A 415 ? 1.1050 0.9112 1.0458 0.0513  0.0701  -0.0766 415  LYS A CD  
2985  C  CE  . LYS A 415 ? 1.1667 0.9590 1.0991 0.0539  0.0612  -0.0815 415  LYS A CE  
2986  N  NZ  . LYS A 415 ? 1.2082 0.9989 1.1191 0.0619  0.0608  -0.0870 415  LYS A NZ  
2987  N  N   . LEU A 416 ? 0.7161 0.5475 0.6899 0.0155  0.0881  -0.0373 416  LEU A N   
2988  C  CA  . LEU A 416 ? 0.6410 0.4866 0.6197 0.0078  0.0960  -0.0293 416  LEU A CA  
2989  C  C   . LEU A 416 ? 0.6718 0.5180 0.6293 0.0058  0.1027  -0.0240 416  LEU A C   
2990  O  O   . LEU A 416 ? 0.6854 0.5143 0.6234 0.0054  0.0988  -0.0214 416  LEU A O   
2991  C  CB  . LEU A 416 ? 0.6825 0.5210 0.6685 -0.0029 0.0923  -0.0207 416  LEU A CB  
2992  C  CG  . LEU A 416 ? 0.5254 0.3595 0.5285 -0.0017 0.0848  -0.0237 416  LEU A CG  
2993  C  CD1 . LEU A 416 ? 0.3760 0.2048 0.3843 -0.0118 0.0814  -0.0151 416  LEU A CD1 
2994  C  CD2 . LEU A 416 ? 0.5517 0.4029 0.5736 0.0043  0.0877  -0.0304 416  LEU A CD2 
2995  N  N   . ALA A 417 ? 0.7004 0.5672 0.6615 0.0049  0.1127  -0.0221 417  ALA A N   
2996  C  CA  . ALA A 417 ? 0.5405 0.4102 0.4815 0.0023  0.1208  -0.0153 417  ALA A CA  
2997  C  C   . ALA A 417 ? 0.5634 0.4322 0.5055 -0.0129 0.1242  -0.0018 417  ALA A C   
2998  O  O   . ALA A 417 ? 0.7347 0.6125 0.6978 -0.0196 0.1238  0.0004  417  ALA A O   
2999  C  CB  . ALA A 417 ? 0.3952 0.2891 0.3382 0.0099  0.1305  -0.0205 417  ALA A CB  
3000  N  N   . PRO A 418 ? 0.4971 0.3534 0.4163 -0.0183 0.1266  0.0072  418  PRO A N   
3001  C  CA  . PRO A 418 ? 0.5470 0.4019 0.4688 -0.0339 0.1296  0.0201  418  PRO A CA  
3002  C  C   . PRO A 418 ? 0.8184 0.7041 0.7558 -0.0384 0.1419  0.0229  418  PRO A C   
3003  O  O   . PRO A 418 ? 0.9445 0.8472 0.8780 -0.0294 0.1495  0.0177  418  PRO A O   
3004  C  CB  . PRO A 418 ? 0.6797 0.5146 0.5706 -0.0369 0.1305  0.0288  418  PRO A CB  
3005  C  CG  . PRO A 418 ? 0.6141 0.4360 0.4879 -0.0223 0.1243  0.0190  418  PRO A CG  
3006  C  CD  . PRO A 418 ? 0.5551 0.3976 0.4456 -0.0112 0.1262  0.0064  418  PRO A CD  
3007  N  N   . VAL A 419 ? 0.9684 0.8623 0.9235 -0.0515 0.1434  0.0301  419  VAL A N   
3008  C  CA  . VAL A 419 ? 0.9872 0.9129 0.9592 -0.0574 0.1552  0.0333  419  VAL A CA  
3009  C  C   . VAL A 419 ? 0.8614 0.7998 0.8156 -0.0559 0.1682  0.0379  419  VAL A C   
3010  O  O   . VAL A 419 ? 0.6316 0.6009 0.5977 -0.0535 0.1786  0.0357  419  VAL A O   
3011  C  CB  . VAL A 419 ? 0.8558 0.7827 0.8419 -0.0754 0.1551  0.0440  419  VAL A CB  
3012  C  CG1 . VAL A 419 ? 0.7622 0.6842 0.7693 -0.0752 0.1437  0.0383  419  VAL A CG1 
3013  C  CG2 . VAL A 419 ? 0.6790 0.5783 0.6414 -0.0865 0.1531  0.0563  419  VAL A CG2 
3014  N  N   . ILE B 28  ? 0.2258 0.5287 0.8374 -0.1339 0.2056  0.2168  28   ILE B N   
3015  C  CA  . ILE B 28  ? 0.5555 0.8483 1.1560 -0.1313 0.1843  0.1967  28   ILE B CA  
3016  C  C   . ILE B 28  ? 0.4484 0.7623 1.0388 -0.1121 0.1849  0.1908  28   ILE B C   
3017  O  O   . ILE B 28  ? 0.4782 0.8045 1.0775 -0.1115 0.1697  0.1792  28   ILE B O   
3018  C  CB  . ILE B 28  ? 0.3975 0.6991 1.0341 -0.1518 0.1668  0.1896  28   ILE B CB  
3019  C  CG1 . ILE B 28  ? 0.4499 0.7327 1.1025 -0.1716 0.1690  0.1980  28   ILE B CG1 
3020  C  CG2 . ILE B 28  ? 0.4193 0.7028 1.0364 -0.1498 0.1453  0.1687  28   ILE B CG2 
3021  C  CD1 . ILE B 28  ? 0.3558 0.6621 1.0388 -0.1797 0.1883  0.2200  28   ILE B CD1 
3022  N  N   . LYS B 29  ? 0.4187 0.7346 0.9885 -0.0963 0.2027  0.1990  29   LYS B N   
3023  C  CA  . LYS B 29  ? 0.4767 0.8104 1.0366 -0.0767 0.2072  0.1954  29   LYS B CA  
3024  C  C   . LYS B 29  ? 0.4105 0.7269 0.9437 -0.0671 0.1902  0.1780  29   LYS B C   
3025  O  O   . LYS B 29  ? 0.5502 0.8815 1.0803 -0.0529 0.1897  0.1737  29   LYS B O   
3026  C  CB  . LYS B 29  ? 0.5754 0.9050 1.1100 -0.0622 0.2289  0.2052  29   LYS B CB  
3027  C  CG  . LYS B 29  ? 0.5157 0.8641 1.0426 -0.0417 0.2371  0.2027  29   LYS B CG  
3028  C  CD  . LYS B 29  ? 0.4373 0.7909 0.9502 -0.0309 0.2614  0.2147  29   LYS B CD  
3029  C  CE  . LYS B 29  ? 0.4972 0.8632 0.9975 -0.0088 0.2690  0.2094  29   LYS B CE  
3030  N  NZ  . LYS B 29  ? 0.4569 0.8349 0.9487 0.0020  0.2939  0.2204  29   LYS B NZ  
3031  N  N   . GLU B 30  ? 0.4825 0.7679 0.9976 -0.0747 0.1767  0.1686  30   GLU B N   
3032  C  CA  . GLU B 30  ? 0.5728 0.8428 1.0641 -0.0675 0.1605  0.1525  30   GLU B CA  
3033  C  C   . GLU B 30  ? 0.4471 0.7331 0.9637 -0.0778 0.1418  0.1434  30   GLU B C   
3034  O  O   . GLU B 30  ? 0.5262 0.8160 1.0684 -0.0955 0.1352  0.1439  30   GLU B O   
3035  C  CB  . GLU B 30  ? 0.6195 0.8497 1.0768 -0.0683 0.1554  0.1459  30   GLU B CB  
3036  C  CG  . GLU B 30  ? 0.6145 0.8263 1.0349 -0.0530 0.1672  0.1488  30   GLU B CG  
3037  C  CD  . GLU B 30  ? 0.6333 0.8085 1.0231 -0.0537 0.1602  0.1419  30   GLU B CD  
3038  O  OE1 . GLU B 30  ? 0.4674 0.6279 0.8654 -0.0670 0.1570  0.1438  30   GLU B OE1 
3039  O  OE2 . GLU B 30  ? 0.5503 0.7114 0.9090 -0.0409 0.1580  0.1347  30   GLU B OE2 
3040  N  N   . ASP B 31  ? 0.2324 0.5269 0.7406 -0.0668 0.1328  0.1350  31   ASP B N   
3041  C  CA  . ASP B 31  ? 0.2999 0.6122 0.8284 -0.0742 0.1147  0.1268  31   ASP B CA  
3042  C  C   . ASP B 31  ? 0.4800 0.7643 0.9807 -0.0761 0.0988  0.1118  31   ASP B C   
3043  O  O   . ASP B 31  ? 0.3789 0.6566 0.8556 -0.0637 0.0934  0.1049  31   ASP B O   
3044  C  CB  . ASP B 31  ? 0.4332 0.7742 0.9713 -0.0602 0.1147  0.1286  31   ASP B CB  
3045  C  CG  . ASP B 31  ? 0.4867 0.8513 1.0484 -0.0677 0.0960  0.1225  31   ASP B CG  
3046  O  OD1 . ASP B 31  ? 0.3552 0.7467 0.9307 -0.0574 0.0946  0.1255  31   ASP B OD1 
3047  O  OD2 . ASP B 31  ? 0.3889 0.7446 0.9550 -0.0835 0.0824  0.1144  31   ASP B OD2 
3048  N  N   . GLU B 32  ? 0.4770 0.7442 0.9814 -0.0917 0.0922  0.1072  32   GLU B N   
3049  C  CA  . GLU B 32  ? 0.1590 0.4015 0.6409 -0.0950 0.0774  0.0922  32   GLU B CA  
3050  C  C   . GLU B 32  ? 0.3384 0.5950 0.8473 -0.1119 0.0613  0.0844  32   GLU B C   
3051  O  O   . GLU B 32  ? 0.4505 0.6900 0.9648 -0.1261 0.0563  0.0792  32   GLU B O   
3052  C  CB  . GLU B 32  ? 0.2194 0.4260 0.6799 -0.0973 0.0833  0.0919  32   GLU B CB  
3053  C  CG  . GLU B 32  ? 0.5423 0.7422 0.9892 -0.0863 0.1025  0.1049  32   GLU B CG  
3054  C  CD  . GLU B 32  ? 0.5066 0.6717 0.9303 -0.0870 0.1073  0.1056  32   GLU B CD  
3055  O  OE1 . GLU B 32  ? 0.3534 0.4974 0.7464 -0.0785 0.1022  0.0967  32   GLU B OE1 
3056  O  OE2 . GLU B 32  ? 0.4748 0.6345 0.9118 -0.0959 0.1163  0.1159  32   GLU B OE2 
3057  N  N   . SER B 33  ? 0.2800 0.5681 0.8065 -0.1102 0.0531  0.0838  33   SER B N   
3058  C  CA  . SER B 33  ? 0.4302 0.7358 0.9813 -0.1255 0.0359  0.0758  33   SER B CA  
3059  C  C   . SER B 33  ? 0.5825 0.8769 1.1081 -0.1235 0.0187  0.0595  33   SER B C   
3060  O  O   . SER B 33  ? 0.6294 0.9378 1.1687 -0.1345 0.0023  0.0505  33   SER B O   
3061  C  CB  . SER B 33  ? 0.6363 0.9853 1.2220 -0.1249 0.0348  0.0846  33   SER B CB  
3062  O  OG  . SER B 33  ? 0.9216 1.2825 1.4926 -0.1083 0.0311  0.0837  33   SER B OG  
3063  N  N   . PHE B 34  ? 0.5352 0.8057 1.0235 -0.1097 0.0224  0.0559  34   PHE B N   
3064  C  CA  . PHE B 34  ? 0.5068 0.7657 0.9683 -0.1069 0.0084  0.0414  34   PHE B CA  
3065  C  C   . PHE B 34  ? 0.5272 0.7571 0.9781 -0.1183 0.0029  0.0291  34   PHE B C   
3066  O  O   . PHE B 34  ? 0.5032 0.7255 0.9378 -0.1205 -0.0102 0.0149  34   PHE B O   
3067  C  CB  . PHE B 34  ? 0.2829 0.5290 0.7110 -0.0883 0.0146  0.0429  34   PHE B CB  
3068  C  CG  . PHE B 34  ? 0.2258 0.4534 0.6428 -0.0802 0.0327  0.0523  34   PHE B CG  
3069  C  CD1 . PHE B 34  ? 0.2660 0.4627 0.6677 -0.0840 0.0372  0.0489  34   PHE B CD1 
3070  C  CD2 . PHE B 34  ? 0.2601 0.5012 0.6814 -0.0681 0.0449  0.0644  34   PHE B CD2 
3071  C  CE1 . PHE B 34  ? 0.3972 0.5782 0.7873 -0.0765 0.0529  0.0582  34   PHE B CE1 
3072  C  CE2 . PHE B 34  ? 0.4306 0.6553 0.8390 -0.0606 0.0612  0.0723  34   PHE B CE2 
3073  C  CZ  . PHE B 34  ? 0.4589 0.6542 0.8513 -0.0652 0.0648  0.0696  34   PHE B CZ  
3074  N  N   . LEU B 35  ? 0.5932 0.8067 1.0531 -0.1248 0.0136  0.0350  35   LEU B N   
3075  C  CA  . LEU B 35  ? 0.6687 0.8532 1.1239 -0.1359 0.0099  0.0252  35   LEU B CA  
3076  C  C   . LEU B 35  ? 0.7798 0.9777 1.2660 -0.1553 -0.0027 0.0183  35   LEU B C   
3077  O  O   . LEU B 35  ? 0.7105 0.8873 1.2032 -0.1680 -0.0056 0.0116  35   LEU B O   
3078  C  CB  . LEU B 35  ? 0.6371 0.7991 1.0902 -0.1345 0.0266  0.0368  35   LEU B CB  
3079  C  CG  . LEU B 35  ? 0.4203 0.5722 0.8453 -0.1160 0.0396  0.0450  35   LEU B CG  
3080  C  CD1 . LEU B 35  ? 0.2191 0.3634 0.6497 -0.1148 0.0570  0.0610  35   LEU B CD1 
3081  C  CD2 . LEU B 35  ? 0.1602 0.2846 0.5501 -0.1079 0.0354  0.0336  35   LEU B CD2 
3082  N  N   . GLN B 36  ? 0.8660 1.0991 1.3717 -0.1573 -0.0109 0.0200  36   GLN B N   
3083  C  CA  . GLN B 36  ? 0.8397 1.0924 1.3770 -0.1756 -0.0245 0.0141  36   GLN B CA  
3084  C  C   . GLN B 36  ? 0.7178 0.9645 1.2376 -0.1802 -0.0435 -0.0064 36   GLN B C   
3085  O  O   . GLN B 36  ? 0.8056 1.0611 1.3034 -0.1687 -0.0497 -0.0107 36   GLN B O   
3086  C  CB  . GLN B 36  ? 0.9354 1.2316 1.5012 -0.1742 -0.0256 0.0255  36   GLN B CB  
3087  C  CG  . GLN B 36  ? 0.9428 1.2626 1.5512 -0.1942 -0.0341 0.0261  36   GLN B CG  
3088  C  CD  . GLN B 36  ? 1.0050 1.3204 1.6397 -0.2030 -0.0185 0.0401  36   GLN B CD  
3089  O  OE1 . GLN B 36  ? 1.2034 1.5372 1.8757 -0.2201 -0.0227 0.0432  36   GLN B OE1 
3090  N  NE2 . GLN B 36  ? 0.7878 1.0797 1.4028 -0.1918 -0.0007 0.0492  36   GLN B NE2 
3091  N  N   . GLN B 37  ? 0.5532 0.7849 1.0829 -0.1971 -0.0525 -0.0188 37   GLN B N   
3092  C  CA  . GLN B 37  ? 0.5172 0.7377 1.0269 -0.2017 -0.0690 -0.0406 37   GLN B CA  
3093  C  C   . GLN B 37  ? 0.6323 0.8353 1.0997 -0.1839 -0.0657 -0.0457 37   GLN B C   
3094  O  O   . GLN B 37  ? 0.7786 1.0009 1.2313 -0.1744 -0.0723 -0.0469 37   GLN B O   
3095  C  CB  . GLN B 37  ? 0.6244 0.8809 1.1478 -0.2086 -0.0871 -0.0467 37   GLN B CB  
3096  C  CG  . GLN B 37  ? 0.9920 1.2766 1.5607 -0.2241 -0.0904 -0.0382 37   GLN B CG  
3097  C  CD  . GLN B 37  ? 1.1610 1.4883 1.7423 -0.2239 -0.1046 -0.0372 37   GLN B CD  
3098  O  OE1 . GLN B 37  ? 1.2110 1.5435 1.7741 -0.2247 -0.1210 -0.0521 37   GLN B OE1 
3099  N  NE2 . GLN B 37  ? 1.1563 1.5157 1.7684 -0.2219 -0.0981 -0.0192 37   GLN B NE2 
3100  N  N   . PRO B 38  ? 0.4803 0.6476 0.9292 -0.1792 -0.0557 -0.0477 38   PRO B N   
3101  C  CA  . PRO B 38  ? 0.3736 0.5248 0.7844 -0.1624 -0.0514 -0.0514 38   PRO B CA  
3102  C  C   . PRO B 38  ? 0.5052 0.6553 0.8934 -0.1629 -0.0663 -0.0713 38   PRO B C   
3103  O  O   . PRO B 38  ? 0.5005 0.6446 0.8952 -0.1762 -0.0779 -0.0870 38   PRO B O   
3104  C  CB  . PRO B 38  ? 0.3740 0.4884 0.7767 -0.1605 -0.0392 -0.0496 38   PRO B CB  
3105  C  CG  . PRO B 38  ? 0.5782 0.6916 1.0151 -0.1744 -0.0343 -0.0403 38   PRO B CG  
3106  C  CD  . PRO B 38  ? 0.3909 0.5312 0.8542 -0.1895 -0.0486 -0.0463 38   PRO B CD  
3107  N  N   . HIS B 39  ? 0.5334 0.6890 0.8943 -0.1482 -0.0657 -0.0707 39   HIS B N   
3108  C  CA  . HIS B 39  ? 0.4658 0.6262 0.8032 -0.1467 -0.0785 -0.0864 39   HIS B CA  
3109  C  C   . HIS B 39  ? 0.4922 0.6537 0.8015 -0.1291 -0.0721 -0.0798 39   HIS B C   
3110  O  O   . HIS B 39  ? 0.4416 0.6091 0.7548 -0.1198 -0.0617 -0.0632 39   HIS B O   
3111  C  CB  . HIS B 39  ? 0.4926 0.6870 0.8465 -0.1559 -0.0942 -0.0891 39   HIS B CB  
3112  C  CG  . HIS B 39  ? 0.4070 0.6317 0.7678 -0.1466 -0.0926 -0.0722 39   HIS B CG  
3113  N  ND1 . HIS B 39  ? 0.5437 0.7752 0.9251 -0.1424 -0.0800 -0.0537 39   HIS B ND1 
3114  C  CD2 . HIS B 39  ? 0.4358 0.6851 0.7855 -0.1400 -0.1018 -0.0707 39   HIS B CD2 
3115  C  CE1 . HIS B 39  ? 0.5131 0.7712 0.8965 -0.1331 -0.0814 -0.0426 39   HIS B CE1 
3116  N  NE2 . HIS B 39  ? 0.4590 0.7279 0.8239 -0.1316 -0.0948 -0.0519 39   HIS B NE2 
3117  N  N   . TYR B 40  ? 0.6248 0.7806 0.9057 -0.1246 -0.0781 -0.0928 40   TYR B N   
3118  C  CA  . TYR B 40  ? 0.5997 0.7566 0.8545 -0.1091 -0.0727 -0.0865 40   TYR B CA  
3119  C  C   . TYR B 40  ? 0.5015 0.6905 0.7557 -0.1056 -0.0813 -0.0796 40   TYR B C   
3120  O  O   . TYR B 40  ? 0.5831 0.7893 0.8372 -0.1129 -0.0955 -0.0890 40   TYR B O   
3121  C  CB  . TYR B 40  ? 0.6604 0.7978 0.8854 -0.1048 -0.0731 -0.1015 40   TYR B CB  
3122  C  CG  . TYR B 40  ? 0.6336 0.7389 0.8548 -0.1016 -0.0612 -0.1028 40   TYR B CG  
3123  C  CD1 . TYR B 40  ? 0.6799 0.7638 0.9052 -0.1100 -0.0633 -0.1175 40   TYR B CD1 
3124  C  CD2 . TYR B 40  ? 0.4426 0.5388 0.6564 -0.0899 -0.0483 -0.0891 40   TYR B CD2 
3125  C  CE1 . TYR B 40  ? 0.7355 0.7901 0.9583 -0.1061 -0.0528 -0.1173 40   TYR B CE1 
3126  C  CE2 . TYR B 40  ? 0.5035 0.5722 0.7137 -0.0865 -0.0385 -0.0893 40   TYR B CE2 
3127  C  CZ  . TYR B 40  ? 0.6055 0.6538 0.8207 -0.0942 -0.0407 -0.1026 40   TYR B CZ  
3128  O  OH  . TYR B 40  ? 0.5496 0.5707 0.7622 -0.0899 -0.0312 -0.1013 40   TYR B OH  
3129  N  N   . ALA B 41  ? 0.3644 0.5606 0.6176 -0.0941 -0.0729 -0.0632 41   ALA B N   
3130  C  CA  . ALA B 41  ? 0.2996 0.5240 0.5540 -0.0887 -0.0796 -0.0539 41   ALA B CA  
3131  C  C   . ALA B 41  ? 0.2963 0.5230 0.5197 -0.0829 -0.0863 -0.0604 41   ALA B C   
3132  O  O   . ALA B 41  ? 0.3913 0.5999 0.5922 -0.0745 -0.0782 -0.0608 41   ALA B O   
3133  C  CB  . ALA B 41  ? 0.3573 0.5838 0.6188 -0.0773 -0.0674 -0.0356 41   ALA B CB  
3134  N  N   . SER B 42  ? 0.4392 0.6897 0.6615 -0.0875 -0.1011 -0.0648 42   SER B N   
3135  C  CA  . SER B 42  ? 0.4335 0.6888 0.6251 -0.0824 -0.1076 -0.0700 42   SER B CA  
3136  C  C   . SER B 42  ? 0.4972 0.7620 0.6808 -0.0692 -0.1035 -0.0527 42   SER B C   
3137  O  O   . SER B 42  ? 0.5252 0.7943 0.7276 -0.0639 -0.0968 -0.0382 42   SER B O   
3138  C  CB  . SER B 42  ? 0.4142 0.6928 0.6053 -0.0918 -0.1257 -0.0799 42   SER B CB  
3139  O  OG  . SER B 42  ? 0.4584 0.7662 0.6669 -0.0899 -0.1331 -0.0659 42   SER B OG  
3140  N  N   . GLN B 43  ? 0.3684 0.6362 0.5242 -0.0638 -0.1071 -0.0541 43   GLN B N   
3141  C  CA  . GLN B 43  ? 0.3216 0.5984 0.4698 -0.0523 -0.1050 -0.0376 43   GLN B CA  
3142  C  C   . GLN B 43  ? 0.3848 0.6887 0.5575 -0.0516 -0.1131 -0.0248 43   GLN B C   
3143  O  O   . GLN B 43  ? 0.2914 0.5968 0.4758 -0.0425 -0.1061 -0.0094 43   GLN B O   
3144  C  CB  . GLN B 43  ? 0.3345 0.6149 0.4505 -0.0490 -0.1098 -0.0409 43   GLN B CB  
3145  C  CG  . GLN B 43  ? 0.5332 0.8190 0.6398 -0.0375 -0.1071 -0.0232 43   GLN B CG  
3146  C  CD  . GLN B 43  ? 0.5797 0.8421 0.6858 -0.0292 -0.0914 -0.0154 43   GLN B CD  
3147  O  OE1 . GLN B 43  ? 0.6706 0.9118 0.7721 -0.0309 -0.0826 -0.0244 43   GLN B OE1 
3148  N  NE2 . GLN B 43  ? 0.5876 0.8531 0.6981 -0.0199 -0.0883 0.0013  43   GLN B NE2 
3149  N  N   . GLU B 44  ? 0.4142 0.7400 0.5958 -0.0611 -0.1279 -0.0317 44   GLU B N   
3150  C  CA  . GLU B 44  ? 0.4363 0.7907 0.6441 -0.0606 -0.1364 -0.0195 44   GLU B CA  
3151  C  C   . GLU B 44  ? 0.4984 0.8505 0.7394 -0.0608 -0.1267 -0.0123 44   GLU B C   
3152  O  O   . GLU B 44  ? 0.5648 0.9274 0.8217 -0.0516 -0.1225 0.0036  44   GLU B O   
3153  C  CB  . GLU B 44  ? 0.4791 0.8588 0.6923 -0.0721 -0.1553 -0.0291 44   GLU B CB  
3154  C  CG  . GLU B 44  ? 0.7226 1.1357 0.9608 -0.0696 -0.1655 -0.0144 44   GLU B CG  
3155  C  CD  . GLU B 44  ? 0.9744 1.4127 1.2310 -0.0838 -0.1828 -0.0238 44   GLU B CD  
3156  O  OE1 . GLU B 44  ? 1.0935 1.5226 1.3389 -0.0957 -0.1884 -0.0430 44   GLU B OE1 
3157  O  OE2 . GLU B 44  ? 0.9866 1.4540 1.2697 -0.0829 -0.1912 -0.0123 44   GLU B OE2 
3158  N  N   . GLN B 45  ? 0.5384 0.8764 0.7896 -0.0711 -0.1227 -0.0237 45   GLN B N   
3159  C  CA  . GLN B 45  ? 0.4627 0.7993 0.7453 -0.0731 -0.1131 -0.0171 45   GLN B CA  
3160  C  C   . GLN B 45  ? 0.4178 0.7389 0.6982 -0.0596 -0.0961 -0.0040 45   GLN B C   
3161  O  O   . GLN B 45  ? 0.3259 0.6553 0.6315 -0.0563 -0.0888 0.0071  45   GLN B O   
3162  C  CB  . GLN B 45  ? 0.3424 0.6608 0.6320 -0.0861 -0.1105 -0.0310 45   GLN B CB  
3163  C  CG  . GLN B 45  ? 0.4167 0.7507 0.7160 -0.1015 -0.1272 -0.0444 45   GLN B CG  
3164  C  CD  . GLN B 45  ? 0.5149 0.8355 0.8350 -0.1150 -0.1241 -0.0531 45   GLN B CD  
3165  O  OE1 . GLN B 45  ? 0.4857 0.7759 0.7936 -0.1157 -0.1146 -0.0605 45   GLN B OE1 
3166  N  NE2 . GLN B 45  ? 0.5253 0.8690 0.8784 -0.1260 -0.1324 -0.0513 45   GLN B NE2 
3167  N  N   . LEU B 46  ? 0.3744 0.6741 0.6246 -0.0520 -0.0900 -0.0057 46   LEU B N   
3168  C  CA  . LEU B 46  ? 0.4062 0.6875 0.6498 -0.0400 -0.0747 0.0043  46   LEU B CA  
3169  C  C   . LEU B 46  ? 0.4522 0.7480 0.6993 -0.0278 -0.0749 0.0196  46   LEU B C   
3170  O  O   . LEU B 46  ? 0.3879 0.6807 0.6477 -0.0196 -0.0642 0.0299  46   LEU B O   
3171  C  CB  . LEU B 46  ? 0.3604 0.6156 0.5725 -0.0370 -0.0692 -0.0031 46   LEU B CB  
3172  C  CG  . LEU B 46  ? 0.4112 0.6485 0.6125 -0.0249 -0.0560 0.0065  46   LEU B CG  
3173  C  CD1 . LEU B 46  ? 0.5479 0.7782 0.7691 -0.0228 -0.0438 0.0130  46   LEU B CD1 
3174  C  CD2 . LEU B 46  ? 0.2879 0.5017 0.4616 -0.0239 -0.0514 -0.0016 46   LEU B CD2 
3175  N  N   . GLU B 47  ? 0.4209 0.7316 0.6558 -0.0260 -0.0869 0.0210  47   GLU B N   
3176  C  CA  . GLU B 47  ? 0.3904 0.7146 0.6291 -0.0143 -0.0887 0.0363  47   GLU B CA  
3177  C  C   . GLU B 47  ? 0.4217 0.7710 0.6959 -0.0143 -0.0914 0.0444  47   GLU B C   
3178  O  O   . GLU B 47  ? 0.4766 0.8282 0.7644 -0.0033 -0.0836 0.0567  47   GLU B O   
3179  C  CB  . GLU B 47  ? 0.4611 0.7983 0.6800 -0.0139 -0.1023 0.0369  47   GLU B CB  
3180  C  CG  . GLU B 47  ? 0.3679 0.6833 0.5520 -0.0129 -0.0987 0.0308  47   GLU B CG  
3181  C  CD  . GLU B 47  ? 0.5119 0.8427 0.6755 -0.0145 -0.1121 0.0301  47   GLU B CD  
3182  O  OE1 . GLU B 47  ? 0.5137 0.8690 0.6866 -0.0211 -0.1259 0.0271  47   GLU B OE1 
3183  O  OE2 . GLU B 47  ? 0.6334 0.9528 0.7714 -0.0097 -0.1091 0.0327  47   GLU B OE2 
3184  N  N   . ASP B 48  ? 0.4717 0.8396 0.7617 -0.0268 -0.1021 0.0367  48   ASP B N   
3185  C  CA  . ASP B 48  ? 0.5189 0.9141 0.8462 -0.0291 -0.1056 0.0435  48   ASP B CA  
3186  C  C   . ASP B 48  ? 0.4162 0.8017 0.7638 -0.0252 -0.0883 0.0491  48   ASP B C   
3187  O  O   . ASP B 48  ? 0.3431 0.7449 0.7141 -0.0164 -0.0840 0.0616  48   ASP B O   
3188  C  CB  . ASP B 48  ? 0.5855 0.9980 0.9254 -0.0460 -0.1196 0.0317  48   ASP B CB  
3189  C  CG  . ASP B 48  ? 0.7062 1.1377 1.0311 -0.0489 -0.1387 0.0283  48   ASP B CG  
3190  O  OD1 . ASP B 48  ? 0.7186 1.1595 1.0347 -0.0374 -0.1423 0.0399  48   ASP B OD1 
3191  O  OD2 . ASP B 48  ? 0.8300 1.2667 1.1514 -0.0628 -0.1503 0.0140  48   ASP B OD2 
3192  N  N   . LEU B 49  ? 0.2851 0.6446 0.6236 -0.0310 -0.0780 0.0404  49   LEU B N   
3193  C  CA  . LEU B 49  ? 0.3377 0.6892 0.6941 -0.0286 -0.0618 0.0458  49   LEU B CA  
3194  C  C   . LEU B 49  ? 0.2722 0.6111 0.6193 -0.0118 -0.0487 0.0563  49   LEU B C   
3195  O  O   . LEU B 49  ? 0.2757 0.6204 0.6427 -0.0056 -0.0377 0.0648  49   LEU B O   
3196  C  CB  . LEU B 49  ? 0.4580 0.7848 0.8070 -0.0389 -0.0548 0.0351  49   LEU B CB  
3197  C  CG  . LEU B 49  ? 0.3316 0.6543 0.7019 -0.0396 -0.0397 0.0410  49   LEU B CG  
3198  C  CD1 . LEU B 49  ? 0.5704 0.8831 0.9484 -0.0555 -0.0400 0.0314  49   LEU B CD1 
3199  C  CD2 . LEU B 49  ? 0.2828 0.5813 0.6344 -0.0269 -0.0239 0.0461  49   LEU B CD2 
3200  N  N   . PHE B 50  ? 0.3018 0.6236 0.6188 -0.0047 -0.0497 0.0553  50   PHE B N   
3201  C  CA  . PHE B 50  ? 0.2439 0.5518 0.5504 0.0105  -0.0391 0.0641  50   PHE B CA  
3202  C  C   . PHE B 50  ? 0.3162 0.6472 0.6419 0.0214  -0.0424 0.0768  50   PHE B C   
3203  O  O   . PHE B 50  ? 0.5381 0.8642 0.8706 0.0333  -0.0309 0.0847  50   PHE B O   
3204  C  CB  . PHE B 50  ? 0.3658 0.6511 0.6372 0.0135  -0.0406 0.0601  50   PHE B CB  
3205  C  CG  . PHE B 50  ? 0.3744 0.6303 0.6272 0.0104  -0.0304 0.0519  50   PHE B CG  
3206  C  CD1 . PHE B 50  ? 0.3558 0.6063 0.6214 0.0041  -0.0221 0.0482  50   PHE B CD1 
3207  C  CD2 . PHE B 50  ? 0.2663 0.5012 0.4901 0.0137  -0.0290 0.0490  50   PHE B CD2 
3208  C  CE1 . PHE B 50  ? 0.2621 0.4863 0.5111 0.0021  -0.0133 0.0421  50   PHE B CE1 
3209  C  CE2 . PHE B 50  ? 0.3353 0.5452 0.5437 0.0115  -0.0203 0.0421  50   PHE B CE2 
3210  C  CZ  . PHE B 50  ? 0.3425 0.5468 0.5631 0.0061  -0.0127 0.0387  50   PHE B CZ  
3211  N  N   . ALA B 51  ? 0.1864 0.5428 0.5206 0.0179  -0.0581 0.0786  51   ALA B N   
3212  C  CA  . ALA B 51  ? 0.3302 0.7117 0.6858 0.0283  -0.0629 0.0916  51   ALA B CA  
3213  C  C   . ALA B 51  ? 0.4772 0.8781 0.8695 0.0290  -0.0554 0.0966  51   ALA B C   
3214  O  O   . ALA B 51  ? 0.5996 1.0074 1.0076 0.0426  -0.0477 0.1071  51   ALA B O   
3215  C  CB  . ALA B 51  ? 0.2107 0.6173 0.5669 0.0232  -0.0828 0.0925  51   ALA B CB  
3216  N  N   . GLY B 52  ? 0.4971 0.9067 0.9036 0.0141  -0.0574 0.0889  52   GLY B N   
3217  C  CA  . GLY B 52  ? 0.3871 0.8175 0.8303 0.0116  -0.0505 0.0935  52   GLY B CA  
3218  C  C   . GLY B 52  ? 0.2821 0.6954 0.7262 0.0223  -0.0295 0.0983  52   GLY B C   
3219  O  O   . GLY B 52  ? 0.2024 0.6338 0.6724 0.0317  -0.0217 0.1079  52   GLY B O   
3220  N  N   . LEU B 53  ? 0.2834 0.6626 0.6984 0.0215  -0.0204 0.0913  53   LEU B N   
3221  C  CA  . LEU B 53  ? 0.3901 0.7505 0.8003 0.0309  -0.0013 0.0943  53   LEU B CA  
3222  C  C   . LEU B 53  ? 0.4326 0.7924 0.8408 0.0497  0.0036  0.1031  53   LEU B C   
3223  O  O   . LEU B 53  ? 0.5109 0.8752 0.9340 0.0598  0.0171  0.1092  53   LEU B O   
3224  C  CB  . LEU B 53  ? 0.3686 0.6931 0.7456 0.0269  0.0046  0.0853  53   LEU B CB  
3225  C  CG  . LEU B 53  ? 0.4187 0.7382 0.7969 0.0096  0.0022  0.0764  53   LEU B CG  
3226  C  CD1 . LEU B 53  ? 0.5505 0.8356 0.9005 0.0090  0.0117  0.0703  53   LEU B CD1 
3227  C  CD2 . LEU B 53  ? 0.2297 0.5712 0.6429 0.0022  0.0073  0.0808  53   LEU B CD2 
3228  N  N   . GLU B 54  ? 0.3471 0.7010 0.7371 0.0545  -0.0072 0.1037  54   GLU B N   
3229  C  CA  . GLU B 54  ? 0.4876 0.8379 0.8753 0.0720  -0.0041 0.1123  54   GLU B CA  
3230  C  C   . GLU B 54  ? 0.5772 0.9600 1.0020 0.0811  -0.0034 0.1229  54   GLU B C   
3231  O  O   . GLU B 54  ? 0.5086 0.8877 0.9409 0.0959  0.0091  0.1285  54   GLU B O   
3232  C  CB  . GLU B 54  ? 0.6159 0.9586 0.9810 0.0734  -0.0177 0.1131  54   GLU B CB  
3233  C  CG  . GLU B 54  ? 0.7431 1.0655 1.0937 0.0895  -0.0120 0.1192  54   GLU B CG  
3234  C  CD  . GLU B 54  ? 0.7821 1.0918 1.1060 0.0885  -0.0232 0.1197  54   GLU B CD  
3235  O  OE1 . GLU B 54  ? 0.7643 1.0534 1.0740 0.0994  -0.0191 0.1241  54   GLU B OE1 
3236  O  OE2 . GLU B 54  ? 0.7667 1.0869 1.0837 0.0766  -0.0359 0.1155  54   GLU B OE2 
3237  N  N   . LYS B 55  ? 0.5557 0.9708 1.0043 0.0727  -0.0167 0.1252  55   LYS B N   
3238  C  CA  . LYS B 55  ? 0.4476 0.8971 0.9348 0.0810  -0.0166 0.1357  55   LYS B CA  
3239  C  C   . LYS B 55  ? 0.3091 0.7696 0.8215 0.0779  -0.0013 0.1357  55   LYS B C   
3240  O  O   . LYS B 55  ? 0.2520 0.7253 0.7863 0.0912  0.0098  0.1435  55   LYS B O   
3241  C  CB  . LYS B 55  ? 0.3178 0.8007 0.8229 0.0736  -0.0374 0.1391  55   LYS B CB  
3242  C  CG  . LYS B 55  ? 0.2993 0.7859 0.7991 0.0520  -0.0484 0.1283  55   LYS B CG  
3243  C  CD  . LYS B 55  ? 0.3980 0.9195 0.9152 0.0449  -0.0699 0.1310  55   LYS B CD  
3244  C  CE  . LYS B 55  ? 0.4497 1.0120 1.0144 0.0477  -0.0703 0.1408  55   LYS B CE  
3245  N  NZ  . LYS B 55  ? 0.4196 1.0178 1.0015 0.0423  -0.0928 0.1446  55   LYS B NZ  
3246  N  N   . ALA B 56  ? 0.1716 0.6258 0.6801 0.0611  0.0001  0.1274  56   ALA B N   
3247  C  CA  . ALA B 56  ? 0.1590 0.6220 0.6895 0.0567  0.0150  0.1285  56   ALA B CA  
3248  C  C   . ALA B 56  ? 0.2341 0.6755 0.7522 0.0716  0.0359  0.1305  56   ALA B C   
3249  O  O   . ALA B 56  ? 0.2974 0.7538 0.8388 0.0766  0.0503  0.1361  56   ALA B O   
3250  C  CB  . ALA B 56  ? 0.1933 0.6451 0.7160 0.0364  0.0130  0.1191  56   ALA B CB  
3251  N  N   . TYR B 57  ? 0.1786 0.5855 0.6599 0.0781  0.0376  0.1256  57   TYR B N   
3252  C  CA  . TYR B 57  ? 0.2360 0.6181 0.6999 0.0902  0.0559  0.1249  57   TYR B CA  
3253  C  C   . TYR B 57  ? 0.2415 0.6042 0.6847 0.1059  0.0541  0.1260  57   TYR B C   
3254  O  O   . TYR B 57  ? 0.3960 0.7258 0.8055 0.1064  0.0556  0.1197  57   TYR B O   
3255  C  CB  . TYR B 57  ? 0.3018 0.6549 0.7384 0.0792  0.0620  0.1162  57   TYR B CB  
3256  C  CG  . TYR B 57  ? 0.4443 0.8119 0.9000 0.0631  0.0640  0.1155  57   TYR B CG  
3257  C  CD1 . TYR B 57  ? 0.4331 0.8086 0.8938 0.0464  0.0485  0.1110  57   TYR B CD1 
3258  C  CD2 . TYR B 57  ? 0.4177 0.7906 0.8863 0.0643  0.0816  0.1195  57   TYR B CD2 
3259  C  CE1 . TYR B 57  ? 0.4436 0.8301 0.9232 0.0308  0.0498  0.1102  57   TYR B CE1 
3260  C  CE2 . TYR B 57  ? 0.2565 0.6422 0.7444 0.0486  0.0835  0.1204  57   TYR B CE2 
3261  C  CZ  . TYR B 57  ? 0.3777 0.7689 0.8715 0.0317  0.0673  0.1156  57   TYR B CZ  
3262  O  OH  . TYR B 57  ? 0.3540 0.7549 0.8675 0.0153  0.0688  0.1161  57   TYR B OH  
3263  N  N   . PRO B 58  ? 0.1311 0.5143 0.5962 0.1189  0.0511  0.1345  58   PRO B N   
3264  C  CA  . PRO B 58  ? 0.2265 0.5963 0.6793 0.1338  0.0464  0.1382  58   PRO B CA  
3265  C  C   . PRO B 58  ? 0.4845 0.8147 0.9053 0.1436  0.0581  0.1329  58   PRO B C   
3266  O  O   . PRO B 58  ? 0.6857 0.9954 1.0851 0.1474  0.0503  0.1327  58   PRO B O   
3267  C  CB  . PRO B 58  ? 0.2379 0.6383 0.7276 0.1485  0.0494  0.1487  58   PRO B CB  
3268  C  CG  . PRO B 58  ? 0.1992 0.6370 0.7217 0.1359  0.0454  0.1513  58   PRO B CG  
3269  C  CD  . PRO B 58  ? 0.2050 0.6281 0.7127 0.1203  0.0533  0.1424  58   PRO B CD  
3270  N  N   . ASN B 59  ? 0.6081 0.9283 1.0254 0.1473  0.0758  0.1291  59   ASN B N   
3271  C  CA  . ASN B 59  ? 0.6012 0.8863 0.9904 0.1584  0.0870  0.1239  59   ASN B CA  
3272  C  C   . ASN B 59  ? 0.4900 0.7457 0.8456 0.1471  0.0904  0.1142  59   ASN B C   
3273  O  O   . ASN B 59  ? 0.3008 0.5268 0.6308 0.1540  0.0980  0.1088  59   ASN B O   
3274  C  CB  . ASN B 59  ? 0.7254 1.0169 1.1293 0.1739  0.1057  0.1256  59   ASN B CB  
3275  C  CG  . ASN B 59  ? 0.8051 1.1302 1.2476 0.1858  0.1045  0.1357  59   ASN B CG  
3276  O  OD1 . ASN B 59  ? 0.7591 1.1111 1.2235 0.1790  0.0904  0.1420  59   ASN B OD1 
3277  N  ND2 . ASN B 59  ? 0.8117 1.1359 1.2627 0.2042  0.1194  0.1367  59   ASN B ND2 
3278  N  N   . GLN B 60  ? 0.3833 0.6474 0.7399 0.1300  0.0845  0.1118  60   GLN B N   
3279  C  CA  . GLN B 60  ? 0.3340 0.5735 0.6632 0.1200  0.0884  0.1037  60   GLN B CA  
3280  C  C   . GLN B 60  ? 0.3778 0.6105 0.6927 0.1050  0.0732  0.0993  60   GLN B C   
3281  O  O   . GLN B 60  ? 0.3413 0.5491 0.6294 0.0992  0.0740  0.0926  60   GLN B O   
3282  C  CB  . GLN B 60  ? 0.3152 0.5659 0.6566 0.1147  0.1014  0.1042  60   GLN B CB  
3283  C  CG  . GLN B 60  ? 0.5464 0.8303 0.9245 0.1217  0.1080  0.1123  60   GLN B CG  
3284  C  CD  . GLN B 60  ? 0.5705 0.8550 0.9510 0.1289  0.1284  0.1133  60   GLN B CD  
3285  O  OE1 . GLN B 60  ? 0.5388 0.8521 0.9495 0.1290  0.1360  0.1197  60   GLN B OE1 
3286  N  NE2 . GLN B 60  ? 0.5153 0.7695 0.8641 0.1346  0.1373  0.1073  60   GLN B NE2 
3287  N  N   . ALA B 61  ? 0.2397 0.4956 0.5726 0.0995  0.0595  0.1029  61   ALA B N   
3288  C  CA  . ALA B 61  ? 0.2221 0.4742 0.5415 0.0868  0.0445  0.0984  61   ALA B CA  
3289  C  C   . ALA B 61  ? 0.2224 0.4744 0.5348 0.0926  0.0322  0.1021  61   ALA B C   
3290  O  O   . ALA B 61  ? 0.2924 0.5662 0.6260 0.0997  0.0271  0.1101  61   ALA B O   
3291  C  CB  . ALA B 61  ? 0.3137 0.5909 0.6549 0.0726  0.0371  0.0976  61   ALA B CB  
3292  N  N   . LYS B 62  ? 0.2576 0.4862 0.5411 0.0895  0.0274  0.0974  62   LYS B N   
3293  C  CA  . LYS B 62  ? 0.1985 0.4253 0.4728 0.0938  0.0163  0.1020  62   LYS B CA  
3294  C  C   . LYS B 62  ? 0.1677 0.3852 0.4190 0.0819  0.0066  0.0957  62   LYS B C   
3295  O  O   . LYS B 62  ? 0.3534 0.5502 0.5853 0.0764  0.0117  0.0880  62   LYS B O   
3296  C  CB  . LYS B 62  ? 0.1629 0.3670 0.4255 0.1080  0.0235  0.1055  62   LYS B CB  
3297  C  CG  . LYS B 62  ? 0.3225 0.5203 0.5738 0.1119  0.0130  0.1114  62   LYS B CG  
3298  C  CD  . LYS B 62  ? 0.6115 0.7860 0.8553 0.1258  0.0205  0.1147  62   LYS B CD  
3299  C  CE  . LYS B 62  ? 0.7808 0.9457 1.0120 0.1281  0.0105  0.1215  62   LYS B CE  
3300  N  NZ  . LYS B 62  ? 0.8860 1.0793 1.1359 0.1301  -0.0014 0.1317  62   LYS B NZ  
3301  N  N   . VAL B 63  ? 0.3214 0.5557 0.5749 0.0783  -0.0073 0.0992  63   VAL B N   
3302  C  CA  . VAL B 63  ? 0.2427 0.4714 0.4745 0.0678  -0.0163 0.0931  63   VAL B CA  
3303  C  C   . VAL B 63  ? 0.4158 0.6257 0.6250 0.0735  -0.0180 0.0973  63   VAL B C   
3304  O  O   . VAL B 63  ? 0.3447 0.5552 0.5591 0.0843  -0.0192 0.1073  63   VAL B O   
3305  C  CB  . VAL B 63  ? 0.2571 0.5142 0.4994 0.0596  -0.0310 0.0933  63   VAL B CB  
3306  C  CG1 . VAL B 63  ? 0.2023 0.4534 0.4191 0.0512  -0.0397 0.0875  63   VAL B CG1 
3307  C  CG2 . VAL B 63  ? 0.3847 0.6575 0.6480 0.0505  -0.0300 0.0874  63   VAL B CG2 
3308  N  N   . HIS B 64  ? 0.4962 0.6893 0.6816 0.0662  -0.0180 0.0898  64   HIS B N   
3309  C  CA  . HIS B 64  ? 0.3059 0.4807 0.4694 0.0691  -0.0188 0.0930  64   HIS B CA  
3310  C  C   . HIS B 64  ? 0.3211 0.5015 0.4676 0.0593  -0.0279 0.0889  64   HIS B C   
3311  O  O   . HIS B 64  ? 0.4061 0.5878 0.5480 0.0499  -0.0280 0.0783  64   HIS B O   
3312  C  CB  . HIS B 64  ? 0.1182 0.2648 0.2691 0.0715  -0.0071 0.0881  64   HIS B CB  
3313  C  CG  . HIS B 64  ? 0.3148 0.4553 0.4793 0.0818  0.0026  0.0911  64   HIS B CG  
3314  N  ND1 . HIS B 64  ? 0.4951 0.6248 0.6603 0.0932  0.0048  0.0988  64   HIS B ND1 
3315  C  CD2 . HIS B 64  ? 0.4099 0.5544 0.5881 0.0829  0.0111  0.0875  64   HIS B CD2 
3316  C  CE1 . HIS B 64  ? 0.4949 0.6220 0.6728 0.1016  0.0145  0.0986  64   HIS B CE1 
3317  N  NE2 . HIS B 64  ? 0.4185 0.5557 0.6043 0.0954  0.0188  0.0923  64   HIS B NE2 
3318  N  N   . PHE B 65  ? 0.3311 0.5152 0.4685 0.0618  -0.0353 0.0976  65   PHE B N   
3319  C  CA  . PHE B 65  ? 0.3896 0.5808 0.5088 0.0538  -0.0435 0.0950  65   PHE B CA  
3320  C  C   . PHE B 65  ? 0.4054 0.5735 0.5025 0.0524  -0.0377 0.0934  65   PHE B C   
3321  O  O   . PHE B 65  ? 0.3916 0.5458 0.4845 0.0590  -0.0352 0.1026  65   PHE B O   
3322  C  CB  . PHE B 65  ? 0.3344 0.5450 0.4553 0.0570  -0.0550 0.1071  65   PHE B CB  
3323  C  CG  . PHE B 65  ? 0.4223 0.6379 0.5202 0.0506  -0.0618 0.1072  65   PHE B CG  
3324  C  CD1 . PHE B 65  ? 0.4868 0.6877 0.5680 0.0532  -0.0596 0.1153  65   PHE B CD1 
3325  C  CD2 . PHE B 65  ? 0.4865 0.7217 0.5792 0.0418  -0.0703 0.0987  65   PHE B CD2 
3326  C  CE1 . PHE B 65  ? 0.5933 0.8007 0.6533 0.0474  -0.0646 0.1162  65   PHE B CE1 
3327  C  CE2 . PHE B 65  ? 0.5225 0.7634 0.5923 0.0367  -0.0755 0.0980  65   PHE B CE2 
3328  C  CZ  . PHE B 65  ? 0.6540 0.8819 0.7074 0.0397  -0.0722 0.1073  65   PHE B CZ  
3329  N  N   . LEU B 66  ? 0.4205 0.5846 0.5051 0.0440  -0.0359 0.0817  66   LEU B N   
3330  C  CA  . LEU B 66  ? 0.3884 0.5331 0.4545 0.0420  -0.0302 0.0790  66   LEU B CA  
3331  C  C   . LEU B 66  ? 0.3894 0.5418 0.4372 0.0379  -0.0359 0.0821  66   LEU B C   
3332  O  O   . LEU B 66  ? 0.5219 0.6616 0.5573 0.0382  -0.0326 0.0866  66   LEU B O   
3333  C  CB  . LEU B 66  ? 0.2560 0.3908 0.3195 0.0366  -0.0237 0.0655  66   LEU B CB  
3334  C  CG  . LEU B 66  ? 0.3587 0.4854 0.4368 0.0392  -0.0165 0.0616  66   LEU B CG  
3335  C  CD1 . LEU B 66  ? 0.2161 0.3311 0.2876 0.0338  -0.0108 0.0501  66   LEU B CD1 
3336  C  CD2 . LEU B 66  ? 0.2917 0.4033 0.3737 0.0482  -0.0105 0.0696  66   LEU B CD2 
3337  N  N   . GLY B 67  ? 0.3566 0.5306 0.4028 0.0335  -0.0445 0.0795  67   GLY B N   
3338  C  CA  . GLY B 67  ? 0.3317 0.5156 0.3587 0.0294  -0.0494 0.0812  67   GLY B CA  
3339  C  C   . GLY B 67  ? 0.3585 0.5627 0.3831 0.0230  -0.0571 0.0709  67   GLY B C   
3340  O  O   . GLY B 67  ? 0.4543 0.6654 0.4946 0.0214  -0.0596 0.0644  67   GLY B O   
3341  N  N   . ARG B 68  ? 0.4129 0.6271 0.4177 0.0188  -0.0607 0.0691  68   ARG B N   
3342  C  CA  . ARG B 68  ? 0.4121 0.6451 0.4111 0.0126  -0.0687 0.0578  68   ARG B CA  
3343  C  C   . ARG B 68  ? 0.4327 0.6614 0.4133 0.0074  -0.0639 0.0441  68   ARG B C   
3344  O  O   . ARG B 68  ? 0.4374 0.6560 0.4061 0.0086  -0.0567 0.0478  68   ARG B O   
3345  C  CB  . ARG B 68  ? 0.2837 0.5396 0.2757 0.0134  -0.0804 0.0684  68   ARG B CB  
3346  C  CG  . ARG B 68  ? 0.3992 0.6716 0.4113 0.0139  -0.0901 0.0700  68   ARG B CG  
3347  C  CD  . ARG B 68  ? 0.4013 0.6907 0.4126 0.0188  -0.0998 0.0876  68   ARG B CD  
3348  N  NE  . ARG B 68  ? 0.4331 0.7425 0.4644 0.0189  -0.1104 0.0886  68   ARG B NE  
3349  C  CZ  . ARG B 68  ? 0.6753 0.9938 0.7224 0.0265  -0.1157 0.1047  68   ARG B CZ  
3350  N  NH1 . ARG B 68  ? 0.6896 0.9961 0.7340 0.0348  -0.1114 0.1210  68   ARG B NH1 
3351  N  NH2 . ARG B 68  ? 0.8846 1.2243 0.9516 0.0259  -0.1256 0.1045  68   ARG B NH2 
3352  N  N   . SER B 69  ? 0.3583 0.5942 0.3384 0.0016  -0.0677 0.0281  69   SER B N   
3353  C  CA  . SER B 69  ? 0.2534 0.4861 0.2168 -0.0024 -0.0636 0.0134  69   SER B CA  
3354  C  C   . SER B 69  ? 0.3794 0.6303 0.3189 -0.0037 -0.0686 0.0156  69   SER B C   
3355  O  O   . SER B 69  ? 0.3493 0.6147 0.2854 -0.0019 -0.0761 0.0291  69   SER B O   
3356  C  CB  . SER B 69  ? 0.3567 0.5893 0.3278 -0.0082 -0.0666 -0.0051 69   SER B CB  
3357  O  OG  . SER B 69  ? 0.2346 0.4883 0.2044 -0.0124 -0.0792 -0.0084 69   SER B OG  
3358  N  N   . LEU B 70  ? 0.3496 0.6000 0.2723 -0.0063 -0.0642 0.0025  70   LEU B N   
3359  C  CA  . LEU B 70  ? 0.4827 0.7506 0.3800 -0.0073 -0.0669 0.0030  70   LEU B CA  
3360  C  C   . LEU B 70  ? 0.4427 0.7316 0.3365 -0.0106 -0.0810 0.0005  70   LEU B C   
3361  O  O   . LEU B 70  ? 0.4187 0.7254 0.2979 -0.0099 -0.0875 0.0114  70   LEU B O   
3362  C  CB  . LEU B 70  ? 0.4823 0.7469 0.3647 -0.0091 -0.0596 -0.0149 70   LEU B CB  
3363  C  CG  . LEU B 70  ? 0.4961 0.7461 0.3776 -0.0060 -0.0461 -0.0124 70   LEU B CG  
3364  C  CD1 . LEU B 70  ? 0.5488 0.7949 0.4214 -0.0068 -0.0395 -0.0326 70   LEU B CD1 
3365  C  CD2 . LEU B 70  ? 0.4260 0.6849 0.2938 -0.0040 -0.0429 0.0057  70   LEU B CD2 
3366  N  N   . GLU B 71  ? 0.4599 0.7467 0.3679 -0.0147 -0.0862 -0.0133 71   GLU B N   
3367  C  CA  . GLU B 71  ? 0.4292 0.7365 0.3337 -0.0196 -0.1003 -0.0201 71   GLU B CA  
3368  C  C   . GLU B 71  ? 0.4083 0.7240 0.3354 -0.0185 -0.1093 -0.0066 71   GLU B C   
3369  O  O   . GLU B 71  ? 0.6003 0.9290 0.5366 -0.0235 -0.1207 -0.0137 71   GLU B O   
3370  C  CB  . GLU B 71  ? 0.4790 0.7806 0.3842 -0.0260 -0.1017 -0.0450 71   GLU B CB  
3371  C  CG  . GLU B 71  ? 0.4695 0.7649 0.3514 -0.0256 -0.0928 -0.0591 71   GLU B CG  
3372  C  CD  . GLU B 71  ? 0.6583 0.9436 0.5424 -0.0308 -0.0932 -0.0843 71   GLU B CD  
3373  O  OE1 . GLU B 71  ? 0.7207 0.9952 0.6288 -0.0344 -0.0955 -0.0890 71   GLU B OE1 
3374  O  OE2 . GLU B 71  ? 0.6335 0.9211 0.4953 -0.0312 -0.0907 -0.0992 71   GLU B OE2 
3375  N  N   . GLY B 72  ? 0.3949 0.7033 0.3318 -0.0118 -0.1041 0.0127  72   GLY B N   
3376  C  CA  . GLY B 72  ? 0.3486 0.6658 0.3061 -0.0084 -0.1114 0.0278  72   GLY B CA  
3377  C  C   . GLY B 72  ? 0.3309 0.6377 0.3191 -0.0081 -0.1088 0.0260  72   GLY B C   
3378  O  O   . GLY B 72  ? 0.4631 0.7748 0.4696 -0.0031 -0.1117 0.0401  72   GLY B O   
3379  N  N   . ARG B 73  ? 0.3123 0.6051 0.3067 -0.0128 -0.1030 0.0094  73   ARG B N   
3380  C  CA  . ARG B 73  ? 0.3996 0.6839 0.4223 -0.0135 -0.1001 0.0077  73   ARG B CA  
3381  C  C   . ARG B 73  ? 0.4438 0.7114 0.4785 -0.0053 -0.0894 0.0215  73   ARG B C   
3382  O  O   . ARG B 73  ? 0.4707 0.7218 0.4931 -0.0019 -0.0799 0.0237  73   ARG B O   
3383  C  CB  . ARG B 73  ? 0.4655 0.7363 0.4905 -0.0204 -0.0958 -0.0120 73   ARG B CB  
3384  C  CG  . ARG B 73  ? 0.3665 0.6510 0.3819 -0.0292 -0.1066 -0.0285 73   ARG B CG  
3385  C  CD  . ARG B 73  ? 0.4458 0.7120 0.4647 -0.0349 -0.1010 -0.0471 73   ARG B CD  
3386  N  NE  . ARG B 73  ? 0.3725 0.6415 0.3683 -0.0394 -0.1048 -0.0641 73   ARG B NE  
3387  C  CZ  . ARG B 73  ? 0.5049 0.7864 0.5001 -0.0477 -0.1167 -0.0777 73   ARG B CZ  
3388  N  NH1 . ARG B 73  ? 0.5147 0.7973 0.4862 -0.0508 -0.1192 -0.0945 73   ARG B NH1 
3389  N  NH2 . ARG B 73  ? 0.6259 0.9198 0.6445 -0.0529 -0.1261 -0.0748 73   ARG B NH2 
3390  N  N   . ASN B 74  ? 0.5606 0.8335 0.6199 -0.0023 -0.0911 0.0300  74   ASN B N   
3391  C  CA  . ASN B 74  ? 0.4698 0.7283 0.5412 0.0063  -0.0817 0.0425  74   ASN B CA  
3392  C  C   . ASN B 74  ? 0.4792 0.7140 0.5559 0.0059  -0.0691 0.0349  74   ASN B C   
3393  O  O   . ASN B 74  ? 0.4941 0.7275 0.5823 -0.0001 -0.0683 0.0240  74   ASN B O   
3394  C  CB  . ASN B 74  ? 0.4464 0.7201 0.5437 0.0105  -0.0868 0.0530  74   ASN B CB  
3395  C  CG  . ASN B 74  ? 0.5991 0.8915 0.6926 0.0157  -0.0970 0.0675  74   ASN B CG  
3396  O  OD1 . ASN B 74  ? 0.6472 0.9325 0.7230 0.0202  -0.0952 0.0764  74   ASN B OD1 
3397  N  ND2 . ASN B 74  ? 0.5590 0.8759 0.6705 0.0148  -0.1079 0.0709  74   ASN B ND2 
3398  N  N   . LEU B 75  ? 0.4963 0.7124 0.5648 0.0118  -0.0597 0.0412  75   LEU B N   
3399  C  CA  . LEU B 75  ? 0.4634 0.6570 0.5358 0.0129  -0.0481 0.0366  75   LEU B CA  
3400  C  C   . LEU B 75  ? 0.3289 0.5181 0.4206 0.0200  -0.0430 0.0463  75   LEU B C   
3401  O  O   . LEU B 75  ? 0.4444 0.6287 0.5345 0.0276  -0.0412 0.0577  75   LEU B O   
3402  C  CB  . LEU B 75  ? 0.4970 0.6738 0.5496 0.0147  -0.0413 0.0367  75   LEU B CB  
3403  C  CG  . LEU B 75  ? 0.4537 0.6290 0.4886 0.0089  -0.0411 0.0245  75   LEU B CG  
3404  C  CD1 . LEU B 75  ? 0.5491 0.7413 0.5841 0.0020  -0.0500 0.0139  75   LEU B CD1 
3405  C  CD2 . LEU B 75  ? 0.3753 0.5504 0.3905 0.0107  -0.0403 0.0309  75   LEU B CD2 
3406  N  N   . LEU B 76  ? 0.2793 0.4698 0.3892 0.0176  -0.0403 0.0415  76   LEU B N   
3407  C  CA  . LEU B 76  ? 0.2459 0.4396 0.3767 0.0240  -0.0366 0.0501  76   LEU B CA  
3408  C  C   . LEU B 76  ? 0.3274 0.5025 0.4632 0.0256  -0.0243 0.0471  76   LEU B C   
3409  O  O   . LEU B 76  ? 0.3944 0.5611 0.5272 0.0190  -0.0213 0.0374  76   LEU B O   
3410  C  CB  . LEU B 76  ? 0.2812 0.4998 0.4337 0.0198  -0.0448 0.0500  76   LEU B CB  
3411  C  CG  . LEU B 76  ? 0.3677 0.6101 0.5203 0.0195  -0.0584 0.0553  76   LEU B CG  
3412  C  CD1 . LEU B 76  ? 0.4781 0.7436 0.6522 0.0123  -0.0666 0.0513  76   LEU B CD1 
3413  C  CD2 . LEU B 76  ? 0.3636 0.6090 0.5205 0.0310  -0.0586 0.0708  76   LEU B CD2 
3414  N  N   . ALA B 77  ? 0.4823 0.6508 0.6254 0.0347  -0.0174 0.0556  77   ALA B N   
3415  C  CA  . ALA B 77  ? 0.3599 0.5131 0.5074 0.0373  -0.0056 0.0539  77   ALA B CA  
3416  C  C   . ALA B 77  ? 0.3749 0.5395 0.5451 0.0437  -0.0018 0.0611  77   ALA B C   
3417  O  O   . ALA B 77  ? 0.4623 0.6344 0.6385 0.0517  -0.0044 0.0698  77   ALA B O   
3418  C  CB  . ALA B 77  ? 0.2279 0.3576 0.3570 0.0427  0.0010  0.0549  77   ALA B CB  
3419  N  N   . LEU B 78  ? 0.3738 0.5400 0.5574 0.0406  0.0049  0.0582  78   LEU B N   
3420  C  CA  . LEU B 78  ? 0.2085 0.3869 0.4150 0.0467  0.0108  0.0648  78   LEU B CA  
3421  C  C   . LEU B 78  ? 0.2697 0.4287 0.4693 0.0546  0.0244  0.0660  78   LEU B C   
3422  O  O   . LEU B 78  ? 0.2346 0.3790 0.4250 0.0504  0.0311  0.0607  78   LEU B O   
3423  C  CB  . LEU B 78  ? 0.1940 0.3899 0.4224 0.0376  0.0100  0.0623  78   LEU B CB  
3424  C  CG  . LEU B 78  ? 0.2429 0.4574 0.4989 0.0435  0.0158  0.0703  78   LEU B CG  
3425  C  CD1 . LEU B 78  ? 0.1599 0.3989 0.4311 0.0474  0.0051  0.0770  78   LEU B CD1 
3426  C  CD2 . LEU B 78  ? 0.2896 0.5138 0.5646 0.0337  0.0197  0.0679  78   LEU B CD2 
3427  N  N   . GLN B 79  ? 0.2305 0.3890 0.4341 0.0664  0.0282  0.0728  79   GLN B N   
3428  C  CA  . GLN B 79  ? 0.2655 0.4077 0.4638 0.0755  0.0412  0.0735  79   GLN B CA  
3429  C  C   . GLN B 79  ? 0.2956 0.4536 0.5173 0.0791  0.0505  0.0771  79   GLN B C   
3430  O  O   . GLN B 79  ? 0.2491 0.4302 0.4940 0.0823  0.0474  0.0830  79   GLN B O   
3431  C  CB  . GLN B 79  ? 0.3526 0.4832 0.5425 0.0871  0.0411  0.0779  79   GLN B CB  
3432  C  CG  . GLN B 79  ? 0.2773 0.4003 0.4714 0.0993  0.0537  0.0798  79   GLN B CG  
3433  C  CD  . GLN B 79  ? 0.3676 0.4776 0.5556 0.1109  0.0528  0.0837  79   GLN B CD  
3434  O  OE1 . GLN B 79  ? 0.4012 0.5187 0.5937 0.1121  0.0428  0.0895  79   GLN B OE1 
3435  N  NE2 . GLN B 79  ? 0.3672 0.4569 0.5444 0.1194  0.0630  0.0807  79   GLN B NE2 
3436  N  N   . ILE B 80  ? 0.4408 0.5876 0.6566 0.0787  0.0620  0.0742  80   ILE B N   
3437  C  CA  . ILE B 80  ? 0.3255 0.4850 0.5601 0.0831  0.0738  0.0781  80   ILE B CA  
3438  C  C   . ILE B 80  ? 0.3819 0.5214 0.6001 0.0946  0.0860  0.0770  80   ILE B C   
3439  O  O   . ILE B 80  ? 0.5435 0.6596 0.7367 0.0928  0.0878  0.0717  80   ILE B O   
3440  C  CB  . ILE B 80  ? 0.2237 0.3880 0.4650 0.0713  0.0777  0.0764  80   ILE B CB  
3441  C  CG1 . ILE B 80  ? 0.2282 0.4090 0.4838 0.0586  0.0651  0.0750  80   ILE B CG1 
3442  C  CG2 . ILE B 80  ? 0.1424 0.3217 0.4037 0.0756  0.0909  0.0820  80   ILE B CG2 
3443  C  CD1 . ILE B 80  ? 0.1491 0.3252 0.4048 0.0458  0.0667  0.0713  80   ILE B CD1 
3444  N  N   . SER B 81  ? 0.2899 0.4391 0.5223 0.1066  0.0941  0.0815  81   SER B N   
3445  C  CA  . SER B 81  ? 0.3733 0.5032 0.5894 0.1187  0.1056  0.0790  81   SER B CA  
3446  C  C   . SER B 81  ? 0.4699 0.6173 0.7071 0.1298  0.1185  0.0836  81   SER B C   
3447  O  O   . SER B 81  ? 0.4643 0.6397 0.7307 0.1287  0.1170  0.0899  81   SER B O   
3448  C  CB  . SER B 81  ? 0.3945 0.5058 0.5960 0.1262  0.0988  0.0774  81   SER B CB  
3449  O  OG  . SER B 81  ? 0.6400 0.7688 0.8633 0.1327  0.0928  0.0841  81   SER B OG  
3450  N  N   . ARG B 82  ? 0.4963 0.6281 0.7187 0.1405  0.1312  0.0802  82   ARG B N   
3451  C  CA  . ARG B 82  ? 0.4825 0.6291 0.7224 0.1537  0.1447  0.0835  82   ARG B CA  
3452  C  C   . ARG B 82  ? 0.5724 0.7319 0.8342 0.1637  0.1384  0.0886  82   ARG B C   
3453  O  O   . ARG B 82  ? 0.6499 0.8375 0.9419 0.1689  0.1428  0.0952  82   ARG B O   
3454  C  CB  . ARG B 82  ? 0.5536 0.6765 0.7683 0.1649  0.1577  0.0767  82   ARG B CB  
3455  C  CG  . ARG B 82  ? 0.5522 0.6896 0.7825 0.1803  0.1742  0.0787  82   ARG B CG  
3456  C  CD  . ARG B 82  ? 0.7176 0.8515 0.9321 0.1811  0.1909  0.0759  82   ARG B CD  
3457  N  NE  . ARG B 82  ? 0.8528 0.9637 1.0428 0.1953  0.2011  0.0672  82   ARG B NE  
3458  C  CZ  . ARG B 82  ? 0.8777 0.9874 1.0543 0.2015  0.2178  0.0643  82   ARG B CZ  
3459  N  NH1 . ARG B 82  ? 0.7818 0.8686 0.9347 0.2144  0.2250  0.0546  82   ARG B NH1 
3460  N  NH2 . ARG B 82  ? 0.8597 0.9904 1.0461 0.1947  0.2274  0.0709  82   ARG B NH2 
3461  N  N   . ASN B 83  ? 0.4431 0.5827 0.6904 0.1661  0.1278  0.0864  83   ASN B N   
3462  C  CA  . ASN B 83  ? 0.3016 0.4491 0.5660 0.1758  0.1204  0.0923  83   ASN B CA  
3463  C  C   . ASN B 83  ? 0.2986 0.4333 0.5503 0.1686  0.1038  0.0928  83   ASN B C   
3464  O  O   . ASN B 83  ? 0.3973 0.5030 0.6246 0.1704  0.1018  0.0881  83   ASN B O   
3465  C  CB  . ASN B 83  ? 0.4963 0.6278 0.7566 0.1945  0.1305  0.0898  83   ASN B CB  
3466  C  CG  . ASN B 83  ? 0.6605 0.7871 0.9285 0.2034  0.1203  0.0950  83   ASN B CG  
3467  O  OD1 . ASN B 83  ? 0.7225 0.8715 1.0112 0.2001  0.1091  0.1036  83   ASN B OD1 
3468  N  ND2 . ASN B 83  ? 0.6664 0.7631 0.9173 0.2144  0.1236  0.0901  83   ASN B ND2 
3469  N  N   . THR B 84  ? 0.4366 0.5941 0.7051 0.1602  0.0917  0.0988  84   THR B N   
3470  C  CA  . THR B 84  ? 0.2795 0.4285 0.5345 0.1513  0.0766  0.0993  84   THR B CA  
3471  C  C   . THR B 84  ? 0.1690 0.3007 0.4168 0.1618  0.0715  0.1029  84   THR B C   
3472  O  O   . THR B 84  ? 0.3652 0.4819 0.5952 0.1557  0.0620  0.1025  84   THR B O   
3473  C  CB  . THR B 84  ? 0.3408 0.5201 0.6155 0.1409  0.0645  0.1045  84   THR B CB  
3474  O  OG1 . THR B 84  ? 0.5702 0.7412 0.8261 0.1257  0.0565  0.0991  84   THR B OG1 
3475  C  CG2 . THR B 84  ? 0.1536 0.3463 0.4431 0.1483  0.0535  0.1140  84   THR B CG2 
3476  N  N   . ARG B 85  ? 0.3134 0.4465 0.5757 0.1779  0.0783  0.1067  85   ARG B N   
3477  C  CA  . ARG B 85  ? 0.4313 0.5483 0.6904 0.1883  0.0727  0.1116  85   ARG B CA  
3478  C  C   . ARG B 85  ? 0.4935 0.5728 0.7207 0.1855  0.0731  0.1043  85   ARG B C   
3479  O  O   . ARG B 85  ? 0.5244 0.5909 0.7411 0.1825  0.0629  0.1081  85   ARG B O   
3480  C  CB  . ARG B 85  ? 0.6049 0.7251 0.8836 0.2078  0.0821  0.1151  85   ARG B CB  
3481  C  CG  . ARG B 85  ? 0.8163 0.9755 1.1309 0.2128  0.0800  0.1247  85   ARG B CG  
3482  C  CD  . ARG B 85  ? 1.0566 1.2154 1.3901 0.2339  0.0850  0.1307  85   ARG B CD  
3483  N  NE  . ARG B 85  ? 1.1871 1.3379 1.5210 0.2383  0.0715  0.1401  85   ARG B NE  
3484  C  CZ  . ARG B 85  ? 1.1566 1.2714 1.4696 0.2428  0.0700  0.1385  85   ARG B CZ  
3485  N  NH1 . ARG B 85  ? 1.0884 1.1989 1.4042 0.2461  0.0576  0.1495  85   ARG B NH1 
3486  N  NH2 . ARG B 85  ? 1.1341 1.2174 1.4234 0.2435  0.0804  0.1264  85   ARG B NH2 
3487  N  N   . SER B 86  ? 0.5206 0.5835 0.7326 0.1863  0.0850  0.0942  86   SER B N   
3488  C  CA  . SER B 86  ? 0.5299 0.5585 0.7120 0.1826  0.0850  0.0862  86   SER B CA  
3489  C  C   . SER B 86  ? 0.7515 0.7762 0.9158 0.1709  0.0895  0.0775  86   SER B C   
3490  O  O   . SER B 86  ? 0.9115 0.9579 1.0838 0.1612  0.0879  0.0789  86   SER B O   
3491  C  CB  . SER B 86  ? 0.4748 0.4783 0.6510 0.1980  0.0941  0.0815  86   SER B CB  
3492  O  OG  . SER B 86  ? 0.5896 0.5910 0.7802 0.2088  0.0888  0.0901  86   SER B OG  
3493  N  N   . ARG B 87  ? 0.6195 0.6155 0.7594 0.1716  0.0941  0.0687  87   ARG B N   
3494  C  CA  . ARG B 87  ? 0.5298 0.5197 0.6515 0.1634  0.0995  0.0606  87   ARG B CA  
3495  C  C   . ARG B 87  ? 0.5868 0.5551 0.6937 0.1741  0.1111  0.0519  87   ARG B C   
3496  O  O   . ARG B 87  ? 0.5262 0.4680 0.6188 0.1782  0.1088  0.0474  87   ARG B O   
3497  C  CB  . ARG B 87  ? 0.2978 0.2745 0.4001 0.1498  0.0894  0.0581  87   ARG B CB  
3498  C  CG  . ARG B 87  ? 0.3751 0.3593 0.4692 0.1380  0.0905  0.0546  87   ARG B CG  
3499  C  CD  . ARG B 87  ? 0.4129 0.3800 0.4855 0.1271  0.0825  0.0504  87   ARG B CD  
3500  N  NE  . ARG B 87  ? 0.4985 0.4405 0.5494 0.1304  0.0873  0.0423  87   ARG B NE  
3501  C  CZ  . ARG B 87  ? 0.5482 0.4677 0.5883 0.1334  0.0837  0.0397  87   ARG B CZ  
3502  N  NH1 . ARG B 87  ? 0.6190 0.5377 0.6676 0.1334  0.0756  0.0460  87   ARG B NH1 
3503  N  NH2 . ARG B 87  ? 0.7038 0.6014 0.7240 0.1357  0.0877  0.0309  87   ARG B NH2 
3504  N  N   . ASN B 88  ? 0.5586 0.5385 0.6691 0.1786  0.1236  0.0495  88   ASN B N   
3505  C  CA  . ASN B 88  ? 0.4637 0.4253 0.5574 0.1887  0.1355  0.0404  88   ASN B CA  
3506  C  C   . ASN B 88  ? 0.5211 0.4536 0.5830 0.1818  0.1313  0.0311  88   ASN B C   
3507  O  O   . ASN B 88  ? 0.3736 0.3069 0.4252 0.1684  0.1250  0.0311  88   ASN B O   
3508  C  CB  . ASN B 88  ? 0.5240 0.5054 0.6238 0.1917  0.1497  0.0405  88   ASN B CB  
3509  C  CG  . ASN B 88  ? 0.5758 0.5877 0.7096 0.1985  0.1540  0.0496  88   ASN B CG  
3510  O  OD1 . ASN B 88  ? 0.7225 0.7600 0.8721 0.1909  0.1552  0.0557  88   ASN B OD1 
3511  N  ND2 . ASN B 88  ? 0.6495 0.6588 0.7963 0.2127  0.1556  0.0509  88   ASN B ND2 
3512  N  N   . LEU B 89  ? 0.4945 0.4012 0.5423 0.1914  0.1346  0.0230  89   LEU B N   
3513  C  CA  . LEU B 89  ? 0.5143 0.3928 0.5326 0.1861  0.1310  0.0129  89   LEU B CA  
3514  C  C   . LEU B 89  ? 0.5063 0.3912 0.5081 0.1772  0.1344  0.0098  89   LEU B C   
3515  O  O   . LEU B 89  ? 0.5021 0.4002 0.5047 0.1823  0.1466  0.0094  89   LEU B O   
3516  C  CB  . LEU B 89  ? 0.4243 0.2779 0.4298 0.1998  0.1386  0.0023  89   LEU B CB  
3517  C  CG  . LEU B 89  ? 0.5620 0.3823 0.5416 0.1945  0.1308  -0.0077 89   LEU B CG  
3518  C  CD1 . LEU B 89  ? 0.3757 0.1851 0.3644 0.1888  0.1173  -0.0016 89   LEU B CD1 
3519  C  CD2 . LEU B 89  ? 0.6425 0.4384 0.6055 0.2075  0.1398  -0.0212 89   LEU B CD2 
3520  N  N   . LEU B 90  ? 0.4713 0.3478 0.4596 0.1641  0.1239  0.0088  90   LEU B N   
3521  C  CA  . LEU B 90  ? 0.5947 0.4731 0.5654 0.1552  0.1247  0.0061  90   LEU B CA  
3522  C  C   . LEU B 90  ? 0.5446 0.4502 0.5306 0.1487  0.1269  0.0148  90   LEU B C   
3523  O  O   . LEU B 90  ? 0.4467 0.3552 0.4207 0.1428  0.1293  0.0142  90   LEU B O   
3524  C  CB  . LEU B 90  ? 0.4251 0.2893 0.3717 0.1624  0.1344  -0.0041 90   LEU B CB  
3525  C  CG  . LEU B 90  ? 0.4582 0.2915 0.3847 0.1644  0.1290  -0.0149 90   LEU B CG  
3526  C  CD1 . LEU B 90  ? 0.4132 0.2326 0.3154 0.1737  0.1393  -0.0266 90   LEU B CD1 
3527  C  CD2 . LEU B 90  ? 0.4352 0.2593 0.3505 0.1502  0.1152  -0.0155 90   LEU B CD2 
3528  N  N   . THR B 91  ? 0.4727 0.3975 0.4852 0.1494  0.1254  0.0231  91   THR B N   
3529  C  CA  . THR B 91  ? 0.4216 0.3702 0.4499 0.1408  0.1244  0.0306  91   THR B CA  
3530  C  C   . THR B 91  ? 0.4653 0.4113 0.4901 0.1281  0.1112  0.0318  91   THR B C   
3531  O  O   . THR B 91  ? 0.4044 0.3454 0.4331 0.1267  0.1020  0.0332  91   THR B O   
3532  C  CB  . THR B 91  ? 0.3151 0.2879 0.3741 0.1451  0.1264  0.0387  91   THR B CB  
3533  O  OG1 . THR B 91  ? 0.3292 0.3085 0.3943 0.1573  0.1403  0.0382  91   THR B OG1 
3534  C  CG2 . THR B 91  ? 0.2161 0.2113 0.2903 0.1340  0.1235  0.0450  91   THR B CG2 
3535  N  N   . PRO B 92  ? 0.4183 0.3677 0.4358 0.1192  0.1107  0.0319  92   PRO B N   
3536  C  CA  . PRO B 92  ? 0.3849 0.3329 0.3991 0.1078  0.0994  0.0324  92   PRO B CA  
3537  C  C   . PRO B 92  ? 0.4998 0.4666 0.5364 0.1030  0.0931  0.0384  92   PRO B C   
3538  O  O   . PRO B 92  ? 0.3164 0.3016 0.3699 0.1023  0.0974  0.0427  92   PRO B O   
3539  C  CB  . PRO B 92  ? 0.4807 0.4303 0.4857 0.1019  0.1028  0.0321  92   PRO B CB  
3540  C  CG  . PRO B 92  ? 0.5435 0.4921 0.5415 0.1103  0.1159  0.0311  92   PRO B CG  
3541  C  CD  . PRO B 92  ? 0.3705 0.3267 0.3841 0.1200  0.1214  0.0327  92   PRO B CD  
3542  N  N   . PRO B 93  ? 0.6828 0.6459 0.7193 0.0993  0.0828  0.0389  93   PRO B N   
3543  C  CA  . PRO B 93  ? 0.5226 0.5035 0.5751 0.0928  0.0754  0.0435  93   PRO B CA  
3544  C  C   . PRO B 93  ? 0.4937 0.4760 0.5401 0.0822  0.0713  0.0412  93   PRO B C   
3545  O  O   . PRO B 93  ? 0.3581 0.3258 0.3873 0.0792  0.0689  0.0372  93   PRO B O   
3546  C  CB  . PRO B 93  ? 0.3879 0.3620 0.4387 0.0939  0.0672  0.0453  93   PRO B CB  
3547  C  CG  . PRO B 93  ? 0.3936 0.3432 0.4237 0.0956  0.0677  0.0400  93   PRO B CG  
3548  C  CD  . PRO B 93  ? 0.4784 0.4209 0.4985 0.0994  0.0773  0.0352  93   PRO B CD  
3549  N  N   . VAL B 94  ? 0.3606 0.3601 0.4218 0.0768  0.0705  0.0434  94   VAL B N   
3550  C  CA  . VAL B 94  ? 0.2583 0.2584 0.3160 0.0678  0.0677  0.0409  94   VAL B CA  
3551  C  C   . VAL B 94  ? 0.2819 0.2984 0.3539 0.0611  0.0602  0.0417  94   VAL B C   
3552  O  O   . VAL B 94  ? 0.4903 0.5213 0.5780 0.0631  0.0589  0.0454  94   VAL B O   
3553  C  CB  . VAL B 94  ? 0.3629 0.3639 0.4224 0.0672  0.0764  0.0416  94   VAL B CB  
3554  C  CG1 . VAL B 94  ? 0.7446 0.7443 0.8020 0.0587  0.0731  0.0395  94   VAL B CG1 
3555  C  CG2 . VAL B 94  ? 0.3739 0.3595 0.4160 0.0738  0.0837  0.0401  94   VAL B CG2 
3556  N  N   . LYS B 95  ? 0.2639 0.2787 0.3306 0.0537  0.0549  0.0380  95   LYS B N   
3557  C  CA  . LYS B 95  ? 0.3836 0.4130 0.4611 0.0472  0.0475  0.0369  95   LYS B CA  
3558  C  C   . LYS B 95  ? 0.4792 0.5082 0.5580 0.0396  0.0467  0.0323  95   LYS B C   
3559  O  O   . LYS B 95  ? 0.2190 0.2347 0.2862 0.0390  0.0491  0.0299  95   LYS B O   
3560  C  CB  . LYS B 95  ? 0.2180 0.2472 0.2870 0.0466  0.0397  0.0364  95   LYS B CB  
3561  C  CG  . LYS B 95  ? 0.3282 0.3424 0.3795 0.0452  0.0390  0.0329  95   LYS B CG  
3562  C  CD  . LYS B 95  ? 0.3670 0.3748 0.4093 0.0486  0.0360  0.0359  95   LYS B CD  
3563  C  CE  . LYS B 95  ? 0.2535 0.2604 0.2861 0.0435  0.0306  0.0334  95   LYS B CE  
3564  N  NZ  . LYS B 95  ? 0.5039 0.5009 0.5280 0.0412  0.0329  0.0286  95   LYS B NZ  
3565  N  N   . TYR B 96  ? 0.3615 0.4049 0.4551 0.0340  0.0426  0.0312  96   TYR B N   
3566  C  CA  . TYR B 96  ? 0.4234 0.4661 0.5192 0.0263  0.0398  0.0253  96   TYR B CA  
3567  C  C   . TYR B 96  ? 0.3535 0.4076 0.4503 0.0219  0.0303  0.0208  96   TYR B C   
3568  O  O   . TYR B 96  ? 0.2776 0.3474 0.3857 0.0213  0.0260  0.0232  96   TYR B O   
3569  C  CB  . TYR B 96  ? 0.3862 0.4354 0.5000 0.0219  0.0436  0.0269  96   TYR B CB  
3570  C  CG  . TYR B 96  ? 0.3252 0.3620 0.4361 0.0236  0.0529  0.0302  96   TYR B CG  
3571  C  CD1 . TYR B 96  ? 0.3990 0.4190 0.4919 0.0263  0.0550  0.0288  96   TYR B CD1 
3572  C  CD2 . TYR B 96  ? 0.3479 0.3916 0.4747 0.0220  0.0594  0.0354  96   TYR B CD2 
3573  C  CE1 . TYR B 96  ? 0.3375 0.3469 0.4261 0.0280  0.0629  0.0327  96   TYR B CE1 
3574  C  CE2 . TYR B 96  ? 0.4120 0.4453 0.5349 0.0234  0.0685  0.0397  96   TYR B CE2 
3575  C  CZ  . TYR B 96  ? 0.4955 0.5114 0.5983 0.0266  0.0699  0.0384  96   TYR B CZ  
3576  O  OH  . TYR B 96  ? 0.5955 0.6021 0.6929 0.0282  0.0783  0.0435  96   TYR B OH  
3577  N  N   . ILE B 97  ? 0.2799 0.3274 0.3652 0.0191  0.0269  0.0145  97   ILE B N   
3578  C  CA  . ILE B 97  ? 0.3997 0.4580 0.4838 0.0144  0.0187  0.0085  97   ILE B CA  
3579  C  C   . ILE B 97  ? 0.4111 0.4663 0.4988 0.0077  0.0170  -0.0008 97   ILE B C   
3580  O  O   . ILE B 97  ? 0.2472 0.2881 0.3325 0.0079  0.0218  -0.0026 97   ILE B O   
3581  C  CB  . ILE B 97  ? 0.3808 0.4376 0.4483 0.0169  0.0158  0.0081  97   ILE B CB  
3582  C  CG1 . ILE B 97  ? 0.3946 0.4514 0.4587 0.0230  0.0168  0.0170  97   ILE B CG1 
3583  C  CG2 . ILE B 97  ? 0.3616 0.4320 0.4267 0.0124  0.0079  0.0026  97   ILE B CG2 
3584  C  CD1 . ILE B 97  ? 0.3718 0.4121 0.4291 0.0280  0.0237  0.0203  97   ILE B CD1 
3585  N  N   . ALA B 98  ? 0.1805 0.2484 0.2736 0.0021  0.0097  -0.0067 98   ALA B N   
3586  C  CA  . ALA B 98  ? 0.1814 0.2447 0.2775 -0.0042 0.0075  -0.0173 98   ALA B CA  
3587  C  C   . ALA B 98  ? 0.3791 0.4516 0.4661 -0.0073 -0.0003 -0.0268 98   ALA B C   
3588  O  O   . ALA B 98  ? 0.4662 0.5511 0.5453 -0.0053 -0.0046 -0.0239 98   ALA B O   
3589  C  CB  . ALA B 98  ? 0.2860 0.3529 0.4022 -0.0104 0.0073  -0.0172 98   ALA B CB  
3590  N  N   . ASN B 99  ? 0.4412 0.5068 0.5288 -0.0119 -0.0018 -0.0381 99   ASN B N   
3591  C  CA  . ASN B 99  ? 0.2706 0.3453 0.3507 -0.0159 -0.0092 -0.0496 99   ASN B CA  
3592  C  C   . ASN B 99  ? 0.4367 0.5192 0.4976 -0.0112 -0.0104 -0.0490 99   ASN B C   
3593  O  O   . ASN B 99  ? 0.5638 0.6611 0.6175 -0.0136 -0.0173 -0.0535 99   ASN B O   
3594  C  CB  . ASN B 99  ? 0.2984 0.3901 0.3908 -0.0225 -0.0174 -0.0504 99   ASN B CB  
3595  C  CG  . ASN B 99  ? 0.5224 0.6208 0.6090 -0.0286 -0.0258 -0.0651 99   ASN B CG  
3596  O  OD1 . ASN B 99  ? 0.5096 0.6270 0.5940 -0.0313 -0.0343 -0.0658 99   ASN B OD1 
3597  N  ND2 . ASN B 99  ? 0.4520 0.5348 0.5358 -0.0303 -0.0236 -0.0772 99   ASN B ND2 
3598  N  N   . MET B 100 ? 0.4227 0.4962 0.4752 -0.0050 -0.0039 -0.0432 100  MET B N   
3599  C  CA  . MET B 100 ? 0.5025 0.5822 0.5381 -0.0016 -0.0040 -0.0431 100  MET B CA  
3600  C  C   . MET B 100 ? 0.4474 0.5275 0.4742 -0.0034 -0.0053 -0.0577 100  MET B C   
3601  O  O   . MET B 100 ? 0.4622 0.5548 0.4755 -0.0032 -0.0080 -0.0608 100  MET B O   
3602  C  CB  . MET B 100 ? 0.5199 0.5896 0.5504 0.0043  0.0027  -0.0345 100  MET B CB  
3603  C  CG  . MET B 100 ? 0.6467 0.7016 0.6761 0.0066  0.0082  -0.0400 100  MET B CG  
3604  S  SD  . MET B 100 ? 0.4634 0.5097 0.4868 0.0124  0.0140  -0.0300 100  MET B SD  
3605  C  CE  . MET B 100 ? 0.3610 0.4227 0.3722 0.0127  0.0112  -0.0243 100  MET B CE  
3606  N  N   . HIS B 101 ? 0.3871 0.4532 0.4214 -0.0046 -0.0029 -0.0663 101  HIS B N   
3607  C  CA  . HIS B 101 ? 0.3600 0.4244 0.3891 -0.0065 -0.0046 -0.0822 101  HIS B CA  
3608  C  C   . HIS B 101 ? 0.4366 0.5055 0.4751 -0.0145 -0.0122 -0.0895 101  HIS B C   
3609  O  O   . HIS B 101 ? 0.2812 0.3395 0.3356 -0.0183 -0.0120 -0.0895 101  HIS B O   
3610  C  CB  . HIS B 101 ? 0.2157 0.2609 0.2485 -0.0028 0.0018  -0.0875 101  HIS B CB  
3611  C  CG  . HIS B 101 ? 0.4485 0.4925 0.4726 0.0044  0.0079  -0.0820 101  HIS B CG  
3612  N  ND1 . HIS B 101 ? 0.5706 0.6034 0.6002 0.0082  0.0129  -0.0719 101  HIS B ND1 
3613  C  CD2 . HIS B 101 ? 0.6378 0.6919 0.6485 0.0080  0.0097  -0.0849 101  HIS B CD2 
3614  C  CE1 . HIS B 101 ? 0.5813 0.6171 0.6026 0.0134  0.0166  -0.0693 101  HIS B CE1 
3615  N  NE2 . HIS B 101 ? 0.6333 0.6822 0.6438 0.0133  0.0153  -0.0766 101  HIS B NE2 
3616  N  N   . GLY B 102 ? 0.4065 0.4928 0.4352 -0.0174 -0.0193 -0.0947 102  GLY B N   
3617  C  CA  . GLY B 102 ? 0.2961 0.3917 0.3335 -0.0254 -0.0284 -0.0997 102  GLY B CA  
3618  C  C   . GLY B 102 ? 0.3402 0.4203 0.3904 -0.0312 -0.0294 -0.1121 102  GLY B C   
3619  O  O   . GLY B 102 ? 0.6685 0.7517 0.7344 -0.0387 -0.0350 -0.1123 102  GLY B O   
3620  N  N   . ASP B 103 ? 0.3451 0.4086 0.3905 -0.0279 -0.0239 -0.1220 103  ASP B N   
3621  C  CA  . ASP B 103 ? 0.5293 0.5757 0.5859 -0.0332 -0.0253 -0.1352 103  ASP B CA  
3622  C  C   . ASP B 103 ? 0.3846 0.4116 0.4586 -0.0323 -0.0185 -0.1260 103  ASP B C   
3623  O  O   . ASP B 103 ? 0.5222 0.5309 0.6067 -0.0358 -0.0179 -0.1342 103  ASP B O   
3624  C  CB  . ASP B 103 ? 0.5978 0.6360 0.6404 -0.0297 -0.0236 -0.1530 103  ASP B CB  
3625  C  CG  . ASP B 103 ? 0.6797 0.7135 0.7123 -0.0189 -0.0141 -0.1479 103  ASP B CG  
3626  O  OD1 . ASP B 103 ? 0.8095 0.8417 0.8294 -0.0143 -0.0116 -0.1606 103  ASP B OD1 
3627  O  OD2 . ASP B 103 ? 0.7614 0.7942 0.7990 -0.0151 -0.0092 -0.1315 103  ASP B OD2 
3628  N  N   . GLU B 104 ? 0.3461 0.3765 0.4221 -0.0277 -0.0134 -0.1089 104  GLU B N   
3629  C  CA  . GLU B 104 ? 0.2248 0.2403 0.3156 -0.0270 -0.0071 -0.0979 104  GLU B CA  
3630  C  C   . GLU B 104 ? 0.2951 0.3226 0.3993 -0.0319 -0.0094 -0.0863 104  GLU B C   
3631  O  O   . GLU B 104 ? 0.4089 0.4483 0.5085 -0.0276 -0.0080 -0.0749 104  GLU B O   
3632  C  CB  . GLU B 104 ? 0.2874 0.2963 0.3690 -0.0172 0.0009  -0.0886 104  GLU B CB  
3633  C  CG  . GLU B 104 ? 0.6443 0.6467 0.7129 -0.0111 0.0033  -0.0992 104  GLU B CG  
3634  C  CD  . GLU B 104 ? 0.6769 0.6774 0.7375 -0.0023 0.0098  -0.0895 104  GLU B CD  
3635  O  OE1 . GLU B 104 ? 0.8009 0.8003 0.8655 -0.0009 0.0126  -0.0759 104  GLU B OE1 
3636  O  OE2 . GLU B 104 ? 0.7363 0.7371 0.7869 0.0033  0.0121  -0.0959 104  GLU B OE2 
3637  N  N   . THR B 105 ? 0.3677 0.3920 0.4898 -0.0408 -0.0126 -0.0891 105  THR B N   
3638  C  CA  . THR B 105 ? 0.4016 0.4446 0.5373 -0.0474 -0.0180 -0.0832 105  THR B CA  
3639  C  C   . THR B 105 ? 0.3369 0.3778 0.4927 -0.0499 -0.0125 -0.0697 105  THR B C   
3640  O  O   . THR B 105 ? 0.2706 0.3296 0.4364 -0.0514 -0.0143 -0.0608 105  THR B O   
3641  C  CB  . THR B 105 ? 0.4925 0.5423 0.6348 -0.0580 -0.0287 -0.0978 105  THR B CB  
3642  O  OG1 . THR B 105 ? 0.5038 0.5323 0.6580 -0.0641 -0.0275 -0.1059 105  THR B OG1 
3643  C  CG2 . THR B 105 ? 0.4683 0.5263 0.5886 -0.0557 -0.0348 -0.1107 105  THR B CG2 
3644  N  N   . VAL B 106 ? 0.2855 0.3055 0.4480 -0.0500 -0.0056 -0.0675 106  VAL B N   
3645  C  CA  . VAL B 106 ? 0.3125 0.3305 0.4935 -0.0531 0.0005  -0.0546 106  VAL B CA  
3646  C  C   . VAL B 106 ? 0.3123 0.3430 0.4904 -0.0456 0.0061  -0.0397 106  VAL B C   
3647  O  O   . VAL B 106 ? 0.3165 0.3614 0.5106 -0.0490 0.0069  -0.0313 106  VAL B O   
3648  C  CB  . VAL B 106 ? 0.5187 0.5111 0.7026 -0.0522 0.0079  -0.0523 106  VAL B CB  
3649  C  CG1 . VAL B 106 ? 0.4164 0.4081 0.6175 -0.0552 0.0153  -0.0374 106  VAL B CG1 
3650  C  CG2 . VAL B 106 ? 0.4486 0.4258 0.6377 -0.0594 0.0026  -0.0674 106  VAL B CG2 
3651  N  N   . GLY B 107 ? 0.4423 0.4680 0.6011 -0.0355 0.0101  -0.0369 107  GLY B N   
3652  C  CA  . GLY B 107 ? 0.4185 0.4534 0.5720 -0.0280 0.0147  -0.0249 107  GLY B CA  
3653  C  C   . GLY B 107 ? 0.3573 0.4158 0.5168 -0.0291 0.0089  -0.0225 107  GLY B C   
3654  O  O   . GLY B 107 ? 0.4563 0.5242 0.6240 -0.0263 0.0129  -0.0119 107  GLY B O   
3655  N  N   . ARG B 108 ? 0.2635 0.3319 0.4184 -0.0326 -0.0006 -0.0322 108  ARG B N   
3656  C  CA  . ARG B 108 ? 0.3091 0.4010 0.4707 -0.0347 -0.0083 -0.0305 108  ARG B CA  
3657  C  C   . ARG B 108 ? 0.3422 0.4458 0.5298 -0.0408 -0.0080 -0.0242 108  ARG B C   
3658  O  O   . ARG B 108 ? 0.4237 0.5418 0.6198 -0.0367 -0.0061 -0.0137 108  ARG B O   
3659  C  CB  . ARG B 108 ? 0.3959 0.4941 0.5496 -0.0402 -0.0189 -0.0443 108  ARG B CB  
3660  C  CG  . ARG B 108 ? 0.3574 0.4796 0.5218 -0.0459 -0.0294 -0.0452 108  ARG B CG  
3661  C  CD  . ARG B 108 ? 0.4425 0.5685 0.5928 -0.0503 -0.0392 -0.0601 108  ARG B CD  
3662  N  NE  . ARG B 108 ? 0.4427 0.5940 0.5996 -0.0547 -0.0506 -0.0599 108  ARG B NE  
3663  C  CZ  . ARG B 108 ? 0.3553 0.5225 0.4974 -0.0506 -0.0569 -0.0579 108  ARG B CZ  
3664  N  NH1 . ARG B 108 ? 0.2769 0.4679 0.4286 -0.0552 -0.0679 -0.0567 108  ARG B NH1 
3665  N  NH2 . ARG B 108 ? 0.4664 0.6269 0.5857 -0.0425 -0.0526 -0.0565 108  ARG B NH2 
3666  N  N   . GLN B 109 ? 0.4557 0.5530 0.6576 -0.0507 -0.0096 -0.0304 109  GLN B N   
3667  C  CA  . GLN B 109 ? 0.4522 0.5619 0.6816 -0.0584 -0.0094 -0.0245 109  GLN B CA  
3668  C  C   . GLN B 109 ? 0.3565 0.4622 0.5941 -0.0532 0.0036  -0.0101 109  GLN B C   
3669  O  O   . GLN B 109 ? 0.2765 0.3998 0.5336 -0.0543 0.0058  -0.0010 109  GLN B O   
3670  C  CB  . GLN B 109 ? 0.5133 0.6142 0.7561 -0.0713 -0.0142 -0.0348 109  GLN B CB  
3671  C  CG  . GLN B 109 ? 0.5670 0.6846 0.8144 -0.0801 -0.0288 -0.0465 109  GLN B CG  
3672  C  CD  . GLN B 109 ? 0.5488 0.6974 0.8127 -0.0809 -0.0341 -0.0380 109  GLN B CD  
3673  O  OE1 . GLN B 109 ? 0.6872 0.8522 0.9411 -0.0782 -0.0431 -0.0409 109  GLN B OE1 
3674  N  NE2 . GLN B 109 ? 0.3347 0.4920 0.6240 -0.0842 -0.0282 -0.0268 109  GLN B NE2 
3675  N  N   . LEU B 110 ? 0.3046 0.3883 0.5274 -0.0473 0.0122  -0.0081 110  LEU B N   
3676  C  CA  . LEU B 110 ? 0.3128 0.3914 0.5388 -0.0419 0.0246  0.0048  110  LEU B CA  
3677  C  C   . LEU B 110 ? 0.4115 0.5052 0.6341 -0.0321 0.0277  0.0134  110  LEU B C   
3678  O  O   . LEU B 110 ? 0.4793 0.5805 0.7135 -0.0294 0.0361  0.0237  110  LEU B O   
3679  C  CB  . LEU B 110 ? 0.4303 0.4835 0.6380 -0.0367 0.0312  0.0047  110  LEU B CB  
3680  C  CG  . LEU B 110 ? 0.3831 0.4176 0.5968 -0.0444 0.0315  -0.0001 110  LEU B CG  
3681  C  CD1 . LEU B 110 ? 0.4070 0.4189 0.6025 -0.0370 0.0380  0.0022  110  LEU B CD1 
3682  C  CD2 . LEU B 110 ? 0.1960 0.2360 0.4350 -0.0530 0.0362  0.0081  110  LEU B CD2 
3683  N  N   . LEU B 111 ? 0.4521 0.5498 0.6588 -0.0265 0.0214  0.0093  111  LEU B N   
3684  C  CA  . LEU B 111 ? 0.3280 0.4368 0.5310 -0.0168 0.0237  0.0171  111  LEU B CA  
3685  C  C   . LEU B 111 ? 0.2880 0.4227 0.5135 -0.0197 0.0188  0.0210  111  LEU B C   
3686  O  O   . LEU B 111 ? 0.3937 0.5390 0.6273 -0.0128 0.0242  0.0301  111  LEU B O   
3687  C  CB  . LEU B 111 ? 0.4337 0.5377 0.6135 -0.0107 0.0186  0.0130  111  LEU B CB  
3688  C  CG  . LEU B 111 ? 0.4322 0.5132 0.5910 -0.0058 0.0246  0.0115  111  LEU B CG  
3689  C  CD1 . LEU B 111 ? 0.3579 0.4368 0.4968 0.0003  0.0208  0.0098  111  LEU B CD1 
3690  C  CD2 . LEU B 111 ? 0.4632 0.5352 0.6223 -0.0002 0.0363  0.0203  111  LEU B CD2 
3691  N  N   . VAL B 112 ? 0.3471 0.4921 0.5830 -0.0298 0.0083  0.0134  112  VAL B N   
3692  C  CA  . VAL B 112 ? 0.3116 0.4834 0.5723 -0.0347 0.0018  0.0166  112  VAL B CA  
3693  C  C   . VAL B 112 ? 0.3068 0.4854 0.5932 -0.0383 0.0110  0.0250  112  VAL B C   
3694  O  O   . VAL B 112 ? 0.3312 0.5316 0.6371 -0.0357 0.0123  0.0334  112  VAL B O   
3695  C  CB  . VAL B 112 ? 0.3430 0.5226 0.6083 -0.0465 -0.0122 0.0048  112  VAL B CB  
3696  C  CG1 . VAL B 112 ? 0.1051 0.3100 0.4014 -0.0549 -0.0176 0.0079  112  VAL B CG1 
3697  C  CG2 . VAL B 112 ? 0.2934 0.4779 0.5377 -0.0424 -0.0222 -0.0007 112  VAL B CG2 
3698  N  N   . TYR B 113 ? 0.3695 0.5296 0.6562 -0.0440 0.0176  0.0235  113  TYR B N   
3699  C  CA  . TYR B 113 ? 0.3400 0.5035 0.6479 -0.0476 0.0282  0.0328  113  TYR B CA  
3700  C  C   . TYR B 113 ? 0.4077 0.5703 0.7091 -0.0346 0.0419  0.0440  113  TYR B C   
3701  O  O   . TYR B 113 ? 0.3188 0.4978 0.6405 -0.0334 0.0498  0.0537  113  TYR B O   
3702  C  CB  . TYR B 113 ? 0.3593 0.4990 0.6646 -0.0558 0.0317  0.0291  113  TYR B CB  
3703  C  CG  . TYR B 113 ? 0.4273 0.5665 0.7447 -0.0702 0.0202  0.0182  113  TYR B CG  
3704  C  CD1 . TYR B 113 ? 0.4981 0.6119 0.8091 -0.0763 0.0206  0.0116  113  TYR B CD1 
3705  C  CD2 . TYR B 113 ? 0.4718 0.6352 0.8070 -0.0774 0.0086  0.0142  113  TYR B CD2 
3706  C  CE1 . TYR B 113 ? 0.5157 0.6261 0.8372 -0.0893 0.0103  0.0001  113  TYR B CE1 
3707  C  CE2 . TYR B 113 ? 0.5154 0.6774 0.8605 -0.0912 -0.0026 0.0026  113  TYR B CE2 
3708  C  CZ  . TYR B 113 ? 0.5625 0.6968 0.9005 -0.0972 -0.0015 -0.0051 113  TYR B CZ  
3709  O  OH  . TYR B 113 ? 0.5429 0.6729 0.8901 -0.1107 -0.0125 -0.0182 113  TYR B OH  
3710  N  N   . MET B 114 ? 0.4334 0.5770 0.7067 -0.0250 0.0450  0.0423  114  MET B N   
3711  C  CA  . MET B 114 ? 0.3817 0.5211 0.6451 -0.0129 0.0571  0.0506  114  MET B CA  
3712  C  C   . MET B 114 ? 0.4413 0.6039 0.7172 -0.0053 0.0568  0.0561  114  MET B C   
3713  O  O   . MET B 114 ? 0.5079 0.6817 0.7977 -0.0008 0.0672  0.0647  114  MET B O   
3714  C  CB  . MET B 114 ? 0.2702 0.3865 0.5019 -0.0052 0.0576  0.0463  114  MET B CB  
3715  C  CG  . MET B 114 ? 0.3254 0.4343 0.5433 0.0069  0.0687  0.0527  114  MET B CG  
3716  S  SD  . MET B 114 ? 0.3379 0.4421 0.5618 0.0063  0.0842  0.0617  114  MET B SD  
3717  C  CE  . MET B 114 ? 0.7346 0.8160 0.9486 -0.0027 0.0815  0.0571  114  MET B CE  
3718  N  N   . ALA B 115 ? 0.2420 0.4123 0.5134 -0.0035 0.0452  0.0516  115  ALA B N   
3719  C  CA  . ALA B 115 ? 0.2346 0.4256 0.5173 0.0047  0.0435  0.0574  115  ALA B CA  
3720  C  C   . ALA B 115 ? 0.2883 0.5031 0.6036 0.0014  0.0487  0.0649  115  ALA B C   
3721  O  O   . ALA B 115 ? 0.3674 0.5870 0.6891 0.0103  0.0608  0.0727  115  ALA B O   
3722  C  CB  . ALA B 115 ? 0.2334 0.4346 0.5135 0.0024  0.0280  0.0524  115  ALA B CB  
3723  N  N   . GLN B 116 ? 0.3752 0.6050 0.7110 -0.0115 0.0396  0.0620  116  GLN B N   
3724  C  CA  . GLN B 116 ? 0.3021 0.5562 0.6726 -0.0182 0.0431  0.0687  116  GLN B CA  
3725  C  C   . GLN B 116 ? 0.3538 0.6013 0.7286 -0.0159 0.0609  0.0766  116  GLN B C   
3726  O  O   . GLN B 116 ? 0.4692 0.7344 0.8609 -0.0086 0.0707  0.0856  116  GLN B O   
3727  C  CB  . GLN B 116 ? 0.1925 0.4525 0.5782 -0.0357 0.0315  0.0617  116  GLN B CB  
3728  C  CG  . GLN B 116 ? 0.2680 0.5393 0.6506 -0.0388 0.0133  0.0539  116  GLN B CG  
3729  C  CD  . GLN B 116 ? 0.3193 0.5930 0.7129 -0.0561 0.0015  0.0443  116  GLN B CD  
3730  O  OE1 . GLN B 116 ? 0.2827 0.5818 0.7058 -0.0653 -0.0054 0.0459  116  GLN B OE1 
3731  N  NE2 . GLN B 116 ? 0.3453 0.5925 0.7158 -0.0606 -0.0012 0.0337  116  GLN B NE2 
3732  N  N   . TYR B 117 ? 0.2855 0.5079 0.6447 -0.0214 0.0653  0.0734  117  TYR B N   
3733  C  CA  . TYR B 117 ? 0.2592 0.4737 0.6188 -0.0198 0.0818  0.0814  117  TYR B CA  
3734  C  C   . TYR B 117 ? 0.2651 0.4828 0.6161 -0.0035 0.0943  0.0881  117  TYR B C   
3735  O  O   . TYR B 117 ? 0.2949 0.5297 0.6648 -0.0007 0.1062  0.0972  117  TYR B O   
3736  C  CB  . TYR B 117 ? 0.2557 0.4387 0.5908 -0.0234 0.0834  0.0769  117  TYR B CB  
3737  C  CG  . TYR B 117 ? 0.3098 0.4837 0.6436 -0.0231 0.0992  0.0860  117  TYR B CG  
3738  C  CD1 . TYR B 117 ? 0.2861 0.4659 0.6435 -0.0357 0.1033  0.0920  117  TYR B CD1 
3739  C  CD2 . TYR B 117 ? 0.2856 0.4448 0.5937 -0.0107 0.1096  0.0889  117  TYR B CD2 
3740  C  CE1 . TYR B 117 ? 0.3540 0.5258 0.7088 -0.0355 0.1180  0.1019  117  TYR B CE1 
3741  C  CE2 . TYR B 117 ? 0.2943 0.4459 0.5982 -0.0102 0.1236  0.0976  117  TYR B CE2 
3742  C  CZ  . TYR B 117 ? 0.3712 0.5295 0.6981 -0.0222 0.1282  0.1047  117  TYR B CZ  
3743  O  OH  . TYR B 117 ? 0.5160 0.6671 0.8373 -0.0215 0.1426  0.1149  117  TYR B OH  
3744  N  N   . LEU B 118 ? 0.3327 0.5341 0.6558 0.0073  0.0920  0.0833  118  LEU B N   
3745  C  CA  . LEU B 118 ? 0.3823 0.5812 0.6933 0.0229  0.1031  0.0873  118  LEU B CA  
3746  C  C   . LEU B 118 ? 0.4561 0.6835 0.7924 0.0305  0.1059  0.0935  118  LEU B C   
3747  O  O   . LEU B 118 ? 0.5942 0.8309 0.9393 0.0375  0.1203  0.1004  118  LEU B O   
3748  C  CB  . LEU B 118 ? 0.4166 0.5933 0.6959 0.0312  0.0977  0.0805  118  LEU B CB  
3749  C  CG  . LEU B 118 ? 0.4381 0.5860 0.6894 0.0291  0.1002  0.0764  118  LEU B CG  
3750  C  CD1 . LEU B 118 ? 0.4964 0.6261 0.7206 0.0358  0.0933  0.0697  118  LEU B CD1 
3751  C  CD2 . LEU B 118 ? 0.4537 0.5953 0.6981 0.0343  0.1164  0.0826  118  LEU B CD2 
3752  N  N   . LEU B 119 ? 0.3710 0.6131 0.7189 0.0298  0.0924  0.0913  119  LEU B N   
3753  C  CA  . LEU B 119 ? 0.4270 0.6980 0.8014 0.0375  0.0932  0.0978  119  LEU B CA  
3754  C  C   . LEU B 119 ? 0.4600 0.7568 0.8683 0.0312  0.1020  0.1058  119  LEU B C   
3755  O  O   . LEU B 119 ? 0.3757 0.6860 0.7964 0.0414  0.1156  0.1129  119  LEU B O   
3756  C  CB  . LEU B 119 ? 0.3137 0.5983 0.6961 0.0351  0.0751  0.0951  119  LEU B CB  
3757  C  CG  . LEU B 119 ? 0.3572 0.6250 0.7138 0.0468  0.0701  0.0920  119  LEU B CG  
3758  C  CD1 . LEU B 119 ? 0.3698 0.6491 0.7295 0.0430  0.0516  0.0897  119  LEU B CD1 
3759  C  CD2 . LEU B 119 ? 0.1636 0.4354 0.5239 0.0642  0.0813  0.0981  119  LEU B CD2 
3760  N  N   . GLY B 120 ? 0.4016 0.7048 0.8250 0.0142  0.0945  0.1043  120  GLY B N   
3761  C  CA  . GLY B 120 ? 0.3130 0.6427 0.7725 0.0051  0.1001  0.1120  120  GLY B CA  
3762  C  C   . GLY B 120 ? 0.2979 0.6227 0.7570 0.0069  0.1202  0.1195  120  GLY B C   
3763  O  O   . GLY B 120 ? 0.3581 0.7081 0.8482 0.0027  0.1288  0.1283  120  GLY B O   
3764  N  N   . ASN B 121 ? 0.2755 0.5696 0.6999 0.0129  0.1277  0.1165  121  ASN B N   
3765  C  CA  . ASN B 121 ? 0.4024 0.6906 0.8220 0.0141  0.1462  0.1239  121  ASN B CA  
3766  C  C   . ASN B 121 ? 0.3858 0.6647 0.7824 0.0325  0.1606  0.1252  121  ASN B C   
3767  O  O   . ASN B 121 ? 0.5194 0.8021 0.9164 0.0358  0.1777  0.1326  121  ASN B O   
3768  C  CB  . ASN B 121 ? 0.4400 0.7017 0.8427 0.0018  0.1445  0.1215  121  ASN B CB  
3769  C  CG  . ASN B 121 ? 0.3886 0.6615 0.8204 -0.0173 0.1369  0.1231  121  ASN B CG  
3770  O  OD1 . ASN B 121 ? 0.2970 0.5824 0.7504 -0.0249 0.1473  0.1328  121  ASN B OD1 
3771  N  ND2 . ASN B 121 ? 0.4627 0.7310 0.8948 -0.0255 0.1188  0.1134  121  ASN B ND2 
3772  N  N   . HIS B 122 ? 0.2238 0.4911 0.6005 0.0442  0.1540  0.1182  122  HIS B N   
3773  C  CA  . HIS B 122 ? 0.3013 0.5542 0.6523 0.0608  0.1654  0.1167  122  HIS B CA  
3774  C  C   . HIS B 122 ? 0.3971 0.6727 0.7658 0.0721  0.1829  0.1244  122  HIS B C   
3775  O  O   . HIS B 122 ? 0.4600 0.7245 0.8083 0.0819  0.1975  0.1249  122  HIS B O   
3776  C  CB  . HIS B 122 ? 0.5624 0.8012 0.8951 0.0702  0.1540  0.1087  122  HIS B CB  
3777  C  CG  . HIS B 122 ? 0.5784 0.8399 0.9333 0.0808  0.1520  0.1112  122  HIS B CG  
3778  N  ND1 . HIS B 122 ? 0.5758 0.8584 0.9562 0.0746  0.1379  0.1124  122  HIS B ND1 
3779  C  CD2 . HIS B 122 ? 0.4995 0.7650 0.8545 0.0980  0.1619  0.1125  122  HIS B CD2 
3780  C  CE1 . HIS B 122 ? 0.5769 0.8766 0.9731 0.0876  0.1389  0.1158  122  HIS B CE1 
3781  N  NE2 . HIS B 122 ? 0.5324 0.8215 0.9144 0.1022  0.1538  0.1156  122  HIS B NE2 
3782  N  N   . GLU B 123 ? 0.4754 0.7839 0.8820 0.0710  0.1816  0.1301  123  GLU B N   
3783  C  CA  . GLU B 123 ? 0.5129 0.8462 0.9397 0.0820  0.1992  0.1379  123  GLU B CA  
3784  C  C   . GLU B 123 ? 0.3958 0.7414 0.8359 0.0723  0.2136  0.1472  123  GLU B C   
3785  O  O   . GLU B 123 ? 0.3973 0.7543 0.8402 0.0821  0.2325  0.1528  123  GLU B O   
3786  C  CB  . GLU B 123 ? 0.6181 0.9844 1.0819 0.0871  0.1932  0.1415  123  GLU B CB  
3787  C  CG  . GLU B 123 ? 0.8652 1.2204 1.3152 0.1024  0.1850  0.1350  123  GLU B CG  
3788  C  CD  . GLU B 123 ? 1.0811 1.4687 1.5653 0.1146  0.1866  0.1407  123  GLU B CD  
3789  O  OE1 . GLU B 123 ? 1.1173 1.5396 1.6399 0.1075  0.1881  0.1489  123  GLU B OE1 
3790  O  OE2 . GLU B 123 ? 1.1750 1.5537 1.6492 0.1313  0.1861  0.1375  123  GLU B OE2 
3791  N  N   . ARG B 124 ? 0.3854 0.7279 0.8331 0.0533  0.2052  0.1488  124  ARG B N   
3792  C  CA  . ARG B 124 ? 0.3215 0.6743 0.7840 0.0420  0.2178  0.1591  124  ARG B CA  
3793  C  C   . ARG B 124 ? 0.3766 0.6993 0.8026 0.0415  0.2274  0.1596  124  ARG B C   
3794  O  O   . ARG B 124 ? 0.5014 0.8320 0.9285 0.0429  0.2455  0.1689  124  ARG B O   
3795  C  CB  . ARG B 124 ? 0.4574 0.8219 0.9497 0.0210  0.2049  0.1616  124  ARG B CB  
3796  C  CG  . ARG B 124 ? 0.6414 1.0016 1.1355 0.0160  0.1820  0.1515  124  ARG B CG  
3797  C  CD  . ARG B 124 ? 0.7353 1.0936 1.2452 -0.0060 0.1700  0.1510  124  ARG B CD  
3798  N  NE  . ARG B 124 ? 0.7261 1.1101 1.2725 -0.0177 0.1797  0.1628  124  ARG B NE  
3799  C  CZ  . ARG B 124 ? 0.7437 1.1609 1.3318 -0.0270 0.1727  0.1663  124  ARG B CZ  
3800  N  NH1 . ARG B 124 ? 0.7710 1.1999 1.3682 -0.0253 0.1555  0.1590  124  ARG B NH1 
3801  N  NH2 . ARG B 124 ? 0.7290 1.1686 1.3500 -0.0384 0.1827  0.1778  124  ARG B NH2 
3802  N  N   . ILE B 125 ? 0.2952 0.5853 0.6895 0.0395  0.2153  0.1503  125  ILE B N   
3803  C  CA  . ILE B 125 ? 0.4421 0.7035 0.8019 0.0387  0.2218  0.1508  125  ILE B CA  
3804  C  C   . ILE B 125 ? 0.5157 0.7558 0.8365 0.0556  0.2259  0.1431  125  ILE B C   
3805  O  O   . ILE B 125 ? 0.5342 0.7591 0.8397 0.0603  0.2129  0.1328  125  ILE B O   
3806  C  CB  . ILE B 125 ? 0.4231 0.6615 0.7744 0.0238  0.2069  0.1467  125  ILE B CB  
3807  C  CG1 . ILE B 125 ? 0.4451 0.6961 0.8270 0.0059  0.2082  0.1563  125  ILE B CG1 
3808  C  CG2 . ILE B 125 ? 0.3637 0.5702 0.6741 0.0278  0.2100  0.1444  125  ILE B CG2 
3809  C  CD1 . ILE B 125 ? 0.4432 0.7255 0.8679 -0.0020 0.2011  0.1577  125  ILE B CD1 
3810  N  N   . SER B 126 ? 0.6769 0.9159 0.9814 0.0639  0.2439  0.1484  126  SER B N   
3811  C  CA  . SER B 126 ? 0.7081 0.9300 0.9772 0.0806  0.2501  0.1410  126  SER B CA  
3812  C  C   . SER B 126 ? 0.7038 0.8919 0.9388 0.0803  0.2357  0.1304  126  SER B C   
3813  O  O   . SER B 126 ? 0.6338 0.8112 0.8548 0.0903  0.2292  0.1205  126  SER B O   
3814  C  CB  . SER B 126 ? 0.7260 0.9501 0.9791 0.0861  0.2711  0.1487  126  SER B CB  
3815  O  OG  . SER B 126 ? 0.7307 0.9495 0.9605 0.1043  0.2806  0.1416  126  SER B OG  
3816  N  N   . ASP B 127 ? 0.7076 0.8792 0.9305 0.0689  0.2311  0.1330  127  ASP B N   
3817  C  CA  . ASP B 127 ? 0.6619 0.8039 0.8550 0.0680  0.2179  0.1240  127  ASP B CA  
3818  C  C   . ASP B 127 ? 0.5051 0.6445 0.7040 0.0693  0.2019  0.1139  127  ASP B C   
3819  O  O   . ASP B 127 ? 0.5180 0.6408 0.6931 0.0780  0.1969  0.1051  127  ASP B O   
3820  C  CB  . ASP B 127 ? 0.8247 0.9544 1.0164 0.0538  0.2125  0.1289  127  ASP B CB  
3821  C  CG  . ASP B 127 ? 1.0310 1.1526 1.2022 0.0546  0.2257  0.1377  127  ASP B CG  
3822  O  OD1 . ASP B 127 ? 1.0695 1.1829 1.2121 0.0665  0.2331  0.1347  127  ASP B OD1 
3823  O  OD2 . ASP B 127 ? 1.0494 1.1720 1.2324 0.0431  0.2282  0.1477  127  ASP B OD2 
3824  N  N   . LEU B 128 ? 0.3989 0.5550 0.6292 0.0601  0.1936  0.1155  128  LEU B N   
3825  C  CA  . LEU B 128 ? 0.4306 0.5866 0.6672 0.0599  0.1777  0.1074  128  LEU B CA  
3826  C  C   . LEU B 128 ? 0.4801 0.6450 0.7185 0.0747  0.1807  0.1044  128  LEU B C   
3827  O  O   . LEU B 128 ? 0.3966 0.5482 0.6200 0.0807  0.1714  0.0967  128  LEU B O   
3828  C  CB  . LEU B 128 ? 0.4462 0.6214 0.7168 0.0467  0.1689  0.1102  128  LEU B CB  
3829  C  CG  . LEU B 128 ? 0.4049 0.5714 0.6791 0.0312  0.1652  0.1127  128  LEU B CG  
3830  C  CD1 . LEU B 128 ? 0.4202 0.6088 0.7314 0.0184  0.1577  0.1150  128  LEU B CD1 
3831  C  CD2 . LEU B 128 ? 0.4100 0.5484 0.6569 0.0290  0.1536  0.1040  128  LEU B CD2 
3832  N  N   . GLY B 129 ? 0.3126 0.5004 0.5709 0.0807  0.1941  0.1112  129  GLY B N   
3833  C  CA  . GLY B 129 ? 0.5386 0.7359 0.8019 0.0962  0.1988  0.1091  129  GLY B CA  
3834  C  C   . GLY B 129 ? 0.5341 0.7044 0.7602 0.1082  0.2017  0.1010  129  GLY B C   
3835  O  O   . GLY B 129 ? 0.5830 0.7482 0.8048 0.1193  0.1983  0.0954  129  GLY B O   
3836  N  N   . GLN B 130 ? 0.2064 0.3587 0.4057 0.1055  0.2073  0.1006  130  GLN B N   
3837  C  CA  . GLN B 130 ? 0.3659 0.4924 0.5285 0.1151  0.2092  0.0925  130  GLN B CA  
3838  C  C   . GLN B 130 ? 0.4587 0.5624 0.6039 0.1096  0.1917  0.0848  130  GLN B C   
3839  O  O   . GLN B 130 ? 0.4927 0.5799 0.6196 0.1180  0.1874  0.0768  130  GLN B O   
3840  C  CB  . GLN B 130 ? 0.4395 0.5587 0.5799 0.1150  0.2222  0.0960  130  GLN B CB  
3841  C  CG  . GLN B 130 ? 0.5863 0.6887 0.6944 0.1288  0.2302  0.0883  130  GLN B CG  
3842  C  CD  . GLN B 130 ? 0.6597 0.7326 0.7373 0.1278  0.2170  0.0786  130  GLN B CD  
3843  O  OE1 . GLN B 130 ? 0.5826 0.6469 0.6586 0.1165  0.2044  0.0790  130  GLN B OE1 
3844  N  NE2 . GLN B 130 ? 0.7624 0.8197 0.8160 0.1398  0.2200  0.0693  130  GLN B NE2 
3845  N  N   . LEU B 131 ? 0.4834 0.5861 0.6351 0.0957  0.1820  0.0871  131  LEU B N   
3846  C  CA  . LEU B 131 ? 0.3010 0.3869 0.4412 0.0902  0.1656  0.0804  131  LEU B CA  
3847  C  C   . LEU B 131 ? 0.2304 0.3204 0.3798 0.0964  0.1575  0.0762  131  LEU B C   
3848  O  O   . LEU B 131 ? 0.3395 0.4116 0.4689 0.1020  0.1522  0.0696  131  LEU B O   
3849  C  CB  . LEU B 131 ? 0.3173 0.4076 0.4719 0.0753  0.1568  0.0831  131  LEU B CB  
3850  C  CG  . LEU B 131 ? 0.4678 0.5430 0.6113 0.0695  0.1409  0.0760  131  LEU B CG  
3851  C  CD1 . LEU B 131 ? 0.3539 0.4042 0.4648 0.0717  0.1400  0.0715  131  LEU B CD1 
3852  C  CD2 . LEU B 131 ? 0.4625 0.5442 0.6236 0.0558  0.1329  0.0775  131  LEU B CD2 
3853  N  N   . VAL B 132 ? 0.2955 0.4097 0.4759 0.0950  0.1564  0.0810  132  VAL B N   
3854  C  CA  . VAL B 132 ? 0.2862 0.4081 0.4794 0.1000  0.1473  0.0794  132  VAL B CA  
3855  C  C   . VAL B 132 ? 0.4327 0.5454 0.6148 0.1160  0.1532  0.0761  132  VAL B C   
3856  O  O   . VAL B 132 ? 0.6028 0.7037 0.7765 0.1200  0.1439  0.0720  132  VAL B O   
3857  C  CB  . VAL B 132 ? 0.3815 0.5349 0.6121 0.0963  0.1461  0.0862  132  VAL B CB  
3858  C  CG1 . VAL B 132 ? 0.4254 0.5888 0.6696 0.1043  0.1382  0.0864  132  VAL B CG1 
3859  C  CG2 . VAL B 132 ? 0.2980 0.4574 0.5396 0.0795  0.1369  0.0873  132  VAL B CG2 
3860  N  N   . ASN B 133 ? 0.3795 0.4975 0.5616 0.1250  0.1690  0.0780  133  ASN B N   
3861  C  CA  . ASN B 133 ? 0.3644 0.4725 0.5354 0.1412  0.1767  0.0736  133  ASN B CA  
3862  C  C   . ASN B 133 ? 0.4377 0.5130 0.5738 0.1432  0.1711  0.0644  133  ASN B C   
3863  O  O   . ASN B 133 ? 0.4813 0.5436 0.6100 0.1534  0.1693  0.0594  133  ASN B O   
3864  C  CB  . ASN B 133 ? 0.5010 0.6185 0.6720 0.1493  0.1962  0.0759  133  ASN B CB  
3865  C  CG  . ASN B 133 ? 0.4644 0.6145 0.6721 0.1549  0.2046  0.0837  133  ASN B CG  
3866  O  OD1 . ASN B 133 ? 0.3565 0.5245 0.5916 0.1511  0.1948  0.0882  133  ASN B OD1 
3867  N  ND2 . ASN B 133 ? 0.5099 0.6694 0.7179 0.1642  0.2229  0.0855  133  ASN B ND2 
3868  N  N   . SER B 134 ? 0.3940 0.4560 0.5099 0.1333  0.1680  0.0624  134  SER B N   
3869  C  CA  . SER B 134 ? 0.4565 0.4900 0.5392 0.1348  0.1645  0.0541  134  SER B CA  
3870  C  C   . SER B 134 ? 0.4955 0.5167 0.5712 0.1253  0.1480  0.0515  134  SER B C   
3871  O  O   . SER B 134 ? 0.5069 0.5061 0.5583 0.1253  0.1431  0.0450  134  SER B O   
3872  C  CB  . SER B 134 ? 0.4985 0.5252 0.5601 0.1323  0.1733  0.0540  134  SER B CB  
3873  O  OG  . SER B 134 ? 0.5260 0.5607 0.5956 0.1192  0.1694  0.0600  134  SER B OG  
3874  N  N   . THR B 135 ? 0.4651 0.5018 0.5624 0.1170  0.1395  0.0562  135  THR B N   
3875  C  CA  . THR B 135 ? 0.4475 0.4757 0.5391 0.1081  0.1250  0.0538  135  THR B CA  
3876  C  C   . THR B 135 ? 0.4061 0.4483 0.5189 0.1072  0.1156  0.0569  135  THR B C   
3877  O  O   . THR B 135 ? 0.5031 0.5679 0.6410 0.1070  0.1176  0.0623  135  THR B O   
3878  C  CB  . THR B 135 ? 0.5651 0.5952 0.6556 0.0957  0.1221  0.0552  135  THR B CB  
3879  O  OG1 . THR B 135 ? 0.4562 0.4829 0.5363 0.0968  0.1334  0.0566  135  THR B OG1 
3880  C  CG2 . THR B 135 ? 0.4305 0.4440 0.5035 0.0893  0.1105  0.0502  135  THR B CG2 
3881  N  N   . ASP B 136 ? 0.3892 0.4190 0.4918 0.1062  0.1052  0.0539  136  ASP B N   
3882  C  CA  . ASP B 136 ? 0.4317 0.4730 0.5493 0.1042  0.0947  0.0573  136  ASP B CA  
3883  C  C   . ASP B 136 ? 0.4461 0.4914 0.5628 0.0912  0.0851  0.0562  136  ASP B C   
3884  O  O   . ASP B 136 ? 0.4390 0.4684 0.5368 0.0866  0.0804  0.0519  136  ASP B O   
3885  C  CB  . ASP B 136 ? 0.5799 0.6044 0.6858 0.1104  0.0895  0.0557  136  ASP B CB  
3886  C  CG  . ASP B 136 ? 0.8003 0.8366 0.9251 0.1189  0.0877  0.0614  136  ASP B CG  
3887  O  OD1 . ASP B 136 ? 0.8314 0.8760 0.9686 0.1284  0.0972  0.0634  136  ASP B OD1 
3888  O  OD2 . ASP B 136 ? 0.9586 0.9969 1.0860 0.1165  0.0770  0.0645  136  ASP B OD2 
3889  N  N   . ILE B 137 ? 0.3170 0.3837 0.4546 0.0852  0.0822  0.0595  137  ILE B N   
3890  C  CA  . ILE B 137 ? 0.2985 0.3683 0.4359 0.0728  0.0754  0.0569  137  ILE B CA  
3891  C  C   . ILE B 137 ? 0.2837 0.3671 0.4308 0.0675  0.0630  0.0575  137  ILE B C   
3892  O  O   . ILE B 137 ? 0.3307 0.4337 0.4980 0.0693  0.0608  0.0621  137  ILE B O   
3893  C  CB  . ILE B 137 ? 0.3168 0.3981 0.4688 0.0673  0.0820  0.0589  137  ILE B CB  
3894  C  CG1 . ILE B 137 ? 0.3367 0.4048 0.4757 0.0716  0.0943  0.0590  137  ILE B CG1 
3895  C  CG2 . ILE B 137 ? 0.2580 0.3414 0.4124 0.0548  0.0743  0.0556  137  ILE B CG2 
3896  C  CD1 . ILE B 137 ? 0.2816 0.3622 0.4364 0.0678  0.1033  0.0636  137  ILE B CD1 
3897  N  N   . TYR B 138 ? 0.4259 0.5004 0.5586 0.0610  0.0552  0.0530  138  TYR B N   
3898  C  CA  . TYR B 138 ? 0.3747 0.4613 0.5117 0.0555  0.0434  0.0525  138  TYR B CA  
3899  C  C   . TYR B 138 ? 0.2866 0.3758 0.4232 0.0442  0.0386  0.0464  138  TYR B C   
3900  O  O   . TYR B 138 ? 0.3677 0.4415 0.4897 0.0412  0.0406  0.0417  138  TYR B O   
3901  C  CB  . TYR B 138 ? 0.3387 0.4140 0.4587 0.0585  0.0380  0.0527  138  TYR B CB  
3902  C  CG  . TYR B 138 ? 0.3326 0.4042 0.4540 0.0693  0.0402  0.0587  138  TYR B CG  
3903  C  CD1 . TYR B 138 ? 0.3666 0.4201 0.4782 0.0765  0.0489  0.0579  138  TYR B CD1 
3904  C  CD2 . TYR B 138 ? 0.2987 0.3839 0.4302 0.0725  0.0331  0.0649  138  TYR B CD2 
3905  C  CE1 . TYR B 138 ? 0.2904 0.3377 0.4031 0.0868  0.0509  0.0620  138  TYR B CE1 
3906  C  CE2 . TYR B 138 ? 0.3545 0.4343 0.4882 0.0831  0.0350  0.0707  138  TYR B CE2 
3907  C  CZ  . TYR B 138 ? 0.3200 0.3799 0.4446 0.0903  0.0441  0.0688  138  TYR B CZ  
3908  O  OH  . TYR B 138 ? 0.3800 0.4325 0.5074 0.1013  0.0458  0.0736  138  TYR B OH  
3909  N  N   . LEU B 139 ? 0.3011 0.4095 0.4539 0.0383  0.0320  0.0462  139  LEU B N   
3910  C  CA  . LEU B 139 ? 0.3911 0.5015 0.5459 0.0276  0.0276  0.0392  139  LEU B CA  
3911  C  C   . LEU B 139 ? 0.3929 0.5128 0.5432 0.0228  0.0157  0.0351  139  LEU B C   
3912  O  O   . LEU B 139 ? 0.3571 0.4960 0.5193 0.0227  0.0089  0.0384  139  LEU B O   
3913  C  CB  . LEU B 139 ? 0.0723 0.1966 0.2508 0.0221  0.0299  0.0405  139  LEU B CB  
3914  C  CG  . LEU B 139 ? 0.3355 0.4543 0.5204 0.0262  0.0428  0.0456  139  LEU B CG  
3915  C  CD1 . LEU B 139 ? 0.3497 0.4841 0.5598 0.0186  0.0444  0.0475  139  LEU B CD1 
3916  C  CD2 . LEU B 139 ? 0.2391 0.3342 0.4045 0.0267  0.0495  0.0428  139  LEU B CD2 
3917  N  N   . VAL B 140 ? 0.3983 0.5064 0.5314 0.0191  0.0133  0.0281  140  VAL B N   
3918  C  CA  . VAL B 140 ? 0.4240 0.5404 0.5493 0.0145  0.0033  0.0229  140  VAL B CA  
3919  C  C   . VAL B 140 ? 0.4242 0.5396 0.5514 0.0051  0.0002  0.0123  140  VAL B C   
3920  O  O   . VAL B 140 ? 0.4206 0.5219 0.5343 0.0037  0.0021  0.0058  140  VAL B O   
3921  C  CB  . VAL B 140 ? 0.3876 0.4932 0.4914 0.0185  0.0031  0.0234  140  VAL B CB  
3922  C  CG1 . VAL B 140 ? 0.2689 0.3865 0.3638 0.0149  -0.0065 0.0202  140  VAL B CG1 
3923  C  CG2 . VAL B 140 ? 0.4093 0.5100 0.5115 0.0275  0.0071  0.0331  140  VAL B CG2 
3924  N  N   . PRO B 141 ? 0.3961 0.5263 0.5413 -0.0014 -0.0047 0.0103  141  PRO B N   
3925  C  CA  . PRO B 141 ? 0.4089 0.5368 0.5590 -0.0111 -0.0079 -0.0003 141  PRO B CA  
3926  C  C   . PRO B 141 ? 0.4088 0.5331 0.5404 -0.0139 -0.0140 -0.0109 141  PRO B C   
3927  O  O   . PRO B 141 ? 0.4436 0.5548 0.5717 -0.0181 -0.0125 -0.0201 141  PRO B O   
3928  C  CB  . PRO B 141 ? 0.3936 0.5434 0.5660 -0.0172 -0.0150 0.0006  141  PRO B CB  
3929  C  CG  . PRO B 141 ? 0.4072 0.5655 0.5919 -0.0098 -0.0095 0.0133  141  PRO B CG  
3930  C  CD  . PRO B 141 ? 0.4400 0.5894 0.6050 0.0003  -0.0067 0.0184  141  PRO B CD  
3931  N  N   . THR B 142 ? 0.3183 0.4540 0.4384 -0.0111 -0.0203 -0.0093 142  THR B N   
3932  C  CA  . THR B 142 ? 0.4834 0.6166 0.5835 -0.0125 -0.0242 -0.0184 142  THR B CA  
3933  C  C   . THR B 142 ? 0.5316 0.6658 0.6139 -0.0057 -0.0237 -0.0116 142  THR B C   
3934  O  O   . THR B 142 ? 0.4795 0.6234 0.5646 -0.0013 -0.0257 -0.0009 142  THR B O   
3935  C  CB  . THR B 142 ? 0.3667 0.5153 0.4673 -0.0203 -0.0353 -0.0283 142  THR B CB  
3936  O  OG1 . THR B 142 ? 0.4128 0.5567 0.4929 -0.0209 -0.0366 -0.0387 142  THR B OG1 
3937  C  CG2 . THR B 142 ? 0.2817 0.4529 0.3854 -0.0189 -0.0437 -0.0201 142  THR B CG2 
3938  N  N   . MET B 143 ? 0.6054 0.7297 0.6710 -0.0050 -0.0210 -0.0177 143  MET B N   
3939  C  CA  . MET B 143 ? 0.4678 0.5920 0.5167 -0.0001 -0.0196 -0.0120 143  MET B CA  
3940  C  C   . MET B 143 ? 0.5110 0.6451 0.5441 -0.0033 -0.0249 -0.0208 143  MET B C   
3941  O  O   . MET B 143 ? 0.3754 0.5138 0.3937 -0.0007 -0.0247 -0.0165 143  MET B O   
3942  C  CB  . MET B 143 ? 0.3614 0.4664 0.4054 0.0038  -0.0105 -0.0108 143  MET B CB  
3943  C  CG  . MET B 143 ? 0.4556 0.5585 0.4861 0.0082  -0.0083 -0.0034 143  MET B CG  
3944  S  SD  . MET B 143 ? 0.5806 0.6636 0.6059 0.0109  0.0005  -0.0055 143  MET B SD  
3945  C  CE  . MET B 143 ? 0.3198 0.4084 0.3280 0.0119  0.0004  -0.0027 143  MET B CE  
3946  N  N   . ASN B 144 ? 0.4215 0.5594 0.4580 -0.0093 -0.0294 -0.0334 144  ASN B N   
3947  C  CA  . ASN B 144 ? 0.3652 0.5118 0.3859 -0.0122 -0.0340 -0.0445 144  ASN B CA  
3948  C  C   . ASN B 144 ? 0.4638 0.6232 0.4902 -0.0195 -0.0440 -0.0541 144  ASN B C   
3949  O  O   . ASN B 144 ? 0.5334 0.6863 0.5605 -0.0242 -0.0450 -0.0689 144  ASN B O   
3950  C  CB  . ASN B 144 ? 0.3280 0.4593 0.3411 -0.0111 -0.0269 -0.0551 144  ASN B CB  
3951  C  CG  . ASN B 144 ? 0.4852 0.6255 0.4797 -0.0121 -0.0292 -0.0661 144  ASN B CG  
3952  O  OD1 . ASN B 144 ? 0.5318 0.6901 0.5160 -0.0138 -0.0361 -0.0647 144  ASN B OD1 
3953  N  ND2 . ASN B 144 ? 0.5558 0.6845 0.5452 -0.0106 -0.0233 -0.0769 144  ASN B ND2 
3954  N  N   . PRO B 145 ? 0.3950 0.5727 0.4259 -0.0204 -0.0522 -0.0457 145  PRO B N   
3955  C  CA  . PRO B 145 ? 0.3454 0.5392 0.3837 -0.0277 -0.0637 -0.0528 145  PRO B CA  
3956  C  C   . PRO B 145 ? 0.3972 0.5976 0.4156 -0.0318 -0.0693 -0.0682 145  PRO B C   
3957  O  O   . PRO B 145 ? 0.4876 0.6923 0.5105 -0.0393 -0.0770 -0.0814 145  PRO B O   
3958  C  CB  . PRO B 145 ? 0.2505 0.4643 0.2922 -0.0248 -0.0706 -0.0375 145  PRO B CB  
3959  C  CG  . PRO B 145 ? 0.3051 0.5089 0.3453 -0.0161 -0.0615 -0.0225 145  PRO B CG  
3960  C  CD  . PRO B 145 ? 0.3340 0.5188 0.3611 -0.0140 -0.0516 -0.0287 145  PRO B CD  
3961  N  N   . ASP B 146 ? 0.4681 0.6700 0.4644 -0.0269 -0.0655 -0.0664 146  ASP B N   
3962  C  CA  . ASP B 146 ? 0.4682 0.6793 0.4422 -0.0293 -0.0698 -0.0798 146  ASP B CA  
3963  C  C   . ASP B 146 ? 0.4678 0.6604 0.4407 -0.0310 -0.0639 -0.0980 146  ASP B C   
3964  O  O   . ASP B 146 ? 0.5401 0.7351 0.5070 -0.0364 -0.0699 -0.1153 146  ASP B O   
3965  C  CB  . ASP B 146 ? 0.5613 0.7815 0.5133 -0.0236 -0.0664 -0.0700 146  ASP B CB  
3966  C  CG  . ASP B 146 ? 0.5131 0.7518 0.4648 -0.0220 -0.0739 -0.0522 146  ASP B CG  
3967  O  OD1 . ASP B 146 ? 0.3917 0.6362 0.3623 -0.0241 -0.0808 -0.0470 146  ASP B OD1 
3968  O  OD2 . ASP B 146 ? 0.5120 0.7600 0.4457 -0.0184 -0.0727 -0.0427 146  ASP B OD2 
3969  N  N   . GLY B 147 ? 0.3639 0.5375 0.3430 -0.0261 -0.0526 -0.0942 147  GLY B N   
3970  C  CA  . GLY B 147 ? 0.3383 0.4924 0.3199 -0.0263 -0.0464 -0.1088 147  GLY B CA  
3971  C  C   . GLY B 147 ? 0.4543 0.6005 0.4545 -0.0339 -0.0519 -0.1185 147  GLY B C   
3972  O  O   . GLY B 147 ? 0.3717 0.5105 0.3690 -0.0378 -0.0541 -0.1366 147  GLY B O   
3973  N  N   . TYR B 148 ? 0.4603 0.6079 0.4805 -0.0361 -0.0538 -0.1064 148  TYR B N   
3974  C  CA  . TYR B 148 ? 0.5599 0.7036 0.6011 -0.0445 -0.0592 -0.1124 148  TYR B CA  
3975  C  C   . TYR B 148 ? 0.6331 0.7908 0.6685 -0.0527 -0.0718 -0.1270 148  TYR B C   
3976  O  O   . TYR B 148 ? 0.6264 0.7730 0.6653 -0.0588 -0.0744 -0.1437 148  TYR B O   
3977  C  CB  . TYR B 148 ? 0.4862 0.6368 0.5484 -0.0449 -0.0596 -0.0955 148  TYR B CB  
3978  C  CG  . TYR B 148 ? 0.4022 0.5537 0.4883 -0.0545 -0.0654 -0.0997 148  TYR B CG  
3979  C  CD1 . TYR B 148 ? 0.5068 0.6370 0.6057 -0.0585 -0.0604 -0.1068 148  TYR B CD1 
3980  C  CD2 . TYR B 148 ? 0.2711 0.4453 0.3684 -0.0598 -0.0761 -0.0955 148  TYR B CD2 
3981  C  CE1 . TYR B 148 ? 0.4181 0.5489 0.5404 -0.0684 -0.0652 -0.1096 148  TYR B CE1 
3982  C  CE2 . TYR B 148 ? 0.2762 0.4532 0.3978 -0.0697 -0.0815 -0.0989 148  TYR B CE2 
3983  C  CZ  . TYR B 148 ? 0.4893 0.6443 0.6235 -0.0744 -0.0757 -0.1059 148  TYR B CZ  
3984  O  OH  . TYR B 148 ? 0.6475 0.8054 0.8074 -0.0853 -0.0808 -0.1081 148  TYR B OH  
3985  N  N   . ALA B 149 ? 0.5420 0.7237 0.5683 -0.0528 -0.0802 -0.1209 149  ALA B N   
3986  C  CA  . ALA B 149 ? 0.4940 0.6919 0.5144 -0.0609 -0.0939 -0.1337 149  ALA B CA  
3987  C  C   . ALA B 149 ? 0.4688 0.6558 0.4706 -0.0627 -0.0935 -0.1563 149  ALA B C   
3988  O  O   . ALA B 149 ? 0.4952 0.6836 0.4985 -0.0715 -0.1031 -0.1728 149  ALA B O   
3989  C  CB  . ALA B 149 ? 0.2952 0.5204 0.3021 -0.0585 -0.1022 -0.1228 149  ALA B CB  
3990  N  N   . LEU B 150 ? 0.5770 0.7529 0.5623 -0.0543 -0.0824 -0.1577 150  LEU B N   
3991  C  CA  . LEU B 150 ? 0.6068 0.7745 0.5730 -0.0537 -0.0807 -0.1788 150  LEU B CA  
3992  C  C   . LEU B 150 ? 0.7531 0.8924 0.7335 -0.0552 -0.0747 -0.1914 150  LEU B C   
3993  O  O   . LEU B 150 ? 0.8060 0.9352 0.7749 -0.0553 -0.0740 -0.2113 150  LEU B O   
3994  C  CB  . LEU B 150 ? 0.5072 0.6797 0.4496 -0.0439 -0.0714 -0.1745 150  LEU B CB  
3995  C  CG  . LEU B 150 ? 0.6437 0.8438 0.5668 -0.0429 -0.0778 -0.1649 150  LEU B CG  
3996  C  CD1 . LEU B 150 ? 0.6204 0.8238 0.5344 -0.0339 -0.0673 -0.1476 150  LEU B CD1 
3997  C  CD2 . LEU B 150 ? 0.6411 0.8534 0.5386 -0.0457 -0.0846 -0.1843 150  LEU B CD2 
3998  N  N   . SER B 151 ? 0.6901 0.8162 0.6951 -0.0558 -0.0701 -0.1795 151  SER B N   
3999  C  CA  . SER B 151 ? 0.5881 0.6865 0.6080 -0.0571 -0.0645 -0.1884 151  SER B CA  
4000  C  C   . SER B 151 ? 0.6853 0.7781 0.7222 -0.0697 -0.0744 -0.2006 151  SER B C   
4001  O  O   . SER B 151 ? 0.6442 0.7563 0.6864 -0.0776 -0.0857 -0.1991 151  SER B O   
4002  C  CB  . SER B 151 ? 0.4670 0.5523 0.5026 -0.0517 -0.0540 -0.1704 151  SER B CB  
4003  O  OG  . SER B 151 ? 0.4830 0.5718 0.5040 -0.0412 -0.0454 -0.1606 151  SER B OG  
4004  N  N   . GLN B 152 ? 0.6164 0.6828 0.6630 -0.0715 -0.0706 -0.2124 152  GLN B N   
4005  C  CA  . GLN B 152 ? 0.5615 0.6185 0.6240 -0.0842 -0.0796 -0.2261 152  GLN B CA  
4006  C  C   . GLN B 152 ? 0.7150 0.7519 0.8069 -0.0884 -0.0746 -0.2164 152  GLN B C   
4007  O  O   . GLN B 152 ? 0.8071 0.8195 0.9022 -0.0824 -0.0646 -0.2164 152  GLN B O   
4008  C  CB  . GLN B 152 ? 0.7641 0.8050 0.8119 -0.0844 -0.0812 -0.2524 152  GLN B CB  
4009  C  CG  . GLN B 152 ? 0.8514 0.8769 0.9163 -0.0978 -0.0901 -0.2685 152  GLN B CG  
4010  C  CD  . GLN B 152 ? 0.9716 0.9767 1.0221 -0.0965 -0.0903 -0.2952 152  GLN B CD  
4011  O  OE1 . GLN B 152 ? 1.1291 1.1127 1.1937 -0.1055 -0.0949 -0.3096 152  GLN B OE1 
4012  N  NE2 . GLN B 152 ? 0.9467 0.9582 0.9695 -0.0851 -0.0848 -0.3023 152  GLN B NE2 
4013  N  N   . GLU B 153 ? 0.5611 0.6096 0.6748 -0.0985 -0.0813 -0.2075 153  GLU B N   
4014  C  CA  . GLU B 153 ? 0.5830 0.6148 0.7248 -0.1037 -0.0763 -0.1974 153  GLU B CA  
4015  C  C   . GLU B 153 ? 0.6546 0.6544 0.8019 -0.1075 -0.0746 -0.2138 153  GLU B C   
4016  O  O   . GLU B 153 ? 0.6000 0.5953 0.7408 -0.1140 -0.0834 -0.2351 153  GLU B O   
4017  C  CB  . GLU B 153 ? 0.5694 0.6201 0.7355 -0.1162 -0.0851 -0.1897 153  GLU B CB  
4018  C  CG  . GLU B 153 ? 0.5959 0.6325 0.7919 -0.1219 -0.0786 -0.1769 153  GLU B CG  
4019  C  CD  . GLU B 153 ? 0.6396 0.6984 0.8619 -0.1341 -0.0866 -0.1688 153  GLU B CD  
4020  O  OE1 . GLU B 153 ? 0.6199 0.6673 0.8682 -0.1449 -0.0862 -0.1672 153  GLU B OE1 
4021  O  OE2 . GLU B 153 ? 0.6295 0.7178 0.8475 -0.1329 -0.0933 -0.1633 153  GLU B OE2 
4022  N  N   . GLY B 154 ? 0.7169 0.6940 0.8754 -0.1028 -0.0635 -0.2039 154  GLY B N   
4023  C  CA  . GLY B 154 ? 0.7021 0.6462 0.8676 -0.1047 -0.0608 -0.2163 154  GLY B CA  
4024  C  C   . GLY B 154 ? 0.6925 0.6196 0.8408 -0.0896 -0.0505 -0.2188 154  GLY B C   
4025  O  O   . GLY B 154 ? 0.8145 0.7137 0.9721 -0.0870 -0.0442 -0.2193 154  GLY B O   
4026  N  N   . ASN B 155 ? 0.5959 0.5408 0.7204 -0.0796 -0.0488 -0.2194 155  ASN B N   
4027  C  CA  . ASN B 155 ? 0.5147 0.4476 0.6234 -0.0656 -0.0396 -0.2232 155  ASN B CA  
4028  C  C   . ASN B 155 ? 0.7286 0.6520 0.8448 -0.0568 -0.0285 -0.2028 155  ASN B C   
4029  O  O   . ASN B 155 ? 0.9285 0.8697 1.0393 -0.0518 -0.0250 -0.1864 155  ASN B O   
4030  C  CB  . ASN B 155 ? 0.3914 0.3478 0.4733 -0.0585 -0.0406 -0.2287 155  ASN B CB  
4031  C  CG  . ASN B 155 ? 0.6302 0.5829 0.6967 -0.0595 -0.0458 -0.2548 155  ASN B CG  
4032  O  OD1 . ASN B 155 ? 0.7659 0.7408 0.8131 -0.0600 -0.0514 -0.2620 155  ASN B OD1 
4033  N  ND2 . ASN B 155 ? 0.8430 0.7666 0.9172 -0.0596 -0.0440 -0.2693 155  ASN B ND2 
4034  N  N   . CYS B 156 ? 0.6801 0.5749 0.8085 -0.0549 -0.0233 -0.2039 156  CYS B N   
4035  C  CA  . CYS B 156 ? 0.8038 0.6888 0.9370 -0.0458 -0.0134 -0.1857 156  CYS B CA  
4036  C  C   . CYS B 156 ? 0.7844 0.6771 0.8977 -0.0315 -0.0074 -0.1862 156  CYS B C   
4037  O  O   . CYS B 156 ? 0.7838 0.6833 0.8944 -0.0244 -0.0014 -0.1695 156  CYS B O   
4038  C  CB  . CYS B 156 ? 0.8777 0.7299 1.0283 -0.0469 -0.0101 -0.1863 156  CYS B CB  
4039  S  SG  . CYS B 156 ? 0.8786 0.7240 1.0567 -0.0621 -0.0124 -0.1726 156  CYS B SG  
4040  N  N   . GLU B 157 ? 0.7950 0.6875 0.8946 -0.0277 -0.0089 -0.2058 157  GLU B N   
4041  C  CA  . GLU B 157 ? 0.7251 0.6293 0.8062 -0.0153 -0.0033 -0.2074 157  GLU B CA  
4042  C  C   . GLU B 157 ? 0.6935 0.6262 0.7561 -0.0178 -0.0083 -0.2123 157  GLU B C   
4043  O  O   . GLU B 157 ? 0.7460 0.6849 0.8073 -0.0275 -0.0169 -0.2229 157  GLU B O   
4044  C  CB  . GLU B 157 ? 0.8762 0.7612 0.9542 -0.0069 0.0007  -0.2250 157  GLU B CB  
4045  C  CG  . GLU B 157 ? 1.1145 0.9726 1.2088 -0.0006 0.0069  -0.2173 157  GLU B CG  
4046  C  CD  . GLU B 157 ? 1.2942 1.1229 1.4047 -0.0077 0.0034  -0.2283 157  GLU B CD  
4047  O  OE1 . GLU B 157 ? 1.3785 1.1908 1.4866 -0.0026 0.0043  -0.2475 157  GLU B OE1 
4048  O  OE2 . GLU B 157 ? 1.2657 1.0874 1.3919 -0.0182 0.0001  -0.2178 157  GLU B OE2 
4049  N  N   . SER B 158 ? 0.7070 0.6575 0.7558 -0.0094 -0.0034 -0.2039 158  SER B N   
4050  C  CA  . SER B 158 ? 0.6450 0.6229 0.6754 -0.0110 -0.0074 -0.2053 158  SER B CA  
4051  C  C   . SER B 158 ? 0.6334 0.6141 0.6484 -0.0114 -0.0108 -0.2292 158  SER B C   
4052  O  O   . SER B 158 ? 0.7292 0.6890 0.7484 -0.0096 -0.0093 -0.2450 158  SER B O   
4053  C  CB  . SER B 158 ? 0.6197 0.6128 0.6398 -0.0019 -0.0004 -0.1914 158  SER B CB  
4054  O  OG  . SER B 158 ? 0.7837 0.8027 0.7880 -0.0042 -0.0043 -0.1886 158  SER B OG  
4055  N  N   . LEU B 159 ? 0.4909 0.4964 0.4874 -0.0135 -0.0153 -0.2318 159  LEU B N   
4056  C  CA  . LEU B 159 ? 0.6141 0.6247 0.5925 -0.0144 -0.0190 -0.2548 159  LEU B CA  
4057  C  C   . LEU B 159 ? 0.6936 0.7097 0.6551 -0.0020 -0.0090 -0.2615 159  LEU B C   
4058  O  O   . LEU B 159 ? 0.5686 0.5960 0.5275 0.0049  -0.0019 -0.2459 159  LEU B O   
4059  C  CB  . LEU B 159 ? 0.7612 0.7974 0.7262 -0.0228 -0.0295 -0.2547 159  LEU B CB  
4060  C  CG  . LEU B 159 ? 0.7247 0.7615 0.7039 -0.0362 -0.0418 -0.2540 159  LEU B CG  
4061  C  CD1 . LEU B 159 ? 0.5101 0.5760 0.4825 -0.0405 -0.0490 -0.2394 159  LEU B CD1 
4062  C  CD2 . LEU B 159 ? 0.5755 0.6022 0.5514 -0.0437 -0.0501 -0.2798 159  LEU B CD2 
4063  N  N   . PRO B 160 ? 0.6595 0.6680 0.6101 0.0007  -0.0084 -0.2854 160  PRO B N   
4064  C  CA  . PRO B 160 ? 0.5979 0.6161 0.5313 0.0127  0.0017  -0.2929 160  PRO B CA  
4065  C  C   . PRO B 160 ? 0.7371 0.7869 0.6543 0.0135  0.0030  -0.2772 160  PRO B C   
4066  O  O   . PRO B 160 ? 1.0317 1.0980 0.9380 0.0051  -0.0061 -0.2756 160  PRO B O   
4067  C  CB  . PRO B 160 ? 0.5183 0.5336 0.4350 0.0111  -0.0023 -0.3213 160  PRO B CB  
4068  C  CG  . PRO B 160 ? 0.4595 0.4505 0.3932 0.0007  -0.0119 -0.3304 160  PRO B CG  
4069  C  CD  . PRO B 160 ? 0.5325 0.5287 0.4828 -0.0081 -0.0178 -0.3069 160  PRO B CD  
4070  N  N   . ASN B 161 ? 0.8990 0.9570 0.8158 0.0229  0.0135  -0.2653 161  ASN B N   
4071  C  CA  . ASN B 161 ? 1.1092 1.1948 1.0133 0.0233  0.0154  -0.2482 161  ASN B CA  
4072  C  C   . ASN B 161 ? 1.0525 1.1380 0.9718 0.0186  0.0121  -0.2241 161  ASN B C   
4073  O  O   . ASN B 161 ? 1.1349 1.2386 1.0481 0.0189  0.0138  -0.2074 161  ASN B O   
4074  C  CB  . ASN B 161 ? 1.2742 1.3815 1.1543 0.0173  0.0082  -0.2552 161  ASN B CB  
4075  C  CG  . ASN B 161 ? 1.3467 1.4558 1.2077 0.0217  0.0111  -0.2807 161  ASN B CG  
4076  O  OD1 . ASN B 161 ? 1.3142 1.4239 1.1635 0.0151  0.0020  -0.2967 161  ASN B OD1 
4077  N  ND2 . ASN B 161 ? 1.3717 1.4823 1.2296 0.0329  0.0238  -0.2851 161  ASN B ND2 
4078  N  N   . TYR B 162 ? 1.0561 1.1205 0.9950 0.0140  0.0075  -0.2227 162  TYR B N   
4079  C  CA  . TYR B 162 ? 1.0814 1.1441 1.0352 0.0096  0.0046  -0.2018 162  TYR B CA  
4080  C  C   . TYR B 162 ? 0.9354 1.0177 0.8810 0.0017  -0.0042 -0.1935 162  TYR B C   
4081  O  O   . TYR B 162 ? 0.8454 0.9342 0.7969 0.0002  -0.0051 -0.1744 162  TYR B O   
4082  C  CB  . TYR B 162 ? 1.0095 1.0740 0.9681 0.0171  0.0134  -0.1853 162  TYR B CB  
4083  C  CG  . TYR B 162 ? 0.8614 0.9058 0.8326 0.0248  0.0205  -0.1905 162  TYR B CG  
4084  C  CD1 . TYR B 162 ? 0.7897 0.8369 0.7538 0.0339  0.0282  -0.2018 162  TYR B CD1 
4085  C  CD2 . TYR B 162 ? 0.6944 0.7178 0.6850 0.0234  0.0196  -0.1836 162  TYR B CD2 
4086  C  CE1 . TYR B 162 ? 0.7848 0.8139 0.7622 0.0419  0.0342  -0.2058 162  TYR B CE1 
4087  C  CE2 . TYR B 162 ? 0.7460 0.7507 0.7481 0.0309  0.0253  -0.1867 162  TYR B CE2 
4088  C  CZ  . TYR B 162 ? 0.7719 0.7793 0.7681 0.0403  0.0322  -0.1978 162  TYR B CZ  
4089  O  OH  . TYR B 162 ? 0.8834 0.8727 0.8929 0.0487  0.0375  -0.2001 162  TYR B OH  
4090  N  N   . VAL B 163 ? 0.7675 0.8587 0.6992 -0.0030 -0.0111 -0.2086 163  VAL B N   
4091  C  CA  . VAL B 163 ? 0.7476 0.8582 0.6717 -0.0105 -0.0211 -0.2026 163  VAL B CA  
4092  C  C   . VAL B 163 ? 0.7705 0.8726 0.7172 -0.0175 -0.0274 -0.1918 163  VAL B C   
4093  O  O   . VAL B 163 ? 0.7875 0.8692 0.7508 -0.0205 -0.0282 -0.1990 163  VAL B O   
4094  C  CB  . VAL B 163 ? 0.5619 0.6803 0.4687 -0.0150 -0.0288 -0.2240 163  VAL B CB  
4095  C  CG1 . VAL B 163 ? 0.5203 0.6524 0.4283 -0.0249 -0.0424 -0.2198 163  VAL B CG1 
4096  C  CG2 . VAL B 163 ? 0.4336 0.5700 0.3134 -0.0085 -0.0230 -0.2295 163  VAL B CG2 
4097  N  N   . GLY B 164 ? 0.6240 0.7414 0.5721 -0.0196 -0.0312 -0.1737 164  GLY B N   
4098  C  CA  . GLY B 164 ? 0.4352 0.5479 0.4047 -0.0251 -0.0360 -0.1622 164  GLY B CA  
4099  C  C   . GLY B 164 ? 0.4120 0.5143 0.3940 -0.0197 -0.0274 -0.1450 164  GLY B C   
4100  O  O   . GLY B 164 ? 0.5157 0.6210 0.5098 -0.0218 -0.0295 -0.1305 164  GLY B O   
4101  N  N   . ARG B 165 ? 0.5164 0.6071 0.4953 -0.0125 -0.0178 -0.1472 165  ARG B N   
4102  C  CA  . ARG B 165 ? 0.5375 0.6190 0.5256 -0.0071 -0.0101 -0.1320 165  ARG B CA  
4103  C  C   . ARG B 165 ? 0.4560 0.5540 0.4340 -0.0042 -0.0088 -0.1165 165  ARG B C   
4104  O  O   . ARG B 165 ? 0.4482 0.5466 0.4346 -0.0047 -0.0093 -0.1015 165  ARG B O   
4105  C  CB  . ARG B 165 ? 0.5009 0.5672 0.4897 -0.0002 -0.0015 -0.1392 165  ARG B CB  
4106  C  CG  . ARG B 165 ? 0.5400 0.5974 0.5374 0.0052  0.0053  -0.1242 165  ARG B CG  
4107  C  CD  . ARG B 165 ? 0.4678 0.5118 0.4680 0.0124  0.0126  -0.1310 165  ARG B CD  
4108  N  NE  . ARG B 165 ? 0.3805 0.4255 0.3813 0.0185  0.0187  -0.1182 165  ARG B NE  
4109  C  CZ  . ARG B 165 ? 0.4526 0.4843 0.4649 0.0203  0.0210  -0.1079 165  ARG B CZ  
4110  N  NH1 . ARG B 165 ? 0.4385 0.4550 0.4631 0.0167  0.0188  -0.1073 165  ARG B NH1 
4111  N  NH2 . ARG B 165 ? 0.3825 0.4171 0.3939 0.0252  0.0253  -0.0977 165  ARG B NH2 
4112  N  N   . GLY B 166 ? 0.3109 0.4224 0.2710 -0.0013 -0.0068 -0.1203 166  GLY B N   
4113  C  CA  . GLY B 166 ? 0.4237 0.5509 0.3736 0.0005  -0.0058 -0.1057 166  GLY B CA  
4114  C  C   . GLY B 166 ? 0.4712 0.6133 0.4176 -0.0047 -0.0153 -0.0998 166  GLY B C   
4115  O  O   . GLY B 166 ? 0.6282 0.7702 0.5801 -0.0099 -0.0227 -0.1083 166  GLY B O   
4116  N  N   . ASN B 167 ? 0.3810 0.5362 0.3198 -0.0035 -0.0156 -0.0848 167  ASN B N   
4117  C  CA  . ASN B 167 ? 0.4559 0.6267 0.3909 -0.0073 -0.0251 -0.0783 167  ASN B CA  
4118  C  C   . ASN B 167 ? 0.4982 0.6858 0.4138 -0.0098 -0.0305 -0.0906 167  ASN B C   
4119  O  O   . ASN B 167 ? 0.4884 0.6713 0.3981 -0.0099 -0.0282 -0.1083 167  ASN B O   
4120  C  CB  . ASN B 167 ? 0.3399 0.5171 0.2744 -0.0049 -0.0245 -0.0574 167  ASN B CB  
4121  C  CG  . ASN B 167 ? 0.3179 0.5055 0.2345 -0.0023 -0.0194 -0.0519 167  ASN B CG  
4122  O  OD1 . ASN B 167 ? 0.4063 0.5984 0.3106 -0.0014 -0.0153 -0.0636 167  ASN B OD1 
4123  N  ND2 . ASN B 167 ? 0.2372 0.4288 0.1530 -0.0009 -0.0191 -0.0337 167  ASN B ND2 
4124  N  N   . ALA B 168 ? 0.5344 0.7409 0.4396 -0.0116 -0.0378 -0.0816 168  ALA B N   
4125  C  CA  . ALA B 168 ? 0.6921 0.9165 0.5763 -0.0143 -0.0441 -0.0924 168  ALA B CA  
4126  C  C   . ALA B 168 ? 0.8060 1.0390 0.6681 -0.0103 -0.0357 -0.0947 168  ALA B C   
4127  O  O   . ALA B 168 ? 0.8733 1.1180 0.7158 -0.0114 -0.0378 -0.1084 168  ALA B O   
4128  C  CB  . ALA B 168 ? 0.7221 0.9655 0.6029 -0.0171 -0.0557 -0.0804 168  ALA B CB  
4129  N  N   . ALA B 169 ? 0.6870 0.9151 0.5523 -0.0060 -0.0261 -0.0814 169  ALA B N   
4130  C  CA  . ALA B 169 ? 0.5334 0.7707 0.3816 -0.0024 -0.0167 -0.0818 169  ALA B CA  
4131  C  C   . ALA B 169 ? 0.4858 0.7091 0.3396 0.0012  -0.0075 -0.0974 169  ALA B C   
4132  O  O   . ALA B 169 ? 0.4747 0.7052 0.3177 0.0049  0.0016  -0.1004 169  ALA B O   
4133  C  CB  . ALA B 169 ? 0.2932 0.5334 0.1431 -0.0007 -0.0118 -0.0595 169  ALA B CB  
4134  N  N   . ASN B 170 ? 0.5027 0.7068 0.3748 0.0003  -0.0096 -0.1060 170  ASN B N   
4135  C  CA  . ASN B 170 ? 0.6780 0.8655 0.5588 0.0041  -0.0021 -0.1199 170  ASN B CA  
4136  C  C   . ASN B 170 ? 0.6514 0.8304 0.5432 0.0089  0.0076  -0.1091 170  ASN B C   
4137  O  O   . ASN B 170 ? 0.7493 0.9224 0.6430 0.0139  0.0155  -0.1184 170  ASN B O   
4138  C  CB  . ASN B 170 ? 0.8760 1.0709 0.7391 0.0065  0.0013  -0.1397 170  ASN B CB  
4139  C  CG  . ASN B 170 ? 0.9868 1.1737 0.8503 0.0025  -0.0066 -0.1595 170  ASN B CG  
4140  O  OD1 . ASN B 170 ? 0.9738 1.1744 0.8189 -0.0004 -0.0126 -0.1696 170  ASN B OD1 
4141  N  ND2 . ASN B 170 ? 1.0440 1.2084 0.9281 0.0018  -0.0072 -0.1647 170  ASN B ND2 
4142  N  N   . ILE B 171 ? 0.5360 0.7143 0.4355 0.0078  0.0065  -0.0900 171  ILE B N   
4143  C  CA  . ILE B 171 ? 0.5695 0.7378 0.4808 0.0113  0.0138  -0.0804 171  ILE B CA  
4144  C  C   . ILE B 171 ? 0.4440 0.5922 0.3745 0.0106  0.0112  -0.0774 171  ILE B C   
4145  O  O   . ILE B 171 ? 0.3971 0.5431 0.3327 0.0069  0.0040  -0.0741 171  ILE B O   
4146  C  CB  . ILE B 171 ? 0.5652 0.7449 0.4712 0.0107  0.0161  -0.0616 171  ILE B CB  
4147  C  CG1 . ILE B 171 ? 0.3805 0.5534 0.2954 0.0080  0.0099  -0.0468 171  ILE B CG1 
4148  C  CG2 . ILE B 171 ? 0.5195 0.7220 0.4044 0.0098  0.0166  -0.0613 171  ILE B CG2 
4149  C  CD1 . ILE B 171 ? 0.5852 0.7410 0.5158 0.0098  0.0134  -0.0395 171  ILE B CD1 
4150  N  N   . ASP B 172 ? 0.5573 0.6922 0.4985 0.0143  0.0172  -0.0781 172  ASP B N   
4151  C  CA  . ASP B 172 ? 0.5423 0.6581 0.5000 0.0143  0.0160  -0.0753 172  ASP B CA  
4152  C  C   . ASP B 172 ? 0.5279 0.6412 0.4907 0.0134  0.0150  -0.0578 172  ASP B C   
4153  O  O   . ASP B 172 ? 0.5560 0.6689 0.5193 0.0155  0.0195  -0.0496 172  ASP B O   
4154  C  CB  . ASP B 172 ? 0.5536 0.6567 0.5197 0.0193  0.0223  -0.0820 172  ASP B CB  
4155  C  CG  . ASP B 172 ? 0.4452 0.5283 0.4265 0.0192  0.0211  -0.0802 172  ASP B CG  
4156  O  OD1 . ASP B 172 ? 0.4607 0.5406 0.4467 0.0165  0.0180  -0.0694 172  ASP B OD1 
4157  O  OD2 . ASP B 172 ? 0.5021 0.5728 0.4906 0.0223  0.0237  -0.0890 172  ASP B OD2 
4158  N  N   . LEU B 173 ? 0.4455 0.5571 0.4129 0.0102  0.0092  -0.0525 173  LEU B N   
4159  C  CA  . LEU B 173 ? 0.4241 0.5319 0.3963 0.0103  0.0084  -0.0372 173  LEU B CA  
4160  C  C   . LEU B 173 ? 0.4292 0.5210 0.4104 0.0131  0.0131  -0.0328 173  LEU B C   
4161  O  O   . LEU B 173 ? 0.4776 0.5656 0.4601 0.0137  0.0136  -0.0213 173  LEU B O   
4162  C  CB  . LEU B 173 ? 0.2546 0.3631 0.2335 0.0076  0.0021  -0.0339 173  LEU B CB  
4163  C  CG  . LEU B 173 ? 0.2127 0.3391 0.1824 0.0047  -0.0044 -0.0353 173  LEU B CG  
4164  C  CD1 . LEU B 173 ? 0.2825 0.4109 0.2625 0.0022  -0.0110 -0.0330 173  LEU B CD1 
4165  C  CD2 . LEU B 173 ? 0.4596 0.5967 0.4183 0.0056  -0.0041 -0.0231 173  LEU B CD2 
4166  N  N   . ASN B 174 ? 0.3312 0.4128 0.3182 0.0150  0.0161  -0.0418 174  ASN B N   
4167  C  CA  . ASN B 174 ? 0.2704 0.3381 0.2645 0.0180  0.0199  -0.0372 174  ASN B CA  
4168  C  C   . ASN B 174 ? 0.2569 0.3289 0.2474 0.0208  0.0242  -0.0363 174  ASN B C   
4169  O  O   . ASN B 174 ? 0.5171 0.5798 0.5132 0.0237  0.0268  -0.0348 174  ASN B O   
4170  C  CB  . ASN B 174 ? 0.3330 0.3861 0.3371 0.0190  0.0207  -0.0438 174  ASN B CB  
4171  C  CG  . ASN B 174 ? 0.3608 0.3999 0.3710 0.0211  0.0228  -0.0356 174  ASN B CG  
4172  O  OD1 . ASN B 174 ? 0.4569 0.4957 0.4652 0.0209  0.0224  -0.0260 174  ASN B OD1 
4173  N  ND2 . ASN B 174 ? 0.2844 0.3112 0.3013 0.0234  0.0250  -0.0396 174  ASN B ND2 
4174  N  N   . ARG B 175 ? 0.3431 0.4309 0.3246 0.0199  0.0250  -0.0365 175  ARG B N   
4175  C  CA  . ARG B 175 ? 0.3560 0.4517 0.3354 0.0214  0.0293  -0.0329 175  ARG B CA  
4176  C  C   . ARG B 175 ? 0.3335 0.4402 0.3055 0.0178  0.0281  -0.0216 175  ARG B C   
4177  O  O   . ARG B 175 ? 0.4988 0.6149 0.4689 0.0174  0.0315  -0.0168 175  ARG B O   
4178  C  CB  . ARG B 175 ? 0.2349 0.3415 0.2107 0.0244  0.0336  -0.0442 175  ARG B CB  
4179  C  CG  . ARG B 175 ? 0.3816 0.4777 0.3631 0.0280  0.0344  -0.0579 175  ARG B CG  
4180  C  CD  . ARG B 175 ? 0.3530 0.4374 0.3459 0.0327  0.0371  -0.0577 175  ARG B CD  
4181  N  NE  . ARG B 175 ? 0.5117 0.5778 0.5119 0.0321  0.0340  -0.0575 175  ARG B NE  
4182  C  CZ  . ARG B 175 ? 0.5903 0.6437 0.5972 0.0347  0.0344  -0.0662 175  ARG B CZ  
4183  N  NH1 . ARG B 175 ? 0.4709 0.5253 0.4793 0.0393  0.0377  -0.0777 175  ARG B NH1 
4184  N  NH2 . ARG B 175 ? 0.7549 0.7937 0.7679 0.0328  0.0318  -0.0627 175  ARG B NH2 
4185  N  N   . ASP B 176 ? 0.3930 0.4987 0.3622 0.0153  0.0234  -0.0165 176  ASP B N   
4186  C  CA  . ASP B 176 ? 0.4333 0.5503 0.3944 0.0124  0.0216  -0.0060 176  ASP B CA  
4187  C  C   . ASP B 176 ? 0.3574 0.4643 0.3227 0.0112  0.0202  0.0071  176  ASP B C   
4188  O  O   . ASP B 176 ? 0.3227 0.4359 0.2830 0.0088  0.0191  0.0177  176  ASP B O   
4189  C  CB  . ASP B 176 ? 0.4513 0.5765 0.4061 0.0109  0.0164  -0.0082 176  ASP B CB  
4190  C  CG  . ASP B 176 ? 0.5335 0.6745 0.4769 0.0085  0.0149  0.0013  176  ASP B CG  
4191  O  OD1 . ASP B 176 ? 0.5303 0.6803 0.4684 0.0077  0.0196  0.0054  176  ASP B OD1 
4192  O  OD2 . ASP B 176 ? 0.5416 0.6870 0.4822 0.0074  0.0091  0.0056  176  ASP B OD2 
4193  N  N   . PHE B 177 ? 0.2805 0.3713 0.2543 0.0130  0.0203  0.0066  177  PHE B N   
4194  C  CA  . PHE B 177 ? 0.3339 0.4128 0.3105 0.0124  0.0189  0.0168  177  PHE B CA  
4195  C  C   . PHE B 177 ? 0.3282 0.4067 0.3054 0.0104  0.0212  0.0220  177  PHE B C   
4196  O  O   . PHE B 177 ? 0.5620 0.6473 0.5405 0.0107  0.0244  0.0168  177  PHE B O   
4197  C  CB  . PHE B 177 ? 0.4392 0.5020 0.4227 0.0151  0.0182  0.0142  177  PHE B CB  
4198  C  CG  . PHE B 177 ? 0.4403 0.5037 0.4260 0.0160  0.0153  0.0134  177  PHE B CG  
4199  C  CD1 . PHE B 177 ? 0.4986 0.5691 0.4853 0.0156  0.0144  0.0043  177  PHE B CD1 
4200  C  CD2 . PHE B 177 ? 0.4390 0.4964 0.4270 0.0171  0.0132  0.0215  177  PHE B CD2 
4201  C  CE1 . PHE B 177 ? 0.5017 0.5750 0.4926 0.0153  0.0109  0.0038  177  PHE B CE1 
4202  C  CE2 . PHE B 177 ? 0.5243 0.5852 0.5169 0.0181  0.0104  0.0215  177  PHE B CE2 
4203  C  CZ  . PHE B 177 ? 0.5425 0.6123 0.5370 0.0167  0.0090  0.0128  177  PHE B CZ  
4204  N  N   . PRO B 178 ? 0.3406 0.4115 0.3178 0.0082  0.0195  0.0322  178  PRO B N   
4205  C  CA  . PRO B 178 ? 0.3842 0.4546 0.3634 0.0047  0.0208  0.0372  178  PRO B CA  
4206  C  C   . PRO B 178 ? 0.4094 0.4716 0.3942 0.0065  0.0216  0.0309  178  PRO B C   
4207  O  O   . PRO B 178 ? 0.3313 0.3799 0.3175 0.0097  0.0204  0.0274  178  PRO B O   
4208  C  CB  . PRO B 178 ? 0.3425 0.4003 0.3214 0.0026  0.0178  0.0476  178  PRO B CB  
4209  C  CG  . PRO B 178 ? 0.2475 0.3083 0.2228 0.0047  0.0157  0.0509  178  PRO B CG  
4210  C  CD  . PRO B 178 ? 0.2695 0.3340 0.2455 0.0086  0.0161  0.0400  178  PRO B CD  
4211  N  N   . ASP B 179 ? 0.4279 0.5001 0.4163 0.0047  0.0238  0.0301  179  ASP B N   
4212  C  CA  . ASP B 179 ? 0.5066 0.5739 0.5008 0.0071  0.0240  0.0245  179  ASP B CA  
4213  C  C   . ASP B 179 ? 0.4963 0.5542 0.4932 0.0031  0.0208  0.0303  179  ASP B C   
4214  O  O   . ASP B 179 ? 0.5591 0.6215 0.5569 -0.0026 0.0203  0.0379  179  ASP B O   
4215  C  CB  . ASP B 179 ? 0.5228 0.6074 0.5214 0.0087  0.0280  0.0194  179  ASP B CB  
4216  C  CG  . ASP B 179 ? 0.6127 0.6926 0.6180 0.0131  0.0278  0.0133  179  ASP B CG  
4217  O  OD1 . ASP B 179 ? 0.6627 0.7283 0.6669 0.0167  0.0261  0.0096  179  ASP B OD1 
4218  O  OD2 . ASP B 179 ? 0.7042 0.7960 0.7168 0.0133  0.0295  0.0131  179  ASP B OD2 
4219  N  N   . ARG B 180 ? 0.3829 0.4274 0.3806 0.0057  0.0185  0.0269  180  ARG B N   
4220  C  CA  . ARG B 180 ? 0.5806 0.6154 0.5794 0.0019  0.0145  0.0303  180  ARG B CA  
4221  C  C   . ARG B 180 ? 0.5962 0.6463 0.6035 -0.0023 0.0143  0.0323  180  ARG B C   
4222  O  O   . ARG B 180 ? 0.5906 0.6389 0.6005 -0.0089 0.0112  0.0377  180  ARG B O   
4223  C  CB  . ARG B 180 ? 0.6396 0.6596 0.6354 0.0064  0.0124  0.0255  180  ARG B CB  
4224  C  CG  . ARG B 180 ? 0.6130 0.6402 0.6132 0.0115  0.0142  0.0198  180  ARG B CG  
4225  C  CD  . ARG B 180 ? 0.6426 0.6553 0.6385 0.0162  0.0131  0.0168  180  ARG B CD  
4226  N  NE  . ARG B 180 ? 0.6816 0.7000 0.6830 0.0207  0.0137  0.0132  180  ARG B NE  
4227  C  CZ  . ARG B 180 ? 0.5176 0.5390 0.5226 0.0206  0.0101  0.0141  180  ARG B CZ  
4228  N  NH1 . ARG B 180 ? 0.3356 0.3543 0.3386 0.0153  0.0054  0.0173  180  ARG B NH1 
4229  N  NH2 . ARG B 180 ? 0.2775 0.3040 0.2887 0.0258  0.0106  0.0117  180  ARG B NH2 
4230  N  N   . LEU B 181 ? 0.5652 0.6306 0.5780 0.0014  0.0177  0.0279  181  LEU B N   
4231  C  CA  . LEU B 181 ? 0.4699 0.5527 0.4934 -0.0011 0.0182  0.0295  181  LEU B CA  
4232  C  C   . LEU B 181 ? 0.6368 0.7370 0.6637 -0.0073 0.0217  0.0362  181  LEU B C   
4233  O  O   . LEU B 181 ? 0.5928 0.7075 0.6301 -0.0116 0.0219  0.0399  181  LEU B O   
4234  C  CB  . LEU B 181 ? 0.2324 0.3253 0.2621 0.0064  0.0212  0.0225  181  LEU B CB  
4235  C  CG  . LEU B 181 ? 0.2953 0.3732 0.3235 0.0122  0.0177  0.0179  181  LEU B CG  
4236  C  CD1 . LEU B 181 ? 0.3784 0.4669 0.4157 0.0194  0.0202  0.0128  181  LEU B CD1 
4237  C  CD2 . LEU B 181 ? 0.1458 0.2140 0.1738 0.0080  0.0108  0.0216  181  LEU B CD2 
4238  N  N   . GLU B 182 ? 0.4214 0.5216 0.4401 -0.0079 0.0245  0.0387  182  GLU B N   
4239  C  CA  . GLU B 182 ? 0.4755 0.5892 0.4949 -0.0145 0.0273  0.0475  182  GLU B CA  
4240  C  C   . GLU B 182 ? 0.6460 0.7454 0.6563 -0.0173 0.0249  0.0540  182  GLU B C   
4241  O  O   . GLU B 182 ? 0.9275 1.0221 0.9294 -0.0126 0.0254  0.0509  182  GLU B O   
4242  C  CB  . GLU B 182 ? 0.7720 0.9083 0.7905 -0.0113 0.0345  0.0446  182  GLU B CB  
4243  C  CG  . GLU B 182 ? 1.0278 1.1795 1.0572 -0.0072 0.0378  0.0385  182  GLU B CG  
4244  C  CD  . GLU B 182 ? 1.2111 1.3679 1.2364 0.0019  0.0422  0.0273  182  GLU B CD  
4245  O  OE1 . GLU B 182 ? 1.2753 1.4394 1.2908 0.0026  0.0460  0.0261  182  GLU B OE1 
4246  O  OE2 . GLU B 182 ? 1.1729 1.3258 1.2044 0.0081  0.0415  0.0198  182  GLU B OE2 
4247  N  N   . GLN B 183 ? 0.5482 0.6408 0.5614 -0.0250 0.0219  0.0631  183  GLN B N   
4248  C  CA  . GLN B 183 ? 0.8729 0.9489 0.8791 -0.0267 0.0192  0.0696  183  GLN B CA  
4249  C  C   . GLN B 183 ? 0.8394 0.9211 0.8486 -0.0357 0.0199  0.0829  183  GLN B C   
4250  O  O   . GLN B 183 ? 0.8220 0.9049 0.8404 -0.0433 0.0184  0.0872  183  GLN B O   
4251  C  CB  . GLN B 183 ? 1.0178 1.0685 1.0228 -0.0254 0.0135  0.0657  183  GLN B CB  
4252  C  CG  . GLN B 183 ? 0.9635 0.9979 0.9603 -0.0201 0.0123  0.0653  183  GLN B CG  
4253  C  CD  . GLN B 183 ? 1.0270 1.0457 1.0229 -0.0246 0.0094  0.0747  183  GLN B CD  
4254  O  OE1 . GLN B 183 ? 0.8837 0.8882 0.8828 -0.0294 0.0057  0.0756  183  GLN B OE1 
4255  N  NE2 . GLN B 183 ? 1.1528 1.1735 1.1446 -0.0229 0.0105  0.0816  183  GLN B NE2 
4256  N  N   . SER B 184 ? 0.4739 0.5598 0.4756 -0.0352 0.0219  0.0901  184  SER B N   
4257  C  CA  . SER B 184 ? 0.7891 0.8828 0.7922 -0.0432 0.0237  0.1045  184  SER B CA  
4258  C  C   . SER B 184 ? 0.8446 0.9141 0.8474 -0.0469 0.0186  0.1139  184  SER B C   
4259  O  O   . SER B 184 ? 0.9327 1.0039 0.9371 -0.0539 0.0193  0.1276  184  SER B O   
4260  C  CB  . SER B 184 ? 1.0836 1.1980 1.0773 -0.0406 0.0288  0.1082  184  SER B CB  
4261  O  OG  . SER B 184 ? 1.1036 1.2367 1.0964 -0.0354 0.0334  0.0968  184  SER B OG  
4262  N  N   . GLN B 192 ? 0.5155 0.6083 0.4697 -0.0031 0.0075  0.1017  192  GLN B N   
4263  C  CA  . GLN B 192 ? 0.7362 0.8522 0.6801 -0.0063 0.0098  0.1042  192  GLN B CA  
4264  C  C   . GLN B 192 ? 0.8652 0.9978 0.8003 -0.0031 0.0063  0.1005  192  GLN B C   
4265  O  O   . GLN B 192 ? 0.4847 0.6122 0.4236 0.0013  0.0017  0.0960  192  GLN B O   
4266  C  CB  . GLN B 192 ? 0.8846 1.0091 0.8290 -0.0089 0.0159  0.0943  192  GLN B CB  
4267  C  CG  . GLN B 192 ? 0.9839 1.1124 0.9297 -0.0155 0.0201  0.1045  192  GLN B CG  
4268  C  CD  . GLN B 192 ? 1.0592 1.2082 0.9938 -0.0185 0.0220  0.1155  192  GLN B CD  
4269  O  OE1 . GLN B 192 ? 1.1596 1.3289 1.0877 -0.0195 0.0274  0.1105  192  GLN B OE1 
4270  N  NE2 . GLN B 192 ? 1.0269 1.1710 0.9586 -0.0195 0.0180  0.1308  192  GLN B NE2 
4271  N  N   . SER B 193 ? 0.9066 1.0600 0.8296 -0.0059 0.0087  0.1025  193  SER B N   
4272  C  CA  . SER B 193 ? 0.8137 0.9857 0.7249 -0.0041 0.0054  0.0979  193  SER B CA  
4273  C  C   . SER B 193 ? 0.7465 0.9240 0.6569 -0.0025 0.0080  0.0777  193  SER B C   
4274  O  O   . SER B 193 ? 0.5773 0.7691 0.4794 -0.0038 0.0134  0.0712  193  SER B O   
4275  C  CB  . SER B 193 ? 1.0699 1.2619 0.9661 -0.0075 0.0074  0.1092  193  SER B CB  
4276  O  OG  . SER B 193 ? 1.2962 1.4800 1.1955 -0.0101 0.0068  0.1289  193  SER B OG  
4277  N  N   . ARG B 194 ? 0.7871 0.9524 0.7070 0.0007  0.0047  0.0681  194  ARG B N   
4278  C  CA  . ARG B 194 ? 0.7490 0.9146 0.6710 0.0022  0.0066  0.0499  194  ARG B CA  
4279  C  C   . ARG B 194 ? 0.5876 0.7651 0.5026 0.0030  0.0006  0.0422  194  ARG B C   
4280  O  O   . ARG B 194 ? 0.7061 0.8989 0.6092 0.0019  -0.0030 0.0492  194  ARG B O   
4281  C  CB  . ARG B 194 ? 0.7616 0.9061 0.6986 0.0044  0.0070  0.0455  194  ARG B CB  
4282  C  CG  . ARG B 194 ? 0.6951 0.8260 0.6386 0.0032  0.0100  0.0553  194  ARG B CG  
4283  C  CD  . ARG B 194 ? 0.7904 0.9156 0.7392 0.0031  0.0155  0.0464  194  ARG B CD  
4284  N  NE  . ARG B 194 ? 0.9830 1.0988 0.9369 0.0005  0.0176  0.0553  194  ARG B NE  
4285  C  CZ  . ARG B 194 ? 1.1818 1.2914 1.1424 0.0002  0.0208  0.0504  194  ARG B CZ  
4286  N  NH1 . ARG B 194 ? 1.1318 1.2426 1.0948 0.0031  0.0229  0.0376  194  ARG B NH1 
4287  N  NH2 . ARG B 194 ? 1.3556 1.4574 1.3208 -0.0033 0.0214  0.0586  194  ARG B NH2 
4288  N  N   . GLN B 195 ? 0.4816 0.6525 0.4040 0.0044  -0.0009 0.0281  195  GLN B N   
4289  C  CA  . GLN B 195 ? 0.4551 0.6344 0.3757 0.0042  -0.0083 0.0215  195  GLN B CA  
4290  C  C   . GLN B 195 ? 0.4601 0.6328 0.3917 0.0057  -0.0142 0.0322  195  GLN B C   
4291  O  O   . GLN B 195 ? 0.4705 0.6268 0.4137 0.0077  -0.0115 0.0377  195  GLN B O   
4292  C  CB  . GLN B 195 ? 0.4491 0.6230 0.3752 0.0042  -0.0077 0.0029  195  GLN B CB  
4293  C  CG  . GLN B 195 ? 0.4992 0.6789 0.4155 0.0042  -0.0018 -0.0099 195  GLN B CG  
4294  C  CD  . GLN B 195 ? 0.5559 0.7570 0.4524 0.0027  -0.0030 -0.0102 195  GLN B CD  
4295  O  OE1 . GLN B 195 ? 0.6040 0.8159 0.4931 0.0010  -0.0104 -0.0147 195  GLN B OE1 
4296  N  NE2 . GLN B 195 ? 0.2785 0.4872 0.1664 0.0032  0.0042  -0.0053 195  GLN B NE2 
4297  N  N   . PRO B 196 ? 0.4558 0.6424 0.3838 0.0052  -0.0224 0.0350  196  PRO B N   
4298  C  CA  . PRO B 196 ? 0.3277 0.5127 0.2671 0.0076  -0.0288 0.0456  196  PRO B CA  
4299  C  C   . PRO B 196 ? 0.3533 0.5214 0.3113 0.0096  -0.0265 0.0409  196  PRO B C   
4300  O  O   . PRO B 196 ? 0.4106 0.5689 0.3792 0.0133  -0.0264 0.0512  196  PRO B O   
4301  C  CB  . PRO B 196 ? 0.3347 0.5393 0.2690 0.0056  -0.0382 0.0406  196  PRO B CB  
4302  C  CG  . PRO B 196 ? 0.3837 0.6022 0.2968 0.0026  -0.0370 0.0340  196  PRO B CG  
