data_8ZVL
# 
_entry.id   8ZVL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8ZVL         pdb_00008zvl 10.2210/pdb8zvl/pdb 
WWPDB D_1300048621 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-18 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZVL 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yl521gl@ustc.edu.cn 
_pdbx_contact_author.name_first         Lin 
_pdbx_contact_author.name_last          Yang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1550-6947 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yang, L.Y.' 1 0000-0003-1550-6947 
'Fang, Y.J.' 2 0009-0009-0272-0830 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'human citrate synthases complexed with oxaloacetate' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yang, L.Y.' 1 0000-0003-1550-6947 
primary 'Fang, Y.J.' 2 0009-0009-0272-0830 
# 
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 'Citrate synthase, mitochondrial' 48761.727 4   2.3.3.1 ? ? ? 
2 non-polymer syn 'OXALOACETATE ION'                131.064   3   ?       ? ? ? 
3 water       nat water                             18.015    555 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Citrate (Si)-synthase' 
# 
_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       
;STNLKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAK
GGEEPLPEGLFWLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAQGI
SRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNFTNMLGYTDHQFTELTRLYLTIHSDHEGGN
VSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAV
LRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA
LGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDSK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;STNLKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAK
GGEEPLPEGLFWLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAQGI
SRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNFTNMLGYTDHQFTELTRLYLTIHSDHEGGN
VSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAV
LRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA
LGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDSK
;
_entity_poly.pdbx_strand_id                 A,D,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'OXALOACETATE ION' OAA 
3 water              HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   THR n 
1 3   ASN n 
1 4   LEU n 
1 5   LYS n 
1 6   ASP n 
1 7   ILE n 
1 8   LEU n 
1 9   ALA n 
1 10  ASP n 
1 11  LEU n 
1 12  ILE n 
1 13  PRO n 
1 14  LYS n 
1 15  GLU n 
1 16  GLN n 
1 17  ALA n 
1 18  ARG n 
1 19  ILE n 
1 20  LYS n 
1 21  THR n 
1 22  PHE n 
1 23  ARG n 
1 24  GLN n 
1 25  GLN n 
1 26  HIS n 
1 27  GLY n 
1 28  LYS n 
1 29  THR n 
1 30  VAL n 
1 31  VAL n 
1 32  GLY n 
1 33  GLN n 
1 34  ILE n 
1 35  THR n 
1 36  VAL n 
1 37  ASP n 
1 38  MET n 
1 39  MET n 
1 40  TYR n 
1 41  GLY n 
1 42  GLY n 
1 43  MET n 
1 44  ARG n 
1 45  GLY n 
1 46  MET n 
1 47  LYS n 
1 48  GLY n 
1 49  LEU n 
1 50  VAL n 
1 51  TYR n 
1 52  GLU n 
1 53  THR n 
1 54  SER n 
1 55  VAL n 
1 56  LEU n 
1 57  ASP n 
1 58  PRO n 
1 59  ASP n 
1 60  GLU n 
1 61  GLY n 
1 62  ILE n 
1 63  ARG n 
1 64  PHE n 
1 65  ARG n 
1 66  GLY n 
1 67  PHE n 
1 68  SER n 
1 69  ILE n 
1 70  PRO n 
1 71  GLU n 
1 72  CYS n 
1 73  GLN n 
1 74  LYS n 
1 75  LEU n 
1 76  LEU n 
1 77  PRO n 
1 78  LYS n 
1 79  ALA n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  GLU n 
1 84  GLU n 
1 85  PRO n 
1 86  LEU n 
1 87  PRO n 
1 88  GLU n 
1 89  GLY n 
1 90  LEU n 
1 91  PHE n 
1 92  TRP n 
1 93  LEU n 
1 94  LEU n 
1 95  VAL n 
1 96  THR n 
1 97  GLY n 
1 98  HIS n 
1 99  ILE n 
1 100 PRO n 
1 101 THR n 
1 102 GLU n 
1 103 GLU n 
1 104 GLN n 
1 105 VAL n 
1 106 SER n 
1 107 TRP n 
1 108 LEU n 
1 109 SER n 
1 110 LYS n 
1 111 GLU n 
1 112 TRP n 
1 113 ALA n 
1 114 LYS n 
1 115 ARG n 
1 116 ALA n 
1 117 ALA n 
1 118 LEU n 
1 119 PRO n 
1 120 SER n 
1 121 HIS n 
1 122 VAL n 
1 123 VAL n 
1 124 THR n 
1 125 MET n 
1 126 LEU n 
1 127 ASP n 
1 128 ASN n 
1 129 PHE n 
1 130 PRO n 
1 131 THR n 
1 132 ASN n 
1 133 LEU n 
1 134 HIS n 
1 135 PRO n 
1 136 MET n 
1 137 SER n 
1 138 GLN n 
1 139 LEU n 
1 140 SER n 
1 141 ALA n 
1 142 ALA n 
1 143 VAL n 
1 144 THR n 
1 145 ALA n 
1 146 LEU n 
1 147 ASN n 
1 148 SER n 
1 149 GLU n 
1 150 SER n 
1 151 ASN n 
1 152 PHE n 
1 153 ALA n 
1 154 ARG n 
1 155 ALA n 
1 156 TYR n 
1 157 ALA n 
1 158 GLN n 
1 159 GLY n 
1 160 ILE n 
1 161 SER n 
1 162 ARG n 
1 163 THR n 
1 164 LYS n 
1 165 TYR n 
1 166 TRP n 
1 167 GLU n 
1 168 LEU n 
1 169 ILE n 
1 170 TYR n 
1 171 GLU n 
1 172 ASP n 
1 173 SER n 
1 174 MET n 
1 175 ASP n 
1 176 LEU n 
1 177 ILE n 
1 178 ALA n 
1 179 LYS n 
1 180 LEU n 
1 181 PRO n 
1 182 CYS n 
1 183 VAL n 
1 184 ALA n 
1 185 ALA n 
1 186 LYS n 
1 187 ILE n 
1 188 TYR n 
1 189 ARG n 
1 190 ASN n 
1 191 LEU n 
1 192 TYR n 
1 193 ARG n 
1 194 GLU n 
1 195 GLY n 
1 196 SER n 
1 197 GLY n 
1 198 ILE n 
1 199 GLY n 
1 200 ALA n 
1 201 ILE n 
1 202 ASP n 
1 203 SER n 
1 204 ASN n 
1 205 LEU n 
1 206 ASP n 
1 207 TRP n 
1 208 SER n 
1 209 HIS n 
1 210 ASN n 
1 211 PHE n 
1 212 THR n 
1 213 ASN n 
1 214 MET n 
1 215 LEU n 
1 216 GLY n 
1 217 TYR n 
1 218 THR n 
1 219 ASP n 
1 220 HIS n 
1 221 GLN n 
1 222 PHE n 
1 223 THR n 
1 224 GLU n 
1 225 LEU n 
1 226 THR n 
1 227 ARG n 
1 228 LEU n 
1 229 TYR n 
1 230 LEU n 
1 231 THR n 
1 232 ILE n 
1 233 HIS n 
1 234 SER n 
1 235 ASP n 
1 236 HIS n 
1 237 GLU n 
1 238 GLY n 
1 239 GLY n 
1 240 ASN n 
1 241 VAL n 
1 242 SER n 
1 243 ALA n 
1 244 HIS n 
1 245 THR n 
1 246 SER n 
1 247 HIS n 
1 248 LEU n 
1 249 VAL n 
1 250 GLY n 
1 251 SER n 
1 252 ALA n 
1 253 LEU n 
1 254 SER n 
1 255 ASP n 
1 256 PRO n 
1 257 TYR n 
1 258 LEU n 
1 259 SER n 
1 260 PHE n 
1 261 ALA n 
1 262 ALA n 
1 263 ALA n 
1 264 MET n 
1 265 ASN n 
1 266 GLY n 
1 267 LEU n 
1 268 ALA n 
1 269 GLY n 
1 270 PRO n 
1 271 LEU n 
1 272 HIS n 
1 273 GLY n 
1 274 LEU n 
1 275 ALA n 
1 276 ASN n 
1 277 GLN n 
1 278 GLU n 
1 279 VAL n 
1 280 LEU n 
1 281 VAL n 
1 282 TRP n 
1 283 LEU n 
1 284 THR n 
1 285 GLN n 
1 286 LEU n 
1 287 GLN n 
1 288 LYS n 
1 289 GLU n 
1 290 VAL n 
1 291 GLY n 
1 292 LYS n 
1 293 ASP n 
1 294 VAL n 
1 295 SER n 
1 296 ASP n 
1 297 GLU n 
1 298 LYS n 
1 299 LEU n 
1 300 ARG n 
1 301 ASP n 
1 302 TYR n 
1 303 ILE n 
1 304 TRP n 
1 305 ASN n 
1 306 THR n 
1 307 LEU n 
1 308 ASN n 
1 309 SER n 
1 310 GLY n 
1 311 ARG n 
1 312 VAL n 
1 313 VAL n 
1 314 PRO n 
1 315 GLY n 
1 316 TYR n 
1 317 GLY n 
1 318 HIS n 
1 319 ALA n 
1 320 VAL n 
1 321 LEU n 
1 322 ARG n 
1 323 LYS n 
1 324 THR n 
1 325 ASP n 
1 326 PRO n 
1 327 ARG n 
1 328 TYR n 
1 329 THR n 
1 330 CYS n 
1 331 GLN n 
1 332 ARG n 
1 333 GLU n 
1 334 PHE n 
1 335 ALA n 
1 336 LEU n 
1 337 LYS n 
1 338 HIS n 
1 339 LEU n 
1 340 PRO n 
1 341 ASN n 
1 342 ASP n 
1 343 PRO n 
1 344 MET n 
1 345 PHE n 
1 346 LYS n 
1 347 LEU n 
1 348 VAL n 
1 349 ALA n 
1 350 GLN n 
1 351 LEU n 
1 352 TYR n 
1 353 LYS n 
1 354 ILE n 
1 355 VAL n 
1 356 PRO n 
1 357 ASN n 
1 358 VAL n 
1 359 LEU n 
1 360 LEU n 
1 361 GLU n 
1 362 GLN n 
1 363 GLY n 
1 364 LYS n 
1 365 ALA n 
1 366 LYS n 
1 367 ASN n 
1 368 PRO n 
1 369 TRP n 
1 370 PRO n 
1 371 ASN n 
1 372 VAL n 
1 373 ASP n 
1 374 ALA n 
1 375 HIS n 
1 376 SER n 
1 377 GLY n 
1 378 VAL n 
1 379 LEU n 
1 380 LEU n 
1 381 GLN n 
1 382 TYR n 
1 383 TYR n 
1 384 GLY n 
1 385 MET n 
1 386 THR n 
1 387 GLU n 
1 388 MET n 
1 389 ASN n 
1 390 TYR n 
1 391 TYR n 
1 392 THR n 
1 393 VAL n 
1 394 LEU n 
1 395 PHE n 
1 396 GLY n 
1 397 VAL n 
1 398 SER n 
1 399 ARG n 
1 400 ALA n 
1 401 LEU n 
1 402 GLY n 
1 403 VAL n 
1 404 LEU n 
1 405 ALA n 
1 406 GLN n 
1 407 LEU n 
1 408 ILE n 
1 409 TRP n 
1 410 SER n 
1 411 ARG n 
1 412 ALA n 
1 413 LEU n 
1 414 GLY n 
1 415 PHE n 
1 416 PRO n 
1 417 LEU n 
1 418 GLU n 
1 419 ARG n 
1 420 PRO n 
1 421 LYS n 
1 422 SER n 
1 423 MET n 
1 424 SER n 
1 425 THR n 
1 426 GLU n 
1 427 GLY n 
1 428 LEU n 
1 429 MET n 
1 430 LYS n 
1 431 PHE n 
1 432 VAL n 
1 433 ASP n 
1 434 SER n 
1 435 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   435 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CS 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
GLN 'L-peptide linking' y GLUTAMINE          ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'    ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE            ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE          ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER              ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE         ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE            ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE             ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE         ? 'C5 H11 N O2 S'  149.211 
OAA non-polymer         . 'OXALOACETATE ION' ? 'C4 H3 O5 -1'    131.064 
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 
# 
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   SER 1   30  30  SER SER A . n 
A 1 2   THR 2   31  31  THR THR A . n 
A 1 3   ASN 3   32  32  ASN ASN A . n 
A 1 4   LEU 4   33  33  LEU LEU A . n 
A 1 5   LYS 5   34  34  LYS LYS A . n 
A 1 6   ASP 6   35  35  ASP ASP A . n 
A 1 7   ILE 7   36  36  ILE ILE A . n 
A 1 8   LEU 8   37  37  LEU LEU A . n 
A 1 9   ALA 9   38  38  ALA ALA A . n 
A 1 10  ASP 10  39  39  ASP ASP A . n 
A 1 11  LEU 11  40  40  LEU LEU A . n 
A 1 12  ILE 12  41  41  ILE ILE A . n 
A 1 13  PRO 13  42  42  PRO PRO A . n 
A 1 14  LYS 14  43  43  LYS LYS A . n 
A 1 15  GLU 15  44  44  GLU GLU A . n 
A 1 16  GLN 16  45  45  GLN GLN A . n 
A 1 17  ALA 17  46  46  ALA ALA A . n 
A 1 18  ARG 18  47  47  ARG ARG A . n 
A 1 19  ILE 19  48  48  ILE ILE A . n 
A 1 20  LYS 20  49  49  LYS LYS A . n 
A 1 21  THR 21  50  50  THR THR A . n 
A 1 22  PHE 22  51  51  PHE PHE A . n 
A 1 23  ARG 23  52  52  ARG ARG A . n 
A 1 24  GLN 24  53  53  GLN GLN A . n 
A 1 25  GLN 25  54  54  GLN GLN A . n 
A 1 26  HIS 26  55  55  HIS HIS A . n 
A 1 27  GLY 27  56  56  GLY GLY A . n 
A 1 28  LYS 28  57  57  LYS LYS A . n 
A 1 29  THR 29  58  58  THR THR A . n 
A 1 30  VAL 30  59  59  VAL VAL A . n 
A 1 31  VAL 31  60  60  VAL VAL A . n 
A 1 32  GLY 32  61  61  GLY GLY A . n 
A 1 33  GLN 33  62  62  GLN GLN A . n 
A 1 34  ILE 34  63  63  ILE ILE A . n 
A 1 35  THR 35  64  64  THR THR A . n 
A 1 36  VAL 36  65  65  VAL VAL A . n 
A 1 37  ASP 37  66  66  ASP ASP A . n 
A 1 38  MET 38  67  67  MET MET A . n 
A 1 39  MET 39  68  68  MET MET A . n 
A 1 40  TYR 40  69  69  TYR TYR A . n 
A 1 41  GLY 41  70  70  GLY GLY A . n 
A 1 42  GLY 42  71  71  GLY GLY A . n 
A 1 43  MET 43  72  72  MET MET A . n 
A 1 44  ARG 44  73  73  ARG ARG A . n 
A 1 45  GLY 45  74  74  GLY GLY A . n 
A 1 46  MET 46  75  75  MET MET A . n 
A 1 47  LYS 47  76  76  LYS LYS A . n 
A 1 48  GLY 48  77  77  GLY GLY A . n 
A 1 49  LEU 49  78  78  LEU LEU A . n 
A 1 50  VAL 50  79  79  VAL VAL A . n 
A 1 51  TYR 51  80  80  TYR TYR A . n 
A 1 52  GLU 52  81  81  GLU GLU A . n 
A 1 53  THR 53  82  82  THR THR A . n 
A 1 54  SER 54  83  83  SER SER A . n 
A 1 55  VAL 55  84  84  VAL VAL A . n 
A 1 56  LEU 56  85  85  LEU LEU A . n 
A 1 57  ASP 57  86  86  ASP ASP A . n 
A 1 58  PRO 58  87  87  PRO PRO A . n 
A 1 59  ASP 59  88  88  ASP ASP A . n 
A 1 60  GLU 60  89  89  GLU GLU A . n 
A 1 61  GLY 61  90  90  GLY GLY A . n 
A 1 62  ILE 62  91  91  ILE ILE A . n 
A 1 63  ARG 63  92  92  ARG ARG A . n 
A 1 64  PHE 64  93  93  PHE PHE A . n 
A 1 65  ARG 65  94  94  ARG ARG A . n 
A 1 66  GLY 66  95  95  GLY GLY A . n 
A 1 67  PHE 67  96  96  PHE PHE A . n 
A 1 68  SER 68  97  97  SER SER A . n 
A 1 69  ILE 69  98  98  ILE ILE A . n 
A 1 70  PRO 70  99  99  PRO PRO A . n 
A 1 71  GLU 71  100 100 GLU GLU A . n 
A 1 72  CYS 72  101 101 CYS CYS A . n 
A 1 73  GLN 73  102 102 GLN GLN A . n 
A 1 74  LYS 74  103 103 LYS LYS A . n 
A 1 75  LEU 75  104 104 LEU LEU A . n 
A 1 76  LEU 76  105 105 LEU LEU A . n 
A 1 77  PRO 77  106 106 PRO PRO A . n 
A 1 78  LYS 78  107 107 LYS LYS A . n 
A 1 79  ALA 79  108 108 ALA ALA A . n 
A 1 80  LYS 80  109 109 LYS LYS A . n 
A 1 81  GLY 81  110 110 GLY GLY A . n 
A 1 82  GLY 82  111 111 GLY GLY A . n 
A 1 83  GLU 83  112 112 GLU GLU A . n 
A 1 84  GLU 84  113 113 GLU GLU A . n 
A 1 85  PRO 85  114 114 PRO PRO A . n 
A 1 86  LEU 86  115 115 LEU LEU A . n 
A 1 87  PRO 87  116 116 PRO PRO A . n 
A 1 88  GLU 88  117 117 GLU GLU A . n 
A 1 89  GLY 89  118 118 GLY GLY A . n 
A 1 90  LEU 90  119 119 LEU LEU A . n 
A 1 91  PHE 91  120 120 PHE PHE A . n 
A 1 92  TRP 92  121 121 TRP TRP A . n 
A 1 93  LEU 93  122 122 LEU LEU A . n 
A 1 94  LEU 94  123 123 LEU LEU A . n 
A 1 95  VAL 95  124 124 VAL VAL A . n 
A 1 96  THR 96  125 125 THR THR A . n 
A 1 97  GLY 97  126 126 GLY GLY A . n 
A 1 98  HIS 98  127 127 HIS HIS A . n 
A 1 99  ILE 99  128 128 ILE ILE A . n 
A 1 100 PRO 100 129 129 PRO PRO A . n 
A 1 101 THR 101 130 130 THR THR A . n 
A 1 102 GLU 102 131 131 GLU GLU A . n 
A 1 103 GLU 103 132 132 GLU GLU A . n 
A 1 104 GLN 104 133 133 GLN GLN A . n 
A 1 105 VAL 105 134 134 VAL VAL A . n 
A 1 106 SER 106 135 135 SER SER A . n 
A 1 107 TRP 107 136 136 TRP TRP A . n 
A 1 108 LEU 108 137 137 LEU LEU A . n 
A 1 109 SER 109 138 138 SER SER A . n 
A 1 110 LYS 110 139 139 LYS LYS A . n 
A 1 111 GLU 111 140 140 GLU GLU A . n 
A 1 112 TRP 112 141 141 TRP TRP A . n 
A 1 113 ALA 113 142 142 ALA ALA A . n 
A 1 114 LYS 114 143 143 LYS LYS A . n 
A 1 115 ARG 115 144 144 ARG ARG A . n 
A 1 116 ALA 116 145 145 ALA ALA A . n 
A 1 117 ALA 117 146 146 ALA ALA A . n 
A 1 118 LEU 118 147 147 LEU LEU A . n 
A 1 119 PRO 119 148 148 PRO PRO A . n 
A 1 120 SER 120 149 149 SER SER A . n 
A 1 121 HIS 121 150 150 HIS HIS A . n 
A 1 122 VAL 122 151 151 VAL VAL A . n 
A 1 123 VAL 123 152 152 VAL VAL A . n 
A 1 124 THR 124 153 153 THR THR A . n 
A 1 125 MET 125 154 154 MET MET A . n 
A 1 126 LEU 126 155 155 LEU LEU A . n 
A 1 127 ASP 127 156 156 ASP ASP A . n 
A 1 128 ASN 128 157 157 ASN ASN A . n 
A 1 129 PHE 129 158 158 PHE PHE A . n 
A 1 130 PRO 130 159 159 PRO PRO A . n 
A 1 131 THR 131 160 160 THR THR A . n 
A 1 132 ASN 132 161 161 ASN ASN A . n 
A 1 133 LEU 133 162 162 LEU LEU A . n 
A 1 134 HIS 134 163 163 HIS HIS A . n 
A 1 135 PRO 135 164 164 PRO PRO A . n 
A 1 136 MET 136 165 165 MET MET A . n 
A 1 137 SER 137 166 166 SER SER A . n 
A 1 138 GLN 138 167 167 GLN GLN A . n 
A 1 139 LEU 139 168 168 LEU LEU A . n 
A 1 140 SER 140 169 169 SER SER A . n 
A 1 141 ALA 141 170 170 ALA ALA A . n 
A 1 142 ALA 142 171 171 ALA ALA A . n 
A 1 143 VAL 143 172 172 VAL VAL A . n 
A 1 144 THR 144 173 173 THR THR A . n 
A 1 145 ALA 145 174 174 ALA ALA A . n 
A 1 146 LEU 146 175 175 LEU LEU A . n 
A 1 147 ASN 147 176 176 ASN ASN A . n 
A 1 148 SER 148 177 177 SER SER A . n 
A 1 149 GLU 149 178 178 GLU GLU A . n 
A 1 150 SER 150 179 179 SER SER A . n 
A 1 151 ASN 151 180 180 ASN ASN A . n 
A 1 152 PHE 152 181 181 PHE PHE A . n 
A 1 153 ALA 153 182 182 ALA ALA A . n 
A 1 154 ARG 154 183 183 ARG ARG A . n 
A 1 155 ALA 155 184 184 ALA ALA A . n 
A 1 156 TYR 156 185 185 TYR TYR A . n 
A 1 157 ALA 157 186 186 ALA ALA A . n 
A 1 158 GLN 158 187 187 GLN GLN A . n 
A 1 159 GLY 159 188 188 GLY GLY A . n 
A 1 160 ILE 160 189 189 ILE ILE A . n 
A 1 161 SER 161 190 190 SER SER A . n 
A 1 162 ARG 162 191 191 ARG ARG A . n 
A 1 163 THR 163 192 192 THR THR A . n 
A 1 164 LYS 164 193 193 LYS LYS A . n 
A 1 165 TYR 165 194 194 TYR TYR A . n 
A 1 166 TRP 166 195 195 TRP TRP A . n 
A 1 167 GLU 167 196 196 GLU GLU A . n 
A 1 168 LEU 168 197 197 LEU LEU A . n 
A 1 169 ILE 169 198 198 ILE ILE A . n 
A 1 170 TYR 170 199 199 TYR TYR A . n 
A 1 171 GLU 171 200 200 GLU GLU A . n 
A 1 172 ASP 172 201 201 ASP ASP A . n 
A 1 173 SER 173 202 202 SER SER A . n 
A 1 174 MET 174 203 203 MET MET A . n 
A 1 175 ASP 175 204 204 ASP ASP A . n 
A 1 176 LEU 176 205 205 LEU LEU A . n 
A 1 177 ILE 177 206 206 ILE ILE A . n 
A 1 178 ALA 178 207 207 ALA ALA A . n 
A 1 179 LYS 179 208 208 LYS LYS A . n 
A 1 180 LEU 180 209 209 LEU LEU A . n 
A 1 181 PRO 181 210 210 PRO PRO A . n 
A 1 182 CYS 182 211 211 CYS CYS A . n 
A 1 183 VAL 183 212 212 VAL VAL A . n 
A 1 184 ALA 184 213 213 ALA ALA A . n 
A 1 185 ALA 185 214 214 ALA ALA A . n 
A 1 186 LYS 186 215 215 LYS LYS A . n 
A 1 187 ILE 187 216 216 ILE ILE A . n 
A 1 188 TYR 188 217 217 TYR TYR A . n 
A 1 189 ARG 189 218 218 ARG ARG A . n 
A 1 190 ASN 190 219 219 ASN ASN A . n 
A 1 191 LEU 191 220 220 LEU LEU A . n 
A 1 192 TYR 192 221 221 TYR TYR A . n 
A 1 193 ARG 193 222 222 ARG ARG A . n 
A 1 194 GLU 194 223 223 GLU GLU A . n 
A 1 195 GLY 195 224 224 GLY GLY A . n 
A 1 196 SER 196 225 225 SER SER A . n 
A 1 197 GLY 197 226 226 GLY GLY A . n 
A 1 198 ILE 198 227 227 ILE ILE A . n 
A 1 199 GLY 199 228 228 GLY GLY A . n 
A 1 200 ALA 200 229 229 ALA ALA A . n 
A 1 201 ILE 201 230 230 ILE ILE A . n 
A 1 202 ASP 202 231 231 ASP ASP A . n 
A 1 203 SER 203 232 232 SER SER A . n 
A 1 204 ASN 204 233 233 ASN ASN A . n 
A 1 205 LEU 205 234 234 LEU LEU A . n 
A 1 206 ASP 206 235 235 ASP ASP A . n 
A 1 207 TRP 207 236 236 TRP TRP A . n 
A 1 208 SER 208 237 237 SER SER A . n 
A 1 209 HIS 209 238 238 HIS HIS A . n 
A 1 210 ASN 210 239 239 ASN ASN A . n 
A 1 211 PHE 211 240 240 PHE PHE A . n 
A 1 212 THR 212 241 241 THR THR A . n 
A 1 213 ASN 213 242 242 ASN ASN A . n 
A 1 214 MET 214 243 243 MET MET A . n 
A 1 215 LEU 215 244 244 LEU LEU A . n 
A 1 216 GLY 216 245 245 GLY GLY A . n 
A 1 217 TYR 217 246 246 TYR TYR A . n 
A 1 218 THR 218 247 247 THR THR A . n 
A 1 219 ASP 219 248 248 ASP ASP A . n 
A 1 220 HIS 220 249 249 HIS HIS A . n 
A 1 221 GLN 221 250 250 GLN GLN A . n 
A 1 222 PHE 222 251 251 PHE PHE A . n 
A 1 223 THR 223 252 252 THR THR A . n 
A 1 224 GLU 224 253 253 GLU GLU A . n 
A 1 225 LEU 225 254 254 LEU LEU A . n 
A 1 226 THR 226 255 255 THR THR A . n 
A 1 227 ARG 227 256 256 ARG ARG A . n 
A 1 228 LEU 228 257 257 LEU LEU A . n 
A 1 229 TYR 229 258 258 TYR TYR A . n 
A 1 230 LEU 230 259 259 LEU LEU A . n 
A 1 231 THR 231 260 260 THR THR A . n 
A 1 232 ILE 232 261 261 ILE ILE A . n 
A 1 233 HIS 233 262 262 HIS HIS A . n 
A 1 234 SER 234 263 263 SER SER A . n 
A 1 235 ASP 235 264 264 ASP ASP A . n 
A 1 236 HIS 236 265 265 HIS HIS A . n 
A 1 237 GLU 237 266 266 GLU GLU A . n 
A 1 238 GLY 238 267 267 GLY GLY A . n 
A 1 239 GLY 239 268 268 GLY GLY A . n 
A 1 240 ASN 240 269 269 ASN ASN A . n 
A 1 241 VAL 241 270 270 VAL VAL A . n 
A 1 242 SER 242 271 271 SER SER A . n 
A 1 243 ALA 243 272 272 ALA ALA A . n 
A 1 244 HIS 244 273 273 HIS HIS A . n 
A 1 245 THR 245 274 274 THR THR A . n 
A 1 246 SER 246 275 275 SER SER A . n 
A 1 247 HIS 247 276 276 HIS HIS A . n 
A 1 248 LEU 248 277 277 LEU LEU A . n 
A 1 249 VAL 249 278 278 VAL VAL A . n 
A 1 250 GLY 250 279 279 GLY GLY A . n 
A 1 251 SER 251 280 280 SER SER A . n 
A 1 252 ALA 252 281 281 ALA ALA A . n 
A 1 253 LEU 253 282 282 LEU LEU A . n 
A 1 254 SER 254 283 283 SER SER A . n 
A 1 255 ASP 255 284 284 ASP ASP A . n 
A 1 256 PRO 256 285 285 PRO PRO A . n 
A 1 257 TYR 257 286 286 TYR TYR A . n 
A 1 258 LEU 258 287 287 LEU LEU A . n 
A 1 259 SER 259 288 288 SER SER A . n 
A 1 260 PHE 260 289 289 PHE PHE A . n 
A 1 261 ALA 261 290 290 ALA ALA A . n 
A 1 262 ALA 262 291 291 ALA ALA A . n 
A 1 263 ALA 263 292 292 ALA ALA A . n 
A 1 264 MET 264 293 293 MET MET A . n 
A 1 265 ASN 265 294 294 ASN ASN A . n 
A 1 266 GLY 266 295 295 GLY GLY A . n 
A 1 267 LEU 267 296 296 LEU LEU A . n 
A 1 268 ALA 268 297 297 ALA ALA A . n 
A 1 269 GLY 269 298 298 GLY GLY A . n 
A 1 270 PRO 270 299 299 PRO PRO A . n 
A 1 271 LEU 271 300 300 LEU LEU A . n 
A 1 272 HIS 272 301 301 HIS HIS A . n 
A 1 273 GLY 273 302 302 GLY GLY A . n 
A 1 274 LEU 274 303 303 LEU LEU A . n 
A 1 275 ALA 275 304 304 ALA ALA A . n 
A 1 276 ASN 276 305 305 ASN ASN A . n 
A 1 277 GLN 277 306 306 GLN GLN A . n 
A 1 278 GLU 278 307 307 GLU GLU A . n 
A 1 279 VAL 279 308 308 VAL VAL A . n 
A 1 280 LEU 280 309 309 LEU LEU A . n 
A 1 281 VAL 281 310 310 VAL VAL A . n 
A 1 282 TRP 282 311 311 TRP TRP A . n 
A 1 283 LEU 283 312 312 LEU LEU A . n 
A 1 284 THR 284 313 313 THR THR A . n 
A 1 285 GLN 285 314 314 GLN GLN A . n 
A 1 286 LEU 286 315 315 LEU LEU A . n 
A 1 287 GLN 287 316 316 GLN GLN A . n 
A 1 288 LYS 288 317 317 LYS LYS A . n 
A 1 289 GLU 289 318 318 GLU GLU A . n 
A 1 290 VAL 290 319 319 VAL VAL A . n 
A 1 291 GLY 291 320 320 GLY GLY A . n 
A 1 292 LYS 292 321 321 LYS LYS A . n 
A 1 293 ASP 293 322 322 ASP ASP A . n 
A 1 294 VAL 294 323 323 VAL VAL A . n 
A 1 295 SER 295 324 324 SER SER A . n 
A 1 296 ASP 296 325 325 ASP ASP A . n 
A 1 297 GLU 297 326 326 GLU GLU A . n 
A 1 298 LYS 298 327 327 LYS LYS A . n 
A 1 299 LEU 299 328 328 LEU LEU A . n 
A 1 300 ARG 300 329 329 ARG ARG A . n 
A 1 301 ASP 301 330 330 ASP ASP A . n 
A 1 302 TYR 302 331 331 TYR TYR A . n 
A 1 303 ILE 303 332 332 ILE ILE A . n 
A 1 304 TRP 304 333 333 TRP TRP A . n 
A 1 305 ASN 305 334 334 ASN ASN A . n 
A 1 306 THR 306 335 335 THR THR A . n 
A 1 307 LEU 307 336 336 LEU LEU A . n 
A 1 308 ASN 308 337 337 ASN ASN A . n 
A 1 309 SER 309 338 338 SER SER A . n 
A 1 310 GLY 310 339 339 GLY GLY A . n 
A 1 311 ARG 311 340 340 ARG ARG A . n 
A 1 312 VAL 312 341 341 VAL VAL A . n 
A 1 313 VAL 313 342 342 VAL VAL A . n 
A 1 314 PRO 314 343 343 PRO PRO A . n 
A 1 315 GLY 315 344 344 GLY GLY A . n 
A 1 316 TYR 316 345 345 TYR TYR A . n 
A 1 317 GLY 317 346 346 GLY GLY A . n 
A 1 318 HIS 318 347 347 HIS HIS A . n 
A 1 319 ALA 319 348 348 ALA ALA A . n 
A 1 320 VAL 320 349 349 VAL VAL A . n 
A 1 321 LEU 321 350 350 LEU LEU A . n 
A 1 322 ARG 322 351 351 ARG ARG A . n 
A 1 323 LYS 323 352 352 LYS LYS A . n 
A 1 324 THR 324 353 353 THR THR A . n 
A 1 325 ASP 325 354 354 ASP ASP A . n 
A 1 326 PRO 326 355 355 PRO PRO A . n 
A 1 327 ARG 327 356 356 ARG ARG A . n 
A 1 328 TYR 328 357 357 TYR TYR A . n 
A 1 329 THR 329 358 358 THR THR A . n 
A 1 330 CYS 330 359 359 CYS CYS A . n 
A 1 331 GLN 331 360 360 GLN GLN A . n 
A 1 332 ARG 332 361 361 ARG ARG A . n 
A 1 333 GLU 333 362 362 GLU GLU A . n 
A 1 334 PHE 334 363 363 PHE PHE A . n 
A 1 335 ALA 335 364 364 ALA ALA A . n 
A 1 336 LEU 336 365 365 LEU LEU A . n 
A 1 337 LYS 337 366 366 LYS LYS A . n 
A 1 338 HIS 338 367 367 HIS HIS A . n 
A 1 339 LEU 339 368 368 LEU LEU A . n 
A 1 340 PRO 340 369 369 PRO PRO A . n 
A 1 341 ASN 341 370 370 ASN ASN A . n 
A 1 342 ASP 342 371 371 ASP ASP A . n 
A 1 343 PRO 343 372 372 PRO PRO A . n 
A 1 344 MET 344 373 373 MET MET A . n 
A 1 345 PHE 345 374 374 PHE PHE A . n 
A 1 346 LYS 346 375 375 LYS LYS A . n 
A 1 347 LEU 347 376 376 LEU LEU A . n 
A 1 348 VAL 348 377 377 VAL VAL A . n 
A 1 349 ALA 349 378 378 ALA ALA A . n 
A 1 350 GLN 350 379 379 GLN GLN A . n 
A 1 351 LEU 351 380 380 LEU LEU A . n 
A 1 352 TYR 352 381 381 TYR TYR A . n 
A 1 353 LYS 353 382 382 LYS LYS A . n 
A 1 354 ILE 354 383 383 ILE ILE A . n 
A 1 355 VAL 355 384 384 VAL VAL A . n 
A 1 356 PRO 356 385 385 PRO PRO A . n 
A 1 357 ASN 357 386 386 ASN ASN A . n 
A 1 358 VAL 358 387 387 VAL VAL A . n 
A 1 359 LEU 359 388 388 LEU LEU A . n 
A 1 360 LEU 360 389 389 LEU LEU A . n 
A 1 361 GLU 361 390 390 GLU GLU A . n 
A 1 362 GLN 362 391 391 GLN GLN A . n 
A 1 363 GLY 363 392 392 GLY GLY A . n 
A 1 364 LYS 364 393 393 LYS LYS A . n 
A 1 365 ALA 365 394 394 ALA ALA A . n 
A 1 366 LYS 366 395 395 LYS LYS A . n 
A 1 367 ASN 367 396 396 ASN ASN A . n 
A 1 368 PRO 368 397 397 PRO PRO A . n 
A 1 369 TRP 369 398 398 TRP TRP A . n 
A 1 370 PRO 370 399 399 PRO PRO A . n 
A 1 371 ASN 371 400 400 ASN ASN A . n 
A 1 372 VAL 372 401 401 VAL VAL A . n 
A 1 373 ASP 373 402 402 ASP ASP A . n 
A 1 374 ALA 374 403 403 ALA ALA A . n 
A 1 375 HIS 375 404 404 HIS HIS A . n 
A 1 376 SER 376 405 405 SER SER A . n 
A 1 377 GLY 377 406 406 GLY GLY A . n 
A 1 378 VAL 378 407 407 VAL VAL A . n 
A 1 379 LEU 379 408 408 LEU LEU A . n 
A 1 380 LEU 380 409 409 LEU LEU A . n 
A 1 381 GLN 381 410 410 GLN GLN A . n 
A 1 382 TYR 382 411 411 TYR TYR A . n 
A 1 383 TYR 383 412 412 TYR TYR A . n 
A 1 384 GLY 384 413 413 GLY GLY A . n 
A 1 385 MET 385 414 414 MET MET A . n 
A 1 386 THR 386 415 415 THR THR A . n 
A 1 387 GLU 387 416 416 GLU GLU A . n 
A 1 388 MET 388 417 417 MET MET A . n 
A 1 389 ASN 389 418 418 ASN ASN A . n 
A 1 390 TYR 390 419 419 TYR TYR A . n 
A 1 391 TYR 391 420 420 TYR TYR A . n 
A 1 392 THR 392 421 421 THR THR A . n 
A 1 393 VAL 393 422 422 VAL VAL A . n 
A 1 394 LEU 394 423 423 LEU LEU A . n 
A 1 395 PHE 395 424 424 PHE PHE A . n 
A 1 396 GLY 396 425 425 GLY GLY A . n 
A 1 397 VAL 397 426 426 VAL VAL A . n 
A 1 398 SER 398 427 427 SER SER A . n 
A 1 399 ARG 399 428 428 ARG ARG A . n 
A 1 400 ALA 400 429 429 ALA ALA A . n 
A 1 401 LEU 401 430 430 LEU LEU A . n 
A 1 402 GLY 402 431 431 GLY GLY A . n 
A 1 403 VAL 403 432 432 VAL VAL A . n 
A 1 404 LEU 404 433 433 LEU LEU A . n 
A 1 405 ALA 405 434 434 ALA ALA A . n 
A 1 406 GLN 406 435 435 GLN GLN A . n 
A 1 407 LEU 407 436 436 LEU LEU A . n 
A 1 408 ILE 408 437 437 ILE ILE A . n 
A 1 409 TRP 409 438 438 TRP TRP A . n 
A 1 410 SER 410 439 439 SER SER A . n 
A 1 411 ARG 411 440 440 ARG ARG A . n 
A 1 412 ALA 412 441 441 ALA ALA A . n 
A 1 413 LEU 413 442 442 LEU LEU A . n 
A 1 414 GLY 414 443 443 GLY GLY A . n 
A 1 415 PHE 415 444 444 PHE PHE A . n 
A 1 416 PRO 416 445 445 PRO PRO A . n 
A 1 417 LEU 417 446 446 LEU LEU A . n 
A 1 418 GLU 418 447 447 GLU GLU A . n 
A 1 419 ARG 419 448 448 ARG ARG A . n 
A 1 420 PRO 420 449 449 PRO PRO A . n 
A 1 421 LYS 421 450 450 LYS LYS A . n 
A 1 422 SER 422 451 451 SER SER A . n 
A 1 423 MET 423 452 452 MET MET A . n 
A 1 424 SER 424 453 453 SER SER A . n 
A 1 425 THR 425 454 454 THR THR A . n 
A 1 426 GLU 426 455 455 GLU GLU A . n 
A 1 427 GLY 427 456 456 GLY GLY A . n 
A 1 428 LEU 428 457 457 LEU LEU A . n 
A 1 429 MET 429 458 458 MET MET A . n 
A 1 430 LYS 430 459 459 LYS LYS A . n 
A 1 431 PHE 431 460 460 PHE PHE A . n 
A 1 432 VAL 432 461 461 VAL VAL A . n 
A 1 433 ASP 433 462 462 ASP ASP A . n 
A 1 434 SER 434 463 463 SER SER A . n 
A 1 435 LYS 435 464 ?   ?   ?   A . n 
B 1 1   SER 1   30  30  SER SER D . n 
B 1 2   THR 2   31  31  THR THR D . n 
B 1 3   ASN 3   32  32  ASN ASN D . n 
B 1 4   LEU 4   33  33  LEU LEU D . n 
B 1 5   LYS 5   34  34  LYS LYS D . n 
B 1 6   ASP 6   35  35  ASP ASP D . n 
B 1 7   ILE 7   36  36  ILE ILE D . n 
B 1 8   LEU 8   37  37  LEU LEU D . n 
B 1 9   ALA 9   38  38  ALA ALA D . n 
B 1 10  ASP 10  39  39  ASP ASP D . n 
B 1 11  LEU 11  40  40  LEU LEU D . n 
B 1 12  ILE 12  41  41  ILE ILE D . n 
B 1 13  PRO 13  42  42  PRO PRO D . n 
B 1 14  LYS 14  43  43  LYS LYS D . n 
B 1 15  GLU 15  44  44  GLU GLU D . n 
B 1 16  GLN 16  45  45  GLN GLN D . n 
B 1 17  ALA 17  46  46  ALA ALA D . n 
B 1 18  ARG 18  47  47  ARG ARG D . n 
B 1 19  ILE 19  48  48  ILE ILE D . n 
B 1 20  LYS 20  49  49  LYS LYS D . n 
B 1 21  THR 21  50  50  THR THR D . n 
B 1 22  PHE 22  51  51  PHE PHE D . n 
B 1 23  ARG 23  52  52  ARG ARG D . n 
B 1 24  GLN 24  53  53  GLN GLN D . n 
B 1 25  GLN 25  54  54  GLN GLN D . n 
B 1 26  HIS 26  55  55  HIS HIS D . n 
B 1 27  GLY 27  56  56  GLY GLY D . n 
B 1 28  LYS 28  57  57  LYS LYS D . n 
B 1 29  THR 29  58  58  THR THR D . n 
B 1 30  VAL 30  59  59  VAL VAL D . n 
B 1 31  VAL 31  60  60  VAL VAL D . n 
B 1 32  GLY 32  61  61  GLY GLY D . n 
B 1 33  GLN 33  62  62  GLN GLN D . n 
B 1 34  ILE 34  63  63  ILE ILE D . n 
B 1 35  THR 35  64  64  THR THR D . n 
B 1 36  VAL 36  65  65  VAL VAL D . n 
B 1 37  ASP 37  66  66  ASP ASP D . n 
B 1 38  MET 38  67  67  MET MET D . n 
B 1 39  MET 39  68  68  MET MET D . n 
B 1 40  TYR 40  69  69  TYR TYR D . n 
B 1 41  GLY 41  70  70  GLY GLY D . n 
B 1 42  GLY 42  71  71  GLY GLY D . n 
B 1 43  MET 43  72  72  MET MET D . n 
B 1 44  ARG 44  73  73  ARG ARG D . n 
B 1 45  GLY 45  74  74  GLY GLY D . n 
B 1 46  MET 46  75  75  MET MET D . n 
B 1 47  LYS 47  76  76  LYS LYS D . n 
B 1 48  GLY 48  77  77  GLY GLY D . n 
B 1 49  LEU 49  78  78  LEU LEU D . n 
B 1 50  VAL 50  79  79  VAL VAL D . n 
B 1 51  TYR 51  80  80  TYR TYR D . n 
B 1 52  GLU 52  81  81  GLU GLU D . n 
B 1 53  THR 53  82  82  THR THR D . n 
B 1 54  SER 54  83  83  SER SER D . n 
B 1 55  VAL 55  84  84  VAL VAL D . n 
B 1 56  LEU 56  85  85  LEU LEU D . n 
B 1 57  ASP 57  86  86  ASP ASP D . n 
B 1 58  PRO 58  87  87  PRO PRO D . n 
B 1 59  ASP 59  88  88  ASP ASP D . n 
B 1 60  GLU 60  89  89  GLU GLU D . n 
B 1 61  GLY 61  90  90  GLY GLY D . n 
B 1 62  ILE 62  91  91  ILE ILE D . n 
B 1 63  ARG 63  92  92  ARG ARG D . n 
B 1 64  PHE 64  93  93  PHE PHE D . n 
B 1 65  ARG 65  94  94  ARG ARG D . n 
B 1 66  GLY 66  95  95  GLY GLY D . n 
B 1 67  PHE 67  96  96  PHE PHE D . n 
B 1 68  SER 68  97  97  SER SER D . n 
B 1 69  ILE 69  98  98  ILE ILE D . n 
B 1 70  PRO 70  99  99  PRO PRO D . n 
B 1 71  GLU 71  100 100 GLU GLU D . n 
B 1 72  CYS 72  101 101 CYS CYS D . n 
B 1 73  GLN 73  102 102 GLN GLN D . n 
B 1 74  LYS 74  103 103 LYS LYS D . n 
B 1 75  LEU 75  104 104 LEU LEU D . n 
B 1 76  LEU 76  105 105 LEU LEU D . n 
B 1 77  PRO 77  106 106 PRO PRO D . n 
B 1 78  LYS 78  107 107 LYS LYS D . n 
B 1 79  ALA 79  108 108 ALA ALA D . n 
B 1 80  LYS 80  109 109 LYS LYS D . n 
B 1 81  GLY 81  110 110 GLY GLY D . n 
B 1 82  GLY 82  111 111 GLY GLY D . n 
B 1 83  GLU 83  112 112 GLU GLU D . n 
B 1 84  GLU 84  113 113 GLU GLU D . n 
B 1 85  PRO 85  114 114 PRO PRO D . n 
B 1 86  LEU 86  115 115 LEU LEU D . n 
B 1 87  PRO 87  116 116 PRO PRO D . n 
B 1 88  GLU 88  117 117 GLU GLU D . n 
B 1 89  GLY 89  118 118 GLY GLY D . n 
B 1 90  LEU 90  119 119 LEU LEU D . n 
B 1 91  PHE 91  120 120 PHE PHE D . n 
B 1 92  TRP 92  121 121 TRP TRP D . n 
B 1 93  LEU 93  122 122 LEU LEU D . n 
B 1 94  LEU 94  123 123 LEU LEU D . n 
B 1 95  VAL 95  124 124 VAL VAL D . n 
B 1 96  THR 96  125 125 THR THR D . n 
B 1 97  GLY 97  126 126 GLY GLY D . n 
B 1 98  HIS 98  127 127 HIS HIS D . n 
B 1 99  ILE 99  128 128 ILE ILE D . n 
B 1 100 PRO 100 129 129 PRO PRO D . n 
B 1 101 THR 101 130 130 THR THR D . n 
B 1 102 GLU 102 131 131 GLU GLU D . n 
B 1 103 GLU 103 132 132 GLU GLU D . n 
B 1 104 GLN 104 133 133 GLN GLN D . n 
B 1 105 VAL 105 134 134 VAL VAL D . n 
B 1 106 SER 106 135 135 SER SER D . n 
B 1 107 TRP 107 136 136 TRP TRP D . n 
B 1 108 LEU 108 137 137 LEU LEU D . n 
B 1 109 SER 109 138 138 SER SER D . n 
B 1 110 LYS 110 139 139 LYS LYS D . n 
B 1 111 GLU 111 140 140 GLU GLU D . n 
B 1 112 TRP 112 141 141 TRP TRP D . n 
B 1 113 ALA 113 142 142 ALA ALA D . n 
B 1 114 LYS 114 143 143 LYS LYS D . n 
B 1 115 ARG 115 144 144 ARG ARG D . n 
B 1 116 ALA 116 145 145 ALA ALA D . n 
B 1 117 ALA 117 146 146 ALA ALA D . n 
B 1 118 LEU 118 147 147 LEU LEU D . n 
B 1 119 PRO 119 148 148 PRO PRO D . n 
B 1 120 SER 120 149 149 SER SER D . n 
B 1 121 HIS 121 150 150 HIS HIS D . n 
B 1 122 VAL 122 151 151 VAL VAL D . n 
B 1 123 VAL 123 152 152 VAL VAL D . n 
B 1 124 THR 124 153 153 THR THR D . n 
B 1 125 MET 125 154 154 MET MET D . n 
B 1 126 LEU 126 155 155 LEU LEU D . n 
B 1 127 ASP 127 156 156 ASP ASP D . n 
B 1 128 ASN 128 157 157 ASN ASN D . n 
B 1 129 PHE 129 158 158 PHE PHE D . n 
B 1 130 PRO 130 159 159 PRO PRO D . n 
B 1 131 THR 131 160 160 THR THR D . n 
B 1 132 ASN 132 161 161 ASN ASN D . n 
B 1 133 LEU 133 162 162 LEU LEU D . n 
B 1 134 HIS 134 163 163 HIS HIS D . n 
B 1 135 PRO 135 164 164 PRO PRO D . n 
B 1 136 MET 136 165 165 MET MET D . n 
B 1 137 SER 137 166 166 SER SER D . n 
B 1 138 GLN 138 167 167 GLN GLN D . n 
B 1 139 LEU 139 168 168 LEU LEU D . n 
B 1 140 SER 140 169 169 SER SER D . n 
B 1 141 ALA 141 170 170 ALA ALA D . n 
B 1 142 ALA 142 171 171 ALA ALA D . n 
B 1 143 VAL 143 172 172 VAL VAL D . n 
B 1 144 THR 144 173 173 THR THR D . n 
B 1 145 ALA 145 174 174 ALA ALA D . n 
B 1 146 LEU 146 175 175 LEU LEU D . n 
B 1 147 ASN 147 176 176 ASN ASN D . n 
B 1 148 SER 148 177 177 SER SER D . n 
B 1 149 GLU 149 178 178 GLU GLU D . n 
B 1 150 SER 150 179 179 SER SER D . n 
B 1 151 ASN 151 180 180 ASN ASN D . n 
B 1 152 PHE 152 181 181 PHE PHE D . n 
B 1 153 ALA 153 182 182 ALA ALA D . n 
B 1 154 ARG 154 183 183 ARG ARG D . n 
B 1 155 ALA 155 184 184 ALA ALA D . n 
B 1 156 TYR 156 185 185 TYR TYR D . n 
B 1 157 ALA 157 186 186 ALA ALA D . n 
B 1 158 GLN 158 187 187 GLN GLN D . n 
B 1 159 GLY 159 188 188 GLY GLY D . n 
B 1 160 ILE 160 189 189 ILE ILE D . n 
B 1 161 SER 161 190 190 SER SER D . n 
B 1 162 ARG 162 191 191 ARG ARG D . n 
B 1 163 THR 163 192 192 THR THR D . n 
B 1 164 LYS 164 193 193 LYS LYS D . n 
B 1 165 TYR 165 194 194 TYR TYR D . n 
B 1 166 TRP 166 195 195 TRP TRP D . n 
B 1 167 GLU 167 196 196 GLU GLU D . n 
B 1 168 LEU 168 197 197 LEU LEU D . n 
B 1 169 ILE 169 198 198 ILE ILE D . n 
B 1 170 TYR 170 199 199 TYR TYR D . n 
B 1 171 GLU 171 200 200 GLU GLU D . n 
B 1 172 ASP 172 201 201 ASP ASP D . n 
B 1 173 SER 173 202 202 SER SER D . n 
B 1 174 MET 174 203 203 MET MET D . n 
B 1 175 ASP 175 204 204 ASP ASP D . n 
B 1 176 LEU 176 205 205 LEU LEU D . n 
B 1 177 ILE 177 206 206 ILE ILE D . n 
B 1 178 ALA 178 207 207 ALA ALA D . n 
B 1 179 LYS 179 208 208 LYS LYS D . n 
B 1 180 LEU 180 209 209 LEU LEU D . n 
B 1 181 PRO 181 210 210 PRO PRO D . n 
B 1 182 CYS 182 211 211 CYS CYS D . n 
B 1 183 VAL 183 212 212 VAL VAL D . n 
B 1 184 ALA 184 213 213 ALA ALA D . n 
B 1 185 ALA 185 214 214 ALA ALA D . n 
B 1 186 LYS 186 215 215 LYS LYS D . n 
B 1 187 ILE 187 216 216 ILE ILE D . n 
B 1 188 TYR 188 217 217 TYR TYR D . n 
B 1 189 ARG 189 218 218 ARG ARG D . n 
B 1 190 ASN 190 219 219 ASN ASN D . n 
B 1 191 LEU 191 220 220 LEU LEU D . n 
B 1 192 TYR 192 221 221 TYR TYR D . n 
B 1 193 ARG 193 222 222 ARG ARG D . n 
B 1 194 GLU 194 223 223 GLU GLU D . n 
B 1 195 GLY 195 224 224 GLY GLY D . n 
B 1 196 SER 196 225 225 SER SER D . n 
B 1 197 GLY 197 226 226 GLY GLY D . n 
B 1 198 ILE 198 227 227 ILE ILE D . n 
B 1 199 GLY 199 228 228 GLY GLY D . n 
B 1 200 ALA 200 229 229 ALA ALA D . n 
B 1 201 ILE 201 230 230 ILE ILE D . n 
B 1 202 ASP 202 231 231 ASP ASP D . n 
B 1 203 SER 203 232 232 SER SER D . n 
B 1 204 ASN 204 233 233 ASN ASN D . n 
B 1 205 LEU 205 234 234 LEU LEU D . n 
B 1 206 ASP 206 235 235 ASP ASP D . n 
B 1 207 TRP 207 236 236 TRP TRP D . n 
B 1 208 SER 208 237 237 SER SER D . n 
B 1 209 HIS 209 238 238 HIS HIS D . n 
B 1 210 ASN 210 239 239 ASN ASN D . n 
B 1 211 PHE 211 240 240 PHE PHE D . n 
B 1 212 THR 212 241 241 THR THR D . n 
B 1 213 ASN 213 242 242 ASN ASN D . n 
B 1 214 MET 214 243 243 MET MET D . n 
B 1 215 LEU 215 244 244 LEU LEU D . n 
B 1 216 GLY 216 245 245 GLY GLY D . n 
B 1 217 TYR 217 246 246 TYR TYR D . n 
B 1 218 THR 218 247 247 THR THR D . n 
B 1 219 ASP 219 248 248 ASP ASP D . n 
B 1 220 HIS 220 249 249 HIS HIS D . n 
B 1 221 GLN 221 250 250 GLN GLN D . n 
B 1 222 PHE 222 251 251 PHE PHE D . n 
B 1 223 THR 223 252 252 THR THR D . n 
B 1 224 GLU 224 253 253 GLU GLU D . n 
B 1 225 LEU 225 254 254 LEU LEU D . n 
B 1 226 THR 226 255 255 THR THR D . n 
B 1 227 ARG 227 256 256 ARG ARG D . n 
B 1 228 LEU 228 257 257 LEU LEU D . n 
B 1 229 TYR 229 258 258 TYR TYR D . n 
B 1 230 LEU 230 259 259 LEU LEU D . n 
B 1 231 THR 231 260 260 THR THR D . n 
B 1 232 ILE 232 261 261 ILE ILE D . n 
B 1 233 HIS 233 262 262 HIS HIS D . n 
B 1 234 SER 234 263 263 SER SER D . n 
B 1 235 ASP 235 264 264 ASP ASP D . n 
B 1 236 HIS 236 265 265 HIS HIS D . n 
B 1 237 GLU 237 266 266 GLU GLU D . n 
B 1 238 GLY 238 267 267 GLY GLY D . n 
B 1 239 GLY 239 268 268 GLY GLY D . n 
B 1 240 ASN 240 269 269 ASN ASN D . n 
B 1 241 VAL 241 270 270 VAL VAL D . n 
B 1 242 SER 242 271 271 SER SER D . n 
B 1 243 ALA 243 272 272 ALA ALA D . n 
B 1 244 HIS 244 273 273 HIS HIS D . n 
B 1 245 THR 245 274 274 THR THR D . n 
B 1 246 SER 246 275 275 SER SER D . n 
B 1 247 HIS 247 276 276 HIS HIS D . n 
B 1 248 LEU 248 277 277 LEU LEU D . n 
B 1 249 VAL 249 278 278 VAL VAL D . n 
B 1 250 GLY 250 279 279 GLY GLY D . n 
B 1 251 SER 251 280 280 SER SER D . n 
B 1 252 ALA 252 281 281 ALA ALA D . n 
B 1 253 LEU 253 282 282 LEU LEU D . n 
B 1 254 SER 254 283 283 SER SER D . n 
B 1 255 ASP 255 284 284 ASP ASP D . n 
B 1 256 PRO 256 285 285 PRO PRO D . n 
B 1 257 TYR 257 286 286 TYR TYR D . n 
B 1 258 LEU 258 287 287 LEU LEU D . n 
B 1 259 SER 259 288 288 SER SER D . n 
B 1 260 PHE 260 289 289 PHE PHE D . n 
B 1 261 ALA 261 290 290 ALA ALA D . n 
B 1 262 ALA 262 291 291 ALA ALA D . n 
B 1 263 ALA 263 292 292 ALA ALA D . n 
B 1 264 MET 264 293 293 MET MET D . n 
B 1 265 ASN 265 294 294 ASN ASN D . n 
B 1 266 GLY 266 295 295 GLY GLY D . n 
B 1 267 LEU 267 296 296 LEU LEU D . n 
B 1 268 ALA 268 297 297 ALA ALA D . n 
B 1 269 GLY 269 298 298 GLY GLY D . n 
B 1 270 PRO 270 299 299 PRO PRO D . n 
B 1 271 LEU 271 300 300 LEU LEU D . n 
B 1 272 HIS 272 301 301 HIS HIS D . n 
B 1 273 GLY 273 302 302 GLY GLY D . n 
B 1 274 LEU 274 303 303 LEU LEU D . n 
B 1 275 ALA 275 304 304 ALA ALA D . n 
B 1 276 ASN 276 305 305 ASN ASN D . n 
B 1 277 GLN 277 306 306 GLN GLN D . n 
B 1 278 GLU 278 307 307 GLU GLU D . n 
B 1 279 VAL 279 308 308 VAL VAL D . n 
B 1 280 LEU 280 309 309 LEU LEU D . n 
B 1 281 VAL 281 310 310 VAL VAL D . n 
B 1 282 TRP 282 311 311 TRP TRP D . n 
B 1 283 LEU 283 312 312 LEU LEU D . n 
B 1 284 THR 284 313 313 THR THR D . n 
B 1 285 GLN 285 314 314 GLN GLN D . n 
B 1 286 LEU 286 315 315 LEU LEU D . n 
B 1 287 GLN 287 316 316 GLN GLN D . n 
B 1 288 LYS 288 317 317 LYS LYS D . n 
B 1 289 GLU 289 318 318 GLU GLU D . n 
B 1 290 VAL 290 319 319 VAL VAL D . n 
B 1 291 GLY 291 320 320 GLY GLY D . n 
B 1 292 LYS 292 321 321 LYS LYS D . n 
B 1 293 ASP 293 322 322 ASP ASP D . n 
B 1 294 VAL 294 323 323 VAL VAL D . n 
B 1 295 SER 295 324 324 SER SER D . n 
B 1 296 ASP 296 325 325 ASP ASP D . n 
B 1 297 GLU 297 326 326 GLU GLU D . n 
B 1 298 LYS 298 327 327 LYS LYS D . n 
B 1 299 LEU 299 328 328 LEU LEU D . n 
B 1 300 ARG 300 329 329 ARG ARG D . n 
B 1 301 ASP 301 330 330 ASP ASP D . n 
B 1 302 TYR 302 331 331 TYR TYR D . n 
B 1 303 ILE 303 332 332 ILE ILE D . n 
B 1 304 TRP 304 333 333 TRP TRP D . n 
B 1 305 ASN 305 334 334 ASN ASN D . n 
B 1 306 THR 306 335 335 THR THR D . n 
B 1 307 LEU 307 336 336 LEU LEU D . n 
B 1 308 ASN 308 337 337 ASN ASN D . n 
B 1 309 SER 309 338 338 SER SER D . n 
B 1 310 GLY 310 339 339 GLY GLY D . n 
B 1 311 ARG 311 340 340 ARG ARG D . n 
B 1 312 VAL 312 341 341 VAL VAL D . n 
B 1 313 VAL 313 342 342 VAL VAL D . n 
B 1 314 PRO 314 343 343 PRO PRO D . n 
B 1 315 GLY 315 344 344 GLY GLY D . n 
B 1 316 TYR 316 345 345 TYR TYR D . n 
B 1 317 GLY 317 346 346 GLY GLY D . n 
B 1 318 HIS 318 347 347 HIS HIS D . n 
B 1 319 ALA 319 348 348 ALA ALA D . n 
B 1 320 VAL 320 349 349 VAL VAL D . n 
B 1 321 LEU 321 350 350 LEU LEU D . n 
B 1 322 ARG 322 351 351 ARG ARG D . n 
B 1 323 LYS 323 352 352 LYS LYS D . n 
B 1 324 THR 324 353 353 THR THR D . n 
B 1 325 ASP 325 354 354 ASP ASP D . n 
B 1 326 PRO 326 355 355 PRO PRO D . n 
B 1 327 ARG 327 356 356 ARG ARG D . n 
B 1 328 TYR 328 357 357 TYR TYR D . n 
B 1 329 THR 329 358 358 THR THR D . n 
B 1 330 CYS 330 359 359 CYS CYS D . n 
B 1 331 GLN 331 360 360 GLN GLN D . n 
B 1 332 ARG 332 361 361 ARG ARG D . n 
B 1 333 GLU 333 362 362 GLU GLU D . n 
B 1 334 PHE 334 363 363 PHE PHE D . n 
B 1 335 ALA 335 364 364 ALA ALA D . n 
B 1 336 LEU 336 365 365 LEU LEU D . n 
B 1 337 LYS 337 366 366 LYS LYS D . n 
B 1 338 HIS 338 367 367 HIS HIS D . n 
B 1 339 LEU 339 368 368 LEU LEU D . n 
B 1 340 PRO 340 369 369 PRO PRO D . n 
B 1 341 ASN 341 370 370 ASN ASN D . n 
B 1 342 ASP 342 371 371 ASP ASP D . n 
B 1 343 PRO 343 372 372 PRO PRO D . n 
B 1 344 MET 344 373 373 MET MET D . n 
B 1 345 PHE 345 374 374 PHE PHE D . n 
B 1 346 LYS 346 375 375 LYS LYS D . n 
B 1 347 LEU 347 376 376 LEU LEU D . n 
B 1 348 VAL 348 377 377 VAL VAL D . n 
B 1 349 ALA 349 378 378 ALA ALA D . n 
B 1 350 GLN 350 379 379 GLN GLN D . n 
B 1 351 LEU 351 380 380 LEU LEU D . n 
B 1 352 TYR 352 381 381 TYR TYR D . n 
B 1 353 LYS 353 382 382 LYS LYS D . n 
B 1 354 ILE 354 383 383 ILE ILE D . n 
B 1 355 VAL 355 384 384 VAL VAL D . n 
B 1 356 PRO 356 385 385 PRO PRO D . n 
B 1 357 ASN 357 386 386 ASN ASN D . n 
B 1 358 VAL 358 387 387 VAL VAL D . n 
B 1 359 LEU 359 388 388 LEU LEU D . n 
B 1 360 LEU 360 389 389 LEU LEU D . n 
B 1 361 GLU 361 390 390 GLU GLU D . n 
B 1 362 GLN 362 391 391 GLN GLN D . n 
B 1 363 GLY 363 392 392 GLY GLY D . n 
B 1 364 LYS 364 393 393 LYS LYS D . n 
B 1 365 ALA 365 394 394 ALA ALA D . n 
B 1 366 LYS 366 395 395 LYS LYS D . n 
B 1 367 ASN 367 396 396 ASN ASN D . n 
B 1 368 PRO 368 397 397 PRO PRO D . n 
B 1 369 TRP 369 398 398 TRP TRP D . n 
B 1 370 PRO 370 399 399 PRO PRO D . n 
B 1 371 ASN 371 400 400 ASN ASN D . n 
B 1 372 VAL 372 401 401 VAL VAL D . n 
B 1 373 ASP 373 402 402 ASP ASP D . n 
B 1 374 ALA 374 403 403 ALA ALA D . n 
B 1 375 HIS 375 404 404 HIS HIS D . n 
B 1 376 SER 376 405 405 SER SER D . n 
B 1 377 GLY 377 406 406 GLY GLY D . n 
B 1 378 VAL 378 407 407 VAL VAL D . n 
B 1 379 LEU 379 408 408 LEU LEU D . n 
B 1 380 LEU 380 409 409 LEU LEU D . n 
B 1 381 GLN 381 410 410 GLN GLN D . n 
B 1 382 TYR 382 411 411 TYR TYR D . n 
B 1 383 TYR 383 412 412 TYR TYR D . n 
B 1 384 GLY 384 413 413 GLY GLY D . n 
B 1 385 MET 385 414 414 MET MET D . n 
B 1 386 THR 386 415 415 THR THR D . n 
B 1 387 GLU 387 416 416 GLU GLU D . n 
B 1 388 MET 388 417 417 MET MET D . n 
B 1 389 ASN 389 418 418 ASN ASN D . n 
B 1 390 TYR 390 419 419 TYR TYR D . n 
B 1 391 TYR 391 420 420 TYR TYR D . n 
B 1 392 THR 392 421 421 THR THR D . n 
B 1 393 VAL 393 422 422 VAL VAL D . n 
B 1 394 LEU 394 423 423 LEU LEU D . n 
B 1 395 PHE 395 424 424 PHE PHE D . n 
B 1 396 GLY 396 425 425 GLY GLY D . n 
B 1 397 VAL 397 426 426 VAL VAL D . n 
B 1 398 SER 398 427 427 SER SER D . n 
B 1 399 ARG 399 428 428 ARG ARG D . n 
B 1 400 ALA 400 429 429 ALA ALA D . n 
B 1 401 LEU 401 430 430 LEU LEU D . n 
B 1 402 GLY 402 431 431 GLY GLY D . n 
B 1 403 VAL 403 432 432 VAL VAL D . n 
B 1 404 LEU 404 433 433 LEU LEU D . n 
B 1 405 ALA 405 434 434 ALA ALA D . n 
B 1 406 GLN 406 435 435 GLN GLN D . n 
B 1 407 LEU 407 436 436 LEU LEU D . n 
B 1 408 ILE 408 437 437 ILE ILE D . n 
B 1 409 TRP 409 438 438 TRP TRP D . n 
B 1 410 SER 410 439 439 SER SER D . n 
B 1 411 ARG 411 440 440 ARG ARG D . n 
B 1 412 ALA 412 441 441 ALA ALA D . n 
B 1 413 LEU 413 442 442 LEU LEU D . n 
B 1 414 GLY 414 443 443 GLY GLY D . n 
B 1 415 PHE 415 444 444 PHE PHE D . n 
B 1 416 PRO 416 445 445 PRO PRO D . n 
B 1 417 LEU 417 446 446 LEU LEU D . n 
B 1 418 GLU 418 447 447 GLU GLU D . n 
B 1 419 ARG 419 448 448 ARG ARG D . n 
B 1 420 PRO 420 449 449 PRO PRO D . n 
B 1 421 LYS 421 450 450 LYS LYS D . n 
B 1 422 SER 422 451 451 SER SER D . n 
B 1 423 MET 423 452 452 MET MET D . n 
B 1 424 SER 424 453 453 SER SER D . n 
B 1 425 THR 425 454 454 THR THR D . n 
B 1 426 GLU 426 455 455 GLU GLU D . n 
B 1 427 GLY 427 456 456 GLY GLY D . n 
B 1 428 LEU 428 457 457 LEU LEU D . n 
B 1 429 MET 429 458 458 MET MET D . n 
B 1 430 LYS 430 459 459 LYS LYS D . n 
B 1 431 PHE 431 460 460 PHE PHE D . n 
B 1 432 VAL 432 461 461 VAL VAL D . n 
B 1 433 ASP 433 462 462 ASP ASP D . n 
B 1 434 SER 434 463 463 SER SER D . n 
B 1 435 LYS 435 464 464 LYS LYS D . n 
C 1 1   SER 1   30  30  SER SER B . n 
C 1 2   THR 2   31  31  THR THR B . n 
C 1 3   ASN 3   32  32  ASN ASN B . n 
C 1 4   LEU 4   33  33  LEU LEU B . n 
C 1 5   LYS 5   34  34  LYS LYS B . n 
C 1 6   ASP 6   35  35  ASP ASP B . n 
C 1 7   ILE 7   36  36  ILE ILE B . n 
C 1 8   LEU 8   37  37  LEU LEU B . n 
C 1 9   ALA 9   38  38  ALA ALA B . n 
C 1 10  ASP 10  39  39  ASP ASP B . n 
C 1 11  LEU 11  40  40  LEU LEU B . n 
C 1 12  ILE 12  41  41  ILE ILE B . n 
C 1 13  PRO 13  42  42  PRO PRO B . n 
C 1 14  LYS 14  43  43  LYS LYS B . n 
C 1 15  GLU 15  44  44  GLU GLU B . n 
C 1 16  GLN 16  45  45  GLN GLN B . n 
C 1 17  ALA 17  46  46  ALA ALA B . n 
C 1 18  ARG 18  47  47  ARG ARG B . n 
C 1 19  ILE 19  48  48  ILE ILE B . n 
C 1 20  LYS 20  49  49  LYS LYS B . n 
C 1 21  THR 21  50  50  THR THR B . n 
C 1 22  PHE 22  51  51  PHE PHE B . n 
C 1 23  ARG 23  52  52  ARG ARG B . n 
C 1 24  GLN 24  53  53  GLN GLN B . n 
C 1 25  GLN 25  54  54  GLN GLN B . n 
C 1 26  HIS 26  55  55  HIS HIS B . n 
C 1 27  GLY 27  56  56  GLY GLY B . n 
C 1 28  LYS 28  57  57  LYS LYS B . n 
C 1 29  THR 29  58  58  THR THR B . n 
C 1 30  VAL 30  59  59  VAL VAL B . n 
C 1 31  VAL 31  60  60  VAL VAL B . n 
C 1 32  GLY 32  61  61  GLY GLY B . n 
C 1 33  GLN 33  62  62  GLN GLN B . n 
C 1 34  ILE 34  63  63  ILE ILE B . n 
C 1 35  THR 35  64  64  THR THR B . n 
C 1 36  VAL 36  65  65  VAL VAL B . n 
C 1 37  ASP 37  66  66  ASP ASP B . n 
C 1 38  MET 38  67  67  MET MET B . n 
C 1 39  MET 39  68  68  MET MET B . n 
C 1 40  TYR 40  69  69  TYR TYR B . n 
C 1 41  GLY 41  70  70  GLY GLY B . n 
C 1 42  GLY 42  71  71  GLY GLY B . n 
C 1 43  MET 43  72  72  MET MET B . n 
C 1 44  ARG 44  73  73  ARG ARG B . n 
C 1 45  GLY 45  74  74  GLY GLY B . n 
C 1 46  MET 46  75  75  MET MET B . n 
C 1 47  LYS 47  76  76  LYS LYS B . n 
C 1 48  GLY 48  77  77  GLY GLY B . n 
C 1 49  LEU 49  78  78  LEU LEU B . n 
C 1 50  VAL 50  79  79  VAL VAL B . n 
C 1 51  TYR 51  80  80  TYR TYR B . n 
C 1 52  GLU 52  81  81  GLU GLU B . n 
C 1 53  THR 53  82  82  THR THR B . n 
C 1 54  SER 54  83  83  SER SER B . n 
C 1 55  VAL 55  84  84  VAL VAL B . n 
C 1 56  LEU 56  85  85  LEU LEU B . n 
C 1 57  ASP 57  86  86  ASP ASP B . n 
C 1 58  PRO 58  87  87  PRO PRO B . n 
C 1 59  ASP 59  88  88  ASP ASP B . n 
C 1 60  GLU 60  89  89  GLU GLU B . n 
C 1 61  GLY 61  90  90  GLY GLY B . n 
C 1 62  ILE 62  91  91  ILE ILE B . n 
C 1 63  ARG 63  92  92  ARG ARG B . n 
C 1 64  PHE 64  93  93  PHE PHE B . n 
C 1 65  ARG 65  94  94  ARG ARG B . n 
C 1 66  GLY 66  95  95  GLY GLY B . n 
C 1 67  PHE 67  96  96  PHE PHE B . n 
C 1 68  SER 68  97  97  SER SER B . n 
C 1 69  ILE 69  98  98  ILE ILE B . n 
C 1 70  PRO 70  99  99  PRO PRO B . n 
C 1 71  GLU 71  100 100 GLU GLU B . n 
C 1 72  CYS 72  101 101 CYS CYS B . n 
C 1 73  GLN 73  102 102 GLN GLN B . n 
C 1 74  LYS 74  103 103 LYS LYS B . n 
C 1 75  LEU 75  104 104 LEU LEU B . n 
C 1 76  LEU 76  105 105 LEU LEU B . n 
C 1 77  PRO 77  106 106 PRO PRO B . n 
C 1 78  LYS 78  107 107 LYS LYS B . n 
C 1 79  ALA 79  108 108 ALA ALA B . n 
C 1 80  LYS 80  109 109 LYS LYS B . n 
C 1 81  GLY 81  110 110 GLY GLY B . n 
C 1 82  GLY 82  111 111 GLY GLY B . n 
C 1 83  GLU 83  112 112 GLU GLU B . n 
C 1 84  GLU 84  113 113 GLU GLU B . n 
C 1 85  PRO 85  114 114 PRO PRO B . n 
C 1 86  LEU 86  115 115 LEU LEU B . n 
C 1 87  PRO 87  116 116 PRO PRO B . n 
C 1 88  GLU 88  117 117 GLU GLU B . n 
C 1 89  GLY 89  118 118 GLY GLY B . n 
C 1 90  LEU 90  119 119 LEU LEU B . n 
C 1 91  PHE 91  120 120 PHE PHE B . n 
C 1 92  TRP 92  121 121 TRP TRP B . n 
C 1 93  LEU 93  122 122 LEU LEU B . n 
C 1 94  LEU 94  123 123 LEU LEU B . n 
C 1 95  VAL 95  124 124 VAL VAL B . n 
C 1 96  THR 96  125 125 THR THR B . n 
C 1 97  GLY 97  126 126 GLY GLY B . n 
C 1 98  HIS 98  127 127 HIS HIS B . n 
C 1 99  ILE 99  128 128 ILE ILE B . n 
C 1 100 PRO 100 129 129 PRO PRO B . n 
C 1 101 THR 101 130 130 THR THR B . n 
C 1 102 GLU 102 131 131 GLU GLU B . n 
C 1 103 GLU 103 132 132 GLU GLU B . n 
C 1 104 GLN 104 133 133 GLN GLN B . n 
C 1 105 VAL 105 134 134 VAL VAL B . n 
C 1 106 SER 106 135 135 SER SER B . n 
C 1 107 TRP 107 136 136 TRP TRP B . n 
C 1 108 LEU 108 137 137 LEU LEU B . n 
C 1 109 SER 109 138 138 SER SER B . n 
C 1 110 LYS 110 139 139 LYS LYS B . n 
C 1 111 GLU 111 140 140 GLU GLU B . n 
C 1 112 TRP 112 141 141 TRP TRP B . n 
C 1 113 ALA 113 142 142 ALA ALA B . n 
C 1 114 LYS 114 143 143 LYS LYS B . n 
C 1 115 ARG 115 144 144 ARG ARG B . n 
C 1 116 ALA 116 145 145 ALA ALA B . n 
C 1 117 ALA 117 146 146 ALA ALA B . n 
C 1 118 LEU 118 147 147 LEU LEU B . n 
C 1 119 PRO 119 148 148 PRO PRO B . n 
C 1 120 SER 120 149 149 SER SER B . n 
C 1 121 HIS 121 150 150 HIS HIS B . n 
C 1 122 VAL 122 151 151 VAL VAL B . n 
C 1 123 VAL 123 152 152 VAL VAL B . n 
C 1 124 THR 124 153 153 THR THR B . n 
C 1 125 MET 125 154 154 MET MET B . n 
C 1 126 LEU 126 155 155 LEU LEU B . n 
C 1 127 ASP 127 156 156 ASP ASP B . n 
C 1 128 ASN 128 157 157 ASN ASN B . n 
C 1 129 PHE 129 158 158 PHE PHE B . n 
C 1 130 PRO 130 159 159 PRO PRO B . n 
C 1 131 THR 131 160 160 THR THR B . n 
C 1 132 ASN 132 161 161 ASN ASN B . n 
C 1 133 LEU 133 162 162 LEU LEU B . n 
C 1 134 HIS 134 163 163 HIS HIS B . n 
C 1 135 PRO 135 164 164 PRO PRO B . n 
C 1 136 MET 136 165 165 MET MET B . n 
C 1 137 SER 137 166 166 SER SER B . n 
C 1 138 GLN 138 167 167 GLN GLN B . n 
C 1 139 LEU 139 168 168 LEU LEU B . n 
C 1 140 SER 140 169 169 SER SER B . n 
C 1 141 ALA 141 170 170 ALA ALA B . n 
C 1 142 ALA 142 171 171 ALA ALA B . n 
C 1 143 VAL 143 172 172 VAL VAL B . n 
C 1 144 THR 144 173 173 THR THR B . n 
C 1 145 ALA 145 174 174 ALA ALA B . n 
C 1 146 LEU 146 175 175 LEU LEU B . n 
C 1 147 ASN 147 176 176 ASN ASN B . n 
C 1 148 SER 148 177 177 SER SER B . n 
C 1 149 GLU 149 178 178 GLU GLU B . n 
C 1 150 SER 150 179 179 SER SER B . n 
C 1 151 ASN 151 180 180 ASN ASN B . n 
C 1 152 PHE 152 181 181 PHE PHE B . n 
C 1 153 ALA 153 182 182 ALA ALA B . n 
C 1 154 ARG 154 183 183 ARG ARG B . n 
C 1 155 ALA 155 184 184 ALA ALA B . n 
C 1 156 TYR 156 185 185 TYR TYR B . n 
C 1 157 ALA 157 186 186 ALA ALA B . n 
C 1 158 GLN 158 187 187 GLN GLN B . n 
C 1 159 GLY 159 188 188 GLY GLY B . n 
C 1 160 ILE 160 189 189 ILE ILE B . n 
C 1 161 SER 161 190 190 SER SER B . n 
C 1 162 ARG 162 191 191 ARG ARG B . n 
C 1 163 THR 163 192 192 THR THR B . n 
C 1 164 LYS 164 193 193 LYS LYS B . n 
C 1 165 TYR 165 194 194 TYR TYR B . n 
C 1 166 TRP 166 195 195 TRP TRP B . n 
C 1 167 GLU 167 196 196 GLU GLU B . n 
C 1 168 LEU 168 197 197 LEU LEU B . n 
C 1 169 ILE 169 198 198 ILE ILE B . n 
C 1 170 TYR 170 199 199 TYR TYR B . n 
C 1 171 GLU 171 200 200 GLU GLU B . n 
C 1 172 ASP 172 201 201 ASP ASP B . n 
C 1 173 SER 173 202 202 SER SER B . n 
C 1 174 MET 174 203 203 MET MET B . n 
C 1 175 ASP 175 204 204 ASP ASP B . n 
C 1 176 LEU 176 205 205 LEU LEU B . n 
C 1 177 ILE 177 206 206 ILE ILE B . n 
C 1 178 ALA 178 207 207 ALA ALA B . n 
C 1 179 LYS 179 208 208 LYS LYS B . n 
C 1 180 LEU 180 209 209 LEU LEU B . n 
C 1 181 PRO 181 210 210 PRO PRO B . n 
C 1 182 CYS 182 211 211 CYS CYS B . n 
C 1 183 VAL 183 212 212 VAL VAL B . n 
C 1 184 ALA 184 213 213 ALA ALA B . n 
C 1 185 ALA 185 214 214 ALA ALA B . n 
C 1 186 LYS 186 215 215 LYS LYS B . n 
C 1 187 ILE 187 216 216 ILE ILE B . n 
C 1 188 TYR 188 217 217 TYR TYR B . n 
C 1 189 ARG 189 218 218 ARG ARG B . n 
C 1 190 ASN 190 219 219 ASN ASN B . n 
C 1 191 LEU 191 220 220 LEU LEU B . n 
C 1 192 TYR 192 221 221 TYR TYR B . n 
C 1 193 ARG 193 222 222 ARG ARG B . n 
C 1 194 GLU 194 223 223 GLU GLU B . n 
C 1 195 GLY 195 224 224 GLY GLY B . n 
C 1 196 SER 196 225 225 SER SER B . n 
C 1 197 GLY 197 226 226 GLY GLY B . n 
C 1 198 ILE 198 227 227 ILE ILE B . n 
C 1 199 GLY 199 228 228 GLY GLY B . n 
C 1 200 ALA 200 229 229 ALA ALA B . n 
C 1 201 ILE 201 230 230 ILE ILE B . n 
C 1 202 ASP 202 231 231 ASP ASP B . n 
C 1 203 SER 203 232 232 SER SER B . n 
C 1 204 ASN 204 233 233 ASN ASN B . n 
C 1 205 LEU 205 234 234 LEU LEU B . n 
C 1 206 ASP 206 235 235 ASP ASP B . n 
C 1 207 TRP 207 236 236 TRP TRP B . n 
C 1 208 SER 208 237 237 SER SER B . n 
C 1 209 HIS 209 238 238 HIS HIS B . n 
C 1 210 ASN 210 239 239 ASN ASN B . n 
C 1 211 PHE 211 240 240 PHE PHE B . n 
C 1 212 THR 212 241 241 THR THR B . n 
C 1 213 ASN 213 242 242 ASN ASN B . n 
C 1 214 MET 214 243 243 MET MET B . n 
C 1 215 LEU 215 244 244 LEU LEU B . n 
C 1 216 GLY 216 245 245 GLY GLY B . n 
C 1 217 TYR 217 246 246 TYR TYR B . n 
C 1 218 THR 218 247 247 THR THR B . n 
C 1 219 ASP 219 248 248 ASP ASP B . n 
C 1 220 HIS 220 249 249 HIS HIS B . n 
C 1 221 GLN 221 250 250 GLN GLN B . n 
C 1 222 PHE 222 251 251 PHE PHE B . n 
C 1 223 THR 223 252 252 THR THR B . n 
C 1 224 GLU 224 253 253 GLU GLU B . n 
C 1 225 LEU 225 254 254 LEU LEU B . n 
C 1 226 THR 226 255 255 THR THR B . n 
C 1 227 ARG 227 256 256 ARG ARG B . n 
C 1 228 LEU 228 257 257 LEU LEU B . n 
C 1 229 TYR 229 258 258 TYR TYR B . n 
C 1 230 LEU 230 259 259 LEU LEU B . n 
C 1 231 THR 231 260 260 THR THR B . n 
C 1 232 ILE 232 261 261 ILE ILE B . n 
C 1 233 HIS 233 262 262 HIS HIS B . n 
C 1 234 SER 234 263 263 SER SER B . n 
C 1 235 ASP 235 264 264 ASP ASP B . n 
C 1 236 HIS 236 265 265 HIS HIS B . n 
C 1 237 GLU 237 266 266 GLU GLU B . n 
C 1 238 GLY 238 267 267 GLY GLY B . n 
C 1 239 GLY 239 268 268 GLY GLY B . n 
C 1 240 ASN 240 269 269 ASN ASN B . n 
C 1 241 VAL 241 270 270 VAL VAL B . n 
C 1 242 SER 242 271 271 SER SER B . n 
C 1 243 ALA 243 272 272 ALA ALA B . n 
C 1 244 HIS 244 273 273 HIS HIS B . n 
C 1 245 THR 245 274 274 THR THR B . n 
C 1 246 SER 246 275 275 SER SER B . n 
C 1 247 HIS 247 276 276 HIS HIS B . n 
C 1 248 LEU 248 277 277 LEU LEU B . n 
C 1 249 VAL 249 278 278 VAL VAL B . n 
C 1 250 GLY 250 279 279 GLY GLY B . n 
C 1 251 SER 251 280 280 SER SER B . n 
C 1 252 ALA 252 281 281 ALA ALA B . n 
C 1 253 LEU 253 282 282 LEU LEU B . n 
C 1 254 SER 254 283 283 SER SER B . n 
C 1 255 ASP 255 284 284 ASP ASP B . n 
C 1 256 PRO 256 285 285 PRO PRO B . n 
C 1 257 TYR 257 286 286 TYR TYR B . n 
C 1 258 LEU 258 287 287 LEU LEU B . n 
C 1 259 SER 259 288 288 SER SER B . n 
C 1 260 PHE 260 289 289 PHE PHE B . n 
C 1 261 ALA 261 290 290 ALA ALA B . n 
C 1 262 ALA 262 291 291 ALA ALA B . n 
C 1 263 ALA 263 292 292 ALA ALA B . n 
C 1 264 MET 264 293 293 MET MET B . n 
C 1 265 ASN 265 294 294 ASN ASN B . n 
C 1 266 GLY 266 295 295 GLY GLY B . n 
C 1 267 LEU 267 296 296 LEU LEU B . n 
C 1 268 ALA 268 297 297 ALA ALA B . n 
C 1 269 GLY 269 298 298 GLY GLY B . n 
C 1 270 PRO 270 299 299 PRO PRO B . n 
C 1 271 LEU 271 300 300 LEU LEU B . n 
C 1 272 HIS 272 301 301 HIS HIS B . n 
C 1 273 GLY 273 302 302 GLY GLY B . n 
C 1 274 LEU 274 303 303 LEU LEU B . n 
C 1 275 ALA 275 304 304 ALA ALA B . n 
C 1 276 ASN 276 305 305 ASN ASN B . n 
C 1 277 GLN 277 306 306 GLN GLN B . n 
C 1 278 GLU 278 307 307 GLU GLU B . n 
C 1 279 VAL 279 308 308 VAL VAL B . n 
C 1 280 LEU 280 309 309 LEU LEU B . n 
C 1 281 VAL 281 310 310 VAL VAL B . n 
C 1 282 TRP 282 311 311 TRP TRP B . n 
C 1 283 LEU 283 312 312 LEU LEU B . n 
C 1 284 THR 284 313 313 THR THR B . n 
C 1 285 GLN 285 314 314 GLN GLN B . n 
C 1 286 LEU 286 315 315 LEU LEU B . n 
C 1 287 GLN 287 316 316 GLN GLN B . n 
C 1 288 LYS 288 317 317 LYS LYS B . n 
C 1 289 GLU 289 318 318 GLU GLU B . n 
C 1 290 VAL 290 319 319 VAL VAL B . n 
C 1 291 GLY 291 320 320 GLY GLY B . n 
C 1 292 LYS 292 321 321 LYS LYS B . n 
C 1 293 ASP 293 322 322 ASP ASP B . n 
C 1 294 VAL 294 323 323 VAL VAL B . n 
C 1 295 SER 295 324 324 SER SER B . n 
C 1 296 ASP 296 325 325 ASP ASP B . n 
C 1 297 GLU 297 326 326 GLU GLU B . n 
C 1 298 LYS 298 327 327 LYS LYS B . n 
C 1 299 LEU 299 328 328 LEU LEU B . n 
C 1 300 ARG 300 329 329 ARG ARG B . n 
C 1 301 ASP 301 330 330 ASP ASP B . n 
C 1 302 TYR 302 331 331 TYR TYR B . n 
C 1 303 ILE 303 332 332 ILE ILE B . n 
C 1 304 TRP 304 333 333 TRP TRP B . n 
C 1 305 ASN 305 334 334 ASN ASN B . n 
C 1 306 THR 306 335 335 THR THR B . n 
C 1 307 LEU 307 336 336 LEU LEU B . n 
C 1 308 ASN 308 337 337 ASN ASN B . n 
C 1 309 SER 309 338 338 SER SER B . n 
C 1 310 GLY 310 339 339 GLY GLY B . n 
C 1 311 ARG 311 340 340 ARG ARG B . n 
C 1 312 VAL 312 341 341 VAL VAL B . n 
C 1 313 VAL 313 342 342 VAL VAL B . n 
C 1 314 PRO 314 343 343 PRO PRO B . n 
C 1 315 GLY 315 344 344 GLY GLY B . n 
C 1 316 TYR 316 345 345 TYR TYR B . n 
C 1 317 GLY 317 346 346 GLY GLY B . n 
C 1 318 HIS 318 347 347 HIS HIS B . n 
C 1 319 ALA 319 348 348 ALA ALA B . n 
C 1 320 VAL 320 349 349 VAL VAL B . n 
C 1 321 LEU 321 350 350 LEU LEU B . n 
C 1 322 ARG 322 351 351 ARG ARG B . n 
C 1 323 LYS 323 352 352 LYS LYS B . n 
C 1 324 THR 324 353 353 THR THR B . n 
C 1 325 ASP 325 354 354 ASP ASP B . n 
C 1 326 PRO 326 355 355 PRO PRO B . n 
C 1 327 ARG 327 356 356 ARG ARG B . n 
C 1 328 TYR 328 357 357 TYR TYR B . n 
C 1 329 THR 329 358 358 THR THR B . n 
C 1 330 CYS 330 359 359 CYS CYS B . n 
C 1 331 GLN 331 360 360 GLN GLN B . n 
C 1 332 ARG 332 361 361 ARG ARG B . n 
C 1 333 GLU 333 362 362 GLU GLU B . n 
C 1 334 PHE 334 363 363 PHE PHE B . n 
C 1 335 ALA 335 364 364 ALA ALA B . n 
C 1 336 LEU 336 365 365 LEU LEU B . n 
C 1 337 LYS 337 366 366 LYS LYS B . n 
C 1 338 HIS 338 367 367 HIS HIS B . n 
C 1 339 LEU 339 368 368 LEU LEU B . n 
C 1 340 PRO 340 369 369 PRO PRO B . n 
C 1 341 ASN 341 370 370 ASN ASN B . n 
C 1 342 ASP 342 371 371 ASP ASP B . n 
C 1 343 PRO 343 372 372 PRO PRO B . n 
C 1 344 MET 344 373 373 MET MET B . n 
C 1 345 PHE 345 374 374 PHE PHE B . n 
C 1 346 LYS 346 375 375 LYS LYS B . n 
C 1 347 LEU 347 376 376 LEU LEU B . n 
C 1 348 VAL 348 377 377 VAL VAL B . n 
C 1 349 ALA 349 378 378 ALA ALA B . n 
C 1 350 GLN 350 379 379 GLN GLN B . n 
C 1 351 LEU 351 380 380 LEU LEU B . n 
C 1 352 TYR 352 381 381 TYR TYR B . n 
C 1 353 LYS 353 382 382 LYS LYS B . n 
C 1 354 ILE 354 383 383 ILE ILE B . n 
C 1 355 VAL 355 384 384 VAL VAL B . n 
C 1 356 PRO 356 385 385 PRO PRO B . n 
C 1 357 ASN 357 386 386 ASN ASN B . n 
C 1 358 VAL 358 387 387 VAL VAL B . n 
C 1 359 LEU 359 388 388 LEU LEU B . n 
C 1 360 LEU 360 389 389 LEU LEU B . n 
C 1 361 GLU 361 390 390 GLU GLU B . n 
C 1 362 GLN 362 391 391 GLN GLN B . n 
C 1 363 GLY 363 392 392 GLY GLY B . n 
C 1 364 LYS 364 393 393 LYS LYS B . n 
C 1 365 ALA 365 394 394 ALA ALA B . n 
C 1 366 LYS 366 395 395 LYS LYS B . n 
C 1 367 ASN 367 396 396 ASN ASN B . n 
C 1 368 PRO 368 397 397 PRO PRO B . n 
C 1 369 TRP 369 398 398 TRP TRP B . n 
C 1 370 PRO 370 399 399 PRO PRO B . n 
C 1 371 ASN 371 400 400 ASN ASN B . n 
C 1 372 VAL 372 401 401 VAL VAL B . n 
C 1 373 ASP 373 402 402 ASP ASP B . n 
C 1 374 ALA 374 403 403 ALA ALA B . n 
C 1 375 HIS 375 404 404 HIS HIS B . n 
C 1 376 SER 376 405 405 SER SER B . n 
C 1 377 GLY 377 406 406 GLY GLY B . n 
C 1 378 VAL 378 407 407 VAL VAL B . n 
C 1 379 LEU 379 408 408 LEU LEU B . n 
C 1 380 LEU 380 409 409 LEU LEU B . n 
C 1 381 GLN 381 410 410 GLN GLN B . n 
C 1 382 TYR 382 411 411 TYR TYR B . n 
C 1 383 TYR 383 412 412 TYR TYR B . n 
C 1 384 GLY 384 413 413 GLY GLY B . n 
C 1 385 MET 385 414 414 MET MET B . n 
C 1 386 THR 386 415 415 THR THR B . n 
C 1 387 GLU 387 416 416 GLU GLU B . n 
C 1 388 MET 388 417 417 MET MET B . n 
C 1 389 ASN 389 418 418 ASN ASN B . n 
C 1 390 TYR 390 419 419 TYR TYR B . n 
C 1 391 TYR 391 420 420 TYR TYR B . n 
C 1 392 THR 392 421 421 THR THR B . n 
C 1 393 VAL 393 422 422 VAL VAL B . n 
C 1 394 LEU 394 423 423 LEU LEU B . n 
C 1 395 PHE 395 424 424 PHE PHE B . n 
C 1 396 GLY 396 425 425 GLY GLY B . n 
C 1 397 VAL 397 426 426 VAL VAL B . n 
C 1 398 SER 398 427 427 SER SER B . n 
C 1 399 ARG 399 428 428 ARG ARG B . n 
C 1 400 ALA 400 429 429 ALA ALA B . n 
C 1 401 LEU 401 430 430 LEU LEU B . n 
C 1 402 GLY 402 431 431 GLY GLY B . n 
C 1 403 VAL 403 432 432 VAL VAL B . n 
C 1 404 LEU 404 433 433 LEU LEU B . n 
C 1 405 ALA 405 434 434 ALA ALA B . n 
C 1 406 GLN 406 435 435 GLN GLN B . n 
C 1 407 LEU 407 436 436 LEU LEU B . n 
C 1 408 ILE 408 437 437 ILE ILE B . n 
C 1 409 TRP 409 438 438 TRP TRP B . n 
C 1 410 SER 410 439 439 SER SER B . n 
C 1 411 ARG 411 440 440 ARG ARG B . n 
C 1 412 ALA 412 441 441 ALA ALA B . n 
C 1 413 LEU 413 442 442 LEU LEU B . n 
C 1 414 GLY 414 443 443 GLY GLY B . n 
C 1 415 PHE 415 444 444 PHE PHE B . n 
C 1 416 PRO 416 445 445 PRO PRO B . n 
C 1 417 LEU 417 446 446 LEU LEU B . n 
C 1 418 GLU 418 447 447 GLU GLU B . n 
C 1 419 ARG 419 448 448 ARG ARG B . n 
C 1 420 PRO 420 449 449 PRO PRO B . n 
C 1 421 LYS 421 450 450 LYS LYS B . n 
C 1 422 SER 422 451 451 SER SER B . n 
C 1 423 MET 423 452 452 MET MET B . n 
C 1 424 SER 424 453 453 SER SER B . n 
C 1 425 THR 425 454 454 THR THR B . n 
C 1 426 GLU 426 455 455 GLU GLU B . n 
C 1 427 GLY 427 456 456 GLY GLY B . n 
C 1 428 LEU 428 457 457 LEU LEU B . n 
C 1 429 MET 429 458 458 MET MET B . n 
C 1 430 LYS 430 459 459 LYS LYS B . n 
C 1 431 PHE 431 460 460 PHE PHE B . n 
C 1 432 VAL 432 461 461 VAL VAL B . n 
C 1 433 ASP 433 462 462 ASP ASP B . n 
C 1 434 SER 434 463 463 SER SER B . n 
C 1 435 LYS 435 464 ?   ?   ?   B . n 
D 1 1   SER 1   30  30  SER SER C . n 
D 1 2   THR 2   31  31  THR THR C . n 
D 1 3   ASN 3   32  32  ASN ASN C . n 
D 1 4   LEU 4   33  33  LEU LEU C . n 
D 1 5   LYS 5   34  34  LYS LYS C . n 
D 1 6   ASP 6   35  35  ASP ASP C . n 
D 1 7   ILE 7   36  36  ILE ILE C . n 
D 1 8   LEU 8   37  37  LEU LEU C . n 
D 1 9   ALA 9   38  38  ALA ALA C . n 
D 1 10  ASP 10  39  39  ASP ASP C . n 
D 1 11  LEU 11  40  40  LEU LEU C . n 
D 1 12  ILE 12  41  41  ILE ILE C . n 
D 1 13  PRO 13  42  42  PRO PRO C . n 
D 1 14  LYS 14  43  43  LYS LYS C . n 
D 1 15  GLU 15  44  44  GLU GLU C . n 
D 1 16  GLN 16  45  45  GLN GLN C . n 
D 1 17  ALA 17  46  46  ALA ALA C . n 
D 1 18  ARG 18  47  47  ARG ARG C . n 
D 1 19  ILE 19  48  48  ILE ILE C . n 
D 1 20  LYS 20  49  49  LYS LYS C . n 
D 1 21  THR 21  50  50  THR THR C . n 
D 1 22  PHE 22  51  51  PHE PHE C . n 
D 1 23  ARG 23  52  52  ARG ARG C . n 
D 1 24  GLN 24  53  53  GLN GLN C . n 
D 1 25  GLN 25  54  54  GLN GLN C . n 
D 1 26  HIS 26  55  55  HIS HIS C . n 
D 1 27  GLY 27  56  56  GLY GLY C . n 
D 1 28  LYS 28  57  57  LYS LYS C . n 
D 1 29  THR 29  58  58  THR THR C . n 
D 1 30  VAL 30  59  59  VAL VAL C . n 
D 1 31  VAL 31  60  60  VAL VAL C . n 
D 1 32  GLY 32  61  61  GLY GLY C . n 
D 1 33  GLN 33  62  62  GLN GLN C . n 
D 1 34  ILE 34  63  63  ILE ILE C . n 
D 1 35  THR 35  64  64  THR THR C . n 
D 1 36  VAL 36  65  65  VAL VAL C . n 
D 1 37  ASP 37  66  66  ASP ASP C . n 
D 1 38  MET 38  67  67  MET MET C . n 
D 1 39  MET 39  68  68  MET MET C . n 
D 1 40  TYR 40  69  69  TYR TYR C . n 
D 1 41  GLY 41  70  70  GLY GLY C . n 
D 1 42  GLY 42  71  71  GLY GLY C . n 
D 1 43  MET 43  72  72  MET MET C . n 
D 1 44  ARG 44  73  73  ARG ARG C . n 
D 1 45  GLY 45  74  74  GLY GLY C . n 
D 1 46  MET 46  75  75  MET MET C . n 
D 1 47  LYS 47  76  76  LYS LYS C . n 
D 1 48  GLY 48  77  77  GLY GLY C . n 
D 1 49  LEU 49  78  78  LEU LEU C . n 
D 1 50  VAL 50  79  79  VAL VAL C . n 
D 1 51  TYR 51  80  80  TYR TYR C . n 
D 1 52  GLU 52  81  81  GLU GLU C . n 
D 1 53  THR 53  82  82  THR THR C . n 
D 1 54  SER 54  83  83  SER SER C . n 
D 1 55  VAL 55  84  84  VAL VAL C . n 
D 1 56  LEU 56  85  85  LEU LEU C . n 
D 1 57  ASP 57  86  86  ASP ASP C . n 
D 1 58  PRO 58  87  87  PRO PRO C . n 
D 1 59  ASP 59  88  88  ASP ASP C . n 
D 1 60  GLU 60  89  89  GLU GLU C . n 
D 1 61  GLY 61  90  90  GLY GLY C . n 
D 1 62  ILE 62  91  91  ILE ILE C . n 
D 1 63  ARG 63  92  92  ARG ARG C . n 
D 1 64  PHE 64  93  93  PHE PHE C . n 
D 1 65  ARG 65  94  94  ARG ARG C . n 
D 1 66  GLY 66  95  95  GLY GLY C . n 
D 1 67  PHE 67  96  96  PHE PHE C . n 
D 1 68  SER 68  97  97  SER SER C . n 
D 1 69  ILE 69  98  98  ILE ILE C . n 
D 1 70  PRO 70  99  99  PRO PRO C . n 
D 1 71  GLU 71  100 100 GLU GLU C . n 
D 1 72  CYS 72  101 101 CYS CYS C . n 
D 1 73  GLN 73  102 102 GLN GLN C . n 
D 1 74  LYS 74  103 103 LYS LYS C . n 
D 1 75  LEU 75  104 104 LEU LEU C . n 
D 1 76  LEU 76  105 105 LEU LEU C . n 
D 1 77  PRO 77  106 106 PRO PRO C . n 
D 1 78  LYS 78  107 107 LYS LYS C . n 
D 1 79  ALA 79  108 108 ALA ALA C . n 
D 1 80  LYS 80  109 109 LYS LYS C . n 
D 1 81  GLY 81  110 110 GLY GLY C . n 
D 1 82  GLY 82  111 111 GLY GLY C . n 
D 1 83  GLU 83  112 112 GLU GLU C . n 
D 1 84  GLU 84  113 113 GLU GLU C . n 
D 1 85  PRO 85  114 114 PRO PRO C . n 
D 1 86  LEU 86  115 115 LEU LEU C . n 
D 1 87  PRO 87  116 116 PRO PRO C . n 
D 1 88  GLU 88  117 117 GLU GLU C . n 
D 1 89  GLY 89  118 118 GLY GLY C . n 
D 1 90  LEU 90  119 119 LEU LEU C . n 
D 1 91  PHE 91  120 120 PHE PHE C . n 
D 1 92  TRP 92  121 121 TRP TRP C . n 
D 1 93  LEU 93  122 122 LEU LEU C . n 
D 1 94  LEU 94  123 123 LEU LEU C . n 
D 1 95  VAL 95  124 124 VAL VAL C . n 
D 1 96  THR 96  125 125 THR THR C . n 
D 1 97  GLY 97  126 126 GLY GLY C . n 
D 1 98  HIS 98  127 127 HIS HIS C . n 
D 1 99  ILE 99  128 128 ILE ILE C . n 
D 1 100 PRO 100 129 129 PRO PRO C . n 
D 1 101 THR 101 130 130 THR THR C . n 
D 1 102 GLU 102 131 131 GLU GLU C . n 
D 1 103 GLU 103 132 132 GLU GLU C . n 
D 1 104 GLN 104 133 133 GLN GLN C . n 
D 1 105 VAL 105 134 134 VAL VAL C . n 
D 1 106 SER 106 135 135 SER SER C . n 
D 1 107 TRP 107 136 136 TRP TRP C . n 
D 1 108 LEU 108 137 137 LEU LEU C . n 
D 1 109 SER 109 138 138 SER SER C . n 
D 1 110 LYS 110 139 139 LYS LYS C . n 
D 1 111 GLU 111 140 140 GLU GLU C . n 
D 1 112 TRP 112 141 141 TRP TRP C . n 
D 1 113 ALA 113 142 142 ALA ALA C . n 
D 1 114 LYS 114 143 143 LYS LYS C . n 
D 1 115 ARG 115 144 144 ARG ARG C . n 
D 1 116 ALA 116 145 145 ALA ALA C . n 
D 1 117 ALA 117 146 146 ALA ALA C . n 
D 1 118 LEU 118 147 147 LEU LEU C . n 
D 1 119 PRO 119 148 148 PRO PRO C . n 
D 1 120 SER 120 149 149 SER SER C . n 
D 1 121 HIS 121 150 150 HIS HIS C . n 
D 1 122 VAL 122 151 151 VAL VAL C . n 
D 1 123 VAL 123 152 152 VAL VAL C . n 
D 1 124 THR 124 153 153 THR THR C . n 
D 1 125 MET 125 154 154 MET MET C . n 
D 1 126 LEU 126 155 155 LEU LEU C . n 
D 1 127 ASP 127 156 156 ASP ASP C . n 
D 1 128 ASN 128 157 157 ASN ASN C . n 
D 1 129 PHE 129 158 158 PHE PHE C . n 
D 1 130 PRO 130 159 159 PRO PRO C . n 
D 1 131 THR 131 160 160 THR THR C . n 
D 1 132 ASN 132 161 161 ASN ASN C . n 
D 1 133 LEU 133 162 162 LEU LEU C . n 
D 1 134 HIS 134 163 163 HIS HIS C . n 
D 1 135 PRO 135 164 164 PRO PRO C . n 
D 1 136 MET 136 165 165 MET MET C . n 
D 1 137 SER 137 166 166 SER SER C . n 
D 1 138 GLN 138 167 167 GLN GLN C . n 
D 1 139 LEU 139 168 168 LEU LEU C . n 
D 1 140 SER 140 169 169 SER SER C . n 
D 1 141 ALA 141 170 170 ALA ALA C . n 
D 1 142 ALA 142 171 171 ALA ALA C . n 
D 1 143 VAL 143 172 172 VAL VAL C . n 
D 1 144 THR 144 173 173 THR THR C . n 
D 1 145 ALA 145 174 174 ALA ALA C . n 
D 1 146 LEU 146 175 175 LEU LEU C . n 
D 1 147 ASN 147 176 176 ASN ASN C . n 
D 1 148 SER 148 177 177 SER SER C . n 
D 1 149 GLU 149 178 178 GLU GLU C . n 
D 1 150 SER 150 179 179 SER SER C . n 
D 1 151 ASN 151 180 180 ASN ASN C . n 
D 1 152 PHE 152 181 181 PHE PHE C . n 
D 1 153 ALA 153 182 182 ALA ALA C . n 
D 1 154 ARG 154 183 183 ARG ARG C . n 
D 1 155 ALA 155 184 184 ALA ALA C . n 
D 1 156 TYR 156 185 185 TYR TYR C . n 
D 1 157 ALA 157 186 186 ALA ALA C . n 
D 1 158 GLN 158 187 187 GLN GLN C . n 
D 1 159 GLY 159 188 188 GLY GLY C . n 
D 1 160 ILE 160 189 189 ILE ILE C . n 
D 1 161 SER 161 190 190 SER SER C . n 
D 1 162 ARG 162 191 191 ARG ARG C . n 
D 1 163 THR 163 192 192 THR THR C . n 
D 1 164 LYS 164 193 193 LYS LYS C . n 
D 1 165 TYR 165 194 194 TYR TYR C . n 
D 1 166 TRP 166 195 195 TRP TRP C . n 
D 1 167 GLU 167 196 196 GLU GLU C . n 
D 1 168 LEU 168 197 197 LEU LEU C . n 
D 1 169 ILE 169 198 198 ILE ILE C . n 
D 1 170 TYR 170 199 199 TYR TYR C . n 
D 1 171 GLU 171 200 200 GLU GLU C . n 
D 1 172 ASP 172 201 201 ASP ASP C . n 
D 1 173 SER 173 202 202 SER SER C . n 
D 1 174 MET 174 203 203 MET MET C . n 
D 1 175 ASP 175 204 204 ASP ASP C . n 
D 1 176 LEU 176 205 205 LEU LEU C . n 
D 1 177 ILE 177 206 206 ILE ILE C . n 
D 1 178 ALA 178 207 207 ALA ALA C . n 
D 1 179 LYS 179 208 208 LYS LYS C . n 
D 1 180 LEU 180 209 209 LEU LEU C . n 
D 1 181 PRO 181 210 210 PRO PRO C . n 
D 1 182 CYS 182 211 211 CYS CYS C . n 
D 1 183 VAL 183 212 212 VAL VAL C . n 
D 1 184 ALA 184 213 213 ALA ALA C . n 
D 1 185 ALA 185 214 214 ALA ALA C . n 
D 1 186 LYS 186 215 215 LYS LYS C . n 
D 1 187 ILE 187 216 216 ILE ILE C . n 
D 1 188 TYR 188 217 217 TYR TYR C . n 
D 1 189 ARG 189 218 218 ARG ARG C . n 
D 1 190 ASN 190 219 219 ASN ASN C . n 
D 1 191 LEU 191 220 220 LEU LEU C . n 
D 1 192 TYR 192 221 221 TYR TYR C . n 
D 1 193 ARG 193 222 222 ARG ARG C . n 
D 1 194 GLU 194 223 223 GLU GLU C . n 
D 1 195 GLY 195 224 224 GLY GLY C . n 
D 1 196 SER 196 225 225 SER SER C . n 
D 1 197 GLY 197 226 226 GLY GLY C . n 
D 1 198 ILE 198 227 227 ILE ILE C . n 
D 1 199 GLY 199 228 228 GLY GLY C . n 
D 1 200 ALA 200 229 229 ALA ALA C . n 
D 1 201 ILE 201 230 230 ILE ILE C . n 
D 1 202 ASP 202 231 231 ASP ASP C . n 
D 1 203 SER 203 232 232 SER SER C . n 
D 1 204 ASN 204 233 233 ASN ASN C . n 
D 1 205 LEU 205 234 234 LEU LEU C . n 
D 1 206 ASP 206 235 235 ASP ASP C . n 
D 1 207 TRP 207 236 236 TRP TRP C . n 
D 1 208 SER 208 237 237 SER SER C . n 
D 1 209 HIS 209 238 238 HIS HIS C . n 
D 1 210 ASN 210 239 239 ASN ASN C . n 
D 1 211 PHE 211 240 240 PHE PHE C . n 
D 1 212 THR 212 241 241 THR THR C . n 
D 1 213 ASN 213 242 242 ASN ASN C . n 
D 1 214 MET 214 243 243 MET MET C . n 
D 1 215 LEU 215 244 244 LEU LEU C . n 
D 1 216 GLY 216 245 245 GLY GLY C . n 
D 1 217 TYR 217 246 246 TYR TYR C . n 
D 1 218 THR 218 247 247 THR THR C . n 
D 1 219 ASP 219 248 248 ASP ASP C . n 
D 1 220 HIS 220 249 249 HIS HIS C . n 
D 1 221 GLN 221 250 250 GLN GLN C . n 
D 1 222 PHE 222 251 251 PHE PHE C . n 
D 1 223 THR 223 252 252 THR THR C . n 
D 1 224 GLU 224 253 253 GLU GLU C . n 
D 1 225 LEU 225 254 254 LEU LEU C . n 
D 1 226 THR 226 255 255 THR THR C . n 
D 1 227 ARG 227 256 256 ARG ARG C . n 
D 1 228 LEU 228 257 257 LEU LEU C . n 
D 1 229 TYR 229 258 258 TYR TYR C . n 
D 1 230 LEU 230 259 259 LEU LEU C . n 
D 1 231 THR 231 260 260 THR THR C . n 
D 1 232 ILE 232 261 261 ILE ILE C . n 
D 1 233 HIS 233 262 262 HIS HIS C . n 
D 1 234 SER 234 263 263 SER SER C . n 
D 1 235 ASP 235 264 264 ASP ASP C . n 
D 1 236 HIS 236 265 265 HIS HIS C . n 
D 1 237 GLU 237 266 266 GLU GLU C . n 
D 1 238 GLY 238 267 267 GLY GLY C . n 
D 1 239 GLY 239 268 268 GLY GLY C . n 
D 1 240 ASN 240 269 269 ASN ASN C . n 
D 1 241 VAL 241 270 270 VAL VAL C . n 
D 1 242 SER 242 271 271 SER SER C . n 
D 1 243 ALA 243 272 272 ALA ALA C . n 
D 1 244 HIS 244 273 273 HIS HIS C . n 
D 1 245 THR 245 274 274 THR THR C . n 
D 1 246 SER 246 275 275 SER SER C . n 
D 1 247 HIS 247 276 276 HIS HIS C . n 
D 1 248 LEU 248 277 277 LEU LEU C . n 
D 1 249 VAL 249 278 278 VAL VAL C . n 
D 1 250 GLY 250 279 279 GLY GLY C . n 
D 1 251 SER 251 280 280 SER SER C . n 
D 1 252 ALA 252 281 281 ALA ALA C . n 
D 1 253 LEU 253 282 282 LEU LEU C . n 
D 1 254 SER 254 283 283 SER SER C . n 
D 1 255 ASP 255 284 284 ASP ASP C . n 
D 1 256 PRO 256 285 285 PRO PRO C . n 
D 1 257 TYR 257 286 286 TYR TYR C . n 
D 1 258 LEU 258 287 287 LEU LEU C . n 
D 1 259 SER 259 288 288 SER SER C . n 
D 1 260 PHE 260 289 289 PHE PHE C . n 
D 1 261 ALA 261 290 290 ALA ALA C . n 
D 1 262 ALA 262 291 291 ALA ALA C . n 
D 1 263 ALA 263 292 292 ALA ALA C . n 
D 1 264 MET 264 293 293 MET MET C . n 
D 1 265 ASN 265 294 294 ASN ASN C . n 
D 1 266 GLY 266 295 295 GLY GLY C . n 
D 1 267 LEU 267 296 296 LEU LEU C . n 
D 1 268 ALA 268 297 297 ALA ALA C . n 
D 1 269 GLY 269 298 298 GLY GLY C . n 
D 1 270 PRO 270 299 299 PRO PRO C . n 
D 1 271 LEU 271 300 300 LEU LEU C . n 
D 1 272 HIS 272 301 301 HIS HIS C . n 
D 1 273 GLY 273 302 302 GLY GLY C . n 
D 1 274 LEU 274 303 303 LEU LEU C . n 
D 1 275 ALA 275 304 304 ALA ALA C . n 
D 1 276 ASN 276 305 305 ASN ASN C . n 
D 1 277 GLN 277 306 306 GLN GLN C . n 
D 1 278 GLU 278 307 307 GLU GLU C . n 
D 1 279 VAL 279 308 308 VAL VAL C . n 
D 1 280 LEU 280 309 309 LEU LEU C . n 
D 1 281 VAL 281 310 310 VAL VAL C . n 
D 1 282 TRP 282 311 311 TRP TRP C . n 
D 1 283 LEU 283 312 312 LEU LEU C . n 
D 1 284 THR 284 313 313 THR THR C . n 
D 1 285 GLN 285 314 314 GLN GLN C . n 
D 1 286 LEU 286 315 315 LEU LEU C . n 
D 1 287 GLN 287 316 316 GLN GLN C . n 
D 1 288 LYS 288 317 317 LYS LYS C . n 
D 1 289 GLU 289 318 318 GLU GLU C . n 
D 1 290 VAL 290 319 319 VAL VAL C . n 
D 1 291 GLY 291 320 320 GLY GLY C . n 
D 1 292 LYS 292 321 321 LYS LYS C . n 
D 1 293 ASP 293 322 322 ASP ASP C . n 
D 1 294 VAL 294 323 323 VAL VAL C . n 
D 1 295 SER 295 324 324 SER SER C . n 
D 1 296 ASP 296 325 325 ASP ASP C . n 
D 1 297 GLU 297 326 326 GLU GLU C . n 
D 1 298 LYS 298 327 327 LYS LYS C . n 
D 1 299 LEU 299 328 328 LEU LEU C . n 
D 1 300 ARG 300 329 329 ARG ARG C . n 
D 1 301 ASP 301 330 330 ASP ASP C . n 
D 1 302 TYR 302 331 331 TYR TYR C . n 
D 1 303 ILE 303 332 332 ILE ILE C . n 
D 1 304 TRP 304 333 333 TRP TRP C . n 
D 1 305 ASN 305 334 334 ASN ASN C . n 
D 1 306 THR 306 335 335 THR THR C . n 
D 1 307 LEU 307 336 336 LEU LEU C . n 
D 1 308 ASN 308 337 337 ASN ASN C . n 
D 1 309 SER 309 338 338 SER SER C . n 
D 1 310 GLY 310 339 339 GLY GLY C . n 
D 1 311 ARG 311 340 340 ARG ARG C . n 
D 1 312 VAL 312 341 341 VAL VAL C . n 
D 1 313 VAL 313 342 342 VAL VAL C . n 
D 1 314 PRO 314 343 343 PRO PRO C . n 
D 1 315 GLY 315 344 344 GLY GLY C . n 
D 1 316 TYR 316 345 345 TYR TYR C . n 
D 1 317 GLY 317 346 346 GLY GLY C . n 
D 1 318 HIS 318 347 347 HIS HIS C . n 
D 1 319 ALA 319 348 348 ALA ALA C . n 
D 1 320 VAL 320 349 349 VAL VAL C . n 
D 1 321 LEU 321 350 350 LEU LEU C . n 
D 1 322 ARG 322 351 351 ARG ARG C . n 
D 1 323 LYS 323 352 352 LYS LYS C . n 
D 1 324 THR 324 353 353 THR THR C . n 
D 1 325 ASP 325 354 354 ASP ASP C . n 
D 1 326 PRO 326 355 355 PRO PRO C . n 
D 1 327 ARG 327 356 356 ARG ARG C . n 
D 1 328 TYR 328 357 357 TYR TYR C . n 
D 1 329 THR 329 358 358 THR THR C . n 
D 1 330 CYS 330 359 359 CYS CYS C . n 
D 1 331 GLN 331 360 360 GLN GLN C . n 
D 1 332 ARG 332 361 361 ARG ARG C . n 
D 1 333 GLU 333 362 362 GLU GLU C . n 
D 1 334 PHE 334 363 363 PHE PHE C . n 
D 1 335 ALA 335 364 364 ALA ALA C . n 
D 1 336 LEU 336 365 365 LEU LEU C . n 
D 1 337 LYS 337 366 366 LYS LYS C . n 
D 1 338 HIS 338 367 367 HIS HIS C . n 
D 1 339 LEU 339 368 368 LEU LEU C . n 
D 1 340 PRO 340 369 369 PRO PRO C . n 
D 1 341 ASN 341 370 370 ASN ASN C . n 
D 1 342 ASP 342 371 371 ASP ASP C . n 
D 1 343 PRO 343 372 372 PRO PRO C . n 
D 1 344 MET 344 373 373 MET MET C . n 
D 1 345 PHE 345 374 374 PHE PHE C . n 
D 1 346 LYS 346 375 375 LYS LYS C . n 
D 1 347 LEU 347 376 376 LEU LEU C . n 
D 1 348 VAL 348 377 377 VAL VAL C . n 
D 1 349 ALA 349 378 378 ALA ALA C . n 
D 1 350 GLN 350 379 379 GLN GLN C . n 
D 1 351 LEU 351 380 380 LEU LEU C . n 
D 1 352 TYR 352 381 381 TYR TYR C . n 
D 1 353 LYS 353 382 382 LYS LYS C . n 
D 1 354 ILE 354 383 383 ILE ILE C . n 
D 1 355 VAL 355 384 384 VAL VAL C . n 
D 1 356 PRO 356 385 385 PRO PRO C . n 
D 1 357 ASN 357 386 386 ASN ASN C . n 
D 1 358 VAL 358 387 387 VAL VAL C . n 
D 1 359 LEU 359 388 388 LEU LEU C . n 
D 1 360 LEU 360 389 389 LEU LEU C . n 
D 1 361 GLU 361 390 390 GLU GLU C . n 
D 1 362 GLN 362 391 391 GLN GLN C . n 
D 1 363 GLY 363 392 392 GLY GLY C . n 
D 1 364 LYS 364 393 393 LYS LYS C . n 
D 1 365 ALA 365 394 394 ALA ALA C . n 
D 1 366 LYS 366 395 395 LYS LYS C . n 
D 1 367 ASN 367 396 396 ASN ASN C . n 
D 1 368 PRO 368 397 397 PRO PRO C . n 
D 1 369 TRP 369 398 398 TRP TRP C . n 
D 1 370 PRO 370 399 399 PRO PRO C . n 
D 1 371 ASN 371 400 400 ASN ASN C . n 
D 1 372 VAL 372 401 401 VAL VAL C . n 
D 1 373 ASP 373 402 402 ASP ASP C . n 
D 1 374 ALA 374 403 403 ALA ALA C . n 
D 1 375 HIS 375 404 404 HIS HIS C . n 
D 1 376 SER 376 405 405 SER SER C . n 
D 1 377 GLY 377 406 406 GLY GLY C . n 
D 1 378 VAL 378 407 407 VAL VAL C . n 
D 1 379 LEU 379 408 408 LEU LEU C . n 
D 1 380 LEU 380 409 409 LEU LEU C . n 
D 1 381 GLN 381 410 410 GLN GLN C . n 
D 1 382 TYR 382 411 411 TYR TYR C . n 
D 1 383 TYR 383 412 412 TYR TYR C . n 
D 1 384 GLY 384 413 413 GLY GLY C . n 
D 1 385 MET 385 414 414 MET MET C . n 
D 1 386 THR 386 415 415 THR THR C . n 
D 1 387 GLU 387 416 416 GLU GLU C . n 
D 1 388 MET 388 417 417 MET MET C . n 
D 1 389 ASN 389 418 418 ASN ASN C . n 
D 1 390 TYR 390 419 419 TYR TYR C . n 
D 1 391 TYR 391 420 420 TYR TYR C . n 
D 1 392 THR 392 421 421 THR THR C . n 
D 1 393 VAL 393 422 422 VAL VAL C . n 
D 1 394 LEU 394 423 423 LEU LEU C . n 
D 1 395 PHE 395 424 424 PHE PHE C . n 
D 1 396 GLY 396 425 425 GLY GLY C . n 
D 1 397 VAL 397 426 426 VAL VAL C . n 
D 1 398 SER 398 427 427 SER SER C . n 
D 1 399 ARG 399 428 428 ARG ARG C . n 
D 1 400 ALA 400 429 429 ALA ALA C . n 
D 1 401 LEU 401 430 430 LEU LEU C . n 
D 1 402 GLY 402 431 431 GLY GLY C . n 
D 1 403 VAL 403 432 432 VAL VAL C . n 
D 1 404 LEU 404 433 433 LEU LEU C . n 
D 1 405 ALA 405 434 434 ALA ALA C . n 
D 1 406 GLN 406 435 435 GLN GLN C . n 
D 1 407 LEU 407 436 436 LEU LEU C . n 
D 1 408 ILE 408 437 437 ILE ILE C . n 
D 1 409 TRP 409 438 438 TRP TRP C . n 
D 1 410 SER 410 439 439 SER SER C . n 
D 1 411 ARG 411 440 440 ARG ARG C . n 
D 1 412 ALA 412 441 441 ALA ALA C . n 
D 1 413 LEU 413 442 442 LEU LEU C . n 
D 1 414 GLY 414 443 443 GLY GLY C . n 
D 1 415 PHE 415 444 444 PHE PHE C . n 
D 1 416 PRO 416 445 445 PRO PRO C . n 
D 1 417 LEU 417 446 446 LEU LEU C . n 
D 1 418 GLU 418 447 447 GLU GLU C . n 
D 1 419 ARG 419 448 448 ARG ARG C . n 
D 1 420 PRO 420 449 449 PRO PRO C . n 
D 1 421 LYS 421 450 450 LYS LYS C . n 
D 1 422 SER 422 451 451 SER SER C . n 
D 1 423 MET 423 452 452 MET MET C . n 
D 1 424 SER 424 453 453 SER SER C . n 
D 1 425 THR 425 454 454 THR THR C . n 
D 1 426 GLU 426 455 455 GLU GLU C . n 
D 1 427 GLY 427 456 456 GLY GLY C . n 
D 1 428 LEU 428 457 457 LEU LEU C . n 
D 1 429 MET 429 458 458 MET MET C . n 
D 1 430 LYS 430 459 459 LYS LYS C . n 
D 1 431 PHE 431 460 460 PHE PHE C . n 
D 1 432 VAL 432 461 461 VAL VAL C . n 
D 1 433 ASP 433 462 462 ASP ASP C . n 
D 1 434 SER 434 463 463 SER SER C . n 
D 1 435 LYS 435 464 464 LYS LYS C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        OAA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   OAA 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 OAA 1   601 601  OAA OAA A . 