4303  C  CD  . PRO B 196 ? 0.3506 0.5567 0.2627 0.0026  -0.0263 0.0265  196  PRO B CD  
4304  N  N   . GLU B 197 ? 0.2731 0.4378 0.2346 0.0076  -0.0245 0.0254  197  GLU B N   
4305  C  CA  . GLU B 197 ? 0.3317 0.4826 0.3099 0.0087  -0.0223 0.0204  197  GLU B CA  
4306  C  C   . GLU B 197 ? 0.2879 0.4195 0.2697 0.0115  -0.0144 0.0242  197  GLU B C   
4307  O  O   . GLU B 197 ? 0.2103 0.3306 0.2034 0.0145  -0.0128 0.0292  197  GLU B O   
4308  C  CB  . GLU B 197 ? 0.2894 0.4407 0.2695 0.0052  -0.0226 0.0034  197  GLU B CB  
4309  C  CG  . GLU B 197 ? 0.3627 0.5310 0.3422 0.0014  -0.0317 -0.0029 197  GLU B CG  
4310  C  CD  . GLU B 197 ? 0.4953 0.6793 0.4547 -0.0008 -0.0348 -0.0075 197  GLU B CD  
4311  O  OE1 . GLU B 197 ? 0.4751 0.6732 0.4306 -0.0044 -0.0429 -0.0148 197  GLU B OE1 
4312  O  OE2 . GLU B 197 ? 0.5017 0.6845 0.4488 0.0008  -0.0290 -0.0039 197  GLU B OE2 
4313  N  N   . THR B 198 ? 0.3770 0.5062 0.3491 0.0105  -0.0094 0.0214  198  THR B N   
4314  C  CA  . THR B 198 ? 0.3619 0.4756 0.3360 0.0121  -0.0032 0.0252  198  THR B CA  
4315  C  C   . THR B 198 ? 0.4186 0.5268 0.3943 0.0142  -0.0043 0.0402  198  THR B C   
4316  O  O   . THR B 198 ? 0.4271 0.5208 0.4115 0.0172  -0.0026 0.0434  198  THR B O   
4317  C  CB  . THR B 198 ? 0.4417 0.5594 0.4060 0.0103  0.0013  0.0212  198  THR B CB  
4318  O  OG1 . THR B 198 ? 0.3972 0.5224 0.3583 0.0091  0.0014  0.0071  198  THR B OG1 
4319  C  CG2 . THR B 198 ? 0.3748 0.4772 0.3439 0.0114  0.0068  0.0218  198  THR B CG2 
4320  N  N   . ALA B 199 ? 0.3383 0.4575 0.3049 0.0130  -0.0069 0.0494  199  ALA B N   
4321  C  CA  . ALA B 199 ? 0.2946 0.4082 0.2629 0.0150  -0.0087 0.0646  199  ALA B CA  
4322  C  C   . ALA B 199 ? 0.4312 0.5373 0.4123 0.0199  -0.0115 0.0682  199  ALA B C   
4323  O  O   . ALA B 199 ? 0.4306 0.5216 0.4171 0.0232  -0.0099 0.0757  199  ALA B O   
4324  C  CB  . ALA B 199 ? 0.2141 0.3442 0.1713 0.0132  -0.0127 0.0742  199  ALA B CB  
4325  N  N   . ALA B 200 ? 0.3599 0.4767 0.3466 0.0204  -0.0155 0.0622  200  ALA B N   
4326  C  CA  . ALA B 200 ? 0.3370 0.4512 0.3380 0.0252  -0.0178 0.0659  200  ALA B CA  
4327  C  C   . ALA B 200 ? 0.3534 0.4491 0.3635 0.0279  -0.0113 0.0612  200  ALA B C   
4328  O  O   . ALA B 200 ? 0.4525 0.5373 0.4700 0.0332  -0.0097 0.0679  200  ALA B O   
4329  C  CB  . ALA B 200 ? 0.3222 0.4546 0.3287 0.0237  -0.0241 0.0605  200  ALA B CB  
4330  N  N   . LEU B 201 ? 0.3485 0.4402 0.3573 0.0248  -0.0075 0.0498  201  LEU B N   
4331  C  CA  . LEU B 201 ? 0.3530 0.4279 0.3677 0.0271  -0.0014 0.0457  201  LEU B CA  
4332  C  C   . LEU B 201 ? 0.4062 0.4642 0.4148 0.0285  0.0025  0.0500  201  LEU B C   
4333  O  O   . LEU B 201 ? 0.3853 0.4298 0.3986 0.0328  0.0055  0.0525  201  LEU B O   
4334  C  CB  . LEU B 201 ? 0.4225 0.4973 0.4377 0.0236  0.0010  0.0336  201  LEU B CB  
4335  C  CG  . LEU B 201 ? 0.4841 0.5670 0.5117 0.0231  -0.0010 0.0296  201  LEU B CG  
4336  C  CD1 . LEU B 201 ? 0.3892 0.4916 0.4156 0.0193  -0.0085 0.0271  201  LEU B CD1 
4337  C  CD2 . LEU B 201 ? 0.5584 0.6319 0.5901 0.0215  0.0037  0.0208  201  LEU B CD2 
4338  N  N   . VAL B 202 ? 0.3177 0.3771 0.3164 0.0247  0.0027  0.0504  202  VAL B N   
4339  C  CA  . VAL B 202 ? 0.3770 0.4228 0.3713 0.0245  0.0049  0.0560  202  VAL B CA  
4340  C  C   . VAL B 202 ? 0.5080 0.5436 0.5070 0.0293  0.0037  0.0653  202  VAL B C   
4341  O  O   . VAL B 202 ? 0.4796 0.4987 0.4814 0.0327  0.0067  0.0642  202  VAL B O   
4342  C  CB  . VAL B 202 ? 0.3542 0.4088 0.3394 0.0196  0.0040  0.0601  202  VAL B CB  
4343  C  CG1 . VAL B 202 ? 0.1270 0.1682 0.1104 0.0184  0.0048  0.0688  202  VAL B CG1 
4344  C  CG2 . VAL B 202 ? 0.2816 0.3425 0.2630 0.0163  0.0069  0.0500  202  VAL B CG2 
4345  N  N   . ASN B 203 ? 0.3738 0.4195 0.3731 0.0302  -0.0008 0.0743  203  ASN B N   
4346  C  CA  . ASN B 203 ? 0.3305 0.3678 0.3358 0.0360  -0.0024 0.0843  203  ASN B CA  
4347  C  C   . ASN B 203 ? 0.2955 0.3235 0.3106 0.0423  0.0007  0.0800  203  ASN B C   
4348  O  O   . ASN B 203 ? 0.4938 0.5042 0.5112 0.0470  0.0031  0.0829  203  ASN B O   
4349  C  CB  . ASN B 203 ? 0.3724 0.4274 0.3793 0.0372  -0.0086 0.0931  203  ASN B CB  
4350  C  CG  . ASN B 203 ? 0.5351 0.5932 0.5327 0.0336  -0.0112 0.1040  203  ASN B CG  
4351  O  OD1 . ASN B 203 ? 0.4857 0.5384 0.4757 0.0283  -0.0083 0.1030  203  ASN B OD1 
4352  N  ND2 . ASN B 203 ? 0.6661 0.7341 0.6651 0.0364  -0.0168 0.1155  203  ASN B ND2 
4353  N  N   . TRP B 204 ? 0.2419 0.2817 0.2629 0.0423  0.0010  0.0729  204  TRP B N   
4354  C  CA  . TRP B 204 ? 0.3702 0.4060 0.4022 0.0480  0.0046  0.0700  204  TRP B CA  
4355  C  C   . TRP B 204 ? 0.3904 0.4069 0.4182 0.0490  0.0112  0.0637  204  TRP B C   
4356  O  O   . TRP B 204 ? 0.4515 0.4552 0.4826 0.0553  0.0149  0.0649  204  TRP B O   
4357  C  CB  . TRP B 204 ? 0.4041 0.4576 0.4439 0.0455  0.0031  0.0641  204  TRP B CB  
4358  C  CG  . TRP B 204 ? 0.2743 0.3296 0.3283 0.0507  0.0064  0.0633  204  TRP B CG  
4359  C  CD1 . TRP B 204 ? 0.3814 0.4355 0.4454 0.0587  0.0073  0.0704  204  TRP B CD1 
4360  C  CD2 . TRP B 204 ? 0.1793 0.2387 0.2404 0.0484  0.0100  0.0557  204  TRP B CD2 
4361  N  NE1 . TRP B 204 ? 0.4047 0.4639 0.4819 0.0616  0.0119  0.0674  204  TRP B NE1 
4362  C  CE2 . TRP B 204 ? 0.2250 0.2871 0.3004 0.0547  0.0134  0.0589  204  TRP B CE2 
4363  C  CE3 . TRP B 204 ? 0.1406 0.2010 0.1981 0.0418  0.0109  0.0469  204  TRP B CE3 
4364  C  CZ2 . TRP B 204 ? 0.2578 0.3249 0.3440 0.0536  0.0180  0.0545  204  TRP B CZ2 
4365  C  CZ3 . TRP B 204 ? 0.2166 0.2794 0.2845 0.0409  0.0148  0.0425  204  TRP B CZ3 
4366  C  CH2 . TRP B 204 ? 0.2479 0.3145 0.3299 0.0462  0.0184  0.0467  204  TRP B CH2 
4367  N  N   . ILE B 205 ? 0.3776 0.3929 0.3976 0.0433  0.0123  0.0568  205  ILE B N   
4368  C  CA  . ILE B 205 ? 0.4701 0.4702 0.4852 0.0435  0.0174  0.0506  205  ILE B CA  
4369  C  C   . ILE B 205 ? 0.4988 0.4800 0.5081 0.0460  0.0184  0.0538  205  ILE B C   
4370  O  O   . ILE B 205 ? 0.6230 0.5903 0.6300 0.0496  0.0225  0.0502  205  ILE B O   
4371  C  CB  . ILE B 205 ? 0.4125 0.4159 0.4209 0.0372  0.0171  0.0444  205  ILE B CB  
4372  C  CG1 . ILE B 205 ? 0.4208 0.4383 0.4348 0.0349  0.0167  0.0390  205  ILE B CG1 
4373  C  CG2 . ILE B 205 ? 0.3722 0.3601 0.3744 0.0374  0.0207  0.0399  205  ILE B CG2 
4374  C  CD1 . ILE B 205 ? 0.3899 0.4123 0.3982 0.0297  0.0160  0.0329  205  ILE B CD1 
4375  N  N   . VAL B 206 ? 0.3794 0.3596 0.3857 0.0437  0.0145  0.0606  206  VAL B N   
4376  C  CA  . VAL B 206 ? 0.3933 0.3539 0.3949 0.0446  0.0146  0.0636  206  VAL B CA  
4377  C  C   . VAL B 206 ? 0.3437 0.2966 0.3518 0.0523  0.0146  0.0700  206  VAL B C   
4378  O  O   . VAL B 206 ? 0.4786 0.4129 0.4840 0.0540  0.0145  0.0724  206  VAL B O   
4379  C  CB  . VAL B 206 ? 0.4789 0.4404 0.4751 0.0373  0.0109  0.0690  206  VAL B CB  
4380  C  CG1 . VAL B 206 ? 0.4088 0.3761 0.3996 0.0309  0.0117  0.0622  206  VAL B CG1 
4381  C  CG2 . VAL B 206 ? 0.4305 0.4083 0.4294 0.0364  0.0071  0.0781  206  VAL B CG2 
4382  N  N   . SER B 207 ? 0.3900 0.3571 0.4077 0.0571  0.0144  0.0724  207  SER B N   
4383  C  CA  . SER B 207 ? 0.3095 0.2733 0.3363 0.0657  0.0142  0.0795  207  SER B CA  
4384  C  C   . SER B 207 ? 0.4088 0.3619 0.4399 0.0741  0.0208  0.0740  207  SER B C   
4385  O  O   . SER B 207 ? 0.5981 0.5422 0.6356 0.0827  0.0221  0.0782  207  SER B O   
4386  C  CB  . SER B 207 ? 0.2711 0.2586 0.3077 0.0667  0.0098  0.0857  207  SER B CB  
4387  O  OG  . SER B 207 ? 0.4610 0.4606 0.5072 0.0697  0.0128  0.0805  207  SER B OG  
4388  N  N   . LYS B 208 ? 0.4744 0.4290 0.5023 0.0722  0.0253  0.0651  208  LYS B N   
4389  C  CA  . LYS B 208 ? 0.4205 0.3664 0.4501 0.0798  0.0328  0.0598  208  LYS B CA  
4390  C  C   . LYS B 208 ? 0.3934 0.3283 0.4098 0.0757  0.0361  0.0510  208  LYS B C   
4391  O  O   . LYS B 208 ? 0.5944 0.5354 0.6057 0.0677  0.0334  0.0487  208  LYS B O   
4392  C  CB  . LYS B 208 ? 0.4938 0.4596 0.5378 0.0834  0.0357  0.0607  208  LYS B CB  
4393  C  CG  . LYS B 208 ? 0.5559 0.5343 0.6148 0.0889  0.0321  0.0697  208  LYS B CG  
4394  C  CD  . LYS B 208 ? 0.4571 0.4578 0.5328 0.0913  0.0342  0.0705  208  LYS B CD  
4395  C  CE  . LYS B 208 ? 0.6015 0.6143 0.6933 0.0988  0.0303  0.0802  208  LYS B CE  
4396  N  NZ  . LYS B 208 ? 0.4952 0.5332 0.6070 0.1008  0.0308  0.0822  208  LYS B NZ  
4397  N  N   . PRO B 209 ? 0.3622 0.2817 0.3730 0.0820  0.0421  0.0460  209  PRO B N   
4398  C  CA  . PRO B 209 ? 0.2318 0.1396 0.2281 0.0792  0.0448  0.0379  209  PRO B CA  
4399  C  C   . PRO B 209 ? 0.3344 0.2547 0.3317 0.0774  0.0490  0.0350  209  PRO B C   
4400  O  O   . PRO B 209 ? 0.4235 0.3359 0.4121 0.0805  0.0548  0.0300  209  PRO B O   
4401  C  CB  . PRO B 209 ? 0.2421 0.1311 0.2324 0.0882  0.0503  0.0338  209  PRO B CB  
4402  C  CG  . PRO B 209 ? 0.3497 0.2484 0.3559 0.0973  0.0541  0.0390  209  PRO B CG  
4403  C  CD  . PRO B 209 ? 0.3076 0.2200 0.3251 0.0930  0.0466  0.0476  209  PRO B CD  
4404  N  N   . PHE B 210 ? 0.3310 0.2696 0.3376 0.0722  0.0462  0.0378  210  PHE B N   
4405  C  CA  . PHE B 210 ? 0.3464 0.2948 0.3551 0.0694  0.0496  0.0353  210  PHE B CA  
4406  C  C   . PHE B 210 ? 0.4069 0.3428 0.4005 0.0681  0.0523  0.0300  210  PHE B C   
4407  O  O   . PHE B 210 ? 0.5195 0.4460 0.5024 0.0641  0.0477  0.0276  210  PHE B O   
4408  C  CB  . PHE B 210 ? 0.2238 0.1878 0.2396 0.0621  0.0442  0.0366  210  PHE B CB  
4409  C  CG  . PHE B 210 ? 0.2899 0.2697 0.3206 0.0633  0.0416  0.0416  210  PHE B CG  
4410  C  CD1 . PHE B 210 ? 0.3299 0.3141 0.3613 0.0613  0.0349  0.0457  210  PHE B CD1 
4411  C  CD2 . PHE B 210 ? 0.3648 0.3563 0.4092 0.0664  0.0459  0.0431  210  PHE B CD2 
4412  C  CE1 . PHE B 210 ? 0.3384 0.3384 0.3826 0.0628  0.0315  0.0509  210  PHE B CE1 
4413  C  CE2 . PHE B 210 ? 0.3613 0.3695 0.4208 0.0674  0.0424  0.0479  210  PHE B CE2 
4414  C  CZ  . PHE B 210 ? 0.2719 0.2842 0.3306 0.0659  0.0348  0.0518  210  PHE B CZ  
4415  N  N   . VAL B 211 ? 0.3053 0.2425 0.2987 0.0714  0.0596  0.0289  211  VAL B N   
4416  C  CA  . VAL B 211 ? 0.2323 0.1591 0.2108 0.0716  0.0628  0.0251  211  VAL B CA  
4417  C  C   . VAL B 211 ? 0.3972 0.3313 0.3770 0.0653  0.0615  0.0254  211  VAL B C   
4418  O  O   . VAL B 211 ? 0.5614 0.4881 0.5294 0.0625  0.0588  0.0230  211  VAL B O   
4419  C  CB  . VAL B 211 ? 0.2141 0.1394 0.1909 0.0791  0.0727  0.0250  211  VAL B CB  
4420  C  CG1 . VAL B 211 ? 0.2899 0.2089 0.2517 0.0784  0.0762  0.0229  211  VAL B CG1 
4421  C  CG2 . VAL B 211 ? 0.3611 0.2745 0.3331 0.0868  0.0747  0.0226  211  VAL B CG2 
4422  N  N   . LEU B 212 ? 0.2989 0.2472 0.2940 0.0631  0.0628  0.0284  212  LEU B N   
4423  C  CA  . LEU B 212 ? 0.3549 0.3086 0.3539 0.0578  0.0624  0.0286  212  LEU B CA  
4424  C  C   . LEU B 212 ? 0.4099 0.3782 0.4255 0.0531  0.0583  0.0294  212  LEU B C   
4425  O  O   . LEU B 212 ? 0.5059 0.4832 0.5321 0.0549  0.0580  0.0316  212  LEU B O   
4426  C  CB  . LEU B 212 ? 0.3970 0.3502 0.3955 0.0603  0.0711  0.0311  212  LEU B CB  
4427  C  CG  . LEU B 212 ? 0.3251 0.2831 0.3311 0.0555  0.0727  0.0333  212  LEU B CG  
4428  C  CD1 . LEU B 212 ? 0.5125 0.4624 0.5082 0.0524  0.0673  0.0309  212  LEU B CD1 
4429  C  CD2 . LEU B 212 ? 0.2616 0.2194 0.2665 0.0586  0.0827  0.0378  212  LEU B CD2 
4430  N  N   . SER B 213 ? 0.3546 0.3253 0.3719 0.0475  0.0548  0.0273  213  SER B N   
4431  C  CA  . SER B 213 ? 0.2886 0.2718 0.3186 0.0426  0.0503  0.0260  213  SER B CA  
4432  C  C   . SER B 213 ? 0.3569 0.3397 0.3901 0.0377  0.0494  0.0230  213  SER B C   
4433  O  O   . SER B 213 ? 0.3250 0.2980 0.3501 0.0383  0.0512  0.0228  213  SER B O   
4434  C  CB  . SER B 213 ? 0.3000 0.2862 0.3260 0.0415  0.0436  0.0247  213  SER B CB  
4435  O  OG  . SER B 213 ? 0.4099 0.4089 0.4451 0.0369  0.0389  0.0226  213  SER B OG  
4436  N  N   . ALA B 214 ? 0.3757 0.3689 0.4211 0.0330  0.0462  0.0207  214  ALA B N   
4437  C  CA  . ALA B 214 ? 0.3359 0.3272 0.3849 0.0284  0.0446  0.0162  214  ALA B CA  
4438  C  C   . ALA B 214 ? 0.2029 0.2059 0.2598 0.0236  0.0386  0.0110  214  ALA B C   
4439  O  O   . ALA B 214 ? 0.2800 0.2945 0.3460 0.0224  0.0368  0.0126  214  ALA B O   
4440  C  CB  . ALA B 214 ? 0.3508 0.3379 0.4083 0.0269  0.0503  0.0194  214  ALA B CB  
4441  N  N   . ASN B 215 ? 0.3912 0.3923 0.4444 0.0213  0.0351  0.0046  215  ASN B N   
4442  C  CA  . ASN B 215 ? 0.4176 0.4291 0.4770 0.0164  0.0297  -0.0021 215  ASN B CA  
4443  C  C   . ASN B 215 ? 0.3955 0.4006 0.4613 0.0125  0.0296  -0.0089 215  ASN B C   
4444  O  O   . ASN B 215 ? 0.2996 0.2928 0.3611 0.0146  0.0322  -0.0098 215  ASN B O   
4445  C  CB  . ASN B 215 ? 0.4963 0.5158 0.5458 0.0170  0.0250  -0.0048 215  ASN B CB  
4446  C  CG  . ASN B 215 ? 0.4262 0.4390 0.4658 0.0187  0.0255  -0.0088 215  ASN B CG  
4447  O  OD1 . ASN B 215 ? 0.5931 0.6090 0.6318 0.0167  0.0233  -0.0167 215  ASN B OD1 
4448  N  ND2 . ASN B 215 ? 0.2398 0.2445 0.2723 0.0225  0.0283  -0.0038 215  ASN B ND2 
4449  N  N   . PHE B 216 ? 0.4190 0.4319 0.4959 0.0068  0.0260  -0.0136 216  PHE B N   
4450  C  CA  . PHE B 216 ? 0.3018 0.3067 0.3887 0.0020  0.0262  -0.0191 216  PHE B CA  
4451  C  C   . PHE B 216 ? 0.3657 0.3714 0.4493 -0.0006 0.0211  -0.0316 216  PHE B C   
4452  O  O   . PHE B 216 ? 0.4477 0.4665 0.5264 -0.0020 0.0158  -0.0363 216  PHE B O   
4453  C  CB  . PHE B 216 ? 0.2579 0.2687 0.3622 -0.0036 0.0266  -0.0156 216  PHE B CB  
4454  C  CG  . PHE B 216 ? 0.3712 0.3811 0.4784 -0.0001 0.0336  -0.0038 216  PHE B CG  
4455  C  CD1 . PHE B 216 ? 0.4128 0.4342 0.5180 0.0038  0.0338  0.0020  216  PHE B CD1 
4456  C  CD2 . PHE B 216 ? 0.3381 0.3350 0.4486 0.0003  0.0403  0.0017  216  PHE B CD2 
4457  C  CE1 . PHE B 216 ? 0.3024 0.3223 0.4088 0.0082  0.0409  0.0113  216  PHE B CE1 
4458  C  CE2 . PHE B 216 ? 0.2941 0.2910 0.4044 0.0042  0.0474  0.0118  216  PHE B CE2 
4459  C  CZ  . PHE B 216 ? 0.2326 0.2409 0.3406 0.0083  0.0479  0.0158  216  PHE B CZ  
4460  N  N   . HIS B 217 ? 0.3135 0.3046 0.3986 -0.0004 0.0230  -0.0366 217  HIS B N   
4461  C  CA  . HIS B 217 ? 0.3671 0.3558 0.4484 -0.0012 0.0198  -0.0496 217  HIS B CA  
4462  C  C   . HIS B 217 ? 0.4285 0.4029 0.5227 -0.0058 0.0199  -0.0554 217  HIS B C   
4463  O  O   . HIS B 217 ? 0.3541 0.3212 0.4598 -0.0086 0.0230  -0.0476 217  HIS B O   
4464  C  CB  . HIS B 217 ? 0.2473 0.2313 0.3165 0.0064  0.0225  -0.0503 217  HIS B CB  
4465  C  CG  . HIS B 217 ? 0.3426 0.3400 0.3995 0.0096  0.0217  -0.0462 217  HIS B CG  
4466  N  ND1 . HIS B 217 ? 0.3368 0.3447 0.3840 0.0105  0.0193  -0.0536 217  HIS B ND1 
4467  C  CD2 . HIS B 217 ? 0.3631 0.3646 0.4161 0.0118  0.0233  -0.0354 217  HIS B CD2 
4468  C  CE1 . HIS B 217 ? 0.3593 0.3768 0.3980 0.0126  0.0193  -0.0462 217  HIS B CE1 
4469  N  NE2 . HIS B 217 ? 0.3851 0.3980 0.4274 0.0135  0.0213  -0.0357 217  HIS B NE2 
4470  N  N   . GLY B 218 ? 0.3709 0.3409 0.4631 -0.0066 0.0170  -0.0690 218  GLY B N   
4471  C  CA  . GLY B 218 ? 0.3850 0.3383 0.4892 -0.0108 0.0167  -0.0762 218  GLY B CA  
4472  C  C   . GLY B 218 ? 0.3993 0.3407 0.4970 -0.0041 0.0185  -0.0855 218  GLY B C   
4473  O  O   . GLY B 218 ? 0.4200 0.3704 0.5046 0.0022  0.0193  -0.0875 218  GLY B O   
4474  N  N   . GLY B 219 ? 0.4027 0.3242 0.5109 -0.0056 0.0193  -0.0909 219  GLY B N   
4475  C  CA  . GLY B 219 ? 0.3182 0.2264 0.4232 0.0018  0.0214  -0.1000 219  GLY B CA  
4476  C  C   . GLY B 219 ? 0.5660 0.4552 0.6786 0.0070  0.0265  -0.0892 219  GLY B C   
4477  O  O   . GLY B 219 ? 0.6971 0.5690 0.8143 0.0117  0.0279  -0.0955 219  GLY B O   
4478  N  N   . ALA B 220 ? 0.5269 0.4193 0.6402 0.0067  0.0292  -0.0727 220  ALA B N   
4479  C  CA  . ALA B 220 ? 0.6006 0.4770 0.7190 0.0111  0.0336  -0.0603 220  ALA B CA  
4480  C  C   . ALA B 220 ? 0.4732 0.3528 0.5952 0.0063  0.0362  -0.0450 220  ALA B C   
4481  O  O   . ALA B 220 ? 0.4853 0.3801 0.6073 0.0004  0.0346  -0.0442 220  ALA B O   
4482  C  CB  . ALA B 220 ? 0.6554 0.5342 0.7632 0.0222  0.0358  -0.0566 220  ALA B CB  
4483  N  N   . VAL B 221 ? 0.4165 0.2827 0.5416 0.0094  0.0403  -0.0324 221  VAL B N   
4484  C  CA  . VAL B 221 ? 0.5787 0.4478 0.7058 0.0060  0.0443  -0.0172 221  VAL B CA  
4485  C  C   . VAL B 221 ? 0.6254 0.4943 0.7400 0.0145  0.0478  -0.0046 221  VAL B C   
4486  O  O   . VAL B 221 ? 0.4426 0.2965 0.5588 0.0185  0.0501  0.0035  221  VAL B O   
4487  C  CB  . VAL B 221 ? 0.4518 0.3053 0.5957 -0.0015 0.0465  -0.0119 221  VAL B CB  
4488  C  CG1 . VAL B 221 ? 0.3918 0.2540 0.5390 -0.0064 0.0513  0.0021  221  VAL B CG1 
4489  C  CG2 . VAL B 221 ? 0.4873 0.3383 0.6434 -0.0099 0.0417  -0.0266 221  VAL B CG2 
4490  N  N   . VAL B 222 ? 0.5763 0.4615 0.6785 0.0170  0.0475  -0.0028 222  VAL B N   
4491  C  CA  . VAL B 222 ? 0.4901 0.3767 0.5787 0.0248  0.0490  0.0057  222  VAL B CA  
4492  C  C   . VAL B 222 ? 0.5489 0.4514 0.6261 0.0252  0.0491  0.0080  222  VAL B C   
4493  O  O   . VAL B 222 ? 0.6858 0.6004 0.7639 0.0218  0.0468  0.0009  222  VAL B O   
4494  C  CB  . VAL B 222 ? 0.5121 0.3967 0.5961 0.0320  0.0459  -0.0009 222  VAL B CB  
4495  C  CG1 . VAL B 222 ? 0.2845 0.1841 0.3640 0.0313  0.0425  -0.0126 222  VAL B CG1 
4496  C  CG2 . VAL B 222 ? 0.6133 0.4974 0.6858 0.0393  0.0464  0.0091  222  VAL B CG2 
4497  N  N   . ALA B 223 ? 0.4677 0.3694 0.5337 0.0298  0.0515  0.0177  223  ALA B N   
4498  C  CA  . ALA B 223 ? 0.3555 0.2687 0.4097 0.0313  0.0517  0.0198  223  ALA B CA  
4499  C  C   . ALA B 223 ? 0.4379 0.3552 0.4809 0.0366  0.0476  0.0165  223  ALA B C   
4500  O  O   . ALA B 223 ? 0.3656 0.2775 0.4008 0.0415  0.0472  0.0220  223  ALA B O   
4501  C  CB  . ALA B 223 ? 0.2464 0.1565 0.2940 0.0325  0.0571  0.0314  223  ALA B CB  
4502  N  N   . SER B 224 ? 0.4630 0.3909 0.5055 0.0354  0.0443  0.0083  224  SER B N   
4503  C  CA  . SER B 224 ? 0.4181 0.3519 0.4527 0.0391  0.0408  0.0052  224  SER B CA  
4504  C  C   . SER B 224 ? 0.3705 0.3116 0.3942 0.0392  0.0401  0.0081  224  SER B C   
4505  O  O   . SER B 224 ? 0.3659 0.3120 0.3901 0.0362  0.0412  0.0083  224  SER B O   
4506  C  CB  . SER B 224 ? 0.3917 0.3324 0.4318 0.0380  0.0383  -0.0053 224  SER B CB  
4507  O  OG  . SER B 224 ? 0.5133 0.4609 0.5480 0.0417  0.0360  -0.0072 224  SER B OG  
4508  N  N   . TYR B 225 ? 0.3599 0.3014 0.3751 0.0426  0.0377  0.0102  225  TYR B N   
4509  C  CA  . TYR B 225 ? 0.2998 0.2448 0.3041 0.0426  0.0364  0.0127  225  TYR B CA  
4510  C  C   . TYR B 225 ? 0.3608 0.3128 0.3620 0.0434  0.0319  0.0103  225  TYR B C   
4511  O  O   . TYR B 225 ? 0.2720 0.2260 0.2784 0.0457  0.0303  0.0082  225  TYR B O   
4512  C  CB  . TYR B 225 ? 0.4192 0.3555 0.4138 0.0450  0.0384  0.0198  225  TYR B CB  
4513  C  CG  . TYR B 225 ? 0.3568 0.2870 0.3491 0.0488  0.0368  0.0238  225  TYR B CG  
4514  C  CD1 . TYR B 225 ? 0.4936 0.4165 0.4932 0.0499  0.0395  0.0270  225  TYR B CD1 
4515  C  CD2 . TYR B 225 ? 0.3600 0.2920 0.3438 0.0510  0.0320  0.0250  225  TYR B CD2 
4516  C  CE1 . TYR B 225 ? 0.5193 0.4363 0.5172 0.0542  0.0377  0.0321  225  TYR B CE1 
4517  C  CE2 . TYR B 225 ? 0.5566 0.4848 0.5390 0.0550  0.0296  0.0295  225  TYR B CE2 
4518  C  CZ  . TYR B 225 ? 0.6260 0.5466 0.6152 0.0571  0.0325  0.0335  225  TYR B CZ  
4519  O  OH  . TYR B 225 ? 0.7204 0.6368 0.7086 0.0619  0.0297  0.0393  225  TYR B OH  
4520  N  N   . PRO B 226 ? 0.3499 0.3056 0.3439 0.0417  0.0300  0.0109  226  PRO B N   
4521  C  CA  . PRO B 226 ? 0.3466 0.3100 0.3388 0.0407  0.0259  0.0096  226  PRO B CA  
4522  C  C   . PRO B 226 ? 0.3714 0.3338 0.3612 0.0433  0.0224  0.0119  226  PRO B C   
4523  O  O   . PRO B 226 ? 0.4542 0.4080 0.4373 0.0457  0.0221  0.0158  226  PRO B O   
4524  C  CB  . PRO B 226 ? 0.3675 0.3292 0.3519 0.0381  0.0250  0.0113  226  PRO B CB  
4525  C  CG  . PRO B 226 ? 0.4733 0.4321 0.4592 0.0379  0.0290  0.0117  226  PRO B CG  
4526  C  CD  . PRO B 226 ? 0.3351 0.2884 0.3247 0.0401  0.0322  0.0126  226  PRO B CD  
4527  N  N   . TYR B 227 ? 0.3197 0.2926 0.3149 0.0429  0.0195  0.0100  227  TYR B N   
4528  C  CA  . TYR B 227 ? 0.2775 0.2619 0.2779 0.0398  0.0203  0.0064  227  TYR B CA  
4529  C  C   . TYR B 227 ? 0.4153 0.4050 0.4251 0.0425  0.0231  0.0013  227  TYR B C   
4530  O  O   . TYR B 227 ? 0.4349 0.4197 0.4493 0.0470  0.0235  0.0011  227  TYR B O   
4531  C  CB  . TYR B 227 ? 0.4645 0.4592 0.4659 0.0373  0.0166  0.0076  227  TYR B CB  
4532  C  CG  . TYR B 227 ? 0.4252 0.4147 0.4179 0.0330  0.0132  0.0109  227  TYR B CG  
4533  C  CD1 . TYR B 227 ? 0.3086 0.2959 0.2974 0.0294  0.0145  0.0114  227  TYR B CD1 
4534  C  CD2 . TYR B 227 ? 0.4057 0.3926 0.3945 0.0328  0.0082  0.0132  227  TYR B CD2 
4535  C  CE1 . TYR B 227 ? 0.4137 0.3938 0.3952 0.0260  0.0115  0.0137  227  TYR B CE1 
4536  C  CE2 . TYR B 227 ? 0.5091 0.4894 0.4894 0.0285  0.0046  0.0145  227  TYR B CE2 
4537  C  CZ  . TYR B 227 ? 0.5897 0.5654 0.5666 0.0253  0.0066  0.0145  227  TYR B CZ  
4538  O  OH  . TYR B 227 ? 0.5714 0.5379 0.5405 0.0216  0.0031  0.0152  227  TYR B OH  
4539  N  N   . ASP B 228 ? 0.4965 0.4956 0.5085 0.0400  0.0248  -0.0028 228  ASP B N   
4540  C  CA  . ASP B 228 ? 0.3242 0.3285 0.3432 0.0423  0.0274  -0.0097 228  ASP B CA  
4541  C  C   . ASP B 228 ? 0.3625 0.3810 0.3869 0.0443  0.0278  -0.0120 228  ASP B C   
4542  O  O   . ASP B 228 ? 0.5335 0.5561 0.5641 0.0481  0.0304  -0.0185 228  ASP B O   
4543  C  CB  . ASP B 228 ? 0.4110 0.4192 0.4278 0.0386  0.0288  -0.0136 228  ASP B CB  
4544  C  CG  . ASP B 228 ? 0.5820 0.5786 0.5992 0.0377  0.0296  -0.0138 228  ASP B CG  
4545  O  OD1 . ASP B 228 ? 0.6868 0.6717 0.7059 0.0402  0.0301  -0.0111 228  ASP B OD1 
4546  O  OD2 . ASP B 228 ? 0.6726 0.6729 0.6888 0.0344  0.0296  -0.0159 228  ASP B OD2 
4547  N  N   . ASN B 229 ? 0.2888 0.3149 0.3117 0.0417  0.0254  -0.0070 229  ASN B N   
4548  C  CA  . ASN B 229 ? 0.5070 0.5495 0.5373 0.0431  0.0260  -0.0077 229  ASN B CA  
4549  C  C   . ASN B 229 ? 0.4688 0.5142 0.5009 0.0415  0.0213  -0.0012 229  ASN B C   
4550  O  O   . ASN B 229 ? 0.3850 0.4180 0.4107 0.0401  0.0176  0.0028  229  ASN B O   
4551  C  CB  . ASN B 229 ? 0.4726 0.5300 0.5014 0.0393  0.0291  -0.0098 229  ASN B CB  
4552  C  CG  . ASN B 229 ? 0.3777 0.4350 0.3992 0.0320  0.0267  -0.0032 229  ASN B CG  
4553  O  OD1 . ASN B 229 ? 0.2925 0.3387 0.3103 0.0299  0.0229  0.0016  229  ASN B OD1 
4554  N  ND2 . ASN B 229 ? 0.2579 0.3271 0.2768 0.0284  0.0291  -0.0030 229  ASN B ND2 
4555  N  N   . SER B 230 ? 0.4688 0.5314 0.5097 0.0416  0.0215  -0.0005 230  SER B N   
4556  C  CA  . SER B 230 ? 0.4023 0.4703 0.4471 0.0390  0.0160  0.0053  230  SER B CA  
4557  C  C   . SER B 230 ? 0.4057 0.4965 0.4610 0.0361  0.0175  0.0068  230  SER B C   
4558  O  O   . SER B 230 ? 0.4643 0.5676 0.5239 0.0383  0.0237  0.0029  230  SER B O   
4559  C  CB  . SER B 230 ? 0.2764 0.3399 0.3264 0.0459  0.0127  0.0062  230  SER B CB  
4560  O  OG  . SER B 230 ? 0.3604 0.4381 0.4242 0.0525  0.0157  0.0033  230  SER B OG  
4561  N  N   . LEU B 231 ? 0.3936 0.4906 0.4531 0.0309  0.0119  0.0123  231  LEU B N   
4562  C  CA  . LEU B 231 ? 0.5414 0.6621 0.6139 0.0273  0.0133  0.0152  231  LEU B CA  
4563  C  C   . LEU B 231 ? 0.6186 0.7570 0.7060 0.0361  0.0175  0.0120  231  LEU B C   
4564  O  O   . LEU B 231 ? 0.5921 0.7516 0.6889 0.0355  0.0232  0.0119  231  LEU B O   
4565  C  CB  . LEU B 231 ? 0.5655 0.6889 0.6418 0.0196  0.0051  0.0212  231  LEU B CB  
4566  C  CG  . LEU B 231 ? 0.6028 0.7178 0.6704 0.0088  0.0027  0.0251  231  LEU B CG  
4567  C  CD1 . LEU B 231 ? 0.3962 0.5075 0.4653 0.0018  -0.0070 0.0287  231  LEU B CD1 
4568  C  CD2 . LEU B 231 ? 0.6157 0.7482 0.6894 0.0036  0.0092  0.0282  231  LEU B CD2 
4569  N  N   . ALA B 232 ? 0.5876 0.7172 0.6772 0.0446  0.0152  0.0098  232  ALA B N   
4570  C  CA  . ALA B 232 ? 0.4512 0.5936 0.5557 0.0549  0.0187  0.0066  232  ALA B CA  
4571  C  C   . ALA B 232 ? 0.5493 0.6938 0.6525 0.0602  0.0283  -0.0017 232  ALA B C   
4572  O  O   . ALA B 232 ? 0.4694 0.6305 0.5853 0.0672  0.0339  -0.0054 232  ALA B O   
4573  C  CB  . ALA B 232 ? 0.2916 0.4196 0.3966 0.0626  0.0135  0.0075  232  ALA B CB  
4574  N  N   . HIS B 233 ? 0.6508 0.7789 0.7387 0.0568  0.0301  -0.0049 233  HIS B N   
4575  C  CA  . HIS B 233 ? 0.5249 0.6507 0.6079 0.0607  0.0373  -0.0139 233  HIS B CA  
4576  C  C   . HIS B 233 ? 0.6439 0.7652 0.7355 0.0723  0.0402  -0.0211 233  HIS B C   
4577  O  O   . HIS B 233 ? 0.6832 0.8157 0.7798 0.0778  0.0472  -0.0288 233  HIS B O   
4578  C  CB  . HIS B 233 ? 0.3041 0.4507 0.3866 0.0569  0.0437  -0.0154 233  HIS B CB  
4579  C  CG  . HIS B 233 ? 0.3551 0.5006 0.4266 0.0459  0.0416  -0.0090 233  HIS B CG  
4580  N  ND1 . HIS B 233 ? 0.5571 0.7149 0.6334 0.0382  0.0392  -0.0002 233  HIS B ND1 
4581  C  CD2 . HIS B 233 ? 0.4838 0.6164 0.5409 0.0413  0.0410  -0.0097 233  HIS B CD2 
4582  C  CE1 . HIS B 233 ? 0.5457 0.6964 0.6105 0.0299  0.0376  0.0042  233  HIS B CE1 
4583  N  NE2 . HIS B 233 ? 0.4564 0.5928 0.5097 0.0322  0.0387  -0.0013 233  HIS B NE2 
4584  N  N   . ASN B 234 ? 0.6750 0.7788 0.7675 0.0761  0.0352  -0.0185 234  ASN B N   
4585  C  CA  . ASN B 234 ? 0.6783 0.7724 0.7789 0.0869  0.0370  -0.0236 234  ASN B CA  
4586  C  C   . ASN B 234 ? 0.5810 0.6589 0.6734 0.0876  0.0412  -0.0331 234  ASN B C   
4587  O  O   . ASN B 234 ? 0.5172 0.5831 0.5972 0.0803  0.0395  -0.0323 234  ASN B O   
4588  C  CB  . ASN B 234 ? 0.6102 0.6902 0.7128 0.0898  0.0300  -0.0157 234  ASN B CB  
4589  C  CG  . ASN B 234 ? 0.3767 0.4717 0.4860 0.0881  0.0238  -0.0067 234  ASN B CG  
4590  O  OD1 . ASN B 234 ? 0.3739 0.4915 0.4955 0.0896  0.0256  -0.0067 234  ASN B OD1 
4591  N  ND2 . ASN B 234 ? 0.3594 0.4429 0.4608 0.0845  0.0165  0.0008  234  ASN B ND2 
4592  N  N   . GLU B 235 ? 0.6039 0.6815 0.7042 0.0964  0.0465  -0.0425 235  GLU B N   
4593  C  CA  . GLU B 235 ? 0.6300 0.6911 0.7239 0.0969  0.0495  -0.0530 235  GLU B CA  
4594  C  C   . GLU B 235 ? 0.7015 0.7378 0.7898 0.0933  0.0447  -0.0484 235  GLU B C   
4595  O  O   . GLU B 235 ? 0.5098 0.5376 0.5877 0.0863  0.0445  -0.0514 235  GLU B O   
4596  C  CB  . GLU B 235 ? 0.5548 0.6141 0.6599 0.1086  0.0548  -0.0637 235  GLU B CB  
4597  C  CG  . GLU B 235 ? 0.8172 0.8581 0.9164 0.1085  0.0572  -0.0762 235  GLU B CG  
4598  C  CD  . GLU B 235 ? 0.9710 1.0052 1.0816 0.1207  0.0620  -0.0876 235  GLU B CD  
4599  O  OE1 . GLU B 235 ? 1.0679 1.0968 1.1731 0.1211  0.0659  -0.1020 235  GLU B OE1 
4600  O  OE2 . GLU B 235 ? 0.8553 0.8893 0.9802 0.1302  0.0616  -0.0826 235  GLU B OE2 
4601  N  N   . CYS B 236 ? 0.8014 0.8279 0.8968 0.0983  0.0409  -0.0405 236  CYS B N   
4602  C  CA  . CYS B 236 ? 0.7013 0.7043 0.7929 0.0966  0.0378  -0.0355 236  CYS B CA  
4603  C  C   . CYS B 236 ? 0.5318 0.5293 0.6283 0.1014  0.0329  -0.0238 236  CYS B C   
4604  O  O   . CYS B 236 ? 0.5762 0.5883 0.6809 0.1065  0.0310  -0.0198 236  CYS B O   
4605  C  CB  . CYS B 236 ? 0.8796 0.8652 0.9764 0.1010  0.0412  -0.0451 236  CYS B CB  
4606  S  SG  . CYS B 236 ? 0.4252 0.4024 0.5396 0.1155  0.0417  -0.0440 236  CYS B SG  
4607  N  N   . CYS B 237 ? 0.6955 0.6729 0.7874 0.0996  0.0310  -0.0180 237  CYS B N   
4608  C  CA  . CYS B 237 ? 0.5912 0.5586 0.6868 0.1054  0.0269  -0.0071 237  CYS B CA  
4609  C  C   . CYS B 237 ? 0.4066 0.3869 0.4975 0.1042  0.0209  0.0028  237  CYS B C   
4610  O  O   . CYS B 237 ? 0.5613 0.5409 0.6575 0.1108  0.0167  0.0111  237  CYS B O   
4611  C  CB  . CYS B 237 ? 0.6038 0.5669 0.7154 0.1172  0.0286  -0.0101 237  CYS B CB  
4612  S  SG  . CYS B 237 ? 0.7607 0.7141 0.8780 0.1186  0.0358  -0.0270 237  CYS B SG  
4613  N  N   . GLU B 238 ? 0.3199 0.3114 0.4012 0.0956  0.0200  0.0021  238  GLU B N   
4614  C  CA  . GLU B 238 ? 0.4320 0.4345 0.5081 0.0927  0.0138  0.0099  238  GLU B CA  
4615  C  C   . GLU B 238 ? 0.4853 0.4833 0.5451 0.0828  0.0129  0.0114  238  GLU B C   
4616  O  O   . GLU B 238 ? 0.5167 0.5207 0.5733 0.0769  0.0158  0.0058  238  GLU B O   
4617  C  CB  . GLU B 238 ? 0.6561 0.6826 0.7427 0.0939  0.0131  0.0072  238  GLU B CB  
4618  C  CG  . GLU B 238 ? 0.8534 0.8910 0.9483 0.0990  0.0062  0.0151  238  GLU B CG  
4619  C  CD  . GLU B 238 ? 0.9699 1.0293 1.0836 0.1053  0.0080  0.0117  238  GLU B CD  
4620  O  OE1 . GLU B 238 ? 1.0889 1.1629 1.2119 0.1084  0.0019  0.0180  238  GLU B OE1 
4621  O  OE2 . GLU B 238 ? 0.9320 0.9951 1.0512 0.1073  0.0157  0.0026  238  GLU B OE2 
4622  N  N   . GLU B 239 ? 0.6874 0.6749 0.7366 0.0818  0.0090  0.0193  239  GLU B N   
4623  C  CA  . GLU B 239 ? 0.5854 0.5665 0.6190 0.0741  0.0088  0.0208  239  GLU B CA  
4624  C  C   . GLU B 239 ? 0.5006 0.4946 0.5302 0.0675  0.0061  0.0187  239  GLU B C   
4625  O  O   . GLU B 239 ? 0.6160 0.6214 0.6485 0.0676  0.0005  0.0213  239  GLU B O   
4626  C  CB  . GLU B 239 ? 0.7764 0.7467 0.7985 0.0755  0.0051  0.0296  239  GLU B CB  
4627  C  CG  . GLU B 239 ? 0.9714 0.9246 0.9925 0.0784  0.0094  0.0332  239  GLU B CG  
4628  C  CD  . GLU B 239 ? 1.0995 1.0435 1.1059 0.0790  0.0069  0.0427  239  GLU B CD  
4629  O  OE1 . GLU B 239 ? 1.0482 0.9795 1.0487 0.0776  0.0118  0.0457  239  GLU B OE1 
4630  O  OE2 . GLU B 239 ? 1.1380 1.0888 1.1387 0.0806  -0.0001 0.0471  239  GLU B OE2 
4631  N  N   . SER B 240 ? 0.4053 0.3974 0.4293 0.0615  0.0097  0.0147  240  SER B N   
4632  C  CA  . SER B 240 ? 0.2461 0.2462 0.2650 0.0547  0.0073  0.0141  240  SER B CA  
4633  C  C   . SER B 240 ? 0.4733 0.4600 0.4773 0.0508  0.0074  0.0161  240  SER B C   
4634  O  O   . SER B 240 ? 0.5703 0.5535 0.5713 0.0476  0.0113  0.0135  240  SER B O   
4635  C  CB  . SER B 240 ? 0.3408 0.3517 0.3658 0.0516  0.0115  0.0087  240  SER B CB  
4636  O  OG  . SER B 240 ? 0.4937 0.5123 0.5155 0.0449  0.0089  0.0100  240  SER B OG  
4637  N  N   . LEU B 241 ? 0.5772 0.5576 0.5717 0.0516  0.0028  0.0206  241  LEU B N   
4638  C  CA  . LEU B 241 ? 0.4049 0.3717 0.3845 0.0500  0.0041  0.0222  241  LEU B CA  
4639  C  C   . LEU B 241 ? 0.5123 0.4781 0.4834 0.0440  0.0022  0.0201  241  LEU B C   
4640  O  O   . LEU B 241 ? 0.4809 0.4559 0.4563 0.0400  -0.0019 0.0189  241  LEU B O   
4641  C  CB  . LEU B 241 ? 0.3259 0.2857 0.2960 0.0540  0.0008  0.0278  241  LEU B CB  
4642  C  CG  . LEU B 241 ? 0.4033 0.3614 0.3819 0.0605  0.0023  0.0317  241  LEU B CG  
4643  C  CD1 . LEU B 241 ? 0.3943 0.3467 0.3617 0.0644  -0.0020 0.0390  241  LEU B CD1 
4644  C  CD2 . LEU B 241 ? 0.1321 0.0818 0.1151 0.0610  0.0103  0.0304  241  LEU B CD2 
4645  N  N   . THR B 242 ? 0.7386 0.6927 0.6985 0.0436  0.0056  0.0202  242  THR B N   
4646  C  CA  . THR B 242 ? 0.4904 0.4399 0.4428 0.0393  0.0055  0.0178  242  THR B CA  
4647  C  C   . THR B 242 ? 0.5406 0.4805 0.4766 0.0393  0.0015  0.0181  242  THR B C   
4648  O  O   . THR B 242 ? 0.6319 0.5678 0.5602 0.0433  0.0012  0.0210  242  THR B O   
4649  C  CB  . THR B 242 ? 0.5630 0.5072 0.5161 0.0401  0.0128  0.0172  242  THR B CB  
4650  O  OG1 . THR B 242 ? 0.5223 0.4748 0.4855 0.0370  0.0140  0.0152  242  THR B OG1 
4651  C  CG2 . THR B 242 ? 0.4642 0.3970 0.4041 0.0402  0.0145  0.0167  242  THR B CG2 
4652  N  N   . PRO B 243 ? 0.5100 0.4457 0.4399 0.0349  -0.0018 0.0151  243  PRO B N   
4653  C  CA  . PRO B 243 ? 0.5299 0.4548 0.4419 0.0350  -0.0055 0.0132  243  PRO B CA  
4654  C  C   . PRO B 243 ? 0.4811 0.3961 0.3814 0.0407  0.0016  0.0144  243  PRO B C   
4655  O  O   . PRO B 243 ? 0.5012 0.4103 0.3861 0.0432  -0.0001 0.0148  243  PRO B O   
4656  C  CB  . PRO B 243 ? 0.5460 0.4642 0.4556 0.0298  -0.0075 0.0090  243  PRO B CB  
4657  C  CG  . PRO B 243 ? 0.6062 0.5363 0.5331 0.0253  -0.0081 0.0105  243  PRO B CG  
4658  C  CD  . PRO B 243 ? 0.6496 0.5891 0.5875 0.0294  -0.0024 0.0133  243  PRO B CD  
4659  N  N   . ASP B 244 ? 0.5296 0.4444 0.4376 0.0424  0.0095  0.0154  244  ASP B N   
4660  C  CA  . ASP B 244 ? 0.5798 0.4877 0.4802 0.0472  0.0173  0.0172  244  ASP B CA  
4661  C  C   . ASP B 244 ? 0.5822 0.4948 0.4906 0.0499  0.0211  0.0226  244  ASP B C   
4662  O  O   . ASP B 244 ? 0.6343 0.5463 0.5481 0.0516  0.0285  0.0246  244  ASP B O   
4663  C  CB  . ASP B 244 ? 0.4912 0.3961 0.3958 0.0473  0.0234  0.0153  244  ASP B CB  
4664  C  CG  . ASP B 244 ? 0.5818 0.4757 0.4732 0.0475  0.0225  0.0105  244  ASP B CG  
4665  O  OD1 . ASP B 244 ? 0.6704 0.5563 0.5469 0.0516  0.0261  0.0095  244  ASP B OD1 
4666  O  OD2 . ASP B 244 ? 0.7233 0.6159 0.6189 0.0436  0.0184  0.0078  244  ASP B OD2 
4667  N  N   . ASP B 245 ? 0.4948 0.4119 0.4052 0.0505  0.0157  0.0252  245  ASP B N   
4668  C  CA  . ASP B 245 ? 0.5451 0.4645 0.4646 0.0534  0.0188  0.0304  245  ASP B CA  
4669  C  C   . ASP B 245 ? 0.5571 0.4689 0.4673 0.0569  0.0255  0.0359  245  ASP B C   
4670  O  O   . ASP B 245 ? 0.6447 0.5560 0.5650 0.0576  0.0315  0.0391  245  ASP B O   
4671  C  CB  . ASP B 245 ? 0.3057 0.2310 0.2297 0.0549  0.0118  0.0331  245  ASP B CB  
4672  C  CG  . ASP B 245 ? 0.6442 0.5716 0.5837 0.0574  0.0148  0.0361  245  ASP B CG  
4673  O  OD1 . ASP B 245 ? 0.8522 0.7829 0.8045 0.0554  0.0183  0.0322  245  ASP B OD1 
4674  O  OD2 . ASP B 245 ? 0.6528 0.5777 0.5913 0.0615  0.0137  0.0423  245  ASP B OD2 
4675  N  N   . ARG B 246 ? 0.3615 0.2678 0.2523 0.0587  0.0247  0.0368  246  ARG B N   
4676  C  CA  . ARG B 246 ? 0.5833 0.4840 0.4634 0.0622  0.0319  0.0429  246  ARG B CA  
4677  C  C   . ARG B 246 ? 0.5997 0.5000 0.4887 0.0616  0.0417  0.0424  246  ARG B C   
4678  O  O   . ARG B 246 ? 0.6337 0.5344 0.5328 0.0619  0.0477  0.0481  246  ARG B O   
4679  C  CB  . ARG B 246 ? 0.6145 0.5099 0.4694 0.0642  0.0302  0.0416  246  ARG B CB  
4680  C  CG  . ARG B 246 ? 0.6815 0.5790 0.5272 0.0641  0.0188  0.0417  246  ARG B CG  
4681  C  CD  . ARG B 246 ? 0.7901 0.6820 0.6110 0.0645  0.0154  0.0366  246  ARG B CD  
4682  N  NE  . ARG B 246 ? 1.0815 0.9711 0.8824 0.0688  0.0165  0.0434  246  ARG B NE  
4683  C  CZ  . ARG B 246 ? 1.2674 1.1517 1.0422 0.0704  0.0154  0.0397  246  ARG B CZ  
4684  N  NH1 . ARG B 246 ? 1.2822 1.1609 1.0489 0.0680  0.0131  0.0283  246  ARG B NH1 
4685  N  NH2 . ARG B 246 ? 1.3842 1.2680 1.1401 0.0744  0.0167  0.0473  246  ARG B NH2 
4686  N  N   . VAL B 247 ? 0.3917 0.2912 0.2785 0.0605  0.0427  0.0358  247  VAL B N   
4687  C  CA  . VAL B 247 ? 0.4982 0.3993 0.3945 0.0606  0.0509  0.0353  247  VAL B CA  
4688  C  C   . VAL B 247 ? 0.4548 0.3624 0.3733 0.0576  0.0520  0.0369  247  VAL B C   
4689  O  O   . VAL B 247 ? 0.5873 0.4967 0.5146 0.0575  0.0590  0.0409  247  VAL B O   
4690  C  CB  . VAL B 247 ? 0.4757 0.3749 0.3696 0.0601  0.0498  0.0281  247  VAL B CB  
4691  C  CG1 . VAL B 247 ? 0.3711 0.2753 0.2806 0.0598  0.0559  0.0281  247  VAL B CG1 
4692  C  CG2 . VAL B 247 ? 0.4496 0.3404 0.3218 0.0638  0.0516  0.0253  247  VAL B CG2 
4693  N  N   . PHE B 248 ? 0.5362 0.4478 0.4638 0.0548  0.0451  0.0335  248  PHE B N   
4694  C  CA  . PHE B 248 ? 0.4167 0.3342 0.3631 0.0522  0.0456  0.0328  248  PHE B CA  
4695  C  C   . PHE B 248 ? 0.4882 0.4032 0.4410 0.0529  0.0486  0.0386  248  PHE B C   
4696  O  O   . PHE B 248 ? 0.4168 0.3338 0.3836 0.0506  0.0523  0.0389  248  PHE B O   
4697  C  CB  . PHE B 248 ? 0.4213 0.3445 0.3741 0.0499  0.0384  0.0280  248  PHE B CB  
4698  C  CG  . PHE B 248 ? 0.5076 0.4357 0.4643 0.0473  0.0374  0.0234  248  PHE B CG  
4699  C  CD1 . PHE B 248 ? 0.5733 0.5065 0.5417 0.0455  0.0407  0.0223  248  PHE B CD1 
4700  C  CD2 . PHE B 248 ? 0.3275 0.2550 0.2765 0.0462  0.0328  0.0208  248  PHE B CD2 
4701  C  CE1 . PHE B 248 ? 0.4931 0.4314 0.4646 0.0436  0.0394  0.0196  248  PHE B CE1 
4702  C  CE2 . PHE B 248 ? 0.3760 0.3068 0.3289 0.0438  0.0321  0.0183  248  PHE B CE2 
4703  C  CZ  . PHE B 248 ? 0.2099 0.1465 0.1736 0.0430  0.0354  0.0182  248  PHE B CZ  
4704  N  N   . LYS B 249 ? 0.4852 0.3953 0.4276 0.0558  0.0465  0.0434  249  LYS B N   
4705  C  CA  . LYS B 249 ? 0.4681 0.3735 0.4151 0.0571  0.0489  0.0509  249  LYS B CA  
4706  C  C   . LYS B 249 ? 0.5033 0.4056 0.4480 0.0571  0.0581  0.0574  249  LYS B C   
4707  O  O   . LYS B 249 ? 0.4680 0.3673 0.4239 0.0557  0.0621  0.0629  249  LYS B O   
4708  C  CB  . LYS B 249 ? 0.4537 0.3562 0.3894 0.0609  0.0431  0.0554  249  LYS B CB  
4709  C  CG  . LYS B 249 ? 0.3103 0.2146 0.2590 0.0619  0.0373  0.0542  249  LYS B CG  
4710  C  CD  . LYS B 249 ? 0.4400 0.3456 0.3796 0.0657  0.0295  0.0574  249  LYS B CD  
4711  C  CE  . LYS B 249 ? 0.5463 0.4559 0.5023 0.0676  0.0248  0.0553  249  LYS B CE  
4712  N  NZ  . LYS B 249 ? 0.7325 0.6487 0.6844 0.0705  0.0159  0.0562  249  LYS B NZ  
4713  N  N   . GLN B 250 ? 0.5095 0.4124 0.4403 0.0586  0.0617  0.0567  250  GLN B N   
4714  C  CA  . GLN B 250 ? 0.5024 0.4057 0.4324 0.0589  0.0718  0.0622  250  GLN B CA  
4715  C  C   . GLN B 250 ? 0.5601 0.4698 0.5108 0.0549  0.0757  0.0594  250  GLN B C   
4716  O  O   . GLN B 250 ? 0.5100 0.4211 0.4719 0.0526  0.0824  0.0653  250  GLN B O   
4717  C  CB  . GLN B 250 ? 0.4563 0.3587 0.3659 0.0628  0.0751  0.0604  250  GLN B CB  
4718  C  CG  . GLN B 250 ? 0.5325 0.4370 0.4398 0.0644  0.0871  0.0669  250  GLN B CG  
4719  C  CD  . GLN B 250 ? 0.5783 0.4801 0.4605 0.0697  0.0908  0.0657  250  GLN B CD  
4720  O  OE1 . GLN B 250 ? 0.8068 0.7032 0.6698 0.0719  0.0851  0.0653  250  GLN B OE1 
4721  N  NE2 . GLN B 250 ? 0.5529 0.4588 0.4353 0.0721  0.1002  0.0646  250  GLN B NE2 
4722  N  N   . LEU B 251 ? 0.4282 0.3425 0.3844 0.0536  0.0710  0.0509  251  LEU B N   
4723  C  CA  . LEU B 251 ? 0.4098 0.3319 0.3845 0.0499  0.0730  0.0481  251  LEU B CA  
4724  C  C   . LEU B 251 ? 0.4508 0.3725 0.4422 0.0455  0.0718  0.0494  251  LEU B C   
4725  O  O   . LEU B 251 ? 0.4923 0.4169 0.4968 0.0423  0.0771  0.0531  251  LEU B O   
4726  C  CB  . LEU B 251 ? 0.5407 0.4674 0.5164 0.0495  0.0672  0.0401  251  LEU B CB  
4727  C  CG  . LEU B 251 ? 0.5753 0.5003 0.5371 0.0535  0.0684  0.0380  251  LEU B CG  
4728  C  CD1 . LEU B 251 ? 0.5354 0.4628 0.4983 0.0524  0.0618  0.0316  251  LEU B CD1 
4729  C  CD2 . LEU B 251 ? 0.4662 0.3954 0.4318 0.0557  0.0774  0.0411  251  LEU B CD2 
4730  N  N   . ALA B 252 ? 0.5719 0.4902 0.5638 0.0454  0.0650  0.0460  252  ALA B N   
4731  C  CA  . ALA B 252 ? 0.5638 0.4792 0.5706 0.0422  0.0634  0.0453  252  ALA B CA  
4732  C  C   . ALA B 252 ? 0.6322 0.5405 0.6435 0.0412  0.0694  0.0548  252  ALA B C   
4733  O  O   . ALA B 252 ? 0.5824 0.4901 0.6100 0.0363  0.0715  0.0552  252  ALA B O   
4734  C  CB  . ALA B 252 ? 0.3311 0.2434 0.3355 0.0445  0.0566  0.0415  252  ALA B CB  
4735  N  N   . HIS B 253 ? 0.5030 0.4058 0.4992 0.0454  0.0717  0.0627  253  HIS B N   
4736  C  CA  . HIS B 253 ? 0.4907 0.3870 0.4886 0.0447  0.0781  0.0740  253  HIS B CA  
4737  C  C   . HIS B 253 ? 0.5462 0.4492 0.5524 0.0409  0.0869  0.0778  253  HIS B C   
4738  O  O   . HIS B 253 ? 0.6805 0.5804 0.6993 0.0367  0.0919  0.0850  253  HIS B O   
4739  C  CB  . HIS B 253 ? 0.4489 0.3400 0.4256 0.0504  0.0785  0.0821  253  HIS B CB  
4740  C  CG  . HIS B 253 ? 0.4827 0.3653 0.4586 0.0532  0.0722  0.0851  253  HIS B CG  
4741  N  ND1 . HIS B 253 ? 0.3862 0.2695 0.3493 0.0578  0.0645  0.0820  253  HIS B ND1 
4742  C  CD2 . HIS B 253 ? 0.5707 0.4439 0.5590 0.0523  0.0722  0.0910  253  HIS B CD2 
4743  C  CE1 . HIS B 253 ? 0.5576 0.4341 0.5256 0.0604  0.0602  0.0862  253  HIS B CE1 
4744  N  NE2 . HIS B 253 ? 0.6496 0.5186 0.6324 0.0575  0.0648  0.0916  253  HIS B NE2 
4745  N  N   . THR B 254 ? 0.4269 0.3391 0.4278 0.0424  0.0889  0.0734  254  THR B N   
4746  C  CA  . THR B 254 ? 0.4825 0.4034 0.4927 0.0401  0.0977  0.0773  254  THR B CA  
4747  C  C   . THR B 254 ? 0.3512 0.2762 0.3869 0.0325  0.0966  0.0752  254  THR B C   
4748  O  O   . THR B 254 ? 0.4032 0.3312 0.4522 0.0280  0.1034  0.0824  254  THR B O   
4749  C  CB  . THR B 254 ? 0.4484 0.3783 0.4516 0.0439  0.0994  0.0718  254  THR B CB  
4750  O  OG1 . THR B 254 ? 0.4830 0.4074 0.4616 0.0504  0.0992  0.0716  254  THR B OG1 
4751  C  CG2 . THR B 254 ? 0.2681 0.2086 0.2821 0.0430  0.1095  0.0770  254  THR B CG2 
4752  N  N   . TYR B 255 ? 0.2107 0.1361 0.2528 0.0306  0.0880  0.0653  255  TYR B N   
4753  C  CA  . TYR B 255 ? 0.3116 0.2411 0.3756 0.0232  0.0856  0.0609  255  TYR B CA  
4754  C  C   . TYR B 255 ? 0.3529 0.2698 0.4270 0.0189  0.0851  0.0644  255  TYR B C   
4755  O  O   . TYR B 255 ? 0.5059 0.4234 0.5974 0.0121  0.0884  0.0682  255  TYR B O   
4756  C  CB  . TYR B 255 ? 0.2126 0.1476 0.2779 0.0229  0.0770  0.0489  255  TYR B CB  
4757  C  CG  . TYR B 255 ? 0.4970 0.4406 0.5825 0.0155  0.0745  0.0438  255  TYR B CG  
4758  C  CD1 . TYR B 255 ? 0.5919 0.5281 0.6913 0.0092  0.0724  0.0418  255  TYR B CD1 
4759  C  CD2 . TYR B 255 ? 0.2916 0.2505 0.3829 0.0147  0.0737  0.0410  255  TYR B CD2 
4760  C  CE1 . TYR B 255 ? 0.5054 0.4495 0.6229 0.0015  0.0691  0.0361  255  TYR B CE1 
4761  C  CE2 . TYR B 255 ? 0.2588 0.2273 0.3686 0.0075  0.0702  0.0366  255  TYR B CE2 
4762  C  CZ  . TYR B 255 ? 0.4508 0.4121 0.5731 0.0005  0.0676  0.0336  255  TYR B CZ  
4763  O  OH  . TYR B 255 ? 0.4732 0.4438 0.6133 -0.0075 0.0630  0.0279  255  TYR B OH  
4764  N  N   . SER B 256 ? 0.4497 0.3551 0.5143 0.0229  0.0807  0.0633  256  SER B N   
4765  C  CA  . SER B 256 ? 0.4414 0.3326 0.5152 0.0205  0.0800  0.0668  256  SER B CA  
4766  C  C   . SER B 256 ? 0.6216 0.5074 0.6975 0.0186  0.0885  0.0817  256  SER B C   
4767  O  O   . SER B 256 ? 0.5666 0.4471 0.6604 0.0115  0.0908  0.0852  256  SER B O   
4768  C  CB  . SER B 256 ? 0.3756 0.2574 0.4377 0.0273  0.0744  0.0647  256  SER B CB  
4769  O  OG  . SER B 256 ? 0.7076 0.5752 0.7813 0.0259  0.0725  0.0652  256  SER B OG  
4770  N  N   . ASP B 257 ? 0.6631 0.5505 0.7204 0.0244  0.0931  0.0903  257  ASP B N   
4771  C  CA  . ASP B 257 ? 0.4909 0.3741 0.5454 0.0239  0.1019  0.1058  257  ASP B CA  
4772  C  C   . ASP B 257 ? 0.5486 0.4397 0.6229 0.0156  0.1095  0.1105  257  ASP B C   
4773  O  O   . ASP B 257 ? 0.5870 0.4716 0.6697 0.0112  0.1155  0.1227  257  ASP B O   
4774  C  CB  . ASP B 257 ? 0.4515 0.3395 0.4807 0.0313  0.1061  0.1114  257  ASP B CB  
4775  C  CG  . ASP B 257 ? 0.8176 0.6959 0.8277 0.0384  0.1000  0.1134  257  ASP B CG  
4776  O  OD1 . ASP B 257 ? 0.9450 0.8138 0.9625 0.0387  0.0928  0.1101  257  ASP B OD1 
4777  O  OD2 . ASP B 257 ? 0.8909 0.7715 0.8786 0.0441  0.1022  0.1177  257  ASP B OD2 
4778  N  N   . ASN B 258 ? 0.4737 0.3795 0.5562 0.0132  0.1089  0.1016  258  ASN B N   
4779  C  CA  . ASN B 258 ? 0.5895 0.5071 0.6936 0.0053  0.1148  0.1048  258  ASN B CA  
4780  C  C   . ASN B 258 ? 0.6293 0.5447 0.7581 -0.0044 0.1083  0.0970  258  ASN B C   
4781  O  O   . ASN B 258 ? 0.5606 0.4875 0.7102 -0.0122 0.1109  0.0979  258  ASN B O   
4782  C  CB  . ASN B 258 ? 0.5426 0.4789 0.6433 0.0089  0.1179  0.1007  258  ASN B CB  
4783  C  CG  . ASN B 258 ? 0.5594 0.5003 0.6428 0.0155  0.1287  0.1107  258  ASN B CG  
4784  O  OD1 . ASN B 258 ? 0.5433 0.4924 0.6363 0.0124  0.1389  0.1209  258  ASN B OD1 
4785  N  ND2 . ASN B 258 ? 0.4376 0.3740 0.4955 0.0244  0.1264  0.1072  258  ASN B ND2 
4786  N  N   . HIS B 259 ? 0.6875 0.5890 0.8145 -0.0036 0.0997  0.0890  259  HIS B N   
4787  C  CA  . HIS B 259 ? 0.6371 0.5343 0.7841 -0.0119 0.0930  0.0794  259  HIS B CA  
4788  C  C   . HIS B 259 ? 0.6741 0.5493 0.8288 -0.0151 0.0926  0.0843  259  HIS B C   
4789  O  O   . HIS B 259 ? 0.6620 0.5233 0.8053 -0.0084 0.0889  0.0826  259  HIS B O   
4790  C  CB  . HIS B 259 ? 0.6332 0.5335 0.7728 -0.0082 0.0836  0.0636  259  HIS B CB  
4791  C  CG  . HIS B 259 ? 0.6483 0.5484 0.8053 -0.0163 0.0765  0.0514  259  HIS B CG  
4792  N  ND1 . HIS B 259 ? 0.5646 0.4478 0.7353 -0.0224 0.0746  0.0499  259  HIS B ND1 
4793  C  CD2 . HIS B 259 ? 0.5579 0.4719 0.7198 -0.0193 0.0703  0.0396  259  HIS B CD2 
4794  C  CE1 . HIS B 259 ? 0.5215 0.4082 0.7039 -0.0289 0.0675  0.0364  259  HIS B CE1 
4795  N  NE2 . HIS B 259 ? 0.4739 0.3802 0.6507 -0.0272 0.0647  0.0303  259  HIS B NE2 
4796  N  N   . PRO B 260 ? 0.7989 0.6711 0.9751 -0.0254 0.0964  0.0909  260  PRO B N   
4797  C  CA  . PRO B 260 ? 0.7533 0.6040 0.9394 -0.0297 0.0985  0.1003  260  PRO B CA  
4798  C  C   . PRO B 260 ? 0.6542 0.4842 0.8386 -0.0262 0.0903  0.0904  260  PRO B C   
4799  O  O   . PRO B 260 ? 0.6088 0.4195 0.7911 -0.0230 0.0917  0.0994  260  PRO B O   
4800  C  CB  . PRO B 260 ? 0.6132 0.4684 0.8275 -0.0440 0.0999  0.1008  260  PRO B CB  
4801  C  CG  . PRO B 260 ? 0.7280 0.6102 0.9434 -0.0448 0.1039  0.1014  260  PRO B CG  
4802  C  CD  . PRO B 260 ? 0.7232 0.6142 0.9181 -0.0345 0.0982  0.0894  260  PRO B CD  
4803  N  N   . ILE B 261 ? 0.6695 0.5043 0.8547 -0.0260 0.0821  0.0723  261  ILE B N   
4804  C  CA  . ILE B 261 ? 0.6587 0.4761 0.8440 -0.0226 0.0750  0.0606  261  ILE B CA  
4805  C  C   . ILE B 261 ? 0.5461 0.3667 0.7094 -0.0098 0.0718  0.0556  261  ILE B C   
4806  O  O   . ILE B 261 ? 0.5996 0.4046 0.7588 -0.0029 0.0696  0.0553  261  ILE B O   
4807  C  CB  . ILE B 261 ? 0.7142 0.5342 0.9140 -0.0311 0.0679  0.0428  261  ILE B CB  
4808  C  CG1 . ILE B 261 ? 0.6439 0.4570 0.8685 -0.0450 0.0697  0.0472  261  ILE B CG1 
4809  C  CG2 . ILE B 261 ? 0.6576 0.4633 0.8532 -0.0252 0.0611  0.0276  261  ILE B CG2 
4810  C  CD1 . ILE B 261 ? 0.7201 0.5398 0.9593 -0.0551 0.0622  0.0302  261  ILE B CD1 
4811  N  N   . MET B 262 ? 0.4606 0.3016 0.6115 -0.0066 0.0714  0.0522  262  MET B N   
4812  C  CA  . MET B 262 ? 0.5276 0.3736 0.6597 0.0037  0.0679  0.0468  262  MET B CA  
4813  C  C   . MET B 262 ? 0.5901 0.4284 0.7081 0.0120  0.0711  0.0602  262  MET B C   
4814  O  O   . MET B 262 ? 0.4931 0.3266 0.6017 0.0202  0.0673  0.0575  262  MET B O   
4815  C  CB  . MET B 262 ? 0.4118 0.2795 0.5353 0.0041  0.0672  0.0421  262  MET B CB  
4816  C  CG  . MET B 262 ? 0.3376 0.2112 0.4426 0.0131  0.0638  0.0375  262  MET B CG  
4817  S  SD  . MET B 262 ? 0.4101 0.3063 0.5084 0.0123  0.0633  0.0331  262  MET B SD  
4818  C  CE  . MET B 262 ? 0.2504 0.1525 0.3654 0.0038  0.0577  0.0191  262  MET B CE  
4819  N  N   . ARG B 263 ? 0.6626 0.5015 0.7797 0.0097  0.0782  0.0751  263  ARG B N   
4820  C  CA  . ARG B 263 ? 0.6211 0.4528 0.7246 0.0162  0.0820  0.0902  263  ARG B CA  
4821  C  C   . ARG B 263 ? 0.7046 0.5160 0.8113 0.0208  0.0787  0.0936  263  ARG B C   
4822  O  O   . ARG B 263 ? 0.7624 0.5695 0.8551 0.0289  0.0782  0.1028  263  ARG B O   
4823  C  CB  . ARG B 263 ? 0.7137 0.5475 0.8215 0.0104  0.0914  0.1053  263  ARG B CB  
4824  C  CG  . ARG B 263 ? 0.8928 0.7232 0.9825 0.0166  0.0965  0.1221  263  ARG B CG  
4825  C  CD  . ARG B 263 ? 0.9770 0.8150 1.0693 0.0111  0.1073  0.1356  263  ARG B CD  
4826  N  NE  . ARG B 263 ? 1.0839 0.9135 1.2015 0.0005  0.1105  0.1404  263  ARG B NE  
4827  C  CZ  . ARG B 263 ? 0.9542 0.7957 1.0869 -0.0084 0.1172  0.1435  263  ARG B CZ  
4828  N  NH1 . ARG B 263 ? 0.7473 0.6093 0.8722 -0.0068 0.1221  0.1421  263  ARG B NH1 
4829  N  NH2 . ARG B 263 ? 0.8156 0.6482 0.9726 -0.0191 0.1189  0.1477  263  ARG B NH2 
4830  N  N   . LYS B 264 ? 0.8957 0.6945 1.0210 0.0160  0.0759  0.0858  264  LYS B N   
4831  C  CA  . LYS B 264 ? 0.9353 0.7122 1.0675 0.0203  0.0734  0.0888  264  LYS B CA  
4832  C  C   . LYS B 264 ? 0.8778 0.6544 1.0021 0.0311  0.0668  0.0788  264  LYS B C   
4833  O  O   . LYS B 264 ? 0.8967 0.6645 1.0151 0.0398  0.0654  0.0877  264  LYS B O   
4834  C  CB  . LYS B 264 ? 0.9029 0.6643 1.0585 0.0109  0.0730  0.0830  264  LYS B CB  
4835  C  CG  . LYS B 264 ? 0.8539 0.6165 1.0211 -0.0007 0.0797  0.0942  264  LYS B CG  
4836  C  CD  . LYS B 264 ? 0.9949 0.7395 1.1865 -0.0108 0.0783  0.0890  264  LYS B CD  
4837  C  CE  . LYS B 264 ? 1.0434 0.7875 1.2487 -0.0225 0.0856  0.1040  264  LYS B CE  
4838  N  NZ  . LYS B 264 ? 1.1796 0.9167 1.3751 -0.0174 0.0922  0.1267  264  LYS B NZ  
4839  N  N   . GLY B 265 ? 0.7928 0.5804 0.9176 0.0305  0.0627  0.0612  265  GLY B N   
4840  C  CA  . GLY B 265 ? 0.6587 0.4521 0.7751 0.0400  0.0576  0.0520  265  GLY B CA  
4841  C  C   . GLY B 265 ? 0.7065 0.4857 0.8354 0.0438  0.0542  0.0407  265  GLY B C   
4842  O  O   . GLY B 265 ? 0.7866 0.5702 0.9112 0.0526  0.0508  0.0338  265  GLY B O   
4843  N  N   . ASN B 266 ? 0.6618 0.4238 0.8069 0.0370  0.0554  0.0382  266  ASN B N   
4844  C  CA  . ASN B 266 ? 0.7636 0.5080 0.9212 0.0406  0.0527  0.0265  266  ASN B CA  
4845  C  C   . ASN B 266 ? 0.7157 0.4581 0.8841 0.0312  0.0509  0.0085  266  ASN B C   
4846  O  O   . ASN B 266 ? 0.8373 0.5585 1.0199 0.0293  0.0500  0.0016  266  ASN B O   
4847  C  CB  . ASN B 266 ? 0.8000 0.5185 0.9680 0.0437  0.0544  0.0401  266  ASN B CB  
4848  C  CG  . ASN B 266 ? 0.9147 0.6248 1.0902 0.0325  0.0588  0.0541  266  ASN B CG  
4849  O  OD1 . ASN B 266 ? 0.9509 0.6759 1.1247 0.0229  0.0608  0.0536  266  ASN B OD1 
4850  N  ND2 . ASN B 266 ? 0.8879 0.5746 1.0731 0.0338  0.0607  0.0676  266  ASN B ND2 
4851  N  N   . ASN B 267 ? 0.5097 0.2738 0.6710 0.0256  0.0498  0.0005  267  ASN B N   
4852  C  CA  . ASN B 267 ? 0.5252 0.2916 0.6949 0.0155  0.0472  -0.0150 267  ASN B CA  
4853  C  C   . ASN B 267 ? 0.5201 0.2924 0.6847 0.0207  0.0434  -0.0348 267  ASN B C   
4854  O  O   . ASN B 267 ? 0.5659 0.3471 0.7198 0.0311  0.0434  -0.0352 267  ASN B O   
4855  C  CB  . ASN B 267 ? 0.6371 0.4251 0.8029 0.0068  0.0479  -0.0112 267  ASN B CB  
4856  C  CG  . ASN B 267 ? 0.6780 0.4671 0.8422 0.0054  0.0533  0.0096  267  ASN B CG  
4857  O  OD1 . ASN B 267 ? 0.5825 0.3556 0.7586 0.0006  0.0563  0.0198  267  ASN B OD1 
4858  N  ND2 . ASN B 267 ? 0.6844 0.4919 0.8333 0.0098  0.0549  0.0161  267  ASN B ND2 
4859  N  N   . CYS B 268 ? 0.6062 0.3746 0.7786 0.0131  0.0401  -0.0510 268  CYS B N   
4860  C  CA  . CYS B 268 ? 0.7170 0.4905 0.8838 0.0171  0.0369  -0.0717 268  CYS B CA  
4861  C  C   . CYS B 268 ? 0.8645 0.6317 1.0270 0.0319  0.0386  -0.0749 268  CYS B C   
4862  O  O   . CYS B 268 ? 0.8382 0.6219 0.9897 0.0381  0.0381  -0.0844 268  CYS B O   
4863  C  CB  . CYS B 268 ? 0.5148 0.3172 0.6682 0.0143  0.0347  -0.0771 268  CYS B CB  
4864  S  SG  . CYS B 268 ? 0.8347 0.6542 0.9865 0.0061  0.0361  -0.0597 268  CYS B SG  
4865  N  N   . ASN B 269 ? 0.9089 0.6534 1.0811 0.0376  0.0407  -0.0661 269  ASN B N   
4866  C  CA  . ASN B 269 ? 0.9657 0.7045 1.1372 0.0525  0.0421  -0.0673 269  ASN B CA  
4867  C  C   . ASN B 269 ? 0.8699 0.6296 1.0291 0.0609  0.0431  -0.0551 269  ASN B C   
4868  O  O   . ASN B 269 ? 0.7066 0.4671 0.8656 0.0731  0.0438  -0.0555 269  ASN B O   
4869  C  CB  . ASN B 269 ? 0.9674 0.7060 1.1382 0.0574  0.0412  -0.0908 269  ASN B CB  
4870  C  CG  . ASN B 269 ? 1.0261 0.7377 1.2102 0.0520  0.0397  -0.1043 269  ASN B CG  
4871  O  OD1 . ASN B 269 ? 0.9703 0.6830 1.1517 0.0506  0.0381  -0.1253 269  ASN B OD1 
4872  N  ND2 . ASN B 269 ? 1.0935 0.7805 1.2913 0.0486  0.0403  -0.0922 269  ASN B ND2 
4873  N  N   . ASP B 270 ? 0.7683 0.5449 0.9182 0.0542  0.0431  -0.0447 270  ASP B N   
4874  C  CA  . ASP B 270 ? 0.5826 0.3779 0.7201 0.0602  0.0434  -0.0339 270  ASP B CA  
4875  C  C   . ASP B 270 ? 0.7474 0.5333 0.8853 0.0628  0.0447  -0.0135 270  ASP B C   
4876  O  O   . ASP B 270 ? 0.7029 0.4729 0.8485 0.0568  0.0462  -0.0052 270  ASP B O   
4877  C  CB  . ASP B 270 ? 0.6601 0.4779 0.7862 0.0524  0.0427  -0.0346 270  ASP B CB  
4878  C  CG  . ASP B 270 ? 0.8098 0.6393 0.9332 0.0492  0.0409  -0.0529 270  ASP B CG  
4879  O  OD1 . ASP B 270 ? 0.8990 0.7274 1.0236 0.0563  0.0409  -0.0649 270  ASP B OD1 
4880  O  OD2 . ASP B 270 ? 0.8060 0.6465 0.9257 0.0400  0.0397  -0.0551 270  ASP B OD2 
4881  N  N   . SER B 271 ? 0.8437 0.6405 0.9730 0.0713  0.0438  -0.0051 271  SER B N   
4882  C  CA  . SER B 271 ? 0.7096 0.5016 0.8347 0.0742  0.0442  0.0144  271  SER B CA  
4883  C  C   . SER B 271 ? 0.7097 0.5231 0.8184 0.0736  0.0431  0.0209  271  SER B C   
4884  O  O   . SER B 271 ? 0.8122 0.6387 0.9152 0.0806  0.0405  0.0197  271  SER B O   
4885  C  CB  . SER B 271 ? 0.7219 0.5033 0.8537 0.0866  0.0426  0.0199  271  SER B CB  
4886  O  OG  . SER B 271 ? 0.7423 0.5214 0.8674 0.0896  0.0420  0.0393  271  SER B OG  
4887  N  N   . PHE B 272 ? 0.6529 0.4696 0.7550 0.0651  0.0454  0.0275  272  PHE B N   
4888  C  CA  . PHE B 272 ? 0.4804 0.3144 0.5666 0.0641  0.0449  0.0328  272  PHE B CA  
4889  C  C   . PHE B 272 ? 0.4475 0.2756 0.5263 0.0634  0.0474  0.0498  272  PHE B C   
4890  O  O   . PHE B 272 ? 0.5904 0.4137 0.6720 0.0560  0.0516  0.0544  272  PHE B O   
4891  C  CB  . PHE B 272 ? 0.5924 0.4389 0.6760 0.0556  0.0460  0.0241  272  PHE B CB  
4892  C  CG  . PHE B 272 ? 0.6225 0.4790 0.7086 0.0560  0.0436  0.0082  272  PHE B CG  
4893  C  CD1 . PHE B 272 ? 0.6177 0.4719 0.7125 0.0498  0.0439  -0.0034 272  PHE B CD1 
4894  C  CD2 . PHE B 272 ? 0.3887 0.2579 0.4681 0.0622  0.0409  0.0051  272  PHE B CD2 
4895  C  CE1 . PHE B 272 ? 0.5368 0.4012 0.6312 0.0504  0.0420  -0.0177 272  PHE B CE1 
4896  C  CE2 . PHE B 272 ? 0.3775 0.2573 0.4583 0.0626  0.0397  -0.0082 272  PHE B CE2 
4897  C  CZ  . PHE B 272 ? 0.4862 0.3636 0.5732 0.0571  0.0405  -0.0198 272  PHE B CZ  
4898  N  N   . SER B 273 ? 0.6380 0.4681 0.7075 0.0708  0.0447  0.0593  273  SER B N   
4899  C  CA  . SER B 273 ? 0.6443 0.4696 0.7031 0.0713  0.0467  0.0761  273  SER B CA  
4900  C  C   . SER B 273 ? 0.7586 0.5930 0.8066 0.0641  0.0511  0.0778  273  SER B C   
4901  O  O   . SER B 273 ? 0.8469 0.6957 0.8853 0.0633  0.0494  0.0709  273  SER B O   
4902  C  CB  . SER B 273 ? 0.7914 0.6229 0.8386 0.0801  0.0413  0.0832  273  SER B CB  
4903  O  OG  . SER B 273 ? 0.8103 0.6396 0.8428 0.0806  0.0427  0.0985  273  SER B OG  
4904  N  N   . GLY B 274 ? 0.7193 0.5451 0.7703 0.0590  0.0570  0.0872  274  GLY B N   
4905  C  CA  . GLY B 274 ? 0.6384 0.4732 0.6814 0.0530  0.0625  0.0898  274  GLY B CA  
4906  C  C   . GLY B 274 ? 0.7259 0.5681 0.7799 0.0456  0.0637  0.0771  274  GLY B C   
4907  O  O   . GLY B 274 ? 0.7213 0.5725 0.7720 0.0410  0.0682  0.0780  274  GLY B O   
4908  N  N   . GLY B 275 ? 0.6729 0.5120 0.7399 0.0451  0.0598  0.0652  275  GLY B N   
4909  C  CA  . GLY B 275 ? 0.5199 0.3666 0.5962 0.0385  0.0594  0.0524  275  GLY B CA  
4910  C  C   . GLY B 275 ? 0.6132 0.4773 0.6782 0.0396  0.0569  0.0448  275  GLY B C   
4911  O  O   . GLY B 275 ? 0.6809 0.5547 0.7495 0.0341  0.0574  0.0383  275  GLY B O   
4912  N  N   . ILE B 276 ? 0.6154 0.4835 0.6674 0.0464  0.0537  0.0463  276  ILE B N   
4913  C  CA  . ILE B 276 ? 0.6573 0.5399 0.6997 0.0473  0.0507  0.0391  276  ILE B CA  
4914  C  C   . ILE B 276 ? 0.5881 0.4736 0.6294 0.0532  0.0453  0.0336  276  ILE B C   
4915  O  O   . ILE B 276 ? 0.5694 0.4463 0.6144 0.0583  0.0438  0.0373  276  ILE B O   
4916  C  CB  . ILE B 276 ? 0.6110 0.4989 0.6371 0.0485  0.0525  0.0465  276  ILE B CB  
4917  C  CG1 . ILE B 276 ? 0.5175 0.4011 0.5323 0.0550  0.0498  0.0544  276  ILE B CG1 
4918  C  CG2 . ILE B 276 ? 0.5692 0.4553 0.5971 0.0441  0.0594  0.0536  276  ILE B CG2 
4919  C  CD1 . ILE B 276 ? 0.4907 0.3796 0.4866 0.0566  0.0499  0.0586  276  ILE B CD1 
4920  N  N   . THR B 277 ? 0.4062 0.3046 0.4434 0.0526  0.0425  0.0255  277  THR B N   
4921  C  CA  . THR B 277 ? 0.5252 0.4301 0.5622 0.0575  0.0382  0.0207  277  THR B CA  
4922  C  C   . THR B 277 ? 0.6240 0.5431 0.6523 0.0559  0.0357  0.0169  277  THR B C   
4923  O  O   . THR B 277 ? 0.6247 0.5485 0.6493 0.0512  0.0372  0.0152  277  THR B O   
4924  C  CB  . THR B 277 ? 0.3599 0.2629 0.4101 0.0586  0.0379  0.0107  277  THR B CB  
4925  O  OG1 . THR B 277 ? 0.4785 0.3883 0.5300 0.0650  0.0349  0.0081  277  THR B OG1 
4926  C  CG2 . THR B 277 ? 0.2017 0.1134 0.2541 0.0529  0.0385  0.0005  277  THR B CG2 
4927  N  N   . ASN B 278 ? 0.6042 0.5302 0.6306 0.0600  0.0319  0.0164  278  ASN B N   
4928  C  CA  . ASN B 278 ? 0.4293 0.3686 0.4505 0.0580  0.0293  0.0126  278  ASN B CA  
4929  C  C   . ASN B 278 ? 0.5408 0.4883 0.5704 0.0569  0.0302  0.0029  278  ASN B C   
4930  O  O   . ASN B 278 ? 0.5982 0.5438 0.6372 0.0607  0.0308  -0.0014 278  ASN B O   
4931  C  CB  . ASN B 278 ? 0.3965 0.3414 0.4145 0.0621  0.0245  0.0165  278  ASN B CB  
4932  C  CG  . ASN B 278 ? 0.5618 0.5205 0.5769 0.0591  0.0216  0.0132  278  ASN B CG  
4933  O  OD1 . ASN B 278 ? 0.5704 0.5397 0.5919 0.0615  0.0190  0.0114  278  ASN B OD1 
4934  N  ND2 . ASN B 278 ? 0.3834 0.3424 0.3899 0.0540  0.0222  0.0130  278  ASN B ND2 
4935  N  N   . GLY B 279 ? 0.4149 0.3710 0.4406 0.0520  0.0304  -0.0007 279  GLY B N   
4936  C  CA  . GLY B 279 ? 0.1961 0.1620 0.2266 0.0506  0.0311  -0.0094 279  GLY B CA  
4937  C  C   . GLY B 279 ? 0.4691 0.4419 0.5058 0.0558  0.0305  -0.0127 279  GLY B C   
4938  O  O   . GLY B 279 ? 0.4910 0.4603 0.5357 0.0594  0.0323  -0.0187 279  GLY B O   
4939  N  N   . ALA B 280 ? 0.4069 0.3894 0.4408 0.0565  0.0279  -0.0089 280  ALA B N   
4940  C  CA  . ALA B 280 ? 0.3624 0.3566 0.4039 0.0610  0.0276  -0.0115 280  ALA B CA  
4941  C  C   . ALA B 280 ? 0.4571 0.4435 0.5081 0.0688  0.0280  -0.0118 280  ALA B C   
4942  O  O   . ALA B 280 ? 0.5420 0.5345 0.6020 0.0738  0.0303  -0.0183 280  ALA B O   
4943  C  CB  . ALA B 280 ? 0.3270 0.3318 0.3658 0.0593  0.0237  -0.0056 280  ALA B CB  
4944  N  N   . HIS B 281 ? 0.4454 0.4179 0.4941 0.0704  0.0263  -0.0045 281  HIS B N   
4945  C  CA  . HIS B 281 ? 0.3830 0.3458 0.4406 0.0781  0.0262  -0.0024 281  HIS B CA  
4946  C  C   . HIS B 281 ? 0.3787 0.3315 0.4442 0.0796  0.0305  -0.0110 281  HIS B C   
4947  O  O   . HIS B 281 ? 0.3801 0.3297 0.4562 0.0868  0.0315  -0.0144 281  HIS B O   
4948  C  CB  . HIS B 281 ? 0.5386 0.4884 0.5897 0.0786  0.0239  0.0086  281  HIS B CB  
4949  C  CG  . HIS B 281 ? 0.6138 0.5555 0.6732 0.0871  0.0224  0.0140  281  HIS B CG  
4950  N  ND1 . HIS B 281 ? 0.5901 0.5144 0.6559 0.0896  0.0253  0.0146  281  HIS B ND1 
4951  C  CD2 . HIS B 281 ? 0.6574 0.6063 0.7210 0.0937  0.0178  0.0195  281  HIS B CD2 
4952  C  CE1 . HIS B 281 ? 0.5211 0.4408 0.5941 0.0980  0.0229  0.0210  281  HIS B CE1 
4953  N  NE2 . HIS B 281 ? 0.6861 0.6216 0.7582 0.1010  0.0182  0.0240  281  HIS B NE2 
4954  N  N   . TRP B 282 ? 0.3591 0.3065 0.4202 0.0728  0.0325  -0.0147 282  TRP B N   
4955  C  CA  . TRP B 282 ? 0.3761 0.3159 0.4441 0.0726  0.0354  -0.0249 282  TRP B CA  
4956  C  C   . TRP B 282 ? 0.5448 0.4991 0.6160 0.0760  0.0370  -0.0355 282  TRP B C   
4957  O  O   . TRP B 282 ? 0.6063 0.5585 0.6869 0.0837  0.0385  -0.0403 282  TRP B O   
4958  C  CB  . TRP B 282 ? 0.5288 0.4663 0.5915 0.0638  0.0361  -0.0272 282  TRP B CB  
4959  C  CG  . TRP B 282 ? 0.6339 0.5629 0.7034 0.0619  0.0377  -0.0377 282  TRP B CG  
4960  C  CD1 . TRP B 282 ? 0.5527 0.4739 0.6312 0.0676  0.0391  -0.0461 282  TRP B CD1 
4961  C  CD2 . TRP B 282 ? 0.5455 0.4724 0.6140 0.0538  0.0376  -0.0415 282  TRP B CD2 
4962  N  NE1 . TRP B 282 ? 0.5305 0.4436 0.6125 0.0627  0.0395  -0.0560 282  TRP B NE1 
4963  C  CE2 . TRP B 282 ? 0.5042 0.4217 0.5806 0.0538  0.0383  -0.0530 282  TRP B CE2 
4964  C  CE3 . TRP B 282 ? 0.5500 0.4824 0.6127 0.0468  0.0369  -0.0366 282  TRP B CE3 
4965  C  CZ2 . TRP B 282 ? 0.4335 0.3481 0.5121 0.0460  0.0372  -0.0597 282  TRP B CZ2 
4966  C  CZ3 . TRP B 282 ? 0.4913 0.4223 0.5575 0.0400  0.0363  -0.0422 282  TRP B CZ3 
4967  C  CH2 . TRP B 282 ? 0.4510 0.3736 0.5250 0.0390  0.0361  -0.0536 282  TRP B CH2 
4968  N  N   . TYR B 283 ? 0.5131 0.4825 0.5766 0.0705  0.0371  -0.0385 283  TYR B N   
4969  C  CA  . TYR B 283 ? 0.5466 0.5344 0.6106 0.0728  0.0390  -0.0453 283  TYR B CA  
4970  C  C   . TYR B 283 ? 0.5713 0.5738 0.6253 0.0658  0.0379  -0.0417 283  TYR B C   
4971  O  O   . TYR B 283 ? 0.5186 0.5169 0.5657 0.0592  0.0365  -0.0398 283  TYR B O   
4972  C  CB  . TYR B 283 ? 0.3687 0.3553 0.4352 0.0744  0.0423  -0.0595 283  TYR B CB  
4973  C  CG  . TYR B 283 ? 0.4888 0.4697 0.5488 0.0664  0.0414  -0.0645 283  TYR B CG  
4974  C  CD1 . TYR B 283 ? 0.5455 0.5411 0.5958 0.0602  0.0409  -0.0659 283  TYR B CD1 
4975  C  CD2 . TYR B 283 ? 0.6287 0.5903 0.6937 0.0648  0.0407  -0.0670 283  TYR B CD2 
4976  C  CE1 . TYR B 283 ? 0.5654 0.5579 0.6111 0.0533  0.0391  -0.0699 283  TYR B CE1 
4977  C  CE2 . TYR B 283 ? 0.5949 0.5536 0.6565 0.0569  0.0392  -0.0714 283  TYR B CE2 
4978  C  CZ  . TYR B 283 ? 0.6344 0.6093 0.6864 0.0515  0.0381  -0.0731 283  TYR B CZ  
4979  O  OH  . TYR B 283 ? 0.6661 0.6399 0.7158 0.0440  0.0356  -0.0769 283  TYR B OH  
4980  N  N   . GLU B 284 ? 0.6049 0.6249 0.6598 0.0671  0.0385  -0.0403 284  GLU B N   
4981  C  CA  . GLU B 284 ? 0.5748 0.6072 0.6215 0.0603  0.0372  -0.0354 284  GLU B CA  
4982  C  C   . GLU B 284 ? 0.5343 0.5746 0.5738 0.0559  0.0394  -0.0422 284  GLU B C   
4983  O  O   . GLU B 284 ? 0.5661 0.6098 0.6070 0.0589  0.0427  -0.0525 284  GLU B O   
4984  C  CB  . GLU B 284 ? 0.5524 0.6017 0.6038 0.0618  0.0370  -0.0308 284  GLU B CB  
4985  C  CG  . GLU B 284 ? 0.6142 0.6583 0.6700 0.0640  0.0326  -0.0221 284  GLU B CG  
4986  C  CD  . GLU B 284 ? 0.4609 0.5228 0.5208 0.0620  0.0306  -0.0164 284  GLU B CD  
4987  O  OE1 . GLU B 284 ? 0.2549 0.3176 0.3208 0.0650  0.0266  -0.0110 284  GLU B OE1 
4988  O  OE2 . GLU B 284 ? 0.5460 0.6216 0.6032 0.0570  0.0326  -0.0168 284  GLU B OE2 
4989  N  N   . LEU B 285 ? 0.2584 0.3012 0.2896 0.0490  0.0373  -0.0365 285  LEU B N   
4990  C  CA  . LEU B 285 ? 0.3839 0.4373 0.4076 0.0448  0.0384  -0.0403 285  LEU B CA  
4991  C  C   . LEU B 285 ? 0.4439 0.5039 0.4619 0.0392  0.0362  -0.0303 285  LEU B C   
4992  O  O   . LEU B 285 ? 0.3904 0.4420 0.4090 0.0380  0.0335  -0.0227 285  LEU B O   
4993  C  CB  . LEU B 285 ? 0.4336 0.4766 0.4544 0.0424  0.0369  -0.0458 285  LEU B CB  
4994  C  CG  . LEU B 285 ? 0.3747 0.4048 0.3946 0.0388  0.0337  -0.0384 285  LEU B CG  
4995  C  CD1 . LEU B 285 ? 0.2793 0.3166 0.2916 0.0333  0.0316  -0.0332 285  LEU B CD1 
4996  C  CD2 . LEU B 285 ? 0.3429 0.3597 0.3676 0.0391  0.0334  -0.0442 285  LEU B CD2 
4997  N  N   . SER B 286 ? 0.5031 0.5772 0.5147 0.0358  0.0375  -0.0304 286  SER B N   
4998  C  CA  . SER B 286 ? 0.5495 0.6290 0.5565 0.0303  0.0357  -0.0203 286  SER B CA  
4999  C  C   . SER B 286 ? 0.4480 0.5294 0.4462 0.0261  0.0339  -0.0188 286  SER B C   
5000  O  O   . SER B 286 ? 0.5052 0.5924 0.4993 0.0267  0.0349  -0.0263 286  SER B O   
5001  C  CB  . SER B 286 ? 0.4665 0.5637 0.4760 0.0296  0.0387  -0.0171 286  SER B CB  
5002  O  OG  . SER B 286 ? 0.5456 0.6427 0.5653 0.0337  0.0393  -0.0176 286  SER B OG  
5003  N  N   . GLY B 287 ? 0.3589 0.4350 0.3545 0.0223  0.0309  -0.0094 287  GLY B N   
5004  C  CA  . GLY B 287 ? 0.2985 0.3775 0.2873 0.0191  0.0287  -0.0056 287  GLY B CA  
5005  C  C   . GLY B 287 ? 0.3473 0.4150 0.3371 0.0199  0.0261  -0.0084 287  GLY B C   
5006  O  O   . GLY B 287 ? 0.3188 0.3912 0.3047 0.0181  0.0239  -0.0078 287  GLY B O   
5007  N  N   . GLY B 288 ? 0.3993 0.4535 0.3950 0.0225  0.0264  -0.0106 288  GLY B N   
5008  C  CA  . GLY B 288 ? 0.3487 0.3923 0.3474 0.0230  0.0250  -0.0120 288  GLY B CA  
5009  C  C   . GLY B 288 ? 0.3489 0.3861 0.3464 0.0218  0.0230  -0.0035 288  GLY B C   
5010  O  O   . GLY B 288 ? 0.3273 0.3610 0.3223 0.0213  0.0227  0.0032  288  GLY B O   
5011  N  N   . MET B 289 ? 0.4394 0.4752 0.4399 0.0214  0.0217  -0.0042 289  MET B N   
5012  C  CA  . MET B 289 ? 0.4572 0.4874 0.4585 0.0218  0.0207  0.0031  289  MET B CA  
5013  C  C   . MET B 289 ? 0.4255 0.4409 0.4277 0.0243  0.0231  0.0057  289  MET B C   
5014  O  O   . MET B 289 ? 0.4297 0.4387 0.4292 0.0253  0.0229  0.0116  289  MET B O   
5015  C  CB  . MET B 289 ? 0.3109 0.3457 0.3181 0.0209  0.0190  0.0014  289  MET B CB  
5016  C  CG  . MET B 289 ? 0.3710 0.4043 0.3810 0.0223  0.0180  0.0091  289  MET B CG  
5017  S  SD  . MET B 289 ? 0.4886 0.5346 0.5074 0.0204  0.0142  0.0076  289  MET B SD  
5018  C  CE  . MET B 289 ? 0.3578 0.3974 0.3854 0.0188  0.0169  -0.0005 289  MET B CE  
5019  N  N   . GLN B 290 ? 0.2904 0.2998 0.2957 0.0256  0.0251  0.0012  290  GLN B N   
5020  C  CA  . GLN B 290 ? 0.2028 0.1992 0.2074 0.0282  0.0272  0.0038  290  GLN B CA  
5021  C  C   . GLN B 290 ? 0.2949 0.2869 0.2925 0.0287  0.0262  0.0078  290  GLN B C   
5022  O  O   . GLN B 290 ? 0.3283 0.3126 0.3221 0.0298  0.0265  0.0118  290  GLN B O   
5023  C  CB  . GLN B 290 ? 0.2979 0.2892 0.3062 0.0296  0.0289  -0.0004 290  GLN B CB  
5024  C  CG  . GLN B 290 ? 0.2356 0.2142 0.2419 0.0324  0.0312  0.0035  290  GLN B CG  
5025  C  CD  . GLN B 290 ? 0.4254 0.3986 0.4342 0.0345  0.0319  0.0015  290  GLN B CD  
5026  O  OE1 . GLN B 290 ? 0.5558 0.5230 0.5700 0.0349  0.0341  0.0013  290  GLN B OE1 
5027  N  NE2 . GLN B 290 ? 0.3727 0.3485 0.3790 0.0359  0.0299  0.0008  290  GLN B NE2 
5028  N  N   . ASP B 291 ? 0.3612 0.3584 0.3579 0.0278  0.0250  0.0060  291  ASP B N   
5029  C  CA  . ASP B 291 ? 0.3818 0.3757 0.3739 0.0271  0.0232  0.0093  291  ASP B CA  
5030  C  C   . ASP B 291 ? 0.4511 0.4457 0.4398 0.0244  0.0215  0.0142  291  ASP B C   
5031  O  O   . ASP B 291 ? 0.4363 0.4230 0.4209 0.0234  0.0198  0.0172  291  ASP B O   
5032  C  CB  . ASP B 291 ? 0.4018 0.4047 0.3970 0.0267  0.0226  0.0069  291  ASP B CB  
5033  C  CG  . ASP B 291 ? 0.6288 0.6274 0.6275 0.0305  0.0236  0.0036  291  ASP B CG  
5034  O  OD1 . ASP B 291 ? 0.5785 0.5674 0.5770 0.0327  0.0251  0.0035  291  ASP B OD1 
5035  O  OD2 . ASP B 291 ? 0.7298 0.7352 0.7324 0.0317  0.0231  0.0019  291  ASP B OD2 
5036  N  N   . PHE B 292 ? 0.3851 0.3887 0.3756 0.0231  0.0216  0.0149  292  PHE B N   
5037  C  CA  . PHE B 292 ? 0.1884 0.1923 0.1764 0.0211  0.0198  0.0210  292  PHE B CA  
5038  C  C   . PHE B 292 ? 0.2649 0.2546 0.2511 0.0238  0.0201  0.0240  292  PHE B C   
5039  O  O   . PHE B 292 ? 0.3349 0.3164 0.3178 0.0228  0.0185  0.0280  292  PHE B O   
5040  C  CB  . PHE B 292 ? 0.2233 0.2404 0.2125 0.0199  0.0192  0.0219  292  PHE B CB  
5041  C  CG  . PHE B 292 ? 0.3620 0.3786 0.3495 0.0190  0.0171  0.0299  292  PHE B CG  
5042  C  CD1 . PHE B 292 ? 0.3072 0.3272 0.2917 0.0153  0.0160  0.0357  292  PHE B CD1 
5043  C  CD2 . PHE B 292 ? 0.3417 0.3543 0.3317 0.0221  0.0166  0.0325  292  PHE B CD2 
5044  C  CE1 . PHE B 292 ? 0.2945 0.3118 0.2779 0.0145  0.0140  0.0443  292  PHE B CE1 
5045  C  CE2 . PHE B 292 ? 0.3666 0.3777 0.3560 0.0224  0.0145  0.0407  292  PHE B CE2 
5046  C  CZ  . PHE B 292 ? 0.3313 0.3436 0.3170 0.0186  0.0131  0.0467  292  PHE B CZ  
5047  N  N   . ASN B 293 ? 0.3608 0.3477 0.3499 0.0273  0.0223  0.0219  293  ASN B N   
5048  C  CA  . ASN B 293 ? 0.4637 0.4383 0.4513 0.0312  0.0243  0.0237  293  ASN B CA  
5049  C  C   . ASN B 293 ? 0.5206 0.4813 0.5003 0.0318  0.0241  0.0231  293  ASN B C   
5050  O  O   . ASN B 293 ? 0.5571 0.5072 0.5328 0.0334  0.0240  0.0251  293  ASN B O   
5051  C  CB  . ASN B 293 ? 0.3164 0.2914 0.3089 0.0340  0.0279  0.0214  293  ASN B CB  
5052  C  CG  . ASN B 293 ? 0.3630 0.3491 0.3642 0.0340  0.0276  0.0226  293  ASN B CG  
5053  O  OD1 . ASN B 293 ? 0.3574 0.3423 0.3621 0.0372  0.0288  0.0261  293  ASN B OD1 
5054  N  ND2 . ASN B 293 ? 0.3351 0.3326 0.3403 0.0308  0.0257  0.0193  293  ASN B ND2 
5055  N  N   . TYR B 294 ? 0.4312 0.3917 0.4086 0.0308  0.0237  0.0200  294  TYR B N   
5056  C  CA  . TYR B 294 ? 0.5517 0.5008 0.5209 0.0312  0.0226  0.0188  294  TYR B CA  
5057  C  C   . TYR B 294 ? 0.5761 0.5232 0.5429 0.0267  0.0181  0.0204  294  TYR B C   
5058  O  O   . TYR B 294 ? 0.4430 0.3774 0.4029 0.0266  0.0164  0.0200  294  TYR B O   
5059  C  CB  . TYR B 294 ? 0.5227 0.4741 0.4916 0.0318  0.0226  0.0163  294  TYR B CB  
5060  C  CG  . TYR B 294 ? 0.4877 0.4290 0.4470 0.0326  0.0205  0.0154  294  TYR B CG  
5061  C  CD1 . TYR B 294 ? 0.5104 0.4400 0.4607 0.0364  0.0232  0.0150  294  TYR B CD1 
5062  C  CD2 . TYR B 294 ? 0.4353 0.3803 0.3943 0.0298  0.0158  0.0149  294  TYR B CD2 
5063  C  CE1 . TYR B 294 ? 0.4699 0.3907 0.4086 0.0372  0.0208  0.0135  294  TYR B CE1 
5064  C  CE2 . TYR B 294 ? 0.4538 0.3908 0.4033 0.0302  0.0124  0.0139  294  TYR B CE2 
5065  C  CZ  . TYR B 294 ? 0.4248 0.3492 0.3629 0.0338  0.0147  0.0129  294  TYR B CZ  
5066  O  OH  . TYR B 294 ? 0.3297 0.2467 0.2559 0.0341  0.0108  0.0112  294  TYR B OH  
5067  N  N   . ALA B 295 ? 0.4846 0.4444 0.4572 0.0228  0.0165  0.0219  295  ALA B N   
5068  C  CA  . ALA B 295 ? 0.3596 0.3206 0.3323 0.0172  0.0126  0.0243  295  ALA B CA  
5069  C  C   . ALA B 295 ? 0.3473 0.3023 0.3195 0.0150  0.0115  0.0292  295  ALA B C   
5070  O  O   . ALA B 295 ? 0.4066 0.3553 0.3777 0.0103  0.0082  0.0312  295  ALA B O   
5071  C  CB  . ALA B 295 ? 0.3149 0.2933 0.2941 0.0143  0.0126  0.0245  295  ALA B CB  
5072  N  N   . PHE B 296 ? 0.4168 0.3736 0.3910 0.0182  0.0139  0.0316  296  PHE B N   
5073  C  CA  . PHE B 296 ? 0.3679 0.3205 0.3431 0.0172  0.0127  0.0380  296  PHE B CA  
5074  C  C   . PHE B 296 ? 0.4523 0.3919 0.4261 0.0235  0.0145  0.0382  296  PHE B C   
5075  O  O   . PHE B 296 ? 0.4427 0.3791 0.4188 0.0246  0.0138  0.0440  296  PHE B O   
5076  C  CB  . PHE B 296 ? 0.4638 0.4338 0.4433 0.0152  0.0129  0.0428  296  PHE B CB  
5077  C  CG  . PHE B 296 ? 0.4949 0.4790 0.4759 0.0097  0.0123  0.0431  296  PHE B CG  
5078  C  CD1 . PHE B 296 ? 0.5694 0.5643 0.5520 0.0106  0.0141  0.0369  296  PHE B CD1 
5079  C  CD2 . PHE B 296 ? 0.4798 0.4661 0.4618 0.0037  0.0106  0.0501  296  PHE B CD2 
5080  C  CE1 . PHE B 296 ? 0.4364 0.4454 0.4215 0.0068  0.0145  0.0368  296  PHE B CE1 
5081  C  CE2 . PHE B 296 ? 0.5374 0.5392 0.5221 -0.0012 0.0112  0.0508  296  PHE B CE2 
5082  C  CZ  . PHE B 296 ? 0.5366 0.5502 0.5229 0.0009  0.0134  0.0437  296  PHE B CZ  
5083  N  N   . SER B 297 ? 0.5028 0.4358 0.4732 0.0281  0.0173  0.0326  297  SER B N   
5084  C  CA  . SER B 297 ? 0.2392 0.1617 0.2087 0.0349  0.0205  0.0322  297  SER B CA  
5085  C  C   . SER B 297 ? 0.3600 0.2730 0.3216 0.0382  0.0232  0.0259  297  SER B C   
5086  O  O   . SER B 297 ? 0.5453 0.4587 0.5021 0.0349  0.0213  0.0227  297  SER B O   
5087  C  CB  . SER B 297 ? 0.3300 0.2654 0.3080 0.0386  0.0230  0.0347  297  SER B CB  
5088  O  OG  . SER B 297 ? 0.3532 0.2950 0.3326 0.0402  0.0263  0.0305  297  SER B OG  
5089  N  N   . ASN B 298 ? 0.4579 0.3637 0.4184 0.0451  0.0279  0.0247  298  ASN B N   
5090  C  CA  . ASN B 298 ? 0.4098 0.3079 0.3613 0.0490  0.0319  0.0196  298  ASN B CA  
5091  C  C   . ASN B 298 ? 0.3571 0.2678 0.3135 0.0501  0.0357  0.0199  298  ASN B C   
5092  O  O   . ASN B 298 ? 0.4775 0.3849 0.4267 0.0520  0.0388  0.0174  298  ASN B O   
5093  C  CB  . ASN B 298 ? 0.2825 0.1686 0.2309 0.0568  0.0368  0.0183  298  ASN B CB  
5094  C  CG  . ASN B 298 ? 0.3954 0.2634 0.3371 0.0565  0.0333  0.0162  298  ASN B CG  
5095  O  OD1 . ASN B 298 ? 0.4547 0.3174 0.3911 0.0497  0.0273  0.0147  298  ASN B OD1 
5096  N  ND2 . ASN B 298 ? 0.3935 0.2518 0.3366 0.0638  0.0370  0.0162  298  ASN B ND2 
5097  N  N   . CYS B 299 ? 0.2219 0.1467 0.1903 0.0486  0.0354  0.0233  299  CYS B N   
5098  C  CA  . CYS B 299 ? 0.2771 0.2126 0.2529 0.0495  0.0392  0.0235  299  CYS B CA  
5099  C  C   . CYS B 299 ? 0.3348 0.2727 0.3077 0.0463  0.0385  0.0212  299  CYS B C   
5100  O  O   . CYS B 299 ? 0.5615 0.5015 0.5327 0.0421  0.0339  0.0201  299  CYS B O   
5101  C  CB  . CYS B 299 ? 0.1054 0.0552 0.0939 0.0479  0.0375  0.0266  299  CYS B CB  
5102  S  SG  . CYS B 299 ? 0.4012 0.3627 0.4015 0.0488  0.0419  0.0268  299  CYS B SG  
5103  N  N   . PHE B 300 ? 0.2978 0.2358 0.2713 0.0485  0.0435  0.0212  300  PHE B N   
5104  C  CA  . PHE B 300 ? 0.4264 0.3656 0.3989 0.0464  0.0432  0.0203  300  PHE B CA  
5105  C  C   . PHE B 300 ? 0.3277 0.2774 0.3138 0.0443  0.0447  0.0208  300  PHE B C   
5106  O  O   . PHE B 300 ? 0.3157 0.2666 0.3069 0.0458  0.0499  0.0229  300  PHE B O   
5107  C  CB  . PHE B 300 ? 0.5174 0.4474 0.4792 0.0499  0.0475  0.0210  300  PHE B CB  
5108  C  CG  . PHE B 300 ? 0.5671 0.4861 0.5132 0.0511  0.0447  0.0187  300  PHE B CG  
5109  C  CD1 . PHE B 300 ? 0.4696 0.3820 0.4032 0.0530  0.0457  0.0189  300  PHE B CD1 
5110  C  CD2 . PHE B 300 ? 0.6495 0.5642 0.5929 0.0499  0.0405  0.0167  300  PHE B CD2 
5111  C  CE1 . PHE B 300 ? 0.3902 0.2928 0.3084 0.0535  0.0420  0.0158  300  PHE B CE1 
5112  C  CE2 . PHE B 300 ? 0.6016 0.5051 0.5313 0.0499  0.0371  0.0136  300  PHE B CE2 
5113  C  CZ  . PHE B 300 ? 0.5467 0.4445 0.4634 0.0516  0.0375  0.0125  300  PHE B CZ  
5114  N  N   . GLU B 301 ? 0.3157 0.2732 0.3076 0.0404  0.0403  0.0187  301  GLU B N   
5115  C  CA  . GLU B 301 ? 0.2309 0.1974 0.2347 0.0377  0.0405  0.0172  301  GLU B CA  
5116  C  C   . GLU B 301 ? 0.3438 0.3075 0.3493 0.0365  0.0407  0.0150  301  GLU B C   
5117  O  O   . GLU B 301 ? 0.4971 0.4593 0.4979 0.0363  0.0378  0.0131  301  GLU B O   
5118  C  CB  . GLU B 301 ? 0.3414 0.3187 0.3494 0.0347  0.0359  0.0152  301  GLU B CB  
5119  C  CG  . GLU B 301 ? 0.2908 0.2773 0.3088 0.0312  0.0346  0.0113  301  GLU B CG  
5120  C  CD  . GLU B 301 ? 0.4010 0.3999 0.4220 0.0290  0.0304  0.0105  301  GLU B CD  
5121  O  OE1 . GLU B 301 ? 0.5289 0.5319 0.5533 0.0303  0.0303  0.0146  301  GLU B OE1 
5122  O  OE2 . GLU B 301 ? 0.4520 0.4574 0.4717 0.0264  0.0274  0.0060  301  GLU B OE2 
5123  N  N   . LEU B 302 ? 0.3844 0.3478 0.3983 0.0356  0.0441  0.0159  302  LEU B N   
5124  C  CA  . LEU B 302 ? 0.4610 0.4206 0.4792 0.0343  0.0440  0.0139  302  LEU B CA  
5125  C  C   . LEU B 302 ? 0.4178 0.3855 0.4460 0.0303  0.0409  0.0078  302  LEU B C   
5126  O  O   . LEU B 302 ? 0.3969 0.3738 0.4302 0.0280  0.0396  0.0068  302  LEU B O   
5127  C  CB  . LEU B 302 ? 0.4589 0.4122 0.4814 0.0345  0.0495  0.0188  302  LEU B CB  
5128  C  CG  . LEU B 302 ? 0.5070 0.4517 0.5176 0.0387  0.0534  0.0248  302  LEU B CG  
5129  C  CD1 . LEU B 302 ? 0.4280 0.3684 0.4444 0.0380  0.0594  0.0306  302  LEU B CD1 
5130  C  CD2 . LEU B 302 ? 0.4354 0.3742 0.4352 0.0412  0.0495  0.0241  302  LEU B CD2 
5131  N  N   . THR B 303 ? 0.4961 0.4604 0.5265 0.0300  0.0396  0.0036  303  THR B N   
5132  C  CA  . THR B 303 ? 0.6189 0.5879 0.6585 0.0263  0.0374  -0.0037 303  THR B CA  
5133  C  C   . THR B 303 ? 0.5995 0.5590 0.6489 0.0245  0.0401  -0.0029 303  THR B C   
5134  O  O   . THR B 303 ? 0.4592 0.4079 0.5069 0.0274  0.0421  0.0003  303  THR B O   
5135  C  CB  . THR B 303 ? 0.5978 0.5691 0.6339 0.0278  0.0346  -0.0105 303  THR B CB  
5136  O  OG1 . THR B 303 ? 0.5869 0.5656 0.6139 0.0292  0.0329  -0.0088 303  THR B OG1 
5137  C  CG2 . THR B 303 ? 0.5017 0.4792 0.5441 0.0241  0.0322  -0.0199 303  THR B CG2 
5138  N  N   . ILE B 304 ? 0.6110 0.5748 0.6713 0.0193  0.0398  -0.0051 304  ILE B N   
5139  C  CA  . ILE B 304 ? 0.5780 0.5330 0.6501 0.0160  0.0424  -0.0036 304  ILE B CA  
5140  C  C   . ILE B 304 ? 0.5843 0.5395 0.6669 0.0104  0.0386  -0.0136 304  ILE B C   
5141  O  O   . ILE B 304 ? 0.3157 0.2830 0.4023 0.0061  0.0347  -0.0187 304  ILE B O   
5142  C  CB  . ILE B 304 ? 0.4812 0.4395 0.5597 0.0139  0.0467  0.0049  304  ILE B CB  
5143  C  CG1 . ILE B 304 ? 0.3447 0.2999 0.4106 0.0199  0.0510  0.0133  304  ILE B CG1 
5144  C  CG2 . ILE B 304 ? 0.5247 0.4746 0.6172 0.0089  0.0498  0.0077  304  ILE B CG2 
5145  C  CD1 . ILE B 304 ? 0.7107 0.6716 0.7809 0.0197  0.0562  0.0207  304  ILE B CD1 
5146  N  N   . GLU B 305 ? 0.4775 0.4187 0.5640 0.0110  0.0393  -0.0165 305  GLU B N   
5147  C  CA  . GLU B 305 ? 0.3940 0.3298 0.4902 0.0064  0.0362  -0.0272 305  GLU B CA  
5148  C  C   . GLU B 305 ? 0.5412 0.4694 0.6532 -0.0006 0.0381  -0.0231 305  GLU B C   
5149  O  O   . GLU B 305 ? 0.5939 0.5103 0.7088 0.0008  0.0430  -0.0133 305  GLU B O   
5150  C  CB  . GLU B 305 ? 0.2662 0.1891 0.3593 0.0121  0.0364  -0.0321 305  GLU B CB  
5151  C  CG  . GLU B 305 ? 0.3036 0.2355 0.3837 0.0184  0.0351  -0.0357 305  GLU B CG  
5152  C  CD  . GLU B 305 ? 0.4992 0.4427 0.5763 0.0161  0.0310  -0.0484 305  GLU B CD  
5153  O  OE1 . GLU B 305 ? 0.5011 0.4546 0.5680 0.0203  0.0304  -0.0510 305  GLU B OE1 
5154  O  OE2 . GLU B 305 ? 0.5114 0.4548 0.5964 0.0096  0.0283  -0.0558 305  GLU B OE2 
5155  N  N   . LEU B 306 ? 0.4916 0.4274 0.6139 -0.0086 0.0341  -0.0299 306  LEU B N   
5156  C  CA  . LEU B 306 ? 0.5242 0.4576 0.6639 -0.0168 0.0357  -0.0248 306  LEU B CA  
5157  C  C   . LEU B 306 ? 0.5234 0.4396 0.6759 -0.0227 0.0339  -0.0321 306  LEU B C   
5158  O  O   . LEU B 306 ? 0.6248 0.5286 0.7886 -0.0261 0.0382  -0.0237 306  LEU B O   
5159  C  CB  . LEU B 306 ? 0.5455 0.4996 0.6924 -0.0228 0.0321  -0.0256 306  LEU B CB  
5160  C  CG  . LEU B 306 ? 0.5854 0.5537 0.7231 -0.0169 0.0351  -0.0162 306  LEU B CG  
5161  C  CD1 . LEU B 306 ? 0.5098 0.4991 0.6542 -0.0212 0.0300  -0.0182 306  LEU B CD1 
5162  C  CD2 . LEU B 306 ? 0.4605 0.4237 0.6010 -0.0146 0.0437  -0.0019 306  LEU B CD2 
5163  N  N   . SER B 307 ? 0.5514 0.4659 0.7017 -0.0239 0.0280  -0.0476 307  SER B N   
5164  C  CA  . SER B 307 ? 0.4879 0.3853 0.6510 -0.0303 0.0255  -0.0569 307  SER B CA  
5165  C  C   . SER B 307 ? 0.5291 0.4133 0.6833 -0.0235 0.0241  -0.0696 307  SER B C   
5166  O  O   . SER B 307 ? 0.5340 0.4285 0.6729 -0.0164 0.0231  -0.0751 307  SER B O   
5167  C  CB  . SER B 307 ? 0.5818 0.4908 0.7558 -0.0417 0.0184  -0.0664 307  SER B CB  
5168  O  OG  . SER B 307 ? 0.5948 0.5236 0.7557 -0.0395 0.0131  -0.0746 307  SER B OG  
5169  N  N   . CYS B 308 ? 0.6478 0.5089 0.8126 -0.0254 0.0245  -0.0738 308  CYS B N   
5170  C  CA  . CYS B 308 ? 0.6493 0.4971 0.8087 -0.0190 0.0232  -0.0882 308  CYS B CA  
5171  C  C   . CYS B 308 ? 0.7110 0.5696 0.8660 -0.0240 0.0162  -0.1073 308  CYS B C   
5172  O  O   . CYS B 308 ? 0.7731 0.6366 0.9145 -0.0169 0.0154  -0.1188 308  CYS B O   
5173  C  CB  . CYS B 308 ? 0.5275 0.3459 0.7012 -0.0202 0.0249  -0.0884 308  CYS B CB  
5174  S  SG  . CYS B 308 ? 0.6930 0.4968 0.8669 -0.0104 0.0326  -0.0678 308  CYS B SG  
5175  N  N   . CYS B 309 ? 0.5659 0.4298 0.7322 -0.0364 0.0112  -0.1104 309  CYS B N   
5176  C  CA  . CYS B 309 ? 0.4887 0.3658 0.6500 -0.0424 0.0031  -0.1276 309  CYS B CA  
5177  C  C   . CYS B 309 ? 0.6379 0.5448 0.7878 -0.0416 0.0010  -0.1220 309  CYS B C   
5178  O  O   . CYS B 309 ? 0.4294 0.3484 0.5870 -0.0455 0.0019  -0.1079 309  CYS B O   
5179  C  CB  . CYS B 309 ? 0.5117 0.3815 0.6919 -0.0568 -0.0029 -0.1342 309  CYS B CB  
5180  S  SG  . CYS B 309 ? 0.6539 0.5413 0.8277 -0.0654 -0.0146 -0.1551 309  CYS B SG  
5181  N  N   . LYS B 310 ? 0.6893 0.6080 0.8212 -0.0361 -0.0013 -0.1326 310  LYS B N   
5182  C  CA  . LYS B 310 ? 0.6419 0.5871 0.7614 -0.0342 -0.0032 -0.1269 310  LYS B CA  
5183  C  C   . LYS B 310 ? 0.7142 0.6763 0.8429 -0.0451 -0.0107 -0.1262 310  LYS B C   
5184  O  O   . LYS B 310 ? 0.6563 0.6337 0.7880 -0.0453 -0.0099 -0.1121 310  LYS B O   
5185  C  CB  . LYS B 310 ? 0.6657 0.6198 0.7648 -0.0277 -0.0045 -0.1396 310  LYS B CB  
5186  C  CG  . LYS B 310 ? 0.6264 0.5721 0.7166 -0.0156 0.0034  -0.1365 310  LYS B CG  
5187  C  CD  . LYS B 310 ? 0.5699 0.5280 0.6411 -0.0093 0.0035  -0.1474 310  LYS B CD  
5188  C  CE  . LYS B 310 ? 0.6571 0.6153 0.7214 0.0019  0.0110  -0.1388 310  LYS B CE  
5189  N  NZ  . LYS B 310 ? 0.7354 0.7110 0.7821 0.0074  0.0122  -0.1449 310  LYS B NZ  
5190  N  N   . TYR B 311 ? 0.6593 0.6185 0.7933 -0.0539 -0.0183 -0.1419 311  TYR B N   
5191  C  CA  . TYR B 311 ? 0.5424 0.5196 0.6856 -0.0649 -0.0274 -0.1435 311  TYR B CA  
5192  C  C   . TYR B 311 ? 0.5516 0.5131 0.7167 -0.0767 -0.0308 -0.1494 311  TYR B C   
5193  O  O   . TYR B 311 ? 0.5721 0.5274 0.7366 -0.0833 -0.0382 -0.1678 311  TYR B O   
5194  C  CB  . TYR B 311 ? 0.5653 0.5583 0.6904 -0.0655 -0.0358 -0.1590 311  TYR B CB  
5195  C  CG  . TYR B 311 ? 0.4843 0.5046 0.6126 -0.0729 -0.0454 -0.1562 311  TYR B CG  
5196  C  CD1 . TYR B 311 ? 0.4154 0.4566 0.5233 -0.0700 -0.0510 -0.1612 311  TYR B CD1 
5197  C  CD2 . TYR B 311 ? 0.5394 0.5660 0.6916 -0.0826 -0.0488 -0.1478 311  TYR B CD2 
5198  C  CE1 . TYR B 311 ? 0.4633 0.5301 0.5739 -0.0759 -0.0606 -0.1577 311  TYR B CE1 
5199  C  CE2 . TYR B 311 ? 0.5043 0.5581 0.6612 -0.0885 -0.0582 -0.1448 311  TYR B CE2 
5200  C  CZ  . TYR B 311 ? 0.4929 0.5662 0.6286 -0.0848 -0.0645 -0.1498 311  TYR B CZ  
5201  O  OH  . TYR B 311 ? 0.4512 0.5519 0.5908 -0.0897 -0.0746 -0.1459 311  TYR B OH  
5202  N  N   . PRO B 312 ? 0.6171 0.5715 0.8012 -0.0797 -0.0252 -0.1339 312  PRO B N   
5203  C  CA  . PRO B 312 ? 0.6174 0.5577 0.8256 -0.0923 -0.0276 -0.1360 312  PRO B CA  
5204  C  C   . PRO B 312 ? 0.7785 0.7401 1.0005 -0.1058 -0.0385 -0.1403 312  PRO B C   
5205  O  O   . PRO B 312 ? 0.8352 0.8225 1.0471 -0.1043 -0.0443 -0.1412 312  PRO B O   
5206  C  CB  . PRO B 312 ? 0.4245 0.3578 0.6458 -0.0901 -0.0171 -0.1145 312  PRO B CB  
5207  C  CG  . PRO B 312 ? 0.5998 0.5372 0.8013 -0.0753 -0.0096 -0.1048 312  PRO B CG  
5208  C  CD  . PRO B 312 ? 0.6803 0.6388 0.8633 -0.0715 -0.0158 -0.1136 312  PRO B CD  
5209  N  N   . ALA B 313 ? 0.7481 0.6994 0.9941 -0.1191 -0.0416 -0.1423 313  ALA B N   
5210  C  CA  . ALA B 313 ? 0.7352 0.7075 0.9984 -0.1332 -0.0526 -0.1460 313  ALA B CA  
5211  C  C   . ALA B 313 ? 0.5661 0.5578 0.8500 -0.1362 -0.0479 -0.1242 313  ALA B C   
5212  O  O   . ALA B 313 ? 0.6173 0.5992 0.9065 -0.1310 -0.0361 -0.1081 313  ALA B O   
5213  C  CB  . ALA B 313 ? 0.7205 0.6728 1.0002 -0.1476 -0.0598 -0.1613 313  ALA B CB  
5214  N  N   . ALA B 314 ? 0.3872 0.4076 0.6828 -0.1444 -0.0573 -0.1240 314  ALA B N   
5215  C  CA  . ALA B 314 ? 0.4372 0.4805 0.7537 -0.1464 -0.0532 -0.1045 314  ALA B CA  
5216  C  C   . ALA B 314 ? 0.5677 0.5965 0.9082 -0.1521 -0.0427 -0.0905 314  ALA B C   
5217  O  O   . ALA B 314 ? 0.6768 0.7101 1.0186 -0.1440 -0.0311 -0.0725 314  ALA B O   
5218  C  CB  . ALA B 314 ? 0.4908 0.5643 0.8230 -0.1576 -0.0669 -0.1089 314  ALA B CB  
5219  N  N   . SER B 315 ? 0.4854 0.4966 0.8441 -0.1661 -0.0468 -0.0987 315  SER B N   
5220  C  CA  . SER B 315 ? 0.4665 0.4644 0.8503 -0.1737 -0.0374 -0.0844 315  SER B CA  
5221  C  C   . SER B 315 ? 0.5483 0.5275 0.9187 -0.1599 -0.0216 -0.0694 315  SER B C   
5222  O  O   . SER B 315 ? 0.4304 0.4081 0.8169 -0.1619 -0.0110 -0.0514 315  SER B O   
5223  C  CB  . SER B 315 ? 0.4473 0.4203 0.8475 -0.1893 -0.0442 -0.0979 315  SER B CB  
5224  O  OG  . SER B 315 ? 0.5674 0.5093 0.9458 -0.1827 -0.0449 -0.1132 315  SER B OG  
5225  N  N   . THR B 316 ? 0.4556 0.4223 0.7964 -0.1461 -0.0203 -0.0769 316  THR B N   
5226  C  CA  . THR B 316 ? 0.3710 0.3219 0.6959 -0.1321 -0.0076 -0.0650 316  THR B CA  
5227  C  C   . THR B 316 ? 0.4380 0.4122 0.7596 -0.1235 0.0005  -0.0471 316  THR B C   
5228  O  O   . THR B 316 ? 0.5175 0.4844 0.8392 -0.1180 0.0122  -0.0312 316  THR B O   
5229  C  CB  . THR B 316 ? 0.4830 0.4200 0.7787 -0.1201 -0.0098 -0.0788 316  THR B CB  
5230  O  OG1 . THR B 316 ? 0.5541 0.4601 0.8522 -0.1240 -0.0116 -0.0907 316  THR B OG1 
5231  C  CG2 . THR B 316 ? 0.5904 0.5252 0.8665 -0.1042 0.0007  -0.0663 316  THR B CG2 
5232  N  N   . LEU B 317 ? 0.4200 0.4223 0.7387 -0.1222 -0.0060 -0.0500 317  LEU B N   
5233  C  CA  . LEU B 317 ? 0.4558 0.4789 0.7673 -0.1116 0.0004  -0.0363 317  LEU B CA  
5234  C  C   . LEU B 317 ? 0.3821 0.4101 0.7107 -0.1124 0.0125  -0.0167 317  LEU B C   
5235  O  O   . LEU B 317 ? 0.3357 0.3613 0.6506 -0.1007 0.0226  -0.0056 317  LEU B O   
5236  C  CB  . LEU B 317 ? 0.3951 0.4489 0.7083 -0.1127 -0.0097 -0.0410 317  LEU B CB  
5237  C  CG  . LEU B 317 ? 0.4325 0.4869 0.7265 -0.1116 -0.0217 -0.0593 317  LEU B CG  
5238  C  CD1 . LEU B 317 ? 0.5806 0.6667 0.8827 -0.1162 -0.0330 -0.0620 317  LEU B CD1 
5239  C  CD2 . LEU B 317 ? 0.2836 0.3285 0.5473 -0.0966 -0.0170 -0.0599 317  LEU B CD2 
5240  N  N   . PRO B 318 ? 0.4269 0.4630 0.7855 -0.1263 0.0116  -0.0124 318  PRO B N   
5241  C  CA  . PRO B 318 ? 0.4571 0.5020 0.8321 -0.1267 0.0244  0.0072  318  PRO B CA  
5242  C  C   . PRO B 318 ? 0.5632 0.5815 0.9265 -0.1204 0.0370  0.0176  318  PRO B C   
5243  O  O   . PRO B 318 ? 0.4729 0.4981 0.8321 -0.1124 0.0486  0.0323  318  PRO B O   
5244  C  CB  . PRO B 318 ? 0.3618 0.4168 0.7720 -0.1450 0.0198  0.0078  318  PRO B CB  
5245  C  CG  . PRO B 318 ? 0.3519 0.4178 0.7636 -0.1517 0.0030  -0.0104 318  PRO B CG  
5246  C  CD  . PRO B 318 ? 0.4823 0.5248 0.8615 -0.1423 -0.0011 -0.0246 318  PRO B CD  
5247  N  N   . GLN B 319 ? 0.5320 0.5208 0.8896 -0.1234 0.0345  0.0098  319  GLN B N   
5248  C  CA  . GLN B 319 ? 0.4754 0.4387 0.8188 -0.1156 0.0444  0.0189  319  GLN B CA  
5249  C  C   . GLN B 319 ? 0.3774 0.3418 0.6904 -0.0983 0.0480  0.0199  319  GLN B C   
5250  O  O   . GLN B 319 ? 0.3964 0.3581 0.6997 -0.0901 0.0588  0.0338  319  GLN B O   
5251  C  CB  . GLN B 319 ? 0.7232 0.6549 1.0651 -0.1198 0.0391  0.0076  319  GLN B CB  
5252  C  CG  . GLN B 319 ? 0.9120 0.8276 1.2791 -0.1336 0.0420  0.0147  319  GLN B CG  
5253  C  CD  . GLN B 319 ? 1.1505 1.0624 1.5365 -0.1486 0.0295  -0.0019 319  GLN B CD  
5254  O  OE1 . GLN B 319 ? 1.2931 1.1798 1.6927 -0.1580 0.0283  -0.0040 319  GLN B OE1 
5255  N  NE2 . GLN B 319 ? 1.0584 0.9946 1.4447 -0.1510 0.0196  -0.0140 319  GLN B NE2 
5256  N  N   . GLU B 320 ? 0.4422 0.4105 0.7398 -0.0934 0.0389  0.0051  320  GLU B N   
5257  C  CA  . GLU B 320 ? 0.5544 0.5239 0.8246 -0.0784 0.0412  0.0052  320  GLU B CA  
5258  C  C   . GLU B 320 ? 0.4197 0.4097 0.6885 -0.0720 0.0490  0.0187  320  GLU B C   
5259  O  O   . GLU B 320 ? 0.5587 0.5429 0.8103 -0.0614 0.0568  0.0269  320  GLU B O   
5260  C  CB  . GLU B 320 ? 0.5940 0.5695 0.8507 -0.0756 0.0303  -0.0116 320  GLU B CB  
5261  C  CG  . GLU B 320 ? 0.6711 0.6265 0.9259 -0.0801 0.0229  -0.0276 320  GLU B CG  
5262  C  CD  . GLU B 320 ? 0.7300 0.6594 0.9698 -0.0714 0.0279  -0.0271 320  GLU B CD  
5263  O  OE1 . GLU B 320 ? 0.6238 0.5499 0.8550 -0.0633 0.0366  -0.0136 320  GLU B OE1 
5264  O  OE2 . GLU B 320 ? 0.8174 0.7297 1.0538 -0.0723 0.0230  -0.0406 320  GLU B OE2 
5265  N  N   . TRP B 321 ? 0.2646 0.2789 0.5521 -0.0781 0.0467  0.0205  321  TRP B N   
5266  C  CA  . TRP B 321 ? 0.4352 0.4692 0.7256 -0.0721 0.0552  0.0334  321  TRP B CA  
5267  C  C   . TRP B 321 ? 0.5139 0.5380 0.8034 -0.0692 0.0693  0.0489  321  TRP B C   
5268  O  O   . TRP B 321 ? 0.3999 0.4240 0.6714 -0.0577 0.0769  0.0555  321  TRP B O   
5269  C  CB  . TRP B 321 ? 0.4404 0.5023 0.7578 -0.0807 0.0513  0.0346  321  TRP B CB  
5270  C  CG  . TRP B 321 ? 0.5221 0.6036 0.8475 -0.0750 0.0621  0.0489  321  TRP B CG  
5271  C  CD1 . TRP B 321 ? 0.3995 0.4920 0.7489 -0.0816 0.0711  0.0611  321  TRP B CD1 
5272  C  CD2 . TRP B 321 ? 0.5744 0.6658 0.8835 -0.0609 0.0662  0.0522  321  TRP B CD2 
5273  N  NE1 . TRP B 321 ? 0.4689 0.5787 0.8173 -0.0716 0.0809  0.0712  321  TRP B NE1 
5274  C  CE2 . TRP B 321 ? 0.4631 0.5713 0.7869 -0.0588 0.0777  0.0655  321  TRP B CE2 
5275  C  CE3 . TRP B 321 ? 0.5598 0.6473 0.8440 -0.0502 0.0614  0.0453  321  TRP B CE3 
5276  C  CZ2 . TRP B 321 ? 0.3896 0.5089 0.7032 -0.0456 0.0844  0.0707  321  TRP B CZ2 
5277  C  CZ3 . TRP B 321 ? 0.4459 0.5437 0.7211 -0.0383 0.0674  0.0514  321  TRP B CZ3 
5278  C  CH2 . TRP B 321 ? 0.3717 0.4844 0.6611 -0.0357 0.0787  0.0633  321  TRP B CH2 
5279  N  N   . GLN B 322 ? 0.5717 0.5871 0.8800 -0.0800 0.0726  0.0546  322  GLN B N   
5280  C  CA  . GLN B 322 ? 0.6163 0.6258 0.9261 -0.0788 0.0863  0.0713  322  GLN B CA  
5281  C  C   . GLN B 322 ? 0.6066 0.5936 0.8873 -0.0674 0.0907  0.0740  322  GLN B C   
5282  O  O   . GLN B 322 ? 0.6172 0.6049 0.8870 -0.0601 0.1017  0.0863  322  GLN B O   
5283  C  CB  . GLN B 322 ? 0.6326 0.6344 0.9688 -0.0938 0.0880  0.0771  322  GLN B CB  
5284  C  CG  . GLN B 322 ? 0.6530 0.6747 1.0110 -0.0990 0.0997  0.0937  322  GLN B CG  
5285  C  CD  . GLN B 322 ? 0.6930 0.7478 1.0700 -0.1017 0.0964  0.0910  322  GLN B CD  
5286  O  OE1 . GLN B 322 ? 0.7695 0.8454 1.1503 -0.0958 0.1063  0.1014  322  GLN B OE1 
5287  N  NE2 . GLN B 322 ? 0.5804 0.6404 0.9691 -0.1098 0.0821  0.0769  322  GLN B NE2 
5288  N  N   . ARG B 323 ? 0.4738 0.4424 0.7418 -0.0655 0.0820  0.0620  323  ARG B N   
5289  C  CA  . ARG B 323 ? 0.4514 0.4003 0.6941 -0.0549 0.0845  0.0638  323  ARG B CA  
5290  C  C   . ARG B 323 ? 0.4829 0.4414 0.7021 -0.0420 0.0855  0.0623  323  ARG B C   
5291  O  O   . ARG B 323 ? 0.4993 0.4513 0.7006 -0.0333 0.0923  0.0707  323  ARG B O   
5292  C  CB  . ARG B 323 ? 0.4692 0.3976 0.7082 -0.0563 0.0752  0.0507  323  ARG B CB  
5293  C  CG  . ARG B 323 ? 0.4718 0.3869 0.7339 -0.0693 0.0730  0.0497  323  ARG B CG  
5294  C  CD  . ARG B 323 ? 0.5465 0.4445 0.8053 -0.0702 0.0628  0.0327  323  ARG B CD  
5295  N  NE  . ARG B 323 ? 0.6586 0.5366 0.9369 -0.0811 0.0613  0.0320  323  ARG B NE  
5296  C  CZ  . ARG B 323 ? 0.8919 0.7524 1.1720 -0.0837 0.0532  0.0165  323  ARG B CZ  
5297  N  NH1 . ARG B 323 ? 0.8689 0.7320 1.1321 -0.0762 0.0464  0.0012  323  ARG B NH1 
5298  N  NH2 . ARG B 323 ? 1.0640 0.9039 1.3627 -0.0938 0.0522  0.0163  323  ARG B NH2 
5299  N  N   . ASN B 324 ? 0.3691 0.3427 0.5881 -0.0411 0.0781  0.0518  324  ASN B N   
5300  C  CA  . ASN B 324 ? 0.4433 0.4233 0.6409 -0.0297 0.0774  0.0491  324  ASN B CA  
5301  C  C   . ASN B 324 ? 0.4260 0.4237 0.6244 -0.0248 0.0853  0.0580  324  ASN B C   
5302  O  O   . ASN B 324 ? 0.4157 0.4147 0.5953 -0.0148 0.0872  0.0583  324  ASN B O   
5303  C  CB  . ASN B 324 ? 0.3231 0.3097 0.5176 -0.0299 0.0661  0.0348  324  ASN B CB  
5304  C  CG  . ASN B 324 ? 0.3947 0.3631 0.5831 -0.0315 0.0595  0.0246  324  ASN B CG  
5305  O  OD1 . ASN B 324 ? 0.5209 0.4805 0.6902 -0.0236 0.0580  0.0208  324  ASN B OD1 
5306  N  ND2 . ASN B 324 ? 0.3301 0.2923 0.5359 -0.0416 0.0561  0.0202  324  ASN B ND2 
5307  N  N   . LYS B 325 ? 0.4368 0.4476 0.6582 -0.0322 0.0901  0.0650  325  LYS B N   
5308  C  CA  . LYS B 325 ? 0.4113 0.4425 0.6393 -0.0281 0.0981  0.0730  325  LYS B CA  
5309  C  C   . LYS B 325 ? 0.4086 0.4329 0.6134 -0.0167 0.1081  0.0804  325  LYS B C   
5310  O  O   . LYS B 325 ? 0.5331 0.5639 0.7249 -0.0072 0.1088  0.0782  325  LYS B O   
5311  C  CB  . LYS B 325 ? 0.4564 0.4995 0.7131 -0.0385 0.1040  0.0820  325  LYS B CB  
5312  C  CG  . LYS B 325 ? 0.2199 0.2894 0.4914 -0.0359 0.1114  0.0892  325  LYS B CG  
5313  C  CD  . LYS B 325 ? 0.4389 0.5190 0.7406 -0.0481 0.1172  0.0986  325  LYS B CD  
5314  C  CE  . LYS B 325 ? 0.5963 0.7056 0.9175 -0.0460 0.1256  0.1067  325  LYS B CE  
5315  N  NZ  . LYS B 325 ? 0.6783 0.7989 1.0310 -0.0594 0.1312  0.1166  325  LYS B NZ  
5316  N  N   . ALA B 326 ? 0.4803 0.4906 0.6795 -0.0178 0.1153  0.0892  326  ALA B N   
5317  C  CA  . ALA B 326 ? 0.6026 0.6059 0.7780 -0.0077 0.1244  0.0965  326  ALA B CA  
5318  C  C   . ALA B 326 ? 0.6145 0.6062 0.7628 0.0016  0.1180  0.0880  326  ALA B C   
5319  O  O   . ALA B 326 ? 0.5429 0.5366 0.6733 0.0110  0.1227  0.0891  326  ALA B O   
5320  C  CB  . ALA B 326 ? 0.5378 0.5272 0.7115 -0.0113 0.1314  0.1079  326  ALA B CB  
5321  N  N   . SER B 327 ? 0.5878 0.5676 0.7339 -0.0012 0.1075  0.0793  327  SER B N   
5322  C  CA  . SER B 327 ? 0.4199 0.3896 0.5433 0.0062  0.1011  0.0717  327  SER B CA  
5323  C  C   . SER B 327 ? 0.3605 0.3424 0.4794 0.0112  0.0972  0.0645  327  SER B C   
5324  O  O   . SER B 327 ? 0.3666 0.3438 0.4654 0.0190  0.0962  0.0621  327  SER B O   
5325  C  CB  . SER B 327 ? 0.3422 0.2989 0.4679 0.0019  0.0919  0.0640  327  SER B CB  
5326  O  OG  . SER B 327 ? 0.4244 0.3676 0.5558 -0.0023 0.0952  0.0713  327  SER B OG  
5327  N  N   . LEU B 328 ? 0.2310 0.2283 0.3694 0.0062  0.0943  0.0616  328  LEU B N   
5328  C  CA  . LEU B 328 ? 0.1497 0.1591 0.2870 0.0103  0.0895  0.0559  328  LEU B CA  
5329  C  C   . LEU B 328 ? 0.4201 0.4377 0.5524 0.0186  0.0983  0.0617  328  LEU B C   
5330  O  O   . LEU B 328 ? 0.3626 0.3810 0.4828 0.0259  0.0961  0.0581  328  LEU B O   
5331  C  CB  . LEU B 328 ? 0.2056 0.2300 0.3660 0.0022  0.0831  0.0519  328  LEU B CB  
5332  C  CG  . LEU B 328 ? 0.1784 0.1975 0.3397 -0.0038 0.0719  0.0415  328  LEU B CG  
5333  C  CD1 . LEU B 328 ? 0.1799 0.2118 0.3658 -0.0142 0.0670  0.0388  328  LEU B CD1 
5334  C  CD2 . LEU B 328 ? 0.2579 0.2795 0.4048 0.0018  0.0649  0.0346  328  LEU B CD2 
5335  N  N   . LEU B 329 ? 0.3571 0.3805 0.4990 0.0175  0.1088  0.0708  329  LEU B N   
5336  C  CA  . LEU B 329 ? 0.4234 0.4554 0.5615 0.0258  0.1193  0.0764  329  LEU B CA  
5337  C  C   . LEU B 329 ? 0.4199 0.4363 0.5291 0.0341  0.1240  0.0772  329  LEU B C   
5338  O  O   . LEU B 329 ? 0.5444 0.5604 0.6401 0.0431  0.1258  0.0743  329  LEU B O   
5339  C  CB  . LEU B 329 ? 0.4399 0.4855 0.5988 0.0213  0.1298  0.0863  329  LEU B CB  
5340  C  CG  . LEU B 329 ? 0.4573 0.5269 0.6467 0.0169  0.1291  0.0876  329  LEU B CG  
5341  C  CD1 . LEU B 329 ? 0.4407 0.5164 0.6335 0.0178  0.1165  0.0784  329  LEU B CD1 
5342  C  CD2 . LEU B 329 ? 0.4879 0.5624 0.7014 0.0036  0.1292  0.0926  329  LEU B CD2 
5343  N  N   . GLN B 330 ? 0.3521 0.3550 0.4520 0.0311  0.1256  0.0814  330  GLN B N   
5344  C  CA  . GLN B 330 ? 0.5118 0.5002 0.5837 0.0379  0.1285  0.0827  330  GLN B CA  
5345  C  C   . GLN B 330 ? 0.5774 0.5554 0.6308 0.0424  0.1187  0.0730  330  GLN B C   
5346  O  O   . GLN B 330 ? 0.6039 0.5757 0.6361 0.0499  0.1209  0.0715  330  GLN B O   
5347  C  CB  . GLN B 330 ? 0.6397 0.6165 0.7082 0.0332  0.1304  0.0902  330  GLN B CB  
5348  C  CG  . GLN B 330 ? 0.6394 0.6242 0.7204 0.0297  0.1424  0.1023  330  GLN B CG  
5349  C  CD  . GLN B 330 ? 0.7516 0.7450 0.8206 0.0381  0.1545  0.1065  330  GLN B CD  
5350  O  OE1 . GLN B 330 ? 0.7020 0.6861 0.7450 0.0446  0.1580  0.1085  330  GLN B OE1 
5351  N  NE2 . GLN B 330 ? 0.8705 0.8825 0.9584 0.0385  0.1607  0.1075  330  GLN B NE2 
5352  N  N   . LEU B 331 ? 0.2709 0.2475 0.3323 0.0376  0.1080  0.0664  331  LEU B N   
5353  C  CA  . LEU B 331 ? 0.2933 0.2638 0.3411 0.0410  0.0993  0.0580  331  LEU B CA  
5354  C  C   . LEU B 331 ? 0.2912 0.2683 0.3356 0.0474  0.1007  0.0552  331  LEU B C   
5355  O  O   . LEU B 331 ? 0.3706 0.3392 0.3958 0.0534  0.1005  0.0525  331  LEU B O   
5356  C  CB  . LEU B 331 ? 0.3990 0.3703 0.4574 0.0349  0.0892  0.0516  331  LEU B CB  
5357  C  CG  . LEU B 331 ? 0.4970 0.4614 0.5415 0.0371  0.0806  0.0444  331  LEU B CG  
5358  C  CD1 . LEU B 331 ? 0.3261 0.2924 0.3808 0.0312  0.0725  0.0382  331  LEU B CD1 
5359  C  CD2 . LEU B 331 ? 0.7125 0.6810 0.7500 0.0423  0.0794  0.0415  331  LEU B CD2 
5360  N  N   . LEU B 332 ? 0.2948 0.2865 0.3586 0.0460  0.1015  0.0557  332  LEU B N   
5361  C  CA  . LEU B 332 ? 0.3437 0.3424 0.4080 0.0529  0.1032  0.0541  332  LEU B CA  
5362  C  C   . LEU B 332 ? 0.4249 0.4170 0.4722 0.0615  0.1125  0.0559  332  LEU B C   
5363  O  O   . LEU B 332 ? 0.4598 0.4450 0.4940 0.0679  0.1109  0.0514  332  LEU B O   
5364  C  CB  . LEU B 332 ? 0.4992 0.5175 0.5895 0.0508  0.1053  0.0574  332  LEU B CB  
5365  C  CG  . LEU B 332 ? 0.5538 0.5805 0.6594 0.0432  0.0945  0.0537  332  LEU B CG  
5366  C  CD1 . LEU B 332 ? 0.4536 0.5011 0.5863 0.0396  0.0963  0.0577  332  LEU B CD1 
5367  C  CD2 . LEU B 332 ? 0.4708 0.4946 0.5672 0.0466  0.0857  0.0482  332  LEU B CD2 
5368  N  N   . ARG B 333 ? 0.5231 0.5169 0.5702 0.0614  0.1223  0.0624  333  ARG B N   
5369  C  CA  . ARG B 333 ? 0.3951 0.3837 0.4238 0.0695  0.1324  0.0641  333  ARG B CA  
5370  C  C   . ARG B 333 ? 0.4330 0.4033 0.4333 0.0726  0.1274  0.0588  333  ARG B C   
5371  O  O   . ARG B 333 ? 0.6728 0.6367 0.6546 0.0803  0.1327  0.0563  333  ARG B O   
5372  C  CB  . ARG B 333 ? 0.3342 0.3282 0.3670 0.0670  0.1431  0.0736  333  ARG B CB  
5373  C  CG  . ARG B 333 ? 0.4874 0.5014 0.5486 0.0643  0.1498  0.0794  333  ARG B CG  
5374  C  CD  . ARG B 333 ? 0.7283 0.7495 0.7849 0.0704  0.1655  0.0861  333  ARG B CD  
5375  N  NE  . ARG B 333 ? 0.7744 0.8176 0.8590 0.0703  0.1728  0.0908  333  ARG B NE  
5376  C  CZ  . ARG B 333 ? 0.8458 0.9002 0.9333 0.0800  0.1828  0.0908  333  ARG B CZ  
5377  N  NH1 . ARG B 333 ? 0.7316 0.7750 0.7935 0.0910  0.1874  0.0852  333  ARG B NH1 
5378  N  NH2 . ARG B 333 ? 0.8928 0.9700 1.0104 0.0786  0.1881  0.0961  333  ARG B NH2 
5379  N  N   . GLN B 334 ? 0.3197 0.2820 0.3167 0.0669  0.1174  0.0567  334  GLN B N   
5380  C  CA  . GLN B 334 ? 0.3398 0.2875 0.3135 0.0689  0.1111  0.0518  334  GLN B CA  
5381  C  C   . GLN B 334 ? 0.4646 0.4077 0.4315 0.0734  0.1065  0.0441  334  GLN B C   
5382  O  O   . GLN B 334 ? 0.5600 0.4911 0.5071 0.0757  0.1024  0.0394  334  GLN B O   
5383  C  CB  . GLN B 334 ? 0.4429 0.3859 0.4190 0.0623  0.1018  0.0514  334  GLN B CB  
5384  C  CG  . GLN B 334 ? 0.5158 0.4566 0.4919 0.0592  0.1054  0.0591  334  GLN B CG  
5385  C  CD  . GLN B 334 ? 0.5555 0.4867 0.5065 0.0637  0.1079  0.0616  334  GLN B CD  
5386  O  OE1 . GLN B 334 ? 0.6932 0.6159 0.6293 0.0648  0.1002  0.0573  334  GLN B OE1 
5387  N  NE2 . GLN B 334 ? 0.4753 0.4092 0.4216 0.0661  0.1187  0.0690  334  GLN B NE2 
5388  N  N   . ALA B 335 ? 0.5097 0.4622 0.4937 0.0743  0.1065  0.0432  335  ALA B N   
5389  C  CA  . ALA B 335 ? 0.5079 0.4554 0.4876 0.0788  0.1026  0.0375  335  ALA B CA  
5390  C  C   . ALA B 335 ? 0.5204 0.4610 0.4854 0.0879  0.1111  0.0352  335  ALA B C   
5391  O  O   . ALA B 335 ? 0.6825 0.6174 0.6446 0.0933  0.1102  0.0306  335  ALA B O   
5392  C  CB  . ALA B 335 ? 0.2995 0.2601 0.3018 0.0782  0.1003  0.0388  335  ALA B CB  
5393  N  N   . HIS B 336 ? 0.4189 0.3594 0.3737 0.0897  0.1196  0.0384  336  HIS B N   
5394  C  CA  . HIS B 336 ? 0.5157 0.4502 0.4537 0.0988  0.1288  0.0353  336  HIS B CA  
5395  C  C   . HIS B 336 ? 0.5379 0.4588 0.4469 0.0994  0.1279  0.0325  336  HIS B C   
5396  O  O   . HIS B 336 ? 0.5642 0.4787 0.4546 0.1067  0.1348  0.0285  336  HIS B O   
5397  C  CB  . HIS B 336 ? 0.4267 0.3767 0.3780 0.1030  0.1426  0.0417  336  HIS B CB  
5398  C  CG  . HIS B 336 ? 0.5102 0.4751 0.4902 0.1033  0.1428  0.0440  336  HIS B CG  
5399  N  ND1 . HIS B 336 ? 0.5303 0.4939 0.5147 0.1112  0.1432  0.0394  336  HIS B ND1 
5400  C  CD2 . HIS B 336 ? 0.5491 0.5300 0.5548 0.0967  0.1414  0.0504  336  HIS B CD2 
5401  C  CE1 . HIS B 336 ? 0.5512 0.5313 0.5629 0.1099  0.1421  0.0439  336  HIS B CE1 
5402  N  NE2 . HIS B 336 ? 0.6666 0.6578 0.6913 0.1006  0.1407  0.0499  336  HIS B NE2 
5403  N  N   . ILE B 337 ? 0.3992 0.3372 0.2468 0.0756  0.0695  0.0770  337  ILE B N   
5404  C  CA  . ILE B 337 ? 0.4859 0.4252 0.3197 0.0789  0.0653  0.0758  337  ILE B CA  
5405  C  C   . ILE B 337 ? 0.5529 0.4912 0.3878 0.0802  0.0577  0.0658  337  ILE B C   
5406  O  O   . ILE B 337 ? 0.6490 0.5838 0.4953 0.0780  0.0556  0.0610  337  ILE B O   
5407  C  CB  . ILE B 337 ? 0.5745 0.5109 0.4047 0.0779  0.0629  0.0839  337  ILE B CB  
5408  C  CG1 . ILE B 337 ? 0.6480 0.5797 0.4912 0.0741  0.0571  0.0837  337  ILE B CG1 
5409  C  CG2 . ILE B 337 ? 0.6239 0.5598 0.4519 0.0764  0.0707  0.0936  337  ILE B CG2 
5410  C  CD1 . ILE B 337 ? 0.5200 0.4495 0.3604 0.0738  0.0540  0.0903  337  ILE B CD1 
5411  N  N   . GLY B 338 ? 0.6205 0.5616 0.4431 0.0838  0.0536  0.0625  338  GLY B N   
5412  C  CA  . GLY B 338 ? 0.5408 0.4817 0.3642 0.0848  0.0462  0.0524  338  GLY B CA  
5413  C  C   . GLY B 338 ? 0.4898 0.4315 0.3131 0.0869  0.0477  0.0435  338  GLY B C   
5414  O  O   . GLY B 338 ? 0.6655 0.6117 0.4798 0.0905  0.0533  0.0435  338  GLY B O   
5415  N  N   . ILE B 339 ? 0.3904 0.3276 0.2236 0.0848  0.0432  0.0361  339  ILE B N   
5416  C  CA  . ILE B 339 ? 0.5123 0.4485 0.3461 0.0870  0.0438  0.0268  339  ILE B CA  
5417  C  C   . ILE B 339 ? 0.5627 0.4916 0.4109 0.0838  0.0446  0.0255  339  ILE B C   
5418  O  O   . ILE B 339 ? 0.5042 0.4287 0.3620 0.0796  0.0442  0.0313  339  ILE B O   
5419  C  CB  . ILE B 339 ? 0.4854 0.4218 0.3146 0.0888  0.0367  0.0163  339  ILE B CB  
5420  C  CG1 . ILE B 339 ? 0.5492 0.4812 0.3880 0.0839  0.0301  0.0155  339  ILE B CG1 
5421  C  CG2 . ILE B 339 ? 0.4591 0.4032 0.2717 0.0939  0.0358  0.0158  339  ILE B CG2 
5422  C  CD1 . ILE B 339 ? 0.3914 0.3241 0.2283 0.0846  0.0228  0.0045  339  ILE B CD1 
5423  N  N   . LYS B 340 ? 0.5523 0.4796 0.4008 0.0866  0.0456  0.0177  340  LYS B N   
5424  C  CA  . LYS B 340 ? 0.5299 0.4488 0.3897 0.0850  0.0453  0.0147  340  LYS B CA  
5425  C  C   . LYS B 340 ? 0.6220 0.5385 0.4787 0.0889  0.0440  0.0036  340  LYS B C   
5426  O  O   . LYS B 340 ? 0.6676 0.5909 0.5138 0.0935  0.0454  -0.0006 340  LYS B O   
5427  C  CB  . LYS B 340 ? 0.5283 0.4483 0.3947 0.0849  0.0514  0.0213  340  LYS B CB  
5428  C  CG  . LYS B 340 ? 0.4531 0.3817 0.3134 0.0894  0.0577  0.0208  340  LYS B CG  
5429  C  CD  . LYS B 340 ? 0.5016 0.4316 0.3716 0.0888  0.0629  0.0258  340  LYS B CD  
5430  C  CE  . LYS B 340 ? 0.4197 0.3601 0.2856 0.0923  0.0704  0.0261  340  LYS B CE  
5431  N  NZ  . LYS B 340 ? 0.4406 0.3836 0.3180 0.0912  0.0750  0.0303  340  LYS B NZ  
5432  N  N   . GLY B 341 ? 0.4348 0.3410 0.2997 0.0875  0.0415  -0.0010 341  GLY B N   
5433  C  CA  . GLY B 341 ? 0.4604 0.3620 0.3229 0.0912  0.0398  -0.0119 341  GLY B CA  
5434  C  C   . GLY B 341 ? 0.5238 0.4112 0.3953 0.0888  0.0369  -0.0156 341  GLY B C   
5435  O  O   . GLY B 341 ? 0.4593 0.3407 0.3390 0.0850  0.0373  -0.0092 341  GLY B O   
5436  N  N   . LEU B 342 ? 0.5636 0.4450 0.4328 0.0912  0.0342  -0.0261 342  LEU B N   
5437  C  CA  . LEU B 342 ? 0.5475 0.4134 0.4236 0.0896  0.0321  -0.0302 342  LEU B CA  
5438  C  C   . LEU B 342 ? 0.5641 0.4232 0.4408 0.0858  0.0264  -0.0383 342  LEU B C   
5439  O  O   . LEU B 342 ? 0.6422 0.5079 0.5120 0.0876  0.0236  -0.0455 342  LEU B O   
5440  C  CB  . LEU B 342 ? 0.5066 0.3690 0.3807 0.0965  0.0343  -0.0363 342  LEU B CB  
5441  C  CG  . LEU B 342 ? 0.5456 0.4163 0.4207 0.1005  0.0400  -0.0299 342  LEU B CG  
5442  C  CD1 . LEU B 342 ? 0.4715 0.3422 0.3439 0.1082  0.0419  -0.0375 342  LEU B CD1 
5443  C  CD2 . LEU B 342 ? 0.4316 0.2960 0.3157 0.0972  0.0411  -0.0209 342  LEU B CD2 
5444  N  N   . VAL B 343 ? 0.4771 0.3231 0.3620 0.0805  0.0248  -0.0373 343  VAL B N   
5445  C  CA  . VAL B 343 ? 0.5933 0.4301 0.4809 0.0765  0.0202  -0.0463 343  VAL B CA  
5446  C  C   . VAL B 343 ? 0.5855 0.4062 0.4743 0.0792  0.0209  -0.0516 343  VAL B C   
5447  O  O   . VAL B 343 ? 0.5808 0.3912 0.4740 0.0787  0.0235  -0.0456 343  VAL B O   
5448  C  CB  . VAL B 343 ? 0.5763 0.4092 0.4726 0.0679  0.0183  -0.0422 343  VAL B CB  
5449  C  CG1 . VAL B 343 ? 0.4911 0.3150 0.3913 0.0634  0.0140  -0.0528 343  VAL B CG1 
5450  C  CG2 . VAL B 343 ? 0.5568 0.4055 0.4517 0.0662  0.0173  -0.0366 343  VAL B CG2 
5451  N  N   . THR B 344 ? 0.6816 0.4999 0.5657 0.0827  0.0184  -0.0630 344  THR B N   
5452  C  CA  . THR B 344 ? 0.6715 0.4761 0.5546 0.0875  0.0193  -0.0686 344  THR B CA  
5453  C  C   . THR B 344 ? 0.7015 0.4930 0.5854 0.0855  0.0151  -0.0807 344  THR B C   
5454  O  O   . THR B 344 ? 0.6396 0.4358 0.5243 0.0811  0.0110  -0.0867 344  THR B O   
5455  C  CB  . THR B 344 ? 0.7047 0.5198 0.5800 0.0969  0.0219  -0.0708 344  THR B CB  
5456  O  OG1 . THR B 344 ? 0.9902 0.7929 0.8661 0.1023  0.0236  -0.0728 344  THR B OG1 
5457  C  CG2 . THR B 344 ? 0.5489 0.3723 0.4162 0.1001  0.0188  -0.0820 344  THR B CG2 
5458  N  N   . ASP B 345 ? 0.5495 0.3243 0.4335 0.0889  0.0159  -0.0843 345  ASP B N   
5459  C  CA  . ASP B 345 ? 0.5940 0.3533 0.4780 0.0885  0.0127  -0.0962 345  ASP B CA  
5460  C  C   . ASP B 345 ? 0.6860 0.4548 0.5625 0.0941  0.0097  -0.1081 345  ASP B C   
5461  O  O   . ASP B 345 ? 0.6654 0.4502 0.5350 0.1008  0.0115  -0.1071 345  ASP B O   
5462  C  CB  . ASP B 345 ? 0.6849 0.4260 0.5677 0.0942  0.0148  -0.0963 345  ASP B CB  
5463  C  CG  . ASP B 345 ? 0.7507 0.4692 0.6396 0.0878  0.0152  -0.0938 345  ASP B CG  
5464  O  OD1 . ASP B 345 ? 0.8836 0.5864 0.7709 0.0926  0.0171  -0.0918 345  ASP B OD1 
5465  O  OD2 . ASP B 345 ? 0.9784 0.6950 0.8735 0.0783  0.0137  -0.0940 345  ASP B OD2 
5466  N  N   . ALA B 346 ? 0.8361 0.5945 0.7139 0.0913  0.0054  -0.1197 346  ALA B N   
5467  C  CA  . ALA B 346 ? 0.7950 0.5552 0.6652 0.0984  0.0027  -0.1328 346  ALA B CA  
5468  C  C   . ALA B 346 ? 0.6781 0.4345 0.5432 0.1083  0.0067  -0.1309 346  ALA B C   
5469  O  O   . ALA B 346 ? 0.5565 0.3265 0.4137 0.1166  0.0078  -0.1341 346  ALA B O   
5470  C  CB  . ALA B 346 ? 0.5300 0.2721 0.4044 0.0939  -0.0017 -0.1448 346  ALA B CB  
5471  N  N   . SER B 347 ? 0.5876 0.3260 0.4574 0.1074  0.0089  -0.1254 347  SER B N   
5472  C  CA  . SER B 347 ? 0.7415 0.4748 0.6081 0.1167  0.0122  -0.1231 347  SER B CA  
5473  C  C   . SER B 347 ? 0.7581 0.5132 0.6219 0.1219  0.0161  -0.1153 347  SER B C   
5474  O  O   . SER B 347 ? 0.7681 0.5274 0.6279 0.1312  0.0182  -0.1175 347  SER B O   
5475  C  CB  . SER B 347 ? 0.9984 0.7108 0.8703 0.1140  0.0140  -0.1153 347  SER B CB  
5476  O  OG  . SER B 347 ? 1.1619 0.8528 1.0371 0.1076  0.0114  -0.1210 347  SER B OG  
5477  N  N   . GLY B 348 ? 0.7524 0.5212 0.6188 0.1158  0.0172  -0.1063 348  GLY B N   
5478  C  CA  . GLY B 348 ? 0.5946 0.3821 0.4598 0.1190  0.0215  -0.0973 348  GLY B CA  
5479  C  C   . GLY B 348 ? 0.6312 0.4128 0.5031 0.1162  0.0242  -0.0852 348  GLY B C   
5480  O  O   . GLY B 348 ? 0.6722 0.4655 0.5449 0.1194  0.0279  -0.0777 348  GLY B O   
5481  N  N   . PHE B 349 ? 0.5578 0.3214 0.4346 0.1099  0.0224  -0.0834 349  PHE B N   
5482  C  CA  . PHE B 349 ? 0.4415 0.1959 0.3234 0.1077  0.0246  -0.0728 349  PHE B CA  
5483  C  C   . PHE B 349 ? 0.6559 0.4152 0.5431 0.0981  0.0248  -0.0641 349  PHE B C   
5484  O  O   . PHE B 349 ? 0.4942 0.2502 0.3837 0.0909  0.0222  -0.0675 349  PHE B O   
5485  C  CB  . PHE B 349 ? 0.5950 0.3235 0.4776 0.1083  0.0236  -0.0758 349  PHE B CB  
5486  C  CG  . PHE B 349 ? 0.6853 0.4037 0.5701 0.1097  0.0259  -0.0659 349  PHE B CG  
5487  C  CD1 . PHE B 349 ? 0.7017 0.4205 0.5842 0.1197  0.0273  -0.0651 349  PHE B CD1 
5488  C  CD2 . PHE B 349 ? 0.6489 0.3588 0.5381 0.1016  0.0267  -0.0577 349  PHE B CD2 
5489  C  CE1 . PHE B 349 ? 0.5816 0.2918 0.4655 0.1218  0.0287  -0.0565 349  PHE B CE1 
5490  C  CE2 . PHE B 349 ? 0.6670 0.3679 0.5569 0.1035  0.0287  -0.0487 349  PHE B CE2 
5491  C  CZ  . PHE B 349 ? 0.7495 0.4504 0.6365 0.1138  0.0294  -0.0481 349  PHE B CZ  
5492  N  N   . PRO B 350 ? 0.6737 0.4407 0.5634 0.0981  0.0277  -0.0533 350  PRO B N   
5493  C  CA  . PRO B 350 ? 0.5370 0.3140 0.4306 0.0908  0.0282  -0.0450 350  PRO B CA  
5494  C  C   . PRO B 350 ? 0.6134 0.3765 0.5124 0.0821  0.0270  -0.0427 350  PRO B C   
5495  O  O   . PRO B 350 ? 0.5798 0.3242 0.4799 0.0820  0.0276  -0.0421 350  PRO B O   
5496  C  CB  . PRO B 350 ? 0.4812 0.2652 0.3765 0.0941  0.0316  -0.0352 350  PRO B CB  
5497  C  CG  . PRO B 350 ? 0.6303 0.4004 0.5247 0.1010  0.0322  -0.0370 350  PRO B CG  
5498  C  CD  . PRO B 350 ? 0.5678 0.3323 0.4575 0.1053  0.0302  -0.0487 350  PRO B CD  
5499  N  N   . ILE B 351 ? 0.5764 0.3486 0.4783 0.0751  0.0254  -0.0418 351  ILE B N   
5500  C  CA  . ILE B 351 ? 0.4204 0.1832 0.3290 0.0662  0.0251  -0.0388 351  ILE B CA  
5501  C  C   . ILE B 351 ? 0.5369 0.3075 0.4490 0.0633  0.0273  -0.0269 351  ILE B C   
5502  O  O   . ILE B 351 ? 0.3725 0.1604 0.2842 0.0629  0.0270  -0.0236 351  ILE B O   
5503  C  CB  . ILE B 351 ? 0.5309 0.2981 0.4424 0.0600  0.0213  -0.0468 351  ILE B CB  
5504  C  CG1 . ILE B 351 ? 0.6497 0.4099 0.5575 0.0631  0.0186  -0.0596 351  ILE B CG1 
5505  C  CG2 . ILE B 351 ? 0.5072 0.2640 0.4271 0.0506  0.0217  -0.0444 351  ILE B CG2 
5506  C  CD1 . ILE B 351 ? 0.4758 0.2451 0.3850 0.0590  0.0138  -0.0693 351  ILE B CD1 
5507  N  N   . ALA B 352 ? 0.5434 0.3003 0.4582 0.0616  0.0297  -0.0204 352  ALA B N   
5508  C  CA  . ALA B 352 ? 0.4629 0.2248 0.3807 0.0595  0.0319  -0.0095 352  ALA B CA  
5509  C  C   . ALA B 352 ? 0.5590 0.3232 0.4833 0.0503  0.0312  -0.0079 352  ALA B C   
5510  O  O   . ALA B 352 ? 0.5947 0.3491 0.5223 0.0450  0.0302  -0.0138 352  ALA B O   
5511  C  CB  . ALA B 352 ? 0.3921 0.1381 0.3088 0.0625  0.0345  -0.0038 352  ALA B CB  
5512  N  N   . ASP B 353 ? 0.4943 0.2714 0.4209 0.0485  0.0318  -0.0005 353  ASP B N   
5513  C  CA  . ASP B 353 ? 0.4161 0.1970 0.3494 0.0406  0.0313  0.0016  353  ASP B CA  
5514  C  C   . ASP B 353 ? 0.5204 0.3095 0.4561 0.0368  0.0274  -0.0074 353  ASP B C   
5515  O  O   . ASP B 353 ? 0.5762 0.3651 0.5191 0.0296  0.0266  -0.0090 353  ASP B O   
5516  C  CB  . ASP B 353 ? 0.7377 0.5008 0.6751 0.0355  0.0340  0.0043  353  ASP B CB  
5517  C  CG  . ASP B 353 ? 1.0217 0.7850 0.9608 0.0345  0.0369  0.0150  353  ASP B CG  
5518  O  OD1 . ASP B 353 ? 1.1075 0.8762 1.0528 0.0282  0.0372  0.0175  353  ASP B OD1 
5519  O  OD2 . ASP B 353 ? 1.1293 0.8881 1.0638 0.0404  0.0386  0.0205  353  ASP B OD2 
5520  N  N   . ALA B 354 ? 0.5878 0.3847 0.5177 0.0418  0.0250  -0.0138 354  ALA B N   
5521  C  CA  . ALA B 354 ? 0.6405 0.4482 0.5709 0.0399  0.0206  -0.0223 354  ALA B CA  
5522  C  C   . ALA B 354 ? 0.6829 0.5082 0.6137 0.0391  0.0192  -0.0170 354  ALA B C   
5523  O  O   . ALA B 354 ? 0.4856 0.3156 0.4144 0.0416  0.0218  -0.0076 354  ALA B O   
5524  C  CB  . ALA B 354 ? 0.5412 0.3516 0.4634 0.0466  0.0188  -0.0304 354  ALA B CB  
5525  N  N   . ASN B 355 ? 0.6402 0.4748 0.5739 0.0358  0.0149  -0.0232 355  ASN B N   
5526  C  CA  . ASN B 355 ? 0.6364 0.4871 0.5701 0.0356  0.0129  -0.0188 355  ASN B CA  
5527  C  C   . ASN B 355 ? 0.6351 0.4992 0.5595 0.0413  0.0093  -0.0236 355  ASN B C   
5528  O  O   . ASN B 355 ? 0.5998 0.4644 0.5219 0.0422  0.0057  -0.0342 355  ASN B O   
5529  C  CB  . ASN B 355 ? 0.7143 0.5678 0.6590 0.0280  0.0106  -0.0207 355  ASN B CB  
5530  C  CG  . ASN B 355 ? 0.7358 0.5808 0.6879 0.0232  0.0151  -0.0120 355  ASN B CG  
5531  O  OD1 . ASN B 355 ? 0.7683 0.6033 0.7287 0.0168  0.0164  -0.0148 355  ASN B OD1 
5532  N  ND2 . ASN B 355 ? 0.7071 0.5559 0.6561 0.0261  0.0177  -0.0016 355  ASN B ND2 
5533  N  N   . VAL B 356 ? 0.5144 0.3887 0.4327 0.0452  0.0104  -0.0157 356  VAL B N   
5534  C  CA  . VAL B 356 ? 0.4757 0.3620 0.3832 0.0510  0.0079  -0.0184 356  VAL B CA  
5535  C  C   . VAL B 356 ? 0.4770 0.3753 0.3847 0.0503  0.0049  -0.0145 356  VAL B C   
5536  O  O   . VAL B 356 ? 0.4106 0.3107 0.3197 0.0498  0.0075  -0.0045 356  VAL B O   
5537  C  CB  . VAL B 356 ? 0.6018 0.4892 0.5000 0.0573  0.0127  -0.0127 356  VAL B CB  
5538  C  CG1 . VAL B 356 ? 0.5921 0.4922 0.4781 0.0631  0.0112  -0.0139 356  VAL B CG1 
5539  C  CG2 . VAL B 356 ? 0.4224 0.2989 0.3201 0.0593  0.0152  -0.0176 356  VAL B CG2 
5540  N  N   . TYR B 357 ? 0.6182 0.5246 0.5245 0.0507  -0.0011 -0.0231 357  TYR B N   
5541  C  CA  . TYR B 357 ? 0.5645 0.4828 0.4713 0.0506  -0.0055 -0.0216 357  TYR B CA  
5542  C  C   . TYR B 357 ? 0.6561 0.5854 0.5476 0.0584  -0.0079 -0.0216 357  TYR B C   
5543  O  O   . TYR B 357 ? 0.6075 0.5377 0.4899 0.0629  -0.0089 -0.0284 357  TYR B O   
5544  C  CB  . TYR B 357 ? 0.5249 0.4456 0.4422 0.0454  -0.0113 -0.0323 357  TYR B CB  
5545  C  CG  . TYR B 357 ? 0.5106 0.4224 0.4435 0.0369  -0.0091 -0.0318 357  TYR B CG  
5546  C  CD1 . TYR B 357 ? 0.4478 0.3469 0.3866 0.0327  -0.0074 -0.0383 357  TYR B CD1 
5547  C  CD2 . TYR B 357 ? 0.5894 0.5053 0.5307 0.0332  -0.0085 -0.0251 357  TYR B CD2 
5548  C  CE1 . TYR B 357 ? 0.5504 0.4403 0.5024 0.0248  -0.0047 -0.0372 357  TYR B CE1 
5549  C  CE2 . TYR B 357 ? 0.4218 0.3299 0.3766 0.0255  -0.0058 -0.0244 357  TYR B CE2 
5550  C  CZ  . TYR B 357 ? 0.5285 0.4235 0.4883 0.0212  -0.0037 -0.0301 357  TYR B CZ  
5551  O  OH  . TYR B 357 ? 0.6850 0.5713 0.6570 0.0135  -0.0002 -0.0286 357  TYR B OH  
5552  N  N   . VAL B 358 ? 0.7865 0.7236 0.6749 0.0603  -0.0088 -0.0140 358  VAL B N   
5553  C  CA  . VAL B 358 ? 0.6502 0.5973 0.5237 0.0677  -0.0116 -0.0133 358  VAL B CA  
5554  C  C   . VAL B 358 ? 0.6946 0.6518 0.5716 0.0676  -0.0193 -0.0173 358  VAL B C   
5555  O  O   . VAL B 358 ? 0.6706 0.6287 0.5585 0.0633  -0.0197 -0.0130 358  VAL B O   
5556  C  CB  . VAL B 358 ? 0.4402 0.3871 0.3045 0.0713  -0.0057 0.0000  358  VAL B CB  
5557  C  CG1 . VAL B 358 ? 0.3499 0.3053 0.1972 0.0790  -0.0080 0.0013  358  VAL B CG1 
5558  C  CG2 . VAL B 358 ? 0.3514 0.2900 0.2143 0.0713  0.0018  0.0035  358  VAL B CG2 
5559  N  N   . ALA B 359 ? 0.6895 0.6551 0.5576 0.0727  -0.0255 -0.0259 359  ALA B N   
5560  C  CA  . ALA B 359 ? 0.6796 0.6564 0.5506 0.0737  -0.0338 -0.0314 359  ALA B CA  
5561  C  C   . ALA B 359 ? 0.5820 0.5628 0.4505 0.0760  -0.0333 -0.0199 359  ALA B C   
5562  O  O   . ALA B 359 ? 0.5744 0.5541 0.4284 0.0817  -0.0297 -0.0107 359  ALA B O   
5563  C  CB  . ALA B 359 ? 0.7293 0.7144 0.5864 0.0812  -0.0402 -0.0406 359  ALA B CB  
5564  N  N   . GLY B 360 ? 0.4055 0.3907 0.2881 0.0716  -0.0366 -0.0207 360  GLY B N   
5565  C  CA  . GLY B 360 ? 0.3917 0.3802 0.2728 0.0739  -0.0364 -0.0104 360  GLY B CA  
5566  C  C   . GLY B 360 ? 0.5655 0.5438 0.4523 0.0694  -0.0281 0.0012  360  GLY B C   
5567  O  O   . GLY B 360 ? 0.7679 0.7472 0.6544 0.0707  -0.0270 0.0102  360  GLY B O   
5568  N  N   . LEU B 361 ? 0.4847 0.4532 0.3766 0.0645  -0.0225 0.0005  361  LEU B N   
5569  C  CA  . LEU B 361 ? 0.4803 0.4393 0.3796 0.0599  -0.0154 0.0097  361  LEU B CA  
5570  C  C   . LEU B 361 ? 0.5509 0.5024 0.4638 0.0524  -0.0134 0.0040  361  LEU B C   
5571  O  O   . LEU B 361 ? 0.5244 0.4657 0.4397 0.0499  -0.0072 0.0090  361  LEU B O   
5572  C  CB  . LEU B 361 ? 0.3828 0.3354 0.2703 0.0634  -0.0089 0.0180  361  LEU B CB  
5573  C  CG  . LEU B 361 ? 0.4699 0.4268 0.3429 0.0702  -0.0087 0.0260  361  LEU B CG  
5574  C  CD1 . LEU B 361 ? 0.5990 0.5505 0.4613 0.0729  -0.0018 0.0316  361  LEU B CD1 
5575  C  CD2 . LEU B 361 ? 0.4686 0.4258 0.3467 0.0692  -0.0083 0.0348  361  LEU B CD2 
5576  N  N   . GLU B 362 ? 0.5532 0.5096 0.4752 0.0491  -0.0187 -0.0067 362  GLU B N   
5577  C  CA  . GLU B 362 ? 0.5380 0.4863 0.4722 0.0418  -0.0170 -0.0134 362  GLU B CA  
5578  C  C   . GLU B 362 ? 0.5811 0.5234 0.5284 0.0351  -0.0125 -0.0073 362  GLU B C   
5579  O  O   . GLU B 362 ? 0.5333 0.4656 0.4891 0.0292  -0.0092 -0.0098 362  GLU B O   
5580  C  CB  . GLU B 362 ? 0.5073 0.4628 0.4482 0.0396  -0.0239 -0.0275 362  GLU B CB  
5581  C  CG  . GLU B 362 ? 0.7633 0.7167 0.6951 0.0429  -0.0260 -0.0366 362  GLU B CG  
5582  C  CD  . GLU B 362 ? 1.0834 1.0507 1.0089 0.0483  -0.0347 -0.0459 362  GLU B CD  
5583  O  OE1 . GLU B 362 ? 1.1099 1.0878 1.0312 0.0527  -0.0383 -0.0420 362  GLU B OE1 
5584  O  OE2 . GLU B 362 ? 1.0795 1.0466 1.0036 0.0486  -0.0382 -0.0574 362  GLU B OE2 
5585  N  N   . GLU B 363 ? 0.5422 0.4897 0.4901 0.0366  -0.0122 0.0010  363  GLU B N   
5586  C  CA  . GLU B 363 ? 0.5070 0.4498 0.4663 0.0310  -0.0081 0.0068  363  GLU B CA  
5587  C  C   . GLU B 363 ? 0.5716 0.5017 0.5268 0.0312  -0.0010 0.0161  363  GLU B C   
5588  O  O   . GLU B 363 ? 0.3889 0.3120 0.3524 0.0265  0.0032  0.0202  363  GLU B O   
5589  C  CB  . GLU B 363 ? 0.7028 0.6562 0.6650 0.0327  -0.0108 0.0112  363  GLU B CB  
5590  C  CG  . GLU B 363 ? 0.9938 0.9600 0.9658 0.0308  -0.0174 0.0013  363  GLU B CG  
5591  C  CD  . GLU B 363 ? 1.1696 1.1460 1.1461 0.0326  -0.0198 0.0056  363  GLU B CD  
5592  O  OE1 . GLU B 363 ? 1.0846 1.0643 1.0495 0.0398  -0.0215 0.0120  363  GLU B OE1 
5593  O  OE2 . GLU B 363 ? 1.3127 1.2936 1.3043 0.0268  -0.0198 0.0024  363  GLU B OE2 
5594  N  N   . LYS B 364 ? 0.5234 0.4514 0.4658 0.0368  0.0003  0.0192  364  LYS B N   
5595  C  CA  . LYS B 364 ? 0.4962 0.4140 0.4347 0.0377  0.0065  0.0266  364  LYS B CA  
5596  C  C   . LYS B 364 ? 0.6112 0.5234 0.5427 0.0400  0.0078  0.0218  364  LYS B C   
5597  O  O   . LYS B 364 ? 0.6637 0.5785 0.5843 0.0454  0.0087  0.0241  364  LYS B O   
5598  C  CB  . LYS B 364 ? 0.4954 0.4164 0.4263 0.0423  0.0082  0.0366  364  LYS B CB  
5599  C  CG  . LYS B 364 ? 0.3943 0.3060 0.3234 0.0428  0.0142  0.0437  364  LYS B CG  
5600  C  CD  . LYS B 364 ? 0.3389 0.2422 0.2784 0.0377  0.0169  0.0451  364  LYS B CD  
5601  C  CE  . LYS B 364 ? 0.4040 0.2993 0.3425 0.0388  0.0219  0.0522  364  LYS B CE  
5602  N  NZ  . LYS B 364 ? 0.2910 0.1761 0.2372 0.0346  0.0244  0.0521  364  LYS B NZ  
5603  N  N   . PRO B 365 ? 0.4705 0.3747 0.4083 0.0359  0.0082  0.0151  365  PRO B N   
5604  C  CA  . PRO B 365 ? 0.4680 0.3648 0.4007 0.0378  0.0096  0.0100  365  PRO B CA  
5605  C  C   . PRO B 365 ? 0.5768 0.4650 0.5065 0.0399  0.0153  0.0175  365  PRO B C   
5606  O  O   . PRO B 365 ? 0.5856 0.4706 0.5200 0.0380  0.0181  0.0252  365  PRO B O   
5607  C  CB  . PRO B 365 ? 0.5913 0.4801 0.5338 0.0316  0.0089  0.0021  365  PRO B CB  
5608  C  CG  . PRO B 365 ? 0.5475 0.4419 0.5005 0.0264  0.0069  0.0023  365  PRO B CG  
5609  C  CD  . PRO B 365 ? 0.5346 0.4353 0.4853 0.0289  0.0081  0.0126  365  PRO B CD  
5610  N  N   . MET B 366 ? 0.5685 0.4539 0.4909 0.0441  0.0169  0.0149  366  MET B N   
5611  C  CA  . MET B 366 ? 0.3543 0.2319 0.2754 0.0463  0.0218  0.0201  366  MET B CA  
5612  C  C   . MET B 366 ? 0.4467 0.3111 0.3718 0.0443  0.0227  0.0145  366  MET B C   
5613  O  O   . MET B 366 ? 0.5085 0.3709 0.4330 0.0438  0.0200  0.0053  366  MET B O   
5614  C  CB  . MET B 366 ? 0.4952 0.3786 0.4065 0.0524  0.0236  0.0209  366  MET B CB  
5615  C  CG  . MET B 366 ? 0.5626 0.4570 0.4682 0.0546  0.0236  0.0272  366  MET B CG  
5616  S  SD  . MET B 366 ? 0.6341 0.5274 0.5449 0.0529  0.0269  0.0391  366  MET B SD  
5617  C  CE  . MET B 366 ? 0.5835 0.4809 0.5002 0.0487  0.0225  0.0401  366  MET B CE  
5618  N  N   . ARG B 367 ? 0.5105 0.3650 0.4391 0.0436  0.0262  0.0201  367  ARG B N   
5619  C  CA  . ARG B 367 ? 0.4976 0.3372 0.4288 0.0424  0.0275  0.0165  367  ARG B CA  
5620  C  C   . ARG B 367 ? 0.5378 0.3742 0.4631 0.0488  0.0298  0.0164  367  ARG B C   
5621  O  O   . ARG B 367 ? 0.7438 0.5831 0.6680 0.0518  0.0323  0.0234  367  ARG B O   
5622  C  CB  . ARG B 367 ? 0.6050 0.4354 0.5426 0.0383  0.0300  0.0229  367  ARG B CB  
5623  C  CG  . ARG B 367 ? 0.8052 0.6183 0.7457 0.0354  0.0314  0.0194  367  ARG B CG  
5624  C  CD  . ARG B 367 ? 0.9951 0.7962 0.9322 0.0399  0.0346  0.0239  367  ARG B CD  
5625  N  NE  . ARG B 367 ? 1.1240 0.9281 1.0621 0.0407  0.0366  0.0333  367  ARG B NE  
5626  C  CZ  . ARG B 367 ? 1.1987 0.9926 1.1387 0.0391  0.0390  0.0390  367  ARG B CZ  
5627  N  NH1 . ARG B 367 ? 1.3072 1.1065 1.2476 0.0406  0.0401  0.0466  367  ARG B NH1 
5628  N  NH2 . ARG B 367 ? 1.1565 0.9346 1.0975 0.0362  0.0407  0.0372  367  ARG B NH2 
5629  N  N   . THR B 368 ? 0.4405 0.2717 0.3627 0.0511  0.0288  0.0081  368  THR B N   
5630  C  CA  . THR B 368 ? 0.4217 0.2521 0.3385 0.0579  0.0308  0.0069  368  THR B CA  
5631  C  C   . THR B 368 ? 0.4634 0.2822 0.3825 0.0595  0.0335  0.0119  368  THR B C   
5632  O  O   . THR B 368 ? 0.3201 0.1282 0.2436 0.0554  0.0339  0.0146  368  THR B O   
5633  C  CB  . THR B 368 ? 0.3861 0.2121 0.2990 0.0606  0.0290  -0.0038 368  THR B CB  
5634  O  OG1 . THR B 368 ? 0.4111 0.2201 0.3276 0.0578  0.0286  -0.0075 368  THR B OG1 
5635  C  CG2 . THR B 368 ? 0.3782 0.2154 0.2879 0.0595  0.0255  -0.0100 368  THR B CG2 
5636  N  N   . SER B 369 ? 0.3739 0.1958 0.2901 0.0658  0.0355  0.0131  369  SER B N   
5637  C  CA  . SER B 369 ? 0.4217 0.2346 0.3394 0.0691  0.0375  0.0171  369  SER B CA  
5638  C  C   . SER B 369 ? 0.5494 0.3469 0.4650 0.0720  0.0369  0.0105  369  SER B C   
5639  O  O   . SER B 369 ? 0.6585 0.4532 0.5721 0.0711  0.0351  0.0026  369  SER B O   
5640  C  CB  . SER B 369 ? 0.4431 0.2674 0.3600 0.0745  0.0397  0.0202  369  SER B CB  
5641  O  OG  . SER B 369 ? 0.3618 0.1922 0.2745 0.0793  0.0401  0.0134  369  SER B OG  
5642  N  N   . LYS B 370 ? 0.5716 0.3589 0.4872 0.0760  0.0381  0.0134  370  LYS B N   
5643  C  CA  . LYS B 370 ? 0.6141 0.3847 0.5267 0.0800  0.0375  0.0079  370  LYS B CA  
5644  C  C   . LYS B 370 ? 0.5798 0.3556 0.4888 0.0856  0.0368  -0.0009 370  LYS B C   
5645  O  O   . LYS B 370 ? 0.6922 0.4554 0.5984 0.0877  0.0356  -0.0080 370  LYS B O   
5646  C  CB  . LYS B 370 ? 0.3348 0.0958 0.2469 0.0852  0.0386  0.0131  370  LYS B CB  
5647  C  CG  . LYS B 370 ? 0.3539 0.1052 0.2677 0.0801  0.0395  0.0208  370  LYS B CG  
5648  C  CD  . LYS B 370 ? 0.4748 0.2248 0.3877 0.0852  0.0402  0.0271  370  LYS B CD  
5649  C  CE  . LYS B 370 ? 0.5660 0.3152 0.4791 0.0781  0.0418  0.0338  370  LYS B CE  
5650  N  NZ  . LYS B 370 ? 0.7045 0.4548 0.6144 0.0818  0.0423  0.0378  370  LYS B NZ  
5651  N  N   . ARG B 371 ? 0.4481 0.2422 0.3568 0.0880  0.0378  -0.0006 371  ARG B N   
5652  C  CA  . ARG B 371 ? 0.5725 0.3744 0.4774 0.0933  0.0378  -0.0086 371  ARG B CA  
5653  C  C   . ARG B 371 ? 0.5119 0.3227 0.4141 0.0891  0.0364  -0.0129 371  ARG B C   
5654  O  O   . ARG B 371 ? 0.5757 0.3969 0.4737 0.0929  0.0369  -0.0181 371  ARG B O   
5655  C  CB  . ARG B 371 ? 0.4918 0.3085 0.3977 0.0988  0.0406  -0.0060 371  ARG B CB  
5656  C  CG  . ARG B 371 ? 0.3558 0.1670 0.2653 0.1032  0.0414  -0.0017 371  ARG B CG  
5657  C  CD  . ARG B 371 ? 0.5558 0.3801 0.4666 0.1103  0.0436  -0.0041 371  ARG B CD  
5658  N  NE  . ARG B 371 ? 0.8510 0.6797 0.7674 0.1121  0.0447  0.0023  371  ARG B NE  
5659  C  CZ  . ARG B 371 ? 1.0088 0.8538 0.9297 0.1108  0.0474  0.0068  371  ARG B CZ  
5660  N  NH1 . ARG B 371 ? 0.8462 0.7051 0.7657 0.1080  0.0500  0.0066  371  ARG B NH1 
5661  N  NH2 . ARG B 371 ? 1.0605 0.9071 0.9871 0.1126  0.0475  0.0115  371  ARG B NH2 
5662  N  N   . GLY B 372 ? 0.5276 0.3347 0.4322 0.0817  0.0346  -0.0110 372  GLY B N   
5663  C  CA  . GLY B 372 ? 0.6089 0.4243 0.5115 0.0780  0.0323  -0.0154 372  GLY B CA  
5664  C  C   . GLY B 372 ? 0.5740 0.4083 0.4734 0.0791  0.0336  -0.0119 372  GLY B C   
5665  O  O   . GLY B 372 ? 0.5315 0.3743 0.4260 0.0795  0.0320  -0.0171 372  GLY B O   
5666  N  N   . GLU B 373 ? 0.4420 0.2826 0.3438 0.0797  0.0366  -0.0031 373  GLU B N   
5667  C  CA  . GLU B 373 ? 0.5494 0.4063 0.4483 0.0802  0.0385  0.0013  373  GLU B CA  
5668  C  C   . GLU B 373 ? 0.5157 0.3765 0.4167 0.0743  0.0371  0.0076  373  GLU B C   
5669  O  O   . GLU B 373 ? 0.5602 0.4133 0.4670 0.0702  0.0363  0.0119  373  GLU B O   
5670  C  CB  . GLU B 373 ? 0.4940 0.3575 0.3947 0.0841  0.0429  0.0065  373  GLU B CB  
5671  C  CG  . GLU B 373 ? 0.6041 0.4584 0.5081 0.0886  0.0436  0.0043  373  GLU B CG  
5672  C  CD  . GLU B 373 ? 0.5759 0.4360 0.4849 0.0904  0.0467  0.0111  373  GLU B CD  
5673  O  OE1 . GLU B 373 ? 0.4976 0.3711 0.4058 0.0923  0.0501  0.0123  373  GLU B OE1 
5674  O  OE2 . GLU B 373 ? 0.5229 0.3743 0.4366 0.0896  0.0459  0.0152  373  GLU B OE2 
5675  N  N   . TYR B 374 ? 0.5035 0.3763 0.3991 0.0744  0.0370  0.0084  374  TYR B N   
5676  C  CA  . TYR B 374 ? 0.5947 0.4727 0.4915 0.0701  0.0357  0.0146  374  TYR B CA  
5677  C  C   . TYR B 374 ? 0.5290 0.4197 0.4197 0.0724  0.0386  0.0198  374  TYR B C   
5678  O  O   . TYR B 374 ? 0.5456 0.4423 0.4294 0.0768  0.0408  0.0165  374  TYR B O   
5679  C  CB  . TYR B 374 ? 0.5149 0.3922 0.4108 0.0669  0.0306  0.0085  374  TYR B CB  
5680  C  CG  . TYR B 374 ? 0.5425 0.4291 0.4288 0.0704  0.0290  0.0025  374  TYR B CG  
5681  C  CD1 . TYR B 374 ? 0.4968 0.3807 0.3790 0.0738  0.0279  -0.0074 374  TYR B CD1 
5682  C  CD2 . TYR B 374 ? 0.5970 0.4946 0.4773 0.0711  0.0285  0.0068  374  TYR B CD2 
5683  C  CE1 . TYR B 374 ? 0.5281 0.4208 0.4002 0.0778  0.0263  -0.0132 374  TYR B CE1 
5684  C  CE2 . TYR B 374 ? 0.5563 0.4620 0.4257 0.0752  0.0271  0.0016  374  TYR B CE2 
5685  C  CZ  . TYR B 374 ? 0.5050 0.4086 0.3704 0.0785  0.0259  -0.0085 374  TYR B CZ  
5686  O  OH  . TYR B 374 ? 0.5786 0.4905 0.4324 0.0831  0.0244  -0.0138 374  TYR B OH  
5687  N  N   . TRP B 375 ? 0.5809 0.4749 0.4738 0.0696  0.0391  0.0281  375  TRP B N   
5688  C  CA  . TRP B 375 ? 0.4798 0.3840 0.3662 0.0710  0.0416  0.0336  375  TRP B CA  
5689  C  C   . TRP B 375 ? 0.5184 0.4248 0.4038 0.0681  0.0376  0.0364  375  TRP B C   
5690  O  O   . TRP B 375 ? 0.6107 0.5127 0.5037 0.0643  0.0360  0.0400  375  TRP B O   
5691  C  CB  . TRP B 375 ? 0.3379 0.2437 0.2290 0.0708  0.0465  0.0418  375  TRP B CB  
5692  C  CG  . TRP B 375 ? 0.4486 0.3525 0.3433 0.0736  0.0498  0.0392  375  TRP B CG  
5693  C  CD1 . TRP B 375 ? 0.4908 0.4020 0.3828 0.0771  0.0548  0.0390  375  TRP B CD1 
5694  C  CD2 . TRP B 375 ? 0.4136 0.3080 0.3155 0.0737  0.0485  0.0363  375  TRP B CD2 
5695  N  NE1 . TRP B 375 ? 0.5592 0.4671 0.4572 0.0796  0.0562  0.0356  375  TRP B NE1 
5696  C  CE2 . TRP B 375 ? 0.5064 0.4033 0.4097 0.0779  0.0521  0.0341  375  TRP B CE2 
5697  C  CE3 . TRP B 375 ? 0.4253 0.3092 0.3321 0.0708  0.0449  0.0355  375  TRP B CE3 
5698  C  CZ2 . TRP B 375 ? 0.3268 0.2156 0.2356 0.0801  0.0515  0.0310  375  TRP B CZ2 
5699  C  CZ3 . TRP B 375 ? 0.5201 0.3947 0.4315 0.0725  0.0450  0.0332  375  TRP B CZ3 
5700  C  CH2 . TRP B 375 ? 0.3710 0.2480 0.2830 0.0775  0.0479  0.0310  375  TRP B CH2 
5701  N  N   . ARG B 376 ? 0.5104 0.4239 0.3861 0.0704  0.0359  0.0343  376  ARG B N   
5702  C  CA  . ARG B 376 ? 0.4855 0.4025 0.3595 0.0689  0.0317  0.0367  376  ARG B CA  
5703  C  C   . ARG B 376 ? 0.5460 0.4695 0.4109 0.0714  0.0346  0.0445  376  ARG B C   
5704  O  O   . ARG B 376 ? 0.4672 0.3960 0.3205 0.0756  0.0359  0.0429  376  ARG B O   
5705  C  CB  . ARG B 376 ? 0.2892 0.2081 0.1600 0.0694  0.0256  0.0271  376  ARG B CB  
5706  C  CG  . ARG B 376 ? 0.4633 0.3873 0.3332 0.0684  0.0205  0.0283  376  ARG B CG  
5707  C  CD  . ARG B 376 ? 0.5310 0.4510 0.4133 0.0631  0.0192  0.0322  376  ARG B CD  
5708  N  NE  . ARG B 376 ? 0.6619 0.5883 0.5437 0.0628  0.0142  0.0329  376  ARG B NE  
5709  C  CZ  . ARG B 376 ? 0.5706 0.4963 0.4613 0.0592  0.0128  0.0370  376  ARG B CZ  
5710  N  NH1 . ARG B 376 ? 0.8759 0.7943 0.7760 0.0554  0.0163  0.0410  376  ARG B NH1 
5711  N  NH2 . ARG B 376 ? 0.6298 0.5626 0.5199 0.0599  0.0080  0.0368  376  ARG B NH2 
5712  N  N   . LEU B 377 ? 0.5797 0.5020 0.4495 0.0690  0.0360  0.0532  377  LEU B N   
5713  C  CA  . LEU B 377 ? 0.4815 0.4076 0.3437 0.0707  0.0391  0.0616  377  LEU B CA  
5714  C  C   . LEU B 377 ? 0.4791 0.4098 0.3316 0.0733  0.0341  0.0603  377  LEU B C   
5715  O  O   . LEU B 377 ? 0.5341 0.4648 0.3917 0.0716  0.0282  0.0573  377  LEU B O   
5716  C  CB  . LEU B 377 ? 0.3316 0.2542 0.2023 0.0673  0.0406  0.0699  377  LEU B CB  
5717  C  CG  . LEU B 377 ? 0.3825 0.3004 0.2640 0.0648  0.0442  0.0711  377  LEU B CG  
5718  C  CD1 . LEU B 377 ? 0.2493 0.1647 0.1372 0.0622  0.0454  0.0793  377  LEU B CD1 
5719  C  CD2 . LEU B 377 ? 0.3431 0.2637 0.2216 0.0671  0.0501  0.0702  377  LEU B CD2 
5720  N  N   . LEU B 378 ? 0.5055 0.4406 0.3442 0.0777  0.0365  0.0623  378  LEU B N   
5721  C  CA  . LEU B 378 ? 0.5143 0.4539 0.3416 0.0816  0.0313  0.0611  378  LEU B CA  
5722  C  C   . LEU B 378 ? 0.5046 0.4454 0.3181 0.0853  0.0352  0.0702  378  LEU B C   
5723  O  O   . LEU B 378 ? 0.6294 0.5698 0.4378 0.0860  0.0427  0.0745  378  LEU B O   
5724  C  CB  . LEU B 378 ? 0.4772 0.4208 0.2978 0.0850  0.0274  0.0502  378  LEU B CB  
5725  C  CG  . LEU B 378 ? 0.3802 0.3222 0.2123 0.0818  0.0218  0.0398  378  LEU B CG  
5726  C  CD1 . LEU B 378 ? 0.4457 0.3899 0.2714 0.0850  0.0206  0.0296  378  LEU B CD1 
5727  C  CD2 . LEU B 378 ? 0.2635 0.2082 0.1005 0.0804  0.0140  0.0373  378  LEU B CD2 
5728  N  N   . THR B 379 ? 0.6571 0.5992 0.4650 0.0876  0.0302  0.0732  379  THR B N   
5729  C  CA  . THR B 379 ? 0.6202 0.5626 0.4118 0.0925  0.0324  0.0809  379  THR B CA  
5730  C  C   . THR B 379 ? 0.6865 0.6334 0.4618 0.0983  0.0327  0.0758  379  THR B C   
5731  O  O   . THR B 379 ? 0.6271 0.5781 0.4041 0.0993  0.0277  0.0652  379  THR B O   
5732  C  CB  . THR B 379 ? 0.6495 0.5930 0.4391 0.0947  0.0249  0.0826  379  THR B CB  
5733  O  OG1 . THR B 379 ? 0.6130 0.5521 0.4157 0.0900  0.0255  0.0884  379  THR B OG1 
5734  C  CG2 . THR B 379 ? 0.8982 0.8416 0.6678 0.1015  0.0255  0.0891  379  THR B CG2 
5735  N  N   . PRO B 380 ? 0.6367 0.5827 0.3961 0.1021  0.0389  0.0831  380  PRO B N   
5736  C  CA  . PRO B 380 ? 0.6432 0.5937 0.3847 0.1087  0.0391  0.0786  380  PRO B CA  
5737  C  C   . PRO B 380 ? 0.6421 0.5977 0.3774 0.1137  0.0282  0.0703  380  PRO B C   
5738  O  O   . PRO B 380 ? 0.4744 0.4299 0.2125 0.1141  0.0218  0.0721  380  PRO B O   
5739  C  CB  . PRO B 380 ? 0.3494 0.2964 0.0743 0.1121  0.0463  0.0903  380  PRO B CB  
5740  C  CG  . PRO B 380 ? 0.5670 0.5084 0.3050 0.1052  0.0535  0.0988  380  PRO B CG  
5741  C  CD  . PRO B 380 ? 0.5540 0.4943 0.3116 0.1002  0.0470  0.0954  380  PRO B CD  
5742  N  N   . GLY B 381 ? 0.6478 0.6087 0.3758 0.1176  0.0257  0.0604  381  GLY B N   
5743  C  CA  . GLY B 381 ? 0.5358 0.5026 0.2586 0.1223  0.0150  0.0507  381  GLY B CA  
5744  C  C   . GLY B 381 ? 0.5936 0.5645 0.3197 0.1224  0.0122  0.0372  381  GLY B C   
5745  O  O   . GLY B 381 ? 0.6707 0.6396 0.3999 0.1202  0.0190  0.0360  381  GLY B O   
5746  N  N   . LEU B 382 ? 0.5616 0.5382 0.2875 0.1252  0.0020  0.0264  382  LEU B N   
5747  C  CA  . LEU B 382 ? 0.6661 0.6453 0.3974 0.1244  -0.0013 0.0126  382  LEU B CA  
5748  C  C   . LEU B 382 ? 0.7143 0.6942 0.4658 0.1183  -0.0091 0.0041  382  LEU B C   
5749  O  O   . LEU B 382 ? 0.5739 0.5575 0.3291 0.1184  -0.0161 0.0038  382  LEU B O   
5750  C  CB  . LEU B 382 ? 0.7677 0.7533 0.4793 0.1333  -0.0054 0.0046  382  LEU B CB  
5751  C  CG  . LEU B 382 ? 0.9391 0.9319 0.6438 0.1389  -0.0169 -0.0019 382  LEU B CG  
5752  C  CD1 . LEU B 382 ? 1.0099 1.0062 0.7328 0.1342  -0.0259 -0.0159 382  LEU B CD1 
5753  C  CD2 . LEU B 382 ? 1.1051 1.1026 0.7846 0.1493  -0.0179 -0.0052 382  LEU B CD2 
5754  N  N   . TYR B 383 ? 0.7130 0.6892 0.4774 0.1131  -0.0074 -0.0029 383  TYR B N   
5755  C  CA  . TYR B 383 ? 0.6086 0.5827 0.3935 0.1057  -0.0122 -0.0094 383  TYR B CA  
5756  C  C   . TYR B 383 ? 0.6876 0.6612 0.4776 0.1045  -0.0157 -0.0238 383  TYR B C   
5757  O  O   . TYR B 383 ? 0.7790 0.7508 0.5609 0.1076  -0.0118 -0.0272 383  TYR B O   
5758  C  CB  . TYR B 383 ? 0.5910 0.5570 0.3904 0.0985  -0.0054 -0.0006 383  TYR B CB  
5759  C  CG  . TYR B 383 ? 0.6618 0.6266 0.4574 0.0989  -0.0007 0.0137  383  TYR B CG  
5760  C  CD1 . TYR B 383 ? 0.6569 0.6210 0.4384 0.1031  0.0066  0.0220  383  TYR B CD1 
5761  C  CD2 . TYR B 383 ? 0.6297 0.5938 0.4365 0.0949  -0.0031 0.0186  383  TYR B CD2 
5762  C  CE1 . TYR B 383 ? 0.6215 0.5831 0.4001 0.1029  0.0111  0.0348  383  TYR B CE1 
5763  C  CE2 . TYR B 383 ? 0.6279 0.5898 0.4314 0.0953  0.0010  0.0312  383  TYR B CE2 
5764  C  CZ  . TYR B 383 ? 0.6742 0.6345 0.4638 0.0992  0.0080  0.0392  383  TYR B CZ  
5765  O  OH  . TYR B 383 ? 0.6259 0.5830 0.4128 0.0991  0.0121  0.0513  383  TYR B OH  
5766  N  N   . SER B 384 ? 0.5485 0.5234 0.3524 0.0999  -0.0229 -0.0325 384  SER B N   
5767  C  CA  . SER B 384 ? 0.5760 0.5474 0.3887 0.0966  -0.0256 -0.0454 384  SER B CA  
5768  C  C   . SER B 384 ? 0.7932 0.7545 0.6245 0.0877  -0.0212 -0.0425 384  SER B C   
5769  O  O   . SER B 384 ? 0.6022 0.5633 0.4473 0.0818  -0.0237 -0.0410 384  SER B O   
5770  C  CB  . SER B 384 ? 0.5691 0.5485 0.3856 0.0969  -0.0361 -0.0583 384  SER B CB  
5771  O  OG  . SER B 384 ? 1.0106 0.9970 0.8092 0.1057  -0.0403 -0.0654 384  SER B OG  
5772  N  N   . VAL B 385 ? 0.7332 0.6863 0.5642 0.0874  -0.0148 -0.0415 385  VAL B N   
5773  C  CA  . VAL B 385 ? 0.6759 0.6183 0.5219 0.0804  -0.0103 -0.0383 385  VAL B CA  
5774  C  C   . VAL B 385 ? 0.6868 0.6218 0.5415 0.0769  -0.0130 -0.0507 385  VAL B C   
5775  O  O   . VAL B 385 ? 0.5598 0.4962 0.4066 0.0812  -0.0154 -0.0604 385  VAL B O   
5776  C  CB  . VAL B 385 ? 0.5255 0.4630 0.3672 0.0822  -0.0015 -0.0288 385  VAL B CB  
5777  C  CG1 . VAL B 385 ? 0.5459 0.4743 0.4020 0.0757  0.0024  -0.0220 385  VAL B CG1 
5778  C  CG2 . VAL B 385 ? 0.5140 0.4589 0.3424 0.0873  0.0016  -0.0188 385  VAL B CG2 
5779  N  N   . HIS B 386 ? 0.5317 0.4583 0.4022 0.0692  -0.0125 -0.0503 386  HIS B N   
5780  C  CA  . HIS B 386 ? 0.5807 0.4971 0.4601 0.0651  -0.0137 -0.0605 386  HIS B CA  
5781  C  C   . HIS B 386 ? 0.5521 0.4551 0.4434 0.0589  -0.0084 -0.0542 386  HIS B C   
5782  O  O   . HIS B 386 ? 0.4400 0.3433 0.3352 0.0566  -0.0051 -0.0433 386  HIS B O   
5783  C  CB  . HIS B 386 ? 0.8074 0.7284 0.6933 0.0619  -0.0219 -0.0734 386  HIS B CB  
5784  C  CG  . HIS B 386 ? 0.9312 0.8539 0.8320 0.0542  -0.0241 -0.0715 386  HIS B CG  
5785  N  ND1 . HIS B 386 ? 1.0392 0.9584 0.9468 0.0503  -0.0191 -0.0594 386  HIS B ND1 
5786  C  CD2 . HIS B 386 ? 0.8981 0.8266 0.8091 0.0496  -0.0306 -0.0810 386  HIS B CD2 
5787  C  CE1 . HIS B 386 ? 0.7356 0.6582 0.6561 0.0440  -0.0221 -0.0611 386  HIS B CE1 
5788  N  NE2 . HIS B 386 ? 0.5767 0.5054 0.5002 0.0432  -0.0290 -0.0741 386  HIS B NE2 
5789  N  N   . ALA B 387 ? 0.5457 0.4364 0.4415 0.0568  -0.0076 -0.0612 387  ALA B N   
5790  C  CA  . ALA B 387 ? 0.5697 0.4461 0.4750 0.0519  -0.0027 -0.0560 387  ALA B CA  
5791  C  C   . ALA B 387 ? 0.6989 0.5649 0.6155 0.0449  -0.0053 -0.0652 387  ALA B C   
5792  O  O   . ALA B 387 ? 0.8034 0.6701 0.7192 0.0452  -0.0100 -0.0775 387  ALA B O   
5793  C  CB  . ALA B 387 ? 0.6213 0.4900 0.5198 0.0572  0.0023  -0.0536 387  ALA B CB  
5794  N  N   . SER B 388 ? 0.5269 0.3825 0.4537 0.0384  -0.0019 -0.0595 388  SER B N   
5795  C  CA  . SER B 388 ? 0.6059 0.4496 0.5439 0.0309  -0.0028 -0.0669 388  SER B CA  
5796  C  C   . SER B 388 ? 0.6115 0.4378 0.5534 0.0281  0.0035  -0.0590 388  SER B C   
5797  O  O   . SER B 388 ? 0.4839 0.3106 0.4222 0.0310  0.0076  -0.0479 388  SER B O   
5798  C  CB  . SER B 388 ? 0.5507 0.4041 0.4996 0.0240  -0.0065 -0.0696 388  SER B CB  
5799  O  OG  . SER B 388 ? 0.6661 0.5253 0.6178 0.0226  -0.0038 -0.0578 388  SER B OG  
5800  N  N   . ALA B 389 ? 0.6920 0.5026 0.6409 0.0226  0.0043  -0.0648 389  ALA B N   
5801  C  CA  . ALA B 389 ? 0.6539 0.4462 0.6058 0.0199  0.0102  -0.0574 389  ALA B CA  
5802  C  C   . ALA B 389 ? 0.6737 0.4505 0.6353 0.0115  0.0107  -0.0644 389  ALA B C   
5803  O  O   . ALA B 389 ? 0.8122 0.5879 0.7757 0.0100  0.0067  -0.0766 389  ALA B O   
5804  C  CB  . ALA B 389 ? 0.4055 0.1888 0.3471 0.0282  0.0130  -0.0544 389  ALA B CB  
5805  N  N   . PHE B 390 ? 0.6882 0.4526 0.6556 0.0059  0.0159  -0.0568 390  PHE B N   
5806  C  CA  . PHE B 390 ? 0.8696 0.6178 0.8463 -0.0029 0.0178  -0.0621 390  PHE B CA  
5807  C  C   . PHE B 390 ? 0.8399 0.5699 0.8108 0.0004  0.0176  -0.0694 390  PHE B C   
5808  O  O   . PHE B 390 ? 0.8096 0.5312 0.7704 0.0083  0.0196  -0.0646 390  PHE B O   
5809  C  CB  . PHE B 390 ? 1.0495 0.7859 1.0303 -0.0079 0.0245  -0.0509 390  PHE B CB  
5810  C  CG  . PHE B 390 ? 1.3234 1.0396 1.3121 -0.0168 0.0282  -0.0546 390  PHE B CG  
5811  C  CD1 . PHE B 390 ? 1.4131 1.1046 1.3954 -0.0149 0.0330  -0.0504 390  PHE B CD1 
5812  C  CD2 . PHE B 390 ? 1.4192 1.1407 1.4218 -0.0270 0.0269  -0.0625 390  PHE B CD2 
5813  C  CE1 . PHE B 390 ? 1.4751 1.1459 1.4636 -0.0233 0.0370  -0.0531 390  PHE B CE1 
5814  C  CE2 . PHE B 390 ? 1.4794 1.1816 1.4900 -0.0361 0.0311  -0.0659 390  PHE B CE2 
5815  C  CZ  . PHE B 390 ? 1.5004 1.1763 1.5034 -0.0344 0.0364  -0.0608 390  PHE B CZ  
5816  N  N   . GLY B 391 ? 0.7601 0.4847 0.7380 -0.0054 0.0149  -0.0816 391  GLY B N   
5817  C  CA  . GLY B 391 ? 0.7637 0.4706 0.7365 -0.0023 0.0141  -0.0901 391  GLY B CA  
5818  C  C   . GLY B 391 ? 0.7791 0.4987 0.7433 0.0064  0.0081  -0.0990 391  GLY B C   
5819  O  O   . GLY B 391 ? 0.6802 0.3881 0.6392 0.0106  0.0066  -0.1072 391  GLY B O   
5820  N  N   . TYR B 392 ? 0.8676 0.6110 0.8297 0.0096  0.0048  -0.0972 392  TYR B N   
5821  C  CA  . TYR B 392 ? 0.8033 0.5606 0.7561 0.0181  -0.0003 -0.1046 392  TYR B CA  
5822  C  C   . TYR B 392 ? 0.8429 0.6211 0.8002 0.0155  -0.0066 -0.1121 392  TYR B C   
5823  O  O   . TYR B 392 ? 0.8939 0.6839 0.8579 0.0110  -0.0067 -0.1066 392  TYR B O   
5824  C  CB  . TYR B 392 ? 0.7414 0.5069 0.6826 0.0277  0.0021  -0.0943 392  TYR B CB  
5825  C  CG  . TYR B 392 ? 0.8735 0.6213 0.8083 0.0331  0.0066  -0.0898 392  TYR B CG  
5826  C  CD1 . TYR B 392 ? 0.9508 0.6955 0.8763 0.0417  0.0053  -0.0968 392  TYR B CD1 
5827  C  CD2 . TYR B 392 ? 0.7349 0.4693 0.6725 0.0304  0.0120  -0.0790 392  TYR B CD2 
5828  C  CE1 . TYR B 392 ? 0.9132 0.6425 0.8333 0.0475  0.0089  -0.0932 392  TYR B CE1 
5829  C  CE2 . TYR B 392 ? 0.7608 0.4793 0.6921 0.0364  0.0155  -0.0751 392  TYR B CE2 
5830  C  CZ  . TYR B 392 ? 0.9247 0.6409 0.8476 0.0450  0.0137  -0.0824 392  TYR B CZ  
5831  O  OH  . TYR B 392 ? 0.9328 0.6341 0.8499 0.0517  0.0167  -0.0791 392  TYR B OH  
5832  N  N   . GLN B 393 ? 0.9269 0.7096 0.8798 0.0193  -0.0122 -0.1252 393  GLN B N   
5833  C  CA  . GLN B 393 ? 0.7797 0.5833 0.7334 0.0197  -0.0192 -0.1332 393  GLN B CA  
5834  C  C   . GLN B 393 ? 0.7911 0.6131 0.7345 0.0271  -0.0190 -0.1233 393  GLN B C   
5835  O  O   . GLN B 393 ? 0.6683 0.4904 0.5992 0.0357  -0.0164 -0.1183 393  GLN B O   
5836  C  CB  . GLN B 393 ? 0.5618 0.3647 0.5105 0.0236  -0.0251 -0.1493 393  GLN B CB  
5837  C  CG  . GLN B 393 ? 0.7450 0.5266 0.7033 0.0165  -0.0247 -0.1589 393  GLN B CG  
5838  C  CD  . GLN B 393 ? 1.0031 0.7848 0.9583 0.0195  -0.0314 -0.1765 393  GLN B CD  
5839  O  OE1 . GLN B 393 ? 1.0286 0.8244 0.9717 0.0287  -0.0356 -0.1809 393  GLN B OE1 
5840  N  NE2 . GLN B 393 ? 0.9948 0.7604 0.9608 0.0118  -0.0323 -0.1868 393  GLN B NE2 
5841  N  N   . THR B 394 ? 0.8120 0.6492 0.7614 0.0236  -0.0215 -0.1204 394  THR B N   
5842  C  CA  . THR B 394 ? 0.7978 0.6515 0.7381 0.0298  -0.0214 -0.1108 394  THR B CA  
5843  C  C   . THR B 394 ? 0.7760 0.6406 0.7013 0.0396  -0.0255 -0.1169 394  THR B C   
5844  O  O   . THR B 394 ? 0.8329 0.7064 0.7580 0.0403  -0.0324 -0.1289 394  THR B O   
5845  C  CB  . THR B 394 ? 0.7562 0.6244 0.7057 0.0248  -0.0246 -0.1091 394  THR B CB  
5846  O  OG1 . THR B 394 ? 0.7443 0.6031 0.7076 0.0157  -0.0200 -0.1030 394  THR B OG1 
5847  C  CG2 . THR B 394 ? 0.8121 0.6954 0.7511 0.0317  -0.0245 -0.0988 394  THR B CG2 
5848  N  N   . SER B 395 ? 0.6664 0.5307 0.5792 0.0473  -0.0210 -0.1089 395  SER B N   
5849  C  CA  . SER B 395 ? 0.6203 0.4939 0.5175 0.0570  -0.0230 -0.1132 395  SER B CA  
5850  C  C   . SER B 395 ? 0.7327 0.6246 0.6247 0.0599  -0.0298 -0.1180 395  SER B C   
5851  O  O   . SER B 395 ? 0.9155 0.8156 0.8145 0.0556  -0.0321 -0.1145 395  SER B O   
5852  C  CB  . SER B 395 ? 0.6071 0.4824 0.4943 0.0633  -0.0163 -0.1005 395  SER B CB  
5853  O  OG  . SER B 395 ? 0.6818 0.5679 0.5687 0.0626  -0.0153 -0.0894 395  SER B OG  
5854  N  N   . ALA B 396 ? 0.6075 0.5059 0.4861 0.0678  -0.0329 -0.1261 396  ALA B N   
5855  C  CA  . ALA B 396 ? 0.5960 0.5120 0.4649 0.0731  -0.0388 -0.1289 396  ALA B CA  
5856  C  C   . ALA B 396 ? 0.7500 0.6740 0.6094 0.0775  -0.0339 -0.1135 396  ALA B C   
5857  O  O   . ALA B 396 ? 0.9437 0.8607 0.8017 0.0780  -0.0263 -0.1032 396  ALA B O   
5858  C  CB  . ALA B 396 ? 0.5309 0.4506 0.3864 0.0811  -0.0427 -0.1411 396  ALA B CB  
5859  N  N   . PRO B 397 ? 0.5950 0.5334 0.4479 0.0807  -0.0384 -0.1120 397  PRO B N   
5860  C  CA  . PRO B 397 ? 0.5827 0.5274 0.4274 0.0841  -0.0340 -0.0970 397  PRO B CA  
5861  C  C   . PRO B 397 ? 0.6334 0.5827 0.4582 0.0937  -0.0303 -0.0936 397  PRO B C   
5862  O  O   . PRO B 397 ? 0.8242 0.7786 0.6376 0.0998  -0.0344 -0.1036 397  PRO B O   
5863  C  CB  . PRO B 397 ? 0.6003 0.5577 0.4464 0.0840  -0.0414 -0.0984 397  PRO B CB  
5864  C  CG  . PRO B 397 ? 0.6817 0.6396 0.5398 0.0792  -0.0493 -0.1140 397  PRO B CG  
5865  C  CD  . PRO B 397 ? 0.7000 0.6486 0.5553 0.0806  -0.0482 -0.1238 397  PRO B CD  
5866  N  N   . GLN B 398 ? 0.8302 0.7778 0.6508 0.0949  -0.0223 -0.0799 398  GLN B N   
5867  C  CA  . GLN B 398 ? 0.7605 0.7131 0.5628 0.1032  -0.0174 -0.0752 398  GLN B CA  
5868  C  C   . GLN B 398 ? 0.6438 0.6043 0.4375 0.1057  -0.0159 -0.0630 398  GLN B C   
5869  O  O   . GLN B 398 ? 0.6826 0.6412 0.4859 0.1006  -0.0144 -0.0535 398  GLN B O   
5870  C  CB  . GLN B 398 ? 0.6906 0.6349 0.4946 0.1032  -0.0086 -0.0706 398  GLN B CB  
5871  C  CG  . GLN B 398 ? 0.6336 0.5692 0.4427 0.1027  -0.0100 -0.0830 398  GLN B CG  
5872  C  CD  . GLN B 398 ? 0.7180 0.6453 0.5306 0.1028  -0.0020 -0.0783 398  GLN B CD  
5873  O  OE1 . GLN B 398 ? 0.7636 0.6950 0.5694 0.1061  0.0049  -0.0688 398  GLN B OE1 
5874  N  NE2 . GLN B 398 ? 0.6831 0.5984 0.5064 0.0993  -0.0028 -0.0850 398  GLN B NE2 
5875  N  N   . GLN B 399 ? 0.5904 0.5591 0.3653 0.1140  -0.0164 -0.0634 399  GLN B N   
5876  C  CA  . GLN B 399 ? 0.8171 0.7920 0.5802 0.1178  -0.0149 -0.0520 399  GLN B CA  
5877  C  C   . GLN B 399 ? 0.8988 0.8717 0.6532 0.1202  -0.0040 -0.0407 399  GLN B C   
5878  O  O   . GLN B 399 ? 0.9609 0.9336 0.7077 0.1241  0.0003  -0.0448 399  GLN B O   
5879  C  CB  . GLN B 399 ? 0.9183 0.9028 0.6643 0.1260  -0.0221 -0.0591 399  GLN B CB  
5880  C  CG  . GLN B 399 ? 1.0741 1.0637 0.8007 0.1329  -0.0188 -0.0480 399  GLN B CG  
5881  C  CD  . GLN B 399 ? 1.2670 1.2645 0.9727 0.1428  -0.0241 -0.0561 399  GLN B CD  
5882  O  OE1 . GLN B 399 ? 1.3472 1.3450 1.0432 0.1473  -0.0214 -0.0624 399  GLN B OE1 
5883  N  NE2 . GLN B 399 ? 1.3294 1.3335 1.0279 0.1470  -0.0319 -0.0564 399  GLN B NE2 
5884  N  N   . VAL B 400 ? 0.8035 0.7753 0.5597 0.1178  0.0007  -0.0271 400  VAL B N   
5885  C  CA  . VAL B 400 ? 0.6772 0.6474 0.4276 0.1189  0.0114  -0.0161 400  VAL B CA  
5886  C  C   . VAL B 400 ? 0.6315 0.6043 0.3712 0.1211  0.0143  -0.0033 400  VAL B C   
5887  O  O   . VAL B 400 ? 0.5865 0.5589 0.3320 0.1184  0.0101  0.0014  400  VAL B O   
5888  C  CB  . VAL B 400 ? 0.8415 0.8040 0.6100 0.1117  0.0168  -0.0118 400  VAL B CB  
5889  C  CG1 . VAL B 400 ? 0.6511 0.6103 0.4329 0.1053  0.0146  -0.0044 400  VAL B CG1 
5890  C  CG2 . VAL B 400 ? 1.0050 0.9676 0.7684 0.1133  0.0276  -0.0035 400  VAL B CG2 
5891  N  N   . ARG B 401 ? 0.6938 0.6689 0.4176 0.1262  0.0217  0.0025  401  ARG B N   
5892  C  CA  . ARG B 401 ? 0.7904 0.7659 0.5031 0.1282  0.0257  0.0155  401  ARG B CA  
5893  C  C   . ARG B 401 ? 0.7346 0.7051 0.4579 0.1223  0.0350  0.0268  401  ARG B C   
5894  O  O   . ARG B 401 ? 0.7683 0.7391 0.4888 0.1227  0.0441  0.0297  401  ARG B O   
5895  C  CB  . ARG B 401 ? 0.8357 0.8157 0.5237 0.1369  0.0293  0.0168  401  ARG B CB  
5896  C  CG  . ARG B 401 ? 1.0013 0.9796 0.6759 0.1391  0.0349  0.0313  401  ARG B CG  
5897  C  CD  . ARG B 401 ? 1.1580 1.1402 0.8052 0.1489  0.0368  0.0319  401  ARG B CD  
5898  N  NE  . ARG B 401 ? 1.2069 1.1927 0.8480 0.1518  0.0423  0.0250  401  ARG B NE  
5899  C  CZ  . ARG B 401 ? 1.3009 1.2921 0.9282 0.1592  0.0375  0.0142  401  ARG B CZ  
5900  N  NH1 . ARG B 401 ? 1.4345 1.4287 1.0580 0.1614  0.0435  0.0084  401  ARG B NH1 
5901  N  NH2 . ARG B 401 ? 1.2999 1.2940 0.9172 0.1647  0.0268  0.0087  401  ARG B NH2 
5902  N  N   . VAL B 402 ? 0.6947 0.6613 0.4310 0.1168  0.0325  0.0325  402  VAL B N   
5903  C  CA  . VAL B 402 ? 0.6062 0.5681 0.3529 0.1113  0.0402  0.0429  402  VAL B CA  
5904  C  C   . VAL B 402 ? 0.8128 0.7740 0.5461 0.1136  0.0469  0.0554  402  VAL B C   
5905  O  O   . VAL B 402 ? 0.5318 0.4913 0.2605 0.1145  0.0434  0.0616  402  VAL B O   
5906  C  CB  . VAL B 402 ? 0.3605 0.3181 0.1254 0.1049  0.0357  0.0446  402  VAL B CB  
5907  C  CG1 . VAL B 402 ? 0.3611 0.3142 0.1349 0.1000  0.0433  0.0553  402  VAL B CG1 
5908  C  CG2 . VAL B 402 ? 0.3501 0.3063 0.1288 0.1016  0.0311  0.0337  402  VAL B CG2 
5909  N  N   . THR B 403 ? 1.0307 0.9932 0.7576 0.1147  0.0566  0.0586  403  THR B N   
5910  C  CA  . THR B 403 ? 1.0013 0.9617 0.7202 0.1145  0.0659  0.0711  403  THR B CA  
5911  C  C   . THR B 403 ? 0.9980 0.9562 0.7361 0.1072  0.0724  0.0747  403  THR B C   
5912  O  O   . THR B 403 ? 1.1169 1.0774 0.8652 0.1057  0.0738  0.0674  403  THR B O   
5913  C  CB  . THR B 403 ? 0.9992 0.9639 0.6987 0.1204  0.0734  0.0714  403  THR B CB  
5914  O  OG1 . THR B 403 ? 1.2626 1.2246 0.9566 0.1187  0.0841  0.0838  403  THR B OG1 
5915  C  CG2 . THR B 403 ? 0.8975 0.8672 0.6033 0.1205  0.0765  0.0617  403  THR B CG2 
5916  N  N   . ASN B 404 ? 0.6682 0.6216 0.4113 0.1031  0.0758  0.0852  404  ASN B N   
5917  C  CA  . ASN B 404 ? 0.7492 0.7011 0.5109 0.0965  0.0812  0.0880  404  ASN B CA  
5918  C  C   . ASN B 404 ? 0.7783 0.7320 0.5365 0.0954  0.0935  0.0947  404  ASN B C   
5919  O  O   . ASN B 404 ? 0.7107 0.6618 0.4798 0.0901  0.0986  0.1015  404  ASN B O   
5920  C  CB  . ASN B 404 ? 0.5808 0.5266 0.3550 0.0917  0.0770  0.0934  404  ASN B CB  
5921  C  CG  . ASN B 404 ? 0.7385 0.6834 0.5221 0.0910  0.0665  0.0855  404  ASN B CG  
5922  O  OD1 . ASN B 404 ? 0.7109 0.6580 0.5012 0.0909  0.0641  0.0762  404  ASN B OD1 
5923  N  ND2 . ASN B 404 ? 0.8891 0.8307 0.6734 0.0905  0.0605  0.0890  404  ASN B ND2 
5924  N  N   . ASP B 405 ? 0.8005 0.7592 0.5438 0.1003  0.0982  0.0923  405  ASP B N   
5925  C  CA  . ASP B 405 ? 0.8360 0.7974 0.5741 0.0995  0.1109  0.0987  405  ASP B CA  
5926  C  C   . ASP B 405 ? 0.7743 0.7420 0.5283 0.0965  0.1167  0.0934  405  ASP B C   
5927  O  O   . ASP B 405 ? 0.7528 0.7228 0.5119 0.0928  0.1269  0.0990  405  ASP B O   
5928  C  CB  . ASP B 405 ? 0.8796 0.8437 0.5931 0.1066  0.1142  0.0991  405  ASP B CB  
5929  C  CG  . ASP B 405 ? 0.8128 0.7704 0.5087 0.1104  0.1099  0.1063  405  ASP B CG  
5930  O  OD1 . ASP B 405 ? 0.4777 0.4285 0.1796 0.1064  0.1090  0.1144  405  ASP B OD1 
5931  O  OD2 . ASP B 405 ? 0.6218 0.5812 0.2975 0.1179  0.1070  0.1035  405  ASP B OD2 
5932  N  N   . ASN B 406 ? 0.5946 0.5649 0.3567 0.0980  0.1103  0.0824  406  ASN B N   
5933  C  CA  . ASN B 406 ? 0.7969 0.7732 0.5726 0.0968  0.1148  0.0762  406  ASN B CA  
5934  C  C   . ASN B 406 ? 0.9776 0.9510 0.7754 0.0909  0.1127  0.0767  406  ASN B C   
5935  O  O   . ASN B 406 ? 1.1061 1.0728 0.9094 0.0888  0.1046  0.0776  406  ASN B O   
5936  C  CB  . ASN B 406 ? 0.8553 0.8350 0.6272 0.1022  0.1098  0.0638  406  ASN B CB  
5937  C  CG  . ASN B 406 ? 0.8748 0.8619 0.6558 0.1030  0.1162  0.0577  406  ASN B CG  
5938  O  OD1 . ASN B 406 ? 0.8978 0.8920 0.6685 0.1068  0.1235  0.0561  406  ASN B OD1 
5939  N  ND2 . ASN B 406 ? 0.4786 0.4643 0.2787 0.1000  0.1135  0.0541  406  ASN B ND2 
5940  N  N   . GLN B 407 ? 0.9689 0.9480 0.7791 0.0887  0.1198  0.0758  407  GLN B N   
5941  C  CA  . GLN B 407 ? 1.0187 0.9959 0.8491 0.0836  0.1186  0.0768  407  GLN B CA  
5942  C  C   . GLN B 407 ? 0.8527 0.8240 0.6923 0.0838  0.1080  0.0705  407  GLN B C   
5943  O  O   . GLN B 407 ? 0.8339 0.8004 0.6856 0.0798  0.1049  0.0737  407  GLN B O   
5944  C  CB  . GLN B 407 ? 1.0744 1.0609 0.9169 0.0827  0.1270  0.0741  407  GLN B CB  
5945  C  CG  . GLN B 407 ? 1.0096 0.9996 0.8552 0.0779  0.1372  0.0830  407  GLN B CG  
5946  C  CD  . GLN B 407 ? 1.1270 1.1282 0.9858 0.0770  0.1454  0.0791  407  GLN B CD  
5947  O  OE1 . GLN B 407 ? 1.1537 1.1613 1.0135 0.0817  0.1453  0.0702  407  GLN B OE1 
5948  N  NE2 . GLN B 407 ? 1.2245 1.2285 1.0941 0.0711  0.1525  0.0853  407  GLN B NE2 
5949  N  N   . GLU B 408 ? 0.6948 0.6658 0.5285 0.0884  0.1028  0.0615  408  GLU B N   
5950  C  CA  . GLU B 408 ? 0.6920 0.6566 0.5344 0.0883  0.0938  0.0552  408  GLU B CA  
5951  C  C   . GLU B 408 ? 0.6877 0.6481 0.5194 0.0909  0.0859  0.0503  408  GLU B C   
5952  O  O   . GLU B 408 ? 0.8079 0.7720 0.6250 0.0949  0.0869  0.0481  408  GLU B O   
5953  C  CB  . GLU B 408 ? 0.7508 0.7182 0.6034 0.0906  0.0949  0.0470  408  GLU B CB  
5954  C  CG  . GLU B 408 ? 0.8430 0.8144 0.7103 0.0876  0.1004  0.0507  408  GLU B CG  
5955  C  CD  . GLU B 408 ? 0.8562 0.8300 0.7339 0.0908  0.1003  0.0424  408  GLU B CD  
5956  O  OE1 . GLU B 408 ? 0.6335 0.6159 0.5193 0.0908  0.1070  0.0425  408  GLU B OE1 
5957  O  OE2 . GLU B 408 ? 1.0457 1.0127 0.9237 0.0933  0.0935  0.0356  408  GLU B OE2 
5958  N  N   . ALA B 409 ? 0.7157 0.6687 0.5548 0.0887  0.0781  0.0483  409  ALA B N   
5959  C  CA  . ALA B 409 ? 0.6304 0.5797 0.4622 0.0899  0.0701  0.0439  409  ALA B CA  
5960  C  C   . ALA B 409 ? 0.6364 0.5883 0.4596 0.0950  0.0685  0.0335  409  ALA B C   
5961  O  O   . ALA B 409 ? 0.5636 0.5161 0.3918 0.0970  0.0705  0.0273  409  ALA B O   
5962  C  CB  . ALA B 409 ? 0.4816 0.4228 0.3254 0.0860  0.0633  0.0427  409  ALA B CB  
5963  N  N   . LEU B 410 ? 0.6286 0.5821 0.4388 0.0977  0.0645  0.0312  410  LEU B N   
5964  C  CA  . LEU B 410 ? 0.4675 0.4233 0.2686 0.1028  0.0618  0.0206  410  LEU B CA  
5965  C  C   . LEU B 410 ? 0.4387 0.3878 0.2508 0.1016  0.0563  0.0113  410  LEU B C   
5966  O  O   . LEU B 410 ? 0.4278 0.3705 0.2482 0.0976  0.0503  0.0109  410  LEU B O   
5967  C  CB  . LEU B 410 ? 0.6106 0.5686 0.3974 0.1056  0.0564  0.0193  410  LEU B CB  
5968  C  CG  . LEU B 410 ? 0.8863 0.8504 0.6572 0.1090  0.0626  0.0270  410  LEU B CG  
5969  C  CD1 . LEU B 410 ? 1.0271 0.9915 0.7864 0.1107  0.0569  0.0301  410  LEU B CD1 
5970  C  CD2 . LEU B 410 ? 0.9583 0.9285 0.7173 0.1151  0.0676  0.0212  410  LEU B CD2 
5971  N  N   . ARG B 411 ? 0.4754 0.4255 0.2875 0.1053  0.0588  0.0039  411  ARG B N   
5972  C  CA  . ARG B 411 ? 0.5638 0.5061 0.3844 0.1051  0.0540  -0.0054 411  ARG B CA  
5973  C  C   . ARG B 411 ? 0.5689 0.5090 0.3830 0.1063  0.0461  -0.0147 411  ARG B C   
5974  O  O   . ARG B 411 ? 0.5298 0.4765 0.3302 0.1108  0.0455  -0.0182 411  ARG B O   
5975  C  CB  . ARG B 411 ? 0.5830 0.5274 0.4045 0.1097  0.0587  -0.0112 411  ARG B CB  
5976  C  CG  . ARG B 411 ? 0.5515 0.4871 0.3775 0.1112  0.0535  -0.0223 411  ARG B CG  
5977  C  CD  . ARG B 411 ? 0.4940 0.4194 0.3345 0.1069  0.0517  -0.0197 411  ARG B CD  
5978  N  NE  . ARG B 411 ? 0.6904 0.6169 0.5373 0.1098  0.0569  -0.0194 411  ARG B NE  
5979  C  CZ  . ARG B 411 ? 0.6960 0.6158 0.5465 0.1134  0.0556  -0.0276 411  ARG B CZ  
5980  N  NH1 . ARG B 411 ? 0.6259 0.5364 0.4743 0.1137  0.0496  -0.0363 411  ARG B NH1 
5981  N  NH2 . ARG B 411 ? 0.6453 0.5676 0.5019 0.1167  0.0601  -0.0273 411  ARG B NH2 
5982  N  N   . LEU B 412 ? 0.5844 0.5152 0.4085 0.1024  0.0401  -0.0189 412  LEU B N   
5983  C  CA  . LEU B 412 ? 0.6274 0.5556 0.4487 0.1023  0.0323  -0.0286 412  LEU B CA  
5984  C  C   . LEU B 412 ? 0.5511 0.4668 0.3850 0.0984  0.0286  -0.0344 412  LEU B C   
5985  O  O   . LEU B 412 ? 0.5624 0.4721 0.4068 0.0929  0.0280  -0.0286 412  LEU B O   
5986  C  CB  . LEU B 412 ? 0.6588 0.5910 0.4772 0.0996  0.0279  -0.0243 412  LEU B CB  
5987  C  CG  . LEU B 412 ? 0.6277 0.5605 0.4432 0.0996  0.0193  -0.0343 412  LEU B CG  
5988  C  CD1 . LEU B 412 ? 0.8109 0.7516 0.6101 0.1070  0.0185  -0.0411 412  LEU B CD1 
5989  C  CD2 . LEU B 412 ? 0.3630 0.2986 0.1813 0.0958  0.0150  -0.0290 412  LEU B CD2 
5990  N  N   . ASP B 413 ? 0.4817 0.3927 0.3139 0.1016  0.0266  -0.0456 413  ASP B N   
5991  C  CA  . ASP B 413 ? 0.4721 0.3693 0.3151 0.0986  0.0242  -0.0509 413  ASP B CA  
5992  C  C   . ASP B 413 ? 0.7299 0.6212 0.5748 0.0956  0.0167  -0.0615 413  ASP B C   
5993  O  O   . ASP B 413 ? 0.6773 0.5762 0.5140 0.0978  0.0126  -0.0678 413  ASP B O   
5994  C  CB  . ASP B 413 ? 0.5224 0.4154 0.3644 0.1041  0.0277  -0.0560 413  ASP B CB  
5995  C  CG  . ASP B 413 ? 0.6242 0.5212 0.4690 0.1060  0.0348  -0.0467 413  ASP B CG  
5996  O  OD1 . ASP B 413 ? 0.7064 0.6086 0.5535 0.1027  0.0373  -0.0362 413  ASP B OD1 
5997  O  OD2 . ASP B 413 ? 0.7242 0.6193 0.5694 0.1110  0.0378  -0.0507 413  ASP B OD2 
5998  N  N   . PHE B 414 ? 0.7385 0.6159 0.5943 0.0908  0.0150  -0.0636 414  PHE B N   
5999  C  CA  . PHE B 414 ? 0.6224 0.4926 0.4829 0.0866  0.0087  -0.0736 414  PHE B CA  
6000  C  C   . PHE B 414 ? 0.7463 0.5997 0.6121 0.0863  0.0086  -0.0808 414  PHE B C   
6001  O  O   . PHE B 414 ? 0.6845 0.5277 0.5561 0.0853  0.0123  -0.0747 414  PHE B O   
6002  C  CB  . PHE B 414 ? 0.6312 0.5008 0.5012 0.0785  0.0064  -0.0681 414  PHE B CB  
6003  C  CG  . PHE B 414 ? 0.6668 0.5512 0.5317 0.0789  0.0057  -0.0615 414  PHE B CG  
6004  C  CD1 . PHE B 414 ? 0.5989 0.4880 0.4629 0.0795  0.0108  -0.0487 414  PHE B CD1 
6005  C  CD2 . PHE B 414 ? 0.8467 0.7400 0.7077 0.0790  -0.0004 -0.0682 414  PHE B CD2 
6006  C  CE1 . PHE B 414 ? 0.6112 0.5123 0.4699 0.0801  0.0103  -0.0424 414  PHE B CE1 
6007  C  CE2 . PHE B 414 ? 0.7759 0.6820 0.6312 0.0803  -0.0013 -0.0619 414  PHE B CE2 
6008  C  CZ  . PHE B 414 ? 0.7356 0.6448 0.5893 0.0808  0.0042  -0.0486 414  PHE B CZ  
6009  N  N   . LYS B 415 ? 0.7664 0.6162 0.6296 0.0877  0.0041  -0.0939 415  LYS B N   
6010  C  CA  . LYS B 415 ? 0.7843 0.6159 0.6534 0.0860  0.0029  -0.1016 415  LYS B CA  
6011  C  C   . LYS B 415 ? 0.8349 0.6606 0.7128 0.0776  -0.0024 -0.1080 415  LYS B C   
6012  O  O   . LYS B 415 ? 0.7328 0.5681 0.6081 0.0772  -0.0077 -0.1159 415  LYS B O   
6013  C  CB  . LYS B 415 ? 0.8271 0.6568 0.6876 0.0940  0.0020  -0.1131 415  LYS B CB  
6014  C  CG  . LYS B 415 ? 1.0223 0.8556 0.8764 0.1022  0.0079  -0.1085 415  LYS B CG  
6015  C  CD  . LYS B 415 ? 1.0804 0.9057 0.9298 0.1093  0.0073  -0.1200 415  LYS B CD  
6016  C  CE  . LYS B 415 ? 1.1387 0.9649 0.9858 0.1165  0.0133  -0.1149 415  LYS B CE  
6017  N  NZ  . LYS B 415 ? 1.1505 0.9658 0.9949 0.1232  0.0127  -0.1257 415  LYS B NZ  
6018  N  N   . LEU B 416 ? 0.7562 0.5663 0.6444 0.0710  -0.0009 -0.1046 416  LEU B N   
6019  C  CA  . LEU B 416 ? 0.7340 0.5382 0.6328 0.0618  -0.0046 -0.1096 416  LEU B CA  
6020  C  C   . LEU B 416 ? 0.7496 0.5337 0.6520 0.0601  -0.0055 -0.1193 416  LEU B C   
6021  O  O   . LEU B 416 ? 0.8750 0.6444 0.7764 0.0628  -0.0015 -0.1157 416  LEU B O   
6022  C  CB  . LEU B 416 ? 0.8041 0.6054 0.7122 0.0545  -0.0014 -0.0977 416  LEU B CB  
6023  C  CG  . LEU B 416 ? 0.5961 0.4142 0.5015 0.0559  0.0003  -0.0863 416  LEU B CG  
6024  C  CD1 . LEU B 416 ? 0.4933 0.3073 0.4092 0.0479  0.0026  -0.0766 416  LEU B CD1 
6025  C  CD2 . LEU B 416 ? 0.4690 0.3053 0.3694 0.0577  -0.0050 -0.0921 416  LEU B CD2 
6026  N  N   . ALA B 417 ? 0.7074 0.4904 0.6141 0.0559  -0.0109 -0.1319 417  ALA B N   
6027  C  CA  . ALA B 417 ? 0.5292 0.2912 0.4405 0.0530  -0.0117 -0.1413 417  ALA B CA  
6028  C  C   . ALA B 417 ? 0.6361 0.3844 0.5604 0.0421  -0.0091 -0.1361 417  ALA B C   
6029  O  O   . ALA B 417 ? 0.7792 0.5375 0.7102 0.0363  -0.0085 -0.1288 417  ALA B O   
6030  C  CB  . ALA B 417 ? 0.5130 0.2790 0.4241 0.0528  -0.0186 -0.1578 417  ALA B CB  
6031  N  N   . PRO B 418 ? 0.5845 0.3093 0.5121 0.0397  -0.0072 -0.1395 418  PRO B N   
6032  C  CA  . PRO B 418 ? 0.7207 0.4308 0.6600 0.0290  -0.0038 -0.1345 418  PRO B CA  
6033  C  C   . PRO B 418 ? 0.7300 0.4423 0.6808 0.0194  -0.0084 -0.1465 418  PRO B C   
6034  O  O   . PRO B 418 ? 0.8063 0.5229 0.7551 0.0218  -0.0141 -0.1602 418  PRO B O   
6035  C  CB  . PRO B 418 ? 0.5299 0.2128 0.4660 0.0313  0.0000  -0.1341 418  PRO B CB  
6036  C  CG  . PRO B 418 ? 0.6954 0.3803 0.6193 0.0434  -0.0023 -0.1407 418  PRO B CG  
6037  C  CD  . PRO B 418 ? 0.5350 0.2448 0.4556 0.0464  -0.0077 -0.1480 418  PRO B CD  
6038  N  N   . VAL B 419 ? 0.5679 0.2788 0.5311 0.0088  -0.0061 -0.1417 419  VAL B N   
6039  C  CA  . VAL B 419 ? 0.5849 0.2994 0.5616 -0.0012 -0.0101 -0.1529 419  VAL B CA  
6040  C  C   . VAL B 419 ? 0.7365 0.4264 0.7174 -0.0056 -0.0100 -0.1638 419  VAL B C   
6041  O  O   . VAL B 419 ? 0.6357 0.3280 0.6235 -0.0098 -0.0155 -0.1787 419  VAL B O   
6042  C  CB  . VAL B 419 ? 0.6930 0.4126 0.6824 -0.0114 -0.0066 -0.1443 419  VAL B CB  
6043  C  CG1 . VAL B 419 ? 0.7951 0.5385 0.7800 -0.0065 -0.0075 -0.1347 419  VAL B CG1 
6044  C  CG2 . VAL B 419 ? 0.6998 0.3959 0.6906 -0.0154 0.0018  -0.1331 419  VAL B CG2 
6045  N  N   . GLU B 420 ? 0.7386 0.4044 0.7147 -0.0040 -0.0039 -0.1566 420  GLU B N   
6046  C  CA  . GLU B 420 ? 0.9675 0.6065 0.9464 -0.0078 -0.0029 -0.1652 420  GLU B CA  
6047  C  C   . GLU B 420 ? 0.9868 0.6293 0.9642 -0.0046 -0.0105 -0.1834 420  GLU B C   
6048  O  O   . GLU B 420 ? 0.7802 0.4257 0.7696 -0.0133 -0.0145 -0.1956 420  GLU B O   
6049  C  CB  . GLU B 420 ? 0.9392 0.5549 0.9070 -0.0007 0.0027  -0.1560 420  GLU B CB  
6050  C  CG  . GLU B 420 ? 1.0102 0.5944 0.9803 -0.0050 0.0048  -0.1626 420  GLU B CG  
6051  C  CD  . GLU B 420 ? 1.1196 0.6863 1.0753 0.0072  0.0056  -0.1621 420  GLU B CD  
6052  O  OE1 . GLU B 420 ? 1.1530 0.7316 1.0981 0.0179  0.0058  -0.1544 420  GLU B OE1 
6053  O  OE2 . GLU B 420 ? 1.0499 0.5911 1.0053 0.0060  0.0060  -0.1695 420  GLU B OE2 
6054  N  N   . GLU C 30  ? 0.2731 0.8436 0.3734 0.0308  0.0919  0.0136  30   GLU C N   
6055  C  CA  . GLU C 30  ? 0.3351 0.8587 0.4254 0.0207  0.0794  0.0191  30   GLU C CA  
6056  C  C   . GLU C 30  ? 0.3006 0.8269 0.4013 0.0014  0.0728  0.0379  30   GLU C C   
6057  O  O   . GLU C 30  ? 0.3324 0.8865 0.4341 -0.0127 0.0774  0.0508  30   GLU C O   
6058  C  CB  . GLU C 30  ? 0.2035 0.7070 0.2675 0.0154  0.0792  0.0182  30   GLU C CB  
6059  C  CG  . GLU C 30  ? 0.1250 0.5806 0.1779 0.0096  0.0675  0.0204  30   GLU C CG  
6060  C  CD  . GLU C 30  ? 0.5474 0.9857 0.5772 0.0118  0.0675  0.0130  30   GLU C CD  
6061  O  OE1 . GLU C 30  ? 0.3922 0.8547 0.4110 0.0136  0.0759  0.0096  30   GLU C OE1 
6062  O  OE2 . GLU C 30  ? 0.6685 1.0707 0.6908 0.0116  0.0591  0.0106  30   GLU C OE2 
6063  N  N   . ASP C 31  ? 0.3820 0.8784 0.4891 0.0002  0.0620  0.0394  31   ASP C N   
6064  C  CA  . ASP C 31  ? 0.2823 0.7755 0.3970 -0.0181 0.0543  0.0553  31   ASP C CA  
6065  C  C   . ASP C 31  ? 0.4952 0.9448 0.5908 -0.0300 0.0458  0.0625  31   ASP C C   
6066  O  O   . ASP C 31  ? 0.2214 0.6339 0.3094 -0.0227 0.0395  0.0550  31   ASP C O   
6067  C  CB  . ASP C 31  ? 0.3667 0.8584 0.5009 -0.0123 0.0474  0.0533  31   ASP C CB  
6068  C  CG  . ASP C 31  ? 0.6317 1.1141 0.7707 -0.0316 0.0377  0.0678  31   ASP C CG  
6069  O  OD1 . ASP C 31  ? 0.7157 1.1878 0.8656 -0.0288 0.0295  0.0668  31   ASP C OD1 
6070  O  OD2 . ASP C 31  ? 0.5789 1.0625 0.7092 -0.0499 0.0380  0.0804  31   ASP C OD2 
6071  N  N   . GLU C 32  ? 0.6056 1.0601 0.6933 -0.0481 0.0461  0.0773  32   GLU C N   
6072  C  CA  . GLU C 32  ? 0.6195 1.0340 0.6890 -0.0592 0.0384  0.0859  32   GLU C CA  
6073  C  C   . GLU C 32  ? 0.4829 0.8970 0.5539 -0.0810 0.0338  0.1037  32   GLU C C   
6074  O  O   . GLU C 32  ? 0.2940 0.6914 0.3485 -0.0930 0.0321  0.1149  32   GLU C O   
6075  C  CB  . GLU C 32  ? 0.8190 1.2286 0.8677 -0.0572 0.0430  0.0852  32   GLU C CB  
6076  C  CG  . GLU C 32  ? 0.7462 1.1485 0.7889 -0.0386 0.0456  0.0676  32   GLU C CG  
6077  C  CD  . GLU C 32  ? 0.6065 1.0036 0.6277 -0.0388 0.0479  0.0680  32   GLU C CD  
6078  O  OE1 . GLU C 32  ? 0.4950 0.8609 0.5035 -0.0437 0.0408  0.0740  32   GLU C OE1 
6079  O  OE2 . GLU C 32  ? 0.5533 0.9782 0.5698 -0.0333 0.0568  0.0621  32   GLU C OE2 
6080  N  N   . SER C 33  ? 0.4779 0.9092 0.5683 -0.0861 0.0309  0.1063  33   SER C N   
6081  C  CA  . SER C 33  ? 0.4848 0.9193 0.5787 -0.1086 0.0262  0.1221  33   SER C CA  
6082  C  C   . SER C 33  ? 0.4106 0.7936 0.4894 -0.1185 0.0145  0.1279  33   SER C C   
6083  O  O   . SER C 33  ? 0.2996 0.6746 0.3741 -0.1385 0.0101  0.1414  33   SER C O   
6084  C  CB  . SER C 33  ? 0.5674 1.0382 0.6879 -0.1106 0.0255  0.1220  33   SER C CB  
6085  O  OG  . SER C 33  ? 0.6594 1.1124 0.7872 -0.0964 0.0187  0.1107  33   SER C OG  
6086  N  N   . PHE C 34  ? 0.3002 0.6477 0.3706 -0.1049 0.0097  0.1177  34   PHE C N   
6087  C  CA  . PHE C 34  ? 0.4395 0.7388 0.4935 -0.1119 0.0003  0.1224  34   PHE C CA  
6088  C  C   . PHE C 34  ? 0.4230 0.7073 0.4577 -0.1237 0.0014  0.1351  34   PHE C C   
6089  O  O   . PHE C 34  ? 0.4561 0.7036 0.4771 -0.1334 -0.0060 0.1425  34   PHE C O   
6090  C  CB  . PHE C 34  ? 0.5331 0.7998 0.5803 -0.0948 -0.0033 0.1098  34   PHE C CB  
6091  C  CG  . PHE C 34  ? 0.5365 0.8092 0.5786 -0.0790 0.0037  0.1003  34   PHE C CG  
6092  C  CD1 . PHE C 34  ? 0.5239 0.7858 0.5488 -0.0802 0.0060  0.1050  34   PHE C CD1 
6093  C  CD2 . PHE C 34  ? 0.4708 0.7576 0.5241 -0.0631 0.0071  0.0866  34   PHE C CD2 
6094  C  CE1 . PHE C 34  ? 0.3800 0.6485 0.3996 -0.0671 0.0113  0.0957  34   PHE C CE1 
6095  C  CE2 . PHE C 34  ? 0.5265 0.8162 0.5735 -0.0502 0.0128  0.0768  34   PHE C CE2 
6096  C  CZ  . PHE C 34  ? 0.2450 0.5270 0.2754 -0.0529 0.0147  0.0811  34   PHE C CZ  
6097  N  N   . LEU C 35  ? 0.2647 0.5769 0.2969 -0.1223 0.0105  0.1375  35   LEU C N   
6098  C  CA  . LEU C 35  ? 0.2406 0.5410 0.2529 -0.1315 0.0120  0.1501  35   LEU C CA  
6099  C  C   . LEU C 35  ? 0.4258 0.7404 0.4402 -0.1545 0.0123  0.1666  35   LEU C C   
6100  O  O   . LEU C 35  ? 0.4667 0.7666 0.4640 -0.1662 0.0119  0.1804  35   LEU C O   
6101  C  CB  . LEU C 35  ? 0.1787 0.5032 0.1849 -0.1206 0.0213  0.1458  35   LEU C CB  
6102  C  CG  . LEU C 35  ? 0.3977 0.7127 0.4005 -0.0997 0.0220  0.1296  35   LEU C CG  
6103  C  CD1 . LEU C 35  ? 0.3427 0.6843 0.3373 -0.0933 0.0308  0.1268  35   LEU C CD1 
6104  C  CD2 . LEU C 35  ? 0.3968 0.6645 0.3851 -0.0953 0.0135  0.1293  35   LEU C CD2 
6105  N  N   . GLN C 36  ? 0.5648 0.9097 0.6006 -0.1609 0.0128  0.1656  36   GLN C N   
6106  C  CA  . GLN C 36  ? 0.7432 1.1019 0.7849 -0.1852 0.0112  0.1804  36   GLN C CA  
6107  C  C   . GLN C 36  ? 0.8612 1.1668 0.8836 -0.1990 0.0006  0.1899  36   GLN C C   
6108  O  O   . GLN C 36  ? 1.0257 1.2968 1.0453 -0.1935 -0.0082 0.1826  36   GLN C O   
6109  C  CB  . GLN C 36  ? 0.9081 1.2972 0.9764 -0.1871 0.0090  0.1752  36   GLN C CB  
6110  C  CG  . GLN C 36  ? 0.7733 1.1953 0.8546 -0.2115 0.0097  0.1892  36   GLN C CG  
6111  C  CD  . GLN C 36  ? 0.6958 1.1662 0.7823 -0.2136 0.0232  0.1952  36   GLN C CD  
6112  O  OE1 . GLN C 36  ? 0.6091 1.1132 0.7060 -0.2338 0.0266  0.2080  36   GLN C OE1 
6113  N  NE2 . GLN C 36  ? 0.5793 1.0548 0.6580 -0.1934 0.0313  0.1860  36   GLN C NE2 
6114  N  N   . GLN C 37  ? 0.8226 1.1199 0.8302 -0.2162 0.0016  0.2063  37   GLN C N   
6115  C  CA  . GLN C 37  ? 0.9389 1.1857 0.9280 -0.2319 -0.0083 0.2167  37   GLN C CA  
6116  C  C   . GLN C 37  ? 0.9016 1.0959 0.8739 -0.2152 -0.0153 0.2078  37   GLN C C   
6117  O  O   . GLN C 37  ? 0.5291 0.6983 0.5032 -0.2147 -0.0236 0.2009  37   GLN C O   
6118  C  CB  . GLN C 37  ? 1.0300 1.2823 1.0336 -0.2506 -0.0156 0.2189  37   GLN C CB  
6119  C  CG  . GLN C 37  ? 1.1138 1.4276 1.1410 -0.2651 -0.0086 0.2255  37   GLN C CG  
6120  C  CD  . GLN C 37  ? 1.0523 1.3804 1.0993 -0.2787 -0.0164 0.2241  37   GLN C CD  
6121  O  OE1 . GLN C 37  ? 1.1562 1.4436 1.1926 -0.2923 -0.0279 0.2270  37   GLN C OE1 
6122  N  NE2 . GLN C 37  ? 0.8181 1.2045 0.8935 -0.2745 -0.0106 0.2192  37   GLN C NE2 
6123  N  N   . PRO C 38  ? 1.1013 1.2809 1.0571 -0.2018 -0.0120 0.2084  38   PRO C N   
6124  C  CA  . PRO C 38  ? 1.0455 1.1843 0.9878 -0.1831 -0.0167 0.1996  38   PRO C CA  
6125  C  C   . PRO C 38  ? 1.1015 1.1844 1.0273 -0.1899 -0.0270 0.2037  38   PRO C C   
6126  O  O   . PRO C 38  ? 1.4640 1.5278 1.3781 -0.2091 -0.0305 0.2178  38   PRO C O   
6127  C  CB  . PRO C 38  ? 0.8515 0.9920 0.7787 -0.1747 -0.0115 0.2055  38   PRO C CB  
6128  C  CG  . PRO C 38  ? 0.7306 0.9215 0.6672 -0.1825 -0.0021 0.2109  38   PRO C CG  
6129  C  CD  . PRO C 38  ? 0.9996 1.2046 0.9483 -0.2048 -0.0034 0.2187  38   PRO C CD  
6130  N  N   . HIS C 39  ? 0.7234 0.7795 0.6471 -0.1744 -0.0315 0.1913  39   HIS C N   
6131  C  CA  . HIS C 39  ? 0.6807 0.6853 0.5891 -0.1784 -0.0406 0.1919  39   HIS C CA  
6132  C  C   . HIS C 39  ? 0.7237 0.7102 0.6322 -0.1572 -0.0425 0.1767  39   HIS C C   
6133  O  O   . HIS C 39  ? 0.6017 0.6177 0.5264 -0.1447 -0.0383 0.1653  39   HIS C O   
6134  C  CB  . HIS C 39  ? 0.6316 0.6375 0.5474 -0.1995 -0.0464 0.1944  39   HIS C CB  
6135  C  CG  . HIS C 39  ? 0.5907 0.6194 0.5267 -0.1933 -0.0476 0.1805  39   HIS C CG  
6136  N  ND1 . HIS C 39  ? 0.7059 0.7830 0.6636 -0.1834 -0.0405 0.1732  39   HIS C ND1 
6137  C  CD2 . HIS C 39  ? 0.6668 0.6746 0.6026 -0.1947 -0.0554 0.1727  39   HIS C CD2 
6138  C  CE1 . HIS C 39  ? 0.6462 0.7308 0.6171 -0.1786 -0.0440 0.1624  39   HIS C CE1 
6139  N  NE2 . HIS C 39  ? 0.5921 0.6363 0.5500 -0.1856 -0.0532 0.1621  39   HIS C NE2 
6140  N  N   . TYR C 40  ? 0.9235 0.8611 0.8133 -0.1533 -0.0485 0.1765  40   TYR C N   
6141  C  CA  . TYR C 40  ? 0.7961 0.7153 0.6846 -0.1346 -0.0500 0.1631  40   TYR C CA  
6142  C  C   . TYR C 40  ? 0.6882 0.6006 0.5827 -0.1398 -0.0553 0.1543  40   TYR C C   
6143  O  O   . TYR C 40  ? 0.8358 0.7217 0.7199 -0.1547 -0.0621 0.1584  40   TYR C O   
6144  C  CB  . TYR C 40  ? 0.8284 0.7005 0.6939 -0.1250 -0.0529 0.1663  40   TYR C CB  
6145  C  CG  . TYR C 40  ? 0.7923 0.6741 0.6543 -0.1118 -0.0480 0.1709  40   TYR C CG  
6146  C  CD1 . TYR C 40  ? 0.8779 0.7484 0.7256 -0.1186 -0.0484 0.1861  40   TYR C CD1 
6147  C  CD2 . TYR C 40  ? 0.6165 0.5192 0.4889 -0.0935 -0.0437 0.1606  40   TYR C CD2 
6148  C  CE1 . TYR C 40  ? 0.8775 0.7587 0.7213 -0.1062 -0.0450 0.1906  40   TYR C CE1 
6149  C  CE2 . TYR C 40  ? 0.6726 0.5865 0.5420 -0.0823 -0.0404 0.1642  40   TYR C CE2 
6150  C  CZ  . TYR C 40  ? 0.7739 0.6780 0.6291 -0.0881 -0.0413 0.1791  40   TYR C CZ  
6151  O  OH  . TYR C 40  ? 0.8042 0.7214 0.6557 -0.0764 -0.0389 0.1830  40   TYR C OH  
6152  N  N   . ALA C 41  ? 0.5713 0.5065 0.4812 -0.1277 -0.0527 0.1422  41   ALA C N   
6153  C  CA  . ALA C 41  ? 0.5749 0.5086 0.4915 -0.1309 -0.0578 0.1341  41   ALA C CA  
6154  C  C   . ALA C 41  ? 0.5729 0.4582 0.4695 -0.1261 -0.0634 0.1294  41   ALA C C   
6155  O  O   . ALA C 41  ? 0.5766 0.4446 0.4649 -0.1095 -0.0606 0.1249  41   ALA C O   
6156  C  CB  . ALA C 41  ? 0.3387 0.3067 0.2752 -0.1177 -0.0533 0.1233  41   ALA C CB  
6157  N  N   . SER C 42  ? 0.6323 0.4971 0.5210 -0.1407 -0.0714 0.1301  42   SER C N   
6158  C  CA  . SER C 42  ? 0.6804 0.4984 0.5479 -0.1365 -0.0767 0.1244  42   SER C CA  
6159  C  C   . SER C 42  ? 0.7182 0.5434 0.5924 -0.1244 -0.0768 0.1120  42   SER C C   
6160  O  O   . SER C 42  ? 0.6030 0.4666 0.4983 -0.1225 -0.0747 0.1087  42   SER C O   
6161  C  CB  . SER C 42  ? 0.7035 0.4961 0.5581 -0.1583 -0.0861 0.1286  42   SER C CB  
6162  O  OG  . SER C 42  ? 0.6572 0.4750 0.5264 -0.1680 -0.0910 0.1243  42   SER C OG  
6163  N  N   . GLN C 43  ? 0.7056 0.4927 0.5608 -0.1160 -0.0791 0.1055  43   GLN C N   
6164  C  CA  . GLN C 43  ? 0.6334 0.4231 0.4912 -0.1063 -0.0797 0.0947  43   GLN C CA  
6165  C  C   . GLN C 43  ? 0.6247 0.4404 0.4966 -0.1197 -0.0858 0.0940  43   GLN C C   
6166  O  O   . GLN C 43  ? 0.4944 0.3407 0.3840 -0.1124 -0.0835 0.0895  43   GLN C O   
6167  C  CB  . GLN C 43  ? 0.7117 0.4542 0.5431 -0.1006 -0.0827 0.0887  43   GLN C CB  
6168  C  CG  . GLN C 43  ? 0.8339 0.5774 0.6649 -0.0889 -0.0818 0.0783  43   GLN C CG  
6169  C  CD  . GLN C 43  ? 0.8078 0.5752 0.6533 -0.0710 -0.0725 0.0753  43   GLN C CD  
6170  O  OE1 . GLN C 43  ? 0.8939 0.6658 0.7427 -0.0633 -0.0667 0.0791  43   GLN C OE1 
6171  N  NE2 . GLN C 43  ? 0.8391 0.6213 0.6925 -0.0648 -0.0717 0.0688  43   GLN C NE2 
6172  N  N   . GLU C 44  ? 0.5891 0.3933 0.4538 -0.1394 -0.0939 0.0987  44   GLU C N   
6173  C  CA  . GLU C 44  ? 0.7282 0.5607 0.6079 -0.1523 -0.1006 0.0986  44   GLU C CA  
6174  C  C   . GLU C 44  ? 0.6252 0.5108 0.5344 -0.1508 -0.0948 0.1025  44   GLU C C   
6175  O  O   . GLU C 44  ? 0.7429 0.6580 0.6691 -0.1452 -0.0952 0.0982  44   GLU C O   
6176  C  CB  . GLU C 44  ? 0.8333 0.6487 0.7023 -0.1768 -0.1107 0.1040  44   GLU C CB  
6177  C  CG  . GLU C 44  ? 1.0865 0.9286 0.9688 -0.1890 -0.1196 0.1023  44   GLU C CG  
6178  C  CD  . GLU C 44  ? 1.3070 1.1566 1.1924 -0.2165 -0.1276 0.1109  44   GLU C CD  
6179  O  OE1 . GLU C 44  ? 1.4327 1.2537 1.3027 -0.2275 -0.1277 0.1174  44   GLU C OE1 
6180  O  OE2 . GLU C 44  ? 1.2826 1.1672 1.1861 -0.2272 -0.1340 0.1119  44   GLU C OE2 
6181  N  N   . GLN C 45  ? 0.5814 0.4782 0.4953 -0.1548 -0.0893 0.1107  45   GLN C N   
6182  C  CA  . GLN C 45  ? 0.5997 0.5469 0.5394 -0.1545 -0.0833 0.1142  45   GLN C CA  
6183  C  C   . GLN C 45  ? 0.6089 0.5760 0.5609 -0.1328 -0.0762 0.1058  45   GLN C C   
6184  O  O   . GLN C 45  ? 0.5872 0.5942 0.5608 -0.1294 -0.0733 0.1044  45   GLN C O   
6185  C  CB  . GLN C 45  ? 0.4965 0.4488 0.4346 -0.1616 -0.0780 0.1245  45   GLN C CB  
6186  C  CG  . GLN C 45  ? 0.5745 0.5084 0.5013 -0.1850 -0.0846 0.1343  45   GLN C CG  
6187  C  CD  . GLN C 45  ? 0.6669 0.6227 0.5997 -0.1951 -0.0790 0.1463  45   GLN C CD  
6188  O  OE1 . GLN C 45  ? 0.5867 0.5331 0.5110 -0.1858 -0.0727 0.1497  45   GLN C OE1 
6189  N  NE2 . GLN C 45  ? 0.8562 0.8439 0.8039 -0.2145 -0.0812 0.1534  45   GLN C NE2 
6190  N  N   . LEU C 46  ? 0.5059 0.4445 0.4439 -0.1181 -0.0732 0.1003  46   LEU C N   
6191  C  CA  . LEU C 46  ? 0.5118 0.4645 0.4590 -0.0993 -0.0665 0.0928  46   LEU C CA  
6192  C  C   . LEU C 46  ? 0.5920 0.5498 0.5453 -0.0940 -0.0704 0.0854  46   LEU C C   
6193  O  O   . LEU C 46  ? 0.5171 0.5024 0.4871 -0.0849 -0.0669 0.0814  46   LEU C O   
6194  C  CB  . LEU C 46  ? 0.4809 0.4042 0.4121 -0.0868 -0.0623 0.0903  46   LEU C CB  
6195  C  CG  . LEU C 46  ? 0.5795 0.5076 0.5156 -0.0691 -0.0568 0.0817  46   LEU C CG  
6196  C  CD1 . LEU C 46  ? 0.6764 0.6431 0.6329 -0.0640 -0.0511 0.0800  46   LEU C CD1 
6197  C  CD2 . LEU C 46  ? 0.4466 0.3499 0.3685 -0.0586 -0.0529 0.0810  46   LEU C CD2 
6198  N  N   . GLU C 47  ? 0.5535 0.4831 0.4916 -0.0994 -0.0779 0.0836  47   GLU C N   
6199  C  CA  . GLU C 47  ? 0.6077 0.5404 0.5486 -0.0952 -0.0827 0.0779  47   GLU C CA  
6200  C  C   . GLU C 47  ? 0.6249 0.5967 0.5877 -0.1028 -0.0866 0.0808  47   GLU C C   
6201  O  O   . GLU C 47  ? 0.5895 0.5828 0.5662 -0.0931 -0.0860 0.0772  47   GLU C O   
6202  C  CB  . GLU C 47  ? 0.6576 0.5530 0.5754 -0.1016 -0.0907 0.0756  47   GLU C CB  
6203  C  CG  . GLU C 47  ? 0.7030 0.5613 0.5995 -0.0908 -0.0862 0.0715  47   GLU C CG  
6204  C  CD  . GLU C 47  ? 0.7851 0.6051 0.6562 -0.0969 -0.0937 0.0683  47   GLU C CD  
6205  O  OE1 . GLU C 47  ? 0.6050 0.4230 0.4730 -0.1135 -0.1029 0.0709  47   GLU C OE1 
6206  O  OE2 . GLU C 47  ? 0.9179 0.7111 0.7721 -0.0854 -0.0902 0.0629  47   GLU C OE2 
6207  N  N   . ASP C 48  ? 0.6540 0.6352 0.6201 -0.1201 -0.0904 0.0881  48   ASP C N   
6208  C  CA  . ASP C 48  ? 0.6865 0.7095 0.6751 -0.1290 -0.0937 0.0922  48   ASP C CA  
6209  C  C   . ASP C 48  ? 0.6245 0.6864 0.6354 -0.1165 -0.0843 0.0913  48   ASP C C   
6210  O  O   . ASP C 48  ? 0.6270 0.7206 0.6568 -0.1112 -0.0856 0.0896  48   ASP C O   
6211  C  CB  . ASP C 48  ? 0.7733 0.7984 0.7602 -0.1516 -0.0980 0.1012  48   ASP C CB  
6212  C  CG  . ASP C 48  ? 0.8461 0.8347 0.8118 -0.1660 -0.1091 0.1011  48   ASP C CG  
6213  O  OD1 . ASP C 48  ? 0.8789 0.8527 0.8363 -0.1599 -0.1149 0.0944  48   ASP C OD1 
6214  O  OD2 . ASP C 48  ? 0.9683 0.9414 0.9239 -0.1839 -0.1123 0.1076  48   ASP C OD2 
6215  N  N   . LEU C 49  ? 0.5195 0.5786 0.5274 -0.1107 -0.0752 0.0920  49   LEU C N   
6216  C  CA  . LEU C 49  ? 0.4431 0.5375 0.4693 -0.0999 -0.0662 0.0902  49   LEU C CA  
6217  C  C   . LEU C 49  ? 0.4095 0.5044 0.4404 -0.0805 -0.0633 0.0809  49   LEU C C   
6218  O  O   . LEU C 49  ? 0.3787 0.5050 0.4274 -0.0717 -0.0592 0.0781  49   LEU C O   
6219  C  CB  . LEU C 49  ? 0.6055 0.6979 0.6255 -0.1000 -0.0581 0.0937  49   LEU C CB  
6220  C  CG  . LEU C 49  ? 0.5568 0.6900 0.5947 -0.0928 -0.0492 0.0926  49   LEU C CG  
6221  C  CD1 . LEU C 49  ? 0.8154 0.9584 0.8499 -0.1030 -0.0441 0.1012  49   LEU C CD1 
6222  C  CD2 . LEU C 49  ? 0.5056 0.6353 0.5436 -0.0735 -0.0432 0.0829  49   LEU C CD2 
6223  N  N   . PHE C 50  ? 0.5024 0.5619 0.5167 -0.0739 -0.0650 0.0763  50   PHE C N   
6224  C  CA  . PHE C 50  ? 0.4505 0.5056 0.4667 -0.0576 -0.0627 0.0685  50   PHE C CA  
6225  C  C   . PHE C 50  ? 0.5126 0.5794 0.5382 -0.0549 -0.0695 0.0671  50   PHE C C   
6226  O  O   . PHE C 50  ? 0.6197 0.6985 0.6555 -0.0419 -0.0669 0.0625  50   PHE C O   
6227  C  CB  . PHE C 50  ? 0.3879 0.4047 0.3839 -0.0525 -0.0621 0.0651  50   PHE C CB  
6228  C  CG  . PHE C 50  ? 0.4284 0.4402 0.4206 -0.0459 -0.0538 0.0634  50   PHE C CG  
6229  C  CD1 . PHE C 50  ? 0.4511 0.4865 0.4526 -0.0479 -0.0486 0.0660  50   PHE C CD1 
6230  C  CD2 . PHE C 50  ? 0.3560 0.3425 0.3355 -0.0380 -0.0512 0.0594  50   PHE C CD2 
6231  C  CE1 . PHE C 50  ? 0.4198 0.4521 0.4170 -0.0422 -0.0421 0.0647  50   PHE C CE1 
6232  C  CE2 . PHE C 50  ? 0.4131 0.3985 0.3906 -0.0322 -0.0445 0.0582  50   PHE C CE2 
6233  C  CZ  . PHE C 50  ? 0.4930 0.5009 0.4789 -0.0344 -0.0405 0.0608  50   PHE C CZ  
6234  N  N   . ALA C 51  ? 0.3457 0.4078 0.3669 -0.0673 -0.0789 0.0712  51   ALA C N   
6235  C  CA  . ALA C 51  ? 0.4904 0.5668 0.5207 -0.0658 -0.0869 0.0711  51   ALA C CA  
6236  C  C   . ALA C 51  ? 0.7019 0.8251 0.7588 -0.0645 -0.0853 0.0737  51   ALA C C   
6237  O  O   . ALA C 51  ? 0.8601 1.0016 0.9301 -0.0532 -0.0871 0.0716  51   ALA C O   
6238  C  CB  . ALA C 51  ? 0.3484 0.4089 0.3661 -0.0811 -0.0983 0.0744  51   ALA C CB  
6239  N  N   . GLY C 52  ? 0.6241 0.7665 0.6883 -0.0752 -0.0815 0.0785  52   GLY C N   
6240  C  CA  . GLY C 52  ? 0.4098 0.5997 0.4990 -0.0746 -0.0783 0.0812  52   GLY C CA  
6241  C  C   . GLY C 52  ? 0.4249 0.6283 0.5244 -0.0539 -0.0693 0.0743  52   GLY C C   
6242  O  O   . GLY C 52  ? 0.4347 0.6685 0.5529 -0.0444 -0.0697 0.0731  52   GLY C O   
6243  N  N   . LEU C 53  ? 0.4130 0.5931 0.4997 -0.0468 -0.0617 0.0696  53   LEU C N   
6244  C  CA  . LEU C 53  ? 0.5426 0.7299 0.6353 -0.0289 -0.0532 0.0618  53   LEU C CA  
6245  C  C   . LEU C 53  ? 0.5129 0.6889 0.6066 -0.0149 -0.0573 0.0569  53   LEU C C   
6246  O  O   . LEU C 53  ? 0.4563 0.6493 0.5624 -0.0004 -0.0536 0.0521  53   LEU C O   
6247  C  CB  . LEU C 53  ? 0.4898 0.6526 0.5671 -0.0265 -0.0462 0.0581  53   LEU C CB  
6248  C  CG  . LEU C 53  ? 0.5013 0.6720 0.5748 -0.0378 -0.0414 0.0633  53   LEU C CG  
6249  C  CD1 . LEU C 53  ? 0.5900 0.7438 0.6517 -0.0315 -0.0346 0.0587  53   LEU C CD1 
6250  C  CD2 . LEU C 53  ? 0.4399 0.6546 0.5318 -0.0399 -0.0370 0.0661  53   LEU C CD2 
6251  N  N   . GLU C 54  ? 0.5405 0.6861 0.6194 -0.0190 -0.0646 0.0581  54   GLU C N   
6252  C  CA  . GLU C 54  ? 0.6412 0.7724 0.7174 -0.0077 -0.0692 0.0552  54   GLU C CA  
6253  C  C   . GLU C 54  ? 0.6959 0.8584 0.7912 -0.0021 -0.0751 0.0576  54   GLU C C   
6254  O  O   . GLU C 54  ? 0.6786 0.8419 0.7795 0.0136  -0.0749 0.0542  54   GLU C O   
6255  C  CB  . GLU C 54  ? 0.7085 0.8047 0.7638 -0.0149 -0.0760 0.0569  54   GLU C CB  
6256  C  CG  . GLU C 54  ? 0.9298 1.0029 0.9763 -0.0028 -0.0774 0.0535  54   GLU C CG  
6257  C  CD  . GLU C 54  ? 0.9115 0.9494 0.9348 -0.0088 -0.0814 0.0542  54   GLU C CD  
6258  O  OE1 . GLU C 54  ? 0.9041 0.9210 0.9174 -0.0005 -0.0809 0.0521  54   GLU C OE1 
6259  O  OE2 . GLU C 54  ? 0.8706 0.9010 0.8847 -0.0220 -0.0847 0.0569  54   GLU C OE2 
6260  N  N   . LYS C 55  ? 0.7174 0.9055 0.8228 -0.0150 -0.0808 0.0640  55   LYS C N   
6261  C  CA  . LYS C 55  ? 0.6515 0.8767 0.7785 -0.0102 -0.0866 0.0671  55   LYS C CA  
6262  C  C   . LYS C 55  ? 0.4088 0.6745 0.5580 -0.0014 -0.0774 0.0654  55   LYS C C   
6263  O  O   . LYS C 55  ? 0.4034 0.6925 0.5690 0.0140  -0.0777 0.0638  55   LYS C O   
6264  C  CB  . LYS C 55  ? 0.5886 0.8260 0.7177 -0.0286 -0.0982 0.0746  55   LYS C CB  
6265  C  CG  . LYS C 55  ? 0.6195 0.8579 0.7439 -0.0495 -0.0965 0.0788  55   LYS C CG  
6266  C  CD  . LYS C 55  ? 0.6633 0.9127 0.7897 -0.0689 -0.1092 0.0857  55   LYS C CD  
6267  C  CE  . LYS C 55  ? 0.6033 0.9072 0.7595 -0.0677 -0.1131 0.0902  55   LYS C CE  
6268  N  NZ  . LYS C 55  ? 0.6477 0.9665 0.8075 -0.0906 -0.1255 0.0974  55   LYS C NZ  
6269  N  N   . ALA C 56  ? 0.3214 0.5944 0.4698 -0.0099 -0.0690 0.0656  56   ALA C N   
6270  C  CA  . ALA C 56  ? 0.3575 0.6685 0.5239 -0.0020 -0.0591 0.0634  56   ALA C CA  
6271  C  C   . ALA C 56  ? 0.4217 0.7220 0.5868 0.0204  -0.0517 0.0535  56   ALA C C   
6272  O  O   . ALA C 56  ? 0.4937 0.8248 0.6754 0.0342  -0.0459 0.0498  56   ALA C O   
6273  C  CB  . ALA C 56  ? 0.3626 0.6793 0.5240 -0.0163 -0.0518 0.0663  56   ALA C CB  
6274  N  N   . TYR C 57  ? 0.4236 0.6801 0.5685 0.0236  -0.0516 0.0489  57   TYR C N   
6275  C  CA  . TYR C 57  ? 0.4038 0.6437 0.5442 0.0417  -0.0452 0.0393  57   TYR C CA  
6276  C  C   . TYR C 57  ? 0.4003 0.6028 0.5279 0.0482  -0.0517 0.0380  57   TYR C C   
6277  O  O   . TYR C 57  ? 0.4077 0.5762 0.5182 0.0472  -0.0492 0.0344  57   TYR C O   
6278  C  CB  . TYR C 57  ? 0.3725 0.5996 0.5008 0.0380  -0.0361 0.0345  57   TYR C CB  
6279  C  CG  . TYR C 57  ? 0.5092 0.7716 0.6470 0.0307  -0.0293 0.0368  57   TYR C CG  
6280  C  CD1 . TYR C 57  ? 0.5208 0.7877 0.6549 0.0115  -0.0314 0.0454  57   TYR C CD1 
6281  C  CD2 . TYR C 57  ? 0.4559 0.7461 0.6049 0.0432  -0.0205 0.0304  57   TYR C CD2 
6282  C  CE1 . TYR C 57  ? 0.4634 0.7620 0.6049 0.0037  -0.0251 0.0491  57   TYR C CE1 
6283  C  CE2 . TYR C 57  ? 0.2930 0.6176 0.4495 0.0363  -0.0134 0.0332  57   TYR C CE2 
6284  C  CZ  . TYR C 57  ? 0.4200 0.7490 0.5730 0.0159  -0.0158 0.0432  57   TYR C CZ  
6285  O  OH  . TYR C 57  ? 0.3566 0.7186 0.5156 0.0075  -0.0087 0.0476  57   TYR C OH  
6286  N  N   . PRO C 58  ? 0.2990 0.5100 0.4354 0.0548  -0.0600 0.0417  58   PRO C N   
6287  C  CA  . PRO C 58  ? 0.3876 0.5676 0.5117 0.0584  -0.0682 0.0436  58   PRO C CA  
6288  C  C   . PRO C 58  ? 0.5984 0.7410 0.7075 0.0684  -0.0635 0.0370  58   PRO C C   
6289  O  O   . PRO C 58  ? 0.7897 0.9002 0.8817 0.0636  -0.0674 0.0389  58   PRO C O   
6290  C  CB  . PRO C 58  ? 0.4965 0.7029 0.6384 0.0711  -0.0748 0.0468  58   PRO C CB  
6291  C  CG  . PRO C 58  ? 0.4061 0.6599 0.5689 0.0645  -0.0736 0.0501  58   PRO C CG  
6292  C  CD  . PRO C 58  ? 0.2360 0.4930 0.3965 0.0597  -0.0618 0.0450  58   PRO C CD  
6293  N  N   . ASN C 59  ? 0.6971 0.8433 0.8116 0.0814  -0.0553 0.0292  59   ASN C N   
6294  C  CA  . ASN C 59  ? 0.6978 0.8081 0.7990 0.0907  -0.0521 0.0230  59   ASN C CA  
6295  C  C   . ASN C 59  ? 0.6107 0.7035 0.6995 0.0828  -0.0441 0.0171  59   ASN C C   
6296  O  O   . ASN C 59  ? 0.5192 0.5819 0.5962 0.0865  -0.0417 0.0124  59   ASN C O   
6297  C  CB  . ASN C 59  ? 0.8290 0.9459 0.9403 0.1114  -0.0492 0.0169  59   ASN C CB  
6298  C  CG  . ASN C 59  ? 0.8464 0.9853 0.9726 0.1223  -0.0573 0.0231  59   ASN C CG  
6299  O  OD1 . ASN C 59  ? 0.7671 0.9305 0.9021 0.1132  -0.0637 0.0308  59   ASN C OD1 
6300  N  ND2 . ASN C 59  ? 0.8792 1.0092 1.0084 0.1421  -0.0573 0.0196  59   ASN C ND2 
6301  N  N   . GLN C 60  ? 0.5360 0.6480 0.6276 0.0715  -0.0405 0.0180  60   GLN C N   
6302  C  CA  . GLN C 60  ? 0.4658 0.5694 0.5489 0.0667  -0.0328 0.0121  60   GLN C CA  
6303  C  C   . GLN C 60  ? 0.4348 0.5313 0.5081 0.0506  -0.0338 0.0176  60   GLN C C   
6304  O  O   . GLN C 60  ? 0.5714 0.6543 0.6348 0.0463  -0.0294 0.0143  60   GLN C O   
6305  C  CB  . GLN C 60  ? 0.4082 0.5421 0.5022 0.0721  -0.0252 0.0065  60   GLN C CB  
6306  C  CG  . GLN C 60  ? 0.6315 0.7948 0.7435 0.0840  -0.0262 0.0069  60   GLN C CG  
6307  C  CD  . GLN C 60  ? 0.7736 0.9477 0.8907 0.0994  -0.0181 -0.0039 60   GLN C CD  
6308  O  OE1 . GLN C 60  ? 0.6655 0.8750 0.7981 0.1069  -0.0149 -0.0045 60   GLN C OE1 
6309  N  NE2 . GLN C 60  ? 0.6856 0.8297 0.7893 0.1039  -0.0146 -0.0128 60   GLN C NE2 
6310  N  N   . ALA C 61  ? 0.3086 0.4142 0.3845 0.0418  -0.0401 0.0258  61   ALA C N   
6311  C  CA  . ALA C 61  ? 0.3616 0.4557 0.4262 0.0273  -0.0418 0.0309  61   ALA C CA  
6312  C  C   . ALA C 61  ? 0.3610 0.4317 0.4151 0.0237  -0.0497 0.0353  61   ALA C C   
6313  O  O   . ALA C 61  ? 0.3472 0.4265 0.4074 0.0253  -0.0566 0.0390  61   ALA C O   
6314  C  CB  . ALA C 61  ? 0.4537 0.5754 0.5267 0.0167  -0.0420 0.0365  61   ALA C CB  
6315  N  N   . LYS C 62  ? 0.3965 0.4394 0.4344 0.0195  -0.0486 0.0349  62   LYS C N   
6316  C  CA  . LYS C 62  ? 0.3550 0.3741 0.3795 0.0164  -0.0547 0.0384  62   LYS C CA  
6317  C  C   . LYS C 62  ? 0.3381 0.3388 0.3475 0.0068  -0.0537 0.0402  62   LYS C C   
6318  O  O   . LYS C 62  ? 0.5269 0.5216 0.5325 0.0072  -0.0472 0.0373  62   LYS C O   
6319  C  CB  . LYS C 62  ? 0.3840 0.3830 0.4027 0.0260  -0.0537 0.0353  62   LYS C CB  
6320  C  CG  . LYS C 62  ? 0.5143 0.4894 0.5172 0.0234  -0.0592 0.0391  62   LYS C CG  
6321  C  CD  . LYS C 62  ? 0.7340 0.6914 0.7319 0.0323  -0.0583 0.0378  62   LYS C CD  
6322  C  CE  . LYS C 62  ? 0.9425 0.8760 0.9220 0.0291  -0.0618 0.0416  62   LYS C CE  
6323  N  NZ  . LYS C 62  ? 1.0777 1.0174 1.0545 0.0247  -0.0715 0.0465  62   LYS C NZ  
6324  N  N   . VAL C 63  ? 0.4020 0.3937 0.4022 -0.0012 -0.0605 0.0446  63   VAL C N   
6325  C  CA  . VAL C 63  ? 0.4378 0.4092 0.4220 -0.0088 -0.0598 0.0458  63   VAL C CA  
6326  C  C   . VAL C 63  ? 0.5873 0.5304 0.5544 -0.0051 -0.0589 0.0441  63   VAL C C   
6327  O  O   . VAL C 63  ? 0.4173 0.3522 0.3790 -0.0024 -0.0634 0.0448  63   VAL C O   
6328  C  CB  . VAL C 63  ? 0.3283 0.3009 0.3084 -0.0209 -0.0674 0.0506  63   VAL C CB  
6329  C  CG1 . VAL C 63  ? 0.2545 0.1985 0.2141 -0.0263 -0.0674 0.0509  63   VAL C CG1 
6330  C  CG2 . VAL C 63  ? 0.4870 0.4865 0.4820 -0.0269 -0.0661 0.0534  63   VAL C CG2 
6331  N  N   . HIS C 64  ? 0.6140 0.5443 0.5726 -0.0047 -0.0527 0.0425  64   HIS C N   
6332  C  CA  . HIS C 64  ? 0.4106 0.3185 0.3546 -0.0010 -0.0497 0.0409  64   HIS C CA  
6333  C  C   . HIS C 64  ? 0.4757 0.3655 0.4036 -0.0053 -0.0499 0.0419  64   HIS C C   
6334  O  O   . HIS C 64  ? 0.4480 0.3410 0.3775 -0.0082 -0.0480 0.0429  64   HIS C O   
6335  C  CB  . HIS C 64  ? 0.3499 0.2612 0.3002 0.0053  -0.0415 0.0375  64   HIS C CB  
6336  C  CG  . HIS C 64  ? 0.5657 0.4885 0.5287 0.0103  -0.0413 0.0354  64   HIS C CG  
6337  N  ND1 . HIS C 64  ? 0.6177 0.5297 0.5767 0.0145  -0.0424 0.0355  64   HIS C ND1 
6338  C  CD2 . HIS C 64  ? 0.6125 0.5553 0.5907 0.0125  -0.0401 0.0332  64   HIS C CD2 
6339  C  CE1 . HIS C 64  ? 0.5520 0.4744 0.5232 0.0197  -0.0423 0.0333  64   HIS C CE1 
6340  N  NE2 . HIS C 64  ? 0.5283 0.4701 0.5113 0.0190  -0.0406 0.0313  64   HIS C NE2 
6341  N  N   . PHE C 65  ? 0.5395 0.4092 0.4503 -0.0052 -0.0523 0.0417  65   PHE C N   
6342  C  CA  . PHE C 65  ? 0.5781 0.4255 0.4696 -0.0072 -0.0521 0.0411  65   PHE C CA  
6343  C  C   . PHE C 65  ? 0.5582 0.3965 0.4431 0.0007  -0.0430 0.0388  65   PHE C C   
6344  O  O   . PHE C 65  ? 0.5988 0.4350 0.4811 0.0046  -0.0401 0.0377  65   PHE C O   
6345  C  CB  . PHE C 65  ? 0.4990 0.3302 0.3733 -0.0118 -0.0601 0.0412  65   PHE C CB  
6346  C  CG  . PHE C 65  ? 0.5405 0.3443 0.3909 -0.0119 -0.0591 0.0388  65   PHE C CG  
6347  C  CD1 . PHE C 65  ? 0.6077 0.3972 0.4434 -0.0048 -0.0534 0.0362  65   PHE C CD1 
6348  C  CD2 . PHE C 65  ? 0.5596 0.3512 0.4015 -0.0189 -0.0635 0.0390  65   PHE C CD2 
6349  C  CE1 . PHE C 65  ? 0.6850 0.4500 0.4982 -0.0029 -0.0516 0.0331  65   PHE C CE1 
6350  C  CE2 . PHE C 65  ? 0.6324 0.3953 0.4506 -0.0174 -0.0625 0.0358  65   PHE C CE2 
6351  C  CZ  . PHE C 65  ? 0.7889 0.5392 0.5929 -0.0085 -0.0563 0.0324  65   PHE C CZ  
6352  N  N   . LEU C 66  ? 0.5878 0.4232 0.4711 0.0027  -0.0384 0.0381  66   LEU C N   
6353  C  CA  . LEU C 66  ? 0.3618 0.1971 0.2435 0.0103  -0.0294 0.0353  66   LEU C CA  
6354  C  C   . LEU C 66  ? 0.4692 0.2803 0.3291 0.0141  -0.0277 0.0341  66   LEU C C   
6355  O  O   . LEU C 66  ? 0.6273 0.4343 0.4811 0.0208  -0.0208 0.0329  66   LEU C O   
6356  C  CB  . LEU C 66  ? 0.3783 0.2290 0.2736 0.0124  -0.0254 0.0361  66   LEU C CB  
6357  C  CG  . LEU C 66  ? 0.4115 0.2837 0.3256 0.0092  -0.0270 0.0377  66   LEU C CG  
6358  C  CD1 . LEU C 66  ? 0.3808 0.2655 0.3035 0.0127  -0.0223 0.0387  66   LEU C CD1 
6359  C  CD2 . LEU C 66  ? 0.2340 0.1141 0.1564 0.0100  -0.0265 0.0362  66   LEU C CD2 
6360  N  N   . GLY C 67  ? 0.4679 0.2610 0.3149 0.0097  -0.0339 0.0351  67   GLY C N   
6361  C  CA  . GLY C 67  ? 0.6037 0.3691 0.4268 0.0136  -0.0330 0.0326  67   GLY C CA  
6362  C  C   . GLY C 67  ? 0.6111 0.3586 0.4241 0.0077  -0.0394 0.0335  67   GLY C C   
6363  O  O   . GLY C 67  ? 0.7630 0.5212 0.5876 -0.0011 -0.0451 0.0371  67   GLY C O   
6364  N  N   . ARG C 68  ? 0.6032 0.3229 0.3941 0.0124  -0.0383 0.0303  68   ARG C N   
6365  C  CA  . ARG C 68  ? 0.5608 0.2579 0.3396 0.0062  -0.0446 0.0313  68   ARG C CA  
6366  C  C   . ARG C 68  ? 0.6678 0.3485 0.4381 0.0177  -0.0386 0.0311  68   ARG C C   
6367  O  O   . ARG C 68  ? 0.7376 0.4180 0.5040 0.0312  -0.0300 0.0281  68   ARG C O   
6368  C  CB  . ARG C 68  ? 0.4870 0.1577 0.2421 -0.0019 -0.0527 0.0271  68   ARG C CB  
6369  C  CG  . ARG C 68  ? 0.6439 0.3239 0.4068 -0.0187 -0.0638 0.0303  68   ARG C CG  
6370  C  CD  . ARG C 68  ? 0.6924 0.3640 0.4405 -0.0246 -0.0709 0.0264  68   ARG C CD  
6371  N  NE  . ARG C 68  ? 0.7075 0.3876 0.4620 -0.0409 -0.0826 0.0294  68   ARG C NE  
6372  C  CZ  . ARG C 68  ? 0.9205 0.6107 0.6750 -0.0470 -0.0900 0.0290  68   ARG C CZ  
6373  N  NH1 . ARG C 68  ? 1.0386 0.7289 0.7853 -0.0384 -0.0866 0.0261  68   ARG C NH1 
6374  N  NH2 . ARG C 68  ? 1.0761 0.7783 0.8390 -0.0617 -0.1008 0.0324  68   ARG C NH2 
6375  N  N   . SER C 69  ? 0.5682 0.2364 0.3360 0.0124  -0.0431 0.0351  69   SER C N   
6376  C  CA  . SER C 69  ? 0.5108 0.1594 0.2685 0.0237  -0.0391 0.0361  69   SER C CA  
6377  C  C   . SER C 69  ? 0.5955 0.2031 0.3222 0.0291  -0.0396 0.0291  69   SER C C   
6378  O  O   . SER C 69  ? 0.5395 0.1331 0.2517 0.0205  -0.0451 0.0243  69   SER C O   
6379  C  CB  . SER C 69  ? 0.5266 0.1714 0.2888 0.0149  -0.0444 0.0438  69   SER C CB  
6380  O  OG  . SER C 69  ? 0.6246 0.2416 0.3697 0.0004  -0.0538 0.0434  69   SER C OG  
6381  N  N   . LEU C 70  ? 0.6526 0.2414 0.3684 0.0443  -0.0341 0.0282  70   LEU C N   
6382  C  CA  . LEU C 70  ? 0.6920 0.2368 0.3758 0.0508  -0.0346 0.0212  70   LEU C CA  
6383  C  C   . LEU C 70  ? 0.7363 0.2517 0.4021 0.0318  -0.0466 0.0198  70   LEU C C   
6384  O  O   . LEU C 70  ? 0.7647 0.2576 0.4082 0.0285  -0.0497 0.0118  70   LEU C O   
6385  C  CB  . LEU C 70  ? 0.7819 0.3065 0.4580 0.0669  -0.0305 0.0234  70   LEU C CB  
6386  C  CG  . LEU C 70  ? 0.8106 0.3594 0.5000 0.0885  -0.0187 0.0236  70   LEU C CG  
6387  C  CD1 . LEU C 70  ? 0.8398 0.3680 0.5219 0.1041  -0.0169 0.0275  70   LEU C CD1 
6388  C  CD2 . LEU C 70  ? 0.5572 0.1043 0.2342 0.0994  -0.0108 0.0142  70   LEU C CD2 
6389  N  N   . GLU C 71  ? 0.7016 0.2188 0.3769 0.0183  -0.0535 0.0279  71   GLU C N   
6390  C  CA  . GLU C 71  ? 0.6950 0.1829 0.3534 -0.0008 -0.0650 0.0278  71   GLU C CA  
6391  C  C   . GLU C 71  ? 0.7721 0.2858 0.4439 -0.0203 -0.0727 0.0289  71   GLU C C   
6392  O  O   . GLU C 71  ? 0.7989 0.3036 0.4678 -0.0394 -0.0825 0.0323  71   GLU C O   
6393  C  CB  . GLU C 71  ? 0.7752 0.2467 0.4330 -0.0062 -0.0685 0.0367  71   GLU C CB  
6394  C  CG  . GLU C 71  ? 0.8014 0.2428 0.4434 0.0141  -0.0624 0.0361  71   GLU C CG  
6395  C  CD  . GLU C 71  ? 1.0225 0.4461 0.6626 0.0090  -0.0663 0.0465  71   GLU C CD  
6396  O  OE1 . GLU C 71  ? 0.9854 0.4376 0.6464 -0.0050 -0.0693 0.0560  71   GLU C OE1 
6397  O  OE2 . GLU C 71  ? 1.1959 0.5761 0.8124 0.0196  -0.0660 0.0455  71   GLU C OE2 
6398  N  N   . GLY C 72  ? 0.8554 0.4014 0.5420 -0.0154 -0.0684 0.0265  72   GLY C N   
6399  C  CA  . GLY C 72  ? 0.7598 0.3264 0.4550 -0.0299 -0.0757 0.0262  72   GLY C CA  
6400  C  C   . GLY C 72  ? 0.7974 0.4055 0.5245 -0.0393 -0.0775 0.0345  72   GLY C C   
6401  O  O   . GLY C 72  ? 0.7916 0.4214 0.5292 -0.0487 -0.0829 0.0348  72   GLY C O   
6402  N  N   . ARG C 73  ? 0.7679 0.3876 0.5095 -0.0358 -0.0730 0.0412  73   ARG C N   
6403  C  CA  . ARG C 73  ? 0.7531 0.4117 0.5232 -0.0435 -0.0734 0.0485  73   ARG C CA  
6404  C  C   . ARG C 73  ? 0.7371 0.4312 0.5279 -0.0347 -0.0674 0.0469  73   ARG C C   
6405  O  O   . ARG C 73  ? 0.8100 0.5046 0.6000 -0.0197 -0.0592 0.0437  73   ARG C O   
6406  C  CB  . ARG C 73  ? 0.7026 0.3621 0.4789 -0.0416 -0.0701 0.0560  73   ARG C CB  
6407  C  CG  . ARG C 73  ? 0.7536 0.3779 0.5107 -0.0531 -0.0768 0.0598  73   ARG C CG  
6408  C  CD  . ARG C 73  ? 0.6648 0.2896 0.4268 -0.0503 -0.0735 0.0687  73   ARG C CD  
6409  N  NE  . ARG C 73  ? 0.5960 0.1731 0.3313 -0.0480 -0.0756 0.0695  73   ARG C NE  
6410  C  CZ  . ARG C 73  ? 0.6824 0.2318 0.4031 -0.0653 -0.0839 0.0734  73   ARG C CZ  
6411  N  NH1 . ARG C 73  ? 0.7671 0.2686 0.4617 -0.0617 -0.0857 0.0737  73   ARG C NH1 
6412  N  NH2 . ARG C 73  ? 0.8265 0.3969 0.5592 -0.0862 -0.0904 0.0771  73   ARG C NH2 
6413  N  N   . ASN C 74  ? 0.7913 0.5150 0.6010 -0.0439 -0.0713 0.0494  74   ASN C N   
6414  C  CA  . ASN C 74  ? 0.7365 0.4904 0.5647 -0.0365 -0.0666 0.0479  74   ASN C CA  
6415  C  C   . ASN C 74  ? 0.6386 0.4173 0.4863 -0.0284 -0.0586 0.0507  74   ASN C C   
6416  O  O   . ASN C 74  ? 0.5479 0.3412 0.4071 -0.0341 -0.0590 0.0560  74   ASN C O   
6417  C  CB  . ASN C 74  ? 0.6903 0.4661 0.5311 -0.0468 -0.0739 0.0491  74   ASN C CB  
6418  C  CG  . ASN C 74  ? 0.7937 0.5522 0.6171 -0.0504 -0.0809 0.0448  74   ASN C CG  
6419  O  OD1 . ASN C 74  ? 0.7946 0.5364 0.6030 -0.0411 -0.0772 0.0399  74   ASN C OD1 
6420  N  ND2 . ASN C 74  ? 0.9418 0.7066 0.7672 -0.0644 -0.0911 0.0468  74   ASN C ND2 
6421  N  N   . LEU C 75  ? 0.6804 0.4643 0.5308 -0.0161 -0.0513 0.0471  75   LEU C N   
6422  C  CA  . LEU C 75  ? 0.6726 0.4820 0.5417 -0.0093 -0.0445 0.0484  75   LEU C CA  
6423  C  C   . LEU C 75  ? 0.4693 0.3049 0.3562 -0.0117 -0.0453 0.0474  75   LEU C C   
6424  O  O   . LEU C 75  ? 0.6548 0.4898 0.5403 -0.0080 -0.0444 0.0441  75   LEU C O   
6425  C  CB  . LEU C 75  ? 0.6653 0.4705 0.5301 0.0037  -0.0364 0.0443  75   LEU C CB  
6426  C  CG  . LEU C 75  ? 0.6519 0.4385 0.5042 0.0106  -0.0337 0.0453  75   LEU C CG  
6427  C  CD1 . LEU C 75  ? 0.7911 0.5500 0.6269 0.0026  -0.0408 0.0486  75   LEU C CD1 
6428  C  CD2 . LEU C 75  ? 0.6873 0.4614 0.5282 0.0227  -0.0273 0.0410  75   LEU C CD2 
6429  N  N   . LEU C 76  ? 0.3719 0.2297 0.2743 -0.0173 -0.0467 0.0506  76   LEU C N   
6430  C  CA  . LEU C 76  ? 0.4565 0.3387 0.3756 -0.0187 -0.0479 0.0496  76   LEU C CA  
6431  C  C   . LEU C 76  ? 0.5013 0.4075 0.4369 -0.0135 -0.0418 0.0486  76   LEU C C   
6432  O  O   . LEU C 76  ? 0.6591 0.5708 0.5966 -0.0133 -0.0389 0.0510  76   LEU C O   
6433  C  CB  . LEU C 76  ? 0.5300 0.4220 0.4543 -0.0301 -0.0549 0.0536  76   LEU C CB  
6434  C  CG  . LEU C 76  ? 0.5823 0.4540 0.4916 -0.0385 -0.0632 0.0542  76   LEU C CG  
6435  C  CD1 . LEU C 76  ? 0.5632 0.4498 0.4807 -0.0520 -0.0696 0.0593  76   LEU C CD1 
6436  C  CD2 . LEU C 76  ? 0.5709 0.4398 0.4774 -0.0342 -0.0657 0.0506  76   LEU C CD2 
6437  N  N   . ALA C 77  ? 0.5529 0.4723 0.4992 -0.0093 -0.0405 0.0451  77   ALA C N   
6438  C  CA  . ALA C 77  ? 0.3809 0.3215 0.3414 -0.0052 -0.0355 0.0426  77   ALA C CA  
6439  C  C   . ALA C 77  ? 0.3958 0.3539 0.3691 -0.0052 -0.0378 0.0413  77   ALA C C   
6440  O  O   . ALA C 77  ? 0.4969 0.4485 0.4689 -0.0033 -0.0411 0.0402  77   ALA C O   
6441  C  CB  . ALA C 77  ? 0.3038 0.2395 0.2634 0.0021  -0.0300 0.0384  77   ALA C CB  
6442  N  N   . LEU C 78  ? 0.4056 0.3863 0.3905 -0.0064 -0.0360 0.0415  78   LEU C N   
6443  C  CA  . LEU C 78  ? 0.2510 0.2524 0.2498 -0.0042 -0.0369 0.0397  78   LEU C CA  
6444  C  C   . LEU C 78  ? 0.3864 0.3941 0.3918 0.0044  -0.0316 0.0327  78   LEU C C   
6445  O  O   . LEU C 78  ? 0.3626 0.3768 0.3687 0.0054  -0.0268 0.0303  78   LEU C O   
6446  C  CB  . LEU C 78  ? 0.2738 0.2985 0.2811 -0.0107 -0.0372 0.0437  78   LEU C CB  
6447  C  CG  . LEU C 78  ? 0.4155 0.4661 0.4389 -0.0074 -0.0377 0.0421  78   LEU C CG  
6448  C  CD1 . LEU C 78  ? 0.2931 0.3424 0.3182 -0.0110 -0.0457 0.0457  78   LEU C CD1 
6449  C  CD2 . LEU C 78  ? 0.3855 0.4643 0.4182 -0.0118 -0.0341 0.0446  78   LEU C CD2 
6450  N  N   . GLN C 79  ? 0.3745 0.3787 0.3835 0.0104  -0.0332 0.0298  79   GLN C N   
6451  C  CA  . GLN C 79  ? 0.2052 0.2104 0.2190 0.0183  -0.0291 0.0228  79   GLN C CA  
6452  C  C   . GLN C 79  ? 0.3488 0.3771 0.3759 0.0233  -0.0283 0.0200  79   GLN C C   
6453  O  O   . GLN C 79  ? 0.3674 0.4075 0.4016 0.0235  -0.0326 0.0236  79   GLN C O   
6454  C  CB  . GLN C 79  ? 0.4000 0.3844 0.4083 0.0225  -0.0313 0.0221  79   GLN C CB  
6455  C  CG  . GLN C 79  ? 0.3573 0.3407 0.3713 0.0310  -0.0293 0.0161  79   GLN C CG  
6456  C  CD  . GLN C 79  ? 0.3741 0.3352 0.3810 0.0344  -0.0321 0.0176  79   GLN C CD  
6457  O  OE1 . GLN C 79  ? 0.3611 0.3138 0.3613 0.0318  -0.0368 0.0233  79   GLN C OE1 
6458  N  NE2 . GLN C 79  ? 0.4256 0.3757 0.4324 0.0395  -0.0295 0.0125  79   GLN C NE2 
6459  N  N   . ILE C 80  ? 0.3368 0.3728 0.3672 0.0277  -0.0230 0.0131  80   ILE C N   
6460  C  CA  . ILE C 80  ? 0.3240 0.3815 0.3656 0.0347  -0.0206 0.0085  80   ILE C CA  
6461  C  C   . ILE C 80  ? 0.3761 0.4207 0.4161 0.0433  -0.0178 -0.0005 80   ILE C C   
6462  O  O   . ILE C 80  ? 0.5152 0.5504 0.5483 0.0410  -0.0147 -0.0052 80   ILE C O   
6463  C  CB  . ILE C 80  ? 0.3476 0.4288 0.3919 0.0308  -0.0160 0.0082  80   ILE C CB  
6464  C  CG1 . ILE C 80  ? 0.2426 0.3336 0.2873 0.0205  -0.0189 0.0181  80   ILE C CG1 
6465  C  CG2 . ILE C 80  ? 0.2585 0.3628 0.3131 0.0398  -0.0117 0.0016  80   ILE C CG2 
6466  C  CD1 . ILE C 80  ? 0.2659 0.3750 0.3096 0.0147  -0.0147 0.0202  80   ILE C CD1 
6467  N  N   . SER C 81  ? 0.4590 0.5028 0.5049 0.0531  -0.0193 -0.0029 81   SER C N   
6468  C  CA  . SER C 81  ? 0.4768 0.5022 0.5192 0.0613  -0.0174 -0.0113 81   SER C CA  
6469  C  C   . SER C 81  ? 0.5002 0.5367 0.5523 0.0751  -0.0168 -0.0159 81   SER C C   
6470  O  O   . SER C 81  ? 0.5567 0.6166 0.6197 0.0782  -0.0187 -0.0113 81   SER C O   
6471  C  CB  . SER C 81  ? 0.3986 0.3940 0.4322 0.0596  -0.0214 -0.0074 81   SER C CB  
6472  O  OG  . SER C 81  ? 0.6613 0.6586 0.6979 0.0609  -0.0273 0.0008  81   SER C OG  
6473  N  N   . ARG C 82  ? 0.5530 0.5728 0.6010 0.0836  -0.0143 -0.0252 82   ARG C N   
6474  C  CA  . ARG C 82  ? 0.5790 0.6030 0.6344 0.0997  -0.0139 -0.0299 82   ARG C CA  
6475  C  C   . ARG C 82  ? 0.6271 0.6469 0.6874 0.1047  -0.0211 -0.0205 82   ARG C C   
6476  O  O   . ARG C 82  ? 0.7140 0.7571 0.7872 0.1142  -0.0226 -0.0184 82   ARG C O   
6477  C  CB  . ARG C 82  ? 0.6276 0.6238 0.6737 0.1070  -0.0113 -0.0412 82   ARG C CB  
6478  C  CG  . ARG C 82  ? 0.6871 0.6858 0.7393 0.1263  -0.0098 -0.0481 82   ARG C CG  
6479  C  CD  . ARG C 82  ? 0.7859 0.7490 0.8256 0.1324  -0.0081 -0.0593 82   ARG C CD  
6480  N  NE  . ARG C 82  ? 0.8096 0.7829 0.8490 0.1426  -0.0017 -0.0730 82   ARG C NE  
6481  C  CZ  . ARG C 82  ? 0.9169 0.8634 0.9470 0.1533  0.0003  -0.0851 82   ARG C CZ  
6482  N  NH1 . ARG C 82  ? 0.7173 0.6221 0.7376 0.1553  -0.0038 -0.0847 82   ARG C NH1 
6483  N  NH2 . ARG C 82  ? 1.0509 1.0121 1.0802 0.1620  0.0068  -0.0979 82   ARG C NH2 
6484  N  N   . ASN C 83  ? 0.5036 0.4960 0.5537 0.0981  -0.0255 -0.0147 83   ASN C N   
6485  C  CA  . ASN C 83  ? 0.4490 0.4346 0.4997 0.1009  -0.0330 -0.0052 83   ASN C CA  
6486  C  C   . ASN C 83  ? 0.5059 0.4779 0.5460 0.0867  -0.0363 0.0027  83   ASN C C   
6487  O  O   . ASN C 83  ? 0.5135 0.4576 0.5411 0.0820  -0.0352 0.0023  83   ASN C O   
6488  C  CB  . ASN C 83  ? 0.6715 0.6294 0.7172 0.1138  -0.0352 -0.0071 83   ASN C CB  
6489  C  CG  . ASN C 83  ? 0.8411 0.7843 0.8816 0.1141  -0.0432 0.0037  83   ASN C CG  
6490  O  OD1 . ASN C 83  ? 0.8269 0.7891 0.8726 0.1099  -0.0484 0.0114  83   ASN C OD1 
6491  N  ND2 . ASN C 83  ? 0.8791 0.7871 0.9076 0.1181  -0.0447 0.0044  83   ASN C ND2 
6492  N  N   . THR C 84  ? 0.4686 0.4599 0.5132 0.0798  -0.0401 0.0098  84   THR C N   
6493  C  CA  . THR C 84  ? 0.2940 0.2743 0.3276 0.0668  -0.0423 0.0159  84   THR C CA  
6494  C  C   . THR C 84  ? 0.4379 0.3906 0.4590 0.0672  -0.0470 0.0212  84   THR C C   
6495  O  O   . THR C 84  ? 0.5447 0.4823 0.5534 0.0581  -0.0467 0.0243  84   THR C O   
6496  C  CB  . THR C 84  ? 0.4026 0.4066 0.4424 0.0593  -0.0463 0.0218  84   THR C CB  
6497  O  OG1 . THR C 84  ? 0.5097 0.5108 0.5419 0.0474  -0.0434 0.0225  84   THR C OG1 
6498  C  CG2 . THR C 84  ? 0.1338 0.1328 0.1700 0.0590  -0.0553 0.0295  84   THR C CG2 
6499  N  N   . ARG C 85  ? 0.4876 0.4339 0.5110 0.0787  -0.0511 0.0227  85   ARG C N   
6500  C  CA  . ARG C 85  ? 0.5467 0.4665 0.5567 0.0798  -0.0559 0.0290  85   ARG C CA  
6501  C  C   . ARG C 85  ? 0.5990 0.4905 0.5950 0.0733  -0.0503 0.0270  85   ARG C C   
6502  O  O   . ARG C 85  ? 0.6609 0.5373 0.6436 0.0659  -0.0513 0.0324  85   ARG C O   
6503  C  CB  . ARG C 85  ? 0.6545 0.5694 0.6691 0.0953  -0.0607 0.0307  85   ARG C CB  
6504  C  CG  . ARG C 85  ? 0.9246 0.8700 0.9541 0.1025  -0.0676 0.0345  85   ARG C CG  
6505  C  CD  . ARG C 85  ? 1.2342 1.1696 1.2628 0.1164  -0.0754 0.0405  85   ARG C CD  
6506  N  NE  . ARG C 85  ? 1.3538 1.2741 1.3672 0.1100  -0.0829 0.0500  85   ARG C NE  
6507  C  CZ  . ARG C 85  ? 1.3291 1.2147 1.3235 0.1077  -0.0823 0.0534  85   ARG C CZ  
6508  N  NH1 . ARG C 85  ? 1.3002 1.1757 1.2800 0.1021  -0.0889 0.0619  85   ARG C NH1 
6509  N  NH2 . ARG C 85  ? 1.2946 1.1558 1.2836 0.1100  -0.0752 0.0483  85   ARG C NH2 
6510  N  N   . SER C 86  ? 0.5827 0.4682 0.5814 0.0758  -0.0443 0.0190  86   SER C N   
6511  C  CA  . SER C 86  ? 0.6007 0.4625 0.5883 0.0684  -0.0393 0.0170  86   SER C CA  
6512  C  C   . SER C 86  ? 0.8177 0.6904 0.8104 0.0631  -0.0327 0.0081  86   SER C C   
6513  O  O   . SER C 86  ? 0.9781 0.8762 0.9798 0.0621  -0.0315 0.0056  86   SER C O   
6514  C  CB  . SER C 86  ? 0.5067 0.3403 0.4880 0.0758  -0.0402 0.0166  86   SER C CB  
6515  O  OG  . SER C 86  ? 0.5494 0.3718 0.5239 0.0807  -0.0468 0.0261  86   SER C OG  
6516  N  N   . ARG C 87  ? 0.7188 0.5719 0.7049 0.0586  -0.0287 0.0039  87   ARG C N   
6517  C  CA  . ARG C 87  ? 0.6176 0.4785 0.6074 0.0543  -0.0235 -0.0055 87   ARG C CA  
6518  C  C   . ARG C 87  ? 0.5747 0.4115 0.5601 0.0584  -0.0226 -0.0122 87   ARG C C   
6519  O  O   . ARG C 87  ? 0.5092 0.3196 0.4851 0.0541  -0.0230 -0.0087 87   ARG C O   
6520  C  CB  . ARG C 87  ? 0.3145 0.1768 0.2999 0.0411  -0.0200 -0.0040 87   ARG C CB  
6521  C  CG  . ARG C 87  ? 0.3094 0.1943 0.3011 0.0370  -0.0166 -0.0104 87   ARG C CG  
6522  C  CD  . ARG C 87  ? 0.3343 0.2204 0.3226 0.0260  -0.0135 -0.0089 87   ARG C CD  
6523  N  NE  . ARG C 87  ? 0.5378 0.4083 0.5227 0.0205  -0.0115 -0.0144 87   ARG C NE  
6524  C  CZ  . ARG C 87  ? 0.5694 0.4210 0.5475 0.0138  -0.0105 -0.0102 87   ARG C CZ  
6525  N  NH1 . ARG C 87  ? 0.6270 0.4734 0.6000 0.0130  -0.0109 -0.0007 87   ARG C NH1 
6526  N  NH2 . ARG C 87  ? 0.6616 0.4998 0.6372 0.0070  -0.0090 -0.0156 87   ARG C NH2 
6527  N  N   . ASN C 88  ? 0.6280 0.4726 0.6192 0.0664  -0.0212 -0.0219 88   ASN C N   
6528  C  CA  . ASN C 88  ? 0.5478 0.3662 0.5330 0.0709  -0.0203 -0.0301 88   ASN C CA  
6529  C  C   . ASN C 88  ? 0.5220 0.3245 0.4991 0.0560  -0.0176 -0.0337 88   ASN C C   
6530  O  O   . ASN C 88  ? 0.5617 0.3835 0.5418 0.0461  -0.0149 -0.0360 88   ASN C O   
6531  C  CB  . ASN C 88  ? 0.6485 0.4813 0.6402 0.0823  -0.0181 -0.0415 88   ASN C CB  
6532  C  CG  . ASN C 88  ? 0.7443 0.5935 0.7457 0.0979  -0.0207 -0.0378 88   ASN C CG  
6533  O  OD1 . ASN C 88  ? 0.8741 0.7559 0.8860 0.1015  -0.0189 -0.0397 88   ASN C OD1 
6534  N  ND2 . ASN C 88  ? 0.8510 0.6793 0.8492 0.1066  -0.0252 -0.0314 88   ASN C ND2 
6535  N  N   . LEU C 89  ? 0.4087 0.1765 0.3758 0.0541  -0.0186 -0.0334 89   LEU C N   
6536  C  CA  . LEU C 89  ? 0.5460 0.2981 0.5060 0.0383  -0.0165 -0.0362 89   LEU C CA  
6537  C  C   . LEU C 89  ? 0.6525 0.4231 0.6163 0.0324  -0.0137 -0.0486 89   LEU C C   
6538  O  O   . LEU C 89  ? 0.5685 0.3430 0.5336 0.0421  -0.0133 -0.0593 89   LEU C O   
6539  C  CB  . LEU C 89  ? 0.5368 0.2457 0.4848 0.0385  -0.0182 -0.0368 89   LEU C CB  
6540  C  CG  . LEU C 89  ? 0.4886 0.1776 0.4285 0.0194  -0.0166 -0.0358 89   LEU C CG  
6541  C  CD1 . LEU C 89  ? 0.3570 0.0495 0.2954 0.0105  -0.0157 -0.0215 89   LEU C CD1 
6542  C  CD2 . LEU C 89  ? 0.6080 0.2524 0.5352 0.0199  -0.0185 -0.0399 89   LEU C CD2 
6543  N  N   . LEU C 90  ? 0.6636 0.4478 0.6291 0.0175  -0.0119 -0.0469 90   LEU C N   
6544  C  CA  . LEU C 90  ? 0.6246 0.4268 0.5927 0.0100  -0.0104 -0.0570 90   LEU C CA  
6545  C  C   . LEU C 90  ? 0.6345 0.4719 0.6109 0.0172  -0.0093 -0.0594 90   LEU C C   
6546  O  O   . LEU C 90  ? 0.6233 0.4776 0.6006 0.0125  -0.0084 -0.0674 90   LEU C O   
6547  C  CB  . LEU C 90  ? 0.5192 0.2960 0.4786 0.0083  -0.0111 -0.0702 90   LEU C CB  
6548  C  CG  . LEU C 90  ? 0.5059 0.2521 0.4572 -0.0061 -0.0120 -0.0677 90   LEU C CG  
6549  C  CD1 . LEU C 90  ? 0.3636 0.0771 0.3036 -0.0083 -0.0136 -0.0810 90   LEU C CD1 
6550  C  CD2 . LEU C 90  ? 0.4554 0.2247 0.4125 -0.0231 -0.0106 -0.0636 90   LEU C CD2 
6551  N  N   . THR C 91  ? 0.4893 0.3382 0.4710 0.0275  -0.0098 -0.0519 91   THR C N   
6552  C  CA  . THR C 91  ? 0.4592 0.3413 0.4485 0.0312  -0.0087 -0.0518 91   THR C CA  
6553  C  C   . THR C 91  ? 0.5122 0.4114 0.5042 0.0210  -0.0081 -0.0442 91   THR C C   
6554  O  O   . THR C 91  ? 0.4102 0.3029 0.4014 0.0182  -0.0087 -0.0345 91   THR C O   
6555  C  CB  . THR C 91  ? 0.3381 0.2297 0.3331 0.0435  -0.0099 -0.0463 91   THR C CB  
6556  O  OG1 . THR C 91  ? 0.4151 0.2943 0.4092 0.0559  -0.0101 -0.0535 91   THR C OG1 
6557  C  CG2 . THR C 91  ? 0.2561 0.1815 0.2581 0.0439  -0.0084 -0.0454 91   THR C CG2 
6558  N  N   . PRO C 92  ? 0.4559 0.3769 0.4501 0.0163  -0.0069 -0.0485 92   PRO C N   
6559  C  CA  . PRO C 92  ? 0.4080 0.3468 0.4050 0.0088  -0.0064 -0.0417 92   PRO C CA  
6560  C  C   . PRO C 92  ? 0.4541 0.4040 0.4545 0.0136  -0.0068 -0.0318 92   PRO C C   
6561  O  O   . PRO C 92  ? 0.4124 0.3751 0.4157 0.0202  -0.0070 -0.0325 92   PRO C O   
6562  C  CB  . PRO C 92  ? 0.4611 0.4217 0.4589 0.0065  -0.0060 -0.0491 92   PRO C CB  
6563  C  CG  . PRO C 92  ? 0.4225 0.3735 0.4159 0.0108  -0.0058 -0.0614 92   PRO C CG  
6564  C  CD  . PRO C 92  ? 0.4135 0.3447 0.4066 0.0202  -0.0059 -0.0600 92   PRO C CD  
6565  N  N   . PRO C 93  ? 0.5714 0.5171 0.5708 0.0099  -0.0068 -0.0229 93   PRO C N   
6566  C  CA  . PRO C 93  ? 0.4912 0.4472 0.4915 0.0125  -0.0075 -0.0145 93   PRO C CA  
6567  C  C   . PRO C 93  ? 0.4693 0.4454 0.4715 0.0090  -0.0065 -0.0132 93   PRO C C   
6568  O  O   . PRO C 93  ? 0.3815 0.3622 0.3844 0.0036  -0.0054 -0.0151 93   PRO C O   
6569  C  CB  . PRO C 93  ? 0.3988 0.3383 0.3943 0.0107  -0.0075 -0.0072 93   PRO C CB  
6570  C  CG  . PRO C 93  ? 0.4009 0.3281 0.3945 0.0043  -0.0056 -0.0104 93   PRO C CG  
6571  C  CD  . PRO C 93  ? 0.3755 0.3078 0.3720 0.0025  -0.0056 -0.0205 93   PRO C CD  
6572  N  N   . VAL C 94  ? 0.4247 0.4134 0.4280 0.0119  -0.0074 -0.0093 94   VAL C N   
6573  C  CA  . VAL C 94  ? 0.3309 0.3372 0.3346 0.0100  -0.0071 -0.0071 94   VAL C CA  
6574  C  C   . VAL C 94  ? 0.2524 0.2592 0.2538 0.0117  -0.0084 0.0017  94   VAL C C   
6575  O  O   . VAL C 94  ? 0.3879 0.3878 0.3891 0.0137  -0.0099 0.0041  94   VAL C O   
6576  C  CB  . VAL C 94  ? 0.5270 0.5502 0.5324 0.0108  -0.0067 -0.0137 94   VAL C CB  
6577  C  CG1 . VAL C 94  ? 0.7430 0.7845 0.7473 0.0088  -0.0070 -0.0102 94   VAL C CG1 
6578  C  CG2 . VAL C 94  ? 0.4158 0.4337 0.4210 0.0092  -0.0061 -0.0244 94   VAL C CG2 
6579  N  N   . LYS C 95  ? 0.2010 0.2156 0.2004 0.0108  -0.0083 0.0067  95   LYS C N   
6580  C  CA  . LYS C 95  ? 0.3278 0.3390 0.3229 0.0116  -0.0099 0.0148  95   LYS C CA  
6581  C  C   . LYS C 95  ? 0.3870 0.4126 0.3806 0.0112  -0.0104 0.0190  95   LYS C C   
6582  O  O   . LYS C 95  ? 0.4075 0.4457 0.4026 0.0111  -0.0097 0.0167  95   LYS C O   
6583  C  CB  . LYS C 95  ? 0.2618 0.2569 0.2515 0.0127  -0.0096 0.0191  95   LYS C CB  
6584  C  CG  . LYS C 95  ? 0.2611 0.2613 0.2519 0.0134  -0.0071 0.0187  95   LYS C CG  
6585  C  CD  . LYS C 95  ? 0.3070 0.2937 0.2959 0.0133  -0.0048 0.0181  95   LYS C CD  
6586  C  CE  . LYS C 95  ? 0.3402 0.3290 0.3274 0.0163  -0.0021 0.0218  95   LYS C CE  
6587  N  NZ  . LYS C 95  ? 0.4992 0.5090 0.4938 0.0160  -0.0016 0.0207  95   LYS C NZ  
6588  N  N   . TYR C 96  ? 0.3401 0.3632 0.3298 0.0102  -0.0122 0.0256  96   TYR C N   
6589  C  CA  . TYR C 96  ? 0.4738 0.5044 0.4590 0.0096  -0.0130 0.0323  96   TYR C CA  
6590  C  C   . TYR C 96  ? 0.4860 0.4973 0.4628 0.0096  -0.0150 0.0401  96   TYR C C   
6591  O  O   . TYR C 96  ? 0.3933 0.3948 0.3682 0.0064  -0.0170 0.0419  96   TYR C O   
6592  C  CB  . TYR C 96  ? 0.3155 0.3626 0.3024 0.0062  -0.0129 0.0333  96   TYR C CB  
6593  C  CG  . TYR C 96  ? 0.3745 0.4424 0.3647 0.0068  -0.0109 0.0269  96   TYR C CG  
6594  C  CD1 . TYR C 96  ? 0.3363 0.4084 0.3268 0.0087  -0.0108 0.0228  96   TYR C CD1 
6595  C  CD2 . TYR C 96  ? 0.4472 0.5319 0.4395 0.0051  -0.0092 0.0249  96   TYR C CD2 
6596  C  CE1 . TYR C 96  ? 0.3455 0.4357 0.3369 0.0080  -0.0099 0.0160  96   TYR C CE1 
6597  C  CE2 . TYR C 96  ? 0.4963 0.5987 0.4885 0.0059  -0.0073 0.0178  96   TYR C CE2 
6598  C  CZ  . TYR C 96  ? 0.4948 0.5986 0.4858 0.0069  -0.0082 0.0131  96   TYR C CZ  
6599  O  OH  . TYR C 96  ? 0.4672 0.5874 0.4563 0.0067  -0.0072 0.0052  96   TYR C OH  
6600  N  N   . ILE C 97  ? 0.3613 0.3670 0.3327 0.0137  -0.0150 0.0442  97   ILE C N   
6601  C  CA  . ILE C 97  ? 0.3888 0.3730 0.3495 0.0147  -0.0169 0.0509  97   ILE C CA  
6602  C  C   . ILE C 97  ? 0.4309 0.4163 0.3851 0.0148  -0.0186 0.0592  97   ILE C C   
6603  O  O   . ILE C 97  ? 0.3813 0.3843 0.3385 0.0172  -0.0181 0.0603  97   ILE C O   
6604  C  CB  . ILE C 97  ? 0.4920 0.4622 0.4487 0.0214  -0.0151 0.0497  97   ILE C CB  
6605  C  CG1 . ILE C 97  ? 0.4831 0.4501 0.4441 0.0203  -0.0133 0.0430  97   ILE C CG1 
6606  C  CG2 . ILE C 97  ? 0.4544 0.3989 0.3972 0.0233  -0.0170 0.0552  97   ILE C CG2 
6607  C  CD1 . ILE C 97  ? 0.5512 0.5369 0.5233 0.0203  -0.0107 0.0370  97   ILE C CD1 
6608  N  N   . ALA C 98  ? 0.2749 0.2405 0.2190 0.0116  -0.0214 0.0655  98   ALA C N   
6609  C  CA  . ALA C 98  ? 0.3427 0.3035 0.2780 0.0109  -0.0234 0.0749  98   ALA C CA  
6610  C  C   . ALA C 98  ? 0.3808 0.3094 0.3014 0.0138  -0.0257 0.0801  98   ALA C C   
6611  O  O   . ALA C 98  ? 0.5128 0.4231 0.4290 0.0155  -0.0257 0.0759  98   ALA C O   
6612  C  CB  . ALA C 98  ? 0.2100 0.1826 0.1470 0.0004  -0.0246 0.0791  98   ALA C CB  
6613  N  N   . ASN C 99  ? 0.5383 0.4587 0.4496 0.0148  -0.0277 0.0893  99   ASN C N   
6614  C  CA  . ASN C 99  ? 0.4347 0.3198 0.3291 0.0157  -0.0307 0.0951  99   ASN C CA  
6615  C  C   . ASN C 99  ? 0.6252 0.4883 0.5127 0.0267  -0.0292 0.0897  99   ASN C C   
6616  O  O   . ASN C 99  ? 0.6199 0.4525 0.4940 0.0244  -0.0314 0.0892  99   ASN C O   
6617  C  CB  . ASN C 99  ? 0.3855 0.2586 0.2750 0.0006  -0.0341 0.0974  99   ASN C CB  
6618  C  CG  . ASN C 99  ? 0.6563 0.4919 0.5263 -0.0021 -0.0383 0.1049  99   ASN C CG  
6619  O  OD1 . ASN C 99  ? 0.7094 0.5208 0.5705 -0.0079 -0.0412 0.1022  99   ASN C OD1 
6620  N  ND2 . ASN C 99  ? 0.5535 0.3824 0.4153 0.0019  -0.0391 0.1144  99   ASN C ND2 
6621  N  N   . MET C 100 ? 0.6678 0.5475 0.5643 0.0380  -0.0253 0.0852  100  MET C N   
6622  C  CA  . MET C 100 ? 0.6511 0.5144 0.5415 0.0501  -0.0225 0.0811  100  MET C CA  
6623  C  C   . MET C 100 ? 0.6806 0.5178 0.5555 0.0605  -0.0241 0.0882  100  MET C C   
6624  O  O   . MET C 100 ? 0.5626 0.3711 0.4240 0.0675  -0.0233 0.0857  100  MET C O   
6625  C  CB  . MET C 100 ? 0.5872 0.4785 0.4928 0.0582  -0.0177 0.0756  100  MET C CB  
6626  C  CG  . MET C 100 ? 0.6460 0.5575 0.5580 0.0676  -0.0176 0.0808  100  MET C CG  
6627  S  SD  . MET C 100 ? 0.7007 0.6463 0.6314 0.0734  -0.0126 0.0739  100  MET C SD  
6628  C  CE  . MET C 100 ? 0.4757 0.4005 0.4001 0.0784  -0.0075 0.0673  100  MET C CE  
6629  N  N   . HIS C 101 ? 0.6074 0.4540 0.4830 0.0623  -0.0264 0.0968  101  HIS C N   
6630  C  CA  . HIS C 101 ? 0.4636 0.2805 0.3220 0.0684  -0.0296 0.1060  101  HIS C CA  
6631  C  C   . HIS C 101 ? 0.6707 0.4692 0.5189 0.0512  -0.0342 0.1115  101  HIS C C   
6632  O  O   . HIS C 101 ? 0.5742 0.3927 0.4284 0.0413  -0.0358 0.1175  101  HIS C O   
6633  C  CB  . HIS C 101 ? 0.4242 0.2606 0.2875 0.0791  -0.0304 0.1139  101  HIS C CB  
6634  C  CG  . HIS C 101 ? 0.6242 0.4821 0.4993 0.0951  -0.0263 0.1092  101  HIS C CG  
6635  N  ND1 . HIS C 101 ? 0.6756 0.5754 0.5697 0.0943  -0.0248 0.1062  101  HIS C ND1 
6636  C  CD2 . HIS C 101 ? 0.8114 0.6559 0.6821 0.1117  -0.0232 0.1067  101  HIS C CD2 
6637  C  CE1 . HIS C 101 ? 0.7471 0.6603 0.6495 0.1085  -0.0214 0.1030  101  HIS C CE1 
6638  N  NE2 . HIS C 101 ? 0.7952 0.6768 0.6842 0.1200  -0.0198 0.1033  101  HIS C NE2 
6639  N  N   . GLY C 102 ? 0.6301 0.3927 0.4630 0.0470  -0.0361 0.1086  102  GLY C N   
6640  C  CA  . GLY C 102 ? 0.5407 0.2859 0.3647 0.0285  -0.0410 0.1126  102  GLY C CA  
6641  C  C   . GLY C 102 ? 0.5773 0.3188 0.3950 0.0208  -0.0445 0.1264  102  GLY C C   
6642  O  O   . GLY C 102 ? 0.7294 0.4721 0.5467 0.0027  -0.0474 0.1310  102  GLY C O   
6643  N  N   . ASP C 103 ? 0.5750 0.3133 0.3877 0.0342  -0.0444 0.1341  103  ASP C N   
6644  C  CA  . ASP C 103 ? 0.6243 0.3587 0.4289 0.0282  -0.0478 0.1488  103  ASP C CA  
6645  C  C   . ASP C 103 ? 0.6412 0.4219 0.4619 0.0269  -0.0458 0.1525  103  ASP C C   
6646  O  O   . ASP C 103 ? 0.6661 0.4496 0.4805 0.0243  -0.0479 0.1647  103  ASP C O   
6647  C  CB  . ASP C 103 ? 0.7650 0.4658 0.5518 0.0439  -0.0501 0.1568  103  ASP C CB  
6648  C  CG  . ASP C 103 ? 0.8402 0.5562 0.6353 0.0676  -0.0466 0.1521  103  ASP C CG  
6649  O  OD1 . ASP C 103 ? 1.0109 0.6983 0.7924 0.0842  -0.0477 0.1562  103  ASP C OD1 
6650  O  OD2 . ASP C 103 ? 0.9129 0.6688 0.7279 0.0698  -0.0429 0.1447  103  ASP C OD2 
6651  N  N   . GLU C 104 ? 0.6002 0.4159 0.4401 0.0289  -0.0419 0.1415  104  GLU C N   
6652  C  CA  . GLU C 104 ? 0.3949 0.2540 0.2494 0.0254  -0.0400 0.1418  104  GLU C CA  
6653  C  C   . GLU C 104 ? 0.6276 0.5036 0.4929 0.0095  -0.0382 0.1349  104  GLU C C   
6654  O  O   . GLU C 104 ? 0.6564 0.5418 0.5327 0.0110  -0.0358 0.1233  104  GLU C O   
6655  C  CB  . GLU C 104 ? 0.3373 0.2223 0.2048 0.0403  -0.0374 0.1346  104  GLU C CB  
6656  C  CG  . GLU C 104 ? 0.6899 0.5596 0.5496 0.0588  -0.0389 0.1399  104  GLU C CG  
6657  C  CD  . GLU C 104 ? 0.8649 0.7618 0.7401 0.0720  -0.0359 0.1316  104  GLU C CD  
6658  O  OE1 . GLU C 104 ? 0.9364 0.8630 0.8268 0.0655  -0.0334 0.1227  104  GLU C OE1 
6659  O  OE2 . GLU C 104 ? 0.9536 0.8425 0.8261 0.0888  -0.0361 0.1338  104  GLU C OE2 
6660  N  N   . THR C 105 ? 0.7497 0.6302 0.6116 -0.0052 -0.0393 0.1429  105  THR C N   
6661  C  CA  . THR C 105 ? 0.6460 0.5326 0.5143 -0.0211 -0.0390 0.1392  105  THR C CA  
6662  C  C   . THR C 105 ? 0.5539 0.4828 0.4373 -0.0288 -0.0353 0.1366  105  THR C C   
6663  O  O   . THR C 105 ? 0.4871 0.4278 0.3807 -0.0371 -0.0342 0.1304  105  THR C O   
6664  C  CB  . THR C 105 ? 0.6286 0.4857 0.4818 -0.0355 -0.0431 0.1502  105  THR C CB  
6665  O  OG1 . THR C 105 ? 0.4099 0.2763 0.2569 -0.0415 -0.0431 0.1634  105  THR C OG1 
6666  C  CG2 . THR C 105 ? 0.7337 0.5432 0.5689 -0.0281 -0.0469 0.1516  105  THR C CG2 
6667  N  N   . VAL C 106 ? 0.5165 0.4682 0.4003 -0.0254 -0.0336 0.1412  106  VAL C N   
6668  C  CA  . VAL C 106 ? 0.5261 0.5164 0.4213 -0.0319 -0.0295 0.1381  106  VAL C CA  
6669  C  C   . VAL C 106 ? 0.5645 0.5743 0.4765 -0.0276 -0.0264 0.1224  106  VAL C C   
6670  O  O   . VAL C 106 ? 0.4735 0.5019 0.3954 -0.0354 -0.0239 0.1180  106  VAL C O   
6671  C  CB  . VAL C 106 ? 0.5992 0.6106 0.4902 -0.0270 -0.0285 0.1434  106  VAL C CB  
6672  C  CG1 . VAL C 106 ? 0.5803 0.6304 0.4812 -0.0329 -0.0235 0.1382  106  VAL C CG1 
6673  C  CG2 . VAL C 106 ? 0.6479 0.6399 0.5213 -0.0315 -0.0315 0.1604  106  VAL C CG2 
6674  N  N   . GLY C 107 ? 0.6074 0.6137 0.5226 -0.0152 -0.0266 0.1147  107  GLY C N   
6675  C  CA  . GLY C 107 ? 0.4894 0.5073 0.4180 -0.0114 -0.0242 0.1009  107  GLY C CA  
6676  C  C   . GLY C 107 ? 0.5596 0.5678 0.4928 -0.0188 -0.0246 0.0974  107  GLY C C   
6677  O  O   . GLY C 107 ? 0.5630 0.5903 0.5077 -0.0215 -0.0223 0.0901  107  GLY C O   
6678  N  N   . ARG C 108 ? 0.4790 0.4569 0.4023 -0.0215 -0.0282 0.1025  108  ARG C N   
6679  C  CA  . ARG C 108 ? 0.5138 0.4803 0.4386 -0.0302 -0.0304 0.1007  108  ARG C CA  
6680  C  C   . ARG C 108 ? 0.4715 0.4639 0.4066 -0.0416 -0.0291 0.1019  108  ARG C C   
6681  O  O   . ARG C 108 ? 0.4777 0.4832 0.4247 -0.0421 -0.0283 0.0942  108  ARG C O   
6682  C  CB  . ARG C 108 ? 0.4860 0.4163 0.3943 -0.0346 -0.0350 0.1087  108  ARG C CB  
6683  C  CG  . ARG C 108 ? 0.5493 0.4691 0.4562 -0.0483 -0.0388 0.1103  108  ARG C CG  
6684  C  CD  . ARG C 108 ? 0.6742 0.5518 0.5613 -0.0512 -0.0437 0.1162  108  ARG C CD  
6685  N  NE  . ARG C 108 ? 0.6757 0.5396 0.5599 -0.0645 -0.0487 0.1156  108  ARG C NE  
6686  C  CZ  . ARG C 108 ? 0.5990 0.4359 0.4742 -0.0628 -0.0522 0.1094  108  ARG C CZ  
6687  N  NH1 . ARG C 108 ? 0.5791 0.4091 0.4526 -0.0773 -0.0577 0.1097  108  ARG C NH1 
6688  N  NH2 . ARG C 108 ? 0.6416 0.4602 0.5093 -0.0476 -0.0504 0.1032  108  ARG C NH2 
6689  N  N   . GLN C 109 ? 0.5177 0.5182 0.4481 -0.0501 -0.0287 0.1121  109  GLN C N   
6690  C  CA  . GLN C 109 ? 0.5362 0.5646 0.4767 -0.0612 -0.0266 0.1144  109  GLN C CA  
6691  C  C   . GLN C 109 ? 0.3833 0.4467 0.3370 -0.0542 -0.0209 0.1055  109  GLN C C   
6692  O  O   . GLN C 109 ? 0.4256 0.5116 0.3923 -0.0574 -0.0187 0.1012  109  GLN C O   
6693  C  CB  . GLN C 109 ? 0.5801 0.6091 0.5111 -0.0730 -0.0268 0.1286  109  GLN C CB  
6694  C  CG  . GLN C 109 ? 0.6561 0.6582 0.5786 -0.0869 -0.0324 0.1369  109  GLN C CG  
6695  C  CD  . GLN C 109 ? 0.6996 0.7149 0.6357 -0.0961 -0.0340 0.1324  109  GLN C CD  
6696  O  OE1 . GLN C 109 ? 0.8530 0.8437 0.7855 -0.0985 -0.0395 0.1293  109  GLN C OE1 
6697  N  NE2 . GLN C 109 ? 0.5148 0.5702 0.4663 -0.1008 -0.0294 0.1320  109  GLN C NE2 
6698  N  N   . LEU C 110 ? 0.3073 0.3750 0.2574 -0.0442 -0.0188 0.1024  110  LEU C N   
6699  C  CA  . LEU C 110 ? 0.4039 0.5006 0.3636 -0.0378 -0.0139 0.0925  110  LEU C CA  
6700  C  C   . LEU C 110 ? 0.4979 0.5958 0.4700 -0.0328 -0.0136 0.0804  110  LEU C C   
6701  O  O   . LEU C 110 ? 0.5251 0.6464 0.5077 -0.0318 -0.0099 0.0738  110  LEU C O   
6702  C  CB  . LEU C 110 ? 0.3527 0.4513 0.3061 -0.0288 -0.0135 0.0903  110  LEU C CB  
6703  C  CG  . LEU C 110 ? 0.3429 0.4501 0.2847 -0.0321 -0.0131 0.1013  110  LEU C CG  
6704  C  CD1 . LEU C 110 ? 0.4302 0.5474 0.3689 -0.0229 -0.0130 0.0966  110  LEU C CD1 
6705  C  CD2 . LEU C 110 ? 0.3291 0.4636 0.2737 -0.0405 -0.0084 0.1043  110  LEU C CD2 
6706  N  N   . LEU C 111 ? 0.4396 0.5116 0.4095 -0.0291 -0.0172 0.0779  111  LEU C N   
6707  C  CA  . LEU C 111 ? 0.3636 0.4336 0.3429 -0.0244 -0.0173 0.0680  111  LEU C CA  
6708  C  C   . LEU C 111 ? 0.3918 0.4691 0.3788 -0.0319 -0.0189 0.0699  111  LEU C C   
6709  O  O   . LEU C 111 ? 0.5644 0.6562 0.5628 -0.0283 -0.0173 0.0628  111  LEU C O   
6710  C  CB  . LEU C 111 ? 0.5466 0.5887 0.5200 -0.0189 -0.0201 0.0655  111  LEU C CB  
6711  C  CG  . LEU C 111 ? 0.5800 0.6212 0.5507 -0.0103 -0.0183 0.0617  111  LEU C CG  
6712  C  CD1 . LEU C 111 ? 0.4296 0.4488 0.3972 -0.0045 -0.0195 0.0583  111  LEU C CD1 
6713  C  CD2 . LEU C 111 ? 0.5919 0.6563 0.5711 -0.0067 -0.0147 0.0528  111  LEU C CD2 
6714  N  N   . VAL C 112 ? 0.3763 0.4434 0.3570 -0.0423 -0.0223 0.0799  112  VAL C N   
6715  C  CA  . VAL C 112 ? 0.4085 0.4860 0.3973 -0.0520 -0.0247 0.0832  112  VAL C CA  
6716  C  C   . VAL C 112 ? 0.4657 0.5819 0.4677 -0.0530 -0.0192 0.0821  112  VAL C C   
6717  O  O   . VAL C 112 ? 0.3862 0.5205 0.4018 -0.0523 -0.0191 0.0782  112  VAL C O   
6718  C  CB  . VAL C 112 ? 0.4166 0.4764 0.3947 -0.0656 -0.0293 0.0947  112  VAL C CB  
6719  C  CG1 . VAL C 112 ? 0.2124 0.2934 0.2011 -0.0784 -0.0309 0.0995  112  VAL C CG1 
6720  C  CG2 . VAL C 112 ? 0.4420 0.4634 0.4077 -0.0643 -0.0350 0.0936  112  VAL C CG2 
6721  N  N   . TYR C 113 ? 0.4274 0.5568 0.4245 -0.0533 -0.0146 0.0856  113  TYR C N   
6722  C  CA  . TYR C 113 ? 0.4736 0.6400 0.4801 -0.0520 -0.0079 0.0832  113  TYR C CA  
6723  C  C   . TYR C 113 ? 0.5622 0.7401 0.5781 -0.0382 -0.0044 0.0688  113  TYR C C   
6724  O  O   . TYR C 113 ? 0.5156 0.7205 0.5439 -0.0355 -0.0004 0.0645  113  TYR C O   
6725  C  CB  . TYR C 113 ? 0.4326 0.6071 0.4279 -0.0543 -0.0041 0.0894  113  TYR C CB  
6726  C  CG  . TYR C 113 ? 0.5756 0.7458 0.5627 -0.0691 -0.0059 0.1048  113  TYR C CG  
6727  C  CD1 . TYR C 113 ? 0.5756 0.7424 0.5482 -0.0716 -0.0047 0.1135  113  TYR C CD1 
6728  C  CD2 . TYR C 113 ? 0.6294 0.7981 0.6224 -0.0813 -0.0094 0.1113  113  TYR C CD2 
6729  C  CE1 . TYR C 113 ? 0.5518 0.7109 0.5150 -0.0857 -0.0065 0.1288  113  TYR C CE1 
6730  C  CE2 . TYR C 113 ? 0.6430 0.8049 0.6273 -0.0970 -0.0114 0.1258  113  TYR C CE2 
6731  C  CZ  . TYR C 113 ? 0.6240 0.7797 0.5930 -0.0991 -0.0097 0.1348  113  TYR C CZ  
6732  O  OH  . TYR C 113 ? 0.6177 0.7629 0.5766 -0.1153 -0.0119 0.1501  113  TYR C OH  
6733  N  N   . MET C 114 ? 0.4659 0.6232 0.4757 -0.0295 -0.0057 0.0617  114  MET C N   
6734  C  CA  . MET C 114 ? 0.4655 0.6279 0.4813 -0.0179 -0.0030 0.0484  114  MET C CA  
6735  C  C   . MET C 114 ? 0.4987 0.6611 0.5266 -0.0141 -0.0048 0.0437  114  MET C C   
6736  O  O   . MET C 114 ? 0.4979 0.6778 0.5351 -0.0065 -0.0012 0.0356  114  MET C O   
6737  C  CB  . MET C 114 ? 0.3536 0.4933 0.3609 -0.0123 -0.0048 0.0436  114  MET C CB  
6738  C  CG  . MET C 114 ? 0.3897 0.5310 0.4011 -0.0026 -0.0024 0.0301  114  MET C CG  
6739  S  SD  . MET C 114 ? 0.6417 0.8140 0.6548 0.0016  0.0045  0.0219  114  MET C SD  
6740  C  CE  . MET C 114 ? 0.6779 0.8536 0.6770 -0.0023 0.0046  0.0266  114  MET C CE  
6741  N  N   . ALA C 115 ? 0.2919 0.4337 0.3184 -0.0185 -0.0108 0.0485  115  ALA C N   
6742  C  CA  . ALA C 115 ? 0.3468 0.4880 0.3831 -0.0159 -0.0142 0.0459  115  ALA C CA  
6743  C  C   . ALA C 115 ? 0.4519 0.6274 0.5029 -0.0161 -0.0113 0.0464  115  ALA C C   
6744  O  O   . ALA C 115 ? 0.6187 0.8067 0.6792 -0.0055 -0.0087 0.0383  115  ALA C O   
6745  C  CB  . ALA C 115 ? 0.3609 0.4799 0.3913 -0.0242 -0.0213 0.0532  115  ALA C CB  
6746  N  N   . GLN C 116 ? 0.3749 0.5654 0.4277 -0.0282 -0.0117 0.0563  116  GLN C N   
6747  C  CA  . GLN C 116 ? 0.2044 0.4325 0.2725 -0.0303 -0.0084 0.0585  116  GLN C CA  
6748  C  C   . GLN C 116 ? 0.3396 0.5917 0.4122 -0.0189 0.0005  0.0498  116  GLN C C   
6749  O  O   . GLN C 116 ? 0.4770 0.7485 0.5628 -0.0088 0.0029  0.0432  116  GLN C O   
6750  C  CB  . GLN C 116 ? 0.1390 0.3779 0.2049 -0.0474 -0.0089 0.0714  116  GLN C CB  
6751  C  CG  . GLN C 116 ? 0.2276 0.4409 0.2873 -0.0600 -0.0182 0.0794  116  GLN C CG  
6752  C  CD  . GLN C 116 ? 0.3149 0.5302 0.3681 -0.0780 -0.0190 0.0923  116  GLN C CD  
6753  O  OE1 . GLN C 116 ? 0.3970 0.6373 0.4614 -0.0894 -0.0198 0.0991  116  GLN C OE1 
6754  N  NE2 . GLN C 116 ? 0.4995 0.6886 0.5347 -0.0807 -0.0190 0.0964  116  GLN C NE2 
6755  N  N   . TYR C 117 ? 0.3271 0.5773 0.3876 -0.0199 0.0049  0.0495  117  TYR C N   
6756  C  CA  . TYR C 117 ? 0.3078 0.5793 0.3682 -0.0105 0.0132  0.0407  117  TYR C CA  
6757  C  C   . TYR C 117 ? 0.3121 0.5775 0.3777 0.0055  0.0143  0.0264  117  TYR C C   
6758  O  O   . TYR C 117 ? 0.3135 0.6031 0.3881 0.0148  0.0200  0.0194  117  TYR C O   
6759  C  CB  . TYR C 117 ? 0.2800 0.5412 0.3234 -0.0130 0.0150  0.0414  117  TYR C CB  
6760  C  CG  . TYR C 117 ? 0.3304 0.6125 0.3700 -0.0049 0.0228  0.0319  117  TYR C CG  
6761  C  CD1 . TYR C 117 ? 0.2783 0.5932 0.3180 -0.0093 0.0298  0.0365  117  TYR C CD1 
6762  C  CD2 . TYR C 117 ? 0.3388 0.6071 0.3732 0.0060  0.0234  0.0183  117  TYR C CD2 
6763  C  CE1 . TYR C 117 ? 0.2822 0.6158 0.3160 -0.0016 0.0372  0.0270  117  TYR C CE1 
6764  C  CE2 . TYR C 117 ? 0.4064 0.6913 0.4348 0.0127  0.0299  0.0084  117  TYR C CE2 
6765  C  CZ  . TYR C 117 ? 0.3423 0.6599 0.3699 0.0096  0.0369  0.0123  117  TYR C CZ  
6766  O  OH  . TYR C 117 ? 0.3832 0.7172 0.4023 0.0167  0.0437  0.0015  117  TYR C OH  
6767  N  N   . LEU C 118 ? 0.3763 0.6087 0.4356 0.0088  0.0090  0.0224  118  LEU C N   
6768  C  CA  . LEU C 118 ? 0.5278 0.7492 0.5894 0.0224  0.0097  0.0098  118  LEU C CA  
6769  C  C   . LEU C 118 ? 0.5615 0.7963 0.6388 0.0300  0.0088  0.0087  118  LEU C C   
6770  O  O   . LEU C 118 ? 0.5209 0.7707 0.6047 0.0423  0.0138  -0.0004 118  LEU C O   
6771  C  CB  . LEU C 118 ? 0.4847 0.6694 0.5368 0.0224  0.0044  0.0078  118  LEU C CB  
6772  C  CG  . LEU C 118 ? 0.5400 0.7144 0.5790 0.0207  0.0060  0.0039  118  LEU C CG  
6773  C  CD1 . LEU C 118 ? 0.5764 0.7189 0.6086 0.0196  0.0011  0.0036  118  LEU C CD1 
6774  C  CD2 . LEU C 118 ? 0.5182 0.7033 0.5553 0.0294  0.0117  -0.0090 118  LEU C CD2 
6775  N  N   . LEU C 119 ? 0.5034 0.7330 0.5862 0.0231  0.0021  0.0177  119  LEU C N   
6776  C  CA  . LEU C 119 ? 0.4010 0.6437 0.4992 0.0293  -0.0009 0.0185  119  LEU C CA  
6777  C  C   . LEU C 119 ? 0.4275 0.7138 0.5405 0.0326  0.0054  0.0188  119  LEU C C   
6778  O  O   . LEU C 119 ? 0.5531 0.8531 0.6761 0.0476  0.0086  0.0111  119  LEU C O   
6779  C  CB  . LEU C 119 ? 0.4611 0.6922 0.5599 0.0180  -0.0100 0.0288  119  LEU C CB  
6780  C  CG  . LEU C 119 ? 0.4747 0.6657 0.5620 0.0197  -0.0161 0.0270  119  LEU C CG  
6781  C  CD1 . LEU C 119 ? 0.4238 0.6004 0.5061 0.0070  -0.0243 0.0365  119  LEU C CD1 
6782  C  CD2 . LEU C 119 ? 0.3860 0.5706 0.4793 0.0350  -0.0175 0.0199  119  LEU C CD2 
6783  N  N   . GLY C 120 ? 0.3913 0.6990 0.5053 0.0190  0.0076  0.0278  120  GLY C N   
6784  C  CA  . GLY C 120 ? 0.2066 0.5597 0.3351 0.0195  0.0144  0.0301  120  GLY C CA  
6785  C  C   . GLY C 120 ? 0.1922 0.5630 0.3196 0.0335  0.0249  0.0186  120  GLY C C   
6786  O  O   . GLY C 120 ? 0.4344 0.8445 0.5751 0.0386  0.0318  0.0180  120  GLY C O   
6787  N  N   . ASN C 121 ? 0.4246 0.7678 0.5359 0.0395  0.0264  0.0091  121  ASN C N   
6788  C  CA  . ASN C 121 ? 0.4914 0.8487 0.5973 0.0504  0.0360  -0.0024 121  ASN C CA  
6789  C  C   . ASN C 121 ? 0.5141 0.8471 0.6153 0.0676  0.0362  -0.0178 121  ASN C C   
6790  O  O   . ASN C 121 ? 0.4664 0.8128 0.5667 0.0806  0.0439  -0.0293 121  ASN C O   
6791  C  CB  . ASN C 121 ? 0.3877 0.7429 0.4762 0.0396  0.0392  0.0002  121  ASN C CB  
6792  C  CG  . ASN C 121 ? 0.3089 0.6965 0.4013 0.0256  0.0428  0.0136  121  ASN C CG  
6793  O  OD1 . ASN C 121 ? 0.3678 0.7914 0.4652 0.0291  0.0518  0.0119  121  ASN C OD1 
6794  N  ND2 . ASN C 121 ? 0.3452 0.7191 0.4344 0.0096  0.0360  0.0269  121  ASN C ND2 
6795  N  N   . HIS C 122 ? 0.3513 0.6474 0.4483 0.0675  0.0280  -0.0180 122  HIS C N   
6796  C  CA  . HIS C 122 ? 0.2539 0.5208 0.3438 0.0805  0.0274  -0.0310 122  HIS C CA  
6797  C  C   . HIS C 122 ? 0.4392 0.7195 0.5392 0.0999  0.0320  -0.0408 122  HIS C C   
6798  O  O   . HIS C 122 ? 0.3900 0.6531 0.4809 0.1113  0.0350  -0.0543 122  HIS C O   
6799  C  CB  . HIS C 122 ? 0.5073 0.7376 0.5939 0.0768  0.0182  -0.0270 122  HIS C CB  
6800  C  CG  . HIS C 122 ? 0.5835 0.8142 0.6837 0.0847  0.0133  -0.0235 122  HIS C CG  
6801  N  ND1 . HIS C 122 ? 0.7372 0.9840 0.8485 0.0764  0.0083  -0.0111 122  HIS C ND1 
6802  C  CD2 . HIS C 122 ? 0.5349 0.7508 0.6382 0.1000  0.0117  -0.0303 122  HIS C CD2 
6803  C  CE1 . HIS C 122 ? 0.7764 1.0213 0.8979 0.0864  0.0036  -0.0104 122  HIS C CE1 
6804  N  NE2 . HIS C 122 ? 0.7067 0.9324 0.8235 0.1015  0.0057  -0.0215 122  HIS C NE2 
6805  N  N   . GLU C 123 ? 0.5164 0.8272 0.6351 0.1040  0.0322  -0.0342 123  GLU C N   
6806  C  CA  . GLU C 123 ? 0.5245 0.8522 0.6544 0.1248  0.0371  -0.0430 123  GLU C CA  
6807  C  C   . GLU C 123 ? 0.5552 0.9184 0.6854 0.1311  0.0491  -0.0504 123  GLU C C   
6808  O  O   . GLU C 123 ? 0.4920 0.8596 0.6232 0.1506  0.0552  -0.0631 123  GLU C O   
6809  C  CB  . GLU C 123 ? 0.7332 1.0813 0.8846 0.1291  0.0318  -0.0336 123  GLU C CB  
6810  C  CG  . GLU C 123 ? 0.9722 1.2828 1.1215 0.1304  0.0208  -0.0304 123  GLU C CG  
6811  C  CD  . GLU C 123 ? 1.1320 1.4607 1.3011 0.1427  0.0160  -0.0256 123  GLU C CD  
6812  O  OE1 . GLU C 123 ? 1.1617 1.5369 1.3496 0.1451  0.0196  -0.0213 123  GLU C OE1 
6813  O  OE2 . GLU C 123 ? 1.2216 1.5195 1.3876 0.1498  0.0083  -0.0254 123  GLU C OE2 
6814  N  N   . ARG C 124 ? 0.5459 0.9324 0.6732 0.1152  0.0527  -0.0426 124  ARG C N   
6815  C  CA  . ARG C 124 ? 0.4904 0.9147 0.6170 0.1192  0.0647  -0.0475 124  ARG C CA  
6816  C  C   . ARG C 124 ? 0.4002 0.8066 0.5027 0.1195  0.0695  -0.0597 124  ARG C C   
6817  O  O   . ARG C 124 ? 0.2656 0.6886 0.3632 0.1322  0.0790  -0.0719 124  ARG C O   
6818  C  CB  . ARG C 124 ? 0.6376 1.1007 0.7735 0.1016  0.0669  -0.0316 124  ARG C CB  
6819  C  CG  . ARG C 124 ? 0.7524 1.2010 0.8925 0.0826  0.0558  -0.0156 124  ARG C CG  
6820  C  CD  . ARG C 124 ? 0.7988 1.2728 0.9380 0.0620  0.0583  -0.0014 124  ARG C CD  
6821  N  NE  . ARG C 124 ? 0.8530 1.3788 1.0038 0.0653  0.0694  -0.0005 124  ARG C NE  
6822  C  CZ  . ARG C 124 ? 0.8626 1.4274 1.0347 0.0587  0.0701  0.0107  124  ARG C CZ  
6823  N  NH1 . ARG C 124 ? 0.8002 1.3559 0.9829 0.0477  0.0592  0.0215  124  ARG C NH1 
6824  N  NH2 . ARG C 124 ? 0.8745 1.4890 1.0571 0.0624  0.0817  0.0109  124  ARG C NH2 
6825  N  N   . ILE C 125 ? 0.3694 0.7438 0.4570 0.1055  0.0627  -0.0564 125  ILE C N   
6826  C  CA  . ILE C 125 ? 0.3961 0.7542 0.4613 0.1033  0.0651  -0.0665 125  ILE C CA  
6827  C  C   . ILE C 125 ? 0.5687 0.8814 0.6235 0.1105  0.0596  -0.0790 125  ILE C C   
6828  O  O   . ILE C 125 ? 0.6823 0.9660 0.7373 0.1032  0.0508  -0.0729 125  ILE C O   
6829  C  CB  . ILE C 125 ? 0.4405 0.7971 0.4958 0.0830  0.0615  -0.0540 125  ILE C CB  
6830  C  CG1 . ILE C 125 ? 0.5361 0.9358 0.5940 0.0755  0.0692  -0.0447 125  ILE C CG1 
6831  C  CG2 . ILE C 125 ? 0.4176 0.7498 0.4515 0.0805  0.0600  -0.0637 125  ILE C CG2 
6832  C  CD1 . ILE C 125 ? 0.5190 0.9479 0.5989 0.0729  0.0699  -0.0324 125  ILE C CD1 
6833  N  N   . SER C 126 ? 0.7286 1.0348 0.7728 0.1241  0.0651  -0.0964 126  SER C N   
6834  C  CA  . SER C 126 ? 0.7401 1.0028 0.7739 0.1314  0.0606  -0.1095 126  SER C CA  
6835  C  C   . SER C 126 ? 0.7018 0.9314 0.7233 0.1158  0.0521  -0.1068 126  SER C C   
6836  O  O   . SER C 126 ? 0.6481 0.8454 0.6714 0.1155  0.0452  -0.1058 126  SER C O   
6837  C  CB  . SER C 126 ? 0.7743 1.0360 0.7941 0.1456  0.0683  -0.1296 126  SER C CB  
6838  O  OG  . SER C 126 ? 0.8197 1.0415 0.8343 0.1571  0.0649  -0.1417 126  SER C OG  
6839  N  N   . ASP C 127 ? 0.7491 0.9887 0.7585 0.1036  0.0528  -0.1053 127  ASP C N   
6840  C  CA  . ASP C 127 ? 0.7103 0.9263 0.7106 0.0891  0.0451  -0.1011 127  ASP C CA  
6841  C  C   . ASP C 127 ? 0.5328 0.7343 0.5454 0.0824  0.0379  -0.0867 127  ASP C C   
6842  O  O   . ASP C 127 ? 0.6492 0.8189 0.6595 0.0805  0.0320  -0.0886 127  ASP C O   
6843  C  CB  . ASP C 127 ? 0.8260 1.0639 0.8163 0.0771  0.0463  -0.0951 127  ASP C CB  
6844  C  CG  . ASP C 127 ? 0.9867 1.2269 0.9580 0.0793  0.0499  -0.1108 127  ASP C CG  
6845  O  OD1 . ASP C 127 ? 0.9452 1.1580 0.9078 0.0838  0.0477  -0.1255 127  ASP C OD1 
6846  O  OD2 . ASP C 127 ? 1.1201 1.3887 1.0837 0.0758  0.0545  -0.1083 127  ASP C OD2 
6847  N  N   . LEU C 128 ? 0.4032 0.6280 0.4276 0.0781  0.0384  -0.0724 128  LEU C N   
6848  C  CA  . LEU C 128 ? 0.3824 0.5947 0.4161 0.0707  0.0315  -0.0588 128  LEU C CA  
6849  C  C   . LEU C 128 ? 0.4944 0.6860 0.5365 0.0808  0.0283  -0.0619 128  LEU C C   
6850  O  O   . LEU C 128 ? 0.5000 0.6648 0.5415 0.0764  0.0218  -0.0576 128  LEU C O   
6851  C  CB  . LEU C 128 ? 0.3901 0.6315 0.4340 0.0636  0.0326  -0.0441 128  LEU C CB  
6852  C  CG  . LEU C 128 ? 0.3751 0.6375 0.4106 0.0530  0.0357  -0.0376 128  LEU C CG  
6853  C  CD1 . LEU C 128 ? 0.3228 0.6116 0.3693 0.0456  0.0368  -0.0231 128  LEU C CD1 
6854  C  CD2 . LEU C 128 ? 0.3803 0.6205 0.4044 0.0429  0.0299  -0.0333 128  LEU C CD2 
6855  N  N   . GLY C 129 ? 0.4747 0.6797 0.5243 0.0952  0.0330  -0.0689 129  GLY C N   
6856  C  CA  . GLY C 129 ? 0.6047 0.7910 0.6619 0.1070  0.0298  -0.0713 129  GLY C CA  
6857  C  C   . GLY C 129 ? 0.5992 0.7435 0.6435 0.1078  0.0261  -0.0804 129  GLY C C   
6858  O  O   . GLY C 129 ? 0.6405 0.7593 0.6872 0.1104  0.0206  -0.0775 129  GLY C O   
6859  N  N   . GLN C 130 ? 0.3322 0.4704 0.3621 0.1045  0.0289  -0.0910 130  GLN C N   
6860  C  CA  . GLN C 130 ? 0.5062 0.6068 0.5232 0.1021  0.0254  -0.1001 130  GLN C CA  
6861  C  C   . GLN C 130 ? 0.4406 0.5278 0.4544 0.0855  0.0194  -0.0904 130  GLN C C   
6862  O  O   . GLN C 130 ? 0.4284 0.4853 0.4395 0.0826  0.0147  -0.0900 130  GLN C O   
6863  C  CB  . GLN C 130 ? 0.6013 0.7017 0.6036 0.1049  0.0301  -0.1165 130  GLN C CB  
6864  C  CG  . GLN C 130 ? 0.6680 0.7286 0.6587 0.1091  0.0278  -0.1301 130  GLN C CG  
6865  C  CD  . GLN C 130 ? 0.6636 0.7006 0.6463 0.0927  0.0216  -0.1281 130  GLN C CD  
6866  O  OE1 . GLN C 130 ? 0.6543 0.7076 0.6370 0.0798  0.0200  -0.1202 130  GLN C OE1 
6867  N  NE2 . GLN C 130 ? 0.7746 0.7736 0.7507 0.0932  0.0182  -0.1347 130  GLN C NE2 
6868  N  N   . LEU C 131 ? 0.3766 0.4867 0.3907 0.0752  0.0198  -0.0821 131  LEU C N   
6869  C  CA  . LEU C 131 ? 0.4002 0.5012 0.4134 0.0621  0.0146  -0.0714 131  LEU C CA  
6870  C  C   . LEU C 131 ? 0.3405 0.4236 0.3616 0.0630  0.0101  -0.0625 131  LEU C C   
6871  O  O   . LEU C 131 ? 0.3183 0.3760 0.3355 0.0580  0.0062  -0.0614 131  LEU C O   
6872  C  CB  . LEU C 131 ? 0.3225 0.4508 0.3369 0.0541  0.0157  -0.0610 131  LEU C CB  
6873  C  CG  . LEU C 131 ? 0.4810 0.6013 0.4938 0.0426  0.0108  -0.0498 131  LEU C CG  
6874  C  CD1 . LEU C 131 ? 0.3331 0.4373 0.3367 0.0373  0.0084  -0.0563 131  LEU C CD1 
6875  C  CD2 . LEU C 131 ? 0.4321 0.5766 0.4446 0.0362  0.0119  -0.0394 131  LEU C CD2 
6876  N  N   . VAL C 132 ? 0.3784 0.4765 0.4104 0.0689  0.0105  -0.0562 132  VAL C N   
6877  C  CA  . VAL C 132 ? 0.2755 0.3623 0.3144 0.0688  0.0055  -0.0463 132  VAL C CA  
6878  C  C   . VAL C 132 ? 0.4379 0.4959 0.4752 0.0774  0.0032  -0.0517 132  VAL C C   
6879  O  O   . VAL C 132 ? 0.6114 0.6473 0.6465 0.0734  -0.0014 -0.0458 132  VAL C O   
6880  C  CB  . VAL C 132 ? 0.2484 0.3626 0.3001 0.0719  0.0059  -0.0386 132  VAL C CB  
6881  C  CG1 . VAL C 132 ? 0.4322 0.5343 0.4899 0.0730  -0.0004 -0.0302 132  VAL C CG1 
6882  C  CG2 . VAL C 132 ? 0.1583 0.2951 0.2101 0.0605  0.0071  -0.0303 132  VAL C CG2 
6883  N  N   . ASN C 133 ? 0.3879 0.4449 0.4250 0.0898  0.0066  -0.0628 133  ASN C N   
6884  C  CA  . ASN C 133 ? 0.4014 0.4267 0.4344 0.0987  0.0045  -0.0686 133  ASN C CA  
6885  C  C   . ASN C 133 ? 0.4294 0.4220 0.4505 0.0884  0.0018  -0.0704 133  ASN C C   
6886  O  O   . ASN C 133 ? 0.4148 0.3788 0.4327 0.0903  -0.0017 -0.0683 133  ASN C O   
6887  C  CB  . ASN C 133 ? 0.4458 0.4723 0.4766 0.1132  0.0096  -0.0829 133  ASN C CB  
6888  C  CG  . ASN C 133 ? 0.5194 0.5694 0.5638 0.1286  0.0115  -0.0811 133  ASN C CG  
6889  O  OD1 . ASN C 133 ? 0.6049 0.6762 0.6614 0.1259  0.0090  -0.0690 133  ASN C OD1 
6890  N  ND2 . ASN C 133 ? 0.6516 0.6983 0.6943 0.1450  0.0158  -0.0934 133  ASN C ND2 
6891  N  N   . SER C 134 ? 0.4590 0.4579 0.4737 0.0773  0.0033  -0.0736 134  SER C N   
6892  C  CA  . SER C 134 ? 0.4937 0.4675 0.4982 0.0676  0.0016  -0.0780 134  SER C CA  
6893  C  C   . SER C 134 ? 0.5159 0.4910 0.5209 0.0541  -0.0011 -0.0672 134  SER C C   
6894  O  O   . SER C 134 ? 0.5479 0.5058 0.5471 0.0450  -0.0025 -0.0685 134  SER C O   
6895  C  CB  . SER C 134 ? 0.4907 0.4708 0.4868 0.0652  0.0046  -0.0913 134  SER C CB  
6896  O  OG  . SER C 134 ? 0.3668 0.3787 0.3652 0.0598  0.0064  -0.0874 134  SER C OG  
6897  N  N   . THR C 135 ? 0.4819 0.4776 0.4938 0.0526  -0.0015 -0.0566 135  THR C N   
6898  C  CA  . THR C 135 ? 0.4706 0.4679 0.4818 0.0419  -0.0034 -0.0472 135  THR C CA  
6899  C  C   . THR C 135 ? 0.3750 0.3725 0.3910 0.0424  -0.0061 -0.0352 135  THR C C   
6900  O  O   . THR C 135 ? 0.5317 0.5449 0.5542 0.0475  -0.0063 -0.0318 135  THR C O   
6901  C  CB  . THR C 135 ? 0.5472 0.5692 0.5578 0.0364  -0.0017 -0.0466 135  THR C CB  
6902  O  OG1 . THR C 135 ? 0.5205 0.5505 0.5271 0.0392  0.0011  -0.0585 135  THR C OG1 
6903  C  CG2 . THR C 135 ? 0.4678 0.4858 0.4751 0.0264  -0.0034 -0.0419 135  THR C CG2 
6904  N  N   . ASP C 136 ? 0.3906 0.3719 0.4030 0.0365  -0.0082 -0.0290 136  ASP C N   
6905  C  CA  . ASP C 136 ? 0.5055 0.4859 0.5190 0.0354  -0.0110 -0.0183 136  ASP C CA  
6906  C  C   . ASP C 136 ? 0.4290 0.4242 0.4418 0.0286  -0.0106 -0.0127 136  ASP C C   
6907  O  O   . ASP C 136 ? 0.4603 0.4531 0.4693 0.0231  -0.0094 -0.0126 136  ASP C O   
6908  C  CB  . ASP C 136 ? 0.7374 0.6927 0.7449 0.0331  -0.0127 -0.0145 136  ASP C CB  
6909  C  CG  . ASP C 136 ? 0.9281 0.8740 0.9361 0.0390  -0.0165 -0.0091 136  ASP C CG  
6910  O  OD1 . ASP C 136 ? 0.8700 0.8170 0.8826 0.0478  -0.0174 -0.0128 136  ASP C OD1 
6911  O  OD2 . ASP C 136 ? 1.0567 0.9946 1.0599 0.0355  -0.0188 -0.0014 136  ASP C OD2 
6912  N  N   . ILE C 137 ? 0.2634 0.2745 0.2802 0.0291  -0.0116 -0.0075 137  ILE C N   
6913  C  CA  . ILE C 137 ? 0.2850 0.3085 0.2999 0.0232  -0.0112 -0.0023 137  ILE C CA  
6914  C  C   . ILE C 137 ? 0.3165 0.3344 0.3288 0.0197  -0.0146 0.0073  137  ILE C C   
6915  O  O   . ILE C 137 ? 0.4542 0.4749 0.4704 0.0209  -0.0174 0.0105  137  ILE C O   
6916  C  CB  . ILE C 137 ? 0.3886 0.4368 0.4078 0.0240  -0.0088 -0.0042 137  ILE C CB  
6917  C  CG1 . ILE C 137 ? 0.3390 0.3918 0.3583 0.0281  -0.0055 -0.0154 137  ILE C CG1 
6918  C  CG2 . ILE C 137 ? 0.3099 0.3681 0.3251 0.0177  -0.0087 0.0028  137  ILE C CG2 
6919  C  CD1 . ILE C 137 ? 0.1882 0.2658 0.2116 0.0316  -0.0022 -0.0187 137  ILE C CD1 
6920  N  N   . TYR C 138 ? 0.4158 0.4259 0.4214 0.0156  -0.0146 0.0115  138  TYR C N   
6921  C  CA  . TYR C 138 ? 0.3689 0.3699 0.3688 0.0124  -0.0177 0.0194  138  TYR C CA  
6922  C  C   . TYR C 138 ? 0.4418 0.4511 0.4385 0.0085  -0.0173 0.0245  138  TYR C C   
6923  O  O   . TYR C 138 ? 0.4006 0.4147 0.3959 0.0090  -0.0149 0.0233  138  TYR C O   
6924  C  CB  . TYR C 138 ? 0.3030 0.2835 0.2952 0.0128  -0.0176 0.0204  138  TYR C CB  
6925  C  CG  . TYR C 138 ? 0.3885 0.3571 0.3809 0.0156  -0.0186 0.0178  138  TYR C CG  
6926  C  CD1 . TYR C 138 ? 0.4359 0.4045 0.4327 0.0182  -0.0163 0.0114  138  TYR C CD1 
6927  C  CD2 . TYR C 138 ? 0.2551 0.2105 0.2417 0.0154  -0.0224 0.0220  138  TYR C CD2 
6928  C  CE1 . TYR C 138 ? 0.4263 0.3806 0.4217 0.0211  -0.0175 0.0103  138  TYR C CE1 
6929  C  CE2 . TYR C 138 ? 0.3178 0.2618 0.3031 0.0184  -0.0238 0.0210  138  TYR C CE2 
6930  C  CZ  . TYR C 138 ? 0.4193 0.3620 0.4092 0.0216  -0.0213 0.0157  138  TYR C CZ  
6931  O  OH  . TYR C 138 ? 0.5590 0.4870 0.5462 0.0249  -0.0230 0.0159  138  TYR C OH  
6932  N  N   . LEU C 139 ? 0.4413 0.4520 0.4366 0.0042  -0.0203 0.0306  139  LEU C N   
6933  C  CA  . LEU C 139 ? 0.4861 0.5007 0.4766 -0.0003 -0.0205 0.0370  139  LEU C CA  
6934  C  C   . LEU C 139 ? 0.4005 0.3941 0.3803 -0.0039 -0.0242 0.0433  139  LEU C C   
6935  O  O   . LEU C 139 ? 0.3629 0.3509 0.3418 -0.0080 -0.0282 0.0455  139  LEU C O   
6936  C  CB  . LEU C 139 ? 0.3898 0.4263 0.3869 -0.0045 -0.0202 0.0396  139  LEU C CB  
6937  C  CG  . LEU C 139 ? 0.4287 0.4871 0.4352 -0.0002 -0.0163 0.0325  139  LEU C CG  
6938  C  CD1 . LEU C 139 ? 0.3181 0.4010 0.3311 -0.0044 -0.0150 0.0360  139  LEU C CD1 
6939  C  CD2 . LEU C 139 ? 0.1937 0.2549 0.1970 0.0031  -0.0130 0.0278  139  LEU C CD2 
6940  N  N   . VAL C 140 ? 0.4961 0.4784 0.4673 -0.0019 -0.0231 0.0459  140  VAL C N   