F 2 OAA 1   501 501  OAA OAA D . 
G 2 OAA 1   501 501  OAA OAA B . 
H 3 HOH 1   701 574  HOH HOH A . 
H 3 HOH 2   702 396  HOH HOH A . 
H 3 HOH 3   703 162  HOH HOH A . 
H 3 HOH 4   704 385  HOH HOH A . 
H 3 HOH 5   705 345  HOH HOH A . 
H 3 HOH 6   706 275  HOH HOH A . 
H 3 HOH 7   707 224  HOH HOH A . 
H 3 HOH 8   708 523  HOH HOH A . 
H 3 HOH 9   709 266  HOH HOH A . 
H 3 HOH 10  710 2    HOH HOH A . 
H 3 HOH 11  711 29   HOH HOH A . 
H 3 HOH 12  712 19   HOH HOH A . 
H 3 HOH 13  713 62   HOH HOH A . 
H 3 HOH 14  714 387  HOH HOH A . 
H 3 HOH 15  715 57   HOH HOH A . 
H 3 HOH 16  716 468  HOH HOH A . 
H 3 HOH 17  717 151  HOH HOH A . 
H 3 HOH 18  718 64   HOH HOH A . 
H 3 HOH 19  719 185  HOH HOH A . 
H 3 HOH 20  720 343  HOH HOH A . 
H 3 HOH 21  721 125  HOH HOH A . 
H 3 HOH 22  722 86   HOH HOH A . 
H 3 HOH 23  723 462  HOH HOH A . 
H 3 HOH 24  724 743  HOH HOH A . 
H 3 HOH 25  725 258  HOH HOH A . 
H 3 HOH 26  726 486  HOH HOH A . 
H 3 HOH 27  727 528  HOH HOH A . 
H 3 HOH 28  728 241  HOH HOH A . 
H 3 HOH 29  729 613  HOH HOH A . 
H 3 HOH 30  730 362  HOH HOH A . 
H 3 HOH 31  731 24   HOH HOH A . 
H 3 HOH 32  732 100  HOH HOH A . 
H 3 HOH 33  733 197  HOH HOH A . 
H 3 HOH 34  734 91   HOH HOH A . 
H 3 HOH 35  735 96   HOH HOH A . 
H 3 HOH 36  736 519  HOH HOH A . 
H 3 HOH 37  737 9    HOH HOH A . 
H 3 HOH 38  738 406  HOH HOH A . 
H 3 HOH 39  739 608  HOH HOH A . 
H 3 HOH 40  740 248  HOH HOH A . 
H 3 HOH 41  741 927  HOH HOH A . 
H 3 HOH 42  742 627  HOH HOH A . 
H 3 HOH 43  743 510  HOH HOH A . 
H 3 HOH 44  744 78   HOH HOH A . 
H 3 HOH 45  745 317  HOH HOH A . 
H 3 HOH 46  746 216  HOH HOH A . 
H 3 HOH 47  747 400  HOH HOH A . 
H 3 HOH 48  748 42   HOH HOH A . 
H 3 HOH 49  749 517  HOH HOH A . 
H 3 HOH 50  750 72   HOH HOH A . 
H 3 HOH 51  751 330  HOH HOH A . 
H 3 HOH 52  752 176  HOH HOH A . 
H 3 HOH 53  753 384  HOH HOH A . 
H 3 HOH 54  754 374  HOH HOH A . 
H 3 HOH 55  755 291  HOH HOH A . 
H 3 HOH 56  756 238  HOH HOH A . 
H 3 HOH 57  757 767  HOH HOH A . 
H 3 HOH 58  758 25   HOH HOH A . 
H 3 HOH 59  759 324  HOH HOH A . 
H 3 HOH 60  760 522  HOH HOH A . 
H 3 HOH 61  761 534  HOH HOH A . 
H 3 HOH 62  762 555  HOH HOH A . 
H 3 HOH 63  763 218  HOH HOH A . 
H 3 HOH 64  764 3    HOH HOH A . 
H 3 HOH 65  765 264  HOH HOH A . 
H 3 HOH 66  766 227  HOH HOH A . 
H 3 HOH 67  767 75   HOH HOH A . 
H 3 HOH 68  768 252  HOH HOH A . 
H 3 HOH 69  769 120  HOH HOH A . 
H 3 HOH 70  770 188  HOH HOH A . 
H 3 HOH 71  771 167  HOH HOH A . 
H 3 HOH 72  772 521  HOH HOH A . 
H 3 HOH 73  773 409  HOH HOH A . 
H 3 HOH 74  774 1041 HOH HOH A . 
H 3 HOH 75  775 121  HOH HOH A . 
H 3 HOH 76  776 44   HOH HOH A . 
H 3 HOH 77  777 800  HOH HOH A . 
H 3 HOH 78  778 36   HOH HOH A . 
H 3 HOH 79  779 635  HOH HOH A . 
H 3 HOH 80  780 503  HOH HOH A . 
H 3 HOH 81  781 719  HOH HOH A . 
H 3 HOH 82  782 138  HOH HOH A . 
H 3 HOH 83  783 281  HOH HOH A . 
H 3 HOH 84  784 837  HOH HOH A . 
H 3 HOH 85  785 425  HOH HOH A . 
H 3 HOH 86  786 163  HOH HOH A . 
H 3 HOH 87  787 222  HOH HOH A . 
H 3 HOH 88  788 701  HOH HOH A . 
H 3 HOH 89  789 408  HOH HOH A . 
H 3 HOH 90  790 154  HOH HOH A . 
H 3 HOH 91  791 136  HOH HOH A . 
H 3 HOH 92  792 716  HOH HOH A . 
H 3 HOH 93  793 957  HOH HOH A . 
H 3 HOH 94  794 28   HOH HOH A . 
H 3 HOH 95  795 223  HOH HOH A . 
H 3 HOH 96  796 98   HOH HOH A . 
H 3 HOH 97  797 560  HOH HOH A . 
H 3 HOH 98  798 293  HOH HOH A . 
H 3 HOH 99  799 22   HOH HOH A . 
H 3 HOH 100 800 118  HOH HOH A . 
H 3 HOH 101 801 255  HOH HOH A . 
H 3 HOH 102 802 251  HOH HOH A . 
H 3 HOH 103 803 320  HOH HOH A . 
H 3 HOH 104 804 698  HOH HOH A . 
H 3 HOH 105 805 388  HOH HOH A . 
H 3 HOH 106 806 609  HOH HOH A . 
H 3 HOH 107 807 625  HOH HOH A . 
H 3 HOH 108 808 54   HOH HOH A . 
H 3 HOH 109 809 146  HOH HOH A . 
H 3 HOH 110 810 287  HOH HOH A . 
H 3 HOH 111 811 979  HOH HOH A . 
H 3 HOH 112 812 253  HOH HOH A . 
H 3 HOH 113 813 55   HOH HOH A . 
H 3 HOH 114 814 949  HOH HOH A . 
H 3 HOH 115 815 116  HOH HOH A . 
H 3 HOH 116 816 130  HOH HOH A . 
H 3 HOH 117 817 279  HOH HOH A . 
H 3 HOH 118 818 415  HOH HOH A . 
H 3 HOH 119 819 547  HOH HOH A . 
H 3 HOH 120 820 288  HOH HOH A . 
H 3 HOH 121 821 363  HOH HOH A . 
H 3 HOH 122 822 109  HOH HOH A . 
H 3 HOH 123 823 1000 HOH HOH A . 
H 3 HOH 124 824 1013 HOH HOH A . 
H 3 HOH 125 825 110  HOH HOH A . 
H 3 HOH 126 826 972  HOH HOH A . 
H 3 HOH 127 827 717  HOH HOH A . 
H 3 HOH 128 828 1033 HOH HOH A . 
H 3 HOH 129 829 1014 HOH HOH A . 
H 3 HOH 130 830 640  HOH HOH A . 
H 3 HOH 131 831 999  HOH HOH A . 
H 3 HOH 132 832 1018 HOH HOH A . 
H 3 HOH 133 833 1002 HOH HOH A . 
H 3 HOH 134 834 646  HOH HOH A . 
H 3 HOH 135 835 654  HOH HOH A . 
H 3 HOH 136 836 1028 HOH HOH A . 
H 3 HOH 137 837 421  HOH HOH A . 
H 3 HOH 138 838 1049 HOH HOH A . 
H 3 HOH 139 839 799  HOH HOH A . 
H 3 HOH 140 840 540  HOH HOH A . 
H 3 HOH 141 841 671  HOH HOH A . 
H 3 HOH 142 842 650  HOH HOH A . 
H 3 HOH 143 843 908  HOH HOH A . 
H 3 HOH 144 844 1019 HOH HOH A . 
H 3 HOH 145 845 1062 HOH HOH A . 
H 3 HOH 146 846 1070 HOH HOH A . 
H 3 HOH 147 847 1051 HOH HOH A . 
H 3 HOH 148 848 1037 HOH HOH A . 
H 3 HOH 149 849 849  HOH HOH A . 
H 3 HOH 150 850 675  HOH HOH A . 
H 3 HOH 151 851 795  HOH HOH A . 
I 3 HOH 1   601 735  HOH HOH D . 
I 3 HOH 2   602 435  HOH HOH D . 
I 3 HOH 3   603 214  HOH HOH D . 
I 3 HOH 4   604 272  HOH HOH D . 
I 3 HOH 5   605 944  HOH HOH D . 
I 3 HOH 6   606 941  HOH HOH D . 
I 3 HOH 7   607 200  HOH HOH D . 
I 3 HOH 8   608 179  HOH HOH D . 
I 3 HOH 9   609 491  HOH HOH D . 
I 3 HOH 10  610 546  HOH HOH D . 
I 3 HOH 11  611 470  HOH HOH D . 
I 3 HOH 12  612 31   HOH HOH D . 
I 3 HOH 13  613 286  HOH HOH D . 
I 3 HOH 14  614 79   HOH HOH D . 
I 3 HOH 15  615 206  HOH HOH D . 
I 3 HOH 16  616 383  HOH HOH D . 
I 3 HOH 17  617 569  HOH HOH D . 
I 3 HOH 18  618 367  HOH HOH D . 
I 3 HOH 19  619 715  HOH HOH D . 
I 3 HOH 20  620 302  HOH HOH D . 
I 3 HOH 21  621 350  HOH HOH D . 
I 3 HOH 22  622 704  HOH HOH D . 
I 3 HOH 23  623 283  HOH HOH D . 
I 3 HOH 24  624 129  HOH HOH D . 
I 3 HOH 25  625 158  HOH HOH D . 
I 3 HOH 26  626 205  HOH HOH D . 
I 3 HOH 27  627 92   HOH HOH D . 
I 3 HOH 28  628 604  HOH HOH D . 
I 3 HOH 29  629 731  HOH HOH D . 
I 3 HOH 30  630 436  HOH HOH D . 
I 3 HOH 31  631 1    HOH HOH D . 
I 3 HOH 32  632 177  HOH HOH D . 
I 3 HOH 33  633 531  HOH HOH D . 
I 3 HOH 34  634 4    HOH HOH D . 
I 3 HOH 35  635 21   HOH HOH D . 
I 3 HOH 36  636 416  HOH HOH D . 
I 3 HOH 37  637 958  HOH HOH D . 
I 3 HOH 38  638 939  HOH HOH D . 
I 3 HOH 39  639 778  HOH HOH D . 
I 3 HOH 40  640 768  HOH HOH D . 
I 3 HOH 41  641 541  HOH HOH D . 
I 3 HOH 42  642 203  HOH HOH D . 
I 3 HOH 43  643 453  HOH HOH D . 
I 3 HOH 44  644 268  HOH HOH D . 
I 3 HOH 45  645 538  HOH HOH D . 
I 3 HOH 46  646 674  HOH HOH D . 
I 3 HOH 47  647 381  HOH HOH D . 
I 3 HOH 48  648 886  HOH HOH D . 
I 3 HOH 49  649 784  HOH HOH D . 
I 3 HOH 50  650 49   HOH HOH D . 
I 3 HOH 51  651 46   HOH HOH D . 
I 3 HOH 52  652 882  HOH HOH D . 
I 3 HOH 53  653 360  HOH HOH D . 
I 3 HOH 54  654 33   HOH HOH D . 
I 3 HOH 55  655 137  HOH HOH D . 
I 3 HOH 56  656 438  HOH HOH D . 
I 3 HOH 57  657 285  HOH HOH D . 
I 3 HOH 58  658 168  HOH HOH D . 
I 3 HOH 59  659 334  HOH HOH D . 
I 3 HOH 60  660 34   HOH HOH D . 
I 3 HOH 61  661 271  HOH HOH D . 
I 3 HOH 62  662 721  HOH HOH D . 
I 3 HOH 63  663 711  HOH HOH D . 
I 3 HOH 64  664 307  HOH HOH D . 
I 3 HOH 65  665 622  HOH HOH D . 
I 3 HOH 66  666 474  HOH HOH D . 
I 3 HOH 67  667 378  HOH HOH D . 
I 3 HOH 68  668 687  HOH HOH D . 
I 3 HOH 69  669 95   HOH HOH D . 
I 3 HOH 70  670 580  HOH HOH D . 
I 3 HOH 71  671 552  HOH HOH D . 
I 3 HOH 72  672 61   HOH HOH D . 
I 3 HOH 73  673 745  HOH HOH D . 
I 3 HOH 74  674 126  HOH HOH D . 
I 3 HOH 75  675 314  HOH HOH D . 
I 3 HOH 76  676 173  HOH HOH D . 
I 3 HOH 77  677 780  HOH HOH D . 
I 3 HOH 78  678 274  HOH HOH D . 
I 3 HOH 79  679 155  HOH HOH D . 
I 3 HOH 80  680 732  HOH HOH D . 
I 3 HOH 81  681 427  HOH HOH D . 
I 3 HOH 82  682 7    HOH HOH D . 
I 3 HOH 83  683 518  HOH HOH D . 
I 3 HOH 84  684 329  HOH HOH D . 
I 3 HOH 85  685 475  HOH HOH D . 
I 3 HOH 86  686 192  HOH HOH D . 
I 3 HOH 87  687 395  HOH HOH D . 
I 3 HOH 88  688 461  HOH HOH D . 
I 3 HOH 89  689 102  HOH HOH D . 
I 3 HOH 90  690 20   HOH HOH D . 
I 3 HOH 91  691 774  HOH HOH D . 
I 3 HOH 92  692 361  HOH HOH D . 
I 3 HOH 93  693 516  HOH HOH D . 
I 3 HOH 94  694 189  HOH HOH D . 
I 3 HOH 95  695 161  HOH HOH D . 
I 3 HOH 96  696 858  HOH HOH D . 
I 3 HOH 97  697 483  HOH HOH D . 
I 3 HOH 98  698 349  HOH HOH D . 
I 3 HOH 99  699 561  HOH HOH D . 
I 3 HOH 100 700 434  HOH HOH D . 
I 3 HOH 101 701 147  HOH HOH D . 
I 3 HOH 102 702 749  HOH HOH D . 
I 3 HOH 103 703 63   HOH HOH D . 
I 3 HOH 104 704 342  HOH HOH D . 
I 3 HOH 105 705 577  HOH HOH D . 
I 3 HOH 106 706 37   HOH HOH D . 
I 3 HOH 107 707 180  HOH HOH D . 
I 3 HOH 108 708 77   HOH HOH D . 
I 3 HOH 109 709 1052 HOH HOH D . 
I 3 HOH 110 710 282  HOH HOH D . 
I 3 HOH 111 711 645  HOH HOH D . 
I 3 HOH 112 712 691  HOH HOH D . 
I 3 HOH 113 713 563  HOH HOH D . 
I 3 HOH 114 714 35   HOH HOH D . 
I 3 HOH 115 715 111  HOH HOH D . 
I 3 HOH 116 716 647  HOH HOH D . 
I 3 HOH 117 717 793  HOH HOH D . 
I 3 HOH 118 718 297  HOH HOH D . 
I 3 HOH 119 719 351  HOH HOH D . 
I 3 HOH 120 720 311  HOH HOH D . 
I 3 HOH 121 721 338  HOH HOH D . 
I 3 HOH 122 722 508  HOH HOH D . 
I 3 HOH 123 723 760  HOH HOH D . 
I 3 HOH 124 724 1057 HOH HOH D . 
I 3 HOH 125 725 80   HOH HOH D . 
I 3 HOH 126 726 485  HOH HOH D . 
I 3 HOH 127 727 822  HOH HOH D . 
I 3 HOH 128 728 855  HOH HOH D . 
I 3 HOH 129 729 995  HOH HOH D . 
I 3 HOH 130 730 114  HOH HOH D . 
I 3 HOH 131 731 263  HOH HOH D . 
I 3 HOH 132 732 709  HOH HOH D . 
I 3 HOH 133 733 58   HOH HOH D . 
I 3 HOH 134 734 1010 HOH HOH D . 
I 3 HOH 135 735 902  HOH HOH D . 
I 3 HOH 136 736 303  HOH HOH D . 
I 3 HOH 137 737 600  HOH HOH D . 
I 3 HOH 138 738 237  HOH HOH D . 
I 3 HOH 139 739 1043 HOH HOH D . 
I 3 HOH 140 740 524  HOH HOH D . 
I 3 HOH 141 741 998  HOH HOH D . 
I 3 HOH 142 742 861  HOH HOH D . 
I 3 HOH 143 743 896  HOH HOH D . 
I 3 HOH 144 744 512  HOH HOH D . 
I 3 HOH 145 745 938  HOH HOH D . 
I 3 HOH 146 746 1031 HOH HOH D . 
I 3 HOH 147 747 352  HOH HOH D . 
I 3 HOH 148 748 1006 HOH HOH D . 
I 3 HOH 149 749 571  HOH HOH D . 
I 3 HOH 150 750 993  HOH HOH D . 
J 3 HOH 1   601 791  HOH HOH B . 
J 3 HOH 2   602 265  HOH HOH B . 
J 3 HOH 3   603 923  HOH HOH B . 
J 3 HOH 4   604 259  HOH HOH B . 
J 3 HOH 5   605 32   HOH HOH B . 
J 3 HOH 6   606 135  HOH HOH B . 
J 3 HOH 7   607 376  HOH HOH B . 
J 3 HOH 8   608 464  HOH HOH B . 
J 3 HOH 9   609 11   HOH HOH B . 
J 3 HOH 10  610 30   HOH HOH B . 
J 3 HOH 11  611 199  HOH HOH B . 
J 3 HOH 12  612 296  HOH HOH B . 
J 3 HOH 13  613 23   HOH HOH B . 
J 3 HOH 14  614 466  HOH HOH B . 
J 3 HOH 15  615 857  HOH HOH B . 
J 3 HOH 16  616 231  HOH HOH B . 
J 3 HOH 17  617 903  HOH HOH B . 
J 3 HOH 18  618 239  HOH HOH B . 
J 3 HOH 19  619 254  HOH HOH B . 
J 3 HOH 20  620 757  HOH HOH B . 
J 3 HOH 21  621 340  HOH HOH B . 
J 3 HOH 22  622 319  HOH HOH B . 
J 3 HOH 23  623 232  HOH HOH B . 
J 3 HOH 24  624 68   HOH HOH B . 
J 3 HOH 25  625 346  HOH HOH B . 
J 3 HOH 26  626 127  HOH HOH B . 
J 3 HOH 27  627 107  HOH HOH B . 
J 3 HOH 28  628 356  HOH HOH B . 
J 3 HOH 29  629 191  HOH HOH B . 
J 3 HOH 30  630 536  HOH HOH B . 
J 3 HOH 31  631 747  HOH HOH B . 
J 3 HOH 32  632 359  HOH HOH B . 
J 3 HOH 33  633 40   HOH HOH B . 
J 3 HOH 34  634 150  HOH HOH B . 
J 3 HOH 35  635 559  HOH HOH B . 
J 3 HOH 36  636 402  HOH HOH B . 
J 3 HOH 37  637 694  HOH HOH B . 
J 3 HOH 38  638 295  HOH HOH B . 
J 3 HOH 39  639 119  HOH HOH B . 
J 3 HOH 40  640 301  HOH HOH B . 
J 3 HOH 41  641 323  HOH HOH B . 
J 3 HOH 42  642 88   HOH HOH B . 
J 3 HOH 43  643 183  HOH HOH B . 
J 3 HOH 44  644 256  HOH HOH B . 
J 3 HOH 45  645 418  HOH HOH B . 
J 3 HOH 46  646 50   HOH HOH B . 
J 3 HOH 47  647 230  HOH HOH B . 
J 3 HOH 48  648 404  HOH HOH B . 
J 3 HOH 49  649 306  HOH HOH B . 
J 3 HOH 50  650 182  HOH HOH B . 
J 3 HOH 51  651 243  HOH HOH B . 
J 3 HOH 52  652 242  HOH HOH B . 
J 3 HOH 53  653 181  HOH HOH B . 
J 3 HOH 54  654 139  HOH HOH B . 
J 3 HOH 55  655 6    HOH HOH B . 
J 3 HOH 56  656 335  HOH HOH B . 
J 3 HOH 57  657 66   HOH HOH B . 
J 3 HOH 58  658 108  HOH HOH B . 
J 3 HOH 59  659 215  HOH HOH B . 
J 3 HOH 60  660 318  HOH HOH B . 
J 3 HOH 61  661 477  HOH HOH B . 
J 3 HOH 62  662 245  HOH HOH B . 
J 3 HOH 63  663 298  HOH HOH B . 
J 3 HOH 64  664 961  HOH HOH B . 
J 3 HOH 65  665 557  HOH HOH B . 
J 3 HOH 66  666 456  HOH HOH B . 
J 3 HOH 67  667 247  HOH HOH B . 
J 3 HOH 68  668 354  HOH HOH B . 
J 3 HOH 69  669 556  HOH HOH B . 
J 3 HOH 70  670 84   HOH HOH B . 
J 3 HOH 71  671 142  HOH HOH B . 
J 3 HOH 72  672 412  HOH HOH B . 
J 3 HOH 73  673 207  HOH HOH B . 
J 3 HOH 74  674 99   HOH HOH B . 
J 3 HOH 75  675 689  HOH HOH B . 
J 3 HOH 76  676 16   HOH HOH B . 
J 3 HOH 77  677 308  HOH HOH B . 
J 3 HOH 78  678 392  HOH HOH B . 
J 3 HOH 79  679 429  HOH HOH B . 
J 3 HOH 80  680 5    HOH HOH B . 
J 3 HOH 81  681 117  HOH HOH B . 
J 3 HOH 82  682 52   HOH HOH B . 
J 3 HOH 83  683 844  HOH HOH B . 
J 3 HOH 84  684 615  HOH HOH B . 
J 3 HOH 85  685 60   HOH HOH B . 
J 3 HOH 86  686 347  HOH HOH B . 
J 3 HOH 87  687 741  HOH HOH B . 
J 3 HOH 88  688 190  HOH HOH B . 
J 3 HOH 89  689 454  HOH HOH B . 
J 3 HOH 90  690 12   HOH HOH B . 
J 3 HOH 91  691 73   HOH HOH B . 
J 3 HOH 92  692 1011 HOH HOH B . 
J 3 HOH 93  693 487  HOH HOH B . 
J 3 HOH 94  694 727  HOH HOH B . 
J 3 HOH 95  695 113  HOH HOH B . 
J 3 HOH 96  696 394  HOH HOH B . 
J 3 HOH 97  697 38   HOH HOH B . 
J 3 HOH 98  698 817  HOH HOH B . 
J 3 HOH 99  699 550  HOH HOH B . 
J 3 HOH 100 700 637  HOH HOH B . 
J 3 HOH 101 701 260  HOH HOH B . 
J 3 HOH 102 702 1012 HOH HOH B . 
J 3 HOH 103 703 859  HOH HOH B . 
J 3 HOH 104 704 928  HOH HOH B . 
J 3 HOH 105 705 278  HOH HOH B . 
J 3 HOH 106 706 331  HOH HOH B . 
J 3 HOH 107 707 39   HOH HOH B . 
J 3 HOH 108 708 219  HOH HOH B . 
J 3 HOH 109 709 642  HOH HOH B . 
J 3 HOH 110 710 1065 HOH HOH B . 
J 3 HOH 111 711 164  HOH HOH B . 
J 3 HOH 112 712 818  HOH HOH B . 
J 3 HOH 113 713 583  HOH HOH B . 
J 3 HOH 114 714 312  HOH HOH B . 
J 3 HOH 115 715 82   HOH HOH B . 
J 3 HOH 116 716 175  HOH HOH B . 
J 3 HOH 117 717 437  HOH HOH B . 
J 3 HOH 118 718 471  HOH HOH B . 
J 3 HOH 119 719 697  HOH HOH B . 
J 3 HOH 120 720 18   HOH HOH B . 
J 3 HOH 121 721 590  HOH HOH B . 
J 3 HOH 122 722 69   HOH HOH B . 
J 3 HOH 123 723 996  HOH HOH B . 
J 3 HOH 124 724 124  HOH HOH B . 
J 3 HOH 125 725 93   HOH HOH B . 
J 3 HOH 126 726 457  HOH HOH B . 
J 3 HOH 127 727 826  HOH HOH B . 
J 3 HOH 128 728 1026 HOH HOH B . 
J 3 HOH 129 729 339  HOH HOH B . 
J 3 HOH 130 730 994  HOH HOH B . 
J 3 HOH 131 731 1004 HOH HOH B . 
J 3 HOH 132 732 1072 HOH HOH B . 
J 3 HOH 133 733 1005 HOH HOH B . 
J 3 HOH 134 734 968  HOH HOH B . 
J 3 HOH 135 735 411  HOH HOH B . 
J 3 HOH 136 736 1007 HOH HOH B . 
J 3 HOH 137 737 1054 HOH HOH B . 
J 3 HOH 138 738 526  HOH HOH B . 
J 3 HOH 139 739 511  HOH HOH B . 
J 3 HOH 140 740 905  HOH HOH B . 
J 3 HOH 141 741 1029 HOH HOH B . 
J 3 HOH 142 742 443  HOH HOH B . 
J 3 HOH 143 743 500  HOH HOH B . 
J 3 HOH 144 744 794  HOH HOH B . 
J 3 HOH 145 745 693  HOH HOH B . 
J 3 HOH 146 746 1060 HOH HOH B . 
J 3 HOH 147 747 1001 HOH HOH B . 
K 3 HOH 1   501 83   HOH HOH C . 
K 3 HOH 2   502 451  HOH HOH C . 
K 3 HOH 3   503 656  HOH HOH C . 
K 3 HOH 4   504 366  HOH HOH C . 
K 3 HOH 5   505 51   HOH HOH C . 
K 3 HOH 6   506 830  HOH HOH C . 
K 3 HOH 7   507 441  HOH HOH C . 
K 3 HOH 8   508 15   HOH HOH C . 
K 3 HOH 9   509 684  HOH HOH C . 
K 3 HOH 10  510 47   HOH HOH C . 
K 3 HOH 11  511 479  HOH HOH C . 
K 3 HOH 12  512 269  HOH HOH C . 
K 3 HOH 13  513 498  HOH HOH C . 
K 3 HOH 14  514 13   HOH HOH C . 
K 3 HOH 15  515 907  HOH HOH C . 
K 3 HOH 16  516 558  HOH HOH C . 
K 3 HOH 17  517 10   HOH HOH C . 
K 3 HOH 18  518 14   HOH HOH C . 
K 3 HOH 19  519 336  HOH HOH C . 
K 3 HOH 20  520 97   HOH HOH C . 
K 3 HOH 21  521 931  HOH HOH C . 
K 3 HOH 22  522 699  HOH HOH C . 
K 3 HOH 23  523 595  HOH HOH C . 
K 3 HOH 24  524 26   HOH HOH C . 
K 3 HOH 25  525 8    HOH HOH C . 
K 3 HOH 26  526 446  HOH HOH C . 
K 3 HOH 27  527 148  HOH HOH C . 
K 3 HOH 28  528 53   HOH HOH C . 
K 3 HOH 29  529 204  HOH HOH C . 
K 3 HOH 30  530 344  HOH HOH C . 
K 3 HOH 31  531 612  HOH HOH C . 
K 3 HOH 32  532 74   HOH HOH C . 
K 3 HOH 33  533 309  HOH HOH C . 
K 3 HOH 34  534 328  HOH HOH C . 
K 3 HOH 35  535 81   HOH HOH C . 
K 3 HOH 36  536 143  HOH HOH C . 
K 3 HOH 37  537 210  HOH HOH C . 
K 3 HOH 38  538 502  HOH HOH C . 
K 3 HOH 39  539 229  HOH HOH C . 
K 3 HOH 40  540 668  HOH HOH C . 
K 3 HOH 41  541 885  HOH HOH C . 
K 3 HOH 42  542 174  HOH HOH C . 
K 3 HOH 43  543 448  HOH HOH C . 
K 3 HOH 44  544 17   HOH HOH C . 
K 3 HOH 45  545 798  HOH HOH C . 
K 3 HOH 46  546 898  HOH HOH C . 
K 3 HOH 47  547 71   HOH HOH C . 
K 3 HOH 48  548 537  HOH HOH C . 
K 3 HOH 49  549 860  HOH HOH C . 
K 3 HOH 50  550 221  HOH HOH C . 
K 3 HOH 51  551 321  HOH HOH C . 
K 3 HOH 52  552 664  HOH HOH C . 
K 3 HOH 53  553 65   HOH HOH C . 
K 3 HOH 54  554 405  HOH HOH C . 
K 3 HOH 55  555 186  HOH HOH C . 
K 3 HOH 56  556 140  HOH HOH C . 
K 3 HOH 57  557 149  HOH HOH C . 
K 3 HOH 58  558 178  HOH HOH C . 
K 3 HOH 59  559 70   HOH HOH C . 
K 3 HOH 60  560 159  HOH HOH C . 
K 3 HOH 61  561 305  HOH HOH C . 
K 3 HOH 62  562 610  HOH HOH C . 
K 3 HOH 63  563 380  HOH HOH C . 
K 3 HOH 64  564 41   HOH HOH C . 
K 3 HOH 65  565 276  HOH HOH C . 
K 3 HOH 66  566 442  HOH HOH C . 
K 3 HOH 67  567 440  HOH HOH C . 
K 3 HOH 68  568 90   HOH HOH C . 
K 3 HOH 69  569 169  HOH HOH C . 
K 3 HOH 70  570 533  HOH HOH C . 
K 3 HOH 71  571 459  HOH HOH C . 
K 3 HOH 72  572 792  HOH HOH C . 
K 3 HOH 73  573 397  HOH HOH C . 
K 3 HOH 74  574 172  HOH HOH C . 
K 3 HOH 75  575 144  HOH HOH C . 
K 3 HOH 76  576 250  HOH HOH C . 
K 3 HOH 77  577 67   HOH HOH C . 
K 3 HOH 78  578 488  HOH HOH C . 
K 3 HOH 79  579 789  HOH HOH C . 
K 3 HOH 80  580 56   HOH HOH C . 
K 3 HOH 81  581 327  HOH HOH C . 
K 3 HOH 82  582 267  HOH HOH C . 
K 3 HOH 83  583 505  HOH HOH C . 
K 3 HOH 84  584 240  HOH HOH C . 
K 3 HOH 85  585 89   HOH HOH C . 
K 3 HOH 86  586 208  HOH HOH C . 
K 3 HOH 87  587 315  HOH HOH C . 
K 3 HOH 88  588 507  HOH HOH C . 
K 3 HOH 89  589 382  HOH HOH C . 
K 3 HOH 90  590 585  HOH HOH C . 
K 3 HOH 91  591 490  HOH HOH C . 
K 3 HOH 92  592 989  HOH HOH C . 
K 3 HOH 93  593 1069 HOH HOH C . 
K 3 HOH 94  594 27   HOH HOH C . 
K 3 HOH 95  595 353  HOH HOH C . 
K 3 HOH 96  596 1048 HOH HOH C . 
K 3 HOH 97  597 922  HOH HOH C . 
K 3 HOH 98  598 602  HOH HOH C . 
K 3 HOH 99  599 679  HOH HOH C . 
K 3 HOH 100 600 925  HOH HOH C . 
K 3 HOH 101 601 1015 HOH HOH C . 
K 3 HOH 102 602 1074 HOH HOH C . 
K 3 HOH 103 603 1056 HOH HOH C . 
K 3 HOH 104 604 1047 HOH HOH C . 
K 3 HOH 105 605 452  HOH HOH C . 
K 3 HOH 106 606 820  HOH HOH C . 
K 3 HOH 107 607 1053 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 215 ? NZ  ? A LYS 186 NZ  
2  1 Y 1 A GLN 391 ? CG  ? A GLN 362 CG  
3  1 Y 1 A GLN 391 ? CD  ? A GLN 362 CD  
4  1 Y 1 A GLN 391 ? OE1 ? A GLN 362 OE1 
5  1 Y 1 A GLN 391 ? NE2 ? A GLN 362 NE2 
6  1 Y 1 B LYS 215 ? NZ  ? C LYS 186 NZ  
7  1 Y 1 C LYS 321 ? CG  ? D LYS 292 CG  
8  1 Y 1 C LYS 321 ? CD  ? D LYS 292 CD  
9  1 Y 1 C LYS 321 ? CE  ? D LYS 292 CE  
10 1 Y 1 C LYS 321 ? NZ  ? D LYS 292 NZ  
11 1 Y 1 C LYS 395 ? CG  ? D LYS 366 CG  
12 1 Y 1 C LYS 395 ? CD  ? D LYS 366 CD  
13 1 Y 1 C LYS 395 ? CE  ? D LYS 366 CE  
14 1 Y 1 C LYS 395 ? NZ  ? D LYS 366 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  70.75 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   81.37 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  74.74 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZVL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     57.600 
_cell.length_a_esd                 ? 
_cell.length_b                     78.010 
_cell.length_b_esd                 ? 
_cell.length_c                     103.120 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8ZVL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZVL 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.16 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.09 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M ammonium acetate pH=7.1, 20% w/v PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-09-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZVL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.05 
_reflns.d_resolution_low                               32.68 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     98576 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           96.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.181 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.990 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.151 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.05 
_reflns_shell.d_res_low                                     2.10 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             7191 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.012 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.423 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.828 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.01 
_refine.aniso_B[1][2]                            -0.03 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -0.01 
_refine.aniso_B[2][3]                            0.03 
_refine.aniso_B[3][3]                            -0.00 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               40.782 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.937 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8ZVL 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.05 
_refine.ls_d_res_low                             32.68 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     93672 
_refine.ls_number_reflns_R_free                  4896 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.38 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.19669 
_refine.ls_R_factor_R_free                       0.25837 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19350 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.255 
_refine.pdbx_overall_ESU_R_Free                  0.213 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             6.405 
_refine.overall_SU_ML                            0.169 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.05 
_refine_hist.d_res_low                        32.68 
_refine_hist.number_atoms_solvent             555 
_refine_hist.number_atoms_total               14274 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        13692 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         27 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  0.012  14068 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  13286 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.777  1.829  19096 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.599  1.749  30609 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.556  5.000  1738  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.324 5.000  79    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.597 10.000 2378  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.086  0.200  2096  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  16560 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  3212  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 4.003  3.919  6952  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.997  3.919  6952  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.630  7.031  8684  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.630  7.031  8685  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.816  4.470  7116  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.816  4.470  7117  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 7.227  7.950  10411 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 10.030 42.16  16636 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 10.033 42.06  16576 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.050 
_refine_ls_shell.d_res_low                        2.103 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             355 
_refine_ls_shell.number_reflns_R_work             6806 
_refine_ls_shell.percent_reflns_obs               95.89 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.305 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.341 
# 
_struct.entry_id                     8ZVL 
_struct.title                        'human citrate synthases complexed with oxaloacetate' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8ZVL 
_struct_keywords.text            'citrate synthase, complex, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 2 ? 
G N N 2 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CISY_HUMAN 
_struct_ref.pdbx_db_accession          O75390 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;STNLKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAK
GGEEPLPEGLFWLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAQGI
SRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNFTNMLGYTDHQFTELTRLYLTIHSDHEGGN
VSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAV
LRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA
LGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDSK
;
_struct_ref.pdbx_align_begin           30 
# 
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 8ZVL A 1 ? 435 ? O75390 30 ? 464 ? 30 464 
2 1 8ZVL D 1 ? 435 ? O75390 30 ? 464 ? 30 464 
3 1 8ZVL B 1 ? 435 ? O75390 30 ? 464 ? 30 464 
4 1 8ZVL C 1 ? 435 ? O75390 30 ? 464 ? 30 464 
# 
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 dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 9820  ? 
1 MORE         -63   ? 
1 'SSA (A^2)'  30930 ? 
2 'ABSA (A^2)' 9530  ? 
2 MORE         -62   ? 
2 'SSA (A^2)'  30330 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,H,I 
2 1 C,D,G,J,K   
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 3   ? GLY A 27  ? ASN A 32  GLY A 56  1 ? 25 
HELX_P HELX_P2  AA2 VAL A 36  ? GLY A 41  ? VAL A 65  GLY A 70  1 ? 6  
HELX_P HELX_P3  AA3 ILE A 69  ? LEU A 76  ? ILE A 98  LEU A 105 1 ? 8  
HELX_P HELX_P4  AA4 LEU A 86  ? GLY A 97  ? LEU A 115 GLY A 126 1 ? 12 
HELX_P HELX_P5  AA5 THR A 101 ? ARG A 115 ? THR A 130 ARG A 144 1 ? 15 
HELX_P HELX_P6  AA6 PRO A 119 ? PHE A 129 ? PRO A 148 PHE A 158 1 ? 11 
HELX_P HELX_P7  AA7 HIS A 134 ? LEU A 146 ? HIS A 163 LEU A 175 1 ? 13 
HELX_P HELX_P8  AA8 ASN A 147 ? GLU A 149 ? ASN A 176 GLU A 178 5 ? 3  
HELX_P HELX_P9  AA9 SER A 150 ? GLN A 158 ? SER A 179 GLN A 187 1 ? 9  
HELX_P HELX_P10 AB1 SER A 161 ? THR A 163 ? SER A 190 THR A 192 5 ? 3  
HELX_P HELX_P11 AB2 LYS A 164 ? ARG A 193 ? LYS A 193 ARG A 222 1 ? 30 
HELX_P HELX_P12 AB3 ASP A 206 ? GLY A 216 ? ASP A 235 GLY A 245 1 ? 11 
HELX_P HELX_P13 AB4 ASP A 219 ? HIS A 233 ? ASP A 248 HIS A 262 1 ? 15 
HELX_P HELX_P14 AB5 ASN A 240 ? SER A 251 ? ASN A 269 SER A 280 1 ? 12 
HELX_P HELX_P15 AB6 ASP A 255 ? ALA A 268 ? ASP A 284 ALA A 297 1 ? 14 
HELX_P HELX_P16 AB7 LEU A 274 ? GLU A 289 ? LEU A 303 GLU A 318 1 ? 16 
HELX_P HELX_P17 AB8 SER A 295 ? SER A 309 ? SER A 324 SER A 338 1 ? 15 
HELX_P HELX_P18 AB9 ASP A 325 ? LEU A 339 ? ASP A 354 LEU A 368 1 ? 15 
HELX_P HELX_P19 AC1 ASP A 342 ? GLY A 363 ? ASP A 371 GLY A 392 1 ? 22 
HELX_P HELX_P20 AC2 VAL A 372 ? TYR A 383 ? VAL A 401 TYR A 412 1 ? 12 
HELX_P HELX_P21 AC3 GLU A 387 ? ASN A 389 ? GLU A 416 ASN A 418 5 ? 3  
HELX_P HELX_P22 AC4 TYR A 390 ? LEU A 413 ? TYR A 419 LEU A 442 1 ? 24 
HELX_P HELX_P23 AC5 SER A 424 ? SER A 434 ? SER A 453 SER A 463 1 ? 11 
HELX_P HELX_P24 AC6 ASN B 3   ? GLY B 27  ? ASN D 32  GLY D 56  1 ? 25 
HELX_P HELX_P25 AC7 VAL B 36  ? GLY B 41  ? VAL D 65  GLY D 70  1 ? 6  
HELX_P HELX_P26 AC8 ILE B 69  ? LEU B 76  ? ILE D 98  LEU D 105 1 ? 8  
HELX_P HELX_P27 AC9 LEU B 86  ? GLY B 97  ? LEU D 115 GLY D 126 1 ? 12 
HELX_P HELX_P28 AD1 THR B 101 ? ARG B 115 ? THR D 130 ARG D 144 1 ? 15 
HELX_P HELX_P29 AD2 PRO B 119 ? PHE B 129 ? PRO D 148 PHE D 158 1 ? 11 
HELX_P HELX_P30 AD3 HIS B 134 ? LEU B 146 ? HIS D 163 LEU D 175 1 ? 13 
HELX_P HELX_P31 AD4 ASN B 147 ? GLU B 149 ? ASN D 176 GLU D 178 5 ? 3  
HELX_P HELX_P32 AD5 SER B 150 ? GLN B 158 ? SER D 179 GLN D 187 1 ? 9  
HELX_P HELX_P33 AD6 SER B 161 ? THR B 163 ? SER D 190 THR D 192 5 ? 3  
HELX_P HELX_P34 AD7 LYS B 164 ? ARG B 193 ? LYS D 193 ARG D 222 1 ? 30 
HELX_P HELX_P35 AD8 ASP B 206 ? GLY B 216 ? ASP D 235 GLY D 245 1 ? 11 
HELX_P HELX_P36 AD9 ASP B 219 ? HIS B 233 ? ASP D 248 HIS D 262 1 ? 15 
HELX_P HELX_P37 AE1 ASN B 240 ? ALA B 252 ? ASN D 269 ALA D 281 1 ? 13 
HELX_P HELX_P38 AE2 ASP B 255 ? ALA B 268 ? ASP D 284 ALA D 297 1 ? 14 
HELX_P HELX_P39 AE3 LEU B 274 ? GLY B 291 ? LEU D 303 GLY D 320 1 ? 18 
HELX_P HELX_P40 AE4 SER B 295 ? SER B 309 ? SER D 324 SER D 338 1 ? 15 
HELX_P HELX_P41 AE5 ASP B 325 ? LEU B 339 ? ASP D 354 LEU D 368 1 ? 15 
HELX_P HELX_P42 AE6 ASP B 342 ? GLN B 362 ? ASP D 371 GLN D 391 1 ? 21 
HELX_P HELX_P43 AE7 VAL B 372 ? TYR B 383 ? VAL D 401 TYR D 412 1 ? 12 
HELX_P HELX_P44 AE8 GLU B 387 ? ASN B 389 ? GLU D 416 ASN D 418 5 ? 3  
HELX_P HELX_P45 AE9 TYR B 390 ? LEU B 413 ? TYR D 419 LEU D 442 1 ? 24 
HELX_P HELX_P46 AF1 SER B 424 ? SER B 434 ? SER D 453 SER D 463 1 ? 11 
HELX_P HELX_P47 AF2 ASN C 3   ? GLY C 27  ? ASN B 32  GLY B 56  1 ? 25 
HELX_P HELX_P48 AF3 VAL C 36  ? GLY C 41  ? VAL B 65  GLY B 70  1 ? 6  
HELX_P HELX_P49 AF4 ILE C 69  ? LEU C 76  ? ILE B 98  LEU B 105 1 ? 8  
HELX_P HELX_P50 AF5 LEU C 86  ? GLY C 97  ? LEU B 115 GLY B 126 1 ? 12 
HELX_P HELX_P51 AF6 THR C 101 ? ARG C 115 ? THR B 130 ARG B 144 1 ? 15 
HELX_P HELX_P52 AF7 PRO C 119 ? PHE C 129 ? PRO B 148 PHE B 158 1 ? 11 
HELX_P HELX_P53 AF8 HIS C 134 ? LEU C 146 ? HIS B 163 LEU B 175 1 ? 13 
HELX_P HELX_P54 AF9 ASN C 147 ? GLU C 149 ? ASN B 176 GLU B 178 5 ? 3  
HELX_P HELX_P55 AG1 SER C 150 ? GLN C 158 ? SER B 179 GLN B 187 1 ? 9  
HELX_P HELX_P56 AG2 SER C 161 ? THR C 163 ? SER B 190 THR B 192 5 ? 3  
HELX_P HELX_P57 AG3 LYS C 164 ? ARG C 193 ? LYS B 193 ARG B 222 1 ? 30 
HELX_P HELX_P58 AG4 ASP C 206 ? GLY C 216 ? ASP B 235 GLY B 245 1 ? 11 
HELX_P HELX_P59 AG5 ASP C 219 ? HIS C 233 ? ASP B 248 HIS B 262 1 ? 15 
HELX_P HELX_P60 AG6 ASN C 240 ? SER C 251 ? ASN B 269 SER B 280 1 ? 12 
HELX_P HELX_P61 AG7 ASP C 255 ? ALA C 268 ? ASP B 284 ALA B 297 1 ? 14 
HELX_P HELX_P62 AG8 LEU C 274 ? GLU C 289 ? LEU B 303 GLU B 318 1 ? 16 
HELX_P HELX_P63 AG9 SER C 295 ? SER C 309 ? SER B 324 SER B 338 1 ? 15 
HELX_P HELX_P64 AH1 ASP C 325 ? LEU C 339 ? ASP B 354 LEU B 368 1 ? 15 
HELX_P HELX_P65 AH2 ASP C 342 ? GLY C 363 ? ASP B 371 GLY B 392 1 ? 22 
HELX_P HELX_P66 AH3 VAL C 372 ? TYR C 383 ? VAL B 401 TYR B 412 1 ? 12 
HELX_P HELX_P67 AH4 GLU C 387 ? ASN C 389 ? GLU B 416 ASN B 418 5 ? 3  
HELX_P HELX_P68 AH5 TYR C 390 ? LEU C 413 ? TYR B 419 LEU B 442 1 ? 24 
HELX_P HELX_P69 AH6 SER C 424 ? SER C 434 ? SER B 453 SER B 463 1 ? 11 
HELX_P HELX_P70 AH7 ASN D 3   ? GLY D 27  ? ASN C 32  GLY C 56  1 ? 25 
HELX_P HELX_P71 AH8 VAL D 36  ? GLY D 41  ? VAL C 65  GLY C 70  1 ? 6  
HELX_P HELX_P72 AH9 ILE D 69  ? LEU D 76  ? ILE C 98  LEU C 105 1 ? 8  
HELX_P HELX_P73 AI1 LEU D 86  ? GLY D 97  ? LEU C 115 GLY C 126 1 ? 12 
HELX_P HELX_P74 AI2 THR D 101 ? ARG D 115 ? THR C 130 ARG C 144 1 ? 15 
HELX_P HELX_P75 AI3 PRO D 119 ? PHE D 129 ? PRO C 148 PHE C 158 1 ? 11 
HELX_P HELX_P76 AI4 HIS D 134 ? LEU D 146 ? HIS C 163 LEU C 175 1 ? 13 
HELX_P HELX_P77 AI5 ASN D 147 ? GLU D 149 ? ASN C 176 GLU C 178 5 ? 3  
HELX_P HELX_P78 AI6 SER D 150 ? GLN D 158 ? SER C 179 GLN C 187 1 ? 9  
HELX_P HELX_P79 AI7 SER D 161 ? THR D 163 ? SER C 190 THR C 192 5 ? 3  
HELX_P HELX_P80 AI8 LYS D 164 ? ARG D 193 ? LYS C 193 ARG C 222 1 ? 30 
HELX_P HELX_P81 AI9 ASP D 206 ? GLY D 216 ? ASP C 235 GLY C 245 1 ? 11 
HELX_P HELX_P82 AJ1 ASP D 219 ? HIS D 233 ? ASP C 248 HIS C 262 1 ? 15 
HELX_P HELX_P83 AJ2 ASN D 240 ? ALA D 252 ? ASN C 269 ALA C 281 1 ? 13 
HELX_P HELX_P84 AJ3 ASP D 255 ? ALA D 268 ? ASP C 284 ALA C 297 1 ? 14 
HELX_P HELX_P85 AJ4 LEU D 274 ? VAL D 290 ? LEU C 303 VAL C 319 1 ? 17 
HELX_P HELX_P86 AJ5 SER D 295 ? SER D 309 ? SER C 324 SER C 338 1 ? 15 
HELX_P HELX_P87 AJ6 ASP D 325 ? LEU D 339 ? ASP C 354 LEU C 368 1 ? 15 
HELX_P HELX_P88 AJ7 ASP D 342 ? LYS D 353 ? ASP C 371 LYS C 382 1 ? 12 
HELX_P HELX_P89 AJ8 ILE D 354 ? GLU D 361 ? ILE C 383 GLU C 390 1 ? 8  
HELX_P HELX_P90 AJ9 VAL D 372 ? TYR D 383 ? VAL C 401 TYR C 412 1 ? 12 
HELX_P HELX_P91 AK1 GLU D 387 ? ASN D 389 ? GLU C 416 ASN C 418 5 ? 3  
HELX_P HELX_P92 AK2 TYR D 390 ? LEU D 413 ? TYR C 419 LEU C 442 1 ? 24 
HELX_P HELX_P93 AK3 SER D 424 ? SER D 434 ? SER C 453 SER C 463 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
AA8 ? 3 ? 
AA9 ? 2 ? 
AB1 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA9 1 2 ? parallel      
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 30  ? THR A 35  ? VAL A 59  THR A 64  
AA1 2 VAL B 30  ? THR B 35  ? VAL D 59  THR D 64  
AA2 1 LYS A 47  ? VAL A 50  ? LYS A 76  VAL A 79  
AA2 2 LYS B 421 ? MET B 423 ? LYS D 450 MET D 452 
AA3 1 SER A 54  ? ASP A 57  ? SER A 83  ASP A 86  
AA3 2 GLY A 61  ? PHE A 64  ? GLY A 90  PHE A 93  
AA3 3 PHE A 67  ? SER A 68  ? PHE A 96  SER A 97  
AA4 1 LYS A 421 ? MET A 423 ? LYS A 450 MET A 452 
AA4 2 LYS B 47  ? VAL B 50  ? LYS D 76  VAL D 79  
AA5 1 SER B 54  ? ASP B 57  ? SER D 83  ASP D 86  
AA5 2 GLY B 61  ? PHE B 64  ? GLY D 90  PHE D 93  
AA5 3 PHE B 67  ? SER B 68  ? PHE D 96  SER D 97  
AA6 1 VAL C 30  ? THR C 35  ? VAL B 59  THR B 64  
AA6 2 VAL D 30  ? THR D 35  ? VAL C 59  THR C 64  
AA7 1 LYS C 47  ? VAL C 50  ? LYS B 76  VAL B 79  
AA7 2 LYS D 421 ? MET D 423 ? LYS C 450 MET C 452 
AA8 1 SER C 54  ? ASP C 57  ? SER B 83  ASP B 86  
AA8 2 GLY C 61  ? PHE C 64  ? GLY B 90  PHE B 93  
AA8 3 PHE C 67  ? SER C 68  ? PHE B 96  SER B 97  
AA9 1 LYS C 421 ? MET C 423 ? LYS B 450 MET B 452 
AA9 2 LYS D 47  ? VAL D 50  ? LYS C 76  VAL C 79  
AB1 1 SER D 54  ? ASP D 57  ? SER C 83  ASP C 86  
AB1 2 GLY D 61  ? PHE D 64  ? GLY C 90  PHE C 93  
AB1 3 PHE D 67  ? SER D 68  ? PHE C 96  SER C 97  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 34  ? N ILE A 63  O VAL B 31  ? O VAL D 60  
AA2 1 2 N GLY A 48  ? N GLY A 77  O LYS B 421 ? O LYS D 450 
AA3 1 2 N ASP A 57  ? N ASP A 86  O GLY A 61  ? O GLY A 90  
AA3 2 3 N PHE A 64  ? N PHE A 93  O PHE A 67  ? O PHE A 96  
AA4 1 2 N LYS A 421 ? N LYS A 450 O GLY B 48  ? O GLY D 77  
AA5 1 2 N ASP B 57  ? N ASP D 86  O GLY B 61  ? O GLY D 90  
AA5 2 3 N PHE B 64  ? N PHE D 93  O PHE B 67  ? O PHE D 96  
AA6 1 2 N VAL C 31  ? N VAL B 60  O ILE D 34  ? O ILE C 63  
AA7 1 2 N GLY C 48  ? N GLY B 77  O LYS D 421 ? O LYS C 450 
AA8 1 2 N ASP C 57  ? N ASP B 86  O GLY C 61  ? O GLY B 90  
AA8 2 3 N PHE C 64  ? N PHE B 93  O PHE C 67  ? O PHE B 96  
AA9 1 2 N LYS C 421 ? N LYS B 450 O GLY D 48  ? O GLY C 77  
AB1 1 2 N VAL D 55  ? N VAL C 84  O ARG D 63  ? O ARG C 92  
AB1 2 3 N PHE D 64  ? N PHE C 93  O PHE D 67  ? O PHE C 96  
# 
_pdbx_entry_details.entry_id                   8ZVL 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
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 OE2 C GLU 326 ? ? O C HOH 501 ? ? 2.04 
2 1 NH1 C ARG 329 ? ? O C HOH 502 ? ? 2.07 
3 1 OG  D SER 288 ? ? O D HOH 601 ? ? 2.12 
4 1 OG  B SER 30  ? ? O B HOH 601 ? ? 2.17 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            B 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             318 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            N 
_pdbx_validate_rmsd_bond.auth_asym_id_2            B 
_pdbx_validate_rmsd_bond.auth_comp_id_2            VAL 
_pdbx_validate_rmsd_bond.auth_seq_id_2             319 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.498 
_pdbx_validate_rmsd_bond.bond_target_value         1.336 
_pdbx_validate_rmsd_bond.bond_deviation            0.162 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.023 
_pdbx_validate_rmsd_bond.linker_flag               Y 
# 
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 CG A MET 293 ? ? SD A MET 293 ? ? CE  A MET 293 ? ? 112.47 100.20 12.27  1.60 N 
2 1 CG A MET 414 ? ? SD A MET 414 ? ? CE  A MET 414 ? ? 112.68 100.20 12.48  1.60 N 
3 1 N  D PRO 397 ? ? CA D PRO 397 ? ? CB  D PRO 397 ? ? 95.06  103.30 -8.24  1.20 N 
4 1 NE D ARG 440 ? ? CZ D ARG 440 ? ? NH2 D ARG 440 ? ? 113.93 120.30 -6.37  0.50 N 
5 1 CG B MET 72  ? ? SD B MET 72  ? ? CE  B MET 72  ? ? 110.16 100.20 9.96   1.60 N 
6 1 CG B ARG 440 ? ? CD B ARG 440 ? ? NE  B ARG 440 ? ? 97.95  111.80 -13.85 2.10 N 
7 1 CG C MET 414 ? ? SD C MET 414 ? ? CE  C MET 414 ? ? 121.34 100.20 21.14  1.60 N 
8 1 NE C ARG 448 ? ? CZ C ARG 448 ? ? NH1 C ARG 448 ? ? 124.47 120.30 4.17   0.50 N 
9 1 NE C ARG 448 ? ? CZ C ARG 448 ? ? NH2 C ARG 448 ? ? 117.11 120.30 -3.19  0.50 N 
# 
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 THR A 31  ? ? -127.40 -57.66  
2  1 HIS A 265 ? ? -151.60 46.89   
3  1 GLU A 266 ? ? 79.85   -178.98 
4  1 HIS A 301 ? ? -126.39 -76.52  
5  1 VAL A 319 ? ? -138.33 -55.31  
6  1 TYR A 345 ? ? -113.88 59.09   
7  1 VAL A 349 ? ? -127.46 -54.42  
8  1 LEU A 368 ? ? -150.55 53.22   
9  1 ASP D 88  ? ? -94.86  -60.56  
10 1 LYS D 109 ? ? -57.08  107.77  
11 1 HIS D 265 ? ? -152.55 64.73   
12 1 GLU D 266 ? ? 66.98   -175.38 
13 1 ALA D 348 ? ? -84.72  -102.67 
14 1 LEU D 368 ? ? -143.23 49.10   
15 1 LYS D 393 ? ? -152.01 -134.39 
16 1 ARG D 448 ? ? -153.13 76.92   
17 1 HIS B 265 ? ? -155.00 52.51   
18 1 GLU B 266 ? ? 75.21   -176.75 
19 1 HIS B 301 ? ? -126.99 -57.04  
20 1 VAL B 319 ? ? -142.24 11.21   
21 1 LEU B 368 ? ? -148.83 43.26   
22 1 ARG B 448 ? ? -151.29 76.72   
23 1 HIS C 55  ? ? -140.05 12.18   
24 1 ASP C 88  ? ? 88.96   -56.86  
25 1 THR C 247 ? ? -160.02 69.13   
26 1 HIS C 265 ? ? -148.79 57.08   
27 1 GLU C 266 ? ? 72.64   -179.73 
28 1 HIS C 301 ? ? -114.12 -117.43 
29 1 LEU C 368 ? ? -148.00 56.39   
30 1 ILE C 383 ? ? -138.54 -48.96  
31 1 LYS C 393 ? ? -85.52  44.00   
32 1 ARG C 448 ? ? -153.71 83.94   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1  1 ARG A 47  ? ? 0.091 'SIDE CHAIN' 
2  1 ARG A 218 ? ? 0.199 'SIDE CHAIN' 
3  1 ARG A 440 ? ? 0.110 'SIDE CHAIN' 
4  1 ARG D 47  ? ? 0.104 'SIDE CHAIN' 
5  1 ARG D 440 ? ? 0.196 'SIDE CHAIN' 
6  1 ARG D 448 ? ? 0.116 'SIDE CHAIN' 
7  1 ARG B 440 ? ? 0.096 'SIDE CHAIN' 
8  1 ARG B 448 ? ? 0.107 'SIDE CHAIN' 
9  1 ARG C 361 ? ? 0.129 'SIDE CHAIN' 
10 1 ARG C 448 ? ? 0.075 'SIDE CHAIN' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 851 ? 5.89 . 
2 1 O ? D HOH 750 ? 6.46 . 
3 1 O ? B HOH 746 ? 5.97 . 
4 1 O ? B HOH 747 ? 6.05 . 
5 1 O ? C HOH 607 ? 6.08 . 
# 
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 LYS 464 ? A LYS 435 
2 1 Y 1 B LYS 464 ? C LYS 435 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
OAA O1   O N N 250 
OAA O2   O N N 251 
OAA O4   O N N 252 
OAA O5   O N N 253 
OAA O3   O N N 254 
OAA C1   C N N 255 
OAA C2   C N N 256 
OAA C3   C N N 257 
OAA C4   C N N 258 
OAA HO5  H N N 259 
OAA H21  H N N 260 
OAA H22  H N N 261 
PHE N    N N N 262 
PHE CA   C N S 263 
PHE C    C N N 264 
PHE O    O N N 265 
PHE CB   C N N 266 
PHE CG   C Y N 267 
PHE CD1  C Y N 268 
PHE CD2  C Y N 269 
PHE CE1  C Y N 270 
PHE CE2  C Y N 271 
PHE CZ   C Y N 272 
PHE OXT  O N N 273 
PHE H    H N N 274 
PHE H2   H N N 275 
PHE HA   H N N 276 
PHE HB2  H N N 277 
PHE HB3  H N N 278 
PHE HD1  H N N 279 
PHE HD2  H N N 280 
PHE HE1  H N N 281 
PHE HE2  H N N 282 
PHE HZ   H N N 283 
PHE HXT  H N N 284 
PRO N    N N N 285 
PRO CA   C N S 286 
PRO C    C N N 287 
PRO O    O N N 288 
PRO CB   C N N 289 
PRO CG   C N N 290 
PRO CD   C N N 291 
PRO OXT  O N N 292 
PRO H    H N N 293 
PRO HA   H N N 294 
PRO HB2  H N N 295 
PRO HB3  H N N 296 
PRO HG2  H N N 297 
PRO HG3  H N N 298 
PRO HD2  H N N 299 
PRO HD3  H N N 300 
PRO HXT  H N N 301 
SER N    N N N 302 
SER CA   C N S 303 
SER C    C N N 304 
SER O    O N N 305 
SER CB   C N N 306 
SER OG   O N N 307 
SER OXT  O N N 308 
SER H    H N N 309 
SER H2   H N N 310 
SER HA   H N N 311 
SER HB2  H N N 312 
SER HB3  H N N 313 
SER HG   H N N 314 
SER HXT  H N N 315 
THR N    N N N 316 
THR CA   C N S 317 
THR C    C N N 318 
THR O    O N N 319 
THR CB   C N R 320 
THR OG1  O N N 321 
THR CG2  C N N 322 
THR OXT  O N N 323 
THR H    H N N 324 
THR H2   H N N 325 
THR HA   H N N 326 
THR HB   H N N 327 
THR HG1  H N N 328 
THR HG21 H N N 329 
THR HG22 H N N 330 
THR HG23 H N N 331 
THR HXT  H N N 332 
TRP N    N N N 333 
TRP CA   C N S 334 
TRP C    C N N 335 
TRP O    O N N 336 
TRP CB   C N N 337 
TRP CG   C Y N 338 
TRP CD1  C Y N 339 
TRP CD2  C Y N 340 
TRP NE1  N Y N 341 
TRP CE2  C Y N 342 
TRP CE3  C Y N 343 
TRP CZ2  C Y N 344 
TRP CZ3  C Y N 345 
TRP CH2  C Y N 346 
TRP OXT  O N N 347 
TRP H    H N N 348 
TRP H2   H N N 349 
TRP HA   H N N 350 
TRP HB2  H N N 351 
TRP HB3  H N N 352 
TRP HD1  H N N 353 
TRP HE1  H N N 354 
TRP HE3  H N N 355 
TRP HZ2  H N N 356 
TRP HZ3  H N N 357 
TRP HH2  H N N 358 
TRP HXT  H N N 359 
TYR N    N N N 360 
TYR CA   C N S 361 
TYR C    C N N 362 
TYR O    O N N 363 
TYR CB   C N N 364 
TYR CG   C Y N 365 
TYR CD1  C Y N 366 
TYR CD2  C Y N 367 
TYR CE1  C Y N 368 
TYR CE2  C Y N 369 
TYR CZ   C Y N 370 
TYR OH   O N N 371 
TYR OXT  O N N 372 
TYR H    H N N 373 
TYR H2   H N N 374 
TYR HA   H N N 375 
TYR HB2  H N N 376 
TYR HB3  H N N 377 
TYR HD1  H N N 378 
TYR HD2  H N N 379 
TYR HE1  H N N 380 
TYR HE2  H N N 381 
TYR HH   H N N 382 
TYR HXT  H N N 383 
VAL N    N N N 384 
VAL CA   C N S 385 
VAL C    C N N 386 
VAL O    O N N 387 
VAL CB   C N N 388 
VAL CG1  C N N 389 
VAL CG2  C N N 390 
VAL OXT  O N N 391 
VAL H    H N N 392 
VAL H2   H N N 393 
VAL HA   H N N 394 
VAL HB   H N N 395 
VAL HG11 H N N 396 
VAL HG12 H N N 397 
VAL HG13 H N N 398 
VAL HG21 H N N 399 
VAL HG22 H N N 400 
VAL HG23 H N N 401 
VAL HXT  H N N 402 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
OAA O1  C1   doub N N 237 
OAA O2  C1   sing N N 238 
OAA O4  C4   doub N N 239 
OAA O5  C4   sing N N 240 
OAA O5  HO5  sing N N 241 
OAA O3  C3   doub N N 242 
OAA C1  C2   sing N N 243 
OAA C2  C3   sing N N 244 
OAA C2  H21  sing N N 245 
OAA C2  H22  sing N N 246 
OAA C3  C4   sing N N 247 
PHE N   CA   sing N N 248 
PHE N   H    sing N N 249 
PHE N   H2   sing N N 250 
PHE CA  C    sing N N 251 
PHE CA  CB   sing N N 252 
PHE CA  HA   sing N N 253 
PHE C   O    doub N N 254 
PHE C   OXT  sing N N 255 
PHE CB  CG   sing N N 256 
PHE CB  HB2  sing N N 257 
PHE CB  HB3  sing N N 258 
PHE CG  CD1  doub Y N 259 
PHE CG  CD2  sing Y N 260 
PHE CD1 CE1  sing Y N 261 
PHE CD1 HD1  sing N N 262 
PHE CD2 CE2  doub Y N 263 
PHE CD2 HD2  sing N N 264 
PHE CE1 CZ   doub Y N 265 
PHE CE1 HE1  sing N N 266 
PHE CE2 CZ   sing Y N 267 
PHE CE2 HE2  sing N N 268 
PHE CZ  HZ   sing N N 269 
PHE OXT HXT  sing N N 270 
PRO N   CA   sing N N 271 
PRO N   CD   sing N N 272 
PRO N   H    sing N N 273 
PRO CA  C    sing N N 274 
PRO CA  CB   sing N N 275 
PRO CA  HA   sing N N 276 
PRO C   O    doub N N 277 
PRO C   OXT  sing N N 278 
PRO CB  CG   sing N N 279 
PRO CB  HB2  sing N N 280 
PRO CB  HB3  sing N N 281 
PRO CG  CD   sing N N 282 
PRO CG  HG2  sing N N 283 
PRO CG  HG3  sing N N 284 
PRO CD  HD2  sing N N 285 
PRO CD  HD3  sing N N 286 
PRO OXT HXT  sing N N 287 
SER N   CA   sing N N 288 
SER N   H    sing N N 289 
SER N   H2   sing N N 290 
SER CA  C    sing N N 291 
SER CA  CB   sing N N 292 
SER CA  HA   sing N N 293 
SER C   O    doub N N 294 
SER C   OXT  sing N N 295 
SER CB  OG   sing N N 296 
SER CB  HB2  sing N N 297 
SER CB  HB3  sing N N 298 
SER OG  HG   sing N N 299 
SER OXT HXT  sing N N 300 
THR N   CA   sing N N 301 
THR N   H    sing N N 302 
THR N   H2   sing N N 303 
THR CA  C    sing N N 304 
THR CA  CB   sing N N 305 
THR CA  HA   sing N N 306 
THR C   O    doub N N 307 
THR C   OXT  sing N N 308 
THR CB  OG1  sing N N 309 
THR CB  CG2  sing N N 310 
THR CB  HB   sing N N 311 
THR OG1 HG1  sing N N 312 
THR CG2 HG21 sing N N 313 
THR CG2 HG22 sing N N 314 
THR CG2 HG23 sing N N 315 
THR OXT HXT  sing N N 316 
TRP N   CA   sing N N 317 
TRP N   H    sing N N 318 
TRP N   H2   sing N N 319 
TRP CA  C    sing N N 320 
TRP CA  CB   sing N N 321 
TRP CA  HA   sing N N 322 
TRP C   O    doub N N 323 
TRP C   OXT  sing N N 324 
TRP CB  CG   sing N N 325 
TRP CB  HB2  sing N N 326 
TRP CB  HB3  sing N N 327 
TRP CG  CD1  doub Y N 328 
TRP CG  CD2  sing Y N 329 
TRP CD1 NE1  sing Y N 330 
TRP CD1 HD1  sing N N 331 
TRP CD2 CE2  doub Y N 332 
TRP CD2 CE3  sing Y N 333 
TRP NE1 CE2  sing Y N 334 
TRP NE1 HE1  sing N N 335 
TRP CE2 CZ2  sing Y N 336 
TRP CE3 CZ3  doub Y N 337 
TRP CE3 HE3  sing N N 338 
TRP CZ2 CH2  doub Y N 339 
TRP CZ2 HZ2  sing N N 340 
TRP CZ3 CH2  sing Y N 341 
TRP CZ3 HZ3  sing N N 342 
TRP CH2 HH2  sing N N 343 
TRP OXT HXT  sing N N 344 
TYR N   CA   sing N N 345 
TYR N   H    sing N N 346 
TYR N   H2   sing N N 347 
TYR CA  C    sing N N 348 
TYR CA  CB   sing N N 349 
TYR CA  HA   sing N N 350 
TYR C   O    doub N N 351 
TYR C   OXT  sing N N 352 
TYR CB  CG   sing N N 353 
TYR CB  HB2  sing N N 354 
TYR CB  HB3  sing N N 355 
TYR CG  CD1  doub Y N 356 
TYR CG  CD2  sing Y N 357 
TYR CD1 CE1  sing Y N 358 
TYR CD1 HD1  sing N N 359 
TYR CD2 CE2  doub Y N 360 
TYR CD2 HD2  sing N N 361 
TYR CE1 CZ   doub Y N 362 
TYR CE1 HE1  sing N N 363 
TYR CE2 CZ   sing Y N 364 
TYR CE2 HE2  sing N N 365 
TYR CZ  OH   sing N N 366 
TYR OH  HH   sing N N 367 
TYR OXT HXT  sing N N 368 
VAL N   CA   sing N N 369 
VAL N   H    sing N N 370 
VAL N   H2   sing N N 371 
VAL CA  C    sing N N 372 
VAL CA  CB   sing N N 373 
VAL CA  HA   sing N N 374 
VAL C   O    doub N N 375 
VAL C   OXT  sing N N 376 
VAL CB  CG1  sing N N 377 
VAL CB  CG2  sing N N 378 
VAL CB  HB   sing N N 379 
VAL CG1 HG11 sing N N 380 
VAL CG1 HG12 sing N N 381 
VAL CG1 HG13 sing N N 382 
VAL CG2 HG21 sing N N 383 
VAL CG2 HG22 sing N N 384 
VAL CG2 HG23 sing N N 385 
VAL OXT HXT  sing N N 386 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5UZR 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZVL 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.017361 
_atom_sites.fract_transf_matrix[1][2]   -0.004736 
_atom_sites.fract_transf_matrix[1][3]   -0.001253 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013287 
_atom_sites.fract_transf_matrix[2][3]   -0.004244 
_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]   0.010297 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . SER A 1 1   ? 53.399  -1.566  14.873  1.00 63.69  ? 30  SER A N   1 
ATOM   2     C CA  . SER A 1 1   ? 54.128  -2.795  14.448  1.00 59.93  ? 30  SER A CA  1 
ATOM   3     C C   . SER A 1 1   ? 53.278  -4.053  14.665  1.00 53.44  ? 30  SER A C   1 
ATOM   4     O O   . SER A 1 1   ? 53.010  -4.757  13.693  1.00 49.74  ? 30  SER A O   1 
ATOM   5     C CB  . SER A 1 1   ? 55.478  -2.913  15.131  1.00 57.42  ? 30  SER A CB  1 
ATOM   6     O OG  . SER A 1 1   ? 56.188  -4.082  14.745  1.00 43.93  ? 30  SER A OG  1 
ATOM   7     N N   . THR A 1 2   ? 52.890  -4.362  15.921  1.00 46.74  ? 31  THR A N   1 
ATOM   8     C CA  . THR A 1 2   ? 52.156  -5.601  16.205  1.00 53.16  ? 31  THR A CA  1 
ATOM   9     C C   . THR A 1 2   ? 50.852  -5.356  16.988  1.00 45.38  ? 31  THR A C   1 
ATOM   10    O O   . THR A 1 2   ? 49.801  -5.815  16.575  1.00 54.04  ? 31  THR A O   1 
ATOM   11    C CB  . THR A 1 2   ? 53.054  -6.608  16.929  1.00 55.18  ? 31  THR A CB  1 
ATOM   12    O OG1 . THR A 1 2   ? 53.862  -5.838  17.814  1.00 58.67  ? 31  THR A OG1 1 
ATOM   13    C CG2 . THR A 1 2   ? 53.917  -7.417  15.975  1.00 62.53  ? 31  THR A CG2 1 
ATOM   14    N N   . ASN A 1 3   ? 50.950  -4.734  18.164  1.00 40.03  ? 32  ASN A N   1 
ATOM   15    C CA  . ASN A 1 3   ? 49.831  -4.184  18.919  1.00 37.94  ? 32  ASN A CA  1 
ATOM   16    C C   . ASN A 1 3   ? 48.923  -3.368  18.012  1.00 31.84  ? 32  ASN A C   1 
ATOM   17    O O   . ASN A 1 3   ? 49.393  -2.514  17.250  1.00 34.45  ? 32  ASN A O   1 
ATOM   18    C CB  . ASN A 1 3   ? 50.336  -3.284  20.046  1.00 40.15  ? 32  ASN A CB  1 
ATOM   19    C CG  . ASN A 1 3   ? 49.278  -2.983  21.080  1.00 47.77  ? 32  ASN A CG  1 
ATOM   20    O OD1 . ASN A 1 3   ? 48.133  -2.645  20.747  1.00 41.70  ? 32  ASN A OD1 1 
ATOM   21    N ND2 . ASN A 1 3   ? 49.642  -3.106  22.346  1.00 49.43  ? 32  ASN A ND2 1 
ATOM   22    N N   . LEU A 1 4   ? 47.616  -3.615  18.141  1.00 33.45  ? 33  LEU A N   1 
ATOM   23    C CA  . LEU A 1 4   ? 46.585  -2.897  17.402  1.00 28.02  ? 33  LEU A CA  1 
ATOM   24    C C   . LEU A 1 4   ? 46.765  -1.398  17.579  1.00 24.14  ? 33  LEU A C   1 
ATOM   25    O O   . LEU A 1 4   ? 46.648  -0.653  16.629  1.00 29.06  ? 33  LEU A O   1 
ATOM   26    C CB  . LEU A 1 4   ? 45.191  -3.372  17.826  1.00 27.61  ? 33  LEU A CB  1 
ATOM   27    C CG  . LEU A 1 4   ? 43.997  -2.767  17.093  1.00 24.97  ? 33  LEU A CG  1 
ATOM   28    C CD1 . LEU A 1 4   ? 44.030  -2.856  15.580  1.00 30.48  ? 33  LEU A CD1 1 
ATOM   29    C CD2 . LEU A 1 4   ? 42.757  -3.400  17.596  1.00 29.78  ? 33  LEU A CD2 1 
ATOM   30    N N   . LYS A 1 5   ? 47.085  -0.939  18.778  1.00 28.58  ? 34  LYS A N   1 
ATOM   31    C CA  . LYS A 1 5   ? 47.168  0.499   19.025  1.00 27.76  ? 34  LYS A CA  1 
ATOM   32    C C   . LYS A 1 5   ? 48.335  1.143   18.241  1.00 30.92  ? 34  LYS A C   1 
ATOM   33    O O   . LYS A 1 5   ? 48.225  2.272   17.737  1.00 28.70  ? 34  LYS A O   1 
ATOM   34    C CB  . LYS A 1 5   ? 47.235  0.718   20.536  1.00 27.78  ? 34  LYS A CB  1 
ATOM   35    C CG  . LYS A 1 5   ? 46.963  2.144   20.970  1.00 29.48  ? 34  LYS A CG  1 
ATOM   36    C CD  . LYS A 1 5   ? 47.271  2.350   22.443  1.00 32.12  ? 34  LYS A CD  1 
ATOM   37    C CE  . LYS A 1 5   ? 46.684  3.617   22.971  1.00 31.74  ? 34  LYS A CE  1 
ATOM   38    N NZ  . LYS A 1 5   ? 47.035  3.712   24.389  1.00 33.51  ? 34  LYS A NZ  1 
ATOM   39    N N   . ASP A 1 6   ? 49.443  0.402   18.085  1.00 33.19  ? 35  ASP A N   1 
ATOM   40    C CA  . ASP A 1 6   ? 50.598  0.848   17.315  1.00 33.27  ? 35  ASP A CA  1 
ATOM   41    C C   . ASP A 1 6   ? 50.323  0.855   15.817  1.00 29.68  ? 35  ASP A C   1 
ATOM   42    O O   . ASP A 1 6   ? 50.668  1.805   15.136  1.00 28.82  ? 35  ASP A O   1 
ATOM   43    C CB  . ASP A 1 6   ? 51.798  -0.017  17.637  1.00 39.90  ? 35  ASP A CB  1 
ATOM   44    C CG  . ASP A 1 6   ? 52.225  0.083   19.093  1.00 45.99  ? 35  ASP A CG  1 
ATOM   45    O OD1 . ASP A 1 6   ? 52.271  1.232   19.587  1.00 50.38  ? 35  ASP A OD1 1 
ATOM   46    O OD2 . ASP A 1 6   ? 52.531  -0.972  19.701  1.00 55.61  ? 35  ASP A OD2 1 
ATOM   47    N N   . ILE A 1 7   ? 49.692  -0.210  15.308  1.00 33.30  ? 36  ILE A N   1 
ATOM   48    C CA  . ILE A 1 7   ? 49.275  -0.262  13.920  1.00 34.08  ? 36  ILE A CA  1 
ATOM   49    C C   . ILE A 1 7   ? 48.301  0.881   13.619  1.00 32.56  ? 36  ILE A C   1 
ATOM   50    O O   . ILE A 1 7   ? 48.336  1.530   12.581  1.00 30.92  ? 36  ILE A O   1 
ATOM   51    C CB  . ILE A 1 7   ? 48.681  -1.652  13.658  1.00 39.00  ? 36  ILE A CB  1 
ATOM   52    C CG1 . ILE A 1 7   ? 49.792  -2.728  13.659  1.00 38.15  ? 36  ILE A CG1 1 
ATOM   53    C CG2 . ILE A 1 7   ? 47.900  -1.657  12.354  1.00 38.27  ? 36  ILE A CG2 1 
ATOM   54    C CD1 . ILE A 1 7   ? 49.335  -4.088  14.117  1.00 39.89  ? 36  ILE A CD1 1 
ATOM   55    N N   . LEU A 1 8   ? 47.411  1.172   14.549  1.00 31.55  ? 37  LEU A N   1 
ATOM   56    C CA  . LEU A 1 8   ? 46.480  2.248   14.319  1.00 29.37  ? 37  LEU A CA  1 
ATOM   57    C C   . LEU A 1 8   ? 47.191  3.601   14.336  1.00 30.06  ? 37  LEU A C   1 
ATOM   58    O O   . LEU A 1 8   ? 46.917  4.445   13.492  1.00 33.11  ? 37  LEU A O   1 
ATOM   59    C CB  . LEU A 1 8   ? 45.444  2.012   15.407  1.00 35.22  ? 37  LEU A CB  1 
ATOM   60    C CG  . LEU A 1 8   ? 44.210  2.891   15.355  1.00 38.89  ? 37  LEU A CG  1 
ATOM   61    C CD1 . LEU A 1 8   ? 43.654  3.002   13.955  1.00 41.47  ? 37  LEU A CD1 1 
ATOM   62    C CD2 . LEU A 1 8   ? 43.232  2.251   16.327  1.00 42.61  ? 37  LEU A CD2 1 
ATOM   63    N N   . ALA A 1 9   ? 48.178  3.776   15.223  1.00 27.46  ? 38  ALA A N   1 
ATOM   64    C CA  . ALA A 1 9   ? 48.960  4.991   15.281  1.00 29.93  ? 38  ALA A CA  1 
ATOM   65    C C   . ALA A 1 9   ? 49.653  5.272   13.960  1.00 32.81  ? 38  ALA A C   1 
ATOM   66    O O   . ALA A 1 9   ? 49.715  6.436   13.597  1.00 28.08  ? 38  ALA A O   1 
ATOM   67    C CB  . ALA A 1 9   ? 49.971  4.961   16.413  1.00 28.52  ? 38  ALA A CB  1 
ATOM   68    N N   . ASP A 1 10  ? 50.132  4.216   13.275  1.00 31.18  ? 39  ASP A N   1 
ATOM   69    C CA  . ASP A 1 10  ? 50.794  4.364   11.992  1.00 33.88  ? 39  ASP A CA  1 
ATOM   70    C C   . ASP A 1 10  ? 49.790  4.737   10.891  1.00 34.22  ? 39  ASP A C   1 
ATOM   71    O O   . ASP A 1 10  ? 50.141  5.461   9.950   1.00 34.14  ? 39  ASP A O   1 
ATOM   72    C CB  . ASP A 1 10  ? 51.594  3.107   11.656  1.00 34.39  ? 39  ASP A CB  1 
ATOM   73    C CG  . ASP A 1 10  ? 52.827  2.789   12.509  1.00 40.48  ? 39  ASP A CG  1 
ATOM   74    O OD1 . ASP A 1 10  ? 53.333  3.689   13.221  1.00 45.22  ? 39  ASP A OD1 1 
ATOM   75    O OD2 . ASP A 1 10  ? 53.290  1.619   12.473  1.00 39.27  ? 39  ASP A OD2 1 
ATOM   76    N N   . LEU A 1 11  ? 48.551  4.206   10.962  1.00 32.79  ? 40  LEU A N   1 
ATOM   77    C CA  . LEU A 1 11  ? 47.550  4.400   9.913   1.00 29.96  ? 40  LEU A CA  1 
ATOM   78    C C   . LEU A 1 11  ? 46.925  5.787   9.985   1.00 31.38  ? 40  LEU A C   1 
ATOM   79    O O   . LEU A 1 11  ? 46.510  6.335   8.960   1.00 31.60  ? 40  LEU A O   1 
ATOM   80    C CB  . LEU A 1 11  ? 46.455  3.333   9.994   1.00 32.60  ? 40  LEU A CB  1 
ATOM   81    C CG  . LEU A 1 11  ? 46.886  1.927   9.594   1.00 35.48  ? 40  LEU A CG  1 
ATOM   82    C CD1 . LEU A 1 11  ? 45.839  0.893   9.895   1.00 43.68  ? 40  LEU A CD1 1 
ATOM   83    C CD2 . LEU A 1 11  ? 47.210  1.919   8.090   1.00 36.68  ? 40  LEU A CD2 1 
ATOM   84    N N   . ILE A 1 12  ? 46.892  6.393   11.184  1.00 29.22  ? 41  ILE A N   1 
ATOM   85    C CA  . ILE A 1 12  ? 46.101  7.593   11.337  1.00 24.49  ? 41  ILE A CA  1 
ATOM   86    C C   . ILE A 1 12  ? 46.691  8.735   10.512  1.00 28.07  ? 41  ILE A C   1 
ATOM   87    O O   . ILE A 1 12  ? 45.932  9.367   9.775   1.00 33.61  ? 41  ILE A O   1 
ATOM   88    C CB  . ILE A 1 12  ? 45.841  7.901   12.815  1.00 28.30  ? 41  ILE A CB  1 
ATOM   89    C CG1 . ILE A 1 12  ? 44.783  6.927   13.388  1.00 30.35  ? 41  ILE A CG1 1 
ATOM   90    C CG2 . ILE A 1 12  ? 45.405  9.346   13.026  1.00 28.38  ? 41  ILE A CG2 1 
ATOM   91    C CD1 . ILE A 1 12  ? 44.785  6.834   14.909  1.00 31.23  ? 41  ILE A CD1 1 
ATOM   92    N N   . PRO A 1 13  ? 48.003  9.065   10.594  1.00 31.50  ? 42  PRO A N   1 
ATOM   93    C CA  . PRO A 1 13  ? 48.570  10.189  9.838   1.00 32.01  ? 42  PRO A CA  1 
ATOM   94    C C   . PRO A 1 13  ? 48.233  10.160  8.355   1.00 30.94  ? 42  PRO A C   1 
ATOM   95    O O   . PRO A 1 13  ? 47.893  11.187  7.767   1.00 37.62  ? 42  PRO A O   1 
ATOM   96    C CB  . PRO A 1 13  ? 50.101  10.093  10.063  1.00 33.40  ? 42  PRO A CB  1 
ATOM   97    C CG  . PRO A 1 13  ? 50.233  9.298   11.365  1.00 34.71  ? 42  PRO A CG  1 
ATOM   98    C CD  . PRO A 1 13  ? 49.008  8.411   11.464  1.00 32.34  ? 42  PRO A CD  1 
ATOM   99    N N   . LYS A 1 14  ? 48.330  8.965   7.787   1.00 33.44  ? 43  LYS A N   1 
ATOM   100   C CA  . LYS A 1 14  ? 48.125  8.715   6.382   1.00 37.17  ? 43  LYS A CA  1 
ATOM   101   C C   . LYS A 1 14  ? 46.691  9.066   6.001   1.00 40.04  ? 43  LYS A C   1 
ATOM   102   O O   . LYS A 1 14  ? 46.480  9.718   4.987   1.00 49.50  ? 43  LYS A O   1 
ATOM   103   C CB  . LYS A 1 14  ? 48.495  7.244   6.152   1.00 47.16  ? 43  LYS A CB  1 
ATOM   104   C CG  . LYS A 1 14  ? 49.960  6.885   6.491   1.00 58.21  ? 43  LYS A CG  1 
ATOM   105   C CD  . LYS A 1 14  ? 50.228  5.400   6.753   1.00 66.28  ? 43  LYS A CD  1 
ATOM   106   C CE  . LYS A 1 14  ? 49.745  4.465   5.685   1.00 74.40  ? 43  LYS A CE  1 
ATOM   107   N NZ  . LYS A 1 14  ? 50.252  4.833   4.360   1.00 85.50  ? 43  LYS A NZ  1 
ATOM   108   N N   . GLU A 1 15  ? 45.715  8.675   6.829   1.00 35.69  ? 44  GLU A N   1 
ATOM   109   C CA  . GLU A 1 15  ? 44.313  8.939   6.550   1.00 38.12  ? 44  GLU A CA  1 
ATOM   110   C C   . GLU A 1 15  ? 43.991  10.408  6.767   1.00 34.54  ? 44  GLU A C   1 
ATOM   111   O O   . GLU A 1 15  ? 43.128  10.943  6.089   1.00 35.40  ? 44  GLU A O   1 
ATOM   112   C CB  . GLU A 1 15  ? 43.324  8.125   7.396   1.00 41.08  ? 44  GLU A CB  1 
ATOM   113   C CG  . GLU A 1 15  ? 43.026  6.746   6.815   1.00 51.44  ? 44  GLU A CG  1 
ATOM   114   C CD  . GLU A 1 15  ? 42.506  6.806   5.385   1.00 59.37  ? 44  GLU A CD  1 
ATOM   115   O OE1 . GLU A 1 15  ? 41.470  7.481   5.119   1.00 56.31  ? 44  GLU A OE1 1 
ATOM   116   O OE2 . GLU A 1 15  ? 43.183  6.183   4.534   1.00 62.33  ? 44  GLU A OE2 1 
ATOM   117   N N   . GLN A 1 16  ? 44.664  11.040  7.723   1.00 30.81  ? 45  GLN A N   1 
ATOM   118   C CA  . GLN A 1 16  ? 44.455  12.448  7.969   1.00 31.56  ? 45  GLN A CA  1 
ATOM   119   C C   . GLN A 1 16  ? 44.952  13.299  6.802   1.00 35.02  ? 45  GLN A C   1 
ATOM   120   O O   . GLN A 1 16  ? 44.302  14.297  6.476   1.00 30.67  ? 45  GLN A O   1 
ATOM   121   C CB  . GLN A 1 16  ? 45.229  12.976  9.171   1.00 33.31  ? 45  GLN A CB  1 
ATOM   122   C CG  . GLN A 1 16  ? 44.816  12.378  10.511  1.00 33.75  ? 45  GLN A CG  1 
ATOM   123   C CD  . GLN A 1 16  ? 45.659  12.915  11.643  1.00 34.63  ? 45  GLN A CD  1 
ATOM   124   O OE1 . GLN A 1 16  ? 46.885  12.994  11.532  1.00 32.02  ? 45  GLN A OE1 1 
ATOM   125   N NE2 . GLN A 1 16  ? 45.028  13.292  12.742  1.00 39.63  ? 45  GLN A NE2 1 
ATOM   126   N N   . ALA A 1 17  ? 46.151  12.980  6.283   1.00 33.42  ? 46  ALA A N   1 
ATOM   127   C CA  . ALA A 1 17  ? 46.734  13.734  5.171   1.00 35.19  ? 46  ALA A CA  1 
ATOM   128   C C   . ALA A 1 17  ? 45.880  13.609  3.913   1.00 39.34  ? 46  ALA A C   1 
ATOM   129   O O   . ALA A 1 17  ? 45.599  14.605  3.256   1.00 41.47  ? 46  ALA A O   1 
ATOM   130   C CB  . ALA A 1 17  ? 48.138  13.256  4.892   1.00 35.05  ? 46  ALA A CB  1 
ATOM   131   N N   . ARG A 1 18  ? 45.478  12.366  3.616   1.00 43.76  ? 47  ARG A N   1 
ATOM   132   C CA  . ARG A 1 18  ? 44.626  11.985  2.496   1.00 45.86  ? 47  ARG A CA  1 
ATOM   133   C C   . ARG A 1 18  ? 43.262  12.683  2.520   1.00 44.27  ? 47  ARG A C   1 
ATOM   134   O O   . ARG A 1 18  ? 42.746  13.064  1.477   1.00 43.89  ? 47  ARG A O   1 
ATOM   135   C CB  . ARG A 1 18  ? 44.524  10.453  2.539   1.00 48.07  ? 47  ARG A CB  1 
ATOM   136   C CG  . ARG A 1 18  ? 43.365  9.838   1.777   1.00 57.67  ? 47  ARG A CG  1 
ATOM   137   C CD  . ARG A 1 18  ? 43.581  8.364   1.443   1.00 64.75  ? 47  ARG A CD  1 
ATOM   138   N NE  . ARG A 1 18  ? 42.336  7.870   0.849   1.00 72.04  ? 47  ARG A NE  1 
ATOM   139   C CZ  . ARG A 1 18  ? 41.762  6.694   1.059   1.00 80.62  ? 47  ARG A CZ  1 
ATOM   140   N NH1 . ARG A 1 18  ? 42.472  5.672   1.497   1.00 83.45  ? 47  ARG A NH1 1 
ATOM   141   N NH2 . ARG A 1 18  ? 40.486  6.520   0.757   1.00 81.55  ? 47  ARG A NH2 1 
ATOM   142   N N   . ILE A 1 19  ? 42.680  12.875  3.706   1.00 43.48  ? 48  ILE A N   1 
ATOM   143   C CA  . ILE A 1 19  ? 41.449  13.631  3.839   1.00 41.55  ? 48  ILE A CA  1 
ATOM   144   C C   . ILE A 1 19  ? 41.702  15.128  3.712   1.00 41.69  ? 48  ILE A C   1 
ATOM   145   O O   . ILE A 1 19  ? 40.833  15.834  3.214   1.00 42.27  ? 48  ILE A O   1 
ATOM   146   C CB  . ILE A 1 19  ? 40.760  13.326  5.174   1.00 37.32  ? 48  ILE A CB  1 
ATOM   147   C CG1 . ILE A 1 19  ? 40.224  11.913  5.191   1.00 40.41  ? 48  ILE A CG1 1 
ATOM   148   C CG2 . ILE A 1 19  ? 39.677  14.360  5.490   1.00 36.90  ? 48  ILE A CG2 1 
ATOM   149   C CD1 . ILE A 1 19  ? 39.824  11.440  6.565   1.00 40.47  ? 48  ILE A CD1 1 
ATOM   150   N N   . LYS A 1 20  ? 42.810  15.629  4.287   1.00 44.52  ? 49  LYS A N   1 
ATOM   151   C CA  . LYS A 1 20  ? 43.111  17.058  4.262   1.00 47.36  ? 49  LYS A CA  1 
ATOM   152   C C   . LYS A 1 20  ? 43.185  17.545  2.815   1.00 44.89  ? 49  LYS A C   1 
ATOM   153   O O   . LYS A 1 20  ? 42.687  18.622  2.487   1.00 40.41  ? 49  LYS A O   1 
ATOM   154   C CB  . LYS A 1 20  ? 44.434  17.291  5.002   1.00 51.59  ? 49  LYS A CB  1 
ATOM   155   C CG  . LYS A 1 20  ? 45.023  18.685  4.999   1.00 54.14  ? 49  LYS A CG  1 
ATOM   156   C CD  . LYS A 1 20  ? 46.441  18.679  5.563   1.00 59.08  ? 49  LYS A CD  1 
ATOM   157   C CE  . LYS A 1 20  ? 47.083  20.031  5.659   1.00 64.59  ? 49  LYS A CE  1 
ATOM   158   N NZ  . LYS A 1 20  ? 46.541  20.827  6.764   1.00 68.60  ? 49  LYS A NZ  1 
ATOM   159   N N   . THR A 1 21  ? 43.824  16.718  1.980   1.00 46.55  ? 50  THR A N   1 
ATOM   160   C CA  . THR A 1 21  ? 44.043  16.950  0.557   1.00 50.26  ? 50  THR A CA  1 
ATOM   161   C C   . THR A 1 21  ? 42.695  16.911  -0.165  1.00 54.92  ? 50  THR A C   1 
ATOM   162   O O   . THR A 1 21  ? 42.334  17.846  -0.889  1.00 53.34  ? 50  THR A O   1 
ATOM   163   C CB  . THR A 1 21  ? 45.031  15.876  0.070   1.00 46.13  ? 50  THR A CB  1 
ATOM   164   O OG1 . THR A 1 21  ? 46.261  16.281  0.670   1.00 43.16  ? 50  THR A OG1 1 
ATOM   165   C CG2 . THR A 1 21  ? 45.209  15.803  -1.440  1.00 51.55  ? 50  THR A CG2 1 
ATOM   166   N N   . PHE A 1 22  ? 41.940  15.831  0.083   1.00 50.49  ? 51  PHE A N   1 
ATOM   167   C CA  . PHE A 1 22  ? 40.622  15.639  -0.502  1.00 44.62  ? 51  PHE A CA  1 
ATOM   168   C C   . PHE A 1 22  ? 39.719  16.851  -0.254  1.00 38.95  ? 51  PHE A C   1 
ATOM   169   O O   . PHE A 1 22  ? 39.077  17.314  -1.179  1.00 41.98  ? 51  PHE A O   1 
ATOM   170   C CB  . PHE A 1 22  ? 40.010  14.343  0.040   1.00 47.34  ? 51  PHE A CB  1 
ATOM   171   C CG  . PHE A 1 22  ? 38.629  14.040  -0.522  1.00 48.70  ? 51  PHE A CG  1 
ATOM   172   C CD1 . PHE A 1 22  ? 38.476  13.670  -1.857  1.00 53.39  ? 51  PHE A CD1 1 
ATOM   173   C CD2 . PHE A 1 22  ? 37.495  14.118  0.276   1.00 47.12  ? 51  PHE A CD2 1 
ATOM   174   C CE1 . PHE A 1 22  ? 37.221  13.399  -2.376  1.00 54.00  ? 51  PHE A CE1 1 
ATOM   175   C CE2 . PHE A 1 22  ? 36.248  13.834  -0.247  1.00 47.02  ? 51  PHE A CE2 1 
ATOM   176   C CZ  . PHE A 1 22  ? 36.108  13.499  -1.575  1.00 44.29  ? 51  PHE A CZ  1 
ATOM   177   N N   . ARG A 1 23  ? 39.650  17.351  0.977   1.00 38.09  ? 52  ARG A N   1 
ATOM   178   C CA  . ARG A 1 23  ? 38.805  18.486  1.316   1.00 41.41  ? 52  ARG A CA  1 
ATOM   179   C C   . ARG A 1 23  ? 39.341  19.815  0.777   1.00 53.31  ? 52  ARG A C   1 
ATOM   180   O O   . ARG A 1 23  ? 38.553  20.767  0.662   1.00 47.87  ? 52  ARG A O   1 
ATOM   181   C CB  . ARG A 1 23  ? 38.646  18.656  2.828   1.00 40.11  ? 52  ARG A CB  1 
ATOM   182   C CG  . ARG A 1 23  ? 37.926  17.477  3.471   1.00 41.20  ? 52  ARG A CG  1 
ATOM   183   C CD  . ARG A 1 23  ? 37.821  17.646  4.960   1.00 40.84  ? 52  ARG A CD  1 
ATOM   184   N NE  . ARG A 1 23  ? 36.972  18.790  5.286   1.00 42.37  ? 52  ARG A NE  1 
ATOM   185   C CZ  . ARG A 1 23  ? 36.770  19.260  6.518   1.00 48.13  ? 52  ARG A CZ  1 
ATOM   186   N NH1 . ARG A 1 23  ? 37.311  18.658  7.566   1.00 47.31  ? 52  ARG A NH1 1 
ATOM   187   N NH2 . ARG A 1 23  ? 35.980  20.309  6.702   1.00 45.26  ? 52  ARG A NH2 1 
ATOM   188   N N   . GLN A 1 24  ? 40.661  19.898  0.507   1.00 49.24  ? 53  GLN A N   1 
ATOM   189   C CA  . GLN A 1 24  ? 41.264  21.062  -0.146  1.00 51.44  ? 53  GLN A CA  1 
ATOM   190   C C   . GLN A 1 24  ? 40.698  21.258  -1.553  1.00 42.57  ? 53  GLN A C   1 
ATOM   191   O O   . GLN A 1 24  ? 40.135  22.297  -1.853  1.00 48.91  ? 53  GLN A O   1 
ATOM   192   C CB  . GLN A 1 24  ? 42.783  20.935  -0.262  1.00 49.01  ? 53  GLN A CB  1 
ATOM   193   C CG  . GLN A 1 24  ? 43.512  21.378  1.000   1.00 56.67  ? 53  GLN A CG  1 
ATOM   194   C CD  . GLN A 1 24  ? 45.016  21.227  0.905   1.00 60.04  ? 53  GLN A CD  1 
ATOM   195   O OE1 . GLN A 1 24  ? 45.564  20.602  -0.018  1.00 57.98  ? 53  GLN A OE1 1 
ATOM   196   N NE2 . GLN A 1 24  ? 45.692  21.811  1.882   1.00 62.74  ? 53  GLN A NE2 1 
ATOM   197   N N   . GLN A 1 25  ? 40.896  20.249  -2.391  1.00 41.23  ? 54  GLN A N   1 
ATOM   198   C CA  . GLN A 1 25  ? 40.396  20.166  -3.750  1.00 55.94  ? 54  GLN A CA  1 
ATOM   199   C C   . GLN A 1 25  ? 38.873  20.127  -3.819  1.00 62.15  ? 54  GLN A C   1 
ATOM   200   O O   . GLN A 1 25  ? 38.254  20.992  -4.440  1.00 61.32  ? 54  GLN A O   1 
ATOM   201   C CB  . GLN A 1 25  ? 40.987  18.863  -4.287  1.00 67.18  ? 54  GLN A CB  1 
ATOM   202   C CG  . GLN A 1 25  ? 40.504  18.452  -5.673  1.00 81.34  ? 54  GLN A CG  1 
ATOM   203   C CD  . GLN A 1 25  ? 41.181  17.194  -6.176  1.00 89.20  ? 54  GLN A CD  1 
ATOM   204   O OE1 . GLN A 1 25  ? 42.054  16.618  -5.513  1.00 98.37  ? 54  GLN A OE1 1 
ATOM   205   N NE2 . GLN A 1 25  ? 40.794  16.766  -7.370  1.00 91.12  ? 54  GLN A NE2 1 
ATOM   206   N N   . HIS A 1 26  ? 38.278  19.102  -3.198  1.00 53.17  ? 55  HIS A N   1 
ATOM   207   C CA  . HIS A 1 26  ? 36.926  18.692  -3.533  1.00 54.54  ? 55  HIS A CA  1 
ATOM   208   C C   . HIS A 1 26  ? 35.949  19.082  -2.430  1.00 49.49  ? 55  HIS A C   1 
ATOM   209   O O   . HIS A 1 26  ? 34.801  18.669  -2.460  1.00 53.23  ? 55  HIS A O   1 
ATOM   210   C CB  . HIS A 1 26  ? 36.897  17.192  -3.850  1.00 63.85  ? 55  HIS A CB  1 
ATOM   211   C CG  . HIS A 1 26  ? 37.244  16.825  -5.256  1.00 80.16  ? 55  HIS A CG  1 
ATOM   212   N ND1 . HIS A 1 26  ? 37.998  15.710  -5.557  1.00 89.61  ? 55  HIS A ND1 1 
ATOM   213   C CD2 . HIS A 1 26  ? 36.933  17.391  -6.434  1.00 93.91  ? 55  HIS A CD2 1 
ATOM   214   C CE1 . HIS A 1 26  ? 38.135  15.612  -6.870  1.00 94.86  ? 55  HIS A CE1 1 
ATOM   215   N NE2 . HIS A 1 26  ? 37.502  16.628  -7.423  1.00 99.15  ? 55  HIS A NE2 1 
ATOM   216   N N   . GLY A 1 27  ? 36.382  19.938  -1.503  1.00 48.59  ? 56  GLY A N   1 
ATOM   217   C CA  . GLY A 1 27  ? 35.588  20.269  -0.336  1.00 47.32  ? 56  GLY A CA  1 
ATOM   218   C C   . GLY A 1 27  ? 34.246  20.894  -0.695  1.00 51.11  ? 56  GLY A C   1 
ATOM   219   O O   . GLY A 1 27  ? 33.283  20.791  0.073   1.00 48.57  ? 56  GLY A O   1 
ATOM   220   N N   . LYS A 1 28  ? 34.206  21.555  -1.855  1.00 48.48  ? 57  LYS A N   1 
ATOM   221   C CA  . LYS A 1 28  ? 33.059  22.359  -2.249  1.00 49.90  ? 57  LYS A CA  1 
ATOM   222   C C   . LYS A 1 28  ? 32.191  21.615  -3.260  1.00 41.67  ? 57  LYS A C   1 
ATOM   223   O O   . LYS A 1 28  ? 31.151  22.137  -3.644  1.00 47.34  ? 57  LYS A O   1 
ATOM   224   C CB  . LYS A 1 28  ? 33.536  23.730  -2.760  1.00 63.93  ? 57  LYS A CB  1 
ATOM   225   C CG  . LYS A 1 28  ? 33.519  24.849  -1.714  1.00 70.53  ? 57  LYS A CG  1 
ATOM   226   C CD  . LYS A 1 28  ? 34.317  24.561  -0.448  1.00 80.65  ? 57  LYS A CD  1 
ATOM   227   C CE  . LYS A 1 28  ? 33.893  25.414  0.704   1.00 86.62  ? 57  LYS A CE  1 
ATOM   228   N NZ  . LYS A 1 28  ? 34.121  26.836  0.441   1.00 92.30  ? 57  LYS A NZ  1 
ATOM   229   N N   . THR A 1 29  ? 32.640  20.441  -3.726  1.00 41.50  ? 58  THR A N   1 
ATOM   230   C CA  . THR A 1 29  ? 31.831  19.580  -4.571  1.00 42.04  ? 58  THR A CA  1 
ATOM   231   C C   . THR A 1 29  ? 30.514  19.252  -3.867  1.00 49.93  ? 58  THR A C   1 
ATOM   232   O O   . THR A 1 29  ? 30.486  18.790  -2.713  1.00 41.76  ? 58  THR A O   1 
ATOM   233   C CB  . THR A 1 29  ? 32.588  18.300  -4.899  1.00 48.47  ? 58  THR A CB  1 
ATOM   234   O OG1 . THR A 1 29  ? 33.841  18.692  -5.461  1.00 54.15  ? 58  THR A OG1 1 
ATOM   235   C CG2 . THR A 1 29  ? 31.819  17.408  -5.854  1.00 50.29  ? 58  THR A CG2 1 
ATOM   236   N N   . VAL A 1 30  ? 29.415  19.489  -4.593  1.00 48.84  ? 59  VAL A N   1 
ATOM   237   C CA  . VAL A 1 30  ? 28.090  19.205  -4.086  1.00 46.81  ? 59  VAL A CA  1 
ATOM   238   C C   . VAL A 1 30  ? 27.864  17.715  -4.274  1.00 44.59  ? 59  VAL A C   1 
ATOM   239   O O   . VAL A 1 30  ? 28.109  17.195  -5.362  1.00 42.36  ? 59  VAL A O   1 
ATOM   240   C CB  . VAL A 1 30  ? 27.021  20.050  -4.809  1.00 47.02  ? 59  VAL A CB  1 
ATOM   241   C CG1 . VAL A 1 30  ? 25.605  19.695  -4.368  1.00 43.83  ? 59  VAL A CG1 1 
ATOM   242   C CG2 . VAL A 1 30  ? 27.263  21.528  -4.598  1.00 45.77  ? 59  VAL A CG2 1 
ATOM   243   N N   . VAL A 1 31  ? 27.420  17.023  -3.214  1.00 40.48  ? 60  VAL A N   1 
ATOM   244   C CA  . VAL A 1 31  ? 27.150  15.598  -3.344  1.00 39.17  ? 60  VAL A CA  1 
ATOM   245   C C   . VAL A 1 31  ? 25.637  15.371  -3.433  1.00 37.07  ? 60  VAL A C   1 
ATOM   246   O O   . VAL A 1 31  ? 25.198  14.324  -3.879  1.00 39.77  ? 60  VAL A O   1 
ATOM   247   C CB  . VAL A 1 31  ? 27.792  14.815  -2.187  1.00 41.57  ? 60  VAL A CB  1 
ATOM   248   C CG1 . VAL A 1 31  ? 29.306  14.929  -2.199  1.00 45.11  ? 60  VAL A CG1 1 
ATOM   249   C CG2 . VAL A 1 31  ? 27.246  15.276  -0.845  1.00 44.54  ? 60  VAL A CG2 1 
ATOM   250   N N   . GLY A 1 32  ? 24.837  16.347  -3.000  1.00 36.25  ? 61  GLY A N   1 
ATOM   251   C CA  . GLY A 1 32  ? 23.400  16.159  -2.875  1.00 39.80  ? 61  GLY A CA  1 
ATOM   252   C C   . GLY A 1 32  ? 22.702  17.477  -2.559  1.00 39.75  ? 61  GLY A C   1 
ATOM   253   O O   . GLY A 1 32  ? 23.376  18.451  -2.259  1.00 37.33  ? 61  GLY A O   1 
ATOM   254   N N   . GLN A 1 33  ? 21.362  17.469  -2.647  1.00 35.33  ? 62  GLN A N   1 
ATOM   255   C CA  . GLN A 1 33  ? 20.511  18.601  -2.352  1.00 40.68  ? 62  GLN A CA  1 
ATOM   256   C C   . GLN A 1 33  ? 19.641  18.251  -1.142  1.00 36.22  ? 62  GLN A C   1 
ATOM   257   O O   . GLN A 1 33  ? 19.350  17.098  -0.927  1.00 38.69  ? 62  GLN A O   1 
ATOM   258   C CB  . GLN A 1 33  ? 19.505  18.850  -3.475  1.00 43.55  ? 62  GLN A CB  1 
ATOM   259   C CG  . GLN A 1 33  ? 20.079  18.864  -4.890  1.00 52.76  ? 62  GLN A CG  1 
ATOM   260   C CD  . GLN A 1 33  ? 20.944  20.069  -5.179  1.00 58.19  ? 62  GLN A CD  1 
ATOM   261   O OE1 . GLN A 1 33  ? 20.547  21.221  -4.962  1.00 65.69  ? 62  GLN A OE1 1 
ATOM   262   N NE2 . GLN A 1 33  ? 22.154  19.812  -5.654  1.00 63.44  ? 62  GLN A NE2 1 
ATOM   263   N N   . ILE A 1 34  ? 19.205  19.249  -0.380  1.00 34.50  ? 63  ILE A N   1 
ATOM   264   C CA  . ILE A 1 34  ? 18.212  19.042  0.658   1.00 36.08  ? 63  ILE A CA  1 
ATOM   265   C C   . ILE A 1 34  ? 16.875  19.629  0.190   1.00 34.46  ? 63  ILE A C   1 
ATOM   266   O O   . ILE A 1 34  ? 16.823  20.751  -0.315  1.00 35.24  ? 63  ILE A O   1 
ATOM   267   C CB  . ILE A 1 34  ? 18.703  19.674  1.966   1.00 33.74  ? 63  ILE A CB  1 
ATOM   268   C CG1 . ILE A 1 34  ? 20.061  19.165  2.352   1.00 34.16  ? 63  ILE A CG1 1 
ATOM   269   C CG2 . ILE A 1 34  ? 17.691  19.473  3.084   1.00 34.65  ? 63  ILE A CG2 1 
ATOM   270   C CD1 . ILE A 1 34  ? 20.863  20.199  3.134   1.00 40.95  ? 63  ILE A CD1 1 
ATOM   271   N N   . THR A 1 35  ? 15.814  18.833  0.329   1.00 33.62  ? 64  THR A N   1 
ATOM   272   C CA  . THR A 1 35  ? 14.461  19.215  -0.026  1.00 33.56  ? 64  THR A CA  1 
ATOM   273   C C   . THR A 1 35  ? 13.638  19.306  1.248   1.00 34.19  ? 64  THR A C   1 
ATOM   274   O O   . THR A 1 35  ? 13.986  18.734  2.267   1.00 32.49  ? 64  THR A O   1 
ATOM   275   C CB  . THR A 1 35  ? 13.795  18.235  -0.989  1.00 31.21  ? 64  THR A CB  1 
ATOM   276   O OG1 . THR A 1 35  ? 13.708  17.004  -0.297  1.00 28.34  ? 64  THR A OG1 1 
ATOM   277   C CG2 . THR A 1 35  ? 14.536  17.966  -2.293  1.00 31.91  ? 64  THR A CG2 1 
ATOM   278   N N   . VAL A 1 36  ? 12.530  20.030  1.169   1.00 33.41  ? 65  VAL A N   1 
ATOM   279   C CA  . VAL A 1 36  ? 11.642  20.142  2.312   1.00 37.12  ? 65  VAL A CA  1 
ATOM   280   C C   . VAL A 1 36  ? 11.231  18.747  2.806   1.00 33.49  ? 65  VAL A C   1 
ATOM   281   O O   . VAL A 1 36  ? 11.224  18.477  4.007   1.00 29.23  ? 65  VAL A O   1 
ATOM   282   C CB  . VAL A 1 36  ? 10.446  21.002  1.872   1.00 31.25  ? 65  VAL A CB  1 
ATOM   283   C CG1 . VAL A 1 36  ? 9.298   20.885  2.861   1.00 32.66  ? 65  VAL A CG1 1 
ATOM   284   C CG2 . VAL A 1 36  ? 10.881  22.443  1.693   1.00 34.61  ? 65  VAL A CG2 1 
ATOM   285   N N   . ASP A 1 37  ? 10.897  17.853  1.868   1.00 33.30  ? 66  ASP A N   1 
ATOM   286   C CA  . ASP A 1 37  ? 10.430  16.521  2.212   1.00 34.67  ? 66  ASP A CA  1 
ATOM   287   C C   . ASP A 1 37  ? 11.489  15.766  3.001   1.00 36.05  ? 66  ASP A C   1 