6941  C  CA  . VAL C 140 ? 0.5305 0.4893 0.4887 -0.0034 -0.0259 0.0508  140  VAL C CA  
6942  C  C   . VAL C 140 ? 0.5134 0.4710 0.4653 -0.0066 -0.0267 0.0582  140  VAL C C   
6943  O  O   . VAL C 140 ? 0.5102 0.4647 0.4578 -0.0010 -0.0248 0.0599  140  VAL C O   
6944  C  CB  . VAL C 140 ? 0.5455 0.4892 0.4973 0.0040  -0.0235 0.0480  140  VAL C CB  
6945  C  CG1 . VAL C 140 ? 0.3201 0.2369 0.2563 0.0042  -0.0258 0.0514  140  VAL C CG1 
6946  C  CG2 . VAL C 140 ? 0.4459 0.3905 0.4030 0.0066  -0.0220 0.0417  140  VAL C CG2 
6947  N  N   . PRO C 141 ? 0.5311 0.4927 0.4831 -0.0156 -0.0297 0.0635  141  PRO C N   
6948  C  CA  . PRO C 141 ? 0.6078 0.5683 0.5533 -0.0208 -0.0306 0.0721  141  PRO C CA  
6949  C  C   . PRO C 141 ? 0.5747 0.5052 0.5040 -0.0175 -0.0323 0.0765  141  PRO C C   
6950  O  O   . PRO C 141 ? 0.6423 0.5723 0.5665 -0.0153 -0.0315 0.0824  141  PRO C O   
6951  C  CB  . PRO C 141 ? 0.4700 0.4360 0.4183 -0.0332 -0.0342 0.0764  141  PRO C CB  
6952  C  CG  . PRO C 141 ? 0.4945 0.4802 0.4570 -0.0316 -0.0333 0.0695  141  PRO C CG  
6953  C  CD  . PRO C 141 ? 0.5902 0.5625 0.5507 -0.0218 -0.0322 0.0620  141  PRO C CD  
6954  N  N   . THR C 142 ? 0.4387 0.3445 0.3589 -0.0163 -0.0347 0.0738  142  THR C N   
6955  C  CA  . THR C 142 ? 0.6123 0.4889 0.5165 -0.0097 -0.0351 0.0758  142  THR C CA  
6956  C  C   . THR C 142 ? 0.5345 0.3987 0.4347 -0.0001 -0.0328 0.0685  142  THR C C   
6957  O  O   . THR C 142 ? 0.4686 0.3333 0.3714 -0.0024 -0.0336 0.0633  142  THR C O   
6958  C  CB  . THR C 142 ? 0.5314 0.3790 0.4196 -0.0187 -0.0406 0.0815  142  THR C CB  
6959  O  OG1 . THR C 142 ? 0.5721 0.3907 0.4442 -0.0092 -0.0402 0.0829  142  THR C OG1 
6960  C  CG2 . THR C 142 ? 0.4469 0.2841 0.3320 -0.0261 -0.0448 0.0770  142  THR C CG2 
6961  N  N   . MET C 143 ? 0.6907 0.5448 0.5842 0.0110  -0.0299 0.0691  143  MET C N   
6962  C  CA  . MET C 143 ? 0.5916 0.4368 0.4811 0.0209  -0.0261 0.0626  143  MET C CA  
6963  C  C   . MET C 143 ? 0.5889 0.4012 0.4587 0.0269  -0.0271 0.0641  143  MET C C   
6964  O  O   . MET C 143 ? 0.4767 0.2767 0.3386 0.0368  -0.0236 0.0599  143  MET C O   
6965  C  CB  . MET C 143 ? 0.5029 0.3719 0.4051 0.0303  -0.0209 0.0617  143  MET C CB  
6966  C  CG  . MET C 143 ? 0.4760 0.3436 0.3779 0.0392  -0.0159 0.0561  143  MET C CG  
6967  S  SD  . MET C 143 ? 0.7091 0.6069 0.6265 0.0483  -0.0108 0.0559  143  MET C SD  
6968  C  CE  . MET C 143 ? 0.3350 0.2207 0.2444 0.0615  -0.0049 0.0532  143  MET C CE  
6969  N  N   . ASN C 144 ? 0.4365 0.2330 0.2970 0.0210  -0.0316 0.0707  144  ASN C N   
6970  C  CA  . ASN C 144 ? 0.5547 0.3141 0.3939 0.0262  -0.0334 0.0723  144  ASN C CA  
6971  C  C   . ASN C 144 ? 0.6959 0.4310 0.5221 0.0119  -0.0406 0.0778  144  ASN C C   
6972  O  O   . ASN C 144 ? 0.7735 0.4960 0.5925 0.0112  -0.0427 0.0860  144  ASN C O   
6973  C  CB  . ASN C 144 ? 0.6104 0.3701 0.4487 0.0407  -0.0302 0.0773  144  ASN C CB  
6974  C  CG  . ASN C 144 ? 0.7477 0.4662 0.5630 0.0492  -0.0316 0.0788  144  ASN C CG  
6975  O  OD1 . ASN C 144 ? 0.7294 0.4188 0.5285 0.0460  -0.0337 0.0737  144  ASN C OD1 
6976  N  ND2 . ASN C 144 ? 0.8296 0.5433 0.6417 0.0607  -0.0310 0.0859  144  ASN C ND2 
6977  N  N   . PRO C 145 ? 0.5591 0.2870 0.3819 -0.0001 -0.0449 0.0743  145  PRO C N   
6978  C  CA  . PRO C 145 ? 0.4350 0.1442 0.2482 -0.0174 -0.0525 0.0796  145  PRO C CA  
6979  C  C   . PRO C 145 ? 0.5700 0.2321 0.3570 -0.0158 -0.0558 0.0817  145  PRO C C   
6980  O  O   . PRO C 145 ? 0.6369 0.2829 0.4158 -0.0287 -0.0611 0.0891  145  PRO C O   
6981  C  CB  . PRO C 145 ? 0.4393 0.1505 0.2530 -0.0253 -0.0559 0.0724  145  PRO C CB  
6982  C  CG  . PRO C 145 ? 0.5498 0.2834 0.3756 -0.0133 -0.0496 0.0659  145  PRO C CG  
6983  C  CD  . PRO C 145 ? 0.5327 0.2661 0.3577 0.0031  -0.0429 0.0652  145  PRO C CD  
6984  N  N   . ASP C 146 ? 0.5955 0.2368 0.3695 -0.0001 -0.0522 0.0747  146  ASP C N   
6985  C  CA  . ASP C 146 ? 0.7052 0.2978 0.4519 0.0055  -0.0544 0.0745  146  ASP C CA  
6986  C  C   . ASP C 146 ? 0.6964 0.2830 0.4413 0.0148  -0.0527 0.0834  146  ASP C C   
6987  O  O   . ASP C 146 ? 0.7529 0.3028 0.4791 0.0100  -0.0576 0.0893  146  ASP C O   
6988  C  CB  . ASP C 146 ? 0.8496 0.4257 0.5836 0.0217  -0.0496 0.0640  146  ASP C CB  
6989  C  CG  . ASP C 146 ? 0.7822 0.3544 0.5098 0.0116  -0.0530 0.0553  146  ASP C CG  
6990  O  OD1 . ASP C 146 ? 0.5895 0.1745 0.3251 -0.0070 -0.0593 0.0575  146  ASP C OD1 
6991  O  OD2 . ASP C 146 ? 0.7972 0.3548 0.5113 0.0226  -0.0493 0.0465  146  ASP C OD2 
6992  N  N   . GLY C 147 ? 0.6362 0.2581 0.4000 0.0275  -0.0464 0.0848  147  GLY C N   
6993  C  CA  . GLY C 147 ? 0.5309 0.1555 0.2965 0.0360  -0.0455 0.0945  147  GLY C CA  
6994  C  C   . GLY C 147 ? 0.6355 0.2664 0.4046 0.0177  -0.0506 0.1053  147  GLY C C   
6995  O  O   . GLY C 147 ? 0.7773 0.3844 0.5335 0.0174  -0.0537 0.1151  147  GLY C O   
6996  N  N   . TYR C 148 ? 0.6723 0.3349 0.4584 0.0028  -0.0513 0.1042  148  TYR C N   
6997  C  CA  . TYR C 148 ? 0.8230 0.4962 0.6138 -0.0158 -0.0551 0.1146  148  TYR C CA  
6998  C  C   . TYR C 148 ? 0.8698 0.4995 0.6386 -0.0304 -0.0622 0.1202  148  TYR C C   
6999  O  O   . TYR C 148 ? 0.8112 0.4237 0.5696 -0.0339 -0.0644 0.1315  148  TYR C O   
7000  C  CB  . TYR C 148 ? 0.7202 0.4335 0.5325 -0.0276 -0.0544 0.1106  148  TYR C CB  
7001  C  CG  . TYR C 148 ? 0.6612 0.3913 0.4801 -0.0469 -0.0572 0.1198  148  TYR C CG  
7002  C  CD1 . TYR C 148 ? 0.6909 0.4397 0.5149 -0.0468 -0.0549 0.1298  148  TYR C CD1 
7003  C  CD2 . TYR C 148 ? 0.4978 0.2278 0.3181 -0.0652 -0.0620 0.1189  148  TYR C CD2 
7004  C  CE1 . TYR C 148 ? 0.6225 0.3887 0.4519 -0.0646 -0.0563 0.1386  148  TYR C CE1 
7005  C  CE2 . TYR C 148 ? 0.5003 0.2495 0.3283 -0.0831 -0.0638 0.1278  148  TYR C CE2 
7006  C  CZ  . TYR C 148 ? 0.7501 0.5173 0.5823 -0.0828 -0.0604 0.1376  148  TYR C CZ  
7007  O  OH  . TYR C 148 ? 0.9121 0.7008 0.7516 -0.1009 -0.0610 0.1468  148  TYR C OH  
7008  N  N   . ALA C 149 ? 0.7802 0.3918 0.5409 -0.0394 -0.0661 0.1124  149  ALA C N   
7009  C  CA  . ALA C 149 ? 0.5634 0.1324 0.3022 -0.0551 -0.0738 0.1152  149  ALA C CA  
7010  C  C   . ALA C 149 ? 0.7255 0.2474 0.4399 -0.0467 -0.0752 0.1218  149  ALA C C   
7011  O  O   . ALA C 149 ? 0.6929 0.1844 0.3918 -0.0622 -0.0812 0.1299  149  ALA C O   
7012  C  CB  . ALA C 149 ? 0.5410 0.0913 0.2695 -0.0577 -0.0771 0.1028  149  ALA C CB  
7013  N  N   . LEU C 150 ? 0.8809 0.3966 0.5919 -0.0219 -0.0698 0.1190  150  LEU C N   
7014  C  CA  . LEU C 150 ? 0.9509 0.4216 0.6387 -0.0097 -0.0709 0.1242  150  LEU C CA  
7015  C  C   . LEU C 150 ? 1.0607 0.5455 0.7545 -0.0063 -0.0699 0.1389  150  LEU C C   
7016  O  O   . LEU C 150 ? 1.1586 0.6055 0.8330 0.0015  -0.0721 0.1467  150  LEU C O   
7017  C  CB  . LEU C 150 ? 0.9604 0.4164 0.6399 0.0168  -0.0656 0.1134  150  LEU C CB  
7018  C  CG  . LEU C 150 ? 0.9075 0.3345 0.5708 0.0150  -0.0672 0.0999  150  LEU C CG  
7019  C  CD1 . LEU C 150 ? 0.8787 0.3200 0.5471 0.0382  -0.0590 0.0886  150  LEU C CD1 
7020  C  CD2 . LEU C 150 ? 0.8589 0.2203 0.4882 0.0116  -0.0734 0.1002  150  LEU C CD2 
7021  N  N   . SER C 151 ? 1.0696 0.6071 0.7887 -0.0118 -0.0669 0.1427  151  SER C N   
7022  C  CA  . SER C 151 ? 0.8548 0.4109 0.5796 -0.0095 -0.0659 0.1564  151  SER C CA  
7023  C  C   . SER C 151 ? 0.8942 0.4412 0.6120 -0.0340 -0.0708 0.1705  151  SER C C   
7024  O  O   . SER C 151 ? 0.8999 0.4412 0.6167 -0.0550 -0.0744 0.1684  151  SER C O   
7025  C  CB  . SER C 151 ? 0.6237 0.2393 0.3764 -0.0031 -0.0601 0.1532  151  SER C CB  
7026  O  OG  . SER C 151 ? 0.6143 0.2397 0.3741 0.0176  -0.0554 0.1418  151  SER C OG  
7027  N  N   . GLN C 152 ? 0.8558 0.4051 0.5698 -0.0318 -0.0709 0.1849  152  GLN C N   
7028  C  CA  . GLN C 152 ? 0.9411 0.4791 0.6457 -0.0547 -0.0749 0.1996  152  GLN C CA  
7029  C  C   . GLN C 152 ? 0.9687 0.5597 0.6919 -0.0627 -0.0712 0.2082  152  GLN C C   
7030  O  O   . GLN C 152 ? 1.0675 0.6749 0.7927 -0.0484 -0.0689 0.2150  152  GLN C O   
7031  C  CB  . GLN C 152 ? 1.1482 0.6311 0.8245 -0.0486 -0.0793 0.2121  152  GLN C CB  
7032  C  CG  . GLN C 152 ? 1.2558 0.7250 0.9204 -0.0726 -0.0832 0.2298  152  GLN C CG  
7033  C  CD  . GLN C 152 ? 1.4018 0.8123 1.0365 -0.0649 -0.0879 0.2431  152  GLN C CD  
7034  O  OE1 . GLN C 152 ? 1.5146 0.9132 1.1380 -0.0803 -0.0905 0.2605  152  GLN C OE1 
7035  N  NE2 . GLN C 152 ? 1.3166 0.6904 0.9380 -0.0406 -0.0886 0.2351  152  GLN C NE2 
7036  N  N   . GLU C 153 ? 0.8064 0.4257 0.5428 -0.0848 -0.0707 0.2077  153  GLU C N   
7037  C  CA  . GLU C 153 ? 0.8063 0.4749 0.5584 -0.0929 -0.0665 0.2153  153  GLU C CA  
7038  C  C   . GLU C 153 ? 0.9920 0.6453 0.7272 -0.0923 -0.0677 0.2338  153  GLU C C   
7039  O  O   . GLU C 153 ? 0.9762 0.5841 0.6896 -0.1027 -0.0727 0.2449  153  GLU C O   
7040  C  CB  . GLU C 153 ? 0.6890 0.3819 0.4531 -0.1190 -0.0665 0.2158  153  GLU C CB  
7041  C  CG  . GLU C 153 ? 0.8383 0.5852 0.6186 -0.1255 -0.0606 0.2222  153  GLU C CG  
7042  C  CD  . GLU C 153 ? 0.9057 0.6823 0.7006 -0.1489 -0.0596 0.2227  153  GLU C CD  
7043  O  OE1 . GLU C 153 ? 0.9303 0.7398 0.7311 -0.1600 -0.0554 0.2328  153  GLU C OE1 
7044  O  OE2 . GLU C 153 ? 0.9389 0.7077 0.7392 -0.1558 -0.0630 0.2131  153  GLU C OE2 
7045  N  N   . GLY C 154 ? 0.9314 0.6207 0.6752 -0.0804 -0.0636 0.2373  154  GLY C N   
7046  C  CA  . GLY C 154 ? 0.8617 0.5429 0.5902 -0.0793 -0.0648 0.2555  154  GLY C CA  
7047  C  C   . GLY C 154 ? 0.8996 0.5714 0.6221 -0.0516 -0.0659 0.2558  154  GLY C C   
7048  O  O   . GLY C 154 ? 0.9939 0.6786 0.7109 -0.0452 -0.0660 0.2679  154  GLY C O   
7049  N  N   . ASN C 155 ? 0.8332 0.4853 0.5569 -0.0347 -0.0667 0.2428  155  ASN C N   
7050  C  CA  . ASN C 155 ? 0.7973 0.4403 0.5163 -0.0076 -0.0677 0.2432  155  ASN C CA  
7051  C  C   . ASN C 155 ? 0.8604 0.5589 0.6004 0.0051  -0.0637 0.2371  155  ASN C C   
7052  O  O   . ASN C 155 ? 0.9883 0.7127 0.7469 0.0099  -0.0601 0.2212  155  ASN C O   
7053  C  CB  . ASN C 155 ? 0.7785 0.3835 0.4912 0.0066  -0.0688 0.2313  155  ASN C CB  
7054  C  CG  . ASN C 155 ? 0.9186 0.4593 0.6026 0.0076  -0.0742 0.2409  155  ASN C CG  
7055  O  OD1 . ASN C 155 ? 1.0370 0.5387 0.7103 0.0064  -0.0759 0.2322  155  ASN C OD1 
7056  N  ND2 . ASN C 155 ? 1.0621 0.5893 0.7315 0.0097  -0.0774 0.2590  155  ASN C ND2 
7057  N  N   . CYS C 156 ? 0.9162 0.6316 0.6516 0.0096  -0.0649 0.2502  156  CYS C N   
7058  C  CA  . CYS C 156 ? 0.9584 0.7235 0.7105 0.0217  -0.0627 0.2453  156  CYS C CA  
7059  C  C   . CYS C 156 ? 0.8938 0.6528 0.6507 0.0473  -0.0636 0.2374  156  CYS C C   
7060  O  O   . CYS C 156 ? 0.8635 0.6599 0.6396 0.0559  -0.0608 0.2255  156  CYS C O   
7061  C  CB  . CYS C 156 ? 0.9779 0.7595 0.7201 0.0203  -0.0649 0.2623  156  CYS C CB  
7062  S  SG  . CYS C 156 ? 1.0087 0.8240 0.7536 -0.0079 -0.0606 0.2676  156  CYS C SG  
7063  N  N   . GLU C 157 ? 0.9299 0.6409 0.6688 0.0591  -0.0673 0.2442  157  GLU C N   
7064  C  CA  . GLU C 157 ? 0.9256 0.6264 0.6679 0.0841  -0.0672 0.2364  157  GLU C CA  
7065  C  C   . GLU C 157 ? 0.9137 0.5780 0.6516 0.0827  -0.0653 0.2241  157  GLU C C   
7066  O  O   . GLU C 157 ? 0.9585 0.5872 0.6820 0.0661  -0.0669 0.2266  157  GLU C O   
7067  C  CB  . GLU C 157 ? 1.0789 0.7543 0.8045 0.1044  -0.0724 0.2515  157  GLU C CB  
7068  C  CG  . GLU C 157 ? 1.2062 0.9224 0.9375 0.1119  -0.0752 0.2620  157  GLU C CG  
7069  C  CD  . GLU C 157 ? 1.4176 1.1219 1.1300 0.0977  -0.0791 0.2814  157  GLU C CD  
7070  O  OE1 . GLU C 157 ? 1.5477 1.2144 1.2392 0.1085  -0.0843 0.2970  157  GLU C OE1 
7071  O  OE2 . GLU C 157 ? 1.3470 1.0790 1.0648 0.0762  -0.0765 0.2813  157  GLU C OE2 
7072  N  N   . SER C 158 ? 0.8878 0.5626 0.6380 0.0993  -0.0618 0.2108  158  SER C N   
7073  C  CA  . SER C 158 ? 0.7229 0.3667 0.4682 0.1003  -0.0595 0.1979  158  SER C CA  
7074  C  C   . SER C 158 ? 0.8736 0.4541 0.5906 0.1068  -0.0634 0.2050  158  SER C C   
7075  O  O   . SER C 158 ? 0.9294 0.4917 0.6329 0.1161  -0.0676 0.2197  158  SER C O   
7076  C  CB  . SER C 158 ? 0.6204 0.2888 0.3824 0.1196  -0.0546 0.1852  158  SER C CB  
7077  O  OG  . SER C 158 ? 0.9973 0.6390 0.7538 0.1193  -0.0517 0.1723  158  SER C OG  
7078  N  N   . LEU C 159 ? 1.1666 0.7113 0.8729 0.1020  -0.0627 0.1947  159  LEU C N   
7079  C  CA  . LEU C 159 ? 1.1864 0.6657 0.8631 0.1070  -0.0666 0.1992  159  LEU C CA  
7080  C  C   . LEU C 159 ? 1.3053 0.7671 0.9757 0.1400  -0.0649 0.1974  159  LEU C C   
7081  O  O   . LEU C 159 ? 1.1933 0.6966 0.8842 0.1571  -0.0604 0.1920  159  LEU C O   
7082  C  CB  . LEU C 159 ? 1.1198 0.5673 0.7858 0.0903  -0.0671 0.1875  159  LEU C CB  
7083  C  CG  . LEU C 159 ? 0.9440 0.4004 0.6132 0.0574  -0.0698 0.1901  159  LEU C CG  
7084  C  CD1 . LEU C 159 ? 0.8108 0.2588 0.4803 0.0454  -0.0691 0.1744  159  LEU C CD1 
7085  C  CD2 . LEU C 159 ? 0.7796 0.1930 0.4252 0.0434  -0.0763 0.2065  159  LEU C CD2 
7086  N  N   . PRO C 160 ? 1.4288 0.8285 1.0706 0.1491  -0.0686 0.2023  160  PRO C N   
7087  C  CA  . PRO C 160 ? 1.3759 0.7518 1.0089 0.1821  -0.0663 0.1987  160  PRO C CA  
7088  C  C   . PRO C 160 ? 1.2466 0.6350 0.8894 0.1895  -0.0592 0.1790  160  PRO C C   
7089  O  O   . PRO C 160 ? 1.3036 0.6883 0.9455 0.1682  -0.0586 0.1689  160  PRO C O   
7090  C  CB  . PRO C 160 ? 1.5351 0.8334 1.1317 0.1816  -0.0718 0.2045  160  PRO C CB  
7091  C  CG  . PRO C 160 ? 1.5081 0.8003 1.0981 0.1536  -0.0780 0.2195  160  PRO C CG  
7092  C  CD  . PRO C 160 ? 1.4421 0.7907 1.0581 0.1293  -0.0752 0.2131  160  PRO C CD  
7093  N  N   . ASN C 161 ? 1.3224 0.7283 0.9746 0.2189  -0.0539 0.1740  161  ASN C N   
7094  C  CA  . ASN C 161 ? 1.4424 0.8669 1.1053 0.2270  -0.0459 0.1562  161  ASN C CA  
7095  C  C   . ASN C 161 ? 1.1759 0.6597 0.8674 0.2078  -0.0429 0.1502  161  ASN C C   
7096  O  O   . ASN C 161 ? 1.3271 0.8284 1.0281 0.2080  -0.0368 0.1364  161  ASN C O   
7097  C  CB  . ASN C 161 ? 1.6573 1.0244 1.2930 0.2212  -0.0457 0.1445  161  ASN C CB  
7098  C  CG  . ASN C 161 ? 1.6903 0.9896 1.2933 0.2382  -0.0492 0.1492  161  ASN C CG  
7099  O  OD1 . ASN C 161 ? 1.7002 0.9436 1.2761 0.2229  -0.0545 0.1483  161  ASN C OD1 
7100  N  ND2 . ASN C 161 ? 1.6335 0.9369 1.2389 0.2701  -0.0469 0.1543  161  ASN C ND2 
7101  N  N   . TYR C 162 ? 0.9923 0.5050 0.6959 0.1913  -0.0472 0.1609  162  TYR C N   
7102  C  CA  . TYR C 162 ? 1.0383 0.6025 0.7664 0.1720  -0.0451 0.1558  162  TYR C CA  
7103  C  C   . TYR C 162 ? 1.0446 0.5927 0.7672 0.1523  -0.0440 0.1440  162  TYR C C   
7104  O  O   . TYR C 162 ? 1.0449 0.6287 0.7860 0.1441  -0.0399 0.1343  162  TYR C O   
7105  C  CB  . TYR C 162 ? 0.9687 0.5874 0.7236 0.1874  -0.0392 0.1500  162  TYR C CB  
7106  C  CG  . TYR C 162 ? 0.9048 0.5564 0.6718 0.1988  -0.0420 0.1623  162  TYR C CG  
7107  C  CD1 . TYR C 162 ? 0.9234 0.5779 0.6919 0.2273  -0.0408 0.1658  162  TYR C CD1 
7108  C  CD2 . TYR C 162 ? 0.8530 0.5345 0.6298 0.1816  -0.0459 0.1702  162  TYR C CD2 
7109  C  CE1 . TYR C 162 ? 0.9768 0.6639 0.7565 0.2376  -0.0447 0.1775  162  TYR C CE1 
7110  C  CE2 . TYR C 162 ? 0.7703 0.4825 0.5562 0.1912  -0.0492 0.1810  162  TYR C CE2 
7111  C  CZ  . TYR C 162 ? 0.9246 0.6398 0.7121 0.2188  -0.0492 0.1850  162  TYR C CZ  
7112  O  OH  . TYR C 162 ? 0.8000 0.5482 0.5967 0.2283  -0.0537 0.1965  162  TYR C OH  
7113  N  N   . VAL C 163 ? 1.0198 0.5129 0.7158 0.1442  -0.0482 0.1449  163  VAL C N   
7114  C  CA  . VAL C 163 ? 1.1925 0.6671 0.8803 0.1239  -0.0492 0.1347  163  VAL C CA  
7115  C  C   . VAL C 163 ? 1.0719 0.5854 0.7784 0.0971  -0.0510 0.1364  163  VAL C C   
7116  O  O   . VAL C 163 ? 1.0029 0.5318 0.7150 0.0880  -0.0540 0.1486  163  VAL C O   
7117  C  CB  . VAL C 163 ? 0.8892 0.2943 0.5429 0.1188  -0.0550 0.1365  163  VAL C CB  
7118  C  CG1 . VAL C 163 ? 0.8298 0.2221 0.4772 0.0891  -0.0595 0.1317  163  VAL C CG1 
7119  C  CG2 . VAL C 163 ? 0.8029 0.1695 0.4378 0.1449  -0.0514 0.1275  163  VAL C CG2 
7120  N  N   . GLY C 164 ? 0.7735 0.3034 0.4891 0.0860  -0.0488 0.1247  164  GLY C N   
7121  C  CA  . GLY C 164 ? 0.6799 0.2492 0.4151 0.0648  -0.0495 0.1249  164  GLY C CA  
7122  C  C   . GLY C 164 ? 0.5949 0.2194 0.3576 0.0728  -0.0437 0.1211  164  GLY C C   
7123  O  O   . GLY C 164 ? 0.7729 0.4269 0.5513 0.0609  -0.0423 0.1149  164  GLY C O   
7124  N  N   . ARG C 165 ? 0.5408 0.1784 0.3090 0.0930  -0.0410 0.1252  165  ARG C N   
7125  C  CA  . ARG C 165 ? 0.7721 0.4602 0.5653 0.1000  -0.0363 0.1220  165  ARG C CA  
7126  C  C   . ARG C 165 ? 0.7914 0.4870 0.5910 0.1049  -0.0307 0.1085  165  ARG C C   
7127  O  O   . ARG C 165 ? 0.6062 0.3314 0.4216 0.0943  -0.0287 0.1023  165  ARG C O   
7128  C  CB  . ARG C 165 ? 0.7068 0.4073 0.5038 0.1207  -0.0359 0.1301  165  ARG C CB  
7129  C  CG  . ARG C 165 ? 0.6403 0.3948 0.4632 0.1271  -0.0319 0.1265  165  ARG C CG  
7130  C  CD  . ARG C 165 ? 0.6554 0.4248 0.4824 0.1468  -0.0329 0.1351  165  ARG C CD  
7131  N  NE  . ARG C 165 ? 0.5534 0.3675 0.4031 0.1565  -0.0283 0.1289  165  ARG C NE  
7132  C  CZ  . ARG C 165 ? 0.5673 0.4263 0.4359 0.1502  -0.0292 0.1296  165  ARG C CZ  
7133  N  NH1 . ARG C 165 ? 0.5695 0.4371 0.4371 0.1359  -0.0337 0.1361  165  ARG C NH1 
7134  N  NH2 . ARG C 165 ? 0.4462 0.3422 0.3342 0.1578  -0.0253 0.1237  165  ARG C NH2 
7135  N  N   . GLY C 166 ? 0.6731 0.3407 0.4589 0.1214  -0.0279 0.1040  166  GLY C N   
7136  C  CA  . GLY C 166 ? 0.6227 0.2965 0.4117 0.1270  -0.0218 0.0919  166  GLY C CA  
7137  C  C   . GLY C 166 ? 0.7396 0.3894 0.5163 0.1095  -0.0246 0.0855  166  GLY C C   
7138  O  O   . GLY C 166 ? 0.9113 0.5438 0.6797 0.0933  -0.0310 0.0902  166  GLY C O   
7139  N  N   . ASN C 167 ? 0.6779 0.3289 0.4536 0.1116  -0.0200 0.0749  167  ASN C N   
7140  C  CA  . ASN C 167 ? 0.6501 0.2779 0.4124 0.0960  -0.0236 0.0687  167  ASN C CA  
7141  C  C   . ASN C 167 ? 0.7649 0.3367 0.4960 0.0990  -0.0273 0.0671  167  ASN C C   
7142  O  O   . ASN C 167 ? 0.7911 0.3405 0.5121 0.1076  -0.0293 0.0741  167  ASN C O   
7143  C  CB  . ASN C 167 ? 0.4408 0.0884 0.2107 0.0960  -0.0182 0.0590  167  ASN C CB  
7144  C  CG  . ASN C 167 ? 0.5998 0.2357 0.3586 0.1161  -0.0105 0.0521  167  ASN C CG  
7145  O  OD1 . ASN C 167 ? 0.7078 0.3216 0.4544 0.1320  -0.0090 0.0538  167  ASN C OD1 
7146  N  ND2 . ASN C 167 ? 0.5250 0.1757 0.2875 0.1159  -0.0053 0.0446  167  ASN C ND2 
7147  N  N   . ALA C 168 ? 0.8264 0.3744 0.5411 0.0919  -0.0288 0.0582  168  ALA C N   
7148  C  CA  . ALA C 168 ? 0.9173 0.4095 0.5999 0.0912  -0.0335 0.0548  168  ALA C CA  
7149  C  C   . ALA C 168 ? 1.0827 0.5503 0.7485 0.1172  -0.0267 0.0492  168  ALA C C   
7150  O  O   . ALA C 168 ? 1.1017 0.5200 0.7407 0.1229  -0.0298 0.0482  168  ALA C O   
7151  C  CB  . ALA C 168 ? 0.9084 0.3869 0.5791 0.0736  -0.0384 0.0467  168  ALA C CB  
7152  N  N   . ALA C 169 ? 0.9624 0.4647 0.6441 0.1328  -0.0173 0.0456  169  ALA C N   
7153  C  CA  . ALA C 169 ? 0.8770 0.3680 0.5486 0.1595  -0.0090 0.0406  169  ALA C CA  
7154  C  C   . ALA C 169 ? 0.8580 0.3642 0.5432 0.1764  -0.0071 0.0506  169  ALA C C   
7155  O  O   . ALA C 169 ? 0.7674 0.2744 0.4510 0.2010  0.0000  0.0487  169  ALA C O   
7156  C  CB  . ALA C 169 ? 0.7494 0.2736 0.4321 0.1662  0.0006  0.0326  169  ALA C CB  
7157  N  N   . ASN C 170 ? 0.7417 0.2622 0.4405 0.1635  -0.0137 0.0615  170  ASN C N   
7158  C  CA  . ASN C 170 ? 0.8804 0.4180 0.5921 0.1768  -0.0136 0.0723  170  ASN C CA  
7159  C  C   . ASN C 170 ? 0.8779 0.4698 0.6174 0.1911  -0.0057 0.0723  170  ASN C C   
7160  O  O   . ASN C 170 ? 0.8903 0.4924 0.6361 0.2106  -0.0038 0.0782  170  ASN C O   
7161  C  CB  . ASN C 170 ? 1.1487 0.6372 0.8351 0.1952  -0.0151 0.0749  170  ASN C CB  
7162  C  CG  . ASN C 170 ? 1.3604 0.8105 1.0302 0.1797  -0.0252 0.0840  170  ASN C CG  
7163  O  OD1 . ASN C 170 ? 1.3691 0.7654 1.0100 0.1751  -0.0293 0.0800  170  ASN C OD1 
7164  N  ND2 . ASN C 170 ? 1.3616 0.8391 1.0485 0.1701  -0.0294 0.0963  170  ASN C ND2 
7165  N  N   . ILE C 171 ? 0.7507 0.3779 0.5072 0.1809  -0.0017 0.0663  171  ILE C N   
7166  C  CA  . ILE C 171 ? 0.8069 0.4874 0.5915 0.1893  0.0045  0.0675  171  ILE C CA  
7167  C  C   . ILE C 171 ? 0.7138 0.4318 0.5212 0.1709  0.0002  0.0729  171  ILE C C   
7168  O  O   . ILE C 171 ? 0.7310 0.4448 0.5373 0.1506  -0.0038 0.0712  171  ILE C O   
7169  C  CB  . ILE C 171 ? 0.7344 0.4317 0.5231 0.1952  0.0140  0.0575  171  ILE C CB  
7170  C  CG1 . ILE C 171 ? 0.6257 0.3449 0.4262 0.1732  0.0133  0.0538  171  ILE C CG1 
7171  C  CG2 . ILE C 171 ? 0.7488 0.4020 0.5087 0.2083  0.0178  0.0495  171  ILE C CG2 
7172  C  CD1 . ILE C 171 ? 0.6377 0.4104 0.4689 0.1698  0.0159  0.0569  171  ILE C CD1 
7173  N  N   . ASP C 172 ? 0.7248 0.4799 0.5524 0.1791  0.0010  0.0791  172  ASP C N   
7174  C  CA  . ASP C 172 ? 0.6144 0.4056 0.4622 0.1645  -0.0029 0.0837  172  ASP C CA  
7175  C  C   . ASP C 172 ? 0.6421 0.4655 0.5072 0.1533  0.0015  0.0762  172  ASP C C   
7176  O  O   . ASP C 172 ? 0.6710 0.5249 0.5512 0.1618  0.0076  0.0734  172  ASP C O   
7177  C  CB  . ASP C 172 ? 0.4955 0.3164 0.3577 0.1778  -0.0038 0.0919  172  ASP C CB  
7178  C  CG  . ASP C 172 ? 0.5682 0.4210 0.4461 0.1630  -0.0089 0.0970  172  ASP C CG  
7179  O  OD1 . ASP C 172 ? 0.5695 0.4391 0.4571 0.1462  -0.0084 0.0916  172  ASP C OD1 
7180  O  OD2 . ASP C 172 ? 0.6544 0.5144 0.5334 0.1691  -0.0136 0.1065  172  ASP C OD2 
7181  N  N   . LEU C 173 ? 0.4974 0.3144 0.3606 0.1339  -0.0018 0.0736  173  LEU C N   
7182  C  CA  . LEU C 173 ? 0.6031 0.4434 0.4794 0.1229  0.0015  0.0670  173  LEU C CA  
7183  C  C   . LEU C 173 ? 0.5151 0.4012 0.4159 0.1224  0.0034  0.0680  173  LEU C C   
7184  O  O   . LEU C 173 ? 0.4560 0.3626 0.3683 0.1178  0.0078  0.0626  173  LEU C O   
7185  C  CB  . LEU C 173 ? 0.6125 0.4402 0.4839 0.1035  -0.0037 0.0656  173  LEU C CB  
7186  C  CG  . LEU C 173 ? 0.5439 0.3282 0.3912 0.1013  -0.0060 0.0630  173  LEU C CG  
7187  C  CD1 . LEU C 173 ? 0.4012 0.1766 0.2455 0.0820  -0.0124 0.0632  173  LEU C CD1 
7188  C  CD2 . LEU C 173 ? 0.5603 0.3375 0.4005 0.1087  0.0004  0.0551  173  LEU C CD2 
7189  N  N   . ASN C 174 ? 0.3676 0.2689 0.2752 0.1264  -0.0005 0.0751  174  ASN C N   
7190  C  CA  . ASN C 174 ? 0.2717 0.2166 0.2013 0.1250  -0.0001 0.0757  174  ASN C CA  
7191  C  C   . ASN C 174 ? 0.4400 0.4064 0.3795 0.1423  0.0048  0.0765  174  ASN C C   
7192  O  O   . ASN C 174 ? 0.5767 0.5790 0.5332 0.1443  0.0037  0.0790  174  ASN C O   
7193  C  CB  . ASN C 174 ? 0.2962 0.2520 0.2285 0.1191  -0.0070 0.0826  174  ASN C CB  
7194  C  CG  . ASN C 174 ? 0.4559 0.4502 0.4070 0.1080  -0.0079 0.0794  174  ASN C CG  
7195  O  OD1 . ASN C 174 ? 0.4827 0.4876 0.4425 0.1000  -0.0044 0.0719  174  ASN C OD1 
7196  N  ND2 . ASN C 174 ? 0.3672 0.3802 0.3225 0.1075  -0.0129 0.0851  174  ASN C ND2 
7197  N  N   . ARG C 175 ? 0.3620 0.3076 0.2906 0.1549  0.0103  0.0740  175  ARG C N   
7198  C  CA  . ARG C 175 ? 0.3515 0.3197 0.2903 0.1714  0.0172  0.0732  175  ARG C CA  
7199  C  C   . ARG C 175 ? 0.4172 0.3776 0.3512 0.1705  0.0256  0.0652  175  ARG C C   
7200  O  O   . ARG C 175 ? 0.5471 0.5259 0.4885 0.1828  0.0333  0.0635  175  ARG C O   
7201  C  CB  . ARG C 175 ? 0.2754 0.2258 0.2032 0.1938  0.0168  0.0788  175  ARG C CB  
7202  C  CG  . ARG C 175 ? 0.3963 0.3418 0.3209 0.1959  0.0078  0.0884  175  ARG C CG  
7203  C  CD  . ARG C 175 ? 0.3751 0.3680 0.3221 0.2002  0.0049  0.0941  175  ARG C CD  
7204  N  NE  . ARG C 175 ? 0.6096 0.6155 0.5619 0.1815  -0.0020 0.0963  175  ARG C NE  
7205  C  CZ  . ARG C 175 ? 0.5808 0.5884 0.5300 0.1811  -0.0097 0.1050  175  ARG C CZ  
7206  N  NH1 . ARG C 175 ? 0.6128 0.6091 0.5538 0.1988  -0.0129 0.1141  175  ARG C NH1 
7207  N  NH2 . ARG C 175 ? 0.6878 0.7082 0.6411 0.1629  -0.0140 0.1045  175  ARG C NH2 
7208  N  N   . ASP C 176 ? 0.6181 0.5536 0.5401 0.1558  0.0242  0.0607  176  ASP C N   
7209  C  CA  . ASP C 176 ? 0.5482 0.4669 0.4585 0.1554  0.0308  0.0539  176  ASP C CA  
7210  C  C   . ASP C 176 ? 0.5088 0.4521 0.4326 0.1419  0.0350  0.0499  176  ASP C C   
7211  O  O   . ASP C 176 ? 0.5123 0.4474 0.4278 0.1417  0.0412  0.0454  176  ASP C O   
7212  C  CB  . ASP C 176 ? 0.4582 0.3313 0.3440 0.1487  0.0261  0.0516  176  ASP C CB  
7213  C  CG  . ASP C 176 ? 0.6186 0.4663 0.4848 0.1555  0.0322  0.0451  176  ASP C CG  
7214  O  OD1 . ASP C 176 ? 0.6762 0.5343 0.5436 0.1718  0.0405  0.0436  176  ASP C OD1 
7215  O  OD2 . ASP C 176 ? 0.6390 0.4581 0.4884 0.1450  0.0289  0.0415  176  ASP C OD2 
7216  N  N   . PHE C 177 ? 0.4752 0.4464 0.4177 0.1302  0.0313  0.0517  177  PHE C N   
7217  C  CA  . PHE C 177 ? 0.3981 0.3889 0.3524 0.1168  0.0345  0.0482  177  PHE C CA  
7218  C  C   . PHE C 177 ? 0.4042 0.4298 0.3748 0.1231  0.0426  0.0485  177  PHE C C   
7219  O  O   . PHE C 177 ? 0.5953 0.6396 0.5742 0.1368  0.0437  0.0520  177  PHE C O   
7220  C  CB  . PHE C 177 ? 0.4669 0.4703 0.4326 0.1016  0.0275  0.0486  177  PHE C CB  
7221  C  CG  . PHE C 177 ? 0.4966 0.4715 0.4493 0.0923  0.0214  0.0476  177  PHE C CG  
7222  C  CD1 . PHE C 177 ? 0.6075 0.5621 0.5487 0.0965  0.0159  0.0512  177  PHE C CD1 
7223  C  CD2 . PHE C 177 ? 0.3841 0.3533 0.3362 0.0793  0.0209  0.0438  177  PHE C CD2 
7224  C  CE1 . PHE C 177 ? 0.6203 0.5527 0.5514 0.0865  0.0103  0.0508  177  PHE C CE1 
7225  C  CE2 . PHE C 177 ? 0.4992 0.4467 0.4416 0.0713  0.0151  0.0432  177  PHE C CE2 
7226  C  CZ  . PHE C 177 ? 0.6006 0.5314 0.5333 0.0743  0.0099  0.0467  177  PHE C CZ  
7227  N  N   . PRO C 178 ? 0.3693 0.4042 0.3443 0.1132  0.0481  0.0457  178  PRO C N   
7228  C  CA  . PRO C 178 ? 0.3472 0.4181 0.3390 0.1160  0.0563  0.0466  178  PRO C CA  
7229  C  C   . PRO C 178 ? 0.4747 0.5830 0.4898 0.1125  0.0518  0.0494  178  PRO C C   
7230  O  O   . PRO C 178 ? 0.3905 0.5000 0.4106 0.0993  0.0444  0.0486  178  PRO C O   
7231  C  CB  . PRO C 178 ? 0.2656 0.3344 0.2563 0.1005  0.0604  0.0441  178  PRO C CB  
7232  C  CG  . PRO C 178 ? 0.3676 0.3938 0.3349 0.0972  0.0567  0.0414  178  PRO C CG  
7233  C  CD  . PRO C 178 ? 0.4011 0.4131 0.3649 0.0996  0.0471  0.0424  178  PRO C CD  
7234  N  N   . ASP C 179 ? 0.5162 0.6562 0.5452 0.1247  0.0564  0.0524  179  ASP C N   
7235  C  CA  . ASP C 179 ? 0.4840 0.6640 0.5358 0.1221  0.0518  0.0553  179  ASP C CA  
7236  C  C   . ASP C 179 ? 0.4633 0.6778 0.5343 0.1070  0.0563  0.0543  179  ASP C C   
7237  O  O   . ASP C 179 ? 0.3677 0.5920 0.4408 0.1090  0.0664  0.0543  179  ASP C O   
7238  C  CB  . ASP C 179 ? 0.4848 0.6833 0.5428 0.1446  0.0530  0.0601  179  ASP C CB  
7239  C  CG  . ASP C 179 ? 0.6273 0.8633 0.7054 0.1436  0.0451  0.0641  179  ASP C CG  
7240  O  OD1 . ASP C 179 ? 0.6022 0.8320 0.6789 0.1310  0.0359  0.0634  179  ASP C OD1 
7241  O  OD2 . ASP C 179 ? 0.5388 0.8116 0.6337 0.1560  0.0480  0.0679  179  ASP C OD2 
7242  N  N   . ARG C 180 ? 0.3668 0.5989 0.4504 0.0912  0.0490  0.0533  180  ARG C N   
7243  C  CA  . ARG C 180 ? 0.4295 0.6937 0.5316 0.0748  0.0517  0.0524  180  ARG C CA  
7244  C  C   . ARG C 180 ? 0.5086 0.8175 0.6304 0.0847  0.0584  0.0567  180  ARG C C   
7245  O  O   . ARG C 180 ? 0.4817 0.8125 0.6147 0.0750  0.0658  0.0571  180  ARG C O   
7246  C  CB  . ARG C 180 ? 0.4145 0.6912 0.5259 0.0594  0.0413  0.0500  180  ARG C CB  
7247  C  CG  . ARG C 180 ? 0.5060 0.8020 0.6239 0.0709  0.0333  0.0532  180  ARG C CG  
7248  C  CD  . ARG C 180 ? 0.4842 0.7847 0.6045 0.0566  0.0227  0.0497  180  ARG C CD  
7249  N  NE  . ARG C 180 ? 0.5627 0.8905 0.6916 0.0663  0.0154  0.0539  180  ARG C NE  
7250  C  CZ  . ARG C 180 ? 0.4322 0.8057 0.5820 0.0628  0.0124  0.0556  180  ARG C CZ  
7251  N  NH1 . ARG C 180 ? 0.2501 0.6464 0.4147 0.0481  0.0166  0.0531  180  ARG C NH1 
7252  N  NH2 . ARG C 180 ? 0.3308 0.7278 0.4865 0.0731  0.0048  0.0603  180  ARG C NH2 
7253  N  N   . LEU C 181 ? 0.4441 0.7674 0.5704 0.1041  0.0558  0.0605  181  LEU C N   
7254  C  CA  . LEU C 181 ? 0.4016 0.7693 0.5474 0.1177  0.0619  0.0650  181  LEU C CA  
7255  C  C   . LEU C 181 ? 0.4473 0.8006 0.5814 0.1382  0.0737  0.0657  181  LEU C C   
7256  O  O   . LEU C 181 ? 0.5373 0.9153 0.6808 0.1588  0.0777  0.0694  181  LEU C O   
7257  C  CB  . LEU C 181 ? 0.1486 0.5419 0.3062 0.1302  0.0527  0.0695  181  LEU C CB  
7258  C  CG  . LEU C 181 ? 0.3903 0.7858 0.5504 0.1133  0.0397  0.0678  181  LEU C CG  
7259  C  CD1 . LEU C 181 ? 0.4291 0.8398 0.5931 0.1283  0.0302  0.0732  181  LEU C CD1 
7260  C  CD2 . LEU C 181 ? 0.6321 1.0630 0.8122 0.0897  0.0386  0.0653  181  LEU C CD2 
7261  N  N   . GLU C 182 ? 0.7397 1.0522 0.8519 0.1335  0.0788  0.0618  182  GLU C N   
7262  C  CA  . GLU C 182 ? 0.8825 1.1833 0.9822 0.1483  0.0914  0.0610  182  GLU C CA  
7263  C  C   . GLU C 182 ? 1.0719 1.3585 1.1601 0.1777  0.0935  0.0619  182  GLU C C   
7264  O  O   . GLU C 182 ? 1.0435 1.3340 1.1362 0.1890  0.0853  0.0649  182  GLU C O   
7265  C  CB  . GLU C 182 ? 0.6782 1.0251 0.7982 0.1435  0.1027  0.0632  182  GLU C CB  
7266  C  CG  . GLU C 182 ? 0.8312 1.1612 0.9350 0.1443  0.1157  0.0611  182  GLU C CG  
7267  C  CD  . GLU C 182 ? 1.1136 1.4137 1.2042 0.1201  0.1136  0.0588  182  GLU C CD  
7268  O  OE1 . GLU C 182 ? 1.1012 1.3914 1.1948 0.1047  0.1022  0.0578  182  GLU C OE1 
7269  O  OE2 . GLU C 182 ? 1.0982 1.3849 1.1747 0.1173  0.1233  0.0580  182  GLU C OE2 
7270  N  N   . GLN C 183 ? 1.0540 1.3223 1.1256 0.1899  0.1045  0.0591  183  GLN C N   
7271  C  CA  . GLN C 183 ? 0.9895 1.2414 1.0476 0.2188  0.1087  0.0585  183  GLN C CA  
7272  C  C   . GLN C 183 ? 1.0646 1.3085 1.1080 0.2284  0.1236  0.0544  183  GLN C C   
7273  O  O   . GLN C 183 ? 1.0616 1.2581 1.0758 0.2284  0.1247  0.0493  183  GLN C O   
7274  C  CB  . GLN C 183 ? 0.8186 1.0165 0.8517 0.2235  0.0984  0.0568  183  GLN C CB  
7275  C  CG  . GLN C 183 ? 0.7621 0.9293 0.7741 0.2512  0.1024  0.0549  183  GLN C CG  
7276  C  CD  . GLN C 183 ? 0.9529 1.1409 0.9781 0.2737  0.0989  0.0606  183  GLN C CD  
7277  O  OE1 . GLN C 183 ? 0.8552 1.0845 0.9063 0.2685  0.0931  0.0663  183  GLN C OE1 
7278  N  NE2 . GLN C 183 ? 0.9728 1.1307 0.9787 0.2993  0.1019  0.0590  183  GLN C NE2 
7279  N  N   . LEU C 189 ? 1.1759 1.2062 1.1233 0.0309  0.0941  0.0508  189  LEU C N   
7280  C  CA  . LEU C 189 ? 1.2411 1.2900 1.1884 0.0463  0.1034  0.0503  189  LEU C CA  
7281  C  C   . LEU C 189 ? 1.2929 1.3322 1.2371 0.0622  0.0975  0.0458  189  LEU C C   
7282  O  O   . LEU C 189 ? 1.2387 1.2874 1.1807 0.0782  0.1039  0.0446  189  LEU C O   
7283  C  CB  . LEU C 189 ? 1.1333 1.2266 1.1063 0.0426  0.1107  0.0535  189  LEU C CB  
7284  C  CG  . LEU C 189 ? 0.9598 1.0719 0.9559 0.0389  0.1020  0.0521  189  LEU C CG  
7285  C  CD1 . LEU C 189 ? 0.9626 1.1213 0.9821 0.0445  0.1086  0.0542  189  LEU C CD1 
7286  C  CD2 . LEU C 189 ? 0.9634 1.0686 0.9661 0.0183  0.0951  0.0527  189  LEU C CD2 
7287  N  N   . ARG C 190 ? 1.2579 1.2783 1.2017 0.0581  0.0857  0.0437  190  ARG C N   
7288  C  CA  . ARG C 190 ? 1.0950 1.1016 1.0333 0.0705  0.0793  0.0406  190  ARG C CA  
7289  C  C   . ARG C 190 ? 1.0055 0.9758 0.9155 0.0768  0.0783  0.0379  190  ARG C C   
7290  O  O   . ARG C 190 ? 0.8150 0.7624 0.7137 0.0676  0.0723  0.0376  190  ARG C O   
7291  C  CB  . ARG C 190 ? 0.9029 0.9081 0.8528 0.0629  0.0679  0.0398  190  ARG C CB  
7292  C  CG  . ARG C 190 ? 0.7153 0.7060 0.6633 0.0474  0.0622  0.0397  190  ARG C CG  
7293  C  CD  . ARG C 190 ? 0.6198 0.6335 0.5891 0.0350  0.0603  0.0403  190  ARG C CD  
7294  N  NE  . ARG C 190 ? 0.8970 0.9239 0.8712 0.0256  0.0680  0.0432  190  ARG C NE  
7295  C  CZ  . ARG C 190 ? 0.7730 0.8108 0.7601 0.0110  0.0667  0.0438  190  ARG C CZ  
7296  N  NH1 . ARG C 190 ? 0.4739 0.5113 0.4699 0.0053  0.0580  0.0405  190  ARG C NH1 
7297  N  NH2 . ARG C 190 ? 0.6849 0.7328 0.6748 0.0014  0.0741  0.0475  190  ARG C NH2 
7298  N  N   . ALA C 191 ? 1.0528 1.0182 0.9511 0.0928  0.0838  0.0357  191  ALA C N   
7299  C  CA  . ALA C 191 ? 1.1955 1.1265 1.0644 0.0992  0.0838  0.0320  191  ALA C CA  
7300  C  C   . ALA C 191 ? 1.2931 1.2112 1.1506 0.1178  0.0851  0.0282  191  ALA C C   
7301  O  O   . ALA C 191 ? 1.3526 1.2666 1.2167 0.1218  0.0779  0.0284  191  ALA C O   
7302  C  CB  . ALA C 191 ? 1.1693 1.1016 1.0250 0.0969  0.0937  0.0327  191  ALA C CB  
7303  N  N   . GLN C 192 ? 1.3346 1.2441 1.1728 0.1291  0.0943  0.0249  192  GLN C N   
7304  C  CA  . GLN C 192 ? 1.3794 1.2728 1.2032 0.1489  0.0970  0.0203  192  GLN C CA  
7305  C  C   . GLN C 192 ? 1.3082 1.1592 1.1120 0.1494  0.0853  0.0166  192  GLN C C   
7306  O  O   . GLN C 192 ? 1.4096 1.2358 1.1976 0.1374  0.0781  0.0150  192  GLN C O   
7307  C  CB  . GLN C 192 ? 1.3795 1.3053 1.2274 0.1620  0.1015  0.0231  192  GLN C CB  
7308  C  CG  . GLN C 192 ? 1.1765 1.1403 1.0363 0.1699  0.1164  0.0246  192  GLN C CG  
7309  C  CD  . GLN C 192 ? 0.9275 0.8786 0.7653 0.1911  0.1269  0.0188  192  GLN C CD  
7310  O  OE1 . GLN C 192 ? 0.8462 0.8224 0.6954 0.2088  0.1354  0.0192  192  GLN C OE1 
7311  N  NE2 . GLN C 192 ? 0.9798 0.8921 0.7854 0.1902  0.1259  0.0131  192  GLN C NE2 
7312  N  N   . SER C 193 ? 1.0509 0.8941 0.8553 0.1632  0.0833  0.0159  193  SER C N   
7313  C  CA  . SER C 193 ? 1.0227 0.8243 0.8070 0.1634  0.0730  0.0129  193  SER C CA  
7314  C  C   . SER C 193 ? 0.8916 0.6952 0.6907 0.1651  0.0649  0.0176  193  SER C C   
7315  O  O   . SER C 193 ? 0.6944 0.4884 0.4891 0.1817  0.0661  0.0174  193  SER C O   
7316  C  CB  . SER C 193 ? 1.1804 0.9488 0.9335 0.1794  0.0779  0.0053  193  SER C CB  
7317  O  OG  . SER C 193 ? 1.3224 1.0612 1.0495 0.1689  0.0739  0.0003  193  SER C OG  
7318  N  N   . ARG C 194 ? 0.7241 0.5391 0.5394 0.1482  0.0567  0.0220  194  ARG C N   
7319  C  CA  . ARG C 194 ? 0.6752 0.4886 0.5006 0.1454  0.0476  0.0266  194  ARG C CA  
7320  C  C   . ARG C 194 ? 0.6184 0.3902 0.4219 0.1383  0.0378  0.0248  194  ARG C C   
7321  O  O   . ARG C 194 ? 0.6735 0.4207 0.4559 0.1339  0.0370  0.0197  194  ARG C O   
7322  C  CB  . ARG C 194 ? 0.6891 0.5331 0.5395 0.1299  0.0439  0.0308  194  ARG C CB  
7323  C  CG  . ARG C 194 ? 0.7784 0.6596 0.6474 0.1297  0.0526  0.0316  194  ARG C CG  
7324  C  CD  . ARG C 194 ? 0.9366 0.8477 0.8243 0.1423  0.0567  0.0351  194  ARG C CD  
7325  N  NE  . ARG C 194 ? 1.1167 1.0663 1.0240 0.1395  0.0646  0.0362  194  ARG C NE  
7326  C  CZ  . ARG C 194 ? 1.2825 1.2691 1.2136 0.1426  0.0659  0.0399  194  ARG C CZ  
7327  N  NH1 . ARG C 194 ? 1.2970 1.2870 1.2345 0.1498  0.0598  0.0432  194  ARG C NH1 
7328  N  NH2 . ARG C 194 ? 1.3695 1.3900 1.3175 0.1375  0.0730  0.0408  194  ARG C NH2 
7329  N  N   . GLN C 195 ? 0.6534 0.4185 0.4613 0.1361  0.0300  0.0295  195  GLN C N   
7330  C  CA  . GLN C 195 ? 0.7006 0.4335 0.4933 0.1242  0.0198  0.0295  195  GLN C CA  
7331  C  C   . GLN C 195 ? 0.7148 0.4530 0.5107 0.1053  0.0150  0.0283  195  GLN C C   
7332  O  O   . GLN C 195 ? 0.6791 0.4483 0.4948 0.0993  0.0174  0.0298  195  GLN C O   
7333  C  CB  . GLN C 195 ? 0.7414 0.4757 0.5433 0.1227  0.0132  0.0367  195  GLN C CB  
7334  C  CG  . GLN C 195 ? 0.6914 0.4165 0.4882 0.1422  0.0162  0.0391  195  GLN C CG  
7335  C  CD  . GLN C 195 ? 0.7403 0.4230 0.5073 0.1533  0.0182  0.0329  195  GLN C CD  
7336  O  OE1 . GLN C 195 ? 0.8950 0.5398 0.6410 0.1449  0.0110  0.0313  195  GLN C OE1 
7337  N  NE2 . GLN C 195 ? 0.5767 0.2664 0.3416 0.1720  0.0280  0.0290  195  GLN C NE2 
7338  N  N   . PRO C 196 ? 0.6342 0.3418 0.4107 0.0958  0.0077  0.0257  196  PRO C N   
7339  C  CA  . PRO C 196 ? 0.4597 0.1713 0.2383 0.0794  0.0019  0.0251  196  PRO C CA  
7340  C  C   . PRO C 196 ? 0.5688 0.3107 0.3737 0.0695  -0.0013 0.0305  196  PRO C C   
7341  O  O   . PRO C 196 ? 0.5741 0.3333 0.3896 0.0617  -0.0015 0.0303  196  PRO C O   
7342  C  CB  . PRO C 196 ? 0.5071 0.1838 0.2651 0.0706  -0.0077 0.0238  196  PRO C CB  
7343  C  CG  . PRO C 196 ? 0.6739 0.3198 0.4106 0.0843  -0.0048 0.0207  196  PRO C CG  
7344  C  CD  . PRO C 196 ? 0.4472 0.1145 0.1996 0.0997  0.0032  0.0240  196  PRO C CD  
7345  N  N   . GLU C 197 ? 0.4687 0.2146 0.2821 0.0705  -0.0039 0.0353  197  GLU C N   
7346  C  CA  . GLU C 197 ? 0.4703 0.2421 0.3052 0.0614  -0.0073 0.0399  197  GLU C CA  
7347  C  C   . GLU C 197 ? 0.5205 0.3262 0.3760 0.0659  -0.0005 0.0400  197  GLU C C   
7348  O  O   . GLU C 197 ? 0.4331 0.2591 0.3033 0.0574  -0.0016 0.0400  197  GLU C O   
7349  C  CB  . GLU C 197 ? 0.4874 0.2529 0.3224 0.0614  -0.0115 0.0457  197  GLU C CB  
7350  C  CG  . GLU C 197 ? 0.4874 0.2197 0.3034 0.0530  -0.0192 0.0467  197  GLU C CG  
7351  C  CD  . GLU C 197 ? 0.6455 0.3418 0.4378 0.0638  -0.0181 0.0445  197  GLU C CD  
7352  O  OE1 . GLU C 197 ? 0.7833 0.4485 0.5581 0.0564  -0.0248 0.0453  197  GLU C OE1 
7353  O  OE2 . GLU C 197 ? 0.6092 0.3083 0.4001 0.0796  -0.0105 0.0419  197  GLU C OE2 
7354  N  N   . THR C 198 ? 0.4968 0.3082 0.3530 0.0794  0.0062  0.0399  198  THR C N   
7355  C  CA  . THR C 198 ? 0.4082 0.2528 0.2839 0.0830  0.0123  0.0402  198  THR C CA  
7356  C  C   . THR C 198 ? 0.4730 0.3233 0.3499 0.0766  0.0156  0.0366  198  THR C C   
7357  O  O   . THR C 198 ? 0.4704 0.3406 0.3625 0.0679  0.0150  0.0368  198  THR C O   
7358  C  CB  . THR C 198 ? 0.5866 0.4360 0.4613 0.0997  0.0192  0.0407  198  THR C CB  
7359  O  OG1 . THR C 198 ? 0.6216 0.4553 0.4889 0.1070  0.0151  0.0445  198  THR C OG1 
7360  C  CG2 . THR C 198 ? 0.6214 0.5102 0.5196 0.1017  0.0239  0.0422  198  THR C CG2 
7361  N  N   . ALA C 199 ? 0.5982 0.4287 0.4569 0.0809  0.0190  0.0332  199  ALA C N   
7362  C  CA  . ALA C 199 ? 0.5316 0.3646 0.3875 0.0755  0.0224  0.0309  199  ALA C CA  
7363  C  C   . ALA C 199 ? 0.6068 0.4409 0.4686 0.0614  0.0150  0.0317  199  ALA C C   
7364  O  O   . ALA C 199 ? 0.5688 0.4175 0.4406 0.0556  0.0171  0.0320  199  ALA C O   
7365  C  CB  . ALA C 199 ? 0.3868 0.1937 0.2171 0.0815  0.0253  0.0270  199  ALA C CB  
7366  N  N   . ALA C 200 ? 0.3752 0.1942 0.2311 0.0559  0.0065  0.0323  200  ALA C N   
7367  C  CA  . ALA C 200 ? 0.4137 0.2367 0.2767 0.0444  -0.0003 0.0331  200  ALA C CA  
7368  C  C   . ALA C 200 ? 0.5554 0.4063 0.4415 0.0414  0.0012  0.0345  200  ALA C C   
7369  O  O   . ALA C 200 ? 0.7092 0.5686 0.6028 0.0359  0.0010  0.0339  200  ALA C O   
7370  C  CB  . ALA C 200 ? 0.3380 0.1466 0.1948 0.0385  -0.0090 0.0345  200  ALA C CB  
7371  N  N   . LEU C 201 ? 0.3461 0.2097 0.2420 0.0452  0.0023  0.0362  201  LEU C N   
7372  C  CA  . LEU C 201 ? 0.4679 0.3568 0.3833 0.0417  0.0026  0.0366  201  LEU C CA  
7373  C  C   . LEU C 201 ? 0.5216 0.4273 0.4466 0.0427  0.0092  0.0351  201  LEU C C   
7374  O  O   . LEU C 201 ? 0.3438 0.2614 0.2799 0.0362  0.0088  0.0337  201  LEU C O   
7375  C  CB  . LEU C 201 ? 0.4541 0.3524 0.3755 0.0446  0.0008  0.0396  201  LEU C CB  
7376  C  CG  . LEU C 201 ? 0.5189 0.4140 0.4409 0.0365  -0.0061 0.0410  201  LEU C CG  
7377  C  CD1 . LEU C 201 ? 0.5273 0.3958 0.4321 0.0354  -0.0104 0.0428  201  LEU C CD1 
7378  C  CD2 . LEU C 201 ? 0.6485 0.5624 0.5814 0.0356  -0.0075 0.0435  201  LEU C CD2 
7379  N  N   . VAL C 202 ? 0.3966 0.3030 0.3172 0.0508  0.0156  0.0354  202  VAL C N   
7380  C  CA  . VAL C 202 ? 0.4253 0.3488 0.3548 0.0501  0.0224  0.0347  202  VAL C CA  
7381  C  C   . VAL C 202 ? 0.5212 0.4361 0.4473 0.0413  0.0218  0.0337  202  VAL C C   
7382  O  O   . VAL C 202 ? 0.4834 0.4108 0.4215 0.0342  0.0221  0.0331  202  VAL C O   
7383  C  CB  . VAL C 202 ? 0.3630 0.2867 0.2852 0.0605  0.0304  0.0351  202  VAL C CB  
7384  C  CG1 . VAL C 202 ? 0.2584 0.1968 0.1869 0.0566  0.0377  0.0352  202  VAL C CG1 
7385  C  CG2 . VAL C 202 ? 0.2634 0.2023 0.1938 0.0706  0.0317  0.0369  202  VAL C CG2 
7386  N  N   . ASN C 203 ? 0.3608 0.2528 0.2694 0.0418  0.0200  0.0335  203  ASN C N   
7387  C  CA  . ASN C 203 ? 0.4474 0.3298 0.3503 0.0352  0.0189  0.0337  203  ASN C CA  
7388  C  C   . ASN C 203 ? 0.2951 0.1838 0.2108 0.0278  0.0134  0.0333  203  ASN C C   
7389  O  O   . ASN C 203 ? 0.4411 0.3336 0.3624 0.0226  0.0150  0.0335  203  ASN C O   
7390  C  CB  . ASN C 203 ? 0.4401 0.2980 0.3225 0.0361  0.0146  0.0335  203  ASN C CB  
7391  C  CG  . ASN C 203 ? 0.7308 0.5788 0.5958 0.0417  0.0215  0.0331  203  ASN C CG  
7392  O  OD1 . ASN C 203 ? 0.7232 0.5842 0.5925 0.0467  0.0301  0.0333  203  ASN C OD1 
7393  N  ND2 . ASN C 203 ? 0.8748 0.7014 0.7198 0.0408  0.0176  0.0325  203  ASN C ND2 
7394  N  N   . TRP C 204 ? 0.4053 0.2941 0.3245 0.0275  0.0072  0.0327  204  TRP C N   
7395  C  CA  . TRP C 204 ? 0.2958 0.1911 0.2260 0.0223  0.0021  0.0316  204  TRP C CA  
7396  C  C   . TRP C 204 ? 0.4107 0.3243 0.3560 0.0198  0.0055  0.0296  204  TRP C C   
7397  O  O   . TRP C 204 ? 0.4718 0.3855 0.4223 0.0153  0.0048  0.0280  204  TRP C O   
7398  C  CB  . TRP C 204 ? 0.3522 0.2490 0.2837 0.0228  -0.0032 0.0320  204  TRP C CB  
7399  C  CG  . TRP C 204 ? 0.4723 0.3751 0.4124 0.0186  -0.0083 0.0310  204  TRP C CG  
7400  C  CD1 . TRP C 204 ? 0.4968 0.3938 0.4366 0.0164  -0.0116 0.0306  204  TRP C CD1 
7401  C  CD2 . TRP C 204 ? 0.3347 0.2519 0.2848 0.0173  -0.0106 0.0305  204  TRP C CD2 
7402  N  NE1 . TRP C 204 ? 0.5110 0.4190 0.4612 0.0147  -0.0153 0.0293  204  TRP C NE1 
7403  C  CE2 . TRP C 204 ? 0.3934 0.3143 0.3495 0.0147  -0.0143 0.0291  204  TRP C CE2 
7404  C  CE3 . TRP C 204 ? 0.1928 0.1207 0.1464 0.0187  -0.0097 0.0317  204  TRP C CE3 
7405  C  CZ2 . TRP C 204 ? 0.2388 0.1750 0.2044 0.0133  -0.0162 0.0281  204  TRP C CZ2 
7406  C  CZ3 . TRP C 204 ? 0.3892 0.3309 0.3509 0.0162  -0.0121 0.0314  204  TRP C CZ3 
7407  C  CH2 . TRP C 204 ? 0.3349 0.2813 0.3025 0.0134  -0.0148 0.0293  204  TRP C CH2 
7408  N  N   . ILE C 205 ? 0.3315 0.2595 0.2830 0.0228  0.0085  0.0297  205  ILE C N   
7409  C  CA  . ILE C 205 ? 0.4445 0.3929 0.4105 0.0196  0.0102  0.0274  205  ILE C CA  
7410  C  C   . ILE C 205 ? 0.5502 0.5000 0.5197 0.0137  0.0143  0.0265  205  ILE C C   
7411  O  O   . ILE C 205 ? 0.5974 0.5544 0.5759 0.0076  0.0132  0.0233  205  ILE C O   
7412  C  CB  . ILE C 205 ? 0.4272 0.3920 0.3982 0.0251  0.0125  0.0290  205  ILE C CB  
7413  C  CG1 . ILE C 205 ? 0.4805 0.4428 0.4482 0.0290  0.0077  0.0306  205  ILE C CG1 
7414  C  CG2 . ILE C 205 ? 0.4811 0.4693 0.4666 0.0206  0.0139  0.0267  205  ILE C CG2 
7415  C  CD1 . ILE C 205 ? 0.3963 0.3674 0.3642 0.0373  0.0093  0.0338  205  ILE C CD1 
7416  N  N   . VAL C 206 ? 0.4107 0.3520 0.3714 0.0150  0.0190  0.0293  206  VAL C N   
7417  C  CA  . VAL C 206 ? 0.4979 0.4396 0.4601 0.0084  0.0236  0.0302  206  VAL C CA  
7418  C  C   . VAL C 206 ? 0.4119 0.3316 0.3648 0.0049  0.0206  0.0311  206  VAL C C   
7419  O  O   . VAL C 206 ? 0.4246 0.3385 0.3755 -0.0012 0.0236  0.0330  206  VAL C O   
7420  C  CB  . VAL C 206 ? 0.4386 0.3854 0.3955 0.0119  0.0317  0.0336  206  VAL C CB  
7421  C  CG1 . VAL C 206 ? 0.3352 0.3069 0.3036 0.0168  0.0348  0.0334  206  VAL C CG1 
7422  C  CG2 . VAL C 206 ? 0.5067 0.4337 0.4453 0.0190  0.0314  0.0352  206  VAL C CG2 
7423  N  N   . SER C 207 ? 0.4637 0.3718 0.4109 0.0085  0.0144  0.0305  207  SER C N   
7424  C  CA  . SER C 207 ? 0.4478 0.3367 0.3858 0.0073  0.0106  0.0322  207  SER C CA  
7425  C  C   . SER C 207 ? 0.4324 0.3199 0.3793 0.0039  0.0068  0.0292  207  SER C C   
7426  O  O   . SER C 207 ? 0.5329 0.4052 0.4743 0.0031  0.0042  0.0309  207  SER C O   
7427  C  CB  . SER C 207 ? 0.2878 0.1668 0.2159 0.0122  0.0050  0.0332  207  SER C CB  
7428  O  OG  . SER C 207 ? 0.4558 0.3405 0.3927 0.0128  -0.0009 0.0306  207  SER C OG  
7429  N  N   . LYS C 208 ? 0.4227 0.3255 0.3820 0.0028  0.0063  0.0246  208  LYS C N   
7430  C  CA  . LYS C 208 ? 0.4715 0.3733 0.4382 0.0008  0.0031  0.0198  208  LYS C CA  
7431  C  C   . LYS C 208 ? 0.3003 0.2182 0.2777 -0.0043 0.0053  0.0150  208  LYS C C   
7432  O  O   . LYS C 208 ? 0.5530 0.4880 0.5350 -0.0036 0.0072  0.0151  208  LYS C O   
7433  C  CB  . LYS C 208 ? 0.5691 0.4732 0.5380 0.0063  -0.0025 0.0180  208  LYS C CB  
7434  C  CG  . LYS C 208 ? 0.5668 0.4571 0.5266 0.0101  -0.0065 0.0223  208  LYS C CG  
7435  C  CD  . LYS C 208 ? 0.4367 0.3338 0.4015 0.0142  -0.0119 0.0208  208  LYS C CD  
7436  C  CE  . LYS C 208 ? 0.6133 0.4980 0.5709 0.0172  -0.0172 0.0250  208  LYS C CE  
7437  N  NZ  . LYS C 208 ? 0.6228 0.5181 0.5868 0.0203  -0.0226 0.0246  208  LYS C NZ  
7438  N  N   . PRO C 209 ? 0.2941 0.2053 0.2744 -0.0091 0.0046  0.0106  209  PRO C N   
7439  C  CA  . PRO C 209 ? 0.3262 0.2507 0.3151 -0.0159 0.0056  0.0048  209  PRO C CA  
7440  C  C   . PRO C 209 ? 0.4443 0.3866 0.4397 -0.0125 0.0027  -0.0007 209  PRO C C   
7441  O  O   . PRO C 209 ? 0.4434 0.3862 0.4415 -0.0153 0.0009  -0.0082 209  PRO C O   
7442  C  CB  . PRO C 209 ? 0.2745 0.1787 0.2607 -0.0209 0.0043  0.0010  209  PRO C CB  
7443  C  CG  . PRO C 209 ? 0.3780 0.2655 0.3581 -0.0122 0.0009  0.0024  209  PRO C CG  
7444  C  CD  . PRO C 209 ? 0.3501 0.2392 0.3249 -0.0076 0.0017  0.0103  209  PRO C CD  
7445  N  N   . PHE C 210 ? 0.3924 0.3477 0.3885 -0.0069 0.0025  0.0027  210  PHE C N   
7446  C  CA  . PHE C 210 ? 0.3606 0.3321 0.3609 -0.0041 0.0001  -0.0007 210  PHE C CA  
7447  C  C   . PHE C 210 ? 0.3877 0.3750 0.3943 -0.0102 -0.0001 -0.0067 210  PHE C C   
7448  O  O   . PHE C 210 ? 0.4461 0.4432 0.4568 -0.0152 0.0019  -0.0053 210  PHE C O   
7449  C  CB  . PHE C 210 ? 0.2691 0.2499 0.2679 0.0014  0.0000  0.0053  210  PHE C CB  
7450  C  CG  . PHE C 210 ? 0.3728 0.3398 0.3648 0.0062  -0.0018 0.0095  210  PHE C CG  
7451  C  CD1 . PHE C 210 ? 0.3777 0.3331 0.3624 0.0082  -0.0003 0.0150  210  PHE C CD1 
7452  C  CD2 . PHE C 210 ? 0.4246 0.3921 0.4174 0.0085  -0.0049 0.0075  210  PHE C CD2 
7453  C  CE1 . PHE C 210 ? 0.2622 0.2051 0.2395 0.0112  -0.0032 0.0183  210  PHE C CE1 
7454  C  CE2 . PHE C 210 ? 0.5224 0.4805 0.5106 0.0115  -0.0075 0.0116  210  PHE C CE2 
7455  C  CZ  . PHE C 210 ? 0.4219 0.3669 0.4019 0.0122  -0.0072 0.0169  210  PHE C CZ  
7456  N  N   . VAL C 211 ? 0.2907 0.2822 0.2978 -0.0096 -0.0025 -0.0137 211  VAL C N   
7457  C  CA  . VAL C 211 ? 0.3708 0.3740 0.3811 -0.0161 -0.0038 -0.0214 211  VAL C CA  
7458  C  C   . VAL C 211 ? 0.3748 0.4037 0.3880 -0.0144 -0.0053 -0.0203 211  VAL C C   
7459  O  O   . VAL C 211 ? 0.4644 0.5099 0.4820 -0.0201 -0.0063 -0.0220 211  VAL C O   
7460  C  CB  . VAL C 211 ? 0.2545 0.2458 0.2611 -0.0158 -0.0053 -0.0314 211  VAL C CB  
7461  C  CG1 . VAL C 211 ? 0.2803 0.2849 0.2872 -0.0221 -0.0073 -0.0408 211  VAL C CG1 
7462  C  CG2 . VAL C 211 ? 0.3202 0.2841 0.3232 -0.0181 -0.0045 -0.0324 211  VAL C CG2 
7463  N  N   . LEU C 212 ? 0.3562 0.3889 0.3669 -0.0072 -0.0058 -0.0166 212  LEU C N   
7464  C  CA  . LEU C 212 ? 0.3119 0.3658 0.3227 -0.0050 -0.0076 -0.0146 212  LEU C CA  
7465  C  C   . LEU C 212 ? 0.2040 0.2553 0.2120 0.0015  -0.0072 -0.0054 212  LEU C C   
7466  O  O   . LEU C 212 ? 0.4438 0.4802 0.4494 0.0041  -0.0066 -0.0037 212  LEU C O   
7467  C  CB  . LEU C 212 ? 0.4470 0.5088 0.4549 -0.0057 -0.0089 -0.0233 212  LEU C CB  
7468  C  CG  . LEU C 212 ? 0.4329 0.5159 0.4379 -0.0035 -0.0105 -0.0215 212  LEU C CG  
7469  C  CD1 . LEU C 212 ? 0.5408 0.6427 0.5483 -0.0064 -0.0131 -0.0187 212  LEU C CD1 
7470  C  CD2 . LEU C 212 ? 0.2475 0.3355 0.2478 -0.0037 -0.0104 -0.0317 212  LEU C CD2 
7471  N  N   . SER C 213 ? 0.2247 0.2897 0.2324 0.0039  -0.0083 0.0008  213  SER C N   
7472  C  CA  . SER C 213 ? 0.1762 0.2346 0.1793 0.0091  -0.0084 0.0098  213  SER C CA  
7473  C  C   . SER C 213 ? 0.3030 0.3770 0.3039 0.0117  -0.0105 0.0155  213  SER C C   
7474  O  O   . SER C 213 ? 0.3503 0.4419 0.3543 0.0105  -0.0119 0.0137  213  SER C O   
7475  C  CB  . SER C 213 ? 0.2425 0.2873 0.2449 0.0117  -0.0065 0.0146  213  SER C CB  
7476  O  OG  . SER C 213 ? 0.3836 0.4210 0.3798 0.0166  -0.0071 0.0225  213  SER C OG  
7477  N  N   . ALA C 214 ? 0.3438 0.4109 0.3388 0.0145  -0.0112 0.0229  214  ALA C N   
7478  C  CA  . ALA C 214 ? 0.3354 0.4122 0.3259 0.0175  -0.0133 0.0306  214  ALA C CA  
7479  C  C   . ALA C 214 ? 0.2465 0.3047 0.2294 0.0206  -0.0138 0.0397  214  ALA C C   
7480  O  O   . ALA C 214 ? 0.3156 0.3607 0.2961 0.0178  -0.0135 0.0398  214  ALA C O   
7481  C  CB  . ALA C 214 ? 0.3780 0.4713 0.3663 0.0141  -0.0144 0.0287  214  ALA C CB  
7482  N  N   . ASN C 215 ? 0.3832 0.4395 0.3621 0.0266  -0.0150 0.0471  215  ASN C N   
7483  C  CA  . ASN C 215 ? 0.3746 0.4099 0.3434 0.0292  -0.0161 0.0554  215  ASN C CA  
7484  C  C   . ASN C 215 ? 0.5431 0.5831 0.5047 0.0315  -0.0189 0.0648  215  ASN C C   
7485  O  O   . ASN C 215 ? 0.5201 0.5772 0.4843 0.0361  -0.0203 0.0666  215  ASN C O   
7486  C  CB  . ASN C 215 ? 0.4293 0.4457 0.3952 0.0356  -0.0143 0.0561  215  ASN C CB  
7487  C  CG  . ASN C 215 ? 0.3395 0.3650 0.3077 0.0451  -0.0139 0.0591  215  ASN C CG  
7488  O  OD1 . ASN C 215 ? 0.5630 0.5765 0.5229 0.0528  -0.0151 0.0664  215  ASN C OD1 
7489  N  ND2 . ASN C 215 ? 0.2597 0.3060 0.2393 0.0448  -0.0123 0.0535  215  ASN C ND2 
7490  N  N   . PHE C 216 ? 0.4282 0.4537 0.3809 0.0273  -0.0204 0.0712  216  PHE C N   
7491  C  CA  . PHE C 216 ? 0.2349 0.2661 0.1800 0.0260  -0.0228 0.0805  216  PHE C CA  
7492  C  C   . PHE C 216 ? 0.3226 0.3305 0.2556 0.0321  -0.0253 0.0911  216  PHE C C   
7493  O  O   . PHE C 216 ? 0.4648 0.4458 0.3911 0.0322  -0.0254 0.0922  216  PHE C O   
7494  C  CB  . PHE C 216 ? 0.3870 0.4226 0.3311 0.0152  -0.0222 0.0811  216  PHE C CB  
7495  C  CG  . PHE C 216 ? 0.4151 0.4724 0.3698 0.0115  -0.0196 0.0705  216  PHE C CG  
7496  C  CD1 . PHE C 216 ? 0.5043 0.5551 0.4660 0.0097  -0.0179 0.0623  216  PHE C CD1 
7497  C  CD2 . PHE C 216 ? 0.4488 0.5314 0.4047 0.0106  -0.0192 0.0683  216  PHE C CD2 
7498  C  CE1 . PHE C 216 ? 0.3515 0.4186 0.3217 0.0077  -0.0156 0.0522  216  PHE C CE1 
7499  C  CE2 . PHE C 216 ? 0.4323 0.5313 0.3959 0.0080  -0.0167 0.0571  216  PHE C CE2 
7500  C  CZ  . PHE C 216 ? 0.2851 0.3752 0.2562 0.0070  -0.0148 0.0491  216  PHE C CZ  
7501  N  N   . HIS C 217 ? 0.2684 0.2855 0.1969 0.0373  -0.0277 0.0989  217  HIS C N   
7502  C  CA  . HIS C 217 ? 0.3837 0.3783 0.3002 0.0459  -0.0303 0.1094  217  HIS C CA  
7503  C  C   . HIS C 217 ? 0.3858 0.3831 0.2919 0.0418  -0.0334 0.1211  217  HIS C C   
7504  O  O   . HIS C 217 ? 0.4880 0.5077 0.3972 0.0330  -0.0327 0.1199  217  HIS C O   
7505  C  CB  . HIS C 217 ? 0.4757 0.4809 0.3979 0.0603  -0.0307 0.1087  217  HIS C CB  
7506  C  CG  . HIS C 217 ? 0.3806 0.3802 0.3106 0.0652  -0.0270 0.0994  217  HIS C CG  
7507  N  ND1 . HIS C 217 ? 0.4695 0.4438 0.3925 0.0759  -0.0259 0.1013  217  HIS C ND1 
7508  C  CD2 . HIS C 217 ? 0.4722 0.4868 0.4148 0.0607  -0.0237 0.0884  217  HIS C CD2 
7509  C  CE1 . HIS C 217 ? 0.5648 0.5415 0.4960 0.0775  -0.0217 0.0921  217  HIS C CE1 
7510  N  NE2 . HIS C 217 ? 0.4562 0.4565 0.3994 0.0679  -0.0206 0.0848  217  HIS C NE2 
7511  N  N   . GLY C 218 ? 0.5424 0.5161 0.4350 0.0487  -0.0365 0.1325  218  GLY C N   
7512  C  CA  . GLY C 218 ? 0.4472 0.4204 0.3275 0.0455  -0.0397 0.1461  218  GLY C CA  
7513  C  C   . GLY C 218 ? 0.4642 0.4285 0.3364 0.0612  -0.0437 0.1561  218  GLY C C   
7514  O  O   . GLY C 218 ? 0.5463 0.4981 0.4208 0.0745  -0.0434 0.1530  218  GLY C O   
7515  N  N   . GLY C 219 ? 0.4689 0.4407 0.3313 0.0604  -0.0472 0.1685  219  GLY C N   
7516  C  CA  . GLY C 219 ? 0.5118 0.4756 0.3651 0.0760  -0.0520 0.1803  219  GLY C CA  
7517  C  C   . GLY C 219 ? 0.6884 0.6934 0.5475 0.0796  -0.0549 0.1823  219  GLY C C   
7518  O  O   . GLY C 219 ? 0.7525 0.7592 0.6034 0.0906  -0.0601 0.1944  219  GLY C O   
7519  N  N   . ALA C 220 ? 0.6123 0.6497 0.4848 0.0704  -0.0519 0.1699  220  ALA C N   
7520  C  CA  . ALA C 220 ? 0.6794 0.7566 0.5565 0.0709  -0.0547 0.1688  220  ALA C CA  
7521  C  C   . ALA C 220 ? 0.4489 0.5492 0.3339 0.0562  -0.0504 0.1560  220  ALA C C   
7522  O  O   . ALA C 220 ? 0.3541 0.4425 0.2450 0.0487  -0.0455 0.1472  220  ALA C O   
7523  C  CB  . ALA C 220 ? 0.6571 0.7536 0.5477 0.0856  -0.0575 0.1641  220  ALA C CB  
7524  N  N   . VAL C 221 ? 0.4388 0.5715 0.3226 0.0529  -0.0525 0.1550  221  VAL C N   
7525  C  CA  . VAL C 221 ? 0.5588 0.7141 0.4485 0.0411  -0.0484 0.1417  221  VAL C CA  
7526  C  C   . VAL C 221 ? 0.5753 0.7611 0.4769 0.0438  -0.0507 0.1292  221  VAL C C   
7527  O  O   . VAL C 221 ? 0.5135 0.7243 0.4097 0.0449  -0.0554 0.1317  221  VAL C O   
7528  C  CB  . VAL C 221 ? 0.4894 0.6567 0.3643 0.0321  -0.0478 0.1491  221  VAL C CB  
7529  C  CG1 . VAL C 221 ? 0.4005 0.5824 0.2808 0.0206  -0.0414 0.1354  221  VAL C CG1 
7530  C  CG2 . VAL C 221 ? 0.4767 0.6147 0.3372 0.0298  -0.0478 0.1662  221  VAL C CG2 
7531  N  N   . VAL C 222 ? 0.5013 0.6847 0.4182 0.0437  -0.0476 0.1160  222  VAL C N   
7532  C  CA  . VAL C 222 ? 0.4659 0.6752 0.3952 0.0448  -0.0500 0.1045  222  VAL C CA  
7533  C  C   . VAL C 222 ? 0.5487 0.7514 0.4921 0.0405  -0.0449 0.0898  222  VAL C C   
7534  O  O   . VAL C 222 ? 0.6405 0.8178 0.5860 0.0411  -0.0408 0.0901  222  VAL C O   
7535  C  CB  . VAL C 222 ? 0.4523 0.6694 0.3867 0.0576  -0.0557 0.1121  222  VAL C CB  
7536  C  CG1 . VAL C 222 ? 0.3210 0.5123 0.2625 0.0657  -0.0524 0.1137  222  VAL C CG1 
7537  C  CG2 . VAL C 222 ? 0.5585 0.8090 0.5047 0.0562  -0.0596 0.1021  222  VAL C CG2 
7538  N  N   . ALA C 223 ? 0.3988 0.6235 0.3504 0.0355  -0.0459 0.0771  223  ALA C N   
7539  C  CA  . ALA C 223 ? 0.3569 0.5758 0.3211 0.0311  -0.0418 0.0638  223  ALA C CA  
7540  C  C   . ALA C 223 ? 0.4625 0.6920 0.4404 0.0363  -0.0442 0.0624  223  ALA C C   
7541  O  O   . ALA C 223 ? 0.4537 0.7098 0.4363 0.0346  -0.0491 0.0588  223  ALA C O   
7542  C  CB  . ALA C 223 ? 0.2124 0.4438 0.1755 0.0210  -0.0407 0.0498  223  ALA C CB  
7543  N  N   . SER C 224 ? 0.4012 0.6113 0.3851 0.0422  -0.0406 0.0652  224  SER C N   
7544  C  CA  . SER C 224 ? 0.3215 0.5422 0.3186 0.0488  -0.0413 0.0656  224  SER C CA  
7545  C  C   . SER C 224 ? 0.3048 0.5212 0.3132 0.0418  -0.0365 0.0540  224  SER C C   
7546  O  O   . SER C 224 ? 0.3326 0.5267 0.3376 0.0369  -0.0319 0.0492  224  SER C O   
7547  C  CB  . SER C 224 ? 0.3518 0.5548 0.3456 0.0626  -0.0404 0.0775  224  SER C CB  
7548  O  OG  . SER C 224 ? 0.4949 0.7136 0.5018 0.0712  -0.0407 0.0786  224  SER C OG  
7549  N  N   . TYR C 225 ? 0.2799 0.5189 0.3018 0.0409  -0.0380 0.0504  225  TYR C N   
7550  C  CA  . TYR C 225 ? 0.1514 0.3890 0.1835 0.0321  -0.0341 0.0402  225  TYR C CA  
7551  C  C   . TYR C 225 ? 0.2740 0.5284 0.3209 0.0379  -0.0329 0.0435  225  TYR C C   
7552  O  O   . TYR C 225 ? 0.2740 0.5463 0.3243 0.0485  -0.0364 0.0520  225  TYR C O   
7553  C  CB  . TYR C 225 ? 0.3383 0.5904 0.3712 0.0184  -0.0374 0.0288  225  TYR C CB  
7554  C  CG  . TYR C 225 ? 0.2206 0.5070 0.2562 0.0169  -0.0454 0.0296  225  TYR C CG  
7555  C  CD1 . TYR C 225 ? 0.2452 0.5390 0.2685 0.0198  -0.0502 0.0340  225  TYR C CD1 
7556  C  CD2 . TYR C 225 ? 0.3650 0.6779 0.4153 0.0118  -0.0483 0.0264  225  TYR C CD2 
7557  C  CE1 . TYR C 225 ? 0.3069 0.6325 0.3313 0.0186  -0.0583 0.0351  225  TYR C CE1 
7558  C  CE2 . TYR C 225 ? 0.4323 0.7790 0.4857 0.0099  -0.0568 0.0272  225  TYR C CE2 
7559  C  CZ  . TYR C 225 ? 0.4250 0.7774 0.4647 0.0138  -0.0621 0.0314  225  TYR C CZ  
7560  O  OH  . TYR C 225 ? 0.5150 0.9017 0.5563 0.0120  -0.0714 0.0325  225  TYR C OH  
7561  N  N   . PRO C 226 ? 0.2765 0.5258 0.3320 0.0316  -0.0276 0.0374  226  PRO C N   
7562  C  CA  . PRO C 226 ? 0.3425 0.6081 0.4127 0.0358  -0.0243 0.0400  226  PRO C CA  
7563  C  C   . PRO C 226 ? 0.3242 0.6322 0.4095 0.0326  -0.0299 0.0401  226  PRO C C   
7564  O  O   . PRO C 226 ? 0.3180 0.6404 0.4027 0.0215  -0.0362 0.0341  226  PRO C O   
7565  C  CB  . PRO C 226 ? 0.3645 0.6135 0.4370 0.0249  -0.0181 0.0324  226  PRO C CB  
7566  C  CG  . PRO C 226 ? 0.3639 0.5796 0.4213 0.0224  -0.0171 0.0291  226  PRO C CG  
7567  C  CD  . PRO C 226 ? 0.2363 0.4598 0.2862 0.0217  -0.0236 0.0290  226  PRO C CD  
7568  N  N   . TYR C 227 ? 0.2388 0.5684 0.3377 0.0421  -0.0277 0.0462  227  TYR C N   
7569  C  CA  . TYR C 227 ? 0.2483 0.5607 0.3458 0.0564  -0.0199 0.0521  227  TYR C CA  
7570  C  C   . TYR C 227 ? 0.3625 0.6691 0.4515 0.0754  -0.0226 0.0622  227  TYR C C   
7571  O  O   . TYR C 227 ? 0.3222 0.6511 0.4129 0.0791  -0.0304 0.0667  227  TYR C O   
7572  C  CB  . TYR C 227 ? 0.2894 0.6318 0.4065 0.0587  -0.0153 0.0537  227  TYR C CB  
7573  C  CG  . TYR C 227 ? 0.2589 0.6038 0.3842 0.0411  -0.0106 0.0461  227  TYR C CG  
7574  C  CD1 . TYR C 227 ? 0.2435 0.5550 0.3595 0.0382  -0.0028 0.0432  227  TYR C CD1 
7575  C  CD2 . TYR C 227 ? 0.3424 0.7228 0.4841 0.0268  -0.0145 0.0425  227  TYR C CD2 
7576  C  CE1 . TYR C 227 ? 0.2646 0.5762 0.3867 0.0222  0.0013  0.0377  227  TYR C CE1 
7577  C  CE2 . TYR C 227 ? 0.2206 0.6004 0.3688 0.0093  -0.0104 0.0364  227  TYR C CE2 
7578  C  CZ  . TYR C 227 ? 0.3197 0.6642 0.4576 0.0075  -0.0022 0.0345  227  TYR C CZ  
7579  O  OH  . TYR C 227 ? 0.4121 0.7532 0.5546 -0.0096 0.0018  0.0299  227  TYR C OH  
7580  N  N   . ASP C 228 ? 0.3521 0.6282 0.4310 0.0874  -0.0166 0.0659  228  ASP C N   
7581  C  CA  . ASP C 228 ? 0.2170 0.4801 0.2858 0.1061  -0.0184 0.0756  228  ASP C CA  
7582  C  C   . ASP C 228 ? 0.3311 0.6186 0.4126 0.1241  -0.0163 0.0819  228  ASP C C   
7583  O  O   . ASP C 228 ? 0.4450 0.7265 0.5198 0.1415  -0.0190 0.0906  228  ASP C O   
7584  C  CB  . ASP C 228 ? 0.2447 0.4605 0.2945 0.1098  -0.0137 0.0759  228  ASP C CB  
7585  C  CG  . ASP C 228 ? 0.5304 0.7232 0.5660 0.0976  -0.0173 0.0736  228  ASP C CG  
7586  O  OD1 . ASP C 228 ? 0.5540 0.7647 0.5910 0.0900  -0.0236 0.0732  228  ASP C OD1 
7587  O  OD2 . ASP C 228 ? 0.6110 0.7692 0.6339 0.0958  -0.0139 0.0720  228  ASP C OD2 
7588  N  N   . ASN C 229 ? 0.2931 0.6074 0.3925 0.1206  -0.0111 0.0780  229  ASN C N   
7589  C  CA  . ASN C 229 ? 0.4144 0.7600 0.5295 0.1377  -0.0083 0.0836  229  ASN C CA  
7590  C  C   . ASN C 229 ? 0.4449 0.8379 0.5849 0.1260  -0.0076 0.0801  229  ASN C C   
7591  O  O   . ASN C 229 ? 0.3161 0.7138 0.4590 0.1042  -0.0100 0.0730  229  ASN C O   
7592  C  CB  . ASN C 229 ? 0.3450 0.6647 0.4523 0.1534  0.0020  0.0845  229  ASN C CB  
7593  C  CG  . ASN C 229 ? 0.3710 0.6833 0.4804 0.1404  0.0111  0.0767  229  ASN C CG  
7594  O  OD1 . ASN C 229 ? 0.2574 0.5864 0.3767 0.1203  0.0100  0.0713  229  ASN C OD1 
7595  N  ND2 . ASN C 229 ? 0.3245 0.6096 0.4226 0.1515  0.0200  0.0760  229  ASN C ND2 
7596  N  N   . SER C 230 ? 0.5016 0.9285 0.6590 0.1405  -0.0038 0.0848  230  SER C N   
7597  C  CA  . SER C 230 ? 0.2436 0.7228 0.4278 0.1303  -0.0033 0.0834  230  SER C CA  
7598  C  C   . SER C 230 ? 0.2583 0.7651 0.4587 0.1485  0.0060  0.0879  230  SER C C   
7599  O  O   . SER C 230 ? 0.3227 0.8115 0.5138 0.1728  0.0099  0.0928  230  SER C O   
7600  C  CB  . SER C 230 ? 0.1947 0.7124 0.3902 0.1269  -0.0163 0.0867  230  SER C CB  
7601  O  OG  . SER C 230 ? 0.3562 0.8920 0.5566 0.1526  -0.0194 0.0968  230  SER C OG  
7602  N  N   . LEU C 231 ? 0.3475 0.8982 0.5718 0.1366  0.0096  0.0862  231  LEU C N   
7603  C  CA  . LEU C 231 ? 0.4205 1.0095 0.6650 0.1527  0.0188  0.0908  231  LEU C CA  
7604  C  C   . LEU C 231 ? 0.4672 1.0881 0.7231 0.1790  0.0134  0.0999  231  LEU C C   
7605  O  O   . LEU C 231 ? 0.4904 1.1233 0.7529 0.2027  0.0219  0.1041  231  LEU C O   
7606  C  CB  . LEU C 231 ? 0.3751 1.0120 0.6457 0.1312  0.0219  0.0884  231  LEU C CB  
7607  C  CG  . LEU C 231 ? 0.4238 1.0427 0.6903 0.1138  0.0337  0.0828  231  LEU C CG  
7608  C  CD1 . LEU C 231 ? 0.3154 0.9819 0.6075 0.0881  0.0330  0.0814  231  LEU C CD1 
7609  C  CD2 . LEU C 231 ? 0.3622 0.9710 0.6238 0.1350  0.0487  0.0849  231  LEU C CD2 
7610  N  N   . ALA C 232 ? 0.4353 1.0713 0.6934 0.1750  -0.0008 0.1028  232  ALA C N   
7611  C  CA  . ALA C 232 ? 0.3768 1.0404 0.6431 0.1992  -0.0087 0.1126  232  ALA C CA  
7612  C  C   . ALA C 232 ? 0.4872 1.1014 0.7289 0.2264  -0.0060 0.1174  232  ALA C C   
7613  O  O   . ALA C 232 ? 0.3299 0.9593 0.5776 0.2545  -0.0062 0.1256  232  ALA C O   
7614  C  CB  . ALA C 232 ? 0.1448 0.8264 0.4120 0.1856  -0.0251 0.1140  232  ALA C CB  
7615  N  N   . HIS C 233 ? 0.5570 1.1117 0.7712 0.2175  -0.0037 0.1121  233  HIS C N   
7616  C  CA  . HIS C 233 ? 0.5175 1.0181 0.7046 0.2368  -0.0027 0.1156  233  HIS C CA  
7617  C  C   . HIS C 233 ? 0.5367 1.0408 0.7187 0.2532  -0.0148 0.1261  233  HIS C C   
7618  O  O   . HIS C 233 ? 0.5409 1.0330 0.7168 0.2809  -0.0135 0.1332  233  HIS C O   
7619  C  CB  . HIS C 233 ? 0.3232 0.8086 0.5070 0.2585  0.0108  0.1150  233  HIS C CB  
7620  C  CG  . HIS C 233 ? 0.4411 0.9006 0.6165 0.2432  0.0220  0.1054  233  HIS C CG  
7621  N  ND1 . HIS C 233 ? 0.5748 1.0672 0.7688 0.2389  0.0327  0.1018  233  HIS C ND1 
7622  C  CD2 . HIS C 233 ? 0.4730 0.8786 0.6235 0.2308  0.0238  0.0995  233  HIS C CD2 
7623  C  CE1 . HIS C 233 ? 0.5395 0.9973 0.7187 0.2250  0.0405  0.0944  233  HIS C CE1 
7624  N  NE2 . HIS C 233 ? 0.4650 0.8706 0.6183 0.2203  0.0349  0.0927  233  HIS C NE2 
7625  N  N   . ASN C 234 ? 0.5584 1.0774 0.7412 0.2359  -0.0266 0.1268  234  ASN C N   
7626  C  CA  . ASN C 234 ? 0.5789 1.1011 0.7542 0.2475  -0.0392 0.1371  234  ASN C CA  
7627  C  C   . ASN C 234 ? 0.5514 1.0095 0.6938 0.2516  -0.0401 0.1399  234  ASN C C   
7628  O  O   . ASN C 234 ? 0.4918 0.9139 0.6191 0.2332  -0.0365 0.1321  234  ASN C O   
7629  C  CB  . ASN C 234 ? 0.4698 1.0293 0.6545 0.2260  -0.0512 0.1358  234  ASN C CB  
7630  C  CG  . ASN C 234 ? 0.4368 1.0633 0.6549 0.2194  -0.0526 0.1339  234  ASN C CG  
7631  O  OD1 . ASN C 234 ? 0.2984 0.9573 0.5359 0.2391  -0.0488 0.1392  234  ASN C OD1 
7632  N  ND2 . ASN C 234 ? 0.3135 0.9614 0.5384 0.1913  -0.0581 0.1261  234  ASN C ND2 
7633  N  N   . GLU C 235 ? 0.5420 0.9862 0.6735 0.2754  -0.0452 0.1515  235  GLU C N   
7634  C  CA  . GLU C 235 ? 0.5775 0.9629 0.6777 0.2773  -0.0475 0.1560  235  GLU C CA  
7635  C  C   . GLU C 235 ? 0.5994 0.9763 0.6886 0.2495  -0.0536 0.1521  235  GLU C C   
7636  O  O   . GLU C 235 ? 0.3281 0.6623 0.3995 0.2365  -0.0493 0.1464  235  GLU C O   
7637  C  CB  . GLU C 235 ? 0.5350 0.9141 0.6263 0.3038  -0.0551 0.1711  235  GLU C CB  
7638  C  CG  . GLU C 235 ? 0.7341 1.0526 0.7924 0.3041  -0.0583 0.1775  235  GLU C CG  
7639  C  CD  . GLU C 235 ? 0.9988 1.3100 1.0468 0.3290  -0.0671 0.1941  235  GLU C CD  
7640  O  OE1 . GLU C 235 ? 1.1820 1.4375 1.2043 0.3389  -0.0663 0.2001  235  GLU C OE1 
7641  O  OE2 . GLU C 235 ? 0.9030 1.2631 0.9678 0.3384  -0.0754 0.2015  235  GLU C OE2 
7642  N  N   . CYS C 236 ? 0.6391 1.0589 0.7392 0.2407  -0.0636 0.1544  236  CYS C N   
7643  C  CA  . CYS C 236 ? 0.5907 1.0024 0.6767 0.2195  -0.0704 0.1526  236  CYS C CA  
7644  C  C   . CYS C 236 ? 0.5392 1.0044 0.6405 0.2064  -0.0801 0.1506  236  CYS C C   
7645  O  O   . CYS C 236 ? 0.5243 1.0370 0.6491 0.2132  -0.0829 0.1520  236  CYS C O   
7646  C  CB  . CYS C 236 ? 0.7722 1.1530 0.8341 0.2314  -0.0770 0.1660  236  CYS C CB  
7647  S  SG  . CYS C 236 ? 0.6309 1.0600 0.7023 0.2493  -0.0908 0.1808  236  CYS C SG  
7648  N  N   . CYS C 237 ? 0.5646 1.0217 0.6512 0.1878  -0.0853 0.1475  237  CYS C N   
7649  C  CA  . CYS C 237 ? 0.3711 0.8701 0.4627 0.1766  -0.0967 0.1472  237  CYS C CA  
7650  C  C   . CYS C 237 ? 0.3564 0.9029 0.4750 0.1642  -0.0972 0.1371  237  CYS C C   
7651  O  O   . CYS C 237 ? 0.4294 1.0224 0.5597 0.1618  -0.1076 0.1391  237  CYS C O   
7652  C  CB  . CYS C 237 ? 0.5319 1.0488 0.6198 0.1971  -0.1073 0.1637  237  CYS C CB  
7653  S  SG  . CYS C 237 ? 0.7211 1.1825 0.7861 0.2218  -0.1037 0.1785  237  CYS C SG  
7654  N  N   . GLU C 238 ? 0.3517 0.8870 0.4798 0.1555  -0.0865 0.1266  238  GLU C N   
7655  C  CA  . GLU C 238 ? 0.3008 0.8758 0.4528 0.1397  -0.0861 0.1167  238  GLU C CA  
7656  C  C   . GLU C 238 ? 0.4142 0.9602 0.5613 0.1187  -0.0773 0.1029  238  GLU C C   
7657  O  O   . GLU C 238 ? 0.3196 0.8311 0.4618 0.1236  -0.0666 0.1013  238  GLU C O   
7658  C  CB  . GLU C 238 ? 0.4415 1.0485 0.6187 0.1559  -0.0817 0.1216  238  GLU C CB  
7659  C  CG  . GLU C 238 ? 0.6161 1.2882 0.8181 0.1525  -0.0915 0.1234  238  GLU C CG  
7660  C  CD  . GLU C 238 ? 0.8215 1.5263 1.0434 0.1792  -0.0908 0.1346  238  GLU C CD  
7661  O  OE1 . GLU C 238 ? 0.9377 1.7009 1.1860 0.1766  -0.0964 0.1357  238  GLU C OE1 
7662  O  OE2 . GLU C 238 ? 0.7842 1.4565 0.9953 0.2029  -0.0847 0.1422  238  GLU C OE2 
7663  N  N   . GLU C 239 ? 0.5722 1.1314 0.7191 0.0958  -0.0826 0.0928  239  GLU C N   
7664  C  CA  . GLU C 239 ? 0.4854 1.0163 0.6256 0.0756  -0.0760 0.0796  239  GLU C CA  
7665  C  C   . GLU C 239 ? 0.3497 0.8849 0.5078 0.0712  -0.0664 0.0748  239  GLU C C   
7666  O  O   . GLU C 239 ? 0.5192 1.0965 0.6995 0.0666  -0.0685 0.0744  239  GLU C O   
7667  C  CB  . GLU C 239 ? 0.6183 1.1658 0.7552 0.0534  -0.0846 0.0692  239  GLU C CB  
7668  C  CG  . GLU C 239 ? 0.7486 1.2789 0.8609 0.0522  -0.0907 0.0697  239  GLU C CG  
7669  C  CD  . GLU C 239 ? 0.8969 1.4401 1.0038 0.0304  -0.0977 0.0569  239  GLU C CD  
7670  O  OE1 . GLU C 239 ? 0.8818 1.3994 0.9675 0.0243  -0.0975 0.0516  239  GLU C OE1 
7671  O  OE2 . GLU C 239 ? 0.9085 1.4877 1.0320 0.0190  -0.1033 0.0517  239  GLU C OE2 
7672  N  N   . SER C 240 ? 0.3014 0.7947 0.4499 0.0721  -0.0559 0.0719  240  SER C N   
7673  C  CA  . SER C 240 ? 0.0876 0.5791 0.2482 0.0635  -0.0464 0.0660  240  SER C CA  
7674  C  C   . SER C 240 ? 0.3839 0.8473 0.5337 0.0421  -0.0446 0.0541  240  SER C C   
7675  O  O   . SER C 240 ? 0.4938 0.9159 0.6295 0.0431  -0.0377 0.0519  240  SER C O   
7676  C  CB  . SER C 240 ? 0.1258 0.5910 0.2826 0.0812  -0.0356 0.0713  240  SER C CB  
7677  O  OG  . SER C 240 ? 0.0941 0.5595 0.2613 0.0727  -0.0262 0.0663  240  SER C OG  
7678  N  N   . LEU C 241 ? 0.4815 0.9670 0.6375 0.0229  -0.0512 0.0463  241  LEU C N   
7679  C  CA  . LEU C 241 ? 0.3569 0.8146 0.4997 0.0044  -0.0514 0.0345  241  LEU C CA  
7680  C  C   . LEU C 241 ? 0.2959 0.7334 0.4424 -0.0076 -0.0424 0.0282  241  LEU C C   
7681  O  O   . LEU C 241 ? 0.3449 0.7999 0.5077 -0.0074 -0.0369 0.0315  241  LEU C O   
7682  C  CB  . LEU C 241 ? 0.3170 0.8007 0.4606 -0.0114 -0.0624 0.0272  241  LEU C CB  
7683  C  CG  . LEU C 241 ? 0.3569 0.8542 0.4904 -0.0014 -0.0718 0.0326  241  LEU C CG  
7684  C  CD1 . LEU C 241 ? 0.1896 0.7144 0.3224 -0.0180 -0.0833 0.0242  241  LEU C CD1 
7685  C  CD2 . LEU C 241 ? 0.0960 0.5519 0.2062 0.0075  -0.0685 0.0342  241  LEU C CD2 
7686  N  N   . THR C 242 ? 0.4687 0.8705 0.5996 -0.0175 -0.0410 0.0195  242  THR C N   
7687  C  CA  . THR C 242 ? 0.4413 0.8158 0.5708 -0.0278 -0.0332 0.0140  242  THR C CA  
7688  C  C   . THR C 242 ? 0.4316 0.8108 0.5640 -0.0509 -0.0374 0.0030  242  THR C C   
7689  O  O   . THR C 242 ? 0.4092 0.7983 0.5363 -0.0584 -0.0460 -0.0035 242  THR C O   
7690  C  CB  . THR C 242 ? 0.4851 0.8139 0.5949 -0.0214 -0.0289 0.0125  242  THR C CB  
7691  O  OG1 . THR C 242 ? 0.4197 0.7325 0.5291 -0.0085 -0.0205 0.0199  242  THR C OG1 
7692  C  CG2 . THR C 242 ? 0.4334 0.7353 0.5351 -0.0369 -0.0278 0.0017  242  THR C CG2 
7693  N  N   . PRO C 243 ? 0.3950 0.7656 0.5340 -0.0628 -0.0314 0.0008  243  PRO C N   
7694  C  CA  . PRO C 243 ? 0.3254 0.6926 0.4643 -0.0857 -0.0354 -0.0099 243  PRO C CA  
7695  C  C   . PRO C 243 ? 0.3498 0.6860 0.4683 -0.0892 -0.0398 -0.0206 243  PRO C C   
7696  O  O   . PRO C 243 ? 0.3058 0.6452 0.4208 -0.1044 -0.0467 -0.0307 243  PRO C O   
7697  C  CB  . PRO C 243 ? 0.1925 0.5386 0.3342 -0.0936 -0.0262 -0.0088 243  PRO C CB  
7698  C  CG  . PRO C 243 ? 0.3645 0.7238 0.5156 -0.0773 -0.0183 0.0029  243  PRO C CG  
7699  C  CD  . PRO C 243 ? 0.4623 0.8215 0.6057 -0.0562 -0.0207 0.0075  243  PRO C CD  
7700  N  N   . ASP C 244 ? 0.4211 0.7279 0.5260 -0.0750 -0.0356 -0.0186 244  ASP C N   
7701  C  CA  . ASP C 244 ? 0.3853 0.6649 0.4720 -0.0758 -0.0380 -0.0278 244  ASP C CA  
7702  C  C   . ASP C 244 ? 0.3991 0.6933 0.4787 -0.0643 -0.0431 -0.0252 244  ASP C C   
7703  O  O   . ASP C 244 ? 0.3803 0.6531 0.4461 -0.0561 -0.0415 -0.0262 244  ASP C O   
7704  C  CB  . ASP C 244 ? 0.3071 0.5462 0.3839 -0.0693 -0.0303 -0.0272 244  ASP C CB  
7705  C  CG  . ASP C 244 ? 0.5254 0.7402 0.6013 -0.0834 -0.0273 -0.0336 244  ASP C CG  
7706  O  OD1 . ASP C 244 ? 0.6031 0.8029 0.6698 -0.0933 -0.0311 -0.0450 244  ASP C OD1 
7707  O  OD2 . ASP C 244 ? 0.5129 0.7224 0.5957 -0.0841 -0.0212 -0.0272 244  ASP C OD2 
7708  N  N   . ASP C 245 ? 0.2578 0.5901 0.3471 -0.0640 -0.0494 -0.0210 245  ASP C N   
7709  C  CA  . ASP C 245 ? 0.3365 0.6834 0.4180 -0.0529 -0.0548 -0.0167 245  ASP C CA  
7710  C  C   . ASP C 245 ? 0.4100 0.7448 0.4730 -0.0579 -0.0589 -0.0273 245  ASP C C   
7711  O  O   . ASP C 245 ? 0.4033 0.7288 0.4540 -0.0471 -0.0580 -0.0237 245  ASP C O   
7712  C  CB  . ASP C 245 ? 0.2851 0.6770 0.3800 -0.0517 -0.0622 -0.0104 245  ASP C CB  
7713  C  CG  . ASP C 245 ? 0.5183 0.9214 0.6063 -0.0350 -0.0657 -0.0003 245  ASP C CG  
7714  O  OD1 . ASP C 245 ? 0.6425 1.0274 0.7275 -0.0201 -0.0595 0.0088  245  ASP C OD1 
7715  O  OD2 . ASP C 245 ? 0.5605 0.9889 0.6448 -0.0372 -0.0749 -0.0013 245  ASP C OD2 
7716  N  N   . ARG C 246 ? 0.3493 0.6847 0.4097 -0.0744 -0.0633 -0.0403 246  ARG C N   
7717  C  CA  . ARG C 246 ? 0.3747 0.6957 0.4159 -0.0786 -0.0660 -0.0525 246  ARG C CA  
7718  C  C   . ARG C 246 ? 0.4272 0.7121 0.4566 -0.0688 -0.0578 -0.0530 246  ARG C C   
7719  O  O   . ARG C 246 ? 0.5279 0.8114 0.5447 -0.0601 -0.0576 -0.0519 246  ARG C O   
7720  C  CB  . ARG C 246 ? 0.3452 0.6599 0.3838 -0.0980 -0.0701 -0.0679 246  ARG C CB  
7721  C  CG  . ARG C 246 ? 0.4349 0.7855 0.4866 -0.1113 -0.0787 -0.0684 246  ARG C CG  
7722  C  CD  . ARG C 246 ? 0.6798 1.0151 0.7305 -0.1326 -0.0809 -0.0823 246  ARG C CD  
7723  N  NE  . ARG C 246 ? 0.8159 1.1531 0.8502 -0.1436 -0.0895 -0.0974 246  ARG C NE  
7724  C  CZ  . ARG C 246 ? 1.0010 1.3171 1.0272 -0.1614 -0.0923 -0.1125 246  ARG C CZ  
7725  N  NH1 . ARG C 246 ? 1.0152 1.3066 1.0487 -0.1706 -0.0872 -0.1132 246  ARG C NH1 
7726  N  NH2 . ARG C 246 ? 1.1293 1.4472 1.1383 -0.1700 -0.1004 -0.1269 246  ARG C NH2 
7727  N  N   . VAL C 247 ? 0.3016 0.5590 0.3349 -0.0705 -0.0511 -0.0541 247  VAL C N   
7728  C  CA  . VAL C 247 ? 0.3750 0.6012 0.3992 -0.0612 -0.0441 -0.0541 247  VAL C CA  
7729  C  C   . VAL C 247 ? 0.3718 0.6026 0.3951 -0.0459 -0.0415 -0.0409 247  VAL C C   
7730  O  O   . VAL C 247 ? 0.4389 0.6597 0.4510 -0.0392 -0.0395 -0.0414 247  VAL C O   
7731  C  CB  . VAL C 247 ? 0.4062 0.6045 0.4356 -0.0642 -0.0381 -0.0545 247  VAL C CB  
7732  C  CG1 . VAL C 247 ? 0.4053 0.5786 0.4283 -0.0524 -0.0319 -0.0506 247  VAL C CG1 
7733  C  CG2 . VAL C 247 ? 0.4488 0.6307 0.4733 -0.0785 -0.0401 -0.0687 247  VAL C CG2 
7734  N  N   . PHE C 248 ? 0.4235 0.6693 0.4585 -0.0405 -0.0413 -0.0291 248  PHE C N   
7735  C  CA  . PHE C 248 ? 0.3682 0.6158 0.4012 -0.0263 -0.0396 -0.0163 248  PHE C CA  
7736  C  C   . PHE C 248 ? 0.3440 0.6086 0.3668 -0.0222 -0.0447 -0.0138 248  PHE C C   
7737  O  O   . PHE C 248 ? 0.3694 0.6242 0.3834 -0.0137 -0.0424 -0.0074 248  PHE C O   
7738  C  CB  . PHE C 248 ? 0.2595 0.5203 0.3059 -0.0201 -0.0387 -0.0054 248  PHE C CB  
7739  C  CG  . PHE C 248 ? 0.3967 0.6334 0.4467 -0.0166 -0.0312 -0.0022 248  PHE C CG  
7740  C  CD1 . PHE C 248 ? 0.4447 0.6564 0.4855 -0.0081 -0.0271 0.0022  248  PHE C CD1 
7741  C  CD2 . PHE C 248 ? 0.3011 0.5406 0.3628 -0.0230 -0.0283 -0.0034 248  PHE C CD2 
7742  C  CE1 . PHE C 248 ? 0.4388 0.6282 0.4809 -0.0051 -0.0210 0.0049  248  PHE C CE1 
7743  C  CE2 . PHE C 248 ? 0.2386 0.4556 0.3010 -0.0196 -0.0213 -0.0001 248  PHE C CE2 
7744  C  CZ  . PHE C 248 ? 0.2116 0.4032 0.2636 -0.0104 -0.0180 0.0037  248  PHE C CZ  
7745  N  N   . LYS C 249 ? 0.1832 0.4739 0.2066 -0.0291 -0.0519 -0.0185 249  LYS C N   
7746  C  CA  . LYS C 249 ? 0.2568 0.5644 0.2677 -0.0269 -0.0573 -0.0175 249  LYS C CA  
7747  C  C   . LYS C 249 ? 0.3782 0.6687 0.3727 -0.0294 -0.0544 -0.0274 249  LYS C C   
7748  O  O   . LYS C 249 ? 0.4080 0.7003 0.3909 -0.0230 -0.0538 -0.0221 249  LYS C O   
7749  C  CB  . LYS C 249 ? 0.2742 0.6152 0.2890 -0.0350 -0.0668 -0.0213 249  LYS C CB  
7750  C  CG  . LYS C 249 ? 0.2449 0.6140 0.2686 -0.0256 -0.0719 -0.0067 249  LYS C CG  
7751  C  CD  . LYS C 249 ? 0.3280 0.7327 0.3627 -0.0345 -0.0810 -0.0098 249  LYS C CD  
7752  C  CE  . LYS C 249 ? 0.4109 0.8449 0.4552 -0.0218 -0.0860 0.0059  249  LYS C CE  
7753  N  NZ  . LYS C 249 ? 0.4388 0.9104 0.5017 -0.0283 -0.0932 0.0057  249  LYS C NZ  
7754  N  N   . GLN C 250 ? 0.3255 0.5993 0.3190 -0.0382 -0.0522 -0.0414 250  GLN C N   
7755  C  CA  . GLN C 250 ? 0.3753 0.6318 0.3546 -0.0380 -0.0482 -0.0514 250  GLN C CA  
7756  C  C   . GLN C 250 ? 0.4081 0.6468 0.3861 -0.0276 -0.0409 -0.0427 250  GLN C C   
7757  O  O   . GLN C 250 ? 0.3660 0.6069 0.3327 -0.0233 -0.0389 -0.0420 250  GLN C O   
7758  C  CB  . GLN C 250 ? 0.3683 0.6051 0.3469 -0.0475 -0.0471 -0.0673 250  GLN C CB  
7759  C  CG  . GLN C 250 ? 0.3798 0.5989 0.3441 -0.0449 -0.0426 -0.0786 250  GLN C CG  
7760  C  CD  . GLN C 250 ? 0.5451 0.7472 0.5036 -0.0547 -0.0439 -0.0966 250  GLN C CD  
7761  O  OE1 . GLN C 250 ? 0.6548 0.8679 0.6125 -0.0660 -0.0507 -0.1037 250  GLN C OE1 
7762  N  NE2 . GLN C 250 ? 0.5764 0.7512 0.5305 -0.0503 -0.0379 -0.1039 250  GLN C NE2 
7763  N  N   . LEU C 251 ? 0.3137 0.5366 0.3029 -0.0245 -0.0372 -0.0360 251  LEU C N   
7764  C  CA  . LEU C 251 ? 0.3351 0.5412 0.3239 -0.0160 -0.0315 -0.0271 251  LEU C CA  
7765  C  C   . LEU C 251 ? 0.3760 0.5947 0.3589 -0.0091 -0.0327 -0.0142 251  LEU C C   
7766  O  O   . LEU C 251 ? 0.4899 0.7052 0.4642 -0.0062 -0.0297 -0.0123 251  LEU C O   
7767  C  CB  . LEU C 251 ? 0.4584 0.6494 0.4588 -0.0142 -0.0288 -0.0212 251  LEU C CB  
7768  C  CG  . LEU C 251 ? 0.5396 0.7056 0.5437 -0.0173 -0.0246 -0.0280 251  LEU C CG  
7769  C  CD1 . LEU C 251 ? 0.3846 0.5407 0.3815 -0.0218 -0.0239 -0.0423 251  LEU C CD1 
7770  C  CD2 . LEU C 251 ? 0.3691 0.5335 0.3841 -0.0219 -0.0246 -0.0268 251  LEU C CD2 
7771  N  N   . ALA C 252 ? 0.3356 0.5690 0.3232 -0.0062 -0.0370 -0.0048 252  ALA C N   
7772  C  CA  . ALA C 252 ? 0.4090 0.6516 0.3901 0.0009  -0.0390 0.0087  252  ALA C CA  
7773  C  C   . ALA C 252 ? 0.5058 0.7625 0.4724 -0.0013 -0.0408 0.0062  252  ALA C C   
7774  O  O   . ALA C 252 ? 0.4738 0.7280 0.4313 0.0024  -0.0389 0.0153  252  ALA C O   
7775  C  CB  . ALA C 252 ? 0.3852 0.6459 0.3739 0.0051  -0.0445 0.0170  252  ALA C CB  
7776  N  N   . HIS C 253 ? 0.4170 0.6883 0.3804 -0.0083 -0.0443 -0.0061 253  HIS C N   
7777  C  CA  . HIS C 253 ? 0.3696 0.6553 0.3170 -0.0106 -0.0457 -0.0105 253  HIS C CA  
7778  C  C   . HIS C 253 ? 0.4823 0.7536 0.4225 -0.0104 -0.0380 -0.0168 253  HIS C C   
7779  O  O   . HIS C 253 ? 0.5637 0.8435 0.4915 -0.0088 -0.0360 -0.0129 253  HIS C O   
7780  C  CB  . HIS C 253 ? 0.3398 0.6433 0.2836 -0.0188 -0.0520 -0.0237 253  HIS C CB  
7781  C  CG  . HIS C 253 ? 0.4411 0.7721 0.3839 -0.0182 -0.0610 -0.0154 253  HIS C CG  
7782  N  ND1 . HIS C 253 ? 0.3583 0.7032 0.3139 -0.0222 -0.0675 -0.0167 253  HIS C ND1 
7783  C  CD2 . HIS C 253 ? 0.4512 0.7994 0.3822 -0.0137 -0.0648 -0.0044 253  HIS C CD2 
7784  C  CE1 . HIS C 253 ? 0.4180 0.7892 0.3707 -0.0191 -0.0754 -0.0075 253  HIS C CE1 
7785  N  NE2 . HIS C 253 ? 0.5992 0.9712 0.5360 -0.0137 -0.0741 0.0004  253  HIS C NE2 
7786  N  N   . THR C 254 ? 0.4139 0.6648 0.3622 -0.0117 -0.0335 -0.0257 254  THR C N   
7787  C  CA  . THR C 254 ? 0.3768 0.6153 0.3211 -0.0098 -0.0264 -0.0315 254  THR C CA  
7788  C  C   . THR C 254 ? 0.4172 0.6556 0.3597 -0.0049 -0.0229 -0.0166 254  THR C C   
7789  O  O   . THR C 254 ? 0.5202 0.7660 0.4537 -0.0041 -0.0187 -0.0171 254  THR C O   
7790  C  CB  . THR C 254 ? 0.4022 0.6163 0.3570 -0.0100 -0.0228 -0.0391 254  THR C CB  
7791  O  OG1 . THR C 254 ? 0.4547 0.6658 0.4119 -0.0164 -0.0266 -0.0509 254  THR C OG1 
7792  C  CG2 . THR C 254 ? 0.3398 0.5458 0.2903 -0.0067 -0.0163 -0.0469 254  THR C CG2 
7793  N  N   . TYR C 255 ? 0.3147 0.5445 0.2648 -0.0022 -0.0245 -0.0035 255  TYR C N   
7794  C  CA  . TYR C 255 ? 0.3406 0.5657 0.2878 0.0009  -0.0221 0.0110  255  TYR C CA  
7795  C  C   . TYR C 255 ? 0.3224 0.5657 0.2567 0.0012  -0.0247 0.0213  255  TYR C C   
7796  O  O   . TYR C 255 ? 0.4128 0.6599 0.3392 0.0002  -0.0210 0.0272  255  TYR C O   
7797  C  CB  . TYR C 255 ? 0.1665 0.3737 0.1225 0.0043  -0.0231 0.0209  255  TYR C CB  
7798  C  CG  . TYR C 255 ? 0.4292 0.6241 0.3825 0.0052  -0.0199 0.0320  255  TYR C CG  
7799  C  CD1 . TYR C 255 ? 0.5252 0.7250 0.4688 0.0058  -0.0215 0.0458  255  TYR C CD1 
7800  C  CD2 . TYR C 255 ? 0.3524 0.5307 0.3123 0.0046  -0.0159 0.0291  255  TYR C CD2 
7801  C  CE1 . TYR C 255 ? 0.5493 0.7366 0.4901 0.0042  -0.0190 0.0562  255  TYR C CE1 
7802  C  CE2 . TYR C 255 ? 0.4359 0.6047 0.3939 0.0034  -0.0139 0.0390  255  TYR C CE2 
7803  C  CZ  . TYR C 255 ? 0.3922 0.5650 0.3406 0.0025  -0.0154 0.0523  255  TYR C CZ  
7804  O  OH  . TYR C 255 ? 0.4289 0.5908 0.3750 -0.0009 -0.0139 0.0622  255  TYR C OH  
7805  N  N   . SER C 256 ? 0.3447 0.6005 0.2771 0.0022  -0.0313 0.0244  256  SER C N   
7806  C  CA  . SER C 256 ? 0.4062 0.6783 0.3258 0.0035  -0.0351 0.0360  256  SER C CA  
7807  C  C   . SER C 256 ? 0.5279 0.8188 0.4332 -0.0007 -0.0332 0.0282  256  SER C C   
7808  O  O   . SER C 256 ? 0.5415 0.8388 0.4349 -0.0013 -0.0307 0.0376  256  SER C O   
7809  C  CB  . SER C 256 ? 0.3293 0.6134 0.2518 0.0068  -0.0434 0.0406  256  SER C CB  
7810  O  OG  . SER C 256 ? 0.5649 0.8616 0.4744 0.0098  -0.0478 0.0546  256  SER C OG  
7811  N  N   . ASP C 257 ? 0.5098 0.8085 0.4152 -0.0042 -0.0342 0.0110  257  ASP C N   
7812  C  CA  . ASP C 257 ? 0.4729 0.7886 0.3627 -0.0074 -0.0325 0.0006  257  ASP C CA  
7813  C  C   . ASP C 257 ? 0.5200 0.8333 0.4045 -0.0068 -0.0231 0.0013  257  ASP C C   
7814  O  O   . ASP C 257 ? 0.6312 0.9618 0.5000 -0.0080 -0.0205 0.0010  257  ASP C O   
7815  C  CB  . ASP C 257 ? 0.4494 0.7644 0.3407 -0.0115 -0.0339 -0.0204 257  ASP C CB  
7816  C  CG  . ASP C 257 ? 0.6842 1.0125 0.5764 -0.0150 -0.0440 -0.0229 257  ASP C CG  
7817  O  OD1 . ASP C 257 ? 0.8021 1.1428 0.6939 -0.0126 -0.0500 -0.0083 257  ASP C OD1 
7818  O  OD2 . ASP C 257 ? 0.8003 1.1267 0.6935 -0.0205 -0.0462 -0.0395 257  ASP C OD2 
7819  N  N   . ASN C 258 ? 0.4432 0.7373 0.3409 -0.0051 -0.0179 0.0022  258  ASN C N   
7820  C  CA  . ASN C 258 ? 0.4141 0.7082 0.3110 -0.0047 -0.0093 0.0037  258  ASN C CA  
7821  C  C   . ASN C 258 ? 0.3748 0.6663 0.2711 -0.0057 -0.0080 0.0239  258  ASN C C   
7822  O  O   . ASN C 258 ? 0.4363 0.7270 0.3359 -0.0068 -0.0014 0.0271  258  ASN C O   
7823  C  CB  . ASN C 258 ? 0.4064 0.6828 0.3174 -0.0026 -0.0050 -0.0072 258  ASN C CB  
7824  C  CG  . ASN C 258 ? 0.5895 0.8680 0.4968 -0.0016 -0.0031 -0.0280 258  ASN C CG  
7825  O  OD1 . ASN C 258 ? 0.5989 0.8906 0.4971 0.0001  0.0028  -0.0356 258  ASN C OD1 
7826  N  ND2 . ASN C 258 ? 0.5038 0.7688 0.4174 -0.0027 -0.0079 -0.0373 258  ASN C ND2 
7827  N  N   . HIS C 259 ? 0.5069 0.7966 0.3992 -0.0053 -0.0145 0.0376  259  HIS C N   
7828  C  CA  . HIS C 259 ? 0.5515 0.8325 0.4411 -0.0065 -0.0144 0.0572  259  HIS C CA  
7829  C  C   . HIS C 259 ? 0.5720 0.8695 0.4438 -0.0075 -0.0177 0.0691  259  HIS C C   
7830  O  O   . HIS C 259 ? 0.6326 0.9321 0.5007 -0.0040 -0.0254 0.0740  259  HIS C O   
7831  C  CB  . HIS C 259 ? 0.6977 0.9550 0.5980 -0.0028 -0.0192 0.0640  259  HIS C CB  
7832  C  CG  . HIS C 259 ? 0.6528 0.8937 0.5500 -0.0040 -0.0193 0.0822  259  HIS C CG  
7833  N  ND1 . HIS C 259 ? 0.6300 0.8751 0.5126 -0.0048 -0.0221 0.0982  259  HIS C ND1 
7834  C  CD2 . HIS C 259 ? 0.5060 0.7239 0.4111 -0.0051 -0.0176 0.0868  259  HIS C CD2 
7835  C  CE1 . HIS C 259 ? 0.5413 0.7646 0.4229 -0.0067 -0.0218 0.1117  259  HIS C CE1 
7836  N  NE2 . HIS C 259 ? 0.4326 0.6398 0.3277 -0.0073 -0.0193 0.1046  259  HIS C NE2 
7837  N  N   . PRO C 260 ? 0.6812 0.9921 0.5418 -0.0122 -0.0118 0.0747  260  PRO C N   
7838  C  CA  . PRO C 260 ? 0.7133 1.0440 0.5536 -0.0143 -0.0130 0.0845  260  PRO C CA  
7839  C  C   . PRO C 260 ? 0.6612 0.9839 0.4937 -0.0115 -0.0219 0.1023  260  PRO C C   
7840  O  O   . PRO C 260 ? 0.6218 0.9622 0.4378 -0.0110 -0.0262 0.1076  260  PRO C O   
7841  C  CB  . PRO C 260 ? 0.6987 1.0354 0.5342 -0.0210 -0.0041 0.0936  260  PRO C CB  
7842  C  CG  . PRO C 260 ? 0.7338 1.0648 0.5869 -0.0210 0.0026  0.0804  260  PRO C CG  
7843  C  CD  . PRO C 260 ? 0.6301 0.9370 0.4985 -0.0161 -0.0034 0.0750  260  PRO C CD  
7844  N  N   . ILE C 261 ? 0.5822 0.8786 0.4251 -0.0087 -0.0248 0.1113  261  ILE C N   
7845  C  CA  . ILE C 261 ? 0.6585 0.9430 0.4940 -0.0040 -0.0325 0.1292  261  ILE C CA  
7846  C  C   . ILE C 261 ? 0.5405 0.8196 0.3877 0.0049  -0.0398 0.1234  261  ILE C C   
7847  O  O   . ILE C 261 ? 0.5522 0.8396 0.3931 0.0110  -0.0476 0.1308  261  ILE C O   
7848  C  CB  . ILE C 261 ? 0.6641 0.9205 0.4994 -0.0069 -0.0305 0.1451  261  ILE C CB  
7849  C  CG1 . ILE C 261 ? 0.6435 0.9088 0.4652 -0.0172 -0.0243 0.1555  261  ILE C CG1 
7850  C  CG2 . ILE C 261 ? 0.6083 0.8457 0.4378 0.0013  -0.0388 0.1609  261  ILE C CG2 
7851  C  CD1 . ILE C 261 ? 0.7889 1.0275 0.6115 -0.0238 -0.0219 0.1690  261  ILE C CD1 
7852  N  N   . MET C 262 ? 0.4352 0.7023 0.3000 0.0058  -0.0372 0.1108  262  MET C N   
7853  C  CA  . MET C 262 ? 0.5690 0.8330 0.4465 0.0130  -0.0427 0.1048  262  MET C CA  
7854  C  C   . MET C 262 ? 0.5630 0.8555 0.4384 0.0135  -0.0481 0.0950  262  MET C C   
7855  O  O   . MET C 262 ? 0.6297 0.9294 0.5097 0.0198  -0.0554 0.0976  262  MET C O   
7856  C  CB  . MET C 262 ? 0.3622 0.6100 0.2567 0.0121  -0.0381 0.0924  262  MET C CB  
7857  C  CG  . MET C 262 ? 0.1804 0.4243 0.0889 0.0184  -0.0421 0.0868  262  MET C CG  
7858  S  SD  . MET C 262 ? 0.4278 0.6501 0.3525 0.0163  -0.0359 0.0745  262  MET C SD  
7859  C  CE  . MET C 262 ? 0.2455 0.4380 0.1657 0.0168  -0.0331 0.0893  262  MET C CE  
7860  N  N   . ARG C 263 ? 0.5627 0.8719 0.4310 0.0069  -0.0444 0.0834  263  ARG C N   
7861  C  CA  . ARG C 263 ? 0.5226 0.8571 0.3860 0.0049  -0.0490 0.0710  263  ARG C CA  
7862  C  C   . ARG C 263 ? 0.5648 0.9181 0.4152 0.0084  -0.0582 0.0833  263  ARG C C   
7863  O  O   . ARG C 263 ? 0.6603 1.0350 0.5089 0.0075  -0.0650 0.0749  263  ARG C O   
7864  C  CB  . ARG C 263 ? 0.6822 1.0275 0.5351 -0.0015 -0.0420 0.0585  263  ARG C CB  
7865  C  CG  . ARG C 263 ? 0.8302 1.1976 0.6746 -0.0049 -0.0457 0.0422  263  ARG C CG  
7866  C  CD  . ARG C 263 ? 0.9223 1.2955 0.7568 -0.0089 -0.0366 0.0289  263  ARG C CD  
7867  N  NE  . ARG C 263 ? 0.9080 1.2885 0.7280 -0.0099 -0.0308 0.0423  263  ARG C NE  
7868  C  CZ  . ARG C 263 ? 0.7876 1.1659 0.6076 -0.0116 -0.0203 0.0395  263  ARG C CZ  
7869  N  NH1 . ARG C 263 ? 0.6958 1.0634 0.5289 -0.0108 -0.0148 0.0239  263  ARG C NH1 
7870  N  NH2 . ARG C 263 ? 0.7787 1.1667 0.5858 -0.0141 -0.0152 0.0532  263  ARG C NH2 
7871  N  N   . LYS C 264 ? 0.7013 1.0461 0.5422 0.0120  -0.0590 0.1035  264  LYS C N   
7872  C  CA  . LYS C 264 ? 0.8161 1.1772 0.6419 0.0163  -0.0677 0.1178  264  LYS C CA  
7873  C  C   . LYS C 264 ? 0.7178 1.0805 0.5551 0.0264  -0.0772 0.1240  264  LYS C C   
7874  O  O   . LYS C 264 ? 0.7012 1.0894 0.5352 0.0286  -0.0862 0.1234  264  LYS C O   
7875  C  CB  . LYS C 264 ? 0.8017 1.1512 0.6102 0.0157  -0.0649 0.1382  264  LYS C CB  
7876  C  CG  . LYS C 264 ? 0.8156 1.1696 0.6136 0.0056  -0.0547 0.1334  264  LYS C CG  
7877  C  CD  . LYS C 264 ? 0.8978 1.2435 0.6783 0.0025  -0.0520 0.1549  264  LYS C CD  
7878  C  CE  . LYS C 264 ? 1.0154 1.3768 0.7841 -0.0074 -0.0421 0.1499  264  LYS C CE  
7879  N  NZ  . LYS C 264 ? 1.1606 1.5540 0.9161 -0.0087 -0.0440 0.1374  264  LYS C NZ  
7880  N  N   . GLY C 265 ? 0.6861 1.0232 0.5368 0.0328  -0.0753 0.1300  265  GLY C N   
7881  C  CA  . GLY C 265 ? 0.5256 0.8646 0.3905 0.0437  -0.0822 0.1339  265  GLY C CA  
7882  C  C   . GLY C 265 ? 0.5726 0.9013 0.4292 0.0559  -0.0879 0.1560  265  GLY C C   
7883  O  O   . GLY C 265 ? 0.6238 0.9546 0.4923 0.0676  -0.0933 0.1603  265  GLY C O   
7884  N  N   . ASN C 266 ? 0.4880 0.8053 0.3243 0.0536  -0.0865 0.1702  266  ASN C N   
7885  C  CA  . ASN C 266 ? 0.6415 0.9461 0.4657 0.0647  -0.0926 0.1926  266  ASN C CA  
7886  C  C   . ASN C 266 ? 0.7021 0.9656 0.5174 0.0636  -0.0866 0.2055  266  ASN C C   
7887  O  O   . ASN C 266 ? 0.6835 0.9347 0.4795 0.0653  -0.0893 0.2245  266  ASN C O   
7888  C  CB  . ASN C 266 ? 0.6914 1.0214 0.4948 0.0633  -0.0994 0.2025  266  ASN C CB  
7889  C  CG  . ASN C 266 ? 0.9364 1.2750 0.7249 0.0479  -0.0924 0.1966  266  ASN C CG  
7890  O  OD1 . ASN C 266 ? 0.9813 1.3071 0.7765 0.0389  -0.0826 0.1858  266  ASN C OD1 
7891  N  ND2 . ASN C 266 ? 0.9067 1.2687 0.6748 0.0455  -0.0973 0.2037  266  ASN C ND2 
7892  N  N   . ASN C 267 ? 0.6174 0.8591 0.4462 0.0602  -0.0793 0.1953  267  ASN C N   
7893  C  CA  . ASN C 267 ? 0.6078 0.8109 0.4300 0.0565  -0.0738 0.2044  267  ASN C CA  
7894  C  C   . ASN C 267 ? 0.5802 0.7519 0.4053 0.0710  -0.0770 0.2138  267  ASN C C   
7895  O  O   . ASN C 267 ? 0.5110 0.6925 0.3497 0.0835  -0.0809 0.2090  267  ASN C O   
7896  C  CB  . ASN C 267 ? 0.6375 0.8345 0.4713 0.0447  -0.0646 0.1883  267  ASN C CB  
7897  C  CG  . ASN C 267 ? 0.6680 0.8980 0.5038 0.0346  -0.0613 0.1736  267  ASN C CG  
7898  O  OD1 . ASN C 267 ? 0.5241 0.7698 0.3445 0.0279  -0.0607 0.1791  267  ASN C OD1 
7899  N  ND2 . ASN C 267 ? 0.6416 0.8813 0.4950 0.0337  -0.0590 0.1547  267  ASN C ND2 
7900  N  N   . CYS C 268 ? 0.6770 0.8114 0.4889 0.0688  -0.0751 0.2270  268  CYS C N   
7901  C  CA  . CYS C 268 ? 0.7360 0.8324 0.5453 0.0823  -0.0777 0.2365  268  CYS C CA  
7902  C  C   . CYS C 268 ? 0.8022 0.9090 0.6144 0.1031  -0.0859 0.2433  268  CYS C C   
7903  O  O   . CYS C 268 ? 0.8275 0.9191 0.6496 0.1170  -0.0862 0.2403  268  CYS C O   
7904  C  CB  . CYS C 268 ? 0.5857 0.6594 0.4090 0.0811  -0.0717 0.2232  268  CYS C CB  
7905  S  SG  . CYS C 268 ? 0.8770 0.9718 0.7159 0.0633  -0.0634 0.2019  268  CYS C SG  
7906  N  N   . ASN C 269 ? 0.9006 1.0345 0.7038 0.1059  -0.0925 0.2525  269  ASN C N   
7907  C  CA  . ASN C 269 ? 0.9670 1.1167 0.7739 0.1260  -0.1015 0.2600  269  ASN C CA  
7908  C  C   . ASN C 269 ? 0.9169 1.1015 0.7500 0.1318  -0.1020 0.2426  269  ASN C C   
7909  O  O   . ASN C 269 ? 0.8710 1.0728 0.7128 0.1489  -0.1087 0.2468  269  ASN C O   
7910  C  CB  . ASN C 269 ? 0.9712 1.0779 0.7695 0.1433  -0.1040 0.2747  269  ASN C CB  
7911  C  CG  . ASN C 269 ? 1.1150 1.1899 0.8848 0.1398  -0.1066 0.2962  269  ASN C CG  
7912  O  OD1 . ASN C 269 ? 1.1824 1.2106 0.9409 0.1466  -0.1064 0.3063  269  ASN C OD1 
7913  N  ND2 . ASN C 269 ? 1.1316 1.2307 0.8884 0.1285  -0.1090 0.3032  269  ASN C ND2 
7914  N  N   . ASP C 270 ? 0.8597 1.0551 0.7056 0.1175  -0.0950 0.2239  270  ASP C N   
7915  C  CA  . ASP C 270 ? 0.7176 0.9441 0.5872 0.1189  -0.0948 0.2069  270  ASP C CA  
7916  C  C   . ASP C 270 ? 0.8040 1.0740 0.6748 0.1089  -0.0989 0.1991  270  ASP C C   
7917  O  O   . ASP C 270 ? 0.7301 1.0040 0.5855 0.0964  -0.0977 0.2001  270  ASP C O   
7918  C  CB  . ASP C 270 ? 0.6751 0.8853 0.5571 0.1094  -0.0852 0.1907  270  ASP C CB  
7919  C  CG  . ASP C 270 ? 0.7128 0.8798 0.5929 0.1180  -0.0811 0.1956  270  ASP C CG  
7920  O  OD1 . ASP C 270 ? 0.8716 1.0269 0.7481 0.1354  -0.0855 0.2076  270  ASP C OD1 
7921  O  OD2 . ASP C 270 ? 0.7383 0.8829 0.6196 0.1080  -0.0739 0.1873  270  ASP C OD2 
7922  N  N   . SER C 271 ? 0.8389 1.1422 0.7277 0.1141  -0.1036 0.1908  271  SER C N   
7923  C  CA  . SER C 271 ? 0.7543 1.0983 0.6457 0.1035  -0.1081 0.1801  271  SER C CA  
7924  C  C   . SER C 271 ? 0.6930 1.0502 0.6064 0.0952  -0.1037 0.1593  271  SER C C   
7925  O  O   . SER C 271 ? 0.7650 1.1366 0.6978 0.1033  -0.1058 0.1563  271  SER C O   
7926  C  CB  . SER C 271 ? 0.5502 0.9273 0.4406 0.1148  -0.1205 0.1909  271  SER C CB  
7927  O  OG  . SER C 271 ? 0.5290 0.9457 0.4217 0.1037  -0.1259 0.1793  271  SER C OG  
7928  N  N   . PHE C 272 ? 0.5765 0.9285 0.4866 0.0793  -0.0972 0.1457  272  PHE C N   
7929  C  CA  . PHE C 272 ? 0.4349 0.7938 0.3623 0.0701  -0.0927 0.1264  272  PHE C CA  
7930  C  C   . PHE C 272 ? 0.4088 0.7899 0.3295 0.0555  -0.0943 0.1130  272  PHE C C   
7931  O  O   . PHE C 272 ? 0.4581 0.8280 0.3642 0.0472  -0.0893 0.1102  272  PHE C O   
7932  C  CB  . PHE C 272 ? 0.3999 0.7227 0.3304 0.0666  -0.0821 0.1213  272  PHE C CB  
7933  C  CG  . PHE C 272 ? 0.5500 0.8488 0.4871 0.0800  -0.0799 0.1306  272  PHE C CG  
7934  C  CD1 . PHE C 272 ? 0.5788 0.8419 0.5033 0.0832  -0.0758 0.1410  272  PHE C CD1 
7935  C  CD2 . PHE C 272 ? 0.3529 0.6655 0.3084 0.0892  -0.0818 0.1288  272  PHE C CD2 
7936  C  CE1 . PHE C 272 ? 0.4394 0.6772 0.3674 0.0959  -0.0740 0.1481  272  PHE C CE1 
7937  C  CE2 . PHE C 272 ? 0.3875 0.6780 0.3475 0.1031  -0.0790 0.1363  272  PHE C CE2 
7938  C  CZ  . PHE C 272 ? 0.4178 0.6690 0.3629 0.1068  -0.0752 0.1454  272  PHE C CZ  
7939  N  N   . SER C 273 ? 0.5278 0.9408 0.4589 0.0522  -0.1012 0.1043  273  SER C N   
7940  C  CA  . SER C 273 ? 0.6008 1.0348 0.5238 0.0385  -0.1041 0.0901  273  SER C CA  
7941  C  C   . SER C 273 ? 0.6296 1.0436 0.5534 0.0270  -0.0944 0.0733  273  SER C C   
7942  O  O   . SER C 273 ? 0.5669 0.9694 0.5076 0.0252  -0.0898 0.0652  273  SER C O   
7943  C  CB  . SER C 273 ? 0.6566 1.1263 0.5935 0.0354  -0.1136 0.0828  273  SER C CB  
7944  O  OG  . SER C 273 ? 0.7251 1.2100 0.6523 0.0208  -0.1163 0.0668  273  SER C OG  
7945  N  N   . GLY C 274 ? 0.5817 0.9925 0.4869 0.0199  -0.0912 0.0685  274  GLY C N   
7946  C  CA  . GLY C 274 ? 0.4651 0.8571 0.3696 0.0114  -0.0817 0.0537  274  GLY C CA  
7947  C  C   . GLY C 274 ? 0.5396 0.8994 0.4489 0.0157  -0.0725 0.0604  274  GLY C C   
7948  O  O   . GLY C 274 ? 0.5526 0.8960 0.4643 0.0104  -0.0648 0.0495  274  GLY C O   
7949  N  N   . GLY C 275 ? 0.3990 0.7490 0.3091 0.0257  -0.0739 0.0780  275  GLY C N   
7950  C  CA  . GLY C 275 ? 0.2632 0.5817 0.1755 0.0294  -0.0667 0.0855  275  GLY C CA  
7951  C  C   . GLY C 275 ? 0.5171 0.8207 0.4486 0.0309  -0.0631 0.0780  275  GLY C C   
7952  O  O   . GLY C 275 ? 0.5243 0.8013 0.4585 0.0315  -0.0566 0.0792  275  GLY C O   
7953  N  N   . ILE C 276 ? 0.5836 0.9055 0.5280 0.0305  -0.0674 0.0703  276  ILE C N   
7954  C  CA  . ILE C 276 ? 0.5925 0.9033 0.5546 0.0313  -0.0638 0.0641  276  ILE C CA  
7955  C  C   . ILE C 276 ? 0.4432 0.7700 0.4177 0.0408  -0.0692 0.0716  276  ILE C C   
7956  O  O   . ILE C 276 ? 0.5337 0.8849 0.5050 0.0450  -0.0770 0.0785  276  ILE C O   
7957  C  CB  . ILE C 276 ? 0.5334 0.8495 0.5024 0.0195  -0.0620 0.0456  276  ILE C CB  
7958  C  CG1 . ILE C 276 ? 0.4440 0.7931 0.4167 0.0146  -0.0704 0.0397  276  ILE C CG1 
7959  C  CG2 . ILE C 276 ? 0.4515 0.7561 0.4079 0.0122  -0.0569 0.0373  276  ILE C CG2 
7960  C  CD1 . ILE C 276 ? 0.4438 0.7947 0.4243 0.0025  -0.0694 0.0222  276  ILE C CD1 
7961  N  N   . THR C 277 ? 0.3863 0.7009 0.3746 0.0451  -0.0648 0.0707  277  THR C N   
7962  C  CA  . THR C 277 ? 0.4092 0.7410 0.4112 0.0554  -0.0684 0.0773  277  THR C CA  
7963  C  C   . THR C 277 ? 0.4685 0.7924 0.4866 0.0543  -0.0621 0.0703  277  THR C C   
7964  O  O   . THR C 277 ? 0.4892 0.7868 0.5052 0.0488  -0.0551 0.0639  277  THR C O   
7965  C  CB  . THR C 277 ? 0.3880 0.7072 0.3823 0.0718  -0.0698 0.0944  277  THR C CB  
7966  O  OG1 . THR C 277 ? 0.4477 0.7900 0.4558 0.0838  -0.0740 0.1006  277  THR C OG1 
7967  C  CG2 . THR C 277 ? 0.2162 0.4951 0.2058 0.0759  -0.0617 0.0970  277  THR C CG2 
7968  N  N   . ASN C 278 ? 0.4694 0.8189 0.5038 0.0595  -0.0648 0.0721  278  ASN C N   
7969  C  CA  . ASN C 278 ? 0.3883 0.7344 0.4383 0.0614  -0.0584 0.0688  278  ASN C CA  
7970  C  C   . ASN C 278 ? 0.5217 0.8461 0.5688 0.0793  -0.0541 0.0800  278  ASN C C   
7971  O  O   . ASN C 278 ? 0.6807 1.0115 0.7237 0.0931  -0.0588 0.0916  278  ASN C O   
7972  C  CB  . ASN C 278 ? 0.3489 0.7368 0.4189 0.0582  -0.0628 0.0661  278  ASN C CB  
7973  C  CG  . ASN C 278 ? 0.4585 0.8484 0.5454 0.0614  -0.0555 0.0650  278  ASN C CG  
7974  O  OD1 . ASN C 278 ? 0.4574 0.8726 0.5582 0.0732  -0.0566 0.0721  278  ASN C OD1 
7975  N  ND2 . ASN C 278 ? 0.2673 0.6321 0.3530 0.0516  -0.0479 0.0564  278  ASN C ND2 
7976  N  N   . GLY C 279 ? 0.2618 0.5585 0.3090 0.0794  -0.0457 0.0765  279  GLY C N   
7977  C  CA  . GLY C 279 ? 0.2229 0.4946 0.2644 0.0953  -0.0414 0.0849  279  GLY C CA  
7978  C  C   . GLY C 279 ? 0.4583 0.7546 0.5100 0.1126  -0.0443 0.0940  279  GLY C C   
7979  O  O   . GLY C 279 ? 0.4289 0.7171 0.4708 0.1264  -0.0482 0.1050  279  GLY C O   
7980  N  N   . ALA C 280 ? 0.3551 0.6829 0.4270 0.1116  -0.0427 0.0898  280  ALA C N   
7981  C  CA  . ALA C 280 ? 0.2982 0.6538 0.3838 0.1291  -0.0439 0.0976  280  ALA C CA  
7982  C  C   . ALA C 280 ? 0.3202 0.6992 0.4039 0.1367  -0.0546 0.1069  280  ALA C C   
7983  O  O   . ALA C 280 ? 0.4304 0.8123 0.5139 0.1573  -0.0567 0.1178  280  ALA C O   
7984  C  CB  . ALA C 280 ? 0.2127 0.6048 0.3220 0.1219  -0.0408 0.0912  280  ALA C CB  
7985  N  N   . HIS C 281 ? 0.3006 0.6954 0.3816 0.1209  -0.0616 0.1026  281  HIS C N   
7986  C  CA  . HIS C 281 ? 0.3113 0.7313 0.3889 0.1259  -0.0726 0.1110  281  HIS C CA  
7987  C  C   . HIS C 281 ? 0.2778 0.6658 0.3336 0.1393  -0.0746 0.1233  281  HIS C C   
7988  O  O   . HIS C 281 ? 0.3660 0.7678 0.4201 0.1544  -0.0815 0.1354  281  HIS C O   
7989  C  CB  . HIS C 281 ? 0.2527 0.6925 0.3279 0.1053  -0.0792 0.1023  281  HIS C CB  
7990  C  CG  . HIS C 281 ? 0.4161 0.8909 0.4906 0.1095  -0.0913 0.1099  281  HIS C CG  
7991  N  ND1 . HIS C 281 ? 0.4390 0.9019 0.4920 0.1120  -0.0970 0.1177  281  HIS C ND1 
7992  C  CD2 . HIS C 281 ? 0.4583 0.9812 0.5509 0.1118  -0.0992 0.1119  281  HIS C CD2 
7993  C  CE1 . HIS C 281 ? 0.3922 0.8929 0.4484 0.1161  -0.1081 0.1241  281  HIS C CE1 
7994  N  NE2 . HIS C 281 ? 0.5832 1.1216 0.6640 0.1161  -0.1101 0.1205  281  HIS C NE2 
7995  N  N   . TRP C 282 ? 0.3827 0.7280 0.4215 0.1330  -0.0689 0.1208  282  TRP C N   
7996  C  CA  . TRP C 282 ? 0.4540 0.7635 0.4724 0.1440  -0.0693 0.1325  282  TRP C CA  
7997  C  C   . TRP C 282 ? 0.4343 0.7334 0.4571 0.1668  -0.0664 0.1404  282  TRP C C   
7998  O  O   . TRP C 282 ? 0.3175 0.6255 0.3386 0.1841  -0.0723 0.1526  282  TRP C O   
7999  C  CB  . TRP C 282 ? 0.4550 0.7236 0.4591 0.1319  -0.0626 0.1268  282  TRP C CB  
8000  C  CG  . TRP C 282 ? 0.5737 0.8050 0.5559 0.1381  -0.0634 0.1383  282  TRP C CG  
8001  C  CD1 . TRP C 282 ? 0.5465 0.7729 0.5191 0.1538  -0.0690 0.1532  282  TRP C CD1 
8002  C  CD2 . TRP C 282 ? 0.5745 0.7681 0.5417 0.1279  -0.0587 0.1366  282  TRP C CD2 
8003  N  NE1 . TRP C 282 ? 0.5048 0.6899 0.4561 0.1528  -0.0680 0.1609  282  TRP C NE1 
8004  C  CE2 . TRP C 282 ? 0.4882 0.6548 0.4367 0.1364  -0.0618 0.1508  282  TRP C CE2 
8005  C  CE3 . TRP C 282 ? 0.5217 0.7025 0.4896 0.1125  -0.0527 0.1249  282  TRP C CE3 
8006  C  CZ2 . TRP C 282 ? 0.4458 0.5750 0.3775 0.1280  -0.0589 0.1535  282  TRP C CZ2 
8007  C  CZ3 . TRP C 282 ? 0.5148 0.6609 0.4671 0.1059  -0.0501 0.1276  282  TRP C CZ3 
8008  C  CH2 . TRP C 282 ? 0.3694 0.4909 0.3042 0.1127  -0.0532 0.1417  282  TRP C CH2 
8009  N  N   . TYR C 283 ? 0.4482 0.7272 0.4754 0.1673  -0.0571 0.1331  283  TYR C N   
8010  C  CA  . TYR C 283 ? 0.4982 0.7741 0.5329 0.1879  -0.0525 0.1366  283  TYR C CA  
8011  C  C   . TYR C 283 ? 0.4566 0.7240 0.4993 0.1804  -0.0423 0.1246  283  TYR C C   
8012  O  O   . TYR C 283 ? 0.3962 0.6405 0.4305 0.1638  -0.0390 0.1170  283  TYR C O   
8013  C  CB  . TYR C 283 ? 0.3763 0.6086 0.3900 0.2048  -0.0526 0.1474  283  TYR C CB  
8014  C  CG  . TYR C 283 ? 0.4462 0.6291 0.4387 0.1932  -0.0490 0.1449  283  TYR C CG  
8015  C  CD1 . TYR C 283 ? 0.4989 0.6523 0.4880 0.1921  -0.0403 0.1370  283  TYR C CD1 
8016  C  CD2 . TYR C 283 ? 0.5926 0.7601 0.5681 0.1832  -0.0545 0.1511  283  TYR C CD2 
8017  C  CE1 . TYR C 283 ? 0.4964 0.6075 0.4673 0.1810  -0.0381 0.1351  283  TYR C CE1 
8018  C  CE2 . TYR C 283 ? 0.6313 0.7579 0.5896 0.1719  -0.0514 0.1496  283  TYR C CE2 
8019  C  CZ  . TYR C 283 ? 0.6558 0.7547 0.6124 0.1708  -0.0437 0.1415  283  TYR C CZ  
8020  O  OH  . TYR C 283 ? 0.7574 0.8186 0.6981 0.1588  -0.0416 0.1401  283  TYR C OH  
8021  N  N   . GLU C 284 ? 0.5335 0.8218 0.5927 0.1928  -0.0374 0.1235  284  GLU C N   
8022  C  CA  . GLU C 284 ? 0.5204 0.8032 0.5869 0.1871  -0.0271 0.1135  284  GLU C CA  
8023  C  C   . GLU C 284 ? 0.4362 0.6678 0.4836 0.1954  -0.0198 0.1126  284  GLU C C   
8024  O  O   . GLU C 284 ? 0.5143 0.7203 0.5482 0.2136  -0.0209 0.1204  284  GLU C O   
8025  C  CB  . GLU C 284 ? 0.4803 0.8082 0.5720 0.1963  -0.0234 0.1128  284  GLU C CB  
8026  C  CG  . GLU C 284 ? 0.5413 0.9216 0.6539 0.1824  -0.0300 0.1108  284  GLU C CG  
8027  C  CD  . GLU C 284 ? 0.4506 0.8751 0.5897 0.1846  -0.0246 0.1082  284  GLU C CD  
8028  O  OE1 . GLU C 284 ? 0.3034 0.7749 0.4615 0.1754  -0.0309 0.1079  284  GLU C OE1 
8029  O  OE2 . GLU C 284 ? 0.4776 0.8907 0.6180 0.1946  -0.0141 0.1065  284  GLU C OE2 
8030  N  N   . LEU C 285 ? 0.2930 0.5085 0.3384 0.1814  -0.0131 0.1030  285  LEU C N   
8031  C  CA  . LEU C 285 ? 0.4302 0.6012 0.4585 0.1870  -0.0063 0.1004  285  LEU C CA  
8032  C  C   . LEU C 285 ? 0.4275 0.6061 0.4648 0.1765  0.0023  0.0907  285  LEU C C   
8033  O  O   . LEU C 285 ? 0.3325 0.5388 0.3842 0.1601  0.0014  0.0859  285  LEU C O   
8034  C  CB  . LEU C 285 ? 0.4260 0.5548 0.4321 0.1767  -0.0104 0.1015  285  LEU C CB  
8035  C  CG  . LEU C 285 ? 0.3884 0.5182 0.3952 0.1524  -0.0119 0.0947  285  LEU C CG  
8036  C  CD1 . LEU C 285 ? 0.3766 0.4778 0.3755 0.1443  -0.0053 0.0867  285  LEU C CD1 
8037  C  CD2 . LEU C 285 ? 0.3578 0.4730 0.3515 0.1450  -0.0192 0.1000  285  LEU C CD2 
8038  N  N   . SER C 286 ? 0.4535 0.6067 0.4812 0.1858  0.0103  0.0878  286  SER C N   
8039  C  CA  . SER C 286 ? 0.4431 0.6033 0.4774 0.1773  0.0191  0.0799  286  SER C CA  
8040  C  C   . SER C 286 ? 0.4216 0.5351 0.4341 0.1725  0.0229  0.0749  286  SER C C   
8041  O  O   . SER C 286 ? 0.5464 0.6230 0.5393 0.1828  0.0216  0.0772  286  SER C O   
8042  C  CB  . SER C 286 ? 0.5282 0.7170 0.5763 0.1942  0.0272  0.0808  286  SER C CB  
8043  O  OG  . SER C 286 ? 0.5685 0.8040 0.6383 0.1994  0.0227  0.0861  286  SER C OG  
8044  N  N   . GLY C 287 ? 0.3801 0.4951 0.3957 0.1561  0.0268  0.0683  287  GLY C N   
8045  C  CA  . GLY C 287 ? 0.3131 0.3885 0.3096 0.1487  0.0292  0.0634  287  GLY C CA  
8046  C  C   . GLY C 287 ? 0.3073 0.3604 0.2943 0.1335  0.0215  0.0628  287  GLY C C   
8047  O  O   . GLY C 287 ? 0.3294 0.3479 0.2993 0.1290  0.0214  0.0602  287  GLY C O   
8048  N  N   . GLY C 288 ? 0.4269 0.5022 0.4252 0.1256  0.0151  0.0650  288  GLY C N   
8049  C  CA  . GLY C 288 ? 0.4651 0.5266 0.4568 0.1118  0.0086  0.0644  288  GLY C CA  
8050  C  C   . GLY C 288 ? 0.4555 0.5118 0.4483 0.0953  0.0102  0.0574  288  GLY C C   
8051  O  O   . GLY C 288 ? 0.2983 0.3677 0.2999 0.0913  0.0154  0.0534  288  GLY C O   
8052  N  N   . MET C 289 ? 0.4444 0.4818 0.4282 0.0860  0.0057  0.0567  289  MET C N   
8053  C  CA  . MET C 289 ? 0.4422 0.4722 0.4260 0.0727  0.0066  0.0506  289  MET C CA  
8054  C  C   . MET C 289 ? 0.3445 0.4024 0.3433 0.0627  0.0049  0.0470  289  MET C C   
8055  O  O   . MET C 289 ? 0.3661 0.4284 0.3708 0.0543  0.0076  0.0419  289  MET C O   
8056  C  CB  . MET C 289 ? 0.3213 0.3248 0.2920 0.0669  0.0024  0.0512  289  MET C CB  
8057  C  CG  . MET C 289 ? 0.3504 0.3436 0.3200 0.0560  0.0031  0.0456  289  MET C CG  
8058  S  SD  . MET C 289 ? 0.6714 0.6361 0.6266 0.0505  -0.0017 0.0471  289  MET C SD  
8059  C  CE  . MET C 289 ? 0.4062 0.3862 0.3656 0.0475  -0.0067 0.0513  289  MET C CE  
8060  N  N   . GLN C 290 ? 0.2954 0.3707 0.2986 0.0634  0.0000  0.0498  290  GLN C N   
8061  C  CA  . GLN C 290 ? 0.2525 0.3518 0.2665 0.0533  -0.0028 0.0454  290  GLN C CA  
8062  C  C   . GLN C 290 ? 0.3214 0.4401 0.3487 0.0491  0.0010  0.0413  290  GLN C C   
8063  O  O   . GLN C 290 ? 0.3412 0.4563 0.3711 0.0383  0.0025  0.0352  290  GLN C O   
8064  C  CB  . GLN C 290 ? 0.4017 0.5214 0.4180 0.0574  -0.0082 0.0501  290  GLN C CB  
8065  C  CG  . GLN C 290 ? 0.3991 0.5454 0.4251 0.0471  -0.0117 0.0445  290  GLN C CG  
8066  C  CD  . GLN C 290 ? 0.3952 0.5659 0.4235 0.0520  -0.0175 0.0498  290  GLN C CD  
8067  O  OE1 . GLN C 290 ? 0.5006 0.6692 0.5203 0.0506  -0.0215 0.0520  290  GLN C OE1 
8068  N  NE2 . GLN C 290 ? 0.1334 0.3295 0.1735 0.0579  -0.0179 0.0524  290  GLN C NE2 
8069  N  N   . ASP C 291 ? 0.3088 0.4482 0.3446 0.0580  0.0026  0.0453  291  ASP C N   
8070  C  CA  . ASP C 291 ? 0.1951 0.3598 0.2459 0.0534  0.0061  0.0429  291  ASP C CA  
8071  C  C   . ASP C 291 ? 0.3716 0.5190 0.4194 0.0490  0.0134  0.0400  291  ASP C C   
8072  O  O   . ASP C 291 ? 0.3093 0.4689 0.3664 0.0382  0.0160  0.0365  291  ASP C O   
8073  C  CB  . ASP C 291 ? 0.3278 0.5196 0.3888 0.0667  0.0069  0.0490  291  ASP C CB  
8074  C  CG  . ASP C 291 ? 0.5541 0.7722 0.6217 0.0679  -0.0011 0.0517  291  ASP C CG  
8075  O  OD1 . ASP C 291 ? 0.6288 0.8412 0.6903 0.0595  -0.0068 0.0491  291  ASP C OD1 
8076  O  OD2 . ASP C 291 ? 0.6027 0.8490 0.6816 0.0778  -0.0018 0.0567  291  ASP C OD2 
8077  N  N   . PHE C 292 ? 0.4528 0.5706 0.4861 0.0565  0.0163  0.0418  292  PHE C N   
8078  C  CA  . PHE C 292 ? 0.2727 0.3719 0.2995 0.0528  0.0223  0.0395  292  PHE C CA  
8079  C  C   . PHE C 292 ? 0.2856 0.3751 0.3121 0.0373  0.0205  0.0342  292  PHE C C   
8080  O  O   . PHE C 292 ? 0.5314 0.6208 0.5606 0.0299  0.0249  0.0325  292  PHE C O   
8081  C  CB  . PHE C 292 ? 0.1621 0.2294 0.1709 0.0623  0.0237  0.0414  292  PHE C CB  
8082  C  CG  . PHE C 292 ? 0.3259 0.3725 0.3251 0.0576  0.0282  0.0390  292  PHE C CG  
8083  C  CD1 . PHE C 292 ? 0.4102 0.4607 0.4083 0.0629  0.0364  0.0399  292  PHE C CD1 
8084  C  CD2 . PHE C 292 ? 0.3131 0.3385 0.3045 0.0484  0.0246  0.0363  292  PHE C CD2 
8085  C  CE1 . PHE C 292 ? 0.3163 0.3479 0.3034 0.0584  0.0405  0.0385  292  PHE C CE1 
8086  C  CE2 . PHE C 292 ? 0.4101 0.4171 0.3920 0.0446  0.0278  0.0351  292  PHE C CE2 
8087  C  CZ  . PHE C 292 ? 0.4324 0.4417 0.4112 0.0491  0.0357  0.0363  292  PHE C CZ  
8088  N  N   . ASN C 293 ? 0.2762 0.3567 0.2987 0.0331  0.0143  0.0319  293  ASN C N   
8089  C  CA  . ASN C 293 ? 0.3993 0.4723 0.4223 0.0209  0.0122  0.0263  293  ASN C CA  
8090  C  C   . ASN C 293 ? 0.3844 0.4782 0.4202 0.0101  0.0126  0.0224  293  ASN C C   
8091  O  O   . ASN C 293 ? 0.3082 0.3923 0.3438 0.0010  0.0148  0.0195  293  ASN C O   
8092  C  CB  . ASN C 293 ? 0.4372 0.5055 0.4560 0.0200  0.0062  0.0244  293  ASN C CB  
8093  C  CG  . ASN C 293 ? 0.4741 0.5163 0.4803 0.0240  0.0053  0.0265  293  ASN C CG  
8094  O  OD1 . ASN C 293 ? 0.3581 0.3840 0.3600 0.0192  0.0051  0.0235  293  ASN C OD1 
8095  N  ND2 . ASN C 293 ? 0.3087 0.3462 0.3085 0.0327  0.0043  0.0318  293  ASN C ND2 
8096  N  N   . TYR C 294 ? 0.4242 0.5457 0.4700 0.0105  0.0097  0.0228  294  TYR C N   
8097  C  CA  . TYR C 294 ? 0.5275 0.6714 0.5856 -0.0014 0.0083  0.0186  294  TYR C CA  
8098  C  C   . TYR C 294 ? 0.4541 0.6105 0.5214 -0.0055 0.0146  0.0210  294  TYR C C   
8099  O  O   . TYR C 294 ? 0.2874 0.4472 0.3602 -0.0195 0.0151  0.0174  294  TYR C O   
8100  C  CB  . TYR C 294 ? 0.3936 0.5672 0.4599 0.0008  0.0027  0.0192  294  TYR C CB  
8101  C  CG  . TYR C 294 ? 0.2694 0.4663 0.3470 -0.0133 -0.0006 0.0137  294  TYR C CG  
8102  C  CD1 . TYR C 294 ? 0.3018 0.4854 0.3747 -0.0257 -0.0037 0.0051  294  TYR C CD1 
8103  C  CD2 . TYR C 294 ? 0.2895 0.5216 0.3822 -0.0140 -0.0011 0.0168  294  TYR C CD2 
8104  C  CE1 . TYR C 294 ? 0.3193 0.5207 0.4003 -0.0400 -0.0076 -0.0010 294  TYR C CE1 
8105  C  CE2 . TYR C 294 ? 0.3015 0.5558 0.4044 -0.0290 -0.0053 0.0116  294  TYR C CE2 
8106  C  CZ  . TYR C 294 ? 0.2854 0.5225 0.3814 -0.0427 -0.0087 0.0024  294  TYR C CZ  
8107  O  OH  . TYR C 294 ? 0.3616 0.6175 0.4657 -0.0589 -0.0135 -0.0038 294  TYR C OH  
8108  N  N   . ALA C 295 ? 0.3573 0.5200 0.4253 0.0067  0.0196  0.0273  295  ALA C N   
8109  C  CA  . ALA C 295 ? 0.3116 0.4927 0.3894 0.0052  0.0269  0.0305  295  ALA C CA  
8110  C  C   . ALA C 295 ? 0.2471 0.4035 0.3151 0.0013  0.0339  0.0311  295  ALA C C   
8111  O  O   . ALA C 295 ? 0.3359 0.5054 0.4114 -0.0066 0.0398  0.0329  295  ALA C O   
8112  C  CB  . ALA C 295 ? 0.2839 0.4848 0.3668 0.0221  0.0298  0.0363  295  ALA C CB  
8113  N  N   . PHE C 296 ? 0.2878 0.4103 0.3391 0.0060  0.0329  0.0303  296  PHE C N   
8114  C  CA  . PHE C 296 ? 0.3888 0.4873 0.4281 0.0051  0.0387  0.0319  296  PHE C CA  
8115  C  C   . PHE C 296 ? 0.4264 0.4962 0.4561 -0.0040 0.0345  0.0283  296  PHE C C   
8116  O  O   . PHE C 296 ? 0.4036 0.4513 0.4220 -0.0055 0.0377  0.0299  296  PHE C O   
8117  C  CB  . PHE C 296 ? 0.3988 0.4831 0.4251 0.0210  0.0419  0.0350  296  PHE C CB  
8118  C  CG  . PHE C 296 ? 0.5602 0.6698 0.5943 0.0325  0.0476  0.0385  296  PHE C CG  
8119  C  CD1 . PHE C 296 ? 0.5343 0.6619 0.5765 0.0418  0.0435  0.0396  296  PHE C CD1 
8120  C  CD2 . PHE C 296 ? 0.5789 0.6956 0.6122 0.0349  0.0573  0.0412  296  PHE C CD2 
8121  C  CE1 . PHE C 296 ? 0.4499 0.6017 0.5001 0.0548  0.0485  0.0432  296  PHE C CE1 
8122  C  CE2 . PHE C 296 ? 0.4943 0.6368 0.5358 0.0477  0.0633  0.0441  296  PHE C CE2 
8123  C  CZ  . PHE C 296 ? 0.4804 0.6403 0.5310 0.0583  0.0586  0.0450  296  PHE C CZ  
8124  N  N   . SER C 297 ? 0.3922 0.4632 0.4259 -0.0091 0.0275  0.0235  297  SER C N   
8125  C  CA  . SER C 297 ? 0.2481 0.2953 0.2751 -0.0168 0.0238  0.0192  297  SER C CA  
8126  C  C   . SER C 297 ? 0.2203 0.2784 0.2558 -0.0264 0.0186  0.0128  297  SER C C   
8127  O  O   . SER C 297 ? 0.4516 0.5371 0.4985 -0.0294 0.0176  0.0121  297  SER C O   
8128  C  CB  . SER C 297 ? 0.3878 0.4131 0.4029 -0.0079 0.0203  0.0191  297  SER C CB  
8129  O  OG  . SER C 297 ? 0.3754 0.4098 0.3935 -0.0045 0.0149  0.0163  297  SER C OG  
8130  N  N   . ASN C 298 ? 0.1649 0.2018 0.1940 -0.0306 0.0150  0.0077  298  ASN C N   
8131  C  CA  . ASN C 298 ? 0.2605 0.3027 0.2936 -0.0381 0.0099  -0.0003 298  ASN C CA  
8132  C  C   . ASN C 298 ? 0.3341 0.3878 0.3672 -0.0301 0.0055  -0.0025 298  ASN C C   
8133  O  O   . ASN C 298 ? 0.3568 0.4233 0.3933 -0.0347 0.0013  -0.0086 298  ASN C O   
8134  C  CB  . ASN C 298 ? 0.2163 0.2294 0.2413 -0.0430 0.0082  -0.0053 298  ASN C CB  
8135  C  CG  . ASN C 298 ? 0.3166 0.3154 0.3400 -0.0533 0.0118  -0.0029 298  ASN C CG  
8136  O  OD1 . ASN C 298 ? 0.3973 0.4131 0.4286 -0.0619 0.0147  -0.0003 298  ASN C OD1 
8137  N  ND2 . ASN C 298 ? 0.3963 0.3648 0.4097 -0.0525 0.0114  -0.0031 298  ASN C ND2 
8138  N  N   . CYS C 299 ? 0.2241 0.2718 0.2516 -0.0189 0.0061  0.0025  299  CYS C N   
8139  C  CA  . CYS C 299 ? 0.1820 0.2345 0.2067 -0.0123 0.0022  0.0015  299  CYS C CA  
8140  C  C   . CYS C 299 ? 0.2887 0.3695 0.3202 -0.0116 -0.0005 0.0017  299  CYS C C   
8141  O  O   . CYS C 299 ? 0.3221 0.4201 0.3604 -0.0098 0.0012  0.0063  299  CYS C O   
8142  C  CB  . CYS C 299 ? 0.1287 0.1681 0.1457 -0.0025 0.0032  0.0077  299  CYS C CB  
8143  S  SG  . CYS C 299 ? 0.2671 0.3028 0.2786 0.0021  -0.0010 0.0067  299  CYS C SG  
8144  N  N   . PHE C 300 ? 0.2440 0.3306 0.2733 -0.0122 -0.0046 -0.0030 300  PHE C N   
8145  C  CA  . PHE C 300 ? 0.1796 0.2916 0.2122 -0.0110 -0.0084 -0.0025 300  PHE C CA  
8146  C  C   . PHE C 300 ? 0.3720 0.4820 0.3975 -0.0015 -0.0096 0.0033  300  PHE C C   
8147  O  O   . PHE C 300 ? 0.3601 0.4652 0.3796 -0.0018 -0.0111 -0.0003 300  PHE C O   
8148  C  CB  . PHE C 300 ? 0.4164 0.5356 0.4485 -0.0197 -0.0121 -0.0126 300  PHE C CB  
8149  C  CG  . PHE C 300 ? 0.4439 0.5684 0.4830 -0.0314 -0.0125 -0.0180 300  PHE C CG  
8150  C  CD1 . PHE C 300 ? 0.3267 0.4687 0.3676 -0.0400 -0.0173 -0.0254 300  PHE C CD1 
8151  C  CD2 . PHE C 300 ? 0.5291 0.6412 0.5717 -0.0349 -0.0081 -0.0153 300  PHE C CD2 
8152  C  CE1 . PHE C 300 ? 0.3721 0.5185 0.4194 -0.0532 -0.0183 -0.0303 300  PHE C CE1 
8153  C  CE2 . PHE C 300 ? 0.4958 0.6130 0.5449 -0.0478 -0.0082 -0.0191 300  PHE C CE2 
8154  C  CZ  . PHE C 300 ? 0.3754 0.5095 0.4274 -0.0576 -0.0136 -0.0267 300  PHE C CZ  
8155  N  N   . GLU C 301 ? 0.2410 0.3538 0.2667 0.0067  -0.0086 0.0121  301  GLU C N   
8156  C  CA  . GLU C 301 ? 0.2577 0.3633 0.2751 0.0144  -0.0098 0.0187  301  GLU C CA  
8157  C  C   . GLU C 301 ? 0.3423 0.4692 0.3597 0.0183  -0.0138 0.0233  301  GLU C C   
8158  O  O   . GLU C 301 ? 0.3576 0.5028 0.3820 0.0212  -0.0148 0.0261  301  GLU C O   
8159  C  CB  . GLU C 301 ? 0.3759 0.4630 0.3889 0.0217  -0.0066 0.0253  301  GLU C CB  
8160  C  CG  . GLU C 301 ? 0.4804 0.5591 0.4843 0.0289  -0.0085 0.0332  301  GLU C CG  
8161  C  CD  . GLU C 301 ? 0.4815 0.5338 0.4770 0.0330  -0.0062 0.0367  301  GLU C CD  
8162  O  OE1 . GLU C 301 ? 0.5349 0.5725 0.5278 0.0283  -0.0053 0.0331  301  GLU C OE1 
8163  O  OE2 . GLU C 301 ? 0.5542 0.5998 0.5447 0.0414  -0.0057 0.0428  301  GLU C OE2 
8164  N  N   . LEU C 302 ? 0.3755 0.5020 0.3853 0.0183  -0.0162 0.0245  302  LEU C N   
8165  C  CA  . LEU C 302 ? 0.4814 0.6244 0.4878 0.0227  -0.0201 0.0311  302  LEU C CA  
8166  C  C   . LEU C 302 ? 0.4667 0.5929 0.4650 0.0307  -0.0197 0.0418  302  LEU C C   
8167  O  O   . LEU C 302 ? 0.4564 0.5604 0.4498 0.0299  -0.0173 0.0423  302  LEU C O   
8168  C  CB  . LEU C 302 ? 0.3968 0.5514 0.3978 0.0173  -0.0226 0.0269  302  LEU C CB  
8169  C  CG  . LEU C 302 ? 0.3897 0.5599 0.3943 0.0091  -0.0243 0.0153  302  LEU C CG  
8170  C  CD1 . LEU C 302 ? 0.4434 0.6245 0.4387 0.0065  -0.0262 0.0125  302  LEU C CD1 
8171  C  CD2 . LEU C 302 ? 0.4022 0.5941 0.4157 0.0085  -0.0277 0.0154  302  LEU C CD2 
8172  N  N   . THR C 303 ? 0.4569 0.5928 0.4531 0.0382  -0.0228 0.0503  303  THR C N   
8173  C  CA  . THR C 303 ? 0.6101 0.7282 0.5953 0.0451  -0.0236 0.0611  303  THR C CA  
8174  C  C   . THR C 303 ? 0.6288 0.7563 0.6055 0.0420  -0.0271 0.0659  303  THR C C   
8175  O  O   . THR C 303 ? 0.5395 0.6909 0.5177 0.0429  -0.0309 0.0670  303  THR C O   
8176  C  CB  . THR C 303 ? 0.6224 0.7414 0.6088 0.0579  -0.0245 0.0690  303  THR C CB  
8177  O  OG1 . THR C 303 ? 0.6303 0.7492 0.6261 0.0607  -0.0204 0.0640  303  THR C OG1 
8178  C  CG2 . THR C 303 ? 0.4606 0.5516 0.4332 0.0646  -0.0249 0.0788  303  THR C CG2 
8179  N  N   . ILE C 304 ? 0.6422 0.7529 0.6099 0.0377  -0.0260 0.0690  304  ILE C N   
8180  C  CA  . ILE C 304 ? 0.5680 0.6886 0.5269 0.0336  -0.0281 0.0742  304  ILE C CA  
8181  C  C   . ILE C 304 ? 0.5614 0.6634 0.5075 0.0362  -0.0298 0.0880  304  ILE C C   
8182  O  O   . ILE C 304 ? 0.4737 0.5508 0.4154 0.0342  -0.0281 0.0906  304  ILE C O   
8183  C  CB  . ILE C 304 ? 0.4890 0.6161 0.4492 0.0240  -0.0253 0.0654  304  ILE C CB  
8184  C  CG1 . ILE C 304 ? 0.4041 0.5485 0.3740 0.0216  -0.0249 0.0523  304  ILE C CG1 
8185  C  CG2 . ILE C 304 ? 0.5123 0.6514 0.4624 0.0200  -0.0262 0.0715  304  ILE C CG2 
8186  C  CD1 . ILE C 304 ? 0.5961 0.7414 0.5682 0.0148  -0.0215 0.0415  304  ILE C CD1 
8187  N  N   . GLU C 305 ? 0.4867 0.6002 0.4258 0.0402  -0.0337 0.0971  305  GLU C N   
8188  C  CA  . GLU C 305 ? 0.3772 0.4725 0.3021 0.0426  -0.0360 0.1118  305  GLU C CA  
8189  C  C   . GLU C 305 ? 0.5227 0.6267 0.4391 0.0321  -0.0353 0.1157  305  GLU C C   
8190  O  O   . GLU C 305 ? 0.6262 0.7571 0.5419 0.0296  -0.0363 0.1134  305  GLU C O   
8191  C  CB  . GLU C 305 ? 0.2875 0.3908 0.2093 0.0546  -0.0410 0.1208  305  GLU C CB  
8192  C  CG  . GLU C 305 ? 0.2171 0.3179 0.1491 0.0662  -0.0409 0.1170  305  GLU C CG  
8193  C  CD  . GLU C 305 ? 0.5593 0.6231 0.4840 0.0734  -0.0395 0.1226  305  GLU C CD  
8194  O  OE1 . GLU C 305 ? 0.6385 0.6989 0.5700 0.0843  -0.0382 0.1198  305  GLU C OE1 
8195  O  OE2 . GLU C 305 ? 0.5428 0.5809 0.4544 0.0680  -0.0396 0.1295  305  GLU C OE2 
8196  N  N   . LEU C 306 ? 0.5153 0.5976 0.4247 0.0252  -0.0335 0.1213  306  LEU C N   
8197  C  CA  . LEU C 306 ? 0.5076 0.6005 0.4123 0.0135  -0.0309 0.1235  306  LEU C CA  
8198  C  C   . LEU C 306 ? 0.5503 0.6398 0.4388 0.0106  -0.0333 0.1401  306  LEU C C   
8199  O  O   . LEU C 306 ? 0.6289 0.7415 0.5125 0.0048  -0.0319 0.1422  306  LEU C O   
8200  C  CB  . LEU C 306 ? 0.5840 0.6621 0.4937 0.0051  -0.0275 0.1191  306  LEU C CB  
8201  C  CG  . LEU C 306 ? 0.5365 0.6190 0.4608 0.0062  -0.0247 0.1035  306  LEU C CG  
8202  C  CD1 . LEU C 306 ? 0.4093 0.4744 0.3365 -0.0008 -0.0230 0.1020  306  LEU C CD1 
8203  C  CD2 . LEU C 306 ? 0.4049 0.5181 0.3360 0.0042  -0.0221 0.0928  306  LEU C CD2 
8204  N  N   . SER C 307 ? 0.6228 0.6821 0.5013 0.0148  -0.0366 0.1520  307  SER C N   
8205  C  CA  . SER C 307 ? 0.5591 0.6081 0.4200 0.0115  -0.0392 0.1696  307  SER C CA  
8206  C  C   . SER C 307 ? 0.5520 0.5833 0.4033 0.0256  -0.0450 0.1804  307  SER C C   
8207  O  O   . SER C 307 ? 0.6542 0.6730 0.5118 0.0375  -0.0463 0.1752  307  SER C O   
8208  C  CB  . SER C 307 ? 0.6478 0.6709 0.5024 -0.0013 -0.0376 0.1761  307  SER C CB  
8209  O  OG  . SER C 307 ? 0.6603 0.6575 0.5208 0.0013  -0.0376 0.1687  307  SER C OG  
8210  N  N   . CYS C 308 ? 0.6586 0.6900 0.4944 0.0253  -0.0483 0.1959  308  CYS C N   
8211  C  CA  . CYS C 308 ? 0.6467 0.6558 0.4708 0.0393  -0.0542 0.2089  308  CYS C CA  
8212  C  C   . CYS C 308 ? 0.7203 0.6817 0.5347 0.0374  -0.0545 0.2150  308  CYS C C   
8213  O  O   . CYS C 308 ? 0.7986 0.7339 0.6106 0.0515  -0.0572 0.2160  308  CYS C O   
8214  C  CB  . CYS C 308 ? 0.5953 0.6145 0.4028 0.0383  -0.0580 0.2254  308  CYS C CB  
8215  S  SG  . CYS C 308 ? 0.8612 0.9289 0.6746 0.0476  -0.0617 0.2214  308  CYS C SG  
8216  N  N   . CYS C 309 ? 0.6221 0.5734 0.4309 0.0194  -0.0517 0.2185  309  CYS C N   
8217  C  CA  . CYS C 309 ? 0.5592 0.4658 0.3581 0.0130  -0.0525 0.2234  309  CYS C CA  
8218  C  C   . CYS C 309 ? 0.7048 0.6061 0.5181 0.0128  -0.0495 0.2064  309  CYS C C   
8219  O  O   . CYS C 309 ? 0.5132 0.4411 0.3407 0.0031  -0.0452 0.1956  309  CYS C O   
8220  C  CB  . CYS C 309 ? 0.4566 0.3613 0.2462 -0.0084 -0.0508 0.2339  309  CYS C CB  
8221  S  SG  . CYS C 309 ? 0.8154 0.6638 0.5888 -0.0205 -0.0535 0.2431  309  CYS C SG  
8222  N  N   . LYS C 310 ? 0.8058 0.6729 0.6147 0.0243  -0.0516 0.2040  310  LYS C N   
8223  C  CA  . LYS C 310 ? 0.7482 0.6093 0.5686 0.0260  -0.0489 0.1883  310  LYS C CA  
8224  C  C   . LYS C 310 ? 0.7976 0.6487 0.6184 0.0064  -0.0475 0.1852  310  LYS C C   
8225  O  O   . LYS C 310 ? 0.7890 0.6610 0.6253 0.0013  -0.0441 0.1725  310  LYS C O   
8226  C  CB  . LYS C 310 ? 0.8160 0.6407 0.6280 0.0429  -0.0509 0.1872  310  LYS C CB  
8227  C  CG  . LYS C 310 ? 0.7425 0.5865 0.5629 0.0643  -0.0509 0.1845  310  LYS C CG  
8228  C  CD  . LYS C 310 ? 0.6732 0.4819 0.4854 0.0821  -0.0516 0.1830  310  LYS C CD  
8229  C  CE  . LYS C 310 ? 0.7122 0.5483 0.5389 0.1019  -0.0501 0.1772  310  LYS C CE  
8230  N  NZ  . LYS C 310 ? 0.9160 0.7219 0.7369 0.1193  -0.0486 0.1729  310  LYS C NZ  
8231  N  N   . TYR C 311 ? 0.7642 0.5836 0.5679 -0.0047 -0.0505 0.1974  311  TYR C N   
8232  C  CA  . TYR C 311 ? 0.7391 0.5481 0.5422 -0.0251 -0.0504 0.1967  311  TYR C CA  
8233  C  C   . TYR C 311 ? 0.7279 0.5437 0.5231 -0.0425 -0.0507 0.2118  311  TYR C C   
8234  O  O   . TYR C 311 ? 0.7708 0.5502 0.5474 -0.0503 -0.0546 0.2245  311  TYR C O   
8235  C  CB  . TYR C 311 ? 0.7543 0.5111 0.5420 -0.0249 -0.0544 0.1962  311  TYR C CB  
8236  C  CG  . TYR C 311 ? 0.7131 0.4626 0.5049 -0.0420 -0.0550 0.1888  311  TYR C CG  
8237  C  CD1 . TYR C 311 ? 0.6072 0.3226 0.3918 -0.0379 -0.0573 0.1798  311  TYR C CD1 
8238  C  CD2 . TYR C 311 ? 0.6978 0.4763 0.5004 -0.0617 -0.0534 0.1908  311  TYR C CD2 
8239  C  CE1 . TYR C 311 ? 0.7554 0.4651 0.5427 -0.0537 -0.0591 0.1733  311  TYR C CE1 
8240  C  CE2 . TYR C 311 ? 0.6290 0.4040 0.4367 -0.0767 -0.0549 0.1846  311  TYR C CE2 
8241  C  CZ  . TYR C 311 ? 0.6796 0.4198 0.4793 -0.0730 -0.0583 0.1761  311  TYR C CZ  
8242  O  OH  . TYR C 311 ? 0.6048 0.3425 0.4087 -0.0880 -0.0610 0.1700  311  TYR C OH  
8243  N  N   . PRO C 312 ? 0.8067 0.6685 0.6150 -0.0491 -0.0463 0.2105  312  PRO C N   
8244  C  CA  . PRO C 312 ? 0.8243 0.6983 0.6252 -0.0651 -0.0452 0.2252  312  PRO C CA  
8245  C  C   . PRO C 312 ? 0.9000 0.7692 0.7035 -0.0874 -0.0447 0.2269  312  PRO C C   
8246  O  O   . PRO C 312 ? 0.9640 0.8179 0.7733 -0.0893 -0.0464 0.2168  312  PRO C O   
8247  C  CB  . PRO C 312 ? 0.7150 0.6420 0.5297 -0.0619 -0.0398 0.2195  312  PRO C CB  
8248  C  CG  . PRO C 312 ? 0.8842 0.8227 0.7131 -0.0446 -0.0391 0.2024  312  PRO C CG  
8249  C  CD  . PRO C 312 ? 0.8272 0.7304 0.6561 -0.0422 -0.0418 0.1955  312  PRO C CD  
8250  N  N   . ALA C 313 ? 0.8937 0.7778 0.6928 -0.1044 -0.0426 0.2399  313  ALA C N   
8251  C  CA  . ALA C 313 ? 0.9284 0.8140 0.7317 -0.1276 -0.0422 0.2433  313  ALA C CA  
8252  C  C   . ALA C 313 ? 0.8133 0.7522 0.6406 -0.1334 -0.0355 0.2330  313  ALA C C   
8253  O  O   . ALA C 313 ? 0.7449 0.7211 0.5804 -0.1240 -0.0303 0.2281  313  ALA C O   
8254  C  CB  . ALA C 313 ? 0.9922 0.8634 0.7774 -0.1449 -0.0433 0.2646  313  ALA C CB  
8255  N  N   . ALA C 314 ? 0.6788 0.6204 0.5164 -0.1487 -0.0363 0.2296  314  ALA C N   
8256  C  CA  . ALA C 314 ? 0.6108 0.6000 0.4722 -0.1531 -0.0307 0.2197  314  ALA C CA  
8257  C  C   . ALA C 314 ? 0.6415 0.6792 0.5094 -0.1542 -0.0223 0.2233  314  ALA C C   
8258  O  O   . ALA C 314 ? 0.5902 0.6634 0.4736 -0.1436 -0.0171 0.2104  314  ALA C O   
8259  C  CB  . ALA C 314 ? 0.6537 0.6403 0.5218 -0.1745 -0.0337 0.2225  314  ALA C CB  
8260  N  N   . SER C 315 ? 0.6541 0.6916 0.5084 -0.1673 -0.0209 0.2409  315  SER C N   
8261  C  CA  . SER C 315 ? 0.6326 0.7163 0.4902 -0.1710 -0.0124 0.2459  315  SER C CA  
8262  C  C   . SER C 315 ? 0.5601 0.6619 0.4178 -0.1493 -0.0093 0.2355  315  SER C C   
8263  O  O   . SER C 315 ? 0.5090 0.6540 0.3749 -0.1464 -0.0018 0.2302  315  SER C O   
8264  C  CB  . SER C 315 ? 0.5659 0.6374 0.4032 -0.1868 -0.0124 0.2684  315  SER C CB  
8265  O  OG  . SER C 315 ? 0.6502 0.6790 0.4656 -0.1762 -0.0188 0.2757  315  SER C OG  
8266  N  N   . THR C 316 ? 0.5103 0.5787 0.3585 -0.1342 -0.0155 0.2322  316  THR C N   
8267  C  CA  . THR C 316 ? 0.5572 0.6398 0.4065 -0.1143 -0.0144 0.2216  316  THR C CA  
8268  C  C   . THR C 316 ? 0.5768 0.6856 0.4478 -0.1056 -0.0108 0.2010  316  THR C C   
8269  O  O   . THR C 316 ? 0.6465 0.7867 0.5222 -0.0968 -0.0061 0.1922  316  THR C O   
8270  C  CB  . THR C 316 ? 0.6762 0.7177 0.5129 -0.1006 -0.0219 0.2235  316  THR C CB  
8271  O  OG1 . THR C 316 ? 0.7113 0.7440 0.5275 -0.1005 -0.0238 0.2403  316  THR C OG1 
8272  C  CG2 . THR C 316 ? 0.7332 0.7844 0.5803 -0.0813 -0.0222 0.2063  316  THR C CG2 
8273  N  N   . LEU C 317 ? 0.4910 0.5850 0.3733 -0.1084 -0.0133 0.1937  317  LEU C N   
8274  C  CA  . LEU C 317 ? 0.5564 0.6672 0.4580 -0.0996 -0.0113 0.1752  317  LEU C CA  
8275  C  C   . LEU C 317 ? 0.5216 0.6796 0.4364 -0.0973 -0.0032 0.1660  317  LEU C C   
8276  O  O   . LEU C 317 ? 0.4594 0.6282 0.3817 -0.0838 -0.0016 0.1515  317  LEU C O   
8277  C  CB  . LEU C 317 ? 0.4248 0.5191 0.3354 -0.1081 -0.0150 0.1726  317  LEU C CB  
8278  C  CG  . LEU C 317 ? 0.4863 0.5311 0.3833 -0.1100 -0.0229 0.1783  317  LEU C CG  
8279  C  CD1 . LEU C 317 ? 0.7673 0.8024 0.6723 -0.1218 -0.0264 0.1761  317  LEU C CD1 
8280  C  CD2 . LEU C 317 ? 0.4531 0.4760 0.3461 -0.0911 -0.0257 0.1692  317  LEU C CD2 
8281  N  N   . PRO C 318 ? 0.5169 0.7026 0.4346 -0.1105 0.0023  0.1741  318  PRO C N   
8282  C  CA  . PRO C 318 ? 0.5472 0.7780 0.4762 -0.1064 0.0110  0.1647  318  PRO C CA  
8283  C  C   . PRO C 318 ? 0.6457 0.8903 0.5645 -0.0940 0.0140  0.1590  318  PRO C C   
8284  O  O   . PRO C 318 ? 0.5742 0.8398 0.5022 -0.0833 0.0181  0.1433  318  PRO C O   
8285  C  CB  . PRO C 318 ? 0.5529 0.8085 0.4831 -0.1243 0.0163  0.1783  318  PRO C CB  
8286  C  CG  . PRO C 318 ? 0.5819 0.8064 0.5105 -0.1386 0.0093  0.1892  318  PRO C CG  
8287  C  CD  . PRO C 318 ? 0.6156 0.7933 0.5283 -0.1303 0.0010  0.1907  318  PRO C CD  
8288  N  N   . GLN C 319 ? 0.5247 0.7567 0.4241 -0.0956 0.0114  0.1716  319  GLN C N   
8289  C  CA  . GLN C 319 ? 0.4724 0.7146 0.3608 -0.0840 0.0118  0.1669  319  GLN C CA  
8290  C  C   . GLN C 319 ? 0.4870 0.7139 0.3814 -0.0688 0.0070  0.1515  319  GLN C C   
8291  O  O   . GLN C 319 ? 0.4102 0.6566 0.3078 -0.0596 0.0097  0.1374  319  GLN C O   
8292  C  CB  . GLN C 319 ? 0.7668 0.9927 0.6333 -0.0875 0.0077  0.1850  319  GLN C CB  
8293  C  CG  . GLN C 319 ? 0.9694 1.2230 0.8235 -0.0975 0.0140  0.1974  319  GLN C CG  
8294  C  CD  . GLN C 319 ? 1.2152 1.4523 1.0611 -0.1150 0.0131  0.2184  319  GLN C CD  
8295  O  OE1 . GLN C 319 ? 1.3175 1.5587 1.1453 -0.1223 0.0144  0.2348  319  GLN C OE1 
8296  N  NE2 . GLN C 319 ? 1.2251 1.4422 1.0828 -0.1225 0.0105  0.2185  319  GLN C NE2 
8297  N  N   . GLU C 320 ? 0.5664 0.7576 0.4610 -0.0669 0.0000  0.1544  320  GLU C N   
8298  C  CA  . GLU C 320 ? 0.6358 0.8118 0.5369 -0.0538 -0.0041 0.1414  320  GLU C CA  
8299  C  C   . GLU C 320 ? 0.4968 0.6906 0.4148 -0.0489 0.0000  0.1231  320  GLU C C   
8300  O  O   . GLU C 320 ? 0.6083 0.8071 0.5293 -0.0388 -0.0005 0.1105  320  GLU C O   
8301  C  CB  . GLU C 320 ? 0.5821 0.7186 0.4822 -0.0536 -0.0104 0.1464  320  GLU C CB  
8302  C  CG  . GLU C 320 ? 0.7075 0.8184 0.5896 -0.0560 -0.0153 0.1639  320  GLU C CG  
8303  C  CD  . GLU C 320 ? 0.7855 0.8981 0.6576 -0.0443 -0.0185 0.1661  320  GLU C CD  
8304  O  OE1 . GLU C 320 ? 0.7825 0.9178 0.6612 -0.0361 -0.0170 0.1537  320  GLU C OE1 
8305  O  OE2 . GLU C 320 ? 0.7564 0.8469 0.6136 -0.0433 -0.0230 0.1805  320  GLU C OE2 
8306  N  N   . TRP C 321 ? 0.3970 0.6001 0.3260 -0.0563 0.0036  0.1222  321  TRP C N   
8307  C  CA  . TRP C 321 ? 0.4881 0.7085 0.4326 -0.0507 0.0077  0.1063  321  TRP C CA  
8308  C  C   . TRP C 321 ? 0.6445 0.8941 0.5869 -0.0440 0.0134  0.0959  321  TRP C C   
8309  O  O   . TRP C 321 ? 0.4879 0.7381 0.4359 -0.0344 0.0135  0.0807  321  TRP C O   
8310  C  CB  . TRP C 321 ? 0.4396 0.6731 0.3963 -0.0599 0.0109  0.1093  321  TRP C CB  
8311  C  CG  . TRP C 321 ? 0.5495 0.8064 0.5209 -0.0524 0.0161  0.0944  321  TRP C CG  
8312  C  CD1 . TRP C 321 ? 0.4714 0.7640 0.4480 -0.0528 0.0242  0.0914  321  TRP C CD1 
8313  C  CD2 . TRP C 321 ? 0.6975 0.9427 0.6790 -0.0421 0.0139  0.0802  321  TRP C CD2 
8314  N  NE1 . TRP C 321 ? 0.5600 0.8624 0.5496 -0.0422 0.0269  0.0759  321  TRP C NE1 
8315  C  CE2 . TRP C 321 ? 0.6319 0.9045 0.6242 -0.0361 0.0204  0.0693  321  TRP C CE2 
8316  C  CE3 . TRP C 321 ? 0.6504 0.8645 0.6320 -0.0371 0.0076  0.0762  321  TRP C CE3 
8317  C  CZ2 . TRP C 321 ? 0.5616 0.8282 0.5641 -0.0255 0.0199  0.0552  321  TRP C CZ2 
8318  C  CZ3 . TRP C 321 ? 0.5045 0.7151 0.4964 -0.0280 0.0076  0.0627  321  TRP C CZ3 
8319  C  CH2 . TRP C 321 ? 0.4421 0.6771 0.4439 -0.0224 0.0133  0.0526  321  TRP C CH2 
8320  N  N   . GLN C 322 ? 0.6953 0.9676 0.6280 -0.0499 0.0180  0.1041  322  GLN C N   
8321  C  CA  . GLN C 322 ? 0.6420 0.9444 0.5704 -0.0446 0.0244  0.0940  322  GLN C CA  
8322  C  C   . GLN C 322 ? 0.6390 0.9349 0.5573 -0.0358 0.0202  0.0858  322  GLN C C   
8323  O  O   . GLN C 322 ? 0.6381 0.9478 0.5567 -0.0285 0.0232  0.0702  322  GLN C O   
8324  C  CB  . GLN C 322 ? 0.6257 0.9541 0.5437 -0.0538 0.0306  0.1064  322  GLN C CB  
8325  C  CG  . GLN C 322 ? 0.7466 1.1116 0.6728 -0.0524 0.0411  0.0974  322  GLN C CG  
8326  C  CD  . GLN C 322 ? 0.8188 1.1874 0.7663 -0.0552 0.0431  0.0961  322  GLN C CD  
8327  O  OE1 . GLN C 322 ? 0.7951 1.1777 0.7553 -0.0463 0.0475  0.0814  322  GLN C OE1 
8328  N  NE2 . GLN C 322 ? 0.7692 1.1241 0.7197 -0.0675 0.0392  0.1115  322  GLN C NE2 
8329  N  N   . ARG C 323 ? 0.5297 0.8042 0.4390 -0.0364 0.0129  0.0962  323  ARG C N   
8330  C  CA  . ARG C 323 ? 0.4256 0.6954 0.3273 -0.0288 0.0075  0.0906  323  ARG C CA  
8331  C  C   . ARG C 323 ? 0.5903 0.8445 0.5047 -0.0212 0.0043  0.0760  323  ARG C C   
8332  O  O   . ARG C 323 ? 0.5230 0.7852 0.4367 -0.0157 0.0036  0.0625  323  ARG C O   
8333  C  CB  . ARG C 323 ? 0.5001 0.7525 0.3902 -0.0303 0.0008  0.1078  323  ARG C CB  
8334  C  CG  . ARG C 323 ? 0.5194 0.7819 0.3952 -0.0391 0.0033  0.1250  323  ARG C CG  
8335  C  CD  . ARG C 323 ? 0.6564 0.8932 0.5215 -0.0396 -0.0038 0.1425  323  ARG C CD  
8336  N  NE  . ARG C 323 ? 0.7005 0.9453 0.5480 -0.0474 -0.0026 0.1601  323  ARG C NE  
8337  C  CZ  . ARG C 323 ? 0.9737 1.1949 0.8088 -0.0490 -0.0082 0.1781  323  ARG C CZ  
8338  N  NH1 . ARG C 323 ? 0.9621 1.1517 0.8010 -0.0422 -0.0149 0.1795  323  ARG C NH1 
8339  N  NH2 . ARG C 323 ? 1.1592 1.3874 0.9770 -0.0568 -0.0069 0.1949  323  ARG C NH2 
8340  N  N   . ASN C 324 ? 0.4412 0.6724 0.3659 -0.0219 0.0022  0.0787  324  ASN C N   
8341  C  CA  . ASN C 324 ? 0.4447 0.6593 0.3799 -0.0156 -0.0007 0.0674  324  ASN C CA  
8342  C  C   . ASN C 324 ? 0.4645 0.6865 0.4112 -0.0129 0.0039  0.0521  324  ASN C C   
8343  O  O   . ASN C 324 ? 0.4328 0.6447 0.3859 -0.0078 0.0022  0.0407  324  ASN C O   
8344  C  CB  . ASN C 324 ? 0.4397 0.6257 0.3783 -0.0165 -0.0049 0.0762  324  ASN C CB  
8345  C  CG  . ASN C 324 ? 0.4813 0.6549 0.4085 -0.0155 -0.0100 0.0892  324  ASN C CG  
8346  O  OD1 . ASN C 324 ? 0.5528 0.7162 0.4807 -0.0087 -0.0142 0.0871  324  ASN C OD1 
8347  N  ND2 . ASN C 324 ? 0.5296 0.7052 0.4464 -0.0218 -0.0097 0.1034  324  ASN C ND2 
8348  N  N   . LYS C 325 ? 0.4162 0.6561 0.3654 -0.0162 0.0098  0.0525  325  LYS C N   
8349  C  CA  . LYS C 325 ? 0.4025 0.6510 0.3631 -0.0120 0.0146  0.0396  325  LYS C CA  
8350  C  C   . LYS C 325 ? 0.4068 0.6562 0.3663 -0.0042 0.0150  0.0221  325  LYS C C   
8351  O  O   . LYS C 325 ? 0.4964 0.7306 0.4646 0.0004  0.0136  0.0128  325  LYS C O   
8352  C  CB  . LYS C 325 ? 0.4354 0.7122 0.3962 -0.0155 0.0219  0.0428  325  LYS C CB  
8353  C  CG  . LYS C 325 ? 0.4593 0.7470 0.4345 -0.0108 0.0270  0.0334  325  LYS C CG  
8354  C  CD  . LYS C 325 ? 0.4201 0.7412 0.3957 -0.0142 0.0351  0.0376  325  LYS C CD  
8355  C  CE  . LYS C 325 ? 0.5155 0.8524 0.5064 -0.0073 0.0406  0.0283  325  LYS C CE  
8356  N  NZ  . LYS C 325 ? 0.6647 1.0386 0.6564 -0.0109 0.0495  0.0334  325  LYS C NZ  
8357  N  N   . ALA C 326 ? 0.5102 0.7764 0.4576 -0.0037 0.0166  0.0180  326  ALA C N   
8358  C  CA  . ALA C 326 ? 0.6657 0.9321 0.6089 0.0016  0.0161  0.0011  326  ALA C CA  
8359  C  C   . ALA C 326 ? 0.5942 0.8389 0.5401 0.0022  0.0088  -0.0019 326  ALA C C   
8360  O  O   . ALA C 326 ? 0.4067 0.6417 0.3560 0.0055  0.0082  -0.0158 326  ALA C O   
8361  C  CB  . ALA C 326 ? 0.3675 0.6575 0.2941 0.0007  0.0183  -0.0019 326  ALA C CB  
8362  N  N   . SER C 327 ? 0.5178 0.7549 0.4616 -0.0009 0.0035  0.0113  327  SER C N   
8363  C  CA  . SER C 327 ? 0.3616 0.5839 0.3081 0.0000  -0.0027 0.0100  327  SER C CA  
8364  C  C   . SER C 327 ? 0.3559 0.5555 0.3151 0.0017  -0.0031 0.0082  327  SER C C   
8365  O  O   . SER C 327 ? 0.5043 0.6928 0.4680 0.0028  -0.0059 0.0015  327  SER C O   
8366  C  CB  . SER C 327 ? 0.3119 0.5338 0.2525 -0.0012 -0.0078 0.0252  327  SER C CB  
8367  O  OG  . SER C 327 ? 0.4390 0.6810 0.3663 -0.0031 -0.0078 0.0309  327  SER C OG  
8368  N  N   . LEU C 328 ? 0.3481 0.5420 0.3125 0.0010  -0.0004 0.0148  328  LEU C N   
8369  C  CA  . LEU C 328 ? 0.4210 0.5940 0.3955 0.0024  -0.0012 0.0141  328  LEU C CA  
8370  C  C   . LEU C 328 ? 0.4439 0.6142 0.4246 0.0063  0.0015  -0.0002 328  LEU C C   
8371  O  O   . LEU C 328 ? 0.4387 0.5909 0.4251 0.0080  -0.0003 -0.0045 328  LEU C O   
8372  C  CB  . LEU C 328 ? 0.2802 0.4492 0.2575 -0.0008 -0.0004 0.0255  328  LEU C CB  
8373  C  CG  . LEU C 328 ? 0.2459 0.4027 0.2175 -0.0039 -0.0043 0.0397  328  LEU C CG  
8374  C  CD1 . LEU C 328 ? 0.2732 0.4333 0.2427 -0.0103 -0.0032 0.0514  328  LEU C CD1 
8375  C  CD2 . LEU C 328 ? 0.2517 0.3837 0.2274 -0.0014 -0.0076 0.0396  328  LEU C CD2 
8376  N  N   . LEU C 329 ? 0.3263 0.5141 0.3048 0.0082  0.0060  -0.0073 329  LEU C N   
8377  C  CA  . LEU C 329 ? 0.4859 0.6703 0.4684 0.0139  0.0089  -0.0215 329  LEU C CA  
8378  C  C   . LEU C 329 ? 0.4804 0.6569 0.4573 0.0141  0.0065  -0.0337 329  LEU C C   
8379  O  O   . LEU C 329 ? 0.6304 0.7883 0.6116 0.0162  0.0054  -0.0414 329  LEU C O   
8380  C  CB  . LEU C 329 ? 0.5617 0.7690 0.5428 0.0174  0.0153  -0.0259 329  LEU C CB  
8381  C  CG  . LEU C 329 ? 0.5427 0.7585 0.5345 0.0188  0.0186  -0.0191 329  LEU C CG  
8382  C  CD1 . LEU C 329 ? 0.5539 0.7493 0.5537 0.0156  0.0135  -0.0093 329  LEU C CD1 
8383  C  CD2 . LEU C 329 ? 0.5043 0.7469 0.4921 0.0141  0.0227  -0.0098 329  LEU C CD2 
8384  N  N   . GLN C 330 ? 0.2740 0.4650 0.2408 0.0109  0.0053  -0.0347 330  GLN C N   
8385  C  CA  . GLN C 330 ? 0.4541 0.6421 0.4145 0.0091  0.0023  -0.0468 330  GLN C CA  
8386  C  C   . GLN C 330 ? 0.5078 0.6797 0.4739 0.0053  -0.0032 -0.0443 330  GLN C C   
8387  O  O   . GLN C 330 ? 0.5834 0.7448 0.5492 0.0032  -0.0051 -0.0552 330  GLN C O   
8388  C  CB  . GLN C 330 ? 0.6722 0.8828 0.6193 0.0064  0.0014  -0.0477 330  GLN C CB  
8389  C  CG  . GLN C 330 ? 0.6450 0.8735 0.5838 0.0102  0.0080  -0.0541 330  GLN C CG  
8390  C  CD  . GLN C 330 ? 0.6758 0.8944 0.6131 0.0157  0.0115  -0.0728 330  GLN C CD  
8391  O  OE1 . GLN C 330 ? 0.5679 0.7789 0.4974 0.0137  0.0085  -0.0859 330  GLN C OE1 
8392  N  NE2 . GLN C 330 ? 0.8366 1.0550 0.7811 0.0228  0.0176  -0.0739 330  GLN C NE2 
8393  N  N   . LEU C 331 ? 0.4194 0.5890 0.3902 0.0042  -0.0053 -0.0301 331  LEU C N   
8394  C  CA  . LEU C 331 ? 0.2948 0.4501 0.2722 0.0022  -0.0089 -0.0269 331  LEU C CA  
8395  C  C   . LEU C 331 ? 0.2763 0.4096 0.2606 0.0038  -0.0071 -0.0327 331  LEU C C   
8396  O  O   . LEU C 331 ? 0.3348 0.4578 0.3208 0.0010  -0.0086 -0.0404 331  LEU C O   
8397  C  CB  . LEU C 331 ? 0.1502 0.3044 0.1296 0.0030  -0.0105 -0.0112 331  LEU C CB  
8398  C  CG  . LEU C 331 ? 0.3219 0.4687 0.3066 0.0023  -0.0137 -0.0074 331  LEU C CG  
8399  C  CD1 . LEU C 331 ? 0.3006 0.4464 0.2842 0.0052  -0.0152 0.0071  331  LEU C CD1 
8400  C  CD2 . LEU C 331 ? 0.7150 0.8412 0.7068 0.0022  -0.0122 -0.0117 331  LEU C CD2 
8401  N  N   . LEU C 332 ? 0.2343 0.3611 0.2223 0.0076  -0.0044 -0.0282 332  LEU C N   
8402  C  CA  . LEU C 332 ? 0.3154 0.4226 0.3089 0.0104  -0.0032 -0.0326 332  LEU C CA  
8403  C  C   . LEU C 332 ? 0.3411 0.4401 0.3320 0.0106  -0.0027 -0.0473 332  LEU C C   
8404  O  O   . LEU C 332 ? 0.3635 0.4436 0.3566 0.0088  -0.0040 -0.0505 332  LEU C O   
8405  C  CB  . LEU C 332 ? 0.4896 0.6000 0.4867 0.0150  -0.0005 -0.0289 332  LEU C CB  
8406  C  CG  . LEU C 332 ? 0.5072 0.6169 0.5066 0.0131  -0.0019 -0.0147 332  LEU C CG  
8407  C  CD1 . LEU C 332 ? 0.3572 0.4707 0.3620 0.0157  -0.0001 -0.0113 332  LEU C CD1 
8408  C  CD2 . LEU C 332 ? 0.4831 0.5728 0.4841 0.0116  -0.0046 -0.0107 332  LEU C CD2 
8409  N  N   . ARG C 333 ? 0.4172 0.5293 0.4018 0.0125  -0.0007 -0.0562 333  ARG C N   
8410  C  CA  . ARG C 333 ? 0.3517 0.4533 0.3310 0.0136  -0.0001 -0.0718 333  ARG C CA  
8411  C  C   . ARG C 333 ? 0.3149 0.4089 0.2912 0.0050  -0.0043 -0.0769 333  ARG C C   
8412  O  O   . ARG C 333 ? 0.7059 0.7833 0.6782 0.0035  -0.0049 -0.0888 333  ARG C O   
8413  C  CB  . ARG C 333 ? 0.3633 0.4828 0.3337 0.0175  0.0033  -0.0809 333  ARG C CB  
8414  C  CG  . ARG C 333 ? 0.6240 0.7526 0.5987 0.0267  0.0088  -0.0788 333  ARG C CG  
8415  C  CD  . ARG C 333 ? 0.7188 0.8508 0.6856 0.0342  0.0133  -0.0943 333  ARG C CD  
8416  N  NE  . ARG C 333 ? 0.6811 0.8239 0.6551 0.0440  0.0188  -0.0922 333  ARG C NE  
8417  C  CZ  . ARG C 333 ? 0.7459 0.8756 0.7246 0.0543  0.0212  -0.0990 333  ARG C CZ  
8418  N  NH1 . ARG C 333 ? 0.6960 0.7961 0.6710 0.0564  0.0188  -0.1092 333  ARG C NH1 
8419  N  NH2 . ARG C 333 ? 0.7993 0.9469 0.7868 0.0625  0.0258  -0.0949 333  ARG C NH2 
8420  N  N   . GLN C 334 ? 0.3239 0.4303 0.3024 -0.0007 -0.0075 -0.0679 334  GLN C N   
8421  C  CA  . GLN C 334 ? 0.2708 0.3754 0.2497 -0.0096 -0.0119 -0.0711 334  GLN C CA  
8422  C  C   . GLN C 334 ? 0.3513 0.4322 0.3372 -0.0122 -0.0119 -0.0694 334  GLN C C   
8423  O  O   . GLN C 334 ? 0.4754 0.5510 0.4624 -0.0208 -0.0146 -0.0735 334  GLN C O   
8424  C  CB  . GLN C 334 ? 0.4149 0.5416 0.3960 -0.0126 -0.0152 -0.0605 334  GLN C CB  
8425  C  CG  . GLN C 334 ? 0.3233 0.4743 0.2950 -0.0131 -0.0170 -0.0628 334  GLN C CG  
8426  C  CD  . GLN C 334 ? 0.4044 0.5606 0.3693 -0.0208 -0.0211 -0.0760 334  GLN C CD  
8427  O  OE1 . GLN C 334 ? 0.5743 0.7363 0.5440 -0.0282 -0.0259 -0.0751 334  GLN C OE1 
8428  N  NE2 . GLN C 334 ? 0.4633 0.6186 0.4170 -0.0194 -0.0194 -0.0888 334  GLN C NE2 
8429  N  N   . ALA C 335 ? 0.3032 0.3711 0.2934 -0.0058 -0.0091 -0.0628 335  ALA C N   
8430  C  CA  . ALA C 335 ? 0.4034 0.4484 0.3980 -0.0075 -0.0088 -0.0603 335  ALA C CA  
8431  C  C   . ALA C 335 ? 0.4709 0.4940 0.4605 -0.0086 -0.0087 -0.0727 335  ALA C C   
8432  O  O   . ALA C 335 ? 0.5116 0.5115 0.5023 -0.0093 -0.0083 -0.0717 335  ALA C O   
8433  C  CB  . ALA C 335 ? 0.4110 0.4489 0.4095 -0.0004 -0.0069 -0.0505 335  ALA C CB  
8434  N  N   . HIS C 336 ? 0.3087 0.3375 0.2909 -0.0084 -0.0090 -0.0846 336  HIS C N   
8435  C  CA  . HIS C 336 ? 0.3965 0.4011 0.3714 -0.0080 -0.0088 -0.0979 336  HIS C CA  
8436  C  C   . HIS C 336 ? 0.5266 0.5298 0.4945 -0.0197 -0.0125 -0.1090 336  HIS C C   
8437  O  O   . HIS C 336 ? 0.5113 0.4890 0.4716 -0.0221 -0.0132 -0.1204 336  HIS C O   
8438  C  CB  . HIS C 336 ? 0.4200 0.4254 0.3903 0.0047  -0.0053 -0.1050 336  HIS C CB  
8439  C  CG  . HIS C 336 ? 0.6329 0.6378 0.6112 0.0151  -0.0026 -0.0950 336  HIS C CG  
8440  N  ND1 . HIS C 336 ? 0.5952 0.5746 0.5761 0.0195  -0.0026 -0.0927 336  HIS C ND1 
8441  C  CD2 . HIS C 336 ? 0.6060 0.6331 0.5897 0.0206  -0.0005 -0.0861 336  HIS C CD2 
8442  C  CE1 . HIS C 336 ? 0.6251 0.6130 0.6133 0.0276  -0.0011 -0.0834 336  HIS C CE1 
8443  N  NE2 . HIS C 336 ? 0.6783 0.6946 0.6687 0.0277  0.0003  -0.0795 336  HIS C NE2 
8444  N  N   . ILE C 337 ? 0.3368 0.7421 0.3017 0.0006  -0.0015 -0.0579 337  ILE C N   
8445  C  CA  . ILE C 337 ? 0.2679 0.6899 0.2380 -0.0053 -0.0038 -0.0727 337  ILE C CA  
8446  C  C   . ILE C 337 ? 0.3036 0.6978 0.2823 -0.0120 -0.0017 -0.0787 337  ILE C C   
8447  O  O   . ILE C 337 ? 0.4261 0.7901 0.4061 -0.0120 0.0018  -0.0690 337  ILE C O   
8448  C  CB  . ILE C 337 ? 0.3922 0.8486 0.3630 -0.0068 -0.0078 -0.0644 337  ILE C CB  
8449  C  CG1 . ILE C 337 ? 0.3430 0.7883 0.3178 -0.0082 -0.0070 -0.0455 337  ILE C CG1 
8450  C  CG2 . ILE C 337 ? 0.4673 0.9553 0.4299 -0.0009 -0.0102 -0.0594 337  ILE C CG2 
8451  C  CD1 . ILE C 337 ? 0.3098 0.7888 0.2860 -0.0091 -0.0113 -0.0362 337  ILE C CD1 
8452  N  N   . GLY C 338 ? 0.3595 0.7640 0.3440 -0.0177 -0.0041 -0.0945 338  GLY C N   
8453  C  CA  . GLY C 338 ? 0.4185 0.8003 0.4130 -0.0249 -0.0026 -0.1004 338  GLY C CA  
8454  C  C   . GLY C 338 ? 0.3223 0.6707 0.3175 -0.0252 0.0003  -0.1117 338  GLY C C   
8455  O  O   . GLY C 338 ? 0.4152 0.7659 0.4064 -0.0228 -0.0009 -0.1264 338  GLY C O   
8456  N  N   . ILE C 339 ? 0.2257 0.5427 0.2259 -0.0280 0.0044  -0.1047 339  ILE C N   
8457  C  CA  . ILE C 339 ? 0.3703 0.6534 0.3722 -0.0292 0.0071  -0.1141 339  ILE C CA  
8458  C  C   . ILE C 339 ? 0.3486 0.5991 0.3473 -0.0266 0.0120  -0.0991 339  ILE C C   
8459  O  O   . ILE C 339 ? 0.3929 0.6459 0.3877 -0.0237 0.0132  -0.0817 339  ILE C O   
8460  C  CB  . ILE C 339 ? 0.4372 0.7112 0.4511 -0.0381 0.0063  -0.1265 339  ILE C CB  
8461  C  CG1 . ILE C 339 ? 0.3988 0.6707 0.4208 -0.0430 0.0086  -0.1132 339  ILE C CG1 
8462  C  CG2 . ILE C 339 ? 0.2695 0.5702 0.2854 -0.0410 0.0002  -0.1452 339  ILE C CG2 
8463  C  CD1 . ILE C 339 ? 0.2240 0.4882 0.2599 -0.0523 0.0080  -0.1229 339  ILE C CD1 
8464  N  N   . LYS C 340 ? 0.2409 0.4598 0.2408 -0.0276 0.0144  -0.1060 340  LYS C N   
8465  C  CA  . LYS C 340 ? 0.3094 0.4937 0.3057 -0.0257 0.0187  -0.0934 340  LYS C CA  
8466  C  C   . LYS C 340 ? 0.5000 0.6541 0.5011 -0.0294 0.0202  -0.1058 340  LYS C C   
8467  O  O   . LYS C 340 ? 0.3088 0.4690 0.3133 -0.0307 0.0175  -0.1234 340  LYS C O   
8468  C  CB  . LYS C 340 ? 0.3980 0.5802 0.3836 -0.0175 0.0185  -0.0826 340  LYS C CB  
8469  C  CG  . LYS C 340 ? 0.4169 0.6029 0.3997 -0.0132 0.0167  -0.0951 340  LYS C CG  
8470  C  CD  . LYS C 340 ? 0.3272 0.5077 0.3016 -0.0056 0.0168  -0.0822 340  LYS C CD  
8471  C  CE  . LYS C 340 ? 0.2757 0.4733 0.2479 -0.0001 0.0152  -0.0923 340  LYS C CE  
8472  N  NZ  . LYS C 340 ? 0.3915 0.5848 0.3574 0.0070  0.0150  -0.0781 340  LYS C NZ  
8473  N  N   . GLY C 341 ? 0.4012 0.5223 0.4021 -0.0309 0.0243  -0.0969 341  GLY C N   
8474  C  CA  . GLY C 341 ? 0.3041 0.3954 0.3102 -0.0349 0.0258  -0.1070 341  GLY C CA  
8475  C  C   . GLY C 341 ? 0.3649 0.4211 0.3688 -0.0361 0.0307  -0.0943 341  GLY C C   
8476  O  O   . GLY C 341 ? 0.2806 0.3320 0.2765 -0.0323 0.0328  -0.0776 341  GLY C O   
8477  N  N   . LEU C 342 ? 0.4540 0.4847 0.4643 -0.0413 0.0322  -0.1024 342  LEU C N   
8478  C  CA  . LEU C 342 ? 0.4971 0.4926 0.5049 -0.0428 0.0371  -0.0916 342  LEU C CA  
8479  C  C   . LEU C 342 ? 0.4499 0.4400 0.4696 -0.0513 0.0400  -0.0938 342  LEU C C   
8480  O  O   . LEU C 342 ? 0.4278 0.4277 0.4592 -0.0573 0.0372  -0.1084 342  LEU C O   
8481  C  CB  . LEU C 342 ? 0.3632 0.3277 0.3672 -0.0408 0.0367  -0.0962 342  LEU C CB  
8482  C  CG  . LEU C 342 ? 0.3453 0.3118 0.3388 -0.0323 0.0342  -0.0925 342  LEU C CG  
8483  C  CD1 . LEU C 342 ? 0.2780 0.2158 0.2707 -0.0309 0.0333  -0.0991 342  LEU C CD1 
8484  C  CD2 . LEU C 342 ? 0.2787 0.2409 0.2606 -0.0273 0.0358  -0.0723 342  LEU C CD2 
8485  N  N   . VAL C 343 ? 0.3887 0.3635 0.4055 -0.0517 0.0455  -0.0790 343  VAL C N   
8486  C  CA  . VAL C 343 ? 0.4872 0.4497 0.5148 -0.0592 0.0496  -0.0790 343  VAL C CA  
8487  C  C   . VAL C 343 ? 0.4336 0.3547 0.4552 -0.0591 0.0529  -0.0753 343  VAL C C   
8488  O  O   . VAL C 343 ? 0.4100 0.3123 0.4176 -0.0532 0.0554  -0.0626 343  VAL C O   
8489  C  CB  . VAL C 343 ? 0.4496 0.4227 0.4784 -0.0594 0.0546  -0.0647 343  VAL C CB  
8490  C  CG1 . VAL C 343 ? 0.3114 0.2693 0.3517 -0.0669 0.0598  -0.0633 343  VAL C CG1 
8491  C  CG2 . VAL C 343 ? 0.3568 0.3715 0.3919 -0.0597 0.0506  -0.0677 343  VAL C CG2 
8492  N  N   . THR C 344 ? 0.5750 0.4815 0.6071 -0.0657 0.0522  -0.0865 344  THR C N   
8493  C  CA  . THR C 344 ? 0.6330 0.5012 0.6597 -0.0655 0.0538  -0.0855 344  THR C CA  
8494  C  C   . THR C 344 ? 0.6240 0.4725 0.6620 -0.0741 0.0576  -0.0861 344  THR C C   
8495  O  O   . THR C 344 ? 0.5167 0.3827 0.5692 -0.0809 0.0578  -0.0903 344  THR C O   
8496  C  CB  . THR C 344 ? 0.6180 0.4827 0.6434 -0.0627 0.0477  -0.0993 344  THR C CB  
8497  O  OG1 . THR C 344 ? 0.8462 0.6750 0.8624 -0.0599 0.0489  -0.0941 344  THR C OG1 
8498  C  CG2 . THR C 344 ? 0.4600 0.3319 0.5009 -0.0698 0.0435  -0.1179 344  THR C CG2 
8499  N  N   . ASP C 345 ? 0.5762 0.3883 0.6073 -0.0737 0.0604  -0.0807 345  ASP C N   
8500  C  CA  . ASP C 345 ? 0.5914 0.3787 0.6310 -0.0812 0.0642  -0.0798 345  ASP C CA  
8501  C  C   . ASP C 345 ? 0.6303 0.4180 0.6863 -0.0886 0.0587  -0.0976 345  ASP C C   
8502  O  O   . ASP C 345 ? 0.4303 0.2362 0.4899 -0.0875 0.0520  -0.1117 345  ASP C O   
8503  C  CB  . ASP C 345 ? 0.5632 0.3107 0.5890 -0.0777 0.0664  -0.0717 345  ASP C CB  
8504  C  CG  . ASP C 345 ? 0.6518 0.3837 0.6647 -0.0746 0.0741  -0.0528 345  ASP C CG  
8505  O  OD1 . ASP C 345 ? 0.8076 0.5071 0.8070 -0.0714 0.0756  -0.0452 345  ASP C OD1 
8506  O  OD2 . ASP C 345 ? 0.8741 0.6254 0.8899 -0.0750 0.0785  -0.0457 345  ASP C OD2 
8507  N  N   . ALA C 346 ? 0.7971 0.5628 0.8622 -0.0961 0.0614  -0.0965 346  ALA C N   
8508  C  CA  . ALA C 346 ? 0.8127 0.5641 0.8890 -0.1019 0.0560  -0.1112 346  ALA C CA  
8509  C  C   . ALA C 346 ? 1.1142 0.8398 1.1767 -0.0951 0.0540  -0.1117 346  ALA C C   
8510  O  O   . ALA C 346 ? 1.3220 1.0472 1.3872 -0.0937 0.0476  -0.1262 346  ALA C O   
8511  C  CB  . ALA C 346 ? 0.5311 0.2629 0.6195 -0.1113 0.0599  -0.1067 346  ALA C CB  
8512  N  N   . SER C 347 ? 1.0861 0.7909 1.1333 -0.0903 0.0596  -0.0956 347  SER C N   
8513  C  CA  . SER C 347 ? 1.0056 0.6852 1.0382 -0.0834 0.0579  -0.0924 347  SER C CA  
8514  C  C   . SER C 347 ? 0.9762 0.6748 1.0027 -0.0755 0.0524  -0.0995 347  SER C C   
8515  O  O   . SER C 347 ? 1.0084 0.6890 1.0262 -0.0702 0.0497  -0.0992 347  SER C O   
8516  C  CB  . SER C 347 ? 0.9011 0.5601 0.9165 -0.0792 0.0644  -0.0727 347  SER C CB  
8517  O  OG  . SER C 347 ? 0.9365 0.5639 0.9490 -0.0812 0.0668  -0.0667 347  SER C OG  
8518  N  N   . GLY C 348 ? 0.7685 0.5036 0.7998 -0.0747 0.0506  -0.1051 348  GLY C N   
8519  C  CA  . GLY C 348 ? 0.6223 0.3788 0.6467 -0.0668 0.0465  -0.1091 348  GLY C CA  
8520  C  C   . GLY C 348 ? 0.6041 0.3561 0.6115 -0.0595 0.0494  -0.0916 348  GLY C C   
8521  O  O   . GLY C 348 ? 0.7738 0.5309 0.7727 -0.0523 0.0462  -0.0903 348  GLY C O   
8522  N  N   . PHE C 349 ? 0.3394 0.0815 0.3422 -0.0614 0.0553  -0.0777 349  PHE C N   
8523  C  CA  . PHE C 349 ? 0.5421 0.2794 0.5282 -0.0547 0.0580  -0.0609 349  PHE C CA  
8524  C  C   . PHE C 349 ? 0.5630 0.3322 0.5496 -0.0536 0.0603  -0.0549 349  PHE C C   
8525  O  O   . PHE C 349 ? 0.4459 0.2262 0.4425 -0.0591 0.0641  -0.0551 349  PHE C O   
8526  C  CB  . PHE C 349 ? 0.4220 0.1216 0.3983 -0.0556 0.0631  -0.0480 349  PHE C CB  
8527  C  CG  . PHE C 349 ? 0.4776 0.1631 0.4339 -0.0478 0.0635  -0.0327 349  PHE C CG  
8528  C  CD1 . PHE C 349 ? 0.4063 0.0706 0.3526 -0.0432 0.0591  -0.0304 349  PHE C CD1 
8529  C  CD2 . PHE C 349 ? 0.4958 0.1916 0.4437 -0.0446 0.0676  -0.0203 349  PHE C CD2 
8530  C  CE1 . PHE C 349 ? 0.4791 0.1423 0.4071 -0.0353 0.0582  -0.0158 349  PHE C CE1 
8531  C  CE2 . PHE C 349 ? 0.4478 0.1296 0.3767 -0.0373 0.0669  -0.0065 349  PHE C CE2 
8532  C  CZ  . PHE C 349 ? 0.4687 0.1371 0.3875 -0.0326 0.0618  -0.0045 349  PHE C CZ  
8533  N  N   . PRO C 350 ? 0.5111 0.2944 0.4873 -0.0463 0.0579  -0.0485 350  PRO C N   
8534  C  CA  . PRO C 350 ? 0.5310 0.3464 0.5071 -0.0441 0.0586  -0.0432 350  PRO C CA  
8535  C  C   . PRO C 350 ? 0.6104 0.4203 0.5848 -0.0458 0.0656  -0.0311 350  PRO C C   
8536  O  O   . PRO C 350 ? 0.4507 0.2294 0.4140 -0.0443 0.0697  -0.0204 350  PRO C O   
8537  C  CB  . PRO C 350 ? 0.4871 0.3033 0.4483 -0.0356 0.0551  -0.0338 350  PRO C CB  
8538  C  CG  . PRO C 350 ? 0.5275 0.3048 0.4781 -0.0335 0.0547  -0.0286 350  PRO C CG  
8539  C  CD  . PRO C 350 ? 0.5295 0.2937 0.4918 -0.0396 0.0545  -0.0423 350  PRO C CD  
8540  N  N   . ILE C 351 ? 0.6258 0.4662 0.6108 -0.0487 0.0670  -0.0328 351  ILE C N   
8541  C  CA  . ILE C 351 ? 0.4494 0.2905 0.4338 -0.0490 0.0740  -0.0206 351  ILE C CA  
8542  C  C   . ILE C 351 ? 0.5100 0.3705 0.4848 -0.0419 0.0730  -0.0103 351  ILE C C   
8543  O  O   . ILE C 351 ? 0.4972 0.3912 0.4788 -0.0416 0.0687  -0.0157 351  ILE C O   
8544  C  CB  . ILE C 351 ? 0.5408 0.4033 0.5453 -0.0572 0.0763  -0.0275 351  ILE C CB  
8545  C  CG1 . ILE C 351 ? 0.5322 0.3785 0.5486 -0.0651 0.0755  -0.0393 351  ILE C CG1 
8546  C  CG2 . ILE C 351 ? 0.4702 0.3317 0.4746 -0.0568 0.0846  -0.0136 351  ILE C CG2 
8547  C  CD1 . ILE C 351 ? 0.4573 0.3264 0.4953 -0.0741 0.0754  -0.0477 351  ILE C CD1 
8548  N  N   . ALA C 352 ? 0.4885 0.3272 0.4470 -0.0360 0.0767  0.0045  352  ALA C N   
8549  C  CA  . ALA C 352 ? 0.4745 0.3272 0.4228 -0.0289 0.0755  0.0155  352  ALA C CA  
8550  C  C   . ALA C 352 ? 0.6304 0.5051 0.5873 -0.0300 0.0808  0.0208  352  ALA C C   
8551  O  O   . ALA C 352 ? 0.6588 0.5260 0.6237 -0.0344 0.0877  0.0215  352  ALA C O   
8552  C  CB  . ALA C 352 ? 0.3345 0.1524 0.2607 -0.0219 0.0762  0.0289  352  ALA C CB  
8553  N  N   . ASP C 353 ? 0.6351 0.5379 0.5916 -0.0260 0.0777  0.0250  353  ASP C N   
8554  C  CA  . ASP C 353 ? 0.5947 0.5189 0.5585 -0.0257 0.0822  0.0317  353  ASP C CA  
8555  C  C   . ASP C 353 ? 0.4905 0.4390 0.4770 -0.0343 0.0838  0.0217  353  ASP C C   
8556  O  O   . ASP C 353 ? 0.5907 0.5512 0.5859 -0.0354 0.0893  0.0275  353  ASP C O   
8557  C  CB  . ASP C 353 ? 0.6312 0.5279 0.5832 -0.0212 0.0906  0.0455  353  ASP C CB  
8558  C  CG  . ASP C 353 ? 0.9192 0.8192 0.8575 -0.0124 0.0898  0.0586  353  ASP C CG  
8559  O  OD1 . ASP C 353 ? 1.0086 0.9319 0.9547 -0.0112 0.0928  0.0635  353  ASP C OD1 
8560  O  OD2 . ASP C 353 ? 1.1193 0.9987 1.0397 -0.0067 0.0856  0.0641  353  ASP C OD2 
8561  N  N   . ALA C 354 ? 0.5007 0.4557 0.4969 -0.0402 0.0789  0.0069  354  ALA C N   
8562  C  CA  . ALA C 354 ? 0.5053 0.4850 0.5226 -0.0487 0.0778  -0.0043 354  ALA C CA  
8563  C  C   . ALA C 354 ? 0.5220 0.5422 0.5460 -0.0477 0.0734  -0.0044 354  ALA C C   
8564  O  O   . ALA C 354 ? 0.5122 0.5419 0.5251 -0.0411 0.0698  0.0009  354  ALA C O   
8565  C  CB  . ALA C 354 ? 0.4100 0.3847 0.4330 -0.0540 0.0723  -0.0208 354  ALA C CB  
8566  N  N   . ASN C 355 ? 0.4853 0.5298 0.5281 -0.0546 0.0733  -0.0100 355  ASN C N   
8567  C  CA  . ASN C 355 ? 0.4877 0.5712 0.5376 -0.0545 0.0682  -0.0113 355  ASN C CA  
8568  C  C   . ASN C 355 ? 0.5007 0.6052 0.5613 -0.0609 0.0602  -0.0290 355  ASN C C   
8569  O  O   . ASN C 355 ? 0.5390 0.6373 0.6119 -0.0687 0.0599  -0.0391 355  ASN C O   
8570  C  CB  . ASN C 355 ? 0.5558 0.6551 0.6180 -0.0560 0.0734  -0.0017 355  ASN C CB  
8571  C  CG  . ASN C 355 ? 0.5551 0.6437 0.6040 -0.0470 0.0793  0.0158  355  ASN C CG  
8572  O  OD1 . ASN C 355 ? 0.6617 0.7312 0.7104 -0.0460 0.0879  0.0250  355  ASN C OD1 
8573  N  ND2 . ASN C 355 ? 0.4512 0.5513 0.4882 -0.0401 0.0746  0.0206  355  ASN C ND2 
8574  N  N   . VAL C 356 ? 0.3102 0.4385 0.3651 -0.0573 0.0534  -0.0326 356  VAL C N   
8575  C  CA  . VAL C 356 ? 0.3352 0.4887 0.3985 -0.0622 0.0456  -0.0489 356  VAL C CA  
8576  C  C   . VAL C 356 ? 0.4127 0.6057 0.4853 -0.0638 0.0417  -0.0472 356  VAL C C   
8577  O  O   . VAL C 356 ? 0.4839 0.6934 0.5484 -0.0576 0.0403  -0.0380 356  VAL C O   
8578  C  CB  . VAL C 356 ? 0.5058 0.6578 0.5557 -0.0572 0.0405  -0.0563 356  VAL C CB  
8579  C  CG1 . VAL C 356 ? 0.4690 0.6496 0.5254 -0.0610 0.0326  -0.0730 356  VAL C CG1 
8580  C  CG2 . VAL C 356 ? 0.4236 0.5373 0.4665 -0.0564 0.0434  -0.0594 356  VAL C CG2 
8581  N  N   . TYR C 357 ? 0.4000 0.6078 0.4902 -0.0725 0.0394  -0.0557 357  TYR C N   
8582  C  CA  . TYR C 357 ? 0.3841 0.6288 0.4853 -0.0753 0.0351  -0.0547 357  TYR C CA  
8583  C  C   . TYR C 357 ? 0.4745 0.7447 0.5784 -0.0791 0.0251  -0.0716 357  TYR C C   
8584  O  O   . TYR C 357 ? 0.3080 0.5673 0.4142 -0.0837 0.0219  -0.0868 357  TYR C O   
8585  C  CB  . TYR C 357 ? 0.3731 0.6204 0.4942 -0.0826 0.0388  -0.0506 357  TYR C CB  
8586  C  CG  . TYR C 357 ? 0.4630 0.6948 0.5839 -0.0786 0.0489  -0.0324 357  TYR C CG  
8587  C  CD1 . TYR C 357 ? 0.4706 0.6686 0.5915 -0.0798 0.0567  -0.0291 357  TYR C CD1 
8588  C  CD2 . TYR C 357 ? 0.4241 0.6752 0.5452 -0.0736 0.0508  -0.0186 357  TYR C CD2 
8589  C  CE1 . TYR C 357 ? 0.3679 0.5517 0.4873 -0.0755 0.0665  -0.0128 357  TYR C CE1 
8590  C  CE2 . TYR C 357 ? 0.3091 0.5456 0.4293 -0.0691 0.0604  -0.0026 357  TYR C CE2 
8591  C  CZ  . TYR C 357 ? 0.3393 0.5423 0.4581 -0.0699 0.0684  0.0000  357  TYR C CZ  
8592  O  OH  . TYR C 357 ? 0.5043 0.6930 0.6204 -0.0646 0.0782  0.0156  357  TYR C OH  
8593  N  N   . VAL C 358 ? 0.5939 0.8973 0.6972 -0.0771 0.0203  -0.0687 358  VAL C N   
8594  C  CA  . VAL C 358 ? 0.4825 0.8150 0.5892 -0.0811 0.0107  -0.0831 358  VAL C CA  
8595  C  C   . VAL C 358 ? 0.4806 0.8413 0.6050 -0.0877 0.0072  -0.0803 358  VAL C C   
8596  O  O   . VAL C 358 ? 0.4476 0.8205 0.5749 -0.0847 0.0103  -0.0650 358  VAL C O   
8597  C  CB  . VAL C 358 ? 0.3540 0.7051 0.4443 -0.0734 0.0066  -0.0826 358  VAL C CB  
8598  C  CG1 . VAL C 358 ? 0.3092 0.6927 0.4016 -0.0771 -0.0031 -0.0967 358  VAL C CG1 
8599  C  CG2 . VAL C 358 ? 0.2726 0.5982 0.3472 -0.0671 0.0093  -0.0854 358  VAL C CG2 
8600  N  N   . ALA C 359 ? 0.5090 0.8793 0.6454 -0.0965 0.0005  -0.0950 359  ALA C N   
8601  C  CA  . ALA C 359 ? 0.5136 0.9120 0.6679 -0.1037 -0.0045 -0.0936 359  ALA C CA  
8602  C  C   . ALA C 359 ? 0.3391 0.7714 0.4885 -0.0992 -0.0087 -0.0861 359  ALA C C   
8603  O  O   . ALA C 359 ? 0.3279 0.7763 0.4651 -0.0965 -0.0153 -0.0948 359  ALA C O   
8604  C  CB  . ALA C 359 ? 0.4248 0.8292 0.5889 -0.1133 -0.0138 -0.1128 359  ALA C CB  
8605  N  N   . GLY C 360 ? 0.2830 0.7262 0.4422 -0.0983 -0.0048 -0.0697 360  GLY C N   
8606  C  CA  . GLY C 360 ? 0.2129 0.6875 0.3691 -0.0942 -0.0086 -0.0608 360  GLY C CA  
8607  C  C   . GLY C 360 ? 0.2856 0.7510 0.4255 -0.0833 -0.0025 -0.0466 360  GLY C C   
8608  O  O   . GLY C 360 ? 0.4884 0.9764 0.6244 -0.0787 -0.0048 -0.0368 360  GLY C O   
8609  N  N   . LEU C 361 ? 0.2681 0.6994 0.3983 -0.0794 0.0048  -0.0452 361  LEU C N   
8610  C  CA  . LEU C 361 ? 0.3327 0.7497 0.4474 -0.0694 0.0105  -0.0315 361  LEU C CA  
8611  C  C   . LEU C 361 ? 0.4296 0.8108 0.5452 -0.0680 0.0207  -0.0237 361  LEU C C   
8612  O  O   . LEU C 361 ? 0.2982 0.6550 0.3987 -0.0610 0.0254  -0.0173 361  LEU C O   
8613  C  CB  . LEU C 361 ? 0.2134 0.6262 0.3094 -0.0645 0.0072  -0.0391 361  LEU C CB  
8614  C  CG  . LEU C 361 ? 0.2515 0.6991 0.3432 -0.0646 -0.0021 -0.0464 361  LEU C CG  
8615  C  CD1 . LEU C 361 ? 0.2951 0.7350 0.3705 -0.0604 -0.0039 -0.0558 361  LEU C CD1 
8616  C  CD2 . LEU C 361 ? 0.2338 0.7059 0.3239 -0.0598 -0.0038 -0.0308 361  LEU C CD2 
8617  N  N   . GLU C 362 ? 0.4795 0.8582 0.6130 -0.0748 0.0238  -0.0238 362  GLU C N   
8618  C  CA  . GLU C 362 ? 0.3859 0.7321 0.5220 -0.0746 0.0336  -0.0175 362  GLU C CA  
8619  C  C   . GLU C 362 ? 0.4259 0.7625 0.5555 -0.0660 0.0416  0.0016  362  GLU C C   
8620  O  O   . GLU C 362 ? 0.3683 0.6739 0.4924 -0.0631 0.0501  0.0080  362  GLU C O   
8621  C  CB  . GLU C 362 ? 0.3310 0.6808 0.4899 -0.0846 0.0344  -0.0218 362  GLU C CB  
8622  C  CG  . GLU C 362 ? 0.6080 0.9405 0.7696 -0.0919 0.0316  -0.0384 362  GLU C CG  
8623  C  CD  . GLU C 362 ? 0.8637 1.2192 1.0443 -0.1026 0.0232  -0.0504 362  GLU C CD  
8624  O  OE1 . GLU C 362 ? 0.9148 1.3032 1.1004 -0.1036 0.0164  -0.0504 362  GLU C OE1 
8625  O  OE2 . GLU C 362 ? 0.8843 1.2243 1.0747 -0.1102 0.0227  -0.0598 362  GLU C OE2 
8626  N  N   . GLU C 363 ? 0.4546 0.8170 0.5838 -0.0617 0.0386  0.0107  363  GLU C N   
8627  C  CA  . GLU C 363 ? 0.3661 0.7202 0.4884 -0.0528 0.0452  0.0285  363  GLU C CA  
8628  C  C   . GLU C 363 ? 0.2587 0.5885 0.3575 -0.0443 0.0463  0.0327  363  GLU C C   
8629  O  O   . GLU C 363 ? 0.3645 0.6760 0.4543 -0.0369 0.0524  0.0460  363  GLU C O   
8630  C  CB  . GLU C 363 ? 0.5582 0.9473 0.6886 -0.0509 0.0410  0.0372  363  GLU C CB  
8631  C  CG  . GLU C 363 ? 0.7588 1.1665 0.9136 -0.0571 0.0430  0.0397  363  GLU C CG  
8632  C  CD  . GLU C 363 ? 0.8751 1.3173 1.0386 -0.0550 0.0386  0.0488  363  GLU C CD  
8633  O  OE1 . GLU C 363 ? 0.7637 1.2313 0.9245 -0.0565 0.0288  0.0432  363  GLU C OE1 
8634  O  OE2 . GLU C 363 ? 1.0062 1.4503 1.1793 -0.0516 0.0451  0.0618  363  GLU C OE2 
8635  N  N   . LYS C 364 ? 0.3531 0.6827 0.4420 -0.0452 0.0401  0.0215  364  LYS C N   
8636  C  CA  . LYS C 364 ? 0.3375 0.6452 0.4056 -0.0378 0.0402  0.0253  364  LYS C CA  
8637  C  C   . LYS C 364 ? 0.3491 0.6320 0.4109 -0.0406 0.0404  0.0126  364  LYS C C   
8638  O  O   . LYS C 364 ? 0.5474 0.8379 0.6027 -0.0407 0.0344  0.0032  364  LYS C O   
8639  C  CB  . LYS C 364 ? 0.3980 0.7315 0.4580 -0.0336 0.0324  0.0283  364  LYS C CB  
8640  C  CG  . LYS C 364 ? 0.3524 0.6658 0.3925 -0.0262 0.0316  0.0339  364  LYS C CG  
8641  C  CD  . LYS C 364 ? 0.2921 0.5739 0.3234 -0.0199 0.0386  0.0480  364  LYS C CD  
8642  C  CE  . LYS C 364 ? 0.3448 0.6089 0.3570 -0.0127 0.0361  0.0551  364  LYS C CE  
8643  N  NZ  . LYS C 364 ? 0.2454 0.4713 0.2462 -0.0072 0.0424  0.0657  364  LYS C NZ  
8644  N  N   . PRO C 365 ? 0.4584 0.7114 0.5223 -0.0425 0.0477  0.0128  365  PRO C N   
8645  C  CA  . PRO C 365 ? 0.4270 0.6525 0.4859 -0.0451 0.0487  0.0022  365  PRO C CA  
8646  C  C   . PRO C 365 ? 0.5268 0.7299 0.5654 -0.0374 0.0483  0.0071  365  PRO C C   
8647  O  O   . PRO C 365 ? 0.5625 0.7629 0.5909 -0.0303 0.0493  0.0210  365  PRO C O   
8648  C  CB  . PRO C 365 ? 0.5731 0.7733 0.6390 -0.0479 0.0576  0.0065  365  PRO C CB  
8649  C  CG  . PRO C 365 ? 0.5381 0.7551 0.6140 -0.0467 0.0616  0.0188  365  PRO C CG  
8650  C  CD  . PRO C 365 ? 0.6118 0.8541 0.6813 -0.0409 0.0561  0.0254  365  PRO C CD  
8651  N  N   . MET C 366 ? 0.4667 0.6539 0.5001 -0.0389 0.0463  -0.0038 366  MET C N   
8652  C  CA  . MET C 366 ? 0.3711 0.5338 0.3870 -0.0323 0.0461  0.0009  366  MET C CA  
8653  C  C   . MET C 366 ? 0.3312 0.4527 0.3418 -0.0322 0.0530  0.0045  366  MET C C   
8654  O  O   . MET C 366 ? 0.5293 0.6397 0.5491 -0.0385 0.0556  -0.0046 366  MET C O   
8655  C  CB  . MET C 366 ? 0.4204 0.5911 0.4330 -0.0328 0.0398  -0.0122 366  MET C CB  
8656  C  CG  . MET C 366 ? 0.3620 0.5716 0.3748 -0.0311 0.0329  -0.0140 366  MET C CG  
8657  S  SD  . MET C 366 ? 0.4398 0.6590 0.4407 -0.0224 0.0311  0.0058  366  MET C SD  
8658  C  CE  . MET C 366 ? 0.3317 0.5815 0.3457 -0.0251 0.0313  0.0115  366  MET C CE  
8659  N  N   . ARG C 367 ? 0.2983 0.3967 0.2938 -0.0251 0.0555  0.0180  367  ARG C N   
8660  C  CA  . ARG C 367 ? 0.4269 0.4846 0.4142 -0.0242 0.0615  0.0221  367  ARG C CA  
8661  C  C   . ARG C 367 ? 0.5258 0.5619 0.5020 -0.0223 0.0577  0.0172  367  ARG C C   
8662  O  O   . ARG C 367 ? 0.7026 0.7376 0.6668 -0.0163 0.0534  0.0239  367  ARG C O   
8663  C  CB  . ARG C 367 ? 0.5534 0.5948 0.5292 -0.0174 0.0663  0.0392  367  ARG C CB  
8664  C  CG  . ARG C 367 ? 0.6655 0.6669 0.6337 -0.0168 0.0742  0.0443  367  ARG C CG  
8665  C  CD  . ARG C 367 ? 0.9665 0.9334 0.9132 -0.0104 0.0725  0.0516  367  ARG C CD  
8666  N  NE  . ARG C 367 ? 1.0829 1.0557 1.0176 -0.0027 0.0683  0.0633  367  ARG C NE  
8667  C  CZ  . ARG C 367 ? 1.1365 1.0890 1.0565 0.0043  0.0711  0.0771  367  ARG C CZ  
8668  N  NH1 . ARG C 367 ? 1.2264 1.1882 1.1379 0.0103  0.0654  0.0861  367  ARG C NH1 
8669  N  NH2 . ARG C 367 ? 1.1463 1.0696 1.0595 0.0055  0.0791  0.0821  367  ARG C NH2 
8670  N  N   . THR C 368 ? 0.3277 0.3475 0.3093 -0.0276 0.0590  0.0059  368  THR C N   
8671  C  CA  . THR C 368 ? 0.3270 0.3282 0.3006 -0.0260 0.0553  0.0002  368  THR C CA  
8672  C  C   . THR C 368 ? 0.3708 0.3401 0.3262 -0.0194 0.0562  0.0137  368  THR C C   
8673  O  O   . THR C 368 ? 0.3213 0.2725 0.2698 -0.0171 0.0614  0.0251  368  THR C O   
8674  C  CB  . THR C 368 ? 0.2870 0.2702 0.2689 -0.0325 0.0570  -0.0128 368  THR C CB  
8675  O  OG1 . THR C 368 ? 0.3520 0.3044 0.3311 -0.0339 0.0641  -0.0055 368  THR C OG1 
8676  C  CG2 . THR C 368 ? 0.2640 0.2758 0.2637 -0.0398 0.0551  -0.0269 368  THR C CG2 
8677  N  N   . SER C 369 ? 0.3471 0.3096 0.2948 -0.0161 0.0510  0.0122  369  SER C N   
8678  C  CA  . SER C 369 ? 0.4475 0.3788 0.3784 -0.0104 0.0500  0.0239  369  SER C CA  
8679  C  C   . SER C 369 ? 0.5356 0.4272 0.4623 -0.0127 0.0541  0.0224  369  SER C C   
8680  O  O   . SER C 369 ? 0.6297 0.5190 0.5675 -0.0188 0.0579  0.0127  369  SER C O   
8681  C  CB  . SER C 369 ? 0.4065 0.3461 0.3335 -0.0068 0.0427  0.0226  369  SER C CB  
8682  O  OG  . SER C 369 ? 0.4926 0.4311 0.4278 -0.0104 0.0417  0.0078  369  SER C OG  
8683  N  N   . LYS C 370 ? 0.4856 0.3459 0.3964 -0.0080 0.0527  0.0326  370  LYS C N   
8684  C  CA  . LYS C 370 ? 0.4552 0.2759 0.3595 -0.0095 0.0558  0.0328  370  LYS C CA  
8685  C  C   . LYS C 370 ? 0.5278 0.3461 0.4429 -0.0143 0.0540  0.0178  370  LYS C C   
8686  O  O   . LYS C 370 ? 0.7063 0.4989 0.6226 -0.0182 0.0575  0.0141  370  LYS C O   
8687  C  CB  . LYS C 370 ? 0.4007 0.1909 0.2852 -0.0032 0.0524  0.0461  370  LYS C CB  
8688  C  CG  . LYS C 370 ? 0.5063 0.2897 0.3777 0.0018  0.0548  0.0607  370  LYS C CG  
8689  C  CD  . LYS C 370 ? 0.4941 0.2585 0.3481 0.0089  0.0490  0.0682  370  LYS C CD  
8690  C  CE  . LYS C 370 ? 0.5163 0.2881 0.3630 0.0151  0.0504  0.0744  370  LYS C CE  
8691  N  NZ  . LYS C 370 ? 0.6231 0.3892 0.4582 0.0213  0.0440  0.0741  370  LYS C NZ  
8692  N  N   . ARG C 371 ? 0.4135 0.2589 0.3363 -0.0139 0.0487  0.0093  371  ARG C N   
8693  C  CA  . ARG C 371 ? 0.4954 0.3408 0.4282 -0.0173 0.0466  -0.0057 371  ARG C CA  
8694  C  C   . ARG C 371 ? 0.5251 0.3992 0.4746 -0.0233 0.0481  -0.0199 371  ARG C C   
8695  O  O   . ARG C 371 ? 0.5527 0.4335 0.5117 -0.0260 0.0458  -0.0345 371  ARG C O   
8696  C  CB  . ARG C 371 ? 0.4781 0.3306 0.4077 -0.0124 0.0400  -0.0065 371  ARG C CB  
8697  C  CG  . ARG C 371 ? 0.5285 0.3570 0.4417 -0.0065 0.0371  0.0100  371  ARG C CG  
8698  C  CD  . ARG C 371 ? 0.7210 0.5398 0.6319 -0.0029 0.0313  0.0098  371  ARG C CD  
8699  N  NE  . ARG C 371 ? 0.8587 0.7129 0.7757 0.0001  0.0272  0.0061  371  ARG C NE  
8700  C  CZ  . ARG C 371 ? 0.9587 0.8236 0.8698 0.0053  0.0222  0.0172  371  ARG C CZ  
8701  N  NH1 . ARG C 371 ? 0.7884 0.6883 0.7070 0.0073  0.0196  0.0119  371  ARG C NH1 
8702  N  NH2 . ARG C 371 ? 1.0940 0.9357 0.9919 0.0085  0.0194  0.0333  371  ARG C NH2 
8703  N  N   . GLY C 372 ? 0.4541 0.3437 0.4074 -0.0253 0.0518  -0.0155 372  GLY C N   
8704  C  CA  . GLY C 372 ? 0.5067 0.4215 0.4761 -0.0317 0.0529  -0.0271 372  GLY C CA  
8705  C  C   . GLY C 372 ? 0.4792 0.4327 0.4547 -0.0307 0.0475  -0.0359 372  GLY C C   
8706  O  O   . GLY C 372 ? 0.4222 0.3950 0.4105 -0.0360 0.0461  -0.0496 372  GLY C O   
8707  N  N   . GLU C 373 ? 0.3758 0.3403 0.3418 -0.0241 0.0439  -0.0278 373  GLU C N   
8708  C  CA  . GLU C 373 ? 0.4233 0.4245 0.3934 -0.0226 0.0390  -0.0349 373  GLU C CA  
8709  C  C   . GLU C 373 ? 0.4543 0.4856 0.4276 -0.0229 0.0392  -0.0290 373  GLU C C   
8710  O  O   . GLU C 373 ? 0.4967 0.5204 0.4645 -0.0209 0.0420  -0.0150 373  GLU C O   
8711  C  CB  . GLU C 373 ? 0.4033 0.4048 0.3634 -0.0155 0.0349  -0.0286 373  GLU C CB  
8712  C  CG  . GLU C 373 ? 0.4855 0.4482 0.4359 -0.0128 0.0354  -0.0211 373  GLU C CG  
8713  C  CD  . GLU C 373 ? 0.5030 0.4682 0.4438 -0.0060 0.0309  -0.0102 373  GLU C CD  
8714  O  OE1 . GLU C 373 ? 0.4160 0.3994 0.3602 -0.0037 0.0275  -0.0175 373  GLU C OE1 
8715  O  OE2 . GLU C 373 ? 0.4554 0.4048 0.3853 -0.0027 0.0306  0.0056  373  GLU C OE2 
8716  N  N   . TYR C 374 ? 0.4200 0.4855 0.4016 -0.0249 0.0357  -0.0398 374  TYR C N   
8717  C  CA  . TYR C 374 ? 0.4415 0.5400 0.4269 -0.0251 0.0345  -0.0352 374  TYR C CA  
8718  C  C   . TYR C 374 ? 0.5270 0.6599 0.5129 -0.0230 0.0289  -0.0427 374  TYR C C   
8719  O  O   . TYR C 374 ? 0.4856 0.6214 0.4739 -0.0238 0.0267  -0.0572 374  TYR C O   
8720  C  CB  . TYR C 374 ? 0.3044 0.4105 0.3032 -0.0326 0.0370  -0.0415 374  TYR C CB  
8721  C  CG  . TYR C 374 ? 0.3797 0.5041 0.3893 -0.0381 0.0334  -0.0607 374  TYR C CG  
8722  C  CD1 . TYR C 374 ? 0.3055 0.4081 0.3203 -0.0425 0.0341  -0.0733 374  TYR C CD1 
8723  C  CD2 . TYR C 374 ? 0.4407 0.6035 0.4549 -0.0389 0.0287  -0.0664 374  TYR C CD2 
8724  C  CE1 . TYR C 374 ? 0.3527 0.4700 0.3766 -0.0473 0.0300  -0.0913 374  TYR C CE1 
8725  C  CE2 . TYR C 374 ? 0.3333 0.5113 0.3557 -0.0438 0.0246  -0.0846 374  TYR C CE2 
8726  C  CZ  . TYR C 374 ? 0.3552 0.5098 0.3822 -0.0478 0.0252  -0.0971 374  TYR C CZ  
8727  O  OH  . TYR C 374 ? 0.3494 0.5171 0.3837 -0.0523 0.0205  -0.1155 374  TYR C OH  
8728  N  N   . TRP C 375 ? 0.4458 0.6042 0.4289 -0.0199 0.0267  -0.0326 375  TRP C N   
8729  C  CA  . TRP C 375 ? 0.2777 0.4734 0.2620 -0.0187 0.0217  -0.0388 375  TRP C CA  
8730  C  C   . TRP C 375 ? 0.3082 0.5317 0.2998 -0.0219 0.0208  -0.0361 375  TRP C C   
8731  O  O   . TRP C 375 ? 0.3621 0.5844 0.3517 -0.0200 0.0223  -0.0212 375  TRP C O   
8732  C  CB  . TRP C 375 ? 0.2380 0.4408 0.2120 -0.0114 0.0189  -0.0273 375  TRP C CB  
8733  C  CG  . TRP C 375 ? 0.2541 0.4270 0.2210 -0.0076 0.0197  -0.0254 375  TRP C CG  
8734  C  CD1 . TRP C 375 ? 0.3266 0.5034 0.2914 -0.0045 0.0177  -0.0330 375  TRP C CD1 
8735  C  CD2 . TRP C 375 ? 0.3226 0.4575 0.2833 -0.0063 0.0225  -0.0148 375  TRP C CD2 
8736  N  NE1 . TRP C 375 ? 0.2260 0.3698 0.1850 -0.0016 0.0187  -0.0273 375  TRP C NE1 
8737  C  CE2 . TRP C 375 ? 0.3909 0.5081 0.3465 -0.0029 0.0213  -0.0162 375  TRP C CE2 
8738  C  CE3 . TRP C 375 ? 0.3437 0.4577 0.3020 -0.0074 0.0260  -0.0041 375  TRP C CE3 
8739  C  CZ2 . TRP C 375 ? 0.3238 0.4027 0.2720 -0.0011 0.0227  -0.0073 375  TRP C CZ2 
8740  C  CZ3 . TRP C 375 ? 0.2957 0.3714 0.2452 -0.0051 0.0279  0.0042  375  TRP C CZ3 
8741  C  CH2 . TRP C 375 ? 0.2599 0.3182 0.2044 -0.0023 0.0258  0.0027  375  TRP C CH2 
8742  N  N   . ARG C 376 ? 0.3883 0.6361 0.3882 -0.0265 0.0179  -0.0507 376  ARG C N   
8743  C  CA  . ARG C 376 ? 0.3023 0.5808 0.3098 -0.0298 0.0156  -0.0491 376  ARG C CA  
8744  C  C   . ARG C 376 ? 0.3622 0.6774 0.3660 -0.0273 0.0098  -0.0533 376  ARG C C   
8745  O  O   . ARG C 376 ? 0.2775 0.6031 0.2816 -0.0286 0.0070  -0.0693 376  ARG C O   
8746  C  CB  . ARG C 376 ? 0.3565 0.6343 0.3775 -0.0382 0.0161  -0.0615 376  ARG C CB  
8747  C  CG  . ARG C 376 ? 0.4384 0.7462 0.4695 -0.0425 0.0136  -0.0594 376  ARG C CG  
8748  C  CD  . ARG C 376 ? 0.3789 0.6840 0.4111 -0.0403 0.0174  -0.0405 376  ARG C CD  
8749  N  NE  . ARG C 376 ? 0.4696 0.8073 0.5121 -0.0437 0.0142  -0.0384 376  ARG C NE  
8750  C  CZ  . ARG C 376 ? 0.5154 0.8618 0.5597 -0.0412 0.0157  -0.0228 376  ARG C CZ  
8751  N  NH1 . ARG C 376 ? 0.6332 0.9573 0.6687 -0.0351 0.0204  -0.0083 376  ARG C NH1 
8752  N  NH2 . ARG C 376 ? 0.6061 0.9829 0.6610 -0.0447 0.0122  -0.0220 376  ARG C NH2 
8753  N  N   . LEU C 377 ? 0.3164 0.6497 0.3158 -0.0232 0.0081  -0.0385 377  LEU C N   
8754  C  CA  . LEU C 377 ? 0.3030 0.6729 0.2988 -0.0208 0.0028  -0.0398 377  LEU C CA  
8755  C  C   . LEU C 377 ? 0.3239 0.7214 0.3291 -0.0270 -0.0008 -0.0499 377  LEU C C   
8756  O  O   . LEU C 377 ? 0.3605 0.7591 0.3748 -0.0310 0.0002  -0.0448 377  LEU C O   
8757  C  CB  . LEU C 377 ? 0.2571 0.6377 0.2469 -0.0154 0.0014  -0.0199 377  LEU C CB  
8758  C  CG  . LEU C 377 ? 0.3481 0.7005 0.3288 -0.0096 0.0038  -0.0070 377  LEU C CG  
8759  C  CD1 . LEU C 377 ? 0.1565 0.5254 0.1315 -0.0046 0.0003  0.0112  377  LEU C CD1 
8760  C  CD2 . LEU C 377 ? 0.2191 0.5584 0.1943 -0.0071 0.0044  -0.0165 377  LEU C CD2 
8761  N  N   . LEU C 378 ? 0.3877 0.8073 0.3907 -0.0276 -0.0050 -0.0643 378  LEU C N   
8762  C  CA  . LEU C 378 ? 0.2989 0.7440 0.3098 -0.0338 -0.0097 -0.0753 378  LEU C CA  
8763  C  C   . LEU C 378 ? 0.2676 0.7490 0.2709 -0.0312 -0.0153 -0.0807 378  LEU C C   
8764  O  O   . LEU C 378 ? 0.3261 0.8098 0.3195 -0.0259 -0.0151 -0.0857 378  LEU C O   
8765  C  CB  . LEU C 378 ? 0.2390 0.6665 0.2570 -0.0399 -0.0095 -0.0939 378  LEU C CB  
8766  C  CG  . LEU C 378 ? 0.1861 0.5832 0.2147 -0.0450 -0.0048 -0.0915 378  LEU C CG  
8767  C  CD1 . LEU C 378 ? 0.2017 0.5828 0.2358 -0.0506 -0.0058 -0.1112 378  LEU C CD1 
8768  C  CD2 . LEU C 378 ? 0.1801 0.5917 0.2204 -0.0497 -0.0055 -0.0823 378  LEU C CD2 
8769  N  N   . THR C 379 ? 0.3581 0.8686 0.3665 -0.0347 -0.0201 -0.0791 379  THR C N   
8770  C  CA  . THR C 379 ? 0.4239 0.9696 0.4264 -0.0343 -0.0263 -0.0876 379  THR C CA  
8771  C  C   . THR C 379 ? 0.5041 1.0458 0.5057 -0.0376 -0.0287 -0.1113 379  THR C C   
8772  O  O   . THR C 379 ? 0.3859 0.9037 0.3963 -0.0429 -0.0273 -0.1200 379  THR C O   
8773  C  CB  . THR C 379 ? 0.4991 1.0724 0.5098 -0.0390 -0.0314 -0.0813 379  THR C CB  
8774  O  OG1 . THR C 379 ? 0.5750 1.1565 0.5841 -0.0346 -0.0303 -0.0601 379  THR C OG1 
8775  C  CG2 . THR C 379 ? 0.5751 1.1823 0.5807 -0.0407 -0.0389 -0.0939 379  THR C CG2 
8776  N  N   . PRO C 380 ? 0.3768 0.9413 0.3674 -0.0342 -0.0323 -0.1218 380  PRO C N   
8777  C  CA  . PRO C 380 ? 0.2737 0.8360 0.2626 -0.0372 -0.0358 -0.1453 380  PRO C CA  
8778  C  C   . PRO C 380 ? 0.4426 1.0073 0.4446 -0.0473 -0.0412 -0.1536 380  PRO C C   
8779  O  O   . PRO C 380 ? 0.2744 0.8568 0.2841 -0.0512 -0.0441 -0.1428 380  PRO C O   
8780  C  CB  . PRO C 380 ? 0.3096 0.9044 0.2842 -0.0318 -0.0395 -0.1511 380  PRO C CB  
8781  C  CG  . PRO C 380 ? 0.2880 0.8886 0.2558 -0.0239 -0.0349 -0.1318 380  PRO C CG  
8782  C  CD  . PRO C 380 ? 0.2878 0.8787 0.2665 -0.0270 -0.0331 -0.1126 380  PRO C CD  
8783  N  N   . GLY C 381 ? 0.4383 0.9849 0.4437 -0.0516 -0.0429 -0.1723 381  GLY C N   
8784  C  CA  . GLY C 381 ? 0.3280 0.8720 0.3476 -0.0618 -0.0481 -0.1803 381  GLY C CA  
8785  C  C   . GLY C 381 ? 0.4314 0.9383 0.4593 -0.0657 -0.0451 -0.1898 381  GLY C C   
8786  O  O   . GLY C 381 ? 0.5134 0.9969 0.5352 -0.0602 -0.0391 -0.1904 381  GLY C O   
8787  N  N   . LEU C 382 ? 0.3271 0.8285 0.3694 -0.0754 -0.0496 -0.1969 382  LEU C N   
8788  C  CA  . LEU C 382 ? 0.3382 0.8046 0.3897 -0.0799 -0.0470 -0.2049 382  LEU C CA  
8789  C  C   . LEU C 382 ? 0.4118 0.8654 0.4811 -0.0861 -0.0429 -0.1901 382  LEU C C   
8790  O  O   . LEU C 382 ? 0.3637 0.8380 0.4430 -0.0911 -0.0462 -0.1822 382  LEU C O   
8791  C  CB  . LEU C 382 ? 0.4850 0.9496 0.5385 -0.0860 -0.0558 -0.2283 382  LEU C CB  
8792  C  CG  . LEU C 382 ? 0.6984 1.1806 0.7650 -0.0965 -0.0652 -0.2333 382  LEU C CG  
8793  C  CD1 . LEU C 382 ? 0.8276 1.2911 0.9161 -0.1056 -0.0629 -0.2252 382  LEU C CD1 
8794  C  CD2 . LEU C 382 ? 0.8432 1.3269 0.9037 -0.0991 -0.0749 -0.2579 382  LEU C CD2 
8795  N  N   . TYR C 383 ? 0.4398 0.8596 0.5127 -0.0857 -0.0356 -0.1862 383  TYR C N   
8796  C  CA  . TYR C 383 ? 0.3395 0.7448 0.4261 -0.0893 -0.0293 -0.1698 383  TYR C CA  
8797  C  C   . TYR C 383 ? 0.3984 0.7699 0.4959 -0.0954 -0.0267 -0.1759 383  TYR C C   
8798  O  O   . TYR C 383 ? 0.5401 0.8914 0.6316 -0.0939 -0.0270 -0.1890 383  TYR C O   
8799  C  CB  . TYR C 383 ? 0.3916 0.7892 0.4688 -0.0806 -0.0209 -0.1512 383  TYR C CB  
8800  C  CG  . TYR C 383 ? 0.5273 0.9550 0.5927 -0.0736 -0.0228 -0.1432 383  TYR C CG  
8801  C  CD1 . TYR C 383 ? 0.4666 0.9052 0.5167 -0.0675 -0.0256 -0.1526 383  TYR C CD1 
8802  C  CD2 . TYR C 383 ? 0.5135 0.9582 0.5833 -0.0729 -0.0215 -0.1255 383  TYR C CD2 
8803  C  CE1 . TYR C 383 ? 0.4339 0.9007 0.4739 -0.0615 -0.0272 -0.1441 383  TYR C CE1 
8804  C  CE2 . TYR C 383 ? 0.3991 0.8706 0.4588 -0.0669 -0.0236 -0.1173 383  TYR C CE2 
8805  C  CZ  . TYR C 383 ? 0.4292 0.9119 0.4742 -0.0615 -0.0265 -0.1262 383  TYR C CZ  
8806  O  OH  . TYR C 383 ? 0.3510 0.8610 0.3868 -0.0560 -0.0285 -0.1167 383  TYR C OH  
8807  N  N   . SER C 384 ? 0.4284 0.7944 0.5425 -0.1019 -0.0238 -0.1656 384  SER C N   
8808  C  CA  . SER C 384 ? 0.4780 0.8112 0.6030 -0.1073 -0.0195 -0.1667 384  SER C CA  
8809  C  C   . SER C 384 ? 0.5673 0.8793 0.6896 -0.1021 -0.0084 -0.1477 384  SER C C   
8810  O  O   . SER C 384 ? 0.4323 0.7513 0.5630 -0.1031 -0.0041 -0.1321 384  SER C O   
8811  C  CB  . SER C 384 ? 0.4269 0.7669 0.5737 -0.1189 -0.0240 -0.1689 384  SER C CB  
8812  O  OG  . SER C 384 ? 0.7986 1.1410 0.9483 -0.1250 -0.0341 -0.1898 384  SER C OG  
8813  N  N   . VAL C 385 ? 0.5296 0.8155 0.6396 -0.0963 -0.0041 -0.1494 385  VAL C N   
8814  C  CA  . VAL C 385 ? 0.4533 0.7164 0.5572 -0.0907 0.0055  -0.1327 385  VAL C CA  
8815  C  C   . VAL C 385 ? 0.4501 0.6806 0.5644 -0.0964 0.0104  -0.1319 385  VAL C C   
8816  O  O   . VAL C 385 ? 0.5043 0.7217 0.6241 -0.1018 0.0066  -0.1467 385  VAL C O   
8817  C  CB  . VAL C 385 ? 0.4126 0.6652 0.4977 -0.0811 0.0069  -0.1338 385  VAL C CB  
8818  C  CG1 . VAL C 385 ? 0.4226 0.6600 0.4989 -0.0743 0.0147  -0.1144 385  VAL C CG1 
8819  C  CG2 . VAL C 385 ? 0.3783 0.6626 0.4543 -0.0770 0.0004  -0.1409 385  VAL C CG2 
8820  N  N   . HIS C 386 ? 0.2954 0.5125 0.4118 -0.0950 0.0188  -0.1147 386  HIS C N   
8821  C  CA  . HIS C 386 ? 0.3649 0.5484 0.4874 -0.0989 0.0249  -0.1118 386  HIS C CA  
8822  C  C   . HIS C 386 ? 0.4261 0.5883 0.5381 -0.0918 0.0345  -0.0936 386  HIS C C   
8823  O  O   . HIS C 386 ? 0.3267 0.5030 0.4311 -0.0854 0.0366  -0.0814 386  HIS C O   
8824  C  CB  . HIS C 386 ? 0.5487 0.7376 0.6936 -0.1096 0.0242  -0.1126 386  HIS C CB  
8825  C  CG  . HIS C 386 ? 0.7505 0.9543 0.9041 -0.1097 0.0298  -0.0954 386  HIS C CG  
8826  N  ND1 . HIS C 386 ? 0.9223 1.1356 1.0644 -0.1008 0.0339  -0.0813 386  HIS C ND1 
8827  C  CD2 . HIS C 386 ? 0.6871 0.8983 0.8609 -0.1173 0.0317  -0.0898 386  HIS C CD2 
8828  C  CE1 . HIS C 386 ? 0.6305 0.8558 0.7846 -0.1025 0.0384  -0.0684 386  HIS C CE1 
8829  N  NE2 . HIS C 386 ? 0.5132 0.7380 0.6868 -0.1124 0.0375  -0.0729 386  HIS C NE2 
8830  N  N   . ALA C 387 ? 0.4811 0.6088 0.5920 -0.0929 0.0398  -0.0919 387  ALA C N   
8831  C  CA  . ALA C 387 ? 0.4446 0.5476 0.5434 -0.0862 0.0484  -0.0758 387  ALA C CA  
8832  C  C   . ALA C 387 ? 0.5436 0.6290 0.6534 -0.0913 0.0561  -0.0667 387  ALA C C   
8833  O  O   . ALA C 387 ? 0.5650 0.6470 0.6907 -0.1003 0.0548  -0.0745 387  ALA C O   
8834  C  CB  . ALA C 387 ? 0.4624 0.5378 0.5457 -0.0810 0.0483  -0.0798 387  ALA C CB  
8835  N  N   . SER C 388 ? 0.4207 0.4947 0.5218 -0.0853 0.0642  -0.0498 388  SER C N   
8836  C  CA  . SER C 388 ? 0.5217 0.5763 0.6301 -0.0885 0.0730  -0.0400 388  SER C CA  
8837  C  C   . SER C 388 ? 0.4960 0.5223 0.5849 -0.0797 0.0806  -0.0258 388  SER C C   
8838  O  O   . SER C 388 ? 0.4035 0.4321 0.4764 -0.0714 0.0791  -0.0210 388  SER C O   
8839  C  CB  . SER C 388 ? 0.4492 0.5308 0.5755 -0.0925 0.0756  -0.0328 388  SER C CB  
8840  O  OG  . SER C 388 ? 0.4471 0.5505 0.5662 -0.0852 0.0756  -0.0238 388  SER C OG  
8841  N  N   . ALA C 389 ? 0.6233 0.6224 0.7134 -0.0817 0.0884  -0.0191 389  ALA C N   
8842  C  CA  . ALA C 389 ? 0.5667 0.5372 0.6377 -0.0737 0.0962  -0.0051 389  ALA C CA  
8843  C  C   . ALA C 389 ? 0.5486 0.5027 0.6274 -0.0772 0.1062  0.0043  389  ALA C C   
8844  O  O   . ALA C 389 ? 0.6760 0.6284 0.7719 -0.0865 0.1062  -0.0022 389  ALA C O   
8845  C  CB  . ALA C 389 ? 0.2792 0.2207 0.3333 -0.0704 0.0928  -0.0100 389  ALA C CB  
8846  N  N   . PHE C 390 ? 0.5256 0.4679 0.5919 -0.0696 0.1148  0.0198  390  PHE C N   
8847  C  CA  . PHE C 390 ? 0.7605 0.6838 0.8298 -0.0709 0.1258  0.0303  390  PHE C CA  
8848  C  C   . PHE C 390 ? 0.7498 0.6395 0.8160 -0.0758 0.1263  0.0252  390  PHE C C   
8849  O  O   . PHE C 390 ? 0.7300 0.5973 0.7790 -0.0720 0.1221  0.0216  390  PHE C O   
8850  C  CB  . PHE C 390 ? 0.9633 0.8728 1.0124 -0.0596 0.1339  0.0464  390  PHE C CB  
8851  C  CG  . PHE C 390 ? 1.2126 1.0996 1.2602 -0.0592 0.1462  0.0579  390  PHE C CG  
8852  C  CD1 . PHE C 390 ? 1.3503 1.1976 1.3763 -0.0548 0.1503  0.0632  390  PHE C CD1 
8853  C  CD2 . PHE C 390 ? 1.3025 1.2088 1.3705 -0.0631 0.1536  0.0640  390  PHE C CD2 
8854  C  CE1 . PHE C 390 ? 1.4213 1.2480 1.4445 -0.0540 0.1620  0.0740  390  PHE C CE1 
8855  C  CE2 . PHE C 390 ? 1.4246 1.3114 1.4913 -0.0623 0.1657  0.0752  390  PHE C CE2 
8856  C  CZ  . PHE C 390 ? 1.4588 1.3057 1.5024 -0.0576 0.1701  0.0801  390  PHE C CZ  
8857  N  N   . GLY C 391 ? 0.5708 0.4578 0.6549 -0.0843 0.1310  0.0255  391  GLY C N   
8858  C  CA  . GLY C 391 ? 0.7065 0.5630 0.7906 -0.0900 0.1312  0.0210  391  GLY C CA  
8859  C  C   . GLY C 391 ? 0.7170 0.5796 0.8136 -0.0982 0.1200  0.0028  391  GLY C C   
8860  O  O   . GLY C 391 ? 0.5614 0.4004 0.6607 -0.1038 0.1187  -0.0027 391  GLY C O   
8861  N  N   . TYR C 392 ? 0.7559 0.6499 0.8595 -0.0986 0.1117  -0.0066 392  TYR C N   
8862  C  CA  . TYR C 392 ? 0.7306 0.6333 0.8446 -0.1053 0.1007  -0.0249 392  TYR C CA  
8863  C  C   . TYR C 392 ? 0.7027 0.6408 0.8406 -0.1132 0.0960  -0.0317 392  TYR C C   
8864  O  O   . TYR C 392 ? 0.8301 0.7954 0.9718 -0.1105 0.0975  -0.0252 392  TYR C O   
8865  C  CB  . TYR C 392 ? 0.7011 0.6063 0.7980 -0.0979 0.0933  -0.0324 392  TYR C CB  
8866  C  CG  . TYR C 392 ? 0.7974 0.6663 0.8734 -0.0919 0.0950  -0.0291 392  TYR C CG  
8867  C  CD1 . TYR C 392 ? 0.8560 0.7058 0.9315 -0.0948 0.0893  -0.0412 392  TYR C CD1 
8868  C  CD2 . TYR C 392 ? 0.6440 0.4969 0.7008 -0.0831 0.1019  -0.0138 392  TYR C CD2 
8869  C  CE1 . TYR C 392 ? 0.8086 0.6253 0.8660 -0.0896 0.0902  -0.0377 392  TYR C CE1 
8870  C  CE2 . TYR C 392 ? 0.7395 0.5584 0.7770 -0.0780 0.1024  -0.0105 392  TYR C CE2 
8871  C  CZ  . TYR C 392 ? 0.8456 0.6471 0.8840 -0.0815 0.0966  -0.0221 392  TYR C CZ  
8872  O  OH  . TYR C 392 ? 0.8289 0.5971 0.8491 -0.0765 0.0966  -0.0183 392  TYR C OH  
8873  N  N   . GLN C 393 ? 0.6620 0.5991 0.8161 -0.1230 0.0896  -0.0446 393  GLN C N   
8874  C  CA  . GLN C 393 ? 0.5973 0.5659 0.7732 -0.1313 0.0826  -0.0533 393  GLN C CA  
8875  C  C   . GLN C 393 ? 0.7044 0.6974 0.8719 -0.1262 0.0742  -0.0631 393  GLN C C   
8876  O  O   . GLN C 393 ? 0.7111 0.6928 0.8638 -0.1216 0.0694  -0.0723 393  GLN C O   
8877  C  CB  . GLN C 393 ? 0.5023 0.4599 0.6946 -0.1424 0.0762  -0.0663 393  GLN C CB  
8878  C  CG  . GLN C 393 ? 0.6449 0.5749 0.8437 -0.1472 0.0843  -0.0566 393  GLN C CG  
8879  C  CD  . GLN C 393 ? 0.8021 0.7229 1.0200 -0.1592 0.0773  -0.0684 393  GLN C CD  
8880  O  OE1 . GLN C 393 ? 0.7465 0.6731 0.9672 -0.1622 0.0662  -0.0858 393  GLN C OE1 
8881  N  NE2 . GLN C 393 ? 0.8957 0.8017 1.1266 -0.1660 0.0839  -0.0586 393  GLN C NE2 
8882  N  N   . THR C 394 ? 0.7610 0.7881 0.9382 -0.1269 0.0726  -0.0603 394  THR C N   
8883  C  CA  . THR C 394 ? 0.7428 0.7963 0.9120 -0.1219 0.0653  -0.0671 394  THR C CA  
8884  C  C   . THR C 394 ? 0.6919 0.7522 0.8662 -0.1274 0.0536  -0.0877 394  THR C C   
8885  O  O   . THR C 394 ? 0.7420 0.8129 0.9358 -0.1373 0.0482  -0.0956 394  THR C O   
8886  C  CB  . THR C 394 ? 0.6828 0.7714 0.8637 -0.1224 0.0660  -0.0589 394  THR C CB  
8887  O  OG1 . THR C 394 ? 0.5678 0.6492 0.7419 -0.1157 0.0772  -0.0399 394  THR C OG1 
8888  C  CG2 . THR C 394 ? 0.6663 0.7838 0.8396 -0.1181 0.0576  -0.0663 394  THR C CG2 
8889  N  N   . SER C 395 ? 0.6108 0.6645 0.7675 -0.1207 0.0496  -0.0962 395  SER C N   
8890  C  CA  . SER C 395 ? 0.5764 0.6330 0.7342 -0.1239 0.0393  -0.1164 395  SER C CA  
8891  C  C   . SER C 395 ? 0.7021 0.7903 0.8762 -0.1315 0.0304  -0.1269 395  SER C C   
8892  O  O   . SER C 395 ? 0.7429 0.8574 0.9247 -0.1324 0.0313  -0.1184 395  SER C O   
8893  C  CB  . SER C 395 ? 0.4584 0.5183 0.5957 -0.1138 0.0366  -0.1210 395  SER C CB  
8894  O  OG  . SER C 395 ? 0.4211 0.5164 0.5567 -0.1108 0.0331  -0.1199 395  SER C OG  
8895  N  N   . ALA C 396 ? 0.5943 0.6791 0.7733 -0.1368 0.0215  -0.1455 396  ALA C N   
8896  C  CA  . ALA C 396 ? 0.4473 0.5612 0.6356 -0.1422 0.0109  -0.1587 396  ALA C CA  
8897  C  C   . ALA C 396 ? 0.5971 0.7351 0.7686 -0.1329 0.0080  -0.1614 396  ALA C C   
8898  O  O   . ALA C 396 ? 0.6879 0.8146 0.8413 -0.1236 0.0117  -0.1592 396  ALA C O   
8899  C  CB  . ALA C 396 ? 0.3447 0.4447 0.5390 -0.1486 0.0021  -0.1784 396  ALA C CB  
8900  N  N   . PRO C 397 ? 0.5461 0.7176 0.7237 -0.1358 0.0011  -0.1657 397  PRO C N   
8901  C  CA  . PRO C 397 ? 0.4376 0.6351 0.6002 -0.1276 -0.0017 -0.1670 397  PRO C CA  
8902  C  C   . PRO C 397 ? 0.4561 0.6523 0.6059 -0.1240 -0.0090 -0.1865 397  PRO C C   
8903  O  O   . PRO C 397 ? 0.5112 0.6972 0.6678 -0.1301 -0.0156 -0.2026 397  PRO C O   
8904  C  CB  . PRO C 397 ? 0.4935 0.7255 0.6697 -0.1337 -0.0076 -0.1658 397  PRO C CB  
8905  C  CG  . PRO C 397 ? 0.4818 0.7051 0.6812 -0.1447 -0.0067 -0.1618 397  PRO C CG  
8906  C  CD  . PRO C 397 ? 0.5304 0.7178 0.7298 -0.1472 -0.0053 -0.1695 397  PRO C CD  
8907  N  N   . GLN C 398 ? 0.5883 0.7949 0.7202 -0.1139 -0.0078 -0.1849 398  GLN C N   
8908  C  CA  . GLN C 398 ? 0.6100 0.8211 0.7292 -0.1092 -0.0140 -0.2025 398  GLN C CA  
8909  C  C   . GLN C 398 ? 0.5019 0.7506 0.6131 -0.1052 -0.0188 -0.2038 398  GLN C C   
8910  O  O   . GLN C 398 ? 0.5063 0.7711 0.6132 -0.1007 -0.0148 -0.1882 398  GLN C O   
8911  C  CB  . GLN C 398 ? 0.5454 0.7318 0.6499 -0.1002 -0.0083 -0.2011 398  GLN C CB  
8912  C  CG  . GLN C 398 ? 0.3470 0.4947 0.4575 -0.1038 -0.0050 -0.2030 398  GLN C CG  
8913  C  CD  . GLN C 398 ? 0.6061 0.7298 0.7032 -0.0951 0.0016  -0.1961 398  GLN C CD  
8914  O  OE1 . GLN C 398 ? 0.6657 0.7957 0.7494 -0.0868 0.0004  -0.2013 398  GLN C OE1 
8915  N  NE2 . GLN C 398 ? 0.6680 0.7641 0.7686 -0.0968 0.0084  -0.1838 398  GLN C NE2 
8916  N  N   . GLN C 399 ? 0.7073 0.9690 0.8156 -0.1066 -0.0278 -0.2227 399  GLN C N   
8917  C  CA  . GLN C 399 ? 0.7302 1.0275 0.8298 -0.1032 -0.0333 -0.2263 399  GLN C CA  
8918  C  C   . GLN C 399 ? 0.7654 1.0649 0.8449 -0.0919 -0.0317 -0.2314 399  GLN C C   
8919  O  O   . GLN C 399 ? 0.8403 1.1197 0.9143 -0.0891 -0.0320 -0.2443 399  GLN C O   
8920  C  CB  . GLN C 399 ? 0.7759 1.0870 0.8833 -0.1115 -0.0447 -0.2440 399  GLN C CB  
8921  C  CG  . GLN C 399 ? 0.9612 1.3040 1.0554 -0.1073 -0.0520 -0.2544 399  GLN C CG  
8922  C  CD  . GLN C 399 ? 1.1988 1.5442 1.2955 -0.1137 -0.0637 -0.2773 399  GLN C CD  
8923  O  OE1 . GLN C 399 ? 1.3510 1.6754 1.4424 -0.1121 -0.0657 -0.2934 399  GLN C OE1 
8924  N  NE2 . GLN C 399 ? 1.1431 1.5138 1.2476 -0.1209 -0.0721 -0.2788 399  GLN C NE2 
8925  N  N   . VAL C 400 ? 0.5667 0.8908 0.6363 -0.0852 -0.0298 -0.2204 400  VAL C N   
8926  C  CA  . VAL C 400 ? 0.4748 0.8042 0.5267 -0.0745 -0.0279 -0.2229 400  VAL C CA  
8927  C  C   . VAL C 400 ? 0.5050 0.8736 0.5476 -0.0708 -0.0324 -0.2227 400  VAL C C   
8928  O  O   . VAL C 400 ? 0.4532 0.8428 0.5005 -0.0732 -0.0331 -0.2100 400  VAL C O   
8929  C  CB  . VAL C 400 ? 0.4905 0.8024 0.5373 -0.0677 -0.0188 -0.2051 400  VAL C CB  
8930  C  CG1 . VAL C 400 ? 0.5232 0.8533 0.5712 -0.0670 -0.0160 -0.1846 400  VAL C CG1 
8931  C  CG2 . VAL C 400 ? 0.6563 0.9684 0.6875 -0.0574 -0.0170 -0.2094 400  VAL C CG2 
8932  N  N   . ARG C 401 ? 0.5116 0.8900 0.5409 -0.0646 -0.0353 -0.2368 401  ARG C N   
8933  C  CA  . ARG C 401 ? 0.5572 0.9722 0.5755 -0.0602 -0.0388 -0.2364 401  ARG C CA  
8934  C  C   . ARG C 401 ? 0.4999 0.9195 0.5074 -0.0502 -0.0319 -0.2210 401  ARG C C   
8935  O  O   . ARG C 401 ? 0.4807 0.8894 0.4790 -0.0428 -0.0286 -0.2264 401  ARG C O   
8936  C  CB  . ARG C 401 ? 0.6151 1.0410 0.6234 -0.0584 -0.0457 -0.2597 401  ARG C CB  
8937  C  CG  . ARG C 401 ? 0.6466 1.1115 0.6414 -0.0533 -0.0494 -0.2600 401  ARG C CG  
8938  C  CD  . ARG C 401 ? 0.8312 1.3062 0.8167 -0.0533 -0.0576 -0.2845 401  ARG C CD  
8939  N  NE  . ARG C 401 ? 1.0407 1.4881 1.0222 -0.0495 -0.0558 -0.3006 401  ARG C NE  
8940  C  CZ  . ARG C 401 ? 1.1139 1.5445 1.0992 -0.0547 -0.0621 -0.3207 401  ARG C CZ  
8941  N  NH1 . ARG C 401 ? 1.2229 1.6282 1.2044 -0.0499 -0.0596 -0.3334 401  ARG C NH1 
8942  N  NH2 . ARG C 401 ? 0.9836 1.4221 0.9770 -0.0647 -0.0715 -0.3280 401  ARG C NH2 
8943  N  N   . VAL C 402 ? 0.4355 0.8708 0.4452 -0.0501 -0.0301 -0.2016 402  VAL C N   
8944  C  CA  . VAL C 402 ? 0.4044 0.8475 0.4044 -0.0413 -0.0251 -0.1855 402  VAL C CA  
8945  C  C   . VAL C 402 ? 0.5682 1.0470 0.5554 -0.0355 -0.0286 -0.1885 402  VAL C C   
8946  O  O   . VAL C 402 ? 0.2921 0.7997 0.2797 -0.0379 -0.0329 -0.1832 402  VAL C O   
8947  C  CB  . VAL C 402 ? 0.3255 0.7686 0.3322 -0.0427 -0.0217 -0.1625 402  VAL C CB  
8948  C  CG1 . VAL C 402 ? 0.2975 0.7509 0.2935 -0.0338 -0.0184 -0.1465 402  VAL C CG1 
8949  C  CG2 . VAL C 402 ? 0.2648 0.6713 0.2817 -0.0467 -0.0167 -0.1573 402  VAL C CG2 
8950  N  N   . THR C 403 ? 0.7451 1.2216 0.7212 -0.0279 -0.0265 -0.1973 403  THR C N   
8951  C  CA  . THR C 403 ? 0.6823 1.1887 0.6448 -0.0199 -0.0268 -0.1954 403  THR C CA  
8952  C  C   . THR C 403 ? 0.7835 1.2806 0.7435 -0.0129 -0.0202 -0.1768 403  THR C C   
8953  O  O   . THR C 403 ? 0.8355 1.3013 0.7984 -0.0114 -0.0157 -0.1764 403  THR C O   
8954  C  CB  . THR C 403 ? 0.7581 1.2676 0.7102 -0.0150 -0.0283 -0.2177 403  THR C CB  
8955  O  OG1 . THR C 403 ? 0.9782 1.5175 0.9169 -0.0064 -0.0273 -0.2141 403  THR C OG1 
8956  C  CG2 . THR C 403 ? 0.6907 1.1647 0.6447 -0.0119 -0.0234 -0.2250 403  THR C CG2 
8957  N  N   . ASN C 404 ? 0.8565 1.3794 0.8115 -0.0092 -0.0202 -0.1608 404  ASN C N   
8958  C  CA  . ASN C 404 ? 0.6848 1.2017 0.6364 -0.0023 -0.0152 -0.1434 404  ASN C CA  
8959  C  C   . ASN C 404 ? 0.8020 1.3403 0.7418 0.0065  -0.0140 -0.1484 404  ASN C C   
8960  O  O   . ASN C 404 ? 0.8871 1.4538 0.8211 0.0106  -0.0146 -0.1362 404  ASN C O   
8961  C  CB  . ASN C 404 ? 0.4882 1.0166 0.4430 -0.0035 -0.0159 -0.1204 404  ASN C CB  
8962  C  CG  . ASN C 404 ? 0.3614 0.8672 0.3276 -0.0108 -0.0155 -0.1142 404  ASN C CG  
8963  O  OD1 . ASN C 404 ? 0.4318 0.9040 0.4029 -0.0126 -0.0122 -0.1178 404  ASN C OD1 
8964  N  ND2 . ASN C 404 ? 0.2766 0.8012 0.2472 -0.0147 -0.0188 -0.1043 404  ASN C ND2 
8965  N  N   . ASP C 405 ? 0.8283 1.3529 0.7650 0.0095  -0.0123 -0.1666 405  ASP C N   
8966  C  CA  . ASP C 405 ? 0.9086 1.4500 0.8345 0.0187  -0.0101 -0.1740 405  ASP C CA  
8967  C  C   . ASP C 405 ? 0.6242 1.1360 0.5522 0.0239  -0.0045 -0.1744 405  ASP C C   
8968  O  O   . ASP C 405 ? 0.6817 1.2022 0.6031 0.0325  -0.0012 -0.1781 405  ASP C O   
8969  C  CB  . ASP C 405 ? 1.3251 1.8804 1.2437 0.0183  -0.0140 -0.1984 405  ASP C CB  
8970  C  CG  . ASP C 405 ? 1.4941 2.0799 1.3988 0.0279  -0.0124 -0.2035 405  ASP C CG  
8971  O  OD1 . ASP C 405 ? 1.5940 2.1895 1.4963 0.0349  -0.0078 -0.1881 405  ASP C OD1 
8972  O  OD2 . ASP C 405 ? 1.4252 2.0252 1.3212 0.0286  -0.0159 -0.2226 405  ASP C OD2 
8973  N  N   . ASN C 406 ? 0.6343 1.1116 0.5719 0.0189  -0.0034 -0.1698 406  ASN C N   
8974  C  CA  . ASN C 406 ? 0.4019 0.8477 0.3427 0.0226  0.0012  -0.1676 406  ASN C CA  
8975  C  C   . ASN C 406 ? 0.6039 1.0457 0.5465 0.0246  0.0033  -0.1419 406  ASN C C   
8976  O  O   . ASN C 406 ? 0.4850 0.9327 0.4302 0.0200  0.0013  -0.1280 406  ASN C O   
8977  C  CB  . ASN C 406 ? 0.7696 1.1790 0.7191 0.0153  0.0007  -0.1773 406  ASN C CB  
8978  C  CG  . ASN C 406 ? 1.0732 1.4537 1.0241 0.0194  0.0039  -0.1877 406  ASN C CG  
8979  O  OD1 . ASN C 406 ? 1.1405 1.5308 1.0855 0.0264  0.0051  -0.2004 406  ASN C OD1 
8980  N  ND2 . ASN C 406 ? 0.9314 1.2759 0.8899 0.0153  0.0055  -0.1824 406  ASN C ND2 
8981  N  N   . GLN C 407 ? 0.8262 1.2584 0.7678 0.0317  0.0070  -0.1357 407  GLN C N   
8982  C  CA  . GLN C 407 ? 0.8052 1.2306 0.7484 0.0338  0.0081  -0.1118 407  GLN C CA  
8983  C  C   . GLN C 407 ? 0.6908 1.0825 0.6399 0.0274  0.0076  -0.1018 407  GLN C C   
8984  O  O   . GLN C 407 ? 0.6503 1.0398 0.5997 0.0271  0.0068  -0.0817 407  GLN C O   
8985  C  CB  . GLN C 407 ? 0.8901 1.3078 0.8328 0.0420  0.0116  -0.1087 407  GLN C CB  
8986  C  CG  . GLN C 407 ? 0.8162 1.2703 0.7538 0.0497  0.0126  -0.1006 407  GLN C CG  
8987  C  CD  . GLN C 407 ? 0.9989 1.4445 0.9384 0.0577  0.0163  -0.0972 407  GLN C CD  
8988  O  OE1 . GLN C 407 ? 1.0516 1.4669 0.9950 0.0581  0.0182  -0.1063 407  GLN C OE1 
8989  N  NE2 . GLN C 407 ? 1.0912 1.5642 1.0289 0.0638  0.0172  -0.0835 407  GLN C NE2 
8990  N  N   . GLU C 408 ? 0.6267 0.9918 0.5803 0.0223  0.0081  -0.1156 408  GLU C N   
8991  C  CA  . GLU C 408 ? 0.5856 0.9191 0.5444 0.0163  0.0085  -0.1073 408  GLU C CA  
8992  C  C   . GLU C 408 ? 0.5864 0.9141 0.5506 0.0079  0.0071  -0.1195 408  GLU C C   
8993  O  O   . GLU C 408 ? 0.5600 0.8949 0.5252 0.0063  0.0058  -0.1390 408  GLU C O   
8994  C  CB  . GLU C 408 ? 0.5953 0.8918 0.5557 0.0186  0.0112  -0.1045 408  GLU C CB  
8995  C  CG  . GLU C 408 ? 0.7162 1.0161 0.6731 0.0255  0.0117  -0.0873 408  GLU C CG  
8996  C  CD  . GLU C 408 ? 0.8056 1.0684 0.7642 0.0274  0.0134  -0.0830 408  GLU C CD  
8997  O  OE1 . GLU C 408 ? 0.5883 0.8545 0.5460 0.0340  0.0140  -0.0780 408  GLU C OE1 
8998  O  OE2 . GLU C 408 ? 1.0126 1.2434 0.9738 0.0222  0.0141  -0.0840 408  GLU C OE2 
8999  N  N   . ALA C 409 ? 0.4738 0.7885 0.4417 0.0028  0.0073  -0.1073 409  ALA C N   
9000  C  CA  . ALA C 409 ? 0.3010 0.6125 0.2759 -0.0054 0.0062  -0.1147 409  ALA C CA  
9001  C  C   . ALA C 409 ? 0.4924 0.7816 0.4723 -0.0091 0.0066  -0.1341 409  ALA C C   
9002  O  O   . ALA C 409 ? 0.5201 0.7821 0.4998 -0.0067 0.0090  -0.1367 409  ALA C O   
9003  C  CB  . ALA C 409 ? 0.3096 0.6037 0.2876 -0.0088 0.0079  -0.0979 409  ALA C CB  
9004  N  N   . LEU C 410 ? 0.5660 0.8671 0.5512 -0.0152 0.0036  -0.1474 410  LEU C N   
9005  C  CA  . LEU C 410 ? 0.4008 0.6829 0.3917 -0.0195 0.0026  -0.1664 410  LEU C CA  
9006  C  C   . LEU C 410 ? 0.3251 0.5685 0.3228 -0.0240 0.0060  -0.1610 410  LEU C C   
9007  O  O   . LEU C 410 ? 0.2420 0.4801 0.2450 -0.0290 0.0073  -0.1499 410  LEU C O   
9008  C  CB  . LEU C 410 ? 0.5061 0.8090 0.5019 -0.0261 -0.0025 -0.1794 410  LEU C CB  
9009  C  CG  . LEU C 410 ? 0.7421 1.0766 0.7296 -0.0216 -0.0063 -0.1925 410  LEU C CG  
9010  C  CD1 . LEU C 410 ? 0.9078 1.2715 0.8979 -0.0274 -0.0120 -0.1967 410  LEU C CD1 
9011  C  CD2 . LEU C 410 ? 0.7623 1.0819 0.7481 -0.0195 -0.0072 -0.2135 410  LEU C CD2 
9012  N  N   . ARG C 411 ? 0.3449 0.5614 0.3422 -0.0217 0.0077  -0.1684 411  ARG C N   
9013  C  CA  . ARG C 411 ? 0.5027 0.6814 0.5059 -0.0262 0.0107  -0.1647 411  ARG C CA  
9014  C  C   . ARG C 411 ? 0.5116 0.6855 0.5259 -0.0361 0.0088  -0.1740 411  ARG C C   
9015  O  O   . ARG C 411 ? 0.4593 0.6493 0.4767 -0.0389 0.0042  -0.1904 411  ARG C O   
9016  C  CB  . ARG C 411 ? 0.3503 0.5026 0.3517 -0.0220 0.0120  -0.1723 411  ARG C CB  
9017  C  CG  . ARG C 411 ? 0.4220 0.5346 0.4295 -0.0271 0.0145  -0.1699 411  ARG C CG  
9018  C  CD  . ARG C 411 ? 0.4336 0.5298 0.4371 -0.0260 0.0185  -0.1479 411  ARG C CD  
9019  N  NE  . ARG C 411 ? 0.5391 0.6154 0.5363 -0.0194 0.0200  -0.1422 411  ARG C NE  
9020  C  CZ  . ARG C 411 ? 0.4516 0.4917 0.4503 -0.0207 0.0218  -0.1417 411  ARG C CZ  
9021  N  NH1 . ARG C 411 ? 0.3536 0.3743 0.3597 -0.0284 0.0228  -0.1460 411  ARG C NH1 
9022  N  NH2 . ARG C 411 ? 0.4070 0.4308 0.4005 -0.0145 0.0223  -0.1362 411  ARG C NH2 
9023  N  N   . LEU C 412 ? 0.5116 0.6637 0.5316 -0.0411 0.0122  -0.1628 412  LEU C N   
9024  C  CA  . LEU C 412 ? 0.5501 0.6956 0.5826 -0.0509 0.0112  -0.1682 412  LEU C CA  
9025  C  C   . LEU C 412 ? 0.5825 0.6959 0.6183 -0.0538 0.0169  -0.1544 412  LEU C C   
9026  O  O   . LEU C 412 ? 0.4848 0.5990 0.5168 -0.0518 0.0207  -0.1368 412  LEU C O   
9027  C  CB  . LEU C 412 ? 0.5074 0.6867 0.5447 -0.0549 0.0082  -0.1665 412  LEU C CB  
9028  C  CG  . LEU C 412 ? 0.6047 0.7858 0.6567 -0.0653 0.0053  -0.1745 412  LEU C CG  
9029  C  CD1 . LEU C 412 ? 0.6964 0.8811 0.7511 -0.0680 -0.0014 -0.1975 412  LEU C CD1 
9030  C  CD2 . LEU C 412 ? 0.3433 0.5547 0.4007 -0.0686 0.0038  -0.1660 412  LEU C CD2 
9031  N  N   . ASP C 413 ? 0.4643 0.5488 0.5064 -0.0582 0.0175  -0.1626 413  ASP C N   
9032  C  CA  . ASP C 413 ? 0.3243 0.3754 0.3674 -0.0602 0.0230  -0.1506 413  ASP C CA  
9033  C  C   . ASP C 413 ? 0.5517 0.5945 0.6092 -0.0703 0.0239  -0.1523 413  ASP C C   
9034  O  O   . ASP C 413 ? 0.4867 0.5434 0.5545 -0.0764 0.0189  -0.1662 413  ASP C O   
9035  C  CB  . ASP C 413 ? 0.4429 0.4628 0.4814 -0.0569 0.0236  -0.1554 413  ASP C CB  
9036  C  CG  . ASP C 413 ? 0.5758 0.5996 0.6015 -0.0469 0.0237  -0.1503 413  ASP C CG  
9037  O  OD1 . ASP C 413 ? 0.6726 0.7212 0.6918 -0.0424 0.0236  -0.1413 413  ASP C OD1 
9038  O  OD2 . ASP C 413 ? 0.6553 0.6569 0.6781 -0.0436 0.0236  -0.1547 413  ASP C OD2 
9039  N  N   . PHE C 414 ? 0.6161 0.6354 0.6739 -0.0719 0.0300  -0.1380 414  PHE C N   
9040  C  CA  . PHE C 414 ? 0.5763 0.5864 0.6479 -0.0810 0.0324  -0.1363 414  PHE C CA  
9041  C  C   . PHE C 414 ? 0.6280 0.5979 0.6988 -0.0826 0.0374  -0.1302 414  PHE C C   
9042  O  O   . PHE C 414 ? 0.6563 0.6076 0.7146 -0.0765 0.0419  -0.1178 414  PHE C O   
9043  C  CB  . PHE C 414 ? 0.5910 0.6213 0.6659 -0.0820 0.0359  -0.1221 414  PHE C CB  
9044  C  CG  . PHE C 414 ? 0.5304 0.6006 0.6074 -0.0814 0.0306  -0.1269 414  PHE C CG  
9045  C  CD1 . PHE C 414 ? 0.5039 0.5916 0.5677 -0.0729 0.0295  -0.1222 414  PHE C CD1 
9046  C  CD2 . PHE C 414 ? 0.6214 0.7116 0.7136 -0.0896 0.0263  -0.1357 414  PHE C CD2 
9047  C  CE1 . PHE C 414 ? 0.4989 0.6236 0.5641 -0.0724 0.0246  -0.1260 414  PHE C CE1 
9048  C  CE2 . PHE C 414 ? 0.5947 0.7215 0.6880 -0.0892 0.0208  -0.1400 414  PHE C CE2 
9049  C  CZ  . PHE C 414 ? 0.6073 0.7514 0.6866 -0.0805 0.0202  -0.1351 414  PHE C CZ  
9050  N  N   . LYS C 415 ? 0.5652 0.5215 0.6493 -0.0910 0.0360  -0.1392 415  LYS C N   
9051  C  CA  . LYS C 415 ? 0.6402 0.5611 0.7261 -0.0943 0.0412  -0.1321 415  LYS C CA  
9052  C  C   . LYS C 415 ? 0.7476 0.6730 0.8472 -0.1021 0.0456  -0.1233 415  LYS C C   
9053  O  O   . LYS C 415 ? 0.6270 0.5727 0.7419 -0.1094 0.0414  -0.1315 415  LYS C O   
9054  C  CB  . LYS C 415 ? 0.5852 0.4837 0.6764 -0.0978 0.0366  -0.1472 415  LYS C CB  
9055  C  CG  . LYS C 415 ? 0.7908 0.6793 0.8689 -0.0893 0.0341  -0.1531 415  LYS C CG  
9056  C  CD  . LYS C 415 ? 0.9853 0.8395 1.0665 -0.0919 0.0327  -0.1607 415  LYS C CD  
9057  C  CE  . LYS C 415 ? 1.0941 0.9339 1.1618 -0.0826 0.0320  -0.1612 415  LYS C CE  
9058  N  NZ  . LYS C 415 ? 1.1622 0.9660 1.2329 -0.0848 0.0312  -0.1660 415  LYS C NZ  
9059  N  N   . LEU C 416 ? 0.6499 0.5566 0.7436 -0.1003 0.0539  -0.1063 416  LEU C N   
9060  C  CA  . LEU C 416 ? 0.6122 0.5228 0.7177 -0.1063 0.0597  -0.0958 416  LEU C CA  
9061  C  C   . LEU C 416 ? 0.6310 0.5069 0.7402 -0.1111 0.0648  -0.0910 416  LEU C C   
9062  O  O   . LEU C 416 ? 0.6455 0.4927 0.7404 -0.1061 0.0680  -0.0852 416  LEU C O   
9063  C  CB  . LEU C 416 ? 0.6270 0.5485 0.7221 -0.0993 0.0663  -0.0785 416  LEU C CB  
9064  C  CG  . LEU C 416 ? 0.3856 0.3408 0.4755 -0.0936 0.0621  -0.0798 416  LEU C CG  
9065  C  CD1 . LEU C 416 ? 0.3115 0.2747 0.3942 -0.0880 0.0689  -0.0620 416  LEU C CD1 
9066  C  CD2 . LEU C 416 ? 0.3755 0.3617 0.4823 -0.1006 0.0552  -0.0926 416  LEU C CD2 
9067  N  N   . ALA C 417 ? 0.6912 0.5698 0.8199 -0.1211 0.0650  -0.0928 417  ALA C N   
9068  C  CA  . ALA C 417 ? 0.5489 0.3969 0.6826 -0.1264 0.0706  -0.0862 417  ALA C CA  
9069  C  C   . ALA C 417 ? 0.5171 0.3645 0.6481 -0.1242 0.0817  -0.0662 417  ALA C C   
9070  O  O   . ALA C 417 ? 0.6956 0.5704 0.8283 -0.1216 0.0835  -0.0604 417  ALA C O   
9071  C  CB  . ALA C 417 ? 0.3738 0.2242 0.5308 -0.1385 0.0651  -0.0971 417  ALA C CB  
9072  N  N   . PRO C 418 ? 0.5368 0.3525 0.6624 -0.1246 0.0891  -0.0557 418  PRO C N   
9073  C  CA  . PRO C 418 ? 0.5194 0.3322 0.6420 -0.1223 0.1006  -0.0369 418  PRO C CA  
9074  C  C   . PRO C 418 ? 0.5013 0.3307 0.6488 -0.1320 0.1038  -0.0334 418  PRO C C   
9075  O  O   . PRO C 418 ? 0.8067 0.6437 0.9735 -0.1416 0.0965  -0.0454 418  PRO C O   
9076  C  CB  . PRO C 418 ? 0.7291 0.5005 0.8375 -0.1203 0.1061  -0.0292 418  PRO C CB  
9077  C  CG  . PRO C 418 ? 0.7460 0.5015 0.8444 -0.1178 0.0975  -0.0420 418  PRO C CG  
9078  C  CD  . PRO C 418 ? 0.7327 0.5127 0.8493 -0.1243 0.0875  -0.0597 418  PRO C CD  
9079  N  N   . VAL C 419 ? 0.5502 0.3855 0.6979 -0.1294 0.1142  -0.0171 419  VAL C N   
9080  C  CA  . VAL C 419 ? 0.5768 0.4255 0.7488 -0.1384 0.1188  -0.0109 419  VAL C CA  
9081  C  C   . VAL C 419 ? 0.6023 0.4207 0.7804 -0.1455 0.1226  -0.0078 419  VAL C C   
9082  O  O   . VAL C 419 ? 0.8527 0.6781 1.0536 -0.1550 0.1248  -0.0043 419  VAL C O   
9083  C  CB  . VAL C 419 ? 0.7030 0.5661 0.8731 -0.1324 0.1303  0.0068  419  VAL C CB  
9084  C  CG1 . VAL C 419 ? 0.4035 0.3061 0.5814 -0.1305 0.1258  0.0039  419  VAL C CG1 
9085  C  CG2 . VAL C 419 ? 0.9488 0.7858 1.0896 -0.1205 0.1385  0.0182  419  VAL C CG2 
9086  N  N   . THR D 27  ? 1.1528 1.9022 1.2155 -0.2972 0.2044  0.1546  27   THR D N   
9087  C  CA  . THR D 27  ? 1.1666 1.8779 1.2390 -0.2888 0.1857  0.1500  27   THR D CA  
9088  C  C   . THR D 27  ? 0.8583 1.5679 0.9365 -0.2551 0.1737  0.1326  27   THR D C   
9089  O  O   . THR D 27  ? 0.6443 1.3956 0.7343 -0.2391 0.1797  0.1187  27   THR D O   
9090  C  CB  . THR D 27  ? 0.9231 1.5685 0.9682 -0.2997 0.1780  0.1688  27   THR D CB  
9091  O  OG1 . THR D 27  ? 1.0487 1.6656 1.0611 -0.2835 0.1754  0.1754  27   THR D OG1 
9092  C  CG2 . THR D 27  ? 0.6307 1.2735 0.6703 -0.3338 0.1902  0.1868  27   THR D CG2 
9093  N  N   . ILE D 28  ? 0.8833 1.5437 0.9532 -0.2444 0.1577  0.1334  28   ILE D N   
9094  C  CA  . ILE D 28  ? 0.9689 1.6268 1.0505 -0.2166 0.1453  0.1171  28   ILE D CA  
9095  C  C   . ILE D 28  ? 0.9997 1.6380 1.0581 -0.1927 0.1421  0.1137  28   ILE D C   
9096  O  O   . ILE D 28  ? 1.2150 1.8226 1.2440 -0.1962 0.1427  0.1263  28   ILE D O   
9097  C  CB  . ILE D 28  ? 0.5832 1.2055 0.6738 -0.2174 0.1297  0.1164  28   ILE D CB  
9098  C  CG1 . ILE D 28  ? 0.3028 0.9301 0.4062 -0.2472 0.1331  0.1239  28   ILE D CG1 
9099  C  CG2 . ILE D 28  ? 0.3217 0.9628 0.4356 -0.1951 0.1204  0.0986  28   ILE D CG2 
9100  C  CD1 . ILE D 28  ? 0.2953 0.8924 0.4078 -0.2512 0.1194  0.1215  28   ILE D CD1 
9101  N  N   . LYS D 29  ? 0.6566 1.3131 0.7288 -0.1687 0.1383  0.0966  29   LYS D N   
9102  C  CA  . LYS D 29  ? 0.4615 1.1038 0.5155 -0.1462 0.1359  0.0899  29   LYS D CA  
9103  C  C   . LYS D 29  ? 0.5672 1.1942 0.6342 -0.1235 0.1226  0.0771  29   LYS D C   
9104  O  O   . LYS D 29  ? 0.7669 1.4240 0.8607 -0.1144 0.1220  0.0653  29   LYS D O   
9105  C  CB  . LYS D 29  ? 0.7018 1.3893 0.7561 -0.1396 0.1508  0.0805  29   LYS D CB  
9106  C  CG  . LYS D 29  ? 0.7857 1.4923 0.8239 -0.1613 0.1661  0.0930  29   LYS D CG  
9107  C  CD  . LYS D 29  ? 0.8650 1.5537 0.8670 -0.1560 0.1690  0.0977  29   LYS D CD  
9108  C  CE  . LYS D 29  ? 0.9803 1.7048 0.9691 -0.1708 0.1876  0.1035  29   LYS D CE  
9109  N  NZ  . LYS D 29  ? 0.9653 1.6773 0.9175 -0.1646 0.1901  0.1063  29   LYS D NZ  
9110  N  N   . GLU D 30  ? 0.6745 1.2558 0.7224 -0.1141 0.1120  0.0802  30   GLU D N   
9111  C  CA  . GLU D 30  ? 0.6738 1.2323 0.7300 -0.0952 0.0990  0.0711  30   GLU D CA  
9112  C  C   . GLU D 30  ? 0.5955 1.1849 0.6717 -0.0748 0.1006  0.0540  30   GLU D C   
9113  O  O   . GLU D 30  ? 0.5582 1.1718 0.6312 -0.0664 0.1103  0.0461  30   GLU D O   
9114  C  CB  . GLU D 30  ? 0.7773 1.2938 0.8085 -0.0853 0.0918  0.0740  30   GLU D CB  
9115  C  CG  . GLU D 30  ? 0.8473 1.3316 0.8574 -0.1015 0.0895  0.0915  30   GLU D CG  
9116  C  CD  . GLU D 30  ? 0.8522 1.3121 0.8364 -0.0928 0.0865  0.0943  30   GLU D CD  
9117  O  OE1 . GLU D 30  ? 0.8525 1.3320 0.8227 -0.0931 0.0953  0.0935  30   GLU D OE1 
9118  O  OE2 . GLU D 30  ? 0.8961 1.3191 0.8740 -0.0861 0.0754  0.0967  30   GLU D OE2 
9119  N  N   . ASP D 31  ? 0.4192 1.0065 0.5151 -0.0663 0.0912  0.0483  31   ASP D N   
9120  C  CA  . ASP D 31  ? 0.4411 1.0477 0.5539 -0.0432 0.0902  0.0336  31   ASP D CA  
9121  C  C   . ASP D 31  ? 0.5763 1.1451 0.6730 -0.0249 0.0835  0.0288  31   ASP D C   
9122  O  O   . ASP D 31  ? 0.7797 1.3143 0.8732 -0.0213 0.0720  0.0316  31   ASP D O   
9123  C  CB  . ASP D 31  ? 0.5861 1.2044 0.7241 -0.0405 0.0815  0.0308  31   ASP D CB  
9124  C  CG  . ASP D 31  ? 0.6106 1.2336 0.7615 -0.0136 0.0767  0.0186  31   ASP D CG  
9125  O  OD1 . ASP D 31  ? 0.7104 1.3187 0.8693 -0.0070 0.0651  0.0184  31   ASP D OD1 
9126  O  OD2 . ASP D 31  ? 0.1730 0.8126 0.3245 0.0009  0.0850  0.0092  31   ASP D OD2 
9127  N  N   . GLU D 32  ? 0.4336 1.0090 0.5199 -0.0141 0.0911  0.0208  32   GLU D N   
9128  C  CA  . GLU D 32  ? 0.4927 1.0351 0.5660 0.0028  0.0853  0.0140  32   GLU D CA  
9129  C  C   . GLU D 32  ? 0.4171 0.9792 0.5042 0.0250  0.0899  -0.0022 32   GLU D C   
9130  O  O   . GLU D 32  ? 0.4118 0.9633 0.4864 0.0366  0.0931  -0.0116 32   GLU D O   
9131  C  CB  . GLU D 32  ? 0.4249 0.9460 0.4690 -0.0045 0.0873  0.0191  32   GLU D CB  
9132  C  CG  . GLU D 32  ? 0.5470 1.0462 0.5793 -0.0242 0.0822  0.0364  32   GLU D CG  
9133  C  CD  . GLU D 32  ? 0.5136 0.9975 0.5179 -0.0318 0.0842  0.0439  32   GLU D CD  
9134  O  OE1 . GLU D 32  ? 0.5142 0.9721 0.5053 -0.0220 0.0780  0.0402  32   GLU D OE1 
9135  O  OE2 . GLU D 32  ? 0.5101 1.0085 0.5054 -0.0481 0.0915  0.0540  32   GLU D OE2 
9136  N  N   . SER D 33  ? 0.3039 0.8943 0.4174 0.0308  0.0896  -0.0056 33   SER D N   
9137  C  CA  . SER D 33  ? 0.3569 0.9702 0.4883 0.0528  0.0940  -0.0196 33   SER D CA  
9138  C  C   . SER D 33  ? 0.3555 0.9314 0.4821 0.0728  0.0859  -0.0261 33   SER D C   
9139  O  O   . SER D 33  ? 0.4216 1.0064 0.5596 0.0934  0.0892  -0.0378 33   SER D O   
9140  C  CB  . SER D 33  ? 0.3003 0.9499 0.4618 0.0537  0.0919  -0.0188 33   SER D CB  
9141  O  OG  . SER D 33  ? 0.2889 0.9153 0.4518 0.0462  0.0786  -0.0091 33   SER D OG  
9142  N  N   . PHE D 34  ? 0.3942 0.9281 0.5049 0.0668  0.0759  -0.0182 34   PHE D N   
9143  C  CA  . PHE D 34  ? 0.4604 0.9569 0.5664 0.0830  0.0682  -0.0227 34   PHE D CA  
9144  C  C   . PHE D 34  ? 0.3936 0.8717 0.4819 0.0910  0.0735  -0.0330 34   PHE D C   
9145  O  O   . PHE D 34  ? 0.4214 0.8693 0.5061 0.1042  0.0690  -0.0386 34   PHE D O   
9146  C  CB  . PHE D 34  ? 0.4454 0.9068 0.5430 0.0737  0.0562  -0.0113 34   PHE D CB  
9147  C  CG  . PHE D 34  ? 0.5102 0.9609 0.5903 0.0527  0.0561  -0.0010 34   PHE D CG  
9148  C  CD1 . PHE D 34  ? 0.5605 0.9811 0.6191 0.0506  0.0546  -0.0003 34   PHE D CD1 
9149  C  CD2 . PHE D 34  ? 0.4358 0.9063 0.5214 0.0351  0.0572  0.0084  34   PHE D CD2 
9150  C  CE1 . PHE D 34  ? 0.4291 0.8396 0.4719 0.0333  0.0537  0.0105  34   PHE D CE1 
9151  C  CE2 . PHE D 34  ? 0.4605 0.9174 0.5294 0.0169  0.0572  0.0191  34   PHE D CE2 
9152  C  CZ  . PHE D 34  ? 0.3849 0.8118 0.4323 0.0170  0.0552  0.0207  34   PHE D CZ  
9153  N  N   . LEU D 35  ? 0.4732 0.9703 0.5502 0.0823  0.0833  -0.0359 35   LEU D N   
9154  C  CA  . LEU D 35  ? 0.4350 0.9185 0.4925 0.0868  0.0884  -0.0463 35   LEU D CA  
9155  C  C   . LEU D 35  ? 0.4896 0.9910 0.5562 0.1058  0.0984  -0.0643 35   LEU D C   
9156  O  O   . LEU D 35  ? 0.5076 0.9927 0.5599 0.1127  0.1018  -0.0763 35   LEU D O   
9157  C  CB  . LEU D 35  ? 0.4990 0.9941 0.5363 0.0682  0.0939  -0.0402 35   LEU D CB  
9158  C  CG  . LEU D 35  ? 0.6193 1.1028 0.6484 0.0483  0.0867  -0.0215 35   LEU D CG  
9159  C  CD1 . LEU D 35  ? 0.4722 0.9766 0.4848 0.0312  0.0950  -0.0145 35   LEU D CD1 
9160  C  CD2 . LEU D 35  ? 0.5452 0.9838 0.5615 0.0480  0.0746  -0.0165 35   LEU D CD2 
9161  N  N   . GLN D 36  ? 0.3918 0.9273 0.4825 0.1142  0.1033  -0.0669 36   GLN D N   
9162  C  CA  . GLN D 36  ? 0.4785 1.0340 0.5807 0.1338  0.1138  -0.0840 36   GLN D CA  
9163  C  C   . GLN D 36  ? 0.5392 1.0591 0.6437 0.1550  0.1091  -0.0935 36   GLN D C   
9164  O  O   . GLN D 36  ? 0.4405 0.9379 0.5533 0.1606  0.0981  -0.0859 36   GLN D O   
9165  C  CB  . GLN D 36  ? 0.6792 1.2822 0.8103 0.1389  0.1190  -0.0835 36   GLN D CB  
9166  C  CG  . GLN D 36  ? 0.8591 1.4947 1.0014 0.1554  0.1337  -0.1008 36   GLN D CG  
9167  C  CD  . GLN D 36  ? 0.8535 1.5284 0.9885 0.1399  0.1474  -0.1022 36   GLN D CD  
9168  O  OE1 . GLN D 36  ? 0.4859 1.1832 0.6209 0.1495  0.1611  -0.1173 36   GLN D OE1 
9169  N  NE2 . GLN D 36  ? 1.0876 1.7699 1.2155 0.1157  0.1444  -0.0863 36   GLN D NE2 
9170  N  N   . GLN D 37  ? 0.5576 1.0723 0.6536 0.1663  0.1181  -0.1106 37   GLN D N   
9171  C  CA  . GLN D 37  ? 0.7014 1.1800 0.7980 0.1855  0.1157  -0.1213 37   GLN D CA  
9172  C  C   . GLN D 37  ? 0.6497 1.0828 0.7324 0.1770  0.1027  -0.1115 37   GLN D C   
9173  O  O   . GLN D 37  ? 0.7865 1.2009 0.8803 0.1844  0.0937  -0.1034 37   GLN D O   
9174  C  CB  . GLN D 37  ? 0.8221 1.3125 0.9471 0.2073  0.1150  -0.1222 37   GLN D CB  
9175  C  CG  . GLN D 37  ? 1.0014 1.5450 1.1459 0.2144  0.1269  -0.1290 37   GLN D CG  
9176  C  CD  . GLN D 37  ? 1.0982 1.6566 1.2726 0.2371  0.1246  -0.1288 37   GLN D CD  
9177  O  OE1 . GLN D 37  ? 1.1337 1.6573 1.3112 0.2515  0.1164  -0.1269 37   GLN D OE1 
9178  N  NE2 . GLN D 37  ? 1.1042 1.7158 1.3012 0.2404  0.1318  -0.1300 37   GLN D NE2 
9179  N  N   . PRO D 38  ? 0.5416 0.9589 0.5998 0.1615  0.1018  -0.1119 38   PRO D N   
9180  C  CA  . PRO D 38  ? 0.4286 0.8062 0.4739 0.1523  0.0901  -0.1031 38   PRO D CA  
9181  C  C   . PRO D 38  ? 0.4177 0.7590 0.4684 0.1688  0.0868  -0.1101 38   PRO D C   
9182  O  O   . PRO D 38  ? 0.5967 0.9345 0.6502 0.1839  0.0947  -0.1262 38   PRO D O   
9183  C  CB  . PRO D 38  ? 0.3256 0.6974 0.3455 0.1395  0.0926  -0.1095 38   PRO D CB  
9184  C  CG  . PRO D 38  ? 0.2899 0.7022 0.3069 0.1367  0.1046  -0.1160 38   PRO D CG  
9185  C  CD  . PRO D 38  ? 0.3943 0.8290 0.4354 0.1552  0.1123  -0.1236 38   PRO D CD  
9186  N  N   . HIS D 39  ? 0.5417 0.8548 0.5933 0.1659  0.0761  -0.0984 39   HIS D N   
9187  C  CA  . HIS D 39  ? 0.6038 0.8798 0.6588 0.1798  0.0730  -0.1027 39   HIS D CA  
9188  C  C   . HIS D 39  ? 0.5731 0.8229 0.6254 0.1712  0.0616  -0.0876 39   HIS D C   
9189  O  O   . HIS D 39  ? 0.4951 0.7592 0.5487 0.1594  0.0562  -0.0740 39   HIS D O   
9190  C  CB  . HIS D 39  ? 0.6054 0.8927 0.6814 0.2016  0.0766  -0.1056 39   HIS D CB  
9191  C  CG  . HIS D 39  ? 0.4973 0.8016 0.5888 0.2023  0.0691  -0.0896 39   HIS D CG  
9192  N  ND1 . HIS D 39  ? 0.5785 0.9175 0.6737 0.1883  0.0679  -0.0803 39   HIS D ND1 
9193  C  CD2 . HIS D 39  ? 0.5121 0.8036 0.6154 0.2147  0.0624  -0.0814 39   HIS D CD2 
9194  C  CE1 . HIS D 39  ? 0.5559 0.9033 0.6651 0.1913  0.0605  -0.0685 39   HIS D CE1 
9195  N  NE2 . HIS D 39  ? 0.5004 0.8206 0.6142 0.2078  0.0567  -0.0687 39   HIS D NE2 
9196  N  N   . TYR D 40  ? 0.6940 0.9046 0.7421 0.1766  0.0586  -0.0904 40   TYR D N   
9197  C  CA  . TYR D 40  ? 0.5954 0.7808 0.6410 0.1695  0.0491  -0.0770 40   TYR D CA  
9198  C  C   . TYR D 40  ? 0.4807 0.6648 0.5408 0.1822  0.0449  -0.0670 40   TYR D C   
9199  O  O   . TYR D 40  ? 0.5855 0.7596 0.6538 0.2001  0.0478  -0.0722 40   TYR D O   
9200  C  CB  . TYR D 40  ? 0.6053 0.7511 0.6395 0.1665  0.0481  -0.0836 40   TYR D CB  
9201  C  CG  . TYR D 40  ? 0.5868 0.7346 0.6057 0.1496  0.0476  -0.0883 40   TYR D CG  
9202  C  CD1 . TYR D 40  ? 0.7761 0.9212 0.7857 0.1498  0.0538  -0.1056 40   TYR D CD1 
9203  C  CD2 . TYR D 40  ? 0.4891 0.6419 0.5025 0.1343  0.0407  -0.0757 40   TYR D CD2 
9204  C  CE1 . TYR D 40  ? 0.7723 0.9220 0.7669 0.1347  0.0521  -0.1094 40   TYR D CE1 
9205  C  CE2 . TYR D 40  ? 0.5798 0.7358 0.5796 0.1205  0.0392  -0.0786 40   TYR D CE2 
9206  C  CZ  . TYR D 40  ? 0.5943 0.7500 0.5845 0.1207  0.0445  -0.0951 40   TYR D CZ  
9207  O  OH  . TYR D 40  ? 0.5452 0.7065 0.5210 0.1074  0.0418  -0.0976 40   TYR D OH  
9208  N  N   . ALA D 41  ? 0.4082 0.6027 0.4708 0.1730  0.0377  -0.0527 41   ALA D N   
9209  C  CA  . ALA D 41  ? 0.4762 0.6722 0.5500 0.1821  0.0318  -0.0420 41   ALA D CA  
9210  C  C   . ALA D 41  ? 0.3490 0.5040 0.4178 0.1886  0.0279  -0.0381 41   ALA D C   
9211  O  O   . ALA D 41  ? 0.4461 0.5785 0.5041 0.1767  0.0245  -0.0337 41   ALA D O   
9212  C  CB  . ALA D 41  ? 0.4318 0.6465 0.5064 0.1675  0.0253  -0.0296 41   ALA D CB  
9213  N  N   . SER D 42  ? 0.4375 0.5834 0.5145 0.2077  0.0288  -0.0390 42   SER D N   
9214  C  CA  . SER D 42  ? 0.4800 0.5855 0.5511 0.2139  0.0260  -0.0338 42   SER D CA  
9215  C  C   . SER D 42  ? 0.5022 0.6079 0.5717 0.2077  0.0171  -0.0181 42   SER D C   
9216  O  O   . SER D 42  ? 0.5525 0.6889 0.6266 0.1997  0.0132  -0.0129 42   SER D O   
9217  C  CB  . SER D 42  ? 0.4228 0.5194 0.5032 0.2375  0.0288  -0.0365 42   SER D CB  
9218  O  OG  . SER D 42  ? 0.4707 0.5957 0.5636 0.2472  0.0232  -0.0269 42   SER D OG  
9219  N  N   . GLN D 43  ? 0.4159 0.4871 0.4783 0.2111  0.0144  -0.0111 43   GLN D N   
9220  C  CA  . GLN D 43  ? 0.3574 0.4268 0.4165 0.2077  0.0064  0.0033  43   GLN D CA  
9221  C  C   . GLN D 43  ? 0.5361 0.6372 0.6072 0.2195  0.0010  0.0097  43   GLN D C   
9222  O  O   . GLN D 43  ? 0.5312 0.6542 0.6033 0.2102  -0.0052 0.0165  43   GLN D O   
9223  C  CB  . GLN D 43  ? 0.4980 0.5255 0.5473 0.2123  0.0061  0.0098  43   GLN D CB  
9224  C  CG  . GLN D 43  ? 0.6991 0.7237 0.7416 0.2077  -0.0013 0.0242  43   GLN D CG  
9225  C  CD  . GLN D 43  ? 0.7338 0.7649 0.7700 0.1868  -0.0034 0.0255  43   GLN D CD  
9226  O  OE1 . GLN D 43  ? 0.8100 0.8337 0.8431 0.1752  0.0007  0.0182  43   GLN D OE1 
9227  N  NE2 . GLN D 43  ? 0.7489 0.7937 0.7830 0.1823  -0.0101 0.0346  43   GLN D NE2 
9228  N  N   . GLU D 44  ? 0.5448 0.6488 0.6258 0.2400  0.0032  0.0069  44   GLU D N   
9229  C  CA  . GLU D 44  ? 0.5935 0.7330 0.6887 0.2521  -0.0024 0.0121  44   GLU D CA  
9230  C  C   . GLU D 44  ? 0.5612 0.7458 0.6667 0.2405  -0.0017 0.0069  44   GLU D C   
9231  O  O   . GLU D 44  ? 0.6635 0.8754 0.7738 0.2339  -0.0088 0.0138  44   GLU D O   
9232  C  CB  . GLU D 44  ? 0.5888 0.7264 0.6954 0.2781  0.0005  0.0092  44   GLU D CB  
9233  C  CG  . GLU D 44  ? 0.8134 0.9877 0.9354 0.2924  -0.0074 0.0171  44   GLU D CG  
9234  C  CD  . GLU D 44  ? 1.1020 1.2926 1.2422 0.3168  -0.0029 0.0103  44   GLU D CD  
9235  O  OE1 . GLU D 44  ? 1.2544 1.4214 1.3931 0.3239  0.0067  -0.0008 44   GLU D OE1 
9236  O  OE2 . GLU D 44  ? 1.1047 1.3328 1.2613 0.3289  -0.0091 0.0151  44   GLU D OE2 
9237  N  N   . GLN D 45  ? 0.4127 0.6046 0.5203 0.2369  0.0069  -0.0054 45   GLN D N   
9238  C  CA  . GLN D 45  ? 0.4452 0.6802 0.5625 0.2272  0.0092  -0.0099 45   GLN D CA  
9239  C  C   . GLN D 45  ? 0.4368 0.6789 0.5465 0.2044  0.0038  -0.0025 45   GLN D C   
9240  O  O   . GLN D 45  ? 0.4355 0.7136 0.5545 0.1961  0.0019  -0.0007 45   GLN D O   
9241  C  CB  . GLN D 45  ? 0.4671 0.7047 0.5831 0.2257  0.0200  -0.0240 45   GLN D CB  
9242  C  CG  . GLN D 45  ? 0.5152 0.7515 0.6412 0.2488  0.0266  -0.0337 45   GLN D CG  
9243  C  CD  . GLN D 45  ? 0.5699 0.8231 0.6971 0.2471  0.0376  -0.0489 45   GLN D CD  
9244  O  OE1 . GLN D 45  ? 0.4458 0.6773 0.5582 0.2369  0.0421  -0.0563 45   GLN D OE1 
9245  N  NE2 . GLN D 45  ? 0.6417 0.9361 0.7867 0.2572  0.0421  -0.0539 45   GLN D NE2 
9246  N  N   . LEU D 46  ? 0.3950 0.6020 0.4886 0.1943  0.0018  0.0014  46   LEU D N   
9247  C  CA  . LEU D 46  ? 0.4982 0.7060 0.5837 0.1739  -0.0023 0.0074  46   LEU D CA  
9248  C  C   . LEU D 46  ? 0.4960 0.7160 0.5848 0.1728  -0.0113 0.0172  46   LEU D C   
9249  O  O   . LEU D 46  ? 0.4018 0.6455 0.4940 0.1595  -0.0142 0.0196  46   LEU D O   
9250  C  CB  . LEU D 46  ? 0.4535 0.6218 0.5229 0.1655  -0.0017 0.0083  46   LEU D CB  
9251  C  CG  . LEU D 46  ? 0.4615 0.6226 0.5217 0.1477  -0.0061 0.0152  46   LEU D CG  
9252  C  CD1 . LEU D 46  ? 0.5937 0.7837 0.6577 0.1335  -0.0057 0.0150  46   LEU D CD1 
9253  C  CD2 . LEU D 46  ? 0.2637 0.3907 0.3115 0.1410  -0.0039 0.0138  46   LEU D CD2 
9254  N  N   . GLU D 47  ? 0.4591 0.6615 0.5456 0.1863  -0.0157 0.0228  47   GLU D N   
9255  C  CA  . GLU D 47  ? 0.4978 0.7105 0.5848 0.1870  -0.0250 0.0319  47   GLU D CA  
9256  C  C   . GLU D 47  ? 0.4460 0.7056 0.5516 0.1915  -0.0281 0.0307  47   GLU D C   
9257  O  O   . GLU D 47  ? 0.4866 0.7695 0.5953 0.1800  -0.0340 0.0339  47   GLU D O   
9258  C  CB  . GLU D 47  ? 0.6167 0.8019 0.6967 0.2032  -0.0282 0.0388  47   GLU D CB  
9259  C  CG  . GLU D 47  ? 0.5404 0.6809 0.6028 0.1971  -0.0253 0.0412  47   GLU D CG  
9260  C  CD  . GLU D 47  ? 0.5630 0.6755 0.6187 0.2132  -0.0266 0.0484  47   GLU D CD  
9261  O  OE1 . GLU D 47  ? 0.6547 0.7755 0.7204 0.2321  -0.0269 0.0483  47   GLU D OE1 
9262  O  OE2 . GLU D 47  ? 0.6471 0.7296 0.6879 0.2076  -0.0270 0.0545  47   GLU D OE2 
9263  N  N   . ASP D 48  ? 0.4962 0.7703 0.6151 0.2080  -0.0235 0.0251  48   ASP D N   
9264  C  CA  . ASP D 48  ? 0.5361 0.8587 0.6760 0.2133  -0.0250 0.0227  48   ASP D CA  
9265  C  C   . ASP D 48  ? 0.5011 0.8515 0.6450 0.1910  -0.0224 0.0193  48   ASP D C   
9266  O  O   . ASP D 48  ? 0.4762 0.8586 0.6296 0.1830  -0.0284 0.0221  48   ASP D O   
9267  C  CB  . ASP D 48  ? 0.5979 0.9289 0.7510 0.2344  -0.0178 0.0151  48   ASP D CB  
9268  C  CG  . ASP D 48  ? 0.7191 1.0262 0.8712 0.2584  -0.0213 0.0203  48   ASP D CG  
9269  O  OD1 . ASP D 48  ? 0.6069 0.9082 0.7537 0.2612  -0.0312 0.0311  48   ASP D OD1 
9270  O  OD2 . ASP D 48  ? 0.8742 1.1672 1.0300 0.2747  -0.0139 0.0136  48   ASP D OD2 
9271  N  N   . LEU D 49  ? 0.4254 0.7625 0.5610 0.1801  -0.0140 0.0136  49   LEU D N   
9272  C  CA  . LEU D 49  ? 0.3243 0.6845 0.4619 0.1596  -0.0107 0.0119  49   LEU D CA  
9273  C  C   . LEU D 49  ? 0.2747 0.6310 0.4050 0.1411  -0.0182 0.0191  49   LEU D C   
9274  O  O   . LEU D 49  ? 0.2340 0.6197 0.3726 0.1272  -0.0190 0.0197  49   LEU D O   
9275  C  CB  . LEU D 49  ? 0.4232 0.7659 0.5494 0.1519  -0.0015 0.0061  49   LEU D CB  
9276  C  CG  . LEU D 49  ? 0.4300 0.8011 0.5596 0.1344  0.0041  0.0043  49   LEU D CG  
9277  C  CD1 . LEU D 49  ? 0.6451 1.0183 0.7716 0.1376  0.0149  -0.0047 49   LEU D CD1 
9278  C  CD2 . LEU D 49  ? 0.4169 0.7721 0.5335 0.1129  0.0009  0.0110  49   LEU D CD2 
9279  N  N   . PHE D 50  ? 0.3913 0.7106 0.5059 0.1405  -0.0228 0.0241  50   PHE D N   
9280  C  CA  . PHE D 50  ? 0.3836 0.6937 0.4889 0.1238  -0.0289 0.0296  50   PHE D CA  
9281  C  C   . PHE D 50  ? 0.4335 0.7695 0.5474 0.1246  -0.0383 0.0330  50   PHE D C   
9282  O  O   . PHE D 50  ? 0.5937 0.9381 0.7062 0.1080  -0.0424 0.0346  50   PHE D O   
9283  C  CB  . PHE D 50  ? 0.4018 0.6674 0.4886 0.1241  -0.0301 0.0331  50   PHE D CB  
9284  C  CG  . PHE D 50  ? 0.4149 0.6581 0.4911 0.1122  -0.0241 0.0313  50   PHE D CG  
9285  C  CD1 . PHE D 50  ? 0.3379 0.5969 0.4186 0.1056  -0.0176 0.0270  50   PHE D CD1 
9286  C  CD2 . PHE D 50  ? 0.2348 0.4429 0.2964 0.1078  -0.0250 0.0344  50   PHE D CD2 
9287  C  CE1 . PHE D 50  ? 0.4006 0.6404 0.4706 0.0955  -0.0134 0.0265  50   PHE D CE1 
9288  C  CE2 . PHE D 50  ? 0.1472 0.3378 0.2008 0.0982  -0.0207 0.0332  50   PHE D CE2 
9289  C  CZ  . PHE D 50  ? 0.3777 0.5837 0.4351 0.0923  -0.0154 0.0296  50   PHE D CZ  
9290  N  N   . ALA D 51  ? 0.3278 0.6754 0.4504 0.1443  -0.0420 0.0341  51   ALA D N   
9291  C  CA  . ALA D 51  ? 0.4079 0.7867 0.5408 0.1472  -0.0519 0.0371  51   ALA D CA  
9292  C  C   . ALA D 51  ? 0.5916 1.0197 0.7460 0.1393  -0.0503 0.0323  51   ALA D C   
9293  O  O   . ALA D 51  ? 0.7080 1.1632 0.8695 0.1278  -0.0573 0.0330  51   ALA D O   
9294  C  CB  . ALA D 51  ? 0.2543 0.6313 0.3906 0.1725  -0.0566 0.0411  51   ALA D CB  
9295  N  N   . GLY D 52  ? 0.5231 0.9635 0.6877 0.1444  -0.0405 0.0267  52   GLY D N   
9296  C  CA  . GLY D 52  ? 0.3805 0.8686 0.5659 0.1375  -0.0367 0.0221  52   GLY D CA  
9297  C  C   . GLY D 52  ? 0.3909 0.8850 0.5728 0.1095  -0.0353 0.0223  52   GLY D C   
9298  O  O   . GLY D 52  ? 0.3396 0.8727 0.5370 0.0983  -0.0380 0.0212  52   GLY D O   
9299  N  N   . LEU D 53  ? 0.3389 0.7944 0.5011 0.0980  -0.0310 0.0238  53   LEU D N   
9300  C  CA  . LEU D 53  ? 0.3389 0.7918 0.4951 0.0726  -0.0294 0.0253  53   LEU D CA  
9301  C  C   . LEU D 53  ? 0.4163 0.8684 0.5696 0.0614  -0.0397 0.0280  53   LEU D C   
9302  O  O   . LEU D 53  ? 0.5601 1.0310 0.7194 0.0420  -0.0404 0.0275  53   LEU D O   
9303  C  CB  . LEU D 53  ? 0.3012 0.7117 0.4371 0.0662  -0.0238 0.0271  53   LEU D CB  
9304  C  CG  . LEU D 53  ? 0.3651 0.7736 0.5001 0.0750  -0.0138 0.0233  53   LEU D CG  
9305  C  CD1 . LEU D 53  ? 0.5977 0.9682 0.7129 0.0667  -0.0100 0.0254  53   LEU D CD1 
9306  C  CD2 . LEU D 53  ? 0.1255 0.5764 0.2762 0.0689  -0.0067 0.0199  53   LEU D CD2 
9307  N  N   . GLU D 54  ? 0.3423 0.7717 0.4852 0.0727  -0.0473 0.0306  54   GLU D N   
9308  C  CA  . GLU D 54  ? 0.5563 0.9840 0.6933 0.0635  -0.0573 0.0323  54   GLU D CA  
9309  C  C   . GLU D 54  ? 0.5730 1.0512 0.7305 0.0596  -0.0642 0.0298  54   GLU D C   
9310  O  O   . GLU D 54  ? 0.4783 0.9664 0.6361 0.0408  -0.0690 0.0281  54   GLU D O   
9311  C  CB  . GLU D 54  ? 0.6548 1.0533 0.7768 0.0789  -0.0635 0.0362  54   GLU D CB  
9312  C  CG  . GLU D 54  ? 0.7847 1.1668 0.8918 0.0671  -0.0710 0.0373  54   GLU D CG  
9313  C  CD  . GLU D 54  ? 0.8368 1.1849 0.9257 0.0804  -0.0742 0.0420  54   GLU D CD  
9314  O  OE1 . GLU D 54  ? 0.8362 1.1658 0.9097 0.0714  -0.0784 0.0424  54   GLU D OE1 
9315  O  OE2 . GLU D 54  ? 0.8308 1.1697 0.9202 0.0995  -0.0717 0.0448  54   GLU D OE2 
9316  N  N   . LYS D 55  ? 0.5525 1.0634 0.7282 0.0774  -0.0645 0.0288  55   LYS D N   
9317  C  CA  . LYS D 55  ? 0.4838 1.0484 0.6825 0.0749  -0.0710 0.0262  55   LYS D CA  
9318  C  C   . LYS D 55  ? 0.4024 0.9994 0.6184 0.0585  -0.0619 0.0219  55   LYS D C   
9319  O  O   . LYS D 55  ? 0.2570 0.8885 0.4866 0.0419  -0.0657 0.0192  55   LYS D O   
9320  C  CB  . LYS D 55  ? 0.3713 0.9602 0.5838 0.1026  -0.0766 0.0277  55   LYS D CB  
9321  C  CG  . LYS D 55  ? 0.4719 1.0514 0.6885 0.1233  -0.0666 0.0269  55   LYS D CG  
9322  C  CD  . LYS D 55  ? 0.5016 1.1049 0.7334 0.1518  -0.0727 0.0288  55   LYS D CD  
9323  C  CE  . LYS D 55  ? 0.4741 1.1426 0.7376 0.1524  -0.0749 0.0247  55   LYS D CE  
9324  N  NZ  . LYS D 55  ? 0.4475 1.1399 0.7275 0.1827  -0.0810 0.0270  55   LYS D NZ  
9325  N  N   . ALA D 56  ? 0.3169 0.9029 0.5314 0.0618  -0.0495 0.0210  56   ALA D N   
9326  C  CA  . ALA D 56  ? 0.2785 0.8920 0.5055 0.0451  -0.0395 0.0181  56   ALA D CA  
9327  C  C   . ALA D 56  ? 0.2955 0.8915 0.5110 0.0159  -0.0391 0.0199  56   ALA D C   
9328  O  O   . ALA D 56  ? 0.2686 0.8942 0.4970 -0.0036 -0.0357 0.0183  56   ALA D O   
9329  C  CB  . ALA D 56  ? 0.1580 0.7596 0.3807 0.0544  -0.0266 0.0168  56   ALA D CB  
9330  N  N   . TYR D 57  ? 0.2675 0.8145 0.4593 0.0131  -0.0424 0.0231  57   TYR D N   
9331  C  CA  . TYR D 57  ? 0.3207 0.8432 0.4997 -0.0117 -0.0416 0.0248  57   TYR D CA  
9332  C  C   . TYR D 57  ? 0.3804 0.8774 0.5454 -0.0142 -0.0523 0.0249  57   TYR D C   
9333  O  O   . TYR D 57  ? 0.4925 0.9443 0.6369 -0.0147 -0.0515 0.0275  57   TYR D O   
9334  C  CB  . TYR D 57  ? 0.2463 0.7308 0.4082 -0.0147 -0.0318 0.0286  57   TYR D CB  
9335  C  CG  . TYR D 57  ? 0.4734 0.9801 0.6443 -0.0124 -0.0204 0.0283  57   TYR D CG  
9336  C  CD1 . TYR D 57  ? 0.4841 0.9951 0.6577 0.0103  -0.0170 0.0260  57   TYR D CD1 
9337  C  CD2 . TYR D 57  ? 0.4261 0.9482 0.6016 -0.0336 -0.0125 0.0300  57   TYR D CD2 
9338  C  CE1 . TYR D 57  ? 0.3869 0.9184 0.5670 0.0125  -0.0059 0.0241  57   TYR D CE1 
9339  C  CE2 . TYR D 57  ? 0.3129 0.8565 0.4944 -0.0319 -0.0012 0.0297  57   TYR D CE2 
9340  C  CZ  . TYR D 57  ? 0.3564 0.9053 0.5400 -0.0086 0.0020  0.0261  57   TYR D CZ  
9341  O  OH  . TYR D 57  ? 0.3399 0.9102 0.5279 -0.0064 0.0136  0.0241  57   TYR D OH  
9342  N  N   . PRO D 58  ? 0.2628 0.7913 0.4393 -0.0160 -0.0624 0.0216  58   PRO D N   
9343  C  CA  . PRO D 58  ? 0.1928 0.7059 0.3566 -0.0152 -0.0738 0.0207  58   PRO D CA  
9344  C  C   . PRO D 58  ? 0.4942 0.9632 0.6368 -0.0325 -0.0729 0.0204  58   PRO D C   
9345  O  O   . PRO D 58  ? 0.8149 1.2547 0.9400 -0.0252 -0.0779 0.0211  58   PRO D O   
9346  C  CB  . PRO D 58  ? 0.2368 0.8004 0.4201 -0.0241 -0.0829 0.0158  58   PRO D CB  
9347  C  CG  . PRO D 58  ? 0.2889 0.8977 0.4980 -0.0165 -0.0773 0.0154  58   PRO D CG  
9348  C  CD  . PRO D 58  ? 0.2589 0.8448 0.4626 -0.0207 -0.0629 0.0180  58   PRO D CD  
9349  N  N   . ASN D 59  ? 0.5046 0.9679 0.6484 -0.0546 -0.0662 0.0196  59   ASN D N   
9350  C  CA  . ASN D 59  ? 0.5838 1.0074 0.7098 -0.0714 -0.0661 0.0183  59   ASN D CA  
9351  C  C   . ASN D 59  ? 0.5007 0.8781 0.6105 -0.0694 -0.0570 0.0238  59   ASN D C   
9352  O  O   . ASN D 59  ? 0.3603 0.7007 0.4550 -0.0791 -0.0562 0.0235  59   ASN D O   
9353  C  CB  . ASN D 59  ? 0.7074 1.1479 0.8429 -0.0992 -0.0657 0.0139  59   ASN D CB  
9354  C  CG  . ASN D 59  ? 0.7863 1.2781 0.9405 -0.1035 -0.0752 0.0077  59   ASN D CG  
9355  O  OD1 . ASN D 59  ? 0.7273 1.2531 0.8944 -0.0853 -0.0794 0.0084  59   ASN D OD1 
9356  N  ND2 . ASN D 59  ? 0.8610 1.3588 1.0174 -0.1277 -0.0789 0.0011  59   ASN D ND2 
9357  N  N   . GLN D 60  ? 0.3094 0.6903 0.4230 -0.0563 -0.0503 0.0283  60   GLN D N   
9358  C  CA  . GLN D 60  ? 0.4181 0.7631 0.5189 -0.0565 -0.0420 0.0336  60   GLN D CA  
9359  C  C   . GLN D 60  ? 0.4040 0.7346 0.4982 -0.0338 -0.0404 0.0360  60   GLN D C   
9360  O  O   . GLN D 60  ? 0.4179 0.7174 0.5003 -0.0316 -0.0355 0.0396  60   GLN D O   
9361  C  CB  . GLN D 60  ? 0.4146 0.7759 0.5241 -0.0696 -0.0332 0.0367  60   GLN D CB  
9362  C  CG  . GLN D 60  ? 0.5898 0.9985 0.7198 -0.0808 -0.0344 0.0329  60   GLN D CG  
9363  C  CD  . GLN D 60  ? 0.6819 1.0929 0.8149 -0.1059 -0.0276 0.0355  60   GLN D CD  
9364  O  OE1 . GLN D 60  ? 0.6196 1.0709 0.7703 -0.1158 -0.0244 0.0341  60   GLN D OE1 
9365  N  NE2 . GLN D 60  ? 0.6096 0.9771 0.7259 -0.1164 -0.0248 0.0397  60   GLN D NE2 
9366  N  N   . ALA D 61  ? 0.3061 0.6595 0.4087 -0.0171 -0.0447 0.0339  61   ALA D N   
9367  C  CA  . ALA D 61  ? 0.2214 0.5587 0.3177 0.0040  -0.0434 0.0355  61   ALA D CA  
9368  C  C   . ALA D 61  ? 0.1299 0.4584 0.2195 0.0152  -0.0520 0.0350  61   ALA D C   
9369  O  O   . ALA D 61  ? 0.1990 0.5564 0.2980 0.0182  -0.0591 0.0332  61   ALA D O   
9370  C  CB  . ALA D 61  ? 0.3352 0.7031 0.4463 0.0166  -0.0392 0.0343  61   ALA D CB  
9371  N  N   . LYS D 62  ? 0.1845 0.4748 0.2576 0.0210  -0.0513 0.0371  62   LYS D N   
9372  C  CA  . LYS D 62  ? 0.1639 0.4419 0.2275 0.0326  -0.0577 0.0380  62   LYS D CA  
9373  C  C   . LYS D 62  ? 0.2094 0.4598 0.2643 0.0484  -0.0535 0.0410  62   LYS D C   
9374  O  O   . LYS D 62  ? 0.3907 0.6182 0.4399 0.0451  -0.0471 0.0417  62   LYS D O   
9375  C  CB  . LYS D 62  ? 0.2863 0.5447 0.3366 0.0196  -0.0614 0.0364  62   LYS D CB  
9376  C  CG  . LYS D 62  ? 0.4534 0.7022 0.4913 0.0291  -0.0681 0.0373  62   LYS D CG  
9377  C  CD  . LYS D 62  ? 0.6952 0.9305 0.7207 0.0143  -0.0714 0.0332  62   LYS D CD  
9378  C  CE  . LYS D 62  ? 0.8486 1.0694 0.8573 0.0232  -0.0761 0.0344  62   LYS D CE  
9379  N  NZ  . LYS D 62  ? 0.9753 1.2240 0.9883 0.0365  -0.0845 0.0374  62   LYS D NZ  
9380  N  N   . VAL D 63  ? 0.3006 0.5537 0.3549 0.0652  -0.0574 0.0431  63   VAL D N   
9381  C  CA  . VAL D 63  ? 0.3169 0.5417 0.3627 0.0791  -0.0536 0.0459  63   VAL D CA  
9382  C  C   . VAL D 63  ? 0.5105 0.7057 0.5384 0.0788  -0.0558 0.0487  63   VAL D C   
9383  O  O   . VAL D 63  ? 0.5253 0.7277 0.5474 0.0768  -0.0628 0.0495  63   VAL D O   
9384  C  CB  . VAL D 63  ? 0.3020 0.5408 0.3563 0.0988  -0.0551 0.0475  63   VAL D CB  
9385  C  CG1 . VAL D 63  ? 0.3170 0.5218 0.3601 0.1114  -0.0517 0.0507  63   VAL D CG1 
9386  C  CG2 . VAL D 63  ? 0.3311 0.5950 0.4020 0.1010  -0.0501 0.0435  63   VAL D CG2 
9387  N  N   . HIS D 64  ? 0.4465 0.6105 0.4658 0.0803  -0.0497 0.0497  64   HIS D N   
9388  C  CA  . HIS D 64  ? 0.3332 0.4689 0.3366 0.0789  -0.0493 0.0518  64   HIS D CA  
9389  C  C   . HIS D 64  ? 0.3907 0.5047 0.3889 0.0920  -0.0455 0.0553  64   HIS D C   
9390  O  O   . HIS D 64  ? 0.4521 0.5592 0.4560 0.0956  -0.0401 0.0538  64   HIS D O   
9391  C  CB  . HIS D 64  ? 0.1809 0.2996 0.1800 0.0648  -0.0450 0.0491  64   HIS D CB  
9392  C  CG  . HIS D 64  ? 0.4096 0.5433 0.4118 0.0505  -0.0482 0.0459  64   HIS D CG  
9393  N  ND1 . HIS D 64  ? 0.5091 0.6400 0.5020 0.0431  -0.0524 0.0439  64   HIS D ND1 
9394  C  CD2 . HIS D 64  ? 0.4468 0.5986 0.4600 0.0414  -0.0474 0.0439  64   HIS D CD2 
9395  C  CE1 . HIS D 64  ? 0.5760 0.7207 0.5746 0.0295  -0.0542 0.0402  64   HIS D CE1 
9396  N  NE2 . HIS D 64  ? 0.4749 0.6324 0.4861 0.0280  -0.0510 0.0409  64   HIS D NE2 
9397  N  N   . PHE D 65  ? 0.3971 0.4999 0.3834 0.0981  -0.0482 0.0599  65   PHE D N   
9398  C  CA  . PHE D 65  ? 0.4416 0.5205 0.4214 0.1092  -0.0442 0.0645  65   PHE D CA  
9399  C  C   . PHE D 65  ? 0.4483 0.4995 0.4171 0.1014  -0.0383 0.0643  65   PHE D C   
9400  O  O   . PHE D 65  ? 0.5793 0.6265 0.5374 0.0944  -0.0398 0.0646  65   PHE D O   
9401  C  CB  . PHE D 65  ? 0.3472 0.4297 0.3195 0.1215  -0.0501 0.0716  65   PHE D CB  
9402  C  CG  . PHE D 65  ? 0.5119 0.5650 0.4737 0.1307  -0.0455 0.0780  65   PHE D CG  
9403  C  CD1 . PHE D 65  ? 0.5916 0.6239 0.5365 0.1256  -0.0431 0.0816  65   PHE D CD1 
9404  C  CD2 . PHE D 65  ? 0.5529 0.5984 0.5215 0.1439  -0.0428 0.0800  65   PHE D CD2 
9405  C  CE1 . PHE D 65  ? 0.7136 0.7188 0.6487 0.1323  -0.0379 0.0883  65   PHE D CE1 
9406  C  CE2 . PHE D 65  ? 0.7315 0.7468 0.6902 0.1509  -0.0380 0.0861  65   PHE D CE2 
9407  C  CZ  . PHE D 65  ? 0.8176 0.8131 0.7596 0.1445  -0.0355 0.0909  65   PHE D CZ  
9408  N  N   . LEU D 66  ? 0.4819 0.5156 0.4540 0.1025  -0.0315 0.0631  66   LEU D N   
9409  C  CA  . LEU D 66  ? 0.4015 0.4131 0.3677 0.0950  -0.0255 0.0621  66   LEU D CA  
9410  C  C   . LEU D 66  ? 0.4200 0.4087 0.3769 0.1012  -0.0213 0.0673  66   LEU D C   
9411  O  O   . LEU D 66  ? 0.4415 0.4148 0.3900 0.0959  -0.0171 0.0683  66   LEU D O   
9412  C  CB  . LEU D 66  ? 0.2643 0.2743 0.2410 0.0905  -0.0213 0.0570  66   LEU D CB  
9413  C  CG  . LEU D 66  ? 0.3063 0.3361 0.2915 0.0835  -0.0239 0.0531  66   LEU D CG  
9414  C  CD1 . LEU D 66  ? 0.2784 0.3023 0.2694 0.0786  -0.0196 0.0498  66   LEU D CD1 
9415  C  CD2 . LEU D 66  ? 0.2965 0.3312 0.2766 0.0744  -0.0271 0.0529  66   LEU D CD2 
9416  N  N   . GLY D 67  ? 0.4717 0.4573 0.4308 0.1125  -0.0216 0.0703  67   GLY D N   
9417  C  CA  . GLY D 67  ? 0.5237 0.4846 0.4743 0.1184  -0.0170 0.0761  67   GLY D CA  
9418  C  C   . GLY D 67  ? 0.5061 0.4621 0.4633 0.1306  -0.0163 0.0769  67   GLY D C   
9419  O  O   . GLY D 67  ? 0.4655 0.4410 0.4330 0.1365  -0.0201 0.0736  67   GLY D O   
9420  N  N   . ARG D 68  ? 0.5906 0.5197 0.5422 0.1340  -0.0106 0.0808  68   ARG D N   
9421  C  CA  . ARG D 68  ? 0.5496 0.4668 0.5066 0.1454  -0.0084 0.0806  68   ARG D CA  
9422  C  C   . ARG D 68  ? 0.6505 0.5418 0.6091 0.1394  0.0002  0.0763  68   ARG D C   
9423  O  O   . ARG D 68  ? 0.6043 0.4804 0.5559 0.1301  0.0050  0.0789  68   ARG D O   
9424  C  CB  . ARG D 68  ? 0.4046 0.3130 0.3520 0.1596  -0.0116 0.0920  68   ARG D CB  
9425  C  CG  . ARG D 68  ? 0.5221 0.4561 0.4779 0.1729  -0.0194 0.0924  68   ARG D CG  
9426  C  CD  . ARG D 68  ? 0.5911 0.5282 0.5351 0.1834  -0.0262 0.1050  68   ARG D CD  
9427  N  NE  . ARG D 68  ? 0.5384 0.5000 0.4929 0.1984  -0.0336 0.1059  68   ARG D NE  
9428  C  CZ  . ARG D 68  ? 0.8699 0.8550 0.8206 0.2041  -0.0433 0.1125  68   ARG D CZ  
9429  N  NH1 . ARG D 68  ? 0.9208 0.9058 0.8552 0.1955  -0.0464 0.1180  68   ARG D NH1 
9430  N  NH2 . ARG D 68  ? 1.0560 1.0666 1.0196 0.2184  -0.0498 0.1128  68   ARG D NH2 
9431  N  N   . SER D 69  ? 0.6253 0.5139 0.5939 0.1441  0.0024  0.0686  69   SER D N   
9432  C  CA  . SER D 69  ? 0.3900 0.2549 0.3611 0.1387  0.0099  0.0626  69   SER D CA  
9433  C  C   . SER D 69  ? 0.5568 0.3886 0.5180 0.1440  0.0145  0.0716  69   SER D C   
9434  O  O   . SER D 69  ? 0.4456 0.2740 0.3986 0.1551  0.0113  0.0825  69   SER D O   
9435  C  CB  . SER D 69  ? 0.3756 0.2459 0.3574 0.1444  0.0107  0.0516  69   SER D CB  
9436  O  OG  . SER D 69  ? 0.4051 0.2634 0.3864 0.1608  0.0109  0.0550  69   SER D OG  
9437  N  N   . LEU D 70  ? 0.6951 0.5031 0.6571 0.1355  0.0220  0.0675  70   LEU D N   
9438  C  CA  . LEU D 70  ? 0.6629 0.4355 0.6161 0.1386  0.0280  0.0755  70   LEU D CA  
9439  C  C   . LEU D 70  ? 0.6744 0.4374 0.6256 0.1581  0.0254  0.0809  70   LEU D C   
9440  O  O   . LEU D 70  ? 0.7403 0.4876 0.6798 0.1666  0.0250  0.0948  70   LEU D O   
9441  C  CB  . LEU D 70  ? 0.6969 0.4475 0.6559 0.1275  0.0359  0.0660  70   LEU D CB  
9442  C  CG  . LEU D 70  ? 0.5862 0.3415 0.5486 0.1087  0.0398  0.0616  70   LEU D CG  
9443  C  CD1 . LEU D 70  ? 0.5981 0.3372 0.5689 0.0991  0.0457  0.0496  70   LEU D CD1 
9444  C  CD2 . LEU D 70  ? 0.4656 0.2079 0.4163 0.1037  0.0440  0.0746  70   LEU D CD2 
9445  N  N   . GLU D 71  ? 0.5825 0.3565 0.5450 0.1660  0.0237  0.0702  71   GLU D N   
9446  C  CA  . GLU D 71  ? 0.5678 0.3299 0.5315 0.1855  0.0230  0.0729  71   GLU D CA  
9447  C  C   . GLU D 71  ? 0.6528 0.4454 0.6186 0.1998  0.0139  0.0793  71   GLU D C   
9448  O  O   . GLU D 71  ? 0.7668 0.5618 0.7391 0.2170  0.0123  0.0783  71   GLU D O   
9449  C  CB  . GLU D 71  ? 0.6347 0.3896 0.6091 0.1878  0.0276  0.0570  71   GLU D CB  
9450  C  CG  . GLU D 71  ? 0.6904 0.4127 0.6629 0.1739  0.0362  0.0500  71   GLU D CG  
9451  C  CD  . GLU D 71  ? 0.8495 0.5650 0.8309 0.1751  0.0405  0.0322  71   GLU D CD  
9452  O  OE1 . GLU D 71  ? 0.9025 0.6480 0.8921 0.1796  0.0371  0.0225  71   GLU D OE1 
9453  O  OE2 . GLU D 71  ? 0.8617 0.5415 0.8410 0.1707  0.0477  0.0276  71   GLU D OE2 
9454  N  N   . GLY D 72  ? 0.6223 0.4388 0.5834 0.1925  0.0083  0.0849  72   GLY D N   
9455  C  CA  . GLY D 72  ? 0.4907 0.3354 0.4517 0.2035  -0.0010 0.0924  72   GLY D CA  
9456  C  C   . GLY D 72  ? 0.6118 0.4973 0.5865 0.2023  -0.0061 0.0827  72   GLY D C   
9457  O  O   . GLY D 72  ? 0.6374 0.5504 0.6134 0.2078  -0.0141 0.0876  72   GLY D O   
9458  N  N   . ARG D 73  ? 0.6677 0.5580 0.6520 0.1942  -0.0017 0.0691  73   ARG D N   
9459  C  CA  . ARG D 73  ? 0.5370 0.4642 0.5334 0.1920  -0.0050 0.0602  73   ARG D CA  
9460  C  C   . ARG D 73  ? 0.5785 0.5293 0.5725 0.1780  -0.0099 0.0620  73   ARG D C   
9461  O  O   . ARG D 73  ? 0.6195 0.5590 0.6067 0.1642  -0.0076 0.0623  73   ARG D O   
9462  C  CB  . ARG D 73  ? 0.5186 0.4424 0.5222 0.1862  0.0013  0.0460  73   ARG D CB  
9463  C  CG  . ARG D 73  ? 0.5284 0.4281 0.5346 0.1990  0.0069  0.0412  73   ARG D CG  
9464  C  CD  . ARG D 73  ? 0.5011 0.4021 0.5135 0.1929  0.0126  0.0251  73   ARG D CD  
9465  N  NE  . ARG D 73  ? 0.4801 0.3436 0.4897 0.1966  0.0196  0.0199  73   ARG D NE  
9466  C  CZ  . ARG D 73  ? 0.4744 0.3269 0.4887 0.2127  0.0231  0.0145  73   ARG D CZ  
9467  N  NH1 . ARG D 73  ? 0.4486 0.2629 0.4594 0.2139  0.0299  0.0093  73   ARG D NH1 
9468  N  NH2 . ARG D 73  ? 0.5940 0.4740 0.6178 0.2275  0.0204  0.0136  73   ARG D NH2 
9469  N  N   . ASN D 74  ? 0.5921 0.5759 0.5928 0.1815  -0.0164 0.0627  74   ASN D N   
9470  C  CA  . ASN D 74  ? 0.4830 0.4874 0.4813 0.1686  -0.0212 0.0641  74   ASN D CA  
9471  C  C   . ASN D 74  ? 0.4694 0.4804 0.4719 0.1536  -0.0179 0.0554  74   ASN D C   
9472  O  O   . ASN D 74  ? 0.5810 0.6039 0.5931 0.1544  -0.0154 0.0475  74   ASN D O   
9473  C  CB  . ASN D 74  ? 0.4091 0.4483 0.4151 0.1748  -0.0290 0.0661  74   ASN D CB  
9474  C  CG  . ASN D 74  ? 0.6440 0.6816 0.6417 0.1854  -0.0354 0.0772  74   ASN D CG  
9475  O  OD1 . ASN D 74  ? 0.7284 0.7447 0.7110 0.1814  -0.0352 0.0841  74   ASN D OD1 
9476  N  ND2 . ASN D 74  ? 0.8012 0.8633 0.8087 0.1993  -0.0412 0.0792  74   ASN D ND2 
9477  N  N   . LEU D 75  ? 0.5297 0.5333 0.5246 0.1404  -0.0177 0.0572  75   LEU D N   
9478  C  CA  . LEU D 75  ? 0.4269 0.4398 0.4255 0.1266  -0.0164 0.0512  75   LEU D CA  
9479  C  C   . LEU D 75  ? 0.3513 0.3908 0.3525 0.1208  -0.0221 0.0523  75   LEU D C   
9480  O  O   . LEU D 75  ? 0.4590 0.4981 0.4526 0.1174  -0.0258 0.0570  75   LEU D O   
9481  C  CB  . LEU D 75  ? 0.5180 0.5092 0.5092 0.1166  -0.0128 0.0521  75   LEU D CB  
9482  C  CG  . LEU D 75  ? 0.4312 0.3995 0.4225 0.1162  -0.0065 0.0484  75   LEU D CG  
9483  C  CD1 . LEU D 75  ? 0.6130 0.5731 0.6070 0.1289  -0.0045 0.0468  75   LEU D CD1 
9484  C  CD2 . LEU D 75  ? 0.4995 0.4457 0.4822 0.1112  -0.0032 0.0533  75   LEU D CD2 
9485  N  N   . LEU D 76  ? 0.4775 0.5400 0.4886 0.1189  -0.0225 0.0474  76   LEU D N   
9486  C  CA  . LEU D 76  ? 0.3924 0.4824 0.4084 0.1135  -0.0275 0.0479  76   LEU D CA  
9487  C  C   . LEU D 76  ? 0.3619 0.4603 0.3807 0.0994  -0.0258 0.0446  76   LEU D C   
9488  O  O   . LEU D 76  ? 0.5516 0.6460 0.5723 0.0974  -0.0213 0.0407  76   LEU D O   
9489  C  CB  . LEU D 76  ? 0.4094 0.5248 0.4369 0.1246  -0.0292 0.0464  76   LEU D CB  
9490  C  CG  . LEU D 76  ? 0.5785 0.6931 0.6061 0.1411  -0.0327 0.0511  76   LEU D CG  
9491  C  CD1 . LEU D 76  ? 0.5021 0.6421 0.5445 0.1533  -0.0324 0.0475  76   LEU D CD1 
9492  C  CD2 . LEU D 76  ? 0.6211 0.7434 0.6422 0.1390  -0.0406 0.0574  76   LEU D CD2 
9493  N  N   . ALA D 77  ? 0.4946 0.6047 0.5128 0.0895  -0.0296 0.0461  77   ALA D N   
9494  C  CA  . ALA D 77  ? 0.3786 0.4960 0.3992 0.0761  -0.0282 0.0445  77   ALA D CA  
9495  C  C   . ALA D 77  ? 0.3289 0.4750 0.3572 0.0701  -0.0317 0.0442  77   ALA D C   
9496  O  O   . ALA D 77  ? 0.4705 0.6233 0.4973 0.0692  -0.0370 0.0455  77   ALA D O   
9497  C  CB  . ALA D 77  ? 0.3613 0.4571 0.3730 0.0668  -0.0279 0.0462  77   ALA D CB  
9498  N  N   . LEU D 78  ? 0.3624 0.5267 0.3984 0.0652  -0.0288 0.0424  78   LEU D N   
9499  C  CA  . LEU D 78  ? 0.2013 0.3942 0.2461 0.0568  -0.0309 0.0420  78   LEU D CA  
9500  C  C   . LEU D 78  ? 0.3171 0.5019 0.3574 0.0395  -0.0306 0.0437  78   LEU D C   
9501  O  O   . LEU D 78  ? 0.3214 0.4952 0.3582 0.0341  -0.0263 0.0451  78   LEU D O   
9502  C  CB  . LEU D 78  ? 0.1708 0.3904 0.2269 0.0603  -0.0267 0.0392  78   LEU D CB  
9503  C  CG  . LEU D 78  ? 0.3567 0.6121 0.4254 0.0521  -0.0279 0.0384  78   LEU D CG  
9504  C  CD1 . LEU D 78  ? 0.1775 0.4533 0.2545 0.0603  -0.0348 0.0378  78   LEU D CD1 
9505  C  CD2 . LEU D 78  ? 0.2615 0.5400 0.3389 0.0532  -0.0210 0.0357  78   LEU D CD2 
9506  N  N   . GLN D 79  ? 0.1856 0.3749 0.2253 0.0313  -0.0354 0.0436  79   GLN D N   
9507  C  CA  . GLN D 79  ? 0.2179 0.3989 0.2543 0.0145  -0.0350 0.0445  79   GLN D CA  
9508  C  C   . GLN D 79  ? 0.3797 0.5899 0.4272 0.0031  -0.0340 0.0441  79   GLN D C   
9509  O  O   . GLN D 79  ? 0.4212 0.6615 0.4795 0.0060  -0.0368 0.0417  79   GLN D O   
9510  C  CB  . GLN D 79  ? 0.2793 0.4485 0.3081 0.0101  -0.0402 0.0426  79   GLN D CB  
9511  C  CG  . GLN D 79  ? 0.2820 0.4500 0.3105 -0.0081 -0.0408 0.0413  79   GLN D CG  
9512  C  CD  . GLN D 79  ? 0.4443 0.6019 0.4640 -0.0124 -0.0459 0.0372  79   GLN D CD  
9513  O  OE1 . GLN D 79  ? 0.3843 0.5471 0.4003 -0.0025 -0.0505 0.0360  79   GLN D OE1 
9514  N  NE2 . GLN D 79  ? 0.4396 0.5815 0.4548 -0.0272 -0.0450 0.0351  79   GLN D NE2 
9515  N  N   . ILE D 80  ? 0.5079 0.7099 0.5533 -0.0096 -0.0297 0.0470  80   ILE D N   
9516  C  CA  . ILE D 80  ? 0.3686 0.5945 0.4229 -0.0240 -0.0273 0.0479  80   ILE D CA  
9517  C  C   . ILE D 80  ? 0.4185 0.6231 0.4664 -0.0412 -0.0272 0.0499  80   ILE D C   
9518  O  O   . ILE D 80  ? 0.5669 0.7413 0.6047 -0.0421 -0.0247 0.0539  80   ILE D O   
9519  C  CB  . ILE D 80  ? 0.2777 0.5138 0.3341 -0.0235 -0.0201 0.0513  80   ILE D CB  
9520  C  CG1 . ILE D 80  ? 0.2212 0.4761 0.2838 -0.0062 -0.0189 0.0478  80   ILE D CG1 
9521  C  CG2 . ILE D 80  ? 0.2056 0.4645 0.2698 -0.0407 -0.0163 0.0534  80   ILE D CG2 
9522  C  CD1 . ILE D 80  ? 0.1746 0.4307 0.2337 -0.0034 -0.0120 0.0496  80   ILE D CD1 
9523  N  N   . SER D 81  ? 0.4282 0.6485 0.4827 -0.0548 -0.0298 0.0468  81   SER D N   
9524  C  CA  . SER D 81  ? 0.4601 0.6569 0.5081 -0.0713 -0.0299 0.0469  81   SER D CA  
9525  C  C   . SER D 81  ? 0.4410 0.6624 0.4996 -0.0904 -0.0297 0.0449  81   SER D C   
9526  O  O   . SER D 81  ? 0.5144 0.7745 0.5866 -0.0894 -0.0309 0.0425  81   SER D O   
9527  C  CB  . SER D 81  ? 0.4432 0.6191 0.4821 -0.0672 -0.0356 0.0414  81   SER D CB  
9528  O  OG  . SER D 81  ? 0.6048 0.8088 0.6504 -0.0648 -0.0422 0.0354  81   SER D OG  
9529  N  N   . ARG D 82  ? 0.4904 0.6891 0.5439 -0.1078 -0.0280 0.0458  82   ARG D N   
9530  C  CA  . ARG D 82  ? 0.5545 0.7719 0.6174 -0.1293 -0.0281 0.0426  82   ARG D CA  
9531  C  C   . ARG D 82  ? 0.6042 0.8473 0.6741 -0.1285 -0.0369 0.0325  82   ARG D C   
9532  O  O   . ARG D 82  ? 0.6250 0.9075 0.7100 -0.1371 -0.0389 0.0291  82   ARG D O   
9533  C  CB  . ARG D 82  ? 0.5383 0.7171 0.5917 -0.1465 -0.0252 0.0441  82   ARG D CB  
9534  C  CG  . ARG D 82  ? 0.6232 0.8150 0.6851 -0.1718 -0.0247 0.0401  82   ARG D CG  
9535  C  CD  . ARG D 82  ? 0.7661 0.9369 0.8250 -0.1882 -0.0160 0.0498  82   ARG D CD  
9536  N  NE  . ARG D 82  ? 0.8655 0.9982 0.9164 -0.2048 -0.0155 0.0468  82   ARG D NE  
9537  C  CZ  . ARG D 82  ? 0.9794 1.0950 1.0296 -0.2255 -0.0090 0.0527  82   ARG D CZ  
9538  N  NH1 . ARG D 82  ? 0.9172 0.9944 0.9597 -0.2385 -0.0088 0.0482  82   ARG D NH1 
9539  N  NH2 . ARG D 82  ? 1.0309 1.1658 1.0873 -0.2336 -0.0021 0.0630  82   ARG D NH2 
9540  N  N   . ASN D 83  ? 0.3730 0.5955 0.4315 -0.1176 -0.0422 0.0281  83   ASN D N   
9541  C  CA  . ASN D 83  ? 0.3976 0.6411 0.4583 -0.1150 -0.0514 0.0197  83   ASN D CA  
9542  C  C   . ASN D 83  ? 0.4366 0.6649 0.4857 -0.0935 -0.0548 0.0198  83   ASN D C   
9543  O  O   . ASN D 83  ? 0.4706 0.6639 0.5049 -0.0920 -0.0545 0.0179  83   ASN D O   
9544  C  CB  . ASN D 83  ? 0.6409 0.8720 0.6965 -0.1351 -0.0548 0.0112  83   ASN D CB  
9545  C  CG  . ASN D 83  ? 0.7925 1.0370 0.8435 -0.1307 -0.0650 0.0023  83   ASN D CG  
9546  O  OD1 . ASN D 83  ? 0.7991 1.0771 0.8577 -0.1178 -0.0709 0.0027  83   ASN D OD1 
9547  N  ND2 . ASN D 83  ? 0.8142 1.0320 0.8518 -0.1410 -0.0670 -0.0057 83   ASN D ND2 
9548  N  N   . THR D 84  ? 0.4999 0.7546 0.5563 -0.0767 -0.0575 0.0219  84   THR D N   
9549  C  CA  . THR D 84  ? 0.3566 0.5968 0.4029 -0.0561 -0.0595 0.0238  84   THR D CA  
9550  C  C   . THR D 84  ? 0.3195 0.5475 0.3522 -0.0555 -0.0662 0.0182  84   THR D C   
9551  O  O   . THR D 84  ? 0.4015 0.6074 0.4218 -0.0422 -0.0659 0.0200  84   THR D O   
9552  C  CB  . THR D 84  ? 0.3928 0.6638 0.4505 -0.0387 -0.0611 0.0268  84   THR D CB  
9553  O  OG1 . THR D 84  ? 0.5094 0.7595 0.5618 -0.0239 -0.0554 0.0320  84   THR D OG1 
9554  C  CG2 . THR D 84  ? 0.2260 0.5154 0.2825 -0.0287 -0.0709 0.0242  84   THR D CG2 
9555  N  N   . ARG D 85  ? 0.3849 0.6278 0.4192 -0.0709 -0.0720 0.0110  85   ARG D N   
9556  C  CA  . ARG D 85  ? 0.4506 0.6864 0.4705 -0.0714 -0.0791 0.0044  85   ARG D CA  
9557  C  C   . ARG D 85  ? 0.5066 0.6961 0.5082 -0.0714 -0.0736 0.0030  85   ARG D C   
9558  O  O   . ARG D 85  ? 0.6221 0.7981 0.6100 -0.0594 -0.0750 0.0031  85   ARG D O   
9559  C  CB  . ARG D 85  ? 0.6143 0.8731 0.6388 -0.0913 -0.0860 -0.0050 85   ARG D CB  
9560  C  CG  . ARG D 85  ? 0.7849 1.0961 0.8282 -0.0902 -0.0937 -0.0050 85   ARG D CG  
9561  C  CD  . ARG D 85  ? 1.0720 1.4059 1.1142 -0.1053 -0.1040 -0.0155 85   ARG D CD  
9562  N  NE  . ARG D 85  ? 1.1748 1.5110 1.2012 -0.0930 -0.1131 -0.0173 85   ARG D NE  
9563  C  CZ  . ARG D 85  ? 1.1513 1.4558 1.1548 -0.0960 -0.1135 -0.0230 85   ARG D CZ  
9564  N  NH1 . ARG D 85  ? 1.0647 1.3754 1.0531 -0.0847 -0.1216 -0.0234 85   ARG D NH1 
9565  N  NH2 . ARG D 85  ? 1.1400 1.4065 1.1351 -0.1096 -0.1054 -0.0281 85   ARG D NH2 
9566  N  N   . SER D 86  ? 0.5324 0.6976 0.5342 -0.0843 -0.0668 0.0023  86   SER D N   
9567  C  CA  . SER D 86  ? 0.4230 0.5453 0.4102 -0.0832 -0.0612 0.0008  86   SER D CA  
9568  C  C   . SER D 86  ? 0.6514 0.7535 0.6434 -0.0809 -0.0527 0.0090  86   SER D C   
9569  O  O   . SER D 86  ? 0.8091 0.9282 0.8115 -0.0741 -0.0511 0.0165  86   SER D O   
9570  C  CB  . SER D 86  ? 0.5258 0.6324 0.5055 -0.1020 -0.0620 -0.0099 86   SER D CB  
9571  O  OG  . SER D 86  ? 0.6790 0.8032 0.6509 -0.1045 -0.0705 -0.0188 86   SER D OG  
9572  N  N   . ARG D 87  ? 0.6703 0.7361 0.6540 -0.0860 -0.0475 0.0073  87   ARG D N   
9573  C  CA  . ARG D 87  ? 0.6062 0.6507 0.5934 -0.0864 -0.0404 0.0153  87   ARG D CA  
9574  C  C   . ARG D 87  ? 0.5287 0.5465 0.5123 -0.1031 -0.0374 0.0110  87   ARG D C   
9575  O  O   . ARG D 87  ? 0.4421 0.4362 0.4152 -0.1047 -0.0369 0.0029  87   ARG D O   
9576  C  CB  . ARG D 87  ? 0.2172 0.2389 0.1981 -0.0695 -0.0364 0.0197  87   ARG D CB  
9577  C  CG  . ARG D 87  ? 0.2451 0.2627 0.2324 -0.0644 -0.0319 0.0302  87   ARG D CG  
9578  C  CD  . ARG D 87  ? 0.4044 0.3979 0.3867 -0.0507 -0.0282 0.0333  87   ARG D CD  