ATOM   288   O O   . ASP A 1 37  ? 11.141  14.941  3.827   1.00 33.59  ? 66  ASP A O   1 
ATOM   289   C CB  . ASP A 1 37  ? 9.932   15.747  0.997   1.00 39.57  ? 66  ASP A CB  1 
ATOM   290   C CG  . ASP A 1 37  ? 8.429   15.883  0.734   1.00 46.75  ? 66  ASP A CG  1 
ATOM   291   O OD1 . ASP A 1 37  ? 7.671   16.181  1.691   1.00 52.76  ? 66  ASP A OD1 1 
ATOM   292   O OD2 . ASP A 1 37  ? 8.015   15.707  -0.418  1.00 51.70  ? 66  ASP A OD2 1 
ATOM   293   N N   . MET A 1 38  ? 12.775  16.021  2.736   1.00 35.72  ? 67  MET A N   1 
ATOM   294   C CA  . MET A 1 38  ? 13.809  15.304  3.442   1.00 36.26  ? 67  MET A CA  1 
ATOM   295   C C   . MET A 1 38  ? 13.838  15.769  4.883   1.00 32.34  ? 67  MET A C   1 
ATOM   296   O O   . MET A 1 38  ? 14.163  14.957  5.730   1.00 32.38  ? 67  MET A O   1 
ATOM   297   C CB  . MET A 1 38  ? 15.210  15.550  2.885   1.00 41.11  ? 67  MET A CB  1 
ATOM   298   C CG  . MET A 1 38  ? 15.482  14.890  1.567   1.00 47.29  ? 67  MET A CG  1 
ATOM   299   S SD  . MET A 1 38  ? 17.090  15.422  0.924   1.00 52.09  ? 67  MET A SD  1 
ATOM   300   C CE  . MET A 1 38  ? 16.864  14.703  -0.712  1.00 50.03  ? 67  MET A CE  1 
ATOM   301   N N   . MET A 1 39  ? 13.586  17.071  5.119   1.00 28.38  ? 68  MET A N   1 
ATOM   302   C CA  . MET A 1 39  ? 13.592  17.609  6.465   1.00 30.36  ? 68  MET A CA  1 
ATOM   303   C C   . MET A 1 39  ? 12.465  16.995  7.313   1.00 31.25  ? 68  MET A C   1 
ATOM   304   O O   . MET A 1 39  ? 12.685  16.752  8.506   1.00 31.91  ? 68  MET A O   1 
ATOM   305   C CB  . MET A 1 39  ? 13.500  19.137  6.458   1.00 33.39  ? 68  MET A CB  1 
ATOM   306   C CG  . MET A 1 39  ? 14.723  19.777  5.821   1.00 39.50  ? 68  MET A CG  1 
ATOM   307   S SD  . MET A 1 39  ? 14.637  21.568  5.771   1.00 42.76  ? 68  MET A SD  1 
ATOM   308   C CE  . MET A 1 39  ? 14.839  21.883  7.534   1.00 46.15  ? 68  MET A CE  1 
ATOM   309   N N   . TYR A 1 40  ? 11.273  16.837  6.705   1.00 31.69  ? 69  TYR A N   1 
ATOM   310   C CA  . TYR A 1 40  ? 10.119  16.236  7.349   1.00 32.27  ? 69  TYR A CA  1 
ATOM   311   C C   . TYR A 1 40  ? 10.224  14.715  7.260   1.00 36.32  ? 69  TYR A C   1 
ATOM   312   O O   . TYR A 1 40  ? 9.571   14.042  8.045   1.00 40.39  ? 69  TYR A O   1 
ATOM   313   C CB  . TYR A 1 40  ? 8.738   16.610  6.792   1.00 31.58  ? 69  TYR A CB  1 
ATOM   314   C CG  . TYR A 1 40  ? 8.302   18.042  7.048   1.00 29.77  ? 69  TYR A CG  1 
ATOM   315   C CD1 . TYR A 1 40  ? 7.763   18.419  8.278   1.00 29.93  ? 69  TYR A CD1 1 
ATOM   316   C CD2 . TYR A 1 40  ? 8.515   19.027  6.091   1.00 26.53  ? 69  TYR A CD2 1 
ATOM   317   C CE1 . TYR A 1 40  ? 7.438   19.734  8.551   1.00 26.71  ? 69  TYR A CE1 1 
ATOM   318   C CE2 . TYR A 1 40  ? 8.209   20.342  6.359   1.00 28.62  ? 69  TYR A CE2 1 
ATOM   319   C CZ  . TYR A 1 40  ? 7.634   20.686  7.573   1.00 28.71  ? 69  TYR A CZ  1 
ATOM   320   O OH  . TYR A 1 40  ? 7.270   21.970  7.803   1.00 26.92  ? 69  TYR A OH  1 
ATOM   321   N N   . GLY A 1 41  ? 11.024  14.183  6.320   1.00 33.06  ? 70  GLY A N   1 
ATOM   322   C CA  . GLY A 1 41  ? 11.176  12.746  6.121   1.00 30.97  ? 70  GLY A CA  1 
ATOM   323   C C   . GLY A 1 41  ? 12.372  12.134  6.859   1.00 31.61  ? 70  GLY A C   1 
ATOM   324   O O   . GLY A 1 41  ? 12.892  11.098  6.454   1.00 31.35  ? 70  GLY A O   1 
ATOM   325   N N   . GLY A 1 42  ? 12.808  12.731  7.973   1.00 28.89  ? 71  GLY A N   1 
ATOM   326   C CA  . GLY A 1 42  ? 13.903  12.146  8.718   1.00 31.20  ? 71  GLY A CA  1 
ATOM   327   C C   . GLY A 1 42  ? 15.191  11.993  7.902   1.00 30.33  ? 71  GLY A C   1 
ATOM   328   O O   . GLY A 1 42  ? 15.907  11.004  8.060   1.00 30.69  ? 71  GLY A O   1 
ATOM   329   N N   . MET A 1 43  ? 15.524  12.994  7.078   1.00 32.63  ? 72  MET A N   1 
ATOM   330   C CA  . MET A 1 43  ? 16.803  13.039  6.377   1.00 29.93  ? 72  MET A CA  1 
ATOM   331   C C   . MET A 1 43  ? 16.981  11.883  5.405   1.00 30.23  ? 72  MET A C   1 
ATOM   332   O O   . MET A 1 43  ? 18.126  11.601  5.015   1.00 27.00  ? 72  MET A O   1 
ATOM   333   C CB  . MET A 1 43  ? 18.012  12.938  7.310   1.00 35.11  ? 72  MET A CB  1 
ATOM   334   C CG  . MET A 1 43  ? 18.067  14.011  8.380   1.00 36.01  ? 72  MET A CG  1 
ATOM   335   S SD  . MET A 1 43  ? 19.615  13.863  9.288   1.00 40.72  ? 72  MET A SD  1 
ATOM   336   C CE  . MET A 1 43  ? 19.541  15.077  10.615  1.00 46.89  ? 72  MET A CE  1 
ATOM   337   N N   . ARG A 1 44  ? 15.872  11.305  4.938   1.00 29.98  ? 73  ARG A N   1 
ATOM   338   C CA  . ARG A 1 44  ? 15.931  10.117  4.096   1.00 35.67  ? 73  ARG A CA  1 
ATOM   339   C C   . ARG A 1 44  ? 16.612  10.493  2.793   1.00 37.22  ? 73  ARG A C   1 
ATOM   340   O O   . ARG A 1 44  ? 16.167  11.425  2.125   1.00 31.84  ? 73  ARG A O   1 
ATOM   341   C CB  . ARG A 1 44  ? 14.563  9.551   3.698   1.00 43.32  ? 73  ARG A CB  1 
ATOM   342   C CG  . ARG A 1 44  ? 14.220  8.146   4.165   1.00 57.78  ? 73  ARG A CG  1 
ATOM   343   C CD  . ARG A 1 44  ? 12.701  7.952   4.307   1.00 71.62  ? 73  ARG A CD  1 
ATOM   344   N NE  . ARG A 1 44  ? 11.917  8.879   3.472   1.00 81.64  ? 73  ARG A NE  1 
ATOM   345   C CZ  . ARG A 1 44  ? 10.929  9.693   3.892   1.00 81.08  ? 73  ARG A CZ  1 
ATOM   346   N NH1 . ARG A 1 44  ? 10.392  9.534   5.094   1.00 67.36  ? 73  ARG A NH1 1 
ATOM   347   N NH2 . ARG A 1 44  ? 10.441  10.631  3.085   1.00 74.83  ? 73  ARG A NH2 1 
ATOM   348   N N   . GLY A 1 45  ? 17.665  9.741   2.449   1.00 41.51  ? 74  GLY A N   1 
ATOM   349   C CA  . GLY A 1 45  ? 18.380  9.928   1.198   1.00 46.28  ? 74  GLY A CA  1 
ATOM   350   C C   . GLY A 1 45  ? 19.411  11.052  1.273   1.00 41.29  ? 74  GLY A C   1 
ATOM   351   O O   . GLY A 1 45  ? 19.973  11.453  0.263   1.00 39.18  ? 74  GLY A O   1 
ATOM   352   N N   . MET A 1 46  ? 19.630  11.599  2.463   1.00 35.02  ? 75  MET A N   1 
ATOM   353   C CA  . MET A 1 46  ? 20.414  12.807  2.594   1.00 40.12  ? 75  MET A CA  1 
ATOM   354   C C   . MET A 1 46  ? 21.814  12.368  2.997   1.00 38.35  ? 75  MET A C   1 
ATOM   355   O O   . MET A 1 46  ? 21.958  11.600  3.937   1.00 34.13  ? 75  MET A O   1 
ATOM   356   C CB  . MET A 1 46  ? 19.807  13.729  3.658   1.00 39.50  ? 75  MET A CB  1 
ATOM   357   C CG  . MET A 1 46  ? 20.524  15.042  3.833   1.00 41.98  ? 75  MET A CG  1 
ATOM   358   S SD  . MET A 1 46  ? 19.891  16.061  5.186   1.00 49.84  ? 75  MET A SD  1 
ATOM   359   C CE  . MET A 1 46  ? 18.248  16.239  4.497   1.00 48.34  ? 75  MET A CE  1 
ATOM   360   N N   . LYS A 1 47  ? 22.828  12.806  2.253   1.00 34.52  ? 76  LYS A N   1 
ATOM   361   C CA  . LYS A 1 47  ? 24.187  12.407  2.551   1.00 41.23  ? 76  LYS A CA  1 
ATOM   362   C C   . LYS A 1 47  ? 24.618  13.272  3.721   1.00 39.38  ? 76  LYS A C   1 
ATOM   363   O O   . LYS A 1 47  ? 24.832  14.463  3.558   1.00 46.98  ? 76  LYS A O   1 
ATOM   364   C CB  . LYS A 1 47  ? 25.123  12.562  1.348   1.00 49.94  ? 76  LYS A CB  1 
ATOM   365   C CG  . LYS A 1 47  ? 24.724  11.739  0.147   1.00 53.34  ? 76  LYS A CG  1 
ATOM   366   C CD  . LYS A 1 47  ? 25.866  11.096  -0.619  1.00 58.50  ? 76  LYS A CD  1 
ATOM   367   C CE  . LYS A 1 47  ? 25.463  10.652  -1.996  1.00 62.85  ? 76  LYS A CE  1 
ATOM   368   N NZ  . LYS A 1 47  ? 24.086  10.156  -2.090  1.00 66.15  ? 76  LYS A NZ  1 
ATOM   369   N N   . GLY A 1 48  ? 24.612  12.690  4.914   1.00 37.79  ? 77  GLY A N   1 
ATOM   370   C CA  . GLY A 1 48  ? 24.670  13.478  6.135   1.00 38.92  ? 77  GLY A CA  1 
ATOM   371   C C   . GLY A 1 48  ? 26.036  13.386  6.809   1.00 34.73  ? 77  GLY A C   1 
ATOM   372   O O   . GLY A 1 48  ? 26.462  14.328  7.486   1.00 41.63  ? 77  GLY A O   1 
ATOM   373   N N   . LEU A 1 49  ? 26.711  12.240  6.661   1.00 29.24  ? 78  LEU A N   1 
ATOM   374   C CA  . LEU A 1 49  ? 27.920  12.056  7.435   1.00 32.39  ? 78  LEU A CA  1 
ATOM   375   C C   . LEU A 1 49  ? 28.900  11.131  6.731   1.00 28.08  ? 78  LEU A C   1 
ATOM   376   O O   . LEU A 1 49  ? 28.587  10.435  5.754   1.00 31.29  ? 78  LEU A O   1 
ATOM   377   C CB  . LEU A 1 49  ? 27.577  11.590  8.842   1.00 40.11  ? 78  LEU A CB  1 
ATOM   378   C CG  . LEU A 1 49  ? 26.960  10.203  8.996   1.00 39.41  ? 78  LEU A CG  1 
ATOM   379   C CD1 . LEU A 1 49  ? 27.109  9.786   10.452  1.00 44.90  ? 78  LEU A CD1 1 
ATOM   380   C CD2 . LEU A 1 49  ? 25.500  10.170  8.614   1.00 46.94  ? 78  LEU A CD2 1 
ATOM   381   N N   . VAL A 1 50  ? 30.126  11.293  7.197   1.00 27.86  ? 79  VAL A N   1 
ATOM   382   C CA  . VAL A 1 50  ? 31.249  10.439  6.889   1.00 31.25  ? 79  VAL A CA  1 
ATOM   383   C C   . VAL A 1 50  ? 31.389  9.405   8.000   1.00 27.78  ? 79  VAL A C   1 
ATOM   384   O O   . VAL A 1 50  ? 31.464  9.746   9.169   1.00 29.05  ? 79  VAL A O   1 
ATOM   385   C CB  . VAL A 1 50  ? 32.510  11.310  6.731   1.00 32.83  ? 79  VAL A CB  1 
ATOM   386   C CG1 . VAL A 1 50  ? 33.778  10.450  6.605   1.00 34.56  ? 79  VAL A CG1 1 
ATOM   387   C CG2 . VAL A 1 50  ? 32.364  12.270  5.539   1.00 33.95  ? 79  VAL A CG2 1 
ATOM   388   N N   . TYR A 1 51  ? 31.356  8.149   7.592   1.00 26.55  ? 80  TYR A N   1 
ATOM   389   C CA  . TYR A 1 51  ? 31.464  7.006   8.476   1.00 29.07  ? 80  TYR A CA  1 
ATOM   390   C C   . TYR A 1 51  ? 32.314  5.979   7.718   1.00 28.80  ? 80  TYR A C   1 
ATOM   391   O O   . TYR A 1 51  ? 31.944  5.600   6.620   1.00 31.54  ? 80  TYR A O   1 
ATOM   392   C CB  . TYR A 1 51  ? 30.022  6.595   8.793   1.00 27.56  ? 80  TYR A CB  1 
ATOM   393   C CG  . TYR A 1 51  ? 29.844  5.622   9.957   1.00 26.54  ? 80  TYR A CG  1 
ATOM   394   C CD1 . TYR A 1 51  ? 29.906  4.265   9.753   1.00 27.63  ? 80  TYR A CD1 1 
ATOM   395   C CD2 . TYR A 1 51  ? 29.539  6.064   11.237  1.00 27.50  ? 80  TYR A CD2 1 
ATOM   396   C CE1 . TYR A 1 51  ? 29.752  3.362   10.798  1.00 28.79  ? 80  TYR A CE1 1 
ATOM   397   C CE2 . TYR A 1 51  ? 29.339  5.170   12.290  1.00 29.80  ? 80  TYR A CE2 1 
ATOM   398   C CZ  . TYR A 1 51  ? 29.495  3.810   12.079  1.00 28.17  ? 80  TYR A CZ  1 
ATOM   399   O OH  . TYR A 1 51  ? 29.278  2.878   13.086  1.00 33.25  ? 80  TYR A OH  1 
ATOM   400   N N   . GLU A 1 52  ? 33.482  5.639   8.272   1.00 32.64  ? 81  GLU A N   1 
ATOM   401   C CA  . GLU A 1 52  ? 34.590  5.032   7.543   1.00 33.99  ? 81  GLU A CA  1 
ATOM   402   C C   . GLU A 1 52  ? 34.537  3.509   7.560   1.00 31.81  ? 81  GLU A C   1 
ATOM   403   O O   . GLU A 1 52  ? 34.976  2.868   6.610   1.00 31.32  ? 81  GLU A O   1 
ATOM   404   C CB  . GLU A 1 52  ? 35.928  5.424   8.158   1.00 37.57  ? 81  GLU A CB  1 
ATOM   405   C CG  . GLU A 1 52  ? 36.227  6.923   8.145   1.00 42.25  ? 81  GLU A CG  1 
ATOM   406   C CD  . GLU A 1 52  ? 36.504  7.500   6.767   1.00 43.49  ? 81  GLU A CD  1 
ATOM   407   O OE1 . GLU A 1 52  ? 36.169  6.900   5.728   1.00 38.29  ? 81  GLU A OE1 1 
ATOM   408   O OE2 . GLU A 1 52  ? 37.072  8.594   6.763   1.00 48.44  ? 81  GLU A OE2 1 
ATOM   409   N N   . THR A 1 53  ? 34.001  2.931   8.637   1.00 30.41  ? 82  THR A N   1 
ATOM   410   C CA  . THR A 1 53  ? 34.101  1.496   8.873   1.00 28.77  ? 82  THR A CA  1 
ATOM   411   C C   . THR A 1 53  ? 33.255  0.686   7.901   1.00 32.20  ? 82  THR A C   1 
ATOM   412   O O   . THR A 1 53  ? 33.687  -0.364  7.455   1.00 35.21  ? 82  THR A O   1 
ATOM   413   C CB  . THR A 1 53  ? 33.751  1.199   10.325  1.00 28.85  ? 82  THR A CB  1 
ATOM   414   O OG1 . THR A 1 53  ? 32.546  1.890   10.663  1.00 27.02  ? 82  THR A OG1 1 
ATOM   415   C CG2 . THR A 1 53  ? 34.856  1.706   11.226  1.00 29.01  ? 82  THR A CG2 1 
ATOM   416   N N   . SER A 1 54  ? 32.056  1.150   7.577   1.00 32.74  ? 83  SER A N   1 
ATOM   417   C CA  . SER A 1 54  ? 31.176  0.403   6.707   1.00 32.04  ? 83  SER A CA  1 
ATOM   418   C C   . SER A 1 54  ? 30.323  1.302   5.831   1.00 32.38  ? 83  SER A C   1 
ATOM   419   O O   . SER A 1 54  ? 29.952  2.396   6.218   1.00 37.83  ? 83  SER A O   1 
ATOM   420   C CB  . SER A 1 54  ? 30.269  -0.532  7.486   1.00 32.80  ? 83  SER A CB  1 
ATOM   421   O OG  . SER A 1 54  ? 29.420  0.206   8.344   1.00 29.00  ? 83  SER A OG  1 
ATOM   422   N N   . VAL A 1 55  ? 29.906  0.727   4.702   1.00 34.66  ? 84  VAL A N   1 
ATOM   423   C CA  . VAL A 1 55  ? 29.144  1.416   3.684   1.00 37.07  ? 84  VAL A CA  1 
ATOM   424   C C   . VAL A 1 55  ? 28.101  0.450   3.143   1.00 35.40  ? 84  VAL A C   1 
ATOM   425   O O   . VAL A 1 55  ? 28.405  -0.705  2.854   1.00 37.36  ? 84  VAL A O   1 
ATOM   426   C CB  . VAL A 1 55  ? 30.026  1.972   2.543   1.00 41.87  ? 84  VAL A CB  1 
ATOM   427   C CG1 . VAL A 1 55  ? 29.232  2.926   1.665   1.00 37.43  ? 84  VAL A CG1 1 
ATOM   428   C CG2 . VAL A 1 55  ? 31.266  2.677   3.071   1.00 39.57  ? 84  VAL A CG2 1 
ATOM   429   N N   . LEU A 1 56  ? 26.861  0.944   3.057   1.00 38.38  ? 85  LEU A N   1 
ATOM   430   C CA  . LEU A 1 56  ? 25.706  0.151   2.672   1.00 44.98  ? 85  LEU A CA  1 
ATOM   431   C C   . LEU A 1 56  ? 25.373  0.476   1.223   1.00 48.60  ? 85  LEU A C   1 
ATOM   432   O O   . LEU A 1 56  ? 24.979  1.593   0.898   1.00 49.43  ? 85  LEU A O   1 
ATOM   433   C CB  . LEU A 1 56  ? 24.536  0.451   3.613   1.00 46.37  ? 85  LEU A CB  1 
ATOM   434   C CG  . LEU A 1 56  ? 23.188  -0.190  3.268   1.00 49.44  ? 85  LEU A CG  1 
ATOM   435   C CD1 . LEU A 1 56  ? 23.260  -1.697  3.070   1.00 45.43  ? 85  LEU A CD1 1 
ATOM   436   C CD2 . LEU A 1 56  ? 22.205  0.163   4.388   1.00 52.61  ? 85  LEU A CD2 1 
ATOM   437   N N   . ASP A 1 57  ? 25.648  -0.490  0.353   1.00 53.88  ? 86  ASP A N   1 
ATOM   438   C CA  . ASP A 1 57  ? 25.129  -0.483  -0.993  1.00 58.70  ? 86  ASP A CA  1 
ATOM   439   C C   . ASP A 1 57  ? 23.644  -0.840  -0.939  1.00 54.80  ? 86  ASP A C   1 
ATOM   440   O O   . ASP A 1 57  ? 23.286  -1.902  -0.440  1.00 51.18  ? 86  ASP A O   1 
ATOM   441   C CB  . ASP A 1 57  ? 25.862  -1.476  -1.882  1.00 63.44  ? 86  ASP A CB  1 
ATOM   442   C CG  . ASP A 1 57  ? 25.632  -1.229  -3.366  1.00 68.22  ? 86  ASP A CG  1 
ATOM   443   O OD1 . ASP A 1 57  ? 26.296  -0.315  -3.893  1.00 73.59  ? 86  ASP A OD1 1 
ATOM   444   O OD2 . ASP A 1 57  ? 24.741  -1.894  -3.959  1.00 66.69  ? 86  ASP A OD2 1 
ATOM   445   N N   . PRO A 1 58  ? 22.726  0.023   -1.423  1.00 48.30  ? 87  PRO A N   1 
ATOM   446   C CA  . PRO A 1 58  ? 21.308  -0.347  -1.493  1.00 51.38  ? 87  PRO A CA  1 
ATOM   447   C C   . PRO A 1 58  ? 21.048  -1.662  -2.241  1.00 54.81  ? 87  PRO A C   1 
ATOM   448   O O   . PRO A 1 58  ? 20.199  -2.456  -1.818  1.00 53.74  ? 87  PRO A O   1 
ATOM   449   C CB  . PRO A 1 58  ? 20.596  0.873   -2.129  1.00 51.24  ? 87  PRO A CB  1 
ATOM   450   C CG  . PRO A 1 58  ? 21.708  1.850   -2.533  1.00 48.83  ? 87  PRO A CG  1 
ATOM   451   C CD  . PRO A 1 58  ? 22.996  1.400   -1.868  1.00 48.89  ? 87  PRO A CD  1 
ATOM   452   N N   . ASP A 1 59  ? 21.831  -1.926  -3.302  1.00 60.25  ? 88  ASP A N   1 
ATOM   453   C CA  . ASP A 1 59  ? 21.650  -3.124  -4.116  1.00 65.84  ? 88  ASP A CA  1 
ATOM   454   C C   . ASP A 1 59  ? 22.351  -4.343  -3.493  1.00 62.37  ? 88  ASP A C   1 
ATOM   455   O O   . ASP A 1 59  ? 21.731  -5.403  -3.363  1.00 49.06  ? 88  ASP A O   1 
ATOM   456   C CB  . ASP A 1 59  ? 21.974  -2.853  -5.584  1.00 69.56  ? 88  ASP A CB  1 
ATOM   457   C CG  . ASP A 1 59  ? 20.789  -2.459  -6.464  1.00 74.48  ? 88  ASP A CG  1 
ATOM   458   O OD1 . ASP A 1 59  ? 19.969  -1.613  -6.032  1.00 73.33  ? 88  ASP A OD1 1 
ATOM   459   O OD2 . ASP A 1 59  ? 20.675  -3.010  -7.582  1.00 82.68  ? 88  ASP A OD2 1 
ATOM   460   N N   . GLU A 1 60  ? 23.631  -4.209  -3.105  1.00 56.72  ? 89  GLU A N   1 
ATOM   461   C CA  . GLU A 1 60  ? 24.438  -5.352  -2.681  1.00 61.94  ? 89  GLU A CA  1 
ATOM   462   C C   . GLU A 1 60  ? 24.529  -5.508  -1.154  1.00 58.93  ? 89  GLU A C   1 
ATOM   463   O O   . GLU A 1 60  ? 24.880  -6.580  -0.661  1.00 53.42  ? 89  GLU A O   1 
ATOM   464   C CB  . GLU A 1 60  ? 25.824  -5.269  -3.324  1.00 72.87  ? 89  GLU A CB  1 
ATOM   465   C CG  . GLU A 1 60  ? 25.972  -6.172  -4.548  1.00 79.37  ? 89  GLU A CG  1 
ATOM   466   C CD  . GLU A 1 60  ? 25.165  -5.769  -5.767  1.00 80.77  ? 89  GLU A CD  1 
ATOM   467   O OE1 . GLU A 1 60  ? 25.810  -5.547  -6.814  1.00 85.46  ? 89  GLU A OE1 1 
ATOM   468   O OE2 . GLU A 1 60  ? 23.919  -5.686  -5.688  1.00 75.77  ? 89  GLU A OE2 1 
ATOM   469   N N   . GLY A 1 61  ? 24.214  -4.449  -0.394  1.00 49.18  ? 90  GLY A N   1 
ATOM   470   C CA  . GLY A 1 61  ? 24.159  -4.528  1.058   1.00 44.11  ? 90  GLY A CA  1 
ATOM   471   C C   . GLY A 1 61  ? 25.466  -4.067  1.683   1.00 34.95  ? 90  GLY A C   1 
ATOM   472   O O   . GLY A 1 61  ? 26.217  -3.319  1.069   1.00 35.50  ? 90  GLY A O   1 
ATOM   473   N N   . ILE A 1 62  ? 25.731  -4.528  2.905   1.00 35.91  ? 91  ILE A N   1 
ATOM   474   C CA  . ILE A 1 62  ? 26.769  -3.922  3.722   1.00 34.23  ? 91  ILE A CA  1 
ATOM   475   C C   . ILE A 1 62  ? 28.148  -4.389  3.250   1.00 36.32  ? 91  ILE A C   1 
ATOM   476   O O   . ILE A 1 62  ? 28.327  -5.549  2.889   1.00 33.02  ? 91  ILE A O   1 
ATOM   477   C CB  . ILE A 1 62  ? 26.512  -4.189  5.210   1.00 33.25  ? 91  ILE A CB  1 
ATOM   478   C CG1 . ILE A 1 62  ? 27.356  -3.269  6.076   1.00 33.52  ? 91  ILE A CG1 1 
ATOM   479   C CG2 . ILE A 1 62  ? 26.656  -5.663  5.600   1.00 31.37  ? 91  ILE A CG2 1 
ATOM   480   C CD1 . ILE A 1 62  ? 26.874  -1.828  6.025   1.00 33.11  ? 91  ILE A CD1 1 
ATOM   481   N N   . ARG A 1 63  ? 29.085  -3.441  3.171   1.00 31.44  ? 92  ARG A N   1 
ATOM   482   C CA  . ARG A 1 63  ? 30.496  -3.778  3.075   1.00 33.54  ? 92  ARG A CA  1 
ATOM   483   C C   . ARG A 1 63  ? 31.225  -3.173  4.273   1.00 31.34  ? 92  ARG A C   1 
ATOM   484   O O   . ARG A 1 63  ? 31.042  -1.993  4.609   1.00 30.06  ? 92  ARG A O   1 
ATOM   485   C CB  . ARG A 1 63  ? 31.130  -3.300  1.762   1.00 37.94  ? 92  ARG A CB  1 
ATOM   486   C CG  . ARG A 1 63  ? 30.533  -3.931  0.509   1.00 44.39  ? 92  ARG A CG  1 
ATOM   487   C CD  . ARG A 1 63  ? 31.290  -3.422  -0.724  1.00 56.76  ? 92  ARG A CD  1 
ATOM   488   N NE  . ARG A 1 63  ? 30.764  -3.986  -1.974  1.00 64.42  ? 92  ARG A NE  1 
ATOM   489   C CZ  . ARG A 1 63  ? 31.204  -5.085  -2.590  1.00 69.50  ? 92  ARG A CZ  1 
ATOM   490   N NH1 . ARG A 1 63  ? 32.116  -5.876  -2.029  1.00 64.83  ? 92  ARG A NH1 1 
ATOM   491   N NH2 . ARG A 1 63  ? 30.696  -5.402  -3.772  1.00 70.44  ? 92  ARG A NH2 1 
ATOM   492   N N   . PHE A 1 64  ? 32.053  -4.025  4.889   1.00 29.91  ? 93  PHE A N   1 
ATOM   493   C CA  . PHE A 1 64  ? 32.961  -3.691  5.983   1.00 30.66  ? 93  PHE A CA  1 
ATOM   494   C C   . PHE A 1 64  ? 34.349  -3.390  5.433   1.00 34.44  ? 93  PHE A C   1 
ATOM   495   O O   . PHE A 1 64  ? 35.021  -4.308  4.933   1.00 32.05  ? 93  PHE A O   1 
ATOM   496   C CB  . PHE A 1 64  ? 33.079  -4.923  6.871   1.00 29.26  ? 93  PHE A CB  1 
ATOM   497   C CG  . PHE A 1 64  ? 31.762  -5.388  7.467   1.00 33.85  ? 93  PHE A CG  1 
ATOM   498   C CD1 . PHE A 1 64  ? 30.897  -4.483  8.076   1.00 32.40  ? 93  PHE A CD1 1 
ATOM   499   C CD2 . PHE A 1 64  ? 31.414  -6.722  7.474   1.00 37.01  ? 93  PHE A CD2 1 
ATOM   500   C CE1 . PHE A 1 64  ? 29.715  -4.913  8.645   1.00 30.80  ? 93  PHE A CE1 1 
ATOM   501   C CE2 . PHE A 1 64  ? 30.216  -7.140  8.041   1.00 35.61  ? 93  PHE A CE2 1 
ATOM   502   C CZ  . PHE A 1 64  ? 29.386  -6.242  8.635   1.00 35.12  ? 93  PHE A CZ  1 
ATOM   503   N N   . ARG A 1 65  ? 34.732  -2.107  5.479   1.00 32.34  ? 94  ARG A N   1 
ATOM   504   C CA  . ARG A 1 65  ? 35.977  -1.643  4.894   1.00 35.29  ? 94  ARG A CA  1 
ATOM   505   C C   . ARG A 1 65  ? 36.148  -2.237  3.495   1.00 39.66  ? 94  ARG A C   1 
ATOM   506   O O   . ARG A 1 65  ? 37.220  -2.753  3.207   1.00 39.67  ? 94  ARG A O   1 
ATOM   507   C CB  . ARG A 1 65  ? 37.136  -2.083  5.813   1.00 34.73  ? 94  ARG A CB  1 
ATOM   508   C CG  . ARG A 1 65  ? 37.114  -1.293  7.116   1.00 34.21  ? 94  ARG A CG  1 
ATOM   509   C CD  . ARG A 1 65  ? 37.427  0.194   6.909   1.00 31.57  ? 94  ARG A CD  1 
ATOM   510   N NE  . ARG A 1 65  ? 37.720  0.787   8.212   1.00 35.24  ? 94  ARG A NE  1 
ATOM   511   C CZ  . ARG A 1 65  ? 38.271  1.965   8.384   1.00 34.90  ? 94  ARG A CZ  1 
ATOM   512   N NH1 . ARG A 1 65  ? 38.600  2.662   7.336   1.00 35.78  ? 94  ARG A NH1 1 
ATOM   513   N NH2 . ARG A 1 65  ? 38.501  2.436   9.583   1.00 34.93  ? 94  ARG A NH2 1 
ATOM   514   N N   . GLY A 1 66  ? 35.080  -2.211  2.675   1.00 42.99  ? 95  GLY A N   1 
ATOM   515   C CA  . GLY A 1 66  ? 35.123  -2.642  1.280   1.00 41.65  ? 95  GLY A CA  1 
ATOM   516   C C   . GLY A 1 66  ? 34.890  -4.146  1.096   1.00 38.77  ? 95  GLY A C   1 
ATOM   517   O O   . GLY A 1 66  ? 34.739  -4.599  -0.014  1.00 38.24  ? 95  GLY A O   1 
ATOM   518   N N   . PHE A 1 67  ? 34.803  -4.918  2.173   1.00 31.53  ? 96  PHE A N   1 
ATOM   519   C CA  . PHE A 1 67  ? 34.594  -6.350  2.080   1.00 32.22  ? 96  PHE A CA  1 
ATOM   520   C C   . PHE A 1 67  ? 33.124  -6.681  2.310   1.00 39.52  ? 96  PHE A C   1 
ATOM   521   O O   . PHE A 1 67  ? 32.574  -6.310  3.344   1.00 32.58  ? 96  PHE A O   1 
ATOM   522   C CB  . PHE A 1 67  ? 35.386  -7.084  3.161   1.00 33.87  ? 96  PHE A CB  1 
ATOM   523   C CG  . PHE A 1 67  ? 36.879  -6.967  2.913   1.00 38.32  ? 96  PHE A CG  1 
ATOM   524   C CD1 . PHE A 1 67  ? 37.502  -7.806  1.986   1.00 37.46  ? 96  PHE A CD1 1 
ATOM   525   C CD2 . PHE A 1 67  ? 37.637  -5.975  3.534   1.00 36.98  ? 96  PHE A CD2 1 
ATOM   526   C CE1 . PHE A 1 67  ? 38.858  -7.657  1.691   1.00 42.28  ? 96  PHE A CE1 1 
ATOM   527   C CE2 . PHE A 1 67  ? 38.996  -5.846  3.255   1.00 41.35  ? 96  PHE A CE2 1 
ATOM   528   C CZ  . PHE A 1 67  ? 39.614  -6.707  2.353   1.00 38.01  ? 96  PHE A CZ  1 
ATOM   529   N N   . SER A 1 68  ? 32.509  -7.420  1.368   1.00 34.62  ? 97  SER A N   1 
ATOM   530   C CA  . SER A 1 68  ? 31.193  -7.991  1.580   1.00 35.17  ? 97  SER A CA  1 
ATOM   531   C C   . SER A 1 68  ? 31.265  -9.049  2.674   1.00 34.03  ? 97  SER A C   1 
ATOM   532   O O   . SER A 1 68  ? 32.331  -9.553  3.022   1.00 39.00  ? 97  SER A O   1 
ATOM   533   C CB  . SER A 1 68  ? 30.622  -8.568  0.286   1.00 42.33  ? 97  SER A CB  1 
ATOM   534   O OG  . SER A 1 68  ? 31.348  -9.722  -0.107  1.00 41.80  ? 97  SER A OG  1 
ATOM   535   N N   . ILE A 1 69  ? 30.097  -9.412  3.192   1.00 33.63  ? 98  ILE A N   1 
ATOM   536   C CA  . ILE A 1 69  ? 29.997  -10.375 4.257   1.00 34.29  ? 98  ILE A CA  1 
ATOM   537   C C   . ILE A 1 69  ? 30.480  -11.737 3.761   1.00 36.57  ? 98  ILE A C   1 
ATOM   538   O O   . ILE A 1 69  ? 31.231  -12.395 4.474   1.00 37.48  ? 98  ILE A O   1 
ATOM   539   C CB  . ILE A 1 69  ? 28.565  -10.410 4.815   1.00 37.07  ? 98  ILE A CB  1 
ATOM   540   C CG1 . ILE A 1 69  ? 28.326  -9.255  5.811   1.00 39.79  ? 98  ILE A CG1 1 
ATOM   541   C CG2 . ILE A 1 69  ? 28.273  -11.739 5.481   1.00 37.42  ? 98  ILE A CG2 1 
ATOM   542   C CD1 . ILE A 1 69  ? 26.915  -9.190  6.360   1.00 40.05  ? 98  ILE A CD1 1 
ATOM   543   N N   . PRO A 1 70  ? 30.027  -12.247 2.592   1.00 38.16  ? 99  PRO A N   1 
ATOM   544   C CA  . PRO A 1 70  ? 30.640  -13.450 2.015   1.00 42.65  ? 99  PRO A CA  1 
ATOM   545   C C   . PRO A 1 70  ? 32.173  -13.409 1.962   1.00 39.47  ? 99  PRO A C   1 
ATOM   546   O O   . PRO A 1 70  ? 32.825  -14.375 2.322   1.00 34.70  ? 99  PRO A O   1 
ATOM   547   C CB  . PRO A 1 70  ? 29.985  -13.499 0.612   1.00 43.25  ? 99  PRO A CB  1 
ATOM   548   C CG  . PRO A 1 70  ? 28.609  -12.889 0.811   1.00 42.63  ? 99  PRO A CG  1 
ATOM   549   C CD  . PRO A 1 70  ? 28.834  -11.800 1.846   1.00 39.85  ? 99  PRO A CD  1 
ATOM   550   N N   . GLU A 1 71  ? 32.756  -12.275 1.526   1.00 40.65  ? 100 GLU A N   1 
ATOM   551   C CA  . GLU A 1 71  ? 34.196  -12.122 1.566   1.00 35.50  ? 100 GLU A CA  1 
ATOM   552   C C   . GLU A 1 71  ? 34.725  -12.327 2.987   1.00 35.66  ? 100 GLU A C   1 
ATOM   553   O O   . GLU A 1 71  ? 35.737  -12.987 3.183   1.00 38.51  ? 100 GLU A O   1 
ATOM   554   C CB  . GLU A 1 71  ? 34.601  -10.798 0.923   1.00 41.84  ? 100 GLU A CB  1 
ATOM   555   C CG  . GLU A 1 71  ? 34.387  -10.787 -0.584  1.00 44.09  ? 100 GLU A CG  1 
ATOM   556   C CD  . GLU A 1 71  ? 34.622  -9.445  -1.252  1.00 50.59  ? 100 GLU A CD  1 
ATOM   557   O OE1 . GLU A 1 71  ? 34.050  -8.439  -0.778  1.00 52.35  ? 100 GLU A OE1 1 
ATOM   558   O OE2 . GLU A 1 71  ? 35.381  -9.409  -2.254  1.00 49.27  ? 100 GLU A OE2 1 
ATOM   559   N N   . CYS A 1 72  ? 34.042  -11.779 3.996   1.00 37.84  ? 101 CYS A N   1 
ATOM   560   C CA  . CYS A 1 72  ? 34.487  -11.860 5.383   1.00 32.00  ? 101 CYS A CA  1 
ATOM   561   C C   . CYS A 1 72  ? 34.419  -13.277 5.935   1.00 34.93  ? 101 CYS A C   1 
ATOM   562   O O   . CYS A 1 72  ? 35.292  -13.683 6.706   1.00 34.35  ? 101 CYS A O   1 
ATOM   563   C CB  . CYS A 1 72  ? 33.679  -10.959 6.319   1.00 33.96  ? 101 CYS A CB  1 
ATOM   564   S SG  . CYS A 1 72  ? 34.071  -9.205  6.070   1.00 36.67  ? 101 CYS A SG  1 
ATOM   565   N N   . GLN A 1 73  ? 33.369  -14.006 5.576   1.00 37.04  ? 102 GLN A N   1 
ATOM   566   C CA  . GLN A 1 73  ? 33.211  -15.389 5.999   1.00 42.43  ? 102 GLN A CA  1 
ATOM   567   C C   . GLN A 1 73  ? 34.385  -16.250 5.536   1.00 42.54  ? 102 GLN A C   1 
ATOM   568   O O   . GLN A 1 73  ? 34.884  -17.080 6.293   1.00 45.60  ? 102 GLN A O   1 
ATOM   569   C CB  . GLN A 1 73  ? 31.877  -15.911 5.473   1.00 46.44  ? 102 GLN A CB  1 
ATOM   570   C CG  . GLN A 1 73  ? 30.721  -15.435 6.340   1.00 49.49  ? 102 GLN A CG  1 
ATOM   571   C CD  . GLN A 1 73  ? 29.412  -16.098 6.008   1.00 47.78  ? 102 GLN A CD  1 
ATOM   572   O OE1 . GLN A 1 73  ? 28.828  -15.838 4.959   1.00 41.05  ? 102 GLN A OE1 1 
ATOM   573   N NE2 . GLN A 1 73  ? 28.936  -16.923 6.928   1.00 55.78  ? 102 GLN A NE2 1 
ATOM   574   N N   . LYS A 1 74  ? 34.841  -16.005 4.309   1.00 46.64  ? 103 LYS A N   1 
ATOM   575   C CA  . LYS A 1 74  ? 36.028  -16.659 3.777   1.00 49.67  ? 103 LYS A CA  1 
ATOM   576   C C   . LYS A 1 74  ? 37.317  -16.166 4.443   1.00 44.72  ? 103 LYS A C   1 
ATOM   577   O O   . LYS A 1 74  ? 38.100  -16.988 4.913   1.00 41.16  ? 103 LYS A O   1 
ATOM   578   C CB  . LYS A 1 74  ? 36.118  -16.461 2.260   1.00 51.83  ? 103 LYS A CB  1 
ATOM   579   C CG  . LYS A 1 74  ? 34.908  -17.003 1.541   1.00 60.25  ? 103 LYS A CG  1 
ATOM   580   C CD  . LYS A 1 74  ? 35.229  -18.007 0.437   1.00 66.65  ? 103 LYS A CD  1 
ATOM   581   C CE  . LYS A 1 74  ? 33.983  -18.590 -0.156  1.00 64.81  ? 103 LYS A CE  1 
ATOM   582   N NZ  . LYS A 1 74  ? 33.144  -19.304 0.812   1.00 63.40  ? 103 LYS A NZ  1 
ATOM   583   N N   . LEU A 1 75  ? 37.549  -14.843 4.463   1.00 40.56  ? 104 LEU A N   1 
ATOM   584   C CA  . LEU A 1 75  ? 38.869  -14.306 4.778   1.00 41.01  ? 104 LEU A CA  1 
ATOM   585   C C   . LEU A 1 75  ? 39.152  -14.200 6.283   1.00 36.99  ? 104 LEU A C   1 
ATOM   586   O O   . LEU A 1 75  ? 40.290  -14.357 6.701   1.00 38.77  ? 104 LEU A O   1 
ATOM   587   C CB  . LEU A 1 75  ? 39.034  -12.959 4.087   1.00 40.11  ? 104 LEU A CB  1 
ATOM   588   C CG  . LEU A 1 75  ? 39.094  -13.022 2.561   1.00 41.56  ? 104 LEU A CG  1 
ATOM   589   C CD1 . LEU A 1 75  ? 38.785  -11.631 2.073   1.00 47.56  ? 104 LEU A CD1 1 
ATOM   590   C CD2 . LEU A 1 75  ? 40.425  -13.541 1.997   1.00 41.47  ? 104 LEU A CD2 1 
ATOM   591   N N   . LEU A 1 76  ? 38.130  -13.942 7.097   1.00 37.98  ? 105 LEU A N   1 
ATOM   592   C CA  . LEU A 1 76  ? 38.300  -13.688 8.515   1.00 35.67  ? 105 LEU A CA  1 
ATOM   593   C C   . LEU A 1 76  ? 38.638  -14.985 9.231   1.00 34.46  ? 105 LEU A C   1 
ATOM   594   O O   . LEU A 1 76  ? 37.960  -15.984 9.023   1.00 38.40  ? 105 LEU A O   1 
ATOM   595   C CB  . LEU A 1 76  ? 37.045  -13.095 9.150   1.00 33.88  ? 105 LEU A CB  1 
ATOM   596   C CG  . LEU A 1 76  ? 36.747  -11.623 8.857   1.00 37.61  ? 105 LEU A CG  1 
ATOM   597   C CD1 . LEU A 1 76  ? 35.463  -11.273 9.637   1.00 36.38  ? 105 LEU A CD1 1 
ATOM   598   C CD2 . LEU A 1 76  ? 37.913  -10.708 9.229   1.00 38.70  ? 105 LEU A CD2 1 
ATOM   599   N N   . PRO A 1 77  ? 39.601  -14.965 10.181  1.00 34.63  ? 106 PRO A N   1 
ATOM   600   C CA  . PRO A 1 77  ? 39.878  -16.111 11.052  1.00 35.70  ? 106 PRO A CA  1 
ATOM   601   C C   . PRO A 1 77  ? 38.691  -16.680 11.823  1.00 39.94  ? 106 PRO A C   1 
ATOM   602   O O   . PRO A 1 77  ? 37.786  -15.952 12.250  1.00 34.38  ? 106 PRO A O   1 
ATOM   603   C CB  . PRO A 1 77  ? 40.945  -15.583 12.028  1.00 37.62  ? 106 PRO A CB  1 
ATOM   604   C CG  . PRO A 1 77  ? 41.587  -14.430 11.313  1.00 37.22  ? 106 PRO A CG  1 
ATOM   605   C CD  . PRO A 1 77  ? 40.497  -13.841 10.450  1.00 35.28  ? 106 PRO A CD  1 
ATOM   606   N N   . LYS A 1 78  ? 38.775  -17.988 12.085  1.00 35.38  ? 107 LYS A N   1 
ATOM   607   C CA  . LYS A 1 78  ? 37.720  -18.713 12.777  1.00 35.17  ? 107 LYS A CA  1 
ATOM   608   C C   . LYS A 1 78  ? 38.322  -19.290 14.048  1.00 33.29  ? 107 LYS A C   1 
ATOM   609   O O   . LYS A 1 78  ? 39.533  -19.363 14.154  1.00 35.82  ? 107 LYS A O   1 
ATOM   610   C CB  . LYS A 1 78  ? 37.173  -19.793 11.829  1.00 40.84  ? 107 LYS A CB  1 
ATOM   611   C CG  . LYS A 1 78  ? 36.526  -19.242 10.574  1.00 44.38  ? 107 LYS A CG  1 
ATOM   612   C CD  . LYS A 1 78  ? 36.796  -20.130 9.362   1.00 59.43  ? 107 LYS A CD  1 
ATOM   613   C CE  . LYS A 1 78  ? 35.997  -19.733 8.143   1.00 67.07  ? 107 LYS A CE  1 
ATOM   614   N NZ  . LYS A 1 78  ? 35.627  -20.893 7.319   1.00 71.74  ? 107 LYS A NZ  1 
ATOM   615   N N   . ALA A 1 79  ? 37.506  -19.714 15.017  1.00 33.01  ? 108 ALA A N   1 
ATOM   616   C CA  . ALA A 1 79  ? 38.038  -20.500 16.121  1.00 36.78  ? 108 ALA A CA  1 
ATOM   617   C C   . ALA A 1 79  ? 38.556  -21.834 15.573  1.00 43.07  ? 108 ALA A C   1 
ATOM   618   O O   . ALA A 1 79  ? 38.175  -22.208 14.466  1.00 42.23  ? 108 ALA A O   1 
ATOM   619   C CB  . ALA A 1 79  ? 36.965  -20.744 17.152  1.00 33.21  ? 108 ALA A CB  1 
ATOM   620   N N   . LYS A 1 80  ? 39.374  -22.555 16.363  1.00 49.06  ? 109 LYS A N   1 
ATOM   621   C CA  . LYS A 1 80  ? 39.800  -23.915 16.038  1.00 51.88  ? 109 LYS A CA  1 
ATOM   622   C C   . LYS A 1 80  ? 38.605  -24.865 16.100  1.00 46.98  ? 109 LYS A C   1 
ATOM   623   O O   . LYS A 1 80  ? 37.962  -24.986 17.140  1.00 47.98  ? 109 LYS A O   1 
ATOM   624   C CB  . LYS A 1 80  ? 40.805  -24.517 17.030  1.00 57.10  ? 109 LYS A CB  1 
ATOM   625   C CG  . LYS A 1 80  ? 42.079  -23.748 17.317  1.00 63.14  ? 109 LYS A CG  1 
ATOM   626   C CD  . LYS A 1 80  ? 43.065  -23.673 16.158  1.00 75.23  ? 109 LYS A CD  1 
ATOM   627   C CE  . LYS A 1 80  ? 44.488  -23.682 16.638  1.00 81.72  ? 109 LYS A CE  1 
ATOM   628   N NZ  . LYS A 1 80  ? 44.732  -22.791 17.780  1.00 81.02  ? 109 LYS A NZ  1 
ATOM   629   N N   . GLY A 1 81  ? 38.351  -25.567 14.992  1.00 50.95  ? 110 GLY A N   1 
ATOM   630   C CA  . GLY A 1 81  ? 37.207  -26.457 14.872  1.00 49.02  ? 110 GLY A CA  1 
ATOM   631   C C   . GLY A 1 81  ? 35.930  -25.714 14.476  1.00 45.19  ? 110 GLY A C   1 
ATOM   632   O O   . GLY A 1 81  ? 34.835  -26.210 14.703  1.00 49.94  ? 110 GLY A O   1 
ATOM   633   N N   . GLY A 1 82  ? 36.061  -24.521 13.882  1.00 44.26  ? 111 GLY A N   1 
ATOM   634   C CA  . GLY A 1 82  ? 34.913  -23.650 13.662  1.00 38.25  ? 111 GLY A CA  1 
ATOM   635   C C   . GLY A 1 82  ? 34.849  -23.206 12.212  1.00 42.58  ? 111 GLY A C   1 
ATOM   636   O O   . GLY A 1 82  ? 35.841  -23.297 11.488  1.00 40.84  ? 111 GLY A O   1 
ATOM   637   N N   . GLU A 1 83  ? 33.671  -22.737 11.798  1.00 43.84  ? 112 GLU A N   1 
ATOM   638   C CA  . GLU A 1 83  ? 33.454  -22.281 10.435  1.00 53.94  ? 112 GLU A CA  1 
ATOM   639   C C   . GLU A 1 83  ? 33.052  -20.805 10.382  1.00 44.59  ? 112 GLU A C   1 
ATOM   640   O O   . GLU A 1 83  ? 33.137  -20.199 9.314   1.00 51.27  ? 112 GLU A O   1 
ATOM   641   C CB  . GLU A 1 83  ? 32.396  -23.164 9.762   1.00 60.46  ? 112 GLU A CB  1 
ATOM   642   C CG  . GLU A 1 83  ? 32.999  -24.272 8.897   1.00 78.24  ? 112 GLU A CG  1 
ATOM   643   C CD  . GLU A 1 83  ? 33.978  -25.208 9.597   1.00 88.54  ? 112 GLU A CD  1 
ATOM   644   O OE1 . GLU A 1 83  ? 33.540  -25.940 10.509  1.00 102.17 ? 112 GLU A OE1 1 
ATOM   645   O OE2 . GLU A 1 83  ? 35.179  -25.210 9.246   1.00 90.81  ? 112 GLU A OE2 1 
ATOM   646   N N   . GLU A 1 84  ? 32.630  -20.236 11.518  1.00 37.92  ? 113 GLU A N   1 
ATOM   647   C CA  . GLU A 1 84  ? 32.081  -18.882 11.554  1.00 38.03  ? 113 GLU A CA  1 
ATOM   648   C C   . GLU A 1 84  ? 33.139  -17.845 11.929  1.00 34.32  ? 113 GLU A C   1 
ATOM   649   O O   . GLU A 1 84  ? 34.017  -18.070 12.760  1.00 34.58  ? 113 GLU A O   1 
ATOM   650   C CB  . GLU A 1 84  ? 30.880  -18.850 12.501  1.00 38.17  ? 113 GLU A CB  1 
ATOM   651   C CG  . GLU A 1 84  ? 29.672  -19.643 12.006  1.00 36.48  ? 113 GLU A CG  1 
ATOM   652   C CD  . GLU A 1 84  ? 29.269  -19.435 10.561  1.00 37.67  ? 113 GLU A CD  1 
ATOM   653   O OE1 . GLU A 1 84  ? 29.650  -18.426 9.918   1.00 41.70  ? 113 GLU A OE1 1 
ATOM   654   O OE2 . GLU A 1 84  ? 28.571  -20.339 10.050  1.00 38.67  ? 113 GLU A OE2 1 
ATOM   655   N N   . PRO A 1 85  ? 33.137  -16.645 11.318  1.00 37.15  ? 114 PRO A N   1 
ATOM   656   C CA  . PRO A 1 85  ? 34.204  -15.692 11.601  1.00 35.56  ? 114 PRO A CA  1 
ATOM   657   C C   . PRO A 1 85  ? 34.088  -15.203 13.042  1.00 33.07  ? 114 PRO A C   1 
ATOM   658   O O   . PRO A 1 85  ? 32.992  -15.092 13.599  1.00 32.40  ? 114 PRO A O   1 
ATOM   659   C CB  . PRO A 1 85  ? 33.935  -14.616 10.565  1.00 37.26  ? 114 PRO A CB  1 
ATOM   660   C CG  . PRO A 1 85  ? 32.436  -14.658 10.365  1.00 35.54  ? 114 PRO A CG  1 
ATOM   661   C CD  . PRO A 1 85  ? 32.152  -16.135 10.352  1.00 37.35  ? 114 PRO A CD  1 
ATOM   662   N N   . LEU A 1 86  ? 35.253  -14.999 13.642  1.00 30.35  ? 115 LEU A N   1 
ATOM   663   C CA  . LEU A 1 86  ? 35.361  -14.448 14.968  1.00 32.35  ? 115 LEU A CA  1 
ATOM   664   C C   . LEU A 1 86  ? 35.061  -12.956 14.926  1.00 33.43  ? 115 LEU A C   1 
ATOM   665   O O   . LEU A 1 86  ? 35.536  -12.272 14.019  1.00 33.97  ? 115 LEU A O   1 
ATOM   666   C CB  . LEU A 1 86  ? 36.759  -14.759 15.473  1.00 36.11  ? 115 LEU A CB  1 
ATOM   667   C CG  . LEU A 1 86  ? 36.998  -16.222 15.850  1.00 38.47  ? 115 LEU A CG  1 
ATOM   668   C CD1 . LEU A 1 86  ? 38.351  -16.370 16.509  1.00 40.37  ? 115 LEU A CD1 1 
ATOM   669   C CD2 . LEU A 1 86  ? 35.897  -16.753 16.762  1.00 44.87  ? 115 LEU A CD2 1 
ATOM   670   N N   . PRO A 1 87  ? 34.191  -12.434 15.827  1.00 30.79  ? 116 PRO A N   1 
ATOM   671   C CA  . PRO A 1 87  ? 33.954  -10.996 15.908  1.00 28.30  ? 116 PRO A CA  1 
ATOM   672   C C   . PRO A 1 87  ? 35.196  -10.134 16.095  1.00 26.09  ? 116 PRO A C   1 
ATOM   673   O O   . PRO A 1 87  ? 35.256  -9.054  15.523  1.00 29.26  ? 116 PRO A O   1 
ATOM   674   C CB  . PRO A 1 87  ? 32.991  -10.860 17.107  1.00 29.32  ? 116 PRO A CB  1 
ATOM   675   C CG  . PRO A 1 87  ? 32.259  -12.176 17.170  1.00 30.87  ? 116 PRO A CG  1 
ATOM   676   C CD  . PRO A 1 87  ? 33.276  -13.208 16.689  1.00 28.18  ? 116 PRO A CD  1 
ATOM   677   N N   . GLU A 1 88  ? 36.177  -10.662 16.834  1.00 26.38  ? 117 GLU A N   1 
ATOM   678   C CA  . GLU A 1 88  ? 37.496  -10.079 17.022  1.00 26.75  ? 117 GLU A CA  1 
ATOM   679   C C   . GLU A 1 88  ? 38.141  -9.653  15.723  1.00 28.73  ? 117 GLU A C   1 
ATOM   680   O O   . GLU A 1 88  ? 38.713  -8.567  15.691  1.00 26.98  ? 117 GLU A O   1 
ATOM   681   C CB  . GLU A 1 88  ? 38.494  -11.036 17.651  1.00 30.18  ? 117 GLU A CB  1 
ATOM   682   C CG  . GLU A 1 88  ? 38.175  -11.304 19.117  1.00 29.75  ? 117 GLU A CG  1 
ATOM   683   C CD  . GLU A 1 88  ? 37.281  -12.471 19.446  1.00 28.26  ? 117 GLU A CD  1 
ATOM   684   O OE1 . GLU A 1 88  ? 36.287  -12.698 18.711  1.00 30.85  ? 117 GLU A OE1 1 
ATOM   685   O OE2 . GLU A 1 88  ? 37.540  -13.116 20.513  1.00 29.77  ? 117 GLU A OE2 1 
ATOM   686   N N   . GLY A 1 89  ? 38.040  -10.515 14.701  1.00 28.89  ? 118 GLY A N   1 
ATOM   687   C CA  . GLY A 1 89  ? 38.616  -10.254 13.397  1.00 27.51  ? 118 GLY A CA  1 
ATOM   688   C C   . GLY A 1 89  ? 37.831  -9.196  12.636  1.00 28.75  ? 118 GLY A C   1 
ATOM   689   O O   . GLY A 1 89  ? 38.432  -8.419  11.881  1.00 25.33  ? 118 GLY A O   1 
ATOM   690   N N   . LEU A 1 90  ? 36.504  -9.163  12.868  1.00 28.10  ? 119 LEU A N   1 
ATOM   691   C CA  . LEU A 1 90  ? 35.682  -8.141  12.266  1.00 31.92  ? 119 LEU A CA  1 
ATOM   692   C C   . LEU A 1 90  ? 36.104  -6.793  12.839  1.00 27.59  ? 119 LEU A C   1 
ATOM   693   O O   . LEU A 1 90  ? 36.215  -5.815  12.116  1.00 26.74  ? 119 LEU A O   1 
ATOM   694   C CB  . LEU A 1 90  ? 34.180  -8.363  12.472  1.00 35.32  ? 119 LEU A CB  1 
ATOM   695   C CG  . LEU A 1 90  ? 33.260  -7.828  11.366  1.00 36.45  ? 119 LEU A CG  1 
ATOM   696   C CD1 . LEU A 1 90  ? 31.889  -7.600  11.920  1.00 47.41  ? 119 LEU A CD1 1 
ATOM   697   C CD2 . LEU A 1 90  ? 33.647  -6.635  10.554  1.00 35.40  ? 119 LEU A CD2 1 
ATOM   698   N N   . PHE A 1 91  ? 36.323  -6.738  14.147  1.00 26.50  ? 120 PHE A N   1 
ATOM   699   C CA  . PHE A 1 91  ? 36.713  -5.482  14.779  1.00 28.00  ? 120 PHE A CA  1 
ATOM   700   C C   . PHE A 1 91  ? 38.076  -5.020  14.268  1.00 26.91  ? 120 PHE A C   1 
ATOM   701   O O   . PHE A 1 91  ? 38.259  -3.856  13.915  1.00 25.33  ? 120 PHE A O   1 
ATOM   702   C CB  . PHE A 1 91  ? 36.653  -5.648  16.293  1.00 27.06  ? 120 PHE A CB  1 
ATOM   703   C CG  . PHE A 1 91  ? 37.036  -4.380  17.048  1.00 25.36  ? 120 PHE A CG  1 
ATOM   704   C CD1 . PHE A 1 91  ? 36.134  -3.340  17.194  1.00 23.89  ? 120 PHE A CD1 1 
ATOM   705   C CD2 . PHE A 1 91  ? 38.315  -4.214  17.579  1.00 27.27  ? 120 PHE A CD2 1 
ATOM   706   C CE1 . PHE A 1 91  ? 36.511  -2.158  17.827  1.00 23.77  ? 120 PHE A CE1 1 
ATOM   707   C CE2 . PHE A 1 91  ? 38.678  -3.040  18.218  1.00 26.09  ? 120 PHE A CE2 1 
ATOM   708   C CZ  . PHE A 1 91  ? 37.760  -2.030  18.375  1.00 26.10  ? 120 PHE A CZ  1 
ATOM   709   N N   . TRP A 1 92  ? 39.031  -5.945  14.155  1.00 29.40  ? 121 TRP A N   1 
ATOM   710   C CA  . TRP A 1 92  ? 40.344  -5.627  13.613  1.00 24.81  ? 121 TRP A CA  1 
ATOM   711   C C   . TRP A 1 92  ? 40.214  -5.007  12.233  1.00 24.84  ? 121 TRP A C   1 
ATOM   712   O O   . TRP A 1 92  ? 40.848  -3.985  11.915  1.00 31.37  ? 121 TRP A O   1 
ATOM   713   C CB  . TRP A 1 92  ? 41.210  -6.896  13.595  1.00 30.05  ? 121 TRP A CB  1 
ATOM   714   C CG  . TRP A 1 92  ? 42.639  -6.583  13.280  1.00 24.63  ? 121 TRP A CG  1 
ATOM   715   C CD1 . TRP A 1 92  ? 43.127  -6.208  12.068  1.00 27.32  ? 121 TRP A CD1 1 
ATOM   716   C CD2 . TRP A 1 92  ? 43.730  -6.557  14.208  1.00 23.78  ? 121 TRP A CD2 1 
ATOM   717   N NE1 . TRP A 1 92  ? 44.471  -5.963  12.178  1.00 31.59  ? 121 TRP A NE1 1 
ATOM   718   C CE2 . TRP A 1 92  ? 44.870  -6.167  13.477  1.00 31.26  ? 121 TRP A CE2 1 
ATOM   719   C CE3 . TRP A 1 92  ? 43.863  -6.833  15.569  1.00 24.29  ? 121 TRP A CE3 1 
ATOM   720   C CZ2 . TRP A 1 92  ? 46.126  -6.033  14.068  1.00 31.19  ? 121 TRP A CZ2 1 
ATOM   721   C CZ3 . TRP A 1 92  ? 45.104  -6.709  16.147  1.00 26.04  ? 121 TRP A CZ3 1 
ATOM   722   C CH2 . TRP A 1 92  ? 46.216  -6.290  15.413  1.00 28.46  ? 121 TRP A CH2 1 
ATOM   723   N N   . LEU A 1 93  ? 39.372  -5.626  11.404  1.00 26.49  ? 122 LEU A N   1 
ATOM   724   C CA  . LEU A 1 93  ? 39.133  -5.172  10.049  1.00 26.28  ? 122 LEU A CA  1 
ATOM   725   C C   . LEU A 1 93  ? 38.514  -3.774  10.053  1.00 27.79  ? 122 LEU A C   1 
ATOM   726   O O   . LEU A 1 93  ? 38.910  -2.906  9.285   1.00 24.75  ? 122 LEU A O   1 
ATOM   727   C CB  . LEU A 1 93  ? 38.226  -6.147  9.307   1.00 29.04  ? 122 LEU A CB  1 
ATOM   728   C CG  . LEU A 1 93  ? 37.656  -5.618  7.989   1.00 29.71  ? 122 LEU A CG  1 
ATOM   729   C CD1 . LEU A 1 93  ? 38.808  -5.430  7.064   1.00 34.88  ? 122 LEU A CD1 1 
ATOM   730   C CD2 . LEU A 1 93  ? 36.658  -6.562  7.411   1.00 31.78  ? 122 LEU A CD2 1 
ATOM   731   N N   . LEU A 1 94  ? 37.524  -3.546  10.900  1.00 27.41  ? 123 LEU A N   1 
ATOM   732   C CA  . LEU A 1 94  ? 36.905  -2.217  10.959  1.00 29.49  ? 123 LEU A CA  1 
ATOM   733   C C   . LEU A 1 94  ? 37.869  -1.129  11.403  1.00 24.73  ? 123 LEU A C   1 
ATOM   734   O O   . LEU A 1 94  ? 37.875  -0.019  10.880  1.00 27.55  ? 123 LEU A O   1 
ATOM   735   C CB  . LEU A 1 94  ? 35.722  -2.327  11.901  1.00 30.85  ? 123 LEU A CB  1 
ATOM   736   C CG  . LEU A 1 94  ? 34.575  -3.175  11.363  1.00 31.61  ? 123 LEU A CG  1 
ATOM   737   C CD1 . LEU A 1 94  ? 33.379  -2.950  12.291  1.00 35.82  ? 123 LEU A CD1 1 
ATOM   738   C CD2 . LEU A 1 94  ? 34.236  -2.792  9.936   1.00 28.15  ? 123 LEU A CD2 1 
ATOM   739   N N   . VAL A 1 95  ? 38.725  -1.458  12.354  1.00 28.36  ? 124 VAL A N   1 
ATOM   740   C CA  . VAL A 1 95  ? 39.674  -0.506  12.905  1.00 26.65  ? 124 VAL A CA  1 
ATOM   741   C C   . VAL A 1 95  ? 40.804  -0.189  11.928  1.00 27.86  ? 124 VAL A C   1 
ATOM   742   O O   . VAL A 1 95  ? 41.254  0.940   11.912  1.00 26.67  ? 124 VAL A O   1 
ATOM   743   C CB  . VAL A 1 95  ? 40.217  -1.079  14.225  1.00 30.34  ? 124 VAL A CB  1 
ATOM   744   C CG1 . VAL A 1 95  ? 41.511  -0.410  14.672  1.00 32.94  ? 124 VAL A CG1 1 
ATOM   745   C CG2 . VAL A 1 95  ? 39.163  -0.891  15.290  1.00 32.93  ? 124 VAL A CG2 1 
ATOM   746   N N   . THR A 1 96  ? 41.323  -1.188  11.204  1.00 30.22  ? 125 THR A N   1 
ATOM   747   C CA  . THR A 1 96  ? 42.567  -1.040  10.476  1.00 29.05  ? 125 THR A CA  1 
ATOM   748   C C   . THR A 1 96  ? 42.328  -0.965  8.975   1.00 30.20  ? 125 THR A C   1 
ATOM   749   O O   . THR A 1 96  ? 43.216  -0.547  8.250   1.00 29.64  ? 125 THR A O   1 
ATOM   750   C CB  . THR A 1 96  ? 43.497  -2.204  10.808  1.00 33.48  ? 125 THR A CB  1 
ATOM   751   O OG1 . THR A 1 96  ? 42.952  -3.409  10.297  1.00 27.87  ? 125 THR A OG1 1 
ATOM   752   C CG2 . THR A 1 96  ? 43.705  -2.334  12.299  1.00 34.05  ? 125 THR A CG2 1 
ATOM   753   N N   . GLY A 1 97  ? 41.151  -1.411  8.518   1.00 27.18  ? 126 GLY A N   1 
ATOM   754   C CA  . GLY A 1 97  ? 40.912  -1.608  7.107   1.00 33.96  ? 126 GLY A CA  1 
ATOM   755   C C   . GLY A 1 97  ? 41.595  -2.862  6.566   1.00 32.12  ? 126 GLY A C   1 
ATOM   756   O O   . GLY A 1 97  ? 41.517  -3.107  5.378   1.00 33.79  ? 126 GLY A O   1 
ATOM   757   N N   . HIS A 1 98  ? 42.268  -3.653  7.410   1.00 30.59  ? 127 HIS A N   1 
ATOM   758   C CA  . HIS A 1 98  ? 42.974  -4.829  6.910   1.00 36.25  ? 127 HIS A CA  1 
ATOM   759   C C   . HIS A 1 98  ? 42.389  -6.097  7.507   1.00 35.97  ? 127 HIS A C   1 
ATOM   760   O O   . HIS A 1 98  ? 41.969  -6.093  8.657   1.00 33.01  ? 127 HIS A O   1 
ATOM   761   C CB  . HIS A 1 98  ? 44.465  -4.811  7.274   1.00 44.11  ? 127 HIS A CB  1 
ATOM   762   C CG  . HIS A 1 98  ? 45.156  -3.600  6.765   1.00 50.39  ? 127 HIS A CG  1 
ATOM   763   N ND1 . HIS A 1 98  ? 44.860  -3.072  5.528   1.00 55.62  ? 127 HIS A ND1 1 
ATOM   764   C CD2 . HIS A 1 98  ? 46.071  -2.798  7.317   1.00 55.52  ? 127 HIS A CD2 1 
ATOM   765   C CE1 . HIS A 1 98  ? 45.584  -1.980  5.340   1.00 58.13  ? 127 HIS A CE1 1 
ATOM   766   N NE2 . HIS A 1 98  ? 46.330  -1.800  6.415   1.00 59.58  ? 127 HIS A NE2 1 
ATOM   767   N N   . ILE A 1 99  ? 42.452  -7.195  6.742   1.00 36.48  ? 128 ILE A N   1 
ATOM   768   C CA  . ILE A 1 99  ? 42.074  -8.496  7.264   1.00 30.91  ? 128 ILE A CA  1 
ATOM   769   C C   . ILE A 1 99  ? 43.122  -8.933  8.272   1.00 32.68  ? 128 ILE A C   1 
ATOM   770   O O   . ILE A 1 99  ? 44.309  -8.815  7.996   1.00 29.83  ? 128 ILE A O   1 
ATOM   771   C CB  . ILE A 1 99  ? 41.948  -9.527  6.136   1.00 32.82  ? 128 ILE A CB  1 
ATOM   772   C CG1 . ILE A 1 99  ? 40.821  -9.150  5.189   1.00 36.19  ? 128 ILE A CG1 1 
ATOM   773   C CG2 . ILE A 1 99  ? 41.788  -10.921 6.755   1.00 31.51  ? 128 ILE A CG2 1 
ATOM   774   C CD1 . ILE A 1 99  ? 39.432  -9.266  5.806   1.00 37.41  ? 128 ILE A CD1 1 
ATOM   775   N N   . PRO A 1 100 ? 42.733  -9.401  9.481   1.00 30.27  ? 129 PRO A N   1 
ATOM   776   C CA  . PRO A 1 100 ? 43.710  -9.803  10.484  1.00 32.04  ? 129 PRO A CA  1 
ATOM   777   C C   . PRO A 1 100 ? 44.276  -11.194 10.238  1.00 32.53  ? 129 PRO A C   1 
ATOM   778   O O   . PRO A 1 100 ? 43.556  -12.031 9.714   1.00 32.63  ? 129 PRO A O   1 
ATOM   779   C CB  . PRO A 1 100 ? 42.872  -9.788  11.777  1.00 29.59  ? 129 PRO A CB  1 
ATOM   780   C CG  . PRO A 1 100 ? 41.487  -10.137 11.316  1.00 28.51  ? 129 PRO A CG  1 
ATOM   781   C CD  . PRO A 1 100 ? 41.344  -9.496  9.966   1.00 29.02  ? 129 PRO A CD  1 
ATOM   782   N N   . THR A 1 101 ? 45.506  -11.433 10.726  1.00 36.66  ? 130 THR A N   1 
ATOM   783   C CA  . THR A 1 101 ? 46.106  -12.767 10.811  1.00 42.56  ? 130 THR A CA  1 
ATOM   784   C C   . THR A 1 101 ? 45.468  -13.502 11.979  1.00 41.07  ? 130 THR A C   1 
ATOM   785   O O   . THR A 1 101 ? 44.968  -12.870 12.897  1.00 38.46  ? 130 THR A O   1 
ATOM   786   C CB  . THR A 1 101 ? 47.621  -12.725 11.055  1.00 38.13  ? 130 THR A CB  1 
ATOM   787   O OG1 . THR A 1 101 ? 47.848  -12.207 12.368  1.00 36.28  ? 130 THR A OG1 1 
ATOM   788   C CG2 . THR A 1 101 ? 48.353  -11.892 10.029  1.00 36.84  ? 130 THR A CG2 1 
ATOM   789   N N   . GLU A 1 102 ? 45.600  -14.826 12.007  1.00 41.69  ? 131 GLU A N   1 
ATOM   790   C CA  . GLU A 1 102 ? 45.172  -15.587 13.174  1.00 42.57  ? 131 GLU A CA  1 
ATOM   791   C C   . GLU A 1 102 ? 45.864  -15.096 14.451  1.00 37.32  ? 131 GLU A C   1 
ATOM   792   O O   . GLU A 1 102 ? 45.273  -15.214 15.516  1.00 38.99  ? 131 GLU A O   1 
ATOM   793   C CB  . GLU A 1 102 ? 45.471  -17.093 13.104  1.00 53.48  ? 131 GLU A CB  1 
ATOM   794   C CG  . GLU A 1 102 ? 44.347  -17.957 12.528  1.00 62.79  ? 131 GLU A CG  1 
ATOM   795   C CD  . GLU A 1 102 ? 44.236  -17.971 11.007  1.00 76.60  ? 131 GLU A CD  1 
ATOM   796   O OE1 . GLU A 1 102 ? 45.088  -17.352 10.318  1.00 81.24  ? 131 GLU A OE1 1 
ATOM   797   O OE2 . GLU A 1 102 ? 43.277  -18.605 10.507  1.00 82.43  ? 131 GLU A OE2 1 
ATOM   798   N N   . GLU A 1 103 ? 47.144  -14.676 14.383  1.00 33.31  ? 132 GLU A N   1 
ATOM   799   C CA  . GLU A 1 103 ? 47.866  -14.251 15.580  1.00 35.97  ? 132 GLU A CA  1 
ATOM   800   C C   . GLU A 1 103 ? 47.220  -12.964 16.136  1.00 32.66  ? 132 GLU A C   1 
ATOM   801   O O   . GLU A 1 103 ? 47.020  -12.796 17.336  1.00 34.66  ? 132 GLU A O   1 
ATOM   802   C CB  . GLU A 1 103 ? 49.360  -14.055 15.307  1.00 39.80  ? 132 GLU A CB  1 
ATOM   803   C CG  . GLU A 1 103 ? 50.117  -15.313 14.872  1.00 51.16  ? 132 GLU A CG  1 
ATOM   804   C CD  . GLU A 1 103 ? 49.642  -16.098 13.639  1.00 56.79  ? 132 GLU A CD  1 
ATOM   805   O OE1 . GLU A 1 103 ? 49.448  -15.547 12.515  1.00 48.58  ? 132 GLU A OE1 1 
ATOM   806   O OE2 . GLU A 1 103 ? 49.473  -17.331 13.823  1.00 68.62  ? 132 GLU A OE2 1 
ATOM   807   N N   . GLN A 1 104 ? 46.902  -12.046 15.236  1.00 32.34  ? 133 GLN A N   1 
ATOM   808   C CA  . GLN A 1 104 ? 46.287  -10.775 15.591  1.00 34.25  ? 133 GLN A CA  1 
ATOM   809   C C   . GLN A 1 104 ? 44.932  -10.998 16.245  1.00 30.36  ? 133 GLN A C   1 
ATOM   810   O O   . GLN A 1 104 ? 44.608  -10.371 17.247  1.00 31.74  ? 133 GLN A O   1 
ATOM   811   C CB  . GLN A 1 104 ? 46.181  -9.937  14.317  1.00 33.31  ? 133 GLN A CB  1 
ATOM   812   C CG  . GLN A 1 104 ? 47.535  -9.425  13.834  1.00 31.74  ? 133 GLN A CG  1 
ATOM   813   C CD  . GLN A 1 104 ? 47.433  -8.656  12.536  1.00 32.83  ? 133 GLN A CD  1 
ATOM   814   O OE1 . GLN A 1 104 ? 46.534  -8.869  11.706  1.00 35.14  ? 133 GLN A OE1 1 
ATOM   815   N NE2 . GLN A 1 104 ? 48.358  -7.729  12.352  1.00 36.26  ? 133 GLN A NE2 1 
ATOM   816   N N   . VAL A 1 105 ? 44.132  -11.918 15.695  1.00 32.28  ? 134 VAL A N   1 
ATOM   817   C CA  . VAL A 1 105 ? 42.862  -12.222 16.313  1.00 29.07  ? 134 VAL A CA  1 
ATOM   818   C C   . VAL A 1 105 ? 43.101  -12.866 17.676  1.00 32.83  ? 134 VAL A C   1 
ATOM   819   O O   . VAL A 1 105 ? 42.406  -12.540 18.642  1.00 34.13  ? 134 VAL A O   1 
ATOM   820   C CB  . VAL A 1 105 ? 42.010  -13.076 15.363  1.00 35.54  ? 134 VAL A CB  1 
ATOM   821   C CG1 . VAL A 1 105 ? 40.857  -13.756 16.077  1.00 32.34  ? 134 VAL A CG1 1 
ATOM   822   C CG2 . VAL A 1 105 ? 41.509  -12.239 14.187  1.00 35.48  ? 134 VAL A CG2 1 
ATOM   823   N N   . SER A 1 106 ? 44.088  -13.776 17.764  1.00 35.56  ? 135 SER A N   1 
ATOM   824   C CA  A SER A 1 106 ? 44.398  -14.434 19.028  0.50 38.69  ? 135 SER A CA  1 
ATOM   825   C CA  B SER A 1 106 ? 44.427  -14.435 19.027  0.50 37.65  ? 135 SER A CA  1 
ATOM   826   C C   . SER A 1 106 ? 44.825  -13.407 20.077  1.00 33.85  ? 135 SER A C   1 
ATOM   827   O O   . SER A 1 106 ? 44.434  -13.485 21.229  1.00 31.96  ? 135 SER A O   1 
ATOM   828   C CB  A SER A 1 106 ? 45.459  -15.501 18.850  0.50 38.98  ? 135 SER A CB  1 
ATOM   829   C CB  B SER A 1 106 ? 45.564  -15.428 18.887  0.50 36.63  ? 135 SER A CB  1 
ATOM   830   O OG  A SER A 1 106 ? 45.943  -15.929 20.112  0.50 41.39  ? 135 SER A OG  1 
ATOM   831   O OG  B SER A 1 106 ? 45.278  -16.409 17.910  0.50 35.73  ? 135 SER A OG  1 
ATOM   832   N N   . TRP A 1 107 ? 45.665  -12.466 19.676  1.00 36.93  ? 136 TRP A N   1 
ATOM   833   C CA  . TRP A 1 107 ? 46.083  -11.402 20.564  1.00 37.63  ? 136 TRP A CA  1 
ATOM   834   C C   . TRP A 1 107 ? 44.876  -10.593 21.061  1.00 34.01  ? 136 TRP A C   1 
ATOM   835   O O   . TRP A 1 107 ? 44.774  -10.277 22.240  1.00 30.52  ? 136 TRP A O   1 
ATOM   836   C CB  . TRP A 1 107 ? 47.088  -10.511 19.823  1.00 37.03  ? 136 TRP A CB  1 
ATOM   837   C CG  . TRP A 1 107 ? 47.502  -9.336  20.656  1.00 42.04  ? 136 TRP A CG  1 
ATOM   838   C CD1 . TRP A 1 107 ? 48.499  -9.274  21.585  1.00 45.11  ? 136 TRP A CD1 1 
ATOM   839   C CD2 . TRP A 1 107 ? 46.870  -8.038  20.646  1.00 39.62  ? 136 TRP A CD2 1 
ATOM   840   N NE1 . TRP A 1 107 ? 48.554  -8.016  22.131  1.00 44.10  ? 136 TRP A NE1 1 
ATOM   841   C CE2 . TRP A 1 107 ? 47.557  -7.247  21.594  1.00 41.27  ? 136 TRP A CE2 1 
ATOM   842   C CE3 . TRP A 1 107 ? 45.794  -7.484  19.937  1.00 35.40  ? 136 TRP A CE3 1 
ATOM   843   C CZ2 . TRP A 1 107 ? 47.203  -5.923  21.841  1.00 43.00  ? 136 TRP A CZ2 1 
ATOM   844   C CZ3 . TRP A 1 107 ? 45.434  -6.182  20.196  1.00 40.55  ? 136 TRP A CZ3 1 
ATOM   845   C CH2 . TRP A 1 107 ? 46.140  -5.412  21.131  1.00 41.39  ? 136 TRP A CH2 1 
ATOM   846   N N   . LEU A 1 108 ? 43.949  -10.266 20.161  1.00 31.82  ? 137 LEU A N   1 
ATOM   847   C CA  . LEU A 1 108 ? 42.796  -9.461  20.536  1.00 34.72  ? 137 LEU A CA  1 
ATOM   848   C C   . LEU A 1 108 ? 41.873  -10.215 21.502  1.00 31.50  ? 137 LEU A C   1 
ATOM   849   O O   . LEU A 1 108 ? 41.381  -9.670  22.491  1.00 29.83  ? 137 LEU A O   1 
ATOM   850   C CB  . LEU A 1 108 ? 42.116  -9.030  19.241  1.00 35.73  ? 137 LEU A CB  1 
ATOM   851   C CG  . LEU A 1 108 ? 40.982  -8.015  19.382  1.00 36.17  ? 137 LEU A CG  1 
ATOM   852   C CD1 . LEU A 1 108 ? 41.381  -6.777  20.168  1.00 37.85  ? 137 LEU A CD1 1 
ATOM   853   C CD2 . LEU A 1 108 ? 40.542  -7.649  18.007  1.00 32.08  ? 137 LEU A CD2 1 
ATOM   854   N N   . SER A 1 109 ? 41.640  -11.502 21.256  1.00 35.45  ? 138 SER A N   1 
ATOM   855   C CA  . SER A 1 109 ? 40.920  -12.323 22.224  1.00 32.87  ? 138 SER A CA  1 
ATOM   856   C C   . SER A 1 109 ? 41.517  -12.187 23.615  1.00 36.10  ? 138 SER A C   1 
ATOM   857   O O   . SER A 1 109 ? 40.776  -11.986 24.590  1.00 31.99  ? 138 SER A O   1 
ATOM   858   C CB  . SER A 1 109 ? 40.890  -13.766 21.838  1.00 34.60  ? 138 SER A CB  1 
ATOM   859   O OG  . SER A 1 109 ? 40.075  -13.959 20.703  1.00 34.13  ? 138 SER A OG  1 
ATOM   860   N N   . LYS A 1 110 ? 42.847  -12.313 23.728  1.00 36.98  ? 139 LYS A N   1 
ATOM   861   C CA  . LYS A 1 110 ? 43.475  -12.294 25.049  1.00 38.40  ? 139 LYS A CA  1 
ATOM   862   C C   . LYS A 1 110 ? 43.294  -10.917 25.692  1.00 36.17  ? 139 LYS A C   1 
ATOM   863   O O   . LYS A 1 110 ? 43.070  -10.816 26.887  1.00 33.46  ? 139 LYS A O   1 
ATOM   864   C CB  . LYS A 1 110 ? 44.944  -12.719 24.989  1.00 42.59  ? 139 LYS A CB  1 
ATOM   865   C CG  . LYS A 1 110 ? 45.133  -14.202 24.765  1.00 48.26  ? 139 LYS A CG  1 
ATOM   866   C CD  . LYS A 1 110 ? 46.514  -14.632 24.269  1.00 53.95  ? 139 LYS A CD  1 
ATOM   867   C CE  . LYS A 1 110 ? 46.534  -16.038 23.714  1.00 61.99  ? 139 LYS A CE  1 
ATOM   868   N NZ  . LYS A 1 110 ? 45.438  -16.294 22.764  1.00 71.75  ? 139 LYS A NZ  1 
ATOM   869   N N   . GLU A 1 111 ? 43.385  -9.874  24.863  1.00 35.59  ? 140 GLU A N   1 
ATOM   870   C CA  . GLU A 1 111 ? 43.301  -8.480  25.263  1.00 35.00  ? 140 GLU A CA  1 
ATOM   871   C C   . GLU A 1 111 ? 41.947  -8.152  25.874  1.00 35.31  ? 140 GLU A C   1 
ATOM   872   O O   . GLU A 1 111 ? 41.921  -7.493  26.898  1.00 35.02  ? 140 GLU A O   1 
ATOM   873   C CB  . GLU A 1 111 ? 43.467  -7.551  24.062  1.00 39.96  ? 140 GLU A CB  1 
ATOM   874   C CG  . GLU A 1 111 ? 44.889  -7.059  23.858  1.00 43.46  ? 140 GLU A CG  1 
ATOM   875   C CD  . GLU A 1 111 ? 45.374  -6.217  25.034  1.00 59.33  ? 140 GLU A CD  1 
ATOM   876   O OE1 . GLU A 1 111 ? 44.734  -5.195  25.484  1.00 57.45  ? 140 GLU A OE1 1 
ATOM   877   O OE2 . GLU A 1 111 ? 46.462  -6.631  25.483  1.00 45.52  ? 140 GLU A OE2 1 
ATOM   878   N N   . TRP A 1 112 ? 40.844  -8.582  25.242  1.00 33.31  ? 141 TRP A N   1 
ATOM   879   C CA  . TRP A 1 112 ? 39.499  -8.424  25.797  1.00 31.46  ? 141 TRP A CA  1 
ATOM   880   C C   . TRP A 1 112 ? 39.243  -9.340  26.992  1.00 40.44  ? 141 TRP A C   1 
ATOM   881   O O   . TRP A 1 112 ? 38.463  -9.010  27.891  1.00 38.73  ? 141 TRP A O   1 
ATOM   882   C CB  . TRP A 1 112 ? 38.454  -8.694  24.706  1.00 32.06  ? 141 TRP A CB  1 
ATOM   883   C CG  . TRP A 1 112 ? 38.442  -7.639  23.621  1.00 27.36  ? 141 TRP A CG  1 
ATOM   884   C CD1 . TRP A 1 112 ? 39.040  -6.417  23.677  1.00 28.59  ? 141 TRP A CD1 1 
ATOM   885   C CD2 . TRP A 1 112 ? 37.766  -7.695  22.364  1.00 27.09  ? 141 TRP A CD2 1 
ATOM   886   N NE1 . TRP A 1 112 ? 38.814  -5.720  22.524  1.00 30.12  ? 141 TRP A NE1 1 
ATOM   887   C CE2 . TRP A 1 112 ? 38.024  -6.473  21.706  1.00 31.85  ? 141 TRP A CE2 1 
ATOM   888   C CE3 . TRP A 1 112 ? 36.973  -8.645  21.725  1.00 30.91  ? 141 TRP A CE3 1 
ATOM   889   C CZ2 . TRP A 1 112 ? 37.513  -6.181  20.454  1.00 26.07  ? 141 TRP A CZ2 1 
ATOM   890   C CZ3 . TRP A 1 112 ? 36.468  -8.353  20.482  1.00 29.52  ? 141 TRP A CZ3 1 
ATOM   891   C CH2 . TRP A 1 112 ? 36.740  -7.134  19.864  1.00 27.80  ? 141 TRP A CH2 1 
ATOM   892   N N   . ALA A 1 113 ? 39.837  -10.538 26.974  1.00 39.03  ? 142 ALA A N   1 
ATOM   893   C CA  . ALA A 1 113 ? 39.793  -11.403 28.145  1.00 41.36  ? 142 ALA A CA  1 
ATOM   894   C C   . ALA A 1 113 ? 40.379  -10.685 29.360  1.00 35.91  ? 142 ALA A C   1 
ATOM   895   O O   . ALA A 1 113 ? 39.756  -10.701 30.407  1.00 40.21  ? 142 ALA A O   1 
ATOM   896   C CB  . ALA A 1 113 ? 40.524  -12.698 27.878  1.00 44.46  ? 142 ALA A CB  1 
ATOM   897   N N   . LYS A 1 114 ? 41.539  -10.006 29.216  1.00 35.83  ? 143 LYS A N   1 
ATOM   898   C CA  . LYS A 1 114 ? 42.208  -9.406  30.368  1.00 39.03  ? 143 LYS A CA  1 
ATOM   899   C C   . LYS A 1 114 ? 41.464  -8.169  30.877  1.00 38.22  ? 143 LYS A C   1 
ATOM   900   O O   . LYS A 1 114 ? 41.689  -7.762  31.996  1.00 33.61  ? 143 LYS A O   1 
ATOM   901   C CB  . LYS A 1 114 ? 43.655  -8.986  30.097  1.00 44.36  ? 143 LYS A CB  1 
ATOM   902   C CG  . LYS A 1 114 ? 44.572  -10.168 29.814  1.00 60.95  ? 143 LYS A CG  1 
ATOM   903   C CD  . LYS A 1 114 ? 46.058  -9.854  29.648  1.00 68.85  ? 143 LYS A CD  1 
ATOM   904   C CE  . LYS A 1 114 ? 46.361  -8.857  28.574  1.00 73.16  ? 143 LYS A CE  1 
ATOM   905   N NZ  . LYS A 1 114 ? 47.806  -8.811  28.323  1.00 72.07  ? 143 LYS A NZ  1 
ATOM   906   N N   . ARG A 1 115 ? 40.592  -7.556  30.073  1.00 36.35  ? 144 ARG A N   1 
ATOM   907   C CA  . ARG A 1 115 ? 40.015  -6.270  30.446  1.00 33.23  ? 144 ARG A CA  1 
ATOM   908   C C   . ARG A 1 115 ? 38.608  -6.395  31.019  1.00 34.90  ? 144 ARG A C   1 
ATOM   909   O O   . ARG A 1 115 ? 38.025  -5.380  31.383  1.00 38.59  ? 144 ARG A O   1 
ATOM   910   C CB  . ARG A 1 115 ? 40.021  -5.398  29.190  1.00 33.74  ? 144 ARG A CB  1 
ATOM   911   C CG  . ARG A 1 115 ? 41.396  -4.949  28.725  1.00 33.65  ? 144 ARG A CG  1 
ATOM   912   C CD  . ARG A 1 115 ? 41.191  -4.180  27.447  1.00 32.35  ? 144 ARG A CD  1 
ATOM   913   N NE  . ARG A 1 115 ? 42.468  -3.672  26.934  1.00 37.21  ? 144 ARG A NE  1 
ATOM   914   C CZ  . ARG A 1 115 ? 42.868  -2.428  26.783  1.00 34.13  ? 144 ARG A CZ  1 
ATOM   915   N NH1 . ARG A 1 115 ? 42.172  -1.403  27.236  1.00 33.98  ? 144 ARG A NH1 1 
ATOM   916   N NH2 . ARG A 1 115 ? 44.032  -2.204  26.218  1.00 39.30  ? 144 ARG A NH2 1 
ATOM   917   N N   . ALA A 1 116 ? 38.090  -7.629  31.159  1.00 40.20  ? 145 ALA A N   1 
ATOM   918   C CA  . ALA A 1 116 ? 36.659  -7.896  31.281  1.00 42.22  ? 145 ALA A CA  1 
ATOM   919   C C   . ALA A 1 116 ? 36.061  -7.597  32.663  1.00 45.71  ? 145 ALA A C   1 
ATOM   920   O O   . ALA A 1 116 ? 34.857  -7.795  32.850  1.00 52.53  ? 145 ALA A O   1 
ATOM   921   C CB  . ALA A 1 116 ? 36.349  -9.340  30.903  1.00 37.74  ? 145 ALA A CB  1 
ATOM   922   N N   . ALA A 1 117 ? 36.838  -7.055  33.600  1.00 43.66  ? 146 ALA A N   1 
ATOM   923   C CA  . ALA A 1 117 ? 36.404  -6.957  34.986  1.00 44.05  ? 146 ALA A CA  1 
ATOM   924   C C   . ALA A 1 117 ? 35.346  -5.867  35.155  1.00 42.42  ? 146 ALA A C   1 
ATOM   925   O O   . ALA A 1 117 ? 35.409  -4.853  34.463  1.00 36.17  ? 146 ALA A O   1 
ATOM   926   C CB  . ALA A 1 117 ? 37.600  -6.708  35.863  1.00 44.27  ? 146 ALA A CB  1 
ATOM   927   N N   . LEU A 1 118 ? 34.324  -6.149  35.987  1.00 37.20  ? 147 LEU A N   1 
ATOM   928   C CA  . LEU A 1 118 ? 33.274  -5.181  36.311  1.00 37.34  ? 147 LEU A CA  1 
ATOM   929   C C   . LEU A 1 118 ? 33.534  -4.570  37.681  1.00 33.95  ? 147 LEU A C   1 
ATOM   930   O O   . LEU A 1 118 ? 33.854  -5.301  38.600  1.00 38.10  ? 147 LEU A O   1 
ATOM   931   C CB  . LEU A 1 118 ? 31.885  -5.807  36.320  1.00 34.87  ? 147 LEU A CB  1 
ATOM   932   C CG  . LEU A 1 118 ? 31.400  -6.363  34.988  1.00 34.06  ? 147 LEU A CG  1 
ATOM   933   C CD1 . LEU A 1 118 ? 29.950  -6.746  35.090  1.00 31.99  ? 147 LEU A CD1 1 
ATOM   934   C CD2 . LEU A 1 118 ? 31.617  -5.350  33.901  1.00 33.96  ? 147 LEU A CD2 1 
ATOM   935   N N   . PRO A 1 119 ? 33.367  -3.244  37.886  1.00 34.53  ? 148 PRO A N   1 
ATOM   936   C CA  . PRO A 1 119 ? 33.544  -2.655  39.211  1.00 31.99  ? 148 PRO A CA  1 
ATOM   937   C C   . PRO A 1 119 ? 32.303  -3.013  40.018  1.00 31.98  ? 148 PRO A C   1 
ATOM   938   O O   . PRO A 1 119 ? 31.254  -3.317  39.470  1.00 31.43  ? 148 PRO A O   1 
ATOM   939   C CB  . PRO A 1 119 ? 33.707  -1.150  38.969  1.00 34.15  ? 148 PRO A CB  1 
ATOM   940   C CG  . PRO A 1 119 ? 32.969  -0.932  37.665  1.00 33.70  ? 148 PRO A CG  1 
ATOM   941   C CD  . PRO A 1 119 ? 33.006  -2.240  36.872  1.00 32.32  ? 148 PRO A CD  1 
ATOM   942   N N   . SER A 1 120 ? 32.443  -2.983  41.334  1.00 29.97  ? 149 SER A N   1 
ATOM   943   C CA  . SER A 1 120 ? 31.456  -3.554  42.234  1.00 34.20  ? 149 SER A CA  1 
ATOM   944   C C   . SER A 1 120 ? 30.114  -2.812  42.133  1.00 32.32  ? 149 SER A C   1 
ATOM   945   O O   . SER A 1 120 ? 29.051  -3.412  42.207  1.00 32.19  ? 149 SER A O   1 
ATOM   946   C CB  . SER A 1 120 ? 32.037  -3.562  43.614  1.00 34.32  ? 149 SER A CB  1 
ATOM   947   O OG  . SER A 1 120 ? 32.155  -2.210  44.032  1.00 51.56  ? 149 SER A OG  1 
ATOM   948   N N   . HIS A 1 121 ? 30.113  -1.500  41.899  1.00 30.45  ? 150 HIS A N   1 
ATOM   949   C CA  . HIS A 1 121 ? 28.837  -0.801  41.872  1.00 30.39  ? 150 HIS A CA  1 
ATOM   950   C C   . HIS A 1 121 ? 27.986  -1.239  40.687  1.00 27.99  ? 150 HIS A C   1 
ATOM   951   O O   . HIS A 1 121 ? 26.776  -1.183  40.787  1.00 29.39  ? 150 HIS A O   1 
ATOM   952   C CB  . HIS A 1 121 ? 28.976  0.730   41.899  1.00 29.03  ? 150 HIS A CB  1 
ATOM   953   C CG  . HIS A 1 121 ? 29.475  1.366   40.649  1.00 29.26  ? 150 HIS A CG  1 
ATOM   954   N ND1 . HIS A 1 121 ? 30.806  1.309   40.309  1.00 33.16  ? 150 HIS A ND1 1 
ATOM   955   C CD2 . HIS A 1 121 ? 28.873  2.022   39.665  1.00 29.51  ? 150 HIS A CD2 1 
ATOM   956   C CE1 . HIS A 1 121 ? 30.984  1.948   39.159  1.00 33.91  ? 150 HIS A CE1 1 
ATOM   957   N NE2 . HIS A 1 121 ? 29.817  2.372   38.744  1.00 30.13  ? 150 HIS A NE2 1 
ATOM   958   N N   . VAL A 1 122 ? 28.617  -1.687  39.596  1.00 25.68  ? 151 VAL A N   1 
ATOM   959   C CA  . VAL A 1 122 ? 27.900  -2.062  38.393  1.00 29.98  ? 151 VAL A CA  1 
ATOM   960   C C   . VAL A 1 122 ? 27.308  -3.453  38.577  1.00 29.85  ? 151 VAL A C   1 
ATOM   961   O O   . VAL A 1 122 ? 26.171  -3.730  38.176  1.00 30.83  ? 151 VAL A O   1 
ATOM   962   C CB  . VAL A 1 122 ? 28.780  -1.979  37.128  1.00 31.03  ? 151 VAL A CB  1 
ATOM   963   C CG1 . VAL A 1 122 ? 28.047  -2.467  35.899  1.00 29.20  ? 151 VAL A CG1 1 
ATOM   964   C CG2 . VAL A 1 122 ? 29.266  -0.547  36.881  1.00 30.36  ? 151 VAL A CG2 1 
ATOM   965   N N   . VAL A 1 123 ? 28.074  -4.330  39.206  1.00 30.16  ? 152 VAL A N   1 
ATOM   966   C CA  . VAL A 1 123 ? 27.548  -5.651  39.520  1.00 31.76  ? 152 VAL A CA  1 
ATOM   967   C C   . VAL A 1 123 ? 26.286  -5.497  40.374  1.00 28.95  ? 152 VAL A C   1 
ATOM   968   O O   . VAL A 1 123 ? 25.267  -6.099  40.111  1.00 29.95  ? 152 VAL A O   1 
ATOM   969   C CB  . VAL A 1 123 ? 28.632  -6.484  40.226  1.00 34.34  ? 152 VAL A CB  1 
ATOM   970   C CG1 . VAL A 1 123 ? 28.087  -7.802  40.783  1.00 36.23  ? 152 VAL A CG1 1 
ATOM   971   C CG2 . VAL A 1 123 ? 29.818  -6.729  39.303  1.00 36.93  ? 152 VAL A CG2 1 
ATOM   972   N N   . THR A 1 124 ? 26.382  -4.666  41.408  1.00 29.77  ? 153 THR A N   1 
ATOM   973   C CA  . THR A 1 124 ? 25.341  -4.446  42.390  1.00 31.37  ? 153 THR A CA  1 
ATOM   974   C C   . THR A 1 124 ? 24.092  -3.859  41.749  1.00 29.77  ? 153 THR A C   1 
ATOM   975   O O   . THR A 1 124 ? 22.978  -4.235  42.078  1.00 30.26  ? 153 THR A O   1 
ATOM   976   C CB  . THR A 1 124 ? 25.946  -3.484  43.430  1.00 32.69  ? 153 THR A CB  1 
ATOM   977   O OG1 . THR A 1 124 ? 26.919  -4.258  44.115  1.00 33.97  ? 153 THR A OG1 1 
ATOM   978   C CG2 . THR A 1 124 ? 24.983  -2.998  44.491  1.00 33.95  ? 153 THR A CG2 1 
ATOM   979   N N   . MET A 1 125 ? 24.267  -2.824  40.913  1.00 32.09  ? 154 MET A N   1 
ATOM   980   C CA  . MET A 1 125 ? 23.150  -2.231  40.198  1.00 31.98  ? 154 MET A CA  1 
ATOM   981   C C   . MET A 1 125 ? 22.382  -3.312  39.428  1.00 28.26  ? 154 MET A C   1 
ATOM   982   O O   . MET A 1 125 ? 21.159  -3.351  39.421  1.00 28.07  ? 154 MET A O   1 
ATOM   983   C CB  . MET A 1 125 ? 23.705  -1.169  39.226  1.00 34.37  ? 154 MET A CB  1 
ATOM   984   C CG  . MET A 1 125 ? 22.677  -0.525  38.307  1.00 40.78  ? 154 MET A CG  1 
ATOM   985   S SD  . MET A 1 125 ? 23.321  0.804   37.256  1.00 43.99  ? 154 MET A SD  1 
ATOM   986   C CE  . MET A 1 125 ? 24.959  0.102   37.179  1.00 32.33  ? 154 MET A CE  1 
ATOM   987   N N   . LEU A 1 126 ? 23.097  -4.198  38.749  1.00 29.93  ? 155 LEU A N   1 
ATOM   988   C CA  . LEU A 1 126 ? 22.446  -5.214  37.936  1.00 30.87  ? 155 LEU A CA  1 
ATOM   989   C C   . LEU A 1 126 ? 21.677  -6.198  38.809  1.00 34.41  ? 155 LEU A C   1 
ATOM   990   O O   . LEU A 1 126 ? 20.541  -6.558  38.497  1.00 34.22  ? 155 LEU A O   1 
ATOM   991   C CB  . LEU A 1 126 ? 23.497  -5.930  37.118  1.00 29.66  ? 155 LEU A CB  1 
ATOM   992   C CG  . LEU A 1 126 ? 24.114  -5.114  35.978  1.00 31.41  ? 155 LEU A CG  1 
ATOM   993   C CD1 . LEU A 1 126 ? 25.438  -5.714  35.500  1.00 29.58  ? 155 LEU A CD1 1 
ATOM   994   C CD2 . LEU A 1 126 ? 23.099  -5.049  34.861  1.00 37.99  ? 155 LEU A CD2 1 
ATOM   995   N N   . ASP A 1 127 ? 22.311  -6.604  39.905  1.00 32.43  ? 156 ASP A N   1 
ATOM   996   C CA  . ASP A 1 127 ? 21.708  -7.525  40.852  1.00 34.26  ? 156 ASP A CA  1 
ATOM   997   C C   . ASP A 1 127 ? 20.468  -6.919  41.510  1.00 34.88  ? 156 ASP A C   1 
ATOM   998   O O   . ASP A 1 127 ? 19.608  -7.665  41.931  1.00 41.38  ? 156 ASP A O   1 
ATOM   999   C CB  . ASP A 1 127 ? 22.769  -8.046  41.811  1.00 32.08  ? 156 ASP A CB  1 
ATOM   1000  C CG  . ASP A 1 127 ? 23.819  -8.973  41.194  1.00 30.78  ? 156 ASP A CG  1 
ATOM   1001  O OD1 . ASP A 1 127 ? 23.640  -9.428  40.041  1.00 37.49  ? 156 ASP A OD1 1 
ATOM   1002  O OD2 . ASP A 1 127 ? 24.842  -9.225  41.855  1.00 40.38  ? 156 ASP A OD2 1 
ATOM   1003  N N   . ASN A 1 128 ? 20.296  -5.588  41.512  1.00 38.93  ? 157 ASN A N   1 
ATOM   1004  C CA  . ASN A 1 128 ? 19.161  -4.970  42.194  1.00 39.74  ? 157 ASN A CA  1 
ATOM   1005  C C   . ASN A 1 128 ? 18.035  -4.563  41.239  1.00 40.03  ? 157 ASN A C   1 
ATOM   1006  O O   . ASN A 1 128 ? 16.938  -4.257  41.680  1.00 40.13  ? 157 ASN A O   1 
ATOM   1007  C CB  . ASN A 1 128 ? 19.584  -3.761  43.023  1.00 40.92  ? 157 ASN A CB  1 
ATOM   1008  C CG  . ASN A 1 128 ? 20.419  -4.169  44.213  1.00 44.37  ? 157 ASN A CG  1 
ATOM   1009  O OD1 . ASN A 1 128 ? 20.317  -5.317  44.654  1.00 40.90  ? 157 ASN A OD1 1 
ATOM   1010  N ND2 . ASN A 1 128 ? 21.267  -3.274  44.712  1.00 44.39  ? 157 ASN A ND2 1 
ATOM   1011  N N   . PHE A 1 129 ? 18.306  -4.539  39.941  1.00 37.06  ? 158 PHE A N   1 
ATOM   1012  C CA  . PHE A 1 129 ? 17.309  -4.170  38.953  1.00 37.69  ? 158 PHE A CA  1 
ATOM   1013  C C   . PHE A 1 129 ? 16.129  -5.129  39.025  1.00 36.16  ? 158 PHE A C   1 
ATOM   1014  O O   . PHE A 1 129 ? 16.330  -6.337  39.024  1.00 37.67  ? 158 PHE A O   1 
ATOM   1015  C CB  . PHE A 1 129 ? 17.893  -4.247  37.544  1.00 34.82  ? 158 PHE A CB  1 
ATOM   1016  C CG  . PHE A 1 129 ? 18.677  -3.019  37.092  1.00 31.79  ? 158 PHE A CG  1 
ATOM   1017  C CD1 . PHE A 1 129 ? 18.347  -1.746  37.522  1.00 31.25  ? 158 PHE A CD1 1 
ATOM   1018  C CD2 . PHE A 1 129 ? 19.717  -3.153  36.187  1.00 32.28  ? 158 PHE A CD2 1 
ATOM   1019  C CE1 . PHE A 1 129 ? 19.053  -0.636  37.060  1.00 28.93  ? 158 PHE A CE1 1 
ATOM   1020  C CE2 . PHE A 1 129 ? 20.424  -2.039  35.739  1.00 29.98  ? 158 PHE A CE2 1 
ATOM   1021  C CZ  . PHE A 1 129 ? 20.076  -0.797  36.168  1.00 27.48  ? 158 PHE A CZ  1 
ATOM   1022  N N   . PRO A 1 130 ? 14.879  -4.621  39.005  1.00 39.55  ? 159 PRO A N   1 
ATOM   1023  C CA  . PRO A 1 130 ? 13.697  -5.473  39.130  1.00 38.32  ? 159 PRO A CA  1 
ATOM   1024  C C   . PRO A 1 130 ? 13.486  -6.195  37.813  1.00 41.00  ? 159 PRO A C   1 
ATOM   1025  O O   . PRO A 1 130 ? 14.057  -5.798  36.795  1.00 38.89  ? 159 PRO A O   1 
ATOM   1026  C CB  . PRO A 1 130 ? 12.568  -4.504  39.467  1.00 34.83  ? 159 PRO A CB  1 
ATOM   1027  C CG  . PRO A 1 130 ? 12.986  -3.222  38.748  1.00 37.70  ? 159 PRO A CG  1 
ATOM   1028  C CD  . PRO A 1 130 ? 14.519  -3.210  38.772  1.00 38.94  ? 159 PRO A CD  1 
ATOM   1029  N N   . THR A 1 131 ? 12.607  -7.197  37.855  1.00 42.30  ? 160 THR A N   1 
ATOM   1030  C CA  . THR A 1 131 ? 12.290  -8.050  36.723  1.00 42.31  ? 160 THR A CA  1 
ATOM   1031  C C   . THR A 1 131 ? 11.540  -7.281  35.645  1.00 36.27  ? 160 THR A C   1 
ATOM   1032  O O   . THR A 1 131 ? 11.560  -7.699  34.485  1.00 37.85  ? 160 THR A O   1 
ATOM   1033  C CB  . THR A 1 131 ? 11.452  -9.241  37.192  1.00 48.70  ? 160 THR A CB  1 
ATOM   1034  O OG1 . THR A 1 131 ? 10.290  -8.639  37.758  1.00 54.24  ? 160 THR A OG1 1 
ATOM   1035  C CG2 . THR A 1 131 ? 12.196  -10.104 38.195  1.00 50.80  ? 160 THR A CG2 1 
ATOM   1036  N N   . ASN A 1 132 ? 10.883  -6.168  35.998  1.00 30.89  ? 161 ASN A N   1 
ATOM   1037  C CA  . ASN A 1 132 ? 10.040  -5.475  35.028  1.00 33.29  ? 161 ASN A CA  1 
ATOM   1038  C C   . ASN A 1 132 ? 10.842  -4.447  34.228  1.00 39.12  ? 161 ASN A C   1 
ATOM   1039  O O   . ASN A 1 132 ? 10.279  -3.834  33.317  1.00 39.06  ? 161 ASN A O   1 
ATOM   1040  C CB  . ASN A 1 132 ? 8.817   -4.807  35.669  1.00 35.79  ? 161 ASN A CB  1 
ATOM   1041  C CG  . ASN A 1 132 ? 9.167   -3.811  36.745  1.00 36.27  ? 161 ASN A CG  1 
ATOM   1042  O OD1 . ASN A 1 132 ? 10.081  -4.047  37.528  1.00 38.82  ? 161 ASN A OD1 1 
ATOM   1043  N ND2 . ASN A 1 132 ? 8.469   -2.686  36.812  1.00 46.55  ? 161 ASN A ND2 1 
ATOM   1044  N N   . LEU A 1 133 ? 12.125  -4.233  34.599  1.00 36.07  ? 162 LEU A N   1 
ATOM   1045  C CA  . LEU A 1 133 ? 12.997  -3.366  33.826  1.00 28.29  ? 162 LEU A CA  1 
ATOM   1046  C C   . LEU A 1 133 ? 13.576  -4.104  32.612  1.00 28.05  ? 162 LEU A C   1 
ATOM   1047  O O   . LEU A 1 133 ? 14.391  -4.999  32.749  1.00 25.01  ? 162 LEU A O   1 
ATOM   1048  C CB  . LEU A 1 133 ? 14.086  -2.760  34.685  1.00 28.91  ? 162 LEU A CB  1 
ATOM   1049  C CG  . LEU A 1 133 ? 14.940  -1.711  33.965  1.00 28.39  ? 162 LEU A CG  1 
ATOM   1050  C CD1 . LEU A 1 133 ? 14.061  -0.548  33.563  1.00 33.96  ? 162 LEU A CD1 1 
ATOM   1051  C CD2 . LEU A 1 133 ? 16.053  -1.267  34.880  1.00 30.95  ? 162 LEU A CD2 1 
ATOM   1052  N N   . HIS A 1 134 ? 13.161  -3.650  31.421  1.00 27.32  ? 163 HIS A N   1 
ATOM   1053  C CA  . HIS A 1 134 ? 13.543  -4.226  30.148  1.00 29.35  ? 163 HIS A CA  1 
ATOM   1054  C C   . HIS A 1 134 ? 15.043  -4.506  30.138  1.00 25.98  ? 163 HIS A C   1 
ATOM   1055  O O   . HIS A 1 134 ? 15.848  -3.731  30.648  1.00 26.12  ? 163 HIS A O   1 
ATOM   1056  C CB  . HIS A 1 134 ? 13.095  -3.286  29.021  1.00 31.30  ? 163 HIS A CB  1 
ATOM   1057  C CG  . HIS A 1 134 ? 13.172  -3.933  27.691  1.00 33.96  ? 163 HIS A CG  1 
ATOM   1058  N ND1 . HIS A 1 134 ? 14.362  -4.160  27.024  1.00 43.12  ? 163 HIS A ND1 1 
ATOM   1059  C CD2 . HIS A 1 134 ? 12.210  -4.515  26.965  1.00 38.41  ? 163 HIS A CD2 1 
ATOM   1060  C CE1 . HIS A 1 134 ? 14.126  -4.838  25.902  1.00 40.44  ? 163 HIS A CE1 1 
ATOM   1061  N NE2 . HIS A 1 134 ? 12.815  -5.062  25.845  1.00 44.56  ? 163 HIS A NE2 1 
ATOM   1062  N N   . PRO A 1 135 ? 15.510  -5.630  29.565  1.00 28.32  ? 164 PRO A N   1 
ATOM   1063  C CA  . PRO A 1 135 ? 16.946  -5.887  29.496  1.00 27.93  ? 164 PRO A CA  1 
ATOM   1064  C C   . PRO A 1 135 ? 17.761  -4.789  28.792  1.00 28.41  ? 164 PRO A C   1 
ATOM   1065  O O   . PRO A 1 135 ? 18.887  -4.529  29.210  1.00 32.34  ? 164 PRO A O   1 
ATOM   1066  C CB  . PRO A 1 135 ? 17.100  -7.223  28.773  1.00 31.36  ? 164 PRO A CB  1 
ATOM   1067  C CG  . PRO A 1 135 ? 15.703  -7.679  28.464  1.00 28.50  ? 164 PRO A CG  1 
ATOM   1068  C CD  . PRO A 1 135 ? 14.698  -6.742  29.074  1.00 30.00  ? 164 PRO A CD  1 
ATOM   1069  N N   . MET A 1 136 ? 17.188  -4.129  27.778  1.00 27.54  ? 165 MET A N   1 
ATOM   1070  C CA  . MET A 1 136 ? 17.909  -3.080  27.048  1.00 28.60  ? 165 MET A CA  1 
ATOM   1071  C C   . MET A 1 136 ? 18.106  -1.822  27.901  1.00 24.82  ? 165 MET A C   1 
ATOM   1072  O O   . MET A 1 136 ? 19.115  -1.132  27.759  1.00 27.39  ? 165 MET A O   1 
ATOM   1073  C CB  . MET A 1 136 ? 17.196  -2.710  25.749  1.00 25.12  ? 165 MET A CB  1 
ATOM   1074  C CG  . MET A 1 136 ? 17.491  -3.703  24.644  1.00 28.69  ? 165 MET A CG  1 
ATOM   1075  S SD  . MET A 1 136 ? 19.232  -3.655  24.179  1.00 34.42  ? 165 MET A SD  1 
ATOM   1076  C CE  . MET A 1 136 ? 19.471  -2.014  23.480  1.00 39.85  ? 165 MET A CE  1 
ATOM   1077  N N   . SER A 1 137 ? 17.136  -1.510  28.756  1.00 23.97  ? 166 SER A N   1 
ATOM   1078  C CA  . SER A 1 137 ? 17.274  -0.437  29.717  1.00 26.12  ? 166 SER A CA  1 
ATOM   1079  C C   . SER A 1 137 ? 18.365  -0.775  30.720  1.00 26.77  ? 166 SER A C   1 
ATOM   1080  O O   . SER A 1 137 ? 19.169  0.073   31.116  1.00 26.75  ? 166 SER A O   1 
ATOM   1081  C CB  . SER A 1 137 ? 15.979  -0.185  30.441  1.00 29.90  ? 166 SER A CB  1 
ATOM   1082  O OG  . SER A 1 137 ? 14.917  0.015   29.540  1.00 30.28  ? 166 SER A OG  1 
ATOM   1083  N N   . GLN A 1 138 ? 18.344  -2.024  31.174  1.00 31.19  ? 167 GLN A N   1 
ATOM   1084  C CA  . GLN A 1 138 ? 19.368  -2.549  32.060  1.00 29.65  ? 167 GLN A CA  1 
ATOM   1085  C C   . GLN A 1 138 ? 20.747  -2.356  31.441  1.00 30.15  ? 167 GLN A C   1 
ATOM   1086  O O   . GLN A 1 138 ? 21.670  -1.949  32.117  1.00 23.82  ? 167 GLN A O   1 
ATOM   1087  C CB  . GLN A 1 138 ? 19.101  -4.025  32.390  1.00 33.72  ? 167 GLN A CB  1 
ATOM   1088  C CG  . GLN A 1 138 ? 18.136  -4.212  33.569  1.00 37.54  ? 167 GLN A CG  1 
ATOM   1089  C CD  . GLN A 1 138 ? 17.978  -5.644  34.052  1.00 35.42  ? 167 GLN A CD  1 
ATOM   1090  O OE1 . GLN A 1 138 ? 16.857  -6.160  34.181  1.00 37.26  ? 167 GLN A OE1 1 
ATOM   1091  N NE2 . GLN A 1 138 ? 19.083  -6.261  34.423  1.00 39.35  ? 167 GLN A NE2 1 
ATOM   1092  N N   . LEU A 1 139 ? 20.906  -2.758  30.181  1.00 28.77  ? 168 LEU A N   1 
ATOM   1093  C CA  . LEU A 1 139 ? 22.180  -2.644  29.494  1.00 28.32  ? 168 LEU A CA  1 
ATOM   1094  C C   . LEU A 1 139 ? 22.582  -1.171  29.437  1.00 26.84  ? 168 LEU A C   1 
ATOM   1095  O O   . LEU A 1 139 ? 23.687  -0.817  29.852  1.00 26.68  ? 168 LEU A O   1 
ATOM   1096  C CB  . LEU A 1 139 ? 22.007  -3.284  28.117  1.00 29.40  ? 168 LEU A CB  1 
ATOM   1097  C CG  . LEU A 1 139 ? 23.180  -3.112  27.165  1.00 28.22  ? 168 LEU A CG  1 
ATOM   1098  C CD1 . LEU A 1 139 ? 24.276  -4.007  27.630  1.00 30.56  ? 168 LEU A CD1 1 
ATOM   1099  C CD2 . LEU A 1 139 ? 22.769  -3.366  25.761  1.00 27.06  ? 168 LEU A CD2 1 
ATOM   1100  N N   . SER A 1 140 ? 21.647  -0.288  29.060  1.00 30.29  ? 169 SER A N   1 
ATOM   1101  C CA  . SER A 1 140 ? 21.978  1.135   28.920  1.00 28.95  ? 169 SER A CA  1 
ATOM   1102  C C   . SER A 1 140 ? 22.448  1.775   30.242  1.00 26.63  ? 169 SER A C   1 
ATOM   1103  O O   . SER A 1 140 ? 23.507  2.418   30.318  1.00 23.63  ? 169 SER A O   1 
ATOM   1104  C CB  . SER A 1 140 ? 20.855  1.911   28.358  1.00 26.93  ? 169 SER A CB  1 
ATOM   1105  O OG  . SER A 1 140 ? 21.327  3.234   28.177  1.00 30.88  ? 169 SER A OG  1 
ATOM   1106  N N   . ALA A 1 141 ? 21.651  1.596   31.287  1.00 23.00  ? 170 ALA A N   1 
ATOM   1107  C CA  . ALA A 1 141 ? 21.981  2.086   32.612  1.00 26.15  ? 170 ALA A CA  1 
ATOM   1108  C C   . ALA A 1 141 ? 23.315  1.526   33.128  1.00 25.72  ? 170 ALA A C   1 
ATOM   1109  O O   . ALA A 1 141 ? 24.102  2.287   33.656  1.00 25.05  ? 170 ALA A O   1 
ATOM   1110  C CB  . ALA A 1 141 ? 20.878  1.776   33.572  1.00 23.80  ? 170 ALA A CB  1 
ATOM   1111  N N   . ALA A 1 142 ? 23.609  0.233   32.938  1.00 28.12  ? 171 ALA A N   1 
ATOM   1112  C CA  . ALA A 1 142 ? 24.876  -0.334  33.373  1.00 27.93  ? 171 ALA A CA  1 
ATOM   1113  C C   . ALA A 1 142 ? 26.069  0.267   32.618  1.00 30.90  ? 171 ALA A C   1 
ATOM   1114  O O   . ALA A 1 142 ? 27.156  0.477   33.159  1.00 28.52  ? 171 ALA A O   1 
ATOM   1115  C CB  . ALA A 1 142 ? 24.858  -1.837  33.164  1.00 30.96  ? 171 ALA A CB  1 
ATOM   1116  N N   . VAL A 1 143 ? 25.909  0.470   31.327  1.00 25.67  ? 172 VAL A N   1 
ATOM   1117  C CA  . VAL A 1 143 ? 27.013  1.017   30.569  1.00 28.50  ? 172 VAL A CA  1 
ATOM   1118  C C   . VAL A 1 143 ? 27.265  2.450   30.999  1.00 24.18  ? 172 VAL A C   1 
ATOM   1119  O O   . VAL A 1 143 ? 28.408  2.822   31.187  1.00 28.95  ? 172 VAL A O   1 
ATOM   1120  C CB  . VAL A 1 143 ? 26.850  0.880   29.058  1.00 27.48  ? 172 VAL A CB  1 
ATOM   1121  C CG1 . VAL A 1 143 ? 27.963  1.635   28.356  1.00 28.03  ? 172 VAL A CG1 1 
ATOM   1122  C CG2 . VAL A 1 143 ? 26.857  -0.600  28.670  1.00 29.12  ? 172 VAL A CG2 1 
ATOM   1123  N N   . THR A 1 144 ? 26.202  3.212   31.227  1.00 26.62  ? 173 THR A N   1 
ATOM   1124  C CA  . THR A 1 144 ? 26.329  4.596   31.652  1.00 26.25  ? 173 THR A CA  1 
ATOM   1125  C C   . THR A 1 144 ? 27.066  4.627   32.989  1.00 26.69  ? 173 THR A C   1 
ATOM   1126  O O   . THR A 1 144 ? 27.999  5.398   33.146  1.00 22.11  ? 173 THR A O   1 
ATOM   1127  C CB  . THR A 1 144 ? 24.958  5.272   31.714  1.00 28.57  ? 173 THR A CB  1 
ATOM   1128  O OG1 . THR A 1 144 ? 24.597  5.468   30.353  1.00 30.81  ? 173 THR A OG1 1 
ATOM   1129  C CG2 . THR A 1 144 ? 24.972  6.607   32.436  1.00 24.41  ? 173 THR A CG2 1 
ATOM   1130  N N   . ALA A 1 145 ? 26.711  3.711   33.894  1.00 23.14  ? 174 ALA A N   1 
ATOM   1131  C CA  . ALA A 1 145 ? 27.348  3.608   35.186  1.00 24.32  ? 174 ALA A CA  1 
ATOM   1132  C C   . ALA A 1 145 ? 28.808  3.183   35.127  1.00 24.49  ? 174 ALA A C   1 
ATOM   1133  O O   . ALA A 1 145 ? 29.563  3.547   36.015  1.00 27.36  ? 174 ALA A O   1 
ATOM   1134  C CB  . ALA A 1 145 ? 26.538  2.674   36.060  1.00 27.95  ? 174 ALA A CB  1 
ATOM   1135  N N   . LEU A 1 146 ? 29.216  2.404   34.114  1.00 28.37  ? 175 LEU A N   1 
ATOM   1136  C CA  . LEU A 1 146 ? 30.610  2.070   33.859  1.00 27.67  ? 175 LEU A CA  1 
ATOM   1137  C C   . LEU A 1 146 ? 31.462  3.290   33.478  1.00 30.54  ? 175 LEU A C   1 
ATOM   1138  O O   . LEU A 1 146 ? 32.681  3.188   33.391  1.00 27.79  ? 175 LEU A O   1 
ATOM   1139  C CB  . LEU A 1 146 ? 30.725  1.038   32.737  1.00 28.04  ? 175 LEU A CB  1 
ATOM   1140  C CG  . LEU A 1 146 ? 30.377  -0.395  33.091  1.00 26.81  ? 175 LEU A CG  1 
ATOM   1141  C CD1 . LEU A 1 146 ? 30.162  -1.235  31.859  1.00 32.13  ? 175 LEU A CD1 1 
ATOM   1142  C CD2 . LEU A 1 146 ? 31.528  -0.922  33.913  1.00 29.64  ? 175 LEU A CD2 1 
ATOM   1143  N N   . ASN A 1 147 ? 30.842  4.431   33.185  1.00 29.77  ? 176 ASN A N   1 
ATOM   1144  C CA  . ASN A 1 147 ? 31.589  5.601   32.754  1.00 29.61  ? 176 ASN A CA  1 
ATOM   1145  C C   . ASN A 1 147 ? 32.476  6.116   33.895  1.00 32.06  ? 176 ASN A C   1 
ATOM   1146  O O   . ASN A 1 147 ? 33.383  6.880   33.652  1.00 25.15  ? 176 ASN A O   1 
ATOM   1147  C CB  . ASN A 1 147 ? 30.664  6.624   32.108  1.00 32.71  ? 176 ASN A CB  1 
ATOM   1148  C CG  . ASN A 1 147 ? 30.797  7.966   32.759  1.00 36.20  ? 176 ASN A CG  1 
ATOM   1149  O OD1 . ASN A 1 147 ? 30.474  8.057   33.940  1.00 41.42  ? 176 ASN A OD1 1 
ATOM   1150  N ND2 . ASN A 1 147 ? 31.276  8.983   32.042  1.00 32.87  ? 176 ASN A ND2 1 
ATOM   1151  N N   . SER A 1 148 ? 32.309  5.589   35.117  1.00 28.58  ? 177 SER A N   1 
ATOM   1152  C CA  . SER A 1 148 ? 33.218  5.880   36.203  1.00 31.02  ? 177 SER A CA  1 
ATOM   1153  C C   . SER A 1 148 ? 34.614  5.328   35.899  1.00 33.78  ? 177 SER A C   1 
ATOM   1154  O O   . SER A 1 148 ? 35.577  5.786   36.488  1.00 34.13  ? 177 SER A O   1 
ATOM   1155  C CB  . SER A 1 148 ? 32.703  5.296   37.479  1.00 30.52  ? 177 SER A CB  1 
ATOM   1156  O OG  . SER A 1 148 ? 32.495  3.893   37.308  1.00 31.89  ? 177 SER A OG  1 
ATOM   1157  N N   . GLU A 1 149 ? 34.721  4.384   34.956  1.00 30.77  ? 178 GLU A N   1 
ATOM   1158  C CA  . GLU A 1 149 ? 36.002  3.826   34.565  1.00 36.12  ? 178 GLU A CA  1 
ATOM   1159  C C   . GLU A 1 149 ? 36.547  4.505   33.301  1.00 33.36  ? 178 GLU A C   1 
ATOM   1160  O O   . GLU A 1 149 ? 37.480  4.004   32.668  1.00 32.28  ? 178 GLU A O   1 
ATOM   1161  C CB  . GLU A 1 149 ? 35.775  2.327   34.356  1.00 42.35  ? 178 GLU A CB  1 
ATOM   1162  C CG  . GLU A 1 149 ? 34.927  1.676   35.457  1.00 49.21  ? 178 GLU A CG  1 
ATOM   1163  C CD  . GLU A 1 149 ? 35.377  1.815   36.915  1.00 54.19  ? 178 GLU A CD  1 
ATOM   1164  O OE1 . GLU A 1 149 ? 36.377  1.097   37.175  1.00 60.58  ? 178 GLU A OE1 1 
ATOM   1165  O OE2 . GLU A 1 149 ? 34.754  2.526   37.797  1.00 53.53  ? 178 GLU A OE2 1 
ATOM   1166  N N   . SER A 1 150 ? 35.948  5.620   32.885  1.00 28.14  ? 179 SER A N   1 
ATOM   1167  C CA  . SER A 1 150 ? 36.403  6.268   31.654  1.00 30.08  ? 179 SER A CA  1 
ATOM   1168  C C   . SER A 1 150 ? 37.749  6.957   31.868  1.00 27.87  ? 179 SER A C   1 
ATOM   1169  O O   . SER A 1 150 ? 37.856  7.900   32.628  1.00 26.43  ? 179 SER A O   1 
ATOM   1170  C CB  . SER A 1 150 ? 35.433  7.273   31.060  1.00 28.64  ? 179 SER A CB  1 
ATOM   1171  O OG  . SER A 1 150 ? 35.982  7.733   29.815  1.00 25.03  ? 179 SER A OG  1 
ATOM   1172  N N   . ASN A 1 151 ? 38.776  6.500   31.165  1.00 30.12  ? 180 ASN A N   1 
ATOM   1173  C CA  . ASN A 1 151 ? 40.047  7.206   31.152  1.00 33.06  ? 180 ASN A CA  1 
ATOM   1174  C C   . ASN A 1 151 ? 39.944  8.415   30.229  1.00 33.14  ? 180 ASN A C   1 
ATOM   1175  O O   . ASN A 1 151 ? 40.688  9.360   30.379  1.00 33.21  ? 180 ASN A O   1 
ATOM   1176  C CB  . ASN A 1 151 ? 41.185  6.316   30.666  1.00 40.30  ? 180 ASN A CB  1 
ATOM   1177  C CG  . ASN A 1 151 ? 41.421  5.177   31.622  1.00 47.47  ? 180 ASN A CG  1 
ATOM   1178  O OD1 . ASN A 1 151 ? 41.679  5.403   32.813  1.00 51.84  ? 180 ASN A OD1 1 
ATOM   1179  N ND2 . ASN A 1 151 ? 41.270  3.963   31.124  1.00 52.12  ? 180 ASN A ND2 1 
ATOM   1180  N N   . PHE A 1 152 ? 39.045  8.386   29.243  1.00 34.40  ? 181 PHE A N   1 
ATOM   1181  C CA  . PHE A 1 152 ? 38.930  9.534   28.346  1.00 31.76  ? 181 PHE A CA  1 
ATOM   1182  C C   . PHE A 1 152 ? 38.310  10.747  29.052  1.00 33.07  ? 181 PHE A C   1 
ATOM   1183  O O   . PHE A 1 152 ? 38.680  11.890  28.762  1.00 34.10  ? 181 PHE A O   1 
ATOM   1184  C CB  . PHE A 1 152 ? 38.109  9.247   27.097  1.00 27.64  ? 181 PHE A CB  1 
ATOM   1185  C CG  . PHE A 1 152 ? 37.927  10.487  26.251  1.00 29.22  ? 181 PHE A CG  1 
ATOM   1186  C CD1 . PHE A 1 152 ? 38.956  10.940  25.435  1.00 31.82  ? 181 PHE A CD1 1 
ATOM   1187  C CD2 . PHE A 1 152 ? 36.771  11.235  26.328  1.00 32.50  ? 181 PHE A CD2 1 
ATOM   1188  C CE1 . PHE A 1 152 ? 38.791  12.051  24.638  1.00 29.93  ? 181 PHE A CE1 1 
ATOM   1189  C CE2 . PHE A 1 152 ? 36.632  12.370  25.550  1.00 34.70  ? 181 PHE A CE2 1 
ATOM   1190  C CZ  . PHE A 1 152 ? 37.636  12.770  24.713  1.00 32.77  ? 181 PHE A CZ  1 
ATOM   1191  N N   . ALA A 1 153 ? 37.314  10.522  29.915  1.00 33.92  ? 182 ALA A N   1 
ATOM   1192  C CA  . ALA A 1 153 ? 36.696  11.632  30.633  1.00 31.66  ? 182 ALA A CA  1 
ATOM   1193  C C   . ALA A 1 153 ? 37.720  12.310  31.558  1.00 34.75  ? 182 ALA A C   1 
ATOM   1194  O O   . ALA A 1 153 ? 37.810  13.528  31.580  1.00 33.95  ? 182 ALA A O   1 
ATOM   1195  C CB  . ALA A 1 153 ? 35.464  11.127  31.379  1.00 32.34  ? 182 ALA A CB  1 
ATOM   1196  N N   . ARG A 1 154 ? 38.488  11.501  32.316  1.00 39.93  ? 183 ARG A N   1 
ATOM   1197  C CA  . ARG A 1 154 ? 39.508  11.965  33.245  1.00 45.25  ? 183 ARG A CA  1 
ATOM   1198  C C   . ARG A 1 154 ? 40.661  12.666  32.527  1.00 44.90  ? 183 ARG A C   1 
ATOM   1199  O O   . ARG A 1 154 ? 41.159  13.679  33.014  1.00 42.13  ? 183 ARG A O   1 
ATOM   1200  C CB  . ARG A 1 154 ? 40.116  10.834  34.081  1.00 52.02  ? 183 ARG A CB  1 
ATOM   1201  C CG  . ARG A 1 154 ? 39.190  10.347  35.187  1.00 63.50  ? 183 ARG A CG  1 
ATOM   1202  C CD  . ARG A 1 154 ? 39.901  9.543   36.280  1.00 73.72  ? 183 ARG A CD  1 
ATOM   1203  N NE  . ARG A 1 154 ? 40.267  8.154   35.963  1.00 86.33  ? 183 ARG A NE  1 
ATOM   1204  C CZ  . ARG A 1 154 ? 39.441  7.101   35.862  1.00 87.01  ? 183 ARG A CZ  1 
ATOM   1205  N NH1 . ARG A 1 154 ? 39.932  5.887   35.632  1.00 76.52  ? 183 ARG A NH1 1 
ATOM   1206  N NH2 . ARG A 1 154 ? 38.134  7.267   36.000  1.00 81.18  ? 183 ARG A NH2 1 
ATOM   1207  N N   . ALA A 1 155 ? 41.109  12.138  31.382  1.00 38.20  ? 184 ALA A N   1 
ATOM   1208  C CA  . ALA A 1 155 ? 42.193  12.784  30.642  1.00 36.30  ? 184 ALA A CA  1 
ATOM   1209  C C   . ALA A 1 155 ? 41.742  14.119  30.041  1.00 35.72  ? 184 ALA A C   1 
ATOM   1210  O O   . ALA A 1 155 ? 42.521  15.075  29.993  1.00 36.51  ? 184 ALA A O   1 
ATOM   1211  C CB  . ALA A 1 155 ? 42.732  11.877  29.554  1.00 32.97  ? 184 ALA A CB  1 
ATOM   1212  N N   . TYR A 1 156 ? 40.529  14.177  29.475  1.00 31.59  ? 185 TYR A N   1 
ATOM   1213  C CA  . TYR A 1 156 ? 40.066  15.435  28.913  1.00 36.32  ? 185 TYR A CA  1 
ATOM   1214  C C   . TYR A 1 156 ? 40.000  16.538  29.989  1.00 37.59  ? 185 TYR A C   1 
ATOM   1215  O O   . TYR A 1 156 ? 40.274  17.703  29.732  1.00 42.60  ? 185 TYR A O   1 
ATOM   1216  C CB  . TYR A 1 156 ? 38.697  15.250  28.262  1.00 38.02  ? 185 TYR A CB  1 
ATOM   1217  C CG  . TYR A 1 156 ? 38.197  16.524  27.612  1.00 37.82  ? 185 TYR A CG  1 
ATOM   1218  C CD1 . TYR A 1 156 ? 37.495  17.454  28.350  1.00 40.53  ? 185 TYR A CD1 1 
ATOM   1219  C CD2 . TYR A 1 156 ? 38.483  16.822  26.280  1.00 47.01  ? 185 TYR A CD2 1 
ATOM   1220  C CE1 . TYR A 1 156 ? 37.070  18.645  27.782  1.00 42.39  ? 185 TYR A CE1 1 
ATOM   1221  C CE2 . TYR A 1 156 ? 38.047  18.002  25.703  1.00 46.92  ? 185 TYR A CE2 1 
ATOM   1222  C CZ  . TYR A 1 156 ? 37.338  18.917  26.463  1.00 40.61  ? 185 TYR A CZ  1 
ATOM   1223  O OH  . TYR A 1 156 ? 36.874  20.080  25.924  1.00 45.61  ? 185 TYR A OH  1 
ATOM   1224  N N   . ALA A 1 157 ? 39.595  16.202  31.209  1.00 42.28  ? 186 ALA A N   1 
ATOM   1225  C CA  . ALA A 1 157 ? 39.523  17.208  32.268  1.00 47.91  ? 186 ALA A CA  1 
ATOM   1226  C C   . ALA A 1 157 ? 40.905  17.793  32.597  1.00 49.17  ? 186 ALA A C   1 
ATOM   1227  O O   . ALA A 1 157 ? 41.022  18.961  32.957  1.00 50.54  ? 186 ALA A O   1 
ATOM   1228  C CB  . ALA A 1 157 ? 38.858  16.607  33.489  1.00 49.64  ? 186 ALA A CB  1 
ATOM   1229  N N   . GLN A 1 158 ? 41.979  17.014  32.411  1.00 56.83  ? 187 GLN A N   1 
ATOM   1230  C CA  . GLN A 1 158 ? 43.328  17.502  32.663  1.00 48.46  ? 187 GLN A CA  1 
ATOM   1231  C C   . GLN A 1 158 ? 43.920  18.194  31.430  1.00 48.58  ? 187 GLN A C   1 
ATOM   1232  O O   . GLN A 1 158 ? 45.104  18.494  31.418  1.00 50.51  ? 187 GLN A O   1 
ATOM   1233  C CB  . GLN A 1 158 ? 44.195  16.332  33.117  1.00 52.85  ? 187 GLN A CB  1 
ATOM   1234  C CG  . GLN A 1 158 ? 43.691  15.642  34.379  1.00 52.50  ? 187 GLN A CG  1 
ATOM   1235  C CD  . GLN A 1 158 ? 44.520  14.428  34.731  1.00 68.89  ? 187 GLN A CD  1 
ATOM   1236  O OE1 . GLN A 1 158 ? 45.622  14.226  34.205  1.00 67.93  ? 187 GLN A OE1 1 
ATOM   1237  N NE2 . GLN A 1 158 ? 44.007  13.603  35.636  1.00 76.18  ? 187 GLN A NE2 1 
ATOM   1238  N N   . GLY A 1 159 ? 43.126  18.393  30.373  1.00 44.28  ? 188 GLY A N   1 
ATOM   1239  C CA  . GLY A 1 159 ? 43.527  19.181  29.212  1.00 42.36  ? 188 GLY A CA  1 
ATOM   1240  C C   . GLY A 1 159 ? 44.421  18.447  28.193  1.00 44.87  ? 188 GLY A C   1 
ATOM   1241  O O   . GLY A 1 159 ? 45.158  19.117  27.463  1.00 48.99  ? 188 GLY A O   1 
ATOM   1242  N N   . ILE A 1 160 ? 44.326  17.110  28.089  1.00 39.20  ? 189 ILE A N   1 
ATOM   1243  C CA  . ILE A 1 160 ? 45.051  16.325  27.079  1.00 40.35  ? 189 ILE A CA  1 
ATOM   1244  C C   . ILE A 1 160 ? 44.938  16.923  25.666  1.00 35.02  ? 189 ILE A C   1 
ATOM   1245  O O   . ILE A 1 160 ? 43.933  17.489  25.283  1.00 30.83  ? 189 ILE A O   1 
ATOM   1246  C CB  . ILE A 1 160 ? 44.598  14.849  27.112  1.00 43.81  ? 189 ILE A CB  1 
ATOM   1247  C CG1 . ILE A 1 160 ? 45.531  13.907  26.319  1.00 55.10  ? 189 ILE A CG1 1 
ATOM   1248  C CG2 . ILE A 1 160 ? 43.162  14.686  26.622  1.00 44.66  ? 189 ILE A CG2 1 
ATOM   1249  C CD1 . ILE A 1 160 ? 46.844  13.560  27.004  1.00 61.90  ? 189 ILE A CD1 1 
ATOM   1250  N N   . SER A 1 161 ? 45.991  16.761  24.853  1.00 35.50  ? 190 SER A N   1 
ATOM   1251  C CA  . SER A 1 161 ? 46.003  17.230  23.477  1.00 32.69  ? 190 SER A CA  1 
ATOM   1252  C C   . SER A 1 161 ? 44.903  16.547  22.669  1.00 30.31  ? 190 SER A C   1 
ATOM   1253  O O   . SER A 1 161 ? 44.684  15.358  22.851  1.00 32.79  ? 190 SER A O   1 
ATOM   1254  C CB  . SER A 1 161 ? 47.341  16.994  22.819  1.00 29.64  ? 190 SER A CB  1 
ATOM   1255  O OG  . SER A 1 161 ? 47.232  17.270  21.427  1.00 27.72  ? 190 SER A OG  1 
ATOM   1256  N N   . ARG A 1 162 ? 44.281  17.313  21.756  1.00 29.59  ? 191 ARG A N   1 
ATOM   1257  C CA  . ARG A 1 162 ? 43.379  16.846  20.711  1.00 35.38  ? 191 ARG A CA  1 
ATOM   1258  C C   . ARG A 1 162 ? 43.981  15.696  19.890  1.00 35.68  ? 191 ARG A C   1 
ATOM   1259  O O   . ARG A 1 162 ? 43.255  14.826  19.393  1.00 36.08  ? 191 ARG A O   1 
ATOM   1260  C CB  . ARG A 1 162 ? 43.132  17.989  19.720  1.00 42.40  ? 191 ARG A CB  1 
ATOM   1261  C CG  . ARG A 1 162 ? 42.067  19.001  20.102  1.00 59.99  ? 191 ARG A CG  1 
ATOM   1262  C CD  . ARG A 1 162 ? 41.693  19.895  18.924  1.00 67.75  ? 191 ARG A CD  1 
ATOM   1263  N NE  . ARG A 1 162 ? 40.479  20.667  19.227  1.00 83.61  ? 191 ARG A NE  1 
ATOM   1264  C CZ  . ARG A 1 162 ? 40.121  21.841  18.679  1.00 86.78  ? 191 ARG A CZ  1 
ATOM   1265  N NH1 . ARG A 1 162 ? 40.851  22.385  17.715  1.00 81.16  ? 191 ARG A NH1 1 
ATOM   1266  N NH2 . ARG A 1 162 ? 39.035  22.474  19.105  1.00 80.25  ? 191 ARG A NH2 1 
ATOM   1267  N N   . THR A 1 163 ? 45.313  15.714  19.717  1.00 33.82  ? 192 THR A N   1 
ATOM   1268  C CA  . THR A 1 163 ? 45.992  14.758  18.845  1.00 32.25  ? 192 THR A CA  1 
ATOM   1269  C C   . THR A 1 163 ? 45.973  13.394  19.517  1.00 30.26  ? 192 THR A C   1 
ATOM   1270  O O   . THR A 1 163 ? 46.206  12.403  18.844  1.00 34.94  ? 192 THR A O   1 
ATOM   1271  C CB  . THR A 1 163 ? 47.424  15.199  18.522  1.00 32.15  ? 192 THR A CB  1 
ATOM   1272  O OG1 . THR A 1 163 ? 48.114  15.198  19.765  1.00 29.47  ? 192 THR A OG1 1 
ATOM   1273  C CG2 . THR A 1 163 ? 47.497  16.601  17.947  1.00 35.34  ? 192 THR A CG2 1 
ATOM   1274  N N   . LYS A 1 164 ? 45.655  13.356  20.820  1.00 29.47  ? 193 LYS A N   1 
ATOM   1275  C CA  . LYS A 1 164 ? 45.717  12.129  21.602  1.00 32.56  ? 193 LYS A CA  1 
ATOM   1276  C C   . LYS A 1 164 ? 44.349  11.615  22.059  1.00 26.75  ? 193 LYS A C   1 
ATOM   1277  O O   . LYS A 1 164 ? 44.281  10.593  22.744  1.00 31.62  ? 193 LYS A O   1 
ATOM   1278  C CB  . LYS A 1 164 ? 46.629  12.321  22.823  1.00 33.91  ? 193 LYS A CB  1 
ATOM   1279  C CG  . LYS A 1 164 ? 48.053  12.768  22.472  1.00 42.33  ? 193 LYS A CG  1 
ATOM   1280  C CD  . LYS A 1 164 ? 48.770  11.893  21.442  1.00 50.78  ? 193 LYS A CD  1 
ATOM   1281  C CE  . LYS A 1 164 ? 50.066  12.430  20.895  1.00 56.79  ? 193 LYS A CE  1 
ATOM   1282  N NZ  . LYS A 1 164 ? 49.925  13.460  19.862  1.00 56.61  ? 193 LYS A NZ  1 
ATOM   1283  N N   . TYR A 1 165 ? 43.263  12.260  21.664  1.00 28.63  ? 194 TYR A N   1 
ATOM   1284  C CA  . TYR A 1 165 ? 41.922  11.802  22.011  1.00 27.99  ? 194 TYR A CA  1 
ATOM   1285  C C   . TYR A 1 165 ? 41.690  10.365  21.558  1.00 29.46  ? 194 TYR A C   1 
ATOM   1286  O O   . TYR A 1 165 ? 41.232  9.515   22.325  1.00 27.10  ? 194 TYR A O   1 
ATOM   1287  C CB  . TYR A 1 165 ? 40.877  12.688  21.341  1.00 29.36  ? 194 TYR A CB  1 
ATOM   1288  C CG  . TYR A 1 165 ? 40.661  14.062  21.957  1.00 26.87  ? 194 TYR A CG  1 
ATOM   1289  C CD1 . TYR A 1 165 ? 41.164  14.407  23.201  1.00 32.92  ? 194 TYR A CD1 1 
ATOM   1290  C CD2 . TYR A 1 165 ? 39.935  15.021  21.265  1.00 33.38  ? 194 TYR A CD2 1 
ATOM   1291  C CE1 . TYR A 1 165 ? 40.966  15.677  23.742  1.00 32.48  ? 194 TYR A CE1 1 
ATOM   1292  C CE2 . TYR A 1 165 ? 39.719  16.283  21.791  1.00 33.79  ? 194 TYR A CE2 1 
ATOM   1293  C CZ  . TYR A 1 165 ? 40.243  16.613  23.026  1.00 33.60  ? 194 TYR A CZ  1 
ATOM   1294  O OH  . TYR A 1 165 ? 40.024  17.862  23.506  1.00 40.46  ? 194 TYR A OH  1 
ATOM   1295  N N   . TRP A 1 166 ? 42.032  10.064  20.310  1.00 25.23  ? 195 TRP A N   1 
ATOM   1296  C CA  . TRP A 1 166 ? 41.784  8.729   19.796  1.00 27.11  ? 195 TRP A CA  1 
ATOM   1297  C C   . TRP A 1 166 ? 42.387  7.636   20.681  1.00 28.13  ? 195 TRP A C   1 
ATOM   1298  O O   . TRP A 1 166 ? 41.757  6.590   20.877  1.00 26.15  ? 195 TRP A O   1 
ATOM   1299  C CB  . TRP A 1 166 ? 42.278  8.577   18.365  1.00 27.10  ? 195 TRP A CB  1 
ATOM   1300  C CG  . TRP A 1 166 ? 43.762  8.390   18.240  1.00 32.09  ? 195 TRP A CG  1 
ATOM   1301  C CD1 . TRP A 1 166 ? 44.662  9.361   17.912  1.00 32.58  ? 195 TRP A CD1 1 
ATOM   1302  C CD2 . TRP A 1 166 ? 44.501  7.151   18.319  1.00 29.31  ? 195 TRP A CD2 1 
ATOM   1303  N NE1 . TRP A 1 166 ? 45.910  8.816   17.812  1.00 32.63  ? 195 TRP A NE1 1 
ATOM   1304  C CE2 . TRP A 1 166 ? 45.851  7.468   18.066  1.00 33.70  ? 195 TRP A CE2 1 
ATOM   1305  C CE3 . TRP A 1 166 ? 44.170  5.832   18.619  1.00 30.17  ? 195 TRP A CE3 1 
ATOM   1306  C CZ2 . TRP A 1 166 ? 46.859  6.505   18.043  1.00 31.14  ? 195 TRP A CZ2 1 
ATOM   1307  C CZ3 . TRP A 1 166 ? 45.167  4.883   18.628  1.00 33.11  ? 195 TRP A CZ3 1 
ATOM   1308  C CH2 . TRP A 1 166 ? 46.496  5.209   18.317  1.00 29.99  ? 195 TRP A CH2 1 
ATOM   1309  N N   . GLU A 1 167 ? 43.560  7.887   21.263  1.00 28.64  ? 196 GLU A N   1 
ATOM   1310  C CA  . GLU A 1 167 ? 44.234  6.900   22.104  1.00 26.87  ? 196 GLU A CA  1 
ATOM   1311  C C   . GLU A 1 167 ? 43.416  6.509   23.332  1.00 28.29  ? 196 GLU A C   1 
ATOM   1312  O O   . GLU A 1 167 ? 43.328  5.327   23.612  1.00 27.11  ? 196 GLU A O   1 
ATOM   1313  C CB  . GLU A 1 167 ? 45.626  7.314   22.586  1.00 31.77  ? 196 GLU A CB  1 
ATOM   1314  C CG  . GLU A 1 167 ? 46.583  7.600   21.429  1.00 35.62  ? 196 GLU A CG  1 
ATOM   1315  C CD  . GLU A 1 167 ? 47.963  8.096   21.837  1.00 42.66  ? 196 GLU A CD  1 
ATOM   1316  O OE1 . GLU A 1 167 ? 48.176  8.156   23.053  1.00 53.49  ? 196 GLU A OE1 1 
ATOM   1317  O OE2 . GLU A 1 167 ? 48.810  8.446   20.980  1.00 57.19  ? 196 GLU A OE2 1 
ATOM   1318  N N   . LEU A 1 168 ? 42.866  7.464   24.098  1.00 28.81  ? 197 LEU A N   1 
ATOM   1319  C CA  . LEU A 1 168 ? 42.063  7.111   25.260  1.00 29.67  ? 197 LEU A CA  1 
ATOM   1320  C C   . LEU A 1 168 ? 40.692  6.596   24.833  1.00 25.07  ? 197 LEU A C   1 
ATOM   1321  O O   . LEU A 1 168 ? 40.094  5.799   25.546  1.00 28.67  ? 197 LEU A O   1 
ATOM   1322  C CB  . LEU A 1 168 ? 41.898  8.250   26.277  1.00 36.52  ? 197 LEU A CB  1 
ATOM   1323  C CG  . LEU A 1 168 ? 43.115  8.657   27.121  1.00 44.21  ? 197 LEU A CG  1 
ATOM   1324  C CD1 . LEU A 1 168 ? 43.904  7.477   27.626  1.00 49.31  ? 197 LEU A CD1 1 
ATOM   1325  C CD2 . LEU A 1 168 ? 44.012  9.607   26.317  1.00 52.40  ? 197 LEU A CD2 1 
ATOM   1326  N N   . ILE A 1 169 ? 40.131  7.091   23.728  1.00 24.53  ? 198 ILE A N   1 
ATOM   1327  C CA  . ILE A 1 169 ? 38.916  6.538   23.143  1.00 25.15  ? 198 ILE A CA  1 
ATOM   1328  C C   . ILE A 1 169 ? 39.120  5.051   22.857  1.00 24.93  ? 198 ILE A C   1 
ATOM   1329  O O   . ILE A 1 169 ? 38.233  4.239   23.133  1.00 23.13  ? 198 ILE A O   1 
ATOM   1330  C CB  . ILE A 1 169 ? 38.500  7.242   21.837  1.00 27.95  ? 198 ILE A CB  1 
ATOM   1331  C CG1 . ILE A 1 169 ? 38.098  8.695   22.052  1.00 32.13  ? 198 ILE A CG1 1 
ATOM   1332  C CG2 . ILE A 1 169 ? 37.410  6.465   21.114  1.00 27.09  ? 198 ILE A CG2 1 
ATOM   1333  C CD1 . ILE A 1 169 ? 36.852  8.939   22.887  1.00 30.95  ? 198 ILE A CD1 1 
ATOM   1334  N N   . TYR A 1 170 ? 40.298  4.714   22.341  1.00 25.16  ? 199 TYR A N   1 
ATOM   1335  C CA  . TYR A 1 170 ? 40.595  3.330   22.006  1.00 26.24  ? 199 TYR A CA  1 
ATOM   1336  C C   . TYR A 1 170 ? 40.672  2.499   23.286  1.00 27.52  ? 199 TYR A C   1 
ATOM   1337  O O   . TYR A 1 170 ? 40.161  1.404   23.286  1.00 26.24  ? 199 TYR A O   1 
ATOM   1338  C CB  . TYR A 1 170 ? 41.867  3.250   21.173  1.00 26.74  ? 199 TYR A CB  1 
ATOM   1339  C CG  . TYR A 1 170 ? 42.570  1.897   21.113  1.00 25.12  ? 199 TYR A CG  1 
ATOM   1340  C CD1 . TYR A 1 170 ? 43.331  1.438   22.182  1.00 27.70  ? 199 TYR A CD1 1 
ATOM   1341  C CD2 . TYR A 1 170 ? 42.407  1.052   20.034  1.00 25.26  ? 199 TYR A CD2 1 
ATOM   1342  C CE1 . TYR A 1 170 ? 43.922  0.182   22.166  1.00 29.99  ? 199 TYR A CE1 1 
ATOM   1343  C CE2 . TYR A 1 170 ? 43.035  -0.183  19.977  1.00 25.00  ? 199 TYR A CE2 1 
ATOM   1344  C CZ  . TYR A 1 170 ? 43.792  -0.623  21.042  1.00 26.71  ? 199 TYR A CZ  1 
ATOM   1345  O OH  . TYR A 1 170 ? 44.430  -1.825  21.006  1.00 28.43  ? 199 TYR A OH  1 
ATOM   1346  N N   . GLU A 1 171 ? 41.321  2.989   24.352  1.00 27.88  ? 200 GLU A N   1 
ATOM   1347  C CA  . GLU A 1 171 ? 41.460  2.193   25.566  1.00 30.49  ? 200 GLU A CA  1 
ATOM   1348  C C   . GLU A 1 171 ? 40.086  1.933   26.195  1.00 29.71  ? 200 GLU A C   1 
ATOM   1349  O O   . GLU A 1 171 ? 39.811  0.831   26.666  1.00 27.40  ? 200 GLU A O   1 
ATOM   1350  C CB  . GLU A 1 171 ? 42.422  2.831   26.582  1.00 29.48  ? 200 GLU A CB  1 
ATOM   1351  C CG  . GLU A 1 171 ? 43.866  2.930   26.087  1.00 35.59  ? 200 GLU A CG  1 
ATOM   1352  C CD  . GLU A 1 171 ? 44.635  1.618   25.912  1.00 37.77  ? 200 GLU A CD  1 
ATOM   1353  O OE1 . GLU A 1 171 ? 44.199  0.608   26.490  1.00 35.44  ? 200 GLU A OE1 1 
ATOM   1354  O OE2 . GLU A 1 171 ? 45.660  1.583   25.180  1.00 38.10  ? 200 GLU A OE2 1 
ATOM   1355  N N   . ASP A 1 172 ? 39.276  2.989   26.316  1.00 28.80  ? 201 ASP A N   1 
ATOM   1356  C CA  . ASP A 1 172 ? 37.938  2.893   26.850  1.00 30.66  ? 201 ASP A CA  1 
ATOM   1357  C C   . ASP A 1 172 ? 37.060  2.009   25.958  1.00 31.51  ? 201 ASP A C   1 
ATOM   1358  O O   . ASP A 1 172 ? 36.200  1.289   26.456  1.00 27.64  ? 201 ASP A O   1 
ATOM   1359  C CB  . ASP A 1 172 ? 37.290  4.265   26.986  1.00 33.07  ? 201 ASP A CB  1 
ATOM   1360  C CG  . ASP A 1 172 ? 37.744  5.150   28.135  1.00 35.36  ? 201 ASP A CG  1 
ATOM   1361  O OD1 . ASP A 1 172 ? 38.543  4.675   28.993  1.00 31.17  ? 201 ASP A OD1 1 
ATOM   1362  O OD2 . ASP A 1 172 ? 37.242  6.306   28.190  1.00 35.46  ? 201 ASP A OD2 1 
ATOM   1363  N N   . SER A 1 173 ? 37.249  2.081   24.641  1.00 27.97  ? 202 SER A N   1 
ATOM   1364  C CA  . SER A 1 173 ? 36.525  1.197   23.740  1.00 30.09  ? 202 SER A CA  1 
ATOM   1365  C C   . SER A 1 173 ? 36.883  -0.279  23.976  1.00 29.73  ? 202 SER A C   1 
ATOM   1366  O O   . SER A 1 173 ? 35.997  -1.152  23.985  1.00 27.36  ? 202 SER A O   1 
ATOM   1367  C CB  . SER A 1 173 ? 36.737  1.588   22.307  1.00 29.98  ? 202 SER A CB  1 
ATOM   1368  O OG  . SER A 1 173 ? 35.933  2.720   21.990  1.00 31.27  ? 202 SER A OG  1 
ATOM   1369  N N   . MET A 1 174 ? 38.179  -0.555  24.177  1.00 29.64  ? 203 MET A N   1 
ATOM   1370  C CA  . MET A 1 174 ? 38.636  -1.925  24.347  1.00 28.22  ? 203 MET A CA  1 
ATOM   1371  C C   . MET A 1 174 ? 38.137  -2.440  25.686  1.00 27.27  ? 203 MET A C   1 
ATOM   1372  O O   . MET A 1 174 ? 37.722  -3.600  25.782  1.00 24.31  ? 203 MET A O   1 
ATOM   1373  C CB  . MET A 1 174 ? 40.149  -2.038  24.185  1.00 27.69  ? 203 MET A CB  1 
ATOM   1374  C CG  . MET A 1 174 ? 40.582  -1.687  22.772  1.00 27.49  ? 203 MET A CG  1 
ATOM   1375  S SD  . MET A 1 174 ? 40.688  -3.124  21.686  1.00 29.55  ? 203 MET A SD  1 
ATOM   1376  C CE  . MET A 1 174 ? 42.102  -3.907  22.484  1.00 32.86  ? 203 MET A CE  1 
ATOM   1377  N N   . ASP A 1 175 ? 38.066  -1.533  26.672  1.00 28.74  ? 204 ASP A N   1 
ATOM   1378  C CA  . ASP A 1 175 ? 37.538  -1.890  27.975  1.00 27.49  ? 204 ASP A CA  1 
ATOM   1379  C C   . ASP A 1 175 ? 36.033  -2.190  27.894  1.00 27.23  ? 204 ASP A C   1 
ATOM   1380  O O   . ASP A 1 175 ? 35.561  -3.126  28.547  1.00 30.12  ? 204 ASP A O   1 
ATOM   1381  C CB  . ASP A 1 175 ? 37.867  -0.849  29.029  1.00 27.64  ? 204 ASP A CB  1 
ATOM   1382  C CG  . ASP A 1 175 ? 39.338  -0.699  29.410  1.00 37.31  ? 204 ASP A CG  1 
ATOM   1383  O OD1 . ASP A 1 175 ? 40.170  -1.563  29.027  1.00 37.61  ? 204 ASP A OD1 1 
ATOM   1384  O OD2 . ASP A 1 175 ? 39.658  0.304   30.090  1.00 36.48  ? 204 ASP A OD2 1 
ATOM   1385  N N   . LEU A 1 176 ? 35.264  -1.385  27.154  1.00 23.76  ? 205 LEU A N   1 
ATOM   1386  C CA  . LEU A 1 176 ? 33.817  -1.530  27.072  1.00 25.98  ? 205 LEU A CA  1 
ATOM   1387  C C   . LEU A 1 176 ? 33.483  -2.835  26.356  1.00 24.93  ? 205 LEU A C   1 
ATOM   1388  O O   . LEU A 1 176 ? 32.656  -3.615  26.801  1.00 22.97  ? 205 LEU A O   1 
ATOM   1389  C CB  . LEU A 1 176 ? 33.198  -0.338  26.335  1.00 26.24  ? 205 LEU A CB  1 
ATOM   1390  C CG  . LEU A 1 176 ? 31.681  -0.358  26.079  1.00 25.83  ? 205 LEU A CG  1 
ATOM   1391  C CD1 . LEU A 1 176 ? 30.864  -0.780  27.266  1.00 28.17  ? 205 LEU A CD1 1 
ATOM   1392  C CD2 . LEU A 1 176 ? 31.163  1.027   25.692  1.00 29.04  ? 205 LEU A CD2 1 
ATOM   1393  N N   . ILE A 1 177 ? 34.133  -3.063  25.219  1.00 27.58  ? 206 ILE A N   1 
ATOM   1394  C CA  . ILE A 1 177 ? 33.950  -4.305  24.500  1.00 28.31  ? 206 ILE A CA  1 
ATOM   1395  C C   . ILE A 1 177 ? 34.205  -5.491  25.424  1.00 25.68  ? 206 ILE A C   1 
ATOM   1396  O O   . ILE A 1 177 ? 33.362  -6.374  25.520  1.00 25.53  ? 206 ILE A O   1 
ATOM   1397  C CB  . ILE A 1 177 ? 34.810  -4.328  23.241  1.00 28.92  ? 206 ILE A CB  1 
ATOM   1398  C CG1 . ILE A 1 177 ? 34.234  -3.323  22.232  1.00 29.83  ? 206 ILE A CG1 1 
ATOM   1399  C CG2 . ILE A 1 177 ? 34.889  -5.744  22.673  1.00 32.17  ? 206 ILE A CG2 1 
ATOM   1400  C CD1 . ILE A 1 177 ? 35.220  -2.917  21.151  1.00 32.25  ? 206 ILE A CD1 1 
ATOM   1401  N N   . ALA A 1 178 ? 35.306  -5.474  26.159  1.00 25.95  ? 207 ALA A N   1 
ATOM   1402  C CA  . ALA A 1 178 ? 35.634  -6.604  27.023  1.00 24.62  ? 207 ALA A CA  1 
ATOM   1403  C C   . ALA A 1 178 ? 34.574  -6.829  28.099  1.00 27.13  ? 207 ALA A C   1 
ATOM   1404  O O   . ALA A 1 178 ? 34.305  -7.968  28.474  1.00 25.31  ? 207 ALA A O   1 
ATOM   1405  C CB  . ALA A 1 178 ? 36.962  -6.396  27.644  1.00 25.19  ? 207 ALA A CB  1 
ATOM   1406  N N   . LYS A 1 179 ? 33.942  -5.752  28.574  1.00 30.64  ? 208 LYS A N   1 
ATOM   1407  C CA  . LYS A 1 179 ? 33.038  -5.833  29.708  1.00 30.04  ? 208 LYS A CA  1 
ATOM   1408  C C   . LYS A 1 179 ? 31.619  -6.181  29.299  1.00 31.78  ? 208 LYS A C   1 
ATOM   1409  O O   . LYS A 1 179 ? 30.847  -6.731  30.091  1.00 25.91  ? 208 LYS A O   1 
ATOM   1410  C CB  . LYS A 1 179 ? 33.021  -4.502  30.464  1.00 34.34  ? 208 LYS A CB  1 
ATOM   1411  C CG  . LYS A 1 179 ? 34.326  -4.260  31.184  1.00 33.59  ? 208 LYS A CG  1 
ATOM   1412  C CD  . LYS A 1 179 ? 34.372  -2.906  31.897  1.00 35.00  ? 208 LYS A CD  1 
ATOM   1413  C CE  . LYS A 1 179 ? 35.787  -2.596  32.300  1.00 37.68  ? 208 LYS A CE  1 
ATOM   1414  N NZ  . LYS A 1 179 ? 35.870  -1.143  32.412  1.00 47.74  ? 208 LYS A NZ  1 
ATOM   1415  N N   . LEU A 1 180 ? 31.266  -5.830  28.068  1.00 31.49  ? 209 LEU A N   1 
ATOM   1416  C CA  . LEU A 1 180 ? 29.910  -5.982  27.575  1.00 33.16  ? 209 LEU A CA  1 
ATOM   1417  C C   . LEU A 1 180 ? 29.353  -7.396  27.765  1.00 32.75  ? 209 LEU A C   1 
ATOM   1418  O O   . LEU A 1 180 ? 28.236  -7.537  28.227  1.00 28.00  ? 209 LEU A O   1 
ATOM   1419  C CB  . LEU A 1 180 ? 29.824  -5.584  26.101  1.00 32.61  ? 209 LEU A CB  1 
ATOM   1420  C CG  . LEU A 1 180 ? 28.975  -4.364  25.730  1.00 34.13  ? 209 LEU A CG  1 
ATOM   1421  C CD1 . LEU A 1 180 ? 28.109  -3.673  26.780  1.00 29.01  ? 209 LEU A CD1 1 
ATOM   1422  C CD2 . LEU A 1 180 ? 29.858  -3.404  24.985  1.00 36.48  ? 209 LEU A CD2 1 
ATOM   1423  N N   . PRO A 1 181 ? 30.049  -8.483  27.356  1.00 30.11  ? 210 PRO A N   1 
ATOM   1424  C CA  . PRO A 1 181 ? 29.540  -9.827  27.583  1.00 34.83  ? 210 PRO A CA  1 
ATOM   1425  C C   . PRO A 1 181 ? 29.222  -10.130 29.049  1.00 34.58  ? 210 PRO A C   1 
ATOM   1426  O O   . PRO A 1 181 ? 28.252  -10.829 29.332  1.00 31.18  ? 210 PRO A O   1 
ATOM   1427  C CB  . PRO A 1 181 ? 30.678  -10.718 26.998  1.00 33.66  ? 210 PRO A CB  1 
ATOM   1428  C CG  . PRO A 1 181 ? 31.286  -9.846  25.930  1.00 32.74  ? 210 PRO A CG  1 
ATOM   1429  C CD  . PRO A 1 181 ? 31.318  -8.471  26.618  1.00 32.06  ? 210 PRO A CD  1 
ATOM   1430  N N   . CYS A 1 182 ? 30.007  -9.553  29.964  1.00 33.45  ? 211 CYS A N   1 
ATOM   1431  C CA  . CYS A 1 182 ? 29.807  -9.773  31.382  1.00 35.85  ? 211 CYS A CA  1 
ATOM   1432  C C   . CYS A 1 182 ? 28.534  -9.091  31.818  1.00 30.88  ? 211 CYS A C   1 
ATOM   1433  O O   . CYS A 1 182 ? 27.716  -9.731  32.450  1.00 28.22  ? 211 CYS A O   1 
ATOM   1434  C CB  . CYS A 1 182 ? 30.965  -9.287  32.245  1.00 38.22  ? 211 CYS A CB  1 
ATOM   1435  S SG  . CYS A 1 182 ? 32.509  -10.064 31.732  1.00 45.20  ? 211 CYS A SG  1 
ATOM   1436  N N   . VAL A 1 183 ? 28.355  -7.836  31.398  1.00 28.67  ? 212 VAL A N   1 
ATOM   1437  C CA  . VAL A 1 183 ? 27.136  -7.080  31.653  1.00 29.87  ? 212 VAL A CA  1 
ATOM   1438  C C   . VAL A 1 183 ? 25.944  -7.808  31.046  1.00 26.23  ? 212 VAL A C   1 
ATOM   1439  O O   . VAL A 1 183 ? 24.974  -8.071  31.737  1.00 27.86  ? 212 VAL A O   1 
ATOM   1440  C CB  . VAL A 1 183 ? 27.196  -5.641  31.106  1.00 28.02  ? 212 VAL A CB  1 
ATOM   1441  C CG1 . VAL A 1 183 ? 25.861  -4.914  31.239  1.00 25.74  ? 212 VAL A CG1 1 
ATOM   1442  C CG2 . VAL A 1 183 ? 28.326  -4.874  31.761  1.00 30.40  ? 212 VAL A CG2 1 
ATOM   1443  N N   . ALA A 1 184 ? 26.063  -8.163  29.770  1.00 23.43  ? 213 ALA A N   1 
ATOM   1444  C CA  . ALA A 1 184 ? 24.987  -8.814  29.031  1.00 23.64  ? 213 ALA A CA  1 
ATOM   1445  C C   . ALA A 1 184 ? 24.611  -10.166 29.675  1.00 28.63  ? 213 ALA A C   1 
ATOM   1446  O O   . ALA A 1 184 ? 23.426  -10.482 29.804  1.00 33.36  ? 213 ALA A O   1 
ATOM   1447  C CB  . ALA A 1 184 ? 25.417  -8.956  27.612  1.00 25.97  ? 213 ALA A CB  1 
ATOM   1448  N N   . ALA A 1 185 ? 25.607  -10.928 30.121  1.00 26.75  ? 214 ALA A N   1 
ATOM   1449  C CA  . ALA A 1 185 ? 25.397  -12.246 30.705  1.00 27.72  ? 214 ALA A CA  1 
ATOM   1450  C C   . ALA A 1 185 ? 24.762  -12.148 32.070  1.00 26.24  ? 214 ALA A C   1 
ATOM   1451  O O   . ALA A 1 185 ? 23.893  -12.957 32.351  1.00 30.01  ? 214 ALA A O   1 
ATOM   1452  C CB  . ALA A 1 185 ? 26.662  -13.032 30.806  1.00 26.95  ? 214 ALA A CB  1 
ATOM   1453  N N   . LYS A 1 186 ? 25.166  -11.143 32.860  1.00 29.91  ? 215 LYS A N   1 
ATOM   1454  C CA  . LYS A 1 186 ? 24.531  -10.823 34.135  1.00 32.78  ? 215 LYS A CA  1 
ATOM   1455  C C   . LYS A 1 186 ? 23.059  -10.437 34.008  1.00 34.81  ? 215 LYS A C   1 
ATOM   1456  O O   . LYS A 1 186 ? 22.201  -10.816 34.826  1.00 32.11  ? 215 LYS A O   1 
ATOM   1457  C CB  . LYS A 1 186 ? 25.299  -9.688  34.811  1.00 34.12  ? 215 LYS A CB  1 
ATOM   1458  C CG  . LYS A 1 186 ? 25.120  -9.610  36.309  1.00 46.96  ? 215 LYS A CG  1 
ATOM   1459  C CD  . LYS A 1 186 ? 26.397  -9.361  37.108  1.00 53.08  ? 215 LYS A CD  1 
ATOM   1460  C CE  . LYS A 1 186 ? 27.509  -10.302 36.746  1.00 58.79  ? 215 LYS A CE  1 
ATOM   1461  N N   . ILE A 1 187 ? 22.751  -9.611  33.009  1.00 31.34  ? 216 ILE A N   1 
ATOM   1462  C CA  . ILE A 1 187 ? 21.364  -9.306  32.712  1.00 26.93  ? 216 ILE A CA  1 
ATOM   1463  C C   . ILE A 1 187 ? 20.575  -10.592 32.466  1.00 26.20  ? 216 ILE A C   1 
ATOM   1464  O O   . ILE A 1 187 ? 19.487  -10.792 33.007  1.00 28.29  ? 216 ILE A O   1 
ATOM   1465  C CB  . ILE A 1 187 ? 21.260  -8.350  31.512  1.00 26.97  ? 216 ILE A CB  1 
ATOM   1466  C CG1 . ILE A 1 187 ? 21.850  -6.979  31.884  1.00 27.38  ? 216 ILE A CG1 1 
ATOM   1467  C CG2 . ILE A 1 187 ? 19.818  -8.280  31.018  1.00 25.07  ? 216 ILE A CG2 1 
ATOM   1468  C CD1 . ILE A 1 187 ? 21.901  -5.950  30.766  1.00 28.96  ? 216 ILE A CD1 1 
ATOM   1469  N N   . TYR A 1 188 ? 21.097  -11.430 31.582  1.00 22.99  ? 217 TYR A N   1 
ATOM   1470  C CA  . TYR A 1 188 ? 20.411  -12.623 31.186  1.00 26.70  ? 217 TYR A CA  1 
ATOM   1471  C C   . TYR A 1 188 ? 20.143  -13.516 32.385  1.00 26.79  ? 217 TYR A C   1 
ATOM   1472  O O   . TYR A 1 188 ? 19.022  -13.955 32.561  1.00 25.50  ? 217 TYR A O   1 
ATOM   1473  C CB  . TYR A 1 188 ? 21.281  -13.433 30.232  1.00 28.16  ? 217 TYR A CB  1 
ATOM   1474  C CG  . TYR A 1 188 ? 20.544  -14.616 29.654  1.00 28.23  ? 217 TYR A CG  1 
ATOM   1475  C CD1 . TYR A 1 188 ? 19.511  -14.420 28.747  1.00 30.84  ? 217 TYR A CD1 1 
ATOM   1476  C CD2 . TYR A 1 188 ? 20.943  -15.917 29.926  1.00 30.19  ? 217 TYR A CD2 1 
ATOM   1477  C CE1 . TYR A 1 188 ? 18.846  -15.485 28.169  1.00 29.77  ? 217 TYR A CE1 1 
ATOM   1478  C CE2 . TYR A 1 188 ? 20.302  -16.991 29.331  1.00 31.91  ? 217 TYR A CE2 1 
ATOM   1479  C CZ  . TYR A 1 188 ? 19.252  -16.776 28.450  1.00 33.22  ? 217 TYR A CZ  1 
ATOM   1480  O OH  . TYR A 1 188 ? 18.605  -17.834 27.859  1.00 34.24  ? 217 TYR A OH  1 
ATOM   1481  N N   . ARG A 1 189 ? 21.186  -13.757 33.177  1.00 29.34  ? 218 ARG A N   1 
ATOM   1482  C CA  . ARG A 1 189 ? 21.128  -14.698 34.287  1.00 31.43  ? 218 ARG A CA  1 
ATOM   1483  C C   . ARG A 1 189 ? 20.220  -14.149 35.379  1.00 34.38  ? 218 ARG A C   1 
ATOM   1484  O O   . ARG A 1 189 ? 19.470  -14.904 35.985  1.00 39.01  ? 218 ARG A O   1 
ATOM   1485  C CB  . ARG A 1 189 ? 22.528  -15.009 34.802  1.00 31.41  ? 218 ARG A CB  1 
ATOM   1486  C CG  . ARG A 1 189 ? 23.160  -15.987 33.816  1.00 37.85  ? 218 ARG A CG  1 
ATOM   1487  C CD  . ARG A 1 189 ? 24.217  -16.936 34.381  1.00 40.74  ? 218 ARG A CD  1 
ATOM   1488  N NE  . ARG A 1 189 ? 23.827  -18.282 33.965  1.00 52.86  ? 218 ARG A NE  1 
ATOM   1489  C CZ  . ARG A 1 189 ? 23.849  -19.352 34.729  1.00 56.18  ? 218 ARG A CZ  1 
ATOM   1490  N NH1 . ARG A 1 189 ? 22.813  -20.164 34.702  1.00 57.92  ? 218 ARG A NH1 1 
ATOM   1491  N NH2 . ARG A 1 189 ? 24.784  -19.503 35.643  1.00 61.82  ? 218 ARG A NH2 1 
ATOM   1492  N N   . ASN A 1 190 ? 20.250  -12.839 35.591  1.00 33.47  ? 219 ASN A N   1 
ATOM   1493  C CA  . ASN A 1 190 ? 19.471  -12.226 36.654  1.00 35.21  ? 219 ASN A CA  1 
ATOM   1494  C C   . ASN A 1 190 ? 17.997  -12.291 36.298  1.00 36.39  ? 219 ASN A C   1 
ATOM   1495  O O   . ASN A 1 190 ? 17.169  -12.541 37.164  1.00 40.26  ? 219 ASN A O   1 
ATOM   1496  C CB  . ASN A 1 190 ? 19.861  -10.773 36.935  1.00 33.30  ? 219 ASN A CB  1 
ATOM   1497  C CG  . ASN A 1 190 ? 21.143  -10.689 37.722  1.00 41.46  ? 219 ASN A CG  1 
ATOM   1498  O OD1 . ASN A 1 190 ? 21.630  -11.722 38.201  1.00 42.10  ? 219 ASN A OD1 1 
ATOM   1499  N ND2 . ASN A 1 190 ? 21.706  -9.494  37.872  1.00 44.14  ? 219 ASN A ND2 1 
ATOM   1500  N N   . LEU A 1 191 ? 17.673  -12.083 35.027  1.00 34.97  ? 220 LEU A N   1 
ATOM   1501  C CA  . LEU A 1 191 ? 16.282  -12.110 34.624  1.00 38.20  ? 220 LEU A CA  1 
ATOM   1502  C C   . LEU A 1 191 ? 15.737  -13.530 34.442  1.00 34.97  ? 220 LEU A C   1 
ATOM   1503  O O   . LEU A 1 191 ? 14.545  -13.738 34.639  1.00 32.39  ? 220 LEU A O   1 
ATOM   1504  C CB  . LEU A 1 191 ? 16.150  -11.305 33.339  1.00 36.07  ? 220 LEU A CB  1 
ATOM   1505  C CG  . LEU A 1 191 ? 16.192  -9.779  33.483  1.00 38.15  ? 220 LEU A CG  1 
ATOM   1506  C CD1 . LEU A 1 191 ? 16.074  -9.154  32.084  1.00 36.21  ? 220 LEU A CD1 1 
ATOM   1507  C CD2 . LEU A 1 191 ? 15.101  -9.274  34.396  1.00 40.59  ? 220 LEU A CD2 1 
ATOM   1508  N N   . TYR A 1 192 ? 16.547  -14.464 33.925  1.00 36.95  ? 221 TYR A N   1 
ATOM   1509  C CA  . TYR A 1 192 ? 15.996  -15.682 33.337  1.00 37.22  ? 221 TYR A CA  1 
ATOM   1510  C C   . TYR A 1 192 ? 16.651  -16.948 33.897  1.00 41.25  ? 221 TYR A C   1 
ATOM   1511  O O   . TYR A 1 192 ? 16.327  -18.047 33.460  1.00 44.03  ? 221 TYR A O   1 
ATOM   1512  C CB  . TYR A 1 192 ? 16.168  -15.667 31.811  1.00 38.73  ? 221 TYR A CB  1 
ATOM   1513  C CG  . TYR A 1 192 ? 15.606  -14.426 31.125  1.00 38.78  ? 221 TYR A CG  1 
ATOM   1514  C CD1 . TYR A 1 192 ? 14.273  -14.032 31.288  1.00 37.39  ? 221 TYR A CD1 1 
ATOM   1515  C CD2 . TYR A 1 192 ? 16.437  -13.622 30.351  1.00 34.60  ? 221 TYR A CD2 1 
ATOM   1516  C CE1 . TYR A 1 192 ? 13.789  -12.872 30.693  1.00 38.85  ? 221 TYR A CE1 1 
ATOM   1517  C CE2 . TYR A 1 192 ? 15.950  -12.483 29.730  1.00 36.83  ? 221 TYR A CE2 1 
ATOM   1518  C CZ  . TYR A 1 192 ? 14.628  -12.120 29.886  1.00 35.53  ? 221 TYR A CZ  1 
ATOM   1519  O OH  . TYR A 1 192 ? 14.241  -10.976 29.264  1.00 39.86  ? 221 TYR A OH  1 
ATOM   1520  N N   . ARG A 1 193 ? 17.624  -16.797 34.801  1.00 41.23  ? 222 ARG A N   1 
ATOM   1521  C CA  . ARG A 1 193 ? 18.249  -17.927 35.470  1.00 39.55  ? 222 ARG A CA  1 
ATOM   1522  C C   . ARG A 1 193 ? 18.370  -17.634 36.965  1.00 37.77  ? 222 ARG A C   1 
ATOM   1523  O O   . ARG A 1 193 ? 19.406  -17.901 37.553  1.00 37.97  ? 222 ARG A O   1 
ATOM   1524  C CB  . ARG A 1 193 ? 19.625  -18.122 34.841  1.00 36.71  ? 222 ARG A CB  1 
ATOM   1525  C CG  . ARG A 1 193 ? 19.653  -18.531 33.382  1.00 38.35  ? 222 ARG A CG  1 
ATOM   1526  C CD  . ARG A 1 193 ? 19.111  -19.910 33.121  1.00 40.36  ? 222 ARG A CD  1 
ATOM   1527  N NE  . ARG A 1 193 ? 19.350  -20.279 31.721  1.00 40.21  ? 222 ARG A NE  1 
ATOM   1528  C CZ  . ARG A 1 193 ? 18.582  -19.970 30.686  1.00 37.86  ? 222 ARG A CZ  1 
ATOM   1529  N NH1 . ARG A 1 193 ? 17.492  -19.239 30.828  1.00 39.63  ? 222 ARG A NH1 1 
ATOM   1530  N NH2 . ARG A 1 193 ? 18.923  -20.377 29.482  1.00 41.48  ? 222 ARG A NH2 1 
ATOM   1531  N N   . GLU A 1 194 ? 17.377  -16.916 37.513  1.00 41.97  ? 223 GLU A N   1 
ATOM   1532  C CA  . GLU A 1 194 ? 17.144  -16.776 38.943  1.00 53.02  ? 223 GLU A CA  1 
ATOM   1533  C C   . GLU A 1 194 ? 18.343  -16.194 39.707  1.00 51.17  ? 223 GLU A C   1 
ATOM   1534  O O   . GLU A 1 194 ? 18.475  -16.422 40.909  1.00 48.18  ? 223 GLU A O   1 
ATOM   1535  C CB  . GLU A 1 194 ? 16.714  -18.172 39.410  1.00 62.52  ? 223 GLU A CB  1 
ATOM   1536  C CG  . GLU A 1 194 ? 15.742  -18.160 40.588  1.00 74.94  ? 223 GLU A CG  1 
ATOM   1537  C CD  . GLU A 1 194 ? 15.680  -19.488 41.330  1.00 79.87  ? 223 GLU A CD  1 
ATOM   1538  O OE1 . GLU A 1 194 ? 16.012  -19.523 42.543  1.00 76.16  ? 223 GLU A OE1 1 
ATOM   1539  O OE2 . GLU A 1 194 ? 15.329  -20.494 40.675  1.00 71.83  ? 223 GLU A OE2 1 
ATOM   1540  N N   . GLY A 1 195 ? 19.208  -15.413 39.040  1.00 41.93  ? 224 GLY A N   1 
ATOM   1541  C CA  . GLY A 1 195 ? 20.308  -14.737 39.716  1.00 39.79  ? 224 GLY A CA  1 
ATOM   1542  C C   . GLY A 1 195 ? 21.601  -15.555 39.777  1.00 42.07  ? 224 GLY A C   1 
ATOM   1543  O O   . GLY A 1 195 ? 22.613  -15.048 40.270  1.00 43.44  ? 224 GLY A O   1 
ATOM   1544  N N   . SER A 1 196 ? 21.587  -16.805 39.279  1.00 36.64  ? 225 SER A N   1 
ATOM   1545  C CA  . SER A 1 196 ? 22.796  -17.602 39.227  1.00 41.96  ? 225 SER A CA  1 
ATOM   1546  C C   . SER A 1 196 ? 23.955  -16.780 38.655  1.00 53.01  ? 225 SER A C   1 
ATOM   1547  O O   . SER A 1 196 ? 23.770  -15.959 37.749  1.00 42.88  ? 225 SER A O   1 
ATOM   1548  C CB  . SER A 1 196 ? 22.602  -18.880 38.448  1.00 47.24  ? 225 SER A CB  1 
ATOM   1549  O OG  . SER A 1 196 ? 22.074  -18.632 37.149  1.00 51.49  ? 225 SER A OG  1 
ATOM   1550  N N   . GLY A 1 197 ? 25.150  -17.027 39.212  1.00 53.49  ? 226 GLY A N   1 
ATOM   1551  C CA  . GLY A 1 197 ? 26.353  -16.289 38.867  1.00 49.28  ? 226 GLY A CA  1 
ATOM   1552  C C   . GLY A 1 197 ? 26.786  -16.606 37.442  1.00 49.05  ? 226 GLY A C   1 
ATOM   1553  O O   . GLY A 1 197 ? 26.313  -17.581 36.857  1.00 46.42  ? 226 GLY A O   1 
ATOM   1554  N N   . ILE A 1 198 ? 27.665  -15.754 36.896  1.00 45.31  ? 227 ILE A N   1 
ATOM   1555  C CA  . ILE A 1 198 ? 28.074  -15.847 35.502  1.00 42.20  ? 227 ILE A CA  1 
ATOM   1556  C C   . ILE A 1 198 ? 29.360  -16.652 35.366  1.00 44.64  ? 227 ILE A C   1 
ATOM   1557  O O   . ILE A 1 198 ? 29.787  -16.951 34.248  1.00 42.31  ? 227 ILE A O   1 
ATOM   1558  C CB  . ILE A 1 198 ? 28.168  -14.461 34.834  1.00 40.50  ? 227 ILE A CB  1 
ATOM   1559  C CG1 . ILE A 1 198 ? 29.097  -13.462 35.565  1.00 47.65  ? 227 ILE A CG1 1 
ATOM   1560  C CG2 . ILE A 1 198 ? 26.753  -13.899 34.661  1.00 38.29  ? 227 ILE A CG2 1 
ATOM   1561  C CD1 . ILE A 1 198 ? 29.426  -12.206 34.764  1.00 50.71  ? 227 ILE A CD1 1 
ATOM   1562  N N   . GLY A 1 199 ? 29.983  -17.014 36.496  1.00 42.24  ? 228 GLY A N   1 
ATOM   1563  C CA  . GLY A 1 199 ? 31.184  -17.824 36.412  1.00 43.93  ? 228 GLY A CA  1 
ATOM   1564  C C   . GLY A 1 199 ? 32.366  -16.921 36.111  1.00 49.13  ? 228 GLY A C   1 
ATOM   1565  O O   . GLY A 1 199 ? 32.340  -15.763 36.490  1.00 48.13  ? 228 GLY A O   1 
ATOM   1566  N N   . ALA A 1 200 ? 33.372  -17.450 35.411  1.00 51.26  ? 229 ALA A N   1 
ATOM   1567  C CA  . ALA A 1 200 ? 34.603  -16.714 35.217  1.00 51.38  ? 229 ALA A CA  1 
ATOM   1568  C C   . ALA A 1 200 ? 34.905  -16.629 33.731  1.00 48.32  ? 229 ALA A C   1 
ATOM   1569  O O   . ALA A 1 200 ? 34.232  -17.247 32.904  1.00 46.78  ? 229 ALA A O   1 
ATOM   1570  C CB  . ALA A 1 200 ? 35.738  -17.347 35.992  1.00 54.87  ? 229 ALA A CB  1 
ATOM   1571  N N   . ILE A 1 201 ? 35.868  -15.764 33.436  1.00 40.73  ? 230 ILE A N   1 
ATOM   1572  C CA  . ILE A 1 201 ? 36.410  -15.574 32.106  1.00 40.36  ? 230 ILE A CA  1 
ATOM   1573  C C   . ILE A 1 201 ? 37.588  -16.534 31.974  1.00 38.47  ? 230 ILE A C   1 
ATOM   1574  O O   . ILE A 1 201 ? 38.439  -16.575 32.845  1.00 38.40  ? 230 ILE A O   1 
ATOM   1575  C CB  . ILE A 1 201 ? 36.866  -14.099 31.957  1.00 42.91  ? 230 ILE A CB  1 
ATOM   1576  C CG1 . ILE A 1 201 ? 35.727  -13.094 32.217  1.00 43.90  ? 230 ILE A CG1 1 
ATOM   1577  C CG2 . ILE A 1 201 ? 37.524  -13.838 30.600  1.00 47.12  ? 230 ILE A CG2 1 
ATOM   1578  C CD1 . ILE A 1 201 ? 34.672  -13.044 31.124  1.00 44.75  ? 230 ILE A CD1 1 
ATOM   1579  N N   . ASP A 1 202 ? 37.682  -17.260 30.866  1.00 40.49  ? 231 ASP A N   1 
ATOM   1580  C CA  . ASP A 1 202 ? 38.907  -17.967 30.542  1.00 43.57  ? 231 ASP A CA  1 
ATOM   1581  C C   . ASP A 1 202 ? 39.710  -17.137 29.532  1.00 43.50  ? 231 ASP A C   1 
ATOM   1582  O O   . ASP A 1 202 ? 39.234  -16.813 28.439  1.00 38.58  ? 231 ASP A O   1 
ATOM   1583  C CB  . ASP A 1 202 ? 38.578  -19.394 30.126  1.00 46.04  ? 231 ASP A CB  1 
ATOM   1584  C CG  . ASP A 1 202 ? 39.727  -20.188 29.513  1.00 48.27  ? 231 ASP A CG  1 
ATOM   1585  O OD1 . ASP A 1 202 ? 40.804  -19.591 29.317  1.00 52.81  ? 231 ASP A OD1 1 
ATOM   1586  O OD2 . ASP A 1 202 ? 39.515  -21.386 29.182  1.00 51.57  ? 231 ASP A OD2 1 
ATOM   1587  N N   . SER A 1 203 ? 40.981  -16.891 29.866  1.00 40.41  ? 232 SER A N   1 
ATOM   1588  C CA  . SER A 1 203 ? 41.830  -15.976 29.121  1.00 41.95  ? 232 SER A CA  1 
ATOM   1589  C C   . SER A 1 203 ? 42.276  -16.553 27.771  1.00 44.26  ? 232 SER A C   1 
ATOM   1590  O O   . SER A 1 203 ? 42.826  -15.836 26.929  1.00 49.14  ? 232 SER A O   1 
ATOM   1591  C CB  . SER A 1 203 ? 43.007  -15.585 29.975  1.00 45.25  ? 232 SER A CB  1 
ATOM   1592  O OG  . SER A 1 203 ? 43.855  -16.708 30.165  1.00 51.01  ? 232 SER A OG  1 
ATOM   1593  N N   . ASN A 1 204 ? 42.031  -17.841 27.540  1.00 38.84  ? 233 ASN A N   1 
ATOM   1594  C CA  . ASN A 1 204 ? 42.417  -18.458 26.285  1.00 43.69  ? 233 ASN A CA  1 
ATOM   1595  C C   . ASN A 1 204 ? 41.208  -18.752 25.396  1.00 41.12  ? 233 ASN A C   1 
ATOM   1596  O O   . ASN A 1 204 ? 41.363  -19.353 24.332  1.00 41.48  ? 233 ASN A O   1 
ATOM   1597  C CB  . ASN A 1 204 ? 43.227  -19.730 26.526  1.00 53.21  ? 233 ASN A CB  1 
ATOM   1598  C CG  . ASN A 1 204 ? 44.613  -19.453 27.058  1.00 58.13  ? 233 ASN A CG  1 
ATOM   1599  O OD1 . ASN A 1 204 ? 44.872  -19.667 28.247  1.00 64.80  ? 233 ASN A OD1 1 
ATOM   1600  N ND2 . ASN A 1 204 ? 45.503  -18.973 26.204  1.00 56.02  ? 233 ASN A ND2 1 
ATOM   1601  N N   . LEU A 1 205 ? 40.001  -18.326 25.790  1.00 44.17  ? 234 LEU A N   1 
ATOM   1602  C CA  . LEU A 1 205 ? 38.845  -18.475 24.910  1.00 38.58  ? 234 LEU A CA  1 
ATOM   1603  C C   . LEU A 1 205 ? 38.613  -17.191 24.132  1.00 35.20  ? 234 LEU A C   1 
ATOM   1604  O O   . LEU A 1 205 ? 38.955  -16.114 24.595  1.00 33.55  ? 234 LEU A O   1 
ATOM   1605  C CB  . LEU A 1 205 ? 37.593  -18.855 25.699  1.00 41.46  ? 234 LEU A CB  1 
ATOM   1606  C CG  . LEU A 1 205 ? 37.668  -20.183 26.456  1.00 43.34  ? 234 LEU A CG  1 
ATOM   1607  C CD1 . LEU A 1 205 ? 36.379  -20.385 27.207  1.00 46.85  ? 234 LEU A CD1 1 
ATOM   1608  C CD2 . LEU A 1 205 ? 37.979  -21.397 25.574  1.00 45.83  ? 234 LEU A CD2 1 
ATOM   1609  N N   . ASP A 1 206 ? 37.972  -17.307 22.971  1.00 35.79  ? 235 ASP A N   1 
ATOM   1610  C CA  . ASP A 1 206 ? 37.551  -16.116 22.242  1.00 36.73  ? 235 ASP A CA  1 
ATOM   1611  C C   . ASP A 1 206 ? 36.372  -15.437 22.943  1.00 36.62  ? 235 ASP A C   1 
ATOM   1612  O O   . ASP A 1 206 ? 35.730  -15.993 23.834  1.00 33.30  ? 235 ASP A O   1 
ATOM   1613  C CB  . ASP A 1 206 ? 37.198  -16.416 20.806  1.00 37.33  ? 235 ASP A CB  1 
ATOM   1614  C CG  . ASP A 1 206 ? 36.036  -17.372 20.617  1.00 36.85  ? 235 ASP A CG  1 
ATOM   1615  O OD1 . ASP A 1 206 ? 36.247  -18.584 20.779  1.00 49.73  ? 235 ASP A OD1 1 
ATOM   1616  O OD2 . ASP A 1 206 ? 34.943  -16.912 20.287  1.00 38.32  ? 235 ASP A OD2 1 
ATOM   1617  N N   . TRP A 1 207 ? 36.097  -14.206 22.519  1.00 32.07  ? 236 TRP A N   1 
ATOM   1618  C CA  . TRP A 1 207 ? 35.097  -13.357 23.162  1.00 29.63  ? 236 TRP A CA  1 
ATOM   1619  C C   . TRP A 1 207 ? 33.703  -13.988 23.086  1.00 30.89  ? 236 TRP A C   1 
ATOM   1620  O O   . TRP A 1 207 ? 32.983  -14.023 24.096  1.00 22.91  ? 236 TRP A O   1 
ATOM   1621  C CB  . TRP A 1 207 ? 35.207  -12.016 22.425  1.00 33.73  ? 236 TRP A CB  1 
ATOM   1622  C CG  . TRP A 1 207 ? 34.425  -10.841 22.924  1.00 31.09  ? 236 TRP A CG  1 
ATOM   1623  C CD1 . TRP A 1 207 ? 34.621  -10.091 24.041  1.00 33.56  ? 236 TRP A CD1 1 
ATOM   1624  C CD2 . TRP A 1 207 ? 33.394  -10.191 22.169  1.00 28.27  ? 236 TRP A CD2 1 
ATOM   1625  N NE1 . TRP A 1 207 ? 33.735  -9.050  24.067  1.00 29.37  ? 236 TRP A NE1 1 
ATOM   1626  C CE2 . TRP A 1 207 ? 32.981  -9.076  22.921  1.00 24.91  ? 236 TRP A CE2 1 
ATOM   1627  C CE3 . TRP A 1 207 ? 32.805  -10.445 20.917  1.00 28.01  ? 236 TRP A CE3 1 
ATOM   1628  C CZ2 . TRP A 1 207 ? 31.996  -8.216  22.457  1.00 24.03  ? 236 TRP A CZ2 1 
ATOM   1629  C CZ3 . TRP A 1 207 ? 31.809  -9.614  20.477  1.00 26.40  ? 236 TRP A CZ3 1 
ATOM   1630  C CH2 . TRP A 1 207 ? 31.411  -8.505  21.246  1.00 24.13  ? 236 TRP A CH2 1 
ATOM   1631  N N   . SER A 1 208 ? 33.331  -14.549 21.912  1.00 28.66  ? 237 SER A N   1 
ATOM   1632  C CA  . SER A 1 208 ? 31.989  -15.114 21.795  1.00 29.34  ? 237 SER A CA  1 
ATOM   1633  C C   . SER A 1 208 ? 31.844  -16.389 22.643  1.00 33.50  ? 237 SER A C   1 
ATOM   1634  O O   . SER A 1 208 ? 30.778  -16.714 23.171  1.00 28.80  ? 237 SER A O   1 
ATOM   1635  C CB  . SER A 1 208 ? 31.637  -15.422 20.402  1.00 28.72  ? 237 SER A CB  1 
ATOM   1636  O OG  . SER A 1 208 ? 31.797  -14.308 19.557  1.00 34.76  ? 237 SER A OG  1 
ATOM   1637  N N   . HIS A 1 209 ? 32.944  -17.118 22.822  1.00 36.06  ? 238 HIS A N   1 
ATOM   1638  C CA  . HIS A 1 209 ? 32.884  -18.344 23.609  1.00 36.22  ? 238 HIS A CA  1 
ATOM   1639  C C   . HIS A 1 209 ? 32.803  -18.017 25.109  1.00 34.05  ? 238 HIS A C   1 
ATOM   1640  O O   . HIS A 1 209 ? 32.023  -18.622 25.846  1.00 36.95  ? 238 HIS A O   1 
ATOM   1641  C CB  . HIS A 1 209 ? 33.997  -19.288 23.139  1.00 36.53  ? 238 HIS A CB  1 
ATOM   1642  C CG  . HIS A 1 209 ? 33.874  -20.650 23.681  1.00 42.52  ? 238 HIS A CG  1 
ATOM   1643  N ND1 . HIS A 1 209 ? 34.852  -21.602 23.512  1.00 42.62  ? 238 HIS A ND1 1 
ATOM   1644  C CD2 . HIS A 1 209 ? 32.860  -21.238 24.350  1.00 39.39  ? 238 HIS A CD2 1 
ATOM   1645  C CE1 . HIS A 1 209 ? 34.444  -22.721 24.098  1.00 41.48  ? 238 HIS A CE1 1 
ATOM   1646  N NE2 . HIS A 1 209 ? 33.242  -22.516 24.620  1.00 38.91  ? 238 HIS A NE2 1 
ATOM   1647  N N   . ASN A 1 210 ? 33.618  -17.081 25.603  1.00 34.93  ? 239 ASN A N   1 
ATOM   1648  C CA  . ASN A 1 210 ? 33.486  -16.635 26.982  1.00 34.40  ? 239 ASN A CA  1 
ATOM   1649  C C   . ASN A 1 210 ? 32.061  -16.156 27.230  1.00 35.87  ? 239 ASN A C   1 
ATOM   1650  O O   . ASN A 1 210 ? 31.508  -16.420 28.291  1.00 32.30  ? 239 ASN A O   1 
ATOM   1651  C CB  . ASN A 1 210 ? 34.448  -15.506 27.359  1.00 38.38  ? 239 ASN A CB  1 
ATOM   1652  C CG  . ASN A 1 210 ? 35.830  -15.988 27.747  1.00 36.07  ? 239 ASN A CG  1 
ATOM   1653  O OD1 . ASN A 1 210 ? 36.843  -15.411 27.345  1.00 41.00  ? 239 ASN A OD1 1 
ATOM   1654  N ND2 . ASN A 1 210 ? 35.909  -17.005 28.578  1.00 33.36  ? 239 ASN A ND2 1 
ATOM   1655  N N   . PHE A 1 211 ? 31.461  -15.464 26.244  1.00 33.39  ? 240 PHE A N   1 
ATOM   1656  C CA  . PHE A 1 211 ? 30.117  -14.926 26.415  1.00 33.13  ? 240 PHE A CA  1 
ATOM   1657  C C   . PHE A 1 211 ? 29.088  -16.058 26.524  1.00 34.73  ? 240 PHE A C   1 
ATOM   1658  O O   . PHE A 1 211 ? 28.226  -16.000 27.389  1.00 30.08  ? 240 PHE A O   1 
ATOM   1659  C CB  . PHE A 1 211 ? 29.758  -13.967 25.271  1.00 29.87  ? 240 PHE A CB  1 
ATOM   1660  C CG  . PHE A 1 211 ? 28.405  -13.268 25.321  1.00 29.17  ? 240 PHE A CG  1 
ATOM   1661  C CD1 . PHE A 1 211 ? 27.772  -12.989 26.528  1.00 27.74  ? 240 PHE A CD1 1 
ATOM   1662  C CD2 . PHE A 1 211 ? 27.779  -12.871 24.143  1.00 29.35  ? 240 PHE A CD2 1 
ATOM   1663  C CE1 . PHE A 1 211 ? 26.546  -12.359 26.554  1.00 30.01  ? 240 PHE A CE1 1 
ATOM   1664  C CE2 . PHE A 1 211 ? 26.564  -12.200 24.171  1.00 30.58  ? 240 PHE A CE2 1 
ATOM   1665  C CZ  . PHE A 1 211 ? 25.969  -11.912 25.379  1.00 30.92  ? 240 PHE A CZ  1 
ATOM   1666  N N   . THR A 1 212 ? 29.143  -17.068 25.638  1.00 31.91  ? 241 THR A N   1 
ATOM   1667  C CA  . THR A 1 212 ? 28.204  -18.170 25.739  1.00 29.35  ? 241 THR A CA  1 
ATOM   1668  C C   . THR A 1 212 ? 28.440  -18.960 27.030  1.00 31.95  ? 241 THR A C   1 
ATOM   1669  O O   . THR A 1 212 ? 27.474  -19.427 27.619  1.00 32.48  ? 241 THR A O   1 
ATOM   1670  C CB  . THR A 1 212 ? 28.180  -19.066 24.492  1.00 30.61  ? 241 THR A CB  1 
ATOM   1671  O OG1 . THR A 1 212 ? 29.442  -19.686 24.297  1.00 31.72  ? 241 THR A OG1 1 
ATOM   1672  C CG2 . THR A 1 212 ? 27.811  -18.282 23.242  1.00 31.67  ? 241 THR A CG2 1 
ATOM   1673  N N   . ASN A 1 213 ? 29.697  -19.092 27.488  1.00 36.04  ? 242 ASN A N   1 
ATOM   1674  C CA  . ASN A 1 213 ? 29.972  -19.684 28.793  1.00 35.16  ? 242 ASN A CA  1 
ATOM   1675  C C   . ASN A 1 213 ? 29.253  -18.920 29.899  1.00 35.02  ? 242 ASN A C   1 
ATOM   1676  O O   . ASN A 1 213 ? 28.742  -19.538 30.819  1.00 37.43  ? 242 ASN A O   1 
ATOM   1677  C CB  . ASN A 1 213 ? 31.452  -19.792 29.141  1.00 36.30  ? 242 ASN A CB  1 
ATOM   1678  C CG  . ASN A 1 213 ? 32.112  -20.930 28.409  1.00 36.94  ? 242 ASN A CG  1 
ATOM   1679  O OD1 . ASN A 1 213 ? 31.449  -21.673 27.685  1.00 38.03  ? 242 ASN A OD1 1 
ATOM   1680  N ND2 . ASN A 1 213 ? 33.418  -21.040 28.521  1.00 37.02  ? 242 ASN A ND2 1 
ATOM   1681  N N   . MET A 1 214 ? 29.205  -17.590 29.827  1.00 37.75  ? 243 MET A N   1 
ATOM   1682  C CA  . MET A 1 214 ? 28.639  -16.798 30.911  1.00 34.19  ? 243 MET A CA  1 
ATOM   1683  C C   . MET A 1 214 ? 27.115  -16.795 30.864  1.00 32.36  ? 243 MET A C   1 
ATOM   1684  O O   . MET A 1 214 ? 26.472  -16.714 31.911  1.00 32.03  ? 243 MET A O   1 
ATOM   1685  C CB  . MET A 1 214 ? 29.139  -15.352 30.845  1.00 38.86  ? 243 MET A CB  1 
ATOM   1686  C CG  . MET A 1 214 ? 30.604  -15.225 31.163  1.00 40.76  ? 243 MET A CG  1 
ATOM   1687  S SD  . MET A 1 214 ? 31.091  -13.494 31.276  1.00 37.68  ? 243 MET A SD  1 
ATOM   1688  C CE  . MET A 1 214 ? 31.347  -13.115 29.534  1.00 38.93  ? 243 MET A CE  1 
ATOM   1689  N N   . LEU A 1 215 ? 26.549  -16.866 29.651  1.00 34.19  ? 244 LEU A N   1 
ATOM   1690  C CA  . LEU A 1 215 ? 25.106  -16.997 29.433  1.00 38.20  ? 244 LEU A CA  1 
ATOM   1691  C C   . LEU A 1 215 ? 24.561  -18.310 30.005  1.00 44.48  ? 244 LEU A C   1 
ATOM   1692  O O   . LEU A 1 215 ? 23.390  -18.379 30.396  1.00 46.68  ? 244 LEU A O   1 
ATOM   1693  C CB  . LEU A 1 215 ? 24.801  -16.946 27.934  1.00 35.26  ? 244 LEU A CB  1 
ATOM   1694  C CG  . LEU A 1 215 ? 24.812  -15.566 27.277  1.00 33.45  ? 244 LEU A CG  1 
ATOM   1695  C CD1 . LEU A 1 215 ? 24.515  -15.625 25.796  1.00 33.11  ? 244 LEU A CD1 1 
ATOM   1696  C CD2 . LEU A 1 215 ? 23.807  -14.649 27.944  1.00 36.40  ? 244 LEU A CD2 1 
ATOM   1697  N N   . GLY A 1 216 ? 25.396  -19.363 29.998  1.00 36.65  ? 245 GLY A N   1 
ATOM   1698  C CA  . GLY A 1 216 ? 24.999  -20.653 30.532  1.00 39.81  ? 245 GLY A CA  1 
ATOM   1699  C C   . GLY A 1 216 ? 24.795  -21.686 29.427  1.00 39.06  ? 245 GLY A C   1 
ATOM   1700  O O   . GLY A 1 216 ? 24.083  -22.657 29.615  1.00 42.67  ? 245 GLY A O   1 
ATOM   1701  N N   . TYR A 1 217 ? 25.426  -21.492 28.277  1.00 38.49  ? 246 TYR A N   1 
ATOM   1702  C CA  . TYR A 1 217 ? 25.249  -22.423 27.177  1.00 44.01  ? 246 TYR A CA  1 
ATOM   1703  C C   . TYR A 1 217 ? 26.539  -23.207 26.985  1.00 46.06  ? 246 TYR A C   1 
ATOM   1704  O O   . TYR A 1 217 ? 27.616  -22.705 27.275  1.00 49.01  ? 246 TYR A O   1 
ATOM   1705  C CB  . TYR A 1 217 ? 24.810  -21.627 25.955  1.00 39.07  ? 246 TYR A CB  1 
ATOM   1706  C CG  . TYR A 1 217 ? 23.390  -21.105 26.036  1.00 38.01  ? 246 TYR A CG  1 
ATOM   1707  C CD1 . TYR A 1 217 ? 23.033  -20.098 26.924  1.00 37.94  ? 246 TYR A CD1 1 
ATOM   1708  C CD2 . TYR A 1 217 ? 22.398  -21.620 25.215  1.00 42.64  ? 246 TYR A CD2 1 
ATOM   1709  C CE1 . TYR A 1 217 ? 21.740  -19.610 26.982  1.00 35.34  ? 246 TYR A CE1 1 
ATOM   1710  C CE2 . TYR A 1 217 ? 21.098  -21.142 25.265  1.00 38.40  ? 246 TYR A CE2 1 
ATOM   1711  C CZ  . TYR A 1 217 ? 20.775  -20.124 26.141  1.00 34.77  ? 246 TYR A CZ  1 
ATOM   1712  O OH  . TYR A 1 217 ? 19.491  -19.682 26.154  1.00 30.06  ? 246 TYR A OH  1 
ATOM   1713  N N   . THR A 1 218 ? 26.412  -24.465 26.557  1.00 51.99  ? 247 THR A N   1 
ATOM   1714  C CA  . THR A 1 218 ? 27.563  -25.339 26.372  1.00 55.51  ? 247 THR A CA  1 
ATOM   1715  C C   . THR A 1 218 ? 27.337  -26.142 25.101  1.00 53.61  ? 247 THR A C   1 
ATOM   1716  O O   . THR A 1 218 ? 27.218  -27.363 25.141  1.00 71.56  ? 247 THR A O   1 
ATOM   1717  C CB  . THR A 1 218 ? 27.734  -26.277 27.573  1.00 63.58  ? 247 THR A CB  1 
ATOM   1718  O OG1 . THR A 1 218 ? 27.482  -25.523 28.757  1.00 65.20  ? 247 THR A OG1 1 
ATOM   1719  C CG2 . THR A 1 218 ? 29.104  -26.941 27.599  1.00 67.07  ? 247 THR A CG2 1 
ATOM   1720  N N   . ASP A 1 219 ? 27.253  -25.429 23.987  1.00 43.97  ? 248 ASP A N   1 
ATOM   1721  C CA  . ASP A 1 219 ? 26.819  -25.995 22.733  1.00 41.14  ? 248 ASP A CA  1 
ATOM   1722  C C   . ASP A 1 219 ? 27.655  -25.369 21.608  1.00 44.02  ? 248 ASP A C   1 
ATOM   1723  O O   . ASP A 1 219 ? 27.529  -24.187 21.283  1.00 36.70  ? 248 ASP A O   1 
ATOM   1724  C CB  . ASP A 1 219 ? 25.311  -25.864 22.631  1.00 43.16  ? 248 ASP A CB  1 
ATOM   1725  C CG  . ASP A 1 219 ? 24.697  -26.453 21.370  1.00 50.52  ? 248 ASP A CG  1 
ATOM   1726  O OD1 . ASP A 1 219 ? 25.441  -26.608 20.368  1.00 59.78  ? 248 ASP A OD1 1 
ATOM   1727  O OD2 . ASP A 1 219 ? 23.490  -26.770 21.389  1.00 56.03  ? 248 ASP A OD2 1 
ATOM   1728  N N   . HIS A 1 220 ? 28.491  -26.193 20.975  1.00 42.37  ? 249 HIS A N   1 
ATOM   1729  C CA  . HIS A 1 220 ? 29.427  -25.727 19.968  1.00 44.41  ? 249 HIS A CA  1 
ATOM   1730  C C   . HIS A 1 220 ? 28.702  -24.887 18.919  1.00 40.64  ? 249 HIS A C   1 
ATOM   1731  O O   . HIS A 1 220 ? 29.223  -23.848 18.496  1.00 39.35  ? 249 HIS A O   1 
ATOM   1732  C CB  . HIS A 1 220 ? 30.175  -26.906 19.333  1.00 47.15  ? 249 HIS A CB  1 
ATOM   1733  C CG  . HIS A 1 220 ? 31.039  -26.475 18.202  1.00 49.27  ? 249 HIS A CG  1 
ATOM   1734  N ND1 . HIS A 1 220 ? 32.164  -25.699 18.386  1.00 48.41  ? 249 HIS A ND1 1 
ATOM   1735  C CD2 . HIS A 1 220 ? 30.900  -26.638 16.880  1.00 51.08  ? 249 HIS A CD2 1 
ATOM   1736  C CE1 . HIS A 1 220 ? 32.698  -25.442 17.197  1.00 50.48  ? 249 HIS A CE1 1 
ATOM   1737  N NE2 . HIS A 1 220 ? 31.948  -26.004 16.270  1.00 51.11  ? 249 HIS A NE2 1 
ATOM   1738  N N   . GLN A 1 221 ? 27.531  -25.369 18.481  1.00 34.85  ? 250 GLN A N   1 
ATOM   1739  C CA  . GLN A 1 221 ? 26.836  -24.747 17.372  1.00 38.59  ? 250 GLN A CA  1 
ATOM   1740  C C   . GLN A 1 221 ? 26.181  -23.462 17.881  1.00 34.20  ? 250 GLN A C   1 
ATOM   1741  O O   . GLN A 1 221 ? 26.014  -22.538 17.102  1.00 32.83  ? 250 GLN A O   1 
ATOM   1742  C CB  . GLN A 1 221 ? 25.845  -25.620 16.589  1.00 42.55  ? 250 GLN A CB  1 
ATOM   1743  C CG  . GLN A 1 221 ? 26.484  -26.584 15.584  1.00 46.30  ? 250 GLN A CG  1 
ATOM   1744  C CD  . GLN A 1 221 ? 27.564  -25.989 14.686  1.00 57.18  ? 250 GLN A CD  1 
ATOM   1745  O OE1 . GLN A 1 221 ? 27.468  -24.872 14.153  1.00 57.00  ? 250 GLN A OE1 1 
ATOM   1746  N NE2 . GLN A 1 221 ? 28.613  -26.763 14.435  1.00 58.56  ? 250 GLN A NE2 1 
ATOM   1747  N N   . PHE A 1 222 ? 25.832  -23.385 19.166  1.00 32.42  ? 251 PHE A N   1 
ATOM   1748  C CA  . PHE A 1 222 ? 25.333  -22.124 19.692  1.00 34.46  ? 251 PHE A CA  1 
ATOM   1749  C C   . PHE A 1 222 ? 26.430  -21.048 19.679  1.00 33.52  ? 251 PHE A C   1 
ATOM   1750  O O   . PHE A 1 222 ? 26.206  -19.918 19.263  1.00 37.20  ? 251 PHE A O   1 
ATOM   1751  C CB  . PHE A 1 222 ? 24.772  -22.235 21.099  1.00 32.90  ? 251 PHE A CB  1 
ATOM   1752  C CG  . PHE A 1 222 ? 24.101  -20.928 21.485  1.00 37.99  ? 251 PHE A CG  1 
ATOM   1753  C CD1 . PHE A 1 222 ? 23.113  -20.367 20.675  1.00 39.11  ? 251 PHE A CD1 1 
ATOM   1754  C CD2 . PHE A 1 222 ? 24.487  -20.246 22.628  1.00 37.82  ? 251 PHE A CD2 1 
ATOM   1755  C CE1 . PHE A 1 222 ? 22.477  -19.194 21.046  1.00 38.68  ? 251 PHE A CE1 1 
ATOM   1756  C CE2 . PHE A 1 222 ? 23.848  -19.063 22.990  1.00 42.05  ? 251 PHE A CE2 1 
ATOM   1757  C CZ  . PHE A 1 222 ? 22.854  -18.535 22.202  1.00 38.40  ? 251 PHE A CZ  1 
ATOM   1758  N N   . THR A 1 223 ? 27.611  -21.387 20.182  1.00 35.58  ? 252 THR A N   1 
ATOM   1759  C CA  . THR A 1 223 ? 28.769  -20.524 20.097  1.00 37.03  ? 252 THR A CA  1 
ATOM   1760  C C   . THR A 1 223 ? 29.036  -20.114 18.651  1.00 31.67  ? 252 THR A C   1 
ATOM   1761  O O   . THR A 1 223 ? 29.394  -18.969 18.435  1.00 31.41  ? 252 THR A O   1 
ATOM   1762  C CB  . THR A 1 223 ? 29.958  -21.235 20.741  1.00 38.25  ? 252 THR A CB  1 
ATOM   1763  O OG1 . THR A 1 223 ? 29.555  -21.421 22.102  1.00 30.55  ? 252 THR A OG1 1 
ATOM   1764  C CG2 . THR A 1 223 ? 31.206  -20.374 20.680  1.00 37.87  ? 252 THR A CG2 1 
ATOM   1765  N N   . GLU A 1 224 ? 28.892  -21.035 17.683  1.00 31.55  ? 253 GLU A N   1 
ATOM   1766  C CA  . GLU A 1 224 ? 29.118  -20.724 16.280  1.00 33.04  ? 253 GLU A CA  1 
ATOM   1767  C C   . GLU A 1 224 ? 28.110  -19.686 15.795  1.00 30.58  ? 253 GLU A C   1 
ATOM   1768  O O   . GLU A 1 224 ? 28.476  -18.801 15.048  1.00 31.08  ? 253 GLU A O   1 
ATOM   1769  C CB  . GLU A 1 224 ? 29.129  -21.991 15.414  1.00 34.35  ? 253 GLU A CB  1 
ATOM   1770  C CG  . GLU A 1 224 ? 30.429  -22.777 15.613  1.00 32.14  ? 253 GLU A CG  1 
ATOM   1771  C CD  . GLU A 1 224 ? 31.602  -22.204 14.835  1.00 31.18  ? 253 GLU A CD  1 
ATOM   1772  O OE1 . GLU A 1 224 ? 31.634  -22.399 13.610  1.00 47.48  ? 253 GLU A OE1 1 
ATOM   1773  O OE2 . GLU A 1 224 ? 32.486  -21.533 15.391  1.00 30.89  ? 253 GLU A OE2 1 
ATOM   1774  N N   . LEU A 1 225 ? 26.841  -19.812 16.172  1.00 30.37  ? 254 LEU A N   1 
ATOM   1775  C CA  . LEU A 1 225 ? 25.814  -18.893 15.721  1.00 34.76  ? 254 LEU A CA  1 
ATOM   1776  C C   . LEU A 1 225 ? 26.090  -17.489 16.270  1.00 34.79  ? 254 LEU A C   1 
ATOM   1777  O O   . LEU A 1 225 ? 25.885  -16.476 15.574  1.00 30.90  ? 254 LEU A O   1 
ATOM   1778  C CB  . LEU A 1 225 ? 24.444  -19.387 16.182  1.00 34.77  ? 254 LEU A CB  1 
ATOM   1779  C CG  . LEU A 1 225 ? 23.282  -18.418 15.946  1.00 35.08  ? 254 LEU A CG  1 
ATOM   1780  C CD1 . LEU A 1 225 ? 23.132  -18.126 14.463  1.00 30.91  ? 254 LEU A CD1 1 
ATOM   1781  C CD2 . LEU A 1 225 ? 21.997  -18.953 16.524  1.00 32.25  ? 254 LEU A CD2 1 
ATOM   1782  N N   . THR A 1 226 ? 26.518  -17.450 17.532  1.00 30.03  ? 255 THR A N   1 
ATOM   1783  C CA  . THR A 1 226 ? 26.896  -16.219 18.212  1.00 30.24  ? 255 THR A CA  1 
ATOM   1784  C C   . THR A 1 226 ? 28.052  -15.564 17.462  1.00 35.77  ? 255 THR A C   1 
ATOM   1785  O O   . THR A 1 226 ? 27.993  -14.382 17.132  1.00 30.56  ? 255 THR A O   1 
ATOM   1786  C CB  . THR A 1 226 ? 27.252  -16.540 19.658  1.00 31.09  ? 255 THR A CB  1 
ATOM   1787  O OG1 . THR A 1 226 ? 26.033  -17.037 20.206  1.00 32.67  ? 255 THR A OG1 1 
ATOM   1788  C CG2 . THR A 1 226 ? 27.626  -15.330 20.489  1.00 31.43  ? 255 THR A CG2 1 
ATOM   1789  N N   . ARG A 1 227 ? 29.080  -16.344 17.136  1.00 28.81  ? 256 ARG A N   1 
ATOM   1790  C CA  . ARG A 1 227 ? 30.201  -15.780 16.415  1.00 28.93  ? 256 ARG A CA  1 
ATOM   1791  C C   . ARG A 1 227 ? 29.688  -15.144 15.146  1.00 26.35  ? 256 ARG A C   1 
ATOM   1792  O O   . ARG A 1 227 ? 30.078  -14.017 14.838  1.00 32.33  ? 256 ARG A O   1 
ATOM   1793  C CB  . ARG A 1 227 ? 31.257  -16.841 16.091  1.00 30.89  ? 256 ARG A CB  1 
ATOM   1794  C CG  . ARG A 1 227 ? 32.036  -17.224 17.330  1.00 31.50  ? 256 ARG A CG  1 
ATOM   1795  C CD  . ARG A 1 227 ? 32.755  -18.534 17.093  1.00 36.54  ? 256 ARG A CD  1 
ATOM   1796  N NE  . ARG A 1 227 ? 33.472  -18.921 18.304  1.00 36.96  ? 256 ARG A NE  1 
ATOM   1797  C CZ  . ARG A 1 227 ? 33.657  -20.168 18.730  1.00 41.82  ? 256 ARG A CZ  1 
ATOM   1798  N NH1 . ARG A 1 227 ? 33.061  -21.214 18.171  1.00 42.81  ? 256 ARG A NH1 1 
ATOM   1799  N NH2 . ARG A 1 227 ? 34.443  -20.353 19.761  1.00 37.23  ? 256 ARG A NH2 1 
ATOM   1800  N N   . LEU A 1 228 ? 28.782  -15.846 14.447  1.00 26.77  ? 257 LEU A N   1 
ATOM   1801  C CA  . LEU A 1 228 ? 28.192  -15.318 13.224  1.00 30.68  ? 257 LEU A CA  1 
ATOM   1802  C C   . LEU A 1 228 ? 27.337  -14.087 13.527  1.00 28.15  ? 257 LEU A C   1 
ATOM   1803  O O   . LEU A 1 228 ? 27.416  -13.095 12.806  1.00 27.74  ? 257 LEU A O   1 
ATOM   1804  C CB  . LEU A 1 228 ? 27.396  -16.392 12.484  1.00 33.61  ? 257 LEU A CB  1 
ATOM   1805  C CG  . LEU A 1 228 ? 26.743  -15.970 11.165  1.00 32.70  ? 257 LEU A CG  1 
ATOM   1806  C CD1 . LEU A 1 228 ? 27.796  -15.601 10.161  1.00 34.34  ? 257 LEU A CD1 1 
ATOM   1807  C CD2 . LEU A 1 228 ? 25.800  -16.997 10.574  1.00 33.65  ? 257 LEU A CD2 1 
ATOM   1808  N N   . TYR A 1 229 ? 26.495  -14.169 14.555  1.00 29.72  ? 258 TYR A N   1 
ATOM   1809  C CA  . TYR A 1 229 ? 25.517  -13.133 14.842  1.00 30.72  ? 258 TYR A CA  1 
ATOM   1810  C C   . TYR A 1 229 ? 26.247  -11.842 15.199  1.00 29.44  ? 258 TYR A C   1 
ATOM   1811  O O   . TYR A 1 229 ? 25.860  -10.768 14.769  1.00 27.78  ? 258 TYR A O   1 
ATOM   1812  C CB  . TYR A 1 229 ? 24.598  -13.642 15.955  1.00 34.24  ? 258 TYR A CB  1 
ATOM   1813  C CG  . TYR A 1 229 ? 23.567  -12.616 16.399  1.00 41.65  ? 258 TYR A CG  1 
ATOM   1814  C CD1 . TYR A 1 229 ? 23.930  -11.600 17.268  1.00 45.01  ? 258 TYR A CD1 1 
ATOM   1815  C CD2 . TYR A 1 229 ? 22.242  -12.678 15.991  1.00 45.45  ? 258 TYR A CD2 1 
ATOM   1816  C CE1 . TYR A 1 229 ? 23.021  -10.646 17.684  1.00 47.16  ? 258 TYR A CE1 1 
ATOM   1817  C CE2 . TYR A 1 229 ? 21.311  -11.739 16.410  1.00 45.99  ? 258 TYR A CE2 1 
ATOM   1818  C CZ  . TYR A 1 229 ? 21.714  -10.705 17.237  1.00 47.41  ? 258 TYR A CZ  1 
ATOM   1819  O OH  . TYR A 1 229 ? 20.870  -9.745  17.711  1.00 53.07  ? 258 TYR A OH  1 
ATOM   1820  N N   . LEU A 1 230 ? 27.350  -11.976 15.938  1.00 30.50  ? 259 LEU A N   1 
ATOM   1821  C CA  . LEU A 1 230 ? 28.062  -10.848 16.478  1.00 28.89  ? 259 LEU A CA  1 
ATOM   1822  C C   . LEU A 1 230 ? 28.898  -10.182 15.386  1.00 31.30  ? 259 LEU A C   1 
ATOM   1823  O O   . LEU A 1 230 ? 29.057  -8.981  15.476  1.00 30.79  ? 259 LEU A O   1 
ATOM   1824  C CB  . LEU A 1 230 ? 28.878  -11.211 17.707  1.00 25.71  ? 259 LEU A CB  1 
ATOM   1825  C CG  . LEU A 1 230 ? 28.074  -11.529 18.969  1.00 26.92  ? 259 LEU A CG  1 
ATOM   1826  C CD1 . LEU A 1 230 ? 28.977  -11.930 20.075  1.00 28.13  ? 259 LEU A CD1 1 
ATOM   1827  C CD2 . LEU A 1 230 ? 27.228  -10.343 19.441  1.00 29.75  ? 259 LEU A CD2 1 
ATOM   1828  N N   . THR A 1 231 ? 29.312  -10.920 14.338  1.00 25.00  ? 260 THR A N   1 
ATOM   1829  C CA  . THR A 1 231 ? 30.023  -10.350 13.205  1.00 24.42  ? 260 THR A CA  1 
ATOM   1830  C C   . THR A 1 231 ? 29.063  -9.553  12.340  1.00 24.12  ? 260 THR A C   1 
ATOM   1831  O O   . THR A 1 231 ? 29.361  -8.434  11.926  1.00 27.29  ? 260 THR A O   1 
ATOM   1832  C CB  . THR A 1 231 ? 30.665  -11.455 12.350  1.00 25.30  ? 260 THR A CB  1 
ATOM   1833  O OG1 . THR A 1 231 ? 31.741  -12.006 13.085  1.00 23.55  ? 260 THR A OG1 1 
ATOM   1834  C CG2 . THR A 1 231 ? 31.243  -10.928 11.058  1.00 26.76  ? 260 THR A CG2 1 
ATOM   1835  N N   . ILE A 1 232 ? 27.918  -10.133 12.014  1.00 27.67  ? 261 ILE A N   1 
ATOM   1836  C CA  . ILE A 1 232 ? 27.114  -9.565  10.938  1.00 34.30  ? 261 ILE A CA  1 
ATOM   1837  C C   . ILE A 1 232 ? 26.226  -8.414  11.418  1.00 33.78  ? 261 ILE A C   1 
ATOM   1838  O O   . ILE A 1 232 ? 25.827  -7.600  10.598  1.00 27.96  ? 261 ILE A O   1 
ATOM   1839  C CB  . ILE A 1 232 ? 26.279  -10.624 10.207  1.00 34.41  ? 261 ILE A CB  1 
ATOM   1840  C CG1 . ILE A 1 232 ? 25.202  -11.219 11.106  1.00 35.46  ? 261 ILE A CG1 1 
ATOM   1841  C CG2 . ILE A 1 232 ? 27.210  -11.669 9.583   1.00 35.80  ? 261 ILE A CG2 1 
ATOM   1842  C CD1 . ILE A 1 232 ? 24.145  -12.023 10.363  1.00 36.94  ? 261 ILE A CD1 1 
ATOM   1843  N N   . HIS A 1 233 ? 25.919  -8.358  12.716  1.00 27.91  ? 262 HIS A N   1 
ATOM   1844  C CA  . HIS A 1 233 ? 25.176  -7.227  13.253  1.00 34.50  ? 262 HIS A CA  1 
ATOM   1845  C C   . HIS A 1 233 ? 26.082  -6.046  13.650  1.00 28.16  ? 262 HIS A C   1 
ATOM   1846  O O   . HIS A 1 233 ? 25.609  -5.053  14.174  1.00 28.66  ? 262 HIS A O   1 
ATOM   1847  C CB  . HIS A 1 233 ? 24.374  -7.658  14.487  1.00 33.82  ? 262 HIS A CB  1 
ATOM   1848  C CG  . HIS A 1 233 ? 23.144  -8.439  14.175  1.00 40.34  ? 262 HIS A CG  1 
ATOM   1849  N ND1 . HIS A 1 233 ? 23.177  -9.810  14.006  1.00 40.91  ? 262 HIS A ND1 1 
ATOM   1850  C CD2 . HIS A 1 233 ? 21.848  -8.054  14.001  1.00 41.90  ? 262 HIS A CD2 1 
ATOM   1851  C CE1 . HIS A 1 233 ? 21.941  -10.229 13.744  1.00 44.34  ? 262 HIS A CE1 1 
ATOM   1852  N NE2 . HIS A 1 233 ? 21.121  -9.187  13.735  1.00 42.06  ? 262 HIS A NE2 1 
ATOM   1853  N N   . SER A 1 234 ? 27.375  -6.138  13.400  1.00 28.91  ? 263 SER A N   1 
ATOM   1854  C CA  . SER A 1 234 ? 28.344  -5.267  14.034  1.00 28.36  ? 263 SER A CA  1 
ATOM   1855  C C   . SER A 1 234 ? 28.235  -3.810  13.587  1.00 26.99  ? 263 SER A C   1 
ATOM   1856  O O   . SER A 1 234 ? 28.557  -2.906  14.340  1.00 30.04  ? 263 SER A O   1 
ATOM   1857  C CB  . SER A 1 234 ? 29.719  -5.792  13.765  1.00 31.43  ? 263 SER A CB  1 
ATOM   1858  O OG  . SER A 1 234 ? 29.969  -5.771  12.370  1.00 36.66  ? 263 SER A OG  1 
ATOM   1859  N N   . ASP A 1 235 ? 27.867  -3.587  12.334  1.00 29.66  ? 264 ASP A N   1 
ATOM   1860  C CA  . ASP A 1 235 ? 27.964  -2.275  11.734  1.00 30.57  ? 264 ASP A CA  1 
ATOM   1861  C C   . ASP A 1 235 ? 27.050  -2.231  10.516  1.00 26.69  ? 264 ASP A C   1 
ATOM   1862  O O   . ASP A 1 235 ? 26.951  -3.190  9.764   1.00 27.61  ? 264 ASP A O   1 
ATOM   1863  C CB  . ASP A 1 235 ? 29.410  -1.925  11.407  1.00 32.43  ? 264 ASP A CB  1 
ATOM   1864  C CG  . ASP A 1 235 ? 29.738  -0.435  11.403  1.00 38.77  ? 264 ASP A CG  1 
ATOM   1865  O OD1 . ASP A 1 235 ? 29.189  0.307   12.286  1.00 38.15  ? 264 ASP A OD1 1 
ATOM   1866  O OD2 . ASP A 1 235 ? 30.569  -0.025  10.557  1.00 39.54  ? 264 ASP A OD2 1 
ATOM   1867  N N   . HIS A 1 236 ? 26.450  -1.076  10.266  1.00 27.63  ? 265 HIS A N   1 
ATOM   1868  C CA  . HIS A 1 236 ? 25.566  -0.956  9.116   1.00 27.27  ? 265 HIS A CA  1 
ATOM   1869  C C   . HIS A 1 236 ? 25.574  0.491   8.631   1.00 25.11  ? 265 HIS A C   1 
ATOM   1870  O O   . HIS A 1 236 ? 24.529  1.092   8.380   1.00 30.27  ? 265 HIS A O   1 
ATOM   1871  C CB  . HIS A 1 236 ? 24.202  -1.544  9.475   1.00 26.42  ? 265 HIS A CB  1 
ATOM   1872  C CG  . HIS A 1 236 ? 23.449  -2.097  8.319   1.00 28.67  ? 265 HIS A CG  1 
ATOM   1873  N ND1 . HIS A 1 236 ? 23.902  -3.177  7.580   1.00 32.62  ? 265 HIS A ND1 1 
ATOM   1874  C CD2 . HIS A 1 236 ? 22.292  -1.720  7.767   1.00 26.20  ? 265 HIS A CD2 1 
ATOM   1875  C CE1 . HIS A 1 236 ? 23.008  -3.447  6.636   1.00 30.70  ? 265 HIS A CE1 1 
ATOM   1876  N NE2 . HIS A 1 236 ? 22.026  -2.567  6.729   1.00 33.89  ? 265 HIS A NE2 1 
ATOM   1877  N N   . GLU A 1 237 ? 26.772  1.046   8.511   1.00 25.13  ? 266 GLU A N   1 
ATOM   1878  C CA  . GLU A 1 237 ? 26.893  2.406   8.052   1.00 34.41  ? 266 GLU A CA  1 
ATOM   1879  C C   . GLU A 1 237 ? 26.601  3.344   9.223   1.00 32.50  ? 266 GLU A C   1 
ATOM   1880  O O   . GLU A 1 237 ? 26.292  2.915   10.333  1.00 28.89  ? 266 GLU A O   1 
ATOM   1881  C CB  . GLU A 1 237 ? 25.836  2.693   6.981   1.00 39.46  ? 266 GLU A CB  1 
ATOM   1882  C CG  . GLU A 1 237 ? 26.412  2.989   5.618   1.00 49.04  ? 266 GLU A CG  1 
ATOM   1883  C CD  . GLU A 1 237 ? 25.411  3.738   4.761   1.00 48.35  ? 266 GLU A CD  1 
ATOM   1884  O OE1 . GLU A 1 237 ? 24.390  4.358   5.202   1.00 42.27  ? 266 GLU A OE1 1 
ATOM   1885  O OE2 . GLU A 1 237 ? 25.768  3.680   3.577   1.00 48.34  ? 266 GLU A OE2 1 
ATOM   1886  N N   . GLY A 1 238 ? 26.662  4.630   8.913   1.00 26.10  ? 267 GLY A N   1 
ATOM   1887  C CA  . GLY A 1 238 ? 26.587  5.662   9.921   1.00 27.05  ? 267 GLY A CA  1 
ATOM   1888  C C   . GLY A 1 238 ? 25.166  6.140   10.168  1.00 27.36  ? 267 GLY A C   1 
ATOM   1889  O O   . GLY A 1 238 ? 24.936  6.821   11.170  1.00 30.65  ? 267 GLY A O   1 
ATOM   1890  N N   . GLY A 1 239 ? 24.246  5.847   9.237   1.00 27.62  ? 268 GLY A N   1 
ATOM   1891  C CA  . GLY A 1 239 ? 22.962  6.514   9.225   1.00 26.66  ? 268 GLY A CA  1 
ATOM   1892  C C   . GLY A 1 239 ? 21.893  5.807   10.064  1.00 26.88  ? 268 GLY A C   1 
ATOM   1893  O O   . GLY A 1 239 ? 20.843  6.395   10.343  1.00 28.53  ? 268 GLY A O   1 
ATOM   1894  N N   . ASN A 1 240 ? 22.111  4.531   10.405  1.00 25.43  ? 269 ASN A N   1 
ATOM   1895  C CA  . ASN A 1 240 ? 21.187  3.807   11.258  1.00 24.75  ? 269 ASN A CA  1 