9579  N  NE  . ARG D 87  ? 0.6335 0.5944 0.6116 -0.0561 -0.0243 0.0328  87   ARG D NE  
9580  C  CZ  . ARG D 87  ? 0.6484 0.5869 0.6185 -0.0546 -0.0228 0.0253  87   ARG D CZ  
9581  N  NH1 . ARG D 87  ? 0.7262 0.6717 0.6897 -0.0488 -0.0248 0.0183  87   ARG D NH1 
9582  N  NH2 . ARG D 87  ? 0.6370 0.5453 0.6050 -0.0584 -0.0187 0.0252  87   ARG D NH2 
9583  N  N   . ASN D 88  ? 0.6582 0.6788 0.6500 -0.1159 -0.0346 0.0163  88   ASN D N   
9584  C  CA  . ASN D 88  ? 0.5802 0.5728 0.5689 -0.1331 -0.0313 0.0132  88   ASN D CA  
9585  C  C   . ASN D 88  ? 0.5200 0.4692 0.4996 -0.1247 -0.0260 0.0153  88   ASN D C   
9586  O  O   . ASN D 88  ? 0.4918 0.4350 0.4718 -0.1094 -0.0236 0.0242  88   ASN D O   
9587  C  CB  . ASN D 88  ? 0.6051 0.6084 0.6037 -0.1484 -0.0282 0.0210  88   ASN D CB  
9588  C  CG  . ASN D 88  ? 0.6897 0.7376 0.6997 -0.1593 -0.0331 0.0165  88   ASN D CG  
9589  O  OD1 . ASN D 88  ? 0.8270 0.9054 0.8472 -0.1563 -0.0325 0.0236  88   ASN D OD1 
9590  N  ND2 . ASN D 88  ? 0.7295 0.7831 0.7377 -0.1713 -0.0381 0.0038  88   ASN D ND2 
9591  N  N   . LEU D 89  ? 0.3261 0.2466 0.2982 -0.1342 -0.0246 0.0059  89   LEU D N   
9592  C  CA  . LEU D 89  ? 0.4144 0.2936 0.3794 -0.1260 -0.0192 0.0065  89   LEU D CA  
9593  C  C   . LEU D 89  ? 0.5479 0.4135 0.5180 -0.1214 -0.0148 0.0222  89   LEU D C   
9594  O  O   . LEU D 89  ? 0.5842 0.4522 0.5590 -0.1347 -0.0133 0.0295  89   LEU D O   
9595  C  CB  . LEU D 89  ? 0.4474 0.2958 0.4054 -0.1409 -0.0170 -0.0054 89   LEU D CB  
9596  C  CG  . LEU D 89  ? 0.5186 0.3268 0.4682 -0.1297 -0.0117 -0.0099 89   LEU D CG  
9597  C  CD1 . LEU D 89  ? 0.3803 0.1996 0.3225 -0.1156 -0.0136 -0.0186 89   LEU D CD1 
9598  C  CD2 . LEU D 89  ? 0.5564 0.3300 0.5002 -0.1458 -0.0084 -0.0207 89   LEU D CD2 
9599  N  N   . LEU D 90  ? 0.6250 0.4784 0.5937 -0.1029 -0.0127 0.0276  90   LEU D N   
9600  C  CA  . LEU D 90  ? 0.6150 0.4541 0.5867 -0.0957 -0.0096 0.0423  90   LEU D CA  
9601  C  C   . LEU D 90  ? 0.5326 0.4030 0.5105 -0.0933 -0.0113 0.0537  90   LEU D C   
9602  O  O   . LEU D 90  ? 0.4773 0.3404 0.4562 -0.0884 -0.0094 0.0663  90   LEU D O   
9603  C  CB  . LEU D 90  ? 0.4894 0.2925 0.4589 -0.1076 -0.0053 0.0462  90   LEU D CB  
9604  C  CG  . LEU D 90  ? 0.5884 0.3533 0.5520 -0.1023 -0.0020 0.0368  90   LEU D CG  
9605  C  CD1 . LEU D 90  ? 0.4312 0.1562 0.3921 -0.1144 0.0024  0.0391  90   LEU D CD1 
9606  C  CD2 . LEU D 90  ? 0.4155 0.1736 0.3807 -0.0796 -0.0009 0.0413  90   LEU D CD2 
9607  N  N   . THR D 91  ? 0.5439 0.4498 0.5255 -0.0957 -0.0150 0.0491  91   THR D N   
9608  C  CA  . THR D 91  ? 0.5965 0.5328 0.5839 -0.0900 -0.0160 0.0576  91   THR D CA  
9609  C  C   . THR D 91  ? 0.4943 0.4326 0.4810 -0.0699 -0.0168 0.0592  91   THR D C   
9610  O  O   . THR D 91  ? 0.3515 0.2912 0.3359 -0.0617 -0.0185 0.0509  91   THR D O   
9611  C  CB  . THR D 91  ? 0.5524 0.5281 0.5463 -0.0975 -0.0193 0.0525  91   THR D CB  
9612  O  OG1 . THR D 91  ? 0.3301 0.3088 0.3272 -0.1180 -0.0182 0.0519  91   THR D OG1 
9613  C  CG2 . THR D 91  ? 0.3259 0.3311 0.3255 -0.0881 -0.0194 0.0595  91   THR D CG2 
9614  N  N   . PRO D 92  ? 0.3845 0.3233 0.3724 -0.0629 -0.0154 0.0699  92   PRO D N   
9615  C  CA  . PRO D 92  ? 0.4460 0.3883 0.4346 -0.0459 -0.0162 0.0717  92   PRO D CA  
9616  C  C   . PRO D 92  ? 0.5335 0.5065 0.5255 -0.0398 -0.0185 0.0675  92   PRO D C   
9617  O  O   . PRO D 92  ? 0.4042 0.4008 0.3997 -0.0440 -0.0186 0.0706  92   PRO D O   
9618  C  CB  . PRO D 92  ? 0.4420 0.3818 0.4303 -0.0441 -0.0150 0.0844  92   PRO D CB  
9619  C  CG  . PRO D 92  ? 0.4046 0.3333 0.3907 -0.0597 -0.0127 0.0904  92   PRO D CG  
9620  C  CD  . PRO D 92  ? 0.4056 0.3451 0.3938 -0.0724 -0.0131 0.0810  92   PRO D CD  
9621  N  N   . PRO D 93  ? 0.5208 0.4929 0.5116 -0.0297 -0.0197 0.0608  93   PRO D N   
9622  C  CA  . PRO D 93  ? 0.4756 0.4713 0.4692 -0.0211 -0.0214 0.0588  93   PRO D CA  
9623  C  C   . PRO D 93  ? 0.4957 0.4922 0.4911 -0.0112 -0.0203 0.0645  93   PRO D C   
9624  O  O   . PRO D 93  ? 0.4339 0.4121 0.4284 -0.0064 -0.0192 0.0673  93   PRO D O   
9625  C  CB  . PRO D 93  ? 0.3443 0.3335 0.3337 -0.0153 -0.0224 0.0511  93   PRO D CB  
9626  C  CG  . PRO D 93  ? 0.3794 0.3396 0.3648 -0.0157 -0.0197 0.0497  93   PRO D CG  
9627  C  CD  . PRO D 93  ? 0.3368 0.2849 0.3235 -0.0250 -0.0184 0.0556  93   PRO D CD  
9628  N  N   . VAL D 94  ? 0.3720 0.3909 0.3706 -0.0082 -0.0208 0.0656  94   VAL D N   
9629  C  CA  . VAL D 94  ? 0.2431 0.2654 0.2425 -0.0006 -0.0202 0.0695  94   VAL D CA  
9630  C  C   . VAL D 94  ? 0.3837 0.4245 0.3858 0.0073  -0.0205 0.0648  94   VAL D C   
9631  O  O   . VAL D 94  ? 0.5082 0.5632 0.5125 0.0061  -0.0214 0.0610  94   VAL D O   
9632  C  CB  . VAL D 94  ? 0.4308 0.4601 0.4291 -0.0076 -0.0191 0.0771  94   VAL D CB  
9633  C  CG1 . VAL D 94  ? 0.7072 0.7411 0.7042 -0.0003 -0.0193 0.0806  94   VAL D CG1 
9634  C  CG2 . VAL D 94  ? 0.5073 0.5155 0.5026 -0.0159 -0.0185 0.0827  94   VAL D CG2 
9635  N  N   . LYS D 95  ? 0.2122 0.2528 0.2146 0.0154  -0.0201 0.0648  95   LYS D N   
9636  C  CA  . LYS D 95  ? 0.2842 0.3377 0.2888 0.0232  -0.0197 0.0599  95   LYS D CA  
9637  C  C   . LYS D 95  ? 0.3881 0.4498 0.3926 0.0266  -0.0188 0.0602  95   LYS D C   
9638  O  O   . LYS D 95  ? 0.3763 0.4312 0.3788 0.0255  -0.0194 0.0641  95   LYS D O   
9639  C  CB  . LYS D 95  ? 0.1848 0.2256 0.1889 0.0305  -0.0198 0.0559  95   LYS D CB  
9640  C  CG  . LYS D 95  ? 0.1779 0.2016 0.1817 0.0326  -0.0191 0.0571  95   LYS D CG  
9641  C  CD  . LYS D 95  ? 0.3233 0.3322 0.3249 0.0337  -0.0182 0.0550  95   LYS D CD  
9642  C  CE  . LYS D 95  ? 0.4284 0.4265 0.4319 0.0395  -0.0160 0.0534  95   LYS D CE  
9643  N  NZ  . LYS D 95  ? 0.5316 0.5274 0.5395 0.0396  -0.0165 0.0562  95   LYS D NZ  
9644  N  N   . TYR D 96  ? 0.3990 0.4760 0.4055 0.0314  -0.0176 0.0555  96   TYR D N   
9645  C  CA  . TYR D 96  ? 0.4388 0.5230 0.4443 0.0358  -0.0163 0.0524  96   TYR D CA  
9646  C  C   . TYR D 96  ? 0.5167 0.5977 0.5247 0.0452  -0.0152 0.0454  96   TYR D C   
9647  O  O   . TYR D 96  ? 0.4003 0.4891 0.4114 0.0494  -0.0147 0.0430  96   TYR D O   
9648  C  CB  . TYR D 96  ? 0.3240 0.4305 0.3288 0.0323  -0.0140 0.0527  96   TYR D CB  
9649  C  CG  . TYR D 96  ? 0.3119 0.4211 0.3111 0.0238  -0.0141 0.0602  96   TYR D CG  
9650  C  CD1 . TYR D 96  ? 0.3713 0.4650 0.3666 0.0227  -0.0168 0.0652  96   TYR D CD1 
9651  C  CD2 . TYR D 96  ? 0.3654 0.4935 0.3632 0.0172  -0.0112 0.0630  96   TYR D CD2 
9652  C  CE1 . TYR D 96  ? 0.2512 0.3458 0.2405 0.0162  -0.0174 0.0738  96   TYR D CE1 
9653  C  CE2 . TYR D 96  ? 0.5176 0.6463 0.5084 0.0091  -0.0109 0.0716  96   TYR D CE2 
9654  C  CZ  . TYR D 96  ? 0.4832 0.5939 0.4691 0.0092  -0.0144 0.0775  96   TYR D CZ  
9655  O  OH  . TYR D 96  ? 0.6362 0.7458 0.6140 0.0024  -0.0147 0.0879  96   TYR D OH  
9656  N  N   . ILE D 97  ? 0.4140 0.4835 0.4212 0.0486  -0.0151 0.0426  97   ILE D N   
9657  C  CA  . ILE D 97  ? 0.3167 0.3802 0.3255 0.0564  -0.0133 0.0363  97   ILE D CA  
9658  C  C   . ILE D 97  ? 0.3177 0.3878 0.3253 0.0582  -0.0117 0.0299  97   ILE D C   
9659  O  O   . ILE D 97  ? 0.3144 0.3897 0.3191 0.0532  -0.0131 0.0310  97   ILE D O   
9660  C  CB  . ILE D 97  ? 0.3525 0.3960 0.3619 0.0579  -0.0132 0.0365  97   ILE D CB  
9661  C  CG1 . ILE D 97  ? 0.3682 0.4043 0.3766 0.0562  -0.0143 0.0414  97   ILE D CG1 
9662  C  CG2 . ILE D 97  ? 0.3010 0.3360 0.3110 0.0651  -0.0106 0.0311  97   ILE D CG2 
9663  C  CD1 . ILE D 97  ? 0.3497 0.3831 0.3576 0.0494  -0.0160 0.0463  97   ILE D CD1 
9664  N  N   . ALA D 98  ? 0.3299 0.3995 0.3390 0.0655  -0.0090 0.0232  98   ALA D N   
9665  C  CA  . ALA D 98  ? 0.3274 0.4003 0.3344 0.0672  -0.0069 0.0145  98   ALA D CA  
9666  C  C   . ALA D 98  ? 0.4704 0.5269 0.4792 0.0744  -0.0041 0.0074  98   ALA D C   
9667  O  O   . ALA D 98  ? 0.5220 0.5656 0.5330 0.0792  -0.0037 0.0106  98   ALA D O   
9668  C  CB  . ALA D 98  ? 0.2639 0.3593 0.2695 0.0680  -0.0046 0.0117  98   ALA D CB  
9669  N  N   . ASN D 99  ? 0.4822 0.5383 0.4888 0.0746  -0.0021 -0.0021 99   ASN D N   
9670  C  CA  . ASN D 99  ? 0.3198 0.3592 0.3275 0.0812  0.0017  -0.0105 99   ASN D CA  
9671  C  C   . ASN D 99  ? 0.5513 0.5663 0.5612 0.0806  0.0018  -0.0072 99   ASN D C   
9672  O  O   . ASN D 99  ? 0.5545 0.5526 0.5653 0.0877  0.0049  -0.0088 99   ASN D O   
9673  C  CB  . ASN D 99  ? 0.3429 0.3885 0.3533 0.0923  0.0049  -0.0124 99   ASN D CB  
9674  C  CG  . ASN D 99  ? 0.4847 0.5145 0.4953 0.1005  0.0097  -0.0231 99   ASN D CG  
9675  O  OD1 . ASN D 99  ? 0.4383 0.4591 0.4524 0.1113  0.0116  -0.0218 99   ASN D OD1 
9676  N  ND2 . ASN D 99  ? 0.3331 0.3590 0.3399 0.0956  0.0113  -0.0339 99   ASN D ND2 
9677  N  N   . MET D 100 ? 0.6061 0.6191 0.6168 0.0725  -0.0011 -0.0021 100  MET D N   
9678  C  CA  . MET D 100 ? 0.5428 0.5355 0.5559 0.0705  0.0002  0.0001  100  MET D CA  
9679  C  C   . MET D 100 ? 0.5476 0.5267 0.5616 0.0682  0.0033  -0.0101 100  MET D C   
9680  O  O   . MET D 100 ? 0.5483 0.5064 0.5634 0.0690  0.0069  -0.0099 100  MET D O   
9681  C  CB  . MET D 100 ? 0.4907 0.4866 0.5063 0.0633  -0.0027 0.0069  100  MET D CB  
9682  C  CG  . MET D 100 ? 0.5969 0.5994 0.6156 0.0559  -0.0051 0.0023  100  MET D CG  
9683  S  SD  . MET D 100 ? 0.4808 0.4861 0.5050 0.0509  -0.0079 0.0109  100  MET D SD  
9684  C  CE  . MET D 100 ? 0.2710 0.2555 0.2961 0.0530  -0.0026 0.0151  100  MET D CE  
9685  N  N   . HIS D 101 ? 0.4994 0.4904 0.5120 0.0644  0.0020  -0.0191 101  HIS D N   
9686  C  CA  . HIS D 101 ? 0.3954 0.3749 0.4075 0.0632  0.0052  -0.0319 101  HIS D CA  
9687  C  C   . HIS D 101 ? 0.4600 0.4406 0.4682 0.0730  0.0086  -0.0383 101  HIS D C   
9688  O  O   . HIS D 101 ? 0.3374 0.3391 0.3421 0.0743  0.0074  -0.0408 101  HIS D O   
9689  C  CB  . HIS D 101 ? 0.2603 0.2526 0.2721 0.0532  0.0015  -0.0399 101  HIS D CB  
9690  C  CG  . HIS D 101 ? 0.4945 0.4889 0.5131 0.0450  -0.0020 -0.0342 101  HIS D CG  
9691  N  ND1 . HIS D 101 ? 0.5012 0.5154 0.5206 0.0419  -0.0078 -0.0270 101  HIS D ND1 
9692  C  CD2 . HIS D 101 ? 0.6501 0.6295 0.6756 0.0396  0.0003  -0.0344 101  HIS D CD2 
9693  C  CE1 . HIS D 101 ? 0.5593 0.5717 0.5870 0.0364  -0.0093 -0.0237 101  HIS D CE1 
9694  N  NE2 . HIS D 101 ? 0.6584 0.6512 0.6901 0.0342  -0.0042 -0.0283 101  HIS D NE2 
9695  N  N   . GLY D 102 ? 0.4571 0.4149 0.4662 0.0804  0.0134  -0.0399 102  GLY D N   
9696  C  CA  . GLY D 102 ? 0.4155 0.3732 0.4236 0.0932  0.0168  -0.0432 102  GLY D CA  
9697  C  C   . GLY D 102 ? 0.3953 0.3646 0.4000 0.0939  0.0190  -0.0577 102  GLY D C   
9698  O  O   . GLY D 102 ? 0.5973 0.5793 0.6019 0.1035  0.0213  -0.0602 102  GLY D O   
9699  N  N   . ASP D 103 ? 0.5552 0.5222 0.5571 0.0835  0.0184  -0.0679 103  ASP D N   
9700  C  CA  . ASP D 103 ? 0.5538 0.5320 0.5498 0.0826  0.0203  -0.0834 103  ASP D CA  
9701  C  C   . ASP D 103 ? 0.4168 0.4285 0.4074 0.0768  0.0158  -0.0814 103  ASP D C   
9702  O  O   . ASP D 103 ? 0.5825 0.6070 0.5657 0.0748  0.0170  -0.0935 103  ASP D O   
9703  C  CB  . ASP D 103 ? 0.5774 0.5370 0.5717 0.0737  0.0217  -0.0976 103  ASP D CB  
9704  C  CG  . ASP D 103 ? 0.6021 0.5613 0.6002 0.0603  0.0164  -0.0920 103  ASP D CG  
9705  O  OD1 . ASP D 103 ? 0.8172 0.7597 0.8171 0.0519  0.0176  -0.1015 103  ASP D OD1 
9706  O  OD2 . ASP D 103 ? 0.6224 0.5980 0.6228 0.0580  0.0113  -0.0786 103  ASP D OD2 
9707  N  N   . GLU D 104 ? 0.4112 0.4353 0.4043 0.0738  0.0109  -0.0662 104  GLU D N   
9708  C  CA  . GLU D 104 ? 0.2521 0.3041 0.2397 0.0684  0.0067  -0.0614 104  GLU D CA  
9709  C  C   . GLU D 104 ? 0.4300 0.4956 0.4196 0.0757  0.0084  -0.0521 104  GLU D C   
9710  O  O   . GLU D 104 ? 0.5293 0.5932 0.5239 0.0757  0.0058  -0.0392 104  GLU D O   
9711  C  CB  . GLU D 104 ? 0.3813 0.4354 0.3713 0.0593  -0.0001 -0.0513 104  GLU D CB  
9712  C  CG  . GLU D 104 ? 0.5159 0.5580 0.5083 0.0514  -0.0022 -0.0590 104  GLU D CG  
9713  C  CD  . GLU D 104 ? 0.6660 0.7124 0.6639 0.0447  -0.0083 -0.0482 104  GLU D CD  
9714  O  OE1 . GLU D 104 ? 0.6746 0.7322 0.6721 0.0459  -0.0111 -0.0357 104  GLU D OE1 
9715  O  OE2 . GLU D 104 ? 0.8672 0.9058 0.8707 0.0382  -0.0100 -0.0523 104  GLU D OE2 
9716  N  N   . THR D 105 ? 0.4623 0.5427 0.4482 0.0811  0.0131  -0.0598 105  THR D N   
9717  C  CA  . THR D 105 ? 0.5672 0.6579 0.5590 0.0908  0.0167  -0.0550 105  THR D CA  
9718  C  C   . THR D 105 ? 0.4310 0.5521 0.4202 0.0874  0.0168  -0.0484 105  THR D C   
9719  O  O   . THR D 105 ? 0.2069 0.3390 0.2032 0.0925  0.0181  -0.0418 105  THR D O   
9720  C  CB  . THR D 105 ? 0.4961 0.5809 0.4900 0.1028  0.0239  -0.0685 105  THR D CB  
9721  O  OG1 . THR D 105 ? 0.4037 0.5036 0.3884 0.1001  0.0275  -0.0816 105  THR D OG1 
9722  C  CG2 . THR D 105 ? 0.6204 0.6715 0.6170 0.1064  0.0249  -0.0738 105  THR D CG2 
9723  N  N   . VAL D 106 ? 0.3757 0.5113 0.3546 0.0785  0.0153  -0.0499 106  VAL D N   
9724  C  CA  . VAL D 106 ? 0.4552 0.6175 0.4301 0.0740  0.0163  -0.0424 106  VAL D CA  
9725  C  C   . VAL D 106 ? 0.3051 0.4675 0.2873 0.0710  0.0124  -0.0261 106  VAL D C   
9726  O  O   . VAL D 106 ? 0.3448 0.5214 0.3334 0.0739  0.0153  -0.0220 106  VAL D O   
9727  C  CB  . VAL D 106 ? 0.5379 0.7132 0.4980 0.0641  0.0140  -0.0435 106  VAL D CB  
9728  C  CG1 . VAL D 106 ? 0.5155 0.7161 0.4700 0.0586  0.0158  -0.0338 106  VAL D CG1 
9729  C  CG2 . VAL D 106 ? 0.4448 0.6217 0.3966 0.0667  0.0183  -0.0618 106  VAL D CG2 
9730  N  N   . GLY D 107 ? 0.5196 0.6671 0.5016 0.0652  0.0060  -0.0179 107  GLY D N   
9731  C  CA  . GLY D 107 ? 0.4156 0.5606 0.4030 0.0619  0.0026  -0.0042 107  GLY D CA  
9732  C  C   . GLY D 107 ? 0.3542 0.4995 0.3519 0.0695  0.0049  -0.0032 107  GLY D C   
9733  O  O   . GLY D 107 ? 0.4590 0.6154 0.4603 0.0663  0.0044  0.0051  107  GLY D O   
9734  N  N   . ARG D 108 ? 0.4237 0.5566 0.4259 0.0794  0.0073  -0.0116 108  ARG D N   
9735  C  CA  . ARG D 108 ? 0.3840 0.5169 0.3957 0.0893  0.0088  -0.0107 108  ARG D CA  
9736  C  C   . ARG D 108 ? 0.3516 0.5137 0.3685 0.0913  0.0122  -0.0104 108  ARG D C   
9737  O  O   . ARG D 108 ? 0.3560 0.5272 0.3797 0.0907  0.0100  -0.0028 108  ARG D O   
9738  C  CB  . ARG D 108 ? 0.4060 0.5210 0.4199 0.1008  0.0119  -0.0205 108  ARG D CB  
9739  C  CG  . ARG D 108 ? 0.4075 0.5308 0.4310 0.1143  0.0147  -0.0218 108  ARG D CG  
9740  C  CD  . ARG D 108 ? 0.5043 0.6089 0.5294 0.1272  0.0190  -0.0321 108  ARG D CD  
9741  N  NE  . ARG D 108 ? 0.5616 0.6376 0.5874 0.1312  0.0163  -0.0265 108  ARG D NE  
9742  C  CZ  . ARG D 108 ? 0.4362 0.5049 0.4680 0.1437  0.0157  -0.0222 108  ARG D CZ  
9743  N  NH1 . ARG D 108 ? 0.3734 0.4623 0.4138 0.1554  0.0174  -0.0236 108  ARG D NH1 
9744  N  NH2 . ARG D 108 ? 0.4077 0.4493 0.4367 0.1447  0.0135  -0.0160 108  ARG D NH2 
9745  N  N   . GLN D 109 ? 0.5107 0.6887 0.5244 0.0930  0.0178  -0.0195 109  GLN D N   
9746  C  CA  . GLN D 109 ? 0.4905 0.7000 0.5097 0.0946  0.0229  -0.0207 109  GLN D CA  
9747  C  C   . GLN D 109 ? 0.3214 0.5489 0.3374 0.0806  0.0217  -0.0103 109  GLN D C   
9748  O  O   . GLN D 109 ? 0.3532 0.6034 0.3778 0.0792  0.0236  -0.0064 109  GLN D O   
9749  C  CB  . GLN D 109 ? 0.5134 0.7341 0.5282 0.1001  0.0305  -0.0346 109  GLN D CB  
9750  C  CG  . GLN D 109 ? 0.5497 0.7631 0.5734 0.1169  0.0344  -0.0451 109  GLN D CG  
9751  C  CD  . GLN D 109 ? 0.6133 0.8435 0.6530 0.1258  0.0344  -0.0400 109  GLN D CD  
9752  O  OE1 . GLN D 109 ? 0.7454 0.9590 0.7923 0.1358  0.0310  -0.0375 109  GLN D OE1 
9753  N  NE2 . GLN D 109 ? 0.5317 0.7965 0.5769 0.1216  0.0381  -0.0380 109  GLN D NE2 
9754  N  N   . LEU D 110 ? 0.2883 0.5060 0.2924 0.0703  0.0185  -0.0055 110  LEU D N   
9755  C  CA  . LEU D 110 ? 0.3728 0.6007 0.3725 0.0571  0.0170  0.0062  110  LEU D CA  
9756  C  C   . LEU D 110 ? 0.3857 0.6102 0.3949 0.0538  0.0130  0.0158  110  LEU D C   
9757  O  O   . LEU D 110 ? 0.3390 0.5801 0.3506 0.0451  0.0144  0.0226  110  LEU D O   
9758  C  CB  . LEU D 110 ? 0.3912 0.6046 0.3779 0.0493  0.0125  0.0110  110  LEU D CB  
9759  C  CG  . LEU D 110 ? 0.4641 0.6875 0.4376 0.0480  0.0155  0.0038  110  LEU D CG  
9760  C  CD1 . LEU D 110 ? 0.5050 0.7183 0.4668 0.0397  0.0093  0.0118  110  LEU D CD1 
9761  C  CD2 . LEU D 110 ? 0.2747 0.5281 0.2453 0.0448  0.0232  0.0030  110  LEU D CD2 
9762  N  N   . LEU D 111 ? 0.4504 0.6533 0.4642 0.0596  0.0084  0.0159  111  LEU D N   
9763  C  CA  . LEU D 111 ? 0.2872 0.4861 0.3077 0.0565  0.0042  0.0236  111  LEU D CA  
9764  C  C   . LEU D 111 ? 0.3051 0.5270 0.3380 0.0619  0.0062  0.0211  111  LEU D C   
9765  O  O   . LEU D 111 ? 0.4805 0.7156 0.5189 0.0543  0.0049  0.0267  111  LEU D O   
9766  C  CB  . LEU D 111 ? 0.3520 0.5224 0.3717 0.0610  -0.0006 0.0245  111  LEU D CB  
9767  C  CG  . LEU D 111 ? 0.3852 0.5365 0.3961 0.0541  -0.0035 0.0287  111  LEU D CG  
9768  C  CD1 . LEU D 111 ? 0.4236 0.5510 0.4357 0.0569  -0.0072 0.0305  111  LEU D CD1 
9769  C  CD2 . LEU D 111 ? 0.3629 0.5211 0.3699 0.0418  -0.0043 0.0377  111  LEU D CD2 
9770  N  N   . VAL D 112 ? 0.4884 0.7153 0.5263 0.0753  0.0093  0.0123  112  VAL D N   
9771  C  CA  . VAL D 112 ? 0.3704 0.6234 0.4218 0.0836  0.0118  0.0088  112  VAL D CA  
9772  C  C   . VAL D 112 ? 0.4130 0.6989 0.4679 0.0734  0.0169  0.0103  112  VAL D C   
9773  O  O   . VAL D 112 ? 0.3678 0.6762 0.4340 0.0697  0.0161  0.0136  112  VAL D O   
9774  C  CB  . VAL D 112 ? 0.3265 0.5768 0.3813 0.1007  0.0160  -0.0020 112  VAL D CB  
9775  C  CG1 . VAL D 112 ? 0.1260 0.4099 0.1947 0.1091  0.0209  -0.0069 112  VAL D CG1 
9776  C  CG2 . VAL D 112 ? 0.3430 0.5656 0.3983 0.1113  0.0112  -0.0011 112  VAL D CG2 
9777  N  N   . TYR D 113 ? 0.3159 0.6053 0.3603 0.0679  0.0221  0.0080  113  TYR D N   
9778  C  CA  . TYR D 113 ? 0.3311 0.6490 0.3753 0.0565  0.0279  0.0109  113  TYR D CA  
9779  C  C   . TYR D 113 ? 0.4432 0.7594 0.4870 0.0404  0.0239  0.0230  113  TYR D C   
9780  O  O   . TYR D 113 ? 0.4047 0.7471 0.4570 0.0318  0.0271  0.0261  113  TYR D O   
9781  C  CB  . TYR D 113 ? 0.2216 0.5388 0.2499 0.0527  0.0328  0.0078  113  TYR D CB  
9782  C  CG  . TYR D 113 ? 0.4865 0.8120 0.5152 0.0664  0.0392  -0.0065 113  TYR D CG  
9783  C  CD1 . TYR D 113 ? 0.5504 0.8683 0.5632 0.0659  0.0418  -0.0127 113  TYR D CD1 
9784  C  CD2 . TYR D 113 ? 0.5291 0.8704 0.5742 0.0802  0.0424  -0.0143 113  TYR D CD2 
9785  C  CE1 . TYR D 113 ? 0.5391 0.8626 0.5514 0.0779  0.0481  -0.0278 113  TYR D CE1 
9786  C  CE2 . TYR D 113 ? 0.4789 0.8248 0.5246 0.0939  0.0489  -0.0282 113  TYR D CE2 
9787  C  CZ  . TYR D 113 ? 0.5306 0.8664 0.5594 0.0922  0.0522  -0.0356 113  TYR D CZ  
9788  O  OH  . TYR D 113 ? 0.5773 0.9157 0.6059 0.1051  0.0592  -0.0513 113  TYR D OH  
9789  N  N   . MET D 114 ? 0.3680 0.6531 0.4028 0.0363  0.0174  0.0290  114  MET D N   
9790  C  CA  . MET D 114 ? 0.4132 0.6899 0.4453 0.0216  0.0140  0.0398  114  MET D CA  
9791  C  C   . MET D 114 ? 0.4371 0.7248 0.4831 0.0194  0.0110  0.0407  114  MET D C   
9792  O  O   . MET D 114 ? 0.5330 0.8348 0.5830 0.0059  0.0124  0.0460  114  MET D O   
9793  C  CB  . MET D 114 ? 0.3253 0.5667 0.3468 0.0205  0.0080  0.0445  114  MET D CB  
9794  C  CG  . MET D 114 ? 0.3028 0.5309 0.3213 0.0068  0.0049  0.0550  114  MET D CG  
9795  S  SD  . MET D 114 ? 0.4486 0.6909 0.4600 -0.0100 0.0104  0.0647  114  MET D SD  
9796  C  CE  . MET D 114 ? 0.8038 1.0375 0.7987 -0.0059 0.0112  0.0658  114  MET D CE  
9797  N  N   . ALA D 115 ? 0.2148 0.4960 0.2675 0.0319  0.0067  0.0359  115  ALA D N   
9798  C  CA  . ALA D 115 ? 0.2216 0.5156 0.2867 0.0315  0.0023  0.0362  115  ALA D CA  
9799  C  C   . ALA D 115 ? 0.2435 0.5787 0.3229 0.0265  0.0068  0.0346  115  ALA D C   
9800  O  O   . ALA D 115 ? 0.3346 0.6815 0.4191 0.0121  0.0057  0.0387  115  ALA D O   
9801  C  CB  . ALA D 115 ? 0.3865 0.6715 0.4555 0.0486  -0.0019 0.0315  115  ALA D CB  
9802  N  N   . GLN D 116 ? 0.3716 0.7288 0.4580 0.0380  0.0124  0.0277  116  GLN D N   
9803  C  CA  . GLN D 116 ? 0.2162 0.6157 0.3169 0.0341  0.0186  0.0253  116  GLN D CA  
9804  C  C   . GLN D 116 ? 0.3181 0.7249 0.4127 0.0130  0.0237  0.0321  116  GLN D C   
9805  O  O   . GLN D 116 ? 0.4238 0.8493 0.5280 -0.0006 0.0233  0.0357  116  GLN D O   
9806  C  CB  . GLN D 116 ? 0.1255 0.5417 0.2303 0.0497  0.0260  0.0161  116  GLN D CB  
9807  C  CG  . GLN D 116 ? 0.2733 0.6780 0.3834 0.0715  0.0219  0.0100  116  GLN D CG  
9808  C  CD  . GLN D 116 ? 0.3554 0.7652 0.4652 0.0867  0.0298  -0.0002 116  GLN D CD  
9809  O  OE1 . GLN D 116 ? 0.3801 0.8225 0.5053 0.0961  0.0351  -0.0065 116  GLN D OE1 
9810  N  NE2 . GLN D 116 ? 0.3542 0.7326 0.4472 0.0892  0.0307  -0.0028 116  GLN D NE2 
9811  N  N   . TYR D 117 ? 0.2971 0.6888 0.3751 0.0099  0.0284  0.0343  117  TYR D N   
9812  C  CA  . TYR D 117 ? 0.2590 0.6546 0.3277 -0.0089 0.0337  0.0427  117  TYR D CA  
9813  C  C   . TYR D 117 ? 0.3680 0.7553 0.4391 -0.0263 0.0294  0.0514  117  TYR D C   
9814  O  O   . TYR D 117 ? 0.4433 0.8548 0.5222 -0.0411 0.0342  0.0548  117  TYR D O   
9815  C  CB  . TYR D 117 ? 0.1986 0.5667 0.2457 -0.0089 0.0342  0.0463  117  TYR D CB  
9816  C  CG  . TYR D 117 ? 0.3894 0.7614 0.4243 -0.0260 0.0399  0.0564  117  TYR D CG  
9817  C  CD1 . TYR D 117 ? 0.4563 0.8599 0.4898 -0.0296 0.0503  0.0546  117  TYR D CD1 
9818  C  CD2 . TYR D 117 ? 0.3665 0.7100 0.3906 -0.0381 0.0355  0.0681  117  TYR D CD2 
9819  C  CE1 . TYR D 117 ? 0.4334 0.8398 0.4533 -0.0460 0.0560  0.0657  117  TYR D CE1 
9820  C  CE2 . TYR D 117 ? 0.3869 0.7310 0.3985 -0.0532 0.0406  0.0793  117  TYR D CE2 
9821  C  CZ  . TYR D 117 ? 0.4443 0.8196 0.4531 -0.0576 0.0507  0.0788  117  TYR D CZ  
9822  O  OH  . TYR D 117 ? 0.3880 0.7623 0.3824 -0.0731 0.0559  0.0917  117  TYR D OH  
9823  N  N   . LEU D 118 ? 0.4702 0.8232 0.5349 -0.0251 0.0211  0.0541  118  LEU D N   
9824  C  CA  . LEU D 118 ? 0.4830 0.8215 0.5477 -0.0405 0.0168  0.0606  118  LEU D CA  
9825  C  C   . LEU D 118 ? 0.3610 0.7298 0.4445 -0.0467 0.0156  0.0568  118  LEU D C   
9826  O  O   . LEU D 118 ? 0.3867 0.7682 0.4747 -0.0650 0.0188  0.0611  118  LEU D O   
9827  C  CB  . LEU D 118 ? 0.4414 0.7404 0.4972 -0.0347 0.0086  0.0616  118  LEU D CB  
9828  C  CG  . LEU D 118 ? 0.4624 0.7304 0.5007 -0.0351 0.0090  0.0682  118  LEU D CG  
9829  C  CD1 . LEU D 118 ? 0.5935 0.8265 0.6257 -0.0284 0.0019  0.0681  118  LEU D CD1 
9830  C  CD2 . LEU D 118 ? 0.4398 0.7035 0.4712 -0.0535 0.0130  0.0787  118  LEU D CD2 
9831  N  N   . LEU D 119 ? 0.2583 0.6390 0.3528 -0.0316 0.0107  0.0492  119  LEU D N   
9832  C  CA  . LEU D 119 ? 0.4121 0.8237 0.5252 -0.0355 0.0072  0.0453  119  LEU D CA  
9833  C  C   . LEU D 119 ? 0.5439 1.0003 0.6720 -0.0445 0.0156  0.0442  119  LEU D C   
9834  O  O   . LEU D 119 ? 0.4879 0.9623 0.6257 -0.0625 0.0158  0.0459  119  LEU D O   
9835  C  CB  . LEU D 119 ? 0.3266 0.7439 0.4477 -0.0146 0.0005  0.0388  119  LEU D CB  
9836  C  CG  . LEU D 119 ? 0.3677 0.7496 0.4782 -0.0117 -0.0087 0.0400  119  LEU D CG  
9837  C  CD1 . LEU D 119 ? 0.3835 0.7684 0.4990 0.0096  -0.0145 0.0355  119  LEU D CD1 
9838  C  CD2 . LEU D 119 ? 0.1734 0.5578 0.2872 -0.0305 -0.0134 0.0414  119  LEU D CD2 
9839  N  N   . GLY D 120 ? 0.4653 0.9397 0.5951 -0.0328 0.0231  0.0407  120  GLY D N   
9840  C  CA  . GLY D 120 ? 0.2011 0.7211 0.3456 -0.0389 0.0325  0.0385  120  GLY D CA  
9841  C  C   . GLY D 120 ? 0.2638 0.7845 0.4000 -0.0623 0.0407  0.0469  120  GLY D C   
9842  O  O   . GLY D 120 ? 0.3618 0.9210 0.5110 -0.0732 0.0488  0.0466  120  GLY D O   
9843  N  N   . ASN D 121 ? 0.4025 0.8811 0.5171 -0.0700 0.0392  0.0552  121  ASN D N   
9844  C  CA  . ASN D 121 ? 0.4921 0.9661 0.5955 -0.0906 0.0470  0.0654  121  ASN D CA  
9845  C  C   . ASN D 121 ? 0.4583 0.9032 0.5559 -0.1101 0.0425  0.0738  121  ASN D C   
9846  O  O   . ASN D 121 ? 0.4313 0.8771 0.5246 -0.1302 0.0491  0.0825  121  ASN D O   
9847  C  CB  . ASN D 121 ? 0.4452 0.8990 0.5264 -0.0839 0.0514  0.0696  121  ASN D CB  
9848  C  CG  . ASN D 121 ? 0.5251 1.0127 0.6099 -0.0721 0.0603  0.0619  121  ASN D CG  
9849  O  OD1 . ASN D 121 ? 0.4724 0.9892 0.5586 -0.0830 0.0711  0.0644  121  ASN D OD1 
9850  N  ND2 . ASN D 121 ? 0.5223 1.0053 0.6084 -0.0500 0.0566  0.0521  121  ASN D ND2 
9851  N  N   . HIS D 122 ? 0.2917 0.7103 0.3889 -0.1044 0.0319  0.0710  122  HIS D N   
9852  C  CA  . HIS D 122 ? 0.3872 0.7727 0.4769 -0.1206 0.0279  0.0773  122  HIS D CA  
9853  C  C   . HIS D 122 ? 0.5218 0.9273 0.6234 -0.1456 0.0317  0.0795  122  HIS D C   
9854  O  O   . HIS D 122 ? 0.5198 0.8985 0.6113 -0.1633 0.0339  0.0882  122  HIS D O   
9855  C  CB  . HIS D 122 ? 0.5593 0.9183 0.6474 -0.1099 0.0167  0.0719  122  HIS D CB  
9856  C  CG  . HIS D 122 ? 0.6135 0.9970 0.7193 -0.1127 0.0106  0.0635  122  HIS D CG  
9857  N  ND1 . HIS D 122 ? 0.6662 1.0806 0.7858 -0.0960 0.0072  0.0552  122  HIS D ND1 
9858  C  CD2 . HIS D 122 ? 0.5096 0.8912 0.6211 -0.1300 0.0067  0.0619  122  HIS D CD2 
9859  C  CE1 . HIS D 122 ? 0.6648 1.0979 0.7980 -0.1025 0.0008  0.0498  122  HIS D CE1 
9860  N  NE2 . HIS D 122 ? 0.6201 1.0345 0.7484 -0.1239 0.0004  0.0529  122  HIS D NE2 
9861  N  N   . GLU D 123 ? 0.5274 0.9798 0.6509 -0.1474 0.0328  0.0718  123  GLU D N   
9862  C  CA  . GLU D 123 ? 0.5237 1.0003 0.6612 -0.1726 0.0367  0.0727  123  GLU D CA  
9863  C  C   . GLU D 123 ? 0.4982 0.9955 0.6347 -0.1873 0.0505  0.0808  123  GLU D C   
9864  O  O   . GLU D 123 ? 0.3704 0.8733 0.5116 -0.2124 0.0557  0.0858  123  GLU D O   
9865  C  CB  . GLU D 123 ? 0.6860 1.2079 0.8497 -0.1701 0.0311  0.0613  123  GLU D CB  
9866  C  CG  . GLU D 123 ? 0.9059 1.4084 1.0695 -0.1641 0.0174  0.0548  123  GLU D CG  
9867  C  CD  . GLU D 123 ? 1.0756 1.6220 1.2637 -0.1706 0.0112  0.0456  123  GLU D CD  
9868  O  OE1 . GLU D 123 ? 1.1188 1.7162 1.3277 -0.1703 0.0161  0.0425  123  GLU D OE1 
9869  O  OE2 . GLU D 123 ? 1.1797 1.7108 1.3663 -0.1758 0.0012  0.0411  123  GLU D OE2 
9870  N  N   . ARG D 124 ? 0.4872 0.9946 0.6164 -0.1724 0.0569  0.0820  124  ARG D N   
9871  C  CA  . ARG D 124 ? 0.4287 0.9593 0.5549 -0.1844 0.0708  0.0890  124  ARG D CA  
9872  C  C   . ARG D 124 ? 0.4881 0.9760 0.5863 -0.1929 0.0748  0.1038  124  ARG D C   
9873  O  O   . ARG D 124 ? 0.5457 1.0365 0.6389 -0.2143 0.0841  0.1143  124  ARG D O   
9874  C  CB  . ARG D 124 ? 0.6307 1.1994 0.7635 -0.1649 0.0769  0.0812  124  ARG D CB  
9875  C  CG  . ARG D 124 ? 0.7008 1.2691 0.8401 -0.1368 0.0675  0.0695  124  ARG D CG  
9876  C  CD  . ARG D 124 ? 0.7653 1.3553 0.9023 -0.1176 0.0750  0.0635  124  ARG D CD  
9877  N  NE  . ARG D 124 ? 0.7943 1.4295 0.9405 -0.1284 0.0892  0.0638  124  ARG D NE  
9878  C  CZ  . ARG D 124 ? 0.7933 1.4799 0.9650 -0.1217 0.0940  0.0538  124  ARG D CZ  
9879  N  NH1 . ARG D 124 ? 0.8305 1.5289 1.0206 -0.1033 0.0848  0.0436  124  ARG D NH1 
9880  N  NH2 . ARG D 124 ? 0.7386 1.4654 0.9172 -0.1328 0.1082  0.0545  124  ARG D NH2 
9881  N  N   . ILE D 125 ? 0.3992 0.8485 0.4794 -0.1760 0.0677  0.1054  125  ILE D N   
9882  C  CA  . ILE D 125 ? 0.4575 0.8681 0.5115 -0.1799 0.0698  0.1194  125  ILE D CA  
9883  C  C   . ILE D 125 ? 0.5784 0.9394 0.6242 -0.1867 0.0615  0.1255  125  ILE D C   
9884  O  O   . ILE D 125 ? 0.6602 0.9999 0.7072 -0.1729 0.0514  0.1185  125  ILE D O   
9885  C  CB  . ILE D 125 ? 0.5407 0.9437 0.5795 -0.1573 0.0682  0.1175  125  ILE D CB  
9886  C  CG1 . ILE D 125 ? 0.5316 0.9743 0.5685 -0.1556 0.0799  0.1162  125  ILE D CG1 
9887  C  CG2 . ILE D 125 ? 0.4396 0.7947 0.4541 -0.1570 0.0642  0.1303  125  ILE D CG2 
9888  C  CD1 . ILE D 125 ? 0.5235 1.0149 0.5848 -0.1473 0.0834  0.1013  125  ILE D CD1 
9889  N  N   . SER D 126 ? 0.7024 1.0441 0.7392 -0.2078 0.0668  0.1387  126  SER D N   
9890  C  CA  . SER D 126 ? 0.7569 1.0519 0.7875 -0.2173 0.0610  0.1443  126  SER D CA  
9891  C  C   . SER D 126 ? 0.7605 1.0143 0.7771 -0.1975 0.0516  0.1449  126  SER D C   
9892  O  O   . SER D 126 ? 0.6423 0.8742 0.6638 -0.1931 0.0433  0.1377  126  SER D O   
9893  C  CB  . SER D 126 ? 0.7782 1.0549 0.7965 -0.2403 0.0698  0.1615  126  SER D CB  
9894  O  OG  . SER D 126 ? 0.9009 1.1417 0.9204 -0.2554 0.0666  0.1636  126  SER D OG  
9895  N  N   . ASP D 127 ? 0.7595 1.0050 0.7588 -0.1863 0.0529  0.1533  127  ASP D N   
9896  C  CA  . ASP D 127 ? 0.7218 0.9325 0.7091 -0.1683 0.0444  0.1545  127  ASP D CA  
9897  C  C   . ASP D 127 ? 0.5728 0.7862 0.5727 -0.1523 0.0360  0.1386  127  ASP D C   
9898  O  O   . ASP D 127 ? 0.7351 0.9165 0.7341 -0.1483 0.0292  0.1367  127  ASP D O   
9899  C  CB  . ASP D 127 ? 0.8621 1.0793 0.8333 -0.1563 0.0463  0.1607  127  ASP D CB  
9900  C  CG  . ASP D 127 ? 1.0745 1.2719 1.0262 -0.1675 0.0510  0.1803  127  ASP D CG  
9901  O  OD1 . ASP D 127 ? 1.1366 1.2978 1.0842 -0.1771 0.0494  0.1899  127  ASP D OD1 
9902  O  OD2 . ASP D 127 ? 1.1645 1.3816 1.1039 -0.1664 0.0564  0.1862  127  ASP D OD2 
9903  N  N   . LEU D 128 ? 0.4834 0.7347 0.4944 -0.1428 0.0371  0.1274  128  LEU D N   
9904  C  CA  . LEU D 128 ? 0.3914 0.6467 0.4127 -0.1260 0.0296  0.1137  128  LEU D CA  
9905  C  C   . LEU D 128 ? 0.4915 0.7426 0.5255 -0.1347 0.0249  0.1073  128  LEU D C   
9906  O  O   . LEU D 128 ? 0.4650 0.6955 0.4993 -0.1251 0.0173  0.1014  128  LEU D O   
9907  C  CB  . LEU D 128 ? 0.4577 0.7546 0.4889 -0.1147 0.0328  0.1040  128  LEU D CB  
9908  C  CG  . LEU D 128 ? 0.4735 0.7801 0.4921 -0.1060 0.0380  0.1068  128  LEU D CG  
9909  C  CD1 . LEU D 128 ? 0.4218 0.7723 0.4524 -0.0975 0.0436  0.0961  128  LEU D CD1 
9910  C  CD2 . LEU D 128 ? 0.4654 0.7414 0.4716 -0.0902 0.0312  0.1067  128  LEU D CD2 
9911  N  N   . GLY D 129 ? 0.5726 0.8448 0.6168 -0.1538 0.0298  0.1081  129  GLY D N   
9912  C  CA  . GLY D 129 ? 0.6027 0.8748 0.6590 -0.1649 0.0252  0.1010  129  GLY D CA  
9913  C  C   . GLY D 129 ? 0.5040 0.7264 0.5489 -0.1689 0.0205  0.1045  129  GLY D C   
9914  O  O   . GLY D 129 ? 0.5196 0.7314 0.5690 -0.1681 0.0137  0.0958  129  GLY D O   
9915  N  N   . GLN D 130 ? 0.2994 0.4916 0.3287 -0.1724 0.0243  0.1174  130  GLN D N   
9916  C  CA  . GLN D 130 ? 0.4793 0.6222 0.4974 -0.1733 0.0207  0.1219  130  GLN D CA  
9917  C  C   . GLN D 130 ? 0.3821 0.5053 0.3936 -0.1499 0.0139  0.1183  130  GLN D C   
9918  O  O   . GLN D 130 ? 0.4611 0.5562 0.4709 -0.1465 0.0089  0.1135  130  GLN D O   
9919  C  CB  . GLN D 130 ? 0.6031 0.7217 0.6077 -0.1851 0.0271  0.1388  130  GLN D CB  
9920  C  CG  . GLN D 130 ? 0.7028 0.7762 0.7020 -0.1971 0.0264  0.1430  130  GLN D CG  
9921  C  CD  . GLN D 130 ? 0.6357 0.6701 0.6252 -0.1796 0.0204  0.1439  130  GLN D CD  
9922  O  OE1 . GLN D 130 ? 0.6208 0.6601 0.6056 -0.1607 0.0174  0.1450  130  GLN D OE1 
9923  N  NE2 . GLN D 130 ? 0.7377 0.7337 0.7250 -0.1863 0.0190  0.1425  130  GLN D NE2 
9924  N  N   . LEU D 131 ? 0.4051 0.5441 0.4130 -0.1346 0.0142  0.1195  131  LEU D N   
9925  C  CA  . LEU D 131 ? 0.4070 0.5337 0.4114 -0.1138 0.0083  0.1146  131  LEU D CA  
9926  C  C   . LEU D 131 ? 0.3199 0.4527 0.3346 -0.1077 0.0027  0.1009  131  LEU D C   
9927  O  O   . LEU D 131 ? 0.4093 0.5162 0.4206 -0.0999 -0.0020 0.0975  131  LEU D O   
9928  C  CB  . LEU D 131 ? 0.4307 0.5805 0.4322 -0.1009 0.0100  0.1148  131  LEU D CB  
9929  C  CG  . LEU D 131 ? 0.5214 0.6619 0.5206 -0.0807 0.0045  0.1088  131  LEU D CG  
9930  C  CD1 . LEU D 131 ? 0.4737 0.5773 0.4621 -0.0762 0.0014  0.1166  131  LEU D CD1 
9931  C  CD2 . LEU D 131 ? 0.3352 0.5016 0.3332 -0.0701 0.0068  0.1058  131  LEU D CD2 
9932  N  N   . VAL D 132 ? 0.3775 0.5463 0.4046 -0.1111 0.0034  0.0937  132  VAL D N   
9933  C  CA  . VAL D 132 ? 0.3979 0.5785 0.4345 -0.1050 -0.0026 0.0819  132  VAL D CA  
9934  C  C   . VAL D 132 ? 0.4635 0.6254 0.5008 -0.1176 -0.0062 0.0777  132  VAL D C   
9935  O  O   . VAL D 132 ? 0.6562 0.8072 0.6923 -0.1095 -0.0119 0.0704  132  VAL D O   
9936  C  CB  . VAL D 132 ? 0.3229 0.5505 0.3745 -0.1048 -0.0013 0.0760  132  VAL D CB  
9937  C  CG1 . VAL D 132 ? 0.4714 0.7106 0.5320 -0.0999 -0.0087 0.0656  132  VAL D CG1 
9938  C  CG2 . VAL D 132 ? 0.1627 0.4073 0.2136 -0.0891 0.0018  0.0764  132  VAL D CG2 
9939  N  N   . ASN D 133 ? 0.4651 0.6236 0.5036 -0.1381 -0.0022 0.0820  133  ASN D N   
9940  C  CA  . ASN D 133 ? 0.4608 0.5992 0.4991 -0.1527 -0.0048 0.0771  133  ASN D CA  
9941  C  C   . ASN D 133 ? 0.5008 0.5929 0.5263 -0.1453 -0.0070 0.0777  133  ASN D C   
9942  O  O   . ASN D 133 ? 0.5972 0.6737 0.6214 -0.1492 -0.0109 0.0691  133  ASN D O   
9943  C  CB  . ASN D 133 ? 0.5546 0.6909 0.5948 -0.1770 0.0015  0.0835  133  ASN D CB  
9944  C  CG  . ASN D 133 ? 0.6194 0.8006 0.6763 -0.1914 0.0022  0.0775  133  ASN D CG  
9945  O  OD1 . ASN D 133 ? 0.6067 0.8236 0.6744 -0.1810 -0.0021 0.0695  133  ASN D OD1 
9946  N  ND2 . ASN D 133 ? 0.7169 0.8963 0.7768 -0.2157 0.0076  0.0815  133  ASN D ND2 
9947  N  N   . SER D 134 ? 0.4934 0.5655 0.5098 -0.1344 -0.0047 0.0873  134  SER D N   
9948  C  CA  . SER D 134 ? 0.4758 0.5041 0.4817 -0.1287 -0.0055 0.0901  134  SER D CA  
9949  C  C   . SER D 134 ? 0.4317 0.4547 0.4345 -0.1069 -0.0092 0.0869  134  SER D C   
9950  O  O   . SER D 134 ? 0.5960 0.5872 0.5924 -0.0997 -0.0098 0.0883  134  SER D O   
9951  C  CB  . SER D 134 ? 0.5466 0.5539 0.5445 -0.1333 -0.0005 0.1052  134  SER D CB  
9952  O  OG  . SER D 134 ? 0.6164 0.6465 0.6130 -0.1242 0.0010  0.1122  134  SER D OG  
9953  N  N   . THR D 135 ? 0.2936 0.3474 0.3019 -0.0965 -0.0111 0.0825  135  THR D N   
9954  C  CA  . THR D 135 ? 0.5183 0.5668 0.5237 -0.0773 -0.0137 0.0804  135  THR D CA  
9955  C  C   . THR D 135 ? 0.3538 0.4261 0.3651 -0.0688 -0.0174 0.0707  135  THR D C   
9956  O  O   . THR D 135 ? 0.3191 0.4232 0.3384 -0.0721 -0.0175 0.0683  135  THR D O   
9957  C  CB  . THR D 135 ? 0.6178 0.6714 0.6198 -0.0685 -0.0115 0.0890  135  THR D CB  
9958  O  OG1 . THR D 135 ? 0.4169 0.4578 0.4136 -0.0789 -0.0080 0.1002  135  THR D OG1 
9959  C  CG2 . THR D 135 ? 0.4189 0.4552 0.4169 -0.0522 -0.0139 0.0882  135  THR D CG2 
9960  N  N   . ASP D 136 ? 0.3903 0.4472 0.3977 -0.0575 -0.0202 0.0658  136  ASP D N   
9961  C  CA  . ASP D 136 ? 0.4836 0.5577 0.4939 -0.0474 -0.0237 0.0587  136  ASP D CA  
9962  C  C   . ASP D 136 ? 0.4769 0.5560 0.4873 -0.0322 -0.0228 0.0610  136  ASP D C   
9963  O  O   . ASP D 136 ? 0.3149 0.3730 0.3202 -0.0245 -0.0220 0.0629  136  ASP D O   
9964  C  CB  . ASP D 136 ? 0.6000 0.6545 0.6042 -0.0449 -0.0264 0.0522  136  ASP D CB  
9965  C  CG  . ASP D 136 ? 0.8128 0.8866 0.8193 -0.0490 -0.0310 0.0448  136  ASP D CG  
9966  O  OD1 . ASP D 136 ? 0.7397 0.8273 0.7514 -0.0632 -0.0318 0.0433  136  ASP D OD1 
9967  O  OD2 . ASP D 136 ? 0.9822 1.0578 0.9852 -0.0384 -0.0339 0.0409  136  ASP D OD2 
9968  N  N   . ILE D 137 ? 0.3985 0.5060 0.4154 -0.0283 -0.0225 0.0601  137  ILE D N   
9969  C  CA  . ILE D 137 ? 0.3655 0.4786 0.3824 -0.0161 -0.0207 0.0614  137  ILE D CA  
9970  C  C   . ILE D 137 ? 0.3692 0.4932 0.3893 -0.0026 -0.0228 0.0559  137  ILE D C   
9971  O  O   . ILE D 137 ? 0.3738 0.5200 0.4006 -0.0018 -0.0248 0.0526  137  ILE D O   
9972  C  CB  . ILE D 137 ? 0.3387 0.4722 0.3586 -0.0207 -0.0167 0.0653  137  ILE D CB  
9973  C  CG1 . ILE D 137 ? 0.4280 0.5481 0.4429 -0.0339 -0.0143 0.0732  137  ILE D CG1 
9974  C  CG2 . ILE D 137 ? 0.2557 0.3924 0.2736 -0.0086 -0.0150 0.0647  137  ILE D CG2 
9975  C  CD1 . ILE D 137 ? 0.3044 0.4484 0.3222 -0.0441 -0.0097 0.0774  137  ILE D CD1 
9976  N  N   . TYR D 138 ? 0.4308 0.5393 0.4466 0.0080  -0.0223 0.0556  138  TYR D N   
9977  C  CA  . TYR D 138 ? 0.3361 0.4474 0.3530 0.0209  -0.0235 0.0516  138  TYR D CA  
9978  C  C   . TYR D 138 ? 0.3662 0.4811 0.3840 0.0293  -0.0205 0.0507  138  TYR D C   
9979  O  O   . TYR D 138 ? 0.4161 0.5181 0.4298 0.0287  -0.0189 0.0526  138  TYR D O   
9980  C  CB  . TYR D 138 ? 0.3286 0.4160 0.3389 0.0246  -0.0250 0.0508  138  TYR D CB  
9981  C  CG  . TYR D 138 ? 0.3981 0.4832 0.4056 0.0181  -0.0282 0.0492  138  TYR D CG  
9982  C  CD1 . TYR D 138 ? 0.3785 0.4521 0.3833 0.0065  -0.0280 0.0501  138  TYR D CD1 
9983  C  CD2 . TYR D 138 ? 0.3543 0.4476 0.3608 0.0238  -0.0318 0.0467  138  TYR D CD2 
9984  C  CE1 . TYR D 138 ? 0.3630 0.4335 0.3641 -0.0003 -0.0308 0.0466  138  TYR D CE1 
9985  C  CE2 . TYR D 138 ? 0.3986 0.4914 0.4006 0.0174  -0.0354 0.0442  138  TYR D CE2 
9986  C  CZ  . TYR D 138 ? 0.4221 0.5036 0.4214 0.0047  -0.0347 0.0432  138  TYR D CZ  
9987  O  OH  . TYR D 138 ? 0.3853 0.4658 0.3794 -0.0026 -0.0382 0.0388  138  TYR D OH  
9988  N  N   . LEU D 139 ? 0.3590 0.4923 0.3825 0.0373  -0.0198 0.0472  139  LEU D N   
9989  C  CA  . LEU D 139 ? 0.2918 0.4289 0.3157 0.0447  -0.0163 0.0442  139  LEU D CA  
9990  C  C   . LEU D 139 ? 0.3775 0.5063 0.4020 0.0579  -0.0166 0.0404  139  LEU D C   
9991  O  O   . LEU D 139 ? 0.3580 0.4975 0.3874 0.0648  -0.0183 0.0392  139  LEU D O   
9992  C  CB  . LEU D 139 ? 0.1418 0.3078 0.1722 0.0432  -0.0133 0.0425  139  LEU D CB  
9993  C  CG  . LEU D 139 ? 0.3199 0.4969 0.3500 0.0288  -0.0119 0.0473  139  LEU D CG  
9994  C  CD1 . LEU D 139 ? 0.1836 0.3915 0.2198 0.0276  -0.0070 0.0452  139  LEU D CD1 
9995  C  CD2 . LEU D 139 ? 0.3205 0.4768 0.3409 0.0227  -0.0116 0.0522  139  LEU D CD2 
9996  N  N   . VAL D 140 ? 0.4483 0.5582 0.4680 0.0612  -0.0150 0.0388  140  VAL D N   
9997  C  CA  . VAL D 140 ? 0.4808 0.5776 0.4999 0.0723  -0.0142 0.0356  140  VAL D CA  
9998  C  C   . VAL D 140 ? 0.4105 0.5083 0.4301 0.0772  -0.0104 0.0294  140  VAL D C   
9999  O  O   . VAL D 140 ? 0.4332 0.5165 0.4490 0.0752  -0.0094 0.0275  140  VAL D O   
10000 C  CB  . VAL D 140 ? 0.5049 0.5766 0.5185 0.0710  -0.0150 0.0380  140  VAL D CB  
10001 C  CG1 . VAL D 140 ? 0.3214 0.3782 0.3337 0.0811  -0.0135 0.0361  140  VAL D CG1 
10002 C  CG2 . VAL D 140 ? 0.4690 0.5386 0.4801 0.0651  -0.0182 0.0426  140  VAL D CG2 
10003 N  N   . PRO D 141 ? 0.4707 0.5872 0.4957 0.0835  -0.0082 0.0252  141  PRO D N   
10004 C  CA  . PRO D 141 ? 0.4241 0.5439 0.4489 0.0885  -0.0037 0.0171  141  PRO D CA  
10005 C  C   . PRO D 141 ? 0.4503 0.5443 0.4714 0.0938  -0.0024 0.0126  141  PRO D C   
10006 O  O   . PRO D 141 ? 0.4831 0.5727 0.5003 0.0907  -0.0003 0.0069  141  PRO D O   
10007 C  CB  . PRO D 141 ? 0.3006 0.4407 0.3340 0.0986  -0.0018 0.0138  141  PRO D CB  
10008 C  CG  . PRO D 141 ? 0.4841 0.6428 0.5223 0.0924  -0.0053 0.0205  141  PRO D CG  
10009 C  CD  . PRO D 141 ? 0.4924 0.6305 0.5247 0.0862  -0.0099 0.0271  141  PRO D CD  
10010 N  N   . THR D 142 ? 0.3124 0.3900 0.3341 0.1007  -0.0035 0.0153  142  THR D N   
10011 C  CA  . THR D 142 ? 0.5111 0.5622 0.5292 0.1030  -0.0016 0.0123  142  THR D CA  
10012 C  C   . THR D 142 ? 0.5056 0.5374 0.5202 0.1004  -0.0036 0.0194  142  THR D C   
10013 O  O   . THR D 142 ? 0.3510 0.3858 0.3652 0.1023  -0.0066 0.0261  142  THR D O   
10014 C  CB  . THR D 142 ? 0.4766 0.5187 0.4970 0.1158  0.0022  0.0059  142  THR D CB  
10015 O  OG1 . THR D 142 ? 0.4652 0.4792 0.4817 0.1149  0.0046  0.0030  142  THR D OG1 
10016 C  CG2 . THR D 142 ? 0.2841 0.3287 0.3080 0.1269  0.0003  0.0118  142  THR D CG2 
10017 N  N   . MET D 143 ? 0.5937 0.6072 0.6057 0.0958  -0.0018 0.0171  143  MET D N   
10018 C  CA  . MET D 143 ? 0.4431 0.4381 0.4520 0.0926  -0.0019 0.0226  143  MET D CA  
10019 C  C   . MET D 143 ? 0.4546 0.4257 0.4623 0.0964  0.0024  0.0192  143  MET D C   
10020 O  O   . MET D 143 ? 0.3687 0.3220 0.3736 0.0941  0.0042  0.0233  143  MET D O   
10021 C  CB  . MET D 143 ? 0.3406 0.3386 0.3498 0.0817  -0.0033 0.0233  143  MET D CB  
10022 C  CG  . MET D 143 ? 0.4222 0.4068 0.4295 0.0778  -0.0028 0.0286  143  MET D CG  
10023 S  SD  . MET D 143 ? 0.4625 0.4505 0.4738 0.0679  -0.0038 0.0272  143  MET D SD  
10024 C  CE  . MET D 143 ? 0.3464 0.3141 0.3578 0.0657  0.0004  0.0295  143  MET D CE  
10025 N  N   . ASN D 144 ? 0.2210 0.1910 0.2305 0.1018  0.0050  0.0112  144  ASN D N   
10026 C  CA  . ASN D 144 ? 0.4298 0.3743 0.4382 0.1054  0.0095  0.0074  144  ASN D CA  
10027 C  C   . ASN D 144 ? 0.5720 0.5146 0.5819 0.1181  0.0119  0.0017  144  ASN D C   
10028 O  O   . ASN D 144 ? 0.6033 0.5445 0.6145 0.1179  0.0149  -0.0096 144  ASN D O   
10029 C  CB  . ASN D 144 ? 0.4473 0.3847 0.4567 0.0946  0.0114  -0.0005 144  ASN D CB  
10030 C  CG  . ASN D 144 ? 0.4941 0.4034 0.5027 0.0954  0.0166  -0.0053 144  ASN D CG  
10031 O  OD1 . ASN D 144 ? 0.5102 0.4004 0.5160 0.1035  0.0191  0.0003  144  ASN D OD1 
10032 N  ND2 . ASN D 144 ? 0.5702 0.4763 0.5809 0.0865  0.0181  -0.0156 144  ASN D ND2 
10033 N  N   . PRO D 145 ? 0.4956 0.4389 0.5056 0.1297  0.0105  0.0091  145  PRO D N   
10034 C  CA  . PRO D 145 ? 0.3923 0.3356 0.4058 0.1449  0.0124  0.0056  145  PRO D CA  
10035 C  C   . PRO D 145 ? 0.4752 0.3852 0.4866 0.1498  0.0182  0.0002  145  PRO D C   
10036 O  O   . PRO D 145 ? 0.5568 0.4642 0.5714 0.1587  0.0218  -0.0093 145  PRO D O   
10037 C  CB  . PRO D 145 ? 0.3005 0.2486 0.3133 0.1545  0.0081  0.0179  145  PRO D CB  
10038 C  CG  . PRO D 145 ? 0.5050 0.4581 0.5130 0.1427  0.0042  0.0260  145  PRO D CG  
10039 C  CD  . PRO D 145 ? 0.4709 0.4104 0.4765 0.1293  0.0074  0.0215  145  PRO D CD  
10040 N  N   . ASP D 146 ? 0.5884 0.4723 0.5942 0.1438  0.0198  0.0060  146  ASP D N   
10041 C  CA  . ASP D 146 ? 0.5825 0.4308 0.5857 0.1468  0.0258  0.0027  146  ASP D CA  
10042 C  C   . ASP D 146 ? 0.5237 0.3679 0.5291 0.1365  0.0295  -0.0128 146  ASP D C   
10043 O  O   . ASP D 146 ? 0.6064 0.4317 0.6123 0.1420  0.0344  -0.0227 146  ASP D O   
10044 C  CB  . ASP D 146 ? 0.6681 0.4922 0.6644 0.1412  0.0272  0.0144  146  ASP D CB  
10045 C  CG  . ASP D 146 ? 0.6325 0.4580 0.6238 0.1528  0.0234  0.0296  146  ASP D CG  
10046 O  OD1 . ASP D 146 ? 0.4778 0.3267 0.4732 0.1638  0.0188  0.0305  146  ASP D OD1 
10047 O  OD2 . ASP D 146 ? 0.6386 0.4437 0.6216 0.1505  0.0250  0.0405  146  ASP D OD2 
10048 N  N   . GLY D 147 ? 0.3617 0.2235 0.3680 0.1219  0.0268  -0.0151 147  GLY D N   
10049 C  CA  . GLY D 147 ? 0.4062 0.2732 0.4142 0.1119  0.0281  -0.0297 147  GLY D CA  
10050 C  C   . GLY D 147 ? 0.4969 0.3808 0.5061 0.1204  0.0287  -0.0405 147  GLY D C   
10051 O  O   . GLY D 147 ? 0.5544 0.4265 0.5628 0.1206  0.0330  -0.0544 147  GLY D O   
10052 N  N   . TYR D 148 ? 0.4844 0.3961 0.4956 0.1268  0.0252  -0.0349 148  TYR D N   
10053 C  CA  . TYR D 148 ? 0.6420 0.5755 0.6552 0.1341  0.0266  -0.0444 148  TYR D CA  
10054 C  C   . TYR D 148 ? 0.7268 0.6409 0.7417 0.1489  0.0326  -0.0525 148  TYR D C   
10055 O  O   . TYR D 148 ? 0.6386 0.5517 0.6522 0.1497  0.0370  -0.0678 148  TYR D O   
10056 C  CB  . TYR D 148 ? 0.5643 0.5294 0.5812 0.1384  0.0225  -0.0352 148  TYR D CB  
10057 C  CG  . TYR D 148 ? 0.5367 0.5265 0.5573 0.1472  0.0253  -0.0435 148  TYR D CG  
10058 C  CD1 . TYR D 148 ? 0.5480 0.5560 0.5652 0.1395  0.0270  -0.0542 148  TYR D CD1 
10059 C  CD2 . TYR D 148 ? 0.3882 0.3862 0.4160 0.1632  0.0261  -0.0401 148  TYR D CD2 
10060 C  CE1 . TYR D 148 ? 0.3890 0.4215 0.4089 0.1470  0.0309  -0.0619 148  TYR D CE1 
10061 C  CE2 . TYR D 148 ? 0.3350 0.3591 0.3683 0.1712  0.0295  -0.0481 148  TYR D CE2 
10062 C  CZ  . TYR D 148 ? 0.4118 0.4526 0.4408 0.1626  0.0326  -0.0591 148  TYR D CZ  
10063 O  OH  . TYR D 148 ? 0.6706 0.7384 0.7043 0.1701  0.0374  -0.0673 148  TYR D OH  
10064 N  N   . ALA D 149 ? 0.6657 0.5640 0.6826 0.1612  0.0325  -0.0422 149  ALA D N   
10065 C  CA  . ALA D 149 ? 0.5299 0.4063 0.5491 0.1781  0.0378  -0.0470 149  ALA D CA  
10066 C  C   . ALA D 149 ? 0.5698 0.4123 0.5848 0.1730  0.0442  -0.0611 149  ALA D C   
10067 O  O   . ALA D 149 ? 0.5321 0.3613 0.5487 0.1844  0.0500  -0.0726 149  ALA D O   
10068 C  CB  . ALA D 149 ? 0.3478 0.2083 0.3672 0.1899  0.0354  -0.0305 149  ALA D CB  
10069 N  N   . LEU D 150 ? 0.6968 0.5260 0.7074 0.1555  0.0435  -0.0611 150  LEU D N   
10070 C  CA  . LEU D 150 ? 0.7442 0.5423 0.7517 0.1479  0.0491  -0.0745 150  LEU D CA  
10071 C  C   . LEU D 150 ? 0.7936 0.6103 0.7993 0.1375  0.0497  -0.0934 150  LEU D C   
10072 O  O   . LEU D 150 ? 0.8425 0.6376 0.8455 0.1311  0.0542  -0.1085 150  LEU D O   
10073 C  CB  . LEU D 150 ? 0.6543 0.4286 0.6594 0.1341  0.0489  -0.0658 150  LEU D CB  
10074 C  CG  . LEU D 150 ? 0.7487 0.4943 0.7519 0.1442  0.0507  -0.0494 150  LEU D CG  
10075 C  CD1 . LEU D 150 ? 0.6424 0.3847 0.6432 0.1316  0.0484  -0.0350 150  LEU D CD1 
10076 C  CD2 . LEU D 150 ? 0.6698 0.3708 0.6710 0.1509  0.0584  -0.0561 150  LEU D CD2 
10077 N  N   . SER D 151 ? 0.7522 0.6084 0.7584 0.1356  0.0452  -0.0925 151  SER D N   
10078 C  CA  . SER D 151 ? 0.6947 0.5721 0.6965 0.1257  0.0449  -0.1078 151  SER D CA  
10079 C  C   . SER D 151 ? 0.6905 0.5768 0.6914 0.1383  0.0506  -0.1223 151  SER D C   
10080 O  O   . SER D 151 ? 0.6406 0.5257 0.6468 0.1557  0.0535  -0.1182 151  SER D O   
10081 C  CB  . SER D 151 ? 0.6003 0.5141 0.6015 0.1162  0.0378  -0.0986 151  SER D CB  
10082 O  OG  . SER D 151 ? 0.5844 0.4912 0.5871 0.1049  0.0333  -0.0873 151  SER D OG  
10083 N  N   . GLN D 152 ? 0.6560 0.5534 0.6501 0.1299  0.0520  -0.1394 152  GLN D N   
10084 C  CA  . GLN D 152 ? 0.6940 0.5993 0.6857 0.1406  0.0589  -0.1560 152  GLN D CA  
10085 C  C   . GLN D 152 ? 0.7298 0.6787 0.7158 0.1362  0.0573  -0.1598 152  GLN D C   
10086 O  O   . GLN D 152 ? 0.7076 0.6695 0.6848 0.1207  0.0536  -0.1657 152  GLN D O   
10087 C  CB  . GLN D 152 ? 0.8771 0.7519 0.8630 0.1363  0.0645  -0.1773 152  GLN D CB  
10088 C  CG  . GLN D 152 ? 0.9784 0.8594 0.9602 0.1470  0.0726  -0.1975 152  GLN D CG  
10089 C  CD  . GLN D 152 ? 1.0955 0.9470 1.0697 0.1395  0.0775  -0.2206 152  GLN D CD  
10090 O  OE1 . GLN D 152 ? 1.2514 1.1124 1.2177 0.1411  0.0829  -0.2409 152  GLN D OE1 
10091 N  NE2 . GLN D 152 ? 0.9854 0.8010 0.9613 0.1302  0.0762  -0.2182 152  GLN D NE2 
10092 N  N   . GLU D 153 ? 0.6834 0.6560 0.6746 0.1496  0.0602  -0.1558 153  GLU D N   
10093 C  CA  . GLU D 153 ? 0.7019 0.7155 0.6875 0.1456  0.0605  -0.1586 153  GLU D CA  
10094 C  C   . GLU D 153 ? 0.6903 0.7054 0.6625 0.1377  0.0643  -0.1804 153  GLU D C   
10095 O  O   . GLU D 153 ? 0.6238 0.6153 0.5945 0.1447  0.0712  -0.1979 153  GLU D O   
10096 C  CB  . GLU D 153 ? 0.5828 0.6195 0.5775 0.1625  0.0660  -0.1565 153  GLU D CB  
10097 C  CG  . GLU D 153 ? 0.5744 0.6549 0.5635 0.1573  0.0678  -0.1582 153  GLU D CG  
10098 C  CD  . GLU D 153 ? 0.6737 0.7806 0.6747 0.1728  0.0736  -0.1558 153  GLU D CD  
10099 O  OE1 . GLU D 153 ? 0.6838 0.8219 0.6804 0.1724  0.0797  -0.1641 153  GLU D OE1 
10100 O  OE2 . GLU D 153 ? 0.6287 0.7270 0.6436 0.1852  0.0721  -0.1456 153  GLU D OE2 
10101 N  N   . GLY D 154 ? 0.6542 0.6955 0.6157 0.1232  0.0594  -0.1793 154  GLY D N   
10102 C  CA  . GLY D 154 ? 0.6840 0.7322 0.6303 0.1144  0.0616  -0.1991 154  GLY D CA  
10103 C  C   . GLY D 154 ? 0.7317 0.7707 0.6710 0.0966  0.0531  -0.2003 154  GLY D C   
10104 O  O   . GLY D 154 ? 0.7743 0.8331 0.6997 0.0853  0.0500  -0.2084 154  GLY D O   
10105 N  N   . ASN D 155 ? 0.7199 0.7308 0.6690 0.0940  0.0492  -0.1917 155  ASN D N   
10106 C  CA  . ASN D 155 ? 0.5698 0.5720 0.5161 0.0774  0.0417  -0.1932 155  ASN D CA  
10107 C  C   . ASN D 155 ? 0.6342 0.6668 0.5769 0.0667  0.0322  -0.1786 155  ASN D C   
10108 O  O   . ASN D 155 ? 0.7759 0.8113 0.7273 0.0675  0.0279  -0.1588 155  ASN D O   
10109 C  CB  . ASN D 155 ? 0.5626 0.5283 0.5209 0.0771  0.0414  -0.1867 155  ASN D CB  
10110 C  CG  . ASN D 155 ? 0.7084 0.6387 0.6656 0.0772  0.0480  -0.2067 155  ASN D CG  
10111 O  OD1 . ASN D 155 ? 0.7576 0.6542 0.7231 0.0838  0.0521  -0.2030 155  ASN D OD1 
10112 N  ND2 . ASN D 155 ? 0.8949 0.8317 0.8406 0.0695  0.0491  -0.2280 155  ASN D ND2 
10113 N  N   . CYS D 156 ? 0.6470 0.7021 0.5758 0.0570  0.0289  -0.1886 156  CYS D N   
10114 C  CA  . CYS D 156 ? 0.7371 0.8185 0.6613 0.0466  0.0189  -0.1753 156  CYS D CA  
10115 C  C   . CYS D 156 ? 0.6949 0.7619 0.6285 0.0365  0.0114  -0.1703 156  CYS D C   
10116 O  O   . CYS D 156 ? 0.7449 0.8238 0.6831 0.0325  0.0040  -0.1529 156  CYS D O   
10117 C  CB  . CYS D 156 ? 0.8530 0.9617 0.7580 0.0390  0.0167  -0.1875 156  CYS D CB  
10118 S  SG  . CYS D 156 ? 0.9118 1.0501 0.8052 0.0481  0.0243  -0.1851 156  CYS D SG  
10119 N  N   . GLU D 157 ? 0.6971 0.7380 0.6341 0.0325  0.0141  -0.1859 157  GLU D N   
10120 C  CA  . GLU D 157 ? 0.7593 0.7829 0.7081 0.0231  0.0095  -0.1820 157  GLU D CA  
10121 C  C   . GLU D 157 ? 0.7185 0.7067 0.6802 0.0308  0.0162  -0.1760 157  GLU D C   
10122 O  O   . GLU D 157 ? 0.6511 0.6194 0.6118 0.0415  0.0248  -0.1835 157  GLU D O   
10123 C  CB  . GLU D 157 ? 0.8677 0.8884 0.8120 0.0088  0.0065  -0.2025 157  GLU D CB  
10124 C  CG  . GLU D 157 ? 1.0500 1.1072 0.9836 -0.0013 -0.0036 -0.2046 157  GLU D CG  
10125 C  CD  . GLU D 157 ? 1.2391 1.3100 1.1535 -0.0010 -0.0008 -0.2235 157  GLU D CD  
10126 O  OE1 . GLU D 157 ? 1.3805 1.4428 1.2894 -0.0101 -0.0002 -0.2458 157  GLU D OE1 
10127 O  OE2 . GLU D 157 ? 1.1949 1.2853 1.0994 0.0074  0.0014  -0.2167 157  GLU D OE2 
10128 N  N   . SER D 158 ? 0.7442 0.7253 0.7173 0.0258  0.0123  -0.1620 158  SER D N   
10129 C  CA  . SER D 158 ? 0.6009 0.5503 0.5840 0.0320  0.0180  -0.1535 158  SER D CA  
10130 C  C   . SER D 158 ? 0.6843 0.5992 0.6678 0.0297  0.0251  -0.1704 158  SER D C   
10131 O  O   . SER D 158 ? 0.6083 0.5232 0.5876 0.0182  0.0240  -0.1884 158  SER D O   
10132 C  CB  . SER D 158 ? 0.5688 0.5193 0.5627 0.0249  0.0131  -0.1377 158  SER D CB  
10133 O  OG  . SER D 158 ? 0.7650 0.6869 0.7658 0.0311  0.0187  -0.1279 158  SER D OG  
10134 N  N   . LEU D 159 ? 0.8983 0.7832 0.8861 0.0407  0.0322  -0.1644 159  LEU D N   
10135 C  CA  . LEU D 159 ? 1.0134 0.8587 1.0016 0.0406  0.0400  -0.1774 159  LEU D CA  
10136 C  C   . LEU D 159 ? 0.9598 0.7897 0.9544 0.0223  0.0388  -0.1809 159  LEU D C   
10137 O  O   . LEU D 159 ? 0.6994 0.5404 0.7016 0.0152  0.0341  -0.1666 159  LEU D O   
10138 C  CB  . LEU D 159 ? 1.0064 0.8243 0.9979 0.0579  0.0466  -0.1657 159  LEU D CB  
10139 C  CG  . LEU D 159 ? 0.8234 0.6500 0.8109 0.0772  0.0503  -0.1678 159  LEU D CG  
10140 C  CD1 . LEU D 159 ? 0.8041 0.6094 0.7968 0.0944  0.0543  -0.1527 159  LEU D CD1 
10141 C  CD2 . LEU D 159 ? 0.5926 0.4084 0.5731 0.0790  0.0564  -0.1923 159  LEU D CD2 
10142 N  N   . PRO D 160 ? 1.1545 0.9589 1.1467 0.0144  0.0436  -0.2008 160  PRO D N   
10143 C  CA  . PRO D 160 ? 1.3699 1.1560 1.3679 -0.0050 0.0444  -0.2108 160  PRO D CA  
10144 C  C   . PRO D 160 ? 1.2833 1.0719 1.2933 -0.0156 0.0415  -0.1940 160  PRO D C   
10145 O  O   . PRO D 160 ? 1.3110 1.1202 1.3274 -0.0326 0.0355  -0.1987 160  PRO D O   
10146 C  CB  . PRO D 160 ? 1.5000 1.2362 1.4957 0.0008  0.0553  -0.2201 160  PRO D CB  
10147 C  CG  . PRO D 160 ? 1.3026 1.0413 1.2891 0.0216  0.0589  -0.2255 160  PRO D CG  
10148 C  CD  . PRO D 160 ? 1.2267 1.0146 1.2104 0.0267  0.0507  -0.2163 160  PRO D CD  
10149 N  N   . ASN D 161 ? 1.0073 0.7763 1.0207 -0.0055 0.0460  -0.1751 161  ASN D N   
10150 C  CA  . ASN D 161 ? 0.6467 0.4162 0.6705 -0.0151 0.0452  -0.1599 161  ASN D CA  
10151 C  C   . ASN D 161 ? 0.5187 0.3188 0.5438 -0.0055 0.0393  -0.1406 161  ASN D C   
10152 O  O   . ASN D 161 ? 0.6974 0.4965 0.7289 -0.0071 0.0399  -0.1246 161  ASN D O   
10153 C  CB  . ASN D 161 ? 0.8066 0.5297 0.8315 -0.0135 0.0552  -0.1527 161  ASN D CB  
10154 C  CG  . ASN D 161 ? 1.1984 0.8874 1.2225 -0.0251 0.0617  -0.1724 161  ASN D CG  
10155 O  OD1 . ASN D 161 ? 1.3785 1.0270 1.3971 -0.0160 0.0698  -0.1742 161  ASN D OD1 
10156 N  ND2 . ASN D 161 ? 1.2440 0.9497 1.2738 -0.0452 0.0577  -0.1877 161  ASN D ND2 
10157 N  N   . TYR D 162 ? 0.5245 0.3517 0.5429 0.0035  0.0340  -0.1431 162  TYR D N   
10158 C  CA  . TYR D 162 ? 0.6640 0.5187 0.6825 0.0126  0.0286  -0.1262 162  TYR D CA  
10159 C  C   . TYR D 162 ? 0.7454 0.5806 0.7620 0.0281  0.0336  -0.1115 162  TYR D C   
10160 O  O   . TYR D 162 ? 0.6366 0.4864 0.6546 0.0339  0.0305  -0.0955 162  TYR D O   
10161 C  CB  . TYR D 162 ? 0.3807 0.2555 0.4089 0.0013  0.0232  -0.1169 162  TYR D CB  
10162 C  CG  . TYR D 162 ? 0.5789 0.4862 0.6081 -0.0089 0.0149  -0.1268 162  TYR D CG  
10163 C  CD1 . TYR D 162 ? 0.7804 0.6901 0.8172 -0.0257 0.0131  -0.1384 162  TYR D CD1 
10164 C  CD2 . TYR D 162 ? 0.6639 0.6006 0.6859 -0.0021 0.0085  -0.1244 162  TYR D CD2 
10165 C  CE1 . TYR D 162 ? 0.8767 0.8194 0.9138 -0.0343 0.0039  -0.1470 162  TYR D CE1 
10166 C  CE2 . TYR D 162 ? 0.7438 0.7106 0.7645 -0.0105 0.0002  -0.1317 162  TYR D CE2 
10167 C  CZ  . TYR D 162 ? 0.8123 0.7828 0.8404 -0.0260 -0.0027 -0.1430 162  TYR D CZ  
10168 O  OH  . TYR D 162 ? 0.9988 1.0022 1.0251 -0.0337 -0.0124 -0.1497 162  TYR D OH  
10169 N  N   . VAL D 163 ? 0.8242 0.6257 0.8374 0.0347  0.0410  -0.1175 163  VAL D N   
10170 C  CA  . VAL D 163 ? 0.8858 0.6688 0.8963 0.0519  0.0451  -0.1051 163  VAL D CA  
10171 C  C   . VAL D 163 ? 0.7882 0.6007 0.7955 0.0655  0.0410  -0.1008 163  VAL D C   
10172 O  O   . VAL D 163 ? 0.7063 0.5369 0.7100 0.0666  0.0397  -0.1137 163  VAL D O   
10173 C  CB  . VAL D 163 ? 0.7086 0.4511 0.7157 0.0584  0.0535  -0.1150 163  VAL D CB  
10174 C  CG1 . VAL D 163 ? 0.6648 0.3996 0.6689 0.0809  0.0558  -0.1064 163  VAL D CG1 
10175 C  CG2 . VAL D 163 ? 0.5597 0.2662 0.5696 0.0474  0.0591  -0.1117 163  VAL D CG2 
10176 N  N   . GLY D 164 ? 0.6013 0.4194 0.6095 0.0747  0.0393  -0.0830 164  GLY D N   
10177 C  CA  . GLY D 164 ? 0.4859 0.3328 0.4929 0.0856  0.0354  -0.0771 164  GLY D CA  
10178 C  C   . GLY D 164 ? 0.4296 0.3072 0.4384 0.0769  0.0284  -0.0689 164  GLY D C   
10179 O  O   . GLY D 164 ? 0.5696 0.4663 0.5784 0.0835  0.0251  -0.0584 164  GLY D O   
10180 N  N   . ARG D 165 ? 0.4552 0.3378 0.4663 0.0620  0.0260  -0.0741 165  ARG D N   
10181 C  CA  . ARG D 165 ? 0.6593 0.5677 0.6735 0.0544  0.0195  -0.0657 165  ARG D CA  
10182 C  C   . ARG D 165 ? 0.6855 0.5857 0.7033 0.0551  0.0199  -0.0498 165  ARG D C   
10183 O  O   . ARG D 165 ? 0.6244 0.5407 0.6417 0.0592  0.0164  -0.0388 165  ARG D O   
10184 C  CB  . ARG D 165 ? 0.5237 0.4411 0.5412 0.0395  0.0164  -0.0757 165  ARG D CB  
10185 C  CG  . ARG D 165 ? 0.5546 0.4975 0.5766 0.0333  0.0096  -0.0667 165  ARG D CG  
10186 C  CD  . ARG D 165 ? 0.4931 0.4509 0.5191 0.0201  0.0048  -0.0770 165  ARG D CD  
10187 N  NE  . ARG D 165 ? 0.3440 0.3187 0.3786 0.0146  -0.0003 -0.0672 165  ARG D NE  
10188 C  CZ  . ARG D 165 ? 0.4493 0.4507 0.4830 0.0153  -0.0075 -0.0614 165  ARG D CZ  
10189 N  NH1 . ARG D 165 ? 0.2902 0.3066 0.3137 0.0196  -0.0106 -0.0638 165  ARG D NH1 
10190 N  NH2 . ARG D 165 ? 0.4680 0.4808 0.5110 0.0119  -0.0112 -0.0528 165  ARG D NH2 
10191 N  N   . GLY D 166 ? 0.5239 0.3985 0.5443 0.0501  0.0248  -0.0491 166  GLY D N   
10192 C  CA  . GLY D 166 ? 0.5287 0.3925 0.5501 0.0507  0.0269  -0.0348 166  GLY D CA  
10193 C  C   . GLY D 166 ? 0.5534 0.4014 0.5682 0.0650  0.0295  -0.0261 166  GLY D C   
10194 O  O   . GLY D 166 ? 0.6515 0.4956 0.6634 0.0748  0.0304  -0.0318 166  GLY D O   
10195 N  N   . ASN D 167 ? 0.4845 0.3254 0.4972 0.0669  0.0306  -0.0125 167  ASN D N   
10196 C  CA  . ASN D 167 ? 0.4819 0.3102 0.4877 0.0808  0.0317  -0.0030 167  ASN D CA  
10197 C  C   . ASN D 167 ? 0.5910 0.3836 0.5935 0.0845  0.0384  -0.0046 167  ASN D C   
10198 O  O   . ASN D 167 ? 0.6723 0.4527 0.6780 0.0777  0.0417  -0.0169 167  ASN D O   
10199 C  CB  . ASN D 167 ? 0.4143 0.2480 0.4162 0.0818  0.0302  0.0115  167  ASN D CB  
10200 C  CG  . ASN D 167 ? 0.4142 0.2271 0.4141 0.0735  0.0360  0.0176  167  ASN D CG  
10201 O  OD1 . ASN D 167 ? 0.5298 0.3260 0.5332 0.0650  0.0410  0.0113  167  ASN D OD1 
10202 N  ND2 . ASN D 167 ? 0.3427 0.1573 0.3365 0.0750  0.0359  0.0296  167  ASN D ND2 
10203 N  N   . ALA D 168 ? 0.6620 0.4373 0.6577 0.0952  0.0401  0.0074  168  ALA D N   
10204 C  CA  . ALA D 168 ? 0.7007 0.4393 0.6921 0.1016  0.0462  0.0079  168  ALA D CA  
10205 C  C   . ALA D 168 ? 0.9287 0.6399 0.9192 0.0874  0.0533  0.0092  168  ALA D C   
10206 O  O   . ALA D 168 ? 1.0596 0.7377 1.0483 0.0877  0.0595  0.0059  168  ALA D O   
10207 C  CB  . ALA D 168 ? 0.7440 0.4744 0.7279 0.1189  0.0446  0.0221  168  ALA D CB  
10208 N  N   . ALA D 169 ? 0.8840 0.6087 0.8765 0.0748  0.0532  0.0139  169  ALA D N   
10209 C  CA  . ALA D 169 ? 0.6094 0.3156 0.6038 0.0590  0.0604  0.0142  169  ALA D CA  
10210 C  C   . ALA D 169 ? 0.6262 0.3470 0.6327 0.0441  0.0596  -0.0022 169  ALA D C   
10211 O  O   . ALA D 169 ? 0.5633 0.2783 0.5758 0.0286  0.0645  -0.0046 169  ALA D O   
10212 C  CB  . ALA D 169 ? 0.4213 0.1357 0.4120 0.0543  0.0617  0.0276  169  ALA D CB  
10213 N  N   . ASN D 170 ? 0.6288 0.3709 0.6389 0.0487  0.0534  -0.0132 170  ASN D N   
10214 C  CA  . ASN D 170 ? 0.7267 0.4852 0.7460 0.0363  0.0511  -0.0289 170  ASN D CA  
10215 C  C   . ASN D 170 ? 0.7511 0.5378 0.7791 0.0245  0.0477  -0.0273 170  ASN D C   
10216 O  O   . ASN D 170 ? 0.8342 0.6294 0.8712 0.0108  0.0473  -0.0380 170  ASN D O   
10217 C  CB  . ASN D 170 ? 0.8951 0.6241 0.9165 0.0261  0.0577  -0.0402 170  ASN D CB  
10218 C  CG  . ASN D 170 ? 1.0961 0.8127 1.1136 0.0348  0.0579  -0.0531 170  ASN D CG  
10219 O  OD1 . ASN D 170 ? 1.1071 0.7882 1.1191 0.0414  0.0640  -0.0526 170  ASN D OD1 
10220 N  ND2 . ASN D 170 ? 1.1573 0.9026 1.1768 0.0354  0.0516  -0.0646 170  ASN D ND2 
10221 N  N   . ILE D 171 ? 0.5284 0.3303 0.5544 0.0297  0.0452  -0.0148 171  ILE D N   
10222 C  CA  . ILE D 171 ? 0.6890 0.5186 0.7241 0.0211  0.0417  -0.0141 171  ILE D CA  
10223 C  C   . ILE D 171 ? 0.5330 0.3920 0.5681 0.0279  0.0329  -0.0152 171  ILE D C   
10224 O  O   . ILE D 171 ? 0.4830 0.3432 0.5102 0.0397  0.0305  -0.0106 171  ILE D O   
10225 C  CB  . ILE D 171 ? 0.6848 0.5121 0.7194 0.0187  0.0462  -0.0013 171  ILE D CB  
10226 C  CG1 . ILE D 171 ? 0.5464 0.3851 0.5731 0.0305  0.0421  0.0091  171  ILE D CG1 
10227 C  CG2 . ILE D 171 ? 0.5182 0.3126 0.5477 0.0148  0.0558  0.0040  171  ILE D CG2 
10228 C  CD1 . ILE D 171 ? 0.5864 0.4552 0.6204 0.0287  0.0361  0.0084  171  ILE D CD1 
10229 N  N   . ASP D 172 ? 0.5565 0.4397 0.6008 0.0199  0.0282  -0.0208 172  ASP D N   
10230 C  CA  . ASP D 172 ? 0.4556 0.3652 0.4995 0.0244  0.0202  -0.0219 172  ASP D CA  
10231 C  C   . ASP D 172 ? 0.4159 0.3372 0.4589 0.0295  0.0180  -0.0098 172  ASP D C   
10232 O  O   . ASP D 172 ? 0.5538 0.4852 0.6047 0.0244  0.0178  -0.0065 172  ASP D O   
10233 C  CB  . ASP D 172 ? 0.4421 0.3720 0.4953 0.0143  0.0153  -0.0316 172  ASP D CB  
10234 C  CG  . ASP D 172 ? 0.4855 0.4418 0.5367 0.0182  0.0070  -0.0313 172  ASP D CG  
10235 O  OD1 . ASP D 172 ? 0.5278 0.4902 0.5747 0.0260  0.0052  -0.0215 172  ASP D OD1 
10236 O  OD2 . ASP D 172 ? 0.5612 0.5322 0.6146 0.0126  0.0023  -0.0408 172  ASP D OD2 
10237 N  N   . LEU D 173 ? 0.3814 0.3022 0.4156 0.0397  0.0164  -0.0043 173  LEU D N   
10238 C  CA  . LEU D 173 ? 0.5825 0.5104 0.6139 0.0443  0.0148  0.0061  173  LEU D CA  
10239 C  C   . LEU D 173 ? 0.4474 0.3977 0.4855 0.0407  0.0095  0.0072  173  LEU D C   
10240 O  O   . LEU D 173 ? 0.3780 0.3316 0.4164 0.0420  0.0095  0.0143  173  LEU D O   
10241 C  CB  . LEU D 173 ? 0.5606 0.4883 0.5830 0.0547  0.0129  0.0099  173  LEU D CB  
10242 C  CG  . LEU D 173 ? 0.4121 0.3182 0.4277 0.0618  0.0172  0.0123  173  LEU D CG  
10243 C  CD1 . LEU D 173 ? 0.2311 0.1453 0.2415 0.0723  0.0139  0.0150  173  LEU D CD1 
10244 C  CD2 . LEU D 173 ? 0.5074 0.3975 0.5192 0.0606  0.0220  0.0209  173  LEU D CD2 
10245 N  N   . ASN D 174 ? 0.2763 0.2411 0.3189 0.0368  0.0051  0.0001  174  ASN D N   
10246 C  CA  . ASN D 174 ? 0.2297 0.2146 0.2786 0.0345  -0.0005 0.0025  174  ASN D CA  
10247 C  C   . ASN D 174 ? 0.3726 0.3613 0.4342 0.0275  0.0010  0.0010  174  ASN D C   
10248 O  O   . ASN D 174 ? 0.5366 0.5435 0.6063 0.0256  -0.0040 0.0013  174  ASN D O   
10249 C  CB  . ASN D 174 ? 0.2117 0.2136 0.2581 0.0340  -0.0068 -0.0025 174  ASN D CB  
10250 C  CG  . ASN D 174 ? 0.4265 0.4448 0.4730 0.0361  -0.0127 0.0050  174  ASN D CG  
10251 O  OD1 . ASN D 174 ? 0.4744 0.4892 0.5211 0.0393  -0.0117 0.0132  174  ASN D OD1 
10252 N  ND2 . ASN D 174 ? 0.4745 0.5097 0.5197 0.0341  -0.0186 0.0022  174  ASN D ND2 
10253 N  N   . ARG D 175 ? 0.3607 0.3330 0.4243 0.0239  0.0082  -0.0001 175  ARG D N   
10254 C  CA  . ARG D 175 ? 0.4589 0.4349 0.5355 0.0169  0.0119  -0.0005 175  ARG D CA  
10255 C  C   . ARG D 175 ? 0.3861 0.3473 0.4595 0.0186  0.0199  0.0071  175  ARG D C   
10256 O  O   . ARG D 175 ? 0.4912 0.4549 0.5744 0.0132  0.0250  0.0075  175  ARG D O   
10257 C  CB  . ARG D 175 ? 0.2548 0.2261 0.3380 0.0069  0.0146  -0.0103 175  ARG D CB  
10258 C  CG  . ARG D 175 ? 0.3435 0.3293 0.4282 0.0038  0.0071  -0.0198 175  ARG D CG  
10259 C  CD  . ARG D 175 ? 0.4048 0.4185 0.4959 0.0059  -0.0017 -0.0174 175  ARG D CD  
10260 N  NE  . ARG D 175 ? 0.5738 0.6025 0.6660 0.0006  -0.0085 -0.0274 175  ARG D NE  
10261 C  CZ  . ARG D 175 ? 0.5740 0.6125 0.6561 0.0046  -0.0150 -0.0290 175  ARG D CZ  
10262 N  NH1 . ARG D 175 ? 0.5839 0.6359 0.6664 -0.0018 -0.0204 -0.0396 175  ARG D NH1 
10263 N  NH2 . ARG D 175 ? 0.6796 0.7161 0.7511 0.0137  -0.0161 -0.0207 175  ARG D NH2 
10264 N  N   . ASP D 176 ? 0.3770 0.3252 0.4365 0.0261  0.0209  0.0129  176  ASP D N   
10265 C  CA  . ASP D 176 ? 0.4057 0.3372 0.4576 0.0277  0.0282  0.0196  176  ASP D CA  
10266 C  C   . ASP D 176 ? 0.4383 0.3760 0.4870 0.0324  0.0279  0.0261  176  ASP D C   
10267 O  O   . ASP D 176 ? 0.4299 0.3569 0.4715 0.0331  0.0339  0.0312  176  ASP D O   
10268 C  CB  . ASP D 176 ? 0.4846 0.3966 0.5227 0.0332  0.0294  0.0218  176  ASP D CB  
10269 C  CG  . ASP D 176 ? 0.6678 0.5594 0.6972 0.0332  0.0374  0.0289  176  ASP D CG  
10270 O  OD1 . ASP D 176 ? 0.6202 0.5075 0.6555 0.0251  0.0444  0.0289  176  ASP D OD1 
10271 O  OD2 . ASP D 176 ? 0.6453 0.5264 0.6616 0.0412  0.0368  0.0349  176  ASP D OD2 
10272 N  N   . PHE D 177 ? 0.3765 0.3301 0.4293 0.0353  0.0212  0.0258  177  PHE D N   
10273 C  CA  . PHE D 177 ? 0.3624 0.3190 0.4122 0.0394  0.0210  0.0306  177  PHE D CA  
10274 C  C   . PHE D 177 ? 0.4069 0.3705 0.4687 0.0366  0.0258  0.0301  177  PHE D C   
10275 O  O   . PHE D 177 ? 0.5882 0.5623 0.6641 0.0319  0.0259  0.0260  177  PHE D O   
10276 C  CB  . PHE D 177 ? 0.3878 0.3551 0.4363 0.0434  0.0129  0.0317  177  PHE D CB  
10277 C  CG  . PHE D 177 ? 0.4601 0.4225 0.4962 0.0472  0.0098  0.0333  177  PHE D CG  
10278 C  CD1 . PHE D 177 ? 0.5651 0.5277 0.5997 0.0472  0.0077  0.0296  177  PHE D CD1 
10279 C  CD2 . PHE D 177 ? 0.4052 0.3642 0.4320 0.0505  0.0090  0.0375  177  PHE D CD2 
10280 C  CE1 . PHE D 177 ? 0.4676 0.4286 0.4932 0.0519  0.0055  0.0308  177  PHE D CE1 
10281 C  CE2 . PHE D 177 ? 0.4613 0.4201 0.4794 0.0539  0.0059  0.0388  177  PHE D CE2 
10282 C  CZ  . PHE D 177 ? 0.4332 0.3938 0.4515 0.0552  0.0043  0.0357  177  PHE D CZ  
10283 N  N   . PRO D 178 ? 0.3959 0.3553 0.4526 0.0394  0.0300  0.0333  178  PRO D N   
10284 C  CA  . PRO D 178 ? 0.4289 0.3970 0.4982 0.0385  0.0352  0.0320  178  PRO D CA  
10285 C  C   . PRO D 178 ? 0.5172 0.5031 0.6026 0.0406  0.0285  0.0301  178  PRO D C   
10286 O  O   . PRO D 178 ? 0.3645 0.3531 0.4465 0.0445  0.0206  0.0319  178  PRO D O   
10287 C  CB  . PRO D 178 ? 0.2982 0.2580 0.3559 0.0427  0.0388  0.0345  178  PRO D CB  
10288 C  CG  . PRO D 178 ? 0.2501 0.1953 0.2883 0.0432  0.0384  0.0378  178  PRO D CG  
10289 C  CD  . PRO D 178 ? 0.3848 0.3321 0.4240 0.0432  0.0308  0.0373  178  PRO D CD  
10290 N  N   . ASP D 179 ? 0.5215 0.5208 0.6247 0.0376  0.0317  0.0271  179  ASP D N   
10291 C  CA  . ASP D 179 ? 0.4441 0.4630 0.5639 0.0402  0.0248  0.0259  179  ASP D CA  
10292 C  C   . ASP D 179 ? 0.4783 0.5020 0.6067 0.0470  0.0281  0.0272  179  ASP D C   
10293 O  O   . ASP D 179 ? 0.4288 0.4494 0.5590 0.0463  0.0381  0.0258  179  ASP D O   
10294 C  CB  . ASP D 179 ? 0.5799 0.6145 0.7165 0.0325  0.0249  0.0208  179  ASP D CB  
10295 C  CG  . ASP D 179 ? 0.6290 0.6862 0.7802 0.0349  0.0146  0.0199  179  ASP D CG  
10296 O  OD1 . ASP D 179 ? 0.6730 0.7295 0.8152 0.0391  0.0059  0.0229  179  ASP D OD1 
10297 O  OD2 . ASP D 179 ? 0.5931 0.6703 0.7646 0.0322  0.0153  0.0165  179  ASP D OD2 
10298 N  N   . ARG D 180 ? 0.4942 0.5241 0.6267 0.0540  0.0204  0.0301  180  ARG D N   
10299 C  CA  . ARG D 180 ? 0.4985 0.5312 0.6403 0.0623  0.0228  0.0312  180  ARG D CA  
10300 C  C   . ARG D 180 ? 0.5319 0.5849 0.6972 0.0621  0.0278  0.0274  180  ARG D C   
10301 O  O   . ARG D 180 ? 0.4976 0.5515 0.6704 0.0670  0.0359  0.0256  180  ARG D O   
10302 C  CB  . ARG D 180 ? 0.6334 0.6692 0.7766 0.0693  0.0123  0.0364  180  ARG D CB  
10303 C  CG  . ARG D 180 ? 0.5959 0.6516 0.7488 0.0672  0.0026  0.0373  180  ARG D CG  
10304 C  CD  . ARG D 180 ? 0.6212 0.6765 0.7684 0.0728  -0.0077 0.0443  180  ARG D CD  
10305 N  NE  . ARG D 180 ? 0.7073 0.7852 0.8645 0.0722  -0.0173 0.0453  180  ARG D NE  
10306 C  CZ  . ARG D 180 ? 0.5088 0.6058 0.6849 0.0789  -0.0219 0.0475  180  ARG D CZ  
10307 N  NH1 . ARG D 180 ? 0.4381 0.5329 0.6260 0.0876  -0.0166 0.0486  180  ARG D NH1 
10308 N  NH2 . ARG D 180 ? 0.2322 0.3516 0.4152 0.0775  -0.0318 0.0481  180  ARG D NH2 
10309 N  N   . LEU D 181 ? 0.2862 0.3570 0.4637 0.0561  0.0234  0.0252  181  LEU D N   
10310 C  CA  . LEU D 181 ? 0.2959 0.3905 0.4983 0.0542  0.0274  0.0210  181  LEU D CA  
10311 C  C   . LEU D 181 ? 0.4365 0.5259 0.6377 0.0442  0.0402  0.0168  181  LEU D C   
10312 O  O   . LEU D 181 ? 0.4573 0.5550 0.6708 0.0452  0.0502  0.0145  181  LEU D O   
10313 C  CB  . LEU D 181 ? 0.2761 0.3937 0.4919 0.0503  0.0166  0.0194  181  LEU D CB  
10314 C  CG  . LEU D 181 ? 0.2915 0.4109 0.5013 0.0581  0.0033  0.0252  181  LEU D CG  
10315 C  CD1 . LEU D 181 ? 0.2526 0.3935 0.4701 0.0522  -0.0072 0.0225  181  LEU D CD1 
10316 C  CD2 . LEU D 181 ? 0.2890 0.4146 0.5104 0.0719  0.0016  0.0301  181  LEU D CD2 
10317 N  N   . ALA D 191 ? 1.0683 0.9499 1.0026 0.0533  0.0490  0.0680  191  ALA D N   
10318 C  CA  . ALA D 191 ? 0.9442 0.8148 0.8844 0.0524  0.0515  0.0710  191  ALA D CA  
10319 C  C   . ALA D 191 ? 1.1072 0.9722 1.0533 0.0444  0.0630  0.0709  191  ALA D C   
10320 O  O   . ALA D 191 ? 1.0221 0.8953 0.9717 0.0405  0.0686  0.0674  191  ALA D O   
10321 C  CB  . ALA D 191 ? 0.7881 0.6456 0.7121 0.0586  0.0492  0.0801  191  ALA D CB  
10322 N  N   . GLN D 192 ? 1.1757 1.0264 1.1234 0.0419  0.0668  0.0746  192  GLN D N   
10323 C  CA  . GLN D 192 ? 1.4339 1.2782 1.3888 0.0324  0.0779  0.0748  192  GLN D CA  
10324 C  C   . GLN D 192 ? 1.3226 1.1484 1.2786 0.0316  0.0781  0.0776  192  GLN D C   
10325 O  O   . GLN D 192 ? 1.4626 1.2758 1.4055 0.0397  0.0734  0.0838  192  GLN D O   
10326 C  CB  . GLN D 192 ? 1.7259 1.5889 1.7041 0.0266  0.0789  0.0648  192  GLN D CB  
10327 C  CG  . GLN D 192 ? 1.8037 1.6671 1.7932 0.0157  0.0906  0.0637  192  GLN D CG  
10328 C  CD  . GLN D 192 ? 1.7613 1.6427 1.7770 0.0107  0.0884  0.0540  192  GLN D CD  
10329 O  OE1 . GLN D 192 ? 1.7034 1.6039 1.7302 0.0126  0.0865  0.0489  192  GLN D OE1 
10330 N  NE2 . GLN D 192 ? 1.7684 1.6434 1.7936 0.0044  0.0882  0.0513  192  GLN D NE2 
10331 N  N   . SER D 193 ? 0.9760 0.8005 0.9481 0.0222  0.0834  0.0725  193  SER D N   
10332 C  CA  . SER D 193 ? 0.7559 0.5647 0.7325 0.0214  0.0817  0.0708  193  SER D CA  
10333 C  C   . SER D 193 ? 0.5800 0.4054 0.5696 0.0255  0.0711  0.0609  193  SER D C   
10334 O  O   . SER D 193 ? 0.5985 0.4233 0.6008 0.0205  0.0700  0.0532  193  SER D O   
10335 C  CB  . SER D 193 ? 0.7647 0.5641 0.7520 0.0076  0.0919  0.0687  193  SER D CB  
10336 O  OG  . SER D 193 ? 0.6245 0.3943 0.6035 0.0073  0.0950  0.0736  193  SER D OG  
10337 N  N   . ARG D 194 ? 0.5179 0.3583 0.5035 0.0337  0.0634  0.0608  194  ARG D N   
10338 C  CA  . ARG D 194 ? 0.5951 0.4491 0.5882 0.0389  0.0533  0.0542  194  ARG D CA  
10339 C  C   . ARG D 194 ? 0.7032 0.5457 0.6853 0.0488  0.0484  0.0578  194  ARG D C   
10340 O  O   . ARG D 194 ? 0.7537 0.5841 0.7208 0.0544  0.0497  0.0667  194  ARG D O   
10341 C  CB  . ARG D 194 ? 0.4132 0.2877 0.4081 0.0420  0.0479  0.0526  194  ARG D CB  
10342 C  CG  . ARG D 194 ? 0.4728 0.3599 0.4794 0.0353  0.0523  0.0490  194  ARG D CG  
10343 C  CD  . ARG D 194 ? 0.5957 0.5007 0.6075 0.0388  0.0458  0.0459  194  ARG D CD  
10344 N  NE  . ARG D 194 ? 0.7293 0.6434 0.7493 0.0353  0.0512  0.0441  194  ARG D NE  
10345 C  CZ  . ARG D 194 ? 0.7389 0.6630 0.7765 0.0295  0.0544  0.0396  194  ARG D CZ  
10346 N  NH1 . ARG D 194 ? 0.5738 0.4991 0.6210 0.0251  0.0521  0.0359  194  ARG D NH1 
10347 N  NH2 . ARG D 194 ? 0.8357 0.7699 0.8820 0.0281  0.0598  0.0381  194  ARG D NH2 
10348 N  N   . GLN D 195 ? 0.6210 0.4693 0.6108 0.0516  0.0426  0.0509  195  GLN D N   
10349 C  CA  . GLN D 195 ? 0.5016 0.3411 0.4845 0.0618  0.0387  0.0527  195  GLN D CA  
10350 C  C   . GLN D 195 ? 0.4762 0.3270 0.4499 0.0709  0.0324  0.0583  195  GLN D C   
10351 O  O   . GLN D 195 ? 0.4202 0.2887 0.3957 0.0689  0.0291  0.0572  195  GLN D O   
10352 C  CB  . GLN D 195 ? 0.4920 0.3379 0.4851 0.0619  0.0350  0.0423  195  GLN D CB  
10353 C  CG  . GLN D 195 ? 0.6184 0.4530 0.6200 0.0519  0.0404  0.0352  195  GLN D CG  
10354 C  CD  . GLN D 195 ? 0.6972 0.5009 0.6916 0.0512  0.0482  0.0406  195  GLN D CD  
10355 O  OE1 . GLN D 195 ? 0.7555 0.5420 0.7440 0.0597  0.0481  0.0415  195  GLN D OE1 
10356 N  NE2 . GLN D 195 ? 0.4668 0.2628 0.4618 0.0413  0.0555  0.0444  195  GLN D NE2 
10357 N  N   . PRO D 196 ? 0.5654 0.4056 0.5298 0.0811  0.0307  0.0643  196  PRO D N   
10358 C  CA  . PRO D 196 ? 0.5219 0.3744 0.4783 0.0903  0.0239  0.0696  196  PRO D CA  
10359 C  C   . PRO D 196 ? 0.5274 0.4058 0.4928 0.0899  0.0171  0.0626  196  PRO D C   
10360 O  O   . PRO D 196 ? 0.5801 0.4735 0.5415 0.0908  0.0123  0.0647  196  PRO D O   
10361 C  CB  . PRO D 196 ? 0.4341 0.2735 0.3868 0.1024  0.0226  0.0734  196  PRO D CB  
10362 C  CG  . PRO D 196 ? 0.4947 0.3059 0.4464 0.0986  0.0308  0.0744  196  PRO D CG  
10363 C  CD  . PRO D 196 ? 0.4154 0.2308 0.3779 0.0847  0.0350  0.0656  196  PRO D CD  
10364 N  N   . GLU D 197 ? 0.3251 0.2080 0.3015 0.0879  0.0168  0.0541  197  GLU D N   
10365 C  CA  . GLU D 197 ? 0.3653 0.2711 0.3489 0.0876  0.0112  0.0486  197  GLU D CA  
10366 C  C   . GLU D 197 ? 0.4070 0.3233 0.3944 0.0783  0.0109  0.0470  197  GLU D C   
10367 O  O   . GLU D 197 ? 0.3921 0.3240 0.3798 0.0776  0.0064  0.0473  197  GLU D O   
10368 C  CB  . GLU D 197 ? 0.3102 0.2171 0.3016 0.0889  0.0115  0.0402  197  GLU D CB  
10369 C  CG  . GLU D 197 ? 0.3747 0.2712 0.3633 0.1006  0.0120  0.0411  197  GLU D CG  
10370 C  CD  . GLU D 197 ? 0.5100 0.3771 0.4953 0.1010  0.0184  0.0425  197  GLU D CD  
10371 O  OE1 . GLU D 197 ? 0.5131 0.3673 0.4968 0.1111  0.0195  0.0426  197  GLU D OE1 
10372 O  OE2 . GLU D 197 ? 0.6282 0.4845 0.6131 0.0912  0.0228  0.0432  197  GLU D OE2 
10373 N  N   . THR D 198 ? 0.4436 0.3507 0.4346 0.0712  0.0160  0.0454  198  THR D N   
10374 C  CA  . THR D 198 ? 0.4863 0.4024 0.4824 0.0640  0.0164  0.0442  198  THR D CA  
10375 C  C   . THR D 198 ? 0.4624 0.3787 0.4495 0.0647  0.0167  0.0497  198  THR D C   
10376 O  O   . THR D 198 ? 0.4634 0.3912 0.4519 0.0631  0.0135  0.0489  198  THR D O   
10377 C  CB  . THR D 198 ? 0.5690 0.4775 0.5726 0.0566  0.0225  0.0414  198  THR D CB  
10378 O  OG1 . THR D 198 ? 0.6162 0.5227 0.6265 0.0549  0.0222  0.0349  198  THR D OG1 
10379 C  CG2 . THR D 198 ? 0.4110 0.3324 0.4231 0.0515  0.0221  0.0395  198  THR D CG2 
10380 N  N   . ALA D 199 ? 0.2726 0.1750 0.2492 0.0669  0.0207  0.0553  199  ALA D N   
10381 C  CA  . ALA D 199 ? 0.3020 0.2042 0.2671 0.0673  0.0214  0.0599  199  ALA D CA  
10382 C  C   . ALA D 199 ? 0.4681 0.3837 0.4289 0.0712  0.0135  0.0601  199  ALA D C   
10383 O  O   . ALA D 199 ? 0.4288 0.3509 0.3860 0.0684  0.0123  0.0592  199  ALA D O   
10384 C  CB  . ALA D 199 ? 0.2573 0.1427 0.2093 0.0699  0.0261  0.0673  199  ALA D CB  
10385 N  N   . ALA D 200 ? 0.4425 0.3626 0.4047 0.0775  0.0087  0.0607  200  ALA D N   
10386 C  CA  . ALA D 200 ? 0.3966 0.3329 0.3573 0.0807  0.0013  0.0607  200  ALA D CA  
10387 C  C   . ALA D 200 ? 0.4628 0.4121 0.4317 0.0742  -0.0010 0.0556  200  ALA D C   
10388 O  O   . ALA D 200 ? 0.4110 0.3678 0.3759 0.0712  -0.0040 0.0554  200  ALA D O   
10389 C  CB  . ALA D 200 ? 0.3161 0.2573 0.2808 0.0889  -0.0019 0.0610  200  ALA D CB  
10390 N  N   . LEU D 201 ? 0.2455 0.1963 0.2249 0.0717  0.0003  0.0517  201  LEU D N   
10391 C  CA  . LEU D 201 ? 0.3607 0.3221 0.3471 0.0664  -0.0020 0.0487  201  LEU D CA  
10392 C  C   . LEU D 201 ? 0.4535 0.4101 0.4393 0.0612  0.0004  0.0484  201  LEU D C   
10393 O  O   . LEU D 201 ? 0.4641 0.4261 0.4492 0.0581  -0.0022 0.0479  201  LEU D O   
10394 C  CB  . LEU D 201 ? 0.3458 0.3120 0.3415 0.0656  -0.0022 0.0450  201  LEU D CB  
10395 C  CG  . LEU D 201 ? 0.3737 0.3539 0.3707 0.0688  -0.0062 0.0441  201  LEU D CG  
10396 C  CD1 . LEU D 201 ? 0.3761 0.3517 0.3709 0.0768  -0.0053 0.0441  201  LEU D CD1 
10397 C  CD2 . LEU D 201 ? 0.5783 0.5692 0.5819 0.0654  -0.0076 0.0409  201  LEU D CD2 
10398 N  N   . VAL D 202 ? 0.3116 0.2578 0.2984 0.0601  0.0062  0.0482  202  VAL D N   
10399 C  CA  . VAL D 202 ? 0.2635 0.2061 0.2507 0.0567  0.0098  0.0472  202  VAL D CA  
10400 C  C   . VAL D 202 ? 0.5081 0.4502 0.4839 0.0563  0.0081  0.0477  202  VAL D C   
10401 O  O   . VAL D 202 ? 0.4264 0.3709 0.4038 0.0535  0.0064  0.0455  202  VAL D O   
10402 C  CB  . VAL D 202 ? 0.3562 0.2891 0.3438 0.0556  0.0176  0.0475  202  VAL D CB  
10403 C  CG1 . VAL D 202 ? 0.1642 0.0940 0.1494 0.0537  0.0227  0.0462  202  VAL D CG1 
10404 C  CG2 . VAL D 202 ? 0.2102 0.1459 0.2117 0.0536  0.0189  0.0450  202  VAL D CG2 
10405 N  N   . ASN D 203 ? 0.3305 0.2690 0.2942 0.0589  0.0083  0.0506  203  ASN D N   
10406 C  CA  . ASN D 203 ? 0.3157 0.2565 0.2670 0.0581  0.0054  0.0505  203  ASN D CA  
10407 C  C   . ASN D 203 ? 0.3152 0.2669 0.2704 0.0552  -0.0011 0.0479  203  ASN D C   
10408 O  O   . ASN D 203 ? 0.4687 0.4192 0.4202 0.0507  -0.0015 0.0444  203  ASN D O   
10409 C  CB  . ASN D 203 ? 0.3926 0.3335 0.3325 0.0632  0.0030  0.0555  203  ASN D CB  
10410 C  CG  . ASN D 203 ? 0.5715 0.4998 0.5000 0.0642  0.0096  0.0590  203  ASN D CG  
10411 O  OD1 . ASN D 203 ? 0.6388 0.5592 0.5717 0.0613  0.0170  0.0576  203  ASN D OD1 
10412 N  ND2 . ASN D 203 ? 0.7234 0.6512 0.6372 0.0684  0.0070  0.0643  203  ASN D ND2 
10413 N  N   . TRP D 204 ? 0.3304 0.2920 0.2925 0.0573  -0.0055 0.0493  204  TRP D N   
10414 C  CA  . TRP D 204 ? 0.3141 0.2882 0.2804 0.0536  -0.0110 0.0478  204  TRP D CA  
10415 C  C   . TRP D 204 ? 0.4904 0.4603 0.4631 0.0479  -0.0095 0.0456  204  TRP D C   
10416 O  O   . TRP D 204 ? 0.5303 0.5002 0.5004 0.0424  -0.0113 0.0434  204  TRP D O   
10417 C  CB  . TRP D 204 ? 0.2789 0.2651 0.2527 0.0576  -0.0139 0.0493  204  TRP D CB  
10418 C  CG  . TRP D 204 ? 0.3243 0.3273 0.3020 0.0540  -0.0189 0.0486  204  TRP D CG  
10419 C  CD1 . TRP D 204 ? 0.3289 0.3414 0.3020 0.0505  -0.0232 0.0477  204  TRP D CD1 
10420 C  CD2 . TRP D 204 ? 0.3754 0.3898 0.3622 0.0524  -0.0198 0.0484  204  TRP D CD2 
10421 N  NE1 . TRP D 204 ? 0.3733 0.4027 0.3539 0.0463  -0.0263 0.0472  204  TRP D NE1 
10422 C  CE2 . TRP D 204 ? 0.3363 0.3668 0.3246 0.0475  -0.0239 0.0479  204  TRP D CE2 
10423 C  CE3 . TRP D 204 ? 0.2248 0.2386 0.2179 0.0538  -0.0176 0.0481  204  TRP D CE3 
10424 C  CZ2 . TRP D 204 ? 0.2126 0.2581 0.2085 0.0441  -0.0246 0.0481  204  TRP D CZ2 
10425 C  CZ3 . TRP D 204 ? 0.2950 0.3235 0.2937 0.0511  -0.0190 0.0481  204  TRP D CZ3 
10426 C  CH2 . TRP D 204 ? 0.3026 0.3464 0.3025 0.0464  -0.0219 0.0485  204  TRP D CH2 
10427 N  N   . ILE D 205 ? 0.3980 0.3638 0.3790 0.0494  -0.0065 0.0461  205  ILE D N   
10428 C  CA  . ILE D 205 ? 0.4123 0.3758 0.4006 0.0461  -0.0063 0.0458  205  ILE D CA  
10429 C  C   . ILE D 205 ? 0.5894 0.5415 0.5737 0.0435  -0.0036 0.0432  205  ILE D C   
10430 O  O   . ILE D 205 ? 0.6685 0.6173 0.6551 0.0399  -0.0049 0.0430  205  ILE D O   
10431 C  CB  . ILE D 205 ? 0.3649 0.3281 0.3627 0.0488  -0.0041 0.0464  205  ILE D CB  
10432 C  CG1 . ILE D 205 ? 0.3014 0.2748 0.3025 0.0505  -0.0067 0.0471  205  ILE D CG1 
10433 C  CG2 . ILE D 205 ? 0.4352 0.3960 0.4402 0.0473  -0.0045 0.0474  205  ILE D CG2 
10434 C  CD1 . ILE D 205 ? 0.3202 0.2935 0.3291 0.0521  -0.0048 0.0460  205  ILE D CD1 
10435 N  N   . VAL D 206 ? 0.4968 0.4419 0.4743 0.0454  0.0008  0.0411  206  VAL D N   
10436 C  CA  . VAL D 206 ? 0.4822 0.4164 0.4548 0.0438  0.0050  0.0368  206  VAL D CA  
10437 C  C   . VAL D 206 ? 0.4367 0.3710 0.3962 0.0394  0.0021  0.0337  206  VAL D C   
10438 O  O   . VAL D 206 ? 0.4663 0.3912 0.4189 0.0369  0.0050  0.0283  206  VAL D O   
10439 C  CB  . VAL D 206 ? 0.3931 0.3214 0.3637 0.0471  0.0125  0.0356  206  VAL D CB  
10440 C  CG1 . VAL D 206 ? 0.2042 0.1348 0.1896 0.0500  0.0151  0.0375  206  VAL D CG1 
10441 C  CG2 . VAL D 206 ? 0.4626 0.3932 0.4218 0.0485  0.0126  0.0381  206  VAL D CG2 
10442 N  N   . SER D 207 ? 0.4016 0.3476 0.3582 0.0387  -0.0038 0.0361  207  SER D N   
10443 C  CA  . SER D 207 ? 0.4021 0.3535 0.3475 0.0345  -0.0080 0.0333  207  SER D CA  
10444 C  C   . SER D 207 ? 0.4043 0.3576 0.3527 0.0263  -0.0118 0.0303  207  SER D C   
10445 O  O   . SER D 207 ? 0.5862 0.5414 0.5258 0.0203  -0.0147 0.0255  207  SER D O   
10446 C  CB  . SER D 207 ? 0.2982 0.2639 0.2406 0.0387  -0.0129 0.0376  207  SER D CB  
10447 O  OG  . SER D 207 ? 0.4126 0.3927 0.3639 0.0367  -0.0183 0.0392  207  SER D OG  
10448 N  N   . LYS D 208 ? 0.4039 0.3568 0.3638 0.0252  -0.0120 0.0333  208  LYS D N   
10449 C  CA  . LYS D 208 ? 0.4619 0.4144 0.4249 0.0165  -0.0146 0.0323  208  LYS D CA  
10450 C  C   . LYS D 208 ? 0.4372 0.3770 0.4084 0.0173  -0.0115 0.0352  208  LYS D C   
10451 O  O   . LYS D 208 ? 0.6548 0.5952 0.6325 0.0242  -0.0096 0.0390  208  LYS D O   
10452 C  CB  . LYS D 208 ? 0.4588 0.4319 0.4266 0.0134  -0.0200 0.0356  208  LYS D CB  
10453 C  CG  . LYS D 208 ? 0.5312 0.5202 0.4928 0.0139  -0.0244 0.0335  208  LYS D CG  
10454 C  CD  . LYS D 208 ? 0.5780 0.5906 0.5472 0.0115  -0.0292 0.0361  208  LYS D CD  
10455 C  CE  . LYS D 208 ? 0.5721 0.6018 0.5359 0.0104  -0.0351 0.0332  208  LYS D CE  
10456 N  NZ  . LYS D 208 ? 0.6707 0.7275 0.6445 0.0089  -0.0396 0.0349  208  LYS D NZ  
10457 N  N   . PRO D 209 ? 0.3138 0.2418 0.2848 0.0101  -0.0114 0.0335  209  PRO D N   
10458 C  CA  . PRO D 209 ? 0.2777 0.1908 0.2554 0.0114  -0.0090 0.0373  209  PRO D CA  
10459 C  C   . PRO D 209 ? 0.4205 0.3440 0.4055 0.0104  -0.0119 0.0461  209  PRO D C   
10460 O  O   . PRO D 209 ? 0.5230 0.4379 0.5095 0.0046  -0.0123 0.0500  209  PRO D O   
10461 C  CB  . PRO D 209 ? 0.2054 0.1015 0.1780 0.0024  -0.0082 0.0323  209  PRO D CB  
10462 C  CG  . PRO D 209 ? 0.4354 0.3470 0.4030 -0.0069 -0.0126 0.0292  209  PRO D CG  
10463 C  CD  . PRO D 209 ? 0.2627 0.1911 0.2268 -0.0003 -0.0140 0.0279  209  PRO D CD  
10464 N  N   . PHE D 210 ? 0.2927 0.2329 0.2812 0.0158  -0.0133 0.0490  210  PHE D N   
10465 C  CA  . PHE D 210 ? 0.3828 0.3345 0.3763 0.0153  -0.0155 0.0560  210  PHE D CA  
10466 C  C   . PHE D 210 ? 0.4572 0.3964 0.4546 0.0166  -0.0149 0.0623  210  PHE D C   
10467 O  O   . PHE D 210 ? 0.5077 0.4361 0.5087 0.0237  -0.0130 0.0619  210  PHE D O   
10468 C  CB  . PHE D 210 ? 0.2415 0.2085 0.2380 0.0223  -0.0161 0.0563  210  PHE D CB  
10469 C  CG  . PHE D 210 ? 0.2057 0.1873 0.1993 0.0220  -0.0176 0.0530  210  PHE D CG  
10470 C  CD1 . PHE D 210 ? 0.1945 0.1744 0.1846 0.0273  -0.0165 0.0491  210  PHE D CD1 
10471 C  CD2 . PHE D 210 ? 0.3005 0.2984 0.2952 0.0167  -0.0200 0.0545  210  PHE D CD2 
10472 C  CE1 . PHE D 210 ? 0.3373 0.3302 0.3247 0.0288  -0.0187 0.0476  210  PHE D CE1 
10473 C  CE2 . PHE D 210 ? 0.4180 0.4317 0.4122 0.0182  -0.0219 0.0517  210  PHE D CE2 
10474 C  CZ  . PHE D 210 ? 0.4500 0.4605 0.4403 0.0250  -0.0217 0.0486  210  PHE D CZ  
10475 N  N   . VAL D 211 ? 0.3349 0.2770 0.3318 0.0100  -0.0166 0.0686  211  VAL D N   
10476 C  CA  . VAL D 211 ? 0.3475 0.2769 0.3459 0.0105  -0.0168 0.0770  211  VAL D CA  
10477 C  C   . VAL D 211 ? 0.3800 0.3232 0.3813 0.0164  -0.0191 0.0833  211  VAL D C   
10478 O  O   . VAL D 211 ? 0.4732 0.4098 0.4786 0.0239  -0.0200 0.0872  211  VAL D O   
10479 C  CB  . VAL D 211 ? 0.2764 0.1994 0.2707 -0.0014 -0.0167 0.0818  211  VAL D CB  
10480 C  CG1 . VAL D 211 ? 0.2879 0.1972 0.2819 -0.0002 -0.0172 0.0931  211  VAL D CG1 
10481 C  CG2 . VAL D 211 ? 0.3111 0.2179 0.3022 -0.0083 -0.0147 0.0741  211  VAL D CG2 
10482 N  N   . LEU D 212 ? 0.2384 0.2023 0.2380 0.0134  -0.0203 0.0835  212  LEU D N   
10483 C  CA  . LEU D 212 ? 0.2799 0.2586 0.2798 0.0171  -0.0224 0.0882  212  LEU D CA  
10484 C  C   . LEU D 212 ? 0.2537 0.2519 0.2546 0.0194  -0.0222 0.0813  212  LEU D C   
10485 O  O   . LEU D 212 ? 0.5007 0.5047 0.5010 0.0164  -0.0210 0.0763  212  LEU D O   
10486 C  CB  . LEU D 212 ? 0.2463 0.2283 0.2408 0.0096  -0.0230 0.0978  212  LEU D CB  
10487 C  CG  . LEU D 212 ? 0.3754 0.3758 0.3661 0.0107  -0.0248 0.1027  212  LEU D CG  
10488 C  CD1 . LEU D 212 ? 0.5239 0.5229 0.5173 0.0200  -0.0284 0.1050  212  LEU D CD1 
10489 C  CD2 . LEU D 212 ? 0.3227 0.3238 0.3060 0.0016  -0.0240 0.1134  212  LEU D CD2 
10490 N  N   . SER D 213 ? 0.3311 0.3391 0.3334 0.0250  -0.0237 0.0808  213  SER D N   
10491 C  CA  . SER D 213 ? 0.3212 0.3427 0.3247 0.0284  -0.0229 0.0733  213  SER D CA  
10492 C  C   . SER D 213 ? 0.4689 0.5033 0.4714 0.0309  -0.0247 0.0735  213  SER D C   
10493 O  O   . SER D 213 ? 0.4869 0.5197 0.4891 0.0319  -0.0276 0.0790  213  SER D O   
10494 C  CB  . SER D 213 ? 0.3366 0.3485 0.3445 0.0338  -0.0214 0.0671  213  SER D CB  
10495 O  OG  . SER D 213 ? 0.5536 0.5742 0.5621 0.0374  -0.0204 0.0608  213  SER D OG  
10496 N  N   . ALA D 214 ? 0.4231 0.4704 0.4248 0.0324  -0.0233 0.0670  214  ALA D N   
10497 C  CA  . ALA D 214 ? 0.3995 0.4583 0.3995 0.0347  -0.0246 0.0637  214  ALA D CA  
10498 C  C   . ALA D 214 ? 0.3076 0.3702 0.3097 0.0389  -0.0220 0.0538  214  ALA D C   
10499 O  O   . ALA D 214 ? 0.3587 0.4234 0.3613 0.0397  -0.0195 0.0514  214  ALA D O   
10500 C  CB  . ALA D 214 ? 0.3131 0.3864 0.3054 0.0301  -0.0250 0.0686  214  ALA D CB  
10501 N  N   . ASN D 215 ? 0.4143 0.4770 0.4181 0.0416  -0.0228 0.0480  215  ASN D N   
10502 C  CA  . ASN D 215 ? 0.4457 0.5097 0.4503 0.0454  -0.0199 0.0384  215  ASN D CA  
10503 C  C   . ASN D 215 ? 0.3820 0.4578 0.3824 0.0447  -0.0207 0.0322  215  ASN D C   
10504 O  O   . ASN D 215 ? 0.4503 0.5307 0.4494 0.0421  -0.0246 0.0340  215  ASN D O   
10505 C  CB  . ASN D 215 ? 0.4724 0.5205 0.4827 0.0487  -0.0181 0.0347  215  ASN D CB  
10506 C  CG  . ASN D 215 ? 0.4595 0.5035 0.4747 0.0474  -0.0198 0.0327  215  ASN D CG  
10507 O  OD1 . ASN D 215 ? 0.4755 0.5169 0.4927 0.0478  -0.0185 0.0249  215  ASN D OD1 
10508 N  ND2 . ASN D 215 ? 0.4282 0.4710 0.4463 0.0457  -0.0226 0.0393  215  ASN D ND2 
10509 N  N   . PHE D 216 ? 0.3076 0.3894 0.3058 0.0476  -0.0172 0.0246  216  PHE D N   
10510 C  CA  . PHE D 216 ? 0.1182 0.2140 0.1097 0.0466  -0.0168 0.0179  216  PHE D CA  
10511 C  C   . PHE D 216 ? 0.3676 0.4560 0.3608 0.0491  -0.0153 0.0056  216  PHE D C   
10512 O  O   . PHE D 216 ? 0.3276 0.4022 0.3258 0.0538  -0.0120 0.0015  216  PHE D O   
10513 C  CB  . PHE D 216 ? 0.3080 0.4188 0.2957 0.0477  -0.0128 0.0175  216  PHE D CB  
10514 C  CG  . PHE D 216 ? 0.2882 0.4057 0.2744 0.0429  -0.0137 0.0293  216  PHE D CG  
10515 C  CD1 . PHE D 216 ? 0.3433 0.4534 0.3358 0.0435  -0.0133 0.0344  216  PHE D CD1 
10516 C  CD2 . PHE D 216 ? 0.2875 0.4174 0.2651 0.0370  -0.0153 0.0354  216  PHE D CD2 
10517 C  CE1 . PHE D 216 ? 0.2951 0.4091 0.2865 0.0374  -0.0139 0.0441  216  PHE D CE1 
10518 C  CE2 . PHE D 216 ? 0.3724 0.5047 0.3485 0.0315  -0.0156 0.0469  216  PHE D CE2 
10519 C  CZ  . PHE D 216 ? 0.3519 0.4756 0.3355 0.0312  -0.0147 0.0505  216  PHE D CZ  
10520 N  N   . HIS D 217 ? 0.3786 0.4758 0.3665 0.0455  -0.0179 -0.0001 217  HIS D N   
10521 C  CA  . HIS D 217 ? 0.4296 0.5200 0.4185 0.0453  -0.0169 -0.0131 217  HIS D CA  
10522 C  C   . HIS D 217 ? 0.4414 0.5476 0.4197 0.0437  -0.0163 -0.0230 217  HIS D C   
10523 O  O   . HIS D 217 ? 0.4128 0.5358 0.3828 0.0427  -0.0163 -0.0183 217  HIS D O   
10524 C  CB  . HIS D 217 ? 0.3623 0.4480 0.3575 0.0404  -0.0220 -0.0119 217  HIS D CB  
10525 C  CG  . HIS D 217 ? 0.3655 0.4350 0.3707 0.0420  -0.0210 -0.0047 217  HIS D CG  
10526 N  ND1 . HIS D 217 ? 0.4014 0.4547 0.4139 0.0416  -0.0182 -0.0103 217  HIS D ND1 
10527 C  CD2 . HIS D 217 ? 0.4205 0.4872 0.4285 0.0435  -0.0217 0.0071  217  HIS D CD2 
10528 C  CE1 . HIS D 217 ? 0.4160 0.4589 0.4346 0.0431  -0.0171 -0.0019 217  HIS D CE1 
10529 N  NE2 . HIS D 217 ? 0.3906 0.4411 0.4065 0.0445  -0.0194 0.0079  217  HIS D NE2 
10530 N  N   . GLY D 218 ? 0.4769 0.5770 0.4547 0.0425  -0.0151 -0.0371 218  GLY D N   
10531 C  CA  . GLY D 218 ? 0.3623 0.4755 0.3289 0.0407  -0.0140 -0.0498 218  GLY D CA  
10532 C  C   . GLY D 218 ? 0.3567 0.4691 0.3228 0.0335  -0.0187 -0.0601 218  GLY D C   
10533 O  O   . GLY D 218 ? 0.3796 0.4784 0.3565 0.0309  -0.0206 -0.0595 218  GLY D O   
10534 N  N   . GLY D 219 ? 0.3471 0.4763 0.3006 0.0294  -0.0206 -0.0699 219  GLY D N   
10535 C  CA  . GLY D 219 ? 0.3994 0.5325 0.3513 0.0213  -0.0261 -0.0813 219  GLY D CA  
10536 C  C   . GLY D 219 ? 0.5975 0.7570 0.5389 0.0159  -0.0352 -0.0752 219  GLY D C   
10537 O  O   . GLY D 219 ? 0.7766 0.9476 0.7123 0.0090  -0.0409 -0.0858 219  GLY D O   
10538 N  N   . ALA D 220 ? 0.5435 0.7127 0.4816 0.0189  -0.0369 -0.0577 220  ALA D N   
10539 C  CA  . ALA D 220 ? 0.5936 0.7851 0.5217 0.0152  -0.0459 -0.0476 220  ALA D CA  
10540 C  C   . ALA D 220 ? 0.5599 0.7560 0.4828 0.0188  -0.0438 -0.0298 220  ALA D C   
10541 O  O   . ALA D 220 ? 0.5829 0.7661 0.5127 0.0234  -0.0367 -0.0258 220  ALA D O   
10542 C  CB  . ALA D 220 ? 0.5628 0.7548 0.5037 0.0124  -0.0551 -0.0415 220  ALA D CB  
10543 N  N   . VAL D 221 ? 0.4727 0.6868 0.3831 0.0162  -0.0503 -0.0185 221  VAL D N   
10544 C  CA  . VAL D 221 ? 0.5310 0.7485 0.4348 0.0177  -0.0477 -0.0014 221  VAL D CA  
10545 C  C   . VAL D 221 ? 0.5625 0.7810 0.4687 0.0178  -0.0567 0.0176  221  VAL D C   
10546 O  O   . VAL D 221 ? 0.5700 0.8051 0.4634 0.0155  -0.0645 0.0234  221  VAL D O   
10547 C  CB  . VAL D 221 ? 0.4853 0.7229 0.3672 0.0149  -0.0440 -0.0043 221  VAL D CB  
10548 C  CG1 . VAL D 221 ? 0.4327 0.6713 0.3107 0.0152  -0.0377 0.0104  221  VAL D CG1 
10549 C  CG2 . VAL D 221 ? 0.3962 0.6341 0.2756 0.0156  -0.0365 -0.0266 221  VAL D CG2 
10550 N  N   . VAL D 222 ? 0.4970 0.6976 0.4187 0.0213  -0.0557 0.0272  222  VAL D N   
10551 C  CA  . VAL D 222 ? 0.4528 0.6499 0.3806 0.0232  -0.0634 0.0434  222  VAL D CA  
10552 C  C   . VAL D 222 ? 0.5922 0.7675 0.5344 0.0267  -0.0593 0.0524  222  VAL D C   
10553 O  O   . VAL D 222 ? 0.6018 0.7644 0.5536 0.0279  -0.0525 0.0441  222  VAL D O   
10554 C  CB  . VAL D 222 ? 0.4581 0.6611 0.3959 0.0235  -0.0721 0.0372  222  VAL D CB  
10555 C  CG1 . VAL D 222 ? 0.4047 0.5917 0.3609 0.0244  -0.0674 0.0251  222  VAL D CG1 
10556 C  CG2 . VAL D 222 ? 0.5081 0.7131 0.4512 0.0273  -0.0811 0.0541  222  VAL D CG2 
10557 N  N   . ALA D 223 ? 0.4853 0.6558 0.4280 0.0285  -0.0635 0.0692  223  ALA D N   
10558 C  CA  . ALA D 223 ? 0.4544 0.6042 0.4096 0.0314  -0.0604 0.0770  223  ALA D CA  
10559 C  C   . ALA D 223 ? 0.5079 0.6514 0.4794 0.0363  -0.0658 0.0779  223  ALA D C   
10560 O  O   . ALA D 223 ? 0.5190 0.6681 0.4904 0.0393  -0.0735 0.0882  223  ALA D O   
10561 C  CB  . ALA D 223 ? 0.2996 0.4438 0.2456 0.0300  -0.0597 0.0944  223  ALA D CB  
10562 N  N   . SER D 224 ? 0.4136 0.5461 0.3989 0.0375  -0.0614 0.0680  224  SER D N   
10563 C  CA  . SER D 224 ? 0.2860 0.4148 0.2883 0.0411  -0.0645 0.0662  224  SER D CA  
10564 C  C   . SER D 224 ? 0.3233 0.4317 0.3357 0.0449  -0.0602 0.0726  224  SER D C   
10565 O  O   . SER D 224 ? 0.3171 0.4122 0.3271 0.0435  -0.0533 0.0713  224  SER D O   
10566 C  CB  . SER D 224 ? 0.3443 0.4757 0.3538 0.0383  -0.0620 0.0497  224  SER D CB  
10567 O  OG  . SER D 224 ? 0.5599 0.6907 0.5865 0.0401  -0.0639 0.0472  224  SER D OG  
10568 N  N   . TYR D 225 ? 0.3189 0.4263 0.3427 0.0500  -0.0644 0.0788  225  TYR D N   
10569 C  CA  . TYR D 225 ? 0.1843 0.2726 0.2167 0.0544  -0.0606 0.0846  225  TYR D CA  
10570 C  C   . TYR D 225 ? 0.2760 0.3666 0.3272 0.0590  -0.0614 0.0806  225  TYR D C   
10571 O  O   . TYR D 225 ? 0.3586 0.4677 0.4170 0.0594  -0.0673 0.0772  225  TYR D O   
10572 C  CB  . TYR D 225 ? 0.3243 0.4058 0.3500 0.0576  -0.0640 0.1001  225  TYR D CB  
10573 C  CG  . TYR D 225 ? 0.3023 0.4003 0.3279 0.0621  -0.0740 0.1086  225  TYR D CG  
10574 C  CD1 . TYR D 225 ? 0.3546 0.4692 0.3648 0.0583  -0.0792 0.1116  225  TYR D CD1 
10575 C  CD2 . TYR D 225 ? 0.3748 0.4737 0.4156 0.0707  -0.0785 0.1135  225  TYR D CD2 
10576 C  CE1 . TYR D 225 ? 0.4477 0.5792 0.4561 0.0625  -0.0894 0.1199  225  TYR D CE1 
10577 C  CE2 . TYR D 225 ? 0.5176 0.6339 0.5590 0.0760  -0.0888 0.1221  225  TYR D CE2 
10578 C  CZ  . TYR D 225 ? 0.5528 0.6854 0.5773 0.0717  -0.0948 0.1256  225  TYR D CZ  
10579 O  OH  . TYR D 225 ? 0.6131 0.7648 0.6367 0.0772  -0.1062 0.1348  225  TYR D OH  
10580 N  N   . PRO D 226 ? 0.2491 0.3226 0.3085 0.0620  -0.0553 0.0805  226  PRO D N   
10581 C  CA  . PRO D 226 ? 0.3327 0.4076 0.4104 0.0664  -0.0535 0.0764  226  PRO D CA  
10582 C  C   . PRO D 226 ? 0.3959 0.4860 0.4860 0.0737  -0.0614 0.0829  226  PRO D C   
10583 O  O   . PRO D 226 ? 0.4615 0.5520 0.5448 0.0777  -0.0675 0.0942  226  PRO D O   
10584 C  CB  . PRO D 226 ? 0.3928 0.4447 0.4710 0.0690  -0.0460 0.0783  226  PRO D CB  
10585 C  CG  . PRO D 226 ? 0.4209 0.4617 0.4825 0.0630  -0.0427 0.0782  226  PRO D CG  
10586 C  CD  . PRO D 226 ? 0.2233 0.2767 0.2739 0.0601  -0.0489 0.0827  226  PRO D CD  
10587 N  N   . TYR D 227 ? 0.2797 0.3826 0.3882 0.0754  -0.0612 0.0765  227  TYR D N   
10588 C  CA  . TYR D 227 ? 0.3088 0.4095 0.4240 0.0696  -0.0532 0.0644  227  TYR D CA  
10589 C  C   . TYR D 227 ? 0.3449 0.4620 0.4582 0.0613  -0.0566 0.0556  227  TYR D C   
10590 O  O   . TYR D 227 ? 0.3097 0.4452 0.4208 0.0610  -0.0659 0.0576  227  TYR D O   
10591 C  CB  . TYR D 227 ? 0.3882 0.4955 0.5253 0.0743  -0.0498 0.0616  227  TYR D CB  
10592 C  CG  . TYR D 227 ? 0.3122 0.4016 0.4530 0.0822  -0.0437 0.0664  227  TYR D CG  
10593 C  CD1 . TYR D 227 ? 0.3179 0.3847 0.4491 0.0794  -0.0342 0.0631  227  TYR D CD1 
10594 C  CD2 . TYR D 227 ? 0.3311 0.4265 0.4851 0.0931  -0.0476 0.0734  227  TYR D CD2 
10595 C  CE1 . TYR D 227 ? 0.2815 0.3316 0.4148 0.0859  -0.0284 0.0655  227  TYR D CE1 
10596 C  CE2 . TYR D 227 ? 0.4246 0.5013 0.5817 0.1009  -0.0413 0.0761  227  TYR D CE2 
10597 C  CZ  . TYR D 227 ? 0.4469 0.5010 0.5933 0.0966  -0.0315 0.0714  227  TYR D CZ  
10598 O  OH  . TYR D 227 ? 0.5017 0.5375 0.6503 0.1037  -0.0253 0.0725  227  TYR D OH  
10599 N  N   . ASP D 228 ? 0.3227 0.4322 0.4362 0.0546  -0.0491 0.0457  228  ASP D N   
10600 C  CA  . ASP D 228 ? 0.3234 0.4432 0.4358 0.0459  -0.0504 0.0352  228  ASP D CA  
10601 C  C   . ASP D 228 ? 0.3509 0.4868 0.4843 0.0423  -0.0502 0.0281  228  ASP D C   
10602 O  O   . ASP D 228 ? 0.3556 0.5032 0.4916 0.0342  -0.0526 0.0187  228  ASP D O   
10603 C  CB  . ASP D 228 ? 0.3667 0.4669 0.4671 0.0409  -0.0422 0.0290  228  ASP D CB  
10604 C  CG  . ASP D 228 ? 0.5099 0.6035 0.5909 0.0415  -0.0438 0.0321  228  ASP D CG  
10605 O  OD1 . ASP D 228 ? 0.5398 0.6450 0.6142 0.0434  -0.0511 0.0377  228  ASP D OD1 
10606 O  OD2 . ASP D 228 ? 0.6628 0.7407 0.7352 0.0402  -0.0374 0.0292  228  ASP D OD2 
10607 N  N   . ASN D 229 ? 0.3001 0.4368 0.4490 0.0477  -0.0466 0.0316  229  ASN D N   
10608 C  CA  . ASN D 229 ? 0.3398 0.4962 0.5112 0.0443  -0.0461 0.0255  229  ASN D CA  
10609 C  C   . ASN D 229 ? 0.4481 0.6167 0.6374 0.0549  -0.0479 0.0324  229  ASN D C   
10610 O  O   . ASN D 229 ? 0.2668 0.4271 0.4497 0.0648  -0.0507 0.0423  229  ASN D O   
10611 C  CB  . ASN D 229 ? 0.4170 0.5608 0.5921 0.0358  -0.0343 0.0172  229  ASN D CB  
10612 C  CG  . ASN D 229 ? 0.4444 0.5649 0.6145 0.0408  -0.0237 0.0216  229  ASN D CG  
10613 O  OD1 . ASN D 229 ? 0.4097 0.5238 0.5767 0.0503  -0.0246 0.0294  229  ASN D OD1 
10614 N  ND2 . ASN D 229 ? 0.2607 0.3674 0.4289 0.0338  -0.0137 0.0164  229  ASN D ND2 
10615 N  N   . SER D 230 ? 0.4793 0.6676 0.6919 0.0526  -0.0458 0.0270  230  SER D N   
10616 C  CA  . SER D 230 ? 0.2648 0.4692 0.4987 0.0636  -0.0471 0.0322  230  SER D CA  
10617 C  C   . SER D 230 ? 0.2867 0.5072 0.5452 0.0586  -0.0389 0.0242  230  SER D C   
10618 O  O   . SER D 230 ? 0.3135 0.5348 0.5730 0.0452  -0.0340 0.0151  230  SER D O   
10619 C  CB  . SER D 230 ? 0.2138 0.4449 0.4544 0.0698  -0.0623 0.0377  230  SER D CB  
10620 O  OG  . SER D 230 ? 0.3336 0.5929 0.5862 0.0595  -0.0681 0.0286  230  SER D OG  
10621 N  N   . LEU D 231 ? 0.3504 0.5839 0.6294 0.0694  -0.0369 0.0275  231  LEU D N   
10622 C  CA  . LEU D 231 ? 0.4241 0.6770 0.7286 0.0648  -0.0282 0.0201  231  LEU D CA  
10623 C  C   . LEU D 231 ? 0.5323 0.8222 0.8564 0.0557  -0.0370 0.0134  231  LEU D C   
10624 O  O   . LEU D 231 ? 0.5549 0.8578 0.8944 0.0436  -0.0298 0.0045  231  LEU D O   
10625 C  CB  . LEU D 231 ? 0.4569 0.7172 0.7802 0.0801  -0.0235 0.0243  231  LEU D CB  
10626 C  CG  . LEU D 231 ? 0.3957 0.6270 0.7095 0.0844  -0.0084 0.0246  231  LEU D CG  
10627 C  CD1 . LEU D 231 ? 0.4142 0.6518 0.7449 0.1024  -0.0065 0.0289  231  LEU D CD1 
10628 C  CD2 . LEU D 231 ? 0.4564 0.6873 0.7748 0.0711  0.0058  0.0160  231  LEU D CD2 
10629 N  N   . ALA D 232 ? 0.4205 0.7275 0.7430 0.0605  -0.0528 0.0178  232  ALA D N   
10630 C  CA  . ALA D 232 ? 0.3402 0.6836 0.6783 0.0514  -0.0634 0.0109  232  ALA D CA  
10631 C  C   . ALA D 232 ? 0.4242 0.7567 0.7478 0.0319  -0.0609 -0.0001 232  ALA D C   
10632 O  O   . ALA D 232 ? 0.4390 0.7972 0.7771 0.0193  -0.0650 -0.0099 232  ALA D O   
10633 C  CB  . ALA D 232 ? 0.1053 0.4679 0.4405 0.0619  -0.0812 0.0194  232  ALA D CB  
10634 N  N   . HIS D 233 ? 0.4766 0.7710 0.7724 0.0295  -0.0543 0.0012  233  HIS D N   
10635 C  CA  . HIS D 233 ? 0.4401 0.7187 0.7195 0.0139  -0.0516 -0.0083 233  HIS D CA  
10636 C  C   . HIS D 233 ? 0.5164 0.8189 0.7948 0.0057  -0.0654 -0.0154 233  HIS D C   
10637 O  O   . HIS D 233 ? 0.5834 0.8954 0.8697 -0.0097 -0.0643 -0.0277 233  HIS D O   
10638 C  CB  . HIS D 233 ? 0.2663 0.5364 0.5561 0.0011  -0.0372 -0.0166 233  HIS D CB  
10639 C  CG  . HIS D 233 ? 0.4328 0.6717 0.7127 0.0064  -0.0231 -0.0109 233  HIS D CG  
10640 N  ND1 . HIS D 233 ? 0.5357 0.7812 0.8331 0.0112  -0.0136 -0.0085 233  HIS D ND1 
10641 C  CD2 . HIS D 233 ? 0.4737 0.6767 0.7275 0.0078  -0.0172 -0.0076 233  HIS D CD2 
10642 C  CE1 . HIS D 233 ? 0.5114 0.7254 0.7921 0.0146  -0.0026 -0.0042 233  HIS D CE1 
10643 N  NE2 . HIS D 233 ? 0.5159 0.7045 0.7707 0.0127  -0.0052 -0.0033 233  HIS D NE2 
10644 N  N   . ASN D 234 ? 0.5603 0.8714 0.8274 0.0154  -0.0780 -0.0079 234  ASN D N   
10645 C  CA  . ASN D 234 ? 0.5463 0.8807 0.8081 0.0087  -0.0918 -0.0139 234  ASN D CA  
10646 C  C   . ASN D 234 ? 0.4144 0.7237 0.6484 -0.0005 -0.0894 -0.0213 234  ASN D C   
10647 O  O   . ASN D 234 ? 0.4570 0.7346 0.6714 0.0046  -0.0822 -0.0156 234  ASN D O   
10648 C  CB  . ASN D 234 ? 0.4453 0.7996 0.7048 0.0233  -0.1061 -0.0012 234  ASN D CB  
10649 C  CG  . ASN D 234 ? 0.4381 0.8130 0.7252 0.0360  -0.1075 0.0071  234  ASN D CG  
10650 O  OD1 . ASN D 234 ? 0.4293 0.8232 0.7431 0.0304  -0.1031 -0.0002 234  ASN D OD1 
10651 N  ND2 . ASN D 234 ? 0.4124 0.7830 0.6940 0.0531  -0.1127 0.0224  234  ASN D ND2 
10652 N  N   . GLU D 235 ? 0.4812 0.8057 0.7146 -0.0141 -0.0951 -0.0348 235  GLU D N   
10653 C  CA  . GLU D 235 ? 0.4729 0.7753 0.6815 -0.0226 -0.0926 -0.0441 235  GLU D CA  
10654 C  C   . GLU D 235 ? 0.5985 0.8920 0.7811 -0.0117 -0.0980 -0.0341 235  GLU D C   
10655 O  O   . GLU D 235 ? 0.5676 0.8309 0.7305 -0.0102 -0.0901 -0.0333 235  GLU D O   
10656 C  CB  . GLU D 235 ? 0.5350 0.8598 0.7471 -0.0383 -0.1003 -0.0611 235  GLU D CB  
10657 C  CG  . GLU D 235 ? 0.7242 1.0260 0.9107 -0.0465 -0.0973 -0.0729 235  GLU D CG  
10658 C  CD  . GLU D 235 ? 0.8106 1.1351 0.9976 -0.0617 -0.1061 -0.0907 235  GLU D CD  
10659 O  OE1 . GLU D 235 ? 0.9449 1.2481 1.1201 -0.0726 -0.0999 -0.1052 235  GLU D OE1 
10660 O  OE2 . GLU D 235 ? 0.7387 1.1024 0.9379 -0.0623 -0.1195 -0.0906 235  GLU D OE2 
10661 N  N   . CYS D 236 ? 0.5736 0.8943 0.7566 -0.0037 -0.1114 -0.0255 236  CYS D N   
10662 C  CA  . CYS D 236 ? 0.6095 0.9245 0.7668 0.0045  -0.1170 -0.0157 236  CYS D CA  
10663 C  C   . CYS D 236 ? 0.4842 0.8262 0.6450 0.0159  -0.1308 -0.0015 236  CYS D C   
10664 O  O   . CYS D 236 ? 0.5807 0.9466 0.7657 0.0197  -0.1363 0.0013  236  CYS D O   
10665 C  CB  . CYS D 236 ? 0.7006 1.0177 0.8370 -0.0062 -0.1202 -0.0292 236  CYS D CB  
10666 S  SG  . CYS D 236 ? 0.7222 1.0869 0.8611 -0.0122 -0.1392 -0.0360 236  CYS D SG  
10667 N  N   . CYS D 237 ? 0.4714 0.8092 0.6075 0.0217  -0.1358 0.0079  237  CYS D N   
10668 C  CA  . CYS D 237 ? 0.4058 0.7693 0.5371 0.0305  -0.1507 0.0208  237  CYS D CA  
10669 C  C   . CYS D 237 ? 0.3895 0.7583 0.5404 0.0454  -0.1538 0.0370  237  CYS D C   
10670 O  O   . CYS D 237 ? 0.3016 0.6971 0.4565 0.0534  -0.1675 0.0469  237  CYS D O   
10671 C  CB  . CYS D 237 ? 0.3607 0.7618 0.4949 0.0212  -0.1638 0.0090  237  CYS D CB  
10672 S  SG  . CYS D 237 ? 0.5318 0.9232 0.6512 0.0020  -0.1571 -0.0159 237  CYS D SG  
10673 N  N   . GLU D 238 ? 0.3494 0.6921 0.5113 0.0498  -0.1411 0.0397  238  GLU D N   
10674 C  CA  . GLU D 238 ? 0.3313 0.6739 0.5115 0.0646  -0.1414 0.0534  238  GLU D CA  
10675 C  C   . GLU D 238 ? 0.4251 0.7283 0.5959 0.0713  -0.1292 0.0621  238  GLU D C   
10676 O  O   . GLU D 238 ? 0.5263 0.8082 0.6997 0.0657  -0.1162 0.0539  238  GLU D O   
10677 C  CB  . GLU D 238 ? 0.4608 0.8230 0.6745 0.0629  -0.1391 0.0445  238  GLU D CB  
10678 C  CG  . GLU D 238 ? 0.6857 1.0844 0.9214 0.0738  -0.1524 0.0523  238  GLU D CG  
10679 C  CD  . GLU D 238 ? 0.8007 1.2318 1.0672 0.0655  -0.1534 0.0385  238  GLU D CD  
10680 O  OE1 . GLU D 238 ? 0.9139 1.3723 1.2069 0.0762  -0.1596 0.0440  238  GLU D OE1 
10681 O  OE2 . GLU D 238 ? 0.7293 1.1584 0.9941 0.0483  -0.1477 0.0222  238  GLU D OE2 
10682 N  N   . GLU D 239 ? 0.5860 0.8798 0.7454 0.0829  -0.1336 0.0791  239  GLU D N   
10683 C  CA  . GLU D 239 ? 0.5687 0.8257 0.7179 0.0883  -0.1232 0.0877  239  GLU D CA  
10684 C  C   . GLU D 239 ? 0.4644 0.7068 0.6345 0.0933  -0.1122 0.0849  239  GLU D C   
10685 O  O   . GLU D 239 ? 0.4787 0.7348 0.6709 0.1035  -0.1152 0.0889  239  GLU D O   
10686 C  CB  . GLU D 239 ? 0.6300 0.8807 0.7669 0.0998  -0.1306 0.1072  239  GLU D CB  
10687 C  CG  . GLU D 239 ? 0.8162 1.0682 0.9239 0.0940  -0.1363 0.1123  239  GLU D CG  
10688 C  CD  . GLU D 239 ? 1.0251 1.2676 1.1201 0.1048  -0.1423 0.1337  239  GLU D CD  
10689 O  OE1 . GLU D 239 ? 1.0292 1.2584 1.0987 0.1000  -0.1406 0.1402  239  GLU D OE1 
10690 O  OE2 . GLU D 239 ? 1.0587 1.3064 1.1696 0.1182  -0.1481 0.1443  239  GLU D OE2 
10691 N  N   . SER D 240 ? 0.3437 0.5598 0.5063 0.0868  -0.0994 0.0780  240  SER D N   
10692 C  CA  . SER D 240 ? 0.2159 0.4139 0.3914 0.0915  -0.0882 0.0767  240  SER D CA  
10693 C  C   . SER D 240 ? 0.4190 0.5844 0.5779 0.0965  -0.0830 0.0863  240  SER D C   
10694 O  O   . SER D 240 ? 0.4152 0.5587 0.5610 0.0898  -0.0741 0.0818  240  SER D O   
10695 C  CB  . SER D 240 ? 0.2798 0.4727 0.4597 0.0803  -0.0776 0.0621  240  SER D CB  
10696 O  OG  . SER D 240 ? 0.3652 0.5444 0.5573 0.0848  -0.0668 0.0608  240  SER D OG  
10697 N  N   . LEU D 241 ? 0.5380 0.7003 0.6979 0.1084  -0.0887 0.0999  241  LEU D N   
10698 C  CA  . LEU D 241 ? 0.4114 0.5442 0.5530 0.1111  -0.0859 0.1103  241  LEU D CA  
10699 C  C   . LEU D 241 ? 0.3313 0.4358 0.4763 0.1141  -0.0740 0.1079  241  LEU D C   
10700 O  O   . LEU D 241 ? 0.2623 0.3702 0.4259 0.1184  -0.0683 0.1012  241  LEU D O   
10701 C  CB  . LEU D 241 ? 0.3209 0.4578 0.4589 0.1217  -0.0968 0.1271  241  LEU D CB  
10702 C  CG  . LEU D 241 ? 0.3929 0.5557 0.5197 0.1175  -0.1090 0.1308  241  LEU D CG  
10703 C  CD1 . LEU D 241 ? 0.2888 0.4549 0.4099 0.1287  -0.1201 0.1500  241  LEU D CD1 
10704 C  CD2 . LEU D 241 ? 0.2282 0.3841 0.3309 0.1034  -0.1054 0.1255  241  LEU D CD2 
10705 N  N   . THR D 242 ? 0.6209 0.6989 0.7472 0.1109  -0.0700 0.1128  242  THR D N   
10706 C  CA  . THR D 242 ? 0.4840 0.5343 0.6087 0.1112  -0.0593 0.1094  242  THR D CA  
10707 C  C   . THR D 242 ? 0.5599 0.5898 0.6855 0.1221  -0.0601 0.1211  242  THR D C   
10708 O  O   . THR D 242 ? 0.5273 0.5594 0.6472 0.1266  -0.0687 0.1340  242  THR D O   
10709 C  CB  . THR D 242 ? 0.4272 0.4630 0.5312 0.0991  -0.0546 0.1062  242  THR D CB  
10710 O  OG1 . THR D 242 ? 0.3754 0.4150 0.4820 0.0922  -0.0478 0.0931  242  THR D OG1 
10711 C  CG2 . THR D 242 ? 0.3729 0.3789 0.4674 0.0997  -0.0494 0.1109  242  THR D CG2 
10712 N  N   . PRO D 243 ? 0.5434 0.5525 0.6752 0.1266  -0.0511 0.1165  243  PRO D N   
10713 C  CA  . PRO D 243 ? 0.4092 0.3935 0.5412 0.1368  -0.0507 0.1261  243  PRO D CA  
10714 C  C   . PRO D 243 ? 0.4275 0.3919 0.5375 0.1300  -0.0533 0.1368  243  PRO D C   
10715 O  O   . PRO D 243 ? 0.3835 0.3327 0.4911 0.1376  -0.0571 0.1498  243  PRO D O   
10716 C  CB  . PRO D 243 ? 0.3058 0.2696 0.4416 0.1374  -0.0387 0.1150  243  PRO D CB  
10717 C  CG  . PRO D 243 ? 0.4428 0.4284 0.5888 0.1331  -0.0342 0.1021  243  PRO D CG  
10718 C  CD  . PRO D 243 ? 0.5566 0.5634 0.6945 0.1228  -0.0407 0.1024  243  PRO D CD  
10719 N  N   . ASP D 244 ? 0.4198 0.3847 0.5146 0.1158  -0.0508 0.1316  244  ASP D N   
10720 C  CA  . ASP D 244 ? 0.4662 0.4176 0.5411 0.1071  -0.0523 0.1404  244  ASP D CA  
10721 C  C   . ASP D 244 ? 0.5441 0.5194 0.6097 0.1026  -0.0607 0.1471  244  ASP D C   
10722 O  O   . ASP D 244 ? 0.6644 0.6399 0.7143 0.0914  -0.0596 0.1475  244  ASP D O   
10723 C  CB  . ASP D 244 ? 0.5215 0.4597 0.5857 0.0948  -0.0442 0.1307  244  ASP D CB  
10724 C  CG  . ASP D 244 ? 0.6654 0.5724 0.7296 0.0961  -0.0369 0.1282  244  ASP D CG  
10725 O  OD1 . ASP D 244 ? 0.7679 0.6528 0.8230 0.0939  -0.0371 0.1375  244  ASP D OD1 
10726 O  OD2 . ASP D 244 ? 0.6548 0.5588 0.7269 0.0982  -0.0306 0.1164  244  ASP D OD2 
10727 N  N   . ASP D 245 ? 0.3933 0.3904 0.4684 0.1112  -0.0691 0.1518  245  ASP D N   
10728 C  CA  . ASP D 245 ? 0.4678 0.4895 0.5330 0.1068  -0.0774 0.1564  245  ASP D CA  
10729 C  C   . ASP D 245 ? 0.5130 0.5243 0.5573 0.1023  -0.0802 0.1711  245  ASP D C   
10730 O  O   . ASP D 245 ? 0.5943 0.6192 0.6240 0.0928  -0.0816 0.1705  245  ASP D O   
10731 C  CB  . ASP D 245 ? 0.4237 0.4719 0.5026 0.1169  -0.0873 0.1595  245  ASP D CB  
10732 C  CG  . ASP D 245 ? 0.6197 0.6978 0.6906 0.1095  -0.0941 0.1557  245  ASP D CG  
10733 O  OD1 . ASP D 245 ? 0.7125 0.7964 0.7803 0.0992  -0.0889 0.1420  245  ASP D OD1 
10734 O  OD2 . ASP D 245 ? 0.7027 0.7978 0.7695 0.1142  -0.1047 0.1663  245  ASP D OD2 
10735 N  N   . ARG D 246 ? 0.4142 0.4010 0.4569 0.1090  -0.0803 0.1845  246  ARG D N   
10736 C  CA  . ARG D 246 ? 0.4912 0.4642 0.5136 0.1031  -0.0813 0.1997  246  ARG D CA  
10737 C  C   . ARG D 246 ? 0.5240 0.4929 0.5328 0.0869  -0.0736 0.1923  246  ARG D C   
10738 O  O   . ARG D 246 ? 0.5895 0.5744 0.5835 0.0785  -0.0754 0.1951  246  ARG D O   
10739 C  CB  . ARG D 246 ? 0.5473 0.4858 0.5713 0.1109  -0.0794 0.2122  246  ARG D CB  
10740 C  CG  . ARG D 246 ? 0.6640 0.6069 0.7035 0.1296  -0.0872 0.2204  246  ARG D CG  
10741 C  CD  . ARG D 246 ? 0.8133 0.7178 0.8566 0.1391  -0.0837 0.2302  246  ARG D CD  
10742 N  NE  . ARG D 246 ? 1.0108 0.9017 1.0398 0.1430  -0.0899 0.2532  246  ARG D NE  
10743 C  CZ  . ARG D 246 ? 1.2022 1.0546 1.2293 0.1493  -0.0870 0.2652  246  ARG D CZ  
10744 N  NH1 . ARG D 246 ? 1.2225 1.0475 1.2611 0.1520  -0.0780 0.2545  246  ARG D NH1 
10745 N  NH2 . ARG D 246 ? 1.3655 1.2054 1.3781 0.1525  -0.0927 0.2878  246  ARG D NH2 
10746 N  N   . VAL D 247 ? 0.3925 0.3421 0.4066 0.0828  -0.0649 0.1822  247  VAL D N   
10747 C  CA  . VAL D 247 ? 0.4389 0.3854 0.4425 0.0685  -0.0581 0.1754  247  VAL D CA  
10748 C  C   . VAL D 247 ? 0.3437 0.3194 0.3454 0.0629  -0.0586 0.1640  247  VAL D C   
10749 O  O   . VAL D 247 ? 0.4671 0.4511 0.4562 0.0530  -0.0566 0.1642  247  VAL D O   
10750 C  CB  . VAL D 247 ? 0.5979 0.5218 0.6081 0.0659  -0.0500 0.1652  247  VAL D CB  
10751 C  CG1 . VAL D 247 ? 0.4465 0.3782 0.4503 0.0531  -0.0446 0.1542  247  VAL D CG1 
10752 C  CG2 . VAL D 247 ? 0.5086 0.3990 0.5149 0.0661  -0.0475 0.1759  247  VAL D CG2 
10753 N  N   . PHE D 248 ? 0.4098 0.4008 0.4244 0.0692  -0.0607 0.1537  248  PHE D N   
10754 C  CA  . PHE D 248 ? 0.4207 0.4361 0.4334 0.0641  -0.0610 0.1424  248  PHE D CA  
10755 C  C   . PHE D 248 ? 0.3967 0.4318 0.3960 0.0613  -0.0671 0.1496  248  PHE D C   
10756 O  O   . PHE D 248 ? 0.4380 0.4856 0.4276 0.0534  -0.0649 0.1439  248  PHE D O   
10757 C  CB  . PHE D 248 ? 0.3363 0.3639 0.3654 0.0700  -0.0621 0.1310  248  PHE D CB  
10758 C  CG  . PHE D 248 ? 0.4192 0.4370 0.4551 0.0675  -0.0541 0.1184  248  PHE D CG  
10759 C  CD1 . PHE D 248 ? 0.4545 0.4765 0.4832 0.0594  -0.0498 0.1097  248  PHE D CD1 
10760 C  CD2 . PHE D 248 ? 0.3342 0.3386 0.3829 0.0739  -0.0506 0.1156  248  PHE D CD2 
10761 C  CE1 . PHE D 248 ? 0.4967 0.5096 0.5298 0.0577  -0.0432 0.0998  248  PHE D CE1 
10762 C  CE2 . PHE D 248 ? 0.3330 0.3288 0.3850 0.0712  -0.0432 0.1048  248  PHE D CE2 
10763 C  CZ  . PHE D 248 ? 0.2278 0.2277 0.2715 0.0631  -0.0400 0.0976  248  PHE D CZ  
10764 N  N   . LYS D 249 ? 0.3635 0.4022 0.3621 0.0686  -0.0749 0.1624  249  LYS D N   
10765 C  CA  . LYS D 249 ? 0.3896 0.4469 0.3726 0.0663  -0.0815 0.1711  249  LYS D CA  
10766 C  C   . LYS D 249 ? 0.4940 0.5422 0.4578 0.0564  -0.0765 0.1799  249  LYS D C   
10767 O  O   . LYS D 249 ? 0.5204 0.5869 0.4703 0.0492  -0.0762 0.1779  249  LYS D O   
10768 C  CB  . LYS D 249 ? 0.4377 0.5002 0.4239 0.0776  -0.0918 0.1848  249  LYS D CB  
10769 C  CG  . LYS D 249 ? 0.4151 0.5050 0.4145 0.0832  -0.0994 0.1752  249  LYS D CG  
10770 C  CD  . LYS D 249 ? 0.3100 0.4083 0.3165 0.0960  -0.1105 0.1884  249  LYS D CD  
10771 C  CE  . LYS D 249 ? 0.3600 0.4918 0.3782 0.0983  -0.1187 0.1777  249  LYS D CE  
10772 N  NZ  . LYS D 249 ? 0.4496 0.5906 0.4854 0.1126  -0.1278 0.1859  249  LYS D NZ  
10773 N  N   . GLN D 250 ? 0.3824 0.4030 0.3459 0.0551  -0.0717 0.1885  250  GLN D N   
10774 C  CA  . GLN D 250 ? 0.4217 0.4341 0.3696 0.0435  -0.0658 0.1957  250  GLN D CA  
10775 C  C   . GLN D 250 ? 0.4388 0.4644 0.3855 0.0336  -0.0587 0.1804  250  GLN D C   
10776 O  O   . GLN D 250 ? 0.4387 0.4781 0.3716 0.0252  -0.0562 0.1826  250  GLN D O   
10777 C  CB  . GLN D 250 ? 0.4717 0.4502 0.4218 0.0423  -0.0613 0.2045  250  GLN D CB  
10778 C  CG  . GLN D 250 ? 0.4624 0.4323 0.3978 0.0284  -0.0549 0.2128  250  GLN D CG  
10779 C  CD  . GLN D 250 ? 0.7257 0.6599 0.6595 0.0277  -0.0527 0.2266  250  GLN D CD  
10780 O  OE1 . GLN D 250 ? 0.8310 0.7514 0.7661 0.0387  -0.0584 0.2389  250  GLN D OE1 
10781 N  NE2 . GLN D 250 ? 0.7840 0.7030 0.7158 0.0148  -0.0447 0.2244  250  GLN D NE2 
10782 N  N   . LEU D 251 ? 0.3282 0.3499 0.2890 0.0353  -0.0553 0.1655  251  LEU D N   
10783 C  CA  . LEU D 251 ? 0.3865 0.4196 0.3477 0.0283  -0.0493 0.1515  251  LEU D CA  
10784 C  C   . LEU D 251 ? 0.4654 0.5263 0.4199 0.0276  -0.0514 0.1446  251  LEU D C   
10785 O  O   . LEU D 251 ? 0.4881 0.5617 0.4327 0.0203  -0.0472 0.1429  251  LEU D O   
10786 C  CB  . LEU D 251 ? 0.4637 0.4881 0.4400 0.0321  -0.0465 0.1382  251  LEU D CB  
10787 C  CG  . LEU D 251 ? 0.5696 0.5670 0.5518 0.0318  -0.0431 0.1408  251  LEU D CG  
10788 C  CD1 . LEU D 251 ? 0.4958 0.4868 0.4909 0.0365  -0.0407 0.1279  251  LEU D CD1 
10789 C  CD2 . LEU D 251 ? 0.3403 0.3300 0.3146 0.0204  -0.0378 0.1444  251  LEU D CD2 
10790 N  N   . ALA D 252 ? 0.4944 0.5655 0.4549 0.0349  -0.0575 0.1399  252  ALA D N   
10791 C  CA  . ALA D 252 ? 0.5081 0.6038 0.4623 0.0341  -0.0603 0.1317  252  ALA D CA  
10792 C  C   . ALA D 252 ? 0.6047 0.7134 0.5393 0.0291  -0.0617 0.1421  252  ALA D C   
10793 O  O   . ALA D 252 ? 0.6524 0.7782 0.5773 0.0241  -0.0585 0.1345  252  ALA D O   
10794 C  CB  . ALA D 252 ? 0.4101 0.5144 0.3742 0.0415  -0.0679 0.1274  252  ALA D CB  
10795 N  N   . HIS D 253 ? 0.5174 0.6172 0.4454 0.0309  -0.0660 0.1597  253  HIS D N   
10796 C  CA  . HIS D 253 ? 0.4505 0.5608 0.3574 0.0257  -0.0669 0.1723  253  HIS D CA  
10797 C  C   . HIS D 253 ? 0.4474 0.5557 0.3462 0.0150  -0.0568 0.1730  253  HIS D C   
10798 O  O   . HIS D 253 ? 0.4672 0.5939 0.3502 0.0088  -0.0541 0.1739  253  HIS D O   
10799 C  CB  . HIS D 253 ? 0.4168 0.5139 0.3183 0.0306  -0.0734 0.1934  253  HIS D CB  
10800 C  CG  . HIS D 253 ? 0.5284 0.6433 0.4262 0.0385  -0.0850 0.1974  253  HIS D CG  
10801 N  ND1 . HIS D 253 ? 0.5470 0.6554 0.4594 0.0499  -0.0930 0.2015  253  HIS D ND1 
10802 C  CD2 . HIS D 253 ? 0.6074 0.7489 0.4891 0.0366  -0.0902 0.1968  253  HIS D CD2 
10803 C  CE1 . HIS D 253 ? 0.6136 0.7452 0.5202 0.0546  -0.1034 0.2040  253  HIS D CE1 
10804 N  NE2 . HIS D 253 ? 0.7569 0.9082 0.6437 0.0463  -0.1022 0.2010  253  HIS D NE2 
10805 N  N   . THR D 254 ? 0.3624 0.4504 0.2722 0.0125  -0.0511 0.1721  254  THR D N   
10806 C  CA  . THR D 254 ? 0.4482 0.5359 0.3529 0.0014  -0.0420 0.1733  254  THR D CA  
10807 C  C   . THR D 254 ? 0.3794 0.4928 0.2822 -0.0015 -0.0373 0.1579  254  THR D C   
10808 O  O   . THR D 254 ? 0.4747 0.6027 0.3666 -0.0097 -0.0312 0.1600  254  THR D O   
10809 C  CB  . THR D 254 ? 0.5301 0.5950 0.4485 -0.0010 -0.0376 0.1707  254  THR D CB  
10810 O  OG1 . THR D 254 ? 0.4633 0.5017 0.3839 0.0028  -0.0413 0.1834  254  THR D OG1 
10811 C  CG2 . THR D 254 ? 0.3955 0.4642 0.3096 -0.0139 -0.0290 0.1722  254  THR D CG2 
10812 N  N   . TYR D 255 ? 0.2883 0.4069 0.2020 0.0055  -0.0394 0.1424  255  TYR D N   
10813 C  CA  . TYR D 255 ? 0.4126 0.5514 0.3257 0.0045  -0.0348 0.1269  255  TYR D CA  
10814 C  C   . TYR D 255 ? 0.3072 0.4680 0.2043 0.0042  -0.0373 0.1257  255  TYR D C   
10815 O  O   . TYR D 255 ? 0.4332 0.6117 0.3203 -0.0009 -0.0310 0.1221  255  TYR D O   
10816 C  CB  . TYR D 255 ? 0.4143 0.5483 0.3432 0.0114  -0.0356 0.1112  255  TYR D CB  
10817 C  CG  . TYR D 255 ? 0.3972 0.5450 0.3283 0.0110  -0.0291 0.0963  255  TYR D CG  
10818 C  CD1 . TYR D 255 ? 0.5273 0.6939 0.4497 0.0119  -0.0286 0.0867  255  TYR D CD1 
10819 C  CD2 . TYR D 255 ? 0.3170 0.4594 0.2585 0.0100  -0.0237 0.0917  255  TYR D CD2 
10820 C  CE1 . TYR D 255 ? 0.5804 0.7580 0.5056 0.0132  -0.0221 0.0728  255  TYR D CE1 
10821 C  CE2 . TYR D 255 ? 0.4332 0.5887 0.3779 0.0117  -0.0182 0.0791  255  TYR D CE2 
10822 C  CZ  . TYR D 255 ? 0.4872 0.6591 0.4242 0.0138  -0.0170 0.0697  255  TYR D CZ  
10823 O  OH  . TYR D 255 ? 0.4765 0.6596 0.4177 0.0171  -0.0109 0.0568  255  TYR D OH  
10824 N  N   . SER D 256 ? 0.3352 0.4969 0.2303 0.0098  -0.0463 0.1279  256  SER D N   
10825 C  CA  . SER D 256 ? 0.4623 0.6459 0.3418 0.0097  -0.0505 0.1249  256  SER D CA  
10826 C  C   . SER D 256 ? 0.6026 0.7963 0.4600 0.0030  -0.0487 0.1402  256  SER D C   
10827 O  O   . SER D 256 ? 0.4952 0.7099 0.3380 -0.0012 -0.0445 0.1340  256  SER D O   
10828 C  CB  . SER D 256 ? 0.4420 0.6257 0.3263 0.0166  -0.0618 0.1255  256  SER D CB  
10829 O  OG  . SER D 256 ? 0.6151 0.8220 0.4845 0.0157  -0.0668 0.1201  256  SER D OG  
10830 N  N   . ASP D 257 ? 0.5819 0.7595 0.4364 0.0021  -0.0512 0.1601  257  ASP D N   
10831 C  CA  . ASP D 257 ? 0.4513 0.6335 0.2845 -0.0051 -0.0489 0.1779  257  ASP D CA  
10832 C  C   . ASP D 257 ? 0.5450 0.7393 0.3726 -0.0150 -0.0362 0.1729  257  ASP D C   
10833 O  O   . ASP D 257 ? 0.5954 0.8059 0.4027 -0.0216 -0.0324 0.1800  257  ASP D O   
10834 C  CB  . ASP D 257 ? 0.5334 0.6883 0.3687 -0.0050 -0.0511 0.1988  257  ASP D CB  
10835 C  CG  . ASP D 257 ? 0.7637 0.9101 0.6017 0.0058  -0.0636 0.2079  257  ASP D CG  
10836 O  OD1 . ASP D 257 ? 0.7837 0.9486 0.6209 0.0117  -0.0714 0.1990  257  ASP D OD1 
10837 O  OD2 . ASP D 257 ? 0.8763 0.9977 0.7182 0.0084  -0.0656 0.2235  257  ASP D OD2 
10838 N  N   . ASN D 258 ? 0.6229 0.8109 0.4688 -0.0159 -0.0297 0.1611  258  ASN D N   
10839 C  CA  . ASN D 258 ? 0.5831 0.7852 0.4285 -0.0241 -0.0181 0.1555  258  ASN D CA  
10840 C  C   . ASN D 258 ? 0.5544 0.7805 0.3995 -0.0210 -0.0140 0.1349  258  ASN D C   
10841 O  O   . ASN D 258 ? 0.5276 0.7685 0.3757 -0.0252 -0.0042 0.1273  258  ASN D O   
10842 C  CB  . ASN D 258 ? 0.4887 0.6737 0.3533 -0.0270 -0.0136 0.1544  258  ASN D CB  
10843 C  CG  . ASN D 258 ? 0.6374 0.8037 0.4978 -0.0357 -0.0121 0.1742  258  ASN D CG  
10844 O  OD1 . ASN D 258 ? 0.6168 0.7929 0.4681 -0.0469 -0.0042 0.1822  258  ASN D OD1 
10845 N  ND2 . ASN D 258 ? 0.4268 0.5658 0.2936 -0.0308 -0.0191 0.1824  258  ASN D ND2 
10846 N  N   . HIS D 259 ? 0.6602 0.8906 0.5029 -0.0134 -0.0214 0.1254  259  HIS D N   
10847 C  CA  . HIS D 259 ? 0.6575 0.9052 0.5006 -0.0097 -0.0183 0.1041  259  HIS D CA  
10848 C  C   . HIS D 259 ? 0.6283 0.8964 0.4482 -0.0108 -0.0216 0.1025  259  HIS D C   
10849 O  O   . HIS D 259 ? 0.4959 0.7620 0.3113 -0.0071 -0.0321 0.1038  259  HIS D O   
10850 C  CB  . HIS D 259 ? 0.5991 0.8325 0.4612 -0.0012 -0.0233 0.0907  259  HIS D CB  
10851 C  CG  . HIS D 259 ? 0.5978 0.8420 0.4638 0.0029  -0.0188 0.0687  259  HIS D CG  
10852 N  ND1 . HIS D 259 ? 0.5311 0.7926 0.3821 0.0029  -0.0195 0.0577  259  HIS D ND1 
10853 C  CD2 . HIS D 259 ? 0.5430 0.7809 0.4255 0.0075  -0.0137 0.0557  259  HIS D CD2 
10854 C  CE1 . HIS D 259 ? 0.4155 0.6791 0.2744 0.0074  -0.0143 0.0382  259  HIS D CE1 
10855 N  NE2 . HIS D 259 ? 0.4229 0.6721 0.3010 0.0108  -0.0109 0.0375  259  HIS D NE2 
10856 N  N   . PRO D 260 ? 0.7286 1.0187 0.5337 -0.0162 -0.0123 0.0989  260  PRO D N   
10857 C  CA  . PRO D 260 ? 0.7363 1.0484 0.5143 -0.0196 -0.0132 0.0999  260  PRO D CA  
10858 C  C   . PRO D 260 ? 0.6104 0.9283 0.3833 -0.0142 -0.0224 0.0854  260  PRO D C   
10859 O  O   . PRO D 260 ? 0.5693 0.9012 0.3198 -0.0165 -0.0284 0.0905  260  PRO D O   
10860 C  CB  . PRO D 260 ? 0.7055 1.0395 0.4782 -0.0234 0.0012  0.0884  260  PRO D CB  
10861 C  CG  . PRO D 260 ? 0.7915 1.1160 0.5847 -0.0253 0.0087  0.0927  260  PRO D CG  
10862 C  CD  . PRO D 260 ? 0.6270 0.9246 0.4424 -0.0187 0.0003  0.0919  260  PRO D CD  
10863 N  N   . ILE D 261 ? 0.5613 0.8689 0.3540 -0.0079 -0.0236 0.0679  261  ILE D N   
10864 C  CA  . ILE D 261 ? 0.6687 0.9814 0.4588 -0.0046 -0.0307 0.0509  261  ILE D CA  
10865 C  C   . ILE D 261 ? 0.5937 0.8894 0.3989 -0.0004 -0.0430 0.0559  261  ILE D C   
10866 O  O   . ILE D 261 ? 0.6411 0.9454 0.4380 -0.0003 -0.0537 0.0553  261  ILE D O   
10867 C  CB  . ILE D 261 ? 0.6469 0.9603 0.4471 -0.0009 -0.0222 0.0258  261  ILE D CB  
10868 C  CG1 . ILE D 261 ? 0.5643 0.9005 0.3469 -0.0039 -0.0109 0.0169  261  ILE D CG1 
10869 C  CG2 . ILE D 261 ? 0.5749 0.8855 0.3780 0.0016  -0.0300 0.0086  261  ILE D CG2 
10870 C  CD1 . ILE D 261 ? 0.7133 1.0486 0.5072 0.0017  -0.0012 -0.0067 261  ILE D CD1 
10871 N  N   . MET D 262 ? 0.3178 0.5919 0.1452 0.0029  -0.0414 0.0606  262  MET D N   
10872 C  CA  . MET D 262 ? 0.5269 0.7847 0.3705 0.0073  -0.0511 0.0658  262  MET D CA  
10873 C  C   . MET D 262 ? 0.6505 0.9114 0.4835 0.0070  -0.0615 0.0860  262  MET D C   
10874 O  O   . MET D 262 ? 0.5979 0.8610 0.4352 0.0103  -0.0724 0.0860  262  MET D O   
10875 C  CB  . MET D 262 ? 0.4149 0.6500 0.2797 0.0100  -0.0464 0.0698  262  MET D CB  
10876 C  CG  . MET D 262 ? 0.2287 0.4473 0.1111 0.0149  -0.0541 0.0725  262  MET D CG  
10877 S  SD  . MET D 262 ? 0.4595 0.6538 0.3638 0.0177  -0.0471 0.0717  262  MET D SD  
10878 C  CE  . MET D 262 ? 0.2782 0.4782 0.1852 0.0184  -0.0380 0.0500  262  MET D CE  
10879 N  N   . ARG D 263 ? 0.6864 0.9478 0.5063 0.0032  -0.0577 0.1035  263  ARG D N   
10880 C  CA  . ARG D 263 ? 0.6648 0.9264 0.4713 0.0031  -0.0660 0.1261  263  ARG D CA  
10881 C  C   . ARG D 263 ? 0.6479 0.9309 0.4382 0.0042  -0.0774 0.1248  263  ARG D C   
10882 O  O   . ARG D 263 ? 0.6955 0.9786 0.4796 0.0074  -0.0876 0.1424  263  ARG D O   
10883 C  CB  . ARG D 263 ? 0.6996 0.9634 0.4889 -0.0042 -0.0572 0.1410  263  ARG D CB  
10884 C  CG  . ARG D 263 ? 0.8996 1.1591 0.6731 -0.0049 -0.0638 0.1671  263  ARG D CG  
10885 C  CD  . ARG D 263 ? 1.0728 1.3306 0.8325 -0.0143 -0.0526 0.1811  263  ARG D CD  
10886 N  NE  . ARG D 263 ? 1.0425 1.3270 0.7836 -0.0211 -0.0439 0.1708  263  ARG D NE  
10887 C  CZ  . ARG D 263 ? 0.9061 1.1957 0.6482 -0.0284 -0.0299 0.1667  263  ARG D CZ  
10888 N  NH1 . ARG D 263 ? 0.7176 0.9881 0.4779 -0.0311 -0.0238 0.1719  263  ARG D NH1 
10889 N  NH2 . ARG D 263 ? 0.8353 1.1512 0.5606 -0.0331 -0.0219 0.1565  263  ARG D NH2 
10890 N  N   . LYS D 264 ? 0.7312 1.0323 0.5149 0.0020  -0.0759 0.1037  264  LYS D N   
10891 C  CA  . LYS D 264 ? 0.7895 1.1145 0.5545 0.0009  -0.0860 0.0997  264  LYS D CA  
10892 C  C   . LYS D 264 ? 0.7545 1.0804 0.5360 0.0059  -0.0992 0.0936  264  LYS D C   
10893 O  O   . LYS D 264 ? 0.7939 1.1328 0.5671 0.0081  -0.1122 0.1045  264  LYS D O   
10894 C  CB  . LYS D 264 ? 0.7666 1.1101 0.5160 -0.0045 -0.0781 0.0780  264  LYS D CB  
10895 C  CG  . LYS D 264 ? 0.7333 1.0820 0.4664 -0.0096 -0.0647 0.0840  264  LYS D CG  
10896 C  CD  . LYS D 264 ? 0.8852 1.2549 0.6014 -0.0136 -0.0571 0.0622  264  LYS D CD  
10897 C  CE  . LYS D 264 ? 0.9654 1.3461 0.6633 -0.0191 -0.0440 0.0700  264  LYS D CE  
10898 N  NZ  . LYS D 264 ? 1.1896 1.5776 0.8642 -0.0229 -0.0497 0.0965  264  LYS D NZ  