ATOM   1896  C C   . ASN A 1 240 ? 21.139  4.510   12.618  1.00 24.16  ? 269 ASN A C   1 
ATOM   1897  O O   . ASN A 1 240 ? 22.134  5.097   13.031  1.00 24.55  ? 269 ASN A O   1 
ATOM   1898  C CB  . ASN A 1 240 ? 21.585  2.340   11.338  1.00 23.78  ? 269 ASN A CB  1 
ATOM   1899  C CG  . ASN A 1 240 ? 22.790  2.094   12.217  1.00 30.93  ? 269 ASN A CG  1 
ATOM   1900  O OD1 . ASN A 1 240 ? 22.655  2.111   13.443  1.00 29.43  ? 269 ASN A OD1 1 
ATOM   1901  N ND2 . ASN A 1 240 ? 23.951  1.782   11.634  1.00 32.23  ? 269 ASN A ND2 1 
ATOM   1902  N N   . VAL A 1 241 ? 20.042  4.364   13.364  1.00 26.30  ? 270 VAL A N   1 
ATOM   1903  C CA  . VAL A 1 241 ? 19.831  5.186   14.558  1.00 25.28  ? 270 VAL A CA  1 
ATOM   1904  C C   . VAL A 1 241 ? 20.886  4.928   15.641  1.00 24.57  ? 270 VAL A C   1 
ATOM   1905  O O   . VAL A 1 241 ? 21.303  5.847   16.352  1.00 21.95  ? 270 VAL A O   1 
ATOM   1906  C CB  . VAL A 1 241 ? 18.397  5.032   15.094  1.00 25.18  ? 270 VAL A CB  1 
ATOM   1907  C CG1 . VAL A 1 241 ? 18.213  5.689   16.461  1.00 24.97  ? 270 VAL A CG1 1 
ATOM   1908  C CG2 . VAL A 1 241 ? 17.386  5.637   14.138  1.00 29.44  ? 270 VAL A CG2 1 
ATOM   1909  N N   . SER A 1 242 ? 21.339  3.681   15.786  1.00 23.94  ? 271 SER A N   1 
ATOM   1910  C CA  . SER A 1 242 ? 22.259  3.379   16.861  1.00 27.18  ? 271 SER A CA  1 
ATOM   1911  C C   . SER A 1 242 ? 23.641  3.967   16.551  1.00 27.98  ? 271 SER A C   1 
ATOM   1912  O O   . SER A 1 242 ? 24.187  4.640   17.409  1.00 25.21  ? 271 SER A O   1 
ATOM   1913  C CB  . SER A 1 242 ? 22.296  1.917   17.245  1.00 27.53  ? 271 SER A CB  1 
ATOM   1914  O OG  . SER A 1 242 ? 22.611  1.081   16.145  1.00 28.85  ? 271 SER A OG  1 
ATOM   1915  N N   . ALA A 1 243 ? 24.139  3.812   15.317  1.00 24.07  ? 272 ALA A N   1 
ATOM   1916  C CA  . ALA A 1 243 ? 25.441  4.323   14.942  1.00 26.03  ? 272 ALA A CA  1 
ATOM   1917  C C   . ALA A 1 243 ? 25.432  5.849   14.883  1.00 21.35  ? 272 ALA A C   1 
ATOM   1918  O O   . ALA A 1 243 ? 26.376  6.492   15.365  1.00 20.99  ? 272 ALA A O   1 
ATOM   1919  C CB  . ALA A 1 243 ? 25.890  3.732   13.621  1.00 23.76  ? 272 ALA A CB  1 
ATOM   1920  N N   . HIS A 1 244 ? 24.342  6.426   14.388  1.00 24.86  ? 273 HIS A N   1 
ATOM   1921  C CA  . HIS A 1 244 ? 24.247  7.880   14.286  1.00 24.52  ? 273 HIS A CA  1 
ATOM   1922  C C   . HIS A 1 244 ? 24.160  8.482   15.676  1.00 25.67  ? 273 HIS A C   1 
ATOM   1923  O O   . HIS A 1 244 ? 24.615  9.598   15.876  1.00 22.26  ? 273 HIS A O   1 
ATOM   1924  C CB  . HIS A 1 244 ? 22.987  8.303   13.529  1.00 25.79  ? 273 HIS A CB  1 
ATOM   1925  C CG  . HIS A 1 244 ? 22.860  9.750   13.170  1.00 23.10  ? 273 HIS A CG  1 
ATOM   1926  N ND1 . HIS A 1 244 ? 21.712  10.270  12.614  1.00 25.87  ? 273 HIS A ND1 1 
ATOM   1927  C CD2 . HIS A 1 244 ? 23.737  10.777  13.189  1.00 29.78  ? 273 HIS A CD2 1 
ATOM   1928  C CE1 . HIS A 1 244 ? 21.876  11.559  12.354  1.00 26.45  ? 273 HIS A CE1 1 
ATOM   1929  N NE2 . HIS A 1 244 ? 23.089  11.895  12.714  1.00 29.29  ? 273 HIS A NE2 1 
ATOM   1930  N N   . THR A 1 245 ? 23.517  7.776   16.617  1.00 23.21  ? 274 THR A N   1 
ATOM   1931  C CA  . THR A 1 245 ? 23.377  8.328   17.958  1.00 22.11  ? 274 THR A CA  1 
ATOM   1932  C C   . THR A 1 245 ? 24.746  8.340   18.612  1.00 18.81  ? 274 THR A C   1 
ATOM   1933  O O   . THR A 1 245 ? 25.115  9.325   19.239  1.00 21.89  ? 274 THR A O   1 
ATOM   1934  C CB  . THR A 1 245 ? 22.357  7.521   18.778  1.00 25.69  ? 274 THR A CB  1 
ATOM   1935  O OG1 . THR A 1 245 ? 21.108  7.794   18.136  1.00 25.08  ? 274 THR A OG1 1 
ATOM   1936  C CG2 . THR A 1 245 ? 22.272  7.942   20.232  1.00 22.87  ? 274 THR A CG2 1 
ATOM   1937  N N   . SER A 1 246 ? 25.511  7.251   18.453  1.00 19.45  ? 275 SER A N   1 
ATOM   1938  C CA  . SER A 1 246 ? 26.824  7.129   19.052  1.00 22.45  ? 275 SER A CA  1 
ATOM   1939  C C   . SER A 1 246 ? 27.768  8.187   18.499  1.00 22.73  ? 275 SER A C   1 
ATOM   1940  O O   . SER A 1 246 ? 28.589  8.709   19.258  1.00 26.25  ? 275 SER A O   1 
ATOM   1941  C CB  . SER A 1 246 ? 27.402  5.746   18.892  1.00 25.11  ? 275 SER A CB  1 
ATOM   1942  O OG  . SER A 1 246 ? 27.825  5.486   17.557  1.00 27.55  ? 275 SER A OG  1 
ATOM   1943  N N   . HIS A 1 247 ? 27.702  8.402   17.180  1.00 23.29  ? 276 HIS A N   1 
ATOM   1944  C CA  . HIS A 1 247 ? 28.484  9.403   16.457  1.00 21.97  ? 276 HIS A CA  1 
ATOM   1945  C C   . HIS A 1 247 ? 28.089  10.807  16.933  1.00 23.74  ? 276 HIS A C   1 
ATOM   1946  O O   . HIS A 1 247 ? 28.908  11.665  17.215  1.00 23.71  ? 276 HIS A O   1 
ATOM   1947  C CB  . HIS A 1 247 ? 28.110  9.276   14.987  1.00 25.96  ? 276 HIS A CB  1 
ATOM   1948  C CG  . HIS A 1 247 ? 28.878  10.097  14.022  1.00 31.74  ? 276 HIS A CG  1 
ATOM   1949  N ND1 . HIS A 1 247 ? 30.182  9.793   13.705  1.00 34.27  ? 276 HIS A ND1 1 
ATOM   1950  C CD2 . HIS A 1 247 ? 28.538  11.155  13.270  1.00 32.04  ? 276 HIS A CD2 1 
ATOM   1951  C CE1 . HIS A 1 247 ? 30.636  10.673  12.814  1.00 34.15  ? 276 HIS A CE1 1 
ATOM   1952  N NE2 . HIS A 1 247 ? 29.654  11.495  12.515  1.00 32.76  ? 276 HIS A NE2 1 
ATOM   1953  N N   . LEU A 1 248 ? 26.796  11.054  17.090  1.00 23.58  ? 277 LEU A N   1 
ATOM   1954  C CA  . LEU A 1 248 ? 26.357  12.380  17.520  1.00 22.63  ? 277 LEU A CA  1 
ATOM   1955  C C   . LEU A 1 248 ? 26.843  12.708  18.935  1.00 19.81  ? 277 LEU A C   1 
ATOM   1956  O O   . LEU A 1 248 ? 27.429  13.757  19.148  1.00 21.76  ? 277 LEU A O   1 
ATOM   1957  C CB  . LEU A 1 248 ? 24.842  12.356  17.426  1.00 24.40  ? 277 LEU A CB  1 
ATOM   1958  C CG  . LEU A 1 248 ? 24.127  13.608  17.944  1.00 27.67  ? 277 LEU A CG  1 
ATOM   1959  C CD1 . LEU A 1 248 ? 24.716  14.837  17.302  1.00 30.78  ? 277 LEU A CD1 1 
ATOM   1960  C CD2 . LEU A 1 248 ? 22.663  13.485  17.600  1.00 27.88  ? 277 LEU A CD2 1 
ATOM   1961  N N   . VAL A 1 249 ? 26.580  11.813  19.889  1.00 22.34  ? 278 VAL A N   1 
ATOM   1962  C CA  . VAL A 1 249 ? 26.968  11.975  21.275  1.00 23.47  ? 278 VAL A CA  1 
ATOM   1963  C C   . VAL A 1 249 ? 28.486  12.007  21.374  1.00 23.27  ? 278 VAL A C   1 
ATOM   1964  O O   . VAL A 1 249 ? 29.011  12.793  22.120  1.00 22.66  ? 278 VAL A O   1 
ATOM   1965  C CB  . VAL A 1 249 ? 26.341  10.867  22.155  1.00 23.66  ? 278 VAL A CB  1 
ATOM   1966  C CG1 . VAL A 1 249 ? 26.854  10.896  23.589  1.00 25.34  ? 278 VAL A CG1 1 
ATOM   1967  C CG2 . VAL A 1 249 ? 24.805  10.932  22.197  1.00 22.66  ? 278 VAL A CG2 1 
ATOM   1968  N N   . GLY A 1 250 ? 29.188  11.138  20.642  1.00 22.36  ? 279 GLY A N   1 
ATOM   1969  C CA  . GLY A 1 250 ? 30.634  11.110  20.628  1.00 22.61  ? 279 GLY A CA  1 
ATOM   1970  C C   . GLY A 1 250 ? 31.259  12.404  20.129  1.00 21.16  ? 279 GLY A C   1 
ATOM   1971  O O   . GLY A 1 250 ? 32.305  12.794  20.657  1.00 23.88  ? 279 GLY A O   1 
ATOM   1972  N N   . SER A 1 251 ? 30.621  13.035  19.134  1.00 20.69  ? 280 SER A N   1 
ATOM   1973  C CA  . SER A 1 251 ? 31.064  14.292  18.541  1.00 24.11  ? 280 SER A CA  1 
ATOM   1974  C C   . SER A 1 251 ? 31.149  15.400  19.608  1.00 25.08  ? 280 SER A C   1 
ATOM   1975  O O   . SER A 1 251 ? 31.829  16.406  19.408  1.00 22.71  ? 280 SER A O   1 
ATOM   1976  C CB  . SER A 1 251 ? 30.118  14.742  17.430  1.00 24.83  ? 280 SER A CB  1 
ATOM   1977  O OG  . SER A 1 251 ? 28.909  15.377  17.871  1.00 22.02  ? 280 SER A OG  1 
ATOM   1978  N N   . ALA A 1 252 ? 30.388  15.247  20.696  1.00 21.94  ? 281 ALA A N   1 
ATOM   1979  C CA  . ALA A 1 252 ? 30.452  16.203  21.801  1.00 23.21  ? 281 ALA A CA  1 
ATOM   1980  C C   . ALA A 1 252 ? 31.531  15.842  22.823  1.00 21.54  ? 281 ALA A C   1 
ATOM   1981  O O   . ALA A 1 252 ? 31.685  16.531  23.816  1.00 24.91  ? 281 ALA A O   1 
ATOM   1982  C CB  . ALA A 1 252 ? 29.097  16.369  22.442  1.00 22.45  ? 281 ALA A CB  1 
ATOM   1983  N N   . LEU A 1 253 ? 32.303  14.791  22.541  1.00 22.53  ? 282 LEU A N   1 
ATOM   1984  C CA  . LEU A 1 253 ? 33.482  14.371  23.256  1.00 23.67  ? 282 LEU A CA  1 
ATOM   1985  C C   . LEU A 1 253 ? 33.039  13.621  24.504  1.00 25.72  ? 282 LEU A C   1 
ATOM   1986  O O   . LEU A 1 253 ? 33.813  13.477  25.439  1.00 25.30  ? 282 LEU A O   1 
ATOM   1987  C CB  . LEU A 1 253 ? 34.545  15.420  23.555  1.00 23.30  ? 282 LEU A CB  1 
ATOM   1988  C CG  . LEU A 1 253 ? 35.202  16.069  22.324  1.00 26.99  ? 282 LEU A CG  1 
ATOM   1989  C CD1 . LEU A 1 253 ? 36.300  17.035  22.764  1.00 25.53  ? 282 LEU A CD1 1 
ATOM   1990  C CD2 . LEU A 1 253 ? 35.808  15.098  21.306  1.00 29.07  ? 282 LEU A CD2 1 
ATOM   1991  N N   . SER A 1 254 ? 31.797  13.148  24.478  1.00 26.20  ? 283 SER A N   1 
ATOM   1992  C CA  . SER A 1 254 ? 31.335  12.187  25.455  1.00 27.71  ? 283 SER A CA  1 
ATOM   1993  C C   . SER A 1 254 ? 32.165  10.922  25.275  1.00 28.10  ? 283 SER A C   1 
ATOM   1994  O O   . SER A 1 254 ? 32.372  10.486  24.144  1.00 28.88  ? 283 SER A O   1 
ATOM   1995  C CB  . SER A 1 254 ? 29.860  11.875  25.263  1.00 26.10  ? 283 SER A CB  1 
ATOM   1996  O OG  . SER A 1 254 ? 29.011  12.950  25.638  1.00 30.25  ? 283 SER A OG  1 
ATOM   1997  N N   . ASP A 1 255 ? 32.458  10.247  26.385  1.00 28.69  ? 284 ASP A N   1 
ATOM   1998  C CA  . ASP A 1 255 ? 33.317  9.081   26.346  1.00 25.80  ? 284 ASP A CA  1 
ATOM   1999  C C   . ASP A 1 255 ? 32.581  7.920   25.673  1.00 23.70  ? 284 ASP A C   1 
ATOM   2000  O O   . ASP A 1 255 ? 31.372  7.940   25.468  1.00 25.70  ? 284 ASP A O   1 
ATOM   2001  C CB  . ASP A 1 255 ? 33.903  8.819   27.719  1.00 29.98  ? 284 ASP A CB  1 
ATOM   2002  C CG  . ASP A 1 255 ? 32.830  8.365   28.699  1.00 38.38  ? 284 ASP A CG  1 
ATOM   2003  O OD1 . ASP A 1 255 ? 32.155  7.372   28.339  1.00 39.90  ? 284 ASP A OD1 1 
ATOM   2004  O OD2 . ASP A 1 255 ? 32.630  9.052   29.756  1.00 30.46  ? 284 ASP A OD2 1 
ATOM   2005  N N   . PRO A 1 256 ? 33.291  6.847   25.282  1.00 23.28  ? 285 PRO A N   1 
ATOM   2006  C CA  . PRO A 1 256 ? 32.654  5.686   24.654  1.00 27.13  ? 285 PRO A CA  1 
ATOM   2007  C C   . PRO A 1 256 ? 31.517  5.042   25.458  1.00 23.71  ? 285 PRO A C   1 
ATOM   2008  O O   . PRO A 1 256 ? 30.568  4.518   24.910  1.00 24.68  ? 285 PRO A O   1 
ATOM   2009  C CB  . PRO A 1 256 ? 33.876  4.759   24.530  1.00 24.93  ? 285 PRO A CB  1 
ATOM   2010  C CG  . PRO A 1 256 ? 34.998  5.689   24.332  1.00 26.16  ? 285 PRO A CG  1 
ATOM   2011  C CD  . PRO A 1 256 ? 34.733  6.688   25.444  1.00 26.52  ? 285 PRO A CD  1 
ATOM   2012  N N   . TYR A 1 257 ? 31.580  5.087   26.785  1.00 23.00  ? 286 TYR A N   1 
ATOM   2013  C CA  . TYR A 1 257 ? 30.497  4.510   27.556  1.00 23.76  ? 286 TYR A CA  1 
ATOM   2014  C C   . TYR A 1 257 ? 29.203  5.297   27.361  1.00 24.54  ? 286 TYR A C   1 
ATOM   2015  O O   . TYR A 1 257 ? 28.156  4.737   27.094  1.00 27.37  ? 286 TYR A O   1 
ATOM   2016  C CB  . TYR A 1 257 ? 30.931  4.444   29.002  1.00 24.01  ? 286 TYR A CB  1 
ATOM   2017  C CG  . TYR A 1 257 ? 32.111  3.548   29.267  1.00 26.65  ? 286 TYR A CG  1 
ATOM   2018  C CD1 . TYR A 1 257 ? 31.911  2.215   29.592  1.00 27.84  ? 286 TYR A CD1 1 
ATOM   2019  C CD2 . TYR A 1 257 ? 33.400  4.058   29.347  1.00 26.72  ? 286 TYR A CD2 1 
ATOM   2020  C CE1 . TYR A 1 257 ? 32.971  1.391   29.899  1.00 28.27  ? 286 TYR A CE1 1 
ATOM   2021  C CE2 . TYR A 1 257 ? 34.466  3.247   29.697  1.00 29.38  ? 286 TYR A CE2 1 
ATOM   2022  C CZ  . TYR A 1 257 ? 34.252  1.902   29.956  1.00 31.29  ? 286 TYR A CZ  1 
ATOM   2023  O OH  . TYR A 1 257 ? 35.297  1.076   30.264  1.00 28.71  ? 286 TYR A OH  1 
ATOM   2024  N N   . LEU A 1 258 ? 29.266  6.613   27.473  1.00 27.50  ? 287 LEU A N   1 
ATOM   2025  C CA  . LEU A 1 258 ? 28.059  7.403   27.370  1.00 25.72  ? 287 LEU A CA  1 
ATOM   2026  C C   . LEU A 1 258 ? 27.529  7.376   25.928  1.00 25.51  ? 287 LEU A C   1 
ATOM   2027  O O   . LEU A 1 258 ? 26.342  7.368   25.693  1.00 23.01  ? 287 LEU A O   1 
ATOM   2028  C CB  . LEU A 1 258 ? 28.436  8.811   27.806  1.00 27.00  ? 287 LEU A CB  1 
ATOM   2029  C CG  . LEU A 1 258 ? 28.836  9.039   29.262  1.00 28.58  ? 287 LEU A CG  1 
ATOM   2030  C CD1 . LEU A 1 258 ? 29.089  10.552  29.390  1.00 30.13  ? 287 LEU A CD1 1 
ATOM   2031  C CD2 . LEU A 1 258 ? 27.823  8.566   30.308  1.00 25.87  ? 287 LEU A CD2 1 
ATOM   2032  N N   . SER A 1 259 ? 28.435  7.319   24.954  1.00 25.45  ? 288 SER A N   1 
ATOM   2033  C CA  . SER A 1 259 ? 28.101  7.293   23.548  1.00 28.47  ? 288 SER A CA  1 
ATOM   2034  C C   . SER A 1 259 ? 27.401  6.000   23.211  1.00 28.15  ? 288 SER A C   1 
ATOM   2035  O O   . SER A 1 259 ? 26.467  6.001   22.423  1.00 24.98  ? 288 SER A O   1 
ATOM   2036  C CB  . SER A 1 259 ? 29.334  7.432   22.665  1.00 27.89  ? 288 SER A CB  1 
ATOM   2037  O OG  . SER A 1 259 ? 29.864  8.716   22.972  1.00 33.74  ? 288 SER A OG  1 
ATOM   2038  N N   . PHE A 1 260 ? 27.955  4.904   23.699  1.00 30.10  ? 289 PHE A N   1 
ATOM   2039  C CA  . PHE A 1 260 ? 27.359  3.608   23.440  1.00 30.70  ? 289 PHE A CA  1 
ATOM   2040  C C   . PHE A 1 260 ? 26.013  3.485   24.159  1.00 26.54  ? 289 PHE A C   1 
ATOM   2041  O O   . PHE A 1 260 ? 25.069  2.918   23.628  1.00 23.77  ? 289 PHE A O   1 
ATOM   2042  C CB  . PHE A 1 260 ? 28.381  2.555   23.830  1.00 29.88  ? 289 PHE A CB  1 
ATOM   2043  C CG  . PHE A 1 260 ? 27.830  1.161   23.652  1.00 30.12  ? 289 PHE A CG  1 
ATOM   2044  C CD1 . PHE A 1 260 ? 27.743  0.583   22.393  1.00 29.90  ? 289 PHE A CD1 1 
ATOM   2045  C CD2 . PHE A 1 260 ? 27.368  0.446   24.745  1.00 30.96  ? 289 PHE A CD2 1 
ATOM   2046  C CE1 . PHE A 1 260 ? 27.176  -0.664  22.239  1.00 29.55  ? 289 PHE A CE1 1 
ATOM   2047  C CE2 . PHE A 1 260 ? 26.802  -0.804  24.573  1.00 31.34  ? 289 PHE A CE2 1 
ATOM   2048  C CZ  . PHE A 1 260 ? 26.732  -1.367  23.330  1.00 29.11  ? 289 PHE A CZ  1 
ATOM   2049  N N   . ALA A 1 261 ? 25.924  3.961   25.395  1.00 26.24  ? 290 ALA A N   1 
ATOM   2050  C CA  . ALA A 1 261 ? 24.682  3.807   26.139  1.00 27.49  ? 290 ALA A CA  1 
ATOM   2051  C C   . ALA A 1 261 ? 23.560  4.619   25.481  1.00 25.39  ? 290 ALA A C   1 
ATOM   2052  O O   . ALA A 1 261 ? 22.404  4.231   25.491  1.00 24.70  ? 290 ALA A O   1 
ATOM   2053  C CB  . ALA A 1 261 ? 24.862  4.234   27.569  1.00 29.06  ? 290 ALA A CB  1 
ATOM   2054  N N   . ALA A 1 262 ? 23.896  5.775   24.924  1.00 22.33  ? 291 ALA A N   1 
ATOM   2055  C CA  . ALA A 1 262 ? 22.947  6.539   24.115  1.00 21.15  ? 291 ALA A CA  1 
ATOM   2056  C C   . ALA A 1 262 ? 22.514  5.732   22.904  1.00 22.37  ? 291 ALA A C   1 
ATOM   2057  O O   . ALA A 1 262 ? 21.333  5.660   22.609  1.00 23.36  ? 291 ALA A O   1 
ATOM   2058  C CB  . ALA A 1 262 ? 23.593  7.808   23.633  1.00 19.26  ? 291 ALA A CB  1 
ATOM   2059  N N   . ALA A 1 263 ? 23.491  5.154   22.188  1.00 19.03  ? 292 ALA A N   1 
ATOM   2060  C CA  . ALA A 1 263 ? 23.179  4.292   21.066  1.00 21.93  ? 292 ALA A CA  1 
ATOM   2061  C C   . ALA A 1 263 ? 22.189  3.194   21.444  1.00 24.66  ? 292 ALA A C   1 
ATOM   2062  O O   . ALA A 1 263 ? 21.220  2.961   20.716  1.00 24.89  ? 292 ALA A O   1 
ATOM   2063  C CB  . ALA A 1 263 ? 24.446  3.707   20.517  1.00 23.89  ? 292 ALA A CB  1 
ATOM   2064  N N   . MET A 1 264 ? 22.440  2.520   22.574  1.00 25.62  ? 293 MET A N   1 
ATOM   2065  C CA  . MET A 1 264 ? 21.549  1.466   23.048  1.00 26.23  ? 293 MET A CA  1 
ATOM   2066  C C   . MET A 1 264 ? 20.115  1.967   23.248  1.00 26.62  ? 293 MET A C   1 
ATOM   2067  O O   . MET A 1 264 ? 19.163  1.242   23.022  1.00 28.75  ? 293 MET A O   1 
ATOM   2068  C CB  . MET A 1 264 ? 22.059  0.875   24.364  1.00 24.58  ? 293 MET A CB  1 
ATOM   2069  C CG  . MET A 1 264 ? 23.327  0.095   24.219  1.00 25.69  ? 293 MET A CG  1 
ATOM   2070  S SD  . MET A 1 264 ? 23.253  -1.105  22.873  1.00 30.39  ? 293 MET A SD  1 
ATOM   2071  C CE  . MET A 1 264 ? 23.461  -0.340  21.257  1.00 32.00  ? 293 MET A CE  1 
ATOM   2072  N N   . ASN A 1 265 ? 19.954  3.164   23.794  1.00 25.10  ? 294 ASN A N   1 
ATOM   2073  C CA  . ASN A 1 265 ? 18.631  3.719   23.944  1.00 26.05  ? 294 ASN A CA  1 
ATOM   2074  C C   . ASN A 1 265 ? 17.961  3.850   22.582  1.00 27.98  ? 294 ASN A C   1 
ATOM   2075  O O   . ASN A 1 265 ? 16.751  3.734   22.497  1.00 28.20  ? 294 ASN A O   1 
ATOM   2076  C CB  . ASN A 1 265 ? 18.715  5.038   24.689  1.00 31.64  ? 294 ASN A CB  1 
ATOM   2077  C CG  . ASN A 1 265 ? 18.840  4.817   26.181  1.00 31.26  ? 294 ASN A CG  1 
ATOM   2078  O OD1 . ASN A 1 265 ? 18.967  3.694   26.648  1.00 30.86  ? 294 ASN A OD1 1 
ATOM   2079  N ND2 . ASN A 1 265 ? 18.815  5.870   26.960  1.00 39.06  ? 294 ASN A ND2 1 
ATOM   2080  N N   . GLY A 1 266 ? 18.740  4.156   21.543  1.00 23.44  ? 295 GLY A N   1 
ATOM   2081  C CA  . GLY A 1 266 ? 18.216  4.242   20.216  1.00 24.54  ? 295 GLY A CA  1 
ATOM   2082  C C   . GLY A 1 266 ? 17.905  2.862   19.646  1.00 27.32  ? 295 GLY A C   1 
ATOM   2083  O O   . GLY A 1 266 ? 16.886  2.678   18.974  1.00 24.16  ? 295 GLY A O   1 
ATOM   2084  N N   . LEU A 1 267 ? 18.781  1.901   19.932  1.00 29.16  ? 296 LEU A N   1 
ATOM   2085  C CA  . LEU A 1 267 ? 18.595  0.529   19.474  1.00 28.56  ? 296 LEU A CA  1 
ATOM   2086  C C   . LEU A 1 267 ? 17.350  -0.069  20.124  1.00 31.84  ? 296 LEU A C   1 
ATOM   2087  O O   . LEU A 1 267 ? 16.651  -0.864  19.488  1.00 29.41  ? 296 LEU A O   1 
ATOM   2088  C CB  . LEU A 1 267 ? 19.823  -0.324  19.776  1.00 32.81  ? 296 LEU A CB  1 
ATOM   2089  C CG  . LEU A 1 267 ? 19.867  -1.684  19.075  1.00 33.20  ? 296 LEU A CG  1 
ATOM   2090  C CD1 . LEU A 1 267 ? 19.900  -1.489  17.583  1.00 35.11  ? 296 LEU A CD1 1 
ATOM   2091  C CD2 . LEU A 1 267 ? 21.041  -2.439  19.519  1.00 33.76  ? 296 LEU A CD2 1 
ATOM   2092  N N   . ALA A 1 268 ? 17.026  0.374   21.346  1.00 26.77  ? 297 ALA A N   1 
ATOM   2093  C CA  . ALA A 1 268 ? 15.876  -0.179  22.047  1.00 27.06  ? 297 ALA A CA  1 
ATOM   2094  C C   . ALA A 1 268 ? 14.558  0.259   21.407  1.00 26.92  ? 297 ALA A C   1 
ATOM   2095  O O   . ALA A 1 268 ? 13.510  -0.214  21.791  1.00 26.14  ? 297 ALA A O   1 
ATOM   2096  C CB  . ALA A 1 268 ? 15.905  0.254   23.485  1.00 26.63  ? 297 ALA A CB  1 
ATOM   2097  N N   . GLY A 1 269 ? 14.575  1.230   20.481  1.00 26.33  ? 298 GLY A N   1 
ATOM   2098  C CA  . GLY A 1 269 ? 13.331  1.672   19.892  1.00 23.63  ? 298 GLY A CA  1 
ATOM   2099  C C   . GLY A 1 269 ? 12.709  0.586   19.019  1.00 26.49  ? 298 GLY A C   1 
ATOM   2100  O O   . GLY A 1 269 ? 13.438  -0.152  18.339  1.00 32.08  ? 298 GLY A O   1 
ATOM   2101  N N   . PRO A 1 270 ? 11.363  0.470   19.012  1.00 24.93  ? 299 PRO A N   1 
ATOM   2102  C CA  . PRO A 1 270 ? 10.651  -0.413  18.104  1.00 28.93  ? 299 PRO A CA  1 
ATOM   2103  C C   . PRO A 1 270 ? 10.988  -0.349  16.613  1.00 30.41  ? 299 PRO A C   1 
ATOM   2104  O O   . PRO A 1 270 ? 11.009  -1.394  15.993  1.00 32.54  ? 299 PRO A O   1 
ATOM   2105  C CB  . PRO A 1 270 ? 9.157   -0.091  18.350  1.00 31.80  ? 299 PRO A CB  1 
ATOM   2106  C CG  . PRO A 1 270 ? 9.108   0.524   19.738  1.00 27.46  ? 299 PRO A CG  1 
ATOM   2107  C CD  . PRO A 1 270 ? 10.470  1.112   19.992  1.00 25.19  ? 299 PRO A CD  1 
ATOM   2108  N N   . LEU A 1 271 ? 11.267  0.829   16.037  1.00 29.01  ? 300 LEU A N   1 
ATOM   2109  C CA  . LEU A 1 271 ? 11.634  0.910   14.625  1.00 29.34  ? 300 LEU A CA  1 
ATOM   2110  C C   . LEU A 1 271 ? 13.101  0.578   14.354  1.00 31.50  ? 300 LEU A C   1 
ATOM   2111  O O   . LEU A 1 271 ? 13.560  0.819   13.240  1.00 30.55  ? 300 LEU A O   1 
ATOM   2112  C CB  . LEU A 1 271 ? 11.320  2.315   14.113  1.00 27.98  ? 300 LEU A CB  1 
ATOM   2113  C CG  . LEU A 1 271 ? 9.878   2.767   14.333  1.00 32.17  ? 300 LEU A CG  1 
ATOM   2114  C CD1 . LEU A 1 271 ? 9.533   4.062   13.572  1.00 35.93  ? 300 LEU A CD1 1 
ATOM   2115  C CD2 . LEU A 1 271 ? 8.916   1.632   13.943  1.00 35.99  ? 300 LEU A CD2 1 
ATOM   2116  N N   . HIS A 1 272 ? 13.858  0.122   15.361  1.00 31.27  ? 301 HIS A N   1 
ATOM   2117  C CA  . HIS A 1 272 ? 15.269  -0.164  15.154  1.00 36.85  ? 301 HIS A CA  1 
ATOM   2118  C C   . HIS A 1 272 ? 15.630  -1.587  15.589  1.00 34.95  ? 301 HIS A C   1 
ATOM   2119  O O   . HIS A 1 272 ? 15.806  -2.458  14.749  1.00 49.14  ? 301 HIS A O   1 
ATOM   2120  C CB  . HIS A 1 272 ? 16.184  0.918   15.751  1.00 34.31  ? 301 HIS A CB  1 
ATOM   2121  C CG  . HIS A 1 272 ? 17.582  0.753   15.276  1.00 33.85  ? 301 HIS A CG  1 
ATOM   2122  N ND1 . HIS A 1 272 ? 18.685  1.304   15.886  1.00 30.26  ? 301 HIS A ND1 1 
ATOM   2123  C CD2 . HIS A 1 272 ? 18.050  0.057   14.220  1.00 35.84  ? 301 HIS A CD2 1 
ATOM   2124  C CE1 . HIS A 1 272 ? 19.779  0.952   15.199  1.00 33.13  ? 301 HIS A CE1 1 
ATOM   2125  N NE2 . HIS A 1 272 ? 19.419  0.201   14.173  1.00 32.65  ? 301 HIS A NE2 1 
ATOM   2126  N N   . GLY A 1 273 ? 15.750  -1.840  16.880  1.00 32.34  ? 302 GLY A N   1 
ATOM   2127  C CA  . GLY A 1 273 ? 16.360  -3.075  17.333  1.00 30.52  ? 302 GLY A CA  1 
ATOM   2128  C C   . GLY A 1 273 ? 15.380  -4.108  17.868  1.00 32.67  ? 302 GLY A C   1 
ATOM   2129  O O   . GLY A 1 273 ? 15.818  -5.191  18.238  1.00 34.74  ? 302 GLY A O   1 
ATOM   2130  N N   . LEU A 1 274 ? 14.084  -3.794  17.936  1.00 34.85  ? 303 LEU A N   1 
ATOM   2131  C CA  . LEU A 1 274 ? 13.096  -4.732  18.464  1.00 35.28  ? 303 LEU A CA  1 
ATOM   2132  C C   . LEU A 1 274 ? 12.412  -5.545  17.365  1.00 37.65  ? 303 LEU A C   1 
ATOM   2133  O O   . LEU A 1 274 ? 11.533  -6.359  17.665  1.00 39.02  ? 303 LEU A O   1 
ATOM   2134  C CB  . LEU A 1 274 ? 12.052  -3.970  19.288  1.00 41.43  ? 303 LEU A CB  1 
ATOM   2135  C CG  . LEU A 1 274 ? 12.446  -3.638  20.739  1.00 44.43  ? 303 LEU A CG  1 
ATOM   2136  C CD1 . LEU A 1 274 ? 13.810  -2.993  20.730  1.00 45.46  ? 303 LEU A CD1 1 
ATOM   2137  C CD2 . LEU A 1 274 ? 11.472  -2.747  21.526  1.00 45.63  ? 303 LEU A CD2 1 
ATOM   2138  N N   . ALA A 1 275 ? 12.802  -5.356  16.094  1.00 39.53  ? 304 ALA A N   1 
ATOM   2139  C CA  . ALA A 1 275 ? 12.163  -6.064  14.985  1.00 37.92  ? 304 ALA A CA  1 
ATOM   2140  C C   . ALA A 1 275 ? 12.365  -7.587  15.031  1.00 35.75  ? 304 ALA A C   1 
ATOM   2141  O O   . ALA A 1 275 ? 11.527  -8.344  14.512  1.00 33.88  ? 304 ALA A O   1 
ATOM   2142  C CB  . ALA A 1 275 ? 12.654  -5.497  13.671  1.00 40.72  ? 304 ALA A CB  1 
ATOM   2143  N N   . ASN A 1 276 ? 13.480  -8.050  15.602  1.00 30.63  ? 305 ASN A N   1 
ATOM   2144  C CA  . ASN A 1 276 ? 13.759  -9.483  15.703  1.00 38.08  ? 305 ASN A CA  1 
ATOM   2145  C C   . ASN A 1 276 ? 12.584  -10.167 16.409  1.00 36.03  ? 305 ASN A C   1 
ATOM   2146  O O   . ASN A 1 276 ? 11.951  -11.075 15.897  1.00 28.60  ? 305 ASN A O   1 
ATOM   2147  C CB  . ASN A 1 276 ? 15.081  -9.760  16.426  1.00 37.16  ? 305 ASN A CB  1 
ATOM   2148  C CG  . ASN A 1 276 ? 15.344  -11.233 16.648  1.00 47.33  ? 305 ASN A CG  1 
ATOM   2149  O OD1 . ASN A 1 276 ? 14.408  -12.049 16.678  1.00 49.48  ? 305 ASN A OD1 1 
ATOM   2150  N ND2 . ASN A 1 276 ? 16.604  -11.597 16.861  1.00 44.83  ? 305 ASN A ND2 1 
ATOM   2151  N N   . GLN A 1 277 ? 12.306  -9.709  17.620  1.00 39.84  ? 306 GLN A N   1 
ATOM   2152  C CA  . GLN A 1 277 ? 11.202  -10.201 18.414  1.00 36.87  ? 306 GLN A CA  1 
ATOM   2153  C C   . GLN A 1 277 ? 9.880   -9.997  17.679  1.00 40.44  ? 306 GLN A C   1 
ATOM   2154  O O   . GLN A 1 277 ? 8.988   -10.836 17.760  1.00 39.64  ? 306 GLN A O   1 
ATOM   2155  C CB  . GLN A 1 277 ? 11.278  -9.457  19.751  1.00 41.73  ? 306 GLN A CB  1 
ATOM   2156  C CG  . GLN A 1 277 ? 10.152  -9.795  20.721  1.00 46.51  ? 306 GLN A CG  1 
ATOM   2157  C CD  . GLN A 1 277 ? 10.228  -9.014  22.016  1.00 53.40  ? 306 GLN A CD  1 
ATOM   2158  O OE1 . GLN A 1 277 ? 10.792  -7.914  22.070  1.00 53.39  ? 306 GLN A OE1 1 
ATOM   2159  N NE2 . GLN A 1 277 ? 9.581   -9.534  23.049  1.00 47.47  ? 306 GLN A NE2 1 
ATOM   2160  N N   . GLU A 1 278 ? 9.720   -8.862  16.990  1.00 41.14  ? 307 GLU A N   1 
ATOM   2161  C CA  . GLU A 1 278 ? 8.449   -8.565  16.347  1.00 43.48  ? 307 GLU A CA  1 
ATOM   2162  C C   . GLU A 1 278 ? 8.217   -9.586  15.239  1.00 39.31  ? 307 GLU A C   1 
ATOM   2163  O O   . GLU A 1 278 ? 7.112   -10.076 15.072  1.00 38.46  ? 307 GLU A O   1 
ATOM   2164  C CB  . GLU A 1 278 ? 8.441   -7.139  15.809  1.00 45.58  ? 307 GLU A CB  1 
ATOM   2165  C CG  . GLU A 1 278 ? 7.166   -6.788  15.053  1.00 49.35  ? 307 GLU A CG  1 
ATOM   2166  C CD  . GLU A 1 278 ? 7.298   -5.493  14.267  1.00 53.82  ? 307 GLU A CD  1 
ATOM   2167  O OE1 . GLU A 1 278 ? 8.434   -4.950  14.187  1.00 55.98  ? 307 GLU A OE1 1 
ATOM   2168  O OE2 . GLU A 1 278 ? 6.260   -5.034  13.738  1.00 55.92  ? 307 GLU A OE2 1 
ATOM   2169  N N   . VAL A 1 279 ? 9.276   -9.908  14.484  1.00 38.44  ? 308 VAL A N   1 
ATOM   2170  C CA  . VAL A 1 279 ? 9.199   -10.965 13.496  1.00 33.75  ? 308 VAL A CA  1 
ATOM   2171  C C   . VAL A 1 279 ? 8.736   -12.234 14.195  1.00 32.78  ? 308 VAL A C   1 
ATOM   2172  O O   . VAL A 1 279 ? 7.729   -12.793 13.826  1.00 31.96  ? 308 VAL A O   1 
ATOM   2173  C CB  . VAL A 1 279 ? 10.511  -11.221 12.737  1.00 34.99  ? 308 VAL A CB  1 
ATOM   2174  C CG1 . VAL A 1 279 ? 10.529  -12.589 12.034  1.00 32.64  ? 308 VAL A CG1 1 
ATOM   2175  C CG2 . VAL A 1 279 ? 10.769  -10.106 11.725  1.00 39.14  ? 308 VAL A CG2 1 
ATOM   2176  N N   . LEU A 1 280 ? 9.450   -12.659 15.230  1.00 35.48  ? 309 LEU A N   1 
ATOM   2177  C CA  . LEU A 1 280 ? 9.190   -13.949 15.858  1.00 38.30  ? 309 LEU A CA  1 
ATOM   2178  C C   . LEU A 1 280 ? 7.768   -14.071 16.428  1.00 36.43  ? 309 LEU A C   1 
ATOM   2179  O O   . LEU A 1 280 ? 7.125   -15.101 16.271  1.00 39.47  ? 309 LEU A O   1 
ATOM   2180  C CB  . LEU A 1 280 ? 10.288  -14.178 16.904  1.00 37.55  ? 309 LEU A CB  1 
ATOM   2181  C CG  . LEU A 1 280 ? 10.400  -15.590 17.495  1.00 40.00  ? 309 LEU A CG  1 
ATOM   2182  C CD1 . LEU A 1 280 ? 10.631  -16.634 16.419  1.00 47.15  ? 309 LEU A CD1 1 
ATOM   2183  C CD2 . LEU A 1 280 ? 11.499  -15.664 18.531  1.00 44.35  ? 309 LEU A CD2 1 
ATOM   2184  N N   . VAL A 1 281 ? 7.285   -13.060 17.146  1.00 38.93  ? 310 VAL A N   1 
ATOM   2185  C CA  . VAL A 1 281 ? 5.909   -13.067 17.644  1.00 40.35  ? 310 VAL A CA  1 
ATOM   2186  C C   . VAL A 1 281 ? 4.884   -13.234 16.503  1.00 41.42  ? 310 VAL A C   1 
ATOM   2187  O O   . VAL A 1 281 ? 3.866   -13.901 16.658  1.00 38.15  ? 310 VAL A O   1 
ATOM   2188  C CB  . VAL A 1 281 ? 5.676   -11.749 18.409  1.00 38.15  ? 310 VAL A CB  1 
ATOM   2189  C CG1 . VAL A 1 281 ? 4.177   -11.408 18.551  1.00 33.29  ? 310 VAL A CG1 1 
ATOM   2190  C CG2 . VAL A 1 281 ? 6.420   -11.750 19.744  1.00 39.64  ? 310 VAL A CG2 1 
ATOM   2191  N N   . TRP A 1 282 ? 5.101   -12.547 15.377  1.00 40.33  ? 311 TRP A N   1 
ATOM   2192  C CA  . TRP A 1 282 ? 4.233   -12.662 14.213  1.00 42.97  ? 311 TRP A CA  1 
ATOM   2193  C C   . TRP A 1 282 ? 4.248   -14.069 13.599  1.00 48.85  ? 311 TRP A C   1 
ATOM   2194  O O   . TRP A 1 282 ? 3.199   -14.652 13.399  1.00 50.16  ? 311 TRP A O   1 
ATOM   2195  C CB  . TRP A 1 282 ? 4.660   -11.608 13.196  1.00 45.33  ? 311 TRP A CB  1 
ATOM   2196  C CG  . TRP A 1 282 ? 3.834   -11.586 11.942  1.00 51.44  ? 311 TRP A CG  1 
ATOM   2197  C CD1 . TRP A 1 282 ? 2.640   -10.963 11.738  1.00 47.57  ? 311 TRP A CD1 1 
ATOM   2198  C CD2 . TRP A 1 282 ? 4.195   -12.207 10.696  1.00 47.87  ? 311 TRP A CD2 1 
ATOM   2199  N NE1 . TRP A 1 282 ? 2.245   -11.142 10.442  1.00 47.21  ? 311 TRP A NE1 1 
ATOM   2200  C CE2 . TRP A 1 282 ? 3.169   -11.901 9.782   1.00 46.74  ? 311 TRP A CE2 1 
ATOM   2201  C CE3 . TRP A 1 282 ? 5.278   -12.978 10.272  1.00 47.58  ? 311 TRP A CE3 1 
ATOM   2202  C CZ2 . TRP A 1 282 ? 3.198   -12.347 8.467   1.00 52.64  ? 311 TRP A CZ2 1 
ATOM   2203  C CZ3 . TRP A 1 282 ? 5.296   -13.432 8.971   1.00 56.44  ? 311 TRP A CZ3 1 
ATOM   2204  C CH2 . TRP A 1 282 ? 4.270   -13.119 8.081   1.00 54.26  ? 311 TRP A CH2 1 
ATOM   2205  N N   . LEU A 1 283 ? 5.438   -14.620 13.328  1.00 48.62  ? 312 LEU A N   1 
ATOM   2206  C CA  . LEU A 1 283 ? 5.593   -15.983 12.837  1.00 45.98  ? 312 LEU A CA  1 
ATOM   2207  C C   . LEU A 1 283 ? 4.927   -16.987 13.768  1.00 49.17  ? 312 LEU A C   1 
ATOM   2208  O O   . LEU A 1 283 ? 4.567   -18.065 13.304  1.00 49.51  ? 312 LEU A O   1 
ATOM   2209  C CB  . LEU A 1 283 ? 7.044   -16.429 12.702  1.00 43.02  ? 312 LEU A CB  1 
ATOM   2210  C CG  . LEU A 1 283 ? 7.941   -15.626 11.759  1.00 46.25  ? 312 LEU A CG  1 
ATOM   2211  C CD1 . LEU A 1 283 ? 9.356   -16.086 12.093  1.00 49.17  ? 312 LEU A CD1 1 
ATOM   2212  C CD2 . LEU A 1 283 ? 7.604   -15.764 10.266  1.00 37.84  ? 312 LEU A CD2 1 
ATOM   2213  N N   . THR A 1 284 ? 4.899   -16.712 15.079  1.00 51.87  ? 313 THR A N   1 
ATOM   2214  C CA  . THR A 1 284 ? 4.319   -17.669 16.009  1.00 46.34  ? 313 THR A CA  1 
ATOM   2215  C C   . THR A 1 284 ? 2.798   -17.590 15.876  1.00 55.12  ? 313 THR A C   1 
ATOM   2216  O O   . THR A 1 284 ? 2.144   -18.627 15.761  1.00 57.42  ? 313 THR A O   1 
ATOM   2217  C CB  . THR A 1 284 ? 4.805   -17.430 17.439  1.00 48.76  ? 313 THR A CB  1 
ATOM   2218  O OG1 . THR A 1 284 ? 6.222   -17.548 17.369  1.00 51.85  ? 313 THR A OG1 1 
ATOM   2219  C CG2 . THR A 1 284 ? 4.295   -18.469 18.430  1.00 50.40  ? 313 THR A CG2 1 
ATOM   2220  N N   . GLN A 1 285 ? 2.243   -16.364 15.854  1.00 46.93  ? 314 GLN A N   1 
ATOM   2221  C CA  . GLN A 1 285 ? 0.806   -16.177 15.657  1.00 57.63  ? 314 GLN A CA  1 
ATOM   2222  C C   . GLN A 1 285 ? 0.378   -16.851 14.349  1.00 59.52  ? 314 GLN A C   1 
ATOM   2223  O O   . GLN A 1 285 ? -0.691  -17.437 14.277  1.00 63.40  ? 314 GLN A O   1 
ATOM   2224  C CB  . GLN A 1 285 ? 0.376   -14.704 15.624  1.00 58.53  ? 314 GLN A CB  1 
ATOM   2225  C CG  . GLN A 1 285 ? -0.883  -14.395 16.436  1.00 72.09  ? 314 GLN A CG  1 
ATOM   2226  C CD  . GLN A 1 285 ? -0.658  -14.190 17.929  1.00 80.33  ? 314 GLN A CD  1 
ATOM   2227  O OE1 . GLN A 1 285 ? -1.455  -14.638 18.767  1.00 67.40  ? 314 GLN A OE1 1 
ATOM   2228  N NE2 . GLN A 1 285 ? 0.399   -13.466 18.285  1.00 78.67  ? 314 GLN A NE2 1 
ATOM   2229  N N   . LEU A 1 286 ? 1.223   -16.748 13.312  1.00 60.53  ? 315 LEU A N   1 
ATOM   2230  C CA  . LEU A 1 286 ? 1.003   -17.374 12.015  1.00 57.20  ? 315 LEU A CA  1 
ATOM   2231  C C   . LEU A 1 286 ? 1.046   -18.902 12.095  1.00 57.58  ? 315 LEU A C   1 
ATOM   2232  O O   . LEU A 1 286 ? 0.290   -19.560 11.392  1.00 63.17  ? 315 LEU A O   1 
ATOM   2233  C CB  . LEU A 1 286 ? 2.068   -16.831 11.060  1.00 56.17  ? 315 LEU A CB  1 
ATOM   2234  C CG  . LEU A 1 286 ? 2.007   -17.297 9.601   1.00 57.03  ? 315 LEU A CG  1 
ATOM   2235  C CD1 . LEU A 1 286 ? 0.643   -17.001 9.022   1.00 55.79  ? 315 LEU A CD1 1 
ATOM   2236  C CD2 . LEU A 1 286 ? 3.083   -16.639 8.742   1.00 55.36  ? 315 LEU A CD2 1 
ATOM   2237  N N   . GLN A 1 287 ? 1.951   -19.464 12.909  1.00 65.45  ? 316 GLN A N   1 
ATOM   2238  C CA  . GLN A 1 287 ? 2.218   -20.897 12.931  1.00 66.90  ? 316 GLN A CA  1 
ATOM   2239  C C   . GLN A 1 287 ? 1.111   -21.632 13.679  1.00 73.57  ? 316 GLN A C   1 
ATOM   2240  O O   . GLN A 1 287 ? 0.885   -22.815 13.434  1.00 70.63  ? 316 GLN A O   1 
ATOM   2241  C CB  . GLN A 1 287 ? 3.559   -21.223 13.601  1.00 79.58  ? 316 GLN A CB  1 
ATOM   2242  C CG  . GLN A 1 287 ? 4.039   -22.668 13.458  1.00 79.59  ? 316 GLN A CG  1 
ATOM   2243  C CD  . GLN A 1 287 ? 4.627   -22.990 12.097  1.00 94.99  ? 316 GLN A CD  1 
ATOM   2244  O OE1 . GLN A 1 287 ? 4.089   -22.614 11.047  1.00 109.75 ? 316 GLN A OE1 1 
ATOM   2245  N NE2 . GLN A 1 287 ? 5.751   -23.695 12.091  1.00 95.28  ? 316 GLN A NE2 1 
ATOM   2246  N N   . LYS A 1 288 ? 0.447   -20.939 14.610  1.00 82.93  ? 317 LYS A N   1 
ATOM   2247  C CA  . LYS A 1 288 ? -0.671  -21.513 15.346  1.00 91.48  ? 317 LYS A CA  1 
ATOM   2248  C C   . LYS A 1 288 ? -1.935  -21.485 14.483  1.00 87.92  ? 317 LYS A C   1 
ATOM   2249  O O   . LYS A 1 288 ? -2.818  -22.321 14.669  1.00 86.05  ? 317 LYS A O   1 
ATOM   2250  C CB  . LYS A 1 288 ? -0.860  -20.780 16.681  1.00 99.76  ? 317 LYS A CB  1 
ATOM   2251  C CG  . LYS A 1 288 ? 0.083   -21.192 17.816  1.00 108.18 ? 317 LYS A CG  1 
ATOM   2252  C CD  . LYS A 1 288 ? -0.504  -22.206 18.797  1.00 112.33 ? 317 LYS A CD  1 
ATOM   2253  C CE  . LYS A 1 288 ? 0.391   -22.518 19.971  1.00 111.76 ? 317 LYS A CE  1 
ATOM   2254  N NZ  . LYS A 1 288 ? 1.393   -23.557 19.706  1.00 101.93 ? 317 LYS A NZ  1 
ATOM   2255  N N   . GLU A 1 289 ? -1.990  -20.540 13.530  1.00 81.59  ? 318 GLU A N   1 
ATOM   2256  C CA  . GLU A 1 289 ? -3.157  -20.309 12.692  1.00 80.21  ? 318 GLU A CA  1 
ATOM   2257  C C   . GLU A 1 289 ? -3.179  -21.148 11.412  1.00 85.29  ? 318 GLU A C   1 
ATOM   2258  O O   . GLU A 1 289 ? -4.156  -21.083 10.675  1.00 95.18  ? 318 GLU A O   1 
ATOM   2259  C CB  . GLU A 1 289 ? -3.219  -18.861 12.216  1.00 78.78  ? 318 GLU A CB  1 
ATOM   2260  C CG  . GLU A 1 289 ? -4.120  -17.975 13.064  1.00 83.45  ? 318 GLU A CG  1 
ATOM   2261  C CD  . GLU A 1 289 ? -4.324  -16.656 12.354  1.00 93.60  ? 318 GLU A CD  1 
ATOM   2262  O OE1 . GLU A 1 289 ? -4.883  -16.694 11.233  1.00 93.01  ? 318 GLU A OE1 1 
ATOM   2263  O OE2 . GLU A 1 289 ? -3.890  -15.611 12.888  1.00 105.47 ? 318 GLU A OE2 1 
ATOM   2264  N N   . VAL A 1 290 ? -2.066  -21.845 11.142  1.00 88.41  ? 319 VAL A N   1 
ATOM   2265  C CA  . VAL A 1 290 ? -2.256  -22.859 10.115  1.00 85.07  ? 319 VAL A CA  1 
ATOM   2266  C C   . VAL A 1 290 ? -1.528  -24.143 10.513  1.00 82.74  ? 319 VAL A C   1 
ATOM   2267  O O   . VAL A 1 290 ? -2.139  -25.210 10.554  1.00 93.03  ? 319 VAL A O   1 
ATOM   2268  C CB  . VAL A 1 290 ? -1.882  -22.389 8.693   1.00 89.38  ? 319 VAL A CB  1 
ATOM   2269  C CG1 . VAL A 1 290 ? -3.076  -21.780 7.965   1.00 93.41  ? 319 VAL A CG1 1 
ATOM   2270  C CG2 . VAL A 1 290 ? -0.709  -21.417 8.658   1.00 85.71  ? 319 VAL A CG2 1 
ATOM   2271  N N   . GLY A 1 291 ? -0.185  -24.015 10.787  1.00 72.99  ? 320 GLY A N   1 
ATOM   2272  C CA  . GLY A 1 291 ? 0.598   -25.163 11.208  1.00 78.89  ? 320 GLY A CA  1 
ATOM   2273  C C   . GLY A 1 291 ? 1.706   -25.455 10.202  1.00 87.93  ? 320 GLY A C   1 
ATOM   2274  O O   . GLY A 1 291 ? 1.771   -24.814 9.154   1.00 92.57  ? 320 GLY A O   1 
ATOM   2275  N N   . LYS A 1 292 ? 2.547   -26.444 10.544  1.00 94.03  ? 321 LYS A N   1 
ATOM   2276  C CA  . LYS A 1 292 ? 3.674   -26.880 9.730   1.00 100.72 ? 321 LYS A CA  1 
ATOM   2277  C C   . LYS A 1 292 ? 3.284   -27.043 8.257   1.00 101.27 ? 321 LYS A C   1 
ATOM   2278  O O   . LYS A 1 292 ? 4.092   -26.780 7.368   1.00 102.00 ? 321 LYS A O   1 
ATOM   2279  C CB  . LYS A 1 292 ? 4.185   -28.219 10.282  1.00 109.14 ? 321 LYS A CB  1 
ATOM   2280  C CG  . LYS A 1 292 ? 4.885   -28.162 11.640  1.00 114.75 ? 321 LYS A CG  1 
ATOM   2281  C CD  . LYS A 1 292 ? 5.161   -29.515 12.300  1.00 118.55 ? 321 LYS A CD  1 
ATOM   2282  C CE  . LYS A 1 292 ? 5.801   -30.574 11.432  1.00 111.94 ? 321 LYS A CE  1 
ATOM   2283  N NZ  . LYS A 1 292 ? 7.120   -30.202 10.911  1.00 107.74 ? 321 LYS A NZ  1 
ATOM   2284  N N   . ASP A 1 293 ? 2.035   -27.460 8.013   1.00 92.04  ? 322 ASP A N   1 
ATOM   2285  C CA  . ASP A 1 293 ? 1.613   -28.016 6.737   1.00 86.60  ? 322 ASP A CA  1 
ATOM   2286  C C   . ASP A 1 293 ? 1.319   -26.917 5.710   1.00 76.14  ? 322 ASP A C   1 
ATOM   2287  O O   . ASP A 1 293 ? 1.260   -27.176 4.510   1.00 75.38  ? 322 ASP A O   1 
ATOM   2288  C CB  . ASP A 1 293 ? 0.433   -28.954 6.965   1.00 85.12  ? 322 ASP A CB  1 
ATOM   2289  C CG  . ASP A 1 293 ? 0.698   -30.120 7.915   1.00 89.69  ? 322 ASP A CG  1 
ATOM   2290  O OD1 . ASP A 1 293 ? 1.506   -29.937 8.855   1.00 92.62  ? 322 ASP A OD1 1 
ATOM   2291  O OD2 . ASP A 1 293 ? 0.075   -31.197 7.731   1.00 80.47  ? 322 ASP A OD2 1 
ATOM   2292  N N   . VAL A 1 294 ? 1.133   -25.677 6.162   1.00 71.21  ? 323 VAL A N   1 
ATOM   2293  C CA  . VAL A 1 294 ? 0.560   -24.655 5.302   1.00 65.42  ? 323 VAL A CA  1 
ATOM   2294  C C   . VAL A 1 294 ? 1.229   -24.696 3.922   1.00 59.57  ? 323 VAL A C   1 
ATOM   2295  O O   . VAL A 1 294 ? 2.441   -24.820 3.803   1.00 64.71  ? 323 VAL A O   1 
ATOM   2296  C CB  . VAL A 1 294 ? 0.630   -23.260 5.961   1.00 68.84  ? 323 VAL A CB  1 
ATOM   2297  C CG1 . VAL A 1 294 ? 2.060   -22.761 6.183   1.00 69.93  ? 323 VAL A CG1 1 
ATOM   2298  C CG2 . VAL A 1 294 ? -0.183  -22.235 5.179   1.00 69.31  ? 323 VAL A CG2 1 
ATOM   2299  N N   . SER A 1 295 ? 0.408   -24.595 2.877   1.00 59.06  ? 324 SER A N   1 
ATOM   2300  C CA  . SER A 1 295 ? 0.844   -24.640 1.494   1.00 61.57  ? 324 SER A CA  1 
ATOM   2301  C C   . SER A 1 295 ? 1.189   -23.239 1.004   1.00 65.27  ? 324 SER A C   1 
ATOM   2302  O O   . SER A 1 295 ? 0.853   -22.244 1.647   1.00 68.69  ? 324 SER A O   1 
ATOM   2303  C CB  . SER A 1 295 ? -0.239  -25.232 0.624   1.00 69.01  ? 324 SER A CB  1 
ATOM   2304  O OG  . SER A 1 295 ? -1.425  -24.451 0.710   1.00 62.28  ? 324 SER A OG  1 
ATOM   2305  N N   . ASP A 1 296 ? 1.842   -23.183 -0.159  1.00 63.89  ? 325 ASP A N   1 
ATOM   2306  C CA  . ASP A 1 296 ? 2.226   -21.922 -0.772  1.00 74.07  ? 325 ASP A CA  1 
ATOM   2307  C C   . ASP A 1 296 ? 0.970   -21.105 -1.084  1.00 69.60  ? 325 ASP A C   1 
ATOM   2308  O O   . ASP A 1 296 ? 0.992   -19.882 -0.959  1.00 74.20  ? 325 ASP A O   1 
ATOM   2309  C CB  . ASP A 1 296 ? 3.132   -22.132 -1.984  1.00 78.16  ? 325 ASP A CB  1 
ATOM   2310  C CG  . ASP A 1 296 ? 4.420   -22.919 -1.744  1.00 77.75  ? 325 ASP A CG  1 
ATOM   2311  O OD1 . ASP A 1 296 ? 4.739   -23.186 -0.568  1.00 71.24  ? 325 ASP A OD1 1 
ATOM   2312  O OD2 . ASP A 1 296 ? 5.093   -23.276 -2.741  1.00 80.11  ? 325 ASP A OD2 1 
ATOM   2313  N N   . GLU A 1 297 ? -0.126  -21.781 -1.468  1.00 70.30  ? 326 GLU A N   1 
ATOM   2314  C CA  . GLU A 1 297 ? -1.387  -21.104 -1.755  1.00 80.44  ? 326 GLU A CA  1 
ATOM   2315  C C   . GLU A 1 297 ? -1.961  -20.494 -0.473  1.00 70.63  ? 326 GLU A C   1 
ATOM   2316  O O   . GLU A 1 297 ? -2.225  -19.291 -0.448  1.00 54.92  ? 326 GLU A O   1 
ATOM   2317  C CB  . GLU A 1 297 ? -2.422  -21.971 -2.483  1.00 96.72  ? 326 GLU A CB  1 
ATOM   2318  C CG  . GLU A 1 297 ? -2.578  -23.383 -1.917  1.00 111.76 ? 326 GLU A CG  1 
ATOM   2319  C CD  . GLU A 1 297 ? -3.959  -24.007 -2.064  1.00 123.07 ? 326 GLU A CD  1 
ATOM   2320  O OE1 . GLU A 1 297 ? -4.050  -25.117 -2.636  1.00 130.35 ? 326 GLU A OE1 1 
ATOM   2321  O OE2 . GLU A 1 297 ? -4.946  -23.392 -1.594  1.00 122.12 ? 326 GLU A OE2 1 
ATOM   2322  N N   . LYS A 1 298 ? -2.117  -21.309 0.587   1.00 62.19  ? 327 LYS A N   1 
ATOM   2323  C CA  . LYS A 1 298 ? -2.598  -20.837 1.881   1.00 69.62  ? 327 LYS A CA  1 
ATOM   2324  C C   . LYS A 1 298 ? -1.755  -19.656 2.378   1.00 59.40  ? 327 LYS A C   1 
ATOM   2325  O O   . LYS A 1 298 ? -2.290  -18.632 2.823   1.00 57.20  ? 327 LYS A O   1 
ATOM   2326  C CB  . LYS A 1 298 ? -2.614  -21.977 2.913   1.00 77.68  ? 327 LYS A CB  1 
ATOM   2327  C CG  . LYS A 1 298 ? -3.886  -22.837 2.947   1.00 91.86  ? 327 LYS A CG  1 
ATOM   2328  C CD  . LYS A 1 298 ? -3.910  -23.929 4.017   1.00 97.24  ? 327 LYS A CD  1 
ATOM   2329  C CE  . LYS A 1 298 ? -3.198  -25.184 3.594   1.00 97.09  ? 327 LYS A CE  1 
ATOM   2330  N NZ  . LYS A 1 298 ? -2.909  -26.087 4.711   1.00 95.76  ? 327 LYS A NZ  1 
ATOM   2331  N N   . LEU A 1 299 ? -0.430  -19.795 2.281   1.00 51.49  ? 328 LEU A N   1 
ATOM   2332  C CA  . LEU A 1 299 ? 0.466   -18.801 2.837   1.00 51.27  ? 328 LEU A CA  1 
ATOM   2333  C C   . LEU A 1 299 ? 0.379   -17.536 1.990   1.00 54.52  ? 328 LEU A C   1 
ATOM   2334  O O   . LEU A 1 299 ? 0.176   -16.449 2.530   1.00 55.39  ? 328 LEU A O   1 
ATOM   2335  C CB  . LEU A 1 299 ? 1.887   -19.347 2.930   1.00 58.62  ? 328 LEU A CB  1 
ATOM   2336  C CG  . LEU A 1 299 ? 2.947   -18.376 3.473   1.00 61.08  ? 328 LEU A CG  1 
ATOM   2337  C CD1 . LEU A 1 299 ? 2.478   -17.715 4.768   1.00 59.54  ? 328 LEU A CD1 1 
ATOM   2338  C CD2 . LEU A 1 299 ? 4.285   -19.082 3.683   1.00 57.05  ? 328 LEU A CD2 1 
ATOM   2339  N N   . ARG A 1 300 ? 0.481   -17.695 0.664   1.00 57.95  ? 329 ARG A N   1 
ATOM   2340  C CA  . ARG A 1 300 ? 0.292   -16.595 -0.277  1.00 65.69  ? 329 ARG A CA  1 
ATOM   2341  C C   . ARG A 1 300 ? -1.013  -15.836 0.013   1.00 65.74  ? 329 ARG A C   1 
ATOM   2342  O O   . ARG A 1 300 ? -1.038  -14.597 -0.006  1.00 61.38  ? 329 ARG A O   1 
ATOM   2343  C CB  . ARG A 1 300 ? 0.339   -17.140 -1.713  1.00 73.28  ? 329 ARG A CB  1 
ATOM   2344  C CG  . ARG A 1 300 ? 0.668   -16.125 -2.799  1.00 79.07  ? 329 ARG A CG  1 
ATOM   2345  C CD  . ARG A 1 300 ? 0.138   -16.597 -4.146  1.00 89.30  ? 329 ARG A CD  1 
ATOM   2346  N NE  . ARG A 1 300 ? -1.330  -16.630 -4.089  1.00 99.51  ? 329 ARG A NE  1 
ATOM   2347  C CZ  . ARG A 1 300 ? -2.144  -17.178 -4.981  1.00 94.91  ? 329 ARG A CZ  1 
ATOM   2348  N NH1 . ARG A 1 300 ? -3.445  -17.240 -4.737  1.00 98.78  ? 329 ARG A NH1 1 
ATOM   2349  N NH2 . ARG A 1 300 ? -1.657  -17.684 -6.099  1.00 87.58  ? 329 ARG A NH2 1 
ATOM   2350  N N   . ASP A 1 301 ? -2.088  -16.588 0.304   1.00 66.07  ? 330 ASP A N   1 
ATOM   2351  C CA  . ASP A 1 301 ? -3.383  -16.020 0.661   1.00 71.00  ? 330 ASP A CA  1 
ATOM   2352  C C   . ASP A 1 301 ? -3.266  -15.178 1.926   1.00 63.19  ? 330 ASP A C   1 
ATOM   2353  O O   . ASP A 1 301 ? -3.608  -13.987 1.926   1.00 58.47  ? 330 ASP A O   1 
ATOM   2354  C CB  . ASP A 1 301 ? -4.440  -17.099 0.854   1.00 81.72  ? 330 ASP A CB  1 
ATOM   2355  C CG  . ASP A 1 301 ? -5.395  -17.304 -0.319  1.00 91.54  ? 330 ASP A CG  1 
ATOM   2356  O OD1 . ASP A 1 301 ? -4.916  -17.330 -1.488  1.00 76.40  ? 330 ASP A OD1 1 
ATOM   2357  O OD2 . ASP A 1 301 ? -6.613  -17.440 -0.058  1.00 98.93  ? 330 ASP A OD2 1 
ATOM   2358  N N   . TYR A 1 302 ? -2.775  -15.823 2.991   1.00 61.54  ? 331 TYR A N   1 
ATOM   2359  C CA  . TYR A 1 302 ? -2.636  -15.181 4.290   1.00 56.80  ? 331 TYR A CA  1 
ATOM   2360  C C   . TYR A 1 302 ? -1.879  -13.861 4.134   1.00 57.24  ? 331 TYR A C   1 
ATOM   2361  O O   . TYR A 1 302 ? -2.247  -12.845 4.724   1.00 52.58  ? 331 TYR A O   1 
ATOM   2362  C CB  . TYR A 1 302 ? -1.980  -16.164 5.262   1.00 56.91  ? 331 TYR A CB  1 
ATOM   2363  C CG  . TYR A 1 302 ? -1.806  -15.563 6.647   1.00 60.44  ? 331 TYR A CG  1 
ATOM   2364  C CD1 . TYR A 1 302 ? -0.732  -14.733 6.935   1.00 68.20  ? 331 TYR A CD1 1 
ATOM   2365  C CD2 . TYR A 1 302 ? -2.727  -15.801 7.661   1.00 69.68  ? 331 TYR A CD2 1 
ATOM   2366  C CE1 . TYR A 1 302 ? -0.579  -14.157 8.188   1.00 71.32  ? 331 TYR A CE1 1 
ATOM   2367  C CE2 . TYR A 1 302 ? -2.578  -15.240 8.921   1.00 70.07  ? 331 TYR A CE2 1 
ATOM   2368  C CZ  . TYR A 1 302 ? -1.499  -14.415 9.187   1.00 64.62  ? 331 TYR A CZ  1 
ATOM   2369  O OH  . TYR A 1 302 ? -1.312  -13.856 10.416  1.00 62.57  ? 331 TYR A OH  1 
ATOM   2370  N N   . ILE A 1 303 ? -0.840  -13.868 3.291   1.00 57.11  ? 332 ILE A N   1 
ATOM   2371  C CA  . ILE A 1 303 ? -0.049  -12.678 3.030   1.00 49.90  ? 332 ILE A CA  1 
ATOM   2372  C C   . ILE A 1 303 ? -0.904  -11.601 2.361   1.00 51.43  ? 332 ILE A C   1 
ATOM   2373  O O   . ILE A 1 303 ? -0.909  -10.449 2.812   1.00 49.96  ? 332 ILE A O   1 
ATOM   2374  C CB  . ILE A 1 303 ? 1.212   -13.057 2.233   1.00 53.57  ? 332 ILE A CB  1 
ATOM   2375  C CG1 . ILE A 1 303 ? 2.105   -14.001 3.060   1.00 55.83  ? 332 ILE A CG1 1 
ATOM   2376  C CG2 . ILE A 1 303 ? 1.980   -11.822 1.756   1.00 51.75  ? 332 ILE A CG2 1 
ATOM   2377  C CD1 . ILE A 1 303 ? 2.567   -13.435 4.397   1.00 51.33  ? 332 ILE A CD1 1 
ATOM   2378  N N   . TRP A 1 304 ? -1.622  -11.975 1.294   1.00 58.25  ? 333 TRP A N   1 
ATOM   2379  C CA  . TRP A 1 304 ? -2.542  -11.076 0.607   1.00 56.74  ? 333 TRP A CA  1 
ATOM   2380  C C   . TRP A 1 304 ? -3.522  -10.450 1.585   1.00 52.92  ? 333 TRP A C   1 
ATOM   2381  O O   . TRP A 1 304 ? -3.768  -9.239  1.551   1.00 52.16  ? 333 TRP A O   1 
ATOM   2382  C CB  . TRP A 1 304 ? -3.366  -11.821 -0.454  1.00 68.78  ? 333 TRP A CB  1 
ATOM   2383  C CG  . TRP A 1 304 ? -2.619  -12.165 -1.709  1.00 63.04  ? 333 TRP A CG  1 
ATOM   2384  C CD1 . TRP A 1 304 ? -2.319  -13.411 -2.177  1.00 62.80  ? 333 TRP A CD1 1 
ATOM   2385  C CD2 . TRP A 1 304 ? -2.082  -11.226 -2.659  1.00 61.39  ? 333 TRP A CD2 1 
ATOM   2386  N NE1 . TRP A 1 304 ? -1.623  -13.310 -3.351  1.00 62.95  ? 333 TRP A NE1 1 
ATOM   2387  C CE2 . TRP A 1 304 ? -1.466  -11.988 -3.674  1.00 57.23  ? 333 TRP A CE2 1 
ATOM   2388  C CE3 . TRP A 1 304 ? -2.062  -9.831  -2.742  1.00 57.35  ? 333 TRP A CE3 1 
ATOM   2389  C CZ2 . TRP A 1 304 ? -0.831  -11.400 -4.761  1.00 61.23  ? 333 TRP A CZ2 1 
ATOM   2390  C CZ3 . TRP A 1 304 ? -1.438  -9.253  -3.823  1.00 66.47  ? 333 TRP A CZ3 1 
ATOM   2391  C CH2 . TRP A 1 304 ? -0.830  -10.026 -4.814  1.00 66.13  ? 333 TRP A CH2 1 
ATOM   2392  N N   . ASN A 1 305 ? -4.131  -11.317 2.398   1.00 54.42  ? 334 ASN A N   1 
ATOM   2393  C CA  . ASN A 1 305 ? -5.109  -10.885 3.379   1.00 60.97  ? 334 ASN A CA  1 
ATOM   2394  C C   . ASN A 1 305 ? -4.472  -9.818  4.275   1.00 64.23  ? 334 ASN A C   1 
ATOM   2395  O O   . ASN A 1 305 ? -5.090  -8.778  4.512   1.00 73.57  ? 334 ASN A O   1 
ATOM   2396  C CB  . ASN A 1 305 ? -5.711  -12.100 4.086   1.00 70.78  ? 334 ASN A CB  1 
ATOM   2397  C CG  . ASN A 1 305 ? -6.450  -13.006 3.123   1.00 72.60  ? 334 ASN A CG  1 
ATOM   2398  O OD1 . ASN A 1 305 ? -6.384  -12.811 1.905   1.00 82.97  ? 334 ASN A OD1 1 
ATOM   2399  N ND2 . ASN A 1 305 ? -7.152  -14.006 3.631   1.00 68.91  ? 334 ASN A ND2 1 
ATOM   2400  N N   . THR A 1 306 ? -3.214  -10.058 4.696   1.00 62.04  ? 335 THR A N   1 
ATOM   2401  C CA  . THR A 1 306 ? -2.446  -9.161  5.552   1.00 60.65  ? 335 THR A CA  1 
ATOM   2402  C C   . THR A 1 306 ? -2.251  -7.804  4.876   1.00 61.44  ? 335 THR A C   1 
ATOM   2403  O O   . THR A 1 306 ? -2.491  -6.776  5.512   1.00 68.44  ? 335 THR A O   1 
ATOM   2404  C CB  . THR A 1 306 ? -1.104  -9.801  5.934   1.00 61.31  ? 335 THR A CB  1 
ATOM   2405  O OG1 . THR A 1 306 ? -1.387  -10.917 6.770   1.00 55.03  ? 335 THR A OG1 1 
ATOM   2406  C CG2 . THR A 1 306 ? -0.191  -8.897  6.747   1.00 62.82  ? 335 THR A CG2 1 
ATOM   2407  N N   . LEU A 1 307 ? -1.809  -7.803  3.606   1.00 71.18  ? 336 LEU A N   1 
ATOM   2408  C CA  . LEU A 1 307 ? -1.509  -6.574  2.872   1.00 70.92  ? 336 LEU A CA  1 
ATOM   2409  C C   . LEU A 1 307 ? -2.792  -5.814  2.517   1.00 66.74  ? 336 LEU A C   1 
ATOM   2410  O O   . LEU A 1 307 ? -2.805  -4.590  2.582   1.00 56.70  ? 336 LEU A O   1 
ATOM   2411  C CB  . LEU A 1 307 ? -0.691  -6.804  1.595   1.00 78.87  ? 336 LEU A CB  1 
ATOM   2412  C CG  . LEU A 1 307 ? 0.844   -6.891  1.689   1.00 82.50  ? 336 LEU A CG  1 
ATOM   2413  C CD1 . LEU A 1 307 ? 1.477   -6.258  2.927   1.00 86.37  ? 336 LEU A CD1 1 
ATOM   2414  C CD2 . LEU A 1 307 ? 1.296   -8.334  1.537   1.00 81.05  ? 336 LEU A CD2 1 
ATOM   2415  N N   . ASN A 1 308 ? -3.850  -6.531  2.112   1.00 74.43  ? 337 ASN A N   1 
ATOM   2416  C CA  . ASN A 1 308 ? -5.102  -5.915  1.684   1.00 72.96  ? 337 ASN A CA  1 
ATOM   2417  C C   . ASN A 1 308 ? -5.726  -5.119  2.825   1.00 70.74  ? 337 ASN A C   1 
ATOM   2418  O O   . ASN A 1 308 ? -6.247  -4.030  2.603   1.00 71.17  ? 337 ASN A O   1 
ATOM   2419  C CB  . ASN A 1 308 ? -6.061  -6.950  1.112   1.00 68.60  ? 337 ASN A CB  1 
ATOM   2420  C CG  . ASN A 1 308 ? -5.486  -7.556  -0.145  1.00 73.02  ? 337 ASN A CG  1 
ATOM   2421  O OD1 . ASN A 1 308 ? -4.935  -6.818  -0.971  1.00 68.93  ? 337 ASN A OD1 1 
ATOM   2422  N ND2 . ASN A 1 308 ? -5.548  -8.875  -0.292  1.00 73.44  ? 337 ASN A ND2 1 
ATOM   2423  N N   . SER A 1 309 ? -5.610  -5.643  4.047   1.00 66.62  ? 338 SER A N   1 
ATOM   2424  C CA  . SER A 1 309 ? -6.054  -4.940  5.236   1.00 65.38  ? 338 SER A CA  1 
ATOM   2425  C C   . SER A 1 309 ? -5.008  -3.935  5.725   1.00 61.88  ? 338 SER A C   1 
ATOM   2426  O O   . SER A 1 309 ? -5.081  -3.493  6.866   1.00 66.56  ? 338 SER A O   1 
ATOM   2427  C CB  . SER A 1 309 ? -6.400  -5.932  6.314   1.00 72.81  ? 338 SER A CB  1 
ATOM   2428  O OG  . SER A 1 309 ? -5.337  -6.856  6.506   1.00 79.43  ? 338 SER A OG  1 
ATOM   2429  N N   . GLY A 1 310 ? -4.037  -3.569  4.877   1.00 62.04  ? 339 GLY A N   1 
ATOM   2430  C CA  . GLY A 1 310 ? -3.046  -2.560  5.225   1.00 62.39  ? 339 GLY A CA  1 
ATOM   2431  C C   . GLY A 1 310 ? -2.212  -2.932  6.460   1.00 67.73  ? 339 GLY A C   1 
ATOM   2432  O O   . GLY A 1 310 ? -1.787  -2.052  7.216   1.00 59.67  ? 339 GLY A O   1 
ATOM   2433  N N   . ARG A 1 311 ? -1.973  -4.237  6.675   1.00 67.72  ? 340 ARG A N   1 
ATOM   2434  C CA  . ARG A 1 311 ? -1.001  -4.672  7.670   1.00 67.87  ? 340 ARG A CA  1 
ATOM   2435  C C   . ARG A 1 311 ? 0.299   -4.917  6.914   1.00 70.82  ? 340 ARG A C   1 
ATOM   2436  O O   . ARG A 1 311 ? 0.357   -4.723  5.696   1.00 73.39  ? 340 ARG A O   1 
ATOM   2437  C CB  . ARG A 1 311 ? -1.468  -5.859  8.525   1.00 66.29  ? 340 ARG A CB  1 
ATOM   2438  C CG  . ARG A 1 311 ? -2.572  -5.519  9.518   1.00 68.99  ? 340 ARG A CG  1 
ATOM   2439  C CD  . ARG A 1 311 ? -3.053  -6.717  10.346  1.00 82.44  ? 340 ARG A CD  1 
ATOM   2440  N NE  . ARG A 1 311 ? -3.913  -7.679  9.634   1.00 92.12  ? 340 ARG A NE  1 
ATOM   2441  C CZ  . ARG A 1 311 ? -5.078  -8.198  10.064  1.00 95.80  ? 340 ARG A CZ  1 
ATOM   2442  N NH1 . ARG A 1 311 ? -5.767  -9.025  9.293   1.00 93.78  ? 340 ARG A NH1 1 
ATOM   2443  N NH2 . ARG A 1 311 ? -5.572  -7.886  11.253  1.00 97.21  ? 340 ARG A NH2 1 
ATOM   2444  N N   . VAL A 1 312 ? 1.358   -5.283  7.637   1.00 66.93  ? 341 VAL A N   1 
ATOM   2445  C CA  . VAL A 1 312 ? 2.650   -5.413  6.985   1.00 69.23  ? 341 VAL A CA  1 
ATOM   2446  C C   . VAL A 1 312 ? 3.298   -6.727  7.395   1.00 54.30  ? 341 VAL A C   1 
ATOM   2447  O O   . VAL A 1 312 ? 3.007   -7.314  8.434   1.00 49.48  ? 341 VAL A O   1 
ATOM   2448  C CB  . VAL A 1 312 ? 3.633   -4.241  7.185   1.00 72.32  ? 341 VAL A CB  1 
ATOM   2449  C CG1 . VAL A 1 312 ? 3.494   -3.204  6.074   1.00 76.61  ? 341 VAL A CG1 1 
ATOM   2450  C CG2 . VAL A 1 312 ? 3.524   -3.612  8.569   1.00 69.73  ? 341 VAL A CG2 1 
ATOM   2451  N N   . VAL A 1 313 ? 4.157   -7.193  6.500   1.00 53.07  ? 342 VAL A N   1 
ATOM   2452  C CA  . VAL A 1 313 ? 5.000   -8.328  6.806   1.00 50.65  ? 342 VAL A CA  1 
ATOM   2453  C C   . VAL A 1 313 ? 6.220   -7.805  7.557   1.00 44.36  ? 342 VAL A C   1 
ATOM   2454  O O   . VAL A 1 313 ? 7.041   -7.054  7.005   1.00 45.03  ? 342 VAL A O   1 
ATOM   2455  C CB  . VAL A 1 313 ? 5.387   -9.086  5.525   1.00 55.21  ? 342 VAL A CB  1 
ATOM   2456  C CG1 . VAL A 1 313 ? 6.286   -10.273 5.854   1.00 55.39  ? 342 VAL A CG1 1 
ATOM   2457  C CG2 . VAL A 1 313 ? 4.146   -9.523  4.745   1.00 52.91  ? 342 VAL A CG2 1 
ATOM   2458  N N   . PRO A 1 314 ? 6.376   -8.172  8.842   1.00 39.65  ? 343 PRO A N   1 
ATOM   2459  C CA  . PRO A 1 314 ? 7.570   -7.778  9.592   1.00 40.66  ? 343 PRO A CA  1 
ATOM   2460  C C   . PRO A 1 314 ? 8.833   -8.405  8.997   1.00 40.36  ? 343 PRO A C   1 
ATOM   2461  O O   . PRO A 1 314 ? 8.794   -9.521  8.500   1.00 41.92  ? 343 PRO A O   1 
ATOM   2462  C CB  . PRO A 1 314 ? 7.261   -8.278  11.021  1.00 39.79  ? 343 PRO A CB  1 
ATOM   2463  C CG  . PRO A 1 314 ? 6.321   -9.460  10.813  1.00 37.86  ? 343 PRO A CG  1 
ATOM   2464  C CD  . PRO A 1 314 ? 5.466   -9.037  9.622   1.00 40.41  ? 343 PRO A CD  1 
ATOM   2465  N N   . GLY A 1 315 ? 9.939   -7.650  9.013   1.00 40.55  ? 344 GLY A N   1 
ATOM   2466  C CA  . GLY A 1 315 ? 11.224  -8.143  8.552   1.00 47.06  ? 344 GLY A CA  1 
ATOM   2467  C C   . GLY A 1 315 ? 11.430  -8.022  7.043   1.00 44.62  ? 344 GLY A C   1 
ATOM   2468  O O   . GLY A 1 315 ? 12.525  -8.302  6.570   1.00 45.49  ? 344 GLY A O   1 
ATOM   2469  N N   . TYR A 1 316 ? 10.392  -7.618  6.299   1.00 48.06  ? 345 TYR A N   1 
ATOM   2470  C CA  . TYR A 1 316 ? 10.444  -7.572  4.843   1.00 51.55  ? 345 TYR A CA  1 
ATOM   2471  C C   . TYR A 1 316 ? 10.359  -6.135  4.333   1.00 66.77  ? 345 TYR A C   1 
ATOM   2472  O O   . TYR A 1 316 ? 9.462   -5.810  3.560   1.00 90.58  ? 345 TYR A O   1 
ATOM   2473  C CB  . TYR A 1 316 ? 9.307   -8.373  4.214   1.00 42.12  ? 345 TYR A CB  1 
ATOM   2474  C CG  . TYR A 1 316 ? 9.654   -9.841  4.031   1.00 41.12  ? 345 TYR A CG  1 
ATOM   2475  C CD1 . TYR A 1 316 ? 9.517   -10.755 5.068   1.00 41.93  ? 345 TYR A CD1 1 
ATOM   2476  C CD2 . TYR A 1 316 ? 10.145  -10.298 2.811   1.00 37.23  ? 345 TYR A CD2 1 
ATOM   2477  C CE1 . TYR A 1 316 ? 9.845   -12.090 4.891   1.00 39.25  ? 345 TYR A CE1 1 
ATOM   2478  C CE2 . TYR A 1 316 ? 10.487  -11.624 2.628   1.00 38.94  ? 345 TYR A CE2 1 
ATOM   2479  C CZ  . TYR A 1 316 ? 10.336  -12.521 3.669   1.00 38.02  ? 345 TYR A CZ  1 
ATOM   2480  O OH  . TYR A 1 316 ? 10.719  -13.816 3.472   1.00 42.50  ? 345 TYR A OH  1 
ATOM   2481  N N   . GLY A 1 317 ? 11.312  -5.301  4.753   1.00 59.13  ? 346 GLY A N   1 
ATOM   2482  C CA  . GLY A 1 317 ? 11.596  -4.023  4.114   1.00 58.24  ? 346 GLY A CA  1 
ATOM   2483  C C   . GLY A 1 317 ? 12.837  -3.385  4.744   1.00 48.31  ? 346 GLY A C   1 
ATOM   2484  O O   . GLY A 1 317 ? 13.378  -3.911  5.717   1.00 44.80  ? 346 GLY A O   1 
ATOM   2485  N N   . HIS A 1 318 ? 13.269  -2.247  4.203   1.00 43.97  ? 347 HIS A N   1 
ATOM   2486  C CA  . HIS A 1 318 ? 14.368  -1.499  4.781   1.00 49.66  ? 347 HIS A CA  1 
ATOM   2487  C C   . HIS A 1 318 ? 14.348  -0.058  4.286   1.00 49.77  ? 347 HIS A C   1 
ATOM   2488  O O   . HIS A 1 318 ? 13.939  0.203   3.157   1.00 48.14  ? 347 HIS A O   1 
ATOM   2489  C CB  . HIS A 1 318 ? 15.724  -2.137  4.430   1.00 49.69  ? 347 HIS A CB  1 
ATOM   2490  C CG  . HIS A 1 318 ? 16.827  -1.808  5.399   1.00 46.93  ? 347 HIS A CG  1 
ATOM   2491  N ND1 . HIS A 1 318 ? 16.900  -2.438  6.621   1.00 45.44  ? 347 HIS A ND1 1 
ATOM   2492  C CD2 . HIS A 1 318 ? 17.876  -0.965  5.371   1.00 45.93  ? 347 HIS A CD2 1 
ATOM   2493  C CE1 . HIS A 1 318 ? 17.944  -1.970  7.292   1.00 43.75  ? 347 HIS A CE1 1 
ATOM   2494  N NE2 . HIS A 1 318 ? 18.555  -1.094  6.552   1.00 46.56  ? 347 HIS A NE2 1 
ATOM   2495  N N   . ALA A 1 319 ? 14.909  0.840   5.111   1.00 50.78  ? 348 ALA A N   1 
ATOM   2496  C CA  . ALA A 1 319 ? 15.027  2.251   4.773   1.00 50.72  ? 348 ALA A CA  1 
ATOM   2497  C C   . ALA A 1 319 ? 16.017  2.477   3.618   1.00 53.45  ? 348 ALA A C   1 
ATOM   2498  O O   . ALA A 1 319 ? 15.908  3.464   2.885   1.00 42.91  ? 348 ALA A O   1 
ATOM   2499  C CB  . ALA A 1 319 ? 15.416  3.019   6.014   1.00 49.77  ? 348 ALA A CB  1 
ATOM   2500  N N   . VAL A 1 320 ? 16.969  1.554   3.414   1.00 50.46  ? 349 VAL A N   1 
ATOM   2501  C CA  . VAL A 1 320 ? 18.062  1.811   2.479   1.00 53.58  ? 349 VAL A CA  1 
ATOM   2502  C C   . VAL A 1 320 ? 18.148  0.652   1.486   1.00 49.18  ? 349 VAL A C   1 
ATOM   2503  O O   . VAL A 1 320 ? 18.126  0.861   0.278   1.00 49.72  ? 349 VAL A O   1 
ATOM   2504  C CB  . VAL A 1 320 ? 19.432  2.062   3.157   1.00 58.14  ? 349 VAL A CB  1 
ATOM   2505  C CG1 . VAL A 1 320 ? 20.472  2.629   2.186   1.00 57.44  ? 349 VAL A CG1 1 
ATOM   2506  C CG2 . VAL A 1 320 ? 19.326  2.951   4.393   1.00 59.01  ? 349 VAL A CG2 1 
ATOM   2507  N N   . LEU A 1 321 ? 18.261  -0.571  2.009   1.00 50.86  ? 350 LEU A N   1 
ATOM   2508  C CA  . LEU A 1 321 ? 18.396  -1.763  1.185   1.00 56.95  ? 350 LEU A CA  1 
ATOM   2509  C C   . LEU A 1 321 ? 17.211  -1.879  0.232   1.00 52.28  ? 350 LEU A C   1 
ATOM   2510  O O   . LEU A 1 321 ? 16.074  -1.562  0.596   1.00 48.79  ? 350 LEU A O   1 
ATOM   2511  C CB  . LEU A 1 321 ? 18.493  -3.014  2.060   1.00 51.43  ? 350 LEU A CB  1 
ATOM   2512  C CG  . LEU A 1 321 ? 19.832  -3.261  2.763   1.00 53.15  ? 350 LEU A CG  1 
ATOM   2513  C CD1 . LEU A 1 321 ? 19.601  -4.073  4.027   1.00 49.23  ? 350 LEU A CD1 1 
ATOM   2514  C CD2 . LEU A 1 321 ? 20.797  -3.980  1.827   1.00 50.45  ? 350 LEU A CD2 1 
ATOM   2515  N N   . ARG A 1 322 ? 17.486  -2.405  -0.967  1.00 51.26  ? 351 ARG A N   1 
ATOM   2516  C CA  . ARG A 1 322 ? 16.415  -2.708  -1.904  1.00 55.66  ? 351 ARG A CA  1 
ATOM   2517  C C   . ARG A 1 322 ? 16.659  -4.055  -2.589  1.00 54.37  ? 351 ARG A C   1 
ATOM   2518  O O   . ARG A 1 322 ? 16.187  -4.273  -3.698  1.00 58.18  ? 351 ARG A O   1 
ATOM   2519  C CB  . ARG A 1 322 ? 16.207  -1.484  -2.806  1.00 65.40  ? 351 ARG A CB  1 
ATOM   2520  C CG  . ARG A 1 322 ? 17.467  -0.722  -3.189  1.00 73.49  ? 351 ARG A CG  1 
ATOM   2521  C CD  . ARG A 1 322 ? 17.125  0.529   -3.994  1.00 88.96  ? 351 ARG A CD  1 
ATOM   2522  N NE  . ARG A 1 322 ? 18.176  0.892   -4.957  1.00 94.49  ? 351 ARG A NE  1 
ATOM   2523  C CZ  . ARG A 1 322 ? 18.703  2.098   -5.156  1.00 86.07  ? 351 ARG A CZ  1 
ATOM   2524  N NH1 . ARG A 1 322 ? 19.568  2.255   -6.146  1.00 82.46  ? 351 ARG A NH1 1 
ATOM   2525  N NH2 . ARG A 1 322 ? 18.352  3.136   -4.405  1.00 79.29  ? 351 ARG A NH2 1 
ATOM   2526  N N   . LYS A 1 323 ? 17.354  -4.968  -1.893  1.00 49.87  ? 352 LYS A N   1 
ATOM   2527  C CA  . LYS A 1 323 ? 17.490  -6.368  -2.282  1.00 45.39  ? 352 LYS A CA  1 
ATOM   2528  C C   . LYS A 1 323 ? 17.616  -7.201  -1.004  1.00 38.11  ? 352 LYS A C   1 
ATOM   2529  O O   . LYS A 1 323 ? 17.554  -6.662  0.110   1.00 48.04  ? 352 LYS A O   1 
ATOM   2530  C CB  . LYS A 1 323 ? 18.656  -6.534  -3.263  1.00 46.87  ? 352 LYS A CB  1 
ATOM   2531  C CG  . LYS A 1 323 ? 18.341  -6.132  -4.704  1.00 57.85  ? 352 LYS A CG  1 
ATOM   2532  C CD  . LYS A 1 323 ? 17.066  -6.770  -5.265  1.00 66.32  ? 352 LYS A CD  1 
ATOM   2533  C CE  . LYS A 1 323 ? 16.776  -6.451  -6.709  1.00 74.85  ? 352 LYS A CE  1 
ATOM   2534  N NZ  . LYS A 1 323 ? 16.655  -5.007  -6.945  1.00 73.47  ? 352 LYS A NZ  1 
ATOM   2535  N N   . THR A 1 324 ? 17.720  -8.510  -1.143  1.00 34.24  ? 353 THR A N   1 
ATOM   2536  C CA  . THR A 1 324 ? 17.822  -9.359  0.039   1.00 36.53  ? 353 THR A CA  1 
ATOM   2537  C C   . THR A 1 324 ? 19.053  -8.906  0.826   1.00 38.44  ? 353 THR A C   1 
ATOM   2538  O O   . THR A 1 324 ? 20.153  -8.788  0.299   1.00 37.27  ? 353 THR A O   1 
ATOM   2539  C CB  . THR A 1 324 ? 17.897  -10.846 -0.307  1.00 36.67  ? 353 THR A CB  1 
ATOM   2540  O OG1 . THR A 1 324 ? 16.763  -11.170 -1.101  1.00 41.30  ? 353 THR A OG1 1 
ATOM   2541  C CG2 . THR A 1 324 ? 17.799  -11.752 0.908   1.00 31.97  ? 353 THR A CG2 1 
ATOM   2542  N N   . ASP A 1 325 ? 18.831  -8.613  2.098   1.00 32.81  ? 354 ASP A N   1 
ATOM   2543  C CA  . ASP A 1 325 ? 19.898  -8.320  3.012   1.00 32.81  ? 354 ASP A CA  1 
ATOM   2544  C C   . ASP A 1 325 ? 20.885  -9.485  3.032   1.00 32.77  ? 354 ASP A C   1 
ATOM   2545  O O   . ASP A 1 325 ? 20.517  -10.593 3.373   1.00 33.16  ? 354 ASP A O   1 
ATOM   2546  C CB  . ASP A 1 325 ? 19.300  -8.054  4.380   1.00 32.24  ? 354 ASP A CB  1 
ATOM   2547  C CG  . ASP A 1 325 ? 20.266  -7.550  5.437   1.00 38.03  ? 354 ASP A CG  1 
ATOM   2548  O OD1 . ASP A 1 325 ? 21.474  -7.439  5.100   1.00 34.83  ? 354 ASP A OD1 1 
ATOM   2549  O OD2 . ASP A 1 325 ? 19.795  -7.279  6.582   1.00 37.38  ? 354 ASP A OD2 1 
ATOM   2550  N N   . PRO A 1 326 ? 22.189  -9.256  2.767   1.00 30.23  ? 355 PRO A N   1 
ATOM   2551  C CA  . PRO A 1 326 ? 23.192  -10.319 2.842   1.00 34.08  ? 355 PRO A CA  1 
ATOM   2552  C C   . PRO A 1 326 ? 23.293  -10.911 4.241   1.00 31.66  ? 355 PRO A C   1 
ATOM   2553  O O   . PRO A 1 326 ? 23.747  -12.026 4.393   1.00 30.49  ? 355 PRO A O   1 
ATOM   2554  C CB  . PRO A 1 326 ? 24.495  -9.630  2.400   1.00 34.38  ? 355 PRO A CB  1 
ATOM   2555  C CG  . PRO A 1 326 ? 24.261  -8.176  2.744   1.00 37.99  ? 355 PRO A CG  1 
ATOM   2556  C CD  . PRO A 1 326 ? 22.783  -7.967  2.398   1.00 35.51  ? 355 PRO A CD  1 
ATOM   2557  N N   . ARG A 1 327 ? 22.832  -10.176 5.264   1.00 32.13  ? 356 ARG A N   1 
ATOM   2558  C CA  . ARG A 1 327 ? 22.829  -10.685 6.632   1.00 29.04  ? 356 ARG A CA  1 
ATOM   2559  C C   . ARG A 1 327 ? 21.712  -11.711 6.834   1.00 30.05  ? 356 ARG A C   1 
ATOM   2560  O O   . ARG A 1 327 ? 21.841  -12.639 7.636   1.00 32.39  ? 356 ARG A O   1 
ATOM   2561  C CB  . ARG A 1 327 ? 22.666  -9.486  7.575   1.00 30.30  ? 356 ARG A CB  1 
ATOM   2562  C CG  . ARG A 1 327 ? 23.794  -8.460  7.509   1.00 26.67  ? 356 ARG A CG  1 
ATOM   2563  C CD  . ARG A 1 327 ? 23.541  -7.284  8.406   1.00 26.91  ? 356 ARG A CD  1 
ATOM   2564  N NE  . ARG A 1 327 ? 22.337  -6.571  7.998   1.00 30.65  ? 356 ARG A NE  1 
ATOM   2565  C CZ  . ARG A 1 327 ? 21.678  -5.639  8.707   1.00 30.57  ? 356 ARG A CZ  1 
ATOM   2566  N NH1 . ARG A 1 327 ? 22.181  -5.173  9.824   1.00 28.96  ? 356 ARG A NH1 1 
ATOM   2567  N NH2 . ARG A 1 327 ? 20.496  -5.212  8.291   1.00 29.83  ? 356 ARG A NH2 1 
ATOM   2568  N N   . TYR A 1 328 ? 20.571  -11.500 6.157   1.00 30.06  ? 357 TYR A N   1 
ATOM   2569  C CA  . TYR A 1 328 ? 19.572  -12.546 5.979   1.00 33.91  ? 357 TYR A CA  1 
ATOM   2570  C C   . TYR A 1 328 ? 20.179  -13.810 5.341   1.00 32.40  ? 357 TYR A C   1 
ATOM   2571  O O   . TYR A 1 328 ? 20.052  -14.892 5.887   1.00 27.38  ? 357 TYR A O   1 
ATOM   2572  C CB  . TYR A 1 328 ? 18.418  -12.006 5.131   1.00 31.22  ? 357 TYR A CB  1 
ATOM   2573  C CG  . TYR A 1 328 ? 17.284  -13.010 5.025   1.00 34.77  ? 357 TYR A CG  1 
ATOM   2574  C CD1 . TYR A 1 328 ? 16.254  -13.021 5.976   1.00 30.76  ? 357 TYR A CD1 1 
ATOM   2575  C CD2 . TYR A 1 328 ? 17.241  -13.956 3.995   1.00 33.24  ? 357 TYR A CD2 1 
ATOM   2576  C CE1 . TYR A 1 328 ? 15.210  -13.925 5.883   1.00 36.26  ? 357 TYR A CE1 1 
ATOM   2577  C CE2 . TYR A 1 328 ? 16.244  -14.923 3.948   1.00 32.94  ? 357 TYR A CE2 1 
ATOM   2578  C CZ  . TYR A 1 328 ? 15.222  -14.898 4.885   1.00 36.38  ? 357 TYR A CZ  1 
ATOM   2579  O OH  . TYR A 1 328 ? 14.164  -15.755 4.826   1.00 35.11  ? 357 TYR A OH  1 
ATOM   2580  N N   . THR A 1 329 ? 20.819  -13.672 4.173   1.00 35.53  ? 358 THR A N   1 
ATOM   2581  C CA  . THR A 1 329 ? 21.327  -14.810 3.398   1.00 32.28  ? 358 THR A CA  1 
ATOM   2582  C C   . THR A 1 329 ? 22.285  -15.613 4.260   1.00 30.96  ? 358 THR A C   1 
ATOM   2583  O O   . THR A 1 329 ? 22.301  -16.837 4.182   1.00 32.86  ? 358 THR A O   1 
ATOM   2584  C CB  . THR A 1 329 ? 22.076  -14.289 2.170   1.00 34.95  ? 358 THR A CB  1 
ATOM   2585  O OG1 . THR A 1 329 ? 21.188  -13.488 1.411   1.00 32.52  ? 358 THR A OG1 1 
ATOM   2586  C CG2 . THR A 1 329 ? 22.632  -15.375 1.274   1.00 34.86  ? 358 THR A CG2 1 
ATOM   2587  N N   . CYS A 1 330 ? 23.129  -14.918 5.045   1.00 39.11  ? 359 CYS A N   1 
ATOM   2588  C CA  . CYS A 1 330 ? 24.059  -15.585 5.957   1.00 38.97  ? 359 CYS A CA  1 
ATOM   2589  C C   . CYS A 1 330 ? 23.330  -16.479 6.940   1.00 32.21  ? 359 CYS A C   1 
ATOM   2590  O O   . CYS A 1 330 ? 23.796  -17.548 7.269   1.00 32.77  ? 359 CYS A O   1 
ATOM   2591  C CB  . CYS A 1 330 ? 24.841  -14.637 6.867   1.00 48.11  ? 359 CYS A CB  1 
ATOM   2592  S SG  . CYS A 1 330 ? 26.076  -13.716 5.935   1.00 66.33  ? 359 CYS A SG  1 
ATOM   2593  N N   . GLN A 1 331 ? 22.255  -15.974 7.523   1.00 36.79  ? 360 GLN A N   1 
ATOM   2594  C CA  . GLN A 1 331 ? 21.523  -16.748 8.523   1.00 35.96  ? 360 GLN A CA  1 
ATOM   2595  C C   . GLN A 1 331 ? 20.744  -17.870 7.839   1.00 37.26  ? 360 GLN A C   1 
ATOM   2596  O O   . GLN A 1 331 ? 20.463  -18.900 8.438   1.00 33.25  ? 360 GLN A O   1 
ATOM   2597  C CB  . GLN A 1 331 ? 20.595  -15.779 9.249   1.00 41.22  ? 360 GLN A CB  1 
ATOM   2598  C CG  . GLN A 1 331 ? 21.373  -14.770 10.095  1.00 46.69  ? 360 GLN A CG  1 
ATOM   2599  C CD  . GLN A 1 331 ? 20.469  -13.945 10.971  1.00 49.67  ? 360 GLN A CD  1 
ATOM   2600  O OE1 . GLN A 1 331 ? 19.663  -13.160 10.471  1.00 54.14  ? 360 GLN A OE1 1 
ATOM   2601  N NE2 . GLN A 1 331 ? 20.587  -14.140 12.277  1.00 51.99  ? 360 GLN A NE2 1 
ATOM   2602  N N   . ARG A 1 332 ? 20.339  -17.638 6.588   1.00 37.64  ? 361 ARG A N   1 
ATOM   2603  C CA  . ARG A 1 332 ? 19.638  -18.666 5.837   1.00 37.30  ? 361 ARG A CA  1 
ATOM   2604  C C   . ARG A 1 332 ? 20.598  -19.842 5.635   1.00 34.90  ? 361 ARG A C   1 
ATOM   2605  O O   . ARG A 1 332 ? 20.224  -20.933 6.009   1.00 33.10  ? 361 ARG A O   1 
ATOM   2606  C CB  . ARG A 1 332 ? 19.009  -18.114 4.560   1.00 36.22  ? 361 ARG A CB  1 
ATOM   2607  C CG  . ARG A 1 332 ? 18.576  -19.232 3.618   1.00 42.68  ? 361 ARG A CG  1 
ATOM   2608  C CD  . ARG A 1 332 ? 17.782  -18.667 2.434   1.00 46.90  ? 361 ARG A CD  1 
ATOM   2609  N NE  . ARG A 1 332 ? 17.315  -19.672 1.464   1.00 51.09  ? 361 ARG A NE  1 
ATOM   2610  C CZ  . ARG A 1 332 ? 16.402  -20.639 1.634   1.00 54.13  ? 361 ARG A CZ  1 
ATOM   2611  N NH1 . ARG A 1 332 ? 16.263  -21.571 0.701   1.00 54.43  ? 361 ARG A NH1 1 
ATOM   2612  N NH2 . ARG A 1 332 ? 15.661  -20.710 2.730   1.00 54.22  ? 361 ARG A NH2 1 
ATOM   2613  N N   . GLU A 1 333 ? 21.857  -19.578 5.218   1.00 34.34  ? 362 GLU A N   1 
ATOM   2614  C CA  . GLU A 1 333 ? 22.882  -20.596 5.003   1.00 36.03  ? 362 GLU A CA  1 
ATOM   2615  C C   . GLU A 1 333 ? 23.214  -21.361 6.297   1.00 36.20  ? 362 GLU A C   1 
ATOM   2616  O O   . GLU A 1 333 ? 23.408  -22.563 6.270   1.00 31.67  ? 362 GLU A O   1 
ATOM   2617  C CB  . GLU A 1 333 ? 24.207  -19.974 4.563   1.00 41.85  ? 362 GLU A CB  1 
ATOM   2618  C CG  . GLU A 1 333 ? 24.204  -19.333 3.173   1.00 41.92  ? 362 GLU A CG  1 
ATOM   2619  C CD  . GLU A 1 333 ? 25.421  -18.446 2.907   1.00 44.64  ? 362 GLU A CD  1 
ATOM   2620  O OE1 . GLU A 1 333 ? 26.190  -18.098 3.840   1.00 38.86  ? 362 GLU A OE1 1 
ATOM   2621  O OE2 . GLU A 1 333 ? 25.600  -18.066 1.740   1.00 47.09  ? 362 GLU A OE2 1 
ATOM   2622  N N   . PHE A 1 334 ? 23.348  -20.664 7.434   1.00 31.71  ? 363 PHE A N   1 
ATOM   2623  C CA  . PHE A 1 334 ? 23.512  -21.299 8.734   1.00 35.50  ? 363 PHE A CA  1 
ATOM   2624  C C   . PHE A 1 334 ? 22.387  -22.314 8.943   1.00 41.23  ? 363 PHE A C   1 
ATOM   2625  O O   . PHE A 1 334 ? 22.650  -23.465 9.271   1.00 40.67  ? 363 PHE A O   1 
ATOM   2626  C CB  . PHE A 1 334 ? 23.512  -20.298 9.913   1.00 33.81  ? 363 PHE A CB  1 
ATOM   2627  C CG  . PHE A 1 334 ? 23.952  -20.877 11.257  1.00 29.83  ? 363 PHE A CG  1 
ATOM   2628  C CD1 . PHE A 1 334 ? 23.038  -21.477 12.102  1.00 29.86  ? 363 PHE A CD1 1 
ATOM   2629  C CD2 . PHE A 1 334 ? 25.287  -20.828 11.658  1.00 29.87  ? 363 PHE A CD2 1 
ATOM   2630  C CE1 . PHE A 1 334 ? 23.445  -22.035 13.296  1.00 31.00  ? 363 PHE A CE1 1 
ATOM   2631  C CE2 . PHE A 1 334 ? 25.692  -21.396 12.850  1.00 32.49  ? 363 PHE A CE2 1 
ATOM   2632  C CZ  . PHE A 1 334 ? 24.766  -21.985 13.675  1.00 32.48  ? 363 PHE A CZ  1 
ATOM   2633  N N   . ALA A 1 335 ? 21.142  -21.852 8.763   1.00 37.23  ? 364 ALA A N   1 
ATOM   2634  C CA  . ALA A 1 335 ? 19.960  -22.616 9.111   1.00 41.29  ? 364 ALA A CA  1 
ATOM   2635  C C   . ALA A 1 335 ? 19.852  -23.863 8.226   1.00 39.39  ? 364 ALA A C   1 
ATOM   2636  O O   . ALA A 1 335 ? 19.704  -24.993 8.682   1.00 35.57  ? 364 ALA A O   1 
ATOM   2637  C CB  . ALA A 1 335 ? 18.771  -21.693 8.950   1.00 42.66  ? 364 ALA A CB  1 
ATOM   2638  N N   . LEU A 1 336 ? 19.980  -23.642 6.930   1.00 40.30  ? 365 LEU A N   1 
ATOM   2639  C CA  . LEU A 1 336 ? 19.986  -24.721 5.961   1.00 44.88  ? 365 LEU A CA  1 
ATOM   2640  C C   . LEU A 1 336 ? 20.955  -25.815 6.381   1.00 40.38  ? 365 LEU A C   1 
ATOM   2641  O O   . LEU A 1 336 ? 20.713  -26.983 6.119   1.00 43.49  ? 365 LEU A O   1 
ATOM   2642  C CB  . LEU A 1 336 ? 20.366  -24.147 4.597   1.00 47.22  ? 365 LEU A CB  1 
ATOM   2643  C CG  . LEU A 1 336 ? 19.300  -24.191 3.497   1.00 53.74  ? 365 LEU A CG  1 
ATOM   2644  C CD1 . LEU A 1 336 ? 17.853  -24.175 3.997   1.00 45.82  ? 365 LEU A CD1 1 
ATOM   2645  C CD2 . LEU A 1 336 ? 19.605  -23.012 2.548   1.00 51.09  ? 365 LEU A CD2 1 
ATOM   2646  N N   . LYS A 1 337 ? 22.084  -25.416 6.955   1.00 46.64  ? 366 LYS A N   1 
ATOM   2647  C CA  . LYS A 1 337 ? 23.115  -26.349 7.380   1.00 47.83  ? 366 LYS A CA  1 
ATOM   2648  C C   . LYS A 1 337 ? 22.757  -26.998 8.718   1.00 42.93  ? 366 LYS A C   1 
ATOM   2649  O O   . LYS A 1 337 ? 22.790  -28.204 8.819   1.00 46.30  ? 366 LYS A O   1 
ATOM   2650  C CB  . LYS A 1 337 ? 24.460  -25.616 7.411   1.00 56.31  ? 366 LYS A CB  1 
ATOM   2651  C CG  . LYS A 1 337 ? 25.607  -26.361 8.065   1.00 67.26  ? 366 LYS A CG  1 
ATOM   2652  C CD  . LYS A 1 337 ? 26.980  -25.779 7.749   1.00 76.54  ? 366 LYS A CD  1 
ATOM   2653  C CE  . LYS A 1 337 ? 27.784  -26.692 6.874   1.00 84.69  ? 366 LYS A CE  1 
ATOM   2654  N NZ  . LYS A 1 337 ? 28.380  -27.760 7.681   1.00 88.53  ? 366 LYS A NZ  1 
ATOM   2655  N N   . HIS A 1 338 ? 22.407  -26.239 9.757   1.00 38.97  ? 367 HIS A N   1 
ATOM   2656  C CA  . HIS A 1 338 ? 22.455  -26.807 11.101  1.00 37.37  ? 367 HIS A CA  1 
ATOM   2657  C C   . HIS A 1 338 ? 21.081  -27.145 11.674  1.00 42.99  ? 367 HIS A C   1 
ATOM   2658  O O   . HIS A 1 338 ? 21.015  -27.839 12.691  1.00 44.43  ? 367 HIS A O   1 
ATOM   2659  C CB  . HIS A 1 338 ? 23.190  -25.863 12.062  1.00 46.09  ? 367 HIS A CB  1 
ATOM   2660  C CG  . HIS A 1 338 ? 24.609  -25.582 11.680  1.00 44.44  ? 367 HIS A CG  1 
ATOM   2661  N ND1 . HIS A 1 338 ? 25.665  -26.420 11.983  1.00 41.50  ? 367 HIS A ND1 1 
ATOM   2662  C CD2 . HIS A 1 338 ? 25.134  -24.550 10.981  1.00 44.80  ? 367 HIS A CD2 1 
ATOM   2663  C CE1 . HIS A 1 338 ? 26.787  -25.905 11.487  1.00 44.90  ? 367 HIS A CE1 1 
ATOM   2664  N NE2 . HIS A 1 338 ? 26.494  -24.753 10.890  1.00 42.57  ? 367 HIS A NE2 1 
ATOM   2665  N N   . LEU A 1 339 ? 19.995  -26.634 11.076  1.00 39.14  ? 368 LEU A N   1 
ATOM   2666  C CA  . LEU A 1 339 ? 18.661  -26.923 11.581  1.00 44.01  ? 368 LEU A CA  1 
ATOM   2667  C C   . LEU A 1 339 ? 17.632  -26.896 10.448  1.00 41.82  ? 368 LEU A C   1 
ATOM   2668  O O   . LEU A 1 339 ? 16.596  -26.226 10.545  1.00 37.36  ? 368 LEU A O   1 
ATOM   2669  C CB  . LEU A 1 339 ? 18.302  -25.921 12.679  1.00 45.81  ? 368 LEU A CB  1 
ATOM   2670  C CG  . LEU A 1 339 ? 18.411  -24.440 12.286  1.00 42.96  ? 368 LEU A CG  1 
ATOM   2671  C CD1 . LEU A 1 339 ? 17.208  -23.653 12.773  1.00 44.36  ? 368 LEU A CD1 1 
ATOM   2672  C CD2 . LEU A 1 339 ? 19.685  -23.833 12.831  1.00 45.84  ? 368 LEU A CD2 1 
ATOM   2673  N N   . PRO A 1 340 ? 17.856  -27.657 9.352   1.00 43.07  ? 369 PRO A N   1 
ATOM   2674  C CA  . PRO A 1 340 ? 16.952  -27.607 8.206   1.00 46.60  ? 369 PRO A CA  1 
ATOM   2675  C C   . PRO A 1 340 ? 15.549  -28.150 8.480   1.00 46.71  ? 369 PRO A C   1 
ATOM   2676  O O   . PRO A 1 340 ? 14.624  -27.813 7.738   1.00 44.55  ? 369 PRO A O   1 
ATOM   2677  C CB  . PRO A 1 340 ? 17.701  -28.394 7.103   1.00 48.53  ? 369 PRO A CB  1 
ATOM   2678  C CG  . PRO A 1 340 ? 18.625  -29.316 7.877   1.00 51.54  ? 369 PRO A CG  1 
ATOM   2679  C CD  . PRO A 1 340 ? 19.008  -28.549 9.140   1.00 47.58  ? 369 PRO A CD  1 
ATOM   2680  N N   . ASN A 1 341 ? 15.382  -28.953 9.544   1.00 42.32  ? 370 ASN A N   1 
ATOM   2681  C CA  . ASN A 1 341 ? 14.085  -29.572 9.800   1.00 52.64  ? 370 ASN A CA  1 
ATOM   2682  C C   . ASN A 1 341 ? 13.283  -28.776 10.824  1.00 53.49  ? 370 ASN A C   1 
ATOM   2683  O O   . ASN A 1 341 ? 12.143  -29.124 11.140  1.00 55.83  ? 370 ASN A O   1 
ATOM   2684  C CB  . ASN A 1 341 ? 14.193  -31.024 10.253  1.00 51.52  ? 370 ASN A CB  1 
ATOM   2685  C CG  . ASN A 1 341 ? 14.963  -31.860 9.259   1.00 54.13  ? 370 ASN A CG  1 
ATOM   2686  O OD1 . ASN A 1 341 ? 14.883  -31.612 8.051   1.00 54.72  ? 370 ASN A OD1 1 
ATOM   2687  N ND2 . ASN A 1 341 ? 15.751  -32.812 9.743   1.00 53.34  ? 370 ASN A ND2 1 
ATOM   2688  N N   . ASP A 1 342 ? 13.862  -27.690 11.332  1.00 52.46  ? 371 ASP A N   1 
ATOM   2689  C CA  . ASP A 1 342 ? 13.137  -26.819 12.243  1.00 50.16  ? 371 ASP A CA  1 
ATOM   2690  C C   . ASP A 1 342 ? 11.868  -26.248 11.586  1.00 46.69  ? 371 ASP A C   1 
ATOM   2691  O O   . ASP A 1 342 ? 11.907  -25.578 10.532  1.00 40.44  ? 371 ASP A O   1 
ATOM   2692  C CB  . ASP A 1 342 ? 14.059  -25.763 12.823  1.00 53.39  ? 371 ASP A CB  1 
ATOM   2693  C CG  . ASP A 1 342 ? 13.350  -24.840 13.796  1.00 48.46  ? 371 ASP A CG  1 
ATOM   2694  O OD1 . ASP A 1 342 ? 13.125  -25.269 14.925  1.00 49.70  ? 371 ASP A OD1 1 
ATOM   2695  O OD2 . ASP A 1 342 ? 12.955  -23.745 13.373  1.00 50.74  ? 371 ASP A OD2 1 
ATOM   2696  N N   . PRO A 1 343 ? 10.683  -26.486 12.197  1.00 48.13  ? 372 PRO A N   1 
ATOM   2697  C CA  . PRO A 1 343 ? 9.412   -26.001 11.632  1.00 50.94  ? 372 PRO A CA  1 
ATOM   2698  C C   . PRO A 1 343 ? 9.321   -24.484 11.427  1.00 48.25  ? 372 PRO A C   1 
ATOM   2699  O O   . PRO A 1 343 ? 8.809   -24.004 10.406  1.00 43.80  ? 372 PRO A O   1 
ATOM   2700  C CB  . PRO A 1 343 ? 8.340   -26.498 12.646  1.00 47.70  ? 372 PRO A CB  1 
ATOM   2701  C CG  . PRO A 1 343 ? 9.022   -27.591 13.467  1.00 43.20  ? 372 PRO A CG  1 
ATOM   2702  C CD  . PRO A 1 343 ? 10.505  -27.268 13.439  1.00 49.45  ? 372 PRO A CD  1 
ATOM   2703  N N   . MET A 1 344 ? 9.766   -23.739 12.450  1.00 48.23  ? 373 MET A N   1 
ATOM   2704  C CA  . MET A 1 344 ? 9.815   -22.288 12.403  1.00 46.15  ? 373 MET A CA  1 
ATOM   2705  C C   . MET A 1 344 ? 10.741  -21.901 11.251  1.00 41.71  ? 373 MET A C   1 
ATOM   2706  O O   . MET A 1 344 ? 10.374  -21.068 10.422  1.00 39.46  ? 373 MET A O   1 
ATOM   2707  C CB  . MET A 1 344 ? 10.291  -21.686 13.733  1.00 50.42  ? 373 MET A CB  1 
ATOM   2708  C CG  . MET A 1 344 ? 9.398   -21.947 14.961  1.00 55.58  ? 373 MET A CG  1 
ATOM   2709  S SD  . MET A 1 344 ? 7.904   -20.944 15.125  1.00 72.52  ? 373 MET A SD  1 
ATOM   2710  C CE  . MET A 1 344 ? 8.417   -19.306 14.586  1.00 63.75  ? 373 MET A CE  1 
ATOM   2711  N N   . PHE A 1 345 ? 11.882  -22.597 11.115  1.00 40.73  ? 374 PHE A N   1 
ATOM   2712  C CA  . PHE A 1 345 ? 12.779  -22.333 9.995   1.00 41.40  ? 374 PHE A CA  1 
ATOM   2713  C C   . PHE A 1 345 ? 12.042  -22.591 8.670   1.00 37.92  ? 374 PHE A C   1 
ATOM   2714  O O   . PHE A 1 345 ? 12.077  -21.763 7.740   1.00 37.99  ? 374 PHE A O   1 
ATOM   2715  C CB  . PHE A 1 345 ? 14.117  -23.081 10.086  1.00 42.61  ? 374 PHE A CB  1 
ATOM   2716  C CG  . PHE A 1 345 ? 14.922  -22.917 8.808   1.00 38.36  ? 374 PHE A CG  1 
ATOM   2717  C CD1 . PHE A 1 345 ? 15.193  -21.651 8.308   1.00 40.55  ? 374 PHE A CD1 1 
ATOM   2718  C CD2 . PHE A 1 345 ? 15.251  -24.022 8.024   1.00 41.88  ? 374 PHE A CD2 1 
ATOM   2719  C CE1 . PHE A 1 345 ? 15.857  -21.481 7.096   1.00 45.13  ? 374 PHE A CE1 1 
ATOM   2720  C CE2 . PHE A 1 345 ? 15.913  -23.855 6.811   1.00 40.70  ? 374 PHE A CE2 1 
ATOM   2721  C CZ  . PHE A 1 345 ? 16.222  -22.585 6.357   1.00 47.31  ? 374 PHE A CZ  1 
ATOM   2722  N N   . LYS A 1 346 ? 11.322  -23.709 8.607   1.00 39.24  ? 375 LYS A N   1 
ATOM   2723  C CA  . LYS A 1 346 ? 10.552  -24.069 7.423   1.00 44.11  ? 375 LYS A CA  1 
ATOM   2724  C C   . LYS A 1 346 ? 9.629   -22.923 7.002   1.00 45.02  ? 375 LYS A C   1 
ATOM   2725  O O   . LYS A 1 346 ? 9.644   -22.516 5.833   1.00 42.17  ? 375 LYS A O   1 
ATOM   2726  C CB  . LYS A 1 346 ? 9.839   -25.404 7.664   1.00 52.56  ? 375 LYS A CB  1 
ATOM   2727  C CG  . LYS A 1 346 ? 10.747  -26.638 7.638   1.00 58.53  ? 375 LYS A CG  1 
ATOM   2728  C CD  . LYS A 1 346 ? 10.118  -27.772 8.437   1.00 69.52  ? 375 LYS A CD  1 
ATOM   2729  C CE  . LYS A 1 346 ? 10.637  -29.129 8.128   1.00 75.02  ? 375 LYS A CE  1 
ATOM   2730  N NZ  . LYS A 1 346 ? 10.000  -30.108 9.014   1.00 79.17  ? 375 LYS A NZ  1 
ATOM   2731  N N   . LEU A 1 347 ? 8.894   -22.333 7.961   1.00 42.82  ? 376 LEU A N   1 
ATOM   2732  C CA  . LEU A 1 347 ? 7.986   -21.244 7.628   1.00 41.79  ? 376 LEU A CA  1 
ATOM   2733  C C   . LEU A 1 347 ? 8.750   -20.022 7.095   1.00 39.24  ? 376 LEU A C   1 
ATOM   2734  O O   . LEU A 1 347 ? 8.330   -19.330 6.161   1.00 38.68  ? 376 LEU A O   1 
ATOM   2735  C CB  . LEU A 1 347 ? 7.127   -20.930 8.860   1.00 42.18  ? 376 LEU A CB  1 
ATOM   2736  C CG  . LEU A 1 347 ? 6.226   -19.691 8.759   1.00 47.02  ? 376 LEU A CG  1 
ATOM   2737  C CD1 . LEU A 1 347 ? 5.291   -19.721 7.558   1.00 51.35  ? 376 LEU A CD1 1 
ATOM   2738  C CD2 . LEU A 1 347 ? 5.434   -19.555 10.041  1.00 51.79  ? 376 LEU A CD2 1 
ATOM   2739  N N   . VAL A 1 348 ? 9.882   -19.712 7.715   1.00 39.81  ? 377 VAL A N   1 
ATOM   2740  C CA  . VAL A 1 348 ? 10.630  -18.542 7.315   1.00 37.09  ? 377 VAL A CA  1 
ATOM   2741  C C   . VAL A 1 348 ? 11.125  -18.767 5.887   1.00 37.10  ? 377 VAL A C   1 
ATOM   2742  O O   . VAL A 1 348 ? 11.011  -17.876 5.055   1.00 41.23  ? 377 VAL A O   1 
ATOM   2743  C CB  . VAL A 1 348 ? 11.746  -18.293 8.350   1.00 39.45  ? 377 VAL A CB  1 
ATOM   2744  C CG1 . VAL A 1 348 ? 12.934  -17.523 7.784   1.00 38.60  ? 377 VAL A CG1 1 
ATOM   2745  C CG2 . VAL A 1 348 ? 11.184  -17.644 9.610   1.00 40.86  ? 377 VAL A CG2 1 
ATOM   2746  N N   . ALA A 1 349 ? 11.620  -19.971 5.580   1.00 35.50  ? 378 ALA A N   1 
ATOM   2747  C CA  . ALA A 1 349 ? 12.016  -20.279 4.207   1.00 39.48  ? 378 ALA A CA  1 
ATOM   2748  C C   . ALA A 1 349 ? 10.839  -20.208 3.232   1.00 38.83  ? 378 ALA A C   1 
ATOM   2749  O O   . ALA A 1 349 ? 10.988  -19.677 2.134   1.00 44.06  ? 378 ALA A O   1 
ATOM   2750  C CB  . ALA A 1 349 ? 12.702  -21.621 4.138   1.00 40.38  ? 378 ALA A CB  1 
ATOM   2751  N N   . GLN A 1 350 ? 9.664   -20.731 3.595   1.00 43.83  ? 379 GLN A N   1 
ATOM   2752  C CA  . GLN A 1 350 ? 8.511   -20.612 2.712   1.00 39.59  ? 379 GLN A CA  1 
ATOM   2753  C C   . GLN A 1 350 ? 8.229   -19.142 2.426   1.00 42.97  ? 379 GLN A C   1 
ATOM   2754  O O   . GLN A 1 350 ? 7.948   -18.755 1.290   1.00 40.04  ? 379 GLN A O   1 
ATOM   2755  C CB  . GLN A 1 350 ? 7.184   -21.000 3.340   1.00 50.87  ? 379 GLN A CB  1 
ATOM   2756  C CG  . GLN A 1 350 ? 6.982   -22.474 3.649   1.00 56.08  ? 379 GLN A CG  1 
ATOM   2757  C CD  . GLN A 1 350 ? 5.553   -22.696 4.094   1.00 58.97  ? 379 GLN A CD  1 
ATOM   2758  O OE1 . GLN A 1 350 ? 4.607   -22.176 3.483   1.00 56.32  ? 379 GLN A OE1 1 
ATOM   2759  N NE2 . GLN A 1 350 ? 5.392   -23.406 5.199   1.00 60.31  ? 379 GLN A NE2 1 
ATOM   2760  N N   . LEU A 1 351 ? 8.309   -18.313 3.474   1.00 40.83  ? 380 LEU A N   1 
ATOM   2761  C CA  . LEU A 1 351 ? 8.013   -16.899 3.317   1.00 41.03  ? 380 LEU A CA  1 
ATOM   2762  C C   . LEU A 1 351 ? 8.951   -16.240 2.307   1.00 43.27  ? 380 LEU A C   1 
ATOM   2763  O O   . LEU A 1 351 ? 8.528   -15.330 1.588   1.00 42.91  ? 380 LEU A O   1 
ATOM   2764  C CB  . LEU A 1 351 ? 8.044   -16.215 4.678   1.00 40.87  ? 380 LEU A CB  1 
ATOM   2765  C CG  . LEU A 1 351 ? 6.803   -16.484 5.532   1.00 41.45  ? 380 LEU A CG  1 
ATOM   2766  C CD1 . LEU A 1 351 ? 7.107   -16.060 6.947   1.00 40.98  ? 380 LEU A CD1 1 
ATOM   2767  C CD2 . LEU A 1 351 ? 5.565   -15.776 4.968   1.00 40.67  ? 380 LEU A CD2 1 
ATOM   2768  N N   . TYR A 1 352 ? 10.215  -16.697 2.262   1.00 47.46  ? 381 TYR A N   1 
ATOM   2769  C CA  . TYR A 1 352 ? 11.191  -16.166 1.320   1.00 48.96  ? 381 TYR A CA  1 
ATOM   2770  C C   . TYR A 1 352 ? 10.799  -16.513 -0.122  1.00 45.61  ? 381 TYR A C   1 
ATOM   2771  O O   . TYR A 1 352 ? 11.068  -15.739 -1.041  1.00 50.86  ? 381 TYR A O   1 
ATOM   2772  C CB  . TYR A 1 352 ? 12.570  -16.717 1.704   1.00 46.04  ? 381 TYR A CB  1 
ATOM   2773  C CG  . TYR A 1 352 ? 13.700  -16.085 0.910   1.00 43.51  ? 381 TYR A CG  1 
ATOM   2774  C CD1 . TYR A 1 352 ? 13.757  -14.712 0.746   1.00 42.69  ? 381 TYR A CD1 1 
ATOM   2775  C CD2 . TYR A 1 352 ? 14.697  -16.850 0.309   1.00 47.87  ? 381 TYR A CD2 1 
ATOM   2776  C CE1 . TYR A 1 352 ? 14.773  -14.116 0.025   1.00 48.24  ? 381 TYR A CE1 1 
ATOM   2777  C CE2 . TYR A 1 352 ? 15.724  -16.261 -0.415  1.00 47.10  ? 381 TYR A CE2 1 
ATOM   2778  C CZ  . TYR A 1 352 ? 15.748  -14.889 -0.577  1.00 43.57  ? 381 TYR A CZ  1 
ATOM   2779  O OH  . TYR A 1 352 ? 16.722  -14.213 -1.263  1.00 44.79  ? 381 TYR A OH  1 
ATOM   2780  N N   . LYS A 1 353 ? 10.205  -17.704 -0.282  1.00 47.88  ? 382 LYS A N   1 
ATOM   2781  C CA  . LYS A 1 353 ? 9.666   -18.232 -1.535  1.00 53.90  ? 382 LYS A CA  1 
ATOM   2782  C C   . LYS A 1 353 ? 8.497   -17.372 -2.038  1.00 54.44  ? 382 LYS A C   1 
ATOM   2783  O O   . LYS A 1 353 ? 8.427   -17.100 -3.232  1.00 46.38  ? 382 LYS A O   1 
ATOM   2784  C CB  . LYS A 1 353 ? 9.278   -19.694 -1.264  1.00 56.73  ? 382 LYS A CB  1 
ATOM   2785  C CG  . LYS A 1 353 ? 9.543   -20.748 -2.338  1.00 65.57  ? 382 LYS A CG  1 
ATOM   2786  C CD  . LYS A 1 353 ? 8.425   -20.880 -3.365  1.00 74.09  ? 382 LYS A CD  1 
ATOM   2787  C CE  . LYS A 1 353 ? 8.393   -22.186 -4.089  1.00 73.88  ? 382 LYS A CE  1 
ATOM   2788  N NZ  . LYS A 1 353 ? 7.750   -23.235 -3.288  1.00 68.26  ? 382 LYS A NZ  1 
ATOM   2789  N N   . ILE A 1 354 ? 7.643   -16.871 -1.116  1.00 52.76  ? 383 ILE A N   1 
ATOM   2790  C CA  . ILE A 1 354 ? 6.338   -16.292 -1.420  1.00 43.92  ? 383 ILE A CA  1 
ATOM   2791  C C   . ILE A 1 354 ? 6.313   -14.765 -1.312  1.00 48.78  ? 383 ILE A C   1 
ATOM   2792  O O   . ILE A 1 354 ? 6.036   -14.101 -2.300  1.00 50.66  ? 383 ILE A O   1 
ATOM   2793  C CB  . ILE A 1 354 ? 5.302   -16.952 -0.497  1.00 56.20  ? 383 ILE A CB  1 
ATOM   2794  C CG1 . ILE A 1 354 ? 5.036   -18.405 -0.955  1.00 49.39  ? 383 ILE A CG1 1 
ATOM   2795  C CG2 . ILE A 1 354 ? 4.014   -16.123 -0.413  1.00 59.48  ? 383 ILE A CG2 1 
ATOM   2796  C CD1 . ILE A 1 354 ? 4.838   -19.391 0.172   1.00 50.61  ? 383 ILE A CD1 1 
ATOM   2797  N N   . VAL A 1 355 ? 6.657   -14.194 -0.140  1.00 45.00  ? 384 VAL A N   1 
ATOM   2798  C CA  . VAL A 1 355 ? 6.356   -12.801 0.182   1.00 35.87  ? 384 VAL A CA  1 
ATOM   2799  C C   . VAL A 1 355 ? 6.973   -11.829 -0.833  1.00 44.30  ? 384 VAL A C   1 
ATOM   2800  O O   . VAL A 1 355 ? 6.325   -10.853 -1.239  1.00 44.68  ? 384 VAL A O   1 
ATOM   2801  C CB  . VAL A 1 355 ? 6.828   -12.475 1.612   1.00 42.11  ? 384 VAL A CB  1 
ATOM   2802  C CG1 . VAL A 1 355 ? 6.704   -10.987 1.936   1.00 47.20  ? 384 VAL A CG1 1 
ATOM   2803  C CG2 . VAL A 1 355 ? 6.125   -13.334 2.663   1.00 41.13  ? 384 VAL A CG2 1 
ATOM   2804  N N   . PRO A 1 356 ? 8.220   -12.022 -1.325  1.00 43.94  ? 385 PRO A N   1 
ATOM   2805  C CA  . PRO A 1 356 ? 8.836   -10.981 -2.153  1.00 47.72  ? 385 PRO A CA  1 
ATOM   2806  C C   . PRO A 1 356 ? 8.077   -10.666 -3.452  1.00 50.90  ? 385 PRO A C   1 
ATOM   2807  O O   . PRO A 1 356 ? 7.999   -9.507  -3.866  1.00 57.35  ? 385 PRO A O   1 
ATOM   2808  C CB  . PRO A 1 356 ? 10.263  -11.515 -2.378  1.00 44.41  ? 385 PRO A CB  1 
ATOM   2809  C CG  . PRO A 1 356 ? 10.444  -12.542 -1.284  1.00 46.14  ? 385 PRO A CG  1 
ATOM   2810  C CD  . PRO A 1 356 ? 9.083   -13.205 -1.156  1.00 44.24  ? 385 PRO A CD  1 
ATOM   2811  N N   . ASN A 1 357 ? 7.503   -11.701 -4.066  1.00 41.61  ? 386 ASN A N   1 
ATOM   2812  C CA  . ASN A 1 357 ? 6.598   -11.562 -5.200  1.00 60.81  ? 386 ASN A CA  1 
ATOM   2813  C C   . ASN A 1 357 ? 5.313   -10.820 -4.812  1.00 56.46  ? 386 ASN A C   1 
ATOM   2814  O O   . ASN A 1 357 ? 4.923   -9.891  -5.508  1.00 52.29  ? 386 ASN A O   1 
ATOM   2815  C CB  . ASN A 1 357 ? 6.254   -12.907 -5.840  1.00 66.28  ? 386 ASN A CB  1 
ATOM   2816  C CG  . ASN A 1 357 ? 7.362   -13.430 -6.731  1.00 78.29  ? 386 ASN A CG  1 
ATOM   2817  O OD1 . ASN A 1 357 ? 8.066   -12.638 -7.376  1.00 73.37  ? 386 ASN A OD1 1 
ATOM   2818  N ND2 . ASN A 1 357 ? 7.545   -14.748 -6.773  1.00 77.54  ? 386 ASN A ND2 1 
ATOM   2819  N N   . VAL A 1 358 ? 4.651   -11.221 -3.722  1.00 52.33  ? 387 VAL A N   1 
ATOM   2820  C CA  . VAL A 1 358 ? 3.409   -10.572 -3.325  1.00 51.93  ? 387 VAL A CA  1 
ATOM   2821  C C   . VAL A 1 358 ? 3.634   -9.067  -3.223  1.00 62.19  ? 387 VAL A C   1 
ATOM   2822  O O   . VAL A 1 358 ? 2.753   -8.286  -3.589  1.00 63.08  ? 387 VAL A O   1 
ATOM   2823  C CB  . VAL A 1 358 ? 2.832   -11.125 -2.008  1.00 50.14  ? 387 VAL A CB  1 
ATOM   2824  C CG1 . VAL A 1 358 ? 1.733   -10.216 -1.447  1.00 51.43  ? 387 VAL A CG1 1 
ATOM   2825  C CG2 . VAL A 1 358 ? 2.333   -12.563 -2.157  1.00 40.98  ? 387 VAL A CG2 1 
ATOM   2826  N N   . LEU A 1 359 ? 4.813   -8.672  -2.721  1.00 61.91  ? 388 LEU A N   1 
ATOM   2827  C CA  . LEU A 1 359 ? 5.120   -7.273  -2.482  1.00 64.92  ? 388 LEU A CA  1 
ATOM   2828  C C   . LEU A 1 359 ? 5.419   -6.555  -3.797  1.00 71.53  ? 388 LEU A C   1 
ATOM   2829  O O   . LEU A 1 359 ? 5.265   -5.334  -3.869  1.00 74.83  ? 388 LEU A O   1 
ATOM   2830  C CB  . LEU A 1 359 ? 6.260   -7.151  -1.468  1.00 59.14  ? 388 LEU A CB  1 
ATOM   2831  C CG  . LEU A 1 359 ? 5.842   -7.210  0.006   1.00 59.63  ? 388 LEU A CG  1 
ATOM   2832  C CD1 . LEU A 1 359 ? 4.918   -8.387  0.263   1.00 64.33  ? 388 LEU A CD1 1 
ATOM   2833  C CD2 . LEU A 1 359 ? 7.036   -7.296  0.940   1.00 60.37  ? 388 LEU A CD2 1 
ATOM   2834  N N   . LEU A 1 360 ? 5.959   -7.287  -4.761  1.00 79.60  ? 389 LEU A N   1 
ATOM   2835  C CA  . LEU A 1 360 ? 6.352   -6.618  -6.025  1.00 87.21  ? 389 LEU A CA  1 
ATOM   2836  C C   . LEU A 1 360 ? 5.086   -6.449  -6.872  1.00 88.71  ? 389 LEU A C   1 
ATOM   2837  O O   . LEU A 1 360 ? 4.823   -5.317  -7.302  1.00 93.86  ? 389 LEU A O   1 
ATOM   2838  C CB  . LEU A 1 360 ? 7.428   -7.427  -6.739  1.00 81.00  ? 389 LEU A CB  1 
ATOM   2839  C CG  . LEU A 1 360 ? 8.866   -7.197  -6.273  1.00 82.24  ? 389 LEU A CG  1 
ATOM   2840  C CD1 . LEU A 1 360 ? 9.700   -8.435  -6.544  1.00 76.27  ? 389 LEU A CD1 1 
ATOM   2841  C CD2 . LEU A 1 360 ? 9.454   -5.988  -6.973  1.00 87.09  ? 389 LEU A CD2 1 
ATOM   2842  N N   . GLU A 1 361 ? 4.328   -7.526  -7.077  1.00 94.62  ? 390 GLU A N   1 
ATOM   2843  C CA  . GLU A 1 361 ? 3.044   -7.411  -7.811  1.00 100.57 ? 390 GLU A CA  1 
ATOM   2844  C C   . GLU A 1 361 ? 2.286   -6.188  -7.286  1.00 98.74  ? 390 GLU A C   1 
ATOM   2845  O O   . GLU A 1 361 ? 1.912   -5.325  -8.103  1.00 100.59 ? 390 GLU A O   1 
ATOM   2846  C CB  . GLU A 1 361 ? 2.153   -8.639  -7.625  1.00 101.78 ? 390 GLU A CB  1 
ATOM   2847  C CG  . GLU A 1 361 ? 2.850   -9.945  -7.991  1.00 105.32 ? 390 GLU A CG  1 
ATOM   2848  C CD  . GLU A 1 361 ? 1.918   -11.052 -8.446  1.00 102.89 ? 390 GLU A CD  1 
ATOM   2849  O OE1 . GLU A 1 361 ? 2.423   -12.091 -8.919  1.00 92.23  ? 390 GLU A OE1 1 
ATOM   2850  O OE2 . GLU A 1 361 ? 0.688   -10.874 -8.331  1.00 95.51  ? 390 GLU A OE2 1 
ATOM   2851  N N   . GLN A 1 362 ? 2.055   -6.141  -5.980  1.00 91.79  ? 391 GLN A N   1 
ATOM   2852  C CA  . GLN A 1 362 ? 1.297   -5.015  -5.392  1.00 90.92  ? 391 GLN A CA  1 
ATOM   2853  C C   . GLN A 1 362 ? 1.909   -3.713  -5.920  1.00 95.30  ? 391 GLN A C   1 
ATOM   2854  O O   . GLN A 1 362 ? 1.184   -2.982  -6.616  1.00 109.35 ? 391 GLN A O   1 
ATOM   2855  C CB  . GLN A 1 362 ? 1.317   -5.171  -3.874  1.00 100.60 ? 391 GLN A CB  1 
ATOM   2856  N N   . GLY A 1 363 ? 3.168   -3.411  -5.591  1.00 87.37  ? 392 GLY A N   1 
ATOM   2857  C CA  . GLY A 1 363 ? 3.816   -2.241  -6.213  1.00 87.27  ? 392 GLY A CA  1 
ATOM   2858  C C   . GLY A 1 363 ? 4.295   -1.190  -5.239  1.00 92.39  ? 392 GLY A C   1 
ATOM   2859  O O   . GLY A 1 363 ? 5.188   -0.413  -5.616  1.00 96.92  ? 392 GLY A O   1 
ATOM   2860  N N   . LYS A 1 364 ? 3.717   -1.121  -4.047  1.00 102.08 ? 393 LYS A N   1 
ATOM   2861  C CA  . LYS A 1 364 ? 4.092   -0.042  -3.135  1.00 109.07 ? 393 LYS A CA  1 
ATOM   2862  C C   . LYS A 1 364 ? 5.299   -0.447  -2.284  1.00 112.18 ? 393 LYS A C   1 
ATOM   2863  O O   . LYS A 1 364 ? 5.677   0.286   -1.366  1.00 103.93 ? 393 LYS A O   1 
ATOM   2864  C CB  . LYS A 1 364 ? 2.923   0.433   -2.250  1.00 108.76 ? 393 LYS A CB  1 
ATOM   2865  C CG  . LYS A 1 364 ? 1.941   -0.648  -1.781  1.00 115.05 ? 393 LYS A CG  1 
ATOM   2866  C CD  . LYS A 1 364 ? 2.561   -1.818  -1.012  1.00 116.06 ? 393 LYS A CD  1 
ATOM   2867  C CE  . LYS A 1 364 ? 2.040   -3.190  -1.375  1.00 94.84  ? 393 LYS A CE  1 
ATOM   2868  N NZ  . LYS A 1 364 ? 0.654   -3.421  -0.966  1.00 81.74  ? 393 LYS A NZ  1 
ATOM   2869  N N   . ALA A 1 365 ? 5.884   -1.621  -2.581  1.00 109.66 ? 394 ALA A N   1 
ATOM   2870  C CA  . ALA A 1 365 ? 7.060   -2.109  -1.875  1.00 94.15  ? 394 ALA A CA  1 
ATOM   2871  C C   . ALA A 1 365 ? 8.319   -1.486  -2.478  1.00 76.48  ? 394 ALA A C   1 
ATOM   2872  O O   . ALA A 1 365 ? 8.743   -1.867  -3.567  1.00 65.42  ? 394 ALA A O   1 
ATOM   2873  C CB  . ALA A 1 365 ? 7.105   -3.624  -1.933  1.00 87.84  ? 394 ALA A CB  1 
ATOM   2874  N N   . LYS A 1 366 ? 8.908   -0.522  -1.759  1.00 77.33  ? 395 LYS A N   1 
ATOM   2875  C CA  . LYS A 1 366 ? 10.161  0.086   -2.179  1.00 84.14  ? 395 LYS A CA  1 
ATOM   2876  C C   . LYS A 1 366 ? 11.296  -0.926  -1.997  1.00 78.31  ? 395 LYS A C   1 
ATOM   2877  O O   . LYS A 1 366 ? 12.278  -0.895  -2.736  1.00 71.18  ? 395 LYS A O   1 
ATOM   2878  C CB  . LYS A 1 366 ? 10.371  1.417   -1.441  1.00 88.24  ? 395 LYS A CB  1 
ATOM   2879  C CG  . LYS A 1 366 ? 10.962  2.547   -2.282  1.00 93.14  ? 395 LYS A CG  1 
ATOM   2880  C CD  . LYS A 1 366 ? 10.365  2.629   -3.685  1.00 98.63  ? 395 LYS A CD  1 
ATOM   2881  C CE  . LYS A 1 366 ? 10.354  3.989   -4.310  1.00 96.32  ? 395 LYS A CE  1 
ATOM   2882  N NZ  . LYS A 1 366 ? 9.687   3.920   -5.612  1.00 90.59  ? 395 LYS A NZ  1 
ATOM   2883  N N   . ASN A 1 367 ? 11.134  -1.845  -1.030  1.00 79.83  ? 396 ASN A N   1 
ATOM   2884  C CA  . ASN A 1 367 ? 12.031  -2.981  -0.860  1.00 68.49  ? 396 ASN A CA  1 
ATOM   2885  C C   . ASN A 1 367 ? 11.202  -4.224  -0.522  1.00 62.42  ? 396 ASN A C   1 
ATOM   2886  O O   . ASN A 1 367 ? 10.761  -4.384  0.618   1.00 49.53  ? 396 ASN A O   1 
ATOM   2887  C CB  . ASN A 1 367 ? 13.139  -2.648  0.141   1.00 65.64  ? 396 ASN A CB  1 
ATOM   2888  C CG  . ASN A 1 367 ? 13.950  -3.854  0.566   1.00 65.86  ? 396 ASN A CG  1 
ATOM   2889  O OD1 . ASN A 1 367 ? 14.233  -4.014  1.760   1.00 57.07  ? 396 ASN A OD1 1 
ATOM   2890  N ND2 . ASN A 1 367 ? 14.354  -4.694  -0.378  1.00 56.64  ? 396 ASN A ND2 1 
ATOM   2891  N N   . PRO A 1 368 ? 10.990  -5.157  -1.488  1.00 56.32  ? 397 PRO A N   1 
ATOM   2892  C CA  . PRO A 1 368 ? 10.174  -6.354  -1.246  1.00 51.74  ? 397 PRO A CA  1 
ATOM   2893  C C   . PRO A 1 368 ? 10.856  -7.536  -0.564  1.00 48.00  ? 397 PRO A C   1 
ATOM   2894  O O   . PRO A 1 368 ? 10.231  -8.587  -0.368  1.00 45.49  ? 397 PRO A O   1 
ATOM   2895  C CB  . PRO A 1 368 ? 9.797   -6.714  -2.695  1.00 56.83  ? 397 PRO A CB  1 
ATOM   2896  C CG  . PRO A 1 368 ? 11.057  -6.430  -3.462  1.00 60.39  ? 397 PRO A CG  1 
ATOM   2897  C CD  . PRO A 1 368 ? 11.520  -5.100  -2.862  1.00 58.21  ? 397 PRO A CD  1 
ATOM   2898  N N   . TRP A 1 369 ? 12.149  -7.375  -0.251  1.00 45.00  ? 398 TRP A N   1 
ATOM   2899  C CA  . TRP A 1 369 ? 12.971  -8.502  0.169   1.00 44.16  ? 398 TRP A CA  1 
ATOM   2900  C C   . TRP A 1 369 ? 13.142  -8.495  1.681   1.00 37.14  ? 398 TRP A C   1 
ATOM   2901  O O   . TRP A 1 369 ? 12.960  -7.462  2.318   1.00 38.42  ? 398 TRP A O   1 
ATOM   2902  C CB  . TRP A 1 369 ? 14.323  -8.448  -0.560  1.00 48.21  ? 398 TRP A CB  1 
ATOM   2903  C CG  . TRP A 1 369 ? 14.184  -8.633  -2.045  1.00 44.67  ? 398 TRP A CG  1 
ATOM   2904  C CD1 . TRP A 1 369 ? 14.181  -7.659  -2.998  1.00 49.08  ? 398 TRP A CD1 1 
ATOM   2905  C CD2 . TRP A 1 369 ? 13.932  -9.875  -2.732  1.00 40.11  ? 398 TRP A CD2 1 
ATOM   2906  N NE1 . TRP A 1 369 ? 13.979  -8.216  -4.233  1.00 43.74  ? 398 TRP A NE1 1 
ATOM   2907  C CE2 . TRP A 1 369 ? 13.821  -9.567  -4.105  1.00 42.64  ? 398 TRP A CE2 1 
ATOM   2908  C CE3 . TRP A 1 369 ? 13.813  -11.209 -2.323  1.00 46.67  ? 398 TRP A CE3 1 
ATOM   2909  C CZ2 . TRP A 1 369 ? 13.586  -10.540 -5.074  1.00 40.02  ? 398 TRP A CZ2 1 
ATOM   2910  C CZ3 . TRP A 1 369 ? 13.583  -12.172 -3.277  1.00 46.82  ? 398 TRP A CZ3 1 
ATOM   2911  C CH2 . TRP A 1 369 ? 13.461  -11.838 -4.633  1.00 47.87  ? 398 TRP A CH2 1 
ATOM   2912  N N   . PRO A 1 370 ? 13.547  -9.620  2.304   1.00 40.07  ? 399 PRO A N   1 
ATOM   2913  C CA  . PRO A 1 370 ? 13.745  -9.652  3.762   1.00 37.66  ? 399 PRO A CA  1 
ATOM   2914  C C   . PRO A 1 370 ? 15.018  -8.955  4.256   1.00 37.98  ? 399 PRO A C   1 
ATOM   2915  O O   . PRO A 1 370 ? 16.022  -8.819  3.539   1.00 36.16  ? 399 PRO A O   1 
ATOM   2916  C CB  . PRO A 1 370 ? 13.762  -11.142 4.057   1.00 40.59  ? 399 PRO A CB  1 
ATOM   2917  C CG  . PRO A 1 370 ? 14.374  -11.766 2.810   1.00 39.77  ? 399 PRO A CG  1 
ATOM   2918  C CD  . PRO A 1 370 ? 13.828  -10.910 1.650   1.00 37.86  ? 399 PRO A CD  1 
ATOM   2919  N N   . ASN A 1 371 ? 14.947  -8.442  5.490   1.00 34.90  ? 400 ASN A N   1 
ATOM   2920  C CA  . ASN A 1 371 ? 16.134  -7.935  6.142   1.00 33.37  ? 400 ASN A CA  1 
ATOM   2921  C C   . ASN A 1 371 ? 16.517  -8.906  7.251   1.00 38.04  ? 400 ASN A C   1 
ATOM   2922  O O   . ASN A 1 371 ? 15.793  -9.869  7.500   1.00 36.27  ? 400 ASN A O   1 
ATOM   2923  C CB  . ASN A 1 371 ? 15.934  -6.496  6.605   1.00 35.98  ? 400 ASN A CB  1 
ATOM   2924  C CG  . ASN A 1 371 ? 15.044  -6.411  7.810   1.00 35.60  ? 400 ASN A CG  1 
ATOM   2925  O OD1 . ASN A 1 371 ? 15.374  -6.980  8.859   1.00 41.47  ? 400 ASN A OD1 1 
ATOM   2926  N ND2 . ASN A 1 371 ? 13.918  -5.736  7.670   1.00 34.66  ? 400 ASN A ND2 1 
ATOM   2927  N N   . VAL A 1 372 ? 17.637  -8.600  7.930   1.00 40.23  ? 401 VAL A N   1 
ATOM   2928  C CA  . VAL A 1 372 ? 18.264  -9.517  8.870   1.00 36.44  ? 401 VAL A CA  1 
ATOM   2929  C C   . VAL A 1 372 ? 17.244  -10.032 9.874   1.00 34.68  ? 401 VAL A C   1 
ATOM   2930  O O   . VAL A 1 372 ? 17.276  -11.203 10.230  1.00 36.28  ? 401 VAL A O   1 
ATOM   2931  C CB  . VAL A 1 372 ? 19.476  -8.858  9.567   1.00 37.99  ? 401 VAL A CB  1 
ATOM   2932  C CG1 . VAL A 1 372 ? 19.101  -7.652  10.412  1.00 38.44  ? 401 VAL A CG1 1 
ATOM   2933  C CG2 . VAL A 1 372 ? 20.245  -9.854  10.414  1.00 43.27  ? 401 VAL A CG2 1 
ATOM   2934  N N   . ASP A 1 373 ? 16.333  -9.164  10.318  1.00 35.40  ? 402 ASP A N   1 
ATOM   2935  C CA  . ASP A 1 373 ? 15.458  -9.448  11.454  1.00 40.14  ? 402 ASP A CA  1 
ATOM   2936  C C   . ASP A 1 373 ? 14.387  -10.521 11.133  1.00 41.41  ? 402 ASP A C   1 
ATOM   2937  O O   . ASP A 1 373 ? 13.828  -11.168 12.024  1.00 34.51  ? 402 ASP A O   1 
ATOM   2938  C CB  . ASP A 1 373 ? 14.896  -8.139  11.998  1.00 46.33  ? 402 ASP A CB  1 
ATOM   2939  C CG  . ASP A 1 373 ? 15.932  -7.120  12.478  1.00 51.77  ? 402 ASP A CG  1 
ATOM   2940  O OD1 . ASP A 1 373 ? 16.659  -7.409  13.472  1.00 51.68  ? 402 ASP A OD1 1 
ATOM   2941  O OD2 . ASP A 1 373 ? 16.027  -6.042  11.846  1.00 58.78  ? 402 ASP A OD2 1 
ATOM   2942  N N   . ALA A 1 374 ? 14.127  -10.762 9.848   1.00 33.37  ? 403 ALA A N   1 
ATOM   2943  C CA  . ALA A 1 374 ? 13.249  -11.845 9.446   1.00 32.18  ? 403 ALA A CA  1 
ATOM   2944  C C   . ALA A 1 374 ? 13.789  -13.230 9.839   1.00 31.66  ? 403 ALA A C   1 
ATOM   2945  O O   . ALA A 1 374 ? 13.031  -14.188 9.971   1.00 35.38  ? 403 ALA A O   1 
ATOM   2946  C CB  . ALA A 1 374 ? 13.039  -11.718 7.967   1.00 26.68  ? 403 ALA A CB  1 
ATOM   2947  N N   . HIS A 1 375 ? 15.101  -13.372 10.028  1.00 34.74  ? 404 HIS A N   1 
ATOM   2948  C CA  . HIS A 1 375 ? 15.685  -14.695 10.139  1.00 34.48  ? 404 HIS A CA  1 
ATOM   2949  C C   . HIS A 1 375 ? 16.291  -14.982 11.500  1.00 37.63  ? 404 HIS A C   1 
ATOM   2950  O O   . HIS A 1 375 ? 16.548  -16.142 11.803  1.00 40.34  ? 404 HIS A O   1 
ATOM   2951  C CB  . HIS A 1 375 ? 16.797  -14.906 9.112   1.00 34.45  ? 404 HIS A CB  1 
ATOM   2952  C CG  . HIS A 1 375 ? 16.840  -16.316 8.668   1.00 31.59  ? 404 HIS A CG  1 
ATOM   2953  N ND1 . HIS A 1 375 ? 16.802  -16.625 7.329   1.00 32.96  ? 404 HIS A ND1 1 
ATOM   2954  C CD2 . HIS A 1 375 ? 16.804  -17.461 9.326   1.00 27.82  ? 404 HIS A CD2 1 
ATOM   2955  C CE1 . HIS A 1 375 ? 16.796  -17.941 7.197   1.00 29.87  ? 404 HIS A CE1 1 
ATOM   2956  N NE2 . HIS A 1 375 ? 16.771  -18.461 8.392   1.00 31.20  ? 404 HIS A NE2 1 
ATOM   2957  N N   . SER A 1 376 ? 16.531  -13.952 12.319  1.00 39.14  ? 405 SER A N   1 
ATOM   2958  C CA  . SER A 1 376 ? 17.449  -14.125 13.433  1.00 37.34  ? 405 SER A CA  1 
ATOM   2959  C C   . SER A 1 376 ? 16.776  -14.881 14.586  1.00 37.84  ? 405 SER A C   1 
ATOM   2960  O O   . SER A 1 376 ? 17.395  -15.737 15.251  1.00 35.53  ? 405 SER A O   1 
ATOM   2961  C CB  . SER A 1 376 ? 18.051  -12.792 13.857  1.00 42.59  ? 405 SER A CB  1 
ATOM   2962  O OG  . SER A 1 376 ? 17.023  -11.852 14.143  1.00 54.21  ? 405 SER A OG  1 
ATOM   2963  N N   . GLY A 1 377 ? 15.504  -14.564 14.836  1.00 34.17  ? 406 GLY A N   1 
ATOM   2964  C CA  . GLY A 1 377 ? 14.787  -15.128 15.974  1.00 35.79  ? 406 GLY A CA  1 
ATOM   2965  C C   . GLY A 1 377 ? 14.703  -16.653 15.945  1.00 37.44  ? 406 GLY A C   1 
ATOM   2966  O O   . GLY A 1 377 ? 14.882  -17.297 16.976  1.00 45.36  ? 406 GLY A O   1 
ATOM   2967  N N   . VAL A 1 378 ? 14.397  -17.235 14.773  1.00 38.72  ? 407 VAL A N   1 
ATOM   2968  C CA  . VAL A 1 378 ? 14.207  -18.674 14.694  1.00 40.27  ? 407 VAL A CA  1 
ATOM   2969  C C   . VAL A 1 378 ? 15.510  -19.396 15.040  1.00 35.86  ? 407 VAL A C   1 
ATOM   2970  O O   . VAL A 1 378 ? 15.470  -20.439 15.681  1.00 37.12  ? 407 VAL A O   1 
ATOM   2971  C CB  . VAL A 1 378 ? 13.624  -19.133 13.345  1.00 41.94  ? 407 VAL A CB  1 
ATOM   2972  C CG1 . VAL A 1 378 ? 12.213  -18.592 13.174  1.00 45.57  ? 407 VAL A CG1 1 
ATOM   2973  C CG2 . VAL A 1 378 ? 14.513  -18.738 12.172  1.00 44.32  ? 407 VAL A CG2 1 
ATOM   2974  N N   . LEU A 1 379 ? 16.667  -18.847 14.652  1.00 35.66  ? 408 LEU A N   1 
ATOM   2975  C CA  . LEU A 1 379 ? 17.953  -19.442 15.003  1.00 32.65  ? 408 LEU A CA  1 
ATOM   2976  C C   . LEU A 1 379 ? 18.175  -19.434 16.516  1.00 34.29  ? 408 LEU A C   1 
ATOM   2977  O O   . LEU A 1 379 ? 18.496  -20.454 17.123  1.00 32.33  ? 408 LEU A O   1 
ATOM   2978  C CB  . LEU A 1 379 ? 19.046  -18.665 14.287  1.00 36.41  ? 408 LEU A CB  1 
ATOM   2979  C CG  . LEU A 1 379 ? 19.042  -18.795 12.767  1.00 42.50  ? 408 LEU A CG  1 
ATOM   2980  C CD1 . LEU A 1 379 ? 20.013  -17.850 12.091  1.00 46.00  ? 408 LEU A CD1 1 
ATOM   2981  C CD2 . LEU A 1 379 ? 19.387  -20.225 12.443  1.00 47.97  ? 408 LEU A CD2 1 
ATOM   2982  N N   . LEU A 1 380 ? 17.973  -18.275 17.126  1.00 31.17  ? 409 LEU A N   1 
ATOM   2983  C CA  . LEU A 1 380 ? 18.139  -18.134 18.560  1.00 33.97  ? 409 LEU A CA  1 
ATOM   2984  C C   . LEU A 1 380 ? 17.244  -19.110 19.313  1.00 31.75  ? 409 LEU A C   1 
ATOM   2985  O O   . LEU A 1 380 ? 17.731  -19.810 20.186  1.00 36.00  ? 409 LEU A O   1 
ATOM   2986  C CB  . LEU A 1 380 ? 17.808  -16.706 18.971  1.00 32.74  ? 409 LEU A CB  1 
ATOM   2987  C CG  . LEU A 1 380 ? 18.838  -15.636 18.599  1.00 33.71  ? 409 LEU A CG  1 
ATOM   2988  C CD1 . LEU A 1 380 ? 18.243  -14.291 19.031  1.00 30.12  ? 409 LEU A CD1 1 
ATOM   2989  C CD2 . LEU A 1 380 ? 20.218  -15.904 19.168  1.00 31.09  ? 409 LEU A CD2 1 
ATOM   2990  N N   . GLN A 1 381 ? 15.942  -19.093 18.999  1.00 36.65  ? 410 GLN A N   1 
ATOM   2991  C CA  . GLN A 1 381 ? 14.932  -19.902 19.673  1.00 38.92  ? 410 GLN A CA  1 
ATOM   2992  C C   . GLN A 1 381 ? 15.309  -21.384 19.585  1.00 38.17  ? 410 GLN A C   1 
ATOM   2993  O O   . GLN A 1 381 ? 15.240  -22.107 20.573  1.00 36.65  ? 410 GLN A O   1 
ATOM   2994  C CB  . GLN A 1 381 ? 13.589  -19.629 19.001  1.00 42.76  ? 410 GLN A CB  1 
ATOM   2995  C CG  . GLN A 1 381 ? 12.399  -20.259 19.708  1.00 57.62  ? 410 GLN A CG  1 
ATOM   2996  C CD  . GLN A 1 381 ? 11.093  -20.030 18.971  1.00 64.53  ? 410 GLN A CD  1 
ATOM   2997  O OE1 . GLN A 1 381 ? 10.928  -20.403 17.799  1.00 68.47  ? 410 GLN A OE1 1 
ATOM   2998  N NE2 . GLN A 1 381 ? 10.148  -19.408 19.657  1.00 63.03  ? 410 GLN A NE2 1 
ATOM   2999  N N   . TYR A 1 382 ? 15.802  -21.793 18.409  1.00 39.48  ? 411 TYR A N   1 
ATOM   3000  C CA  . TYR A 1 382 ? 16.205  -23.166 18.146  1.00 39.39  ? 411 TYR A CA  1 
ATOM   3001  C C   . TYR A 1 382 ? 17.216  -23.684 19.168  1.00 42.75  ? 411 TYR A C   1 
ATOM   3002  O O   . TYR A 1 382 ? 17.181  -24.874 19.475  1.00 41.42  ? 411 TYR A O   1 
ATOM   3003  C CB  . TYR A 1 382 ? 16.780  -23.296 16.739  1.00 38.76  ? 411 TYR A CB  1 
ATOM   3004  C CG  . TYR A 1 382 ? 17.147  -24.730 16.389  1.00 39.31  ? 411 TYR A CG  1 
ATOM   3005  C CD1 . TYR A 1 382 ? 16.175  -25.658 16.036  1.00 39.84  ? 411 TYR A CD1 1 
ATOM   3006  C CD2 . TYR A 1 382 ? 18.459  -25.155 16.487  1.00 42.00  ? 411 TYR A CD2 1 
ATOM   3007  C CE1 . TYR A 1 382 ? 16.506  -26.972 15.749  1.00 39.04  ? 411 TYR A CE1 1 
ATOM   3008  C CE2 . TYR A 1 382 ? 18.808  -26.460 16.197  1.00 47.76  ? 411 TYR A CE2 1 
ATOM   3009  C CZ  . TYR A 1 382 ? 17.826  -27.370 15.831  1.00 41.12  ? 411 TYR A CZ  1 
ATOM   3010  O OH  . TYR A 1 382 ? 18.247  -28.626 15.539  1.00 44.37  ? 411 TYR A OH  1 
ATOM   3011  N N   . TYR A 1 383 ? 18.103  -22.818 19.695  1.00 42.17  ? 412 TYR A N   1 
ATOM   3012  C CA  . TYR A 1 383 ? 19.147  -23.259 20.626  1.00 40.47  ? 412 TYR A CA  1 
ATOM   3013  C C   . TYR A 1 383 ? 18.737  -23.051 22.088  1.00 37.80  ? 412 TYR A C   1 
ATOM   3014  O O   . TYR A 1 383 ? 19.563  -23.242 22.982  1.00 38.72  ? 412 TYR A O   1 
ATOM   3015  C CB  . TYR A 1 383 ? 20.495  -22.606 20.277  1.00 38.24  ? 412 TYR A CB  1 
ATOM   3016  C CG  . TYR A 1 383 ? 21.063  -23.114 18.952  1.00 41.57  ? 412 TYR A CG  1 
ATOM   3017  C CD1 . TYR A 1 383 ? 21.788  -24.289 18.897  1.00 34.77  ? 412 TYR A CD1 1 
ATOM   3018  C CD2 . TYR A 1 383 ? 20.860  -22.433 17.760  1.00 45.29  ? 412 TYR A CD2 1 
ATOM   3019  C CE1 . TYR A 1 383 ? 22.288  -24.780 17.702  1.00 37.77  ? 412 TYR A CE1 1 
ATOM   3020  C CE2 . TYR A 1 383 ? 21.365  -22.902 16.560  1.00 43.37  ? 412 TYR A CE2 1 
ATOM   3021  C CZ  . TYR A 1 383 ? 22.083  -24.085 16.536  1.00 39.01  ? 412 TYR A CZ  1 
ATOM   3022  O OH  . TYR A 1 383 ? 22.603  -24.590 15.394  1.00 44.65  ? 412 TYR A OH  1 
ATOM   3023  N N   . GLY A 1 384 ? 17.469  -22.709 22.365  1.00 39.67  ? 413 GLY A N   1 
ATOM   3024  C CA  . GLY A 1 384 ? 17.016  -22.609 23.752  1.00 40.15  ? 413 GLY A CA  1 
ATOM   3025  C C   . GLY A 1 384 ? 16.944  -21.174 24.291  1.00 42.86  ? 413 GLY A C   1 
ATOM   3026  O O   . GLY A 1 384 ? 16.500  -20.956 25.424  1.00 42.46  ? 413 GLY A O   1 
ATOM   3027  N N   . MET A 1 385 ? 17.337  -20.198 23.456  1.00 40.14  ? 414 MET A N   1 
ATOM   3028  C CA  . MET A 1 385 ? 17.325  -18.777 23.800  1.00 42.52  ? 414 MET A CA  1 
ATOM   3029  C C   . MET A 1 385 ? 15.993  -18.196 23.333  1.00 42.75  ? 414 MET A C   1 
ATOM   3030  O O   . MET A 1 385 ? 15.876  -17.661 22.233  1.00 39.99  ? 414 MET A O   1 
ATOM   3031  C CB  . MET A 1 385 ? 18.557  -18.123 23.159  1.00 42.98  ? 414 MET A CB  1 
ATOM   3032  C CG  . MET A 1 385 ? 18.506  -16.648 22.872  1.00 48.82  ? 414 MET A CG  1 
ATOM   3033  S SD  . MET A 1 385 ? 19.302  -15.607 24.100  1.00 44.54  ? 414 MET A SD  1 
ATOM   3034  C CE  . MET A 1 385 ? 20.856  -16.296 24.692  1.00 35.88  ? 414 MET A CE  1 
ATOM   3035  N N   . THR A 1 386 ? 14.985  -18.364 24.195  1.00 41.22  ? 415 THR A N   1 
ATOM   3036  C CA  . THR A 1 386 ? 13.580  -18.145 23.875  1.00 40.27  ? 415 THR A CA  1 
ATOM   3037  C C   . THR A 1 386 ? 13.069  -16.871 24.554  1.00 42.95  ? 415 THR A C   1 
ATOM   3038  O O   . THR A 1 386 ? 11.889  -16.535 24.430  1.00 49.34  ? 415 THR A O   1 
ATOM   3039  C CB  . THR A 1 386 ? 12.788  -19.362 24.372  1.00 42.96  ? 415 THR A CB  1 
ATOM   3040  O OG1 . THR A 1 386 ? 13.155  -19.395 25.747  1.00 36.42  ? 415 THR A OG1 1 
ATOM   3041  C CG2 . THR A 1 386 ? 13.194  -20.666 23.701  1.00 43.44  ? 415 THR A CG2 1 
ATOM   3042  N N   . GLU A 1 387 ? 13.948  -16.181 25.295  1.00 39.92  ? 416 GLU A N   1 
ATOM   3043  C CA  . GLU A 1 387 ? 13.560  -14.976 26.019  1.00 40.17  ? 416 GLU A CA  1 
ATOM   3044  C C   . GLU A 1 387 ? 13.718  -13.794 25.067  1.00 38.78  ? 416 GLU A C   1 
ATOM   3045  O O   . GLU A 1 387 ? 14.805  -13.252 24.895  1.00 40.95  ? 416 GLU A O   1 
ATOM   3046  C CB  . GLU A 1 387 ? 14.391  -14.780 27.280  1.00 38.19  ? 416 GLU A CB  1 
ATOM   3047  C CG  . GLU A 1 387 ? 14.373  -15.982 28.223  1.00 38.61  ? 416 GLU A CG  1 
ATOM   3048  C CD  . GLU A 1 387 ? 15.418  -17.072 27.998  1.00 38.25  ? 416 GLU A CD  1 
ATOM   3049  O OE1 . GLU A 1 387 ? 16.158  -17.100 26.986  1.00 37.84  ? 416 GLU A OE1 1 
ATOM   3050  O OE2 . GLU A 1 387 ? 15.484  -17.938 28.895  1.00 44.14  ? 416 GLU A OE2 1 
ATOM   3051  N N   . MET A 1 388 ? 12.620  -13.436 24.419  1.00 35.41  ? 417 MET A N   1 
ATOM   3052  C CA  . MET A 1 388 ? 12.660  -12.587 23.242  1.00 39.98  ? 417 MET A CA  1 
ATOM   3053  C C   . MET A 1 388 ? 12.963  -11.137 23.593  1.00 33.61  ? 417 MET A C   1 
ATOM   3054  O O   . MET A 1 388 ? 13.412  -10.386 22.736  1.00 37.26  ? 417 MET A O   1 
ATOM   3055  C CB  . MET A 1 388 ? 11.317  -12.640 22.517  1.00 42.73  ? 417 MET A CB  1 
ATOM   3056  C CG  . MET A 1 388 ? 10.942  -14.034 22.039  1.00 46.13  ? 417 MET A CG  1 
ATOM   3057  S SD  . MET A 1 388 ? 9.515   -13.899 20.945  1.00 53.05  ? 417 MET A SD  1 
ATOM   3058  C CE  . MET A 1 388 ? 8.370   -13.337 22.215  1.00 54.80  ? 417 MET A CE  1 
ATOM   3059  N N   . ASN A 1 389 ? 12.673  -10.736 24.830  1.00 32.81  ? 418 ASN A N   1 
ATOM   3060  C CA  . ASN A 1 389 ? 13.013  -9.408  25.298  1.00 39.74  ? 418 ASN A CA  1 
ATOM   3061  C C   . ASN A 1 389 ? 14.531  -9.224  25.215  1.00 35.73  ? 418 ASN A C   1 
ATOM   3062  O O   . ASN A 1 389 ? 15.008  -8.107  25.043  1.00 35.03  ? 418 ASN A O   1 
ATOM   3063  C CB  . ASN A 1 389 ? 12.421  -9.146  26.681  1.00 38.61  ? 418 ASN A CB  1 
ATOM   3064  C CG  . ASN A 1 389 ? 10.967  -8.726  26.643  1.00 46.97  ? 418 ASN A CG  1 
ATOM   3065  O OD1 . ASN A 1 389 ? 10.390  -8.521  25.571  1.00 47.79  ? 418 ASN A OD1 1 
ATOM   3066  N ND2 . ASN A 1 389 ? 10.351  -8.568  27.804  1.00 51.42  ? 418 ASN A ND2 1 
ATOM   3067  N N   . TYR A 1 390 ? 15.292  -10.326 25.274  1.00 31.33  ? 419 TYR A N   1 
ATOM   3068  C CA  . TYR A 1 390 ? 16.726  -10.211 25.460  1.00 30.53  ? 419 TYR A CA  1 
ATOM   3069  C C   . TYR A 1 390 ? 17.426  -10.053 24.108  1.00 29.08  ? 419 TYR A C   1 
ATOM   3070  O O   . TYR A 1 390 ? 18.588  -9.693  24.066  1.00 24.98  ? 419 TYR A O   1 
ATOM   3071  C CB  . TYR A 1 390 ? 17.171  -11.398 26.321  1.00 30.18  ? 419 TYR A CB  1 
ATOM   3072  C CG  . TYR A 1 390 ? 18.660  -11.379 26.602  1.00 29.36  ? 419 TYR A CG  1 
ATOM   3073  C CD1 . TYR A 1 390 ? 19.181  -10.640 27.644  1.00 27.45  ? 419 TYR A CD1 1 
ATOM   3074  C CD2 . TYR A 1 390 ? 19.550  -12.078 25.792  1.00 30.81  ? 419 TYR A CD2 1 
ATOM   3075  C CE1 . TYR A 1 390 ? 20.534  -10.627 27.906  1.00 31.70  ? 419 TYR A CE1 1 
ATOM   3076  C CE2 . TYR A 1 390 ? 20.919  -12.031 26.012  1.00 24.92  ? 419 TYR A CE2 1 
ATOM   3077  C CZ  . TYR A 1 390 ? 21.404  -11.328 27.085  1.00 27.85  ? 419 TYR A CZ  1 
ATOM   3078  O OH  . TYR A 1 390 ? 22.748  -11.310 27.297  1.00 26.99  ? 419 TYR A OH  1 
ATOM   3079  N N   . TYR A 1 391 ? 16.719  -10.288 23.002  1.00 29.68  ? 420 TYR A N   1 
ATOM   3080  C CA  . TYR A 1 391 ? 17.370  -10.412 21.708  1.00 34.81  ? 420 TYR A CA  1 
ATOM   3081  C C   . TYR A 1 391 ? 18.119  -9.128  21.346  1.00 30.32  ? 420 TYR A C   1 
ATOM   3082  O O   . TYR A 1 391 ? 19.196  -9.154  20.732  1.00 28.47  ? 420 TYR A O   1 
ATOM   3083  C CB  . TYR A 1 391 ? 16.327  -10.779 20.638  1.00 34.23  ? 420 TYR A CB  1 
ATOM   3084  C CG  . TYR A 1 391 ? 15.763  -12.200 20.709  1.00 38.52  ? 420 TYR A CG  1 
ATOM   3085  C CD1 . TYR A 1 391 ? 16.206  -13.134 21.645  1.00 38.28  ? 420 TYR A CD1 1 
ATOM   3086  C CD2 . TYR A 1 391 ? 14.806  -12.621 19.793  1.00 36.37  ? 420 TYR A CD2 1 
ATOM   3087  C CE1 . TYR A 1 391 ? 15.677  -14.412 21.706  1.00 42.59  ? 420 TYR A CE1 1 
ATOM   3088  C CE2 . TYR A 1 391 ? 14.292  -13.900 19.828  1.00 37.07  ? 420 TYR A CE2 1 
ATOM   3089  C CZ  . TYR A 1 391 ? 14.704  -14.796 20.797  1.00 42.64  ? 420 TYR A CZ  1 
ATOM   3090  O OH  . TYR A 1 391 ? 14.187  -16.065 20.793  1.00 41.35  ? 420 TYR A OH  1 
ATOM   3091  N N   . THR A 1 392 ? 17.537  -7.989  21.709  1.00 27.18  ? 421 THR A N   1 
ATOM   3092  C CA  . THR A 1 392 ? 18.166  -6.725  21.356  1.00 30.54  ? 421 THR A CA  1 
ATOM   3093  C C   . THR A 1 392 ? 19.485  -6.540  22.115  1.00 26.76  ? 421 THR A C   1 
ATOM   3094  O O   . THR A 1 392 ? 20.382  -5.839  21.644  1.00 26.15  ? 421 THR A O   1 
ATOM   3095  C CB  . THR A 1 392 ? 17.162  -5.596  21.584  1.00 30.54  ? 421 THR A CB  1 
ATOM   3096  O OG1 . THR A 1 392 ? 16.114  -5.984  20.709  1.00 33.46  ? 421 THR A OG1 1 
ATOM   3097  C CG2 . THR A 1 392 ? 17.644  -4.254  21.059  1.00 40.55  ? 421 THR A CG2 1 
ATOM   3098  N N   . VAL A 1 393 ? 19.637  -7.201  23.265  1.00 26.33  ? 422 VAL A N   1 
ATOM   3099  C CA  . VAL A 1 393 ? 20.885  -7.140  24.007  1.00 27.32  ? 422 VAL A CA  1 
ATOM   3100  C C   . VAL A 1 393 ? 21.998  -7.769  23.180  1.00 26.84  ? 422 VAL A C   1 
ATOM   3101  O O   . VAL A 1 393 ? 23.077  -7.179  23.060  1.00 30.58  ? 422 VAL A O   1 
ATOM   3102  C CB  . VAL A 1 393 ? 20.840  -7.731  25.428  1.00 32.07  ? 422 VAL A CB  1 
ATOM   3103  C CG1 . VAL A 1 393 ? 22.225  -7.797  26.042  1.00 31.35  ? 422 VAL A CG1 1 
ATOM   3104  C CG2 . VAL A 1 393 ? 19.915  -6.913  26.333  1.00 30.67  ? 422 VAL A CG2 1 
ATOM   3105  N N   . LEU A 1 394 ? 21.735  -8.907  22.547  1.00 27.02  ? 423 LEU A N   1 
ATOM   3106  C CA  . LEU A 1 394 ? 22.726  -9.473  21.624  1.00 27.76  ? 423 LEU A CA  1 
ATOM   3107  C C   . LEU A 1 394 ? 23.046  -8.499  20.490  1.00 26.80  ? 423 LEU A C   1 
ATOM   3108  O O   . LEU A 1 394 ? 24.205  -8.321  20.148  1.00 25.44  ? 423 LEU A O   1 
ATOM   3109  C CB  . LEU A 1 394 ? 22.245  -10.803 21.066  1.00 27.73  ? 423 LEU A CB  1 
ATOM   3110  C CG  . LEU A 1 394 ? 21.897  -11.843 22.133  1.00 30.50  ? 423 LEU A CG  1 
ATOM   3111  C CD1 . LEU A 1 394 ? 21.251  -13.024 21.439  1.00 34.10  ? 423 LEU A CD1 1 
ATOM   3112  C CD2 . LEU A 1 394 ? 23.145  -12.249 22.918  1.00 32.46  ? 423 LEU A CD2 1 
ATOM   3113  N N   . PHE A 1 395 ? 22.047  -7.845  19.907  1.00 29.91  ? 424 PHE A N   1 
ATOM   3114  C CA  . PHE A 1 395 ? 22.320  -6.916  18.816  1.00 28.69  ? 424 PHE A CA  1 
ATOM   3115  C C   . PHE A 1 395 ? 23.248  -5.818  19.323  1.00 31.26  ? 424 PHE A C   1 
ATOM   3116  O O   . PHE A 1 395 ? 24.272  -5.509  18.714  1.00 28.29  ? 424 PHE A O   1 
ATOM   3117  C CB  . PHE A 1 395 ? 20.951  -6.466  18.319  1.00 28.82  ? 424 PHE A CB  1 
ATOM   3118  C CG  . PHE A 1 395 ? 20.834  -5.635  17.057  1.00 31.17  ? 424 PHE A CG  1 
ATOM   3119  C CD1 . PHE A 1 395 ? 21.915  -5.004  16.481  1.00 28.64  ? 424 PHE A CD1 1 
ATOM   3120  C CD2 . PHE A 1 395 ? 19.586  -5.497  16.441  1.00 39.02  ? 424 PHE A CD2 1 
ATOM   3121  C CE1 . PHE A 1 395 ? 21.763  -4.263  15.307  1.00 33.35  ? 424 PHE A CE1 1 
ATOM   3122  C CE2 . PHE A 1 395 ? 19.427  -4.746  15.277  1.00 37.16  ? 424 PHE A CE2 1 
ATOM   3123  C CZ  . PHE A 1 395 ? 20.522  -4.108  14.716  1.00 33.21  ? 424 PHE A CZ  1 
ATOM   3124  N N   . GLY A 1 396 ? 22.892  -5.271  20.487  1.00 29.24  ? 425 GLY A N   1 
ATOM   3125  C CA  . GLY A 1 396 ? 23.671  -4.259  21.160  1.00 29.22  ? 425 GLY A CA  1 
ATOM   3126  C C   . GLY A 1 396 ? 25.129  -4.664  21.324  1.00 29.90  ? 425 GLY A C   1 
ATOM   3127  O O   . GLY A 1 396 ? 26.016  -3.882  21.028  1.00 30.02  ? 425 GLY A O   1 
ATOM   3128  N N   . VAL A 1 397 ? 25.379  -5.870  21.824  1.00 27.46  ? 426 VAL A N   1 
ATOM   3129  C CA  . VAL A 1 397 ? 26.736  -6.311  22.059  1.00 27.28  ? 426 VAL A CA  1 
ATOM   3130  C C   . VAL A 1 397 ? 27.512  -6.318  20.752  1.00 28.13  ? 426 VAL A C   1 
ATOM   3131  O O   . VAL A 1 397 ? 28.704  -6.013  20.734  1.00 27.60  ? 426 VAL A O   1 
ATOM   3132  C CB  . VAL A 1 397 ? 26.773  -7.670  22.769  1.00 27.01  ? 426 VAL A CB  1 
ATOM   3133  C CG1 . VAL A 1 397 ? 28.180  -8.236  22.823  1.00 29.82  ? 426 VAL A CG1 1 
ATOM   3134  C CG2 . VAL A 1 397 ? 26.204  -7.516  24.185  1.00 29.37  ? 426 VAL A CG2 1 
ATOM   3135  N N   . SER A 1 398 ? 26.822  -6.706  19.683  1.00 27.56  ? 427 SER A N   1 
ATOM   3136  C CA  . SER A 1 398 ? 27.410  -6.790  18.370  1.00 27.46  ? 427 SER A CA  1 
ATOM   3137  C C   . SER A 1 398 ? 27.727  -5.397  17.842  1.00 26.70  ? 427 SER A C   1 
ATOM   3138  O O   . SER A 1 398 ? 28.806  -5.178  17.283  1.00 26.29  ? 427 SER A O   1 
ATOM   3139  C CB  . SER A 1 398 ? 26.495  -7.509  17.431  1.00 28.49  ? 427 SER A CB  1 
ATOM   3140  O OG  . SER A 1 398 ? 27.025  -7.448  16.126  1.00 29.14  ? 427 SER A OG  1 
ATOM   3141  N N   . ARG A 1 399 ? 26.742  -4.498  17.979  1.00 26.75  ? 428 ARG A N   1 
ATOM   3142  C CA  . ARG A 1 399 ? 26.824  -3.164  17.401  1.00 27.96  ? 428 ARG A CA  1 
ATOM   3143  C C   . ARG A 1 399 ? 27.956  -2.363  18.052  1.00 23.84  ? 428 ARG A C   1 
ATOM   3144  O O   . ARG A 1 399 ? 28.485  -1.458  17.437  1.00 23.38  ? 428 ARG A O   1 
ATOM   3145  C CB  . ARG A 1 399 ? 25.418  -2.556  17.450  1.00 24.95  ? 428 ARG A CB  1 
ATOM   3146  C CG  . ARG A 1 399 ? 25.281  -1.200  16.794  1.00 25.77  ? 428 ARG A CG  1 
ATOM   3147  C CD  . ARG A 1 399 ? 25.842  -1.173  15.371  1.00 24.90  ? 428 ARG A CD  1 
ATOM   3148  N NE  . ARG A 1 399 ? 25.285  -2.117  14.414  1.00 25.10  ? 428 ARG A NE  1 
ATOM   3149  C CZ  . ARG A 1 399 ? 24.159  -1.997  13.703  1.00 26.66  ? 428 ARG A CZ  1 
ATOM   3150  N NH1 . ARG A 1 399 ? 23.347  -0.945  13.838  1.00 27.58  ? 428 ARG A NH1 1 
ATOM   3151  N NH2 . ARG A 1 399 ? 23.883  -2.941  12.830  1.00 24.20  ? 428 ARG A NH2 1 
ATOM   3152  N N   . ALA A 1 400 ? 28.345  -2.717  19.273  1.00 24.27  ? 429 ALA A N   1 
ATOM   3153  C CA  . ALA A 1 400 ? 29.445  -2.074  19.982  1.00 26.09  ? 429 ALA A CA  1 
ATOM   3154  C C   . ALA A 1 400 ? 30.699  -2.057  19.115  1.00 25.82  ? 429 ALA A C   1 
ATOM   3155  O O   . ALA A 1 400 ? 31.406  -1.077  19.140  1.00 29.34  ? 429 ALA A O   1 
ATOM   3156  C CB  . ALA A 1 400 ? 29.718  -2.782  21.282  1.00 25.07  ? 429 ALA A CB  1 
ATOM   3157  N N   . LEU A 1 401 ? 30.910  -3.091  18.282  1.00 29.06  ? 430 LEU A N   1 
ATOM   3158  C CA  . LEU A 1 401 ? 32.153  -3.263  17.549  1.00 25.57  ? 430 LEU A CA  1 
ATOM   3159  C C   . LEU A 1 401 ? 32.237  -2.224  16.432  1.00 27.11  ? 430 LEU A C   1 
ATOM   3160  O O   . LEU A 1 401 ? 33.280  -1.591  16.259  1.00 23.91  ? 430 LEU A O   1 
ATOM   3161  C CB  . LEU A 1 401 ? 32.240  -4.690  17.003  1.00 27.22  ? 430 LEU A CB  1 
ATOM   3162  C CG  . LEU A 1 401 ? 32.236  -5.820  18.043  1.00 28.24  ? 430 LEU A CG  1 
ATOM   3163  C CD1 . LEU A 1 401 ? 32.102  -7.141  17.338  1.00 29.81  ? 430 LEU A CD1 1 
ATOM   3164  C CD2 . LEU A 1 401 ? 33.489  -5.855  18.913  1.00 29.75  ? 430 LEU A CD2 1 
ATOM   3165  N N   . GLY A 1 402 ? 31.127  -2.038  15.707  1.00 21.96  ? 431 GLY A N   1 
ATOM   3166  C CA  . GLY A 1 402 ? 31.099  -1.088  14.620  1.00 23.60  ? 431 GLY A CA  1 
ATOM   3167  C C   . GLY A 1 402 ? 31.182  0.362   15.093  1.00 23.63  ? 431 GLY A C   1 
ATOM   3168  O O   . GLY A 1 402 ? 31.957  1.180   14.560  1.00 23.19  ? 431 GLY A O   1 
ATOM   3169  N N   . VAL A 1 403 ? 30.339  0.697   16.062  1.00 20.77  ? 432 VAL A N   1 
ATOM   3170  C CA  . VAL A 1 403 ? 30.254  2.087   16.479  1.00 22.94  ? 432 VAL A CA  1 
ATOM   3171  C C   . VAL A 1 403 ? 31.513  2.476   17.240  1.00 20.33  ? 432 VAL A C   1 
ATOM   3172  O O   . VAL A 1 403 ? 31.991  3.563   17.036  1.00 20.18  ? 432 VAL A O   1 
ATOM   3173  C CB  . VAL A 1 403 ? 28.974  2.396   17.269  1.00 24.69  ? 432 VAL A CB  1 
ATOM   3174  C CG1 . VAL A 1 403 ? 27.730  1.988   16.486  1.00 29.17  ? 432 VAL A CG1 1 
ATOM   3175  C CG2 . VAL A 1 403 ? 28.950  1.719   18.635  1.00 26.37  ? 432 VAL A CG2 1 
ATOM   3176  N N   . LEU A 1 404 ? 32.099  1.589   18.060  1.00 21.10  ? 433 LEU A N   1 
ATOM   3177  C CA  . LEU A 1 404 ? 33.312  1.920   18.781  1.00 21.91  ? 433 LEU A CA  1 
ATOM   3178  C C   . LEU A 1 404 ? 34.494  1.990   17.811  1.00 23.24  ? 433 LEU A C   1 
ATOM   3179  O O   . LEU A 1 404 ? 35.340  2.870   17.954  1.00 25.83  ? 433 LEU A O   1 
ATOM   3180  C CB  . LEU A 1 404 ? 33.564  0.991   19.968  1.00 25.15  ? 433 LEU A CB  1 
ATOM   3181  C CG  . LEU A 1 404 ? 32.444  0.954   21.009  1.00 28.14  ? 433 LEU A CG  1 
ATOM   3182  C CD1 . LEU A 1 404 ? 32.748  -0.018  22.127  1.00 32.58  ? 433 LEU A CD1 1 
ATOM   3183  C CD2 . LEU A 1 404 ? 32.155  2.283   21.600  1.00 29.72  ? 433 LEU A CD2 1 
ATOM   3184  N N   . ALA A 1 405 ? 34.499  1.164   16.765  1.00 23.90  ? 434 ALA A N   1 
ATOM   3185  C CA  . ALA A 1 405 ? 35.569  1.217   15.797  1.00 25.59  ? 434 ALA A CA  1 
ATOM   3186  C C   . ALA A 1 405 ? 35.530  2.557   15.065  1.00 25.41  ? 434 ALA A C   1 
ATOM   3187  O O   . ALA A 1 405 ? 36.595  3.170   14.902  1.00 26.11  ? 434 ALA A O   1 
ATOM   3188  C CB  . ALA A 1 405 ? 35.468  0.051   14.849  1.00 30.97  ? 434 ALA A CB  1 
ATOM   3189  N N   . GLN A 1 406 ? 34.325  3.024   14.696  1.00 22.95  ? 435 GLN A N   1 
ATOM   3190  C CA  . GLN A 1 406 ? 34.173  4.317   14.038  1.00 27.56  ? 435 GLN A CA  1 
ATOM   3191  C C   . GLN A 1 406 ? 34.485  5.449   15.028  1.00 27.82  ? 435 GLN A C   1 
ATOM   3192  O O   . GLN A 1 406 ? 34.998  6.510   14.674  1.00 28.03  ? 435 GLN A O   1 
ATOM   3193  C CB  . GLN A 1 406 ? 32.760  4.529   13.503  1.00 24.54  ? 435 GLN A CB  1 
ATOM   3194  C CG  . GLN A 1 406 ? 32.504  5.927   12.964  1.00 27.98  ? 435 GLN A CG  1 
ATOM   3195  C CD  . GLN A 1 406 ? 33.449  6.285   11.835  1.00 32.12  ? 435 GLN A CD  1 
ATOM   3196  O OE1 . GLN A 1 406 ? 33.706  5.480   10.934  1.00 38.56  ? 435 GLN A OE1 1 
ATOM   3197  N NE2 . GLN A 1 406 ? 34.091  7.433   11.929  1.00 35.18  ? 435 GLN A NE2 1 
ATOM   3198  N N   . LEU A 1 407 ? 34.105  5.282   16.290  1.00 26.98  ? 436 LEU A N   1 
ATOM   3199  C CA  . LEU A 1 407 ? 34.365  6.344   17.258  1.00 24.52  ? 436 LEU A CA  1 
ATOM   3200  C C   . LEU A 1 407 ? 35.879  6.598   17.413  1.00 21.97  ? 436 LEU A C   1 
ATOM   3201  O O   . LEU A 1 407 ? 36.319  7.732   17.573  1.00 25.51  ? 436 LEU A O   1 
ATOM   3202  C CB  . LEU A 1 407 ? 33.716  5.977   18.580  1.00 24.84  ? 436 LEU A CB  1 
ATOM   3203  C CG  . LEU A 1 407 ? 33.695  7.096   19.610  1.00 27.97  ? 436 LEU A CG  1 
ATOM   3204  C CD1 . LEU A 1 407 ? 32.896  8.266   19.049  1.00 26.13  ? 436 LEU A CD1 1 
ATOM   3205  C CD2 . LEU A 1 407 ? 33.081  6.541   20.905  1.00 28.33  ? 436 LEU A CD2 1 
ATOM   3206  N N   . ILE A 1 408 ? 36.713  5.578   17.315  1.00 23.62  ? 437 ILE A N   1 
ATOM   3207  C CA  . ILE A 1 408 ? 38.157  5.755   17.399  1.00 24.07  ? 437 ILE A CA  1 
ATOM   3208  C C   . ILE A 1 408 ? 38.663  6.648   16.254  1.00 23.79  ? 437 ILE A C   1 
ATOM   3209  O O   . ILE A 1 408 ? 39.319  7.657   16.510  1.00 23.85  ? 437 ILE A O   1 
ATOM   3210  C CB  . ILE A 1 408 ? 38.833  4.378   17.474  1.00 26.37  ? 437 ILE A CB  1 
ATOM   3211  C CG1 . ILE A 1 408 ? 38.479  3.720   18.788  1.00 26.30  ? 437 ILE A CG1 1 
ATOM   3212  C CG2 . ILE A 1 408 ? 40.347  4.466   17.276  1.00 27.19  ? 437 ILE A CG2 1 
ATOM   3213  C CD1 . ILE A 1 408 ? 38.763  2.229   18.832  1.00 29.98  ? 437 ILE A CD1 1 
ATOM   3214  N N   . TRP A 1 409 ? 38.176  6.382   15.053  1.00 21.89  ? 438 TRP A N   1 
ATOM   3215  C CA  . TRP A 1 409 ? 38.441  7.144   13.832  1.00 24.28  ? 438 TRP A CA  1 
ATOM   3216  C C   . TRP A 1 409 ? 37.847  8.557   13.815  1.00 25.16  ? 438 TRP A C   1 
ATOM   3217  O O   . TRP A 1 409 ? 38.494  9.478   13.304  1.00 21.88  ? 438 TRP A O   1 
ATOM   3218  C CB  . TRP A 1 409 ? 37.944  6.298   12.648  1.00 24.47  ? 438 TRP A CB  1 
ATOM   3219  C CG  . TRP A 1 409 ? 38.969  5.247   12.299  1.00 26.40  ? 438 TRP A CG  1 
ATOM   3220  C CD1 . TRP A 1 409 ? 38.990  3.912   12.584  1.00 28.63  ? 438 TRP A CD1 1 
ATOM   3221  C CD2 . TRP A 1 409 ? 40.218  5.534   11.635  1.00 26.89  ? 438 TRP A CD2 1 
ATOM   3222  N NE1 . TRP A 1 409 ? 40.156  3.345   12.118  1.00 27.52  ? 438 TRP A NE1 1 
ATOM   3223  C CE2 . TRP A 1 409 ? 40.927  4.323   11.537  1.00 24.56  ? 438 TRP A CE2 1 
ATOM   3224  C CE3 . TRP A 1 409 ? 40.795  6.704   11.121  1.00 26.40  ? 438 TRP A CE3 1 
ATOM   3225  C CZ2 . TRP A 1 409 ? 42.191  4.267   10.956  1.00 26.45  ? 438 TRP A CZ2 1 
ATOM   3226  C CZ3 . TRP A 1 409 ? 42.031  6.634   10.511  1.00 29.17  ? 438 TRP A CZ3 1 
ATOM   3227  C CH2 . TRP A 1 409 ? 42.711  5.428   10.420  1.00 29.98  ? 438 TRP A CH2 1 
ATOM   3228  N N   . SER A 1 410 ? 36.623  8.739   14.347  1.00 20.48  ? 439 SER A N   1 
ATOM   3229  C CA  . SER A 1 410 ? 36.019  10.062  14.495  1.00 22.07  ? 439 SER A CA  1 
ATOM   3230  C C   . SER A 1 410 ? 36.867  11.016  15.350  1.00 23.40  ? 439 SER A C   1 
ATOM   3231  O O   . SER A 1 410 ? 37.142  12.142  14.939  1.00 24.06  ? 439 SER A O   1 
ATOM   3232  C CB  . SER A 1 410 ? 34.562  9.984   14.985  1.00 21.37  ? 439 SER A CB  1 
ATOM   3233  O OG  . SER A 1 410 ? 33.788  9.230   14.057  1.00 22.12  ? 439 SER A OG  1 
ATOM   3234  N N   . ARG A 1 411 ? 37.434  10.534  16.447  1.00 27.37  ? 440 ARG A N   1 
ATOM   3235  C CA  . ARG A 1 411 ? 38.410  11.279  17.243  1.00 25.92  ? 440 ARG A CA  1 
ATOM   3236  C C   . ARG A 1 411 ? 39.776  11.362  16.560  1.00 27.36  ? 440 ARG A C   1 
ATOM   3237  O O   . ARG A 1 411 ? 40.401  12.431  16.543  1.00 30.10  ? 440 ARG A O   1 
ATOM   3238  C CB  . ARG A 1 411 ? 38.470  10.666  18.640  1.00 29.47  ? 440 ARG A CB  1 
ATOM   3239  C CG  . ARG A 1 411 ? 37.118  10.873  19.313  1.00 33.95  ? 440 ARG A CG  1 
ATOM   3240  C CD  . ARG A 1 411 ? 36.354  12.228  19.098  1.00 38.38  ? 440 ARG A CD  1 
ATOM   3241  N NE  . ARG A 1 411 ? 35.059  11.870  19.682  1.00 58.91  ? 440 ARG A NE  1 
ATOM   3242  C CZ  . ARG A 1 411 ? 34.946  11.565  21.002  1.00 61.27  ? 440 ARG A CZ  1 
ATOM   3243  N NH1 . ARG A 1 411 ? 35.829  12.044  21.871  1.00 69.05  ? 440 ARG A NH1 1 
ATOM   3244  N NH2 . ARG A 1 411 ? 33.916  10.883  21.488  1.00 41.41  ? 440 ARG A NH2 1 
ATOM   3245  N N   . ALA A 1 412 ? 40.212  10.279  15.912  1.00 23.34  ? 441 ALA A N   1 
ATOM   3246  C CA  . ALA A 1 412 ? 41.523  10.271  15.310  1.00 26.18  ? 441 ALA A CA  1 
ATOM   3247  C C   . ALA A 1 412 ? 41.574  11.340  14.214  1.00 25.96  ? 441 ALA A C   1 
ATOM   3248  O O   . ALA A 1 412 ? 42.569  12.010  14.083  1.00 28.10  ? 441 ALA A O   1 
ATOM   3249  C CB  . ALA A 1 412 ? 41.843  8.872   14.776  1.00 27.89  ? 441 ALA A CB  1 
ATOM   3250  N N   . LEU A 1 413 ? 40.464  11.524  13.463  1.00 28.51  ? 442 LEU A N   1 
ATOM   3251  C CA  . LEU A 1 413 ? 40.379  12.467  12.361  1.00 25.08  ? 442 LEU A CA  1 
ATOM   3252  C C   . LEU A 1 413 ? 39.818  13.826  12.742  1.00 30.49  ? 442 LEU A C   1 
ATOM   3253  O O   . LEU A 1 413 ? 39.714  14.687  11.870  1.00 35.43  ? 442 LEU A O   1 
ATOM   3254  C CB  . LEU A 1 413 ? 39.503  11.809  11.314  1.00 27.03  ? 442 LEU A CB  1 
ATOM   3255  C CG  . LEU A 1 413 ? 40.056  10.498  10.747  1.00 27.53  ? 442 LEU A CG  1 
ATOM   3256  C CD1 . LEU A 1 413 ? 39.003  9.888   9.818   1.00 27.10  ? 442 LEU A CD1 1 
ATOM   3257  C CD2 . LEU A 1 413 ? 41.377  10.721  10.022  1.00 28.53  ? 442 LEU A CD2 1 
ATOM   3258  N N   . GLY A 1 414 ? 39.422  14.006  14.006  1.00 31.02  ? 443 GLY A N   1 
ATOM   3259  C CA  . GLY A 1 414 ? 39.012  15.300  14.528  1.00 32.63  ? 443 GLY A CA  1 
ATOM   3260  C C   . GLY A 1 414 ? 37.687  15.806  13.950  1.00 30.61  ? 443 GLY A C   1 
ATOM   3261  O O   . GLY A 1 414 ? 37.487  17.011  13.867  1.00 30.92  ? 443 GLY A O   1 
ATOM   3262  N N   . PHE A 1 415 ? 36.751  14.886  13.680  1.00 29.27  ? 444 PHE A N   1 
ATOM   3263  C CA  . PHE A 1 415 ? 35.385  15.208  13.322  1.00 28.70  ? 444 PHE A CA  1 
ATOM   3264  C C   . PHE A 1 415 ? 34.830  16.152  14.394  1.00 30.71  ? 444 PHE A C   1 
ATOM   3265  O O   . PHE A 1 415 ? 34.973  15.907  15.580  1.00 21.97  ? 444 PHE A O   1 
ATOM   3266  C CB  . PHE A 1 415 ? 34.567  13.922  13.146  1.00 32.96  ? 444 PHE A CB  1 
ATOM   3267  C CG  . PHE A 1 415 ? 34.844  13.049  11.911  1.00 30.41  ? 444 PHE A CG  1 
ATOM   3268  C CD1 . PHE A 1 415 ? 35.840  13.367  10.994  1.00 32.75  ? 444 PHE A CD1 1 
ATOM   3269  C CD2 . PHE A 1 415 ? 34.165  11.850  11.739  1.00 33.32  ? 444 PHE A CD2 1 
ATOM   3270  C CE1 . PHE A 1 415 ? 36.086  12.544  9.906   1.00 33.31  ? 444 PHE A CE1 1 
ATOM   3271  C CE2 . PHE A 1 415 ? 34.433  11.021  10.654  1.00 32.13  ? 444 PHE A CE2 1 
ATOM   3272  C CZ  . PHE A 1 415 ? 35.366  11.385  9.731   1.00 31.57  ? 444 PHE A CZ  1 
ATOM   3273  N N   . PRO A 1 416 ? 34.231  17.289  13.998  1.00 30.78  ? 445 PRO A N   1 
ATOM   3274  C CA  . PRO A 1 416 ? 33.697  18.261  14.966  1.00 30.14  ? 445 PRO A CA  1 
ATOM   3275  C C   . PRO A 1 416 ? 32.351  17.877  15.574  1.00 27.17  ? 445 PRO A C   1 
ATOM   3276  O O   . PRO A 1 416 ? 31.818  16.821  15.310  1.00 33.32  ? 445 PRO A O   1 
ATOM   3277  C CB  . PRO A 1 416 ? 33.600  19.514  14.068  1.00 28.61  ? 445 PRO A CB  1 
ATOM   3278  C CG  . PRO A 1 416 ? 33.206  18.943  12.737  1.00 33.59  ? 445 PRO A CG  1 
ATOM   3279  C CD  . PRO A 1 416 ? 34.132  17.725  12.593  1.00 32.68  ? 445 PRO A CD  1 
ATOM   3280  N N   . LEU A 1 417 ? 31.819  18.721  16.441  1.00 26.74  ? 446 LEU A N   1 
ATOM   3281  C CA  . LEU A 1 417 ? 30.456  18.555  16.914  1.00 31.44  ? 446 LEU A CA  1 
ATOM   3282  C C   . LEU A 1 417 ? 29.503  18.424  15.736  1.00 29.91  ? 446 LEU A C   1 
ATOM   3283  O O   . LEU A 1 417 ? 29.618  19.117  14.733  1.00 25.76  ? 446 LEU A O   1 
ATOM   3284  C CB  . LEU A 1 417 ? 30.165  19.807  17.724  1.00 33.12  ? 446 LEU A CB  1 
ATOM   3285  C CG  . LEU A 1 417 ? 28.863  19.804  18.512  1.00 37.33  ? 446 LEU A CG  1 
ATOM   3286  C CD1 . LEU A 1 417 ? 28.894  18.727  19.578  1.00 37.28  ? 446 LEU A CD1 1 
ATOM   3287  C CD2 . LEU A 1 417 ? 28.668  21.206  19.114  1.00 37.69  ? 446 LEU A CD2 1 
ATOM   3288  N N   . GLU A 1 418 ? 28.578  17.484  15.823  1.00 28.73  ? 447 GLU A N   1 
ATOM   3289  C CA  . GLU A 1 418 ? 27.541  17.394  14.817  1.00 29.97  ? 447 GLU A CA  1 
ATOM   3290  C C   . GLU A 1 418 ? 26.476  18.414  15.220  1.00 34.54  ? 447 GLU A C   1 
ATOM   3291  O O   . GLU A 1 418 ? 25.937  18.303  16.302  1.00 30.05  ? 447 GLU A O   1 
ATOM   3292  C CB  . GLU A 1 418 ? 27.003  15.966  14.720  1.00 31.51  ? 447 GLU A CB  1 
ATOM   3293  C CG  . GLU A 1 418 ? 25.927  15.811  13.638  1.00 34.51  ? 447 GLU A CG  1 
ATOM   3294  C CD  . GLU A 1 418 ? 25.352  14.432  13.359  1.00 40.69  ? 447 GLU A CD  1 
ATOM   3295  O OE1 . GLU A 1 418 ? 26.153  13.477  13.110  1.00 37.67  ? 447 GLU A OE1 1 
ATOM   3296  O OE2 . GLU A 1 418 ? 24.080  14.335  13.297  1.00 37.81  ? 447 GLU A OE2 1 
ATOM   3297  N N   . ARG A 1 419 ? 26.215  19.417  14.375  1.00 34.11  ? 448 ARG A N   1 
ATOM   3298  C CA  . ARG A 1 419 ? 25.328  20.515  14.706  1.00 39.99  ? 448 ARG A CA  1 
ATOM   3299  C C   . ARG A 1 419 ? 24.670  20.955  13.396  1.00 43.57  ? 448 ARG A C   1 
ATOM   3300  O O   . ARG A 1 419 ? 25.041  21.953  12.761  1.00 40.40  ? 448 ARG A O   1 
ATOM   3301  C CB  . ARG A 1 419 ? 26.073  21.624  15.468  1.00 49.54  ? 448 ARG A CB  1 
ATOM   3302  C CG  . ARG A 1 419 ? 25.275  22.331  16.563  1.00 59.69  ? 448 ARG A CG  1 
ATOM   3303  C CD  . ARG A 1 419 ? 24.373  23.468  16.054  1.00 65.54  ? 448 ARG A CD  1 
ATOM   3304  N NE  . ARG A 1 419 ? 23.070  23.591  16.730  1.00 63.80  ? 448 ARG A NE  1 
ATOM   3305  C CZ  . ARG A 1 419 ? 22.583  24.605  17.468  1.00 60.79  ? 448 ARG A CZ  1 
ATOM   3306  N NH1 . ARG A 1 419 ? 21.305  24.635  17.841  1.00 55.60  ? 448 ARG A NH1 1 
ATOM   3307  N NH2 . ARG A 1 419 ? 23.345  25.632  17.791  1.00 61.68  ? 448 ARG A NH2 1 
ATOM   3308  N N   . PRO A 1 420 ? 23.680  20.178  12.919  1.00 39.37  ? 449 PRO A N   1 
ATOM   3309  C CA  . PRO A 1 420 ? 22.863  20.615  11.795  1.00 36.88  ? 449 PRO A CA  1 
ATOM   3310  C C   . PRO A 1 420 ? 21.983  21.771  12.249  1.00 35.86  ? 449 PRO A C   1 
ATOM   3311  O O   . PRO A 1 420 ? 21.813  22.044  13.434  1.00 32.81  ? 449 PRO A O   1 
ATOM   3312  C CB  . PRO A 1 420 ? 22.051  19.361  11.384  1.00 38.08  ? 449 PRO A CB  1 
ATOM   3313  C CG  . PRO A 1 420 ? 21.937  18.580  12.675  1.00 38.98  ? 449 PRO A CG  1 
ATOM   3314  C CD  . PRO A 1 420 ? 23.222  18.890  13.473  1.00 38.94  ? 449 PRO A CD  1 
ATOM   3315  N N   . LYS A 1 421 ? 21.421  22.449  11.257  1.00 33.42  ? 450 LYS A N   1 
ATOM   3316  C CA  . LYS A 1 421 ? 20.511  23.547  11.490  1.00 31.47  ? 450 LYS A CA  1 
ATOM   3317  C C   . LYS A 1 421 ? 19.097  22.981  11.477  1.00 27.17  ? 450 LYS A C   1 
ATOM   3318  O O   . LYS A 1 421 ? 18.745  22.212  10.583  1.00 30.10  ? 450 LYS A O   1 
ATOM   3319  C CB  . LYS A 1 421 ? 20.764  24.559  10.353  1.00 38.38  ? 450 LYS A CB  1 
ATOM   3320  C CG  . LYS A 1 421 ? 19.890  25.794  10.415  1.00 39.26  ? 450 LYS A CG  1 
ATOM   3321  C CD  . LYS A 1 421 ? 19.850  26.418  11.799  1.00 37.83  ? 450 LYS A CD  1 
ATOM   3322  C CE  . LYS A 1 421 ? 19.019  27.656  11.798  1.00 42.78  ? 450 LYS A CE  1 
ATOM   3323  N NZ  . LYS A 1 421 ? 19.174  28.328  13.090  1.00 45.16  ? 450 LYS A NZ  1 
ATOM   3324  N N   . SER A 1 422 ? 18.295  23.335  12.482  1.00 26.90  ? 451 SER A N   1 
ATOM   3325  C CA  . SER A 1 422 ? 16.901  22.934  12.518  1.00 30.99  ? 451 SER A CA  1 
ATOM   3326  C C   . SER A 1 422 ? 16.085  24.119  12.037  1.00 28.48  ? 451 SER A C   1 
ATOM   3327  O O   . SER A 1 422 ? 16.589  25.234  12.111  1.00 27.61  ? 451 SER A O   1 
ATOM   3328  C CB  . SER A 1 422 ? 16.465  22.467  13.884  1.00 27.93  ? 451 SER A CB  1 
ATOM   3329  O OG  . SER A 1 422 ? 16.359  23.558  14.786  1.00 27.06  ? 451 SER A OG  1 
ATOM   3330  N N   . MET A 1 423 ? 14.873  23.849  11.520  1.00 28.52  ? 452 MET A N   1 
ATOM   3331  C CA  . MET A 1 423 ? 13.914  24.897  11.217  1.00 33.71  ? 452 MET A CA  1 
ATOM   3332  C C   . MET A 1 423 ? 12.559  24.540  11.784  1.00 28.94  ? 452 MET A C   1 
ATOM   3333  O O   . MET A 1 423 ? 12.214  23.380  11.843  1.00 28.97  ? 452 MET A O   1 
ATOM   3334  C CB  . MET A 1 423 ? 13.725  25.110  9.713   1.00 37.02  ? 452 MET A CB  1 
ATOM   3335  C CG  . MET A 1 423 ? 15.015  25.399  8.985   1.00 41.16  ? 452 MET A CG  1 
ATOM   3336  S SD  . MET A 1 423 ? 15.663  27.035  9.365   1.00 52.02  ? 452 MET A SD  1 
ATOM   3337  C CE  . MET A 1 423 ? 14.438  28.042  8.509   1.00 51.37  ? 452 MET A CE  1 
ATOM   3338  N N   . SER A 1 424 ? 11.774  25.564  12.140  1.00 31.82  ? 453 SER A N   1 
ATOM   3339  C CA  . SER A 1 424 ? 10.361  25.359  12.380  1.00 32.53  ? 453 SER A CA  1 
ATOM   3340  C C   . SER A 1 424 ? 9.628   25.349  11.034  1.00 30.26  ? 453 SER A C   1 
ATOM   3341  O O   . SER A 1 424 ? 10.126  25.891  10.044  1.00 29.25  ? 453 SER A O   1 
ATOM   3342  C CB  . SER A 1 424 ? 9.799   26.420  13.302  1.00 34.91  ? 453 SER A CB  1 
ATOM   3343  O OG  . SER A 1 424 ? 9.747   27.694  12.670  1.00 35.24  ? 453 SER A OG  1 
ATOM   3344  N N   . THR A 1 425 ? 8.424   24.779  11.018  1.00 30.97  ? 454 THR A N   1 
ATOM   3345  C CA  . THR A 1 425 ? 7.600   24.756  9.813   1.00 37.71  ? 454 THR A CA  1 
ATOM   3346  C C   . THR A 1 425 ? 7.349   26.194  9.378   1.00 40.73  ? 454 THR A C   1 
ATOM   3347  O O   . THR A 1 425 ? 7.400   26.490  8.192   1.00 37.01  ? 454 THR A O   1 
ATOM   3348  C CB  . THR A 1 425 ? 6.271   24.037  10.052  1.00 40.57  ? 454 THR A CB  1 
ATOM   3349  O OG1 . THR A 1 425 ? 6.593   22.687  10.322  1.00 35.86  ? 454 THR A OG1 1 
ATOM   3350  C CG2 . THR A 1 425 ? 5.306   24.103  8.877   1.00 38.91  ? 454 THR A CG2 1 
ATOM   3351  N N   . GLU A 1 426 ? 7.087   27.067  10.364  1.00 43.61  ? 455 GLU A N   1 
ATOM   3352  C CA  . GLU A 1 426 ? 6.810   28.472  10.107  1.00 45.13  ? 455 GLU A CA  1 
ATOM   3353  C C   . GLU A 1 426 ? 8.040   29.109  9.485   1.00 39.20  ? 455 GLU A C   1 
ATOM   3354  O O   . GLU A 1 426 ? 7.924   29.771  8.463   1.00 38.43  ? 455 GLU A O   1 
ATOM   3355  C CB  . GLU A 1 426 ? 6.365   29.169  11.399  1.00 56.42  ? 455 GLU A CB  1 
ATOM   3356  C CG  . GLU A 1 426 ? 5.695   30.521  11.174  1.00 69.62  ? 455 GLU A CG  1 
ATOM   3357  C CD  . GLU A 1 426 ? 4.561   30.875  12.135  1.00 73.09  ? 455 GLU A CD  1 
ATOM   3358  O OE1 . GLU A 1 426 ? 4.306   30.103  13.091  1.00 70.58  ? 455 GLU A OE1 1 
ATOM   3359  O OE2 . GLU A 1 426 ? 3.905   31.924  11.904  1.00 67.93  ? 455 GLU A OE2 1 
ATOM   3360  N N   . GLY A 1 427 ? 9.213   28.890  10.101  1.00 35.70  ? 456 GLY A N   1 
ATOM   3361  C CA  . GLY A 1 427 ? 10.456  29.450  9.601   1.00 32.65  ? 456 GLY A CA  1 
ATOM   3362  C C   . GLY A 1 427 ? 10.814  28.888  8.226   1.00 32.51  ? 456 GLY A C   1 
ATOM   3363  O O   . GLY A 1 427 ? 11.421  29.572  7.380   1.00 33.58  ? 456 GLY A O   1 
ATOM   3364  N N   . LEU A 1 428 ? 10.472  27.620  8.024   1.00 30.13  ? 457 LEU A N   1 
ATOM   3365  C CA  . LEU A 1 428 ? 10.820  26.948  6.784   1.00 33.38  ? 457 LEU A CA  1 
ATOM   3366  C C   . LEU A 1 428 ? 9.953   27.464  5.630   1.00 36.82  ? 457 LEU A C   1 
ATOM   3367  O O   . LEU A 1 428 ? 10.492  27.695  4.546   1.00 32.55  ? 457 LEU A O   1 
ATOM   3368  C CB  . LEU A 1 428 ? 10.679  25.450  6.993   1.00 30.08  ? 457 LEU A CB  1 
ATOM   3369  C CG  . LEU A 1 428 ? 11.223  24.534  5.893   1.00 31.03  ? 457 LEU A CG  1 
ATOM   3370  C CD1 . LEU A 1 428 ? 12.675  24.789  5.566   1.00 32.06  ? 457 LEU A CD1 1 
ATOM   3371  C CD2 . LEU A 1 428 ? 11.033  23.124  6.343   1.00 31.13  ? 457 LEU A CD2 1 
ATOM   3372  N N   . MET A 1 429 ? 8.643   27.659  5.876   1.00 36.87  ? 458 MET A N   1 
ATOM   3373  C CA  . MET A 1 429 ? 7.754   28.281  4.898   1.00 40.18  ? 458 MET A CA  1 
ATOM   3374  C C   . MET A 1 429 ? 8.302   29.645  4.478   1.00 45.19  ? 458 MET A C   1 
ATOM   3375  O O   . MET A 1 429 ? 8.398   29.925  3.271   1.00 34.71  ? 458 MET A O   1 
ATOM   3376  C CB  . MET A 1 429 ? 6.343   28.432  5.465   1.00 46.05  ? 458 MET A CB  1 
ATOM   3377  C CG  . MET A 1 429 ? 5.571   27.130  5.622   1.00 46.21  ? 458 MET A CG  1 
ATOM   3378  S SD  . MET A 1 429 ? 4.056   27.476  6.538   1.00 56.04  ? 458 MET A SD  1 
ATOM   3379  C CE  . MET A 1 429 ? 3.183   25.911  6.562   1.00 57.26  ? 458 MET A CE  1 
ATOM   3380  N N   . LYS A 1 430 ? 8.732   30.453  5.475   1.00 43.64  ? 459 LYS A N   1 
ATOM   3381  C CA  . LYS A 1 430 ? 9.235   31.799  5.208   1.00 42.45  ? 459 LYS A CA  1 
ATOM   3382  C C   . LYS A 1 430 ? 10.555  31.770  4.445   1.00 43.13  ? 459 LYS A C   1 
ATOM   3383  O O   . LYS A 1 430 ? 10.821  32.658  3.641   1.00 38.54  ? 459 LYS A O   1 
ATOM   3384  C CB  . LYS A 1 430 ? 9.441   32.645  6.468   1.00 49.56  ? 459 LYS A CB  1 
ATOM   3385  C CG  . LYS A 1 430 ? 8.136   32.990  7.153   1.00 52.19  ? 459 LYS A CG  1 
ATOM   3386  C CD  . LYS A 1 430 ? 8.294   33.809  8.425   1.00 65.97  ? 459 LYS A CD  1 
ATOM   3387  C CE  . LYS A 1 430 ? 6.954   34.040  9.061   1.00 67.74  ? 459 LYS A CE  1 
ATOM   3388  N NZ  . LYS A 1 430 ? 7.100   34.854  10.266  1.00 72.40  ? 459 LYS A NZ  1 
ATOM   3389  N N   . PHE A 1 431 ? 11.401  30.778  4.725   1.00 38.27  ? 460 PHE A N   1 
ATOM   3390  C CA  . PHE A 1 431 ? 12.680  30.650  4.055   1.00 42.84  ? 460 PHE A CA  1 
ATOM   3391  C C   . PHE A 1 431 ? 12.478  30.251  2.593   1.00 46.24  ? 460 PHE A C   1 
ATOM   3392  O O   . PHE A 1 431 ? 13.189  30.716  1.705   1.00 42.93  ? 460 PHE A O   1 
ATOM   3393  C CB  . PHE A 1 431 ? 13.515  29.578  4.747   1.00 42.05  ? 460 PHE A CB  1 
ATOM   3394  C CG  . PHE A 1 431 ? 14.847  29.372  4.060   1.00 41.88  ? 460 PHE A CG  1 
ATOM   3395  C CD1 . PHE A 1 431 ? 15.898  30.267  4.272   1.00 40.18  ? 460 PHE A CD1 1 
ATOM   3396  C CD2 . PHE A 1 431 ? 15.047  28.295  3.205   1.00 38.06  ? 460 PHE A CD2 1 
ATOM   3397  C CE1 . PHE A 1 431 ? 17.107  30.085  3.630   1.00 42.00  ? 460 PHE A CE1 1 
ATOM   3398  C CE2 . PHE A 1 431 ? 16.268  28.117  2.584   1.00 38.07  ? 460 PHE A CE2 1 
ATOM   3399  C CZ  . PHE A 1 431 ? 17.291  29.006  2.800   1.00 38.77  ? 460 PHE A CZ  1 
ATOM   3400  N N   . VAL A 1 432 ? 11.545  29.328  2.362   1.00 44.00  ? 461 VAL A N   1 
ATOM   3401  C CA  . VAL A 1 432 ? 11.239  28.894  1.012   1.00 47.06  ? 461 VAL A CA  1 
ATOM   3402  C C   . VAL A 1 432 ? 10.664  30.038  0.172   1.00 45.67  ? 461 VAL A C   1 
ATOM   3403  O O   . VAL A 1 432 ? 10.991  30.136  -1.004  1.00 51.20  ? 461 VAL A O   1 
ATOM   3404  C CB  . VAL A 1 432 ? 10.282  27.702  1.048   1.00 41.85  ? 461 VAL A CB  1 
ATOM   3405  C CG1 . VAL A 1 432 ? 9.580   27.530  -0.288  1.00 43.27  ? 461 VAL A CG1 1 
ATOM   3406  C CG2 . VAL A 1 432 ? 11.052  26.448  1.426   1.00 41.60  ? 461 VAL A CG2 1 
ATOM   3407  N N   . ASP A 1 433 ? 9.815   30.880  0.770   1.00 46.21  ? 462 ASP A N   1 
ATOM   3408  C CA  . ASP A 1 433 ? 9.222   32.035  0.102   1.00 53.99  ? 462 ASP A CA  1 
ATOM   3409  C C   . ASP A 1 433 ? 10.261  33.123  -0.227  1.00 61.50  ? 462 ASP A C   1 
ATOM   3410  O O   . ASP A 1 433 ? 10.031  33.952  -1.101  1.00 67.83  ? 462 ASP A O   1 
ATOM   3411  C CB  . ASP A 1 433 ? 8.058   32.607  0.908   1.00 52.05  ? 462 ASP A CB  1 
ATOM   3412  C CG  . ASP A 1 433 ? 6.846   31.701  1.120   1.00 60.55  ? 462 ASP A CG  1 
ATOM   3413  O OD1 . ASP A 1 433 ? 6.943   30.476  0.853   1.00 61.14  ? 462 ASP A OD1 1 
ATOM   3414  O OD2 . ASP A 1 433 ? 5.794   32.222  1.551   1.00 62.60  ? 462 ASP A OD2 1 
ATOM   3415  N N   . SER A 1 434 ? 11.406  33.147  0.464   1.00 65.29  ? 463 SER A N   1 
ATOM   3416  C CA  . SER A 1 434 ? 12.442  34.144  0.225   1.00 64.88  ? 463 SER A CA  1 
ATOM   3417  C C   . SER A 1 434 ? 13.271  33.820  -1.030  1.00 57.04  ? 463 SER A C   1 
ATOM   3418  O O   . SER A 1 434 ? 13.245  32.638  -1.476  1.00 56.66  ? 463 SER A O   1 
ATOM   3419  C CB  . SER A 1 434 ? 13.310  34.278  1.456   1.00 64.17  ? 463 SER A CB  1 
ATOM   3420  O OG  . SER A 1 434 ? 12.525  34.830  2.504   1.00 70.73  ? 463 SER A OG  1 
ATOM   3421  N N   . SER B 1 1   ? -10.086 23.199  28.475  1.00 61.85  ? 30  SER D N   1 
ATOM   3422  C CA  . SER B 1 1   ? -10.067 24.563  29.083  1.00 80.40  ? 30  SER D CA  1 
ATOM   3423  C C   . SER B 1 1   ? -8.894  24.710  30.049  1.00 85.59  ? 30  SER D C   1 
ATOM   3424  O O   . SER B 1 1   ? -8.112  25.670  30.003  1.00 69.89  ? 30  SER D O   1 
ATOM   3425  C CB  . SER B 1 1   ? -11.363 24.880  29.806  1.00 84.46  ? 30  SER D CB  1 
ATOM   3426  O OG  . SER B 1 1   ? -11.327 26.197  30.351  1.00 77.96  ? 30  SER D OG  1 
ATOM   3427  N N   . THR B 1 2   ? -8.802  23.757  30.973  1.00 84.28  ? 31  THR D N   1 
ATOM   3428  C CA  . THR B 1 2   ? -7.679  23.770  31.883  1.00 76.52  ? 31  THR D CA  1 
ATOM   3429  C C   . THR B 1 2   ? -6.766  22.583  31.586  1.00 64.25  ? 31  THR D C   1 
ATOM   3430  O O   . THR B 1 2   ? -5.572  22.677  31.859  1.00 65.92  ? 31  THR D O   1 
ATOM   3431  C CB  . THR B 1 2   ? -8.195  23.835  33.321  1.00 80.37  ? 31  THR D CB  1 
ATOM   3432  O OG1 . THR B 1 2   ? -7.088  24.421  34.004  1.00 70.27  ? 31  THR D OG1 1 
ATOM   3433  C CG2 . THR B 1 2   ? -8.688  22.496  33.850  1.00 78.56  ? 31  THR D CG2 1 
ATOM   3434  N N   . ASN B 1 3   ? -7.307  21.508  30.986  1.00 52.09  ? 32  ASN D N   1 
ATOM   3435  C CA  . ASN B 1 3   ? -6.526  20.292  30.815  1.00 48.20  ? 32  ASN D CA  1 
ATOM   3436  C C   . ASN B 1 3   ? -5.671  20.443  29.569  1.00 31.98  ? 32  ASN D C   1 
ATOM   3437  O O   . ASN B 1 3   ? -6.222  20.524  28.507  1.00 29.97  ? 32  ASN D O   1 
ATOM   3438  C CB  . ASN B 1 3   ? -7.377  19.030  30.710  1.00 46.10  ? 32  ASN D CB  1 
ATOM   3439  C CG  . ASN B 1 3   ? -6.575  17.788  31.036  1.00 48.29  ? 32  ASN D CG  1 
ATOM   3440  O OD1 . ASN B 1 3   ? -5.450  17.605  30.558  1.00 42.66  ? 32  ASN D OD1 1 
ATOM   3441  N ND2 . ASN B 1 3   ? -7.090  16.954  31.925  1.00 53.06  ? 32  ASN D ND2 1 
ATOM   3442  N N   . LEU B 1 4   ? -4.348  20.459  29.720  1.00 31.20  ? 33  LEU D N   1 
ATOM   3443  C CA  . LEU B 1 4   ? -3.425  20.676  28.611  1.00 28.91  ? 33  LEU D CA  1 
ATOM   3444  C C   . LEU B 1 4   ? -3.573  19.598  27.536  1.00 28.78  ? 33  LEU D C   1 
ATOM   3445  O O   . LEU B 1 4   ? -3.394  19.878  26.359  1.00 28.21  ? 33  LEU D O   1 
ATOM   3446  C CB  . LEU B 1 4   ? -2.018  20.715  29.192  1.00 27.24  ? 33  LEU D CB  1 
ATOM   3447  C CG  . LEU B 1 4   ? -0.841  20.789  28.214  1.00 25.95  ? 33  LEU D CG  1 
ATOM   3448  C CD1 . LEU B 1 4   ? -0.861  22.007  27.306  1.00 29.97  ? 33  LEU D CD1 1 
ATOM   3449  C CD2 . LEU B 1 4   ? 0.408   20.819  29.063  1.00 28.89  ? 33  LEU D CD2 1 
ATOM   3450  N N   . LYS B 1 5   ? -3.870  18.363  27.945  1.00 30.44  ? 34  LYS D N   1 
ATOM   3451  C CA  . LYS B 1 5   ? -3.994  17.261  27.013  1.00 33.79  ? 34  LYS D CA  1 
ATOM   3452  C C   . LYS B 1 5   ? -5.154  17.480  26.033  1.00 33.50  ? 34  LYS D C   1 
ATOM   3453  O O   . LYS B 1 5   ? -5.046  17.101  24.871  1.00 30.54  ? 34  LYS D O   1 
ATOM   3454  C CB  . LYS B 1 5   ? -4.220  15.940  27.758  1.00 33.88  ? 34  LYS D CB  1 
ATOM   3455  C CG  . LYS B 1 5   ? -3.852  14.710  26.948  1.00 35.16  ? 34  LYS D CG  1 
ATOM   3456  C CD  . LYS B 1 5   ? -4.178  13.414  27.688  1.00 37.22  ? 34  LYS D CD  1 
ATOM   3457  C CE  . LYS B 1 5   ? -3.666  12.198  27.002  1.00 41.12  ? 34  LYS D CE  1 
ATOM   3458  N NZ  . LYS B 1 5   ? -3.972  10.979  27.765  1.00 43.37  ? 34  LYS D NZ  1 
ATOM   3459  N N   . ASP B 1 6   ? -6.270  18.052  26.509  1.00 33.68  ? 35  ASP D N   1 
ATOM   3460  C CA  . ASP B 1 6   ? -7.422  18.311  25.656  1.00 36.30  ? 35  ASP D CA  1 
ATOM   3461  C C   . ASP B 1 6   ? -7.190  19.538  24.788  1.00 32.18  ? 35  ASP D C   1 
ATOM   3462  O O   . ASP B 1 6   ? -7.665  19.562  23.664  1.00 30.13  ? 35  ASP D O   1 
ATOM   3463  C CB  . ASP B 1 6   ? -8.700  18.427  26.457  1.00 40.27  ? 35  ASP D CB  1 
ATOM   3464  C CG  . ASP B 1 6   ? -9.040  17.157  27.232  1.00 44.98  ? 35  ASP D CG  1 
ATOM   3465  O OD1 . ASP B 1 6   ? -9.259  16.132  26.564  1.00 52.79  ? 35  ASP D OD1 1 
ATOM   3466  O OD2 . ASP B 1 6   ? -9.086  17.201  28.482  1.00 52.22  ? 35  ASP D OD2 1 
ATOM   3467  N N   . ILE B 1 7   ? -6.427  20.528  25.282  1.00 31.23  ? 36  ILE D N   1 
ATOM   3468  C CA  . ILE B 1 7   ? -6.106  21.699  24.471  1.00 31.36  ? 36  ILE D CA  1 
ATOM   3469  C C   . ILE B 1 7   ? -5.202  21.255  23.321  1.00 31.73  ? 36  ILE D C   1 
ATOM   3470  O O   . ILE B 1 7   ? -5.392  21.613  22.160  1.00 32.58  ? 36  ILE D O   1 
ATOM   3471  C CB  . ILE B 1 7   ? -5.518  22.803  25.368  1.00 37.23  ? 36  ILE D CB  1 
ATOM   3472  C CG1 . ILE B 1 7   ? -6.607  23.339  26.290  1.00 37.55  ? 36  ILE D CG1 1 
ATOM   3473  C CG2 . ILE B 1 7   ? -4.869  23.945  24.585  1.00 38.96  ? 36  ILE D CG2 1 
ATOM   3474  C CD1 . ILE B 1 7   ? -6.109  24.263  27.379  1.00 42.56  ? 36  ILE D CD1 1 
ATOM   3475  N N   . LEU B 1 8   ? -4.226  20.433  23.656  1.00 31.22  ? 37  LEU D N   1 
ATOM   3476  C CA  . LEU B 1 8   ? -3.280  19.931  22.679  1.00 33.28  ? 37  LEU D CA  1 
ATOM   3477  C C   . LEU B 1 8   ? -3.972  19.059  21.631  1.00 34.28  ? 37  LEU D C   1 
ATOM   3478  O O   . LEU B 1 8   ? -3.643  19.163  20.464  1.00 34.47  ? 37  LEU D O   1 
ATOM   3479  C CB  . LEU B 1 8   ? -2.221  19.191  23.475  1.00 30.13  ? 37  LEU D CB  1 
ATOM   3480  C CG  . LEU B 1 8   ? -1.074  18.606  22.666  1.00 33.27  ? 37  LEU D CG  1 
ATOM   3481  C CD1 . LEU B 1 8   ? -0.463  19.625  21.754  1.00 36.43  ? 37  LEU D CD1 1 
ATOM   3482  C CD2 . LEU B 1 8   ? -0.086  18.023  23.675  1.00 33.09  ? 37  LEU D CD2 1 
ATOM   3483  N N   . ALA B 1 9   ? -4.942  18.232  22.035  1.00 27.79  ? 38  ALA D N   1 
ATOM   3484  C CA  . ALA B 1 9   ? -5.704  17.440  21.086  1.00 30.63  ? 38  ALA D CA  1 
ATOM   3485  C C   . ALA B 1 9   ? -6.422  18.324  20.077  1.00 30.52  ? 38  ALA D C   1 
ATOM   3486  O O   . ALA B 1 9   ? -6.663  17.886  18.964  1.00 29.02  ? 38  ALA D O   1 
ATOM   3487  C CB  . ALA B 1 9   ? -6.685  16.531  21.806  1.00 28.99  ? 38  ALA D CB  1 
ATOM   3488  N N   . ASP B 1 10  ? -6.831  19.538  20.465  1.00 29.37  ? 39  ASP D N   1 
ATOM   3489  C CA  . ASP B 1 10  ? -7.522  20.412  19.535  1.00 32.64  ? 39  ASP D CA  1 
ATOM   3490  C C   . ASP B 1 10  ? -6.536  21.123  18.606  1.00 36.20  ? 39  ASP D C   1 
ATOM   3491  O O   . ASP B 1 10  ? -6.915  21.471  17.486  1.00 41.67  ? 39  ASP D O   1 
ATOM   3492  C CB  . ASP B 1 10  ? -8.452  21.375  20.262  1.00 38.48  ? 39  ASP D CB  1 
ATOM   3493  C CG  . ASP B 1 10  ? -9.590  20.721  21.051  1.00 44.49  ? 39  ASP D CG  1 
ATOM   3494  O OD1 . ASP B 1 10  ? -10.010 19.591  20.677  1.00 48.60  ? 39  ASP D OD1 1 
ATOM   3495  O OD2 . ASP B 1 10  ? -10.027 21.319  22.066  1.00 52.96  ? 39  ASP D OD2 1 
ATOM   3496  N N   . LEU B 1 11  ? -5.301  21.360  19.073  1.00 28.22  ? 40  LEU D N   1 
ATOM   3497  C CA  . LEU B 1 11  ? -4.261  22.020  18.286  1.00 30.42  ? 40  LEU D CA  1 
ATOM   3498  C C   . LEU B 1 11  ? -3.629  21.087  17.240  1.00 31.09  ? 40  LEU D C   1 
ATOM   3499  O O   . LEU B 1 11  ? -3.096  21.560  16.245  1.00 28.81  ? 40  LEU D O   1 
ATOM   3500  C CB  . LEU B 1 11  ? -3.154  22.525  19.211  1.00 31.17  ? 40  LEU D CB  1 
ATOM   3501  C CG  . LEU B 1 11  ? -3.514  23.636  20.192  1.00 38.74  ? 40  LEU D CG  1 
ATOM   3502  C CD1 . LEU B 1 11  ? -2.307  23.806  21.077  1.00 42.86  ? 40  LEU D CD1 1 
ATOM   3503  C CD2 . LEU B 1 11  ? -3.873  24.949  19.502  1.00 43.53  ? 40  LEU D CD2 1 