10899 N  N   . GLY D 265 ? 0.7639 1.0773 0.5694 0.0076  -0.0958 0.0768  265  GLY D N   
10900 C  CA  . GLY D 265 ? 0.5492 0.8617 0.3747 0.0115  -0.1062 0.0718  265  GLY D CA  
10901 C  C   . GLY D 265 ? 0.5613 0.8922 0.3845 0.0072  -0.1114 0.0492  265  GLY D C   
10902 O  O   . GLY D 265 ? 0.7000 1.0337 0.5405 0.0086  -0.1199 0.0436  265  GLY D O   
10903 N  N   . ASN D 266 ? 0.5210 0.8646 0.3236 0.0015  -0.1057 0.0351  266  ASN D N   
10904 C  CA  . ASN D 266 ? 0.5727 0.9329 0.3703 -0.0038 -0.1103 0.0117  266  ASN D CA  
10905 C  C   . ASN D 266 ? 0.6603 1.0107 0.4595 -0.0069 -0.0971 -0.0127 266  ASN D C   
10906 O  O   . ASN D 266 ? 0.7498 1.1149 0.5315 -0.0122 -0.0960 -0.0307 266  ASN D O   
10907 C  CB  . ASN D 266 ? 0.5838 0.9734 0.3508 -0.0078 -0.1189 0.0150  266  ASN D CB  
10908 C  CG  . ASN D 266 ? 0.8750 1.2686 0.6165 -0.0092 -0.1092 0.0249  266  ASN D CG  
10909 O  OD1 . ASN D 266 ? 0.9468 1.3229 0.6951 -0.0078 -0.0958 0.0266  266  ASN D OD1 
10910 N  ND2 . ASN D 266 ? 0.8506 1.2691 0.5624 -0.0125 -0.1159 0.0315  266  ASN D ND2 
10911 N  N   . ASN D 267 ? 0.4904 0.8155 0.3100 -0.0031 -0.0873 -0.0136 267  ASN D N   
10912 C  CA  . ASN D 267 ? 0.4695 0.7831 0.2919 -0.0034 -0.0743 -0.0336 267  ASN D CA  
10913 C  C   . ASN D 267 ? 0.5128 0.8141 0.3533 -0.0052 -0.0754 -0.0531 267  ASN D C   
10914 O  O   . ASN D 267 ? 0.4591 0.7576 0.3159 -0.0055 -0.0841 -0.0487 267  ASN D O   
10915 C  CB  . ASN D 267 ? 0.5262 0.8213 0.3589 0.0018  -0.0632 -0.0232 267  ASN D CB  
10916 C  CG  . ASN D 267 ? 0.5991 0.9016 0.4194 0.0022  -0.0634 0.0002  267  ASN D CG  
10917 O  OD1 . ASN D 267 ? 0.5778 0.8986 0.3750 -0.0011 -0.0611 0.0018  267  ASN D OD1 
10918 N  ND2 . ASN D 267 ? 0.5597 0.8473 0.3948 0.0057  -0.0656 0.0184  267  ASN D ND2 
10919 N  N   . CYS D 268 ? 0.6174 0.9113 0.4553 -0.0062 -0.0659 -0.0745 268  CYS D N   
10920 C  CA  . CYS D 268 ? 0.6226 0.9004 0.4756 -0.0088 -0.0646 -0.0945 268  CYS D CA  
10921 C  C   . CYS D 268 ? 0.7586 1.0476 0.6173 -0.0161 -0.0777 -0.1000 268  CYS D C   
10922 O  O   . CYS D 268 ? 0.6855 0.9592 0.5652 -0.0179 -0.0784 -0.1056 268  CYS D O   
10923 C  CB  . CYS D 268 ? 0.4938 0.7430 0.3703 -0.0027 -0.0573 -0.0893 268  CYS D CB  
10924 S  SG  . CYS D 268 ? 0.9071 1.1507 0.7855 0.0055  -0.0507 -0.0660 268  CYS D SG  
10925 N  N   . ASN D 269 ? 0.8353 1.1526 0.6755 -0.0207 -0.0879 -0.0985 269  ASN D N   
10926 C  CA  . ASN D 269 ? 0.8301 1.1647 0.6759 -0.0274 -0.1023 -0.1026 269  ASN D CA  
10927 C  C   . ASN D 269 ? 0.7858 1.1207 0.6525 -0.0229 -0.1109 -0.0810 269  ASN D C   
10928 O  O   . ASN D 269 ? 0.6611 1.0111 0.5385 -0.0272 -0.1226 -0.0828 269  ASN D O   
10929 C  CB  . ASN D 269 ? 0.8705 1.1941 0.7272 -0.0355 -0.1001 -0.1290 269  ASN D CB  
10930 C  CG  . ASN D 269 ? 0.9433 1.2719 0.7773 -0.0412 -0.0950 -0.1533 269  ASN D CG  
10931 O  OD1 . ASN D 269 ? 0.9265 1.2363 0.7664 -0.0456 -0.0879 -0.1753 269  ASN D OD1 
10932 N  ND2 . ASN D 269 ? 0.9916 1.3445 0.7985 -0.0412 -0.0981 -0.1494 269  ASN D ND2 
10933 N  N   . ASP D 270 ? 0.7239 1.0431 0.5970 -0.0145 -0.1049 -0.0616 270  ASP D N   
10934 C  CA  . ASP D 270 ? 0.6851 1.0014 0.5773 -0.0089 -0.1112 -0.0416 270  ASP D CA  
10935 C  C   . ASP D 270 ? 0.7562 1.0922 0.6337 -0.0049 -0.1210 -0.0199 270  ASP D C   
10936 O  O   . ASP D 270 ? 0.7321 1.0764 0.5851 -0.0052 -0.1186 -0.0155 270  ASP D O   
10937 C  CB  . ASP D 270 ? 0.6503 0.9371 0.5575 -0.0023 -0.0998 -0.0328 270  ASP D CB  
10938 C  CG  . ASP D 270 ? 0.6282 0.8928 0.5500 -0.0048 -0.0904 -0.0506 270  ASP D CG  
10939 O  OD1 . ASP D 270 ? 0.7012 0.9698 0.6296 -0.0118 -0.0936 -0.0672 270  ASP D OD1 
10940 O  OD2 . ASP D 270 ? 0.5967 0.8395 0.5234 0.0000  -0.0798 -0.0474 270  ASP D OD2 
10941 N  N   . SER D 271 ? 0.7114 1.0547 0.6042 -0.0008 -0.1315 -0.0062 271  SER D N   
10942 C  CA  . SER D 271 ? 0.6621 1.0178 0.5441 0.0055  -0.1405 0.0178  271  SER D CA  
10943 C  C   . SER D 271 ? 0.6446 0.9799 0.5457 0.0147  -0.1382 0.0374  271  SER D C   
10944 O  O   . SER D 271 ? 0.7533 1.0905 0.6772 0.0184  -0.1444 0.0401  271  SER D O   
10945 C  CB  . SER D 271 ? 0.5339 0.9224 0.4127 0.0039  -0.1577 0.0181  271  SER D CB  
10946 O  OG  . SER D 271 ? 0.5105 0.9098 0.3763 0.0111  -0.1666 0.0429  271  SER D OG  
10947 N  N   . PHE D 272 ? 0.5814 0.8982 0.4734 0.0178  -0.1289 0.0498  272  PHE D N   
10948 C  CA  . PHE D 272 ? 0.4565 0.7506 0.3634 0.0253  -0.1252 0.0668  272  PHE D CA  
10949 C  C   . PHE D 272 ? 0.4304 0.7237 0.3200 0.0294  -0.1278 0.0906  272  PHE D C   
10950 O  O   . PHE D 272 ? 0.5536 0.8397 0.4264 0.0261  -0.1191 0.0946  272  PHE D O   
10951 C  CB  . PHE D 272 ? 0.4429 0.7109 0.3578 0.0241  -0.1103 0.0593  272  PHE D CB  
10952 C  CG  . PHE D 272 ? 0.5263 0.7870 0.4606 0.0216  -0.1064 0.0402  272  PHE D CG  
10953 C  CD1 . PHE D 272 ? 0.5006 0.7563 0.4298 0.0163  -0.0977 0.0218  272  PHE D CD1 
10954 C  CD2 . PHE D 272 ? 0.4321 0.6902 0.3901 0.0248  -0.1107 0.0410  272  PHE D CD2 
10955 C  CE1 . PHE D 272 ? 0.3763 0.6216 0.3221 0.0137  -0.0936 0.0057  272  PHE D CE1 
10956 C  CE2 . PHE D 272 ? 0.3246 0.5751 0.2996 0.0212  -0.1062 0.0247  272  PHE D CE2 
10957 C  CZ  . PHE D 272 ? 0.3180 0.5606 0.2865 0.0154  -0.0978 0.0076  272  PHE D CZ  
10958 N  N   . SER D 273 ? 0.5065 0.8070 0.4010 0.0366  -0.1393 0.1068  273  SER D N   
10959 C  CA  . SER D 273 ? 0.6744 0.9708 0.5527 0.0413  -0.1425 0.1317  273  SER D CA  
10960 C  C   . SER D 273 ? 0.7022 0.9686 0.5796 0.0408  -0.1295 0.1411  273  SER D C   
10961 O  O   . SER D 273 ? 0.6124 0.8573 0.5108 0.0440  -0.1236 0.1392  273  SER D O   
10962 C  CB  . SER D 273 ? 0.6760 0.9784 0.5675 0.0521  -0.1558 0.1473  273  SER D CB  
10963 O  OG  . SER D 273 ? 0.6961 0.9899 0.5723 0.0576  -0.1588 0.1728  273  SER D OG  
10964 N  N   . GLY D 274 ? 0.6974 0.9642 0.5500 0.0358  -0.1248 0.1506  274  GLY D N   
10965 C  CA  . GLY D 274 ? 0.6033 0.8461 0.4537 0.0330  -0.1126 0.1590  274  GLY D CA  
10966 C  C   . GLY D 274 ? 0.7233 0.9575 0.5839 0.0278  -0.1002 0.1395  274  GLY D C   
10967 O  O   . GLY D 274 ? 0.6873 0.9039 0.5495 0.0250  -0.0901 0.1438  274  GLY D O   
10968 N  N   . GLY D 275 ? 0.6373 0.8840 0.5053 0.0265  -0.1012 0.1184  275  GLY D N   
10969 C  CA  . GLY D 275 ? 0.4741 0.7131 0.3510 0.0230  -0.0903 0.0998  275  GLY D CA  
10970 C  C   . GLY D 275 ? 0.5277 0.7440 0.4297 0.0273  -0.0869 0.0977  275  GLY D C   
10971 O  O   . GLY D 275 ? 0.5356 0.7405 0.4448 0.0256  -0.0774 0.0876  275  GLY D O   
10972 N  N   . ILE D 276 ? 0.5393 0.7498 0.4540 0.0336  -0.0946 0.1077  276  ILE D N   
10973 C  CA  . ILE D 276 ? 0.5661 0.7572 0.5042 0.0378  -0.0914 0.1048  276  ILE D CA  
10974 C  C   . ILE D 276 ? 0.4324 0.6334 0.3872 0.0421  -0.0997 0.0989  276  ILE D C   
10975 O  O   . ILE D 276 ? 0.4048 0.6276 0.3540 0.0422  -0.1095 0.0991  276  ILE D O   
10976 C  CB  . ILE D 276 ? 0.5539 0.7232 0.4957 0.0420  -0.0894 0.1223  276  ILE D CB  
10977 C  CG1 . ILE D 276 ? 0.4472 0.6212 0.3899 0.0493  -0.1003 0.1381  276  ILE D CG1 
10978 C  CG2 . ILE D 276 ? 0.6030 0.7647 0.5287 0.0360  -0.0816 0.1300  276  ILE D CG2 
10979 C  CD1 . ILE D 276 ? 0.4290 0.5778 0.3771 0.0545  -0.0983 0.1540  276  ILE D CD1 
10980 N  N   . THR D 277 ? 0.4360 0.6227 0.4114 0.0449  -0.0958 0.0934  277  THR D N   
10981 C  CA  . THR D 277 ? 0.5325 0.7296 0.5269 0.0477  -0.1017 0.0865  277  THR D CA  
10982 C  C   . THR D 277 ? 0.6302 0.8075 0.6447 0.0515  -0.0951 0.0849  277  THR D C   
10983 O  O   . THR D 277 ? 0.6903 0.8473 0.7030 0.0500  -0.0856 0.0836  277  THR D O   
10984 C  CB  . THR D 277 ? 0.4851 0.6983 0.4792 0.0403  -0.1025 0.0669  277  THR D CB  
10985 O  OG1 . THR D 277 ? 0.4723 0.6992 0.4857 0.0414  -0.1091 0.0613  277  THR D OG1 
10986 C  CG2 . THR D 277 ? 0.3566 0.5525 0.3522 0.0357  -0.0906 0.0535  277  THR D CG2 
10987 N  N   . ASN D 278 ? 0.6495 0.8351 0.6829 0.0564  -0.1002 0.0848  278  ASN D N   
10988 C  CA  . ASN D 278 ? 0.4086 0.5804 0.4621 0.0593  -0.0938 0.0807  278  ASN D CA  
10989 C  C   . ASN D 278 ? 0.4867 0.6614 0.5473 0.0516  -0.0887 0.0628  278  ASN D C   
10990 O  O   . ASN D 278 ? 0.6778 0.8726 0.7388 0.0464  -0.0943 0.0536  278  ASN D O   
10991 C  CB  . ASN D 278 ? 0.2484 0.4312 0.3203 0.0685  -0.1009 0.0884  278  ASN D CB  
10992 C  CG  . ASN D 278 ? 0.4042 0.5792 0.4983 0.0708  -0.0940 0.0818  278  ASN D CG  
10993 O  OD1 . ASN D 278 ? 0.4815 0.6757 0.5941 0.0717  -0.0978 0.0762  278  ASN D OD1 
10994 N  ND2 . ASN D 278 ? 0.3621 0.5108 0.4544 0.0713  -0.0837 0.0822  278  ASN D ND2 
10995 N  N   . GLY D 279 ? 0.2710 0.4249 0.3357 0.0503  -0.0783 0.0578  279  GLY D N   
10996 C  CA  . GLY D 279 ? 0.2454 0.3972 0.3161 0.0435  -0.0725 0.0428  279  GLY D CA  
10997 C  C   . GLY D 279 ? 0.4419 0.6147 0.5291 0.0404  -0.0780 0.0351  279  GLY D C   
10998 O  O   . GLY D 279 ? 0.3829 0.5679 0.4665 0.0330  -0.0809 0.0241  279  GLY D O   
10999 N  N   . ALA D 280 ? 0.3729 0.5512 0.4788 0.0460  -0.0793 0.0402  280  ALA D N   
11000 C  CA  . ALA D 280 ? 0.3040 0.5046 0.4301 0.0428  -0.0834 0.0327  280  ALA D CA  
11001 C  C   . ALA D 280 ? 0.3247 0.5539 0.4472 0.0402  -0.0963 0.0311  280  ALA D C   
11002 O  O   . ALA D 280 ? 0.3801 0.6250 0.5081 0.0309  -0.0990 0.0183  280  ALA D O   
11003 C  CB  . ALA D 280 ? 0.2533 0.4577 0.4006 0.0515  -0.0826 0.0397  280  ALA D CB  
11004 N  N   . HIS D 281 ? 0.3577 0.5933 0.4698 0.0479  -0.1044 0.0443  281  HIS D N   
11005 C  CA  . HIS D 281 ? 0.2706 0.5344 0.3759 0.0464  -0.1176 0.0446  281  HIS D CA  
11006 C  C   . HIS D 281 ? 0.3298 0.5966 0.4194 0.0343  -0.1167 0.0297  281  HIS D C   
11007 O  O   . HIS D 281 ? 0.3493 0.6402 0.4426 0.0275  -0.1243 0.0197  281  HIS D O   
11008 C  CB  . HIS D 281 ? 0.3584 0.6222 0.4482 0.0555  -0.1245 0.0626  281  HIS D CB  
11009 C  CG  . HIS D 281 ? 0.5298 0.8258 0.6149 0.0565  -0.1396 0.0663  281  HIS D CG  
11010 N  ND1 . HIS D 281 ? 0.5383 0.8439 0.5985 0.0505  -0.1446 0.0642  281  HIS D ND1 
11011 C  CD2 . HIS D 281 ? 0.5662 0.8891 0.6682 0.0632  -0.1513 0.0717  281  HIS D CD2 
11012 C  CE1 . HIS D 281 ? 0.5232 0.8596 0.5832 0.0529  -0.1591 0.0686  281  HIS D CE1 
11013 N  NE2 . HIS D 281 ? 0.6674 1.0154 0.7534 0.0609  -0.1639 0.0734  281  HIS D NE2 
11014 N  N   . TRP D 282 ? 0.4299 0.6730 0.5025 0.0318  -0.1074 0.0274  282  TRP D N   
11015 C  CA  . TRP D 282 ? 0.4030 0.6453 0.4631 0.0217  -0.1044 0.0114  282  TRP D CA  
11016 C  C   . TRP D 282 ? 0.4909 0.7359 0.5699 0.0133  -0.1015 -0.0040 282  TRP D C   
11017 O  O   . TRP D 282 ? 0.5174 0.7856 0.6014 0.0061  -0.1093 -0.0140 282  TRP D O   
11018 C  CB  . TRP D 282 ? 0.3907 0.6060 0.4361 0.0222  -0.0932 0.0113  282  TRP D CB  
11019 C  CG  . TRP D 282 ? 0.5968 0.8099 0.6283 0.0143  -0.0894 -0.0046 282  TRP D CG  
11020 C  CD1 . TRP D 282 ? 0.5390 0.7693 0.5680 0.0060  -0.0947 -0.0193 282  TRP D CD1 
11021 C  CD2 . TRP D 282 ? 0.4901 0.6830 0.5092 0.0147  -0.0794 -0.0081 282  TRP D CD2 
11022 N  NE1 . TRP D 282 ? 0.4220 0.6411 0.4370 0.0016  -0.0878 -0.0323 282  TRP D NE1 
11023 C  CE2 . TRP D 282 ? 0.4914 0.6885 0.5009 0.0076  -0.0784 -0.0251 282  TRP D CE2 
11024 C  CE3 . TRP D 282 ? 0.4561 0.6291 0.4718 0.0203  -0.0716 0.0008  282  TRP D CE3 
11025 C  CZ2 . TRP D 282 ? 0.4307 0.6125 0.4285 0.0079  -0.0694 -0.0327 282  TRP D CZ2 
11026 C  CZ3 . TRP D 282 ? 0.3964 0.5573 0.4010 0.0197  -0.0635 -0.0063 282  TRP D CZ3 
11027 C  CH2 . TRP D 282 ? 0.2867 0.4519 0.2831 0.0144  -0.0623 -0.0226 282  TRP D CH2 
11028 N  N   . TYR D 283 ? 0.4199 0.6412 0.5086 0.0133  -0.0902 -0.0058 283  TYR D N   
11029 C  CA  . TYR D 283 ? 0.4634 0.6847 0.5722 0.0060  -0.0858 -0.0164 283  TYR D CA  
11030 C  C   . TYR D 283 ? 0.5278 0.7256 0.6457 0.0110  -0.0750 -0.0097 283  TYR D C   
11031 O  O   . TYR D 283 ? 0.4785 0.6551 0.5836 0.0167  -0.0692 -0.0029 283  TYR D O   
11032 C  CB  . TYR D 283 ? 0.4282 0.6419 0.5306 -0.0059 -0.0817 -0.0345 283  TYR D CB  
11033 C  CG  . TYR D 283 ? 0.5127 0.6981 0.5965 -0.0045 -0.0723 -0.0369 283  TYR D CG  
11034 C  CD1 . TYR D 283 ? 0.4892 0.6469 0.5768 -0.0035 -0.0607 -0.0365 283  TYR D CD1 
11035 C  CD2 . TYR D 283 ? 0.5433 0.7319 0.6059 -0.0038 -0.0751 -0.0397 283  TYR D CD2 
11036 C  CE1 . TYR D 283 ? 0.4359 0.5708 0.5082 -0.0008 -0.0532 -0.0382 283  TYR D CE1 
11037 C  CE2 . TYR D 283 ? 0.4327 0.5993 0.4811 -0.0014 -0.0665 -0.0423 283  TYR D CE2 
11038 C  CZ  . TYR D 283 ? 0.5126 0.6530 0.5667 0.0005  -0.0562 -0.0415 283  TYR D CZ  
11039 O  OH  . TYR D 283 ? 0.6625 0.7839 0.7040 0.0041  -0.0487 -0.0437 283  TYR D OH  
11040 N  N   . GLU D 284 ? 0.5397 0.7436 0.6797 0.0085  -0.0722 -0.0119 284  GLU D N   
11041 C  CA  . GLU D 284 ? 0.5396 0.7235 0.6873 0.0132  -0.0617 -0.0058 284  GLU D CA  
11042 C  C   . GLU D 284 ? 0.4671 0.6235 0.6085 0.0067  -0.0498 -0.0133 284  GLU D C   
11043 O  O   . GLU D 284 ? 0.5085 0.6638 0.6508 -0.0038 -0.0481 -0.0254 284  GLU D O   
11044 C  CB  . GLU D 284 ? 0.4582 0.6609 0.6321 0.0145  -0.0622 -0.0041 284  GLU D CB  
11045 C  CG  . GLU D 284 ? 0.4167 0.6386 0.5976 0.0263  -0.0717 0.0077  284  GLU D CG  
11046 C  CD  . GLU D 284 ? 0.4383 0.6743 0.6459 0.0307  -0.0691 0.0099  284  GLU D CD  
11047 O  OE1 . GLU D 284 ? 0.2413 0.5004 0.4611 0.0394  -0.0782 0.0169  284  GLU D OE1 
11048 O  OE2 . GLU D 284 ? 0.5933 0.8178 0.8098 0.0259  -0.0575 0.0051  284  GLU D OE2 
11049 N  N   . LEU D 285 ? 0.2529 0.3863 0.3876 0.0130  -0.0418 -0.0058 285  LEU D N   
11050 C  CA  . LEU D 285 ? 0.4156 0.5231 0.5448 0.0090  -0.0309 -0.0100 285  LEU D CA  
11051 C  C   . LEU D 285 ? 0.4845 0.5786 0.6167 0.0153  -0.0233 -0.0013 285  LEU D C   
11052 O  O   . LEU D 285 ? 0.5076 0.6059 0.6400 0.0238  -0.0262 0.0076  285  LEU D O   
11053 C  CB  . LEU D 285 ? 0.3913 0.4826 0.4996 0.0102  -0.0300 -0.0122 285  LEU D CB  
11054 C  CG  . LEU D 285 ? 0.4047 0.4896 0.4996 0.0197  -0.0314 -0.0019 285  LEU D CG  
11055 C  CD1 . LEU D 285 ? 0.2787 0.3400 0.3686 0.0235  -0.0224 0.0028  285  LEU D CD1 
11056 C  CD2 . LEU D 285 ? 0.3061 0.3942 0.3851 0.0197  -0.0357 -0.0055 285  LEU D CD2 
11057 N  N   . SER D 286 ? 0.5301 0.6068 0.6634 0.0108  -0.0132 -0.0039 286  SER D N   
11058 C  CA  . SER D 286 ? 0.5080 0.5729 0.6424 0.0157  -0.0054 0.0032  286  SER D CA  
11059 C  C   . SER D 286 ? 0.5051 0.5424 0.6223 0.0169  0.0018  0.0051  286  SER D C   
11060 O  O   . SER D 286 ? 0.6114 0.6369 0.7211 0.0123  0.0036  -0.0002 286  SER D O   
11061 C  CB  . SER D 286 ? 0.4491 0.5242 0.6031 0.0100  0.0005  0.0004  286  SER D CB  
11062 O  OG  . SER D 286 ? 0.4534 0.5576 0.6249 0.0107  -0.0075 -0.0008 286  SER D OG  
11063 N  N   . GLY D 287 ? 0.4064 0.4337 0.5171 0.0237  0.0055  0.0124  287  GLY D N   
11064 C  CA  . GLY D 287 ? 0.2792 0.2841 0.3736 0.0259  0.0107  0.0153  287  GLY D CA  
11065 C  C   . GLY D 287 ? 0.3604 0.3617 0.4407 0.0313  0.0049  0.0175  287  GLY D C   
11066 O  O   . GLY D 287 ? 0.4202 0.4062 0.4881 0.0335  0.0077  0.0189  287  GLY D O   
11067 N  N   . GLY D 288 ? 0.3595 0.3760 0.4419 0.0336  -0.0031 0.0185  288  GLY D N   
11068 C  CA  . GLY D 288 ? 0.4232 0.4395 0.4931 0.0373  -0.0079 0.0207  288  GLY D CA  
11069 C  C   . GLY D 288 ? 0.4197 0.4270 0.4811 0.0425  -0.0065 0.0278  288  GLY D C   
11070 O  O   . GLY D 288 ? 0.2556 0.2599 0.3211 0.0444  -0.0039 0.0314  288  GLY D O   
11071 N  N   . MET D 289 ? 0.4258 0.4300 0.4759 0.0446  -0.0081 0.0289  289  MET D N   
11072 C  CA  . MET D 289 ? 0.3533 0.3513 0.3956 0.0478  -0.0077 0.0345  289  MET D CA  
11073 C  C   . MET D 289 ? 0.4170 0.4224 0.4611 0.0487  -0.0122 0.0398  289  MET D C   
11074 O  O   . MET D 289 ? 0.4395 0.4379 0.4821 0.0503  -0.0109 0.0438  289  MET D O   
11075 C  CB  . MET D 289 ? 0.2362 0.2331 0.2687 0.0495  -0.0082 0.0337  289  MET D CB  
11076 C  CG  . MET D 289 ? 0.3536 0.3466 0.3786 0.0516  -0.0082 0.0385  289  MET D CG  
11077 S  SD  . MET D 289 ? 0.5031 0.4990 0.5205 0.0548  -0.0085 0.0371  289  MET D SD  
11078 C  CE  . MET D 289 ? 0.3565 0.3676 0.3751 0.0533  -0.0118 0.0335  289  MET D CE  
11079 N  N   . GLN D 290 ? 0.2758 0.2941 0.3221 0.0478  -0.0176 0.0399  290  GLN D N   
11080 C  CA  . GLN D 290 ? 0.3844 0.4083 0.4307 0.0491  -0.0224 0.0469  290  GLN D CA  
11081 C  C   . GLN D 290 ? 0.3959 0.4141 0.4510 0.0521  -0.0209 0.0502  290  GLN D C   
11082 O  O   . GLN D 290 ? 0.3732 0.3817 0.4250 0.0537  -0.0198 0.0547  290  GLN D O   
11083 C  CB  . GLN D 290 ? 0.4520 0.4923 0.4996 0.0479  -0.0286 0.0467  290  GLN D CB  
11084 C  CG  . GLN D 290 ? 0.2056 0.2514 0.2495 0.0494  -0.0341 0.0560  290  GLN D CG  
11085 C  CD  . GLN D 290 ? 0.2744 0.3376 0.3220 0.0495  -0.0411 0.0568  290  GLN D CD  
11086 O  OE1 . GLN D 290 ? 0.5044 0.5783 0.5425 0.0474  -0.0450 0.0578  290  GLN D OE1 
11087 N  NE2 . GLN D 290 ? 0.1409 0.2091 0.2021 0.0521  -0.0429 0.0562  290  GLN D NE2 
11088 N  N   . ASP D 291 ? 0.4382 0.4633 0.5054 0.0526  -0.0205 0.0470  291  ASP D N   
11089 C  CA  . ASP D 291 ? 0.4325 0.4559 0.5107 0.0567  -0.0188 0.0494  291  ASP D CA  
11090 C  C   . ASP D 291 ? 0.4331 0.4405 0.5080 0.0573  -0.0108 0.0478  291  ASP D C   
11091 O  O   . ASP D 291 ? 0.4883 0.4900 0.5681 0.0614  -0.0082 0.0495  291  ASP D O   
11092 C  CB  . ASP D 291 ? 0.5039 0.5429 0.5982 0.0565  -0.0200 0.0456  291  ASP D CB  
11093 C  CG  . ASP D 291 ? 0.6088 0.6659 0.7065 0.0573  -0.0295 0.0484  291  ASP D CG  
11094 O  OD1 . ASP D 291 ? 0.6199 0.6758 0.7062 0.0581  -0.0343 0.0542  291  ASP D OD1 
11095 O  OD2 . ASP D 291 ? 0.5800 0.6538 0.6912 0.0564  -0.0323 0.0450  291  ASP D OD2 
11096 N  N   . PHE D 292 ? 0.4060 0.4062 0.4717 0.0539  -0.0072 0.0444  292  PHE D N   
11097 C  CA  . PHE D 292 ? 0.2292 0.2159 0.2890 0.0542  -0.0003 0.0433  292  PHE D CA  
11098 C  C   . PHE D 292 ? 0.1726 0.1502 0.2237 0.0557  -0.0015 0.0467  292  PHE D C   
11099 O  O   . PHE D 292 ? 0.3928 0.3616 0.4435 0.0575  0.0028  0.0460  292  PHE D O   
11100 C  CB  . PHE D 292 ? 0.1550 0.1359 0.2062 0.0514  0.0028  0.0406  292  PHE D CB  
11101 C  CG  . PHE D 292 ? 0.2251 0.1934 0.2663 0.0519  0.0082  0.0409  292  PHE D CG  
11102 C  CD1 . PHE D 292 ? 0.3184 0.2818 0.3622 0.0516  0.0155  0.0392  292  PHE D CD1 
11103 C  CD2 . PHE D 292 ? 0.1908 0.1544 0.2199 0.0523  0.0058  0.0427  292  PHE D CD2 
11104 C  CE1 . PHE D 292 ? 0.3291 0.2820 0.3611 0.0519  0.0203  0.0396  292  PHE D CE1 
11105 C  CE2 . PHE D 292 ? 0.4311 0.3855 0.4500 0.0525  0.0095  0.0427  292  PHE D CE2 
11106 C  CZ  . PHE D 292 ? 0.4772 0.4255 0.4962 0.0525  0.0167  0.0412  292  PHE D CZ  
11107 N  N   . ASN D 293 ? 0.2686 0.2487 0.3126 0.0541  -0.0066 0.0496  293  ASN D N   
11108 C  CA  . ASN D 293 ? 0.3941 0.3666 0.4310 0.0533  -0.0082 0.0531  293  ASN D CA  
11109 C  C   . ASN D 293 ? 0.3611 0.3275 0.4046 0.0567  -0.0082 0.0560  293  ASN D C   
11110 O  O   . ASN D 293 ? 0.4604 0.4139 0.5001 0.0569  -0.0052 0.0550  293  ASN D O   
11111 C  CB  . ASN D 293 ? 0.3708 0.3511 0.4022 0.0504  -0.0134 0.0566  293  ASN D CB  
11112 C  CG  . ASN D 293 ? 0.3422 0.3251 0.3654 0.0481  -0.0127 0.0540  293  ASN D CG  
11113 O  OD1 . ASN D 293 ? 0.3416 0.3208 0.3583 0.0455  -0.0128 0.0547  293  ASN D OD1 
11114 N  ND2 . ASN D 293 ? 0.3281 0.3175 0.3523 0.0491  -0.0123 0.0505  293  ASN D ND2 
11115 N  N   . TYR D 294 ? 0.2539 0.2294 0.3071 0.0599  -0.0119 0.0592  294  TYR D N   
11116 C  CA  . TYR D 294 ? 0.5210 0.4910 0.5813 0.0652  -0.0131 0.0637  294  TYR D CA  
11117 C  C   . TYR D 294 ? 0.5278 0.4921 0.5971 0.0700  -0.0066 0.0590  294  TYR D C   
11118 O  O   . TYR D 294 ? 0.4307 0.3818 0.5011 0.0740  -0.0044 0.0599  294  TYR D O   
11119 C  CB  . TYR D 294 ? 0.5450 0.5297 0.6135 0.0684  -0.0199 0.0692  294  TYR D CB  
11120 C  CG  . TYR D 294 ? 0.4883 0.4666 0.5636 0.0757  -0.0223 0.0762  294  TYR D CG  
11121 C  CD1 . TYR D 294 ? 0.4888 0.4511 0.5551 0.0749  -0.0236 0.0829  294  TYR D CD1 
11122 C  CD2 . TYR D 294 ? 0.3440 0.3323 0.4358 0.0835  -0.0232 0.0763  294  TYR D CD2 
11123 C  CE1 . TYR D 294 ? 0.4791 0.4316 0.5512 0.0825  -0.0255 0.0902  294  TYR D CE1 
11124 C  CE2 . TYR D 294 ? 0.2543 0.2363 0.3535 0.0923  -0.0256 0.0832  294  TYR D CE2 
11125 C  CZ  . TYR D 294 ? 0.4658 0.4281 0.5545 0.0923  -0.0267 0.0905  294  TYR D CZ  
11126 O  OH  . TYR D 294 ? 0.5069 0.4592 0.6025 0.1020  -0.0288 0.0982  294  TYR D OH  
11127 N  N   . ALA D 295 ? 0.4568 0.4307 0.5325 0.0694  -0.0030 0.0538  295  ALA D N   
11128 C  CA  . ALA D 295 ? 0.3881 0.3617 0.4744 0.0736  0.0041  0.0492  295  ALA D CA  
11129 C  C   . ALA D 295 ? 0.3123 0.2716 0.3878 0.0715  0.0124  0.0439  295  ALA D C   
11130 O  O   . ALA D 295 ? 0.3082 0.2639 0.3893 0.0754  0.0194  0.0399  295  ALA D O   
11131 C  CB  . ALA D 295 ? 0.2622 0.2537 0.3614 0.0723  0.0049  0.0464  295  ALA D CB  
11132 N  N   . PHE D 296 ? 0.3353 0.2881 0.3952 0.0658  0.0115  0.0436  296  PHE D N   
11133 C  CA  . PHE D 296 ? 0.4156 0.3579 0.4634 0.0635  0.0180  0.0390  296  PHE D CA  
11134 C  C   . PHE D 296 ? 0.4743 0.4050 0.5077 0.0603  0.0152  0.0392  296  PHE D C   
11135 O  O   . PHE D 296 ? 0.3374 0.2610 0.3584 0.0577  0.0188  0.0354  296  PHE D O   
11136 C  CB  . PHE D 296 ? 0.4573 0.4044 0.5001 0.0597  0.0205  0.0379  296  PHE D CB  
11137 C  CG  . PHE D 296 ? 0.5859 0.5431 0.6426 0.0603  0.0250  0.0364  296  PHE D CG  
11138 C  CD1 . PHE D 296 ? 0.5467 0.5169 0.6160 0.0602  0.0198  0.0380  296  PHE D CD1 
11139 C  CD2 . PHE D 296 ? 0.5982 0.5534 0.6551 0.0600  0.0345  0.0330  296  PHE D CD2 
11140 C  CE1 . PHE D 296 ? 0.4892 0.4708 0.5727 0.0591  0.0235  0.0357  296  PHE D CE1 
11141 C  CE2 . PHE D 296 ? 0.4306 0.3968 0.5018 0.0589  0.0393  0.0314  296  PHE D CE2 
11142 C  CZ  . PHE D 296 ? 0.5361 0.5158 0.6216 0.0581  0.0335  0.0325  296  PHE D CZ  
11143 N  N   . SER D 297 ? 0.4410 0.3708 0.4758 0.0598  0.0089  0.0438  297  SER D N   
11144 C  CA  . SER D 297 ? 0.3147 0.2342 0.3384 0.0551  0.0064  0.0441  297  SER D CA  
11145 C  C   . SER D 297 ? 0.2875 0.2008 0.3159 0.0561  0.0023  0.0499  297  SER D C   
11146 O  O   . SER D 297 ? 0.4435 0.3595 0.4834 0.0623  0.0014  0.0534  297  SER D O   
11147 C  CB  . SER D 297 ? 0.3302 0.2581 0.3447 0.0495  0.0024  0.0453  297  SER D CB  
11148 O  OG  . SER D 297 ? 0.2938 0.2324 0.3129 0.0489  -0.0030 0.0508  297  SER D OG  
11149 N  N   . ASN D 298 ? 0.1641 0.0699 0.1837 0.0497  -0.0004 0.0513  298  ASN D N   
11150 C  CA  . ASN D 298 ? 0.4170 0.3149 0.4386 0.0489  -0.0039 0.0585  298  ASN D CA  
11151 C  C   . ASN D 298 ? 0.4406 0.3541 0.4631 0.0468  -0.0097 0.0662  298  ASN D C   
11152 O  O   . ASN D 298 ? 0.3701 0.2805 0.3941 0.0470  -0.0130 0.0744  298  ASN D O   
11153 C  CB  . ASN D 298 ? 0.3994 0.2819 0.4112 0.0405  -0.0034 0.0563  298  ASN D CB  
11154 C  CG  . ASN D 298 ? 0.4316 0.2951 0.4412 0.0423  0.0023  0.0482  298  ASN D CG  
11155 O  OD1 . ASN D 298 ? 0.4529 0.3121 0.4705 0.0514  0.0062  0.0462  298  ASN D OD1 
11156 N  ND2 . ASN D 298 ? 0.3189 0.1724 0.3179 0.0333  0.0031  0.0422  298  ASN D ND2 
11157 N  N   . CYS D 299 ? 0.2864 0.2158 0.3068 0.0450  -0.0105 0.0636  299  CYS D N   
11158 C  CA  . CYS D 299 ? 0.3153 0.2595 0.3337 0.0417  -0.0148 0.0682  299  CYS D CA  
11159 C  C   . CYS D 299 ? 0.3590 0.3125 0.3841 0.0463  -0.0184 0.0741  299  CYS D C   
11160 O  O   . CYS D 299 ? 0.4874 0.4446 0.5209 0.0524  -0.0178 0.0720  299  CYS D O   
11161 C  CB  . CYS D 299 ? 0.1280 0.0846 0.1431 0.0403  -0.0143 0.0631  299  CYS D CB  
11162 S  SG  . CYS D 299 ? 0.3669 0.3390 0.3773 0.0346  -0.0177 0.0666  299  CYS D SG  
11163 N  N   . PHE D 300 ? 0.3802 0.3389 0.4011 0.0428  -0.0221 0.0814  300  PHE D N   
11164 C  CA  . PHE D 300 ? 0.3434 0.3147 0.3670 0.0461  -0.0267 0.0872  300  PHE D CA  
11165 C  C   . PHE D 300 ? 0.3927 0.3830 0.4115 0.0426  -0.0282 0.0847  300  PHE D C   
11166 O  O   . PHE D 300 ? 0.4124 0.4082 0.4235 0.0369  -0.0289 0.0887  300  PHE D O   
11167 C  CB  . PHE D 300 ? 0.4123 0.3755 0.4322 0.0452  -0.0296 0.0986  300  PHE D CB  
11168 C  CG  . PHE D 300 ? 0.5336 0.4774 0.5595 0.0512  -0.0288 0.1018  300  PHE D CG  
11169 C  CD1 . PHE D 300 ? 0.4423 0.3804 0.4688 0.0557  -0.0328 0.1133  300  PHE D CD1 
11170 C  CD2 . PHE D 300 ? 0.6094 0.5402 0.6396 0.0532  -0.0237 0.0937  300  PHE D CD2 
11171 C  CE1 . PHE D 300 ? 0.4684 0.3870 0.5016 0.0632  -0.0317 0.1164  300  PHE D CE1 
11172 C  CE2 . PHE D 300 ? 0.6541 0.5665 0.6901 0.0598  -0.0219 0.0953  300  PHE D CE2 
11173 C  CZ  . PHE D 300 ? 0.5191 0.4248 0.5577 0.0654  -0.0258 0.1066  300  PHE D CZ  
11174 N  N   . GLU D 301 ? 0.2822 0.2820 0.3059 0.0456  -0.0279 0.0777  301  GLU D N   
11175 C  CA  . GLU D 301 ? 0.1388 0.1537 0.1585 0.0435  -0.0284 0.0734  301  GLU D CA  
11176 C  C   . GLU D 301 ? 0.3383 0.3675 0.3586 0.0448  -0.0333 0.0754  301  GLU D C   
11177 O  O   . GLU D 301 ? 0.3188 0.3501 0.3473 0.0487  -0.0357 0.0751  301  GLU D O   
11178 C  CB  . GLU D 301 ? 0.2587 0.2722 0.2817 0.0451  -0.0247 0.0643  301  GLU D CB  
11179 C  CG  . GLU D 301 ? 0.4140 0.4394 0.4341 0.0445  -0.0246 0.0584  301  GLU D CG  
11180 C  CD  . GLU D 301 ? 0.5462 0.5656 0.5667 0.0461  -0.0204 0.0518  301  GLU D CD  
11181 O  OE1 . GLU D 301 ? 0.6171 0.6320 0.6336 0.0455  -0.0186 0.0524  301  GLU D OE1 
11182 O  OE2 . GLU D 301 ? 0.5907 0.6098 0.6152 0.0475  -0.0191 0.0464  301  GLU D OE2 
11183 N  N   . LEU D 302 ? 0.4256 0.4666 0.4371 0.0412  -0.0348 0.0773  302  LEU D N   
11184 C  CA  . LEU D 302 ? 0.4173 0.4745 0.4260 0.0415  -0.0390 0.0762  302  LEU D CA  
11185 C  C   . LEU D 302 ? 0.4665 0.5315 0.4753 0.0410  -0.0365 0.0643  302  LEU D C   
11186 O  O   . LEU D 302 ? 0.4947 0.5549 0.5026 0.0405  -0.0318 0.0597  302  LEU D O   
11187 C  CB  . LEU D 302 ? 0.3998 0.4662 0.3965 0.0375  -0.0408 0.0840  302  LEU D CB  
11188 C  CG  . LEU D 302 ? 0.4244 0.4823 0.4178 0.0372  -0.0434 0.0979  302  LEU D CG  
11189 C  CD1 . LEU D 302 ? 0.4394 0.5100 0.4190 0.0324  -0.0446 0.1050  302  LEU D CD1 
11190 C  CD2 . LEU D 302 ? 0.5141 0.5702 0.5159 0.0438  -0.0490 0.1016  302  LEU D CD2 
11191 N  N   . THR D 303 ? 0.4150 0.4917 0.4246 0.0412  -0.0400 0.0592  303  THR D N   
11192 C  CA  . THR D 303 ? 0.4917 0.5747 0.4992 0.0400  -0.0376 0.0473  303  THR D CA  
11193 C  C   . THR D 303 ? 0.5550 0.6547 0.5501 0.0373  -0.0397 0.0471  303  THR D C   
11194 O  O   . THR D 303 ? 0.6162 0.7263 0.6070 0.0364  -0.0456 0.0528  303  THR D O   
11195 C  CB  . THR D 303 ? 0.5084 0.5926 0.5252 0.0400  -0.0393 0.0391  303  THR D CB  
11196 O  OG1 . THR D 303 ? 0.5350 0.6070 0.5631 0.0423  -0.0375 0.0414  303  THR D OG1 
11197 C  CG2 . THR D 303 ? 0.4051 0.4875 0.4203 0.0389  -0.0351 0.0264  303  THR D CG2 
11198 N  N   . ILE D 304 ? 0.6179 0.7211 0.6069 0.0367  -0.0348 0.0410  304  ILE D N   
11199 C  CA  . ILE D 304 ? 0.6508 0.7711 0.6271 0.0340  -0.0349 0.0404  304  ILE D CA  
11200 C  C   . ILE D 304 ? 0.5910 0.7188 0.5634 0.0344  -0.0318 0.0254  304  ILE D C   
11201 O  O   . ILE D 304 ? 0.3358 0.4578 0.3113 0.0374  -0.0260 0.0181  304  ILE D O   
11202 C  CB  . ILE D 304 ? 0.5092 0.6323 0.4798 0.0319  -0.0312 0.0492  304  ILE D CB  
11203 C  CG1 . ILE D 304 ? 0.4343 0.5487 0.4060 0.0303  -0.0347 0.0638  304  ILE D CG1 
11204 C  CG2 . ILE D 304 ? 0.4305 0.5733 0.3874 0.0286  -0.0297 0.0480  304  ILE D CG2 
11205 C  CD1 . ILE D 304 ? 0.5728 0.6851 0.5418 0.0265  -0.0308 0.0718  304  ILE D CD1 
11206 N  N   . GLU D 305 ? 0.4709 0.6117 0.4357 0.0318  -0.0362 0.0209  305  GLU D N   
11207 C  CA  . GLU D 305 ? 0.4316 0.5790 0.3911 0.0314  -0.0336 0.0052  305  GLU D CA  
11208 C  C   . GLU D 305 ? 0.5074 0.6712 0.4525 0.0303  -0.0296 0.0046  305  GLU D C   
11209 O  O   . GLU D 305 ? 0.6194 0.7968 0.5535 0.0268  -0.0331 0.0138  305  GLU D O   
11210 C  CB  . GLU D 305 ? 0.3265 0.4817 0.2848 0.0278  -0.0408 -0.0006 305  GLU D CB  
11211 C  CG  . GLU D 305 ? 0.2635 0.4063 0.2378 0.0279  -0.0441 -0.0003 305  GLU D CG  
11212 C  CD  . GLU D 305 ? 0.4673 0.5937 0.4504 0.0286  -0.0383 -0.0135 305  GLU D CD  
11213 O  OE1 . GLU D 305 ? 0.4566 0.5717 0.4526 0.0283  -0.0388 -0.0125 305  GLU D OE1 
11214 O  OE2 . GLU D 305 ? 0.4262 0.5502 0.4032 0.0298  -0.0326 -0.0244 305  GLU D OE2 
11215 N  N   . LEU D 306 ? 0.4298 0.5932 0.3750 0.0336  -0.0219 -0.0057 306  LEU D N   
11216 C  CA  . LEU D 306 ? 0.4556 0.6365 0.3901 0.0331  -0.0162 -0.0057 306  LEU D CA  
11217 C  C   . LEU D 306 ? 0.4793 0.6755 0.4001 0.0319  -0.0138 -0.0199 306  LEU D C   
11218 O  O   . LEU D 306 ? 0.4791 0.6947 0.3859 0.0284  -0.0121 -0.0166 306  LEU D O   
11219 C  CB  . LEU D 306 ? 0.4304 0.6069 0.3744 0.0385  -0.0088 -0.0063 306  LEU D CB  
11220 C  CG  . LEU D 306 ? 0.5354 0.6999 0.4899 0.0383  -0.0109 0.0075  306  LEU D CG  
11221 C  CD1 . LEU D 306 ? 0.4122 0.5714 0.3775 0.0444  -0.0055 0.0050  306  LEU D CD1 
11222 C  CD2 . LEU D 306 ? 0.4681 0.6428 0.4152 0.0318  -0.0126 0.0224  306  LEU D CD2 
11223 N  N   . SER D 307 ? 0.5332 0.7200 0.4570 0.0340  -0.0132 -0.0361 307  SER D N   
11224 C  CA  . SER D 307 ? 0.4423 0.6406 0.3534 0.0331  -0.0101 -0.0530 307  SER D CA  
11225 C  C   . SER D 307 ? 0.4868 0.6775 0.3975 0.0292  -0.0157 -0.0660 307  SER D C   
11226 O  O   . SER D 307 ? 0.5710 0.7440 0.4950 0.0291  -0.0191 -0.0650 307  SER D O   
11227 C  CB  . SER D 307 ? 0.4403 0.6352 0.3556 0.0410  0.0006  -0.0646 307  SER D CB  
11228 O  OG  . SER D 307 ? 0.4535 0.6236 0.3844 0.0467  0.0018  -0.0684 307  SER D OG  
11229 N  N   . CYS D 308 ? 0.6145 0.8202 0.5094 0.0251  -0.0162 -0.0789 308  CYS D N   
11230 C  CA  . CYS D 308 ? 0.6013 0.8017 0.4952 0.0201  -0.0207 -0.0950 308  CYS D CA  
11231 C  C   . CYS D 308 ? 0.5735 0.7499 0.4775 0.0249  -0.0127 -0.1114 308  CYS D C   
11232 O  O   . CYS D 308 ? 0.6207 0.7799 0.5343 0.0217  -0.0154 -0.1187 308  CYS D O   
11233 C  CB  . CYS D 308 ? 0.4363 0.6601 0.3083 0.0142  -0.0231 -0.1059 308  CYS D CB  
11234 S  SG  . CYS D 308 ? 0.6166 0.8644 0.4772 0.0071  -0.0367 -0.0886 308  CYS D SG  
11235 N  N   . CYS D 309 ? 0.5025 0.6784 0.4044 0.0328  -0.0026 -0.1166 309  CYS D N   
11236 C  CA  . CYS D 309 ? 0.4937 0.6460 0.4050 0.0405  0.0057  -0.1301 309  CYS D CA  
11237 C  C   . CYS D 309 ? 0.5711 0.7057 0.4999 0.0475  0.0071  -0.1157 309  CYS D C   
11238 O  O   . CYS D 309 ? 0.3874 0.5323 0.3189 0.0523  0.0093  -0.1028 309  CYS D O   
11239 C  CB  . CYS D 309 ? 0.4528 0.6158 0.3550 0.0477  0.0160  -0.1425 309  CYS D CB  
11240 S  SG  . CYS D 309 ? 0.7173 0.8505 0.6313 0.0607  0.0269  -0.1585 309  CYS D SG  
11241 N  N   . LYS D 310 ? 0.6422 0.7509 0.5821 0.0470  0.0059  -0.1182 310  LYS D N   
11242 C  CA  . LYS D 310 ? 0.5959 0.6874 0.5505 0.0525  0.0063  -0.1043 310  LYS D CA  
11243 C  C   . LYS D 310 ? 0.6505 0.7385 0.6094 0.0651  0.0143  -0.1033 310  LYS D C   
11244 O  O   . LYS D 310 ? 0.7291 0.8211 0.6946 0.0691  0.0136  -0.0884 310  LYS D O   
11245 C  CB  . LYS D 310 ? 0.6780 0.7414 0.6418 0.0494  0.0057  -0.1089 310  LYS D CB  
11246 C  CG  . LYS D 310 ? 0.6042 0.6721 0.5708 0.0378  -0.0029 -0.1044 310  LYS D CG  
11247 C  CD  . LYS D 310 ? 0.5387 0.5802 0.5153 0.0337  -0.0017 -0.1100 310  LYS D CD  
11248 C  CE  . LYS D 310 ? 0.6055 0.6554 0.5885 0.0232  -0.0098 -0.1041 310  LYS D CE  
11249 N  NZ  . LYS D 310 ? 0.7912 0.8166 0.7862 0.0186  -0.0074 -0.1061 310  LYS D NZ  
11250 N  N   . TYR D 311 ? 0.6349 0.7163 0.5907 0.0715  0.0215  -0.1200 311  TYR D N   
11251 C  CA  . TYR D 311 ? 0.6225 0.7018 0.5841 0.0857  0.0294  -0.1214 311  TYR D CA  
11252 C  C   . TYR D 311 ? 0.7050 0.8047 0.6568 0.0893  0.0362  -0.1358 311  TYR D C   
11253 O  O   . TYR D 311 ? 0.7531 0.8398 0.7019 0.0942  0.0423  -0.1542 311  TYR D O   
11254 C  CB  . TYR D 311 ? 0.6867 0.7311 0.6569 0.0937  0.0334  -0.1277 311  TYR D CB  
11255 C  CG  . TYR D 311 ? 0.5886 0.6275 0.5694 0.1095  0.0380  -0.1208 311  TYR D CG  
11256 C  CD1 . TYR D 311 ? 0.5027 0.5106 0.4917 0.1159  0.0385  -0.1160 311  TYR D CD1 
11257 C  CD2 . TYR D 311 ? 0.4873 0.5534 0.4699 0.1175  0.0415  -0.1185 311  TYR D CD2 
11258 C  CE1 . TYR D 311 ? 0.5328 0.5371 0.5309 0.1311  0.0413  -0.1088 311  TYR D CE1 
11259 C  CE2 . TYR D 311 ? 0.5489 0.6136 0.5430 0.1321  0.0445  -0.1122 311  TYR D CE2 
11260 C  CZ  . TYR D 311 ? 0.5406 0.5743 0.5420 0.1394  0.0437  -0.1072 311  TYR D CZ  
11261 O  OH  . TYR D 311 ? 0.5793 0.6126 0.5914 0.1547  0.0453  -0.1000 311  TYR D OH  
11262 N  N   . PRO D 312 ? 0.6662 0.7973 0.6123 0.0866  0.0359  -0.1279 312  PRO D N   
11263 C  CA  . PRO D 312 ? 0.5722 0.7268 0.5080 0.0893  0.0434  -0.1402 312  PRO D CA  
11264 C  C   . PRO D 312 ? 0.7946 0.9526 0.7417 0.1052  0.0528  -0.1441 312  PRO D C   
11265 O  O   . PRO D 312 ? 0.7979 0.9413 0.7599 0.1139  0.0522  -0.1355 312  PRO D O   
11266 C  CB  . PRO D 312 ? 0.5264 0.7115 0.4538 0.0799  0.0396  -0.1257 312  PRO D CB  
11267 C  CG  . PRO D 312 ? 0.6971 0.8713 0.6298 0.0723  0.0294  -0.1081 312  PRO D CG  
11268 C  CD  . PRO D 312 ? 0.6483 0.7933 0.5962 0.0797  0.0291  -0.1073 312  PRO D CD  
11269 N  N   . ALA D 313 ? 0.8027 0.9820 0.7424 0.1092  0.0614  -0.1570 313  ALA D N   
11270 C  CA  . ALA D 313 ? 0.6903 0.8780 0.6418 0.1253  0.0710  -0.1624 313  ALA D CA  
11271 C  C   . ALA D 313 ? 0.6303 0.8500 0.5890 0.1247  0.0715  -0.1458 313  ALA D C   
11272 O  O   . ALA D 313 ? 0.6121 0.8512 0.5609 0.1114  0.0677  -0.1352 313  ALA D O   
11273 C  CB  . ALA D 313 ? 0.7269 0.9236 0.6680 0.1303  0.0814  -0.1855 313  ALA D CB  
11274 N  N   . ALA D 314 ? 0.6064 0.8318 0.5829 0.1390  0.0762  -0.1437 314  ALA D N   
11275 C  CA  . ALA D 314 ? 0.5430 0.7998 0.5301 0.1388  0.0771  -0.1295 314  ALA D CA  
11276 C  C   . ALA D 314 ? 0.6522 0.9451 0.6268 0.1274  0.0818  -0.1286 314  ALA D C   
11277 O  O   . ALA D 314 ? 0.6690 0.9762 0.6422 0.1155  0.0772  -0.1120 314  ALA D O   
11278 C  CB  . ALA D 314 ? 0.5379 0.8030 0.5447 0.1579  0.0836  -0.1339 314  ALA D CB  
11279 N  N   . SER D 315 ? 0.6257 0.9317 0.5901 0.1308  0.0915  -0.1465 315  SER D N   
11280 C  CA  . SER D 315 ? 0.4812 0.8239 0.4326 0.1215  0.0984  -0.1468 315  SER D CA  
11281 C  C   . SER D 315 ? 0.4498 0.7941 0.3839 0.1023  0.0897  -0.1318 315  SER D C   
11282 O  O   . SER D 315 ? 0.5047 0.8774 0.4297 0.0921  0.0930  -0.1233 315  SER D O   
11283 C  CB  . SER D 315 ? 0.4931 0.8416 0.4306 0.1266  0.1087  -0.1707 315  SER D CB  
11284 O  OG  . SER D 315 ? 0.4951 0.8151 0.4166 0.1210  0.1026  -0.1802 315  SER D OG  
11285 N  N   . THR D 316 ? 0.4796 0.7928 0.4099 0.0979  0.0789  -0.1282 316  THR D N   
11286 C  CA  . THR D 316 ? 0.4958 0.8066 0.4124 0.0823  0.0692  -0.1139 316  THR D CA  
11287 C  C   . THR D 316 ? 0.4816 0.7967 0.4101 0.0771  0.0642  -0.0914 316  THR D C   
11288 O  O   . THR D 316 ? 0.5307 0.8559 0.4488 0.0646  0.0603  -0.0769 316  THR D O   
11289 C  CB  . THR D 316 ? 0.4489 0.7272 0.3612 0.0803  0.0601  -0.1191 316  THR D CB  
11290 O  OG1 . THR D 316 ? 0.4743 0.7574 0.3661 0.0755  0.0616  -0.1346 316  THR D OG1 
11291 C  CG2 . THR D 316 ? 0.6731 0.9410 0.5855 0.0700  0.0483  -0.0995 316  THR D CG2 
11292 N  N   . LEU D 317 ? 0.2436 0.5508 0.1930 0.0870  0.0644  -0.0888 317  LEU D N   
11293 C  CA  . LEU D 317 ? 0.3937 0.6996 0.3551 0.0826  0.0584  -0.0701 317  LEU D CA  
11294 C  C   . LEU D 317 ? 0.3837 0.7186 0.3422 0.0714  0.0614  -0.0571 317  LEU D C   
11295 O  O   . LEU D 317 ? 0.4623 0.7912 0.4180 0.0606  0.0546  -0.0411 317  LEU D O   
11296 C  CB  . LEU D 317 ? 0.3427 0.6413 0.3257 0.0963  0.0590  -0.0713 317  LEU D CB  
11297 C  CG  . LEU D 317 ? 0.3912 0.6575 0.3781 0.1078  0.0569  -0.0820 317  LEU D CG  
11298 C  CD1 . LEU D 317 ? 0.5776 0.8434 0.5845 0.1230  0.0588  -0.0822 317  LEU D CD1 
11299 C  CD2 . LEU D 317 ? 0.2577 0.4938 0.2392 0.1003  0.0467  -0.0744 317  LEU D CD2 
11300 N  N   . PRO D 318 ? 0.4138 0.7798 0.3735 0.0737  0.0723  -0.0637 318  PRO D N   
11301 C  CA  . PRO D 318 ? 0.4910 0.8846 0.4473 0.0608  0.0762  -0.0506 318  PRO D CA  
11302 C  C   . PRO D 318 ? 0.5392 0.9295 0.4718 0.0454  0.0718  -0.0395 318  PRO D C   
11303 O  O   . PRO D 318 ? 0.4595 0.8500 0.3917 0.0340  0.0681  -0.0220 318  PRO D O   
11304 C  CB  . PRO D 318 ? 0.4707 0.8985 0.4299 0.0668  0.0902  -0.0635 318  PRO D CB  
11305 C  CG  . PRO D 318 ? 0.4320 0.8492 0.4065 0.0861  0.0921  -0.0797 318  PRO D CG  
11306 C  CD  . PRO D 318 ? 0.4910 0.8684 0.4568 0.0880  0.0823  -0.0828 318  PRO D CD  
11307 N  N   . GLN D 319 ? 0.4070 0.7939 0.3200 0.0452  0.0720  -0.0494 319  GLN D N   
11308 C  CA  . GLN D 319 ? 0.4629 0.8447 0.3539 0.0329  0.0653  -0.0384 319  GLN D CA  
11309 C  C   . GLN D 319 ? 0.4568 0.8103 0.3536 0.0293  0.0526  -0.0237 319  GLN D C   
11310 O  O   . GLN D 319 ? 0.3364 0.6894 0.2276 0.0187  0.0487  -0.0055 319  GLN D O   
11311 C  CB  . GLN D 319 ? 0.7186 1.0970 0.5904 0.0350  0.0644  -0.0539 319  GLN D CB  
11312 C  CG  . GLN D 319 ? 0.9197 1.3281 0.7710 0.0307  0.0745  -0.0609 319  GLN D CG  
11313 C  CD  . GLN D 319 ? 1.1762 1.5935 1.0310 0.0427  0.0849  -0.0858 319  GLN D CD  
11314 O  OE1 . GLN D 319 ? 1.2598 1.6922 1.0945 0.0413  0.0909  -0.0987 319  GLN D OE1 
11315 N  NE2 . GLN D 319 ? 1.1644 1.5713 1.0439 0.0551  0.0871  -0.0928 319  GLN D NE2 
11316 N  N   . GLU D 320 ? 0.4485 0.7774 0.3562 0.0381  0.0469  -0.0319 320  GLU D N   
11317 C  CA  . GLU D 320 ? 0.4550 0.7575 0.3684 0.0357  0.0358  -0.0205 320  GLU D CA  
11318 C  C   . GLU D 320 ? 0.3783 0.6827 0.3016 0.0296  0.0350  -0.0031 320  GLU D C   
11319 O  O   . GLU D 320 ? 0.5306 0.8235 0.4492 0.0220  0.0281  0.0115  320  GLU D O   
11320 C  CB  . GLU D 320 ? 0.5048 0.7834 0.4317 0.0464  0.0327  -0.0314 320  GLU D CB  
11321 C  CG  . GLU D 320 ? 0.5774 0.8488 0.4952 0.0506  0.0329  -0.0492 320  GLU D CG  
11322 C  CD  . GLU D 320 ? 0.6227 0.8871 0.5258 0.0424  0.0240  -0.0459 320  GLU D CD  
11323 O  OE1 . GLU D 320 ? 0.5152 0.7803 0.4144 0.0347  0.0180  -0.0288 320  GLU D OE1 
11324 O  OE2 . GLU D 320 ? 0.6933 0.9517 0.5892 0.0437  0.0228  -0.0607 320  GLU D OE2 
11325 N  N   . TRP D 321 ? 0.3288 0.6488 0.2661 0.0330  0.0422  -0.0053 321  TRP D N   
11326 C  CA  . TRP D 321 ? 0.4666 0.7913 0.4142 0.0258  0.0420  0.0088  321  TRP D CA  
11327 C  C   . TRP D 321 ? 0.6114 0.9463 0.5447 0.0112  0.0432  0.0239  321  TRP D C   
11328 O  O   . TRP D 321 ? 0.5297 0.8517 0.4649 0.0031  0.0382  0.0384  321  TRP D O   
11329 C  CB  . TRP D 321 ? 0.4978 0.8451 0.4632 0.0314  0.0497  0.0027  321  TRP D CB  
11330 C  CG  . TRP D 321 ? 0.6233 0.9831 0.5968 0.0199  0.0509  0.0163  321  TRP D CG  
11331 C  CD1 . TRP D 321 ? 0.5151 0.9043 0.4867 0.0100  0.0596  0.0210  321  TRP D CD1 
11332 C  CD2 . TRP D 321 ? 0.6901 1.0329 0.6740 0.0156  0.0436  0.0265  321  TRP D CD2 
11333 N  NE1 . TRP D 321 ? 0.4646 0.8550 0.4458 -0.0009 0.0579  0.0333  321  TRP D NE1 
11334 C  CE2 . TRP D 321 ? 0.4693 0.8312 0.4577 0.0026  0.0479  0.0363  321  TRP D CE2 
11335 C  CE3 . TRP D 321 ? 0.7073 1.0208 0.6964 0.0208  0.0345  0.0278  321  TRP D CE3 
11336 C  CZ2 . TRP D 321 ? 0.2996 0.6511 0.2974 -0.0053 0.0429  0.0458  321  TRP D CZ2 
11337 C  CZ3 . TRP D 321 ? 0.5182 0.8226 0.5158 0.0138  0.0299  0.0375  321  TRP D CZ3 
11338 C  CH2 . TRP D 321 ? 0.3486 0.6714 0.3503 0.0009  0.0338  0.0458  321  TRP D CH2 
11339 N  N   . GLN D 322 ? 0.6272 0.9840 0.5451 0.0077  0.0503  0.0206  322  GLN D N   
11340 C  CA  . GLN D 322 ? 0.6373 1.0052 0.5399 -0.0065 0.0529  0.0361  322  GLN D CA  
11341 C  C   . GLN D 322 ? 0.6213 0.9661 0.5081 -0.0112 0.0425  0.0486  322  GLN D C   
11342 O  O   . GLN D 322 ? 0.5906 0.9312 0.4694 -0.0221 0.0411  0.0664  322  GLN D O   
11343 C  CB  . GLN D 322 ? 0.5951 0.9946 0.4836 -0.0088 0.0642  0.0291  322  GLN D CB  
11344 C  CG  . GLN D 322 ? 0.6534 1.0790 0.5443 -0.0206 0.0745  0.0392  322  GLN D CG  
11345 C  CD  . GLN D 322 ? 0.7372 1.1775 0.6560 -0.0164 0.0799  0.0326  322  GLN D CD  
11346 O  OE1 . GLN D 322 ? 0.7072 1.1534 0.6365 -0.0267 0.0816  0.0440  322  GLN D OE1 
11347 N  NE2 . GLN D 322 ? 0.6745 1.1208 0.6053 -0.0011 0.0823  0.0141  322  GLN D NE2 
11348 N  N   . ARG D 323 ? 0.4650 0.7945 0.3486 -0.0030 0.0352  0.0394  323  ARG D N   
11349 C  CA  . ARG D 323 ? 0.5520 0.8629 0.4235 -0.0055 0.0245  0.0496  323  ARG D CA  
11350 C  C   . ARG D 323 ? 0.6060 0.8899 0.4915 -0.0055 0.0166  0.0604  323  ARG D C   
11351 O  O   . ARG D 323 ? 0.5295 0.8017 0.4079 -0.0115 0.0111  0.0769  323  ARG D O   
11352 C  CB  . ARG D 323 ? 0.4809 0.7882 0.3458 0.0020  0.0197  0.0343  323  ARG D CB  
11353 C  CG  . ARG D 323 ? 0.4668 0.7986 0.3165 0.0025  0.0275  0.0205  323  ARG D CG  
11354 C  CD  . ARG D 323 ? 0.4915 0.8161 0.3387 0.0097  0.0232  0.0022  323  ARG D CD  
11355 N  NE  . ARG D 323 ? 0.6133 0.9595 0.4409 0.0087  0.0289  -0.0109 323  ARG D NE  
11356 C  CZ  . ARG D 323 ? 0.8901 1.2336 0.7121 0.0132  0.0270  -0.0298 323  ARG D CZ  
11357 N  NH1 . ARG D 323 ? 0.8538 1.1739 0.6892 0.0182  0.0198  -0.0367 323  ARG D NH1 
11358 N  NH2 . ARG D 323 ? 1.1210 1.4849 0.9233 0.0116  0.0329  -0.0424 323  ARG D NH2 
11359 N  N   . ASN D 324 ? 0.4638 0.7372 0.3684 0.0019  0.0162  0.0512  324  ASN D N   
11360 C  CA  . ASN D 324 ? 0.4442 0.6925 0.3611 0.0029  0.0093  0.0585  324  ASN D CA  
11361 C  C   . ASN D 324 ? 0.3325 0.5798 0.2583 -0.0046 0.0122  0.0695  324  ASN D C   
11362 O  O   . ASN D 324 ? 0.4473 0.6737 0.3789 -0.0065 0.0070  0.0782  324  ASN D O   
11363 C  CB  . ASN D 324 ? 0.4692 0.7052 0.4000 0.0135  0.0072  0.0446  324  ASN D CB  
11364 C  CG  . ASN D 324 ? 0.4199 0.6523 0.3431 0.0187  0.0034  0.0339  324  ASN D CG  
11365 O  OD1 . ASN D 324 ? 0.4800 0.6953 0.4046 0.0200  -0.0041 0.0362  324  ASN D OD1 
11366 N  ND2 . ASN D 324 ? 0.4387 0.6883 0.3543 0.0211  0.0090  0.0213  324  ASN D ND2 
11367 N  N   . LYS D 325 ? 0.3876 0.6585 0.3144 -0.0094 0.0210  0.0684  325  LYS D N   
11368 C  CA  . LYS D 325 ? 0.4387 0.7141 0.3756 -0.0182 0.0247  0.0765  325  LYS D CA  
11369 C  C   . LYS D 325 ? 0.4372 0.6913 0.3680 -0.0278 0.0200  0.0938  325  LYS D C   
11370 O  O   . LYS D 325 ? 0.4980 0.7336 0.4395 -0.0290 0.0161  0.0971  325  LYS D O   
11371 C  CB  . LYS D 325 ? 0.4577 0.7656 0.3918 -0.0249 0.0354  0.0756  325  LYS D CB  
11372 C  CG  . LYS D 325 ? 0.3832 0.7041 0.3324 -0.0336 0.0405  0.0793  325  LYS D CG  
11373 C  CD  . LYS D 325 ? 0.4832 0.8392 0.4286 -0.0404 0.0521  0.0782  325  LYS D CD  
11374 C  CE  . LYS D 325 ? 0.5689 0.9457 0.5323 -0.0491 0.0580  0.0795  325  LYS D CE  
11375 N  NZ  . LYS D 325 ? 0.7004 1.1150 0.6611 -0.0547 0.0706  0.0770  325  LYS D NZ  
11376 N  N   . ALA D 326 ? 0.4253 0.6812 0.3377 -0.0341 0.0205  0.1048  326  ALA D N   
11377 C  CA  . ALA D 326 ? 0.5658 0.8000 0.4711 -0.0424 0.0166  0.1228  326  ALA D CA  
11378 C  C   . ALA D 326 ? 0.6144 0.8186 0.5248 -0.0345 0.0065  0.1240  326  ALA D C   
11379 O  O   . ALA D 326 ? 0.4430 0.6253 0.3586 -0.0388 0.0041  0.1330  326  ALA D O   
11380 C  CB  . ALA D 326 ? 0.3827 0.6245 0.2652 -0.0483 0.0180  0.1351  326  ALA D CB  
11381 N  N   . SER D 327 ? 0.5965 0.8004 0.5062 -0.0234 0.0015  0.1139  327  SER D N   
11382 C  CA  . SER D 327 ? 0.3933 0.5736 0.3077 -0.0158 -0.0075 0.1146  327  SER D CA  
11383 C  C   . SER D 327 ? 0.4078 0.5728 0.3400 -0.0127 -0.0081 0.1085  327  SER D C   
11384 O  O   . SER D 327 ? 0.5661 0.7083 0.5030 -0.0115 -0.0128 0.1144  327  SER D O   
11385 C  CB  . SER D 327 ? 0.2789 0.4662 0.1892 -0.0069 -0.0118 0.1036  327  SER D CB  
11386 O  OG  . SER D 327 ? 0.4111 0.6133 0.3027 -0.0096 -0.0124 0.1088  327  SER D OG  
11387 N  N   . LEU D 328 ? 0.3771 0.5556 0.3189 -0.0109 -0.0033 0.0967  328  LEU D N   
11388 C  CA  . LEU D 328 ? 0.2586 0.4268 0.2155 -0.0081 -0.0039 0.0910  328  LEU D CA  
11389 C  C   . LEU D 328 ? 0.3697 0.5295 0.3308 -0.0185 -0.0024 0.1001  328  LEU D C   
11390 O  O   . LEU D 328 ? 0.3328 0.4748 0.3019 -0.0175 -0.0054 0.0993  328  LEU D O   
11391 C  CB  . LEU D 328 ? 0.2706 0.4584 0.2357 -0.0027 0.0007  0.0776  328  LEU D CB  
11392 C  CG  . LEU D 328 ? 0.2364 0.4258 0.2009 0.0083  -0.0005 0.0655  328  LEU D CG  
11393 C  CD1 . LEU D 328 ? 0.2446 0.4568 0.2140 0.0126  0.0060  0.0545  328  LEU D CD1 
11394 C  CD2 . LEU D 328 ? 0.2621 0.4295 0.2351 0.0156  -0.0055 0.0614  328  LEU D CD2 
11395 N  N   . LEU D 329 ? 0.4252 0.5982 0.3803 -0.0293 0.0027  0.1079  329  LEU D N   
11396 C  CA  . LEU D 329 ? 0.4113 0.5762 0.3697 -0.0416 0.0047  0.1163  329  LEU D CA  
11397 C  C   . LEU D 329 ? 0.4059 0.5407 0.3566 -0.0443 0.0004  0.1291  329  LEU D C   
11398 O  O   . LEU D 329 ? 0.5257 0.6394 0.4824 -0.0478 -0.0014 0.1310  329  LEU D O   
11399 C  CB  . LEU D 329 ? 0.5448 0.7342 0.4997 -0.0537 0.0128  0.1210  329  LEU D CB  
11400 C  CG  . LEU D 329 ? 0.5502 0.7696 0.5186 -0.0554 0.0184  0.1105  329  LEU D CG  
11401 C  CD1 . LEU D 329 ? 0.4903 0.7077 0.4725 -0.0436 0.0139  0.0974  329  LEU D CD1 
11402 C  CD2 . LEU D 329 ? 0.5168 0.7673 0.4792 -0.0540 0.0253  0.1068  329  LEU D CD2 
11403 N  N   . GLN D 330 ? 0.4722 0.6056 0.4092 -0.0421 -0.0014 0.1376  330  GLN D N   
11404 C  CA  . GLN D 330 ? 0.5695 0.6762 0.4986 -0.0430 -0.0057 0.1519  330  GLN D CA  
11405 C  C   . GLN D 330 ? 0.5500 0.6338 0.4870 -0.0318 -0.0127 0.1479  330  GLN D C   
11406 O  O   . GLN D 330 ? 0.6482 0.7056 0.5861 -0.0328 -0.0149 0.1559  330  GLN D O   
11407 C  CB  . GLN D 330 ? 0.7304 0.8458 0.6420 -0.0426 -0.0068 0.1627  330  GLN D CB  
11408 C  CG  . GLN D 330 ? 0.8154 0.9478 0.7160 -0.0560 0.0012  0.1715  330  GLN D CG  
11409 C  CD  . GLN D 330 ? 0.7840 0.8976 0.6865 -0.0698 0.0053  0.1829  330  GLN D CD  
11410 O  OE1 . GLN D 330 ? 0.7851 0.8707 0.6811 -0.0709 0.0020  0.1969  330  GLN D OE1 
11411 N  NE2 . GLN D 330 ? 0.7269 0.8560 0.6389 -0.0801 0.0123  0.1765  330  GLN D NE2 
11412 N  N   . LEU D 331 ? 0.3121 0.4055 0.2551 -0.0215 -0.0152 0.1351  331  LEU D N   
11413 C  CA  . LEU D 331 ? 0.2803 0.3556 0.2324 -0.0121 -0.0201 0.1297  331  LEU D CA  
11414 C  C   . LEU D 331 ? 0.3778 0.4384 0.3396 -0.0160 -0.0181 0.1259  331  LEU D C   
11415 O  O   . LEU D 331 ? 0.3709 0.4076 0.3360 -0.0137 -0.0205 0.1289  331  LEU D O   
11416 C  CB  . LEU D 331 ? 0.2813 0.3700 0.2382 -0.0029 -0.0216 0.1161  331  LEU D CB  
11417 C  CG  . LEU D 331 ? 0.3856 0.4590 0.3508 0.0065  -0.0262 0.1112  331  LEU D CG  
11418 C  CD1 . LEU D 331 ? 0.3399 0.4270 0.3080 0.0131  -0.0267 0.0988  331  LEU D CD1 
11419 C  CD2 . LEU D 331 ? 0.6964 0.7527 0.6709 0.0059  -0.0247 0.1078  331  LEU D CD2 
11420 N  N   . LEU D 332 ? 0.3791 0.4555 0.3456 -0.0212 -0.0139 0.1185  332  LEU D N   
11421 C  CA  . LEU D 332 ? 0.4680 0.5359 0.4428 -0.0265 -0.0126 0.1142  332  LEU D CA  
11422 C  C   . LEU D 332 ? 0.4517 0.4966 0.4232 -0.0364 -0.0119 0.1244  332  LEU D C   
11423 O  O   . LEU D 332 ? 0.4143 0.4379 0.3900 -0.0362 -0.0133 0.1217  332  LEU D O   
11424 C  CB  . LEU D 332 ? 0.5036 0.5975 0.4838 -0.0320 -0.0086 0.1074  332  LEU D CB  
11425 C  CG  . LEU D 332 ? 0.5135 0.6232 0.4995 -0.0207 -0.0093 0.0954  332  LEU D CG  
11426 C  CD1 . LEU D 332 ? 0.3230 0.4604 0.3162 -0.0240 -0.0055 0.0893  332  LEU D CD1 
11427 C  CD2 . LEU D 332 ? 0.4752 0.5661 0.4663 -0.0130 -0.0131 0.0895  332  LEU D CD2 
11428 N  N   . ARG D 333 ? 0.3829 0.4311 0.3459 -0.0450 -0.0092 0.1359  333  ARG D N   
11429 C  CA  . ARG D 333 ? 0.3651 0.3889 0.3236 -0.0554 -0.0077 0.1472  333  ARG D CA  
11430 C  C   . ARG D 333 ? 0.4066 0.3997 0.3623 -0.0467 -0.0121 0.1542  333  ARG D C   
11431 O  O   . ARG D 333 ? 0.6690 0.6347 0.6228 -0.0527 -0.0111 0.1615  333  ARG D O   
11432 C  CB  . ARG D 333 ? 0.3567 0.3921 0.3056 -0.0671 -0.0029 0.1592  333  ARG D CB  
11433 C  CG  . ARG D 333 ? 0.5362 0.6052 0.4904 -0.0753 0.0024  0.1517  333  ARG D CG  
11434 C  CD  . ARG D 333 ? 0.7556 0.8319 0.7034 -0.0926 0.0093  0.1630  333  ARG D CD  
11435 N  NE  . ARG D 333 ? 0.7559 0.8147 0.7093 -0.1071 0.0116  0.1644  333  ARG D NE  
11436 C  CZ  . ARG D 333 ? 0.7945 0.8724 0.7572 -0.1212 0.0164  0.1591  333  ARG D CZ  
11437 N  NH1 . ARG D 333 ? 0.7988 0.8558 0.7653 -0.1347 0.0175  0.1601  333  ARG D NH1 
11438 N  NH2 . ARG D 333 ? 0.7886 0.9060 0.7574 -0.1221 0.0202  0.1523  333  ARG D NH2 
11439 N  N   . GLN D 334 ? 0.4049 0.4026 0.3613 -0.0327 -0.0167 0.1514  334  GLN D N   
11440 C  CA  . GLN D 334 ? 0.4232 0.3971 0.3810 -0.0222 -0.0212 0.1556  334  GLN D CA  
11441 C  C   . GLN D 334 ? 0.5231 0.4781 0.4908 -0.0193 -0.0209 0.1454  334  GLN D C   
11442 O  O   . GLN D 334 ? 0.5874 0.5192 0.5577 -0.0121 -0.0228 0.1482  334  GLN D O   
11443 C  CB  . GLN D 334 ? 0.3839 0.3728 0.3416 -0.0096 -0.0262 0.1538  334  GLN D CB  
11444 C  CG  . GLN D 334 ? 0.4776 0.4786 0.4230 -0.0101 -0.0283 0.1659  334  GLN D CG  
11445 C  CD  . GLN D 334 ? 0.6318 0.6089 0.5710 -0.0085 -0.0310 0.1829  334  GLN D CD  
11446 O  OE1 . GLN D 334 ? 0.7425 0.7068 0.6872 0.0029  -0.0361 0.1850  334  GLN D OE1 
11447 N  NE2 . GLN D 334 ? 0.5579 0.5289 0.4861 -0.0197 -0.0274 0.1956  334  GLN D NE2 
11448 N  N   . ALA D 335 ? 0.3762 0.3422 0.3491 -0.0242 -0.0184 0.1335  335  ALA D N   
11449 C  CA  . ALA D 335 ? 0.5144 0.4648 0.4938 -0.0229 -0.0180 0.1235  335  ALA D CA  
11450 C  C   . ALA D 335 ? 0.5694 0.4934 0.5464 -0.0334 -0.0154 0.1275  335  ALA D C   
11451 O  O   . ALA D 335 ? 0.5532 0.4640 0.5335 -0.0359 -0.0143 0.1185  335  ALA D O   
11452 C  CB  . ALA D 335 ? 0.3698 0.3413 0.3539 -0.0248 -0.0171 0.1109  335  ALA D CB  
11453 N  N   . HIS D 336 ? 0.4272 0.3428 0.3976 -0.0402 -0.0142 0.1411  336  HIS D N   
11454 C  CA  . HIS D 336 ? 0.4883 0.3760 0.4558 -0.0520 -0.0110 0.1458  336  HIS D CA  
11455 C  C   . HIS D 336 ? 0.5739 0.4302 0.5370 -0.0454 -0.0120 0.1591  336  HIS D C   
11456 O  O   . HIS D 336 ? 0.5070 0.3333 0.4673 -0.0535 -0.0091 0.1636  336  HIS D O   
11457 C  CB  . HIS D 336 ? 0.5173 0.4199 0.4814 -0.0698 -0.0071 0.1501  336  HIS D CB  
11458 C  CG  . HIS D 336 ? 0.5953 0.5273 0.5664 -0.0756 -0.0064 0.1367  336  HIS D CG  
11459 N  ND1 . HIS D 336 ? 0.5848 0.5109 0.5611 -0.0832 -0.0060 0.1250  336  HIS D ND1 
11460 C  CD2 . HIS D 336 ? 0.5205 0.4884 0.4942 -0.0737 -0.0065 0.1328  336  HIS D CD2 
11461 C  CE1 . HIS D 336 ? 0.5610 0.5193 0.5433 -0.0853 -0.0065 0.1159  336  HIS D CE1 
11462 N  NE2 . HIS D 336 ? 0.6617 0.6447 0.6431 -0.0791 -0.0064 0.1203  336  HIS D NE2 
11463 N  N   . ILE D 337 ? 0.4619 0.3115 0.4677 0.0417  -0.0427 0.1174  337  ILE D N   
11464 C  CA  . ILE D 337 ? 0.4388 0.2804 0.4561 0.0489  -0.0443 0.1261  337  ILE D CA  
11465 C  C   . ILE D 337 ? 0.4849 0.3178 0.5182 0.0518  -0.0369 0.1220  337  ILE D C   
11466 O  O   . ILE D 337 ? 0.6618 0.4973 0.6976 0.0487  -0.0316 0.1130  337  ILE D O   
11467 C  CB  . ILE D 337 ? 0.6596 0.5123 0.6824 0.0563  -0.0558 0.1324  337  ILE D CB  
11468 C  CG1 . ILE D 337 ? 0.6739 0.5388 0.7079 0.0588  -0.0589 0.1261  337  ILE D CG1 
11469 C  CG2 . ILE D 337 ? 0.5581 0.4190 0.5640 0.0546  -0.0633 0.1371  337  ILE D CG2 
11470 C  CD1 . ILE D 337 ? 0.5308 0.4061 0.5721 0.0663  -0.0709 0.1319  337  ILE D CD1 
11471 N  N   . GLY D 338 ? 0.5847 0.4071 0.6285 0.0578  -0.0370 0.1285  338  GLY D N   
11472 C  CA  . GLY D 338 ? 0.5124 0.3277 0.5731 0.0621  -0.0305 0.1243  338  GLY D CA  
11473 C  C   . GLY D 338 ? 0.3382 0.1385 0.3940 0.0570  -0.0205 0.1194  338  GLY D C   
11474 O  O   . GLY D 338 ? 0.5791 0.3675 0.6246 0.0535  -0.0198 0.1241  338  GLY D O   
11475 N  N   . ILE D 339 ? 0.3324 0.1330 0.3953 0.0563  -0.0127 0.1099  339  ILE D N   
11476 C  CA  . ILE D 339 ? 0.4952 0.2807 0.5542 0.0524  -0.0034 0.1043  339  ILE D CA  
11477 C  C   . ILE D 339 ? 0.5183 0.3091 0.5713 0.0461  0.0028  0.0935  339  ILE D C   
11478 O  O   . ILE D 339 ? 0.6041 0.4098 0.6578 0.0452  -0.0001 0.0905  339  ILE D O   
11479 C  CB  . ILE D 339 ? 0.4784 0.2534 0.5543 0.0600  0.0010  0.1030  339  ILE D CB  
11480 C  CG1 . ILE D 339 ? 0.4988 0.2883 0.5921 0.0661  0.0014  0.0990  339  ILE D CG1 
11481 C  CG2 . ILE D 339 ? 0.3807 0.1438 0.4598 0.0651  -0.0051 0.1134  339  ILE D CG2 
11482 C  CD1 . ILE D 339 ? 0.3998 0.1827 0.5107 0.0733  0.0077  0.0943  339  ILE D CD1 
11483 N  N   . LYS D 340 ? 0.4192 0.1969 0.4660 0.0416  0.0106  0.0877  340  LYS D N   
11484 C  CA  . LYS D 340 ? 0.4842 0.2636 0.5260 0.0363  0.0170  0.0769  340  LYS D CA  
11485 C  C   . LYS D 340 ? 0.6588 0.4202 0.7001 0.0354  0.0258  0.0714  340  LYS D C   
11486 O  O   . LYS D 340 ? 0.6145 0.3621 0.6564 0.0371  0.0256  0.0765  340  LYS D O   
11487 C  CB  . LYS D 340 ? 0.4905 0.2766 0.5154 0.0278  0.0135  0.0748  340  LYS D CB  
11488 C  CG  . LYS D 340 ? 0.4999 0.2760 0.5123 0.0225  0.0132  0.0781  340  LYS D CG  
11489 C  CD  . LYS D 340 ? 0.3605 0.1438 0.3577 0.0142  0.0110  0.0729  340  LYS D CD  
11490 C  CE  . LYS D 340 ? 0.4061 0.1865 0.3927 0.0095  0.0087  0.0784  340  LYS D CE  
11491 N  NZ  . LYS D 340 ? 0.4829 0.2724 0.4565 0.0023  0.0061  0.0724  340  LYS D NZ  
11492 N  N   . GLY D 341 ? 0.4494 0.2102 0.4894 0.0327  0.0330  0.0613  341  GLY D N   
11493 C  CA  . GLY D 341 ? 0.4850 0.2286 0.5240 0.0325  0.0412  0.0549  341  GLY D CA  
11494 C  C   . GLY D 341 ? 0.5159 0.2606 0.5534 0.0303  0.0491  0.0437  341  GLY D C   
11495 O  O   . GLY D 341 ? 0.4606 0.2178 0.4934 0.0261  0.0479  0.0405  341  GLY D O   
11496 N  N   . LEU D 342 ? 0.5872 0.3181 0.6281 0.0331  0.0566  0.0377  342  LEU D N   
11497 C  CA  . LEU D 342 ? 0.5606 0.2907 0.5981 0.0309  0.0649  0.0267  342  LEU D CA  
11498 C  C   . LEU D 342 ? 0.4978 0.2289 0.5519 0.0398  0.0718  0.0225  342  LEU D C   
11499 O  O   . LEU D 342 ? 0.5992 0.3220 0.6645 0.0474  0.0715  0.0254  342  LEU D O   
11500 C  CB  . LEU D 342 ? 0.4679 0.1801 0.4900 0.0245  0.0683  0.0205  342  LEU D CB  
11501 C  CG  . LEU D 342 ? 0.3960 0.1078 0.4031 0.0158  0.0619  0.0236  342  LEU D CG  
11502 C  CD1 . LEU D 342 ? 0.3744 0.0670 0.3704 0.0108  0.0648  0.0186  342  LEU D CD1 
11503 C  CD2 . LEU D 342 ? 0.3489 0.0754 0.3476 0.0098  0.0591  0.0206  342  LEU D CD2 
11504 N  N   . VAL D 343 ? 0.5236 0.2654 0.5793 0.0387  0.0777  0.0157  343  VAL D N   
11505 C  CA  . VAL D 343 ? 0.4539 0.1964 0.5221 0.0457  0.0867  0.0087  343  VAL D CA  
11506 C  C   . VAL D 343 ? 0.4921 0.2230 0.5452 0.0403  0.0946  -0.0020 343  VAL D C   
11507 O  O   . VAL D 343 ? 0.5572 0.2931 0.5972 0.0320  0.0956  -0.0055 343  VAL D O   
11508 C  CB  . VAL D 343 ? 0.5120 0.2768 0.5935 0.0479  0.0886  0.0088  343  VAL D CB  
11509 C  CG1 . VAL D 343 ? 0.3767 0.1438 0.4700 0.0542  0.0995  -0.0001 343  VAL D CG1 
11510 C  CG2 . VAL D 343 ? 0.4712 0.2468 0.5679 0.0538  0.0799  0.0192  343  VAL D CG2 
11511 N  N   . THR D 344 ? 0.6837 0.3979 0.7382 0.0451  0.0994  -0.0072 344  THR D N   
11512 C  CA  . THR D 344 ? 0.7145 0.4132 0.7524 0.0398  0.1048  -0.0165 344  THR D CA  
11513 C  C   . THR D 344 ? 0.7381 0.4309 0.7823 0.0468  0.1148  -0.0269 344  THR D C   
11514 O  O   . THR D 344 ? 0.6510 0.3487 0.7140 0.0569  0.1167  -0.0267 344  THR D O   
11515 C  CB  . THR D 344 ? 0.8401 0.5192 0.8676 0.0362  0.0989  -0.0131 344  THR D CB  
11516 O  OG1 . THR D 344 ? 1.0501 0.7164 1.0593 0.0288  0.1021  -0.0213 344  THR D OG1 
11517 C  CG2 . THR D 344 ? 0.6200 0.2847 0.6596 0.0454  0.0981  -0.0114 344  THR D CG2 
11518 N  N   . ASP D 345 ? 0.9176 0.6001 0.9458 0.0416  0.1207  -0.0365 345  ASP D N   
11519 C  CA  . ASP D 345 ? 0.7682 0.4421 0.7973 0.0474  0.1303  -0.0480 345  ASP D CA  
11520 C  C   . ASP D 345 ? 0.8742 0.5298 0.9117 0.0557  0.1277  -0.0479 345  ASP D C   
11521 O  O   . ASP D 345 ? 0.7685 0.4158 0.8067 0.0546  0.1188  -0.0389 345  ASP D O   
11522 C  CB  . ASP D 345 ? 0.6258 0.2871 0.6321 0.0389  0.1342  -0.0568 345  ASP D CB  
11523 C  CG  . ASP D 345 ? 0.8672 0.5374 0.8699 0.0390  0.1453  -0.0669 345  ASP D CG  
11524 O  OD1 . ASP D 345 ? 1.0740 0.7367 1.0567 0.0310  0.1480  -0.0732 345  ASP D OD1 
11525 O  OD2 . ASP D 345 ? 0.9189 0.6039 0.9384 0.0466  0.1514  -0.0687 345  ASP D OD2 
11526 N  N   . ALA D 346 ? 1.0631 0.7124 1.1065 0.0639  0.1351  -0.0579 346  ALA D N   
11527 C  CA  . ALA D 346 ? 0.8477 0.4737 0.8929 0.0700  0.1324  -0.0606 346  ALA D CA  
11528 C  C   . ALA D 346 ? 0.7985 0.4067 0.8212 0.0596  0.1299  -0.0621 346  ALA D C   
11529 O  O   . ALA D 346 ? 0.7899 0.3808 0.8095 0.0579  0.1225  -0.0571 346  ALA D O   
11530 C  CB  . ALA D 346 ? 0.8521 0.4753 0.9050 0.0802  0.1414  -0.0735 346  ALA D CB  
11531 N  N   . SER D 347 ? 0.9781 0.5913 0.9852 0.0519  0.1355  -0.0685 347  SER D N   
11532 C  CA  . SER D 347 ? 1.1033 0.7018 1.0887 0.0414  0.1328  -0.0707 347  SER D CA  
11533 C  C   . SER D 347 ? 1.0709 0.6676 1.0537 0.0345  0.1222  -0.0589 347  SER D C   
11534 O  O   . SER D 347 ? 0.8840 0.4657 0.8532 0.0273  0.1181  -0.0594 347  SER D O   
11535 C  CB  . SER D 347 ? 1.0806 0.6891 1.0506 0.0335  0.1384  -0.0767 347  SER D CB  
11536 O  OG  . SER D 347 ? 1.0870 0.6934 1.0534 0.0377  0.1487  -0.0889 347  SER D OG  
11537 N  N   . GLY D 348 ? 0.8746 0.4872 0.8709 0.0368  0.1179  -0.0486 348  GLY D N   
11538 C  CA  . GLY D 348 ? 0.5560 0.1729 0.5486 0.0297  0.1090  -0.0378 348  GLY D CA  
11539 C  C   . GLY D 348 ? 0.8146 0.4465 0.7958 0.0210  0.1087  -0.0383 348  GLY D C   
11540 O  O   . GLY D 348 ? 0.9085 0.5429 0.8818 0.0134  0.1018  -0.0328 348  GLY D O   
11541 N  N   . PHE D 349 ? 0.6852 0.3274 0.6657 0.0218  0.1160  -0.0452 349  PHE D N   
11542 C  CA  . PHE D 349 ? 0.6214 0.2762 0.5905 0.0132  0.1153  -0.0460 349  PHE D CA  
11543 C  C   . PHE D 349 ? 0.5652 0.2440 0.5470 0.0150  0.1141  -0.0393 349  PHE D C   
11544 O  O   . PHE D 349 ? 0.4319 0.1206 0.4275 0.0221  0.1203  -0.0409 349  PHE D O   
11545 C  CB  . PHE D 349 ? 0.4876 0.1365 0.4424 0.0097  0.1233  -0.0576 349  PHE D CB  
11546 C  CG  . PHE D 349 ? 0.5213 0.1775 0.4608 -0.0007 0.1203  -0.0583 349  PHE D CG  
11547 C  CD1 . PHE D 349 ? 0.4274 0.0700 0.3487 -0.0090 0.1153  -0.0615 349  PHE D CD1 
11548 C  CD2 . PHE D 349 ? 0.4612 0.1379 0.4054 -0.0022 0.1213  -0.0554 349  PHE D CD2 
11549 C  CE1 . PHE D 349 ? 0.7456 0.3938 0.6529 -0.0182 0.1110  -0.0625 349  PHE D CE1 
11550 C  CE2 . PHE D 349 ? 0.5153 0.1971 0.4451 -0.0120 0.1170  -0.0557 349  PHE D CE2 
11551 C  CZ  . PHE D 349 ? 0.4084 0.0756 0.3195 -0.0197 0.1115  -0.0594 349  PHE D CZ  
11552 N  N   . PRO D 350 ? 0.5887 0.2772 0.5655 0.0085  0.1059  -0.0327 350  PRO D N   
11553 C  CA  . PRO D 350 ? 0.6259 0.3355 0.6149 0.0102  0.1016  -0.0246 350  PRO D CA  
11554 C  C   . PRO D 350 ? 0.6465 0.3713 0.6426 0.0117  0.1087  -0.0281 350  PRO D C   
11555 O  O   . PRO D 350 ? 0.5759 0.2985 0.5599 0.0066  0.1146  -0.0359 350  PRO D O   
11556 C  CB  . PRO D 350 ? 0.5715 0.2852 0.5469 0.0009  0.0925  -0.0214 350  PRO D CB  
11557 C  CG  . PRO D 350 ? 0.5836 0.2824 0.5395 -0.0064 0.0946  -0.0304 350  PRO D CG  
11558 C  CD  . PRO D 350 ? 0.6172 0.2977 0.5748 -0.0014 0.1005  -0.0347 350  PRO D CD  
11559 N  N   . ILE D 351 ? 0.6145 0.3548 0.6300 0.0185  0.1079  -0.0219 351  ILE D N   
11560 C  CA  . ILE D 351 ? 0.5105 0.2694 0.5357 0.0193  0.1134  -0.0233 351  ILE D CA  
11561 C  C   . ILE D 351 ? 0.5547 0.3301 0.5811 0.0143  0.1045  -0.0155 351  ILE D C   
11562 O  O   . ILE D 351 ? 0.5007 0.2812 0.5360 0.0176  0.0959  -0.0069 351  ILE D O   
11563 C  CB  . ILE D 351 ? 0.5084 0.2749 0.5572 0.0309  0.1188  -0.0231 351  ILE D CB  
11564 C  CG1 . ILE D 351 ? 0.5054 0.2537 0.5539 0.0372  0.1255  -0.0307 351  ILE D CG1 
11565 C  CG2 . ILE D 351 ? 0.4726 0.2588 0.5308 0.0307  0.1263  -0.0261 351  ILE D CG2 
11566 C  CD1 . ILE D 351 ? 0.5024 0.2549 0.5745 0.0499  0.1280  -0.0303 351  ILE D CD1 
11567 N  N   . ALA D 352 ? 0.5542 0.3370 0.5706 0.0061  0.1060  -0.0184 352  ALA D N   
11568 C  CA  . ALA D 352 ? 0.5677 0.3646 0.5833 0.0004  0.0966  -0.0119 352  ALA D CA  
11569 C  C   . ALA D 352 ? 0.5249 0.3426 0.5612 0.0046  0.0988  -0.0080 352  ALA D C   
11570 O  O   . ALA D 352 ? 0.5606 0.3839 0.6056 0.0076  0.1097  -0.0129 352  ALA D O   
11571 C  CB  . ALA D 352 ? 0.4286 0.2215 0.4225 -0.0112 0.0953  -0.0167 352  ALA D CB  
11572 N  N   . ASP D 353 ? 0.5201 0.3501 0.5646 0.0049  0.0884  0.0005  353  ASP D N   
11573 C  CA  . ASP D 353 ? 0.4843 0.3349 0.5489 0.0080  0.0890  0.0048  353  ASP D CA  
11574 C  C   . ASP D 353 ? 0.4744 0.3295 0.5620 0.0199  0.0956  0.0048  353  ASP D C   
11575 O  O   . ASP D 353 ? 0.5784 0.4504 0.6841 0.0229  0.1001  0.0053  353  ASP D O   
11576 C  CB  . ASP D 353 ? 0.6821 0.5417 0.7416 -0.0002 0.0958  0.0004  353  ASP D CB  
11577 C  CG  . ASP D 353 ? 0.9300 0.8008 0.9857 -0.0083 0.0852  0.0061  353  ASP D CG  
11578 O  OD1 . ASP D 353 ? 0.9849 0.8740 1.0587 -0.0066 0.0836  0.0112  353  ASP D OD1 
11579 O  OD2 . ASP D 353 ? 1.0595 0.9204 1.0947 -0.0162 0.0776  0.0053  353  ASP D OD2 
11580 N  N   . ALA D 354 ? 0.4123 0.2523 0.4997 0.0264  0.0959  0.0041  354  ALA D N   
11581 C  CA  . ALA D 354 ? 0.5280 0.3704 0.6373 0.0383  0.0986  0.0054  354  ALA D CA  
11582 C  C   . ALA D 354 ? 0.5895 0.4445 0.7141 0.0427  0.0877  0.0156  354  ALA D C   
11583 O  O   . ALA D 354 ? 0.5423 0.4000 0.6578 0.0372  0.0775  0.0215  354  ALA D O   
11584 C  CB  . ALA D 354 ? 0.5674 0.3884 0.6708 0.0431  0.0993  0.0033  354  ALA D CB  
11585 N  N   . ASN D 355 ? 0.5031 0.3657 0.6510 0.0530  0.0891  0.0172  355  ASN D N   
11586 C  CA  . ASN D 355 ? 0.5421 0.4149 0.7048 0.0582  0.0781  0.0268  355  ASN D CA  
11587 C  C   . ASN D 355 ? 0.6333 0.4930 0.8021 0.0674  0.0726  0.0314  355  ASN D C   
11588 O  O   . ASN D 355 ? 0.6515 0.5033 0.8295 0.0750  0.0788  0.0268  355  ASN D O   
11589 C  CB  . ASN D 355 ? 0.6333 0.5284 0.8202 0.0621  0.0810  0.0268  355  ASN D CB  
11590 C  CG  . ASN D 355 ? 0.6776 0.5877 0.8593 0.0518  0.0807  0.0272  355  ASN D CG  
11591 O  OD1 . ASN D 355 ? 0.7092 0.6300 0.8956 0.0487  0.0910  0.0213  355  ASN D OD1 
11592 N  ND2 . ASN D 355 ? 0.7675 0.6784 0.9388 0.0464  0.0687  0.0341  355  ASN D ND2 
11593 N  N   . VAL D 356 ? 0.5439 0.4013 0.7068 0.0666  0.0606  0.0404  356  VAL D N   
11594 C  CA  . VAL D 356 ? 0.5595 0.4051 0.7265 0.0740  0.0539  0.0466  356  VAL D CA  
11595 C  C   . VAL D 356 ? 0.5411 0.3994 0.7267 0.0811  0.0443  0.0549  356  VAL D C   
11596 O  O   . VAL D 356 ? 0.4424 0.3106 0.6243 0.0775  0.0355  0.0609  356  VAL D O   
11597 C  CB  . VAL D 356 ? 0.5893 0.4205 0.7334 0.0677  0.0480  0.0506  356  VAL D CB  
11598 C  CG1 . VAL D 356 ? 0.5370 0.3568 0.6841 0.0742  0.0405  0.0586  356  VAL D CG1 
11599 C  CG2 . VAL D 356 ? 0.4714 0.2886 0.5990 0.0616  0.0570  0.0421  356  VAL D CG2 
11600 N  N   . TYR D 357 ? 0.5042 0.3618 0.7100 0.0917  0.0454  0.0547  357  TYR D N   
11601 C  CA  . TYR D 357 ? 0.5304 0.3999 0.7564 0.0994  0.0365  0.0615  357  TYR D CA  
11602 C  C   . TYR D 357 ? 0.5506 0.4060 0.7765 0.1060  0.0261  0.0701  357  TYR D C   
11603 O  O   . TYR D 357 ? 0.5917 0.4287 0.8124 0.1086  0.0283  0.0689  357  TYR D O   
11604 C  CB  . TYR D 357 ? 0.4545 0.3360 0.7070 0.1075  0.0437  0.0552  357  TYR D CB  
11605 C  CG  . TYR D 357 ? 0.5186 0.4197 0.7769 0.1020  0.0525  0.0488  357  TYR D CG  
11606 C  CD1 . TYR D 357 ? 0.4680 0.3669 0.7194 0.0980  0.0661  0.0386  357  TYR D CD1 
11607 C  CD2 . TYR D 357 ? 0.5598 0.4813 0.8308 0.1007  0.0470  0.0532  357  TYR D CD2 
11608 C  CE1 . TYR D 357 ? 0.4689 0.3857 0.7246 0.0921  0.0745  0.0334  357  TYR D CE1 
11609 C  CE2 . TYR D 357 ? 0.4902 0.4297 0.7667 0.0946  0.0549  0.0482  357  TYR D CE2 
11610 C  CZ  . TYR D 357 ? 0.4768 0.4139 0.7450 0.0900  0.0689  0.0385  357  TYR D CZ  
11611 O  OH  . TYR D 357 ? 0.6528 0.6078 0.9252 0.0831  0.0768  0.0343  357  TYR D OH  
11612 N  N   . VAL D 358 ? 0.6611 0.5246 0.8926 0.1085  0.0144  0.0789  358  VAL D N   
11613 C  CA  . VAL D 358 ? 0.6027 0.4549 0.8366 0.1156  0.0037  0.0878  358  VAL D CA  
11614 C  C   . VAL D 358 ? 0.6498 0.5133 0.9113 0.1262  -0.0020 0.0900  358  VAL D C   
11615 O  O   . VAL D 358 ? 0.6310 0.5135 0.9029 0.1256  -0.0053 0.0910  358  VAL D O   
11616 C  CB  . VAL D 358 ? 0.4347 0.2847 0.6488 0.1100  -0.0070 0.0971  358  VAL D CB  
11617 C  CG1 . VAL D 358 ? 0.4256 0.2643 0.6414 0.1169  -0.0179 0.1067  358  VAL D CG1 
11618 C  CG2 . VAL D 358 ? 0.4410 0.2806 0.6293 0.0998  -0.0022 0.0948  358  VAL D CG2 
11619 N  N   . ALA D 359 ? 0.5897 0.4413 0.8634 0.1358  -0.0041 0.0905  359  ALA D N   
11620 C  CA  . ALA D 359 ? 0.5416 0.4026 0.8428 0.1469  -0.0101 0.0918  359  ALA D CA  
11621 C  C   . ALA D 359 ? 0.4163 0.2878 0.7189 0.1470  -0.0231 0.1013  359  ALA D C   
11622 O  O   . ALA D 359 ? 0.5123 0.3727 0.7980 0.1451  -0.0328 0.1104  359  ALA D O   
11623 C  CB  . ALA D 359 ? 0.6529 0.4946 0.9614 0.1566  -0.0146 0.0934  359  ALA D CB  
11624 N  N   . GLY D 360 ? 0.3877 0.2809 0.7101 0.1489  -0.0234 0.0992  360  GLY D N   
11625 C  CA  . GLY D 360 ? 0.3362 0.2399 0.6623 0.1498  -0.0365 0.1075  360  GLY D CA  
11626 C  C   . GLY D 360 ? 0.3849 0.2987 0.6936 0.1385  -0.0363 0.1084  360  GLY D C   
11627 O  O   . GLY D 360 ? 0.6387 0.5623 0.9483 0.1380  -0.0469 0.1143  360  GLY D O   
11628 N  N   . LEU D 361 ? 0.3658 0.2759 0.6582 0.1299  -0.0251 0.1022  361  LEU D N   
11629 C  CA  . LEU D 361 ? 0.4638 0.3818 0.7388 0.1188  -0.0246 0.1017  361  LEU D CA  
11630 C  C   . LEU D 361 ? 0.4989 0.4246 0.7755 0.1125  -0.0100 0.0917  361  LEU D C   
11631 O  O   . LEU D 361 ? 0.3777 0.3036 0.6356 0.1025  -0.0066 0.0891  361  LEU D O   
11632 C  CB  . LEU D 361 ? 0.3497 0.2520 0.5952 0.1129  -0.0281 0.1057  361  LEU D CB  
11633 C  CG  . LEU D 361 ? 0.3700 0.2657 0.6077 0.1167  -0.0423 0.1161  361  LEU D CG  
11634 C  CD1 . LEU D 361 ? 0.3916 0.2722 0.6013 0.1104  -0.0424 0.1185  361  LEU D CD1 
11635 C  CD2 . LEU D 361 ? 0.3803 0.2918 0.6215 0.1161  -0.0534 0.1203  361  LEU D CD2 
11636 N  N   . GLU D 362 ? 0.5865 0.5186 0.8856 0.1187  -0.0018 0.0857  362  GLU D N   
11637 C  CA  . GLU D 362 ? 0.4760 0.4146 0.7770 0.1138  0.0132  0.0757  362  GLU D CA  
11638 C  C   . GLU D 362 ? 0.5421 0.5007 0.8457 0.1054  0.0147  0.0746  362  GLU D C   
11639 O  O   . GLU D 362 ? 0.5638 0.5278 0.8641 0.0990  0.0266  0.0672  362  GLU D O   
11640 C  CB  . GLU D 362 ? 0.4904 0.4322 0.8161 0.1237  0.0213  0.0691  362  GLU D CB  
11641 C  CG  . GLU D 362 ? 0.6861 0.6060 1.0040 0.1284  0.0261  0.0653  362  GLU D CG  
11642 C  CD  . GLU D 362 ? 0.9770 0.8922 1.3170 0.1421  0.0210  0.0663  362  GLU D CD  
11643 O  OE1 . GLU D 362 ? 1.0040 0.9257 1.3568 0.1473  0.0091  0.0737  362  GLU D OE1 
11644 O  OE2 . GLU D 362 ? 0.9969 0.9012 1.3414 0.1479  0.0279  0.0594  362  GLU D OE2 
11645 N  N   . GLU D 363 ? 0.4970 0.4659 0.8059 0.1052  0.0023  0.0819  363  GLU D N   
11646 C  CA  . GLU D 363 ? 0.4190 0.4053 0.7292 0.0963  0.0018  0.0818  363  GLU D CA  
11647 C  C   . GLU D 363 ? 0.4459 0.4239 0.7262 0.0851  0.0002  0.0818  363  GLU D C   
11648 O  O   . GLU D 363 ? 0.4956 0.4838 0.7715 0.0758  0.0017  0.0801  363  GLU D O   
11649 C  CB  . GLU D 363 ? 0.5066 0.5069 0.8341 0.1001  -0.0118 0.0891  363  GLU D CB  
11650 C  CG  . GLU D 363 ? 0.8017 0.8175 1.1629 0.1085  -0.0089 0.0873  363  GLU D CG  
11651 C  CD  . GLU D 363 ? 1.0171 1.0477 1.3958 0.1110  -0.0226 0.0943  363  GLU D CD  
11652 O  OE1 . GLU D 363 ? 1.0340 1.0560 1.4054 0.1150  -0.0369 0.1018  363  GLU D OE1 
11653 O  OE2 . GLU D 363 ? 1.0893 1.1404 1.4891 0.1087  -0.0192 0.0924  363  GLU D OE2 
11654 N  N   . LYS D 364 ? 0.3707 0.3303 0.6308 0.0857  -0.0032 0.0838  364  LYS D N   
11655 C  CA  . LYS D 364 ? 0.3873 0.3383 0.6194 0.0759  -0.0048 0.0830  364  LYS D CA  
11656 C  C   . LYS D 364 ? 0.5097 0.4421 0.7254 0.0747  0.0044  0.0782  364  LYS D C   
11657 O  O   . LYS D 364 ? 0.6801 0.5988 0.8826 0.0765  -0.0007 0.0818  364  LYS D O   
11658 C  CB  . LYS D 364 ? 0.4562 0.4057 0.6774 0.0761  -0.0207 0.0908  364  LYS D CB  
11659 C  CG  . LYS D 364 ? 0.4530 0.3960 0.6470 0.0666  -0.0238 0.0893  364  LYS D CG  
11660 C  CD  . LYS D 364 ? 0.4335 0.3853 0.6244 0.0569  -0.0194 0.0840  364  LYS D CD  
11661 C  CE  . LYS D 364 ? 0.3667 0.3126 0.5322 0.0480  -0.0249 0.0822  364  LYS D CE  
11662 N  NZ  . LYS D 364 ? 0.2606 0.2127 0.4228 0.0384  -0.0201 0.0771  364  LYS D NZ  
11663 N  N   . PRO D 365 ? 0.5131 0.4453 0.7296 0.0715  0.0180  0.0699  365  PRO D N   
11664 C  CA  . PRO D 365 ? 0.5174 0.4322 0.7179 0.0692  0.0273  0.0639  365  PRO D CA  
11665 C  C   . PRO D 365 ? 0.5163 0.4235 0.6899 0.0589  0.0245  0.0630  365  PRO D C   
11666 O  O   . PRO D 365 ? 0.5432 0.4602 0.7117 0.0525  0.0184  0.0644  365  PRO D O   
11667 C  CB  . PRO D 365 ? 0.5957 0.5173 0.8056 0.0680  0.0417  0.0551  365  PRO D CB  
11668 C  CG  . PRO D 365 ? 0.5398 0.4835 0.7729 0.0699  0.0402  0.0570  365  PRO D CG  
11669 C  CD  . PRO D 365 ? 0.5714 0.5211 0.8028 0.0685  0.0250  0.0658  365  PRO D CD  
11670 N  N   . MET D 366 ? 0.5356 0.4253 0.6928 0.0573  0.0283  0.0603  366  MET D N   
11671 C  CA  . MET D 366 ? 0.3917 0.2739 0.5245 0.0474  0.0273  0.0573  366  MET D CA  
11672 C  C   . MET D 366 ? 0.4725 0.3499 0.5983 0.0418  0.0400  0.0477  366  MET D C   
11673 O  O   . MET D 366 ? 0.4778 0.3485 0.6107 0.0464  0.0500  0.0431  366  MET D O   
11674 C  CB  . MET D 366 ? 0.5327 0.3996 0.6508 0.0479  0.0228  0.0604  366  MET D CB  
11675 C  CG  . MET D 366 ? 0.4133 0.2842 0.5337 0.0524  0.0100  0.0700  366  MET D CG  
11676 S  SD  . MET D 366 ? 0.6343 0.5199 0.7473 0.0466  -0.0023 0.0725  366  MET D SD  
11677 C  CE  . MET D 366 ? 0.5049 0.4082 0.6441 0.0535  -0.0070 0.0774  366  MET D CE  
11678 N  N   . ARG D 367 ? 0.4232 0.3035 0.5348 0.0322  0.0389  0.0446  367  ARG D N   
11679 C  CA  . ARG D 367 ? 0.4251 0.2998 0.5261 0.0256  0.0496  0.0358  367  ARG D CA  
11680 C  C   . ARG D 367 ? 0.4407 0.2980 0.5185 0.0201  0.0488  0.0323  367  ARG D C   
11681 O  O   . ARG D 367 ? 0.7642 0.6209 0.8287 0.0148  0.0392  0.0342  367  ARG D O   
11682 C  CB  . ARG D 367 ? 0.5913 0.4795 0.6915 0.0178  0.0487  0.0348  367  ARG D CB  
11683 C  CG  . ARG D 367 ? 0.7954 0.6781 0.8822 0.0097  0.0587  0.0264  367  ARG D CG  
11684 C  CD  . ARG D 367 ? 0.9106 0.7846 0.9732 -0.0001 0.0511  0.0247  367  ARG D CD  
11685 N  NE  . ARG D 367 ? 1.0346 0.9136 1.0894 -0.0096 0.0539  0.0212  367  ARG D NE  
11686 C  CZ  . ARG D 367 ? 1.1390 1.0255 1.1885 -0.0169 0.0440  0.0241  367  ARG D CZ  
11687 N  NH1 . ARG D 367 ? 1.2587 1.1493 1.3091 -0.0154 0.0297  0.0301  367  ARG D NH1 
11688 N  NH2 . ARG D 367 ? 1.0709 0.9601 1.1129 -0.0259 0.0482  0.0209  367  ARG D NH2 
11689 N  N   . THR D 368 ? 0.3977 0.2409 0.4714 0.0218  0.0582  0.0267  368  THR D N   
11690 C  CA  . THR D 368 ? 0.3803 0.2065 0.4344 0.0173  0.0573  0.0237  368  THR D CA  
11691 C  C   . THR D 368 ? 0.3282 0.1523 0.3634 0.0067  0.0564  0.0180  368  THR D C   
11692 O  O   . THR D 368 ? 0.2948 0.1257 0.3300 0.0026  0.0609  0.0144  368  THR D O   
11693 C  CB  . THR D 368 ? 0.3123 0.1232 0.3666 0.0211  0.0673  0.0183  368  THR D CB  
11694 O  OG1 . THR D 368 ? 0.4322 0.2429 0.4839 0.0181  0.0779  0.0097  368  THR D OG1 
11695 C  CG2 . THR D 368 ? 0.4064 0.2188 0.4809 0.0321  0.0680  0.0231  368  THR D CG2 
11696 N  N   . SER D 369 ? 0.3954 0.2097 0.4142 0.0021  0.0505  0.0173  369  SER D N   
11697 C  CA  . SER D 369 ? 0.4202 0.2295 0.4199 -0.0075 0.0480  0.0114  369  SER D CA  
11698 C  C   . SER D 369 ? 0.5573 0.3528 0.5473 -0.0108 0.0590  0.0024  369  SER D C   
11699 O  O   . SER D 369 ? 0.6078 0.3978 0.6062 -0.0051 0.0687  0.0003  369  SER D O   
11700 C  CB  . SER D 369 ? 0.4369 0.2402 0.4244 -0.0101 0.0389  0.0126  369  SER D CB  
11701 O  OG  . SER D 369 ? 0.4343 0.2228 0.4185 -0.0081 0.0443  0.0107  369  SER D OG  
11702 N  N   . LYS D 370 ? 0.5348 0.3239 0.5064 -0.0197 0.0567  -0.0034 370  LYS D N   
11703 C  CA  . LYS D 370 ? 0.5546 0.3293 0.5136 -0.0238 0.0658  -0.0124 370  LYS D CA  
11704 C  C   . LYS D 370 ? 0.5735 0.3319 0.5307 -0.0199 0.0705  -0.0152 370  LYS D C   
11705 O  O   . LYS D 370 ? 0.7720 0.5192 0.7253 -0.0194 0.0800  -0.0218 370  LYS D O   
11706 C  CB  . LYS D 370 ? 0.4420 0.2110 0.3804 -0.0341 0.0595  -0.0175 370  LYS D CB  
11707 C  CG  . LYS D 370 ? 0.3981 0.1789 0.3352 -0.0396 0.0568  -0.0163 370  LYS D CG  
11708 C  CD  . LYS D 370 ? 0.3675 0.1431 0.2855 -0.0490 0.0457  -0.0195 370  LYS D CD  
11709 C  CE  . LYS D 370 ? 0.4333 0.2219 0.3524 -0.0542 0.0396  -0.0159 370  LYS D CE  
11710 N  NZ  . LYS D 370 ? 0.5940 0.3745 0.4925 -0.0642 0.0299  -0.0202 370  LYS D NZ  
11711 N  N   . ARG D 371 ? 0.4552 0.2122 0.4148 -0.0174 0.0638  -0.0100 371  ARG D N   
11712 C  CA  . ARG D 371 ? 0.4676 0.2097 0.4268 -0.0143 0.0673  -0.0111 371  ARG D CA  
11713 C  C   . ARG D 371 ? 0.5831 0.3286 0.5615 -0.0045 0.0708  -0.0049 371  ARG D C   
11714 O  O   . ARG D 371 ? 0.5940 0.3292 0.5751 -0.0011 0.0710  -0.0025 371  ARG D O   
11715 C  CB  . ARG D 371 ? 0.5212 0.2597 0.4712 -0.0183 0.0583  -0.0090 371  ARG D CB  
11716 C  CG  . ARG D 371 ? 0.4127 0.1503 0.3460 -0.0271 0.0520  -0.0146 371  ARG D CG  
11717 C  CD  . ARG D 371 ? 0.5932 0.3228 0.5179 -0.0304 0.0468  -0.0155 371  ARG D CD  
11718 N  NE  . ARG D 371 ? 0.7578 0.4945 0.6726 -0.0361 0.0365  -0.0173 371  ARG D NE  
11719 C  CZ  . ARG D 371 ? 0.8892 0.6358 0.8051 -0.0359 0.0278  -0.0129 371  ARG D CZ  
11720 N  NH1 . ARG D 371 ? 0.8163 0.5666 0.7416 -0.0311 0.0281  -0.0054 371  ARG D NH1 
11721 N  NH2 . ARG D 371 ? 1.0402 0.7926 0.9468 -0.0408 0.0182  -0.0166 371  ARG D NH2 
11722 N  N   . GLY D 372 ? 0.6281 0.3880 0.6203 -0.0001 0.0728  -0.0021 372  GLY D N   
11723 C  CA  . GLY D 372 ? 0.7047 0.4682 0.7163 0.0098  0.0756  0.0028  372  GLY D CA  
11724 C  C   . GLY D 372 ? 0.5872 0.3533 0.6053 0.0135  0.0668  0.0126  372  GLY D C   
11725 O  O   . GLY D 372 ? 0.4448 0.2058 0.4743 0.0210  0.0681  0.0163  372  GLY D O   
11726 N  N   . GLU D 373 ? 0.4713 0.2450 0.4815 0.0087  0.0573  0.0165  373  GLU D N   
11727 C  CA  . GLU D 373 ? 0.5218 0.2995 0.5362 0.0118  0.0489  0.0257  373  GLU D CA  
11728 C  C   . GLU D 373 ? 0.5956 0.3907 0.6243 0.0169  0.0435  0.0324  373  GLU D C   
11729 O  O   . GLU D 373 ? 0.5604 0.3668 0.5919 0.0150  0.0435  0.0303  373  GLU D O   
11730 C  CB  . GLU D 373 ? 0.4353 0.2124 0.4339 0.0048  0.0412  0.0260  373  GLU D CB  
11731 C  CG  . GLU D 373 ? 0.5789 0.3468 0.5614 -0.0033 0.0439  0.0167  373  GLU D CG  
11732 C  CD  . GLU D 373 ? 0.5700 0.3440 0.5400 -0.0096 0.0344  0.0160  373  GLU D CD  
11733 O  OE1 . GLU D 373 ? 0.5555 0.3287 0.5219 -0.0101 0.0298  0.0198  373  GLU D OE1 
11734 O  OE2 . GLU D 373 ? 0.6292 0.4090 0.5930 -0.0141 0.0313  0.0117  373  GLU D OE2 
11735 N  N   . TYR D 374 ? 0.6348 0.4314 0.6722 0.0229  0.0385  0.0409  374  TYR D N   
11736 C  CA  . TYR D 374 ? 0.5814 0.3933 0.6322 0.0283  0.0318  0.0480  374  TYR D CA  
11737 C  C   . TYR D 374 ? 0.5066 0.3183 0.5547 0.0304  0.0229  0.0568  374  TYR D C   
11738 O  O   . TYR D 374 ? 0.4629 0.2620 0.5059 0.0305  0.0242  0.0589  374  TYR D O   
11739 C  CB  . TYR D 374 ? 0.4915 0.3055 0.5625 0.0368  0.0374  0.0486  374  TYR D CB  
11740 C  CG  . TYR D 374 ? 0.4656 0.2677 0.5432 0.0437  0.0374  0.0536  374  TYR D CG  
11741 C  CD1 . TYR D 374 ? 0.4053 0.1911 0.4812 0.0446  0.0453  0.0487  374  TYR D CD1 
11742 C  CD2 . TYR D 374 ? 0.6069 0.4131 0.6915 0.0490  0.0286  0.0634  374  TYR D CD2 
11743 C  CE1 . TYR D 374 ? 0.5500 0.3232 0.6315 0.0505  0.0441  0.0535  374  TYR D CE1 
11744 C  CE2 . TYR D 374 ? 0.6153 0.4091 0.7046 0.0546  0.0275  0.0686  374  TYR D CE2 
11745 C  CZ  . TYR D 374 ? 0.6179 0.3949 0.7059 0.0551  0.0351  0.0637  374  TYR D CZ  
11746 O  OH  . TYR D 374 ? 0.5583 0.3211 0.6506 0.0602  0.0330  0.0691  374  TYR D OH  
11747 N  N   . TRP D 375 ? 0.5133 0.3392 0.5643 0.0317  0.0136  0.0620  375  TRP D N   
11748 C  CA  . TRP D 375 ? 0.4825 0.3103 0.5329 0.0352  0.0050  0.0711  375  TRP D CA  
11749 C  C   . TRP D 375 ? 0.5358 0.3746 0.6042 0.0432  0.0001  0.0769  375  TRP D C   
11750 O  O   . TRP D 375 ? 0.5690 0.4206 0.6437 0.0429  -0.0025 0.0752  375  TRP D O   
11751 C  CB  . TRP D 375 ? 0.3364 0.1714 0.3713 0.0296  -0.0035 0.0713  375  TRP D CB  
11752 C  CG  . TRP D 375 ? 0.3250 0.1522 0.3438 0.0213  0.0004  0.0639  375  TRP D CG  
11753 C  CD1 . TRP D 375 ? 0.4472 0.2670 0.4538 0.0175  0.0002  0.0646  375  TRP D CD1 
11754 C  CD2 . TRP D 375 ? 0.3772 0.2030 0.3902 0.0154  0.0046  0.0545  375  TRP D CD2 
11755 N  NE1 . TRP D 375 ? 0.4337 0.2479 0.4286 0.0101  0.0039  0.0558  375  TRP D NE1 
11756 C  CE2 . TRP D 375 ? 0.5065 0.3235 0.5042 0.0088  0.0063  0.0496  375  TRP D CE2 
11757 C  CE3 . TRP D 375 ? 0.4071 0.2384 0.4260 0.0146  0.0071  0.0501  375  TRP D CE3 
11758 C  CZ2 . TRP D 375 ? 0.4733 0.2855 0.4613 0.0021  0.0095  0.0402  375  TRP D CZ2 
11759 C  CZ3 . TRP D 375 ? 0.3775 0.2041 0.3854 0.0073  0.0107  0.0413  375  TRP D CZ3 
11760 C  CH2 . TRP D 375 ? 0.2980 0.1145 0.2904 0.0014  0.0115  0.0363  375  TRP D CH2 
11761 N  N   . ARG D 376 ? 0.5216 0.3548 0.5986 0.0501  -0.0016 0.0840  376  ARG D N   
11762 C  CA  . ARG D 376 ? 0.4266 0.2697 0.5200 0.0581  -0.0082 0.0903  376  ARG D CA  
11763 C  C   . ARG D 376 ? 0.5507 0.3952 0.6378 0.0603  -0.0191 0.0997  376  ARG D C   
11764 O  O   . ARG D 376 ? 0.5042 0.3371 0.5886 0.0627  -0.0197 0.1055  376  ARG D O   
11765 C  CB  . ARG D 376 ? 0.4603 0.2971 0.5721 0.0658  -0.0024 0.0902  376  ARG D CB  
11766 C  CG  . ARG D 376 ? 0.5295 0.3770 0.6612 0.0746  -0.0091 0.0957  376  ARG D CG  
11767 C  CD  . ARG D 376 ? 0.4731 0.3389 0.6142 0.0732  -0.0103 0.0925  376  ARG D CD  
11768 N  NE  . ARG D 376 ? 0.5026 0.3787 0.6627 0.0814  -0.0181 0.0983  376  ARG D NE  
11769 C  CZ  . ARG D 376 ? 0.5845 0.4772 0.7544 0.0812  -0.0230 0.0985  376  ARG D CZ  
11770 N  NH1 . ARG D 376 ? 0.7619 0.6626 0.9237 0.0731  -0.0213 0.0936  376  ARG D NH1 
11771 N  NH2 . ARG D 376 ? 0.7107 0.6114 0.8987 0.0891  -0.0305 0.1040  376  ARG D NH2 
11772 N  N   . LEU D 377 ? 0.3852 0.2434 0.4688 0.0592  -0.0279 0.1011  377  LEU D N   
11773 C  CA  . LEU D 377 ? 0.3718 0.2338 0.4504 0.0624  -0.0389 0.1096  377  LEU D CA  
11774 C  C   . LEU D 377 ? 0.4538 0.3135 0.5488 0.0719  -0.0428 0.1173  377  LEU D C   
11775 O  O   . LEU D 377 ? 0.4389 0.3057 0.5524 0.0770  -0.0432 0.1164  377  LEU D O   
11776 C  CB  . LEU D 377 ? 0.3732 0.2509 0.4480 0.0607  -0.0484 0.1086  377  LEU D CB  
11777 C  CG  . LEU D 377 ? 0.3244 0.2048 0.3842 0.0519  -0.0466 0.1003  377  LEU D CG  
11778 C  CD1 . LEU D 377 ? 0.2477 0.1420 0.3025 0.0513  -0.0585 0.1000  377  LEU D CD1 
11779 C  CD2 . LEU D 377 ? 0.3258 0.1962 0.3688 0.0471  -0.0425 0.0997  377  LEU D CD2 
11780 N  N   . LEU D 378 ? 0.5929 0.4428 0.6810 0.0740  -0.0462 0.1250  378  LEU D N   
11781 C  CA  . LEU D 378 ? 0.5778 0.4225 0.6797 0.0830  -0.0510 0.1326  378  LEU D CA  
11782 C  C   . LEU D 378 ? 0.4297 0.2726 0.5209 0.0851  -0.0616 0.1429  378  LEU D C   
11783 O  O   . LEU D 378 ? 0.6398 0.4783 0.7119 0.0794  -0.0615 0.1453  378  LEU D O   
11784 C  CB  . LEU D 378 ? 0.4871 0.3150 0.5957 0.0849  -0.0426 0.1315  378  LEU D CB  
11785 C  CG  . LEU D 378 ? 0.3340 0.1636 0.4578 0.0859  -0.0327 0.1220  378  LEU D CG  
11786 C  CD1 . LEU D 378 ? 0.4071 0.2188 0.5355 0.0886  -0.0260 0.1210  378  LEU D CD1 
11787 C  CD2 . LEU D 378 ? 0.3211 0.1645 0.4664 0.0931  -0.0366 0.1217  378  LEU D CD2 
11788 N  N   . THR D 379 ? 0.4948 0.3416 0.5987 0.0934  -0.0706 0.1487  379  THR D N   
11789 C  CA  . THR D 379 ? 0.5346 0.3772 0.6301 0.0968  -0.0809 0.1592  379  THR D CA  
11790 C  C   . THR D 379 ? 0.5925 0.4151 0.6849 0.0974  -0.0780 0.1649  379  THR D C   
11791 O  O   . THR D 379 ? 0.4578 0.2711 0.5633 0.0998  -0.0711 0.1613  379  THR D O   
11792 C  CB  . THR D 379 ? 0.6599 0.5101 0.7725 0.1061  -0.0913 0.1631  379  THR D CB  
11793 O  OG1 . THR D 379 ? 0.7911 0.6590 0.9036 0.1049  -0.0964 0.1593  379  THR D OG1 
11794 C  CG2 . THR D 379 ? 0.8401 0.6822 0.9454 0.1108  -0.1020 0.1745  379  THR D CG2 
11795 N  N   . PRO D 380 ? 0.5892 0.4048 0.6636 0.0950  -0.0831 0.1737  380  PRO D N   
11796 C  CA  . PRO D 380 ? 0.6256 0.4207 0.6978 0.0955  -0.0822 0.1805  380  PRO D CA  
11797 C  C   . PRO D 380 ? 0.7329 0.5199 0.8283 0.1058  -0.0854 0.1818  380  PRO D C   
11798 O  O   . PRO D 380 ? 0.6985 0.4958 0.8081 0.1132  -0.0926 0.1820  380  PRO D O   
11799 C  CB  . PRO D 380 ? 0.4478 0.2408 0.5007 0.0938  -0.0910 0.1917  380  PRO D CB  
11800 C  CG  . PRO D 380 ? 0.5382 0.3491 0.5773 0.0884  -0.0912 0.1876  380  PRO D CG  
11801 C  CD  . PRO D 380 ? 0.5628 0.3883 0.6178 0.0913  -0.0897 0.1776  380  PRO D CD  
11802 N  N   . GLY D 381 ? 0.7006 0.4694 0.8005 0.1064  -0.0808 0.1821  381  GLY D N   
11803 C  CA  . GLY D 381 ? 0.5809 0.3416 0.7036 0.1165  -0.0833 0.1814  381  GLY D CA  
11804 C  C   . GLY D 381 ? 0.5833 0.3333 0.7144 0.1157  -0.0723 0.1732  381  GLY D C   
11805 O  O   . GLY D 381 ? 0.6744 0.4216 0.7922 0.1069  -0.0635 0.1691  381  GLY D O   
11806 N  N   . LEU D 382 ? 0.4806 0.2245 0.6336 0.1250  -0.0730 0.1701  382  LEU D N   
11807 C  CA  . LEU D 382 ? 0.6464 0.3802 0.8073 0.1253  -0.0629 0.1613  382  LEU D CA  
11808 C  C   . LEU D 382 ? 0.6434 0.3925 0.8274 0.1310  -0.0558 0.1495  382  LEU D C   
11809 O  O   . LEU D 382 ? 0.4672 0.2281 0.6695 0.1390  -0.0614 0.1495  382  LEU D O   
11810 C  CB  . LEU D 382 ? 0.7372 0.4461 0.9010 0.1300  -0.0681 0.1666  382  LEU D CB  
11811 C  CG  . LEU D 382 ? 0.9054 0.6095 1.0920 0.1431  -0.0772 0.1682  382  LEU D CG  
11812 C  CD1 . LEU D 382 ? 0.9649 0.6762 1.1766 0.1508  -0.0692 0.1549  382  LEU D CD1 
11813 C  CD2 . LEU D 382 ? 1.0654 0.7424 1.2454 0.1447  -0.0857 0.1772  382  LEU D CD2 
11814 N  N   . TYR D 383 ? 0.6207 0.3697 0.8034 0.1265  -0.0435 0.1394  383  TYR D N   
11815 C  CA  . TYR D 383 ? 0.5533 0.3188 0.7529 0.1291  -0.0348 0.1280  383  TYR D CA  
11816 C  C   . TYR D 383 ? 0.6217 0.3774 0.8296 0.1315  -0.0244 0.1178  383  TYR D C   
11817 O  O   . TYR D 383 ? 0.6818 0.4190 0.8769 0.1274  -0.0214 0.1178  383  TYR D O   
11818 C  CB  . TYR D 383 ? 0.5752 0.3570 0.7616 0.1194  -0.0296 0.1246  383  TYR D CB  
11819 C  CG  . TYR D 383 ? 0.6261 0.4178 0.8022 0.1168  -0.0397 0.1333  383  TYR D CG  
11820 C  CD1 . TYR D 383 ? 0.6236 0.4058 0.7772 0.1107  -0.0446 0.1415  383  TYR D CD1 
11821 C  CD2 . TYR D 383 ? 0.6170 0.4279 0.8058 0.1203  -0.0445 0.1332  383  TYR D CD2 
11822 C  CE1 . TYR D 383 ? 0.6435 0.4354 0.7870 0.1089  -0.0538 0.1487  383  TYR D CE1 
11823 C  CE2 . TYR D 383 ? 0.6562 0.4755 0.8353 0.1186  -0.0546 0.1405  383  TYR D CE2 
11824 C  CZ  . TYR D 383 ? 0.7441 0.5540 0.9002 0.1133  -0.0591 0.1479  383  TYR D CZ  
11825 O  OH  . TYR D 383 ? 0.7399 0.5591 0.8859 0.1123  -0.0691 0.1544  383  TYR D OH  
11826 N  N   . SER D 384 ? 0.6329 0.4018 0.8627 0.1380  -0.0189 0.1089  384  SER D N   
11827 C  CA  . SER D 384 ? 0.6074 0.3721 0.8451 0.1401  -0.0074 0.0970  384  SER D CA  
11828 C  C   . SER D 384 ? 0.6720 0.4538 0.9051 0.1325  0.0038  0.0885  384  SER D C   
11829 O  O   . SER D 384 ? 0.4870 0.2895 0.7350 0.1346  0.0062  0.0847  384  SER D O   
11830 C  CB  . SER D 384 ? 0.5632 0.3301 0.8293 0.1534  -0.0085 0.0920  384  SER D CB  
11831 O  OG  . SER D 384 ? 0.9289 0.6722 1.1959 0.1595  -0.0154 0.0958  384  SER D OG  
11832 N  N   . VAL D 385 ? 0.7060 0.4785 0.9183 0.1232  0.0101  0.0858  385  VAL D N   
11833 C  CA  . VAL D 385 ? 0.6422 0.4271 0.8466 0.1151  0.0199  0.0779  385  VAL D CA  
11834 C  C   . VAL D 385 ? 0.6397 0.4208 0.8501 0.1171  0.0323  0.0653  385  VAL D C   
11835 O  O   . VAL D 385 ? 0.6491 0.4112 0.8585 0.1205  0.0337  0.0629  385  VAL D O   
11836 C  CB  . VAL D 385 ? 0.5395 0.3177 0.7172 0.1035  0.0190  0.0815  385  VAL D CB  
11837 C  CG1 . VAL D 385 ? 0.4563 0.2512 0.6265 0.0954  0.0237  0.0767  385  VAL D CG1 
11838 C  CG2 . VAL D 385 ? 0.4968 0.2709 0.6663 0.1030  0.0066  0.0943  385  VAL D CG2 
11839 N  N   . HIS D 386 ? 0.4997 0.2985 0.7160 0.1148  0.0409  0.0574  386  HIS D N   
11840 C  CA  . HIS D 386 ? 0.4511 0.2480 0.6685 0.1148  0.0538  0.0449  386  HIS D CA  
11841 C  C   . HIS D 386 ? 0.4776 0.2884 0.6846 0.1049  0.0619  0.0393  386  HIS D C   
11842 O  O   . HIS D 386 ? 0.4104 0.2364 0.6155 0.0998  0.0576  0.0441  386  HIS D O   
11843 C  CB  . HIS D 386 ? 0.6087 0.4115 0.8526 0.1271  0.0579  0.0380  386  HIS D CB  
11844 C  CG  . HIS D 386 ? 0.7492 0.5787 1.0124 0.1294  0.0602  0.0362  386  HIS D CG  
11845 N  ND1 . HIS D 386 ? 0.9493 0.7953 1.2058 0.1205  0.0595  0.0396  386  HIS D ND1 
11846 C  CD2 . HIS D 386 ? 0.7840 0.6269 1.0742 0.1395  0.0629  0.0312  386  HIS D CD2 
11847 C  CE1 . HIS D 386 ? 0.7039 0.5718 0.9819 0.1244  0.0616  0.0375  386  HIS D CE1 
11848 N  NE2 . HIS D 386 ? 0.6039 0.4713 0.9031 0.1359  0.0641  0.0323  386  HIS D NE2 
11849 N  N   . ALA D 387 ? 0.4522 0.2564 0.6515 0.1023  0.0727  0.0291  387  ALA D N   
11850 C  CA  . ALA D 387 ? 0.5209 0.3346 0.7073 0.0923  0.0800  0.0237  387  ALA D CA  
11851 C  C   . ALA D 387 ? 0.5835 0.4063 0.7809 0.0955  0.0927  0.0123  387  ALA D C   
11852 O  O   . ALA D 387 ? 0.6258 0.4408 0.8340 0.1044  0.0973  0.0060  387  ALA D O   
11853 C  CB  . ALA D 387 ? 0.6077 0.4038 0.7678 0.0830  0.0806  0.0226  387  ALA D CB  
11854 N  N   . SER D 388 ? 0.4079 0.2472 0.6020 0.0881  0.0981  0.0094  388  SER D N   
11855 C  CA  . SER D 388 ? 0.5576 0.4081 0.7597 0.0892  0.1111  -0.0011 388  SER D CA  
11856 C  C   . SER D 388 ? 0.5867 0.4425 0.7694 0.0763  0.1164  -0.0042 388  SER D C   
11857 O  O   . SER D 388 ? 0.4429 0.2993 0.6121 0.0677  0.1085  0.0026  388  SER D O   
11858 C  CB  . SER D 388 ? 0.5039 0.3772 0.7350 0.0971  0.1119  -0.0005 388  SER D CB  
11859 O  OG  . SER D 388 ? 0.5994 0.4890 0.8329 0.0912  0.1047  0.0079  388  SER D OG  
11860 N  N   . ALA D 389 ? 0.6754 0.5345 0.8561 0.0751  0.1293  -0.0147 389  ALA D N   
11861 C  CA  . ALA D 389 ? 0.5716 0.4349 0.7335 0.0628  0.1350  -0.0183 389  ALA D CA  
11862 C  C   . ALA D 389 ? 0.6105 0.4847 0.7784 0.0641  0.1502  -0.0292 389  ALA D C   
11863 O  O   . ALA D 389 ? 0.7274 0.5969 0.9055 0.0739  0.1570  -0.0369 389  ALA D O   
11864 C  CB  . ALA D 389 ? 0.3727 0.2129 0.5072 0.0559  0.1325  -0.0196 389  ALA D CB  
11865 N  N   . PHE D 390 ? 0.5330 0.4221 0.6947 0.0542  0.1551  -0.0300 390  PHE D N   
11866 C  CA  . PHE D 390 ? 0.7784 0.6806 0.9445 0.0538  0.1701  -0.0397 390  PHE D CA  
11867 C  C   . PHE D 390 ? 0.7500 0.6326 0.8982 0.0548  0.1789  -0.0507 390  PHE D C   
11868 O  O   . PHE D 390 ? 0.7037 0.5673 0.8267 0.0471  0.1753  -0.0506 390  PHE D O   
11869 C  CB  . PHE D 390 ? 0.9285 0.8471 1.0863 0.0405  0.1724  -0.0371 390  PHE D CB  
11870 C  CG  . PHE D 390 ? 1.1843 1.1150 1.3410 0.0375  0.1886  -0.0468 390  PHE D CG  
11871 C  CD1 . PHE D 390 ? 1.2777 1.1974 1.4063 0.0270  0.1943  -0.0520 390  PHE D CD1 
11872 C  CD2 . PHE D 390 ? 1.2747 1.2284 1.4583 0.0452  0.1979  -0.0509 390  PHE D CD2 
11873 C  CE1 . PHE D 390 ? 1.3285 1.2595 1.4540 0.0239  0.2096  -0.0608 390  PHE D CE1 
11874 C  CE2 . PHE D 390 ? 1.3441 1.3108 1.5262 0.0423  0.2138  -0.0602 390  PHE D CE2 
11875 C  CZ  . PHE D 390 ? 1.3492 1.3043 1.5014 0.0314  0.2198  -0.0650 390  PHE D CZ  
11876 N  N   . GLY D 391 ? 0.6638 0.5510 0.8258 0.0645  0.1898  -0.0606 391  GLY D N   
11877 C  CA  . GLY D 391 ? 0.6551 0.5235 0.8019 0.0671  0.1976  -0.0718 391  GLY D CA  
11878 C  C   . GLY D 391 ? 0.6525 0.4973 0.8010 0.0768  0.1901  -0.0718 391  GLY D C   
11879 O  O   . GLY D 391 ? 0.5520 0.3773 0.6874 0.0791  0.1940  -0.0802 391  GLY D O   
11880 N  N   . TYR D 392 ? 0.7519 0.5977 0.9158 0.0820  0.1787  -0.0621 392  TYR D N   
11881 C  CA  . TYR D 392 ? 0.7215 0.5457 0.8883 0.0906  0.1704  -0.0602 392  TYR D CA  
11882 C  C   . TYR D 392 ? 0.7769 0.6113 0.9735 0.1033  0.1660  -0.0572 392  TYR D C   
11883 O  O   . TYR D 392 ? 0.8284 0.6837 1.0407 0.1030  0.1630  -0.0506 392  TYR D O   
11884 C  CB  . TYR D 392 ? 0.6790 0.4877 0.8284 0.0825  0.1579  -0.0496 392  TYR D CB  
11885 C  CG  . TYR D 392 ? 0.8133 0.6066 0.9333 0.0714  0.1599  -0.0531 392  TYR D CG  
11886 C  CD1 . TYR D 392 ? 0.8360 0.6034 0.9426 0.0728  0.1585  -0.0572 392  TYR D CD1 
11887 C  CD2 . TYR D 392 ? 0.7289 0.5326 0.8347 0.0594  0.1623  -0.0523 392  TYR D CD2 
11888 C  CE1 . TYR D 392 ? 0.8543 0.6073 0.9347 0.0627  0.1597  -0.0608 392  TYR D CE1 
11889 C  CE2 . TYR D 392 ? 0.7380 0.5265 0.8166 0.0494  0.1630  -0.0559 392  TYR D CE2 
11890 C  CZ  . TYR D 392 ? 0.8574 0.6210 0.9238 0.0513  0.1619  -0.0603 392  TYR D CZ  
11891 O  OH  . TYR D 392 ? 0.8340 0.5825 0.8745 0.0416  0.1620  -0.0642 392  TYR D OH  
11892 N  N   . GLN D 393 ? 0.8610 0.6795 1.0654 0.1145  0.1647  -0.0620 393  GLN D N   
11893 C  CA  . GLN D 393 ? 0.6874 0.5101 0.9186 0.1274  0.1581  -0.0591 393  GLN D CA  
11894 C  C   . GLN D 393 ? 0.7323 0.5482 0.9615 0.1243  0.1431  -0.0440 393  GLN D C   
11895 O  O   . GLN D 393 ? 0.7428 0.5382 0.9515 0.1180  0.1368  -0.0389 393  GLN D O   
11896 C  CB  . GLN D 393 ? 0.5243 0.3281 0.7611 0.1394  0.1592  -0.0684 393  GLN D CB  
11897 C  CG  . GLN D 393 ? 0.6186 0.4266 0.8525 0.1420  0.1742  -0.0843 393  GLN D CG  
11898 C  CD  . GLN D 393 ? 0.8334 0.6231 1.0747 0.1553  0.1741  -0.0944 393  GLN D CD  
11899 O  OE1 . GLN D 393 ? 0.9371 0.7048 1.1783 0.1596  0.1626  -0.0889 393  GLN D OE1 
11900 N  NE2 . GLN D 393 ? 0.8476 0.6464 1.0951 0.1617  0.1866  -0.1093 393  GLN D NE2 
11901 N  N   . THR D 394 ? 0.7705 0.6043 1.0207 0.1286  0.1376  -0.0372 394  THR D N   
11902 C  CA  . THR D 394 ? 0.7276 0.5581 0.9768 0.1261  0.1235  -0.0230 394  THR D CA  
11903 C  C   . THR D 394 ? 0.7271 0.5326 0.9754 0.1330  0.1137  -0.0188 394  THR D C   
11904 O  O   . THR D 394 ? 0.7358 0.5376 1.0030 0.1454  0.1122  -0.0226 394  THR D O   
11905 C  CB  . THR D 394 ? 0.6899 0.5446 0.9641 0.1309  0.1195  -0.0177 394  THR D CB  
11906 O  OG1 . THR D 394 ? 0.7353 0.6135 1.0105 0.1234  0.1283  -0.0208 394  THR D OG1 
11907 C  CG2 . THR D 394 ? 0.6870 0.5378 0.9579 0.1283  0.1046  -0.0034 394  THR D CG2 
11908 N  N   . SER D 395 ? 0.7217 0.5104 0.9481 0.1246  0.1066  -0.0109 395  SER D N   
11909 C  CA  . SER D 395 ? 0.6407 0.4036 0.8614 0.1281  0.0979  -0.0063 395  SER D CA  
11910 C  C   . SER D 395 ? 0.7250 0.4876 0.9672 0.1394  0.0880  -0.0001 395  SER D C   
11911 O  O   . SER D 395 ? 0.7416 0.5239 1.0005 0.1427  0.0853  0.0036  395  SER D O   
11912 C  CB  . SER D 395 ? 0.5831 0.3360 0.7809 0.1167  0.0907  0.0038  395  SER D CB  
11913 O  OG  . SER D 395 ? 0.6890 0.4562 0.8924 0.1151  0.0823  0.0145  395  SER D OG  
11914 N  N   . ALA D 396 ? 0.7439 0.4827 0.9851 0.1449  0.0817  0.0013  396  ALA D N   
11915 C  CA  . ALA D 396 ? 0.6437 0.3769 0.9006 0.1541  0.0697  0.0093  396  ALA D CA  
11916 C  C   . ALA D 396 ? 0.7328 0.4682 0.9789 0.1463  0.0596  0.0242  396  ALA D C   
11917 O  O   . ALA D 396 ? 0.8733 0.6076 1.0979 0.1344  0.0612  0.0276  396  ALA D O   
11918 C  CB  . ALA D 396 ? 0.4979 0.2025 0.7524 0.1598  0.0646  0.0081  396  ALA D CB  
11919 N  N   . PRO D 397 ? 0.6394 0.3781 0.9003 0.1532  0.0489  0.0327  397  PRO D N   
11920 C  CA  . PRO D 397 ? 0.5527 0.2938 0.8042 0.1473  0.0385  0.0467  397  PRO D CA  
11921 C  C   . PRO D 397 ? 0.5440 0.2599 0.7765 0.1425  0.0304  0.0559  397  PRO D C   
11922 O  O   . PRO D 397 ? 0.7611 0.4569 0.9975 0.1487  0.0267  0.0551  397  PRO D O   
11923 C  CB  . PRO D 397 ? 0.5222 0.2731 0.7982 0.1584  0.0298  0.0510  397  PRO D CB  
11924 C  CG  . PRO D 397 ? 0.6546 0.4131 0.9539 0.1692  0.0373  0.0381  397  PRO D CG  
11925 C  CD  . PRO D 397 ? 0.7250 0.4670 1.0132 0.1677  0.0459  0.0285  397  PRO D CD  
11926 N  N   . GLN D 398 ? 0.6115 0.3290 0.8243 0.1316  0.0274  0.0643  398  GLN D N   
11927 C  CA  . GLN D 398 ? 0.6451 0.3427 0.8411 0.1266  0.0187  0.0751  398  GLN D CA  
11928 C  C   . GLN D 398 ? 0.6167 0.3214 0.8124 0.1266  0.0072  0.0882  398  GLN D C   
11929 O  O   . GLN D 398 ? 0.6796 0.4045 0.8758 0.1239  0.0070  0.0898  398  GLN D O   
11930 C  CB  . GLN D 398 ? 0.5794 0.2705 0.7511 0.1137  0.0242  0.0741  398  GLN D CB  
11931 C  CG  . GLN D 398 ? 0.5162 0.1963 0.6855 0.1134  0.0342  0.0619  398  GLN D CG  
11932 C  CD  . GLN D 398 ? 0.6823 0.3590 0.8291 0.1008  0.0400  0.0593  398  GLN D CD  
11933 O  OE1 . GLN D 398 ? 0.6931 0.3618 0.8239 0.0927  0.0350  0.0676  398  GLN D OE1 
11934 N  NE2 . GLN D 398 ? 0.7508 0.4334 0.8963 0.0992  0.0507  0.0473  398  GLN D NE2 
11935 N  N   . GLN D 399 ? 0.7262 0.4131 0.9204 0.1296  -0.0029 0.0976  399  GLN D N   
11936 C  CA  . GLN D 399 ? 0.7405 0.4305 0.9316 0.1296  -0.0146 0.1105  399  GLN D CA  
11937 C  C   . GLN D 399 ? 0.8805 0.5639 1.0454 0.1173  -0.0165 0.1191  399  GLN D C   
11938 O  O   . GLN D 399 ? 1.0295 0.6947 1.1820 0.1118  -0.0143 0.1193  399  GLN D O   
11939 C  CB  . GLN D 399 ? 0.8516 0.5251 1.0550 0.1396  -0.0252 0.1162  399  GLN D CB  
11940 C  CG  . GLN D 399 ? 1.0933 0.7592 1.2855 0.1373  -0.0380 0.1315  399  GLN D CG  
11941 C  CD  . GLN D 399 ? 1.3194 0.9602 1.5165 0.1440  -0.0479 0.1373  399  GLN D CD  
11942 O  OE1 . GLN D 399 ? 1.3898 1.0093 1.5770 0.1401  -0.0470 0.1378  399  GLN D OE1 
11943 N  NE2 . GLN D 399 ? 1.3675 1.0096 1.5803 0.1541  -0.0583 0.1416  399  GLN D NE2 
11944 N  N   . VAL D 400 ? 0.8159 0.5145 0.9728 0.1131  -0.0208 0.1257  400  VAL D N   
11945 C  CA  . VAL D 400 ? 0.7212 0.4172 0.8540 0.1017  -0.0225 0.1331  400  VAL D CA  
11946 C  C   . VAL D 400 ? 0.6797 0.3822 0.8066 0.1020  -0.0337 0.1454  400  VAL D C   
11947 O  O   . VAL D 400 ? 0.5852 0.3037 0.7231 0.1076  -0.0378 0.1456  400  VAL D O   
11948 C  CB  . VAL D 400 ? 0.6994 0.4094 0.8213 0.0928  -0.0132 0.1251  400  VAL D CB  
11949 C  CG1 . VAL D 400 ? 0.7309 0.4650 0.8602 0.0949  -0.0144 0.1231  400  VAL D CG1 
11950 C  CG2 . VAL D 400 ? 0.9064 0.6118 1.0048 0.0814  -0.0140 0.1310  400  VAL D CG2 
11951 N  N   . ARG D 401 ? 0.7130 0.4028 0.8223 0.0958  -0.0387 0.1555  401  ARG D N   
11952 C  CA  . ARG D 401 ? 0.7436 0.4394 0.8435 0.0948  -0.0486 0.1671  401  ARG D CA  
11953 C  C   . ARG D 401 ? 0.7595 0.4717 0.8418 0.0852  -0.0455 0.1665  401  ARG D C   
11954 O  O   . ARG D 401 ? 0.8615 0.5680 0.9266 0.0755  -0.0417 0.1680  401  ARG D O   
11955 C  CB  . ARG D 401 ? 0.8750 0.5489 0.9645 0.0929  -0.0562 0.1793  401  ARG D CB  
11956 C  CG  . ARG D 401 ? 0.9632 0.6416 1.0396 0.0913  -0.0664 0.1920  401  ARG D CG  
11957 C  CD  . ARG D 401 ? 1.1130 0.7679 1.1825 0.0913  -0.0753 0.2046  401  ARG D CD  
11958 N  NE  . ARG D 401 ? 1.2264 0.8632 1.2857 0.0828  -0.0700 0.2053  401  ARG D NE  
11959 C  CZ  . ARG D 401 ? 1.2796 0.8921 1.3442 0.0854  -0.0735 0.2081  401  ARG D CZ  
11960 N  NH1 . ARG D 401 ? 1.3954 0.9931 1.4498 0.0766  -0.0685 0.2084  401  ARG D NH1 
11961 N  NH2 . ARG D 401 ? 1.2035 0.8059 1.2837 0.0968  -0.0825 0.2102  401  ARG D NH2 
11962 N  N   . VAL D 402 ? 0.7103 0.4432 0.7978 0.0881  -0.0477 0.1638  402  VAL D N   
11963 C  CA  . VAL D 402 ? 0.5769 0.3263 0.6490 0.0804  -0.0467 0.1626  402  VAL D CA  
11964 C  C   . VAL D 402 ? 0.7326 0.4838 0.7892 0.0782  -0.0559 0.1742  402  VAL D C   
11965 O  O   . VAL D 402 ? 0.5857 0.3447 0.6469 0.0844  -0.0650 0.1793  402  VAL D O   
11966 C  CB  . VAL D 402 ? 0.4379 0.2083 0.5205 0.0837  -0.0466 0.1552  402  VAL D CB  
11967 C  CG1 . VAL D 402 ? 0.3796 0.1649 0.4455 0.0766  -0.0482 0.1548  402  VAL D CG1 
11968 C  CG2 . VAL D 402 ? 0.5645 0.3360 0.6592 0.0841  -0.0362 0.1433  402  VAL D CG2 
11969 N  N   . THR D 403 ? 0.9770 0.7208 1.0150 0.0690  -0.0535 0.1783  403  THR D N   
11970 C  CA  . THR D 403 ? 1.0166 0.7670 1.0362 0.0644  -0.0594 0.1869  403  THR D CA  
11971 C  C   . THR D 403 ? 0.9887 0.7553 0.9977 0.0568  -0.0536 0.1786  403  THR D C   
11972 O  O   . THR D 403 ? 1.0678 0.8314 1.0771 0.0517  -0.0446 0.1703  403  THR D O   
11973 C  CB  . THR D 403 ? 1.0148 0.7475 1.0204 0.0580  -0.0600 0.1971  403  THR D CB  
11974 O  OG1 . THR D 403 ? 1.1947 0.9373 1.1806 0.0520  -0.0637 0.2041  403  THR D OG1 
11975 C  CG2 . THR D 403 ? 0.9139 0.6363 0.9168 0.0501  -0.0497 0.1911  403  THR D CG2 
11976 N  N   . ASN D 404 ? 0.6548 0.4382 0.6545 0.0564  -0.0591 0.1801  404  ASN D N   
11977 C  CA  . ASN D 404 ? 0.6447 0.4427 0.6345 0.0496  -0.0547 0.1717  404  ASN D CA  
11978 C  C   . ASN D 404 ? 0.6802 0.4803 0.6494 0.0410  -0.0543 0.1771  404  ASN D C   
11979 O  O   . ASN D 404 ? 0.6916 0.5081 0.6499 0.0396  -0.0584 0.1765  404  ASN D O   
11980 C  CB  . ASN D 404 ? 0.7314 0.5486 0.7266 0.0545  -0.0602 0.1660  404  ASN D CB  
11981 C  CG  . ASN D 404 ? 0.8583 0.6757 0.8737 0.0601  -0.0575 0.1583  404  ASN D CG  
11982 O  OD1 . ASN D 404 ? 0.7724 0.5844 0.7921 0.0566  -0.0486 0.1504  404  ASN D OD1 
11983 N  ND2 . ASN D 404 ? 0.7976 0.6217 0.8255 0.0686  -0.0653 0.1606  404  ASN D ND2 
11984 N  N   . ASP D 405 ? 0.9561 0.7398 0.9202 0.0351  -0.0494 0.1820  405  ASP D N   
11985 C  CA  . ASP D 405 ? 1.1932 0.9780 1.1387 0.0252  -0.0472 0.1873  405  ASP D CA  
11986 C  C   . ASP D 405 ? 1.1563 0.9470 1.0972 0.0167  -0.0384 0.1768  405  ASP D C   
11987 O  O   . ASP D 405 ? 0.9449 0.7524 0.8744 0.0119  -0.0382 0.1733  405  ASP D O   
11988 C  CB  . ASP D 405 ? 1.3807 1.1440 1.3228 0.0220  -0.0472 0.1988  405  ASP D CB  
11989 C  CG  . ASP D 405 ? 1.4869 1.2510 1.4109 0.0099  -0.0433 0.2040  405  ASP D CG  
11990 O  OD1 . ASP D 405 ? 1.3617 1.1448 1.2759 0.0050  -0.0410 0.1987  405  ASP D OD1 
11991 O  OD2 . ASP D 405 ? 1.5854 1.3312 1.5055 0.0052  -0.0428 0.2133  405  ASP D OD2 
11992 N  N   . ASN D 406 ? 1.2156 0.9924 1.1653 0.0151  -0.0316 0.1712  406  ASN D N   
11993 C  CA  . ASN D 406 ? 1.2240 1.0042 1.1696 0.0071  -0.0239 0.1611  406  ASN D CA  
11994 C  C   . ASN D 406 ? 1.2343 1.0343 1.1799 0.0086  -0.0249 0.1500  406  ASN D C   
11995 O  O   . ASN D 406 ? 1.2755 1.0815 1.2308 0.0165  -0.0289 0.1469  406  ASN D O   
11996 C  CB  . ASN D 406 ? 1.1434 0.9050 1.0989 0.0066  -0.0172 0.1557  406  ASN D CB  
11997 C  CG  . ASN D 406 ? 1.1124 0.8717 1.0602 -0.0038 -0.0100 0.1495  406  ASN D CG  
11998 O  OD1 . ASN D 406 ? 1.2976 1.0439 1.2402 -0.0103 -0.0076 0.1557  406  ASN D OD1 
11999 N  ND2 . ASN D 406 ? 0.8908 0.6624 0.8377 -0.0056 -0.0073 0.1376  406  ASN D ND2 
12000 N  N   . GLN D 407 ? 1.1149 0.9250 1.0501 0.0007  -0.0217 0.1441  407  GLN D N   
12001 C  CA  . GLN D 407 ? 0.9706 0.7986 0.9040 0.0011  -0.0235 0.1330  407  GLN D CA  
12002 C  C   . GLN D 407 ? 0.8320 0.6567 0.7773 0.0051  -0.0217 0.1233  407  GLN D C   
12003 O  O   . GLN D 407 ? 0.8515 0.6895 0.7975 0.0075  -0.0257 0.1160  407  GLN D O   
12004 C  CB  . GLN D 407 ? 1.0249 0.8601 0.9476 -0.0086 -0.0192 0.1269  407  GLN D CB  
12005 C  CG  . GLN D 407 ? 1.0536 0.9048 0.9631 -0.0119 -0.0225 0.1317  407  GLN D CG  
12006 C  CD  . GLN D 407 ? 1.2606 1.1181 1.1617 -0.0220 -0.0171 0.1260  407  GLN D CD  
12007 O  OE1 . GLN D 407 ? 1.2803 1.1248 1.1842 -0.0278 -0.0104 0.1231  407  GLN D OE1 
12008 N  NE2 . GLN D 407 ? 1.3366 1.2148 1.2280 -0.0239 -0.0201 0.1238  407  GLN D NE2 
12009 N  N   . GLU D 408 ? 0.6901 0.4969 0.6440 0.0056  -0.0159 0.1229  408  GLU D N   
12010 C  CA  . GLU D 408 ? 0.7273 0.5315 0.6917 0.0090  -0.0130 0.1136  408  GLU D CA  
12011 C  C   . GLU D 408 ? 0.7453 0.5371 0.7241 0.0166  -0.0119 0.1173  408  GLU D C   
12012 O  O   . GLU D 408 ? 0.7880 0.5659 0.7688 0.0176  -0.0112 0.1253  408  GLU D O   
12013 C  CB  . GLU D 408 ? 0.7239 0.5220 0.6839 0.0017  -0.0059 0.1035  408  GLU D CB  
12014 C  CG  . GLU D 408 ? 0.8088 0.6222 0.7579 -0.0038 -0.0084 0.0966  408  GLU D CG  
12015 C  CD  . GLU D 408 ? 0.9334 0.7404 0.8783 -0.0110 -0.0025 0.0864  408  GLU D CD  
12016 O  OE1 . GLU D 408 ? 0.7549 0.5676 0.6903 -0.0179 -0.0022 0.0840  408  GLU D OE1 
12017 O  OE2 . GLU D 408 ? 1.1604 0.9570 1.1116 -0.0096 0.0019  0.0805  408  GLU D OE2 
12018 N  N   . ALA D 409 ? 0.7457 0.5430 0.7349 0.0218  -0.0123 0.1114  409  ALA D N   
12019 C  CA  . ALA D 409 ? 0.6498 0.4393 0.6551 0.0297  -0.0111 0.1130  409  ALA D CA  
12020 C  C   . ALA D 409 ? 0.7614 0.5303 0.7703 0.0291  -0.0041 0.1131  409  ALA D C   
12021 O  O   . ALA D 409 ? 0.6652 0.4262 0.6674 0.0226  0.0021  0.1070  409  ALA D O   
12022 C  CB  . ALA D 409 ? 0.5259 0.3248 0.5403 0.0326  -0.0098 0.1043  409  ALA D CB  
12023 N  N   . LEU D 410 ? 0.7732 0.5330 0.7932 0.0363  -0.0062 0.1197  410  LEU D N   
12024 C  CA  . LEU D 410 ? 0.5175 0.2569 0.5429 0.0375  -0.0013 0.1197  410  LEU D CA  
12025 C  C   . LEU D 410 ? 0.4285 0.1642 0.4605 0.0379  0.0072  0.1075  410  LEU D C   
12026 O  O   . LEU D 410 ? 0.4324 0.1771 0.4756 0.0433  0.0085  0.1023  410  LEU D O   
12027 C  CB  . LEU D 410 ? 0.6488 0.3808 0.6871 0.0468  -0.0067 0.1277  410  LEU D CB  
12028 C  CG  . LEU D 410 ? 0.9055 0.6327 0.9349 0.0454  -0.0144 0.1411  410  LEU D CG  
12029 C  CD1 . LEU D 410 ? 1.0302 0.7585 1.0709 0.0552  -0.0230 0.1489  410  LEU D CD1 
12030 C  CD2 . LEU D 410 ? 0.9436 0.6494 0.9667 0.0403  -0.0120 0.1449  410  LEU D CD2 
12031 N  N   . ARG D 411 ? 0.5270 0.2493 0.5513 0.0317  0.0130  0.1031  411  ARG D N   
12032 C  CA  . ARG D 411 ? 0.6438 0.3603 0.6726 0.0321  0.0211  0.0915  411  ARG D CA  
12033 C  C   . ARG D 411 ? 0.5877 0.2942 0.6329 0.0418  0.0230  0.0907  411  ARG D C   
12034 O  O   . ARG D 411 ? 0.5684 0.2628 0.6180 0.0456  0.0189  0.0984  411  ARG D O   
12035 C  CB  . ARG D 411 ? 0.5645 0.2675 0.5814 0.0237  0.0259  0.0872  411  ARG D CB  
12036 C  CG  . ARG D 411 ? 0.5755 0.2689 0.5963 0.0250  0.0338  0.0758  411  ARG D CG  
12037 C  CD  . ARG D 411 ? 0.5402 0.2476 0.5572 0.0222  0.0371  0.0663  411  ARG D CD  
12038 N  NE  . ARG D 411 ? 0.6392 0.3432 0.6414 0.0125  0.0390  0.0610  411  ARG D NE  
12039 C  CZ  . ARG D 411 ? 0.6158 0.3079 0.6137 0.0096  0.0453  0.0515  411  ARG D CZ  
12040 N  NH1 . ARG D 411 ? 0.5657 0.2493 0.5725 0.0157  0.0508  0.0461  411  ARG D NH1 
12041 N  NH2 . ARG D 411 ? 0.6011 0.2901 0.5860 0.0008  0.0459  0.0470  411  ARG D NH2 
12042 N  N   . LEU D 412 ? 0.6624 0.3743 0.7165 0.0456  0.0289  0.0811  412  LEU D N   
12043 C  CA  . LEU D 412 ? 0.6581 0.3637 0.7293 0.0553  0.0319  0.0777  412  LEU D CA  
12044 C  C   . LEU D 412 ? 0.6818 0.3920 0.7560 0.0554  0.0412  0.0649  412  LEU D C   
12045 O  O   . LEU D 412 ? 0.6376 0.3652 0.7133 0.0544  0.0424  0.0616  412  LEU D O   
12046 C  CB  . LEU D 412 ? 0.5759 0.2933 0.6622 0.0639  0.0255  0.0843  412  LEU D CB  
12047 C  CG  . LEU D 412 ? 0.6189 0.3315 0.7253 0.0752  0.0269  0.0816  412  LEU D CG  
12048 C  CD1 . LEU D 412 ? 0.8338 0.5241 0.9412 0.0784  0.0227  0.0873  412  LEU D CD1 
12049 C  CD2 . LEU D 412 ? 0.4076 0.1374 0.5291 0.0823  0.0215  0.0857  412  LEU D CD2 
12050 N  N   . ASP D 413 ? 0.5562 0.2502 0.6300 0.0562  0.0475  0.0577  413  ASP D N   
12051 C  CA  . ASP D 413 ? 0.5726 0.2691 0.6450 0.0549  0.0568  0.0453  413  ASP D CA  
12052 C  C   . ASP D 413 ? 0.7203 0.4162 0.8101 0.0651  0.0622  0.0388  413  ASP D C   
12053 O  O   . ASP D 413 ? 0.7897 0.4787 0.8925 0.0735  0.0585  0.0429  413  ASP D O   
12054 C  CB  . ASP D 413 ? 0.5764 0.2560 0.6332 0.0475  0.0606  0.0397  413  ASP D CB  
12055 C  CG  . ASP D 413 ? 0.6012 0.2845 0.6411 0.0367  0.0571  0.0427  413  ASP D CG  
12056 O  OD1 . ASP D 413 ? 0.6205 0.3199 0.6594 0.0350  0.0518  0.0486  413  ASP D OD1 
12057 O  OD2 . ASP D 413 ? 0.7213 0.3913 0.7492 0.0303  0.0593  0.0386  413  ASP D OD2 
12058 N  N   . PHE D 414 ? 0.6892 0.3921 0.7788 0.0643  0.0710  0.0282  414  PHE D N   
12059 C  CA  . PHE D 414 ? 0.6683 0.3731 0.7737 0.0735  0.0779  0.0201  414  PHE D CA  
12060 C  C   . PHE D 414 ? 0.7314 0.4287 0.8278 0.0708  0.0880  0.0074  414  PHE D C   
12061 O  O   . PHE D 414 ? 0.7533 0.4558 0.8356 0.0621  0.0915  0.0035  414  PHE D O   
12062 C  CB  . PHE D 414 ? 0.6861 0.4150 0.8059 0.0771  0.0787  0.0208  414  PHE D CB  
12063 C  CG  . PHE D 414 ? 0.6368 0.3734 0.7669 0.0811  0.0686  0.0324  414  PHE D CG  
12064 C  CD1 . PHE D 414 ? 0.6207 0.3655 0.7406 0.0741  0.0614  0.0404  414  PHE D CD1 
12065 C  CD2 . PHE D 414 ? 0.7786 0.5140 0.9285 0.0923  0.0655  0.0346  414  PHE D CD2 
12066 C  CE1 . PHE D 414 ? 0.6714 0.4231 0.7996 0.0780  0.0519  0.0508  414  PHE D CE1 
12067 C  CE2 . PHE D 414 ? 0.7526 0.4941 0.9111 0.0961  0.0555  0.0453  414  PHE D CE2 
12068 C  CZ  . PHE D 414 ? 0.7222 0.4717 0.8694 0.0889  0.0488  0.0535  414  PHE D CZ  
12069 N  N   . LYS D 415 ? 0.5691 0.2535 0.6736 0.0787  0.0921  0.0008  415  LYS D N   
12070 C  CA  . LYS D 415 ? 0.6310 0.3104 0.7298 0.0787  0.1023  -0.0124 415  LYS D CA  
12071 C  C   . LYS D 415 ? 0.7302 0.4252 0.8483 0.0882  0.1094  -0.0193 415  LYS D C   
12072 O  O   . LYS D 415 ? 0.7339 0.4302 0.8710 0.0986  0.1061  -0.0170 415  LYS D O   
12073 C  CB  . LYS D 415 ? 0.7560 0.4088 0.8484 0.0805  0.1020  -0.0166 415  LYS D CB  
12074 C  CG  . LYS D 415 ? 0.9611 0.5993 1.0340 0.0697  0.0967  -0.0117 415  LYS D CG  
12075 C  CD  . LYS D 415 ? 1.0871 0.7012 1.1502 0.0692  0.0994  -0.0199 415  LYS D CD  
12076 C  CE  . LYS D 415 ? 1.1848 0.7889 1.2275 0.0568  0.0966  -0.0177 415  LYS D CE  
12077 N  NZ  . LYS D 415 ? 1.2213 0.8031 1.2536 0.0554  0.0996  -0.0271 415  LYS D NZ  
12078 N  N   . LEU D 416 ? 0.6280 0.3353 0.7413 0.0845  0.1189  -0.0277 416  LEU D N   
12079 C  CA  . LEU D 416 ? 0.6146 0.3397 0.7456 0.0923  0.1271  -0.0347 416  LEU D CA  
12080 C  C   . LEU D 416 ? 0.6897 0.4081 0.8142 0.0939  0.1386  -0.0491 416  LEU D C   
12081 O  O   . LEU D 416 ? 0.7236 0.4337 0.8269 0.0849  0.1421  -0.0533 416  LEU D O   
12082 C  CB  . LEU D 416 ? 0.7204 0.4710 0.8538 0.0862  0.1286  -0.0310 416  LEU D CB  
12083 C  CG  . LEU D 416 ? 0.5813 0.3412 0.7174 0.0826  0.1175  -0.0176 416  LEU D CG  
12084 C  CD1 . LEU D 416 ? 0.4973 0.2821 0.6372 0.0775  0.1198  -0.0162 416  LEU D CD1 
12085 C  CD2 . LEU D 416 ? 0.5305 0.2889 0.6861 0.0932  0.1096  -0.0107 416  LEU D CD2 
12086 N  N   . ALA D 417 ? 0.7757 0.4979 0.9183 0.1058  0.1441  -0.0571 417  ALA D N   
12087 C  CA  . ALA D 417 ? 0.6382 0.3568 0.7760 0.1088  0.1558  -0.0718 417  ALA D CA  
12088 C  C   . ALA D 417 ? 0.6385 0.3833 0.7790 0.1053  0.1669  -0.0770 417  ALA D C   
12089 O  O   . ALA D 417 ? 0.7225 0.4894 0.8792 0.1063  0.1659  -0.0713 417  ALA D O   
12090 C  CB  . ALA D 417 ? 0.5144 0.2246 0.6704 0.1238  0.1562  -0.0791 417  ALA D CB  
12091 N  N   . PRO D 418 ? 0.9380 0.6799 1.0621 0.1007  0.1772  -0.0876 418  PRO D N   
12092 C  CA  . PRO D 418 ? 0.7711 0.5372 0.8949 0.0954  0.1878  -0.0916 418  PRO D CA  
12093 C  C   . PRO D 418 ? 0.6451 0.4277 0.7930 0.1080  0.1967  -0.1006 418  PRO D C   
12094 O  O   . PRO D 418 ? 0.6144 0.3841 0.7715 0.1196  0.1960  -0.1071 418  PRO D O   
12095 C  CB  . PRO D 418 ? 0.6390 0.3917 0.7357 0.0874  0.1947  -0.1003 418  PRO D CB  
12096 C  CG  . PRO D 418 ? 0.6578 0.3858 0.7529 0.0965  0.1935  -0.1079 418  PRO D CG  
12097 C  CD  . PRO D 418 ? 0.8105 0.5281 0.9184 0.1019  0.1802  -0.0975 418  PRO D CD  
12098 N  N   . VAL D 419 ? 0.8936 0.7042 1.0521 0.1057  0.2046  -0.1013 419  VAL D N   
12099 C  CA  . VAL D 419 ? 0.9333 0.7627 1.1155 0.1174  0.2144  -0.1112 419  VAL D CA  
12100 C  C   . VAL D 419 ? 0.8993 0.7244 1.0689 0.1190  0.2281  -0.1269 419  VAL D C   
12101 O  O   . VAL D 419 ? 0.7976 0.6144 0.9404 0.1079  0.2323  -0.1290 419  VAL D O   
12102 C  CB  . VAL D 419 ? 0.8223 0.6850 1.0234 0.1147  0.2181  -0.1063 419  VAL D CB  
12103 C  CG1 . VAL D 419 ? 0.6388 0.5108 0.8189 0.0981  0.2227  -0.1027 419  VAL D CG1 
12104 C  CG2 . VAL D 419 ? 0.5005 0.3844 0.7268 0.1267  0.2294  -0.1180 419  VAL D CG2 
12105 N  N   . GLU D 420 ? 0.9090 0.7387 1.0976 0.1335  0.2340  -0.1383 420  GLU D N   
12106 C  CA  . GLU D 420 ? 0.7982 0.6223 0.9768 0.1380  0.2459  -0.1545 420  GLU D CA  
12107 C  C   . GLU D 420 ? 0.7005 0.4889 0.8544 0.1364  0.2398  -0.1569 420  GLU D C   
12108 O  O   . GLU D 420 ? 0.7777 0.5494 0.9366 0.1484  0.2383  -0.1659 420  GLU D O   
12109 C  CB  . GLU D 420 ? 0.8058 0.6509 0.9717 0.1274  0.2606  -0.1593 420  GLU D CB  
12110 C  CG  . GLU D 420 ? 0.8893 0.7352 1.0486 0.1336  0.2749  -0.1772 420  GLU D CG  
12111 C  CD  . GLU D 420 ? 1.0028 0.8222 1.1267 0.1254  0.2760  -0.1816 420  GLU D CD  
12112 O  OE1 . GLU D 420 ? 0.9343 0.7385 1.0523 0.1343  0.2800  -0.1949 420  GLU D OE1 
12113 O  OE2 . GLU D 420 ? 1.0415 0.8551 1.1439 0.1102  0.2720  -0.1722 420  GLU D OE2 
12114 C  C1  . NAG E .   ? 0.6291 0.5706 0.9022 -0.0661 -0.0326 -0.2071 501  NAG A C1  
12115 C  C2  . NAG E .   ? 0.7850 0.7175 1.0794 -0.0806 -0.0272 -0.2254 501  NAG A C2  
12116 C  C3  . NAG E .   ? 0.9132 0.8795 1.2445 -0.0922 -0.0318 -0.2529 501  NAG A C3  
12117 C  C4  . NAG E .   ? 0.8196 0.8242 1.1450 -0.0772 -0.0529 -0.2637 501  NAG A C4  
12118 C  C5  . NAG E .   ? 0.6457 0.6510 0.9495 -0.0633 -0.0542 -0.2409 501  NAG A C5  
12119 C  C6  . NAG E .   ? 0.8529 0.8906 1.1479 -0.0460 -0.0743 -0.2492 501  NAG A C6  
12120 C  C7  . NAG E .   ? 0.7868 0.6809 1.1049 -0.1042 0.0100  -0.2024 501  NAG A C7  
12121 C  C8  . NAG E .   ? 0.8282 0.7506 1.1548 -0.1029 0.0091  -0.1984 501  NAG A C8  
12122 N  N2  . NAG E .   ? 0.8685 0.7670 1.1677 -0.0920 -0.0067 -0.2113 501  NAG A N2  
12123 O  O3  . NAG E .   ? 1.0360 0.9944 1.3816 -0.1026 -0.0309 -0.2733 501  NAG A O3  
12124 O  O4  . NAG E .   ? 0.8289 0.8703 1.1914 -0.0873 -0.0566 -0.2876 501  NAG A O4  
12125 O  O5  . NAG E .   ? 0.4234 0.3959 0.6931 -0.0543 -0.0510 -0.2194 501  NAG A O5  
12126 O  O6  . NAG E .   ? 0.8818 0.9087 1.1458 -0.0324 -0.0858 -0.2479 501  NAG A O6  
12127 O  O7  . NAG E .   ? 0.5184 0.3848 0.8462 -0.1156 0.0270  -0.1967 501  NAG A O7  
12128 ZN ZN  . ZN  F .   ? 0.5234 0.6905 0.4067 0.0764  -0.0069 -0.0210 999  ZN  A ZN  
12129 C  C8  . GEM G .   ? 0.7780 0.8762 0.5115 0.0433  0.0490  0.0771  601  GEM A C8  
12130 S  S7  . GEM G .   ? 0.7807 0.8824 0.5185 0.0442  0.0454  0.0787  601  GEM A S7  
12131 C  C6  . GEM G .   ? 0.7095 0.8072 0.4435 0.0432  0.0361  0.0777  601  GEM A C6  
12132 C  C5  . GEM G .   ? 0.4927 0.5861 0.2209 0.0439  0.0329  0.0723  601  GEM A C5  
12133 N  N3  . GEM G .   ? 0.5150 0.6102 0.2437 0.0460  0.0323  0.0678  601  GEM A N3  
12134 C  C1  . GEM G .   ? 0.6070 0.7000 0.3317 0.0472  0.0306  0.0622  601  GEM A C1  
12135 N  N4  . GEM G .   ? 0.4706 0.5655 0.1966 0.0492  0.0305  0.0586  601  GEM A N4  
12136 N  N2  . GEM G .   ? 0.6745 0.7637 0.3942 0.0467  0.0292  0.0602  601  GEM A N2  
12137 C  C9  . GEM G .   ? 0.8693 0.9702 0.6058 0.0442  0.0570  0.0763  601  GEM A C9  
12138 O  O14 . GEM G .   ? 0.4675 0.5721 0.2089 0.0454  0.0599  0.0777  601  GEM A O14 
12139 O  O15 . GEM G .   ? 0.8828 0.9824 0.6172 0.0439  0.0605  0.0742  601  GEM A O15 
12140 C  C10 . GEM G .   ? 0.6387 0.7349 0.3711 0.0411  0.0487  0.0818  601  GEM A C10 
12141 C  C11 . GEM G .   ? 0.7403 0.8397 0.4778 0.0400  0.0534  0.0876  601  GEM A C11 
12142 O  O12 . GEM G .   ? 0.5505 0.6496 0.2893 0.0384  0.0506  0.0918  601  GEM A O12 
12143 O  O13 . GEM G .   ? 0.4740 0.5761 0.2143 0.0406  0.0601  0.0880  601  GEM A O13 
12144 C  C1  . GOL H .   ? 0.4459 0.5431 0.4156 0.0028  0.0431  -0.0210 801  GOL A C1  
12145 O  O1  . GOL H .   ? 0.4913 0.5883 0.4591 0.0035  0.0430  -0.0228 801  GOL A O1  
12146 C  C2  . GOL H .   ? 0.4197 0.5205 0.3895 0.0010  0.0407  -0.0233 801  GOL A C2  
12147 O  O2  . GOL H .   ? 0.4915 0.5922 0.4647 -0.0028 0.0395  -0.0243 801  GOL A O2  
12148 C  C3  . GOL H .   ? 0.3572 0.4588 0.3277 0.0013  0.0407  -0.0217 801  GOL A C3  
12149 O  O3  . GOL H .   ? 0.4581 0.5635 0.4275 0.0007  0.0388  -0.0240 801  GOL A O3  
12150 C  C1  . GOL I .   ? 0.8186 0.7999 0.8196 0.0150  -0.0478 -0.0281 802  GOL A C1  
12151 O  O1  . GOL I .   ? 0.8639 0.8494 0.8664 0.0112  -0.0430 -0.0261 802  GOL A O1  
12152 C  C2  . GOL I .   ? 0.7397 0.7218 0.7442 0.0175  -0.0516 -0.0304 802  GOL A C2  
12153 O  O2  . GOL I .   ? 0.6941 0.6749 0.7070 0.0191  -0.0555 -0.0328 802  GOL A O2  
12154 C  C3  . GOL I .   ? 0.6735 0.6608 0.6823 0.0150  -0.0488 -0.0296 802  GOL A C3  
12155 O  O3  . GOL I .   ? 0.6826 0.6706 0.6920 0.0175  -0.0518 -0.0314 802  GOL A O3  
12156 C  C1  . GOL J .   ? 0.6873 0.7625 0.6841 -0.0468 0.0408  -0.0239 803  GOL A C1  
12157 O  O1  . GOL J .   ? 0.7140 0.7909 0.7135 -0.0482 0.0428  -0.0257 803  GOL A O1  
12158 C  C2  . GOL J .   ? 0.7310 0.8025 0.7275 -0.0469 0.0407  -0.0226 803  GOL A C2  
12159 O  O2  . GOL J .   ? 0.4893 0.5612 0.4887 -0.0482 0.0420  -0.0238 803  GOL A O2  
12160 C  C3  . GOL J .   ? 0.7538 0.8249 0.7494 -0.0456 0.0386  -0.0216 803  GOL A C3  
12161 O  O3  . GOL J .   ? 0.6016 0.6687 0.5966 -0.0455 0.0383  -0.0201 803  GOL A O3  
12162 C  C1  . NAG K .   ? 0.6360 0.8306 0.8826 0.1661  0.2304  0.0946  501  NAG B C1  
12163 C  C2  . NAG K .   ? 0.7122 0.9075 0.9435 0.1673  0.2489  0.0966  501  NAG B C2  
12164 C  C3  . NAG K .   ? 0.7610 0.9863 1.0170 0.1779  0.2681  0.1031  501  NAG B C3  
12165 C  C4  . NAG K .   ? 0.8817 1.1169 1.1571 0.1945  0.2689  0.1006  501  NAG B C4  
12166 C  C5  . NAG K .   ? 0.6746 0.9087 0.9656 0.1899  0.2478  0.1003  501  NAG B C5  
12167 C  C6  . NAG K .   ? 0.6817 0.9177 0.9843 0.2086  0.2486  0.0974  501  NAG B C6  
12168 C  C7  . NAG K .   ? 0.5638 0.7839 0.8208 0.1386  0.2484  0.1125  501  NAG B C7  
12169 C  C8  . NAG K .   ? 0.3784 0.6237 0.6754 0.1336  0.2378  0.1170  501  NAG B C8  
12170 N  N2  . NAG K .   ? 0.6920 0.8865 0.9200 0.1496  0.2452  0.1020  501  NAG B N2  
12171 O  O3  . NAG K .   ? 0.6933 0.9091 0.9215 0.1853  0.2853  0.1004  501  NAG B O3  
12172 O  O4  . NAG K .   ? 1.0433 1.3151 1.3536 0.2000  0.2832  0.1096  501  NAG B O4  
12173 O  O5  . NAG K .   ? 0.6464 0.8477 0.9059 0.1827  0.2338  0.0928  501  NAG B O5  
12174 O  O6  . NAG K .   ? 0.6240 0.8233 0.8940 0.2135  0.2402  0.0869  501  NAG B O6  
12175 O  O7  . NAG K .   ? 0.4981 0.7213 0.7500 0.1320  0.2589  0.1188  501  NAG B O7  
12176 ZN ZN  . ZN  L .   ? 0.4743 0.4801 0.5210 0.0086  0.0166  -0.0749 999  ZN  B ZN  
12177 C  C8  . GEM M .   ? 0.3151 0.2111 0.3577 -0.0273 0.0850  -0.1497 601  GEM B C8  
12178 S  S7  . GEM M .   ? 0.4802 0.3798 0.5242 -0.0287 0.0854  -0.1489 601  GEM B S7  
12179 C  C6  . GEM M .   ? 0.7420 0.6449 0.7920 -0.0295 0.0888  -0.1452 601  GEM B C6  
12180 C  C5  . GEM M .   ? 0.6127 0.5166 0.6599 -0.0287 0.0911  -0.1422 601  GEM B C5  
12181 N  N3  . GEM M .   ? 0.5375 0.4445 0.5788 -0.0287 0.0920  -0.1408 601  GEM B N3  
12182 C  C1  . GEM M .   ? 0.3076 0.2156 0.3440 -0.0280 0.0933  -0.1390 601  GEM B C1  
12183 N  N4  . GEM M .   ? 0.3056 0.2163 0.3367 -0.0282 0.0939  -0.1378 601  GEM B N4  
12184 N  N2  . GEM M .   ? 0.3096 0.2157 0.3465 -0.0269 0.0940  -0.1385 601  GEM B N2  
12185 C  C9  . GEM M .   ? 0.5408 0.4341 0.5789 -0.0268 0.0820  -0.1530 601  GEM B C9  
12186 O  O14 . GEM M .   ? 0.4274 0.3212 0.4641 -0.0275 0.0804  -0.1543 601  GEM B O14 
12187 O  O15 . GEM M .   ? 0.6255 0.5163 0.6618 -0.0257 0.0812  -0.1544 601  GEM B O15 
12188 C  C10 . GEM M .   ? 0.3171 0.2106 0.3667 -0.0274 0.0850  -0.1501 601  GEM B C10 
12189 C  C11 . GEM M .   ? 0.4607 0.3524 0.5138 -0.0281 0.0825  -0.1531 601  GEM B C11 
12190 O  O12 . GEM M .   ? 0.4324 0.3261 0.4906 -0.0293 0.0832  -0.1522 601  GEM B O12 
12191 O  O13 . GEM M .   ? 0.3358 0.2243 0.3865 -0.0275 0.0799  -0.1563 601  GEM B O13 
12192 C  C1  . NAG N .   ? 0.8356 0.9132 0.8945 0.1598  0.0181  -0.0904 501  NAG C C1  
12193 C  C2  . NAG N .   ? 0.7269 0.8229 0.7844 0.1742  0.0270  -0.1048 501  NAG C C2  
12194 C  C3  . NAG N .   ? 0.8451 0.9618 0.9178 0.1967  0.0298  -0.1058 501  NAG C C3  
12195 C  C4  . NAG N .   ? 0.7661 0.8496 0.8404 0.2057  0.0219  -0.1011 501  NAG C C4  
12196 C  C5  . NAG N .   ? 0.6996 0.7878 0.7811 0.1890  0.0141  -0.0837 501  NAG C C5  
12197 C  C6  . NAG N .   ? 0.6861 0.7551 0.7730 0.1984  0.0059  -0.0753 501  NAG C C6  
12198 C  C7  . NAG N .   ? 1.1858 1.3573 1.2568 0.1583  0.0347  -0.0939 501  NAG C C7  
12199 C  C8  . NAG N .   ? 1.2480 1.4320 1.3363 0.1567  0.0285  -0.0785 501  NAG C C8  
12200 N  N2  . NAG N .   ? 0.8776 1.0065 0.9343 0.1624  0.0323  -0.1040 501  NAG C N2  
12201 O  O3  . NAG N .   ? 0.8519 0.9737 0.9193 0.2135  0.0382  -0.1220 501  NAG C O3  
12202 O  O4  . NAG N .   ? 0.7896 0.8881 0.8768 0.2292  0.0237  -0.1032 501  NAG C O4  
12203 O  O5  . NAG N .   ? 0.9024 0.9665 0.9691 0.1696  0.0121  -0.0833 501  NAG C O5  
12204 O  O6  . NAG N .   ? 0.8422 0.8603 0.9122 0.2004  0.0031  -0.0809 501  NAG C O6  
12205 O  O7  . NAG N .   ? 1.2378 1.4383 1.3068 0.1544  0.0414  -0.0964 501  NAG C O7  
12206 ZN ZN  . ZN  O .   ? 0.5935 0.5256 0.4923 0.0876  -0.0304 0.1171  999  ZN  C ZN  
12207 C  C8  . GEM P .   ? 0.4692 0.3492 0.6290 -0.0464 0.0693  0.1108  601  GEM C C8  
12208 S  S7  . GEM P .   ? 0.5479 0.4222 0.7054 -0.0493 0.0780  0.1108  601  GEM C S7  
12209 C  C6  . GEM P .   ? 0.6054 0.4856 0.7607 -0.0500 0.0860  0.1082  601  GEM C C6  
12210 C  C5  . GEM P .   ? 0.5887 0.4709 0.7370 -0.0527 0.0917  0.0992  601  GEM C C5  
12211 N  N3  . GEM P .   ? 0.6725 0.5619 0.8175 -0.0520 0.0883  0.0938  601  GEM C N3  
12212 C  C1  . GEM P .   ? 0.5753 0.4687 0.7145 -0.0535 0.0898  0.0849  601  GEM C C1  
12213 N  N4  . GEM P .   ? 0.5797 0.4795 0.7178 -0.0524 0.0857  0.0808  601  GEM C N4  
12214 N  N2  . GEM P .   ? 0.4678 0.3585 0.6026 -0.0564 0.0953  0.0803  601  GEM C N2  
12215 C  C9  . GEM P .   ? 0.4426 0.3197 0.6044 -0.0458 0.0624  0.1106  601  GEM C C9  
12216 O  O14 . GEM P .   ? 0.5176 0.3882 0.6805 -0.0468 0.0625  0.1141  601  GEM C O14 
12217 O  O15 . GEM P .   ? 0.7318 0.6132 0.8944 -0.0446 0.0565  0.1067  601  GEM C O15 