ATOM   3504  N N   . ILE B 1 12  ? -3.622  19.767  17.469  1.00 33.00  ? 41  ILE D N   1 
ATOM   3505  C CA  . ILE B 1 12  ? -2.821  18.861  16.654  1.00 32.66  ? 41  ILE D CA  1 
ATOM   3506  C C   . ILE B 1 12  ? -3.322  18.770  15.210  1.00 36.07  ? 41  ILE D C   1 
ATOM   3507  O O   . ILE B 1 12  ? -2.489  18.862  14.303  1.00 32.64  ? 41  ILE D O   1 
ATOM   3508  C CB  . ILE B 1 12  ? -2.676  17.490  17.322  1.00 31.36  ? 41  ILE D CB  1 
ATOM   3509  C CG1 . ILE B 1 12  ? -1.581  17.577  18.401  1.00 31.05  ? 41  ILE D CG1 1 
ATOM   3510  C CG2 . ILE B 1 12  ? -2.381  16.399  16.292  1.00 31.96  ? 41  ILE D CG2 1 
ATOM   3511  C CD1 . ILE B 1 12  ? -1.616  16.456  19.429  1.00 32.82  ? 41  ILE D CD1 1 
ATOM   3512  N N   . PRO B 1 13  ? -4.641  18.604  14.940  1.00 33.96  ? 42  PRO D N   1 
ATOM   3513  C CA  . PRO B 1 13  ? -5.155  18.576  13.560  1.00 40.14  ? 42  PRO D CA  1 
ATOM   3514  C C   . PRO B 1 13  ? -4.885  19.796  12.670  1.00 34.98  ? 42  PRO D C   1 
ATOM   3515  O O   . PRO B 1 13  ? -4.619  19.639  11.484  1.00 34.60  ? 42  PRO D O   1 
ATOM   3516  C CB  . PRO B 1 13  ? -6.685  18.296  13.671  1.00 39.72  ? 42  PRO D CB  1 
ATOM   3517  C CG  . PRO B 1 13  ? -6.960  18.147  15.165  1.00 38.47  ? 42  PRO D CG  1 
ATOM   3518  C CD  . PRO B 1 13  ? -5.684  18.318  15.938  1.00 37.26  ? 42  PRO D CD  1 
ATOM   3519  N N   . LYS B 1 14  ? -4.910  20.998  13.242  1.00 36.53  ? 43  LYS D N   1 
ATOM   3520  C CA  . LYS B 1 14  ? -4.566  22.219  12.521  1.00 37.53  ? 43  LYS D CA  1 
ATOM   3521  C C   . LYS B 1 14  ? -3.105  22.251  12.080  1.00 37.50  ? 43  LYS D C   1 
ATOM   3522  O O   . LYS B 1 14  ? -2.776  22.731  10.990  1.00 33.87  ? 43  LYS D O   1 
ATOM   3523  C CB  . LYS B 1 14  ? -4.747  23.461  13.404  1.00 44.42  ? 43  LYS D CB  1 
ATOM   3524  C CG  . LYS B 1 14  ? -6.114  24.101  13.251  1.00 58.59  ? 43  LYS D CG  1 
ATOM   3525  C CD  . LYS B 1 14  ? -6.453  25.178  14.277  1.00 61.64  ? 43  LYS D CD  1 
ATOM   3526  C CE  . LYS B 1 14  ? -6.649  24.573  15.627  1.00 63.58  ? 43  LYS D CE  1 
ATOM   3527  N NZ  . LYS B 1 14  ? -7.858  25.095  16.260  1.00 70.35  ? 43  LYS D NZ  1 
ATOM   3528  N N   . GLU B 1 15  ? -2.223  21.783  12.958  1.00 33.15  ? 44  GLU D N   1 
ATOM   3529  C CA  . GLU B 1 15  ? -0.806  21.788  12.667  1.00 33.49  ? 44  GLU D CA  1 
ATOM   3530  C C   . GLU B 1 15  ? -0.487  20.690  11.655  1.00 29.88  ? 44  GLU D C   1 
ATOM   3531  O O   . GLU B 1 15  ? 0.379   20.892  10.817  1.00 30.29  ? 44  GLU D O   1 
ATOM   3532  C CB  . GLU B 1 15  ? -0.035  21.629  13.973  1.00 38.78  ? 44  GLU D CB  1 
ATOM   3533  C CG  . GLU B 1 15  ? 1.459   21.900  13.845  1.00 53.15  ? 44  GLU D CG  1 
ATOM   3534  C CD  . GLU B 1 15  ? 1.865   23.264  13.297  1.00 59.26  ? 44  GLU D CD  1 
ATOM   3535  O OE1 . GLU B 1 15  ? 1.173   24.280  13.573  1.00 47.26  ? 44  GLU D OE1 1 
ATOM   3536  O OE2 . GLU B 1 15  ? 2.928   23.285  12.625  1.00 69.45  ? 44  GLU D OE2 1 
ATOM   3537  N N   . GLN B 1 16  ? -1.153  19.534  11.769  1.00 28.15  ? 45  GLN D N   1 
ATOM   3538  C CA  . GLN B 1 16  ? -1.006  18.430  10.827  1.00 31.32  ? 45  GLN D CA  1 
ATOM   3539  C C   . GLN B 1 16  ? -1.400  18.880  9.421   1.00 34.91  ? 45  GLN D C   1 
ATOM   3540  O O   . GLN B 1 16  ? -0.677  18.586  8.490   1.00 36.44  ? 45  GLN D O   1 
ATOM   3541  C CB  . GLN B 1 16  ? -1.879  17.220  11.139  1.00 29.02  ? 45  GLN D CB  1 
ATOM   3542  C CG  . GLN B 1 16  ? -1.411  16.439  12.358  1.00 29.67  ? 45  GLN D CG  1 
ATOM   3543  C CD  . GLN B 1 16  ? -2.339  15.336  12.820  1.00 30.92  ? 45  GLN D CD  1 
ATOM   3544  O OE1 . GLN B 1 16  ? -3.530  15.323  12.542  1.00 38.05  ? 45  GLN D OE1 1 
ATOM   3545  N NE2 . GLN B 1 16  ? -1.794  14.397  13.574  1.00 33.19  ? 45  GLN D NE2 1 
ATOM   3546  N N   . ALA B 1 17  ? -2.507  19.621  9.291   1.00 35.18  ? 46  ALA D N   1 
ATOM   3547  C CA  . ALA B 1 17  ? -2.978  20.117  7.996   1.00 38.30  ? 46  ALA D CA  1 
ATOM   3548  C C   . ALA B 1 17  ? -2.058  21.216  7.459   1.00 38.85  ? 46  ALA D C   1 
ATOM   3549  O O   . ALA B 1 17  ? -1.817  21.336  6.245   1.00 37.08  ? 46  ALA D O   1 
ATOM   3550  C CB  . ALA B 1 17  ? -4.400  20.632  8.137   1.00 35.16  ? 46  ALA D CB  1 
ATOM   3551  N N   . ARG B 1 18  ? -1.549  22.038  8.380   1.00 36.89  ? 47  ARG D N   1 
ATOM   3552  C CA  . ARG B 1 18  ? -0.636  23.094  7.996   1.00 39.06  ? 47  ARG D CA  1 
ATOM   3553  C C   . ARG B 1 18  ? 0.574   22.480  7.316   1.00 40.06  ? 47  ARG D C   1 
ATOM   3554  O O   . ARG B 1 18  ? 1.037   22.964  6.288   1.00 39.33  ? 47  ARG D O   1 
ATOM   3555  C CB  . ARG B 1 18  ? -0.154  23.936  9.169   1.00 42.72  ? 47  ARG D CB  1 
ATOM   3556  C CG  . ARG B 1 18  ? 0.328   25.305  8.714   1.00 54.20  ? 47  ARG D CG  1 
ATOM   3557  C CD  . ARG B 1 18  ? -0.023  26.377  9.746   1.00 62.36  ? 47  ARG D CD  1 
ATOM   3558  N NE  . ARG B 1 18  ? 0.905   26.247  10.872  1.00 66.95  ? 47  ARG D NE  1 
ATOM   3559  C CZ  . ARG B 1 18  ? 2.141   26.732  10.872  1.00 77.10  ? 47  ARG D CZ  1 
ATOM   3560  N NH1 . ARG B 1 18  ? 3.051   26.232  11.696  1.00 76.34  ? 47  ARG D NH1 1 
ATOM   3561  N NH2 . ARG B 1 18  ? 2.489   27.651  9.987   1.00 80.38  ? 47  ARG D NH2 1 
ATOM   3562  N N   . ILE B 1 19  ? 1.097   21.430  7.928   1.00 31.75  ? 48  ILE D N   1 
ATOM   3563  C CA  . ILE B 1 19  ? 2.322   20.820  7.450   1.00 34.19  ? 48  ILE D CA  1 
ATOM   3564  C C   . ILE B 1 19  ? 2.036   20.060  6.162   1.00 29.78  ? 48  ILE D C   1 
ATOM   3565  O O   . ILE B 1 19  ? 2.845   20.094  5.237   1.00 32.43  ? 48  ILE D O   1 
ATOM   3566  C CB  . ILE B 1 19  ? 2.947   19.907  8.522   1.00 30.48  ? 48  ILE D CB  1 
ATOM   3567  C CG1 . ILE B 1 19  ? 3.595   20.735  9.608   1.00 38.57  ? 48  ILE D CG1 1 
ATOM   3568  C CG2 . ILE B 1 19  ? 3.933   18.909  7.902   1.00 34.78  ? 48  ILE D CG2 1 
ATOM   3569  C CD1 . ILE B 1 19  ? 3.929   19.934  10.859  1.00 42.21  ? 48  ILE D CD1 1 
ATOM   3570  N N   . LYS B 1 20  ? 0.916   19.347  6.133   1.00 31.51  ? 49  LYS D N   1 
ATOM   3571  C CA  . LYS B 1 20  ? 0.561   18.579  4.949   1.00 37.97  ? 49  LYS D CA  1 
ATOM   3572  C C   . LYS B 1 20  ? 0.391   19.548  3.774   1.00 38.84  ? 49  LYS D C   1 
ATOM   3573  O O   . LYS B 1 20  ? 0.823   19.251  2.678   1.00 34.94  ? 49  LYS D O   1 
ATOM   3574  C CB  . LYS B 1 20  ? -0.654  17.702  5.265   1.00 41.03  ? 49  LYS D CB  1 
ATOM   3575  C CG  . LYS B 1 20  ? -1.103  16.728  4.190   1.00 45.76  ? 49  LYS D CG  1 
ATOM   3576  C CD  . LYS B 1 20  ? -2.486  16.172  4.528   1.00 54.47  ? 49  LYS D CD  1 
ATOM   3577  C CE  . LYS B 1 20  ? -3.268  15.634  3.359   1.00 62.82  ? 49  LYS D CE  1 
ATOM   3578  N NZ  . LYS B 1 20  ? -2.956  14.233  3.046   1.00 65.14  ? 49  LYS D NZ  1 
ATOM   3579  N N   . THR B 1 21  ? -0.188  20.730  4.003   1.00 36.68  ? 50  THR D N   1 
ATOM   3580  C CA  . THR B 1 21  ? -0.347  21.701  2.930   1.00 41.93  ? 50  THR D CA  1 
ATOM   3581  C C   . THR B 1 21  ? 1.028   22.117  2.405   1.00 38.30  ? 50  THR D C   1 
ATOM   3582  O O   . THR B 1 21  ? 1.195   22.322  1.223   1.00 31.05  ? 50  THR D O   1 
ATOM   3583  C CB  . THR B 1 21  ? -1.178  22.899  3.415   1.00 48.34  ? 50  THR D CB  1 
ATOM   3584  O OG1 . THR B 1 21  ? -2.449  22.426  3.867   1.00 59.14  ? 50  THR D OG1 1 
ATOM   3585  C CG2 . THR B 1 21  ? -1.456  23.919  2.328   1.00 53.58  ? 50  THR D CG2 1 
ATOM   3586  N N   . PHE B 1 22  ? 2.003   22.320  3.287   1.00 36.16  ? 51  PHE D N   1 
ATOM   3587  C CA  . PHE B 1 22  ? 3.257   22.928  2.887   1.00 33.58  ? 51  PHE D CA  1 
ATOM   3588  C C   . PHE B 1 22  ? 4.107   21.910  2.129   1.00 31.97  ? 51  PHE D C   1 
ATOM   3589  O O   . PHE B 1 22  ? 4.822   22.261  1.186   1.00 29.34  ? 51  PHE D O   1 
ATOM   3590  C CB  . PHE B 1 22  ? 3.902   23.496  4.151   1.00 33.70  ? 51  PHE D CB  1 
ATOM   3591  C CG  . PHE B 1 22  ? 5.342   23.949  3.975   1.00 36.38  ? 51  PHE D CG  1 
ATOM   3592  C CD1 . PHE B 1 22  ? 5.685   24.839  2.962   1.00 33.82  ? 51  PHE D CD1 1 
ATOM   3593  C CD2 . PHE B 1 22  ? 6.353   23.426  4.776   1.00 34.52  ? 51  PHE D CD2 1 
ATOM   3594  C CE1 . PHE B 1 22  ? 7.004   25.198  2.756   1.00 31.33  ? 51  PHE D CE1 1 
ATOM   3595  C CE2 . PHE B 1 22  ? 7.662   23.837  4.608   1.00 34.13  ? 51  PHE D CE2 1 
ATOM   3596  C CZ  . PHE B 1 22  ? 7.985   24.716  3.593   1.00 35.60  ? 51  PHE D CZ  1 
ATOM   3597  N N   . ARG B 1 23  ? 4.019   20.651  2.555   1.00 29.31  ? 52  ARG D N   1 
ATOM   3598  C CA  . ARG B 1 23  ? 4.721   19.573  1.906   1.00 33.19  ? 52  ARG D CA  1 
ATOM   3599  C C   . ARG B 1 23  ? 4.141   19.309  0.519   1.00 36.61  ? 52  ARG D C   1 
ATOM   3600  O O   . ARG B 1 23  ? 4.875   19.080  -0.437  1.00 38.79  ? 52  ARG D O   1 
ATOM   3601  C CB  . ARG B 1 23  ? 4.637   18.357  2.836   1.00 34.07  ? 52  ARG D CB  1 
ATOM   3602  C CG  . ARG B 1 23  ? 5.493   18.488  4.093   1.00 34.83  ? 52  ARG D CG  1 
ATOM   3603  C CD  . ARG B 1 23  ? 5.435   17.215  4.919   1.00 34.91  ? 52  ARG D CD  1 
ATOM   3604  N NE  . ARG B 1 23  ? 6.161   16.168  4.217   1.00 36.51  ? 52  ARG D NE  1 
ATOM   3605  C CZ  . ARG B 1 23  ? 6.337   14.931  4.656   1.00 48.34  ? 52  ARG D CZ  1 
ATOM   3606  N NH1 . ARG B 1 23  ? 5.676   14.518  5.716   1.00 42.42  ? 52  ARG D NH1 1 
ATOM   3607  N NH2 . ARG B 1 23  ? 7.182   14.121  4.022   1.00 52.77  ? 52  ARG D NH2 1 
ATOM   3608  N N   . GLN B 1 24  ? 2.815   19.311  0.422   1.00 36.35  ? 53  GLN D N   1 
ATOM   3609  C CA  . GLN B 1 24  ? 2.138   19.136  -0.855  1.00 40.55  ? 53  GLN D CA  1 
ATOM   3610  C C   . GLN B 1 24  ? 2.462   20.308  -1.792  1.00 36.06  ? 53  GLN D C   1 
ATOM   3611  O O   . GLN B 1 24  ? 2.510   20.147  -3.005  1.00 36.51  ? 53  GLN D O   1 
ATOM   3612  C CB  . GLN B 1 24  ? 0.626   18.973  -0.644  1.00 41.16  ? 53  GLN D CB  1 
ATOM   3613  C CG  . GLN B 1 24  ? 0.201   17.581  -0.194  1.00 43.96  ? 53  GLN D CG  1 
ATOM   3614  C CD  . GLN B 1 24  ? -1.302  17.419  -0.257  1.00 50.84  ? 53  GLN D CD  1 
ATOM   3615  O OE1 . GLN B 1 24  ? -2.047  18.210  0.334   1.00 51.56  ? 53  GLN D OE1 1 
ATOM   3616  N NE2 . GLN B 1 24  ? -1.767  16.453  -1.038  1.00 61.90  ? 53  GLN D NE2 1 
ATOM   3617  N N   . GLN B 1 25  ? 2.725   21.491  -1.240  1.00 34.13  ? 54  GLN D N   1 
ATOM   3618  C CA  . GLN B 1 25  ? 3.093   22.624  -2.069  1.00 38.69  ? 54  GLN D CA  1 
ATOM   3619  C C   . GLN B 1 25  ? 4.587   22.699  -2.381  1.00 37.10  ? 54  GLN D C   1 
ATOM   3620  O O   . GLN B 1 25  ? 4.935   23.162  -3.463  1.00 34.76  ? 54  GLN D O   1 
ATOM   3621  C CB  . GLN B 1 25  ? 2.457   23.806  -1.366  1.00 38.46  ? 54  GLN D CB  1 
ATOM   3622  C CG  . GLN B 1 25  ? 3.098   25.153  -1.612  1.00 43.07  ? 54  GLN D CG  1 
ATOM   3623  C CD  . GLN B 1 25  ? 2.380   26.182  -0.768  1.00 48.83  ? 54  GLN D CD  1 
ATOM   3624  O OE1 . GLN B 1 25  ? 1.269   26.598  -1.095  1.00 51.78  ? 54  GLN D OE1 1 
ATOM   3625  N NE2 . GLN B 1 25  ? 2.962   26.533  0.368   1.00 52.93  ? 54  GLN D NE2 1 
ATOM   3626  N N   . HIS B 1 26  ? 5.460   22.265  -1.457  1.00 33.11  ? 55  HIS D N   1 
ATOM   3627  C CA  . HIS B 1 26  ? 6.873   22.592  -1.567  1.00 34.99  ? 55  HIS D CA  1 
ATOM   3628  C C   . HIS B 1 26  ? 7.808   21.437  -1.232  1.00 32.94  ? 55  HIS D C   1 
ATOM   3629  O O   . HIS B 1 26  ? 9.004   21.681  -1.019  1.00 36.29  ? 55  HIS D O   1 
ATOM   3630  C CB  . HIS B 1 26  ? 7.212   23.802  -0.693  1.00 38.84  ? 55  HIS D CB  1 
ATOM   3631  C CG  . HIS B 1 26  ? 7.032   25.114  -1.376  1.00 33.49  ? 55  HIS D CG  1 
ATOM   3632  N ND1 . HIS B 1 26  ? 7.641   25.444  -2.569  1.00 36.06  ? 55  HIS D ND1 1 
ATOM   3633  C CD2 . HIS B 1 26  ? 6.329   26.197  -0.995  1.00 39.26  ? 55  HIS D CD2 1 
ATOM   3634  C CE1 . HIS B 1 26  ? 7.306   26.690  -2.893  1.00 37.16  ? 55  HIS D CE1 1 
ATOM   3635  N NE2 . HIS B 1 26  ? 6.485   27.161  -1.966  1.00 37.69  ? 55  HIS D NE2 1 
ATOM   3636  N N   . GLY B 1 27  ? 7.291   20.205  -1.298  1.00 32.89  ? 56  GLY D N   1 
ATOM   3637  C CA  . GLY B 1 27  ? 8.012   19.026  -0.842  1.00 33.84  ? 56  GLY D CA  1 
ATOM   3638  C C   . GLY B 1 27  ? 9.332   18.849  -1.593  1.00 39.01  ? 56  GLY D C   1 
ATOM   3639  O O   . GLY B 1 27  ? 10.362  18.524  -1.007  1.00 34.24  ? 56  GLY D O   1 
ATOM   3640  N N   . LYS B 1 28  ? 9.302   19.060  -2.911  1.00 41.83  ? 57  LYS D N   1 
ATOM   3641  C CA  . LYS B 1 28  ? 10.464  18.784  -3.737  1.00 36.40  ? 57  LYS D CA  1 
ATOM   3642  C C   . LYS B 1 28  ? 11.357  20.023  -3.853  1.00 32.11  ? 57  LYS D C   1 
ATOM   3643  O O   . LYS B 1 28  ? 12.409  19.950  -4.464  1.00 40.57  ? 57  LYS D O   1 
ATOM   3644  C CB  . LYS B 1 28  ? 9.972   18.255  -5.081  1.00 40.87  ? 57  LYS D CB  1 
ATOM   3645  C CG  . LYS B 1 28  ? 9.486   16.815  -5.145  1.00 39.74  ? 57  LYS D CG  1 
ATOM   3646  C CD  . LYS B 1 28  ? 8.605   16.614  -6.381  1.00 43.79  ? 57  LYS D CD  1 
ATOM   3647  C CE  . LYS B 1 28  ? 8.656   15.241  -7.008  1.00 49.61  ? 57  LYS D CE  1 
ATOM   3648  N NZ  . LYS B 1 28  ? 7.610   15.013  -8.014  1.00 46.95  ? 57  LYS D NZ  1 
ATOM   3649  N N   . THR B 1 29  ? 10.975  21.150  -3.239  1.00 34.21  ? 58  THR D N   1 
ATOM   3650  C CA  . THR B 1 29  ? 11.761  22.380  -3.318  1.00 38.29  ? 58  THR D CA  1 
ATOM   3651  C C   . THR B 1 29  ? 13.105  22.187  -2.604  1.00 42.03  ? 58  THR D C   1 
ATOM   3652  O O   . THR B 1 29  ? 13.138  21.723  -1.467  1.00 37.26  ? 58  THR D O   1 
ATOM   3653  C CB  . THR B 1 29  ? 11.000  23.539  -2.679  1.00 37.35  ? 58  THR D CB  1 
ATOM   3654  O OG1 . THR B 1 29  ? 9.767   23.584  -3.379  1.00 41.22  ? 58  THR D OG1 1 
ATOM   3655  C CG2 . THR B 1 29  ? 11.781  24.838  -2.705  1.00 41.93  ? 58  THR D CG2 1 
ATOM   3656  N N   . VAL B 1 30  ? 14.202  22.569  -3.275  1.00 37.45  ? 59  VAL D N   1 
ATOM   3657  C CA  . VAL B 1 30  ? 15.537  22.468  -2.717  1.00 40.06  ? 59  VAL D CA  1 
ATOM   3658  C C   . VAL B 1 30  ? 15.746  23.604  -1.712  1.00 38.49  ? 59  VAL D C   1 
ATOM   3659  O O   . VAL B 1 30  ? 15.481  24.764  -2.002  1.00 35.34  ? 59  VAL D O   1 
ATOM   3660  C CB  . VAL B 1 30  ? 16.607  22.498  -3.824  1.00 39.42  ? 59  VAL D CB  1 
ATOM   3661  C CG1 . VAL B 1 30  ? 18.002  22.600  -3.213  1.00 42.12  ? 59  VAL D CG1 1 
ATOM   3662  C CG2 . VAL B 1 30  ? 16.511  21.287  -4.751  1.00 36.74  ? 59  VAL D CG2 1 
ATOM   3663  N N   . VAL B 1 31  ? 16.203  23.265  -0.500  1.00 37.44  ? 60  VAL D N   1 
ATOM   3664  C CA  . VAL B 1 31  ? 16.410  24.282  0.523   1.00 33.46  ? 60  VAL D CA  1 
ATOM   3665  C C   . VAL B 1 31  ? 17.892  24.535  0.754   1.00 29.89  ? 60  VAL D C   1 
ATOM   3666  O O   . VAL B 1 31  ? 18.229  25.540  1.342   1.00 38.99  ? 60  VAL D O   1 
ATOM   3667  C CB  . VAL B 1 31  ? 15.679  23.935  1.829   1.00 40.30  ? 60  VAL D CB  1 
ATOM   3668  C CG1 . VAL B 1 31  ? 14.175  24.083  1.658   1.00 44.57  ? 60  VAL D CG1 1 
ATOM   3669  C CG2 . VAL B 1 31  ? 16.015  22.530  2.294   1.00 44.41  ? 60  VAL D CG2 1 
ATOM   3670  N N   . GLY B 1 32  ? 18.762  23.623  0.325   1.00 32.43  ? 61  GLY D N   1 
ATOM   3671  C CA  . GLY B 1 32  ? 20.195  23.828  0.381   1.00 32.82  ? 61  GLY D CA  1 
ATOM   3672  C C   . GLY B 1 32  ? 20.911  22.715  -0.381  1.00 33.81  ? 61  GLY D C   1 
ATOM   3673  O O   . GLY B 1 32  ? 20.312  21.794  -0.929  1.00 36.05  ? 61  GLY D O   1 
ATOM   3674  N N   . GLN B 1 33  ? 22.224  22.801  -0.363  1.00 37.48  ? 62  GLN D N   1 
ATOM   3675  C CA  . GLN B 1 33  ? 23.076  21.845  -1.029  1.00 42.02  ? 62  GLN D CA  1 
ATOM   3676  C C   . GLN B 1 33  ? 23.895  21.215  0.073   1.00 39.47  ? 62  GLN D C   1 
ATOM   3677  O O   . GLN B 1 33  ? 23.986  21.796  1.151   1.00 41.76  ? 62  GLN D O   1 
ATOM   3678  C CB  . GLN B 1 33  ? 23.864  22.579  -2.103  1.00 46.58  ? 62  GLN D CB  1 
ATOM   3679  C CG  . GLN B 1 33  ? 22.949  23.161  -3.176  1.00 57.79  ? 62  GLN D CG  1 
ATOM   3680  C CD  . GLN B 1 33  ? 23.545  23.033  -4.556  1.00 67.23  ? 62  GLN D CD  1 
ATOM   3681  O OE1 . GLN B 1 33  ? 23.157  22.179  -5.362  1.00 64.80  ? 62  GLN D OE1 1 
ATOM   3682  N NE2 . GLN B 1 33  ? 24.547  23.858  -4.814  1.00 84.95  ? 62  GLN D NE2 1 
ATOM   3683  N N   . ILE B 1 34  ? 24.385  20.012  -0.199  1.00 40.14  ? 63  ILE D N   1 
ATOM   3684  C CA  . ILE B 1 34  ? 25.277  19.332  0.718   1.00 44.10  ? 63  ILE D CA  1 
ATOM   3685  C C   . ILE B 1 34  ? 26.618  19.291  0.019   1.00 41.58  ? 63  ILE D C   1 
ATOM   3686  O O   . ILE B 1 34  ? 26.684  18.785  -1.085  1.00 40.86  ? 63  ILE D O   1 
ATOM   3687  C CB  . ILE B 1 34  ? 24.759  17.927  1.059   1.00 40.28  ? 63  ILE D CB  1 
ATOM   3688  C CG1 . ILE B 1 34  ? 23.363  17.985  1.636   1.00 42.23  ? 63  ILE D CG1 1 
ATOM   3689  C CG2 . ILE B 1 34  ? 25.690  17.193  2.018   1.00 44.54  ? 63  ILE D CG2 1 
ATOM   3690  C CD1 . ILE B 1 34  ? 22.664  16.645  1.643   1.00 40.83  ? 63  ILE D CD1 1 
ATOM   3691  N N   . THR B 1 35  ? 27.647  19.843  0.662   1.00 38.29  ? 64  THR D N   1 
ATOM   3692  C CA  . THR B 1 35  ? 28.995  19.722  0.148   1.00 38.30  ? 64  THR D CA  1 
ATOM   3693  C C   . THR B 1 35  ? 29.726  18.643  0.922   1.00 38.15  ? 64  THR D C   1 
ATOM   3694  O O   . THR B 1 35  ? 29.275  18.185  1.982   1.00 33.80  ? 64  THR D O   1 
ATOM   3695  C CB  . THR B 1 35  ? 29.751  21.035  0.264   1.00 44.14  ? 64  THR D CB  1 
ATOM   3696  O OG1 . THR B 1 35  ? 29.843  21.172  1.679   1.00 44.56  ? 64  THR D OG1 1 
ATOM   3697  C CG2 . THR B 1 35  ? 29.033  22.195  -0.410  1.00 47.13  ? 64  THR D CG2 1 
ATOM   3698  N N   . VAL B 1 36  ? 30.862  18.262  0.339   1.00 39.52  ? 65  VAL D N   1 
ATOM   3699  C CA  . VAL B 1 36  ? 31.808  17.358  0.947   1.00 38.91  ? 65  VAL D CA  1 
ATOM   3700  C C   . VAL B 1 36  ? 32.261  17.954  2.278   1.00 36.34  ? 65  VAL D C   1 
ATOM   3701  O O   . VAL B 1 36  ? 32.248  17.257  3.285   1.00 39.01  ? 65  VAL D O   1 
ATOM   3702  C CB  . VAL B 1 36  ? 32.946  17.078  -0.050  1.00 38.83  ? 65  VAL D CB  1 
ATOM   3703  C CG1 . VAL B 1 36  ? 34.128  16.373  0.601   1.00 36.47  ? 65  VAL D CG1 1 
ATOM   3704  C CG2 . VAL B 1 36  ? 32.453  16.269  -1.241  1.00 39.34  ? 65  VAL D CG2 1 
ATOM   3705  N N   . ASP B 1 37  ? 32.536  19.259  2.331   1.00 36.04  ? 66  ASP D N   1 
ATOM   3706  C CA  . ASP B 1 37  ? 32.910  19.893  3.582   1.00 39.83  ? 66  ASP D CA  1 
ATOM   3707  C C   . ASP B 1 37  ? 31.864  19.696  4.676   1.00 46.55  ? 66  ASP D C   1 
ATOM   3708  O O   . ASP B 1 37  ? 32.240  19.604  5.851   1.00 36.66  ? 66  ASP D O   1 
ATOM   3709  C CB  . ASP B 1 37  ? 33.273  21.356  3.407   1.00 50.09  ? 66  ASP D CB  1 
ATOM   3710  C CG  . ASP B 1 37  ? 34.732  21.583  3.030   1.00 57.98  ? 66  ASP D CG  1 
ATOM   3711  O OD1 . ASP B 1 37  ? 35.528  20.629  3.192   1.00 52.68  ? 66  ASP D OD1 1 
ATOM   3712  O OD2 . ASP B 1 37  ? 35.056  22.693  2.551   1.00 67.19  ? 66  ASP D OD2 1 
ATOM   3713  N N   . MET B 1 38  ? 30.569  19.679  4.312   1.00 41.83  ? 67  MET D N   1 
ATOM   3714  C CA  . MET B 1 38  ? 29.532  19.695  5.331   1.00 40.36  ? 67  MET D CA  1 
ATOM   3715  C C   . MET B 1 38  ? 29.457  18.323  5.980   1.00 34.20  ? 67  MET D C   1 
ATOM   3716  O O   . MET B 1 38  ? 29.139  18.228  7.152   1.00 34.88  ? 67  MET D O   1 
ATOM   3717  C CB  . MET B 1 38  ? 28.146  20.019  4.776   1.00 40.35  ? 67  MET D CB  1 
ATOM   3718  C CG  . MET B 1 38  ? 28.058  21.385  4.155   1.00 50.37  ? 67  MET D CG  1 
ATOM   3719  S SD  . MET B 1 38  ? 26.432  21.612  3.409   1.00 53.16  ? 67  MET D SD  1 
ATOM   3720  C CE  . MET B 1 38  ? 26.873  22.963  2.309   1.00 53.77  ? 67  MET D CE  1 
ATOM   3721  N N   . MET B 1 39  ? 29.732  17.284  5.181   1.00 35.11  ? 68  MET D N   1 
ATOM   3722  C CA  . MET B 1 39  ? 29.757  15.904  5.635   1.00 34.02  ? 68  MET D CA  1 
ATOM   3723  C C   . MET B 1 39  ? 30.920  15.687  6.612   1.00 34.18  ? 68  MET D C   1 
ATOM   3724  O O   . MET B 1 39  ? 30.768  14.972  7.609   1.00 40.73  ? 68  MET D O   1 
ATOM   3725  C CB  . MET B 1 39  ? 29.896  14.962  4.434   1.00 35.16  ? 68  MET D CB  1 
ATOM   3726  C CG  . MET B 1 39  ? 28.720  15.020  3.468   1.00 36.78  ? 68  MET D CG  1 
ATOM   3727  S SD  . MET B 1 39  ? 28.850  13.757  2.193   1.00 40.25  ? 68  MET D SD  1 
ATOM   3728  C CE  . MET B 1 39  ? 28.740  12.312  3.273   1.00 39.66  ? 68  MET D CE  1 
ATOM   3729  N N   . TYR B 1 40  ? 32.102  16.229  6.291   1.00 32.57  ? 69  TYR D N   1 
ATOM   3730  C CA  . TYR B 1 40  ? 33.230  16.169  7.210   1.00 32.40  ? 69  TYR D CA  1 
ATOM   3731  C C   . TYR B 1 40  ? 33.045  17.137  8.372   1.00 32.22  ? 69  TYR D C   1 
ATOM   3732  O O   . TYR B 1 40  ? 33.643  16.924  9.421   1.00 37.84  ? 69  TYR D O   1 
ATOM   3733  C CB  . TYR B 1 40  ? 34.569  16.436  6.528   1.00 31.14  ? 69  TYR D CB  1 
ATOM   3734  C CG  . TYR B 1 40  ? 35.072  15.274  5.695   1.00 27.57  ? 69  TYR D CG  1 
ATOM   3735  C CD1 . TYR B 1 40  ? 35.697  14.196  6.291   1.00 28.52  ? 69  TYR D CD1 1 
ATOM   3736  C CD2 . TYR B 1 40  ? 34.889  15.244  4.324   1.00 29.71  ? 69  TYR D CD2 1 
ATOM   3737  C CE1 . TYR B 1 40  ? 36.160  13.132  5.549   1.00 30.99  ? 69  TYR D CE1 1 
ATOM   3738  C CE2 . TYR B 1 40  ? 35.350  14.185  3.566   1.00 32.19  ? 69  TYR D CE2 1 
ATOM   3739  C CZ  . TYR B 1 40  ? 35.979  13.115  4.178   1.00 30.98  ? 69  TYR D CZ  1 
ATOM   3740  O OH  . TYR B 1 40  ? 36.430  12.050  3.433   1.00 31.71  ? 69  TYR D OH  1 
ATOM   3741  N N   . GLY B 1 41  ? 32.241  18.201  8.206   1.00 31.44  ? 70  GLY D N   1 
ATOM   3742  C CA  . GLY B 1 41  ? 32.167  19.276  9.188   1.00 29.74  ? 70  GLY D CA  1 
ATOM   3743  C C   . GLY B 1 41  ? 30.979  19.140  10.154  1.00 32.93  ? 70  GLY D C   1 
ATOM   3744  O O   . GLY B 1 41  ? 30.532  20.111  10.767  1.00 34.71  ? 70  GLY D O   1 
ATOM   3745  N N   . GLY B 1 42  ? 30.448  17.935  10.315  1.00 32.60  ? 71  GLY D N   1 
ATOM   3746  C CA  . GLY B 1 42  ? 29.343  17.732  11.239  1.00 35.79  ? 71  GLY D CA  1 
ATOM   3747  C C   . GLY B 1 42  ? 28.062  18.436  10.800  1.00 34.89  ? 71  GLY D C   1 
ATOM   3748  O O   . GLY B 1 42  ? 27.374  19.045  11.621  1.00 38.14  ? 71  GLY D O   1 
ATOM   3749  N N   . MET B 1 43  ? 27.775  18.358  9.500   1.00 33.71  ? 72  MET D N   1 
ATOM   3750  C CA  . MET B 1 43  ? 26.556  18.886  8.912   1.00 38.53  ? 72  MET D CA  1 
ATOM   3751  C C   . MET B 1 43  ? 26.441  20.387  9.169   1.00 37.91  ? 72  MET D C   1 
ATOM   3752  O O   . MET B 1 43  ? 25.335  20.911  9.193   1.00 33.88  ? 72  MET D O   1 
ATOM   3753  C CB  . MET B 1 43  ? 25.287  18.248  9.498   1.00 38.58  ? 72  MET D CB  1 
ATOM   3754  C CG  . MET B 1 43  ? 25.213  16.721  9.478   1.00 48.56  ? 72  MET D CG  1 
ATOM   3755  S SD  . MET B 1 43  ? 23.752  16.097  10.356  1.00 46.42  ? 72  MET D SD  1 
ATOM   3756  C CE  . MET B 1 43  ? 23.716  14.372  9.844   1.00 54.57  ? 72  MET D CE  1 
ATOM   3757  N N   . ARG B 1 44  ? 27.554  21.074  9.432   1.00 36.38  ? 73  ARG D N   1 
ATOM   3758  C CA  . ARG B 1 44  ? 27.472  22.474  9.812   1.00 48.67  ? 73  ARG D CA  1 
ATOM   3759  C C   . ARG B 1 44  ? 26.726  23.257  8.725   1.00 40.64  ? 73  ARG D C   1 
ATOM   3760  O O   . ARG B 1 44  ? 26.992  23.068  7.559   1.00 38.38  ? 73  ARG D O   1 
ATOM   3761  C CB  . ARG B 1 44  ? 28.873  23.039  10.077  1.00 54.33  ? 73  ARG D CB  1 
ATOM   3762  C CG  . ARG B 1 44  ? 28.861  24.078  11.192  1.00 64.28  ? 73  ARG D CG  1 
ATOM   3763  C CD  . ARG B 1 44  ? 30.105  23.988  12.070  1.00 73.23  ? 73  ARG D CD  1 
ATOM   3764  N NE  . ARG B 1 44  ? 29.775  23.996  13.503  1.00 74.54  ? 73  ARG D NE  1 
ATOM   3765  C CZ  . ARG B 1 44  ? 29.903  22.973  14.351  1.00 78.61  ? 73  ARG D CZ  1 
ATOM   3766  N NH1 . ARG B 1 44  ? 29.783  23.186  15.653  1.00 71.57  ? 73  ARG D NH1 1 
ATOM   3767  N NH2 . ARG B 1 44  ? 30.208  21.759  13.912  1.00 74.01  ? 73  ARG D NH2 1 
ATOM   3768  N N   . GLY B 1 45  ? 25.750  24.082  9.132   1.00 46.93  ? 74  GLY D N   1 
ATOM   3769  C CA  . GLY B 1 45  ? 24.929  24.864  8.215   1.00 52.49  ? 74  GLY D CA  1 
ATOM   3770  C C   . GLY B 1 45  ? 24.183  24.016  7.178   1.00 51.37  ? 74  GLY D C   1 
ATOM   3771  O O   . GLY B 1 45  ? 23.976  24.440  6.044   1.00 55.43  ? 74  GLY D O   1 
ATOM   3772  N N   . MET B 1 46  ? 23.825  22.793  7.559   1.00 44.18  ? 75  MET D N   1 
ATOM   3773  C CA  . MET B 1 46  ? 22.962  21.935  6.775   1.00 42.27  ? 75  MET D CA  1 
ATOM   3774  C C   . MET B 1 46  ? 21.602  21.960  7.468   1.00 37.76  ? 75  MET D C   1 
ATOM   3775  O O   . MET B 1 46  ? 21.520  21.645  8.651   1.00 34.09  ? 75  MET D O   1 
ATOM   3776  C CB  . MET B 1 46  ? 23.583  20.537  6.755   1.00 44.52  ? 75  MET D CB  1 
ATOM   3777  C CG  . MET B 1 46  ? 22.921  19.520  5.875   1.00 55.73  ? 75  MET D CG  1 
ATOM   3778  S SD  . MET B 1 46  ? 23.726  17.896  5.869   1.00 52.84  ? 75  MET D SD  1 
ATOM   3779  C CE  . MET B 1 46  ? 25.372  18.460  5.463   1.00 44.42  ? 75  MET D CE  1 
ATOM   3780  N N   . LYS B 1 47  ? 20.563  22.412  6.756   1.00 36.33  ? 76  LYS D N   1 
ATOM   3781  C CA  . LYS B 1 47  ? 19.191  22.337  7.241   1.00 36.31  ? 76  LYS D CA  1 
ATOM   3782  C C   . LYS B 1 47  ? 18.770  20.869  7.241   1.00 36.14  ? 76  LYS D C   1 
ATOM   3783  O O   . LYS B 1 47  ? 18.499  20.292  6.199   1.00 45.24  ? 76  LYS D O   1 
ATOM   3784  C CB  . LYS B 1 47  ? 18.228  23.178  6.409   1.00 39.57  ? 76  LYS D CB  1 
ATOM   3785  C CG  . LYS B 1 47  ? 18.413  24.683  6.575   1.00 40.15  ? 76  LYS D CG  1 
ATOM   3786  C CD  . LYS B 1 47  ? 17.610  25.507  5.580   1.00 41.54  ? 76  LYS D CD  1 
ATOM   3787  C CE  . LYS B 1 47  ? 17.824  26.981  5.803   1.00 44.95  ? 76  LYS D CE  1 
ATOM   3788  N NZ  . LYS B 1 47  ? 19.218  27.416  5.641   1.00 47.56  ? 76  LYS D NZ  1 
ATOM   3789  N N   . GLY B 1 48  ? 18.765  20.261  8.426   1.00 34.89  ? 77  GLY D N   1 
ATOM   3790  C CA  . GLY B 1 48  ? 18.697  18.814  8.551   1.00 34.66  ? 77  GLY D CA  1 
ATOM   3791  C C   . GLY B 1 48  ? 17.364  18.335  9.115   1.00 31.55  ? 77  GLY D C   1 
ATOM   3792  O O   . GLY B 1 48  ? 16.943  17.214  8.858   1.00 32.09  ? 77  GLY D O   1 
ATOM   3793  N N   . LEU B 1 49  ? 16.706  19.156  9.923   1.00 31.76  ? 78  LEU D N   1 
ATOM   3794  C CA  . LEU B 1 49  ? 15.544  18.660  10.631  1.00 33.62  ? 78  LEU D CA  1 
ATOM   3795  C C   . LEU B 1 49  ? 14.566  19.777  10.966  1.00 28.92  ? 78  LEU D C   1 
ATOM   3796  O O   . LEU B 1 49  ? 14.896  20.952  10.968  1.00 31.05  ? 78  LEU D O   1 
ATOM   3797  C CB  . LEU B 1 49  ? 16.022  17.950  11.891  1.00 43.33  ? 78  LEU D CB  1 
ATOM   3798  C CG  . LEU B 1 49  ? 16.513  18.845  13.029  1.00 39.45  ? 78  LEU D CG  1 
ATOM   3799  C CD1 . LEU B 1 49  ? 16.357  18.126  14.351  1.00 44.51  ? 78  LEU D CD1 1 
ATOM   3800  C CD2 . LEU B 1 49  ? 17.944  19.216  12.790  1.00 43.15  ? 78  LEU D CD2 1 
ATOM   3801  N N   . VAL B 1 50  ? 13.331  19.362  11.195  1.00 28.27  ? 79  VAL D N   1 
ATOM   3802  C CA  . VAL B 1 50  ? 12.242  20.242  11.543  1.00 29.94  ? 79  VAL D CA  1 
ATOM   3803  C C   . VAL B 1 50  ? 12.023  20.138  13.038  1.00 29.76  ? 79  VAL D C   1 
ATOM   3804  O O   . VAL B 1 50  ? 11.878  19.033  13.560  1.00 25.85  ? 79  VAL D O   1 
ATOM   3805  C CB  . VAL B 1 50  ? 10.944  19.899  10.798  1.00 30.73  ? 79  VAL D CB  1 
ATOM   3806  C CG1 . VAL B 1 50  ? 9.822   20.832  11.269  1.00 31.31  ? 79  VAL D CG1 1 
ATOM   3807  C CG2 . VAL B 1 50  ? 11.148  19.937  9.290   1.00 32.52  ? 79  VAL D CG2 1 
ATOM   3808  N N   . TYR B 1 51  ? 11.986  21.301  13.691  1.00 26.79  ? 80  TYR D N   1 
ATOM   3809  C CA  . TYR B 1 51  ? 11.850  21.350  15.136  1.00 31.59  ? 80  TYR D CA  1 
ATOM   3810  C C   . TYR B 1 51  ? 11.080  22.618  15.511  1.00 32.81  ? 80  TYR D C   1 
ATOM   3811  O O   . TYR B 1 51  ? 11.520  23.722  15.227  1.00 36.69  ? 80  TYR D O   1 
ATOM   3812  C CB  . TYR B 1 51  ? 13.277  21.271  15.668  1.00 31.49  ? 80  TYR D CB  1 
ATOM   3813  C CG  . TYR B 1 51  ? 13.464  21.056  17.156  1.00 28.70  ? 80  TYR D CG  1 
ATOM   3814  C CD1 . TYR B 1 51  ? 13.436  22.140  18.029  1.00 35.52  ? 80  TYR D CD1 1 
ATOM   3815  C CD2 . TYR B 1 51  ? 13.706  19.798  17.682  1.00 31.48  ? 80  TYR D CD2 1 
ATOM   3816  C CE1 . TYR B 1 51  ? 13.640  21.972  19.383  1.00 33.43  ? 80  TYR D CE1 1 
ATOM   3817  C CE2 . TYR B 1 51  ? 13.889  19.611  19.051  1.00 32.22  ? 80  TYR D CE2 1 
ATOM   3818  C CZ  . TYR B 1 51  ? 13.834  20.699  19.897  1.00 34.38  ? 80  TYR D CZ  1 
ATOM   3819  O OH  . TYR B 1 51  ? 14.022  20.534  21.236  1.00 35.84  ? 80  TYR D OH  1 
ATOM   3820  N N   . GLU B 1 52  ? 9.923   22.431  16.130  1.00 32.12  ? 81  GLU D N   1 
ATOM   3821  C CA  . GLU B 1 52  ? 8.871   23.434  16.116  1.00 40.12  ? 81  GLU D CA  1 
ATOM   3822  C C   . GLU B 1 52  ? 8.965   24.394  17.306  1.00 37.47  ? 81  GLU D C   1 
ATOM   3823  O O   . GLU B 1 52  ? 8.432   25.502  17.228  1.00 38.77  ? 81  GLU D O   1 
ATOM   3824  C CB  . GLU B 1 52  ? 7.507   22.732  16.093  1.00 41.04  ? 81  GLU D CB  1 
ATOM   3825  C CG  . GLU B 1 52  ? 7.304   21.744  14.945  1.00 45.42  ? 81  GLU D CG  1 
ATOM   3826  C CD  . GLU B 1 52  ? 7.039   22.373  13.580  1.00 45.90  ? 81  GLU D CD  1 
ATOM   3827  O OE1 . GLU B 1 52  ? 7.346   23.565  13.416  1.00 42.05  ? 81  GLU D OE1 1 
ATOM   3828  O OE2 . GLU B 1 52  ? 6.512   21.680  12.679  1.00 51.86  ? 81  GLU D OE2 1 
ATOM   3829  N N   . THR B 1 53  ? 9.632   23.988  18.394  1.00 36.71  ? 82  THR D N   1 
ATOM   3830  C CA  . THR B 1 53  ? 9.412   24.630  19.678  1.00 35.45  ? 82  THR D CA  1 
ATOM   3831  C C   . THR B 1 53  ? 10.193  25.936  19.799  1.00 32.79  ? 82  THR D C   1 
ATOM   3832  O O   . THR B 1 53  ? 9.687   26.860  20.425  1.00 29.24  ? 82  THR D O   1 
ATOM   3833  C CB  . THR B 1 53  ? 9.741   23.711  20.850  1.00 38.95  ? 82  THR D CB  1 
ATOM   3834  O OG1 . THR B 1 53  ? 10.954  23.073  20.489  1.00 41.04  ? 82  THR D OG1 1 
ATOM   3835  C CG2 . THR B 1 53  ? 8.644   22.710  21.163  1.00 40.36  ? 82  THR D CG2 1 
ATOM   3836  N N   . SER B 1 54  ? 11.417  25.984  19.275  1.00 33.43  ? 83  SER D N   1 
ATOM   3837  C CA  . SER B 1 54  ? 12.258  27.167  19.379  1.00 31.01  ? 83  SER D CA  1 
ATOM   3838  C C   . SER B 1 54  ? 13.086  27.373  18.112  1.00 32.39  ? 83  SER D C   1 
ATOM   3839  O O   . SER B 1 54  ? 13.408  26.420  17.414  1.00 27.36  ? 83  SER D O   1 
ATOM   3840  C CB  . SER B 1 54  ? 13.123  27.115  20.601  1.00 29.84  ? 83  SER D CB  1 
ATOM   3841  O OG  . SER B 1 54  ? 14.089  26.081  20.556  1.00 28.71  ? 83  SER D OG  1 
ATOM   3842  N N   . VAL B 1 55  ? 13.370  28.644  17.819  1.00 32.85  ? 84  VAL D N   1 
ATOM   3843  C CA  . VAL B 1 55  ? 14.088  29.088  16.625  1.00 33.33  ? 84  VAL D CA  1 
ATOM   3844  C C   . VAL B 1 55  ? 15.064  30.187  17.057  1.00 32.99  ? 84  VAL D C   1 
ATOM   3845  O O   . VAL B 1 55  ? 14.690  31.070  17.830  1.00 32.32  ? 84  VAL D O   1 
ATOM   3846  C CB  . VAL B 1 55  ? 13.114  29.661  15.569  1.00 35.56  ? 84  VAL D CB  1 
ATOM   3847  C CG1 . VAL B 1 55  ? 13.840  30.221  14.342  1.00 34.21  ? 84  VAL D CG1 1 
ATOM   3848  C CG2 . VAL B 1 55  ? 12.028  28.679  15.141  1.00 39.84  ? 84  VAL D CG2 1 
ATOM   3849  N N   . LEU B 1 56  ? 16.299  30.159  16.541  1.00 37.41  ? 85  LEU D N   1 
ATOM   3850  C CA  . LEU B 1 56  ? 17.295  31.201  16.769  1.00 44.34  ? 85  LEU D CA  1 
ATOM   3851  C C   . LEU B 1 56  ? 17.062  32.432  15.881  1.00 52.44  ? 85  LEU D C   1 
ATOM   3852  O O   . LEU B 1 56  ? 17.407  32.437  14.709  1.00 44.96  ? 85  LEU D O   1 
ATOM   3853  C CB  . LEU B 1 56  ? 18.691  30.625  16.540  1.00 51.99  ? 85  LEU D CB  1 
ATOM   3854  C CG  . LEU B 1 56  ? 19.845  31.626  16.659  1.00 56.50  ? 85  LEU D CG  1 
ATOM   3855  C CD1 . LEU B 1 56  ? 19.828  32.358  17.990  1.00 55.35  ? 85  LEU D CD1 1 
ATOM   3856  C CD2 . LEU B 1 56  ? 21.173  30.924  16.450  1.00 56.07  ? 85  LEU D CD2 1 
ATOM   3857  N N   . ASP B 1 57  ? 16.509  33.510  16.457  1.00 62.09  ? 86  ASP D N   1 
ATOM   3858  C CA  . ASP B 1 57  ? 16.388  34.785  15.760  1.00 65.48  ? 86  ASP D CA  1 
ATOM   3859  C C   . ASP B 1 57  ? 17.784  35.411  15.728  1.00 66.88  ? 86  ASP D C   1 
ATOM   3860  O O   . ASP B 1 57  ? 18.373  35.667  16.784  1.00 65.58  ? 86  ASP D O   1 
ATOM   3861  C CB  . ASP B 1 57  ? 15.294  35.673  16.357  1.00 66.12  ? 86  ASP D CB  1 
ATOM   3862  C CG  . ASP B 1 57  ? 14.958  36.938  15.572  1.00 60.79  ? 86  ASP D CG  1 
ATOM   3863  O OD1 . ASP B 1 57  ? 15.891  37.702  15.288  1.00 63.80  ? 86  ASP D OD1 1 
ATOM   3864  O OD2 . ASP B 1 57  ? 13.771  37.157  15.250  1.00 60.00  ? 86  ASP D OD2 1 
ATOM   3865  N N   . PRO B 1 58  ? 18.373  35.626  14.526  1.00 59.00  ? 87  PRO D N   1 
ATOM   3866  C CA  . PRO B 1 58  ? 19.802  35.933  14.434  1.00 70.18  ? 87  PRO D CA  1 
ATOM   3867  C C   . PRO B 1 58  ? 20.181  37.288  15.039  1.00 78.83  ? 87  PRO D C   1 
ATOM   3868  O O   . PRO B 1 58  ? 21.347  37.507  15.384  1.00 74.82  ? 87  PRO D O   1 
ATOM   3869  C CB  . PRO B 1 58  ? 20.152  35.793  12.930  1.00 65.76  ? 87  PRO D CB  1 
ATOM   3870  C CG  . PRO B 1 58  ? 18.817  35.829  12.214  1.00 68.98  ? 87  PRO D CG  1 
ATOM   3871  C CD  . PRO B 1 58  ? 17.720  35.495  13.216  1.00 60.26  ? 87  PRO D CD  1 
ATOM   3872  N N   . ASP B 1 59  ? 19.192  38.174  15.227  1.00 71.21  ? 88  ASP D N   1 
ATOM   3873  C CA  . ASP B 1 59  ? 19.442  39.376  16.003  1.00 79.04  ? 88  ASP D CA  1 
ATOM   3874  C C   . ASP B 1 59  ? 19.014  39.114  17.448  1.00 77.53  ? 88  ASP D C   1 
ATOM   3875  O O   . ASP B 1 59  ? 19.874  39.108  18.328  1.00 87.00  ? 88  ASP D O   1 
ATOM   3876  C CB  . ASP B 1 59  ? 18.960  40.626  15.275  1.00 82.13  ? 88  ASP D CB  1 
ATOM   3877  C CG  . ASP B 1 59  ? 17.611  41.203  15.675  1.00 90.92  ? 88  ASP D CG  1 
ATOM   3878  O OD1 . ASP B 1 59  ? 17.526  41.770  16.781  1.00 94.13  ? 88  ASP D OD1 1 
ATOM   3879  O OD2 . ASP B 1 59  ? 16.672  41.128  14.856  1.00 94.11  ? 88  ASP D OD2 1 
ATOM   3880  N N   . GLU B 1 60  ? 17.724  38.804  17.673  1.00 67.85  ? 89  GLU D N   1 
ATOM   3881  C CA  . GLU B 1 60  ? 17.110  38.866  19.001  1.00 71.27  ? 89  GLU D CA  1 
ATOM   3882  C C   . GLU B 1 60  ? 17.260  37.579  19.830  1.00 63.06  ? 89  GLU D C   1 
ATOM   3883  O O   . GLU B 1 60  ? 16.603  37.473  20.870  1.00 65.44  ? 89  GLU D O   1 
ATOM   3884  C CB  . GLU B 1 60  ? 15.649  39.318  18.867  1.00 80.81  ? 89  GLU D CB  1 
ATOM   3885  C CG  . GLU B 1 60  ? 15.497  40.840  18.808  1.00 90.30  ? 89  GLU D CG  1 
ATOM   3886  C CD  . GLU B 1 60  ? 14.522  41.402  17.780  1.00 97.24  ? 89  GLU D CD  1 
ATOM   3887  O OE1 . GLU B 1 60  ? 13.578  40.676  17.402  1.00 102.74 ? 89  GLU D OE1 1 
ATOM   3888  O OE2 . GLU B 1 60  ? 14.725  42.556  17.322  1.00 95.19  ? 89  GLU D OE2 1 
ATOM   3889  N N   . GLY B 1 61  ? 18.119  36.629  19.395  1.00 58.28  ? 90  GLY D N   1 
ATOM   3890  C CA  . GLY B 1 61  ? 18.468  35.417  20.145  1.00 50.43  ? 90  GLY D CA  1 
ATOM   3891  C C   . GLY B 1 61  ? 17.382  34.346  20.044  1.00 42.15  ? 90  GLY D C   1 
ATOM   3892  O O   . GLY B 1 61  ? 16.570  34.403  19.136  1.00 41.55  ? 90  GLY D O   1 
ATOM   3893  N N   . ILE B 1 62  ? 17.311  33.419  21.016  1.00 36.77  ? 91  ILE D N   1 
ATOM   3894  C CA  . ILE B 1 62  ? 16.332  32.344  20.972  1.00 34.54  ? 91  ILE D CA  1 
ATOM   3895  C C   . ILE B 1 62  ? 14.903  32.875  21.117  1.00 33.13  ? 91  ILE D C   1 
ATOM   3896  O O   . ILE B 1 62  ? 14.640  33.821  21.847  1.00 38.70  ? 91  ILE D O   1 
ATOM   3897  C CB  . ILE B 1 62  ? 16.638  31.252  22.012  1.00 34.77  ? 91  ILE D CB  1 
ATOM   3898  C CG1 . ILE B 1 62  ? 15.801  29.989  21.767  1.00 34.27  ? 91  ILE D CG1 1 
ATOM   3899  C CG2 . ILE B 1 62  ? 16.483  31.772  23.438  1.00 35.55  ? 91  ILE D CG2 1 
ATOM   3900  C CD1 . ILE B 1 62  ? 16.155  29.280  20.467  1.00 38.45  ? 91  ILE D CD1 1 
ATOM   3901  N N   . ARG B 1 63  ? 13.993  32.257  20.356  1.00 32.71  ? 92  ARG D N   1 
ATOM   3902  C CA  . ARG B 1 63  ? 12.574  32.514  20.430  1.00 34.08  ? 92  ARG D CA  1 
ATOM   3903  C C   . ARG B 1 63  ? 11.858  31.213  20.735  1.00 31.23  ? 92  ARG D C   1 
ATOM   3904  O O   . ARG B 1 63  ? 12.089  30.219  20.056  1.00 30.11  ? 92  ARG D O   1 
ATOM   3905  C CB  . ARG B 1 63  ? 11.996  33.100  19.144  1.00 37.95  ? 92  ARG D CB  1 
ATOM   3906  C CG  . ARG B 1 63  ? 12.250  34.591  18.992  1.00 47.52  ? 92  ARG D CG  1 
ATOM   3907  C CD  . ARG B 1 63  ? 11.670  35.074  17.668  1.00 51.53  ? 92  ARG D CD  1 
ATOM   3908  N NE  . ARG B 1 63  ? 12.024  36.475  17.421  1.00 56.53  ? 92  ARG D NE  1 
ATOM   3909  C CZ  . ARG B 1 63  ? 11.528  37.538  18.060  1.00 65.34  ? 92  ARG D CZ  1 
ATOM   3910  N NH1 . ARG B 1 63  ? 10.638  37.409  19.036  1.00 60.92  ? 92  ARG D NH1 1 
ATOM   3911  N NH2 . ARG B 1 63  ? 11.937  38.747  17.707  1.00 67.62  ? 92  ARG D NH2 1 
ATOM   3912  N N   . PHE B 1 64  ? 10.960  31.281  21.726  1.00 28.36  ? 93  PHE D N   1 
ATOM   3913  C CA  . PHE B 1 64  ? 10.119  30.172  22.127  1.00 30.14  ? 93  PHE D CA  1 
ATOM   3914  C C   . PHE B 1 64  ? 8.753   30.368  21.505  1.00 31.04  ? 93  PHE D C   1 
ATOM   3915  O O   . PHE B 1 64  ? 8.017   31.266  21.914  1.00 31.36  ? 93  PHE D O   1 
ATOM   3916  C CB  . PHE B 1 64  ? 10.046  30.172  23.649  1.00 29.51  ? 93  PHE D CB  1 
ATOM   3917  C CG  . PHE B 1 64  ? 11.385  30.028  24.343  1.00 31.62  ? 93  PHE D CG  1 
ATOM   3918  C CD1 . PHE B 1 64  ? 12.263  29.010  23.995  1.00 34.80  ? 93  PHE D CD1 1 
ATOM   3919  C CD2 . PHE B 1 64  ? 11.728  30.861  25.400  1.00 33.64  ? 93  PHE D CD2 1 
ATOM   3920  C CE1 . PHE B 1 64  ? 13.484  28.882  24.625  1.00 34.76  ? 93  PHE D CE1 1 
ATOM   3921  C CE2 . PHE B 1 64  ? 12.937  30.695  26.061  1.00 36.17  ? 93  PHE D CE2 1 
ATOM   3922  C CZ  . PHE B 1 64  ? 13.813  29.714  25.677  1.00 35.74  ? 93  PHE D CZ  1 
ATOM   3923  N N   . ARG B 1 65  ? 8.473   29.575  20.468  1.00 30.11  ? 94  ARG D N   1 
ATOM   3924  C CA  . ARG B 1 65  ? 7.246   29.707  19.706  1.00 32.01  ? 94  ARG D CA  1 
ATOM   3925  C C   . ARG B 1 65  ? 6.991   31.170  19.370  1.00 34.62  ? 94  ARG D C   1 
ATOM   3926  O O   . ARG B 1 65  ? 5.910   31.658  19.644  1.00 34.14  ? 94  ARG D O   1 
ATOM   3927  C CB  . ARG B 1 65  ? 6.044   29.254  20.534  1.00 31.47  ? 94  ARG D CB  1 
ATOM   3928  C CG  . ARG B 1 65  ? 6.022   27.757  20.790  1.00 29.40  ? 94  ARG D CG  1 
ATOM   3929  C CD  . ARG B 1 65  ? 5.812   27.011  19.452  1.00 28.36  ? 94  ARG D CD  1 
ATOM   3930  N NE  . ARG B 1 65  ? 5.596   25.598  19.807  1.00 29.02  ? 94  ARG D NE  1 
ATOM   3931  C CZ  . ARG B 1 65  ? 5.141   24.652  18.994  1.00 33.65  ? 94  ARG D CZ  1 
ATOM   3932  N NH1 . ARG B 1 65  ? 4.800   24.957  17.753  1.00 28.22  ? 94  ARG D NH1 1 
ATOM   3933  N NH2 . ARG B 1 65  ? 5.024   23.406  19.434  1.00 36.24  ? 94  ARG D NH2 1 
ATOM   3934  N N   . GLY B 1 66  ? 8.015   31.863  18.871  1.00 35.74  ? 95  GLY D N   1 
ATOM   3935  C CA  . GLY B 1 66  ? 7.876   33.246  18.460  1.00 32.41  ? 95  GLY D CA  1 
ATOM   3936  C C   . GLY B 1 66  ? 8.216   34.269  19.558  1.00 34.06  ? 95  GLY D C   1 
ATOM   3937  O O   . GLY B 1 66  ? 8.467   35.425  19.219  1.00 36.32  ? 95  GLY D O   1 
ATOM   3938  N N   . PHE B 1 67  ? 8.220   33.876  20.845  1.00 30.81  ? 96  PHE D N   1 
ATOM   3939  C CA  . PHE B 1 67  ? 8.454   34.808  21.943  1.00 32.50  ? 96  PHE D CA  1 
ATOM   3940  C C   . PHE B 1 67  ? 9.938   34.811  22.341  1.00 37.12  ? 96  PHE D C   1 
ATOM   3941  O O   . PHE B 1 67  ? 10.528  33.766  22.639  1.00 36.43  ? 96  PHE D O   1 
ATOM   3942  C CB  . PHE B 1 67  ? 7.591   34.493  23.167  1.00 32.94  ? 96  PHE D CB  1 
ATOM   3943  C CG  . PHE B 1 67  ? 6.098   34.561  22.896  1.00 36.61  ? 96  PHE D CG  1 
ATOM   3944  C CD1 . PHE B 1 67  ? 5.430   33.500  22.304  1.00 34.44  ? 96  PHE D CD1 1 
ATOM   3945  C CD2 . PHE B 1 67  ? 5.385   35.737  23.141  1.00 41.38  ? 96  PHE D CD2 1 
ATOM   3946  C CE1 . PHE B 1 67  ? 4.073   33.580  22.030  1.00 34.55  ? 96  PHE D CE1 1 
ATOM   3947  C CE2 . PHE B 1 67  ? 4.034   35.822  22.856  1.00 42.56  ? 96  PHE D CE2 1 
ATOM   3948  C CZ  . PHE B 1 67  ? 3.373   34.734  22.319  1.00 41.54  ? 96  PHE D CZ  1 
ATOM   3949  N N   . SER B 1 68  ? 10.539  36.012  22.351  1.00 35.45  ? 97  SER D N   1 
ATOM   3950  C CA  . SER B 1 68  ? 11.885  36.257  22.860  1.00 33.68  ? 97  SER D CA  1 
ATOM   3951  C C   . SER B 1 68  ? 11.917  36.082  24.373  1.00 32.36  ? 97  SER D C   1 
ATOM   3952  O O   . SER B 1 68  ? 10.883  36.125  25.029  1.00 34.38  ? 97  SER D O   1 
ATOM   3953  C CB  . SER B 1 68  ? 12.321  37.655  22.531  1.00 35.91  ? 97  SER D CB  1 
ATOM   3954  O OG  . SER B 1 68  ? 11.625  38.566  23.388  1.00 38.32  ? 97  SER D OG  1 
ATOM   3955  N N   . ILE B 1 69  ? 13.119  35.982  24.946  1.00 32.11  ? 98  ILE D N   1 
ATOM   3956  C CA  . ILE B 1 69  ? 13.238  35.865  26.398  1.00 35.41  ? 98  ILE D CA  1 
ATOM   3957  C C   . ILE B 1 69  ? 12.606  37.072  27.117  1.00 36.60  ? 98  ILE D C   1 
ATOM   3958  O O   . ILE B 1 69  ? 11.793  36.895  28.027  1.00 32.98  ? 98  ILE D O   1 
ATOM   3959  C CB  . ILE B 1 69  ? 14.701  35.574  26.803  1.00 36.71  ? 98  ILE D CB  1 
ATOM   3960  C CG1 . ILE B 1 69  ? 15.036  34.092  26.489  1.00 35.09  ? 98  ILE D CG1 1 
ATOM   3961  C CG2 . ILE B 1 69  ? 14.958  35.924  28.267  1.00 38.01  ? 98  ILE D CG2 1 
ATOM   3962  C CD1 . ILE B 1 69  ? 16.489  33.743  26.621  1.00 41.66  ? 98  ILE D CD1 1 
ATOM   3963  N N   . PRO B 1 70  ? 12.943  38.330  26.763  1.00 35.06  ? 99  PRO D N   1 
ATOM   3964  C CA  . PRO B 1 70  ? 12.287  39.497  27.359  1.00 39.38  ? 99  PRO D CA  1 
ATOM   3965  C C   . PRO B 1 70  ? 10.764  39.449  27.307  1.00 37.57  ? 99  PRO D C   1 
ATOM   3966  O O   . PRO B 1 70  ? 10.139  39.815  28.289  1.00 39.71  ? 99  PRO D O   1 
ATOM   3967  C CB  . PRO B 1 70  ? 12.851  40.697  26.547  1.00 42.32  ? 99  PRO D CB  1 
ATOM   3968  C CG  . PRO B 1 70  ? 14.193  40.217  26.036  1.00 39.14  ? 99  PRO D CG  1 
ATOM   3969  C CD  . PRO B 1 70  ? 14.049  38.709  25.867  1.00 42.56  ? 99  PRO D CD  1 
ATOM   3970  N N   . GLU B 1 71  ? 10.176  38.935  26.205  1.00 38.06  ? 100 GLU D N   1 
ATOM   3971  C CA  . GLU B 1 71  ? 8.726   38.802  26.112  1.00 35.42  ? 100 GLU D CA  1 
ATOM   3972  C C   . GLU B 1 71  ? 8.202   37.733  27.077  1.00 45.06  ? 100 GLU D C   1 
ATOM   3973  O O   . GLU B 1 71  ? 7.184   37.936  27.757  1.00 42.96  ? 100 GLU D O   1 
ATOM   3974  C CB  . GLU B 1 71  ? 8.344   38.532  24.670  1.00 42.29  ? 100 GLU D CB  1 
ATOM   3975  C CG  . GLU B 1 71  ? 8.652   39.721  23.766  1.00 47.04  ? 100 GLU D CG  1 
ATOM   3976  C CD  . GLU B 1 71  ? 8.396   39.408  22.298  1.00 54.00  ? 100 GLU D CD  1 
ATOM   3977  O OE1 . GLU B 1 71  ? 8.817   38.325  21.824  1.00 53.80  ? 100 GLU D OE1 1 
ATOM   3978  O OE2 . GLU B 1 71  ? 7.782   40.254  21.615  1.00 62.88  ? 100 GLU D OE2 1 
ATOM   3979  N N   . CYS B 1 72  ? 8.929   36.608  27.178  1.00 38.26  ? 101 CYS D N   1 
ATOM   3980  C CA  . CYS B 1 72  ? 8.557   35.554  28.112  1.00 38.02  ? 101 CYS D CA  1 
ATOM   3981  C C   . CYS B 1 72  ? 8.668   36.048  29.550  1.00 37.15  ? 101 CYS D C   1 
ATOM   3982  O O   . CYS B 1 72  ? 7.802   35.721  30.368  1.00 37.93  ? 101 CYS D O   1 
ATOM   3983  C CB  . CYS B 1 72  ? 9.412   34.299  27.945  1.00 38.79  ? 101 CYS D CB  1 
ATOM   3984  S SG  . CYS B 1 72  ? 9.111   33.445  26.375  1.00 36.15  ? 101 CYS D SG  1 
ATOM   3985  N N   . GLN B 1 73  ? 9.741   36.805  29.840  1.00 34.80  ? 102 GLN D N   1 
ATOM   3986  C CA  . GLN B 1 73  ? 9.915   37.431  31.141  1.00 42.15  ? 102 GLN D CA  1 
ATOM   3987  C C   . GLN B 1 73  ? 8.725   38.333  31.449  1.00 37.14  ? 102 GLN D C   1 
ATOM   3988  O O   . GLN B 1 73  ? 8.219   38.312  32.560  1.00 43.42  ? 102 GLN D O   1 
ATOM   3989  C CB  . GLN B 1 73  ? 11.229  38.195  31.279  1.00 43.85  ? 102 GLN D CB  1 
ATOM   3990  C CG  . GLN B 1 73  ? 12.353  37.365  31.877  1.00 46.76  ? 102 GLN D CG  1 
ATOM   3991  C CD  . GLN B 1 73  ? 13.627  38.163  32.084  1.00 53.60  ? 102 GLN D CD  1 
ATOM   3992  O OE1 . GLN B 1 73  ? 14.153  38.803  31.163  1.00 49.24  ? 102 GLN D OE1 1 
ATOM   3993  N NE2 . GLN B 1 73  ? 14.146  38.122  33.303  1.00 60.35  ? 102 GLN D NE2 1 
ATOM   3994  N N   . LYS B 1 74  ? 8.252   39.068  30.456  1.00 40.93  ? 103 LYS D N   1 
ATOM   3995  C CA  . LYS B 1 74  ? 7.093   39.928  30.624  1.00 45.18  ? 103 LYS D CA  1 
ATOM   3996  C C   . LYS B 1 74  ? 5.799   39.114  30.755  1.00 42.33  ? 103 LYS D C   1 
ATOM   3997  O O   . LYS B 1 74  ? 4.990   39.405  31.641  1.00 39.16  ? 103 LYS D O   1 
ATOM   3998  C CB  . LYS B 1 74  ? 7.038   40.927  29.459  1.00 50.65  ? 103 LYS D CB  1 
ATOM   3999  C CG  . LYS B 1 74  ? 6.029   42.084  29.600  1.00 64.37  ? 103 LYS D CG  1 
ATOM   4000  C CD  . LYS B 1 74  ? 5.940   43.080  28.434  1.00 71.04  ? 103 LYS D CD  1 
ATOM   4001  C CE  . LYS B 1 74  ? 7.257   43.642  27.945  1.00 76.65  ? 103 LYS D CE  1 
ATOM   4002  N NZ  . LYS B 1 74  ? 7.914   42.802  26.930  1.00 77.90  ? 103 LYS D NZ  1 
ATOM   4003  N N   . LEU B 1 75  ? 5.575   38.120  29.869  1.00 39.87  ? 104 LEU D N   1 
ATOM   4004  C CA  . LEU B 1 75  ? 4.226   37.586  29.670  1.00 37.84  ? 104 LEU D CA  1 
ATOM   4005  C C   . LEU B 1 75  ? 3.928   36.373  30.540  1.00 35.61  ? 104 LEU D C   1 
ATOM   4006  O O   . LEU B 1 75  ? 2.772   36.142  30.885  1.00 34.77  ? 104 LEU D O   1 
ATOM   4007  C CB  . LEU B 1 75  ? 3.976   37.273  28.200  1.00 40.81  ? 104 LEU D CB  1 
ATOM   4008  C CG  . LEU B 1 75  ? 3.996   38.487  27.262  1.00 45.21  ? 104 LEU D CG  1 
ATOM   4009  C CD1 . LEU B 1 75  ? 4.167   38.083  25.802  1.00 46.09  ? 104 LEU D CD1 1 
ATOM   4010  C CD2 . LEU B 1 75  ? 2.731   39.301  27.433  1.00 49.99  ? 104 LEU D CD2 1 
ATOM   4011  N N   . LEU B 1 76  ? 4.937   35.552  30.832  1.00 38.36  ? 105 LEU D N   1 
ATOM   4012  C CA  . LEU B 1 76  ? 4.684   34.271  31.473  1.00 36.29  ? 105 LEU D CA  1 
ATOM   4013  C C   . LEU B 1 76  ? 4.288   34.499  32.927  1.00 39.69  ? 105 LEU D C   1 
ATOM   4014  O O   . LEU B 1 76  ? 4.809   35.413  33.551  1.00 38.00  ? 105 LEU D O   1 
ATOM   4015  C CB  . LEU B 1 76  ? 5.906   33.368  31.346  1.00 35.24  ? 105 LEU D CB  1 
ATOM   4016  C CG  . LEU B 1 76  ? 6.190   32.859  29.927  1.00 35.64  ? 105 LEU D CG  1 
ATOM   4017  C CD1 . LEU B 1 76  ? 7.436   31.990  29.997  1.00 36.15  ? 105 LEU D CD1 1 
ATOM   4018  C CD2 . LEU B 1 76  ? 4.994   32.079  29.364  1.00 32.56  ? 105 LEU D CD2 1 
ATOM   4019  N N   . PRO B 1 77  ? 3.327   33.723  33.495  1.00 36.18  ? 106 PRO D N   1 
ATOM   4020  C CA  . PRO B 1 77  ? 3.009   33.850  34.914  1.00 40.21  ? 106 PRO D CA  1 
ATOM   4021  C C   . PRO B 1 77  ? 4.228   33.616  35.811  1.00 43.88  ? 106 PRO D C   1 
ATOM   4022  O O   . PRO B 1 77  ? 5.116   32.834  35.463  1.00 38.38  ? 106 PRO D O   1 
ATOM   4023  C CB  . PRO B 1 77  ? 1.932   32.803  35.167  1.00 40.85  ? 106 PRO D CB  1 
ATOM   4024  C CG  . PRO B 1 77  ? 1.375   32.488  33.796  1.00 38.22  ? 106 PRO D CG  1 
ATOM   4025  C CD  . PRO B 1 77  ? 2.491   32.736  32.804  1.00 34.82  ? 106 PRO D CD  1 
ATOM   4026  N N   . LYS B 1 78  ? 4.165   34.240  37.002  1.00 34.47  ? 107 LYS D N   1 
ATOM   4027  C CA  . LYS B 1 78  ? 5.207   34.257  38.009  1.00 32.41  ? 107 LYS D CA  1 
ATOM   4028  C C   . LYS B 1 78  ? 4.634   33.542  39.221  1.00 32.90  ? 107 LYS D C   1 
ATOM   4029  O O   . LYS B 1 78  ? 3.442   33.292  39.263  1.00 32.41  ? 107 LYS D O   1 
ATOM   4030  C CB  . LYS B 1 78  ? 5.536   35.744  38.133  1.00 38.97  ? 107 LYS D CB  1 
ATOM   4031  C CG  . LYS B 1 78  ? 6.168   36.334  36.871  1.00 39.92  ? 107 LYS D CG  1 
ATOM   4032  C CD  . LYS B 1 78  ? 6.131   37.848  36.756  1.00 55.12  ? 107 LYS D CD  1 
ATOM   4033  C CE  . LYS B 1 78  ? 6.901   38.386  35.578  1.00 56.42  ? 107 LYS D CE  1 
ATOM   4034  N NZ  . LYS B 1 78  ? 6.696   37.558  34.387  1.00 62.88  ? 107 LYS D NZ  1 
ATOM   4035  N N   . ALA B 1 79  ? 5.476   33.111  40.155  1.00 37.87  ? 108 ALA D N   1 
ATOM   4036  C CA  . ALA B 1 79  ? 4.983   32.753  41.478  1.00 42.12  ? 108 ALA D CA  1 
ATOM   4037  C C   . ALA B 1 79  ? 4.300   33.968  42.122  1.00 48.21  ? 108 ALA D C   1 
ATOM   4038  O O   . ALA B 1 79  ? 4.577   35.120  41.752  1.00 38.46  ? 108 ALA D O   1 
ATOM   4039  C CB  . ALA B 1 79  ? 6.134   32.281  42.330  1.00 43.55  ? 108 ALA D CB  1 
ATOM   4040  N N   . LYS B 1 80  ? 3.421   33.692  43.095  1.00 45.08  ? 109 LYS D N   1 
ATOM   4041  C CA  . LYS B 1 80  ? 2.872   34.723  43.967  1.00 51.08  ? 109 LYS D CA  1 
ATOM   4042  C C   . LYS B 1 80  ? 4.006   35.460  44.675  1.00 49.91  ? 109 LYS D C   1 
ATOM   4043  O O   . LYS B 1 80  ? 4.642   34.916  45.576  1.00 56.20  ? 109 LYS D O   1 
ATOM   4044  C CB  . LYS B 1 80  ? 1.896   34.132  44.991  1.00 53.66  ? 109 LYS D CB  1 
ATOM   4045  C CG  . LYS B 1 80  ? 0.698   33.408  44.385  1.00 58.05  ? 109 LYS D CG  1 
ATOM   4046  C CD  . LYS B 1 80  ? 0.084   34.148  43.194  1.00 61.37  ? 109 LYS D CD  1 
ATOM   4047  C CE  . LYS B 1 80  ? -1.006  33.353  42.568  1.00 59.55  ? 109 LYS D CE  1 
ATOM   4048  N NZ  . LYS B 1 80  ? -1.926  32.940  43.623  1.00 57.17  ? 109 LYS D NZ  1 
ATOM   4049  N N   . GLY B 1 81  ? 4.231   36.704  44.248  1.00 46.35  ? 110 GLY D N   1 
ATOM   4050  C CA  . GLY B 1 81  ? 5.213   37.582  44.862  1.00 56.04  ? 110 GLY D CA  1 
ATOM   4051  C C   . GLY B 1 81  ? 6.557   37.573  44.133  1.00 59.61  ? 110 GLY D C   1 
ATOM   4052  O O   . GLY B 1 81  ? 7.486   38.248  44.573  1.00 55.86  ? 110 GLY D O   1 
ATOM   4053  N N   . GLY B 1 82  ? 6.654   36.810  43.027  1.00 56.70  ? 111 GLY D N   1 
ATOM   4054  C CA  . GLY B 1 82  ? 7.910   36.656  42.308  1.00 51.04  ? 111 GLY D CA  1 
ATOM   4055  C C   . GLY B 1 82  ? 7.964   37.541  41.065  1.00 45.59  ? 111 GLY D C   1 
ATOM   4056  O O   . GLY B 1 82  ? 6.969   38.129  40.672  1.00 45.46  ? 111 GLY D O   1 
ATOM   4057  N N   . GLU B 1 83  ? 9.146   37.644  40.455  1.00 43.51  ? 112 GLU D N   1 
ATOM   4058  C CA  . GLU B 1 83  ? 9.316   38.357  39.203  1.00 43.69  ? 112 GLU D CA  1 
ATOM   4059  C C   . GLU B 1 83  ? 9.714   37.377  38.092  1.00 39.08  ? 112 GLU D C   1 
ATOM   4060  O O   . GLU B 1 83  ? 9.779   37.733  36.932  1.00 44.34  ? 112 GLU D O   1 
ATOM   4061  C CB  . GLU B 1 83  ? 10.407  39.417  39.380  1.00 50.27  ? 112 GLU D CB  1 
ATOM   4062  C CG  . GLU B 1 83  ? 11.818  38.822  39.391  1.00 62.44  ? 112 GLU D CG  1 
ATOM   4063  C CD  . GLU B 1 83  ? 13.038  39.720  39.646  1.00 73.62  ? 112 GLU D CD  1 
ATOM   4064  O OE1 . GLU B 1 83  ? 14.122  39.138  39.964  1.00 52.14  ? 112 GLU D OE1 1 
ATOM   4065  O OE2 . GLU B 1 83  ? 12.935  40.974  39.509  1.00 65.09  ? 112 GLU D OE2 1 
ATOM   4066  N N   . GLU B 1 84  ? 10.111  36.155  38.419  1.00 37.69  ? 113 GLU D N   1 
ATOM   4067  C CA  . GLU B 1 84  ? 10.762  35.343  37.395  1.00 38.95  ? 113 GLU D CA  1 
ATOM   4068  C C   . GLU B 1 84  ? 9.743   34.352  36.814  1.00 35.96  ? 113 GLU D C   1 
ATOM   4069  O O   . GLU B 1 84  ? 8.991   33.742  37.572  1.00 39.58  ? 113 GLU D O   1 
ATOM   4070  C CB  . GLU B 1 84  ? 12.016  34.700  37.995  1.00 35.21  ? 113 GLU D CB  1 
ATOM   4071  C CG  . GLU B 1 84  ? 13.123  35.688  38.363  1.00 38.66  ? 113 GLU D CG  1 
ATOM   4072  C CD  . GLU B 1 84  ? 13.600  36.644  37.274  1.00 40.03  ? 113 GLU D CD  1 
ATOM   4073  O OE1 . GLU B 1 84  ? 13.359  36.381  36.076  1.00 40.54  ? 113 GLU D OE1 1 
ATOM   4074  O OE2 . GLU B 1 84  ? 14.145  37.711  37.628  1.00 41.80  ? 113 GLU D OE2 1 
ATOM   4075  N N   . PRO B 1 85  ? 9.681   34.163  35.470  1.00 38.86  ? 114 PRO D N   1 
ATOM   4076  C CA  . PRO B 1 85  ? 8.700   33.268  34.831  1.00 35.44  ? 114 PRO D CA  1 
ATOM   4077  C C   . PRO B 1 85  ? 8.757   31.857  35.405  1.00 33.58  ? 114 PRO D C   1 
ATOM   4078  O O   . PRO B 1 85  ? 9.845   31.346  35.644  1.00 34.53  ? 114 PRO D O   1 
ATOM   4079  C CB  . PRO B 1 85  ? 9.099   33.289  33.340  1.00 35.88  ? 114 PRO D CB  1 
ATOM   4080  C CG  . PRO B 1 85  ? 10.535  33.778  33.320  1.00 36.48  ? 114 PRO D CG  1 
ATOM   4081  C CD  . PRO B 1 85  ? 10.584  34.777  34.479  1.00 40.48  ? 114 PRO D CD  1 
ATOM   4082  N N   . LEU B 1 86  ? 7.594   31.242  35.656  1.00 27.16  ? 115 LEU D N   1 
ATOM   4083  C CA  . LEU B 1 86  ? 7.580   29.841  36.030  1.00 30.26  ? 115 LEU D CA  1 
ATOM   4084  C C   . LEU B 1 86  ? 7.890   28.973  34.804  1.00 29.31  ? 115 LEU D C   1 
ATOM   4085  O O   . LEU B 1 86  ? 7.301   29.169  33.756  1.00 26.32  ? 115 LEU D O   1 
ATOM   4086  C CB  . LEU B 1 86  ? 6.249   29.475  36.676  1.00 32.12  ? 115 LEU D CB  1 
ATOM   4087  C CG  . LEU B 1 86  ? 5.869   30.333  37.882  1.00 38.57  ? 115 LEU D CG  1 
ATOM   4088  C CD1 . LEU B 1 86  ? 4.705   29.782  38.674  1.00 40.62  ? 115 LEU D CD1 1 
ATOM   4089  C CD2 . LEU B 1 86  ? 7.081   30.503  38.757  1.00 41.11  ? 115 LEU D CD2 1 
ATOM   4090  N N   . PRO B 1 87  ? 8.847   28.013  34.898  1.00 29.68  ? 116 PRO D N   1 
ATOM   4091  C CA  . PRO B 1 87  ? 9.095   27.018  33.841  1.00 30.79  ? 116 PRO D CA  1 
ATOM   4092  C C   . PRO B 1 87  ? 7.881   26.244  33.361  1.00 28.24  ? 116 PRO D C   1 
ATOM   4093  O O   . PRO B 1 87  ? 7.847   25.806  32.217  1.00 29.87  ? 116 PRO D O   1 
ATOM   4094  C CB  . PRO B 1 87  ? 10.104  26.039  34.464  1.00 30.30  ? 116 PRO D CB  1 
ATOM   4095  C CG  . PRO B 1 87  ? 10.726  26.777  35.608  1.00 31.15  ? 116 PRO D CG  1 
ATOM   4096  C CD  . PRO B 1 87  ? 9.745   27.847  36.037  1.00 28.81  ? 116 PRO D CD  1 
ATOM   4097  N N   . GLU B 1 88  ? 6.901   26.032  34.260  1.00 30.31  ? 117 GLU D N   1 
ATOM   4098  C CA  . GLU B 1 88  ? 5.632   25.450  33.863  1.00 30.96  ? 117 GLU D CA  1 
ATOM   4099  C C   . GLU B 1 88  ? 5.041   26.237  32.692  1.00 30.97  ? 117 GLU D C   1 
ATOM   4100  O O   . GLU B 1 88  ? 4.495   25.687  31.740  1.00 33.94  ? 117 GLU D O   1 
ATOM   4101  C CB  . GLU B 1 88  ? 4.568   25.497  34.954  1.00 30.65  ? 117 GLU D CB  1 
ATOM   4102  C CG  . GLU B 1 88  ? 4.815   24.570  36.139  1.00 30.35  ? 117 GLU D CG  1 
ATOM   4103  C CD  . GLU B 1 88  ? 5.603   25.118  37.325  1.00 31.29  ? 117 GLU D CD  1 
ATOM   4104  O OE1 . GLU B 1 88  ? 6.578   25.900  37.151  1.00 33.23  ? 117 GLU D OE1 1 
ATOM   4105  O OE2 . GLU B 1 88  ? 5.299   24.622  38.442  1.00 30.40  ? 117 GLU D OE2 1 
ATOM   4106  N N   . GLY B 1 89  ? 5.062   27.549  32.827  1.00 30.71  ? 118 GLY D N   1 
ATOM   4107  C CA  . GLY B 1 89  ? 4.370   28.386  31.874  1.00 30.16  ? 118 GLY D CA  1 
ATOM   4108  C C   . GLY B 1 89  ? 5.129   28.367  30.567  1.00 29.15  ? 118 GLY D C   1 
ATOM   4109  O O   . GLY B 1 89  ? 4.541   28.434  29.509  1.00 30.59  ? 118 GLY D O   1 
ATOM   4110  N N   . LEU B 1 90  ? 6.451   28.249  30.669  1.00 31.45  ? 119 LEU D N   1 
ATOM   4111  C CA  . LEU B 1 90  ? 7.268   28.050  29.494  1.00 29.97  ? 119 LEU D CA  1 
ATOM   4112  C C   . LEU B 1 90  ? 6.943   26.713  28.807  1.00 26.08  ? 119 LEU D C   1 
ATOM   4113  O O   . LEU B 1 90  ? 6.918   26.613  27.602  1.00 24.47  ? 119 LEU D O   1 
ATOM   4114  C CB  . LEU B 1 90  ? 8.738   28.144  29.869  1.00 31.40  ? 119 LEU D CB  1 
ATOM   4115  C CG  . LEU B 1 90  ? 9.639   27.593  28.772  1.00 34.42  ? 119 LEU D CG  1 
ATOM   4116  C CD1 . LEU B 1 90  ? 10.169  28.674  27.892  1.00 32.55  ? 119 LEU D CD1 1 
ATOM   4117  C CD2 . LEU B 1 90  ? 10.680  26.695  29.339  1.00 48.01  ? 119 LEU D CD2 1 
ATOM   4118  N N   . PHE B 1 91  ? 6.717   25.649  29.573  1.00 27.38  ? 120 PHE D N   1 
ATOM   4119  C CA  . PHE B 1 91  ? 6.411   24.373  28.969  1.00 29.35  ? 120 PHE D CA  1 
ATOM   4120  C C   . PHE B 1 91  ? 5.073   24.467  28.221  1.00 26.92  ? 120 PHE D C   1 
ATOM   4121  O O   . PHE B 1 91  ? 4.940   23.916  27.134  1.00 23.65  ? 120 PHE D O   1 
ATOM   4122  C CB  . PHE B 1 91  ? 6.405   23.268  30.031  1.00 27.05  ? 120 PHE D CB  1 
ATOM   4123  C CG  . PHE B 1 91  ? 6.056   21.904  29.466  1.00 27.30  ? 120 PHE D CG  1 
ATOM   4124  C CD1 . PHE B 1 91  ? 6.982   21.207  28.701  1.00 26.22  ? 120 PHE D CD1 1 
ATOM   4125  C CD2 . PHE B 1 91  ? 4.806   21.332  29.673  1.00 29.98  ? 120 PHE D CD2 1 
ATOM   4126  C CE1 . PHE B 1 91  ? 6.697   19.955  28.198  1.00 26.79  ? 120 PHE D CE1 1 
ATOM   4127  C CE2 . PHE B 1 91  ? 4.535   20.061  29.190  1.00 27.33  ? 120 PHE D CE2 1 
ATOM   4128  C CZ  . PHE B 1 91  ? 5.479   19.371  28.459  1.00 25.90  ? 120 PHE D CZ  1 
ATOM   4129  N N   . TRP B 1 92  ? 4.089   25.124  28.834  1.00 27.13  ? 121 TRP D N   1 
ATOM   4130  C CA  . TRP B 1 92  ? 2.783   25.323  28.227  1.00 27.07  ? 121 TRP D CA  1 
ATOM   4131  C C   . TRP B 1 92  ? 2.933   26.023  26.880  1.00 24.00  ? 121 TRP D C   1 
ATOM   4132  O O   . TRP B 1 92  ? 2.348   25.633  25.865  1.00 26.93  ? 121 TRP D O   1 
ATOM   4133  C CB  . TRP B 1 92  ? 1.893   26.181  29.144  1.00 24.96  ? 121 TRP D CB  1 
ATOM   4134  C CG  . TRP B 1 92  ? 0.465   26.212  28.679  1.00 23.57  ? 121 TRP D CG  1 
ATOM   4135  C CD1 . TRP B 1 92  ? -0.088  26.940  27.667  1.00 24.25  ? 121 TRP D CD1 1 
ATOM   4136  C CD2 . TRP B 1 92  ? -0.615  25.460  29.271  1.00 25.31  ? 121 TRP D CD2 1 
ATOM   4137  N NE1 . TRP B 1 92  ? -1.423  26.647  27.551  1.00 27.93  ? 121 TRP D NE1 1 
ATOM   4138  C CE2 . TRP B 1 92  ? -1.786  25.773  28.547  1.00 28.40  ? 121 TRP D CE2 1 
ATOM   4139  C CE3 . TRP B 1 92  ? -0.707  24.605  30.373  1.00 26.09  ? 121 TRP D CE3 1 
ATOM   4140  C CZ2 . TRP B 1 92  ? -3.019  25.223  28.880  1.00 27.97  ? 121 TRP D CZ2 1 
ATOM   4141  C CZ3 . TRP B 1 92  ? -1.925  24.038  30.676  1.00 27.61  ? 121 TRP D CZ3 1 
ATOM   4142  C CH2 . TRP B 1 92  ? -3.066  24.356  29.955  1.00 26.51  ? 121 TRP D CH2 1 
ATOM   4143  N N   . LEU B 1 93  ? 3.725   27.077  26.890  1.00 23.15  ? 122 LEU D N   1 
ATOM   4144  C CA  . LEU B 1 93  ? 3.976   27.839  25.670  1.00 23.64  ? 122 LEU D CA  1 
ATOM   4145  C C   . LEU B 1 93  ? 4.601   26.947  24.591  1.00 26.69  ? 122 LEU D C   1 
ATOM   4146  O O   . LEU B 1 93  ? 4.191   26.982  23.429  1.00 31.14  ? 122 LEU D O   1 
ATOM   4147  C CB  . LEU B 1 93  ? 4.898   28.998  25.992  1.00 23.62  ? 122 LEU D CB  1 
ATOM   4148  C CG  . LEU B 1 93  ? 5.438   29.733  24.764  1.00 22.87  ? 122 LEU D CG  1 
ATOM   4149  C CD1 . LEU B 1 93  ? 4.278   30.278  23.984  1.00 24.32  ? 122 LEU D CD1 1 
ATOM   4150  C CD2 . LEU B 1 93  ? 6.371   30.754  25.208  1.00 25.76  ? 122 LEU D CD2 1 
ATOM   4151  N N   . LEU B 1 94  ? 5.575   26.122  24.980  1.00 26.12  ? 123 LEU D N   1 
ATOM   4152  C CA  . LEU B 1 94  ? 6.261   25.266  24.013  1.00 27.54  ? 123 LEU D CA  1 
ATOM   4153  C C   . LEU B 1 94  ? 5.306   24.281  23.359  1.00 28.47  ? 123 LEU D C   1 
ATOM   4154  O O   . LEU B 1 94  ? 5.325   24.092  22.139  1.00 29.90  ? 123 LEU D O   1 
ATOM   4155  C CB  . LEU B 1 94  ? 7.430   24.565  24.696  1.00 26.27  ? 123 LEU D CB  1 
ATOM   4156  C CG  . LEU B 1 94  ? 8.568   25.499  25.115  1.00 28.65  ? 123 LEU D CG  1 
ATOM   4157  C CD1 . LEU B 1 94  ? 9.826   24.753  25.493  1.00 29.43  ? 123 LEU D CD1 1 
ATOM   4158  C CD2 . LEU B 1 94  ? 8.880   26.512  24.000  1.00 30.45  ? 123 LEU D CD2 1 
ATOM   4159  N N   . VAL B 1 95  ? 4.490   23.647  24.187  1.00 29.18  ? 124 VAL D N   1 
ATOM   4160  C CA  . VAL B 1 95  ? 3.527   22.665  23.741  1.00 33.95  ? 124 VAL D CA  1 
ATOM   4161  C C   . VAL B 1 95  ? 2.374   23.265  22.929  1.00 33.23  ? 124 VAL D C   1 
ATOM   4162  O O   . VAL B 1 95  ? 1.956   22.632  21.967  1.00 33.04  ? 124 VAL D O   1 
ATOM   4163  C CB  . VAL B 1 95  ? 2.999   21.922  24.972  1.00 35.31  ? 124 VAL D CB  1 
ATOM   4164  C CG1 . VAL B 1 95  ? 1.820   21.039  24.599  1.00 43.86  ? 124 VAL D CG1 1 
ATOM   4165  C CG2 . VAL B 1 95  ? 4.098   21.101  25.633  1.00 35.75  ? 124 VAL D CG2 1 
ATOM   4166  N N   . THR B 1 96  ? 1.824   24.421  23.346  1.00 30.34  ? 125 THR D N   1 
ATOM   4167  C CA  . THR B 1 96  ? 0.567   24.931  22.811  1.00 30.71  ? 125 THR D CA  1 
ATOM   4168  C C   . THR B 1 96  ? 0.832   26.059  21.808  1.00 31.69  ? 125 THR D C   1 
ATOM   4169  O O   . THR B 1 96  ? -0.010  26.320  20.955  1.00 29.24  ? 125 THR D O   1 
ATOM   4170  C CB  . THR B 1 96  ? -0.378  25.445  23.916  1.00 31.20  ? 125 THR D CB  1 
ATOM   4171  O OG1 . THR B 1 96  ? 0.255   26.574  24.515  1.00 25.32  ? 125 THR D OG1 1 
ATOM   4172  C CG2 . THR B 1 96  ? -0.696  24.404  24.975  1.00 30.78  ? 125 THR D CG2 1 
ATOM   4173  N N   . GLY B 1 97  ? 2.003   26.718  21.897  1.00 35.22  ? 126 GLY D N   1 
ATOM   4174  C CA  . GLY B 1 97  ? 2.291   27.901  21.095  1.00 33.71  ? 126 GLY D CA  1 
ATOM   4175  C C   . GLY B 1 97  ? 1.606   29.155  21.644  1.00 33.87  ? 126 GLY D C   1 
ATOM   4176  O O   . GLY B 1 97  ? 1.750   30.215  21.042  1.00 32.94  ? 126 GLY D O   1 
ATOM   4177  N N   . HIS B 1 98  ? 0.921   29.023  22.793  1.00 28.85  ? 127 HIS D N   1 
ATOM   4178  C CA  . HIS B 1 98  ? 0.182   30.107  23.430  1.00 31.77  ? 127 HIS D CA  1 
ATOM   4179  C C   . HIS B 1 98  ? 0.755   30.385  24.818  1.00 33.47  ? 127 HIS D C   1 
ATOM   4180  O O   . HIS B 1 98  ? 1.215   29.483  25.518  1.00 35.41  ? 127 HIS D O   1 
ATOM   4181  C CB  . HIS B 1 98  ? -1.302  29.758  23.663  1.00 35.65  ? 127 HIS D CB  1 
ATOM   4182  C CG  . HIS B 1 98  ? -2.113  29.561  22.420  1.00 47.38  ? 127 HIS D CG  1 
ATOM   4183  N ND1 . HIS B 1 98  ? -2.097  30.447  21.361  1.00 58.52  ? 127 HIS D ND1 1 
ATOM   4184  C CD2 . HIS B 1 98  ? -2.967  28.579  22.061  1.00 56.35  ? 127 HIS D CD2 1 
ATOM   4185  C CE1 . HIS B 1 98  ? -2.885  29.997  20.387  1.00 58.15  ? 127 HIS D CE1 1 
ATOM   4186  N NE2 . HIS B 1 98  ? -3.439  28.873  20.797  1.00 56.57  ? 127 HIS D NE2 1 
ATOM   4187  N N   . ILE B 1 99  ? 0.638   31.637  25.239  1.00 32.93  ? 128 ILE D N   1 
ATOM   4188  C CA  . ILE B 1 99  ? 0.921   32.048  26.600  1.00 34.98  ? 128 ILE D CA  1 
ATOM   4189  C C   . ILE B 1 99  ? -0.129  31.473  27.540  1.00 30.09  ? 128 ILE D C   1 
ATOM   4190  O O   . ILE B 1 99  ? -1.304  31.755  27.376  1.00 35.29  ? 128 ILE D O   1 
ATOM   4191  C CB  . ILE B 1 99  ? 0.969   33.587  26.657  1.00 35.12  ? 128 ILE D CB  1 
ATOM   4192  C CG1 . ILE B 1 99  ? 2.141   34.109  25.802  1.00 35.87  ? 128 ILE D CG1 1 
ATOM   4193  C CG2 . ILE B 1 99  ? 1.046   34.104  28.102  1.00 38.47  ? 128 ILE D CG2 1 
ATOM   4194  C CD1 . ILE B 1 99  ? 3.519   33.719  26.308  1.00 31.49  ? 128 ILE D CD1 1 
ATOM   4195  N N   . PRO B 1 100 ? 0.241   30.714  28.602  1.00 30.06  ? 129 PRO D N   1 
ATOM   4196  C CA  . PRO B 1 100 ? -0.755  30.238  29.551  1.00 30.15  ? 129 PRO D CA  1 
ATOM   4197  C C   . PRO B 1 100 ? -1.317  31.388  30.386  1.00 34.73  ? 129 PRO D C   1 
ATOM   4198  O O   . PRO B 1 100 ? -0.687  32.430  30.510  1.00 33.48  ? 129 PRO D O   1 
ATOM   4199  C CB  . PRO B 1 100 ? 0.036   29.278  30.433  1.00 29.57  ? 129 PRO D CB  1 
ATOM   4200  C CG  . PRO B 1 100 ? 1.429   29.839  30.445  1.00 29.50  ? 129 PRO D CG  1 
ATOM   4201  C CD  . PRO B 1 100 ? 1.615   30.445  29.056  1.00 25.48  ? 129 PRO D CD  1 
ATOM   4202  N N   . THR B 1 101 ? -2.494  31.161  30.971  1.00 32.69  ? 130 THR D N   1 
ATOM   4203  C CA  . THR B 1 101 ? -3.018  32.022  32.006  1.00 34.94  ? 130 THR D CA  1 
ATOM   4204  C C   . THR B 1 101 ? -2.426  31.512  33.309  1.00 40.66  ? 130 THR D C   1 
ATOM   4205  O O   . THR B 1 101 ? -1.833  30.424  33.313  1.00 40.76  ? 130 THR D O   1 
ATOM   4206  C CB  . THR B 1 101 ? -4.543  31.945  32.002  1.00 36.60  ? 130 THR D CB  1 
ATOM   4207  O OG1 . THR B 1 101 ? -4.848  30.586  32.311  1.00 35.53  ? 130 THR D OG1 1 
ATOM   4208  C CG2 . THR B 1 101 ? -5.145  32.300  30.653  1.00 40.29  ? 130 THR D CG2 1 
ATOM   4209  N N   . GLU B 1 102 ? -2.633  32.283  34.390  1.00 38.65  ? 131 GLU D N   1 
ATOM   4210  C CA  . GLU B 1 102 ? -2.171  31.918  35.720  1.00 45.68  ? 131 GLU D CA  1 
ATOM   4211  C C   . GLU B 1 102 ? -2.891  30.648  36.166  1.00 40.52  ? 131 GLU D C   1 
ATOM   4212  O O   . GLU B 1 102 ? -2.300  29.822  36.839  1.00 39.94  ? 131 GLU D O   1 
ATOM   4213  C CB  . GLU B 1 102 ? -2.333  33.027  36.775  1.00 51.54  ? 131 GLU D CB  1 
ATOM   4214  C CG  . GLU B 1 102 ? -1.865  34.401  36.302  1.00 61.57  ? 131 GLU D CG  1 
ATOM   4215  C CD  . GLU B 1 102 ? -0.956  35.184  37.236  1.00 71.01  ? 131 GLU D CD  1 
ATOM   4216  O OE1 . GLU B 1 102 ? -1.310  35.384  38.427  1.00 79.96  ? 131 GLU D OE1 1 
ATOM   4217  O OE2 . GLU B 1 102 ? 0.118   35.613  36.746  1.00 71.40  ? 131 GLU D OE2 1 
ATOM   4218  N N   . GLU B 1 103 ? -4.153  30.484  35.759  1.00 41.01  ? 132 GLU D N   1 
ATOM   4219  C CA  . GLU B 1 103 ? -4.896  29.278  36.099  1.00 45.36  ? 132 GLU D CA  1 
ATOM   4220  C C   . GLU B 1 103 ? -4.304  28.064  35.375  1.00 33.65  ? 132 GLU D C   1 
ATOM   4221  O O   . GLU B 1 103 ? -4.258  26.982  35.946  1.00 36.82  ? 132 GLU D O   1 
ATOM   4222  C CB  . GLU B 1 103 ? -6.421  29.377  35.932  1.00 55.12  ? 132 GLU D CB  1 
ATOM   4223  C CG  . GLU B 1 103 ? -6.926  30.623  35.204  1.00 66.45  ? 132 GLU D CG  1 
ATOM   4224  C CD  . GLU B 1 103 ? -6.764  31.933  35.971  1.00 68.23  ? 132 GLU D CD  1 
ATOM   4225  O OE1 . GLU B 1 103 ? -5.632  32.472  36.082  1.00 63.51  ? 132 GLU D OE1 1 
ATOM   4226  O OE2 . GLU B 1 103 ? -7.798  32.400  36.495  1.00 78.72  ? 132 GLU D OE2 1 
ATOM   4227  N N   . GLN B 1 104 ? -3.845  28.205  34.139  1.00 32.68  ? 133 GLN D N   1 
ATOM   4228  C CA  . GLN B 1 104 ? -3.229  27.062  33.456  1.00 33.43  ? 133 GLN D CA  1 
ATOM   4229  C C   . GLN B 1 104 ? -1.876  26.673  34.066  1.00 31.23  ? 133 GLN D C   1 
ATOM   4230  O O   . GLN B 1 104 ? -1.620  25.487  34.316  1.00 36.68  ? 133 GLN D O   1 
ATOM   4231  C CB  . GLN B 1 104 ? -3.177  27.344  31.964  1.00 31.88  ? 133 GLN D CB  1 
ATOM   4232  C CG  . GLN B 1 104 ? -4.560  27.319  31.325  1.00 33.79  ? 133 GLN D CG  1 
ATOM   4233  C CD  . GLN B 1 104 ? -4.606  28.000  29.979  1.00 31.06  ? 133 GLN D CD  1 
ATOM   4234  O OE1 . GLN B 1 104 ? -3.704  28.756  29.590  1.00 34.59  ? 133 GLN D OE1 1 
ATOM   4235  N NE2 . GLN B 1 104 ? -5.615  27.640  29.217  1.00 33.88  ? 133 GLN D NE2 1 
ATOM   4236  N N   . VAL B 1 105 ? -1.010  27.650  34.339  1.00 31.60  ? 134 VAL D N   1 
ATOM   4237  C CA  . VAL B 1 105 ? 0.244   27.348  35.016  1.00 36.31  ? 134 VAL D CA  1 
ATOM   4238  C C   . VAL B 1 105 ? -0.023  26.672  36.357  1.00 39.07  ? 134 VAL D C   1 
ATOM   4239  O O   . VAL B 1 105 ? 0.603   25.666  36.677  1.00 41.89  ? 134 VAL D O   1 
ATOM   4240  C CB  . VAL B 1 105 ? 1.078   28.627  35.153  1.00 38.62  ? 134 VAL D CB  1 
ATOM   4241  C CG1 . VAL B 1 105 ? 2.241   28.436  36.119  1.00 36.33  ? 134 VAL D CG1 1 
ATOM   4242  C CG2 . VAL B 1 105 ? 1.512   29.090  33.756  1.00 35.10  ? 134 VAL D CG2 1 
ATOM   4243  N N   . SER B 1 106 ? -1.006  27.174  37.113  1.00 37.66  ? 135 SER D N   1 
ATOM   4244  C CA  . SER B 1 106 ? -1.328  26.607  38.413  1.00 39.51  ? 135 SER D CA  1 
ATOM   4245  C C   . SER B 1 106 ? -1.803  25.144  38.319  1.00 33.51  ? 135 SER D C   1 
ATOM   4246  O O   . SER B 1 106 ? -1.353  24.309  39.086  1.00 42.58  ? 135 SER D O   1 
ATOM   4247  C CB  . SER B 1 106 ? -2.330  27.501  39.119  1.00 45.94  ? 135 SER D CB  1 
ATOM   4248  O OG  . SER B 1 106 ? -2.764  26.886  40.320  1.00 49.33  ? 135 SER D OG  1 
ATOM   4249  N N   . TRP B 1 107 ? -2.756  24.826  37.445  1.00 30.54  ? 136 TRP D N   1 
ATOM   4250  C CA  . TRP B 1 107 ? -3.088  23.444  37.096  1.00 33.67  ? 136 TRP D CA  1 
ATOM   4251  C C   . TRP B 1 107 ? -1.849  22.606  36.754  1.00 29.67  ? 136 TRP D C   1 
ATOM   4252  O O   . TRP B 1 107 ? -1.736  21.467  37.174  1.00 32.00  ? 136 TRP D O   1 
ATOM   4253  C CB  . TRP B 1 107 ? -4.079  23.424  35.914  1.00 33.26  ? 136 TRP D CB  1 
ATOM   4254  C CG  . TRP B 1 107 ? -4.458  22.052  35.432  1.00 32.91  ? 136 TRP D CG  1 
ATOM   4255  C CD1 . TRP B 1 107 ? -5.541  21.333  35.842  1.00 37.49  ? 136 TRP D CD1 1 
ATOM   4256  C CD2 . TRP B 1 107 ? -3.778  21.233  34.454  1.00 33.44  ? 136 TRP D CD2 1 
ATOM   4257  N NE1 . TRP B 1 107 ? -5.593  20.140  35.168  1.00 37.99  ? 136 TRP D NE1 1 
ATOM   4258  C CE2 . TRP B 1 107 ? -4.512  20.034  34.336  1.00 36.48  ? 136 TRP D CE2 1 
ATOM   4259  C CE3 . TRP B 1 107 ? -2.632  21.382  33.674  1.00 37.12  ? 136 TRP D CE3 1 
ATOM   4260  C CZ2 . TRP B 1 107 ? -4.125  19.001  33.489  1.00 35.97  ? 136 TRP D CZ2 1 
ATOM   4261  C CZ3 . TRP B 1 107 ? -2.231  20.350  32.854  1.00 34.57  ? 136 TRP D CZ3 1 
ATOM   4262  C CH2 . TRP B 1 107 ? -2.956  19.169  32.776  1.00 36.66  ? 136 TRP D CH2 1 
ATOM   4263  N N   . LEU B 1 108 ? -0.935  23.125  35.938  1.00 29.92  ? 137 LEU D N   1 
ATOM   4264  C CA  . LEU B 1 108 ? 0.241   22.347  35.554  1.00 31.01  ? 137 LEU D CA  1 
ATOM   4265  C C   . LEU B 1 108 ? 1.159   22.050  36.738  1.00 29.75  ? 137 LEU D C   1 
ATOM   4266  O O   . LEU B 1 108 ? 1.671   20.923  36.809  1.00 32.57  ? 137 LEU D O   1 
ATOM   4267  C CB  . LEU B 1 108 ? 1.036   23.039  34.460  1.00 31.13  ? 137 LEU D CB  1 
ATOM   4268  C CG  . LEU B 1 108 ? 2.166   22.229  33.823  1.00 27.93  ? 137 LEU D CG  1 
ATOM   4269  C CD1 . LEU B 1 108 ? 1.673   20.873  33.351  1.00 27.85  ? 137 LEU D CD1 1 
ATOM   4270  C CD2 . LEU B 1 108 ? 2.669   23.079  32.657  1.00 30.01  ? 137 LEU D CD2 1 
ATOM   4271  N N   . SER B 1 109 ? 1.372   23.023  37.648  1.00 30.13  ? 138 SER D N   1 
ATOM   4272  C CA  . SER B 1 109 ? 2.147   22.779  38.861  1.00 29.88  ? 138 SER D CA  1 
ATOM   4273  C C   . SER B 1 109 ? 1.532   21.599  39.625  1.00 31.86  ? 138 SER D C   1 
ATOM   4274  O O   . SER B 1 109 ? 2.233   20.708  40.126  1.00 28.86  ? 138 SER D O   1 
ATOM   4275  C CB  . SER B 1 109 ? 2.211   23.997  39.777  1.00 31.53  ? 138 SER D CB  1 
ATOM   4276  O OG  . SER B 1 109 ? 2.812   25.137  39.173  1.00 33.54  ? 138 SER D OG  1 
ATOM   4277  N N   . LYS B 1 110 ? 0.195   21.587  39.731  1.00 32.35  ? 139 LYS D N   1 
ATOM   4278  C CA  . LYS B 1 110 ? -0.469  20.573  40.555  1.00 33.68  ? 139 LYS D CA  1 
ATOM   4279  C C   . LYS B 1 110 ? -0.291  19.220  39.870  1.00 33.44  ? 139 LYS D C   1 
ATOM   4280  O O   . LYS B 1 110 ? -0.085  18.181  40.503  1.00 39.01  ? 139 LYS D O   1 
ATOM   4281  C CB  . LYS B 1 110 ? -1.966  20.815  40.782  1.00 36.59  ? 139 LYS D CB  1 
ATOM   4282  C CG  . LYS B 1 110 ? -2.399  21.532  42.064  1.00 46.61  ? 139 LYS D CG  1 
ATOM   4283  C CD  . LYS B 1 110 ? -2.116  23.025  42.099  1.00 55.43  ? 139 LYS D CD  1 
ATOM   4284  C CE  . LYS B 1 110 ? -3.139  23.820  42.878  1.00 60.28  ? 139 LYS D CE  1 
ATOM   4285  N NZ  . LYS B 1 110 ? -4.249  24.270  42.026  1.00 62.01  ? 139 LYS D NZ  1 
ATOM   4286  N N   . GLU B 1 111 ? -0.365  19.236  38.552  1.00 29.36  ? 140 GLU D N   1 
ATOM   4287  C CA  . GLU B 1 111 ? -0.266  17.993  37.812  1.00 34.80  ? 140 GLU D CA  1 
ATOM   4288  C C   . GLU B 1 111 ? 1.149   17.429  37.977  1.00 32.86  ? 140 GLU D C   1 
ATOM   4289  O O   . GLU B 1 111 ? 1.319   16.235  38.182  1.00 33.93  ? 140 GLU D O   1 
ATOM   4290  C CB  . GLU B 1 111 ? -0.676  18.310  36.378  1.00 41.80  ? 140 GLU D CB  1 
ATOM   4291  C CG  . GLU B 1 111 ? -0.917  17.052  35.553  1.00 54.95  ? 140 GLU D CG  1 
ATOM   4292  C CD  . GLU B 1 111 ? -2.234  16.350  35.818  1.00 53.74  ? 140 GLU D CD  1 
ATOM   4293  O OE1 . GLU B 1 111 ? -3.055  16.794  36.673  1.00 42.13  ? 140 GLU D OE1 1 
ATOM   4294  O OE2 . GLU B 1 111 ? -2.400  15.345  35.088  1.00 57.85  ? 140 GLU D OE2 1 
ATOM   4295  N N   . TRP B 1 112 ? 2.173   18.287  37.931  1.00 30.83  ? 141 TRP D N   1 
ATOM   4296  C CA  . TRP B 1 112 ? 3.529   17.793  38.067  1.00 30.91  ? 141 TRP D CA  1 
ATOM   4297  C C   . TRP B 1 112 ? 3.827   17.328  39.496  1.00 36.92  ? 141 TRP D C   1 
ATOM   4298  O O   . TRP B 1 112 ? 4.499   16.321  39.653  1.00 35.47  ? 141 TRP D O   1 
ATOM   4299  C CB  . TRP B 1 112 ? 4.576   18.791  37.579  1.00 27.38  ? 141 TRP D CB  1 
ATOM   4300  C CG  . TRP B 1 112 ? 4.639   18.930  36.088  1.00 27.81  ? 141 TRP D CG  1 
ATOM   4301  C CD1 . TRP B 1 112 ? 4.075   18.139  35.133  1.00 32.52  ? 141 TRP D CD1 1 
ATOM   4302  C CD2 . TRP B 1 112 ? 5.312   19.983  35.377  1.00 31.67  ? 141 TRP D CD2 1 
ATOM   4303  N NE1 . TRP B 1 112 ? 4.311   18.647  33.880  1.00 34.41  ? 141 TRP D NE1 1 
ATOM   4304  C CE2 . TRP B 1 112 ? 5.079   19.768  33.996  1.00 33.61  ? 141 TRP D CE2 1 
ATOM   4305  C CE3 . TRP B 1 112 ? 6.090   21.071  35.772  1.00 33.83  ? 141 TRP D CE3 1 
ATOM   4306  C CZ2 . TRP B 1 112 ? 5.602   20.604  33.014  1.00 30.42  ? 141 TRP D CZ2 1 
ATOM   4307  C CZ3 . TRP B 1 112 ? 6.633   21.882  34.799  1.00 33.38  ? 141 TRP D CZ3 1 