12218 C  C10 . GEM P .   ? 0.4428 0.3240 0.6081 -0.0443 0.0674  0.1189  601  GEM C C10 
12219 C  C11 . GEM P .   ? 0.5743 0.4489 0.7460 -0.0431 0.0650  0.1275  601  GEM C C11 
12220 O  O12 . GEM P .   ? 0.7313 0.6048 0.9062 -0.0431 0.0690  0.1327  601  GEM C O12 
12221 O  O13 . GEM P .   ? 0.4679 0.3388 0.6419 -0.0422 0.0592  0.1288  601  GEM C O13 
12222 C  C1  . GOL Q .   ? 0.8160 0.8681 0.7443 0.0376  0.0676  -0.0286 804  GOL C C1  
12223 O  O1  . GOL Q .   ? 0.6660 0.7175 0.6009 0.0328  0.0674  -0.0286 804  GOL C O1  
12224 C  C2  . GOL Q .   ? 0.8920 0.9451 0.8135 0.0420  0.0662  -0.0321 804  GOL C C2  
12225 O  O2  . GOL Q .   ? 0.5809 0.6314 0.4947 0.0482  0.0685  -0.0304 804  GOL C O2  
12226 C  C3  . GOL Q .   ? 0.8364 0.8876 0.7597 0.0407  0.0667  -0.0329 804  GOL C C3  
12227 O  O3  . GOL Q .   ? 0.8114 0.8654 0.7310 0.0427  0.0638  -0.0375 804  GOL C O3  
12228 C  C1  . NAG R .   ? 0.8913 1.1197 0.9696 -0.2292 0.0091  0.0763  501  NAG D C1  
12229 C  C2  . NAG R .   ? 1.0308 1.2449 1.1057 -0.2530 0.0187  0.0876  501  NAG D C2  
12230 C  C3  . NAG R .   ? 1.0480 1.3032 1.1413 -0.2770 0.0227  0.0840  501  NAG D C3  
12231 C  C4  . NAG R .   ? 1.2719 1.5427 1.3777 -0.2840 0.0136  0.0679  501  NAG D C4  
12232 C  C5  . NAG R .   ? 1.1658 1.4504 1.2730 -0.2570 0.0036  0.0587  501  NAG D C5  
12233 C  C6  . NAG R .   ? 1.3114 1.6074 1.4267 -0.2642 -0.0064 0.0438  501  NAG D C6  
12234 C  C7  . NAG R .   ? 1.3834 1.6315 1.4533 -0.2373 0.0305  0.1044  501  NAG D C7  
12235 C  C8  . NAG R .   ? 1.3346 1.6351 1.4241 -0.2289 0.0270  0.0919  501  NAG D C8  
12236 N  N2  . NAG R .   ? 1.2682 1.4765 1.3321 -0.2441 0.0257  0.1016  501  NAG D N2  
12237 O  O3  . NAG R .   ? 0.9261 1.1581 1.0140 -0.3015 0.0314  0.0942  501  NAG D O3  
12238 O  O4  . NAG R .   ? 1.3845 1.7038 1.5112 -0.3035 0.0167  0.0640  501  NAG D O4  
12239 O  O5  . NAG R .   ? 0.9469 1.1890 1.0355 -0.2372 0.0017  0.0629  501  NAG D O5  
12240 O  O6  . NAG R .   ? 1.3972 1.6542 1.5043 -0.2855 -0.0056 0.0415  501  NAG D O6  
12241 O  O7  . NAG R .   ? 1.4867 1.7292 1.5457 -0.2366 0.0377  0.1168  501  NAG D O7  
12242 ZN ZN  . ZN  S .   ? 0.4095 0.4566 0.4193 0.0386  -0.0150 -0.0310 999  ZN  D ZN  
12243 C  C8  . GEM T .   ? 0.4638 0.6475 0.4840 -0.0501 0.0039  0.1536  601  GEM D C8  
12244 S  S7  . GEM T .   ? 0.4640 0.6492 0.4874 -0.0491 0.0131  0.1519  601  GEM D S7  
12245 C  C6  . GEM T .   ? 0.4205 0.6095 0.4445 -0.0515 0.0175  0.1566  601  GEM D C6  
12246 C  C5  . GEM T .   ? 0.4104 0.5995 0.4407 -0.0516 0.0224  0.1647  601  GEM D C5  
12247 N  N3  . GEM T .   ? 0.6354 0.8240 0.6664 -0.0533 0.0177  0.1721  601  GEM D N3  
12248 C  C1  . GEM T .   ? 0.5639 0.7514 0.5996 -0.0538 0.0174  0.1807  601  GEM D C1  
12249 N  N4  . GEM T .   ? 0.5226 0.7100 0.5576 -0.0554 0.0123  0.1859  601  GEM D N4  
12250 N  N2  . GEM T .   ? 0.2999 0.4864 0.3409 -0.0526 0.0221  0.1843  601  GEM D N2  
12251 C  C9  . GEM T .   ? 0.2850 0.4651 0.3063 -0.0483 0.0000  0.1527  601  GEM D C9  
12252 O  O14 . GEM T .   ? 0.4630 0.6417 0.4873 -0.0464 0.0033  0.1514  601  GEM D O14 
12253 O  O15 . GEM T .   ? 0.7969 0.9756 0.8160 -0.0488 -0.0065 0.1535  601  GEM D O15 
12254 C  C10 . GEM T .   ? 0.2899 0.4748 0.3037 -0.0509 0.0004  0.1469  601  GEM D C10 
12255 C  C11 . GEM T .   ? 0.4200 0.6042 0.4304 -0.0490 0.0000  0.1369  601  GEM D C11 
12256 O  O12 . GEM T .   ? 0.4544 0.6409 0.4612 -0.0495 0.0017  0.1315  601  GEM D O12 
12257 O  O13 . GEM T .   ? 0.2881 0.4696 0.2992 -0.0471 -0.0022 0.1345  601  GEM D O13 
12258 O  O   . HOH U .   ? 0.4621 0.5603 0.4249 -0.0154 0.0107  -0.0155 1001 HOH A O   
12259 O  O   . HOH U .   ? 0.1832 0.2849 0.1777 -0.0113 0.0327  -0.0110 1002 HOH A O   
12260 O  O   . HOH U .   ? 0.3401 0.4033 0.3249 -0.0160 0.0041  -0.0130 1003 HOH A O   
12261 O  O   . HOH U .   ? 0.5052 0.5579 0.5637 -0.0100 0.0022  -0.0122 1004 HOH A O   
12262 O  O   . HOH U .   ? 0.2576 0.3141 0.3551 -0.0040 0.0101  -0.0096 1005 HOH A O   
12263 O  O   . HOH U .   ? 0.3480 0.3967 0.3545 -0.0132 -0.0030 -0.0138 1006 HOH A O   
12264 O  O   . HOH U .   ? 0.4243 0.4789 0.4261 -0.0409 0.0307  -0.0140 1007 HOH A O   
12265 O  O   . HOH U .   ? 0.7442 0.7744 0.7647 -0.0289 0.0126  -0.0093 1008 HOH A O   
12266 O  O   . HOH U .   ? 0.6822 0.6863 0.5902 0.0109  -0.0076 -0.0106 1009 HOH A O   
12267 O  O   . HOH U .   ? 0.4837 0.5352 0.4918 -0.0088 0.0603  -0.0044 1010 HOH A O   
12268 O  O   . HOH U .   ? 0.3464 0.4832 0.3329 -0.0233 0.0248  -0.0417 1011 HOH A O   
12269 O  O   . HOH U .   ? 0.3533 0.4008 0.3963 -0.0085 -0.0074 -0.0157 1012 HOH A O   
12270 O  O   . HOH U .   ? 0.3574 0.4371 0.4686 0.0053  0.0082  -0.0114 1013 HOH A O   
12271 O  O   . HOH U .   ? 0.2297 0.2869 0.2484 -0.0202 0.0111  -0.0101 1014 HOH A O   
12272 O  O   . HOH U .   ? 0.3110 0.3633 0.3136 -0.0440 0.0334  -0.0149 1015 HOH A O   
12273 O  O   . HOH U .   ? 0.4667 0.4760 0.4164 -0.0249 0.0268  -0.0036 1016 HOH A O   
12274 O  O   . HOH U .   ? 0.2045 0.2371 0.2355 0.0039  -0.0298 -0.0249 1017 HOH A O   
12275 O  O   . HOH U .   ? 0.4093 0.4312 0.4096 0.0089  -0.0348 -0.0254 1018 HOH A O   
12276 O  O   . HOH U .   ? 0.4452 0.4729 0.4335 0.0087  -0.0315 -0.0239 1019 HOH A O   
12277 O  O   . HOH U .   ? 0.5610 0.5967 0.5658 0.0081  -0.0321 -0.0254 1020 HOH A O   
12278 O  O   . HOH U .   ? 0.4285 0.4546 0.4083 0.0048  -0.0253 -0.0207 1021 HOH A O   
12279 O  O   . HOH U .   ? 0.3246 0.3797 0.2921 -0.0370 0.0388  -0.0129 1022 HOH A O   
12280 O  O   . HOH U .   ? 0.4209 0.4981 0.4240 -0.0280 0.0322  -0.0140 1023 HOH A O   
12281 O  O   . HOH U .   ? 0.6955 0.7731 0.6977 -0.0356 0.0346  -0.0203 1024 HOH A O   
12282 O  O   . HOH U .   ? 0.4032 0.4774 0.4161 0.0114  0.0611  0.0081  1025 HOH A O   
12283 O  O   . HOH U .   ? 0.7697 0.8505 0.7682 -0.0393 0.0335  -0.0224 1026 HOH A O   
12284 O  O   . HOH U .   ? 0.4983 0.6056 0.4878 -0.0120 0.0314  -0.0138 1027 HOH A O   
12285 O  O   . HOH U .   ? 0.3457 0.4015 0.3505 -0.0068 0.0590  -0.0044 1028 HOH A O   
12286 O  O   . HOH U .   ? 0.4835 0.5882 0.4717 -0.0235 0.0316  -0.0264 1029 HOH A O   
12287 O  O   . HOH U .   ? 0.3791 0.3930 0.3632 0.0087  -0.0325 -0.0230 1030 HOH A O   
12288 O  O   . HOH U .   ? 0.3953 0.4702 0.4078 -0.0215 0.0300  -0.0085 1031 HOH A O   
12289 O  O   . HOH U .   ? 0.2862 0.2915 0.3833 0.0014  -0.0351 -0.0295 1032 HOH A O   
12290 O  O   . HOH U .   ? 0.6360 0.6502 0.7639 0.0046  -0.0345 -0.0322 1033 HOH A O   
12291 O  O   . HOH U .   ? 0.4018 0.4118 0.5135 0.0035  -0.0358 -0.0313 1034 HOH A O   
12292 O  O   . HOH U .   ? 0.3109 0.3401 0.3228 -0.0325 0.0164  -0.0090 1035 HOH A O   
12293 O  O   . HOH U .   ? 0.5781 0.6129 0.5625 -0.0396 0.0311  -0.0098 1036 HOH A O   
12294 O  O   . HOH U .   ? 0.7271 0.7551 0.7079 -0.0412 0.0365  -0.0085 1037 HOH A O   
12295 O  O   . HOH U .   ? 0.6292 0.6374 0.5748 -0.0085 0.0013  -0.0086 1038 HOH A O   
12296 O  O   . HOH U .   ? 0.5961 0.6748 0.6079 -0.0151 0.0367  -0.0063 1039 HOH A O   
12297 O  O   . HOH U .   ? 0.3169 0.3412 0.2532 -0.0253 0.0421  -0.0038 1040 HOH A O   
12298 O  O   . HOH U .   ? 0.4454 0.5296 0.4435 -0.0288 0.0319  -0.0172 1041 HOH A O   
12299 O  O   . HOH U .   ? 0.8062 0.8868 0.7645 0.0362  0.0687  0.0039  1042 HOH A O   
12300 O  O   . HOH U .   ? 0.5047 0.5802 0.4761 0.0331  0.0719  0.0082  1043 HOH A O   
12301 O  O   . HOH U .   ? 0.3324 0.3735 0.3703 -0.0306 0.0317  -0.0059 1044 HOH A O   
12302 O  O   . HOH U .   ? 0.3367 0.3940 0.3703 -0.0203 0.0357  -0.0036 1045 HOH A O   
12303 O  O   . HOH U .   ? 0.2001 0.2371 0.2593 -0.0087 0.0602  0.0080  1046 HOH A O   
12304 O  O   . HOH U .   ? 0.3717 0.4095 0.4223 -0.0106 0.0600  0.0063  1047 HOH A O   
12305 O  O   . HOH U .   ? 0.4674 0.5199 0.4843 0.0279  0.0855  0.0208  1048 HOH A O   
12306 O  O   . HOH U .   ? 0.8130 0.8834 0.7574 -0.0284 0.0495  -0.0129 1049 HOH A O   
12307 O  O   . HOH U .   ? 0.3056 0.3748 0.3668 0.0013  -0.0126 -0.0196 1050 HOH A O   
12308 O  O   . HOH V .   ? 0.3198 0.3927 0.3453 0.0343  0.0827  0.0240  1001 HOH B O   
12309 O  O   . HOH V .   ? 0.1751 0.2712 0.1844 0.0105  0.0503  0.0045  1002 HOH B O   
12310 O  O   . HOH V .   ? 0.4749 0.5203 0.5510 0.0807  0.1490  0.0633  1003 HOH B O   
12311 O  O   . HOH V .   ? 0.4141 0.4799 0.5860 0.0319  0.0857  0.0259  1004 HOH B O   
12312 O  O   . HOH V .   ? 0.3642 0.4810 0.4926 0.0162  0.0215  -0.0055 1005 HOH B O   
12313 O  O   . HOH V .   ? 0.2570 0.3733 0.2811 -0.0002 -0.0007 -0.0153 1006 HOH B O   
12314 O  O   . HOH V .   ? 0.3815 0.5393 0.3435 0.0154  0.0278  -0.0201 1007 HOH B O   
12315 O  O   . HOH V .   ? 0.4521 0.6023 0.4300 0.0082  0.0296  -0.0124 1008 HOH B O   
12316 O  O   . HOH V .   ? 0.3857 0.5058 0.3709 0.0063  0.0379  -0.0069 1009 HOH B O   
12317 O  O   . HOH V .   ? 0.7002 0.8163 0.6826 0.0076  0.0400  -0.0070 1010 HOH B O   
12318 O  O   . HOH V .   ? 0.3398 0.4640 0.2661 0.0818  0.0757  0.0185  1011 HOH B O   
12319 O  O   . HOH V .   ? 0.3779 0.4871 0.3333 0.0828  0.0942  0.0334  1012 HOH B O   
12320 O  O   . HOH V .   ? 0.3855 0.5165 0.4136 0.0605  0.0867  0.0339  1013 HOH B O   
12321 O  O   . HOH V .   ? 0.3484 0.5087 0.3650 0.0362  0.0531  0.0132  1014 HOH B O   
12322 O  O   . HOH V .   ? 0.4557 0.5928 0.4624 0.0186  0.0425  0.0038  1015 HOH B O   
12323 O  O   . HOH V .   ? 0.4483 0.5693 0.4013 0.0432  0.0564  0.0027  1016 HOH B O   
12324 O  O   . HOH V .   ? 0.4103 0.4841 0.4573 0.0639  0.1143  0.0454  1017 HOH B O   
12325 O  O   . HOH V .   ? 0.3488 0.4354 0.3223 0.0557  0.0857  0.0236  1018 HOH B O   
12326 O  O   . HOH V .   ? 0.2443 0.3771 0.1783 0.0426  0.0433  -0.0132 1019 HOH B O   
12327 O  O   . HOH V .   ? 0.4936 0.6091 0.4582 0.0258  0.0492  -0.0036 1020 HOH B O   
12328 O  O   . HOH V .   ? 0.7865 0.8967 0.6906 0.0593  0.0483  -0.0213 1021 HOH B O   
12329 O  O   . HOH V .   ? 0.3873 0.4506 0.3914 0.0791  0.1239  0.0492  1022 HOH B O   
12330 O  O   . HOH V .   ? 0.4372 0.5668 0.4414 -0.0032 0.0026  -0.0155 1023 HOH B O   
12331 O  O   . HOH V .   ? 0.2549 0.3261 0.4856 0.0503  0.1143  0.0380  1024 HOH B O   
12332 O  O   . HOH V .   ? 0.3235 0.4275 0.4004 0.0115  0.0386  0.0051  1025 HOH B O   
12333 O  O   . HOH V .   ? 0.4504 0.5213 0.3587 0.1034  0.1091  0.0345  1026 HOH B O   
12334 O  O   . HOH V .   ? 0.3312 0.4261 0.4121 0.0060  -0.0036 -0.0166 1027 HOH B O   
12335 O  O   . HOH V .   ? 0.1223 0.2562 0.2253 0.0175  0.0295  0.0002  1028 HOH B O   
12336 O  O   . HOH V .   ? 0.3766 0.5102 0.3907 -0.0013 0.0035  -0.0146 1029 HOH B O   
12337 O  O   . HOH V .   ? 0.2988 0.4174 0.2904 -0.0127 0.0230  -0.0129 1030 HOH B O   
12338 O  O   . HOH V .   ? 0.4459 0.6142 0.4270 0.0118  0.0277  -0.0115 1031 HOH B O   
12339 O  O   . HOH V .   ? 0.3919 0.5614 0.3657 0.0497  0.0518  0.0088  1032 HOH B O   
12340 O  O   . HOH V .   ? 0.5601 0.6515 0.6307 0.0037  -0.0034 -0.0160 1033 HOH B O   
12341 O  O   . HOH V .   ? 0.7749 0.8288 0.8021 0.0794  0.1337  0.0548  1034 HOH B O   
12342 O  O   . HOH V .   ? 0.4476 0.6034 0.5332 0.0467  0.0735  0.0271  1035 HOH B O   
12343 O  O   . HOH V .   ? 0.3389 0.4605 0.3458 -0.0059 0.0080  -0.0128 1036 HOH B O   
12344 O  O   . HOH V .   ? 0.7243 0.7743 0.8472 0.0235  0.0842  0.0256  1037 HOH B O   
12345 O  O   . HOH V .   ? 0.3542 0.4800 0.4412 0.0291  0.0582  0.0166  1038 HOH B O   
12346 O  O   . HOH V .   ? 0.7245 0.8215 0.7590 0.0044  0.0407  0.0035  1039 HOH B O   
12347 O  O   . HOH V .   ? 0.1515 0.3374 0.1257 0.0193  0.0263  -0.0143 1040 HOH B O   
12348 O  O   . HOH V .   ? 0.2539 0.4072 0.2164 0.0549  0.0573  0.0106  1041 HOH B O   
12349 O  O   . HOH V .   ? 0.4245 0.5690 0.3242 0.0747  0.0449  -0.0120 1042 HOH B O   
12350 O  O   . HOH V .   ? 0.2086 0.3684 0.2015 0.0065  0.0268  -0.0087 1043 HOH B O   
12351 O  O   . HOH V .   ? 0.2280 0.3893 0.2274 0.0114  0.0300  -0.0047 1044 HOH B O   
12352 O  O   . HOH V .   ? 0.5234 0.6825 0.5244 0.0066  0.0265  -0.0067 1045 HOH B O   
12353 O  O   . HOH V .   ? 0.6489 0.7343 0.7474 0.0046  0.0192  -0.0053 1046 HOH B O   
12354 O  O   . HOH V .   ? 0.3551 0.5071 0.3072 0.0247  0.0315  -0.0192 1047 HOH B O   
12355 O  O   . HOH V .   ? 0.2834 0.4352 0.2428 0.0208  0.0321  -0.0161 1048 HOH B O   
12356 O  O   . HOH V .   ? 0.5517 0.6763 0.5644 -0.0020 0.0019  -0.0149 1049 HOH B O   
12357 O  O   . HOH V .   ? 0.3964 0.4441 0.5663 0.0243  0.0833  0.0236  1050 HOH B O   
12358 O  O   . HOH V .   ? 0.3180 0.4226 0.4462 0.0135  0.0174  -0.0077 1051 HOH B O   
12359 O  O   . HOH V .   ? 0.6054 0.7034 0.5432 0.0866  0.0954  0.0311  1052 HOH B O   
12360 O  O   . HOH V .   ? 0.4229 0.5421 0.3356 0.0471  0.0351  -0.0387 1053 HOH B O   
12361 O  O   . HOH V .   ? 0.4562 0.5877 0.3909 0.0289  0.0229  -0.0562 1054 HOH B O   
12362 O  O   . HOH W .   ? 0.3426 0.2861 0.3459 0.0275  0.1444  0.0192  1001 HOH C O   
12363 O  O   . HOH W .   ? 0.2275 0.2655 0.2806 -0.0562 0.0613  -0.0369 1002 HOH C O   
12364 O  O   . HOH W .   ? 0.5659 0.6016 0.5322 0.0136  0.0753  -0.0200 1003 HOH C O   
12365 O  O   . HOH W .   ? 0.4515 0.4772 0.4243 0.0127  0.0819  -0.0144 1004 HOH C O   
12366 O  O   . HOH W .   ? 0.3474 0.3492 0.3645 0.0124  0.1020  0.0143  1005 HOH C O   
12367 O  O   . HOH W .   ? 0.4159 0.3825 0.4697 -0.0024 0.1177  0.0172  1006 HOH C O   
12368 O  O   . HOH W .   ? 0.3329 0.3689 0.3749 -0.0402 0.0672  -0.0527 1007 HOH C O   
12369 O  O   . HOH W .   ? 0.3159 0.3366 0.3727 -0.0549 0.0665  -0.0251 1008 HOH C O   
12370 O  O   . HOH W .   ? 0.2383 0.2896 0.2221 -0.0028 0.0631  -0.0207 1009 HOH C O   
12371 O  O   . HOH W .   ? 0.1923 0.2617 0.2273 -0.0351 0.0500  -0.0706 1010 HOH C O   
12372 O  O   . HOH W .   ? 0.2740 0.3404 0.3296 -0.0503 0.0532  -0.0663 1011 HOH C O   
12373 O  O   . HOH W .   ? 0.3175 0.3700 0.4103 -0.0780 0.0641  -0.0535 1012 HOH C O   
12374 O  O   . HOH W .   ? 0.5512 0.6460 0.6562 -0.0659 0.0505  -0.0901 1013 HOH C O   
12375 O  O   . HOH W .   ? 0.3075 0.3706 0.3495 -0.0432 0.0534  -0.0617 1014 HOH C O   
12376 O  O   . HOH W .   ? 0.2285 0.2689 0.2432 -0.0178 0.0627  -0.0089 1015 HOH C O   
12377 O  O   . HOH W .   ? 0.6592 0.6558 0.5699 0.0753  0.1204  0.0136  1016 HOH C O   
12378 O  O   . HOH W .   ? 0.5244 0.5683 0.4537 0.0461  0.0812  -0.0079 1017 HOH C O   
12379 O  O   . HOH W .   ? 0.3976 0.5045 0.3960 -0.0130 0.0301  -0.0757 1018 HOH C O   
12380 O  O   . HOH W .   ? 0.5466 0.5506 0.4991 0.0261  0.0914  -0.0341 1019 HOH C O   
12381 O  O   . HOH W .   ? 0.2877 0.2970 0.2678 0.0062  0.0864  -0.0368 1020 HOH C O   
12382 O  O   . HOH W .   ? 0.4196 0.4740 0.3863 0.0222  0.0492  -0.0939 1021 HOH C O   
12383 O  O   . HOH W .   ? 0.3894 0.4375 0.4825 -0.0687 0.0653  -0.0665 1022 HOH C O   
12384 O  O   . HOH W .   ? 0.7934 0.8104 0.6289 0.1110  0.0963  -0.0140 1023 HOH C O   
12385 O  O   . HOH W .   ? 0.5272 0.5058 0.5982 -0.0468 0.0985  -0.0222 1024 HOH C O   
12386 O  O   . HOH W .   ? 0.5043 0.4836 0.5495 -0.0002 0.1100  0.0157  1025 HOH C O   
12387 O  O   . HOH W .   ? 0.3464 0.3686 0.4223 -0.0675 0.0688  -0.0354 1026 HOH C O   
12388 O  O   . HOH W .   ? 0.3828 0.4194 0.4396 -0.0495 0.0671  -0.0548 1027 HOH C O   
12389 O  O   . HOH W .   ? 0.4308 0.4258 0.5145 -0.0650 0.0661  -0.0114 1028 HOH C O   
12390 O  O   . HOH W .   ? 0.7187 0.6998 0.7076 0.0446  0.1310  0.0284  1029 HOH C O   
12391 O  O   . HOH W .   ? 1.2475 1.2581 1.1773 0.0602  0.1093  0.0104  1030 HOH C O   
12392 O  O   . HOH W .   ? 0.3874 0.3825 0.3107 0.0591  0.1128  0.0020  1031 HOH C O   
12393 O  O   . HOH W .   ? 0.5791 0.6672 0.6279 -0.0448 0.0434  -0.0747 1032 HOH C O   
12394 O  O   . HOH W .   ? 0.3782 0.4631 0.4273 -0.0485 0.0453  -0.0682 1033 HOH C O   
12395 O  O   . HOH W .   ? 0.3055 0.3892 0.3063 -0.0200 0.0422  -0.0585 1034 HOH C O   
12396 O  O   . HOH W .   ? 0.2951 0.4037 0.3455 -0.0470 0.0378  -0.0759 1035 HOH C O   
12397 O  O   . HOH W .   ? 0.3487 0.4072 0.3759 -0.0505 0.0464  -0.0284 1036 HOH C O   
12398 O  O   . HOH W .   ? 0.3440 0.4051 0.3706 -0.0372 0.0532  -0.0512 1037 HOH C O   
12399 O  O   . HOH W .   ? 0.6274 0.6335 0.5294 0.0646  0.0995  -0.0151 1038 HOH C O   
12400 O  O   . HOH W .   ? 0.5412 0.6106 0.4146 0.0781  0.0420  -0.0725 1039 HOH C O   
12401 O  O   . HOH W .   ? 0.4767 0.5501 0.3772 0.0636  0.0346  -0.0910 1040 HOH C O   
12402 O  O   . HOH W .   ? 0.5244 0.6131 0.4904 0.0048  0.0403  -0.0554 1041 HOH C O   
12403 O  O   . HOH W .   ? 0.5108 0.4764 0.4940 0.0503  0.1423  0.0310  1042 HOH C O   
12404 O  O   . HOH W .   ? 0.4284 0.4921 0.4591 -0.0278 0.0519  -0.0774 1043 HOH C O   
12405 O  O   . HOH W .   ? 0.7680 0.8726 0.9305 -0.0692 0.0489  -0.1284 1044 HOH C O   
12406 O  O   . HOH W .   ? 0.5124 0.6065 0.6548 -0.0695 0.0522  -0.1134 1045 HOH C O   
12407 O  O   . HOH W .   ? 0.3438 0.3906 0.4456 -0.0758 0.0669  -0.0627 1046 HOH C O   
12408 O  O   . HOH W .   ? 0.3022 0.3073 0.3209 0.0128  0.1004  0.0152  1047 HOH C O   
12409 O  O   . HOH W .   ? 0.9341 1.0390 0.9234 -0.0097 0.0315  -0.0689 1048 HOH C O   
12410 O  O   . HOH W .   ? 0.3524 0.3290 0.4290 -0.0500 0.0999  -0.0243 1049 HOH C O   
12411 O  O   . HOH W .   ? 0.1965 0.2564 0.2196 -0.0442 0.0477  -0.0295 1050 HOH C O   
12412 O  O   . HOH W .   ? 0.5428 0.5256 0.6012 -0.0396 0.0972  -0.0224 1051 HOH C O   
12413 O  O   . HOH X .   ? 0.4473 0.4776 0.4880 -0.0442 0.0523  -0.0123 1001 HOH D O   
12414 O  O   . HOH X .   ? 0.3363 0.3608 0.3368 -0.0504 0.0425  -0.0101 1002 HOH D O   
12415 O  O   . HOH X .   ? 0.6693 0.7127 0.7103 -0.0564 0.0517  -0.0263 1003 HOH D O   
12416 O  O   . HOH X .   ? 0.4507 0.5259 0.5394 -0.0724 0.0582  -0.0640 1004 HOH D O   
12417 O  O   . HOH X .   ? 0.4660 0.5199 0.5274 -0.0689 0.0568  -0.0407 1005 HOH D O   
12418 O  O   . HOH X .   ? 0.4483 0.4400 0.5002 -0.0244 -0.0042 -0.0123 1006 HOH D O   
12419 O  O   . HOH X .   ? 0.5885 0.6004 0.6559 -0.0689 0.0571  -0.0169 1007 HOH D O   
12420 O  O   . HOH X .   ? 0.3288 0.3357 0.4055 -0.0790 0.0615  -0.0182 1008 HOH D O   
12421 O  O   . HOH X .   ? 0.4375 0.4146 0.5241 -0.0533 0.0304  -0.0045 1009 HOH D O   
12422 O  O   . HOH X .   ? 0.3138 0.3051 0.3042 -0.0260 0.0077  -0.0065 1010 HOH D O   
12423 O  O   . HOH X .   ? 0.4168 0.4664 0.4369 -0.0422 0.0378  -0.0140 1011 HOH D O   
12424 O  O   . HOH X .   ? 0.4649 0.4817 0.4394 -0.0436 0.0553  -0.0052 1012 HOH D O   
12425 O  O   . HOH X .   ? 0.3445 0.3752 0.3885 -0.0531 0.0519  -0.0173 1013 HOH D O   
12426 O  O   . HOH X .   ? 0.3709 0.3744 0.4125 -0.0528 0.0337  -0.0071 1014 HOH D O   
12427 O  O   . HOH X .   ? 0.4489 0.4183 0.5651 -0.0605 0.0518  -0.0013 1015 HOH D O   
12428 O  O   . HOH X .   ? 0.2928 0.2645 0.4099 -0.0562 0.0529  -0.0003 1016 HOH D O   
12429 O  O   . HOH X .   ? 0.3587 0.3369 0.4642 -0.0567 0.0542  -0.0013 1017 HOH D O   
12430 O  O   . HOH X .   ? 0.5932 0.5350 0.6588 -0.0722 0.0549  0.0046  1018 HOH D O   
12431 O  O   . HOH X .   ? 0.4866 0.4075 0.4642 -0.0187 0.0096  0.0042  1019 HOH D O   
12432 O  O   . HOH X .   ? 0.6366 0.5861 0.6347 -0.0307 0.0135  -0.0001 1020 HOH D O   
12433 O  O   . HOH X .   ? 0.5173 0.4664 0.5284 -0.0029 -0.0306 -0.0168 1021 HOH D O   
12434 O  O   . HOH X .   ? 0.4536 0.4112 0.5065 -0.0283 -0.0071 -0.0106 1022 HOH D O   
12435 O  O   . HOH X .   ? 0.3767 0.3352 0.4480 -0.0292 -0.0081 -0.0121 1023 HOH D O   
12436 O  O   . HOH X .   ? 0.2765 0.2379 0.3551 -0.0269 -0.0109 -0.0139 1024 HOH D O   
12437 O  O   . HOH X .   ? 0.2189 0.2549 0.2908 -0.0735 0.0613  -0.0349 1025 HOH D O   
12438 O  O   . HOH X .   ? 0.4876 0.5464 0.5015 -0.0332 0.0469  -0.0194 1026 HOH D O   
12439 O  O   . HOH X .   ? 0.3863 0.3858 0.3899 -0.0559 0.0797  -0.0030 1027 HOH D O   
12440 O  O   . HOH X .   ? 0.4874 0.5599 0.5301 -0.0633 0.0541  -0.0400 1028 HOH D O   
12441 O  O   . HOH X .   ? 0.3634 0.4027 0.4103 -0.0623 0.0527  -0.0259 1029 HOH D O   
12442 O  O   . HOH X .   ? 0.4074 0.4351 0.4602 -0.0319 0.0459  -0.0025 1030 HOH D O   
12443 O  O   . HOH X .   ? 0.3162 0.3379 0.3791 -0.0312 0.0472  -0.0007 1031 HOH D O   
12444 O  O   . HOH X .   ? 0.3702 0.4077 0.4047 -0.0363 0.0340  -0.0075 1032 HOH D O   
12445 O  O   . HOH X .   ? 0.4012 0.4228 0.4962 -0.0886 0.0799  -0.0288 1033 HOH D O   
12446 O  O   . HOH X .   ? 0.1792 0.1801 0.2177 -0.0475 0.0269  -0.0065 1034 HOH D O   
12447 O  O   . HOH X .   ? 0.5360 0.5333 0.5585 -0.0467 0.0271  -0.0057 1035 HOH D O   
12448 O  O   . HOH X .   ? 0.5559 0.5861 0.5662 -0.0560 0.0491  -0.0136 1036 HOH D O   
12449 O  O   . HOH X .   ? 0.6071 0.6574 0.6959 -0.0812 0.0787  -0.0406 1037 HOH D O   
12450 O  O   . HOH X .   ? 0.3744 0.3708 0.4118 -0.0694 0.0746  -0.0070 1038 HOH D O   
12451 O  O   . HOH X .   ? 0.5567 0.5781 0.6211 -0.0674 0.0591  -0.0226 1039 HOH D O   
12452 O  O   . HOH X .   ? 0.3825 0.3736 0.4628 -0.0742 0.0554  -0.0102 1040 HOH D O   
12453 O  O   . HOH X .   ? 0.2836 0.2282 0.4110 -0.0550 0.0201  -0.0056 1041 HOH D O   
12454 O  O   . HOH X .   ? 0.4438 0.4028 0.5486 -0.0392 0.0044  -0.0099 1042 HOH D O   
12455 O  O   . HOH X .   ? 0.3478 0.2975 0.3777 -0.0049 -0.0329 -0.0190 1043 HOH D O   
12456 O  O   . HOH X .   ? 0.5551 0.5249 0.5277 -0.0269 0.0187  -0.0003 1044 HOH D O   
12457 O  O   . HOH X .   ? 1.0748 1.0598 1.0641 -0.0336 0.0197  -0.0032 1045 HOH D O   
12458 O  O   . HOH X .   ? 0.3463 0.3219 0.3392 -0.0492 0.0560  0.0031  1046 HOH D O   
12459 O  O   . HOH X .   ? 0.3576 0.3707 0.4883 -0.0997 0.0810  -0.0370 1047 HOH D O   
12460 O  O   . HOH X .   ? 0.3974 0.4198 0.5140 -0.0889 0.0755  -0.0453 1048 HOH D O   
12461 O  O   . HOH X .   ? 0.4068 0.4046 0.5324 -0.0992 0.0792  -0.0266 1049 HOH D O   
12462 O  O   . HOH X .   ? 0.3141 0.3014 0.4252 -0.0971 0.0864  -0.0153 1050 HOH D O   
12463 O  O   . HOH X .   ? 0.3772 0.3524 0.4741 -0.0920 0.0882  -0.0072 1051 HOH D O   
12464 O  O   . HOH X .   ? 0.4562 0.4652 0.4195 -0.0394 0.0598  -0.0018 1052 HOH D O   
12465 O  O   . HOH X .   ? 0.2845 0.2980 0.2444 -0.0376 0.0563  -0.0028 1053 HOH D O   
12466 O  O   . HOH X .   ? 0.6941 0.7012 0.6446 -0.0339 0.0590  -0.0002 1054 HOH D O   
12467 O  O   . HOH X .   ? 0.5427 0.5081 0.6688 -0.0589 0.0553  0.0002  1055 HOH D O   
12468 O  O   . HOH X .   ? 0.5239 0.4896 0.6536 -0.0555 0.0570  0.0014  1056 HOH D 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   MET 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   THR 3   3   ?   ?   ?   A . n 
A 1 4   LEU 4   4   ?   ?   ?   A . n 
A 1 5   GLY 5   5   ?   ?   ?   A . n 
A 1 6   LEU 6   6   ?   ?   ?   A . n 
A 1 7   LEU 7   7   ?   ?   ?   A . n 
A 1 8   PHE 8   8   ?   ?   ?   A . n 
A 1 9   ALA 9   9   ?   ?   ?   A . n 
A 1 10  SER 10  10  ?   ?   ?   A . n 
A 1 11  ILE 11  11  ?   ?   ?   A . n 
A 1 12  GLY 12  12  ?   ?   ?   A . n 
A 1 13  ILE 13  13  ?   ?   ?   A . n 
A 1 14  ALA 14  14  ?   ?   ?   A . n 
A 1 15  VAL 15  15  ?   ?   ?   A . n 
A 1 16  LEU 16  16  ?   ?   ?   A . n 
A 1 17  ALA 17  17  ?   ?   ?   A . n 
A 1 18  MET 18  18  ?   ?   ?   A . n 
A 1 19  GLY 19  19  ?   ?   ?   A . n 
A 1 20  VAL 20  20  ?   ?   ?   A . n 
A 1 21  PRO 21  21  ?   ?   ?   A . n 
A 1 22  HIS 22  22  ?   ?   ?   A . n 
A 1 23  CYS 23  23  ?   ?   ?   A . n 
A 1 24  ARG 24  24  ?   ?   ?   A . n 
A 1 25  GLY 25  25  ?   ?   ?   A . n 
A 1 26  TYR 26  26  ?   ?   ?   A . n 
A 1 27  THR 27  27  ?   ?   ?   A . n 
A 1 28  ILE 28  28  ?   ?   ?   A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  GLU 32  32  32  GLU GLU A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  PHE 34  34  34  PHE PHE A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  GLN 36  36  36  GLN GLN A . n 
A 1 37  GLN 37  37  37  GLN GLN A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  HIS 39  39  39  HIS HIS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  GLN 45  45  45  GLN GLN A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  TYR 57  57  57  TYR TYR A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  GLN 60  60  60  GLN GLN A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  LYS 62  62  62  LYS LYS A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  PHE 65  65  65  PHE PHE A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  SER 69  69  69  SER SER A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ARG 82  82  82  ARG ARG A . n 
A 1 83  ASN 83  83  83  ASN ASN A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  ARG 85  85  85  ARG ARG A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ARG 87  87  87  ARG ARG A . n 
A 1 88  ASN 88  88  88  ASN ASN A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  PRO 92  92  92  PRO PRO A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  LYS 95  95  95  LYS LYS A . n 
A 1 96  TYR 96  96  96  TYR TYR A . n 
A 1 97  ILE 97  97  97  ILE ILE A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 MET 100 100 100 MET MET A . n 
A 1 101 HIS 101 101 101 HIS HIS A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 GLN 109 109 109 GLN GLN A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 MET 114 114 114 MET MET A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 GLN 116 116 116 GLN GLN A . n 
A 1 117 TYR 117 117 117 TYR TYR A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 ASN 121 121 121 ASN ASN A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 ASP 127 127 127 ASP ASP A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLN 130 130 130 GLN GLN A . n 
A 1 131 LEU 131 131 131 LEU LEU A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 TYR 138 138 138 TYR TYR A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 VAL 140 140 140 VAL VAL A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 MET 143 143 143 MET MET A . n 
A 1 144 ASN 144 144 144 ASN ASN A . n 
A 1 145 PRO 145 145 145 PRO PRO A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 TYR 148 148 148 TYR TYR A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 GLN 152 152 152 GLN GLN A . n 
A 1 153 GLU 153 153 153 GLU GLU A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 ASN 155 155 155 ASN ASN A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 GLU 157 157 157 GLU GLU A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 PRO 160 160 160 PRO PRO A . n 
A 1 161 ASN 161 161 161 ASN ASN A . n 
A 1 162 TYR 162 162 162 TYR TYR A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 ARG 165 165 165 ARG ARG A . n 
A 1 166 GLY 166 166 166 GLY GLY A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 ASN 170 170 170 ASN ASN A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 ASP 172 172 172 ASP ASP A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 ASN 174 174 174 ASN ASN A . n 
A 1 175 ARG 175 175 175 ARG ARG A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 PRO 178 178 178 PRO PRO A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 ARG 180 180 180 ARG ARG A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 GLN 183 183 ?   ?   ?   A . n 
A 1 184 SER 184 184 ?   ?   ?   A . n 
A 1 185 HIS 185 185 ?   ?   ?   A . n 
A 1 186 VAL 186 186 ?   ?   ?   A . n 
A 1 187 HIS 187 187 ?   ?   ?   A . n 
A 1 188 GLN 188 188 ?   ?   ?   A . n 
A 1 189 LEU 189 189 ?   ?   ?   A . n 
A 1 190 ARG 190 190 ?   ?   ?   A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 GLN 195 195 195 GLN GLN A . n 
A 1 196 PRO 196 196 196 PRO PRO A . n 
A 1 197 GLU 197 197 197 GLU GLU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 ALA 200 200 200 ALA ALA A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 TRP 204 204 204 TRP TRP A . n 
A 1 205 ILE 205 205 205 ILE ILE A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 SER 207 207 207 SER SER A . n 
A 1 208 LYS 208 208 208 LYS LYS A . n 
A 1 209 PRO 209 209 209 PRO PRO A . n 
A 1 210 PHE 210 210 210 PHE PHE A . n 
A 1 211 VAL 211 211 211 VAL VAL A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 ASN 215 215 215 ASN ASN A . n 
A 1 216 PHE 216 216 216 PHE PHE A . n 
A 1 217 HIS 217 217 217 HIS HIS A . n 
A 1 218 GLY 218 218 218 GLY GLY A . n 
A 1 219 GLY 219 219 219 GLY GLY A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 SER 224 224 224 SER SER A . n 
A 1 225 TYR 225 225 225 TYR TYR A . n 
A 1 226 PRO 226 226 226 PRO PRO A . n 
A 1 227 TYR 227 227 227 TYR TYR A . n 
A 1 228 ASP 228 228 228 ASP ASP A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 ASN 234 234 234 ASN ASN A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 CYS 236 236 236 CYS CYS A . n 
A 1 237 CYS 237 237 237 CYS CYS A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 SER 240 240 240 SER SER A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 THR 242 242 242 THR THR A . n 
A 1 243 PRO 243 243 243 PRO PRO A . n 
A 1 244 ASP 244 244 244 ASP ASP A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 ARG 246 246 246 ARG ARG A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 LYS 249 249 249 LYS LYS A . n 
A 1 250 GLN 250 250 250 GLN GLN A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 ALA 252 252 252 ALA ALA A . n 
A 1 253 HIS 253 253 253 HIS HIS A . n 
A 1 254 THR 254 254 254 THR THR A . n 
A 1 255 TYR 255 255 255 TYR TYR A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 ASP 257 257 257 ASP ASP A . n 
A 1 258 ASN 258 258 258 ASN ASN A . n 
A 1 259 HIS 259 259 259 HIS HIS A . n 
A 1 260 PRO 260 260 260 PRO PRO A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 MET 262 262 262 MET MET A . n 
A 1 263 ARG 263 263 263 ARG ARG A . n 
A 1 264 LYS 264 264 264 LYS LYS A . n 
A 1 265 GLY 265 265 265 GLY GLY A . n 
A 1 266 ASN 266 266 266 ASN ASN A . n 
A 1 267 ASN 267 267 267 ASN ASN A . n 
A 1 268 CYS 268 268 268 CYS CYS A . n 
A 1 269 ASN 269 269 269 ASN ASN A . n 
A 1 270 ASP 270 270 270 ASP ASP A . n 
A 1 271 SER 271 271 271 SER SER A . n 
A 1 272 PHE 272 272 272 PHE PHE A . n 
A 1 273 SER 273 273 273 SER SER A . n 
A 1 274 GLY 274 274 274 GLY GLY A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 ILE 276 276 276 ILE ILE A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 ASN 278 278 278 ASN ASN A . n 
A 1 279 GLY 279 279 279 GLY GLY A . n 
A 1 280 ALA 280 280 280 ALA ALA A . n 
A 1 281 HIS 281 281 281 HIS HIS A . n 
A 1 282 TRP 282 282 282 TRP TRP A . n 
A 1 283 TYR 283 283 283 TYR TYR A . n 
A 1 284 GLU 284 284 284 GLU GLU A . n 
A 1 285 LEU 285 285 285 LEU LEU A . n 
A 1 286 SER 286 286 286 SER SER A . n 
A 1 287 GLY 287 287 287 GLY GLY A . n 
A 1 288 GLY 288 288 288 GLY GLY A . n 
A 1 289 MET 289 289 289 MET MET A . n 
A 1 290 GLN 290 290 290 GLN GLN A . n 
A 1 291 ASP 291 291 291 ASP ASP A . n 
A 1 292 PHE 292 292 292 PHE PHE A . n 
A 1 293 ASN 293 293 293 ASN ASN A . n 
A 1 294 TYR 294 294 294 TYR TYR A . n 
A 1 295 ALA 295 295 295 ALA ALA A . n 
A 1 296 PHE 296 296 296 PHE PHE A . n 
A 1 297 SER 297 297 297 SER SER A . n 
A 1 298 ASN 298 298 298 ASN ASN A . n 
A 1 299 CYS 299 299 299 CYS CYS A . n 
A 1 300 PHE 300 300 300 PHE PHE A . n 
A 1 301 GLU 301 301 301 GLU GLU A . n 
A 1 302 LEU 302 302 302 LEU LEU A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 ILE 304 304 304 ILE ILE A . n 
A 1 305 GLU 305 305 305 GLU GLU A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 SER 307 307 307 SER SER A . n 
A 1 308 CYS 308 308 308 CYS CYS A . n 
A 1 309 CYS 309 309 309 CYS CYS A . n 
A 1 310 LYS 310 310 310 LYS LYS A . n 
A 1 311 TYR 311 311 311 TYR TYR A . n 
A 1 312 PRO 312 312 312 PRO PRO A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 ALA 314 314 314 ALA ALA A . n 
A 1 315 SER 315 315 315 SER SER A . n 
A 1 316 THR 316 316 316 THR THR A . n 
A 1 317 LEU 317 317 317 LEU LEU A . n 
A 1 318 PRO 318 318 318 PRO PRO A . n 
A 1 319 GLN 319 319 319 GLN GLN A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 TRP 321 321 321 TRP TRP A . n 
A 1 322 GLN 322 322 322 GLN GLN A . n 
A 1 323 ARG 323 323 323 ARG ARG A . n 
A 1 324 ASN 324 324 324 ASN ASN A . n 
A 1 325 LYS 325 325 325 LYS LYS A . n 
A 1 326 ALA 326 326 326 ALA ALA A . n 
A 1 327 SER 327 327 327 SER SER A . n 
A 1 328 LEU 328 328 328 LEU LEU A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 GLN 330 330 330 GLN GLN A . n 
A 1 331 LEU 331 331 331 LEU LEU A . n 
A 1 332 LEU 332 332 332 LEU LEU A . n 
A 1 333 ARG 333 333 333 ARG ARG A . n 
A 1 334 GLN 334 334 334 GLN GLN A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 HIS 336 336 336 HIS HIS A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 GLY 338 338 338 GLY GLY A . n 
A 1 339 ILE 339 339 339 ILE ILE A . n 
A 1 340 LYS 340 340 340 LYS LYS A . n 
A 1 341 GLY 341 341 341 GLY GLY A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 VAL 343 343 343 VAL VAL A . n 
A 1 344 THR 344 344 344 THR THR A . n 
A 1 345 ASP 345 345 345 ASP ASP A . n 
A 1 346 ALA 346 346 346 ALA ALA A . n 
A 1 347 SER 347 347 347 SER SER A . n 
A 1 348 GLY 348 348 348 GLY GLY A . n 
A 1 349 PHE 349 349 349 PHE PHE A . n 
A 1 350 PRO 350 350 350 PRO PRO A . n 
A 1 351 ILE 351 351 351 ILE ILE A . n 
A 1 352 ALA 352 352 352 ALA ALA A . n 
A 1 353 ASP 353 353 353 ASP ASP A . n 
A 1 354 ALA 354 354 354 ALA ALA A . n 
A 1 355 ASN 355 355 355 ASN ASN A . n 
A 1 356 VAL 356 356 356 VAL VAL A . n 
A 1 357 TYR 357 357 357 TYR TYR A . n 
A 1 358 VAL 358 358 358 VAL VAL A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 GLY 360 360 360 GLY GLY A . n 
A 1 361 LEU 361 361 361 LEU LEU A . n 
A 1 362 GLU 362 362 362 GLU GLU A . n 
A 1 363 GLU 363 363 363 GLU GLU A . n 
A 1 364 LYS 364 364 364 LYS LYS A . n 
A 1 365 PRO 365 365 365 PRO PRO A . n 
A 1 366 MET 366 366 366 MET MET A . n 
A 1 367 ARG 367 367 367 ARG ARG A . n 
A 1 368 THR 368 368 368 THR THR A . n 
A 1 369 SER 369 369 369 SER SER A . n 
A 1 370 LYS 370 370 370 LYS LYS A . n 
A 1 371 ARG 371 371 371 ARG ARG A . n 
A 1 372 GLY 372 372 372 GLY GLY A . n 
A 1 373 GLU 373 373 373 GLU GLU A . n 
A 1 374 TYR 374 374 374 TYR TYR A . n 
A 1 375 TRP 375 375 375 TRP TRP A . n 
A 1 376 ARG 376 376 376 ARG ARG A . n 
A 1 377 LEU 377 377 377 LEU LEU A . n 
A 1 378 LEU 378 378 378 LEU LEU A . n 
A 1 379 THR 379 379 379 THR THR A . n 
A 1 380 PRO 380 380 380 PRO PRO A . n 
A 1 381 GLY 381 381 381 GLY GLY A . n 
A 1 382 LEU 382 382 382 LEU LEU A . n 
A 1 383 TYR 383 383 383 TYR TYR A . n 
A 1 384 SER 384 384 384 SER SER A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 HIS 386 386 386 HIS HIS A . n 
A 1 387 ALA 387 387 387 ALA ALA A . n 
A 1 388 SER 388 388 388 SER SER A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 PHE 390 390 390 PHE PHE A . n 
A 1 391 GLY 391 391 391 GLY GLY A . n 
A 1 392 TYR 392 392 392 TYR TYR A . n 
A 1 393 GLN 393 393 393 GLN GLN A . n 
A 1 394 THR 394 394 394 THR THR A . n 
A 1 395 SER 395 395 395 SER SER A . n 
A 1 396 ALA 396 396 396 ALA ALA A . n 
A 1 397 PRO 397 397 397 PRO PRO A . n 
A 1 398 GLN 398 398 398 GLN GLN A . n 
A 1 399 GLN 399 399 399 GLN GLN A . n 
A 1 400 VAL 400 400 400 VAL VAL A . n 
A 1 401 ARG 401 401 401 ARG ARG A . n 
A 1 402 VAL 402 402 402 VAL VAL A . n 
A 1 403 THR 403 403 403 THR THR A . n 
A 1 404 ASN 404 404 404 ASN ASN A . n 
A 1 405 ASP 405 405 405 ASP ASP A . n 
A 1 406 ASN 406 406 406 ASN ASN A . n 
A 1 407 GLN 407 407 407 GLN GLN A . n 
A 1 408 GLU 408 408 408 GLU GLU A . n 
A 1 409 ALA 409 409 409 ALA ALA A . n 
A 1 410 LEU 410 410 410 LEU LEU A . n 
A 1 411 ARG 411 411 411 ARG ARG A . n 
A 1 412 LEU 412 412 412 LEU LEU A . n 
A 1 413 ASP 413 413 413 ASP ASP A . n 
A 1 414 PHE 414 414 414 PHE PHE A . n 
A 1 415 LYS 415 415 415 LYS LYS A . n 
A 1 416 LEU 416 416 416 LEU LEU A . n 
A 1 417 ALA 417 417 417 ALA ALA A . n 
A 1 418 PRO 418 418 418 PRO PRO A . n 
A 1 419 VAL 419 419 419 VAL VAL A . n 
A 1 420 GLU 420 420 ?   ?   ?   A . n 
A 1 421 THR 421 421 ?   ?   ?   A . n 
A 1 422 ASN 422 422 ?   ?   ?   A . n 
A 1 423 PHE 423 423 ?   ?   ?   A . n 
A 1 424 ASP 424 424 ?   ?   ?   A . n 
A 1 425 GLY 425 425 ?   ?   ?   A . n 
A 1 426 ILE 426 426 ?   ?   ?   A . n 
A 1 427 SER 427 427 ?   ?   ?   A . n 
A 1 428 SER 428 428 ?   ?   ?   A . n 
A 1 429 PHE 429 429 ?   ?   ?   A . n 
A 1 430 TYR 430 430 ?   ?   ?   A . n 
A 1 431 SER 431 431 ?   ?   ?   A . n 
A 1 432 PRO 432 432 ?   ?   ?   A . n 
A 1 433 TYR 433 433 ?   ?   ?   A . n 
A 1 434 TYR 434 434 ?   ?   ?   A . n 
A 1 435 PHE 435 435 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   THR 3   3   ?   ?   ?   B . n 
B 1 4   LEU 4   4   ?   ?   ?   B . n 
B 1 5   GLY 5   5   ?   ?   ?   B . n 
B 1 6   LEU 6   6   ?   ?   ?   B . n 
B 1 7   LEU 7   7   ?   ?   ?   B . n 
B 1 8   PHE 8   8   ?   ?   ?   B . n 
B 1 9   ALA 9   9   ?   ?   ?   B . n 
B 1 10  SER 10  10  ?   ?   ?   B . n 
B 1 11  ILE 11  11  ?   ?   ?   B . n 
B 1 12  GLY 12  12  ?   ?   ?   B . n 
B 1 13  ILE 13  13  ?   ?   ?   B . n 
B 1 14  ALA 14  14  ?   ?   ?   B . n 
B 1 15  VAL 15  15  ?   ?   ?   B . n 
B 1 16  LEU 16  16  ?   ?   ?   B . n 
B 1 17  ALA 17  17  ?   ?   ?   B . n 
B 1 18  MET 18  18  ?   ?   ?   B . n 
B 1 19  GLY 19  19  ?   ?   ?   B . n 
B 1 20  VAL 20  20  ?   ?   ?   B . n 
B 1 21  PRO 21  21  ?   ?   ?   B . n 
B 1 22  HIS 22  22  ?   ?   ?   B . n 
B 1 23  CYS 23  23  ?   ?   ?   B . n 
B 1 24  ARG 24  24  ?   ?   ?   B . n 
B 1 25  GLY 25  25  ?   ?   ?   B . n 
B 1 26  TYR 26  26  ?   ?   ?   B . n 
B 1 27  THR 27  27  ?   ?   ?   B . n 
B 1 28  ILE 28  28  28  ILE ILE B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  GLU 30  30  30  GLU GLU B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  GLU 32  32  32  GLU GLU B . n 
B 1 33  SER 33  33  33  SER SER B . n 
B 1 34  PHE 34  34  34  PHE PHE B . n 
B 1 35  LEU 35  35  35  LEU LEU B . n 
B 1 36  GLN 36  36  36  GLN GLN B . n 
B 1 37  GLN 37  37  37  GLN GLN B . n 
B 1 38  PRO 38  38  38  PRO PRO B . n 
B 1 39  HIS 39  39  39  HIS HIS B . n 
B 1 40  TYR 40  40  40  TYR TYR B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  SER 42  42  42  SER SER B . n 
B 1 43  GLN 43  43  43  GLN GLN B . n 
B 1 44  GLU 44  44  44  GLU GLU B . n 
B 1 45  GLN 45  45  45  GLN GLN B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  PHE 50  50  50  PHE PHE B . n 
B 1 51  ALA 51  51  51  ALA ALA B . n 
B 1 52  GLY 52  52  52  GLY GLY B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  GLU 54  54  54  GLU GLU B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  TYR 57  57  57  TYR TYR B . n 
B 1 58  PRO 58  58  58  PRO PRO B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  GLN 60  60  60  GLN GLN B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  LYS 62  62  62  LYS LYS B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  PHE 65  65  65  PHE PHE B . n 
B 1 66  LEU 66  66  66  LEU LEU B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  ARG 68  68  68  ARG ARG B . n 
B 1 69  SER 69  69  69  SER SER B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  GLU 71  71  71  GLU GLU B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  ARG 73  73  73  ARG ARG B . n 
B 1 74  ASN 74  74  74  ASN ASN B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  ALA 77  77  77  ALA ALA B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  GLN 79  79  79  GLN GLN B . n 
B 1 80  ILE 80  80  80  ILE ILE B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  ARG 82  82  82  ARG ARG B . n 
B 1 83  ASN 83  83  83  ASN ASN B . n 
B 1 84  THR 84  84  84  THR THR B . n 
B 1 85  ARG 85  85  85  ARG ARG B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  ARG 87  87  87  ARG ARG B . n 
B 1 88  ASN 88  88  88  ASN ASN B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  THR 91  91  91  THR THR B . n 
B 1 92  PRO 92  92  92  PRO PRO B . n 
B 1 93  PRO 93  93  93  PRO PRO B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  LYS 95  95  95  LYS LYS B . n 
B 1 96  TYR 96  96  96  TYR TYR B . n 
B 1 97  ILE 97  97  97  ILE ILE B . n 
B 1 98  ALA 98  98  98  ALA ALA B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 MET 100 100 100 MET MET B . n 
B 1 101 HIS 101 101 101 HIS HIS B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 THR 105 105 105 THR THR B . n 
B 1 106 VAL 106 106 106 VAL VAL B . n 
B 1 107 GLY 107 107 107 GLY GLY B . n 
B 1 108 ARG 108 108 108 ARG ARG B . n 
B 1 109 GLN 109 109 109 GLN GLN B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 MET 114 114 114 MET MET B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 GLN 116 116 116 GLN GLN B . n 
B 1 117 TYR 117 117 117 TYR TYR B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 ASN 121 121 121 ASN ASN B . n 
B 1 122 HIS 122 122 122 HIS HIS B . n 
B 1 123 GLU 123 123 123 GLU GLU B . n 
B 1 124 ARG 124 124 124 ARG ARG B . n 
B 1 125 ILE 125 125 125 ILE ILE B . n 
B 1 126 SER 126 126 126 SER SER B . n 
B 1 127 ASP 127 127 127 ASP ASP B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 GLY 129 129 129 GLY GLY B . n 
B 1 130 GLN 130 130 130 GLN GLN B . n 
B 1 131 LEU 131 131 131 LEU LEU B . n 
B 1 132 VAL 132 132 132 VAL VAL B . n 
B 1 133 ASN 133 133 133 ASN ASN B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 ASP 136 136 136 ASP ASP B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 TYR 138 138 138 TYR TYR B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 VAL 140 140 140 VAL VAL B . n 
B 1 141 PRO 141 141 141 PRO PRO B . n 
B 1 142 THR 142 142 142 THR THR B . n 
B 1 143 MET 143 143 143 MET MET B . n 
B 1 144 ASN 144 144 144 ASN ASN B . n 
B 1 145 PRO 145 145 145 PRO PRO B . n 
B 1 146 ASP 146 146 146 ASP ASP B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 TYR 148 148 148 TYR TYR B . n 
B 1 149 ALA 149 149 149 ALA ALA B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 SER 151 151 151 SER SER B . n 
B 1 152 GLN 152 152 152 GLN GLN B . n 
B 1 153 GLU 153 153 153 GLU GLU B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 ASN 155 155 155 ASN ASN B . n 
B 1 156 CYS 156 156 156 CYS CYS B . n 
B 1 157 GLU 157 157 157 GLU GLU B . n 
B 1 158 SER 158 158 158 SER SER B . n 
B 1 159 LEU 159 159 159 LEU LEU B . n 
B 1 160 PRO 160 160 160 PRO PRO B . n 
B 1 161 ASN 161 161 161 ASN ASN B . n 
B 1 162 TYR 162 162 162 TYR TYR B . n 
B 1 163 VAL 163 163 163 VAL VAL B . n 
B 1 164 GLY 164 164 164 GLY GLY B . n 
B 1 165 ARG 165 165 165 ARG ARG B . n 
B 1 166 GLY 166 166 166 GLY GLY B . n 
B 1 167 ASN 167 167 167 ASN ASN B . n 
B 1 168 ALA 168 168 168 ALA ALA B . n 
B 1 169 ALA 169 169 169 ALA ALA B . n 
B 1 170 ASN 170 170 170 ASN ASN B . n 
B 1 171 ILE 171 171 171 ILE ILE B . n 
B 1 172 ASP 172 172 172 ASP ASP B . n 
B 1 173 LEU 173 173 173 LEU LEU B . n 
B 1 174 ASN 174 174 174 ASN ASN B . n 
B 1 175 ARG 175 175 175 ARG ARG B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 PHE 177 177 177 PHE PHE B . n 
B 1 178 PRO 178 178 178 PRO PRO B . n 
B 1 179 ASP 179 179 179 ASP ASP B . n 
B 1 180 ARG 180 180 180 ARG ARG B . n 
B 1 181 LEU 181 181 181 LEU LEU B . n 
B 1 182 GLU 182 182 182 GLU GLU B . n 
B 1 183 GLN 183 183 183 GLN GLN B . n 
B 1 184 SER 184 184 184 SER SER B . n 
B 1 185 HIS 185 185 ?   ?   ?   B . n 
B 1 186 VAL 186 186 ?   ?   ?   B . n 
B 1 187 HIS 187 187 ?   ?   ?   B . n 
B 1 188 GLN 188 188 ?   ?   ?   B . n 
B 1 189 LEU 189 189 ?   ?   ?   B . n 
B 1 190 ARG 190 190 ?   ?   ?   B . n 
B 1 191 ALA 191 191 ?   ?   ?   B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 SER 193 193 193 SER SER B . n 
B 1 194 ARG 194 194 194 ARG ARG B . n 
B 1 195 GLN 195 195 195 GLN GLN B . n 
B 1 196 PRO 196 196 196 PRO PRO B . n 
B 1 197 GLU 197 197 197 GLU GLU B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 ALA 199 199 199 ALA ALA B . n 
B 1 200 ALA 200 200 200 ALA ALA B . n 
B 1 201 LEU 201 201 201 LEU LEU B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 TRP 204 204 204 TRP TRP B . n 
B 1 205 ILE 205 205 205 ILE ILE B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 SER 207 207 207 SER SER B . n 
B 1 208 LYS 208 208 208 LYS LYS B . n 
B 1 209 PRO 209 209 209 PRO PRO B . n 
B 1 210 PHE 210 210 210 PHE PHE B . n 
B 1 211 VAL 211 211 211 VAL VAL B . n 
B 1 212 LEU 212 212 212 LEU LEU B . n 
B 1 213 SER 213 213 213 SER SER B . n 
B 1 214 ALA 214 214 214 ALA ALA B . n 
B 1 215 ASN 215 215 215 ASN ASN B . n 
B 1 216 PHE 216 216 216 PHE PHE B . n 
B 1 217 HIS 217 217 217 HIS HIS B . n 
B 1 218 GLY 218 218 218 GLY GLY B . n 
B 1 219 GLY 219 219 219 GLY GLY B . n 
B 1 220 ALA 220 220 220 ALA ALA B . n 
B 1 221 VAL 221 221 221 VAL VAL B . n 
B 1 222 VAL 222 222 222 VAL VAL B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 SER 224 224 224 SER SER B . n 
B 1 225 TYR 225 225 225 TYR TYR B . n 
B 1 226 PRO 226 226 226 PRO PRO B . n 
B 1 227 TYR 227 227 227 TYR TYR B . n 
B 1 228 ASP 228 228 228 ASP ASP B . n 
B 1 229 ASN 229 229 229 ASN ASN B . n 
B 1 230 SER 230 230 230 SER SER B . n 
B 1 231 LEU 231 231 231 LEU LEU B . n 
B 1 232 ALA 232 232 232 ALA ALA B . n 
B 1 233 HIS 233 233 233 HIS HIS B . n 
B 1 234 ASN 234 234 234 ASN ASN B . n 
B 1 235 GLU 235 235 235 GLU GLU B . n 
B 1 236 CYS 236 236 236 CYS CYS B . n 
B 1 237 CYS 237 237 237 CYS CYS B . n 
B 1 238 GLU 238 238 238 GLU GLU B . n 
B 1 239 GLU 239 239 239 GLU GLU B . n 
B 1 240 SER 240 240 240 SER SER B . n 
B 1 241 LEU 241 241 241 LEU LEU B . n 
B 1 242 THR 242 242 242 THR THR B . n 
B 1 243 PRO 243 243 243 PRO PRO B . n 
B 1 244 ASP 244 244 244 ASP ASP B . n 
B 1 245 ASP 245 245 245 ASP ASP B . n 
B 1 246 ARG 246 246 246 ARG ARG B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 PHE 248 248 248 PHE PHE B . n 
B 1 249 LYS 249 249 249 LYS LYS B . n 
B 1 250 GLN 250 250 250 GLN GLN B . n 
B 1 251 LEU 251 251 251 LEU LEU B . n 
B 1 252 ALA 252 252 252 ALA ALA B . n 
B 1 253 HIS 253 253 253 HIS HIS B . n 
B 1 254 THR 254 254 254 THR THR B . n 
B 1 255 TYR 255 255 255 TYR TYR B . n 
B 1 256 SER 256 256 256 SER SER B . n 
B 1 257 ASP 257 257 257 ASP ASP B . n 
B 1 258 ASN 258 258 258 ASN ASN B . n 
B 1 259 HIS 259 259 259 HIS HIS B . n 
B 1 260 PRO 260 260 260 PRO PRO B . n 
B 1 261 ILE 261 261 261 ILE ILE B . n 
B 1 262 MET 262 262 262 MET MET B . n 
B 1 263 ARG 263 263 263 ARG ARG B . n 
B 1 264 LYS 264 264 264 LYS LYS B . n 
B 1 265 GLY 265 265 265 GLY GLY B . n 
B 1 266 ASN 266 266 266 ASN ASN B . n 
B 1 267 ASN 267 267 267 ASN ASN B . n 
B 1 268 CYS 268 268 268 CYS CYS B . n 
B 1 269 ASN 269 269 269 ASN ASN B . n 
B 1 270 ASP 270 270 270 ASP ASP B . n 
B 1 271 SER 271 271 271 SER SER B . n 
B 1 272 PHE 272 272 272 PHE PHE B . n 
B 1 273 SER 273 273 273 SER SER B . n 
B 1 274 GLY 274 274 274 GLY GLY B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 ILE 276 276 276 ILE ILE B . n 
B 1 277 THR 277 277 277 THR THR B . n 
B 1 278 ASN 278 278 278 ASN ASN B . n 
B 1 279 GLY 279 279 279 GLY GLY B . n 
B 1 280 ALA 280 280 280 ALA ALA B . n 
B 1 281 HIS 281 281 281 HIS HIS B . n 
B 1 282 TRP 282 282 282 TRP TRP B . n 
B 1 283 TYR 283 283 283 TYR TYR B . n 
B 1 284 GLU 284 284 284 GLU GLU B . n 
B 1 285 LEU 285 285 285 LEU LEU B . n 
B 1 286 SER 286 286 286 SER SER B . n 
B 1 287 GLY 287 287 287 GLY GLY B . n 
B 1 288 GLY 288 288 288 GLY GLY B . n 
B 1 289 MET 289 289 289 MET MET B . n 
B 1 290 GLN 290 290 290 GLN GLN B . n 
B 1 291 ASP 291 291 291 ASP ASP B . n 
B 1 292 PHE 292 292 292 PHE PHE B . n 
B 1 293 ASN 293 293 293 ASN ASN B . n 
B 1 294 TYR 294 294 294 TYR TYR B . n 
B 1 295 ALA 295 295 295 ALA ALA B . n 
B 1 296 PHE 296 296 296 PHE PHE B . n 
B 1 297 SER 297 297 297 SER SER B . n 
B 1 298 ASN 298 298 298 ASN ASN B . n 
B 1 299 CYS 299 299 299 CYS CYS B . n 
B 1 300 PHE 300 300 300 PHE PHE B . n 
B 1 301 GLU 301 301 301 GLU GLU B . n 
B 1 302 LEU 302 302 302 LEU LEU B . n 
B 1 303 THR 303 303 303 THR THR B . n 
B 1 304 ILE 304 304 304 ILE ILE B . n 
B 1 305 GLU 305 305 305 GLU GLU B . n 
B 1 306 LEU 306 306 306 LEU LEU B . n 
B 1 307 SER 307 307 307 SER SER B . n 
B 1 308 CYS 308 308 308 CYS CYS B . n 
B 1 309 CYS 309 309 309 CYS CYS B . n 
B 1 310 LYS 310 310 310 LYS LYS B . n 
B 1 311 TYR 311 311 311 TYR TYR B . n 
B 1 312 PRO 312 312 312 PRO PRO B . n 
B 1 313 ALA 313 313 313 ALA ALA B . n 
B 1 314 ALA 314 314 314 ALA ALA B . n 
B 1 315 SER 315 315 315 SER SER B . n 
B 1 316 THR 316 316 316 THR THR B . n 
B 1 317 LEU 317 317 317 LEU LEU B . n 
B 1 318 PRO 318 318 318 PRO PRO B . n 
B 1 319 GLN 319 319 319 GLN GLN B . n 
B 1 320 GLU 320 320 320 GLU GLU B . n 
B 1 321 TRP 321 321 321 TRP TRP B . n 
B 1 322 GLN 322 322 322 GLN GLN B . n 
B 1 323 ARG 323 323 323 ARG ARG B . n 
B 1 324 ASN 324 324 324 ASN ASN B . n 
B 1 325 LYS 325 325 325 LYS LYS B . n 
B 1 326 ALA 326 326 326 ALA ALA B . n 
B 1 327 SER 327 327 327 SER SER B . n 
B 1 328 LEU 328 328 328 LEU LEU B . n 
B 1 329 LEU 329 329 329 LEU LEU B . n 
B 1 330 GLN 330 330 330 GLN GLN B . n 
B 1 331 LEU 331 331 331 LEU LEU B . n 
B 1 332 LEU 332 332 332 LEU LEU B . n 
B 1 333 ARG 333 333 333 ARG ARG B . n 
B 1 334 GLN 334 334 334 GLN GLN B . n 
B 1 335 ALA 335 335 335 ALA ALA B . n 
B 1 336 HIS 336 336 336 HIS HIS B . n 
B 1 337 ILE 337 337 337 ILE ILE B . n 
B 1 338 GLY 338 338 338 GLY GLY B . n 
B 1 339 ILE 339 339 339 ILE ILE B . n 
B 1 340 LYS 340 340 340 LYS LYS B . n 
B 1 341 GLY 341 341 341 GLY GLY B . n 
B 1 342 LEU 342 342 342 LEU LEU B . n 
B 1 343 VAL 343 343 343 VAL VAL B . n 
B 1 344 THR 344 344 344 THR THR B . n 
B 1 345 ASP 345 345 345 ASP ASP B . n 
B 1 346 ALA 346 346 346 ALA ALA B . n 
B 1 347 SER 347 347 347 SER SER B . n 
B 1 348 GLY 348 348 348 GLY GLY B . n 
B 1 349 PHE 349 349 349 PHE PHE B . n 
B 1 350 PRO 350 350 350 PRO PRO B . n 
B 1 351 ILE 351 351 351 ILE ILE B . n 
B 1 352 ALA 352 352 352 ALA ALA B . n 
B 1 353 ASP 353 353 353 ASP ASP B . n 
B 1 354 ALA 354 354 354 ALA ALA B . n 
B 1 355 ASN 355 355 355 ASN ASN B . n 
B 1 356 VAL 356 356 356 VAL VAL B . n 
B 1 357 TYR 357 357 357 TYR TYR B . n 
B 1 358 VAL 358 358 358 VAL VAL B . n 
B 1 359 ALA 359 359 359 ALA ALA B . n 
B 1 360 GLY 360 360 360 GLY GLY B . n 
B 1 361 LEU 361 361 361 LEU LEU B . n 
B 1 362 GLU 362 362 362 GLU GLU B . n 
B 1 363 GLU 363 363 363 GLU GLU B . n 
B 1 364 LYS 364 364 364 LYS LYS B . n 
B 1 365 PRO 365 365 365 PRO PRO B . n 
B 1 366 MET 366 366 366 MET MET B . n 
B 1 367 ARG 367 367 367 ARG ARG B . n 
B 1 368 THR 368 368 368 THR THR B . n 
B 1 369 SER 369 369 369 SER SER B . n 
B 1 370 LYS 370 370 370 LYS LYS B . n 
B 1 371 ARG 371 371 371 ARG ARG B . n 
B 1 372 GLY 372 372 372 GLY GLY B . n 
B 1 373 GLU 373 373 373 GLU GLU B . n 
B 1 374 TYR 374 374 374 TYR TYR B . n 
B 1 375 TRP 375 375 375 TRP TRP B . n 
B 1 376 ARG 376 376 376 ARG ARG B . n 
B 1 377 LEU 377 377 377 LEU LEU B . n 
B 1 378 LEU 378 378 378 LEU LEU B . n 
B 1 379 THR 379 379 379 THR THR B . n 
B 1 380 PRO 380 380 380 PRO PRO B . n 
B 1 381 GLY 381 381 381 GLY GLY B . n 
B 1 382 LEU 382 382 382 LEU LEU B . n 
B 1 383 TYR 383 383 383 TYR TYR B . n 
B 1 384 SER 384 384 384 SER SER B . n 
B 1 385 VAL 385 385 385 VAL VAL B . n 
B 1 386 HIS 386 386 386 HIS HIS B . n 
B 1 387 ALA 387 387 387 ALA ALA B . n 
B 1 388 SER 388 388 388 SER SER B . n 
B 1 389 ALA 389 389 389 ALA ALA B . n 
B 1 390 PHE 390 390 390 PHE PHE B . n 
B 1 391 GLY 391 391 391 GLY GLY B . n 
B 1 392 TYR 392 392 392 TYR TYR B . n 
B 1 393 GLN 393 393 393 GLN GLN B . n 
B 1 394 THR 394 394 394 THR THR B . n 
B 1 395 SER 395 395 395 SER SER B . n 
B 1 396 ALA 396 396 396 ALA ALA B . n 
B 1 397 PRO 397 397 397 PRO PRO B . n 
B 1 398 GLN 398 398 398 GLN GLN B . n 
B 1 399 GLN 399 399 399 GLN GLN B . n 
B 1 400 VAL 400 400 400 VAL VAL B . n 
B 1 401 ARG 401 401 401 ARG ARG B . n 
B 1 402 VAL 402 402 402 VAL VAL B . n 
B 1 403 THR 403 403 403 THR THR B . n 
B 1 404 ASN 404 404 404 ASN ASN B . n 
B 1 405 ASP 405 405 405 ASP ASP B . n 
B 1 406 ASN 406 406 406 ASN ASN B . n 
B 1 407 GLN 407 407 407 GLN GLN B . n 
B 1 408 GLU 408 408 408 GLU GLU B . n 
B 1 409 ALA 409 409 409 ALA ALA B . n 
B 1 410 LEU 410 410 410 LEU LEU B . n 
B 1 411 ARG 411 411 411 ARG ARG B . n 
B 1 412 LEU 412 412 412 LEU LEU B . n 
B 1 413 ASP 413 413 413 ASP ASP B . n 
B 1 414 PHE 414 414 414 PHE PHE B . n 
B 1 415 LYS 415 415 415 LYS LYS B . n 
B 1 416 LEU 416 416 416 LEU LEU B . n 
B 1 417 ALA 417 417 417 ALA ALA B . n 
B 1 418 PRO 418 418 418 PRO PRO B . n 
B 1 419 VAL 419 419 419 VAL VAL B . n 
B 1 420 GLU 420 420 420 GLU GLU B . n 
B 1 421 THR 421 421 ?   ?   ?   B . n 
B 1 422 ASN 422 422 ?   ?   ?   B . n 
B 1 423 PHE 423 423 ?   ?   ?   B . n 
B 1 424 ASP 424 424 ?   ?   ?   B . n 
B 1 425 GLY 425 425 ?   ?   ?   B . n 
B 1 426 ILE 426 426 ?   ?   ?   B . n 
B 1 427 SER 427 427 ?   ?   ?   B . n 
B 1 428 SER 428 428 ?   ?   ?   B . n 
B 1 429 PHE 429 429 ?   ?   ?   B . n 
B 1 430 TYR 430 430 ?   ?   ?   B . n 
B 1 431 SER 431 431 ?   ?   ?   B . n 
B 1 432 PRO 432 432 ?   ?   ?   B . n 
B 1 433 TYR 433 433 ?   ?   ?   B . n 
B 1 434 TYR 434 434 ?   ?   ?   B . n 
B 1 435 PHE 435 435 ?   ?   ?   B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   PRO 2   2   ?   ?   ?   C . n 
C 1 3   THR 3   3   ?   ?   ?   C . n 
C 1 4   LEU 4   4   ?   ?   ?   C . n 
C 1 5   GLY 5   5   ?   ?   ?   C . n 
C 1 6   LEU 6   6   ?   ?   ?   C . n 
C 1 7   LEU 7   7   ?   ?   ?   C . n 
C 1 8   PHE 8   8   ?   ?   ?   C . n 
C 1 9   ALA 9   9   ?   ?   ?   C . n 
C 1 10  SER 10  10  ?   ?   ?   C . n 
C 1 11  ILE 11  11  ?   ?   ?   C . n 
C 1 12  GLY 12  12  ?   ?   ?   C . n 
C 1 13  ILE 13  13  ?   ?   ?   C . n 
C 1 14  ALA 14  14  ?   ?   ?   C . n 
C 1 15  VAL 15  15  ?   ?   ?   C . n 
C 1 16  LEU 16  16  ?   ?   ?   C . n 
C 1 17  ALA 17  17  ?   ?   ?   C . n 
C 1 18  MET 18  18  ?   ?   ?   C . n 
C 1 19  GLY 19  19  ?   ?   ?   C . n 
C 1 20  VAL 20  20  ?   ?   ?   C . n 
C 1 21  PRO 21  21  ?   ?   ?   C . n 
C 1 22  HIS 22  22  ?   ?   ?   C . n 
C 1 23  CYS 23  23  ?   ?   ?   C . n 
C 1 24  ARG 24  24  ?   ?   ?   C . n 
C 1 25  GLY 25  25  ?   ?   ?   C . n 
C 1 26  TYR 26  26  ?   ?   ?   C . n 
C 1 27  THR 27  27  ?   ?   ?   C . n 
C 1 28  ILE 28  28  ?   ?   ?   C . n 
C 1 29  LYS 29  29  ?   ?   ?   C . n 
C 1 30  GLU 30  30  30  GLU GLU C . n 
C 1 31  ASP 31  31  31  ASP ASP C . n 
C 1 32  GLU 32  32  32  GLU GLU C . n 
C 1 33  SER 33  33  33  SER SER C . n 
C 1 34  PHE 34  34  34  PHE PHE C . n 
C 1 35  LEU 35  35  35  LEU LEU C . n 
C 1 36  GLN 36  36  36  GLN GLN C . n 
C 1 37  GLN 37  37  37  GLN GLN C . n 
C 1 38  PRO 38  38  38  PRO PRO C . n 
C 1 39  HIS 39  39  39  HIS HIS C . n 
C 1 40  TYR 40  40  40  TYR TYR C . n 
C 1 41  ALA 41  41  41  ALA ALA C . n 
C 1 42  SER 42  42  42  SER SER C . n 
C 1 43  GLN 43  43  43  GLN GLN C . n 
C 1 44  GLU 44  44  44  GLU GLU C . n 
C 1 45  GLN 45  45  45  GLN GLN C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  GLU 47  47  47  GLU GLU C . n 
C 1 48  ASP 48  48  48  ASP ASP C . n 
C 1 49  LEU 49  49  49  LEU LEU C . n 
C 1 50  PHE 50  50  50  PHE PHE C . n 
C 1 51  ALA 51  51  51  ALA ALA C . n 
C 1 52  GLY 52  52  52  GLY GLY C . n 
C 1 53  LEU 53  53  53  LEU LEU C . n 
C 1 54  GLU 54  54  54  GLU GLU C . n 
C 1 55  LYS 55  55  55  LYS LYS C . n 
C 1 56  ALA 56  56  56  ALA ALA C . n 
C 1 57  TYR 57  57  57  TYR TYR C . n 
C 1 58  PRO 58  58  58  PRO PRO C . n 
C 1 59  ASN 59  59  59  ASN ASN C . n 
C 1 60  GLN 60  60  60  GLN GLN C . n 
C 1 61  ALA 61  61  61  ALA ALA C . n 
C 1 62  LYS 62  62  62  LYS LYS C . n 
C 1 63  VAL 63  63  63  VAL VAL C . n 
C 1 64  HIS 64  64  64  HIS HIS C . n 
C 1 65  PHE 65  65  65  PHE PHE C . n 
C 1 66  LEU 66  66  66  LEU LEU C . n 
C 1 67  GLY 67  67  67  GLY GLY C . n 
C 1 68  ARG 68  68  68  ARG ARG C . n 
C 1 69  SER 69  69  69  SER SER C . n 
C 1 70  LEU 70  70  70  LEU LEU C . n 
C 1 71  GLU 71  71  71  GLU GLU C . n 
C 1 72  GLY 72  72  72  GLY GLY C . n 
C 1 73  ARG 73  73  73  ARG ARG C . n 
C 1 74  ASN 74  74  74  ASN ASN C . n 
C 1 75  LEU 75  75  75  LEU LEU C . n 
C 1 76  LEU 76  76  76  LEU LEU C . n 
C 1 77  ALA 77  77  77  ALA ALA C . n 
C 1 78  LEU 78  78  78  LEU LEU C . n 
C 1 79  GLN 79  79  79  GLN GLN C . n 
C 1 80  ILE 80  80  80  ILE ILE C . n 
C 1 81  SER 81  81  81  SER SER C . n 
C 1 82  ARG 82  82  82  ARG ARG C . n 
C 1 83  ASN 83  83  83  ASN ASN C . n 
C 1 84  THR 84  84  84  THR THR C . n 
C 1 85  ARG 85  85  85  ARG ARG C . n 
C 1 86  SER 86  86  86  SER SER C . n 
C 1 87  ARG 87  87  87  ARG ARG C . n 
C 1 88  ASN 88  88  88  ASN ASN C . n 
C 1 89  LEU 89  89  89  LEU LEU C . n 
C 1 90  LEU 90  90  90  LEU LEU C . n 
C 1 91  THR 91  91  91  THR THR C . n 
C 1 92  PRO 92  92  92  PRO PRO C . n 
C 1 93  PRO 93  93  93  PRO PRO C . n 
C 1 94  VAL 94  94  94  VAL VAL C . n 
C 1 95  LYS 95  95  95  LYS LYS C . n 
C 1 96  TYR 96  96  96  TYR TYR C . n 
C 1 97  ILE 97  97  97  ILE ILE C . n 
C 1 98  ALA 98  98  98  ALA ALA C . n 
C 1 99  ASN 99  99  99  ASN ASN C . n 
C 1 100 MET 100 100 100 MET MET C . n 
C 1 101 HIS 101 101 101 HIS HIS C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 ASP 103 103 103 ASP ASP C . n 
C 1 104 GLU 104 104 104 GLU GLU C . n 
C 1 105 THR 105 105 105 THR THR C . n 
C 1 106 VAL 106 106 106 VAL VAL C . n 
C 1 107 GLY 107 107 107 GLY GLY C . n 
C 1 108 ARG 108 108 108 ARG ARG C . n 
C 1 109 GLN 109 109 109 GLN GLN C . n 
C 1 110 LEU 110 110 110 LEU LEU C . n 
C 1 111 LEU 111 111 111 LEU LEU C . n 
C 1 112 VAL 112 112 112 VAL VAL C . n 
C 1 113 TYR 113 113 113 TYR TYR C . n 
C 1 114 MET 114 114 114 MET MET C . n 
C 1 115 ALA 115 115 115 ALA ALA C . n 
C 1 116 GLN 116 116 116 GLN GLN C . n 
C 1 117 TYR 117 117 117 TYR TYR C . n 
C 1 118 LEU 118 118 118 LEU LEU C . n 
C 1 119 LEU 119 119 119 LEU LEU C . n 
C 1 120 GLY 120 120 120 GLY GLY C . n 
C 1 121 ASN 121 121 121 ASN ASN C . n 
C 1 122 HIS 122 122 122 HIS HIS C . n 
C 1 123 GLU 123 123 123 GLU GLU C . n 
C 1 124 ARG 124 124 124 ARG ARG C . n 
C 1 125 ILE 125 125 125 ILE ILE C . n 
C 1 126 SER 126 126 126 SER SER C . n 
C 1 127 ASP 127 127 127 ASP ASP C . n 
C 1 128 LEU 128 128 128 LEU LEU C . n 
C 1 129 GLY 129 129 129 GLY GLY C . n 
C 1 130 GLN 130 130 130 GLN GLN C . n 
C 1 131 LEU 131 131 131 LEU LEU C . n 
C 1 132 VAL 132 132 132 VAL VAL C . n 
C 1 133 ASN 133 133 133 ASN ASN C . n 
C 1 134 SER 134 134 134 SER SER C . n 
C 1 135 THR 135 135 135 THR THR C . n 
C 1 136 ASP 136 136 136 ASP ASP C . n 
C 1 137 ILE 137 137 137 ILE ILE C . n 
C 1 138 TYR 138 138 138 TYR TYR C . n 
C 1 139 LEU 139 139 139 LEU LEU C . n 
C 1 140 VAL 140 140 140 VAL VAL C . n 
C 1 141 PRO 141 141 141 PRO PRO C . n 
C 1 142 THR 142 142 142 THR THR C . n 
C 1 143 MET 143 143 143 MET MET C . n 
C 1 144 ASN 144 144 144 ASN ASN C . n 
C 1 145 PRO 145 145 145 PRO PRO C . n 
C 1 146 ASP 146 146 146 ASP ASP C . n 
C 1 147 GLY 147 147 147 GLY GLY C . n 
C 1 148 TYR 148 148 148 TYR TYR C . n 
C 1 149 ALA 149 149 149 ALA ALA C . n 
C 1 150 LEU 150 150 150 LEU LEU C . n 
C 1 151 SER 151 151 151 SER SER C . n 
C 1 152 GLN 152 152 152 GLN GLN C . n 
C 1 153 GLU 153 153 153 GLU GLU C . n 
C 1 154 GLY 154 154 154 GLY GLY C . n 
C 1 155 ASN 155 155 155 ASN ASN C . n 
C 1 156 CYS 156 156 156 CYS CYS C . n 
C 1 157 GLU 157 157 157 GLU GLU C . n 
C 1 158 SER 158 158 158 SER SER C . n 
C 1 159 LEU 159 159 159 LEU LEU C . n 
C 1 160 PRO 160 160 160 PRO PRO C . n 
C 1 161 ASN 161 161 161 ASN ASN C . n 
C 1 162 TYR 162 162 162 TYR TYR C . n 
C 1 163 VAL 163 163 163 VAL VAL C . n 
C 1 164 GLY 164 164 164 GLY GLY C . n 
C 1 165 ARG 165 165 165 ARG ARG C . n 
C 1 166 GLY 166 166 166 GLY GLY C . n 
C 1 167 ASN 167 167 167 ASN ASN C . n 
C 1 168 ALA 168 168 168 ALA ALA C . n 
C 1 169 ALA 169 169 169 ALA ALA C . n 
C 1 170 ASN 170 170 170 ASN ASN C . n 
C 1 171 ILE 171 171 171 ILE ILE C . n 
C 1 172 ASP 172 172 172 ASP ASP C . n 
C 1 173 LEU 173 173 173 LEU LEU C . n 
C 1 174 ASN 174 174 174 ASN ASN C . n 
C 1 175 ARG 175 175 175 ARG ARG C . n 
C 1 176 ASP 176 176 176 ASP ASP C . n 
C 1 177 PHE 177 177 177 PHE PHE C . n 
C 1 178 PRO 178 178 178 PRO PRO C . n 
C 1 179 ASP 179 179 179 ASP ASP C . n 
C 1 180 ARG 180 180 180 ARG ARG C . n 
C 1 181 LEU 181 181 181 LEU LEU C . n 
C 1 182 GLU 182 182 182 GLU GLU C . n 
C 1 183 GLN 183 183 183 GLN GLN C . n 
C 1 184 SER 184 184 ?   ?   ?   C . n 
C 1 185 HIS 185 185 ?   ?   ?   C . n 
C 1 186 VAL 186 186 ?   ?   ?   C . n 
C 1 187 HIS 187 187 ?   ?   ?   C . n 
C 1 188 GLN 188 188 ?   ?   ?   C . n 
C 1 189 LEU 189 189 189 LEU LEU C . n 
C 1 190 ARG 190 190 190 ARG ARG C . n 
C 1 191 ALA 191 191 191 ALA ALA C . n 
C 1 192 GLN 192 192 192 GLN GLN C . n 
C 1 193 SER 193 193 193 SER SER C . n 
C 1 194 ARG 194 194 194 ARG ARG C . n 
C 1 195 GLN 195 195 195 GLN GLN C . n 
C 1 196 PRO 196 196 196 PRO PRO C . n 
C 1 197 GLU 197 197 197 GLU GLU C . n 
C 1 198 THR 198 198 198 THR THR C . n 
C 1 199 ALA 199 199 199 ALA ALA C . n 
C 1 200 ALA 200 200 200 ALA ALA C . n 
C 1 201 LEU 201 201 201 LEU LEU C . n 
C 1 202 VAL 202 202 202 VAL VAL C . n 
C 1 203 ASN 203 203 203 ASN ASN C . n 
C 1 204 TRP 204 204 204 TRP TRP C . n 
C 1 205 ILE 205 205 205 ILE ILE C . n 
C 1 206 VAL 206 206 206 VAL VAL C . n 
C 1 207 SER 207 207 207 SER SER C . n 
C 1 208 LYS 208 208 208 LYS LYS C . n 
C 1 209 PRO 209 209 209 PRO PRO C . n 
C 1 210 PHE 210 210 210 PHE PHE C . n 
C 1 211 VAL 211 211 211 VAL VAL C . n 
C 1 212 LEU 212 212 212 LEU LEU C . n 
C 1 213 SER 213 213 213 SER SER C . n 
C 1 214 ALA 214 214 214 ALA ALA C . n 
C 1 215 ASN 215 215 215 ASN ASN C . n 
C 1 216 PHE 216 216 216 PHE PHE C . n 
C 1 217 HIS 217 217 217 HIS HIS C . n 
C 1 218 GLY 218 218 218 GLY GLY C . n 
C 1 219 GLY 219 219 219 GLY GLY C . n 
C 1 220 ALA 220 220 220 ALA ALA C . n 
C 1 221 VAL 221 221 221 VAL VAL C . n 
C 1 222 VAL 222 222 222 VAL VAL C . n 
C 1 223 ALA 223 223 223 ALA ALA C . n 
C 1 224 SER 224 224 224 SER SER C . n 
C 1 225 TYR 225 225 225 TYR TYR C . n 
C 1 226 PRO 226 226 226 PRO PRO C . n 
C 1 227 TYR 227 227 227 TYR TYR C . n 
C 1 228 ASP 228 228 228 ASP ASP C . n 
C 1 229 ASN 229 229 229 ASN ASN C . n 
C 1 230 SER 230 230 230 SER SER C . n 
C 1 231 LEU 231 231 231 LEU LEU C . n 
C 1 232 ALA 232 232 232 ALA ALA C . n 
C 1 233 HIS 233 233 233 HIS HIS C . n 
C 1 234 ASN 234 234 234 ASN ASN C . n 
C 1 235 GLU 235 235 235 GLU GLU C . n 
C 1 236 CYS 236 236 236 CYS CYS C . n 
C 1 237 CYS 237 237 237 CYS CYS C . n 
C 1 238 GLU 238 238 238 GLU GLU C . n 
C 1 239 GLU 239 239 239 GLU GLU C . n 
C 1 240 SER 240 240 240 SER SER C . n 
C 1 241 LEU 241 241 241 LEU LEU C . n 
C 1 242 THR 242 242 242 THR THR C . n 
C 1 243 PRO 243 243 243 PRO PRO C . n 
C 1 244 ASP 244 244 244 ASP ASP C . n 
C 1 245 ASP 245 245 245 ASP ASP C . n 
C 1 246 ARG 246 246 246 ARG ARG C . n 
C 1 247 VAL 247 247 247 VAL VAL C . n 
C 1 248 PHE 248 248 248 PHE PHE C . n 
C 1 249 LYS 249 249 249 LYS LYS C . n 
C 1 250 GLN 250 250 250 GLN GLN C . n 
C 1 251 LEU 251 251 251 LEU LEU C . n 
C 1 252 ALA 252 252 252 ALA ALA C . n 
C 1 253 HIS 253 253 253 HIS HIS C . n 
C 1 254 THR 254 254 254 THR THR C . n 
C 1 255 TYR 255 255 255 TYR TYR C . n 
C 1 256 SER 256 256 256 SER SER C . n 
C 1 257 ASP 257 257 257 ASP ASP C . n 
C 1 258 ASN 258 258 258 ASN ASN C . n 
C 1 259 HIS 259 259 259 HIS HIS C . n 
C 1 260 PRO 260 260 260 PRO PRO C . n 
C 1 261 ILE 261 261 261 ILE ILE C . n 
C 1 262 MET 262 262 262 MET MET C . n 
C 1 263 ARG 263 263 263 ARG ARG C . n 
C 1 264 LYS 264 264 264 LYS LYS C . n 
C 1 265 GLY 265 265 265 GLY GLY C . n 
C 1 266 ASN 266 266 266 ASN ASN C . n 
C 1 267 ASN 267 267 267 ASN ASN C . n 
C 1 268 CYS 268 268 268 CYS CYS C . n 
C 1 269 ASN 269 269 269 ASN ASN C . n 
C 1 270 ASP 270 270 270 ASP ASP C . n 
C 1 271 SER 271 271 271 SER SER C . n 
C 1 272 PHE 272 272 272 PHE PHE C . n 
C 1 273 SER 273 273 273 SER SER C . n 
C 1 274 GLY 274 274 274 GLY GLY C . n 
C 1 275 GLY 275 275 275 GLY GLY C . n 
C 1 276 ILE 276 276 276 ILE ILE C . n 
C 1 277 THR 277 277 277 THR THR C . n 
C 1 278 ASN 278 278 278 ASN ASN C . n 
C 1 279 GLY 279 279 279 GLY GLY C . n 
C 1 280 ALA 280 280 280 ALA ALA C . n 
C 1 281 HIS 281 281 281 HIS HIS C . n 
C 1 282 TRP 282 282 282 TRP TRP C . n 
C 1 283 TYR 283 283 283 TYR TYR C . n 
C 1 284 GLU 284 284 284 GLU GLU C . n 
C 1 285 LEU 285 285 285 LEU LEU C . n 
C 1 286 SER 286 286 286 SER SER C . n 
C 1 287 GLY 287 287 287 GLY GLY C . n 
C 1 288 GLY 288 288 288 GLY GLY C . n 
C 1 289 MET 289 289 289 MET MET C . n 
C 1 290 GLN 290 290 290 GLN GLN C . n 
C 1 291 ASP 291 291 291 ASP ASP C . n 
C 1 292 PHE 292 292 292 PHE PHE C . n 
C 1 293 ASN 293 293 293 ASN ASN C . n 
C 1 294 TYR 294 294 294 TYR TYR C . n 
C 1 295 ALA 295 295 295 ALA ALA C . n 
C 1 296 PHE 296 296 296 PHE PHE C . n 
C 1 297 SER 297 297 297 SER SER C . n 
C 1 298 ASN 298 298 298 ASN ASN C . n 
C 1 299 CYS 299 299 299 CYS CYS C . n 
C 1 300 PHE 300 300 300 PHE PHE C . n 
C 1 301 GLU 301 301 301 GLU GLU C . n 
C 1 302 LEU 302 302 302 LEU LEU C . n 
C 1 303 THR 303 303 303 THR THR C . n 
C 1 304 ILE 304 304 304 ILE ILE C . n 
C 1 305 GLU 305 305 305 GLU GLU C . n 
C 1 306 LEU 306 306 306 LEU LEU C . n 
C 1 307 SER 307 307 307 SER SER C . n 
C 1 308 CYS 308 308 308 CYS CYS C . n 
C 1 309 CYS 309 309 309 CYS CYS C . n 
C 1 310 LYS 310 310 310 LYS LYS C . n 
C 1 311 TYR 311 311 311 TYR TYR C . n 
C 1 312 PRO 312 312 312 PRO PRO C . n 
C 1 313 ALA 313 313 313 ALA ALA C . n 
C 1 314 ALA 314 314 314 ALA ALA C . n 
C 1 315 SER 315 315 315 SER SER C . n 
C 1 316 THR 316 316 316 THR THR C . n 
C 1 317 LEU 317 317 317 LEU LEU C . n 
C 1 318 PRO 318 318 318 PRO PRO C . n 
C 1 319 GLN 319 319 319 GLN GLN C . n 
C 1 320 GLU 320 320 320 GLU GLU C . n 
C 1 321 TRP 321 321 321 TRP TRP C . n 
C 1 322 GLN 322 322 322 GLN GLN C . n 
C 1 323 ARG 323 323 323 ARG ARG C . n 
C 1 324 ASN 324 324 324 ASN ASN C . n 
C 1 325 LYS 325 325 325 LYS LYS C . n 
C 1 326 ALA 326 326 326 ALA ALA C . n 
C 1 327 SER 327 327 327 SER SER C . n 
C 1 328 LEU 328 328 328 LEU LEU C . n 
C 1 329 LEU 329 329 329 LEU LEU C . n 
C 1 330 GLN 330 330 330 GLN GLN C . n 
C 1 331 LEU 331 331 331 LEU LEU C . n 
C 1 332 LEU 332 332 332 LEU LEU C . n 
C 1 333 ARG 333 333 333 ARG ARG C . n 
C 1 334 GLN 334 334 334 GLN GLN C . n 
C 1 335 ALA 335 335 335 ALA ALA C . n 
C 1 336 HIS 336 336 336 HIS HIS C . n 
C 1 337 ILE 337 337 337 ILE ILE C . n 
C 1 338 GLY 338 338 338 GLY GLY C . n 
C 1 339 ILE 339 339 339 ILE ILE C . n 
C 1 340 LYS 340 340 340 LYS LYS C . n 
C 1 341 GLY 341 341 341 GLY GLY C . n 
C 1 342 LEU 342 342 342 LEU LEU C . n 
C 1 343 VAL 343 343 343 VAL VAL C . n 
C 1 344 THR 344 344 344 THR THR C . n 
C 1 345 ASP 345 345 345 ASP ASP C . n 
C 1 346 ALA 346 346 346 ALA ALA C . n 
C 1 347 SER 347 347 347 SER SER C . n 
C 1 348 GLY 348 348 348 GLY GLY C . n 
C 1 349 PHE 349 349 349 PHE PHE C . n 
C 1 350 PRO 350 350 350 PRO PRO C . n 
C 1 351 ILE 351 351 351 ILE ILE C . n 
C 1 352 ALA 352 352 352 ALA ALA C . n 
C 1 353 ASP 353 353 353 ASP ASP C . n 
C 1 354 ALA 354 354 354 ALA ALA C . n 
C 1 355 ASN 355 355 355 ASN ASN C . n 
C 1 356 VAL 356 356 356 VAL VAL C . n 
C 1 357 TYR 357 357 357 TYR TYR C . n 
C 1 358 VAL 358 358 358 VAL VAL C . n 
C 1 359 ALA 359 359 359 ALA ALA C . n 
C 1 360 GLY 360 360 360 GLY GLY C . n 
C 1 361 LEU 361 361 361 LEU LEU C . n 
C 1 362 GLU 362 362 362 GLU GLU C . n 
C 1 363 GLU 363 363 363 GLU GLU C . n 
C 1 364 LYS 364 364 364 LYS LYS C . n 
C 1 365 PRO 365 365 365 PRO PRO C . n 
C 1 366 MET 366 366 366 MET MET C . n 
C 1 367 ARG 367 367 367 ARG ARG C . n 
C 1 368 THR 368 368 368 THR THR C . n 
C 1 369 SER 369 369 369 SER SER C . n 
C 1 370 LYS 370 370 370 LYS LYS C . n 
C 1 371 ARG 371 371 371 ARG ARG C . n 
C 1 372 GLY 372 372 372 GLY GLY C . n 
C 1 373 GLU 373 373 373 GLU GLU C . n 
C 1 374 TYR 374 374 374 TYR TYR C . n 
C 1 375 TRP 375 375 375 TRP TRP C . n 
C 1 376 ARG 376 376 376 ARG ARG C . n 
C 1 377 LEU 377 377 377 LEU LEU C . n 
C 1 378 LEU 378 378 378 LEU LEU C . n 
C 1 379 THR 379 379 379 THR THR C . n 
C 1 380 PRO 380 380 380 PRO PRO C . n 
C 1 381 GLY 381 381 381 GLY GLY C . n 
C 1 382 LEU 382 382 382 LEU LEU C . n 
C 1 383 TYR 383 383 383 TYR TYR C . n 
C 1 384 SER 384 384 384 SER SER C . n 
C 1 385 VAL 385 385 385 VAL VAL C . n 
C 1 386 HIS 386 386 386 HIS HIS C . n 
C 1 387 ALA 387 387 387 ALA ALA C . n 
C 1 388 SER 388 388 388 SER SER C . n 
C 1 389 ALA 389 389 389 ALA ALA C . n 
C 1 390 PHE 390 390 390 PHE PHE C . n 
C 1 391 GLY 391 391 391 GLY GLY C . n 
C 1 392 TYR 392 392 392 TYR TYR C . n 
C 1 393 GLN 393 393 393 GLN GLN C . n 
C 1 394 THR 394 394 394 THR THR C . n 
C 1 395 SER 395 395 395 SER SER C . n 
C 1 396 ALA 396 396 396 ALA ALA C . n 
C 1 397 PRO 397 397 397 PRO PRO C . n 
C 1 398 GLN 398 398 398 GLN GLN C . n 
C 1 399 GLN 399 399 399 GLN GLN C . n 
C 1 400 VAL 400 400 400 VAL VAL C . n 
C 1 401 ARG 401 401 401 ARG ARG C . n 
C 1 402 VAL 402 402 402 VAL VAL C . n 
C 1 403 THR 403 403 403 THR THR C . n 
C 1 404 ASN 404 404 404 ASN ASN C . n 
C 1 405 ASP 405 405 405 ASP ASP C . n 
C 1 406 ASN 406 406 406 ASN ASN C . n 
C 1 407 GLN 407 407 407 GLN GLN C . n 
C 1 408 GLU 408 408 408 GLU GLU C . n 
C 1 409 ALA 409 409 409 ALA ALA C . n 
C 1 410 LEU 410 410 410 LEU LEU C . n 
C 1 411 ARG 411 411 411 ARG ARG C . n 
C 1 412 LEU 412 412 412 LEU LEU C . n 
C 1 413 ASP 413 413 413 ASP ASP C . n 
C 1 414 PHE 414 414 414 PHE PHE C . n 
C 1 415 LYS 415 415 415 LYS LYS C . n 
C 1 416 LEU 416 416 416 LEU LEU C . n 
C 1 417 ALA 417 417 417 ALA ALA C . n 
C 1 418 PRO 418 418 418 PRO PRO C . n 
C 1 419 VAL 419 419 419 VAL VAL C . n 
C 1 420 GLU 420 420 ?   ?   ?   C . n 
C 1 421 THR 421 421 ?   ?   ?   C . n 
C 1 422 ASN 422 422 ?   ?   ?   C . n 
C 1 423 PHE 423 423 ?   ?   ?   C . n 
C 1 424 ASP 424 424 ?   ?   ?   C . n 
C 1 425 GLY 425 425 ?   ?   ?   C . n 
C 1 426 ILE 426 426 ?   ?   ?   C . n 
C 1 427 SER 427 427 ?   ?   ?   C . n 
C 1 428 SER 428 428 ?   ?   ?   C . n 
C 1 429 PHE 429 429 ?   ?   ?   C . n 
C 1 430 TYR 430 430 ?   ?   ?   C . n 
C 1 431 SER 431 431 ?   ?   ?   C . n 
C 1 432 PRO 432 432 ?   ?   ?   C . n 
C 1 433 TYR 433 433 ?   ?   ?   C . n 
C 1 434 TYR 434 434 ?   ?   ?   C . n 
C 1 435 PHE 435 435 ?   ?   ?   C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   PRO 2   2   ?   ?   ?   D . n 
D 1 3   THR 3   3   ?   ?   ?   D . n 
D 1 4   LEU 4   4   ?   ?   ?   D . n 
D 1 5   GLY 5   5   ?   ?   ?   D . n 
D 1 6   LEU 6   6   ?   ?   ?   D . n 
D 1 7   LEU 7   7   ?   ?   ?   D . n 
D 1 8   PHE 8   8   ?   ?   ?   D . n 
D 1 9   ALA 9   9   ?   ?   ?   D . n 
D 1 10  SER 10  10  ?   ?   ?   D . n 
D 1 11  ILE 11  11  ?   ?   ?   D . n 
D 1 12  GLY 12  12  ?   ?   ?   D . n 
D 1 13  ILE 13  13  ?   ?   ?   D . n 
D 1 14  ALA 14  14  ?   ?   ?   D . n 
D 1 15  VAL 15  15  ?   ?   ?   D . n 
D 1 16  LEU 16  16  ?   ?   ?   D . n 
D 1 17  ALA 17  17  ?   ?   ?   D . n 
D 1 18  MET 18  18  ?   ?   ?   D . n 
D 1 19  GLY 19  19  ?   ?   ?   D . n 
D 1 20  VAL 20  20  ?   ?   ?   D . n 
D 1 21  PRO 21  21  ?   ?   ?   D . n 
D 1 22  HIS 22  22  ?   ?   ?   D . n 
D 1 23  CYS 23  23  ?   ?   ?   D . n 
D 1 24  ARG 24  24  ?   ?   ?   D . n 
D 1 25  GLY 25  25  ?   ?   ?   D . n 
D 1 26  TYR 26  26  ?   ?   ?   D . n 
D 1 27  THR 27  27  27  THR THR D . n 
D 1 28  ILE 28  28  28  ILE ILE D . n 
D 1 29  LYS 29  29  29  LYS LYS D . n 
D 1 30  GLU 30  30  30  GLU GLU D . n 
D 1 31  ASP 31  31  31  ASP ASP D . n 
D 1 32  GLU 32  32  32  GLU GLU D . n 
D 1 33  SER 33  33  33  SER SER D . n 
D 1 34  PHE 34  34  34  PHE PHE D . n 
D 1 35  LEU 35  35  35  LEU LEU D . n 
D 1 36  GLN 36  36  36  GLN GLN D . n 
D 1 37  GLN 37  37  37  GLN GLN D . n 
D 1 38  PRO 38  38  38  PRO PRO D . n 
D 1 39  HIS 39  39  39  HIS HIS D . n 
D 1 40  TYR 40  40  40  TYR TYR D . n 
D 1 41  ALA 41  41  41  ALA ALA D . n 
D 1 42  SER 42  42  42  SER SER D . n 
D 1 43  GLN 43  43  43  GLN GLN D . n 
D 1 44  GLU 44  44  44  GLU GLU D . n 
D 1 45  GLN 45  45  45  GLN GLN D . n 
D 1 46  LEU 46  46  46  LEU LEU D . n 
D 1 47  GLU 47  47  47  GLU GLU D . n 
D 1 48  ASP 48  48  48  ASP ASP D . n 
D 1 49  LEU 49  49  49  LEU LEU D . n 
D 1 50  PHE 50  50  50  PHE PHE D . n 
D 1 51  ALA 51  51  51  ALA ALA D . n 
D 1 52  GLY 52  52  52  GLY GLY D . n 
D 1 53  LEU 53  53  53  LEU LEU D . n 
D 1 54  GLU 54  54  54  GLU GLU D . n 
D 1 55  LYS 55  55  55  LYS LYS D . n 
D 1 56  ALA 56  56  56  ALA ALA D . n 
D 1 57  TYR 57  57  57  TYR TYR D . n 
D 1 58  PRO 58  58  58  PRO PRO D . n 
D 1 59  ASN 59  59  59  ASN ASN D . n 
D 1 60  GLN 60  60  60  GLN GLN D . n 
D 1 61  ALA 61  61  61  ALA ALA D . n 
D 1 62  LYS 62  62  62  LYS LYS D . n 
D 1 63  VAL 63  63  63  VAL VAL D . n 
D 1 64  HIS 64  64  64  HIS HIS D . n 
D 1 65  PHE 65  65  65  PHE PHE D . n 
D 1 66  LEU 66  66  66  LEU LEU D . n 
D 1 67  GLY 67  67  67  GLY GLY D . n 
D 1 68  ARG 68  68  68  ARG ARG D . n 
D 1 69  SER 69  69  69  SER SER D . n 
D 1 70  LEU 70  70  70  LEU LEU D . n 
D 1 71  GLU 71  71  71  GLU GLU D . n 
D 1 72  GLY 72  72  72  GLY GLY D . n 
D 1 73  ARG 73  73  73  ARG ARG D . n 
D 1 74  ASN 74  74  74  ASN ASN D . n 
D 1 75  LEU 75  75  75  LEU LEU D . n 
D 1 76  LEU 76  76  76  LEU LEU D . n 
D 1 77  ALA 77  77  77  ALA ALA D . n 
D 1 78  LEU 78  78  78  LEU LEU D . n 
D 1 79  GLN 79  79  79  GLN GLN D . n 
D 1 80  ILE 80  80  80  ILE ILE D . n 
D 1 81  SER 81  81  81  SER SER D . n 
D 1 82  ARG 82  82  82  ARG ARG D . n 
D 1 83  ASN 83  83  83  ASN ASN D . n 
D 1 84  THR 84  84  84  THR THR D . n 
D 1 85  ARG 85  85  85  ARG ARG D . n 
D 1 86  SER 86  86  86  SER SER D . n 
D 1 87  ARG 87  87  87  ARG ARG D . n 
D 1 88  ASN 88  88  88  ASN ASN D . n 
D 1 89  LEU 89  89  89  LEU LEU D . n 
D 1 90  LEU 90  90  90  LEU LEU D . n 
D 1 91  THR 91  91  91  THR THR D . n 
D 1 92  PRO 92  92  92  PRO PRO D . n 
D 1 93  PRO 93  93  93  PRO PRO D . n 
D 1 94  VAL 94  94  94  VAL VAL D . n 
D 1 95  LYS 95  95  95  LYS LYS D . n 
D 1 96  TYR 96  96  96  TYR TYR D . n 
D 1 97  ILE 97  97  97  ILE ILE D . n 
D 1 98  ALA 98  98  98  ALA ALA D . n 
D 1 99  ASN 99  99  99  ASN ASN D . n 
D 1 100 MET 100 100 100 MET MET D . n 
D 1 101 HIS 101 101 101 HIS HIS D . n 
D 1 102 GLY 102 102 102 GLY GLY D . n 
D 1 103 ASP 103 103 103 ASP ASP D . n 
D 1 104 GLU 104 104 104 GLU GLU D . n 
D 1 105 THR 105 105 105 THR THR D . n 
D 1 106 VAL 106 106 106 VAL VAL D . n 
D 1 107 GLY 107 107 107 GLY GLY D . n 
D 1 108 ARG 108 108 108 ARG ARG D . n 
D 1 109 GLN 109 109 109 GLN GLN D . n 
D 1 110 LEU 110 110 110 LEU LEU D . n 
D 1 111 LEU 111 111 111 LEU LEU D . n 
D 1 112 VAL 112 112 112 VAL VAL D . n 
D 1 113 TYR 113 113 113 TYR TYR D . n 
D 1 114 MET 114 114 114 MET MET D . n 
D 1 115 ALA 115 115 115 ALA ALA D . n 
D 1 116 GLN 116 116 116 GLN GLN D . n 
D 1 117 TYR 117 117 117 TYR TYR D . n 
D 1 118 LEU 118 118 118 LEU LEU D . n 
D 1 119 LEU 119 119 119 LEU LEU D . n 
D 1 120 GLY 120 120 120 GLY GLY D . n 
D 1 121 ASN 121 121 121 ASN ASN D . n 
D 1 122 HIS 122 122 122 HIS HIS D . n 
D 1 123 GLU 123 123 123 GLU GLU D . n 
D 1 124 ARG 124 124 124 ARG ARG D . n 
D 1 125 ILE 125 125 125 ILE ILE D . n 
D 1 126 SER 126 126 126 SER SER D . n 
D 1 127 ASP 127 127 127 ASP ASP D . n 
D 1 128 LEU 128 128 128 LEU LEU D . n 
D 1 129 GLY 129 129 129 GLY GLY D . n 
D 1 130 GLN 130 130 130 GLN GLN D . n 
D 1 131 LEU 131 131 131 LEU LEU D . n 
D 1 132 VAL 132 132 132 VAL VAL D . n 
D 1 133 ASN 133 133 133 ASN ASN D . n 
D 1 134 SER 134 134 134 SER SER D . n 
D 1 135 THR 135 135 135 THR THR D . n 
D 1 136 ASP 136 136 136 ASP ASP D . n 
D 1 137 ILE 137 137 137 ILE ILE D . n 
D 1 138 TYR 138 138 138 TYR TYR D . n 
D 1 139 LEU 139 139 139 LEU LEU D . n 
D 1 140 VAL 140 140 140 VAL VAL D . n 
D 1 141 PRO 141 141 141 PRO PRO D . n 
D 1 142 THR 142 142 142 THR THR D . n 
D 1 143 MET 143 143 143 MET MET D . n 
D 1 144 ASN 144 144 144 ASN ASN D . n 
D 1 145 PRO 145 145 145 PRO PRO D . n 
D 1 146 ASP 146 146 146 ASP ASP D . n 
D 1 147 GLY 147 147 147 GLY GLY D . n 
D 1 148 TYR 148 148 148 TYR TYR D . n 
D 1 149 ALA 149 149 149 ALA ALA D . n 
D 1 150 LEU 150 150 150 LEU LEU D . n 
D 1 151 SER 151 151 151 SER SER D . n 
D 1 152 GLN 152 152 152 GLN GLN D . n 
D 1 153 GLU 153 153 153 GLU GLU D . n 
D 1 154 GLY 154 154 154 GLY GLY D . n 
D 1 155 ASN 155 155 155 ASN ASN D . n 
D 1 156 CYS 156 156 156 CYS CYS D . n 
D 1 157 GLU 157 157 157 GLU GLU D . n 
D 1 158 SER 158 158 158 SER SER D . n 
D 1 159 LEU 159 159 159 LEU LEU D . n 
D 1 160 PRO 160 160 160 PRO PRO D . n 
D 1 161 ASN 161 161 161 ASN ASN D . n 
D 1 162 TYR 162 162 162 TYR TYR D . n 
D 1 163 VAL 163 163 163 VAL VAL D . n 
D 1 164 GLY 164 164 164 GLY GLY D . n 
D 1 165 ARG 165 165 165 ARG ARG D . n 
D 1 166 GLY 166 166 166 GLY GLY D . n 
D 1 167 ASN 167 167 167 ASN ASN D . n 
D 1 168 ALA 168 168 168 ALA ALA D . n 
D 1 169 ALA 169 169 169 ALA ALA D . n 
D 1 170 ASN 170 170 170 ASN ASN D . n 
D 1 171 ILE 171 171 171 ILE ILE D . n 
D 1 172 ASP 172 172 172 ASP ASP D . n 
D 1 173 LEU 173 173 173 LEU LEU D . n 
D 1 174 ASN 174 174 174 ASN ASN D . n 
D 1 175 ARG 175 175 175 ARG ARG D . n 
D 1 176 ASP 176 176 176 ASP ASP D . n 
D 1 177 PHE 177 177 177 PHE PHE D . n 
D 1 178 PRO 178 178 178 PRO PRO D . n 
D 1 179 ASP 179 179 179 ASP ASP D . n 
D 1 180 ARG 180 180 180 ARG ARG D . n 
D 1 181 LEU 181 181 181 LEU LEU D . n 
D 1 182 GLU 182 182 ?   ?   ?   D . n 
D 1 183 GLN 183 183 ?   ?   ?   D . n 
D 1 184 SER 184 184 ?   ?   ?   D . n 
D 1 185 HIS 185 185 ?   ?   ?   D . n 
D 1 186 VAL 186 186 ?   ?   ?   D . n 
D 1 187 HIS 187 187 ?   ?   ?   D . n 
D 1 188 GLN 188 188 ?   ?   ?   D . n 
D 1 189 LEU 189 189 ?   ?   ?   D . n 
D 1 190 ARG 190 190 ?   ?   ?   D . n 
D 1 191 ALA 191 191 191 ALA ALA D . n 
D 1 192 GLN 192 192 192 GLN GLN D . n 
D 1 193 SER 193 193 193 SER SER D . n 
D 1 194 ARG 194 194 194 ARG ARG D . n 
D 1 195 GLN 195 195 195 GLN GLN D . n 
D 1 196 PRO 196 196 196 PRO PRO D . n 
D 1 197 GLU 197 197 197 GLU GLU D . n 
D 1 198 THR 198 198 198 THR THR D . n 
D 1 199 ALA 199 199 199 ALA ALA D . n 
D 1 200 ALA 200 200 200 ALA ALA D . n 
D 1 201 LEU 201 201 201 LEU LEU D . n 
D 1 202 VAL 202 202 202 VAL VAL D . n 
D 1 203 ASN 203 203 203 ASN ASN D . n 
D 1 204 TRP 204 204 204 TRP TRP D . n 
D 1 205 ILE 205 205 205 ILE ILE D . n 
D 1 206 VAL 206 206 206 VAL VAL D . n 
D 1 207 SER 207 207 207 SER SER D . n 
D 1 208 LYS 208 208 208 LYS LYS D . n 
D 1 209 PRO 209 209 209 PRO PRO D . n 
D 1 210 PHE 210 210 210 PHE PHE D . n 
D 1 211 VAL 211 211 211 VAL VAL D . n 
D 1 212 LEU 212 212 212 LEU LEU D . n 
D 1 213 SER 213 213 213 SER SER D . n 
D 1 214 ALA 214 214 214 ALA ALA D . n 
D 1 215 ASN 215 215 215 ASN ASN D . n 
D 1 216 PHE 216 216 216 PHE PHE D . n 
D 1 217 HIS 217 217 217 HIS HIS D . n 
D 1 218 GLY 218 218 218 GLY GLY D . n 
D 1 219 GLY 219 219 219 GLY GLY D . n 
D 1 220 ALA 220 220 220 ALA ALA D . n 
D 1 221 VAL 221 221 221 VAL VAL D . n 
D 1 222 VAL 222 222 222 VAL VAL D . n 
D 1 223 ALA 223 223 223 ALA ALA D . n 
D 1 224 SER 224 224 224 SER SER D . n 
D 1 225 TYR 225 225 225 TYR TYR D . n 
D 1 226 PRO 226 226 226 PRO PRO D . n 
D 1 227 TYR 227 227 227 TYR TYR D . n 
D 1 228 ASP 228 228 228 ASP ASP D . n 
D 1 229 ASN 229 229 229 ASN ASN D . n 
D 1 230 SER 230 230 230 SER SER D . n 
D 1 231 LEU 231 231 231 LEU LEU D . n 
D 1 232 ALA 232 232 232 ALA ALA D . n 
D 1 233 HIS 233 233 233 HIS HIS D . n 
D 1 234 ASN 234 234 234 ASN ASN D . n 
D 1 235 GLU 235 235 235 GLU GLU D . n 
D 1 236 CYS 236 236 236 CYS CYS D . n 
D 1 237 CYS 237 237 237 CYS CYS D . n 
D 1 238 GLU 238 238 238 GLU GLU D . n 
D 1 239 GLU 239 239 239 GLU GLU D . n 
D 1 240 SER 240 240 240 SER SER D . n 
D 1 241 LEU 241 241 241 LEU LEU D . n 
D 1 242 THR 242 242 242 THR THR D . n 
D 1 243 PRO 243 243 243 PRO PRO D . n 
D 1 244 ASP 244 244 244 ASP ASP D . n 
D 1 245 ASP 245 245 245 ASP ASP D . n 
D 1 246 ARG 246 246 246 ARG ARG D . n 
D 1 247 VAL 247 247 247 VAL VAL D . n 
D 1 248 PHE 248 248 248 PHE PHE D . n 
D 1 249 LYS 249 249 249 LYS LYS D . n 
D 1 250 GLN 250 250 250 GLN GLN D . n 
D 1 251 LEU 251 251 251 LEU LEU D . n 
D 1 252 ALA 252 252 252 ALA ALA D . n 
D 1 253 HIS 253 253 253 HIS HIS D . n 
D 1 254 THR 254 254 254 THR THR D . n 
D 1 255 TYR 255 255 255 TYR TYR D . n 
D 1 256 SER 256 256 256 SER SER D . n 
D 1 257 ASP 257 257 257 ASP ASP D . n 
D 1 258 ASN 258 258 258 ASN ASN D . n 
D 1 259 HIS 259 259 259 HIS HIS D . n 
D 1 260 PRO 260 260 260 PRO PRO D . n 
D 1 261 ILE 261 261 261 ILE ILE D . n 
D 1 262 MET 262 262 262 MET MET D . n 
D 1 263 ARG 263 263 263 ARG ARG D . n 
D 1 264 LYS 264 264 264 LYS LYS D . n 
D 1 265 GLY 265 265 265 GLY GLY D . n 
D 1 266 ASN 266 266 266 ASN ASN D . n 
D 1 267 ASN 267 267 267 ASN ASN D . n 
D 1 268 CYS 268 268 268 CYS CYS D . n 
D 1 269 ASN 269 269 269 ASN ASN D . n 
D 1 270 ASP 270 270 270 ASP ASP D . n 
D 1 271 SER 271 271 271 SER SER D . n 
D 1 272 PHE 272 272 272 PHE PHE D . n 
D 1 273 SER 273 273 273 SER SER D . n 
D 1 274 GLY 274 274 274 GLY GLY D . n 
D 1 275 GLY 275 275 275 GLY GLY D . n 
D 1 276 ILE 276 276 276 ILE ILE D . n 
D 1 277 THR 277 277 277 THR THR D . n 
D 1 278 ASN 278 278 278 ASN ASN D . n 
D 1 279 GLY 279 279 279 GLY GLY D . n 
D 1 280 ALA 280 280 280 ALA ALA D . n 
D 1 281 HIS 281 281 281 HIS HIS D . n 
D 1 282 TRP 282 282 282 TRP TRP D . n 
D 1 283 TYR 283 283 283 TYR TYR D . n 
D 1 284 GLU 284 284 284 GLU GLU D . n 
D 1 285 LEU 285 285 285 LEU LEU D . n 
D 1 286 SER 286 286 286 SER SER D . n 
D 1 287 GLY 287 287 287 GLY GLY D . n 
D 1 288 GLY 288 288 288 GLY GLY D . n 
D 1 289 MET 289 289 289 MET MET D . n 
D 1 290 GLN 290 290 290 GLN GLN D . n 
D 1 291 ASP 291 291 291 ASP ASP D . n 
D 1 292 PHE 292 292 292 PHE PHE D . n 
D 1 293 ASN 293 293 293 ASN ASN D . n 
D 1 294 TYR 294 294 294 TYR TYR D . n 
D 1 295 ALA 295 295 295 ALA ALA D . n 
D 1 296 PHE 296 296 296 PHE PHE D . n 
D 1 297 SER 297 297 297 SER SER D . n 
D 1 298 ASN 298 298 298 ASN ASN D . n 
D 1 299 CYS 299 299 299 CYS CYS D . n 
D 1 300 PHE 300 300 300 PHE PHE D . n 
D 1 301 GLU 301 301 301 GLU GLU D . n 
D 1 302 LEU 302 302 302 LEU LEU D . n 
D 1 303 THR 303 303 303 THR THR D . n 
D 1 304 ILE 304 304 304 ILE ILE D . n 
D 1 305 GLU 305 305 305 GLU GLU D . n 
D 1 306 LEU 306 306 306 LEU LEU D . n 
D 1 307 SER 307 307 307 SER SER D . n 
D 1 308 CYS 308 308 308 CYS CYS D . n 
D 1 309 CYS 309 309 309 CYS CYS D . n 
D 1 310 LYS 310 310 310 LYS LYS D . n 
D 1 311 TYR 311 311 311 TYR TYR D . n 
D 1 312 PRO 312 312 312 PRO PRO D . n 
D 1 313 ALA 313 313 313 ALA ALA D . n 
D 1 314 ALA 314 314 314 ALA ALA D . n 
D 1 315 SER 315 315 315 SER SER D . n 
D 1 316 THR 316 316 316 THR THR D . n 
D 1 317 LEU 317 317 317 LEU LEU D . n 
D 1 318 PRO 318 318 318 PRO PRO D . n 
D 1 319 GLN 319 319 319 GLN GLN D . n 
D 1 320 GLU 320 320 320 GLU GLU D . n 
D 1 321 TRP 321 321 321 TRP TRP D . n 
D 1 322 GLN 322 322 322 GLN GLN D . n 
D 1 323 ARG 323 323 323 ARG ARG D . n 
D 1 324 ASN 324 324 324 ASN ASN D . n 
D 1 325 LYS 325 325 325 LYS LYS D . n 
D 1 326 ALA 326 326 326 ALA ALA D . n 
D 1 327 SER 327 327 327 SER SER D . n 
D 1 328 LEU 328 328 328 LEU LEU D . n 
D 1 329 LEU 329 329 329 LEU LEU D . n 
D 1 330 GLN 330 330 330 GLN GLN D . n 
D 1 331 LEU 331 331 331 LEU LEU D . n 
D 1 332 LEU 332 332 332 LEU LEU D . n 
D 1 333 ARG 333 333 333 ARG ARG D . n 
D 1 334 GLN 334 334 334 GLN GLN D . n 
D 1 335 ALA 335 335 335 ALA ALA D . n 
D 1 336 HIS 336 336 336 HIS HIS D . n 
D 1 337 ILE 337 337 337 ILE ILE D . n 
D 1 338 GLY 338 338 338 GLY GLY D . n 
D 1 339 ILE 339 339 339 ILE ILE D . n 
D 1 340 LYS 340 340 340 LYS LYS D . n 
D 1 341 GLY 341 341 341 GLY GLY D . n 
D 1 342 LEU 342 342 342 LEU LEU D . n 
D 1 343 VAL 343 343 343 VAL VAL D . n 
D 1 344 THR 344 344 344 THR THR D . n 
D 1 345 ASP 345 345 345 ASP ASP D . n 
D 1 346 ALA 346 346 346 ALA ALA D . n 
D 1 347 SER 347 347 347 SER SER D . n 
D 1 348 GLY 348 348 348 GLY GLY D . n 
D 1 349 PHE 349 349 349 PHE PHE D . n 
D 1 350 PRO 350 350 350 PRO PRO D . n 
D 1 351 ILE 351 351 351 ILE ILE D . n 
D 1 352 ALA 352 352 352 ALA ALA D . n 
D 1 353 ASP 353 353 353 ASP ASP D . n 
D 1 354 ALA 354 354 354 ALA ALA D . n 
D 1 355 ASN 355 355 355 ASN ASN D . n 
D 1 356 VAL 356 356 356 VAL VAL D . n 
D 1 357 TYR 357 357 357 TYR TYR D . n 
D 1 358 VAL 358 358 358 VAL VAL D . n 
D 1 359 ALA 359 359 359 ALA ALA D . n 
D 1 360 GLY 360 360 360 GLY GLY D . n 
D 1 361 LEU 361 361 361 LEU LEU D . n 
D 1 362 GLU 362 362 362 GLU GLU D . n 
D 1 363 GLU 363 363 363 GLU GLU D . n 
D 1 364 LYS 364 364 364 LYS LYS D . n 
D 1 365 PRO 365 365 365 PRO PRO D . n 
D 1 366 MET 366 366 366 MET MET D . n 
D 1 367 ARG 367 367 367 ARG ARG D . n 
D 1 368 THR 368 368 368 THR THR D . n 
D 1 369 SER 369 369 369 SER SER D . n 
D 1 370 LYS 370 370 370 LYS LYS D . n 
D 1 371 ARG 371 371 371 ARG ARG D . n 
D 1 372 GLY 372 372 372 GLY GLY D . n 
D 1 373 GLU 373 373 373 GLU GLU D . n 
D 1 374 TYR 374 374 374 TYR TYR D . n 
D 1 375 TRP 375 375 375 TRP TRP D . n 
D 1 376 ARG 376 376 376 ARG ARG D . n 
D 1 377 LEU 377 377 377 LEU LEU D . n 
D 1 378 LEU 378 378 378 LEU LEU D . n 
D 1 379 THR 379 379 379 THR THR D . n 
D 1 380 PRO 380 380 380 PRO PRO D . n 
D 1 381 GLY 381 381 381 GLY GLY D . n 
D 1 382 LEU 382 382 382 LEU LEU D . n 
D 1 383 TYR 383 383 383 TYR TYR D . n 
D 1 384 SER 384 384 384 SER SER D . n 
D 1 385 VAL 385 385 385 VAL VAL D . n 
D 1 386 HIS 386 386 386 HIS HIS D . n 
D 1 387 ALA 387 387 387 ALA ALA D . n 
D 1 388 SER 388 388 388 SER SER D . n 
D 1 389 ALA 389 389 389 ALA ALA D . n 
D 1 390 PHE 390 390 390 PHE PHE D . n 
D 1 391 GLY 391 391 391 GLY GLY D . n 
D 1 392 TYR 392 392 392 TYR TYR D . n 
D 1 393 GLN 393 393 393 GLN GLN D . n 
D 1 394 THR 394 394 394 THR THR D . n 
D 1 395 SER 395 395 395 SER SER D . n 
D 1 396 ALA 396 396 396 ALA ALA D . n 
D 1 397 PRO 397 397 397 PRO PRO D . n 
D 1 398 GLN 398 398 398 GLN GLN D . n 
D 1 399 GLN 399 399 399 GLN GLN D . n 
D 1 400 VAL 400 400 400 VAL VAL D . n 
D 1 401 ARG 401 401 401 ARG ARG D . n 
D 1 402 VAL 402 402 402 VAL VAL D . n 
D 1 403 THR 403 403 403 THR THR D . n 
D 1 404 ASN 404 404 404 ASN ASN D . n 
D 1 405 ASP 405 405 405 ASP ASP D . n 
D 1 406 ASN 406 406 406 ASN ASN D . n 
D 1 407 GLN 407 407 407 GLN GLN D . n 
D 1 408 GLU 408 408 408 GLU GLU D . n 
D 1 409 ALA 409 409 409 ALA ALA D . n 
D 1 410 LEU 410 410 410 LEU LEU D . n 
D 1 411 ARG 411 411 411 ARG ARG D . n 
D 1 412 LEU 412 412 412 LEU LEU D . n 
D 1 413 ASP 413 413 413 ASP ASP D . n 
D 1 414 PHE 414 414 414 PHE PHE D . n 
D 1 415 LYS 415 415 415 LYS LYS D . n 
D 1 416 LEU 416 416 416 LEU LEU D . n 
D 1 417 ALA 417 417 417 ALA ALA D . n 
D 1 418 PRO 418 418 418 PRO PRO D . n 
D 1 419 VAL 419 419 419 VAL VAL D . n 
D 1 420 GLU 420 420 420 GLU GLU D . n 
D 1 421 THR 421 421 ?   ?   ?   D . n 
D 1 422 ASN 422 422 ?   ?   ?   D . n 
D 1 423 PHE 423 423 ?   ?   ?   D . n 
D 1 424 ASP 424 424 ?   ?   ?   D . n 
D 1 425 GLY 425 425 ?   ?   ?   D . n 
D 1 426 ILE 426 426 ?   ?   ?   D . n 
D 1 427 SER 427 427 ?   ?   ?   D . n 
D 1 428 SER 428 428 ?   ?   ?   D . n 
D 1 429 PHE 429 429 ?   ?   ?   D . n 
D 1 430 TYR 430 430 ?   ?   ?   D . n 
D 1 431 SER 431 431 ?   ?   ?   D . n 
D 1 432 PRO 432 432 ?   ?   ?   D . n 
D 1 433 TYR 433 433 ?   ?   ?   D . n 
D 1 434 TYR 434 434 ?   ?   ?   D . n 
D 1 435 PHE 435 435 ?   ?   ?   D . 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 
E 2 NAG 1  501  501  NAG NAG A . 
F 3 ZN  1  999  999  ZN  ZN  A . 
G 4 GEM 1  601  601  GEM GEM A . 
H 5 GOL 1  801  801  GOL GOL A . 
I 5 GOL 1  802  802  GOL GOL A . 
J 5 GOL 1  803  803  GOL GOL A . 
K 2 NAG 1  501  501  NAG NAG B . 
L 3 ZN  1  999  999  ZN  ZN  B . 
M 4 GEM 1  601  601  GEM GEM B . 
N 2 NAG 1  501  501  NAG NAG C . 
O 3 ZN  1  999  999  ZN  ZN  C . 
P 4 GEM 1  601  601  GEM GEM C . 
Q 5 GOL 1  804  804  GOL GOL C . 
R 2 NAG 1  501  501  NAG NAG D . 
S 3 ZN  1  999  999  ZN  ZN  D . 
T 4 GEM 1  601  601  GEM GEM D . 
U 6 HOH 1  1001 1001 HOH HOH A . 
U 6 HOH 2  1002 1002 HOH HOH A . 
U 6 HOH 3  1003 1003 HOH HOH A . 
U 6 HOH 4  1004 1004 HOH HOH A . 
U 6 HOH 5  1005 1005 HOH HOH A . 
U 6 HOH 6  1006 1006 HOH HOH A . 
U 6 HOH 7  1007 1007 HOH HOH A . 
U 6 HOH 8  1008 1008 HOH HOH A . 
U 6 HOH 9  1009 1009 HOH HOH A . 
U 6 HOH 10 1010 1010 HOH HOH A . 
U 6 HOH 11 1011 1011 HOH HOH A . 
U 6 HOH 12 1012 1012 HOH HOH A . 
U 6 HOH 13 1013 1013 HOH HOH A . 
U 6 HOH 14 1014 1014 HOH HOH A . 
U 6 HOH 15 1015 1015 HOH HOH A . 
U 6 HOH 16 1016 1016 HOH HOH A . 
U 6 HOH 17 1017 1017 HOH HOH A . 
U 6 HOH 18 1018 1018 HOH HOH A . 
U 6 HOH 19 1019 1019 HOH HOH A . 
U 6 HOH 20 1020 1020 HOH HOH A . 
U 6 HOH 21 1021 1021 HOH HOH A . 
U 6 HOH 22 1022 1022 HOH HOH A . 
U 6 HOH 23 1023 1023 HOH HOH A . 
U 6 HOH 24 1024 1024 HOH HOH A . 
U 6 HOH 25 1025 1025 HOH HOH A . 
U 6 HOH 26 1026 1026 HOH HOH A . 
U 6 HOH 27 1027 1027 HOH HOH A . 
U 6 HOH 28 1028 1028 HOH HOH A . 
U 6 HOH 29 1029 1029 HOH HOH A . 
U 6 HOH 30 1030 1030 HOH HOH A . 
U 6 HOH 31 1031 1031 HOH HOH A . 
U 6 HOH 32 1032 1032 HOH HOH A . 
U 6 HOH 33 1033 1033 HOH HOH A . 
U 6 HOH 34 1034 1034 HOH HOH A . 
U 6 HOH 35 1035 1035 HOH HOH A . 
U 6 HOH 36 1036 1036 HOH HOH A . 
U 6 HOH 37 1037 1037 HOH HOH A . 
U 6 HOH 38 1038 1038 HOH HOH A . 
U 6 HOH 39 1039 1039 HOH HOH A . 
U 6 HOH 40 1040 1040 HOH HOH A . 
U 6 HOH 41 1041 1041 HOH HOH A . 
U 6 HOH 42 1042 1042 HOH HOH A . 
U 6 HOH 43 1043 1043 HOH HOH A . 
U 6 HOH 44 1044 1044 HOH HOH A . 
U 6 HOH 45 1045 1045 HOH HOH A . 
U 6 HOH 46 1046 1046 HOH HOH A . 
U 6 HOH 47 1047 1047 HOH HOH A . 
U 6 HOH 48 1048 1048 HOH HOH A . 
U 6 HOH 49 1049 1049 HOH HOH A . 
U 6 HOH 50 1050 1050 HOH HOH A . 
V 6 HOH 1  1001 1001 HOH HOH B . 
V 6 HOH 2  1002 1002 HOH HOH B . 
V 6 HOH 3  1003 1003 HOH HOH B . 
V 6 HOH 4  1004 1004 HOH HOH B . 
V 6 HOH 5  1005 1005 HOH HOH B . 
V 6 HOH 6  1006 1006 HOH HOH B . 
V 6 HOH 7  1007 1007 HOH HOH B . 
V 6 HOH 8  1008 1008 HOH HOH B . 
V 6 HOH 9  1009 1009 HOH HOH B . 
V 6 HOH 10 1010 1010 HOH HOH B . 
V 6 HOH 11 1011 1011 HOH HOH B . 
V 6 HOH 12 1012 1012 HOH HOH B . 
V 6 HOH 13 1013 1013 HOH HOH B . 
V 6 HOH 14 1014 1014 HOH HOH B . 
V 6 HOH 15 1015 1015 HOH HOH B . 
V 6 HOH 16 1016 1016 HOH HOH B . 
V 6 HOH 17 1017 1017 HOH HOH B . 
V 6 HOH 18 1018 1018 HOH HOH B . 
V 6 HOH 19 1019 1019 HOH HOH B . 
V 6 HOH 20 1020 1020 HOH HOH B . 
V 6 HOH 21 1021 1021 HOH HOH B . 
V 6 HOH 22 1022 1022 HOH HOH B . 
V 6 HOH 23 1023 1023 HOH HOH B . 
V 6 HOH 24 1024 1024 HOH HOH B . 
V 6 HOH 25 1025 1025 HOH HOH B . 
V 6 HOH 26 1026 1026 HOH HOH B . 
V 6 HOH 27 1027 1027 HOH HOH B . 
V 6 HOH 28 1028 1028 HOH HOH B . 
V 6 HOH 29 1029 1029 HOH HOH B . 
V 6 HOH 30 1030 1030 HOH HOH B . 
V 6 HOH 31 1031 1031 HOH HOH B . 
V 6 HOH 32 1032 1032 HOH HOH B . 
V 6 HOH 33 1033 1033 HOH HOH B . 
V 6 HOH 34 1034 1034 HOH HOH B . 
V 6 HOH 35 1035 1035 HOH HOH B . 
V 6 HOH 36 1036 1036 HOH HOH B . 
V 6 HOH 37 1037 1037 HOH HOH B . 
V 6 HOH 38 1038 1038 HOH HOH B . 
V 6 HOH 39 1039 1039 HOH HOH B . 
V 6 HOH 40 1040 1040 HOH HOH B . 
V 6 HOH 41 1041 1041 HOH HOH B . 
V 6 HOH 42 1042 1042 HOH HOH B . 
V 6 HOH 43 1043 1043 HOH HOH B . 
V 6 HOH 44 1044 1044 HOH HOH B . 
V 6 HOH 45 1045 1045 HOH HOH B . 
V 6 HOH 46 1046 1046 HOH HOH B . 
V 6 HOH 47 1047 1047 HOH HOH B . 
V 6 HOH 48 1048 1048 HOH HOH B . 
V 6 HOH 49 1049 1049 HOH HOH B . 
V 6 HOH 50 1050 1050 HOH HOH B . 
V 6 HOH 51 1051 1051 HOH HOH B . 
V 6 HOH 52 1052 1052 HOH HOH B . 
V 6 HOH 53 1053 1053 HOH HOH B . 
V 6 HOH 54 1054 1054 HOH HOH B . 
W 6 HOH 1  1001 1001 HOH HOH C . 
W 6 HOH 2  1002 1002 HOH HOH C . 
W 6 HOH 3  1003 1003 HOH HOH C . 
W 6 HOH 4  1004 1004 HOH HOH C . 
W 6 HOH 5  1005 1005 HOH HOH C . 
W 6 HOH 6  1006 1006 HOH HOH C . 
W 6 HOH 7  1007 1007 HOH HOH C . 
W 6 HOH 8  1008 1008 HOH HOH C . 
W 6 HOH 9  1009 1009 HOH HOH C . 
W 6 HOH 10 1010 1010 HOH HOH C . 
W 6 HOH 11 1011 1011 HOH HOH C . 
W 6 HOH 12 1012 1012 HOH HOH C . 
W 6 HOH 13 1013 1013 HOH HOH C . 
W 6 HOH 14 1014 1014 HOH HOH C . 
W 6 HOH 15 1015 1015 HOH HOH C . 
W 6 HOH 16 1016 1016 HOH HOH C . 
W 6 HOH 17 1017 1017 HOH HOH C . 
W 6 HOH 18 1018 1018 HOH HOH C . 
W 6 HOH 19 1019 1019 HOH HOH C . 
W 6 HOH 20 1020 1020 HOH HOH C . 
W 6 HOH 21 1021 1021 HOH HOH C . 
W 6 HOH 22 1022 1022 HOH HOH C . 
W 6 HOH 23 1023 1023 HOH HOH C . 
W 6 HOH 24 1024 1024 HOH HOH C . 
W 6 HOH 25 1025 1025 HOH HOH C . 
W 6 HOH 26 1026 1026 HOH HOH C . 
W 6 HOH 27 1027 1027 HOH HOH C . 
W 6 HOH 28 1028 1028 HOH HOH C . 
W 6 HOH 29 1029 1029 HOH HOH C . 
W 6 HOH 30 1030 1030 HOH HOH C . 
W 6 HOH 31 1031 1031 HOH HOH C . 
W 6 HOH 32 1032 1032 HOH HOH C . 
W 6 HOH 33 1033 1033 HOH HOH C . 
W 6 HOH 34 1034 1034 HOH HOH C . 
W 6 HOH 35 1035 1035 HOH HOH C . 
W 6 HOH 36 1036 1036 HOH HOH C . 
W 6 HOH 37 1037 1037 HOH HOH C . 
W 6 HOH 38 1038 1038 HOH HOH C . 
W 6 HOH 39 1039 1039 HOH HOH C . 
W 6 HOH 40 1040 1040 HOH HOH C . 
W 6 HOH 41 1041 1041 HOH HOH C . 
W 6 HOH 42 1042 1042 HOH HOH C . 
W 6 HOH 43 1043 1043 HOH HOH C . 
W 6 HOH 44 1044 1044 HOH HOH C . 
W 6 HOH 45 1045 1045 HOH HOH C . 
W 6 HOH 46 1046 1046 HOH HOH C . 
W 6 HOH 47 1047 1047 HOH HOH C . 
W 6 HOH 48 1048 1048 HOH HOH C . 
W 6 HOH 49 1049 1049 HOH HOH C . 
W 6 HOH 50 1050 1050 HOH HOH C . 
W 6 HOH 51 1051 1051 HOH HOH C . 
X 6 HOH 1  1001 1001 HOH HOH D . 
X 6 HOH 2  1002 1002 HOH HOH D . 
X 6 HOH 3  1003 1003 HOH HOH D . 
X 6 HOH 4  1004 1004 HOH HOH D . 
X 6 HOH 5  1005 1005 HOH HOH D . 
X 6 HOH 6  1006 1006 HOH HOH D . 
X 6 HOH 7  1007 1007 HOH HOH D . 
X 6 HOH 8  1008 1008 HOH HOH D . 
X 6 HOH 9  1009 1009 HOH HOH D . 
X 6 HOH 10 1010 1010 HOH HOH D . 
X 6 HOH 11 1011 1011 HOH HOH D . 
X 6 HOH 12 1012 1012 HOH HOH D . 
X 6 HOH 13 1013 1013 HOH HOH D . 
X 6 HOH 14 1014 1014 HOH HOH D . 
X 6 HOH 15 1015 1015 HOH HOH D . 
X 6 HOH 16 1016 1016 HOH HOH D . 
X 6 HOH 17 1017 1017 HOH HOH D . 
X 6 HOH 18 1018 1018 HOH HOH D . 
X 6 HOH 19 1019 1019 HOH HOH D . 
X 6 HOH 20 1020 1020 HOH HOH D . 
X 6 HOH 21 1021 1021 HOH HOH D . 
X 6 HOH 22 1022 1022 HOH HOH D . 
X 6 HOH 23 1023 1023 HOH HOH D . 
X 6 HOH 24 1024 1024 HOH HOH D . 
X 6 HOH 25 1025 1025 HOH HOH D . 
X 6 HOH 26 1026 1026 HOH HOH D . 
X 6 HOH 27 1027 1027 HOH HOH D . 
X 6 HOH 28 1028 1028 HOH HOH D . 
X 6 HOH 29 1029 1029 HOH HOH D . 
X 6 HOH 30 1030 1030 HOH HOH D . 
X 6 HOH 31 1031 1031 HOH HOH D . 
X 6 HOH 32 1032 1032 HOH HOH D . 
X 6 HOH 33 1033 1033 HOH HOH D . 
X 6 HOH 34 1034 1034 HOH HOH D . 
X 6 HOH 35 1035 1035 HOH HOH D . 
X 6 HOH 36 1036 1036 HOH HOH D . 
X 6 HOH 37 1037 1037 HOH HOH D . 
X 6 HOH 38 1038 1038 HOH HOH D . 
X 6 HOH 39 1039 1039 HOH HOH D . 
X 6 HOH 40 1040 1040 HOH HOH D . 
X 6 HOH 41 1041 1041 HOH HOH D . 
X 6 HOH 42 1042 1042 HOH HOH D . 
X 6 HOH 43 1043 1043 HOH HOH D . 
X 6 HOH 44 1044 1044 HOH HOH D . 
X 6 HOH 45 1045 1045 HOH HOH D . 
X 6 HOH 46 1046 1046 HOH HOH D . 
X 6 HOH 47 1047 1047 HOH HOH D . 
X 6 HOH 48 1048 1048 HOH HOH D . 
X 6 HOH 49 1049 1049 HOH HOH D . 
X 6 HOH 50 1050 1050 HOH HOH D . 
X 6 HOH 51 1051 1051 HOH HOH D . 
X 6 HOH 52 1052 1052 HOH HOH D . 
X 6 HOH 53 1053 1053 HOH HOH D . 
X 6 HOH 54 1054 1054 HOH HOH D . 
X 6 HOH 55 1055 1055 HOH HOH D . 
X 6 HOH 56 1056 1056 HOH HOH D . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 133 A ASN 133 ? ASN 'GLYCOSYLATION SITE' 
2 B ASN 133 B ASN 133 ? ASN 'GLYCOSYLATION SITE' 
3 C ASN 133 C ASN 133 ? ASN 'GLYCOSYLATION SITE' 
4 D ASN 133 D ASN 133 ? ASN 'GLYCOSYLATION SITE' 
# 
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_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
3 author_and_software_defined_assembly PISA monomeric 1 
4 author_and_software_defined_assembly PISA 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,E,F,G,H,I,J,U 
2 1 B,K,L,M,V       
3 1 C,N,O,P,Q,W     
4 1 D,R,S,T,X       
# 
_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_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE1 ? D GLU 104 ? D GLU 104 ? 1_555 ZN ? S ZN . ? D ZN 999 ? 1_555 OE2 ? D GLU 104 ? D GLU 104 ? 1_555 64.9  ? 
2  OE1 ? D GLU 104 ? D GLU 104 ? 1_555 ZN ? S ZN . ? D ZN 999 ? 1_555 O13 ? T GEM .   ? D GEM 601 ? 1_555 146.3 ? 
3  OE2 ? D GLU 104 ? D GLU 104 ? 1_555 ZN ? S ZN . ? D ZN 999 ? 1_555 O13 ? T GEM .   ? D GEM 601 ? 1_555 94.7  ? 
4  OE1 ? D GLU 104 ? D GLU 104 ? 1_555 ZN ? S ZN . ? D ZN 999 ? 1_555 ND1 ? D HIS 217 ? D HIS 217 ? 1_555 99.4  ? 
5  OE2 ? D GLU 104 ? D GLU 104 ? 1_555 ZN ? S ZN . ? D ZN 999 ? 1_555 ND1 ? D HIS 217 ? D HIS 217 ? 1_555 163.9 ? 
6  O13 ? T GEM .   ? D GEM 601 ? 1_555 ZN ? S ZN . ? D ZN 999 ? 1_555 ND1 ? D HIS 217 ? D HIS 217 ? 1_555 100.9 ? 
7  OE1 ? D GLU 104 ? D GLU 104 ? 1_555 ZN ? S ZN . ? D ZN 999 ? 1_555 ND1 ? D HIS 101 ? D HIS 101 ? 1_555 116.7 ? 
8  OE2 ? D GLU 104 ? D GLU 104 ? 1_555 ZN ? S ZN . ? D ZN 999 ? 1_555 ND1 ? D HIS 101 ? D HIS 101 ? 1_555 96.5  ? 
9  O13 ? T GEM .   ? D GEM 601 ? 1_555 ZN ? S ZN . ? D ZN 999 ? 1_555 ND1 ? D HIS 101 ? D HIS 101 ? 1_555 90.9  ? 
10 ND1 ? D HIS 217 ? D HIS 217 ? 1_555 ZN ? S ZN . ? D ZN 999 ? 1_555 ND1 ? D HIS 101 ? D HIS 101 ? 1_555 87.3  ? 
11 OE1 ? D GLU 104 ? D GLU 104 ? 1_555 ZN ? S ZN . ? D ZN 999 ? 1_555 O12 ? T GEM .   ? D GEM 601 ? 1_555 96.9  ? 
12 OE2 ? D GLU 104 ? D GLU 104 ? 1_555 ZN ? S ZN . ? D ZN 999 ? 1_555 O12 ? T GEM .   ? D GEM 601 ? 1_555 92.5  ? 
13 O13 ? T GEM .   ? D GEM 601 ? 1_555 ZN ? S ZN . ? D ZN 999 ? 1_555 O12 ? T GEM .   ? D GEM 601 ? 1_555 55.6  ? 
14 ND1 ? D HIS 217 ? D HIS 217 ? 1_555 ZN ? S ZN . ? D ZN 999 ? 1_555 O12 ? T GEM .   ? D GEM 601 ? 1_555 93.0  ? 
15 ND1 ? D HIS 101 ? D HIS 101 ? 1_555 ZN ? S ZN . ? D ZN 999 ? 1_555 O12 ? T GEM .   ? D GEM 601 ? 1_555 145.9 ? 
16 OE1 ? A GLU 104 ? A GLU 104 ? 1_555 ZN ? F ZN . ? A ZN 999 ? 1_555 OE2 ? A GLU 104 ? A GLU 104 ? 1_555 65.4  ? 
17 OE1 ? A GLU 104 ? A GLU 104 ? 1_555 ZN ? F ZN . ? A ZN 999 ? 1_555 O13 ? G GEM .   ? A GEM 601 ? 1_555 145.8 ? 
18 OE2 ? A GLU 104 ? A GLU 104 ? 1_555 ZN ? F ZN . ? A ZN 999 ? 1_555 O13 ? G GEM .   ? A GEM 601 ? 1_555 94.8  ? 
19 OE1 ? A GLU 104 ? A GLU 104 ? 1_555 ZN ? F ZN . ? A ZN 999 ? 1_555 ND1 ? A HIS 217 ? A HIS 217 ? 1_555 92.3  ? 
20 OE2 ? A GLU 104 ? A GLU 104 ? 1_555 ZN ? F ZN . ? A ZN 999 ? 1_555 ND1 ? A HIS 217 ? A HIS 217 ? 1_555 157.7 ? 
21 O13 ? G GEM .   ? A GEM 601 ? 1_555 ZN ? F ZN . ? A ZN 999 ? 1_555 ND1 ? A HIS 217 ? A HIS 217 ? 1_555 104.2 ? 
22 OE1 ? A GLU 104 ? A GLU 104 ? 1_555 ZN ? F ZN . ? A ZN 999 ? 1_555 ND1 ? A HIS 101 ? A HIS 101 ? 1_555 113.0 ? 
23 OE2 ? A GLU 104 ? A GLU 104 ? 1_555 ZN ? F ZN . ? A ZN 999 ? 1_555 ND1 ? A HIS 101 ? A HIS 101 ? 1_555 104.7 ? 
24 O13 ? G GEM .   ? A GEM 601 ? 1_555 ZN ? F ZN . ? A ZN 999 ? 1_555 ND1 ? A HIS 101 ? A HIS 101 ? 1_555 98.5  ? 
25 ND1 ? A HIS 217 ? A HIS 217 ? 1_555 ZN ? F ZN . ? A ZN 999 ? 1_555 ND1 ? A HIS 101 ? A HIS 101 ? 1_555 84.2  ? 
26 OE1 ? A GLU 104 ? A GLU 104 ? 1_555 ZN ? F ZN . ? A ZN 999 ? 1_555 O12 ? G GEM .   ? A GEM 601 ? 1_555 97.5  ? 
27 OE2 ? A GLU 104 ? A GLU 104 ? 1_555 ZN ? F ZN . ? A ZN 999 ? 1_555 O12 ? G GEM .   ? A GEM 601 ? 1_555 95.8  ? 
28 O13 ? G GEM .   ? A GEM 601 ? 1_555 ZN ? F ZN . ? A ZN 999 ? 1_555 O12 ? G GEM .   ? A GEM 601 ? 1_555 55.1  ? 
29 ND1 ? A HIS 217 ? A HIS 217 ? 1_555 ZN ? F ZN . ? A ZN 999 ? 1_555 O12 ? G GEM .   ? A GEM 601 ? 1_555 85.9  ? 
30 ND1 ? A HIS 101 ? A HIS 101 ? 1_555 ZN ? F ZN . ? A ZN 999 ? 1_555 O12 ? G GEM .   ? A GEM 601 ? 1_555 148.2 ? 
31 OE1 ? C GLU 104 ? C GLU 104 ? 1_555 ZN ? O ZN . ? C ZN 999 ? 1_555 OE2 ? C GLU 104 ? C GLU 104 ? 1_555 65.3  ? 
32 OE1 ? C GLU 104 ? C GLU 104 ? 1_555 ZN ? O ZN . ? C ZN 999 ? 1_555 O13 ? P GEM .   ? C GEM 601 ? 1_555 140.6 ? 
33 OE2 ? C GLU 104 ? C GLU 104 ? 1_555 ZN ? O ZN . ? C ZN 999 ? 1_555 O13 ? P GEM .   ? C GEM 601 ? 1_555 93.8  ? 
34 OE1 ? C GLU 104 ? C GLU 104 ? 1_555 ZN ? O ZN . ? C ZN 999 ? 1_555 ND1 ? C HIS 101 ? C HIS 101 ? 1_555 119.8 ? 
35 OE2 ? C GLU 104 ? C GLU 104 ? 1_555 ZN ? O ZN . ? C ZN 999 ? 1_555 ND1 ? C HIS 101 ? C HIS 101 ? 1_555 104.7 ? 
36 O13 ? P GEM .   ? C GEM 601 ? 1_555 ZN ? O ZN . ? C ZN 999 ? 1_555 ND1 ? C HIS 101 ? C HIS 101 ? 1_555 97.1  ? 
37 OE1 ? C GLU 104 ? C GLU 104 ? 1_555 ZN ? O ZN . ? C ZN 999 ? 1_555 ND1 ? C HIS 217 ? C HIS 217 ? 1_555 92.8  ? 
38 OE2 ? C GLU 104 ? C GLU 104 ? 1_555 ZN ? O ZN . ? C ZN 999 ? 1_555 ND1 ? C HIS 217 ? C HIS 217 ? 1_555 158.0 ? 
39 O13 ? P GEM .   ? C GEM 601 ? 1_555 ZN ? O ZN . ? C ZN 999 ? 1_555 ND1 ? C HIS 217 ? C HIS 217 ? 1_555 102.6 ? 
40 ND1 ? C HIS 101 ? C HIS 101 ? 1_555 ZN ? O ZN . ? C ZN 999 ? 1_555 ND1 ? C HIS 217 ? C HIS 217 ? 1_555 87.8  ? 
41 OE1 ? C GLU 104 ? C GLU 104 ? 1_555 ZN ? O ZN . ? C ZN 999 ? 1_555 O12 ? P GEM .   ? C GEM 601 ? 1_555 94.1  ? 
42 OE2 ? C GLU 104 ? C GLU 104 ? 1_555 ZN ? O ZN . ? C ZN 999 ? 1_555 O12 ? P GEM .   ? C GEM 601 ? 1_555 98.2  ? 
43 O13 ? P GEM .   ? C GEM 601 ? 1_555 ZN ? O ZN . ? C ZN 999 ? 1_555 O12 ? P GEM .   ? C GEM 601 ? 1_555 54.3  ? 
44 ND1 ? C HIS 101 ? C HIS 101 ? 1_555 ZN ? O ZN . ? C ZN 999 ? 1_555 O12 ? P GEM .   ? C GEM 601 ? 1_555 144.7 ? 
45 ND1 ? C HIS 217 ? C HIS 217 ? 1_555 ZN ? O ZN . ? C ZN 999 ? 1_555 O12 ? P GEM .   ? C GEM 601 ? 1_555 80.3  ? 
46 OE1 ? B GLU 104 ? B GLU 104 ? 1_555 ZN ? L ZN . ? B ZN 999 ? 1_555 OE2 ? B GLU 104 ? B GLU 104 ? 1_555 65.2  ? 
47 OE1 ? B GLU 104 ? B GLU 104 ? 1_555 ZN ? L ZN . ? B ZN 999 ? 1_555 O13 ? M GEM .   ? B GEM 601 ? 1_555 142.2 ? 
48 OE2 ? B GLU 104 ? B GLU 104 ? 1_555 ZN ? L ZN . ? B ZN 999 ? 1_555 O13 ? M GEM .   ? B GEM 601 ? 1_555 93.9  ? 
49 OE1 ? B GLU 104 ? B GLU 104 ? 1_555 ZN ? L ZN . ? B ZN 999 ? 1_555 ND1 ? B HIS 101 ? B HIS 101 ? 1_555 116.4 ? 
50 OE2 ? B GLU 104 ? B GLU 104 ? 1_555 ZN ? L ZN . ? B ZN 999 ? 1_555 ND1 ? B HIS 101 ? B HIS 101 ? 1_555 104.1 ? 
51 O13 ? M GEM .   ? B GEM 601 ? 1_555 ZN ? L ZN . ? B ZN 999 ? 1_555 ND1 ? B HIS 101 ? B HIS 101 ? 1_555 98.5  ? 
52 OE1 ? B GLU 104 ? B GLU 104 ? 1_555 ZN ? L ZN . ? B ZN 999 ? 1_555 ND1 ? B HIS 217 ? B HIS 217 ? 1_555 92.2  ? 
53 OE2 ? B GLU 104 ? B GLU 104 ? 1_555 ZN ? L ZN . ? B ZN 999 ? 1_555 ND1 ? B HIS 217 ? B HIS 217 ? 1_555 157.0 ? 
54 O13 ? M GEM .   ? B GEM 601 ? 1_555 ZN ? L ZN . ? B ZN 999 ? 1_555 ND1 ? B HIS 217 ? B HIS 217 ? 1_555 107.6 ? 
55 ND1 ? B HIS 101 ? B HIS 101 ? 1_555 ZN ? L ZN . ? B ZN 999 ? 1_555 ND1 ? B HIS 217 ? B HIS 217 ? 1_555 81.4  ? 
56 OE1 ? B GLU 104 ? B GLU 104 ? 1_555 ZN ? L ZN . ? B ZN 999 ? 1_555 O12 ? M GEM .   ? B GEM 601 ? 1_555 102.9 ? 
57 OE2 ? B GLU 104 ? B GLU 104 ? 1_555 ZN ? L ZN . ? B ZN 999 ? 1_555 O12 ? M GEM .   ? B GEM 601 ? 1_555 114.5 ? 
58 O13 ? M GEM .   ? B GEM 601 ? 1_555 ZN ? L ZN . ? B ZN 999 ? 1_555 O12 ? M GEM .   ? B GEM 601 ? 1_555 55.7  ? 
59 ND1 ? B HIS 101 ? B HIS 101 ? 1_555 ZN ? L ZN . ? B ZN 999 ? 1_555 O12 ? M GEM .   ? B GEM 601 ? 1_555 133.6 ? 
60 ND1 ? B HIS 217 ? B HIS 217 ? 1_555 ZN ? L ZN . ? B ZN 999 ? 1_555 O12 ? M GEM .   ? B GEM 601 ? 1_555 73.2  ? 
# 
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 2010-07-28 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-11-08 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Refinement description'    
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    3 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            software 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    3 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_software.name' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.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[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1  ? refined 13.7723  -13.5882 -21.7594 0.1690 0.1171  0.1459 0.0319  0.0201  0.0151  2.4003 1.4128 2.0497  
-0.6114 -0.7253 0.6724  0.1397  0.6022  0.1664  -0.2141 -0.0229 -0.1788 -0.1993 -0.0942 -0.0000 
'X-RAY DIFFRACTION' 2  ? refined 3.4188   -14.7408 -29.1434 0.4735 0.5716  0.2068 0.0438  0.0455  0.0760  0.5235 0.1139 0.1243  
-0.1814 -0.2225 0.0971  -0.1150 0.0103  0.0000  -0.0728 -0.0656 -0.0732 -0.0598 0.0379  -0.0036 
'X-RAY DIFFRACTION' 3  ? refined 2.8757   -7.1633  2.5295   0.1740 -0.0345 0.2437 0.0154  0.0467  -0.0348 1.0465 0.9174 1.5099  
-0.5736 0.4857  0.2982  -0.0034 -0.2154 0.1794  0.1316  0.0286  0.1616  0.0224  -0.2275 -0.0000 
'X-RAY DIFFRACTION' 4  ? refined 15.1905  -46.2737 -0.7561  0.0797 0.1092  0.1681 0.0110  0.0302  0.0041  1.8663 1.3650 1.4155  
-0.0789 0.0646  -0.2728 -0.0467 0.2216  -0.2504 0.0035  0.0957  0.3161  0.1017  -0.2255 0.0001  
'X-RAY DIFFRACTION' 5  ? refined 21.7399  -26.0133 16.7833  0.2846 0.1788  0.1606 0.0713  0.0167  -0.0201 0.7249 0.7999 0.8674  
-0.3646 -0.0487 0.3807  -0.0918 -0.4030 0.2543  0.2214  0.1042  -0.0919 -0.1864 0.0255  0.0003  
'X-RAY DIFFRACTION' 6  ? refined 26.3924  -51.3109 -3.6543  0.3133 0.2116  0.3568 -0.0279 0.0863  -0.1480 0.2528 0.0430 0.2311  
0.0454  0.1867  0.0229  -0.0012 -0.0232 -0.1307 -0.0537 -0.0340 0.1084  0.0367  0.0162  0.0001  
'X-RAY DIFFRACTION' 7  ? refined -7.8690  22.7790  26.8777  0.1013 0.1277  0.0676 0.0164  -0.0166 0.0541  1.4753 1.2373 2.5107  
0.0404  0.1713  -0.2395 0.0484  -0.3929 -0.0761 -0.0214 -0.0126 -0.0207 0.2758  0.0613  0.0000  
'X-RAY DIFFRACTION' 8  ? refined 1.9639   47.9449  23.0751  0.2293 0.3720  0.2722 -0.0572 0.0308  -0.0894 0.7328 0.9176 0.6130  
-0.1466 0.3826  -0.4524 -0.0169 -0.6435 0.4276  -0.0448 -0.0308 -0.2660 -0.2678 0.2394  0.0005  
'X-RAY DIFFRACTION' 9  ? refined 2.3509   15.9803  29.1542  0.4448 0.3250  0.6015 -0.0480 0.0748  0.1082  0.7412 0.3954 0.1425  
0.4311  0.2424  0.2343  0.1017  -0.1037 -0.0310 -0.0031 0.1314  0.1166  -0.0432 0.1044  0.0020  
'X-RAY DIFFRACTION' 10 ? refined -9.4850  27.6366  -11.6120 0.1013 0.1903  0.1018 0.0459  -0.0146 0.0380  1.9764 1.3720 2.1297  
0.1492  -0.2783 0.1763  -0.0641 0.3792  -0.0536 -0.1054 0.0396  -0.0064 0.0193  0.2669  0.0000  
'X-RAY DIFFRACTION' 11 ? refined -16.7079 51.8684  -0.1554  0.3467 0.1344  0.4642 0.0657  0.0472  0.0530  0.7244 0.8872 0.7688  
0.0521  0.7242  0.2503  0.0690  -0.0099 0.4375  0.0425  -0.0390 0.4364  -0.3400 -0.2378 -0.0003 
'X-RAY DIFFRACTION' 12 ? refined -21.0044 22.8362  -14.9256 0.2846 0.4692  0.3074 -0.0503 0.0082  0.1562  0.0144 0.0592 0.0188  
0.0292  -0.0165 -0.0334 0.0664  0.1185  0.0227  -0.0696 0.1540  0.0741  0.0431  0.0172  0.0026  
'X-RAY DIFFRACTION' 13 ? refined 1.7223   1.2015   0.0132   0.1497 0.2118  0.1642 -0.0287 0.0395  -0.0113 0.1419 0.2586 -0.0038 
-0.1642 -0.0517 0.0607  -0.0207 -0.0414 0.0049  0.0218  0.0413  0.0692  -0.0111 0.0702  -0.0000 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1  1  ? ? ? ? ? ? ? ? ? 'chain A and (resid 29:182 or resid 191:336' 
'X-RAY DIFFRACTION' 2  2  ? ? ? ? ? ? ? ? ? 'chain A and resid 601' 
'X-RAY DIFFRACTION' 3  3  ? ? ? ? ? ? ? ? ? 'chain A and resid 337:419' 
'X-RAY DIFFRACTION' 4  4  ? ? ? ? ? ? ? ? ? 'chain B and (resid 28:184 or resid 192:336' 
'X-RAY DIFFRACTION' 5  5  ? ? ? ? ? ? ? ? ? 'chain B and resid 337:420' 
'X-RAY DIFFRACTION' 6  6  ? ? ? ? ? ? ? ? ? 'chain B and resid 601' 
'X-RAY DIFFRACTION' 7  7  ? ? ? ? ? ? ? ? ? 'chain C and (resid 30:183 or resid 189:336' 
'X-RAY DIFFRACTION' 8  8  ? ? ? ? ? ? ? ? ? 'chain C and resid 337:419' 
'X-RAY DIFFRACTION' 9  9  ? ? ? ? ? ? ? ? ? 'chain C and resid 601' 
'X-RAY DIFFRACTION' 10 10 ? ? ? ? ? ? ? ? ? 'chain D and (resid 27:181 or resid 191:336' 
'X-RAY DIFFRACTION' 11 11 ? ? ? ? ? ? ? ? ? 'chain D and resid 337:420' 
'X-RAY DIFFRACTION' 12 12 ? ? ? ? ? ? ? ? ? 'chain D and resid 601' 
'X-RAY DIFFRACTION' 13 13 ? ? ? ? ? ? ? ? ? 
'(chain A and resid 1001:1050)  or (chain B and resid 1001:1054) or (chain C and resid 1001:1051) or (chain D and resid 1001:1056)' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
ProDC  'data collection' .                 ? 1 
PHASER phasing           .                 ? 2 
PHENIX refinement        '(phenix.refine)' ? 3 
XDS    'data reduction'  .                 ? 4 
SCALA  'data scaling'    .                 ? 5 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 ND2 A ASN 133 ? ? C2 A NAG 501 ? ? 2.10 
2 1 ND2 B ASN 133 ? ? C2 B NAG 501 ? ? 2.11 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 401 ? ? CZ A ARG 401 ? ? NH2 A ARG 401 ? ? 117.26 120.30 -3.04 0.50 N 
2 1 NE B ARG 175 ? ? CZ B ARG 175 ? ? NH1 B ARG 175 ? ? 123.33 120.30 3.03  0.50 N 
3 1 NE B ARG 175 ? ? CZ B ARG 175 ? ? NH2 B ARG 175 ? ? 116.86 120.30 -3.44 0.50 N 
4 1 C  D LEU 159 ? ? N  D PRO 160 ? ? CA  D PRO 160 ? ? 131.73 119.30 12.43 1.50 Y 
# 
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 GLU A 32  ? ? -109.41 42.66   
2  1 PHE A 34  ? ? -52.40  -1.93   
3  1 GLN A 37  ? ? -169.16 67.29   
4  1 SER A 86  ? ? -127.43 -157.67 
5  1 ASN A 161 ? ? 70.32   -2.37   
6  1 ASN A 167 ? ? -76.33  -158.74 
7  1 GLN A 192 ? ? -6.17   -152.56 
8  1 SER A 193 ? ? 80.28   28.71   
9  1 ARG A 194 ? ? -86.91  -157.00 
10 1 SER A 240 ? ? -118.34 74.42   
11 1 ASP A 244 ? ? -96.54  36.96   
12 1 TRP A 282 ? ? -57.97  -76.10  
13 1 ALA A 335 ? ? -69.94  7.26    
14 1 ASP A 345 ? ? -57.04  171.01  
15 1 SER A 347 ? ? -59.32  -4.63   
16 1 LYS A 364 ? ? -119.44 77.99   
17 1 ASN A 404 ? ? -101.09 55.99   
18 1 LEU A 412 ? ? -167.27 111.05  
19 1 GLU B 32  ? ? -116.90 66.19   
20 1 GLN B 37  ? ? 40.98   81.03   
21 1 SER B 86  ? ? -130.05 -153.67 
22 1 ASN B 161 ? ? 86.60   -7.61   
23 1 ASN B 167 ? ? -72.99  -154.90 
24 1 ARG B 194 ? ? -100.02 -148.33 
25 1 PRO B 209 ? ? -74.36  42.77   
26 1 PHE B 210 ? ? -38.88  130.37  
27 1 ASP B 244 ? ? -99.90  41.94   
28 1 CYS B 268 ? ? 38.12   41.16   
29 1 TRP B 282 ? ? -60.10  -73.78  
30 1 SER B 395 ? ? -45.83  159.15  
31 1 ASN B 404 ? ? -97.94  37.35   
32 1 GLN C 37  ? ? 53.47   72.89   
33 1 SER C 86  ? ? -133.29 -156.98 
34 1 ASN C 167 ? ? -74.55  -153.80 
35 1 GLU C 182 ? ? 60.02   172.14  
36 1 ALA C 191 ? ? -152.64 -125.72 
37 1 GLN C 192 ? ? 61.93   -139.56 
38 1 PRO C 209 ? ? -69.56  52.94   
39 1 CYS C 268 ? ? 39.18   41.53   
40 1 TRP C 282 ? ? -60.35  -71.10  
41 1 SER C 395 ? ? -43.35  159.15  
42 1 ASN C 404 ? ? -100.06 68.04   
43 1 LEU C 412 ? ? -165.59 112.96  
44 1 GLN D 37  ? ? 53.75   70.07   
45 1 SER D 86  ? ? -129.06 -153.44 
46 1 PRO D 160 ? ? -16.07  -56.35  
47 1 ASN D 167 ? ? -73.33  -158.30 
48 1 GLN D 192 ? ? 173.66  -143.60 
49 1 SER D 193 ? ? -85.18  36.34   
50 1 SER D 240 ? ? -107.63 79.87   
51 1 ASP D 244 ? ? -98.27  37.62   
52 1 ARG D 263 ? ? -47.90  -18.90  
53 1 TRP D 282 ? ? -54.65  -76.25  
54 1 ASN D 404 ? ? -103.89 58.41   
55 1 LEU D 412 ? ? -161.52 112.54  
# 
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 MET 1   ? A MET 1   
2   1 Y 1 A PRO 2   ? A PRO 2   
3   1 Y 1 A THR 3   ? A THR 3   
4   1 Y 1 A LEU 4   ? A LEU 4   
5   1 Y 1 A GLY 5   ? A GLY 5   
6   1 Y 1 A LEU 6   ? A LEU 6   
7   1 Y 1 A LEU 7   ? A LEU 7   
8   1 Y 1 A PHE 8   ? A PHE 8   
9   1 Y 1 A ALA 9   ? A ALA 9   
10  1 Y 1 A SER 10  ? A SER 10  
11  1 Y 1 A ILE 11  ? A ILE 11  
12  1 Y 1 A GLY 12  ? A GLY 12  
13  1 Y 1 A ILE 13  ? A ILE 13  
14  1 Y 1 A ALA 14  ? A ALA 14  
15  1 Y 1 A VAL 15  ? A VAL 15  
16  1 Y 1 A LEU 16  ? A LEU 16  
17  1 Y 1 A ALA 17  ? A ALA 17  
18  1 Y 1 A MET 18  ? A MET 18  
19  1 Y 1 A GLY 19  ? A GLY 19  
20  1 Y 1 A VAL 20  ? A VAL 20  
21  1 Y 1 A PRO 21  ? A PRO 21  
22  1 Y 1 A HIS 22  ? A HIS 22  
23  1 Y 1 A CYS 23  ? A CYS 23  
24  1 Y 1 A ARG 24  ? A ARG 24  
25  1 Y 1 A GLY 25  ? A GLY 25  
26  1 Y 1 A TYR 26  ? A TYR 26  
27  1 Y 1 A THR 27  ? A THR 27  
28  1 Y 1 A ILE 28  ? A ILE 28  
29  1 Y 1 A GLN 183 ? A GLN 183 
30  1 Y 1 A SER 184 ? A SER 184 
31  1 Y 1 A HIS 185 ? A HIS 185 
32  1 Y 1 A VAL 186 ? A VAL 186 
33  1 Y 1 A HIS 187 ? A HIS 187 
34  1 Y 1 A GLN 188 ? A GLN 188 
35  1 Y 1 A LEU 189 ? A LEU 189 
36  1 Y 1 A ARG 190 ? A ARG 190 
37  1 Y 1 A GLU 420 ? A GLU 420 
38  1 Y 1 A THR 421 ? A THR 421 
39  1 Y 1 A ASN 422 ? A ASN 422 
40  1 Y 1 A PHE 423 ? A PHE 423 
41  1 Y 1 A ASP 424 ? A ASP 424 
42  1 Y 1 A GLY 425 ? A GLY 425 
43  1 Y 1 A ILE 426 ? A ILE 426 
44  1 Y 1 A SER 427 ? A SER 427 
45  1 Y 1 A SER 428 ? A SER 428 
46  1 Y 1 A PHE 429 ? A PHE 429 
47  1 Y 1 A TYR 430 ? A TYR 430 
48  1 Y 1 A SER 431 ? A SER 431 
49  1 Y 1 A PRO 432 ? A PRO 432 
50  1 Y 1 A TYR 433 ? A TYR 433 
51  1 Y 1 A TYR 434 ? A TYR 434 
52  1 Y 1 A PHE 435 ? A PHE 435 
53  1 Y 1 B MET 1   ? B MET 1   
54  1 Y 1 B PRO 2   ? B PRO 2   
55  1 Y 1 B THR 3   ? B THR 3   
56  1 Y 1 B LEU 4   ? B LEU 4   
57  1 Y 1 B GLY 5   ? B GLY 5   
58  1 Y 1 B LEU 6   ? B LEU 6   
59  1 Y 1 B LEU 7   ? B LEU 7   
60  1 Y 1 B PHE 8   ? B PHE 8   
61  1 Y 1 B ALA 9   ? B ALA 9   
62  1 Y 1 B SER 10  ? B SER 10  
63  1 Y 1 B ILE 11  ? B ILE 11  
64  1 Y 1 B GLY 12  ? B GLY 12  
65  1 Y 1 B ILE 13  ? B ILE 13  
66  1 Y 1 B ALA 14  ? B ALA 14  
67  1 Y 1 B VAL 15  ? B VAL 15  
68  1 Y 1 B LEU 16  ? B LEU 16  
69  1 Y 1 B ALA 17  ? B ALA 17  
70  1 Y 1 B MET 18  ? B MET 18  
71  1 Y 1 B GLY 19  ? B GLY 19  
72  1 Y 1 B VAL 20  ? B VAL 20  
73  1 Y 1 B PRO 21  ? B PRO 21  
74  1 Y 1 B HIS 22  ? B HIS 22  
75  1 Y 1 B CYS 23  ? B CYS 23  
76  1 Y 1 B ARG 24  ? B ARG 24  
77  1 Y 1 B GLY 25  ? B GLY 25  
78  1 Y 1 B TYR 26  ? B TYR 26  
79  1 Y 1 B THR 27  ? B THR 27  
80  1 Y 1 B HIS 185 ? B HIS 185 
81  1 Y 1 B VAL 186 ? B VAL 186 
82  1 Y 1 B HIS 187 ? B HIS 187 
83  1 Y 1 B GLN 188 ? B GLN 188 
84  1 Y 1 B LEU 189 ? B LEU 189 
85  1 Y 1 B ARG 190 ? B ARG 190 
86  1 Y 1 B ALA 191 ? B ALA 191 
87  1 Y 1 B THR 421 ? B THR 421 
88  1 Y 1 B ASN 422 ? B ASN 422 
89  1 Y 1 B PHE 423 ? B PHE 423 
90  1 Y 1 B ASP 424 ? B ASP 424 
91  1 Y 1 B GLY 425 ? B GLY 425 
92  1 Y 1 B ILE 426 ? B ILE 426 
93  1 Y 1 B SER 427 ? B SER 427 
94  1 Y 1 B SER 428 ? B SER 428 
95  1 Y 1 B PHE 429 ? B PHE 429 
96  1 Y 1 B TYR 430 ? B TYR 430 
97  1 Y 1 B SER 431 ? B SER 431 
98  1 Y 1 B PRO 432 ? B PRO 432 
99  1 Y 1 B TYR 433 ? B TYR 433 
100 1 Y 1 B TYR 434 ? B TYR 434 
101 1 Y 1 B PHE 435 ? B PHE 435 
102 1 Y 1 C MET 1   ? C MET 1   
103 1 Y 1 C PRO 2   ? C PRO 2   
104 1 Y 1 C THR 3   ? C THR 3   
105 1 Y 1 C LEU 4   ? C LEU 4   
106 1 Y 1 C GLY 5   ? C GLY 5   
107 1 Y 1 C LEU 6   ? C LEU 6   
108 1 Y 1 C LEU 7   ? C LEU 7   
109 1 Y 1 C PHE 8   ? C PHE 8   
110 1 Y 1 C ALA 9   ? C ALA 9   
111 1 Y 1 C SER 10  ? C SER 10  
112 1 Y 1 C ILE 11  ? C ILE 11  
113 1 Y 1 C GLY 12  ? C GLY 12  
114 1 Y 1 C ILE 13  ? C ILE 13  
115 1 Y 1 C ALA 14  ? C ALA 14  
116 1 Y 1 C VAL 15  ? C VAL 15  
117 1 Y 1 C LEU 16  ? C LEU 16  
118 1 Y 1 C ALA 17  ? C ALA 17  
119 1 Y 1 C MET 18  ? C MET 18  
120 1 Y 1 C GLY 19  ? C GLY 19  
121 1 Y 1 C VAL 20  ? C VAL 20  
122 1 Y 1 C PRO 21  ? C PRO 21  
123 1 Y 1 C HIS 22  ? C HIS 22  
124 1 Y 1 C CYS 23  ? C CYS 23  
125 1 Y 1 C ARG 24  ? C ARG 24  
126 1 Y 1 C GLY 25  ? C GLY 25  
127 1 Y 1 C TYR 26  ? C TYR 26  
128 1 Y 1 C THR 27  ? C THR 27  
129 1 Y 1 C ILE 28  ? C ILE 28  
130 1 Y 1 C LYS 29  ? C LYS 29  
131 1 Y 1 C SER 184 ? C SER 184 
132 1 Y 1 C HIS 185 ? C HIS 185 
133 1 Y 1 C VAL 186 ? C VAL 186 
134 1 Y 1 C HIS 187 ? C HIS 187 
135 1 Y 1 C GLN 188 ? C GLN 188 
136 1 Y 1 C GLU 420 ? C GLU 420 
137 1 Y 1 C THR 421 ? C THR 421 
138 1 Y 1 C ASN 422 ? C ASN 422 
139 1 Y 1 C PHE 423 ? C PHE 423 
140 1 Y 1 C ASP 424 ? C ASP 424 
141 1 Y 1 C GLY 425 ? C GLY 425 
142 1 Y 1 C ILE 426 ? C ILE 426 
143 1 Y 1 C SER 427 ? C SER 427 
144 1 Y 1 C SER 428 ? C SER 428 
145 1 Y 1 C PHE 429 ? C PHE 429 
146 1 Y 1 C TYR 430 ? C TYR 430 
147 1 Y 1 C SER 431 ? C SER 431 
148 1 Y 1 C PRO 432 ? C PRO 432 
149 1 Y 1 C TYR 433 ? C TYR 433 
150 1 Y 1 C TYR 434 ? C TYR 434 
151 1 Y 1 C PHE 435 ? C PHE 435 
152 1 Y 1 D MET 1   ? D MET 1   
153 1 Y 1 D PRO 2   ? D PRO 2   
154 1 Y 1 D THR 3   ? D THR 3   
155 1 Y 1 D LEU 4   ? D LEU 4   
156 1 Y 1 D GLY 5   ? D GLY 5   
157 1 Y 1 D LEU 6   ? D LEU 6   
158 1 Y 1 D LEU 7   ? D LEU 7   
159 1 Y 1 D PHE 8   ? D PHE 8   
160 1 Y 1 D ALA 9   ? D ALA 9   
161 1 Y 1 D SER 10  ? D SER 10  
162 1 Y 1 D ILE 11  ? D ILE 11  
163 1 Y 1 D GLY 12  ? D GLY 12  
164 1 Y 1 D ILE 13  ? D ILE 13  
165 1 Y 1 D ALA 14  ? D ALA 14  
166 1 Y 1 D VAL 15  ? D VAL 15  
167 1 Y 1 D LEU 16  ? D LEU 16  
168 1 Y 1 D ALA 17  ? D ALA 17  
169 1 Y 1 D MET 18  ? D MET 18  
170 1 Y 1 D GLY 19  ? D GLY 19  
171 1 Y 1 D VAL 20  ? D VAL 20  
172 1 Y 1 D PRO 21  ? D PRO 21  
173 1 Y 1 D HIS 22  ? D HIS 22  
174 1 Y 1 D CYS 23  ? D CYS 23  
175 1 Y 1 D ARG 24  ? D ARG 24  
176 1 Y 1 D GLY 25  ? D GLY 25  
177 1 Y 1 D TYR 26  ? D TYR 26  
178 1 Y 1 D GLU 182 ? D GLU 182 
179 1 Y 1 D GLN 183 ? D GLN 183 
180 1 Y 1 D SER 184 ? D SER 184 
181 1 Y 1 D HIS 185 ? D HIS 185 
182 1 Y 1 D VAL 186 ? D VAL 186 
183 1 Y 1 D HIS 187 ? D HIS 187 
184 1 Y 1 D GLN 188 ? D GLN 188 
185 1 Y 1 D LEU 189 ? D LEU 189 
186 1 Y 1 D ARG 190 ? D ARG 190 
187 1 Y 1 D THR 421 ? D THR 421 
188 1 Y 1 D ASN 422 ? D ASN 422 
189 1 Y 1 D PHE 423 ? D PHE 423 
190 1 Y 1 D ASP 424 ? D ASP 424 
191 1 Y 1 D GLY 425 ? D GLY 425 
192 1 Y 1 D ILE 426 ? D ILE 426 
193 1 Y 1 D SER 427 ? D SER 427 
194 1 Y 1 D SER 428 ? D SER 428 
195 1 Y 1 D PHE 429 ? D PHE 429 
196 1 Y 1 D TYR 430 ? D TYR 430 
197 1 Y 1 D SER 431 ? D SER 431 
198 1 Y 1 D PRO 432 ? D PRO 432 
199 1 Y 1 D TYR 433 ? D TYR 433 
200 1 Y 1 D TYR 434 ? D TYR 434 
201 1 Y 1 D PHE 435 ? D PHE 435 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE                    NAG 
3 'ZINC ION'                                ZN  
4 '(2-GUANIDINOETHYLMERCAPTO)SUCCINIC ACID' GEM 
5 GLYCEROL                                  GOL 
6 water                                     HOH 
# 