ATOM   4308  C CH2 . TRP B 1 112 ? 6.351   21.673  33.443  1.00 32.34  ? 141 TRP D CH2 1 
ATOM   4309  N N   . ALA B 1 113 ? 3.300   18.007  40.520  1.00 35.12  ? 142 ALA D N   1 
ATOM   4310  C CA  . ALA B 1 113 ? 3.474   17.568  41.892  1.00 34.55  ? 142 ALA D CA  1 
ATOM   4311  C C   . ALA B 1 113 ? 2.815   16.208  42.133  1.00 34.70  ? 142 ALA D C   1 
ATOM   4312  O O   . ALA B 1 113 ? 3.373   15.406  42.872  1.00 32.48  ? 142 ALA D O   1 
ATOM   4313  C CB  . ALA B 1 113 ? 2.946   18.621  42.846  1.00 38.79  ? 142 ALA D CB  1 
ATOM   4314  N N   . LYS B 1 114 ? 1.692   15.911  41.464  1.00 31.67  ? 143 LYS D N   1 
ATOM   4315  C CA  . LYS B 1 114 ? 0.992   14.664  41.709  1.00 35.63  ? 143 LYS D CA  1 
ATOM   4316  C C   . LYS B 1 114 ? 1.647   13.465  41.014  1.00 34.36  ? 143 LYS D C   1 
ATOM   4317  O O   . LYS B 1 114 ? 1.422   12.351  41.462  1.00 33.22  ? 143 LYS D O   1 
ATOM   4318  C CB  . LYS B 1 114 ? -0.500  14.740  41.387  1.00 40.84  ? 143 LYS D CB  1 
ATOM   4319  C CG  . LYS B 1 114 ? -0.977  14.331  40.000  1.00 52.08  ? 143 LYS D CG  1 
ATOM   4320  C CD  . LYS B 1 114 ? -2.430  14.734  39.746  1.00 55.51  ? 143 LYS D CD  1 
ATOM   4321  C CE  . LYS B 1 114 ? -2.851  15.986  40.492  1.00 57.42  ? 143 LYS D CE  1 
ATOM   4322  N NZ  . LYS B 1 114 ? -4.202  16.426  40.147  1.00 58.85  ? 143 LYS D NZ  1 
ATOM   4323  N N   . ARG B 1 115 ? 2.504   13.673  40.011  1.00 32.46  ? 144 ARG D N   1 
ATOM   4324  C CA  . ARG B 1 115 ? 3.179   12.578  39.320  1.00 32.61  ? 144 ARG D CA  1 
ATOM   4325  C C   . ARG B 1 115 ? 4.618   12.342  39.796  1.00 30.90  ? 144 ARG D C   1 
ATOM   4326  O O   . ARG B 1 115 ? 5.327   11.498  39.252  1.00 32.41  ? 144 ARG D O   1 
ATOM   4327  C CB  . ARG B 1 115 ? 3.216   12.908  37.823  1.00 34.18  ? 144 ARG D CB  1 
ATOM   4328  C CG  . ARG B 1 115 ? 1.877   13.036  37.121  1.00 30.36  ? 144 ARG D CG  1 
ATOM   4329  C CD  . ARG B 1 115 ? 1.995   13.808  35.818  1.00 35.02  ? 144 ARG D CD  1 
ATOM   4330  N NE  . ARG B 1 115 ? 0.710   13.774  35.108  1.00 36.34  ? 144 ARG D NE  1 
ATOM   4331  C CZ  . ARG B 1 115 ? 0.345   13.036  34.081  1.00 35.49  ? 144 ARG D CZ  1 
ATOM   4332  N NH1 . ARG B 1 115 ? 1.122   12.061  33.623  1.00 37.50  ? 144 ARG D NH1 1 
ATOM   4333  N NH2 . ARG B 1 115 ? -0.835  13.252  33.540  1.00 32.54  ? 144 ARG D NH2 1 
ATOM   4334  N N   . ALA B 1 116 ? 5.057   13.061  40.824  1.00 35.14  ? 145 ALA D N   1 
ATOM   4335  C CA  . ALA B 1 116 ? 6.472   13.187  41.142  1.00 42.12  ? 145 ALA D CA  1 
ATOM   4336  C C   . ALA B 1 116 ? 7.099   11.966  41.835  1.00 43.23  ? 145 ALA D C   1 
ATOM   4337  O O   . ALA B 1 116 ? 8.324   11.917  41.943  1.00 41.87  ? 145 ALA D O   1 
ATOM   4338  C CB  . ALA B 1 116 ? 6.670   14.423  41.981  1.00 41.34  ? 145 ALA D CB  1 
ATOM   4339  N N   . ALA B 1 117 ? 6.304   10.974  42.256  1.00 39.97  ? 146 ALA D N   1 
ATOM   4340  C CA  . ALA B 1 117 ? 6.801   9.868   43.067  1.00 42.39  ? 146 ALA D CA  1 
ATOM   4341  C C   . ALA B 1 117 ? 7.779   9.010   42.264  1.00 37.18  ? 146 ALA D C   1 
ATOM   4342  O O   . ALA B 1 117 ? 7.537   8.751   41.099  1.00 35.94  ? 146 ALA D O   1 
ATOM   4343  C CB  . ALA B 1 117 ? 5.642   9.025   43.570  1.00 40.27  ? 146 ALA D CB  1 
ATOM   4344  N N   . LEU B 1 118 ? 8.903   8.625   42.882  1.00 34.47  ? 147 LEU D N   1 
ATOM   4345  C CA  . LEU B 1 118 ? 9.883   7.759   42.245  1.00 37.98  ? 147 LEU D CA  1 
ATOM   4346  C C   . LEU B 1 118 ? 9.600   6.310   42.646  1.00 41.57  ? 147 LEU D C   1 
ATOM   4347  O O   . LEU B 1 118 ? 9.287   6.035   43.802  1.00 36.80  ? 147 LEU D O   1 
ATOM   4348  C CB  . LEU B 1 118 ? 11.314  8.139   42.616  1.00 37.04  ? 147 LEU D CB  1 
ATOM   4349  C CG  . LEU B 1 118 ? 11.754  9.577   42.340  1.00 38.65  ? 147 LEU D CG  1 
ATOM   4350  C CD1 . LEU B 1 118 ? 13.209  9.687   42.808  1.00 36.65  ? 147 LEU D CD1 1 
ATOM   4351  C CD2 . LEU B 1 118 ? 11.568  9.934   40.873  1.00 35.09  ? 147 LEU D CD2 1 
ATOM   4352  N N   . PRO B 1 119 ? 9.731   5.348   41.706  1.00 38.82  ? 148 PRO D N   1 
ATOM   4353  C CA  . PRO B 1 119 ? 9.715   3.936   42.061  1.00 37.38  ? 148 PRO D CA  1 
ATOM   4354  C C   . PRO B 1 119 ? 10.913  3.564   42.926  1.00 36.05  ? 148 PRO D C   1 
ATOM   4355  O O   . PRO B 1 119 ? 12.033  4.061   42.773  1.00 37.41  ? 148 PRO D O   1 
ATOM   4356  C CB  . PRO B 1 119 ? 9.676   3.145   40.744  1.00 45.07  ? 148 PRO D CB  1 
ATOM   4357  C CG  . PRO B 1 119 ? 9.785   4.189   39.630  1.00 43.24  ? 148 PRO D CG  1 
ATOM   4358  C CD  . PRO B 1 119 ? 9.856   5.581   40.263  1.00 42.84  ? 148 PRO D CD  1 
ATOM   4359  N N   . SER B 1 120 ? 10.663  2.593   43.797  1.00 33.38  ? 149 SER D N   1 
ATOM   4360  C CA  . SER B 1 120 ? 11.631  2.196   44.788  1.00 34.01  ? 149 SER D CA  1 
ATOM   4361  C C   . SER B 1 120 ? 12.956  1.802   44.130  1.00 32.57  ? 149 SER D C   1 
ATOM   4362  O O   . SER B 1 120 ? 14.007  2.195   44.633  1.00 27.70  ? 149 SER D O   1 
ATOM   4363  C CB  . SER B 1 120 ? 11.053  1.109   45.662  1.00 37.24  ? 149 SER D CB  1 
ATOM   4364  O OG  . SER B 1 120 ? 11.857  0.988   46.817  1.00 43.38  ? 149 SER D OG  1 
ATOM   4365  N N   . HIS B 1 121 ? 12.912  1.085   42.991  1.00 28.85  ? 150 HIS D N   1 
ATOM   4366  C CA  . HIS B 1 121 ? 14.133  0.546   42.416  1.00 30.48  ? 150 HIS D CA  1 
ATOM   4367  C C   . HIS B 1 121 ? 15.023  1.723   41.990  1.00 32.84  ? 150 HIS D C   1 
ATOM   4368  O O   . HIS B 1 121 ? 16.245  1.622   41.973  1.00 34.01  ? 150 HIS D O   1 
ATOM   4369  C CB  . HIS B 1 121 ? 13.842  -0.451  41.282  1.00 31.45  ? 150 HIS D CB  1 
ATOM   4370  C CG  . HIS B 1 121 ? 13.423  0.164   39.987  1.00 33.52  ? 150 HIS D CG  1 
ATOM   4371  N ND1 . HIS B 1 121 ? 12.124  0.577   39.717  1.00 37.82  ? 150 HIS D ND1 1 
ATOM   4372  C CD2 . HIS B 1 121 ? 14.121  0.399   38.862  1.00 35.76  ? 150 HIS D CD2 1 
ATOM   4373  C CE1 . HIS B 1 121 ? 12.052  1.070   38.491  1.00 35.14  ? 150 HIS D CE1 1 
ATOM   4374  N NE2 . HIS B 1 121 ? 13.247  0.974   37.940  1.00 35.44  ? 150 HIS D NE2 1 
ATOM   4375  N N   . VAL B 1 122 ? 14.424  2.875   41.685  1.00 33.55  ? 151 VAL D N   1 
ATOM   4376  C CA  . VAL B 1 122 ? 15.232  3.997   41.217  1.00 35.35  ? 151 VAL D CA  1 
ATOM   4377  C C   . VAL B 1 122 ? 15.887  4.630   42.435  1.00 34.61  ? 151 VAL D C   1 
ATOM   4378  O O   . VAL B 1 122 ? 17.068  4.951   42.386  1.00 32.28  ? 151 VAL D O   1 
ATOM   4379  C CB  . VAL B 1 122 ? 14.471  5.052   40.392  1.00 33.17  ? 151 VAL D CB  1 
ATOM   4380  C CG1 . VAL B 1 122 ? 15.319  6.280   40.080  1.00 31.91  ? 151 VAL D CG1 1 
ATOM   4381  C CG2 . VAL B 1 122 ? 13.984  4.452   39.091  1.00 35.32  ? 151 VAL D CG2 1 
ATOM   4382  N N   . VAL B 1 123 ? 15.111  4.808   43.511  1.00 36.79  ? 152 VAL D N   1 
ATOM   4383  C CA  . VAL B 1 123 ? 15.663  5.325   44.759  1.00 36.52  ? 152 VAL D CA  1 
ATOM   4384  C C   . VAL B 1 123 ? 16.852  4.465   45.204  1.00 39.15  ? 152 VAL D C   1 
ATOM   4385  O O   . VAL B 1 123 ? 17.935  4.964   45.528  1.00 43.80  ? 152 VAL D O   1 
ATOM   4386  C CB  . VAL B 1 123 ? 14.560  5.419   45.830  1.00 34.54  ? 152 VAL D CB  1 
ATOM   4387  C CG1 . VAL B 1 123 ? 15.109  5.833   47.181  1.00 39.23  ? 152 VAL D CG1 1 
ATOM   4388  C CG2 . VAL B 1 123 ? 13.445  6.374   45.411  1.00 35.67  ? 152 VAL D CG2 1 
ATOM   4389  N N   . THR B 1 124 ? 16.649  3.150   45.229  1.00 40.42  ? 153 THR D N   1 
ATOM   4390  C CA  . THR B 1 124 ? 17.697  2.216   45.611  1.00 40.35  ? 153 THR D CA  1 
ATOM   4391  C C   . THR B 1 124 ? 18.913  2.391   44.699  1.00 35.44  ? 153 THR D C   1 
ATOM   4392  O O   . THR B 1 124 ? 20.044  2.559   45.146  1.00 34.94  ? 153 THR D O   1 
ATOM   4393  C CB  . THR B 1 124 ? 17.142  0.797   45.512  1.00 43.26  ? 153 THR D CB  1 
ATOM   4394  O OG1 . THR B 1 124 ? 16.143  0.742   46.524  1.00 38.87  ? 153 THR D OG1 1 
ATOM   4395  C CG2 . THR B 1 124 ? 18.218  -0.259  45.703  1.00 51.37  ? 153 THR D CG2 1 
ATOM   4396  N N   . MET B 1 125 ? 18.681  2.366   43.397  1.00 34.81  ? 154 MET D N   1 
ATOM   4397  C CA  . MET B 1 125 ? 19.782  2.552   42.466  1.00 37.88  ? 154 MET D CA  1 
ATOM   4398  C C   . MET B 1 125 ? 20.609  3.791   42.855  1.00 32.30  ? 154 MET D C   1 
ATOM   4399  O O   . MET B 1 125 ? 21.841  3.762   42.888  1.00 28.97  ? 154 MET D O   1 
ATOM   4400  C CB  . MET B 1 125 ? 19.187  2.714   41.065  1.00 43.22  ? 154 MET D CB  1 
ATOM   4401  C CG  . MET B 1 125 ? 20.140  2.466   39.915  1.00 51.71  ? 154 MET D CG  1 
ATOM   4402  S SD  . MET B 1 125 ? 19.318  3.074   38.425  1.00 51.80  ? 154 MET D SD  1 
ATOM   4403  C CE  . MET B 1 125 ? 20.596  2.573   37.280  1.00 54.47  ? 154 MET D CE  1 
ATOM   4404  N N   . LEU B 1 126 ? 19.910  4.905   43.083  1.00 30.27  ? 155 LEU D N   1 
ATOM   4405  C CA  . LEU B 1 126 ? 20.526  6.193   43.312  1.00 30.56  ? 155 LEU D CA  1 
ATOM   4406  C C   . LEU B 1 126 ? 21.301  6.160   44.616  1.00 32.33  ? 155 LEU D C   1 
ATOM   4407  O O   . LEU B 1 126 ? 22.448  6.581   44.668  1.00 35.25  ? 155 LEU D O   1 
ATOM   4408  C CB  . LEU B 1 126 ? 19.464  7.281   43.337  1.00 29.04  ? 155 LEU D CB  1 
ATOM   4409  C CG  . LEU B 1 126 ? 18.984  7.785   41.970  1.00 32.22  ? 155 LEU D CG  1 
ATOM   4410  C CD1 . LEU B 1 126 ? 17.774  8.703   42.112  1.00 28.88  ? 155 LEU D CD1 1 
ATOM   4411  C CD2 . LEU B 1 126 ? 20.102  8.486   41.196  1.00 37.19  ? 155 LEU D CD2 1 
ATOM   4412  N N   . ASP B 1 127 ? 20.689  5.603   45.663  1.00 37.04  ? 156 ASP D N   1 
ATOM   4413  C CA  . ASP B 1 127 ? 21.343  5.496   46.957  1.00 38.18  ? 156 ASP D CA  1 
ATOM   4414  C C   . ASP B 1 127 ? 22.591  4.614   46.856  1.00 36.43  ? 156 ASP D C   1 
ATOM   4415  O O   . ASP B 1 127 ? 23.495  4.753   47.671  1.00 38.08  ? 156 ASP D O   1 
ATOM   4416  C CB  . ASP B 1 127 ? 20.327  5.114   48.028  1.00 43.40  ? 156 ASP D CB  1 
ATOM   4417  C CG  . ASP B 1 127 ? 19.267  6.186   48.296  1.00 43.35  ? 156 ASP D CG  1 
ATOM   4418  O OD1 . ASP B 1 127 ? 19.498  7.339   47.925  1.00 41.33  ? 156 ASP D OD1 1 
ATOM   4419  O OD2 . ASP B 1 127 ? 18.182  5.865   48.821  1.00 45.24  ? 156 ASP D OD2 1 
ATOM   4420  N N   . ASN B 1 128 ? 22.690  3.732   45.850  1.00 31.19  ? 157 ASN D N   1 
ATOM   4421  C CA  . ASN B 1 128 ? 23.821  2.818   45.792  1.00 31.05  ? 157 ASN D CA  1 
ATOM   4422  C C   . ASN B 1 128 ? 24.917  3.302   44.842  1.00 34.68  ? 157 ASN D C   1 
ATOM   4423  O O   . ASN B 1 128 ? 25.974  2.663   44.755  1.00 34.84  ? 157 ASN D O   1 
ATOM   4424  C CB  . ASN B 1 128 ? 23.380  1.403   45.430  1.00 40.37  ? 157 ASN D CB  1 
ATOM   4425  C CG  . ASN B 1 128 ? 22.641  0.716   46.565  1.00 42.82  ? 157 ASN D CG  1 
ATOM   4426  O OD1 . ASN B 1 128 ? 22.700  1.165   47.715  1.00 47.49  ? 157 ASN D OD1 1 
ATOM   4427  N ND2 . ASN B 1 128 ? 21.898  -0.332  46.252  1.00 43.36  ? 157 ASN D ND2 1 
ATOM   4428  N N   . PHE B 1 129 ? 24.694  4.417   44.131  1.00 31.30  ? 158 PHE D N   1 
ATOM   4429  C CA  . PHE B 1 129 ? 25.727  4.926   43.245  1.00 30.37  ? 158 PHE D CA  1 
ATOM   4430  C C   . PHE B 1 129 ? 26.912  5.429   44.084  1.00 31.16  ? 158 PHE D C   1 
ATOM   4431  O O   . PHE B 1 129 ? 26.745  6.100   45.089  1.00 34.14  ? 158 PHE D O   1 
ATOM   4432  C CB  . PHE B 1 129 ? 25.166  6.031   42.351  1.00 31.31  ? 158 PHE D CB  1 
ATOM   4433  C CG  . PHE B 1 129 ? 24.359  5.612   41.124  1.00 29.47  ? 158 PHE D CG  1 
ATOM   4434  C CD1 . PHE B 1 129 ? 24.581  4.408   40.469  1.00 32.36  ? 158 PHE D CD1 1 
ATOM   4435  C CD2 . PHE B 1 129 ? 23.385  6.446   40.620  1.00 31.01  ? 158 PHE D CD2 1 
ATOM   4436  C CE1 . PHE B 1 129 ? 23.857  4.064   39.343  1.00 35.99  ? 158 PHE D CE1 1 
ATOM   4437  C CE2 . PHE B 1 129 ? 22.683  6.104   39.480  1.00 30.26  ? 158 PHE D CE2 1 
ATOM   4438  C CZ  . PHE B 1 129 ? 22.935  4.929   38.841  1.00 30.54  ? 158 PHE D CZ  1 
ATOM   4439  N N   . PRO B 1 130 ? 28.169  5.157   43.681  1.00 30.55  ? 159 PRO D N   1 
ATOM   4440  C CA  . PRO B 1 130 ? 29.312  5.754   44.362  1.00 30.66  ? 159 PRO D CA  1 
ATOM   4441  C C   . PRO B 1 130 ? 29.466  7.223   43.982  1.00 35.30  ? 159 PRO D C   1 
ATOM   4442  O O   . PRO B 1 130 ? 29.019  7.644   42.910  1.00 34.29  ? 159 PRO D O   1 
ATOM   4443  C CB  . PRO B 1 130 ? 30.473  4.890   43.829  1.00 30.18  ? 159 PRO D CB  1 
ATOM   4444  C CG  . PRO B 1 130 ? 30.042  4.564   42.391  1.00 32.53  ? 159 PRO D CG  1 
ATOM   4445  C CD  . PRO B 1 130 ? 28.551  4.321   42.522  1.00 33.16  ? 159 PRO D CD  1 
ATOM   4446  N N   . THR B 1 131 ? 30.233  7.918   44.838  1.00 35.73  ? 160 THR D N   1 
ATOM   4447  C CA  . THR B 1 131 ? 30.659  9.305   44.743  1.00 41.51  ? 160 THR D CA  1 
ATOM   4448  C C   . THR B 1 131 ? 31.468  9.593   43.480  1.00 41.28  ? 160 THR D C   1 
ATOM   4449  O O   . THR B 1 131 ? 31.478  10.731  43.030  1.00 40.02  ? 160 THR D O   1 
ATOM   4450  C CB  . THR B 1 131 ? 31.469  9.581   46.016  1.00 44.13  ? 160 THR D CB  1 
ATOM   4451  O OG1 . THR B 1 131 ? 30.469  9.473   47.018  1.00 47.32  ? 160 THR D OG1 1 
ATOM   4452  C CG2 . THR B 1 131 ? 32.081  10.963  46.112  1.00 50.96  ? 160 THR D CG2 1 
ATOM   4453  N N   . ASN B 1 132 ? 32.186  8.599   42.926  1.00 39.66  ? 161 ASN D N   1 
ATOM   4454  C CA  . ASN B 1 132 ? 32.983  8.853   41.734  1.00 38.76  ? 161 ASN D CA  1 
ATOM   4455  C C   . ASN B 1 132 ? 32.165  8.691   40.440  1.00 34.65  ? 161 ASN D C   1 
ATOM   4456  O O   . ASN B 1 132 ? 32.732  8.798   39.357  1.00 39.47  ? 161 ASN D O   1 
ATOM   4457  C CB  . ASN B 1 132 ? 34.294  8.058   41.758  1.00 41.49  ? 161 ASN D CB  1 
ATOM   4458  C CG  . ASN B 1 132 ? 34.100  6.566   41.591  1.00 46.83  ? 161 ASN D CG  1 
ATOM   4459  O OD1 . ASN B 1 132 ? 34.836  5.909   40.845  1.00 52.72  ? 161 ASN D OD1 1 
ATOM   4460  N ND2 . ASN B 1 132 ? 33.146  5.995   42.300  1.00 44.30  ? 161 ASN D ND2 1 
ATOM   4461  N N   . LEU B 1 133 ? 30.868  8.356   40.515  1.00 32.48  ? 162 LEU D N   1 
ATOM   4462  C CA  . LEU B 1 133 ? 30.027  8.330   39.316  1.00 27.02  ? 162 LEU D CA  1 
ATOM   4463  C C   . LEU B 1 133 ? 29.496  9.726   39.134  1.00 27.59  ? 162 LEU D C   1 
ATOM   4464  O O   . LEU B 1 133 ? 28.793  10.210  40.023  1.00 23.02  ? 162 LEU D O   1 
ATOM   4465  C CB  . LEU B 1 133 ? 28.852  7.361   39.405  1.00 29.61  ? 162 LEU D CB  1 
ATOM   4466  C CG  . LEU B 1 133 ? 28.073  7.148   38.104  1.00 29.17  ? 162 LEU D CG  1 
ATOM   4467  C CD1 . LEU B 1 133 ? 29.010  6.630   36.972  1.00 28.07  ? 162 LEU D CD1 1 
ATOM   4468  C CD2 . LEU B 1 133 ? 26.909  6.217   38.351  1.00 31.17  ? 162 LEU D CD2 1 
ATOM   4469  N N   . HIS B 1 134 ? 29.901  10.377  38.026  1.00 29.31  ? 163 HIS D N   1 
ATOM   4470  C CA  . HIS B 1 134 ? 29.585  11.776  37.802  1.00 29.90  ? 163 HIS D CA  1 
ATOM   4471  C C   . HIS B 1 134 ? 28.077  11.981  37.917  1.00 28.08  ? 163 HIS D C   1 
ATOM   4472  O O   . HIS B 1 134 ? 27.317  11.124  37.493  1.00 30.95  ? 163 HIS D O   1 
ATOM   4473  C CB  . HIS B 1 134 ? 30.141  12.195  36.442  1.00 36.89  ? 163 HIS D CB  1 
ATOM   4474  C CG  . HIS B 1 134 ? 30.011  13.635  36.121  1.00 43.43  ? 163 HIS D CG  1 
ATOM   4475  N ND1 . HIS B 1 134 ? 28.860  14.205  35.610  1.00 39.72  ? 163 HIS D ND1 1 
ATOM   4476  C CD2 . HIS B 1 134 ? 30.926  14.616  36.201  1.00 43.31  ? 163 HIS D CD2 1 
ATOM   4477  C CE1 . HIS B 1 134 ? 29.063  15.497  35.441  1.00 39.27  ? 163 HIS D CE1 1 
ATOM   4478  N NE2 . HIS B 1 134 ? 30.314  15.757  35.784  1.00 43.63  ? 163 HIS D NE2 1 
ATOM   4479  N N   . PRO B 1 135 ? 27.589  13.108  38.482  1.00 30.68  ? 164 PRO D N   1 
ATOM   4480  C CA  . PRO B 1 135 ? 26.154  13.395  38.558  1.00 30.32  ? 164 PRO D CA  1 
ATOM   4481  C C   . PRO B 1 135 ? 25.323  13.221  37.278  1.00 28.47  ? 164 PRO D C   1 
ATOM   4482  O O   . PRO B 1 135 ? 24.158  12.848  37.342  1.00 22.80  ? 164 PRO D O   1 
ATOM   4483  C CB  . PRO B 1 135 ? 26.106  14.868  39.010  1.00 31.68  ? 164 PRO D CB  1 
ATOM   4484  C CG  . PRO B 1 135 ? 27.404  15.144  39.674  1.00 31.74  ? 164 PRO D CG  1 
ATOM   4485  C CD  . PRO B 1 135 ? 28.411  14.161  39.091  1.00 32.24  ? 164 PRO D CD  1 
ATOM   4486  N N   . MET B 1 136 ? 25.900  13.561  36.123  1.00 28.21  ? 165 MET D N   1 
ATOM   4487  C CA  . MET B 1 136 ? 25.214  13.475  34.836  1.00 32.16  ? 165 MET D CA  1 
ATOM   4488  C C   . MET B 1 136 ? 24.960  12.014  34.422  1.00 29.75  ? 165 MET D C   1 
ATOM   4489  O O   . MET B 1 136 ? 23.948  11.707  33.768  1.00 27.58  ? 165 MET D O   1 
ATOM   4490  C CB  . MET B 1 136 ? 26.005  14.195  33.728  1.00 30.17  ? 165 MET D CB  1 
ATOM   4491  C CG  . MET B 1 136 ? 25.770  15.700  33.675  1.00 30.58  ? 165 MET D CG  1 
ATOM   4492  S SD  . MET B 1 136 ? 24.045  16.155  33.390  1.00 32.99  ? 165 MET D SD  1 
ATOM   4493  C CE  . MET B 1 136 ? 23.820  15.514  31.725  1.00 32.95  ? 165 MET D CE  1 
ATOM   4494  N N   . SER B 1 137 ? 25.882  11.132  34.803  1.00 27.46  ? 166 SER D N   1 
ATOM   4495  C CA  . SER B 1 137 ? 25.782  9.716   34.481  1.00 30.86  ? 166 SER D CA  1 
ATOM   4496  C C   . SER B 1 137 ? 24.742  9.090   35.400  1.00 27.68  ? 166 SER D C   1 
ATOM   4497  O O   . SER B 1 137 ? 23.991  8.218   34.991  1.00 23.32  ? 166 SER D O   1 
ATOM   4498  C CB  . SER B 1 137 ? 27.078  8.990   34.678  1.00 29.03  ? 166 SER D CB  1 
ATOM   4499  O OG  . SER B 1 137 ? 28.112  9.600   33.939  1.00 27.53  ? 166 SER D OG  1 
ATOM   4500  N N   . GLN B 1 138 ? 24.697  9.601   36.632  1.00 26.04  ? 167 GLN D N   1 
ATOM   4501  C CA  . GLN B 1 138 ? 23.700  9.154   37.590  1.00 27.39  ? 167 GLN D CA  1 
ATOM   4502  C C   . GLN B 1 138 ? 22.319  9.582   37.103  1.00 25.08  ? 167 GLN D C   1 
ATOM   4503  O O   . GLN B 1 138 ? 21.361  8.864   37.275  1.00 27.02  ? 167 GLN D O   1 
ATOM   4504  C CB  . GLN B 1 138 ? 23.958  9.726   38.976  1.00 25.26  ? 167 GLN D CB  1 
ATOM   4505  C CG  . GLN B 1 138 ? 25.320  9.393   39.581  1.00 30.31  ? 167 GLN D CG  1 
ATOM   4506  C CD  . GLN B 1 138 ? 25.307  9.541   41.095  1.00 31.12  ? 167 GLN D CD  1 
ATOM   4507  O OE1 . GLN B 1 138 ? 24.234  9.655   41.683  1.00 31.50  ? 167 GLN D OE1 1 
ATOM   4508  N NE2 . GLN B 1 138 ? 26.464  9.575   41.740  1.00 31.08  ? 167 GLN D NE2 1 
ATOM   4509  N N   . LEU B 1 139 ? 22.204  10.798  36.559  1.00 24.25  ? 168 LEU D N   1 
ATOM   4510  C CA  . LEU B 1 139 ? 20.947  11.287  36.039  1.00 25.70  ? 168 LEU D CA  1 
ATOM   4511  C C   . LEU B 1 139 ? 20.516  10.431  34.847  1.00 25.46  ? 168 LEU D C   1 
ATOM   4512  O O   . LEU B 1 139 ? 19.409  9.919   34.815  1.00 23.96  ? 168 LEU D O   1 
ATOM   4513  C CB  . LEU B 1 139 ? 21.116  12.733  35.627  1.00 25.90  ? 168 LEU D CB  1 
ATOM   4514  C CG  . LEU B 1 139 ? 19.896  13.398  34.982  1.00 29.97  ? 168 LEU D CG  1 
ATOM   4515  C CD1 . LEU B 1 139 ? 18.675  13.469  35.859  1.00 29.48  ? 168 LEU D CD1 1 
ATOM   4516  C CD2 . LEU B 1 139 ? 20.261  14.799  34.514  1.00 28.96  ? 168 LEU D CD2 1 
ATOM   4517  N N   . SER B 1 140 ? 21.427  10.213  33.899  1.00 23.29  ? 169 SER D N   1 
ATOM   4518  C CA  . SER B 1 140 ? 21.126  9.438   32.714  1.00 23.48  ? 169 SER D CA  1 
ATOM   4519  C C   . SER B 1 140 ? 20.704  8.017   33.063  1.00 22.34  ? 169 SER D C   1 
ATOM   4520  O O   . SER B 1 140 ? 19.648  7.562   32.617  1.00 24.77  ? 169 SER D O   1 
ATOM   4521  C CB  . SER B 1 140 ? 22.262  9.434   31.745  1.00 25.81  ? 169 SER D CB  1 
ATOM   4522  O OG  . SER B 1 140 ? 21.887  8.536   30.716  1.00 32.90  ? 169 SER D OG  1 
ATOM   4523  N N   . ALA B 1 141 ? 21.475  7.332   33.914  1.00 25.57  ? 170 ALA D N   1 
ATOM   4524  C CA  . ALA B 1 141 ? 21.171  5.964   34.320  1.00 24.91  ? 170 ALA D CA  1 
ATOM   4525  C C   . ALA B 1 141 ? 19.830  5.871   35.048  1.00 25.71  ? 170 ALA D C   1 
ATOM   4526  O O   . ALA B 1 141 ? 19.067  4.935   34.831  1.00 26.66  ? 170 ALA D O   1 
ATOM   4527  C CB  . ALA B 1 141 ? 22.267  5.404   35.201  1.00 26.68  ? 170 ALA D CB  1 
ATOM   4528  N N   . ALA B 1 142 ? 19.591  6.792   35.986  1.00 27.59  ? 171 ALA D N   1 
ATOM   4529  C CA  . ALA B 1 142 ? 18.333  6.844   36.700  1.00 30.23  ? 171 ALA D CA  1 
ATOM   4530  C C   . ALA B 1 142 ? 17.151  7.073   35.758  1.00 30.69  ? 171 ALA D C   1 
ATOM   4531  O O   . ALA B 1 142 ? 16.076  6.494   35.925  1.00 29.82  ? 171 ALA D O   1 
ATOM   4532  C CB  . ALA B 1 142 ? 18.421  7.901   37.768  1.00 29.38  ? 171 ALA D CB  1 
ATOM   4533  N N   . VAL B 1 143 ? 17.339  7.909   34.743  1.00 28.04  ? 172 VAL D N   1 
ATOM   4534  C CA  . VAL B 1 143 ? 16.245  8.169   33.844  1.00 26.69  ? 172 VAL D CA  1 
ATOM   4535  C C   . VAL B 1 143 ? 15.963  6.921   33.011  1.00 26.33  ? 172 VAL D C   1 
ATOM   4536  O O   . VAL B 1 143 ? 14.808  6.498   32.899  1.00 23.71  ? 172 VAL D O   1 
ATOM   4537  C CB  . VAL B 1 143 ? 16.488  9.443   33.021  1.00 33.35  ? 172 VAL D CB  1 
ATOM   4538  C CG1 . VAL B 1 143 ? 15.567  9.530   31.834  1.00 30.44  ? 172 VAL D CG1 1 
ATOM   4539  C CG2 . VAL B 1 143 ? 16.267  10.668  33.897  1.00 37.56  ? 172 VAL D CG2 1 
ATOM   4540  N N   . THR B 1 144 ? 17.020  6.279   32.516  1.00 25.58  ? 173 THR D N   1 
ATOM   4541  C CA  . THR B 1 144 ? 16.872  5.028   31.786  1.00 24.12  ? 173 THR D CA  1 
ATOM   4542  C C   . THR B 1 144 ? 16.071  4.020   32.607  1.00 27.57  ? 173 THR D C   1 
ATOM   4543  O O   . THR B 1 144 ? 15.177  3.364   32.075  1.00 27.90  ? 173 THR D O   1 
ATOM   4544  C CB  . THR B 1 144 ? 18.250  4.492   31.454  1.00 25.27  ? 173 THR D CB  1 
ATOM   4545  O OG1 . THR B 1 144 ? 18.771  5.506   30.590  1.00 26.86  ? 173 THR D OG1 1 
ATOM   4546  C CG2 . THR B 1 144 ? 18.155  3.150   30.756  1.00 28.45  ? 173 THR D CG2 1 
ATOM   4547  N N   . ALA B 1 145 ? 16.418  3.907   33.887  1.00 28.57  ? 174 ALA D N   1 
ATOM   4548  C CA  . ALA B 1 145 ? 15.800  2.953   34.797  1.00 26.06  ? 174 ALA D CA  1 
ATOM   4549  C C   . ALA B 1 145 ? 14.335  3.284   35.069  1.00 31.29  ? 174 ALA D C   1 
ATOM   4550  O O   . ALA B 1 145 ? 13.539  2.364   35.291  1.00 26.98  ? 174 ALA D O   1 
ATOM   4551  C CB  . ALA B 1 145 ? 16.577  2.869   36.060  1.00 27.77  ? 174 ALA D CB  1 
ATOM   4552  N N   . LEU B 1 146 ? 13.972  4.571   34.959  1.00 32.19  ? 175 LEU D N   1 
ATOM   4553  C CA  . LEU B 1 146 ? 12.588  5.002   35.079  1.00 29.42  ? 175 LEU D CA  1 
ATOM   4554  C C   . LEU B 1 146 ? 11.727  4.491   33.925  1.00 28.48  ? 175 LEU D C   1 
ATOM   4555  O O   . LEU B 1 146 ? 10.511  4.563   34.013  1.00 27.79  ? 175 LEU D O   1 
ATOM   4556  C CB  . LEU B 1 146 ? 12.428  6.519   35.152  1.00 28.00  ? 175 LEU D CB  1 
ATOM   4557  C CG  . LEU B 1 146 ? 12.596  7.165   36.524  1.00 27.97  ? 175 LEU D CG  1 
ATOM   4558  C CD1 . LEU B 1 146 ? 12.475  8.673   36.402  1.00 28.96  ? 175 LEU D CD1 1 
ATOM   4559  C CD2 . LEU B 1 146 ? 11.634  6.636   37.542  1.00 30.20  ? 175 LEU D CD2 1 
ATOM   4560  N N   . ASN B 1 147 ? 12.325  3.970   32.857  1.00 30.25  ? 176 ASN D N   1 
ATOM   4561  C CA  . ASN B 1 147 ? 11.542  3.564   31.705  1.00 33.00  ? 176 ASN D CA  1 
ATOM   4562  C C   . ASN B 1 147 ? 10.647  2.376   32.057  1.00 33.67  ? 176 ASN D C   1 
ATOM   4563  O O   . ASN B 1 147 ? 9.685   2.100   31.343  1.00 30.38  ? 176 ASN D O   1 
ATOM   4564  C CB  . ASN B 1 147 ? 12.402  3.389   30.463  1.00 36.93  ? 176 ASN D CB  1 
ATOM   4565  C CG  . ASN B 1 147 ? 12.250  2.023   29.855  1.00 37.38  ? 176 ASN D CG  1 
ATOM   4566  O OD1 . ASN B 1 147 ? 12.627  1.055   30.508  1.00 41.96  ? 176 ASN D OD1 1 
ATOM   4567  N ND2 . ASN B 1 147 ? 11.713  1.920   28.647  1.00 38.81  ? 176 ASN D ND2 1 
ATOM   4568  N N   . SER B 1 148 ? 10.922  1.716   33.191  1.00 32.80  ? 177 SER D N   1 
ATOM   4569  C CA  . SER B 1 148 ? 9.989   0.740   33.734  1.00 31.79  ? 177 SER D CA  1 
ATOM   4570  C C   . SER B 1 148 ? 8.583   1.319   33.949  1.00 33.24  ? 177 SER D C   1 
ATOM   4571  O O   . SER B 1 148 ? 7.610   0.593   34.095  1.00 42.88  ? 177 SER D O   1 
ATOM   4572  C CB  . SER B 1 148 ? 10.534  0.180   35.021  1.00 31.22  ? 177 SER D CB  1 
ATOM   4573  O OG  . SER B 1 148 ? 10.530  1.134   36.076  1.00 32.20  ? 177 SER D OG  1 
ATOM   4574  N N   . GLU B 1 149 ? 8.448   2.629   34.042  1.00 35.46  ? 178 GLU D N   1 
ATOM   4575  C CA  . GLU B 1 149 ? 7.144   3.227   34.270  1.00 39.77  ? 178 GLU D CA  1 
ATOM   4576  C C   . GLU B 1 149 ? 6.523   3.722   32.966  1.00 36.19  ? 178 GLU D C   1 
ATOM   4577  O O   . GLU B 1 149 ? 5.456   4.312   33.005  1.00 40.94  ? 178 GLU D O   1 
ATOM   4578  C CB  . GLU B 1 149 ? 7.244   4.394   35.258  1.00 39.70  ? 178 GLU D CB  1 
ATOM   4579  C CG  . GLU B 1 149 ? 8.082   4.070   36.491  1.00 51.01  ? 178 GLU D CG  1 
ATOM   4580  C CD  . GLU B 1 149 ? 7.682   2.844   37.316  1.00 59.31  ? 178 GLU D CD  1 
ATOM   4581  O OE1 . GLU B 1 149 ? 6.516   2.808   37.788  1.00 64.35  ? 178 GLU D OE1 1 
ATOM   4582  O OE2 . GLU B 1 149 ? 8.549   1.945   37.534  1.00 56.34  ? 178 GLU D OE2 1 
ATOM   4583  N N   . SER B 1 150 ? 7.153   3.437   31.816  1.00 35.17  ? 179 SER D N   1 
ATOM   4584  C CA  . SER B 1 150 ? 6.763   4.072   30.563  1.00 35.38  ? 179 SER D CA  1 
ATOM   4585  C C   . SER B 1 150 ? 5.427   3.497   30.102  1.00 34.72  ? 179 SER D C   1 
ATOM   4586  O O   . SER B 1 150 ? 5.264   2.294   29.981  1.00 34.78  ? 179 SER D O   1 
ATOM   4587  C CB  . SER B 1 150 ? 7.822   3.931   29.500  1.00 29.70  ? 179 SER D CB  1 
ATOM   4588  O OG  . SER B 1 150 ? 7.323   4.350   28.249  1.00 29.18  ? 179 SER D OG  1 
ATOM   4589  N N   . ASN B 1 151 ? 4.465   4.388   29.903  1.00 40.49  ? 180 ASN D N   1 
ATOM   4590  C CA  . ASN B 1 151 ? 3.176   4.044   29.339  1.00 39.40  ? 180 ASN D CA  1 
ATOM   4591  C C   . ASN B 1 151 ? 3.337   3.682   27.860  1.00 38.61  ? 180 ASN D C   1 
ATOM   4592  O O   . ASN B 1 151 ? 2.644   2.793   27.369  1.00 33.16  ? 180 ASN D O   1 
ATOM   4593  C CB  . ASN B 1 151 ? 2.192   5.190   29.549  1.00 46.57  ? 180 ASN D CB  1 
ATOM   4594  C CG  . ASN B 1 151 ? 2.081   5.598   31.002  1.00 47.37  ? 180 ASN D CG  1 
ATOM   4595  O OD1 . ASN B 1 151 ? 2.315   6.773   31.351  1.00 48.01  ? 180 ASN D OD1 1 
ATOM   4596  N ND2 . ASN B 1 151 ? 1.735   4.634   31.846  1.00 45.29  ? 180 ASN D ND2 1 
ATOM   4597  N N   . PHE B 1 152 ? 4.248   4.387   27.163  1.00 36.69  ? 181 PHE D N   1 
ATOM   4598  C CA  . PHE B 1 152 ? 4.360   4.322   25.719  1.00 33.83  ? 181 PHE D CA  1 
ATOM   4599  C C   . PHE B 1 152 ? 5.039   3.031   25.271  1.00 37.05  ? 181 PHE D C   1 
ATOM   4600  O O   . PHE B 1 152 ? 4.687   2.466   24.229  1.00 37.79  ? 181 PHE D O   1 
ATOM   4601  C CB  . PHE B 1 152 ? 5.123   5.502   25.134  1.00 32.07  ? 181 PHE D CB  1 
ATOM   4602  C CG  . PHE B 1 152 ? 5.224   5.398   23.622  1.00 31.76  ? 181 PHE D CG  1 
ATOM   4603  C CD1 . PHE B 1 152 ? 4.181   5.809   22.808  1.00 32.95  ? 181 PHE D CD1 1 
ATOM   4604  C CD2 . PHE B 1 152 ? 6.379   4.927   23.027  1.00 30.78  ? 181 PHE D CD2 1 
ATOM   4605  C CE1 . PHE B 1 152 ? 4.281   5.719   21.426  1.00 34.40  ? 181 PHE D CE1 1 
ATOM   4606  C CE2 . PHE B 1 152 ? 6.477   4.829   21.655  1.00 35.13  ? 181 PHE D CE2 1 
ATOM   4607  C CZ  . PHE B 1 152 ? 5.436   5.245   20.850  1.00 39.33  ? 181 PHE D CZ  1 
ATOM   4608  N N   . ALA B 1 153 ? 5.992   2.551   26.063  1.00 34.13  ? 182 ALA D N   1 
ATOM   4609  C CA  . ALA B 1 153 ? 6.735   1.352   25.690  1.00 37.83  ? 182 ALA D CA  1 
ATOM   4610  C C   . ALA B 1 153 ? 5.792   0.149   25.531  1.00 42.60  ? 182 ALA D C   1 
ATOM   4611  O O   . ALA B 1 153 ? 5.949   -0.638  24.603  1.00 49.77  ? 182 ALA D O   1 
ATOM   4612  C CB  . ALA B 1 153 ? 7.841   1.108   26.699  1.00 34.11  ? 182 ALA D CB  1 
ATOM   4613  N N   . ARG B 1 154 ? 4.810   0.003   26.424  1.00 49.85  ? 183 ARG D N   1 
ATOM   4614  C CA  . ARG B 1 154 ? 3.952   -1.177  26.441  1.00 65.80  ? 183 ARG D CA  1 
ATOM   4615  C C   . ARG B 1 154 ? 3.071   -1.163  25.192  1.00 75.62  ? 183 ARG D C   1 
ATOM   4616  O O   . ARG B 1 154 ? 2.940   -2.166  24.496  1.00 76.99  ? 183 ARG D O   1 
ATOM   4617  C CB  . ARG B 1 154 ? 3.058   -1.238  27.693  1.00 75.66  ? 183 ARG D CB  1 
ATOM   4618  C CG  . ARG B 1 154 ? 3.680   -0.716  28.986  1.00 84.91  ? 183 ARG D CG  1 
ATOM   4619  C CD  . ARG B 1 154 ? 2.877   -0.972  30.276  1.00 89.85  ? 183 ARG D CD  1 
ATOM   4620  N NE  . ARG B 1 154 ? 2.942   0.149   31.232  1.00 95.86  ? 183 ARG D NE  1 
ATOM   4621  C CZ  . ARG B 1 154 ? 3.639   0.237   32.376  1.00 99.23  ? 183 ARG D CZ  1 
ATOM   4622  N NH1 . ARG B 1 154 ? 4.457   -0.735  32.745  1.00 97.84  ? 183 ARG D NH1 1 
ATOM   4623  N NH2 . ARG B 1 154 ? 3.538   1.316   33.144  1.00 92.75  ? 183 ARG D NH2 1 
ATOM   4624  N N   . ALA B 1 155 ? 2.534   0.020   24.876  1.00 81.14  ? 184 ALA D N   1 
ATOM   4625  C CA  . ALA B 1 155 ? 1.418   0.155   23.961  1.00 73.20  ? 184 ALA D CA  1 
ATOM   4626  C C   . ALA B 1 155 ? 1.810   -0.094  22.502  1.00 76.04  ? 184 ALA D C   1 
ATOM   4627  O O   . ALA B 1 155 ? 0.935   -0.370  21.684  1.00 84.45  ? 184 ALA D O   1 
ATOM   4628  C CB  . ALA B 1 155 ? 0.808   1.522   24.144  1.00 80.60  ? 184 ALA D CB  1 
ATOM   4629  N N   . TYR B 1 156 ? 3.096   -0.015  22.141  1.00 60.32  ? 185 TYR D N   1 
ATOM   4630  C CA  . TYR B 1 156 ? 3.456   -0.221  20.743  1.00 53.73  ? 185 TYR D CA  1 
ATOM   4631  C C   . TYR B 1 156 ? 3.367   -1.705  20.361  1.00 62.00  ? 185 TYR D C   1 
ATOM   4632  O O   . TYR B 1 156 ? 3.082   -2.048  19.201  1.00 50.01  ? 185 TYR D O   1 
ATOM   4633  C CB  . TYR B 1 156 ? 4.865   0.273   20.424  1.00 47.68  ? 185 TYR D CB  1 
ATOM   4634  C CG  . TYR B 1 156 ? 5.296   0.025   18.985  1.00 43.37  ? 185 TYR D CG  1 
ATOM   4635  C CD1 . TYR B 1 156 ? 5.845   -1.169  18.588  1.00 41.15  ? 185 TYR D CD1 1 
ATOM   4636  C CD2 . TYR B 1 156 ? 5.163   1.002   18.015  1.00 45.61  ? 185 TYR D CD2 1 
ATOM   4637  C CE1 . TYR B 1 156 ? 6.224   -1.408  17.276  1.00 43.00  ? 185 TYR D CE1 1 
ATOM   4638  C CE2 . TYR B 1 156 ? 5.546   0.780   16.703  1.00 42.22  ? 185 TYR D CE2 1 
ATOM   4639  C CZ  . TYR B 1 156 ? 6.095   -0.422  16.325  1.00 49.55  ? 185 TYR D CZ  1 
ATOM   4640  O OH  . TYR B 1 156 ? 6.484   -0.638  15.020  1.00 51.74  ? 185 TYR D OH  1 
ATOM   4641  N N   . ALA B 1 157 ? 3.685   -2.581  21.326  1.00 63.54  ? 186 ALA D N   1 
ATOM   4642  C CA  . ALA B 1 157 ? 3.649   -4.022  21.118  1.00 65.21  ? 186 ALA D CA  1 
ATOM   4643  C C   . ALA B 1 157 ? 2.193   -4.475  21.026  1.00 62.39  ? 186 ALA D C   1 
ATOM   4644  O O   . ALA B 1 157 ? 1.871   -5.414  20.282  1.00 45.36  ? 186 ALA D O   1 
ATOM   4645  C CB  . ALA B 1 157 ? 4.368   -4.727  22.249  1.00 63.43  ? 186 ALA D CB  1 
ATOM   4646  N N   . GLN B 1 158 ? 1.348   -3.741  21.775  1.00 56.32  ? 187 GLN D N   1 
ATOM   4647  C CA  . GLN B 1 158 ? -0.092  -3.944  21.835  1.00 57.08  ? 187 GLN D CA  1 
ATOM   4648  C C   . GLN B 1 158 ? -0.819  -3.413  20.606  1.00 47.62  ? 187 GLN D C   1 
ATOM   4649  O O   . GLN B 1 158 ? -2.007  -3.643  20.489  1.00 52.64  ? 187 GLN D O   1 
ATOM   4650  C CB  . GLN B 1 158 ? -0.666  -3.251  23.067  1.00 58.65  ? 187 GLN D CB  1 
ATOM   4651  C CG  . GLN B 1 158 ? -0.273  -3.946  24.364  1.00 63.78  ? 187 GLN D CG  1 
ATOM   4652  C CD  . GLN B 1 158 ? -0.736  -3.197  25.590  1.00 70.02  ? 187 GLN D CD  1 
ATOM   4653  O OE1 . GLN B 1 158 ? -1.429  -2.179  25.491  1.00 68.20  ? 187 GLN D OE1 1 
ATOM   4654  N NE2 . GLN B 1 158 ? -0.326  -3.681  26.755  1.00 69.89  ? 187 GLN D NE2 1 
ATOM   4655  N N   . GLY B 1 159 ? -0.142  -2.667  19.728  1.00 45.41  ? 188 GLY D N   1 
ATOM   4656  C CA  . GLY B 1 159 ? -0.698  -2.334  18.428  1.00 39.53  ? 188 GLY D CA  1 
ATOM   4657  C C   . GLY B 1 159 ? -1.572  -1.081  18.477  1.00 40.93  ? 188 GLY D C   1 
ATOM   4658  O O   . GLY B 1 159 ? -2.557  -0.955  17.725  1.00 36.38  ? 188 GLY D O   1 
ATOM   4659  N N   . ILE B 1 160 ? -1.169  -0.120  19.312  1.00 35.21  ? 189 ILE D N   1 
ATOM   4660  C CA  . ILE B 1 160 ? -1.926  1.115   19.445  1.00 32.25  ? 189 ILE D CA  1 
ATOM   4661  C C   . ILE B 1 160 ? -1.826  1.944   18.160  1.00 30.45  ? 189 ILE D C   1 
ATOM   4662  O O   . ILE B 1 160 ? -0.816  1.937   17.471  1.00 31.35  ? 189 ILE D O   1 
ATOM   4663  C CB  . ILE B 1 160 ? -1.451  1.825   20.716  1.00 44.73  ? 189 ILE D CB  1 
ATOM   4664  C CG1 . ILE B 1 160 ? -2.469  2.869   21.181  1.00 54.90  ? 189 ILE D CG1 1 
ATOM   4665  C CG2 . ILE B 1 160 ? -0.052  2.415   20.519  1.00 48.91  ? 189 ILE D CG2 1 
ATOM   4666  C CD1 . ILE B 1 160 ? -2.402  3.202   22.661  1.00 53.72  ? 189 ILE D CD1 1 
ATOM   4667  N N   . SER B 1 161 ? -2.919  2.579   17.731  1.00 34.26  ? 190 SER D N   1 
ATOM   4668  C CA  . SER B 1 161 ? -2.881  3.401   16.530  1.00 29.72  ? 190 SER D CA  1 
ATOM   4669  C C   . SER B 1 161 ? -1.749  4.432   16.647  1.00 30.92  ? 190 SER D C   1 
ATOM   4670  O O   . SER B 1 161 ? -1.573  5.064   17.683  1.00 27.10  ? 190 SER D O   1 
ATOM   4671  C CB  . SER B 1 161 ? -4.219  4.063   16.284  1.00 30.32  ? 190 SER D CB  1 
ATOM   4672  O OG  . SER B 1 161 ? -4.216  4.920   15.130  1.00 33.76  ? 190 SER D OG  1 
ATOM   4673  N N   . ARG B 1 162 ? -0.963  4.573   15.581  1.00 30.79  ? 191 ARG D N   1 
ATOM   4674  C CA  . ARG B 1 162 ? -0.050  5.682   15.389  1.00 37.16  ? 191 ARG D CA  1 
ATOM   4675  C C   . ARG B 1 162 ? -0.684  7.026   15.783  1.00 35.83  ? 191 ARG D C   1 
ATOM   4676  O O   . ARG B 1 162 ? 0.045   7.931   16.168  1.00 39.16  ? 191 ARG D O   1 
ATOM   4677  C CB  . ARG B 1 162 ? 0.341   5.810   13.908  1.00 41.33  ? 191 ARG D CB  1 
ATOM   4678  C CG  . ARG B 1 162 ? 1.323   4.759   13.409  1.00 57.47  ? 191 ARG D CG  1 
ATOM   4679  C CD  . ARG B 1 162 ? 1.728   4.960   11.946  1.00 63.69  ? 191 ARG D CD  1 
ATOM   4680  N NE  . ARG B 1 162 ? 0.564   5.416   11.173  1.00 70.72  ? 191 ARG D NE  1 
ATOM   4681  C CZ  . ARG B 1 162 ? -0.249  4.662   10.428  1.00 77.19  ? 191 ARG D CZ  1 
ATOM   4682  N NH1 . ARG B 1 162 ? -0.049  3.355   10.288  1.00 76.54  ? 191 ARG D NH1 1 
ATOM   4683  N NH2 . ARG B 1 162 ? -1.285  5.226   9.826   1.00 72.80  ? 191 ARG D NH2 1 
ATOM   4684  N N   . THR B 1 163 ? -2.001  7.184   15.570  1.00 33.69  ? 192 THR D N   1 
ATOM   4685  C CA  . THR B 1 163 ? -2.694  8.457   15.762  1.00 33.78  ? 192 THR D CA  1 
ATOM   4686  C C   . THR B 1 163 ? -2.696  8.817   17.236  1.00 30.64  ? 192 THR D C   1 
ATOM   4687  O O   . THR B 1 163 ? -3.026  9.940   17.596  1.00 36.23  ? 192 THR D O   1 
ATOM   4688  C CB  . THR B 1 163 ? -4.139  8.385   15.240  1.00 35.59  ? 192 THR D CB  1 
ATOM   4689  O OG1 . THR B 1 163 ? -4.804  7.305   15.901  1.00 31.83  ? 192 THR D OG1 1 
ATOM   4690  C CG2 . THR B 1 163 ? -4.208  8.191   13.739  1.00 42.09  ? 192 THR D CG2 1 
ATOM   4691  N N   . LYS B 1 164 ? -2.450  7.818   18.075  1.00 32.77  ? 193 LYS D N   1 
ATOM   4692  C CA  . LYS B 1 164 ? -2.511  7.948   19.519  1.00 34.32  ? 193 LYS D CA  1 
ATOM   4693  C C   . LYS B 1 164 ? -1.120  7.953   20.145  1.00 32.79  ? 193 LYS D C   1 
ATOM   4694  O O   . LYS B 1 164 ? -1.015  8.163   21.347  1.00 34.47  ? 193 LYS D O   1 
ATOM   4695  C CB  . LYS B 1 164 ? -3.426  6.876   20.125  1.00 38.12  ? 193 LYS D CB  1 
ATOM   4696  C CG  . LYS B 1 164 ? -4.913  7.118   19.868  1.00 41.68  ? 193 LYS D CG  1 
ATOM   4697  C CD  . LYS B 1 164 ? -5.855  6.079   20.472  1.00 53.72  ? 193 LYS D CD  1 
ATOM   4698  C CE  . LYS B 1 164 ? -5.839  6.005   21.970  1.00 53.84  ? 193 LYS D CE  1 
ATOM   4699  N NZ  . LYS B 1 164 ? -6.314  7.251   22.581  1.00 59.47  ? 193 LYS D NZ  1 
ATOM   4700  N N   . TYR B 1 165 ? -0.043  7.845   19.343  1.00 29.96  ? 194 TYR D N   1 
ATOM   4701  C CA  . TYR B 1 165 ? 1.288   7.853   19.926  1.00 27.49  ? 194 TYR D CA  1 
ATOM   4702  C C   . TYR B 1 165 ? 1.453   9.102   20.803  1.00 27.94  ? 194 TYR D C   1 
ATOM   4703  O O   . TYR B 1 165 ? 1.855   9.003   21.940  1.00 29.49  ? 194 TYR D O   1 
ATOM   4704  C CB  . TYR B 1 165 ? 2.352   7.724   18.832  1.00 27.31  ? 194 TYR D CB  1 
ATOM   4705  C CG  . TYR B 1 165 ? 2.559   6.354   18.207  1.00 25.67  ? 194 TYR D CG  1 
ATOM   4706  C CD1 . TYR B 1 165 ? 2.000   5.206   18.752  1.00 29.81  ? 194 TYR D CD1 1 
ATOM   4707  C CD2 . TYR B 1 165 ? 3.347   6.214   17.064  1.00 28.83  ? 194 TYR D CD2 1 
ATOM   4708  C CE1 . TYR B 1 165 ? 2.163   3.967   18.150  1.00 32.16  ? 194 TYR D CE1 1 
ATOM   4709  C CE2 . TYR B 1 165 ? 3.535   4.983   16.457  1.00 29.15  ? 194 TYR D CE2 1 
ATOM   4710  C CZ  . TYR B 1 165 ? 2.963   3.849   17.027  1.00 33.17  ? 194 TYR D CZ  1 
ATOM   4711  O OH  . TYR B 1 165 ? 3.150   2.602   16.508  1.00 31.48  ? 194 TYR D OH  1 
ATOM   4712  N N   . TRP B 1 166 ? 1.139   10.300  20.315  1.00 31.84  ? 195 TRP D N   1 
ATOM   4713  C CA  . TRP B 1 166 ? 1.402   11.528  21.053  1.00 28.84  ? 195 TRP D CA  1 
ATOM   4714  C C   . TRP B 1 166 ? 0.804   11.515  22.465  1.00 29.93  ? 195 TRP D C   1 
ATOM   4715  O O   . TRP B 1 166 ? 1.292   12.229  23.335  1.00 23.88  ? 195 TRP D O   1 
ATOM   4716  C CB  . TRP B 1 166 ? 0.912   12.762  20.267  1.00 30.14  ? 195 TRP D CB  1 
ATOM   4717  C CG  . TRP B 1 166 ? -0.585  12.981  20.270  1.00 30.87  ? 195 TRP D CG  1 
ATOM   4718  C CD1 . TRP B 1 166 ? -1.495  12.598  19.320  1.00 32.19  ? 195 TRP D CD1 1 
ATOM   4719  C CD2 . TRP B 1 166 ? -1.354  13.665  21.284  1.00 32.34  ? 195 TRP D CD2 1 
ATOM   4720  N NE1 . TRP B 1 166 ? -2.762  12.953  19.689  1.00 30.18  ? 195 TRP D NE1 1 
ATOM   4721  C CE2 . TRP B 1 166 ? -2.711  13.615  20.884  1.00 30.31  ? 195 TRP D CE2 1 
ATOM   4722  C CE3 . TRP B 1 166 ? -1.023  14.295  22.490  1.00 30.51  ? 195 TRP D CE3 1 
ATOM   4723  C CZ2 . TRP B 1 166 ? -3.738  14.203  21.627  1.00 32.83  ? 195 TRP D CZ2 1 
ATOM   4724  C CZ3 . TRP B 1 166 ? -2.044  14.863  23.231  1.00 31.59  ? 195 TRP D CZ3 1 
ATOM   4725  C CH2 . TRP B 1 166 ? -3.381  14.807  22.811  1.00 32.53  ? 195 TRP D CH2 1 
ATOM   4726  N N   . GLU B 1 167 ? -0.310  10.799  22.671  1.00 29.92  ? 196 GLU D N   1 
ATOM   4727  C CA  . GLU B 1 167 ? -1.008  10.825  23.943  1.00 32.91  ? 196 GLU D CA  1 
ATOM   4728  C C   . GLU B 1 167 ? -0.204  10.092  25.007  1.00 30.55  ? 196 GLU D C   1 
ATOM   4729  O O   . GLU B 1 167 ? -0.200  10.455  26.175  1.00 29.10  ? 196 GLU D O   1 
ATOM   4730  C CB  . GLU B 1 167 ? -2.366  10.124  23.907  1.00 35.08  ? 196 GLU D CB  1 
ATOM   4731  C CG  . GLU B 1 167 ? -3.272  10.605  22.780  1.00 44.05  ? 196 GLU D CG  1 
ATOM   4732  C CD  . GLU B 1 167 ? -4.753  10.327  22.984  1.00 54.87  ? 196 GLU D CD  1 
ATOM   4733  O OE1 . GLU B 1 167 ? -5.507  10.359  21.977  1.00 58.46  ? 196 GLU D OE1 1 
ATOM   4734  O OE2 . GLU B 1 167 ? -5.152  10.115  24.155  1.00 54.16  ? 196 GLU D OE2 1 
ATOM   4735  N N   . LEU B 1 168 ? 0.451   9.013   24.611  1.00 28.73  ? 197 LEU D N   1 
ATOM   4736  C CA  . LEU B 1 168 ? 1.248   8.287   25.558  1.00 28.37  ? 197 LEU D CA  1 
ATOM   4737  C C   . LEU B 1 168 ? 2.576   8.973   25.788  1.00 27.57  ? 197 LEU D C   1 
ATOM   4738  O O   . LEU B 1 168 ? 3.061   8.996   26.919  1.00 28.53  ? 197 LEU D O   1 
ATOM   4739  C CB  . LEU B 1 168 ? 1.392   6.880   25.007  1.00 34.16  ? 197 LEU D CB  1 
ATOM   4740  C CG  . LEU B 1 168 ? 0.073   6.111   25.012  1.00 41.22  ? 197 LEU D CG  1 
ATOM   4741  C CD1 . LEU B 1 168 ? 0.251   4.896   24.131  1.00 43.54  ? 197 LEU D CD1 1 
ATOM   4742  C CD2 . LEU B 1 168 ? -0.297  5.750   26.435  1.00 40.30  ? 197 LEU D CD2 1 
ATOM   4743  N N   . ILE B 1 169 ? 3.157   9.514   24.716  1.00 25.01  ? 198 ILE D N   1 
ATOM   4744  C CA  . ILE B 1 169 ? 4.315   10.373  24.838  1.00 25.75  ? 198 ILE D CA  1 
ATOM   4745  C C   . ILE B 1 169 ? 4.014   11.529  25.809  1.00 23.57  ? 198 ILE D C   1 
ATOM   4746  O O   . ILE B 1 169 ? 4.822   11.880  26.662  1.00 26.74  ? 198 ILE D O   1 
ATOM   4747  C CB  . ILE B 1 169 ? 4.750   10.836  23.432  1.00 27.68  ? 198 ILE D CB  1 
ATOM   4748  C CG1 . ILE B 1 169 ? 5.157   9.651   22.563  1.00 34.92  ? 198 ILE D CG1 1 
ATOM   4749  C CG2 . ILE B 1 169 ? 5.884   11.839  23.524  1.00 24.73  ? 198 ILE D CG2 1 
ATOM   4750  C CD1 . ILE B 1 169 ? 6.326   8.866   23.143  1.00 34.90  ? 198 ILE D CD1 1 
ATOM   4751  N N   . TYR B 1 170 ? 2.841   12.122  25.710  1.00 23.06  ? 199 TYR D N   1 
ATOM   4752  C CA  . TYR B 1 170 ? 2.490   13.210  26.615  1.00 24.67  ? 199 TYR D CA  1 
ATOM   4753  C C   . TYR B 1 170 ? 2.495   12.702  28.062  1.00 25.00  ? 199 TYR D C   1 
ATOM   4754  O O   . TYR B 1 170 ? 3.079   13.331  28.932  1.00 24.89  ? 199 TYR D O   1 
ATOM   4755  C CB  . TYR B 1 170 ? 1.149   13.793  26.178  1.00 24.86  ? 199 TYR D CB  1 
ATOM   4756  C CG  . TYR B 1 170 ? 0.483   14.708  27.207  1.00 26.00  ? 199 TYR D CG  1 
ATOM   4757  C CD1 . TYR B 1 170 ? -0.304  14.178  28.232  1.00 27.45  ? 199 TYR D CD1 1 
ATOM   4758  C CD2 . TYR B 1 170 ? 0.691   16.071  27.219  1.00 25.54  ? 199 TYR D CD2 1 
ATOM   4759  C CE1 . TYR B 1 170 ? -0.893  14.994  29.193  1.00 28.35  ? 199 TYR D CE1 1 
ATOM   4760  C CE2 . TYR B 1 170 ? 0.097   16.900  28.182  1.00 27.64  ? 199 TYR D CE2 1 
ATOM   4761  C CZ  . TYR B 1 170 ? -0.706  16.358  29.164  1.00 24.68  ? 199 TYR D CZ  1 
ATOM   4762  O OH  . TYR B 1 170 ? -1.299  17.144  30.117  1.00 32.42  ? 199 TYR D OH  1 
ATOM   4763  N N   . GLU B 1 171 ? 1.852   11.558  28.303  1.00 25.74  ? 200 GLU D N   1 
ATOM   4764  C CA  . GLU B 1 171 ? 1.744   11.046  29.659  1.00 27.69  ? 200 GLU D CA  1 
ATOM   4765  C C   . GLU B 1 171 ? 3.142   10.806  30.233  1.00 25.92  ? 200 GLU D C   1 
ATOM   4766  O O   . GLU B 1 171 ? 3.420   11.218  31.341  1.00 26.75  ? 200 GLU D O   1 
ATOM   4767  C CB  . GLU B 1 171 ? 0.788   9.862   29.747  1.00 23.54  ? 200 GLU D CB  1 
ATOM   4768  C CG  . GLU B 1 171 ? -0.663  10.195  29.426  1.00 26.85  ? 200 GLU D CG  1 
ATOM   4769  C CD  . GLU B 1 171 ? -1.322  11.174  30.383  1.00 31.21  ? 200 GLU D CD  1 
ATOM   4770  O OE1 . GLU B 1 171 ? -0.802  11.290  31.500  1.00 32.02  ? 200 GLU D OE1 1 
ATOM   4771  O OE2 . GLU B 1 171 ? -2.352  11.787  30.022  1.00 34.47  ? 200 GLU D OE2 1 
ATOM   4772  N N   . ASP B 1 172 ? 4.003   10.162  29.449  1.00 26.62  ? 201 ASP D N   1 
ATOM   4773  C CA  . ASP B 1 172 ? 5.314   9.755   29.867  1.00 26.98  ? 201 ASP D CA  1 
ATOM   4774  C C   . ASP B 1 172 ? 6.147   10.995  30.106  1.00 23.27  ? 201 ASP D C   1 
ATOM   4775  O O   . ASP B 1 172 ? 6.948   11.041  31.051  1.00 23.14  ? 201 ASP D O   1 
ATOM   4776  C CB  . ASP B 1 172 ? 5.939   8.814   28.842  1.00 31.13  ? 201 ASP D CB  1 
ATOM   4777  C CG  . ASP B 1 172 ? 5.569   7.344   28.989  1.00 33.64  ? 201 ASP D CG  1 
ATOM   4778  O OD1 . ASP B 1 172 ? 4.865   7.025   29.969  1.00 36.55  ? 201 ASP D OD1 1 
ATOM   4779  O OD2 . ASP B 1 172 ? 6.028   6.514   28.157  1.00 32.48  ? 201 ASP D OD2 1 
ATOM   4780  N N   . SER B 1 173 ? 5.974   11.985  29.222  1.00 24.61  ? 202 SER D N   1 
ATOM   4781  C CA  . SER B 1 173 ? 6.694   13.250  29.325  1.00 23.04  ? 202 SER D CA  1 
ATOM   4782  C C   . SER B 1 173 ? 6.292   14.030  30.571  1.00 22.44  ? 202 SER D C   1 
ATOM   4783  O O   . SER B 1 173 ? 7.161   14.503  31.310  1.00 25.10  ? 202 SER D O   1 
ATOM   4784  C CB  . SER B 1 173 ? 6.486   14.113  28.138  1.00 23.60  ? 202 SER D CB  1 
ATOM   4785  O OG  . SER B 1 173 ? 7.086   13.475  27.041  1.00 25.02  ? 202 SER D OG  1 
ATOM   4786  N N   . MET B 1 174 ? 4.995   14.097  30.855  1.00 27.50  ? 203 MET D N   1 
ATOM   4787  C CA  . MET B 1 174 ? 4.535   14.755  32.070  1.00 28.63  ? 203 MET D CA  1 
ATOM   4788  C C   . MET B 1 174 ? 5.073   14.050  33.307  1.00 29.96  ? 203 MET D C   1 
ATOM   4789  O O   . MET B 1 174 ? 5.457   14.734  34.255  1.00 32.45  ? 203 MET D O   1 
ATOM   4790  C CB  . MET B 1 174 ? 3.015   14.758  32.187  1.00 28.99  ? 203 MET D CB  1 
ATOM   4791  C CG  . MET B 1 174 ? 2.368   15.570  31.059  1.00 31.87  ? 203 MET D CG  1 
ATOM   4792  S SD  . MET B 1 174 ? 2.436   17.351  31.293  1.00 31.86  ? 203 MET D SD  1 
ATOM   4793  C CE  . MET B 1 174 ? 1.162   17.422  32.567  1.00 32.56  ? 203 MET D CE  1 
ATOM   4794  N N   . ASP B 1 175 ? 5.100   12.706  33.284  1.00 34.77  ? 204 ASP D N   1 
ATOM   4795  C CA  . ASP B 1 175 ? 5.625   11.913  34.396  1.00 31.04  ? 204 ASP D CA  1 
ATOM   4796  C C   . ASP B 1 175 ? 7.122   12.132  34.596  1.00 31.75  ? 204 ASP D C   1 
ATOM   4797  O O   . ASP B 1 175 ? 7.547   12.229  35.732  1.00 31.91  ? 204 ASP D O   1 
ATOM   4798  C CB  . ASP B 1 175 ? 5.385   10.431  34.222  1.00 35.19  ? 204 ASP D CB  1 
ATOM   4799  C CG  . ASP B 1 175 ? 3.959   9.971   34.495  1.00 39.23  ? 204 ASP D CG  1 
ATOM   4800  O OD1 . ASP B 1 175 ? 3.188   10.763  35.068  1.00 35.13  ? 204 ASP D OD1 1 
ATOM   4801  O OD2 . ASP B 1 175 ? 3.614   8.861   34.045  1.00 35.31  ? 204 ASP D OD2 1 
ATOM   4802  N N   . LEU B 1 176 ? 7.906   12.164  33.497  1.00 29.01  ? 205 LEU D N   1 
ATOM   4803  C CA  . LEU B 1 176 ? 9.338   12.378  33.546  1.00 25.25  ? 205 LEU D CA  1 
ATOM   4804  C C   . LEU B 1 176 ? 9.654   13.774  34.098  1.00 25.26  ? 205 LEU D C   1 
ATOM   4805  O O   . LEU B 1 176 ? 10.476  13.918  35.008  1.00 25.47  ? 205 LEU D O   1 
ATOM   4806  C CB  . LEU B 1 176 ? 9.970   12.170  32.185  1.00 24.03  ? 205 LEU D CB  1 
ATOM   4807  C CG  . LEU B 1 176 ? 11.474  12.426  32.081  1.00 26.87  ? 205 LEU D CG  1 
ATOM   4808  C CD1 . LEU B 1 176 ? 12.269  11.803  33.216  1.00 26.51  ? 205 LEU D CD1 1 
ATOM   4809  C CD2 . LEU B 1 176 ? 11.933  11.899  30.718  1.00 28.91  ? 205 LEU D CD2 1 
ATOM   4810  N N   . ILE B 1 177 ? 9.031   14.802  33.536  1.00 28.04  ? 206 ILE D N   1 
ATOM   4811  C CA  . ILE B 1 177 ? 9.245   16.154  34.022  1.00 29.72  ? 206 ILE D CA  1 
ATOM   4812  C C   . ILE B 1 177 ? 8.959   16.209  35.519  1.00 26.01  ? 206 ILE D C   1 
ATOM   4813  O O   . ILE B 1 177 ? 9.764   16.779  36.247  1.00 25.15  ? 206 ILE D O   1 
ATOM   4814  C CB  . ILE B 1 177 ? 8.426   17.198  33.254  1.00 29.81  ? 206 ILE D CB  1 
ATOM   4815  C CG1 . ILE B 1 177 ? 9.002   17.379  31.868  1.00 28.34  ? 206 ILE D CG1 1 
ATOM   4816  C CG2 . ILE B 1 177 ? 8.370   18.531  34.022  1.00 30.48  ? 206 ILE D CG2 1 
ATOM   4817  C CD1 . ILE B 1 177 ? 8.085   18.090  30.882  1.00 32.57  ? 206 ILE D CD1 1 
ATOM   4818  N N   . ALA B 1 178 ? 7.854   15.624  35.965  1.00 26.81  ? 207 ALA D N   1 
ATOM   4819  C CA  . ALA B 1 178 ? 7.507   15.652  37.388  1.00 30.21  ? 207 ALA D CA  1 
ATOM   4820  C C   . ALA B 1 178 ? 8.580   14.990  38.243  1.00 29.53  ? 207 ALA D C   1 
ATOM   4821  O O   . ALA B 1 178 ? 8.832   15.436  39.371  1.00 29.06  ? 207 ALA D O   1 
ATOM   4822  C CB  . ALA B 1 178 ? 6.182   15.025  37.658  1.00 28.34  ? 207 ALA D CB  1 
ATOM   4823  N N   . LYS B 1 179 ? 9.209   13.932  37.713  1.00 27.41  ? 208 LYS D N   1 
ATOM   4824  C CA  . LYS B 1 179 ? 10.112  13.112  38.507  1.00 29.19  ? 208 LYS D CA  1 
ATOM   4825  C C   . LYS B 1 179 ? 11.535  13.681  38.505  1.00 27.96  ? 208 LYS D C   1 
ATOM   4826  O O   . LYS B 1 179 ? 12.309  13.404  39.409  1.00 27.78  ? 208 LYS D O   1 
ATOM   4827  C CB  . LYS B 1 179 ? 10.116  11.653  38.041  1.00 31.52  ? 208 LYS D CB  1 
ATOM   4828  C CG  . LYS B 1 179 ? 8.848   10.861  38.370  1.00 32.51  ? 208 LYS D CG  1 
ATOM   4829  C CD  . LYS B 1 179 ? 8.746   9.509   37.662  1.00 33.82  ? 208 LYS D CD  1 
ATOM   4830  C CE  . LYS B 1 179 ? 7.296   9.146   37.397  1.00 41.14  ? 208 LYS D CE  1 
ATOM   4831  N NZ  . LYS B 1 179 ? 6.485   9.179   38.631  1.00 39.33  ? 208 LYS D NZ  1 
ATOM   4832  N N   . LEU B 1 180 ? 11.873  14.493  37.507  1.00 28.80  ? 209 LEU D N   1 
ATOM   4833  C CA  . LEU B 1 180 ? 13.251  14.893  37.292  1.00 27.97  ? 209 LEU D CA  1 
ATOM   4834  C C   . LEU B 1 180 ? 13.807  15.631  38.505  1.00 28.86  ? 209 LEU D C   1 
ATOM   4835  O O   . LEU B 1 180 ? 14.887  15.303  38.952  1.00 26.75  ? 209 LEU D O   1 
ATOM   4836  C CB  . LEU B 1 180 ? 13.392  15.711  36.019  1.00 27.76  ? 209 LEU D CB  1 
ATOM   4837  C CG  . LEU B 1 180 ? 13.695  14.885  34.777  1.00 31.50  ? 209 LEU D CG  1 
ATOM   4838  C CD1 . LEU B 1 180 ? 13.708  15.840  33.581  1.00 34.42  ? 209 LEU D CD1 1 
ATOM   4839  C CD2 . LEU B 1 180 ? 14.996  14.127  34.908  1.00 32.48  ? 209 LEU D CD2 1 
ATOM   4840  N N   . PRO B 1 181 ? 13.096  16.611  39.118  1.00 30.40  ? 210 PRO D N   1 
ATOM   4841  C CA  . PRO B 1 181 ? 13.588  17.255  40.333  1.00 27.59  ? 210 PRO D CA  1 
ATOM   4842  C C   . PRO B 1 181 ? 13.883  16.326  41.511  1.00 29.73  ? 210 PRO D C   1 
ATOM   4843  O O   . PRO B 1 181 ? 14.819  16.598  42.272  1.00 31.78  ? 210 PRO D O   1 
ATOM   4844  C CB  . PRO B 1 181 ? 12.440  18.173  40.668  1.00 31.13  ? 210 PRO D CB  1 
ATOM   4845  C CG  . PRO B 1 181 ? 11.815  18.483  39.352  1.00 33.38  ? 210 PRO D CG  1 
ATOM   4846  C CD  . PRO B 1 181 ? 11.823  17.149  38.663  1.00 29.67  ? 210 PRO D CD  1 
ATOM   4847  N N   . CYS B 1 182 ? 13.066  15.261  41.687  1.00 30.52  ? 211 CYS D N   1 
ATOM   4848  C CA  . CYS B 1 182 ? 13.334  14.284  42.742  1.00 34.17  ? 211 CYS D CA  1 
ATOM   4849  C C   . CYS B 1 182 ? 14.617  13.493  42.478  1.00 31.71  ? 211 CYS D C   1 
ATOM   4850  O O   . CYS B 1 182 ? 15.417  13.293  43.392  1.00 29.50  ? 211 CYS D O   1 
ATOM   4851  C CB  . CYS B 1 182 ? 12.170  13.329  42.935  1.00 37.91  ? 211 CYS D CB  1 
ATOM   4852  S SG  . CYS B 1 182 ? 10.591  14.190  43.156  1.00 50.20  ? 211 CYS D SG  1 
ATOM   4853  N N   . VAL B 1 183 ? 14.808  13.054  41.224  1.00 29.32  ? 212 VAL D N   1 
ATOM   4854  C CA  . VAL B 1 183 ? 16.037  12.394  40.821  1.00 27.40  ? 212 VAL D CA  1 
ATOM   4855  C C   . VAL B 1 183 ? 17.220  13.339  41.032  1.00 30.09  ? 212 VAL D C   1 
ATOM   4856  O O   . VAL B 1 183 ? 18.218  12.982  41.664  1.00 27.68  ? 212 VAL D O   1 
ATOM   4857  C CB  . VAL B 1 183 ? 15.998  11.906  39.368  1.00 27.16  ? 212 VAL D CB  1 
ATOM   4858  C CG1 . VAL B 1 183 ? 17.296  11.217  38.981  1.00 27.63  ? 212 VAL D CG1 1 
ATOM   4859  C CG2 . VAL B 1 183 ? 14.808  11.020  39.082  1.00 29.83  ? 212 VAL D CG2 1 
ATOM   4860  N N   . ALA B 1 184 ? 17.096  14.558  40.493  1.00 30.25  ? 213 ALA D N   1 
ATOM   4861  C CA  . ALA B 1 184 ? 18.177  15.517  40.516  1.00 27.51  ? 213 ALA D CA  1 
ATOM   4862  C C   . ALA B 1 184 ? 18.547  15.854  41.967  1.00 31.08  ? 213 ALA D C   1 
ATOM   4863  O O   . ALA B 1 184 ? 19.731  15.943  42.306  1.00 27.78  ? 213 ALA D O   1 
ATOM   4864  C CB  . ALA B 1 184 ? 17.773  16.744  39.738  1.00 26.70  ? 213 ALA D CB  1 
ATOM   4865  N N   . ALA B 1 185 ? 17.543  16.011  42.832  1.00 29.10  ? 214 ALA D N   1 
ATOM   4866  C CA  . ALA B 1 185 ? 17.781  16.341  44.228  1.00 27.92  ? 214 ALA D CA  1 
ATOM   4867  C C   . ALA B 1 185 ? 18.371  15.181  45.031  1.00 28.80  ? 214 ALA D C   1 
ATOM   4868  O O   . ALA B 1 185 ? 19.206  15.398  45.911  1.00 30.18  ? 214 ALA D O   1 
ATOM   4869  C CB  . ALA B 1 185 ? 16.506  16.862  44.842  1.00 32.57  ? 214 ALA D CB  1 
ATOM   4870  N N   . LYS B 1 186 ? 17.906  13.957  44.795  1.00 29.45  ? 215 LYS D N   1 
ATOM   4871  C CA  . LYS B 1 186 ? 18.502  12.777  45.411  1.00 34.20  ? 215 LYS D CA  1 
ATOM   4872  C C   . LYS B 1 186 ? 19.986  12.619  45.053  1.00 35.17  ? 215 LYS D C   1 
ATOM   4873  O O   . LYS B 1 186 ? 20.825  12.225  45.875  1.00 31.40  ? 215 LYS D O   1 
ATOM   4874  C CB  . LYS B 1 186 ? 17.672  11.590  44.935  1.00 39.70  ? 215 LYS D CB  1 
ATOM   4875  C CG  . LYS B 1 186 ? 18.021  10.259  45.527  1.00 50.65  ? 215 LYS D CG  1 
ATOM   4876  C CD  . LYS B 1 186 ? 16.764  9.443   45.803  1.00 59.10  ? 215 LYS D CD  1 
ATOM   4877  C CE  . LYS B 1 186 ? 16.140  9.805   47.113  1.00 61.30  ? 215 LYS D CE  1 
ATOM   4878  N NZ  . LYS B 1 186 ? 16.988  9.322   48.206  1.00 61.49  ? 215 LYS D NZ  1 
ATOM   4879  N N   . ILE B 1 187 ? 20.316  12.893  43.794  1.00 32.28  ? 216 ILE D N   1 
ATOM   4880  C CA  . ILE B 1 187 ? 21.695  12.891  43.367  1.00 31.03  ? 216 ILE D CA  1 
ATOM   4881  C C   . ILE B 1 187 ? 22.461  13.975  44.118  1.00 30.73  ? 216 ILE D C   1 
ATOM   4882  O O   . ILE B 1 187 ? 23.577  13.753  44.572  1.00 31.92  ? 216 ILE D O   1 
ATOM   4883  C CB  . ILE B 1 187 ? 21.831  13.120  41.861  1.00 30.97  ? 216 ILE D CB  1 
ATOM   4884  C CG1 . ILE B 1 187 ? 21.365  11.934  41.056  1.00 27.42  ? 216 ILE D CG1 1 
ATOM   4885  C CG2 . ILE B 1 187 ? 23.257  13.538  41.530  1.00 30.48  ? 216 ILE D CG2 1 
ATOM   4886  C CD1 . ILE B 1 187 ? 20.941  12.283  39.639  1.00 28.96  ? 216 ILE D CD1 1 
ATOM   4887  N N   . TYR B 1 188 ? 21.901  15.177  44.165  1.00 29.55  ? 217 TYR D N   1 
ATOM   4888  C CA  . TYR B 1 188 ? 22.564  16.235  44.887  1.00 26.62  ? 217 TYR D CA  1 
ATOM   4889  C C   . TYR B 1 188 ? 22.828  15.816  46.330  1.00 29.66  ? 217 TYR D C   1 
ATOM   4890  O O   . TYR B 1 188 ? 23.927  15.966  46.829  1.00 31.45  ? 217 TYR D O   1 
ATOM   4891  C CB  . TYR B 1 188 ? 21.744  17.513  44.807  1.00 27.34  ? 217 TYR D CB  1 
ATOM   4892  C CG  . TYR B 1 188 ? 22.463  18.730  45.355  1.00 27.40  ? 217 TYR D CG  1 
ATOM   4893  C CD1 . TYR B 1 188 ? 23.507  19.295  44.648  1.00 30.60  ? 217 TYR D CD1 1 
ATOM   4894  C CD2 . TYR B 1 188 ? 22.086  19.329  46.547  1.00 28.39  ? 217 TYR D CD2 1 
ATOM   4895  C CE1 . TYR B 1 188 ? 24.208  20.377  45.140  1.00 28.05  ? 217 TYR D CE1 1 
ATOM   4896  C CE2 . TYR B 1 188 ? 22.743  20.447  47.028  1.00 31.60  ? 217 TYR D CE2 1 
ATOM   4897  C CZ  . TYR B 1 188 ? 23.805  20.980  46.313  1.00 28.98  ? 217 TYR D CZ  1 
ATOM   4898  O OH  . TYR B 1 188 ? 24.498  22.064  46.770  1.00 28.55  ? 217 TYR D OH  1 
ATOM   4899  N N   . ARG B 1 189 ? 21.815  15.343  47.029  1.00 27.90  ? 218 ARG D N   1 
ATOM   4900  C CA  . ARG B 1 189 ? 21.967  15.056  48.443  1.00 31.30  ? 218 ARG D CA  1 
ATOM   4901  C C   . ARG B 1 189 ? 22.902  13.885  48.704  1.00 32.74  ? 218 ARG D C   1 
ATOM   4902  O O   . ARG B 1 189 ? 23.588  13.865  49.725  1.00 31.62  ? 218 ARG D O   1 
ATOM   4903  C CB  . ARG B 1 189 ? 20.669  14.584  49.088  1.00 33.71  ? 218 ARG D CB  1 
ATOM   4904  C CG  . ARG B 1 189 ? 19.553  15.608  49.091  1.00 36.12  ? 218 ARG D CG  1 
ATOM   4905  C CD  . ARG B 1 189 ? 19.550  16.410  50.355  1.00 40.81  ? 218 ARG D CD  1 
ATOM   4906  N NE  . ARG B 1 189 ? 18.199  16.957  50.477  1.00 47.85  ? 218 ARG D NE  1 
ATOM   4907  C CZ  . ARG B 1 189 ? 17.758  17.665  51.515  1.00 53.49  ? 218 ARG D CZ  1 
ATOM   4908  N NH1 . ARG B 1 189 ? 18.509  17.744  52.606  1.00 42.19  ? 218 ARG D NH1 1 
ATOM   4909  N NH2 . ARG B 1 189 ? 16.560  18.251  51.446  1.00 52.14  ? 218 ARG D NH2 1 
ATOM   4910  N N   . ASN B 1 190 ? 22.880  12.884  47.819  1.00 33.13  ? 219 ASN D N   1 
ATOM   4911  C CA  . ASN B 1 190 ? 23.695  11.697  48.008  1.00 30.54  ? 219 ASN D CA  1 
ATOM   4912  C C   . ASN B 1 190 ? 25.144  12.098  47.874  1.00 30.90  ? 219 ASN D C   1 
ATOM   4913  O O   . ASN B 1 190 ? 25.974  11.602  48.628  1.00 30.40  ? 219 ASN D O   1 
ATOM   4914  C CB  . ASN B 1 190 ? 23.303  10.547  47.087  1.00 28.83  ? 219 ASN D CB  1 
ATOM   4915  C CG  . ASN B 1 190 ? 21.956  10.009  47.503  1.00 34.79  ? 219 ASN D CG  1 
ATOM   4916  O OD1 . ASN B 1 190 ? 21.482  10.308  48.602  1.00 36.45  ? 219 ASN D OD1 1 
ATOM   4917  N ND2 . ASN B 1 190 ? 21.338  9.191   46.666  1.00 38.22  ? 219 ASN D ND2 1 
ATOM   4918  N N   . LEU B 1 191 ? 25.412  13.000  46.923  1.00 29.70  ? 220 LEU D N   1 
ATOM   4919  C CA  . LEU B 1 191 ? 26.772  13.348  46.578  1.00 30.63  ? 220 LEU D CA  1 
ATOM   4920  C C   . LEU B 1 191 ? 27.329  14.347  47.584  1.00 33.38  ? 220 LEU D C   1 
ATOM   4921  O O   . LEU B 1 191 ? 28.495  14.255  47.950  1.00 31.11  ? 220 LEU D O   1 
ATOM   4922  C CB  . LEU B 1 191 ? 26.847  13.884  45.152  1.00 32.61  ? 220 LEU D CB  1 
ATOM   4923  C CG  . LEU B 1 191 ? 26.845  12.820  44.040  1.00 32.29  ? 220 LEU D CG  1 
ATOM   4924  C CD1 . LEU B 1 191 ? 26.774  13.505  42.676  1.00 30.16  ? 220 LEU D CD1 1 
ATOM   4925  C CD2 . LEU B 1 191 ? 28.081  11.958  44.140  1.00 34.21  ? 220 LEU D CD2 1 
ATOM   4926  N N   . TYR B 1 192 ? 26.496  15.281  48.045  1.00 31.28  ? 221 TYR D N   1 
ATOM   4927  C CA  . TYR B 1 192 ? 27.025  16.444  48.725  1.00 33.50  ? 221 TYR D CA  1 
ATOM   4928  C C   . TYR B 1 192 ? 26.372  16.742  50.066  1.00 33.51  ? 221 TYR D C   1 
ATOM   4929  O O   . TYR B 1 192 ? 26.805  17.659  50.745  1.00 39.36  ? 221 TYR D O   1 
ATOM   4930  C CB  . TYR B 1 192 ? 26.842  17.654  47.820  1.00 37.30  ? 221 TYR D CB  1 
ATOM   4931  C CG  . TYR B 1 192 ? 27.319  17.396  46.407  1.00 36.04  ? 221 TYR D CG  1 
ATOM   4932  C CD1 . TYR B 1 192 ? 28.666  17.191  46.126  1.00 41.45  ? 221 TYR D CD1 1 
ATOM   4933  C CD2 . TYR B 1 192 ? 26.437  17.488  45.347  1.00 42.81  ? 221 TYR D CD2 1 
ATOM   4934  C CE1 . TYR B 1 192 ? 29.113  17.020  44.824  1.00 37.48  ? 221 TYR D CE1 1 
ATOM   4935  C CE2 . TYR B 1 192 ? 26.866  17.311  44.043  1.00 44.27  ? 221 TYR D CE2 1 
ATOM   4936  C CZ  . TYR B 1 192 ? 28.205  17.081  43.782  1.00 40.66  ? 221 TYR D CZ  1 
ATOM   4937  O OH  . TYR B 1 192 ? 28.565  16.915  42.484  1.00 35.69  ? 221 TYR D OH  1 
ATOM   4938  N N   . ARG B 1 193 ? 25.333  16.016  50.451  1.00 35.92  ? 222 ARG D N   1 
ATOM   4939  C CA  . ARG B 1 193 ? 24.711  16.265  51.746  1.00 40.66  ? 222 ARG D CA  1 
ATOM   4940  C C   . ARG B 1 193 ? 24.548  14.935  52.465  1.00 39.72  ? 222 ARG D C   1 
ATOM   4941  O O   . ARG B 1 193 ? 23.506  14.680  53.053  1.00 42.14  ? 222 ARG D O   1 
ATOM   4942  C CB  . ARG B 1 193 ? 23.378  17.001  51.609  1.00 40.93  ? 222 ARG D CB  1 
ATOM   4943  C CG  . ARG B 1 193 ? 23.464  18.363  50.945  1.00 43.46  ? 222 ARG D CG  1 
ATOM   4944  C CD  . ARG B 1 193 ? 23.767  19.527  51.874  1.00 50.10  ? 222 ARG D CD  1 
ATOM   4945  N NE  . ARG B 1 193 ? 23.717  20.829  51.178  1.00 52.51  ? 222 ARG D NE  1 
ATOM   4946  C CZ  . ARG B 1 193 ? 24.636  21.333  50.343  1.00 46.24  ? 222 ARG D CZ  1 
ATOM   4947  N NH1 . ARG B 1 193 ? 25.703  20.632  50.011  1.00 44.22  ? 222 ARG D NH1 1 
ATOM   4948  N NH2 . ARG B 1 193 ? 24.503  22.550  49.842  1.00 46.70  ? 222 ARG D NH2 1 
ATOM   4949  N N   . GLU B 1 194 ? 25.564  14.081  52.311  1.00 40.71  ? 223 GLU D N   1 
ATOM   4950  C CA  . GLU B 1 194 ? 25.742  12.889  53.122  1.00 53.75  ? 223 GLU D CA  1 
ATOM   4951  C C   . GLU B 1 194 ? 24.523  11.959  53.019  1.00 49.53  ? 223 GLU D C   1 
ATOM   4952  O O   . GLU B 1 194 ? 24.263  11.176  53.927  1.00 40.59  ? 223 GLU D O   1 
ATOM   4953  C CB  . GLU B 1 194 ? 26.172  13.305  54.540  1.00 66.35  ? 223 GLU D CB  1 
ATOM   4954  C CG  . GLU B 1 194 ? 25.070  13.854  55.455  1.00 78.30  ? 223 GLU D CG  1 
ATOM   4955  C CD  . GLU B 1 194 ? 24.875  15.365  55.602  1.00 89.74  ? 223 GLU D CD  1 
ATOM   4956  O OE1 . GLU B 1 194 ? 25.803  16.128  55.257  1.00 102.90 ? 223 GLU D OE1 1 
ATOM   4957  O OE2 . GLU B 1 194 ? 23.782  15.793  56.057  1.00 85.89  ? 223 GLU D OE2 1 
ATOM   4958  N N   . GLY B 1 195 ? 23.804  11.976  51.882  1.00 45.00  ? 224 GLY D N   1 
ATOM   4959  C CA  . GLY B 1 195 ? 22.747  11.005  51.648  1.00 44.11  ? 224 GLY D CA  1 
ATOM   4960  C C   . GLY B 1 195 ? 21.483  11.246  52.474  1.00 43.10  ? 224 GLY D C   1 
ATOM   4961  O O   . GLY B 1 195 ? 20.628  10.374  52.528  1.00 44.45  ? 224 GLY D O   1 
ATOM   4962  N N   . SER B 1 196 ? 21.340  12.424  53.083  1.00 43.35  ? 225 SER D N   1 
ATOM   4963  C CA  . SER B 1 196 ? 20.097  12.786  53.745  1.00 50.10  ? 225 SER D CA  1 
ATOM   4964  C C   . SER B 1 196 ? 18.969  12.805  52.719  1.00 48.71  ? 225 SER D C   1 
ATOM   4965  O O   . SER B 1 196 ? 19.226  12.972  51.523  1.00 41.60  ? 225 SER D O   1 
ATOM   4966  C CB  . SER B 1 196 ? 20.196  14.130  54.433  1.00 47.15  ? 225 SER D CB  1 
ATOM   4967  O OG  . SER B 1 196 ? 20.565  15.115  53.481  1.00 44.48  ? 225 SER D OG  1 
ATOM   4968  N N   . GLY B 1 197 ? 17.737  12.734  53.239  1.00 45.24  ? 226 GLY D N   1 
ATOM   4969  C CA  . GLY B 1 197 ? 16.531  12.581  52.444  1.00 43.03  ? 226 GLY D CA  1 
ATOM   4970  C C   . GLY B 1 197 ? 16.093  13.887  51.771  1.00 44.44  ? 226 GLY D C   1 
ATOM   4971  O O   . GLY B 1 197 ? 16.253  14.975  52.313  1.00 43.63  ? 226 GLY D O   1 
ATOM   4972  N N   . ILE B 1 198 ? 15.416  13.751  50.626  1.00 42.16  ? 227 ILE D N   1 
ATOM   4973  C CA  . ILE B 1 198 ? 14.974  14.896  49.857  1.00 47.22  ? 227 ILE D CA  1 
ATOM   4974  C C   . ILE B 1 198 ? 13.703  15.476  50.454  1.00 47.00  ? 227 ILE D C   1 
ATOM   4975  O O   . ILE B 1 198 ? 13.276  16.548  50.027  1.00 42.43  ? 227 ILE D O   1 
ATOM   4976  C CB  . ILE B 1 198 ? 14.813  14.560  48.363  1.00 45.70  ? 227 ILE D CB  1 
ATOM   4977  C CG1 . ILE B 1 198 ? 13.788  13.431  48.081  1.00 48.48  ? 227 ILE D CG1 1 
ATOM   4978  C CG2 . ILE B 1 198 ? 16.192  14.256  47.774  1.00 44.65  ? 227 ILE D CG2 1 
ATOM   4979  C CD1 . ILE B 1 198 ? 13.491  13.207  46.595  1.00 42.04  ? 227 ILE D CD1 1 
ATOM   4980  N N   . GLY B 1 199 ? 13.093  14.771  51.415  1.00 41.60  ? 228 GLY D N   1 
ATOM   4981  C CA  . GLY B 1 199 ? 11.834  15.238  51.972  1.00 43.18  ? 228 GLY D CA  1 
ATOM   4982  C C   . GLY B 1 199 ? 10.684  15.047  50.981  1.00 47.73  ? 228 GLY D C   1 
ATOM   4983  O O   . GLY B 1 199 ? 10.764  14.240  50.059  1.00 49.15  ? 228 GLY D O   1 
ATOM   4984  N N   . ALA B 1 200 ? 9.613   15.814  51.175  1.00 47.24  ? 229 ALA D N   1 
ATOM   4985  C CA  . ALA B 1 200 ? 8.340   15.521  50.542  1.00 51.46  ? 229 ALA D CA  1 
ATOM   4986  C C   . ALA B 1 200 ? 8.032   16.599  49.517  1.00 49.57  ? 229 ALA D C   1 
ATOM   4987  O O   . ALA B 1 200 ? 8.497   17.732  49.630  1.00 51.49  ? 229 ALA D O   1 
ATOM   4988  C CB  . ALA B 1 200 ? 7.235   15.429  51.575  1.00 53.08  ? 229 ALA D CB  1 
ATOM   4989  N N   . ILE B 1 201 ? 7.291   16.190  48.491  1.00 45.88  ? 230 ILE D N   1 
ATOM   4990  C CA  . ILE B 1 201 ? 6.751   17.111  47.521  1.00 41.17  ? 230 ILE D CA  1 
ATOM   4991  C C   . ILE B 1 201 ? 5.538   17.782  48.141  1.00 41.44  ? 230 ILE D C   1 
ATOM   4992  O O   . ILE B 1 201 ? 4.683   17.101  48.694  1.00 48.10  ? 230 ILE D O   1 
ATOM   4993  C CB  . ILE B 1 201 ? 6.378   16.380  46.221  1.00 41.40  ? 230 ILE D CB  1 
ATOM   4994  C CG1 . ILE B 1 201 ? 7.604   16.029  45.386  1.00 47.55  ? 230 ILE D CG1 1 
ATOM   4995  C CG2 . ILE B 1 201 ? 5.369   17.190  45.413  1.00 41.72  ? 230 ILE D CG2 1 
ATOM   4996  C CD1 . ILE B 1 201 ? 8.308   17.218  44.746  1.00 48.04  ? 230 ILE D CD1 1 
ATOM   4997  N N   . ASP B 1 202 ? 5.444   19.101  47.964  1.00 41.87  ? 231 ASP D N   1 
ATOM   4998  C CA  . ASP B 1 202 ? 4.256   19.837  48.340  1.00 45.18  ? 231 ASP D CA  1 
ATOM   4999  C C   . ASP B 1 202 ? 3.357   19.980  47.111  1.00 46.11  ? 231 ASP D C   1 
ATOM   5000  O O   . ASP B 1 202 ? 3.729   20.563  46.084  1.00 38.21  ? 231 ASP D O   1 
ATOM   5001  C CB  . ASP B 1 202 ? 4.613   21.131  49.053  1.00 46.18  ? 231 ASP D CB  1 
ATOM   5002  C CG  . ASP B 1 202 ? 3.450   21.964  49.591  1.00 52.04  ? 231 ASP D CG  1 
ATOM   5003  O OD1 . ASP B 1 202 ? 2.258   21.667  49.249  1.00 50.16  ? 231 ASP D OD1 1 
ATOM   5004  O OD2 . ASP B 1 202 ? 3.752   22.913  50.351  1.00 47.53  ? 231 ASP D OD2 1 
ATOM   5005  N N   . SER B 1 203 ? 2.119   19.503  47.274  1.00 39.29  ? 232 SER D N   1 
ATOM   5006  C CA  . SER B 1 203 ? 1.186   19.439  46.162  1.00 42.70  ? 232 SER D CA  1 
ATOM   5007  C C   . SER B 1 203 ? 0.808   20.838  45.688  1.00 39.90  ? 232 SER D C   1 
ATOM   5008  O O   . SER B 1 203 ? 0.237   20.969  44.612  1.00 44.28  ? 232 SER D O   1 
ATOM   5009  C CB  . SER B 1 203 ? -0.046  18.642  46.532  1.00 47.96  ? 232 SER D CB  1 
ATOM   5010  O OG  . SER B 1 203 ? -0.990  19.470  47.200  1.00 56.04  ? 232 SER D OG  1 
ATOM   5011  N N   . ASN B 1 204 ? 1.052   21.870  46.513  1.00 41.38  ? 233 ASN D N   1 
ATOM   5012  C CA  . ASN B 1 204 ? 0.605   23.209  46.177  1.00 39.90  ? 233 ASN D CA  1 
ATOM   5013  C C   . ASN B 1 204 ? 1.739   24.128  45.724  1.00 41.49  ? 233 ASN D C   1 
ATOM   5014  O O   . ASN B 1 204 ? 1.497   25.308  45.511  1.00 44.60  ? 233 ASN D O   1 
ATOM   5015  C CB  . ASN B 1 204 ? -0.136  23.812  47.357  1.00 50.05  ? 233 ASN D CB  1 
ATOM   5016  C CG  . ASN B 1 204 ? -1.398  23.029  47.595  1.00 54.32  ? 233 ASN D CG  1 
ATOM   5017  O OD1 . ASN B 1 204 ? -2.188  22.854  46.654  1.00 52.40  ? 233 ASN D OD1 1 
ATOM   5018  N ND2 . ASN B 1 204 ? -1.543  22.480  48.792  1.00 55.43  ? 233 ASN D ND2 1 
ATOM   5019  N N   . LEU B 1 205 ? 2.953   23.603  45.528  1.00 38.98  ? 234 LEU D N   1 
ATOM   5020  C CA  . LEU B 1 205 ? 4.087   24.440  45.159  1.00 39.93  ? 234 LEU D CA  1 
ATOM   5021  C C   . LEU B 1 205 ? 4.384   24.242  43.676  1.00 38.26  ? 234 LEU D C   1 
ATOM   5022  O O   . LEU B 1 205 ? 4.178   23.149  43.139  1.00 39.53  ? 234 LEU D O   1 
ATOM   5023  C CB  . LEU B 1 205 ? 5.325   24.134  46.007  1.00 41.55  ? 234 LEU D CB  1 
ATOM   5024  C CG  . LEU B 1 205 ? 5.280   24.464  47.507  1.00 43.17  ? 234 LEU D CG  1 
ATOM   5025  C CD1 . LEU B 1 205 ? 6.503   23.927  48.262  1.00 40.70  ? 234 LEU D CD1 1 
ATOM   5026  C CD2 . LEU B 1 205 ? 5.149   25.962  47.728  1.00 43.23  ? 234 LEU D CD2 1 
ATOM   5027  N N   . ASP B 1 206 ? 4.937   25.284  43.041  1.00 34.08  ? 235 ASP D N   1 
ATOM   5028  C CA  . ASP B 1 206 ? 5.449   25.135  41.688  1.00 33.15  ? 235 ASP D CA  1 
ATOM   5029  C C   . ASP B 1 206 ? 6.682   24.232  41.722  1.00 31.02  ? 235 ASP D C   1 
ATOM   5030  O O   . ASP B 1 206 ? 7.313   24.016  42.740  1.00 34.82  ? 235 ASP D O   1 
ATOM   5031  C CB  . ASP B 1 206 ? 5.771   26.459  41.007  1.00 34.80  ? 235 ASP D CB  1 
ATOM   5032  C CG  . ASP B 1 206 ? 6.778   27.339  41.737  1.00 42.32  ? 235 ASP D CG  1 
ATOM   5033  O OD1 . ASP B 1 206 ? 6.382   27.983  42.734  1.00 49.95  ? 235 ASP D OD1 1 
ATOM   5034  O OD2 . ASP B 1 206 ? 7.949   27.366  41.319  1.00 40.34  ? 235 ASP D OD2 1 
ATOM   5035  N N   . TRP B 1 207 ? 7.010   23.735  40.550  1.00 28.70  ? 236 TRP D N   1 
ATOM   5036  C CA  . TRP B 1 207 ? 8.034   22.750  40.312  1.00 26.24  ? 236 TRP D CA  1 
ATOM   5037  C C   . TRP B 1 207 ? 9.417   23.227  40.797  1.00 31.12  ? 236 TRP D C   1 
ATOM   5038  O O   . TRP B 1 207 ? 10.181  22.462  41.383  1.00 24.28  ? 236 TRP D O   1 
ATOM   5039  C CB  . TRP B 1 207 ? 7.931   22.557  38.794  1.00 27.32  ? 236 TRP D CB  1 
ATOM   5040  C CG  . TRP B 1 207 ? 8.695   21.441  38.158  1.00 31.69  ? 236 TRP D CG  1 
ATOM   5041  C CD1 . TRP B 1 207 ? 8.442   20.102  38.250  1.00 34.35  ? 236 TRP D CD1 1 
ATOM   5042  C CD2 . TRP B 1 207 ? 9.735   21.596  37.172  1.00 28.80  ? 236 TRP D CD2 1 
ATOM   5043  N NE1 . TRP B 1 207 ? 9.300   19.408  37.448  1.00 29.31  ? 236 TRP D NE1 1 
ATOM   5044  C CE2 . TRP B 1 207 ? 10.101  20.303  36.772  1.00 26.57  ? 236 TRP D CE2 1 
ATOM   5045  C CE3 . TRP B 1 207 ? 10.403  22.698  36.626  1.00 28.03  ? 236 TRP D CE3 1 
ATOM   5046  C CZ2 . TRP B 1 207 ? 11.105  20.085  35.834  1.00 29.91  ? 236 TRP D CZ2 1 
ATOM   5047  C CZ3 . TRP B 1 207 ? 11.375  22.485  35.672  1.00 30.50  ? 236 TRP D CZ3 1 
ATOM   5048  C CH2 . TRP B 1 207 ? 11.729  21.186  35.293  1.00 31.39  ? 236 TRP D CH2 1 
ATOM   5049  N N   . SER B 1 208 ? 9.780   24.484  40.498  1.00 29.06  ? 237 SER D N   1 
ATOM   5050  C CA  . SER B 1 208 ? 11.069  25.004  40.904  1.00 31.17  ? 237 SER D CA  1 
ATOM   5051  C C   . SER B 1 208 ? 11.207  25.026  42.427  1.00 32.89  ? 237 SER D C   1 
ATOM   5052  O O   . SER B 1 208 ? 12.292  24.807  42.947  1.00 28.06  ? 237 SER D O   1 
ATOM   5053  C CB  . SER B 1 208 ? 11.321  26.363  40.355  1.00 30.88  ? 237 SER D CB  1 
ATOM   5054  O OG  . SER B 1 208 ? 11.250  26.363  38.934  1.00 30.28  ? 237 SER D OG  1 
ATOM   5055  N N   . HIS B 1 209 ? 10.111  25.281  43.134  1.00 36.61  ? 238 HIS D N   1 
ATOM   5056  C CA  . HIS B 1 209 ? 10.149  25.427  44.580  1.00 37.16  ? 238 HIS D CA  1 
ATOM   5057  C C   . HIS B 1 209 ? 10.253  24.055  45.244  1.00 31.38  ? 238 HIS D C   1 
ATOM   5058  O O   . HIS B 1 209 ? 11.025  23.883  46.183  1.00 33.27  ? 238 HIS D O   1 
ATOM   5059  C CB  . HIS B 1 209 ? 8.899   26.167  45.076  1.00 41.06  ? 238 HIS D CB  1 
ATOM   5060  C CG  . HIS B 1 209 ? 9.044   26.717  46.458  1.00 42.92  ? 238 HIS D CG  1 
ATOM   5061  N ND1 . HIS B 1 209 ? 8.148   27.626  46.967  1.00 43.52  ? 238 HIS D ND1 1 
ATOM   5062  C CD2 . HIS B 1 209 ? 9.944   26.499  47.420  1.00 40.91  ? 238 HIS D CD2 1 
ATOM   5063  C CE1 . HIS B 1 209 ? 8.528   27.976  48.182  1.00 46.81  ? 238 HIS D CE1 1 
ATOM   5064  N NE2 . HIS B 1 209 ? 9.610   27.304  48.476  1.00 47.20  ? 238 HIS D NE2 1 
ATOM   5065  N N   . ASN B 1 210 ? 9.461   23.095  44.762  1.00 31.06  ? 239 ASN D N   1 
ATOM   5066  C CA  . ASN B 1 210 ? 9.625   21.699  45.138  1.00 32.19  ? 239 ASN D CA  1 
ATOM   5067  C C   . ASN B 1 210 ? 11.081  21.293  44.901  1.00 32.74  ? 239 ASN D C   1 
ATOM   5068  O O   . ASN B 1 210 ? 11.686  20.639  45.744  1.00 33.81  ? 239 ASN D O   1 
ATOM   5069  C CB  . ASN B 1 210 ? 8.626   20.764  44.435  1.00 33.34  ? 239 ASN D CB  1 
ATOM   5070  C CG  . ASN B 1 210 ? 7.285   20.718  45.145  1.00 36.47  ? 239 ASN D CG  1 
ATOM   5071  O OD1 . ASN B 1 210 ? 6.213   20.621  44.519  1.00 31.51  ? 239 ASN D OD1 1 
ATOM   5072  N ND2 . ASN B 1 210 ? 7.331   20.740  46.465  1.00 34.50  ? 239 ASN D ND2 1 
ATOM   5073  N N   . PHE B 1 211 ? 11.662  21.682  43.760  1.00 30.39  ? 240 PHE D N   1 
ATOM   5074  C CA  . PHE B 1 211 ? 13.037  21.287  43.467  1.00 31.19  ? 240 PHE D CA  1 
ATOM   5075  C C   . PHE B 1 211 ? 14.022  21.898  44.463  1.00 27.58  ? 240 PHE D C   1 
ATOM   5076  O O   . PHE B 1 211 ? 14.961  21.240  44.898  1.00 28.38  ? 240 PHE D O   1 
ATOM   5077  C CB  . PHE B 1 211 ? 13.468  21.743  42.064  1.00 29.70  ? 240 PHE D CB  1 
ATOM   5078  C CG  . PHE B 1 211 ? 14.814  21.262  41.538  1.00 27.38  ? 240 PHE D CG  1 
ATOM   5079  C CD1 . PHE B 1 211 ? 15.433  20.138  42.044  1.00 25.94  ? 240 PHE D CD1 1 
ATOM   5080  C CD2 . PHE B 1 211 ? 15.447  21.935  40.492  1.00 31.26  ? 240 PHE D CD2 1 
ATOM   5081  C CE1 . PHE B 1 211 ? 16.636  19.702  41.539  1.00 28.45  ? 240 PHE D CE1 1 
ATOM   5082  C CE2 . PHE B 1 211 ? 16.655  21.490  39.989  1.00 32.26  ? 240 PHE D CE2 1 
ATOM   5083  C CZ  . PHE B 1 211 ? 17.263  20.389  40.530  1.00 32.46  ? 240 PHE D CZ  1 
ATOM   5084  N N   . THR B 1 212 ? 13.911  23.199  44.748  1.00 26.57  ? 241 THR D N   1 
ATOM   5085  C CA  . THR B 1 212 ? 14.864  23.791  45.684  1.00 28.38  ? 241 THR D CA  1 
ATOM   5086  C C   . THR B 1 212 ? 14.644  23.260  47.107  1.00 29.70  ? 241 THR D C   1 
ATOM   5087  O O   . THR B 1 212 ? 15.607  23.060  47.831  1.00 30.30  ? 241 THR D O   1 
ATOM   5088  C CB  . THR B 1 212 ? 14.887  25.316  45.622  1.00 31.45  ? 241 THR D CB  1 
ATOM   5089  O OG1 . THR B 1 212 ? 13.602  25.811  45.947  1.00 28.16  ? 241 THR D OG1 1 
ATOM   5090  C CG2 . THR B 1 212 ? 15.289  25.816  44.249  1.00 32.05  ? 241 THR D CG2 1 
ATOM   5091  N N   . ASN B 1 213 ? 13.400  22.957  47.493  1.00 32.96  ? 242 ASN D N   1 
ATOM   5092  C CA  . ASN B 1 213 ? 13.144  22.340  48.791  1.00 33.82  ? 242 ASN D CA  1 
ATOM   5093  C C   . ASN B 1 213 ? 13.919  21.032  48.889  1.00 31.10  ? 242 ASN D C   1 
ATOM   5094  O O   . ASN B 1 213 ? 14.604  20.785  49.874  1.00 30.79  ? 242 ASN D O   1 
ATOM   5095  C CB  . ASN B 1 213 ? 11.661  22.119  49.042  1.00 32.69  ? 242 ASN D CB  1 
ATOM   5096  C CG  . ASN B 1 213 ? 10.970  23.391  49.483  1.00 36.34  ? 242 ASN D CG  1 
ATOM   5097  O OD1 . ASN B 1 213 ? 11.657  24.330  49.869  1.00 30.08  ? 242 ASN D OD1 1 
ATOM   5098  N ND2 . ASN B 1 213 ? 9.637   23.422  49.474  1.00 34.94  ? 242 ASN D ND2 1 
ATOM   5099  N N   . MET B 1 214 ? 13.854  20.241  47.820  1.00 29.96  ? 243 MET D N   1 
ATOM   5100  C CA  . MET B 1 214 ? 14.418  18.906  47.830  1.00 30.30  ? 243 MET D CA  1 
ATOM   5101  C C   . MET B 1 214 ? 15.946  19.003  47.841  1.00 27.24  ? 243 MET D C   1 
ATOM   5102  O O   . MET B 1 214 ? 16.614  18.170  48.436  1.00 25.10  ? 243 MET D O   1 
ATOM   5103  C CB  . MET B 1 214 ? 13.862  18.098  46.645  1.00 32.92  ? 243 MET D CB  1 
ATOM   5104  C CG  . MET B 1 214 ? 12.401  17.639  46.839  1.00 32.07  ? 243 MET D CG  1 
ATOM   5105  S SD  . MET B 1 214 ? 11.839  16.499  45.558  1.00 40.90  ? 243 MET D SD  1 
ATOM   5106  C CE  . MET B 1 214 ? 11.725  17.685  44.214  1.00 34.26  ? 243 MET D CE  1 
ATOM   5107  N N   . LEU B 1 215 ? 16.526  19.990  47.152  1.00 27.66  ? 244 LEU D N   1 
ATOM   5108  C CA  . LEU B 1 215 ? 17.972  20.179  47.197  1.00 29.96  ? 244 LEU D CA  1 
ATOM   5109  C C   . LEU B 1 215 ? 18.421  20.542  48.614  1.00 32.18  ? 244 LEU D C   1 
ATOM   5110  O O   . LEU B 1 215 ? 19.587  20.402  48.957  1.00 34.25  ? 244 LEU D O   1 
ATOM   5111  C CB  . LEU B 1 215 ? 18.370  21.264  46.187  1.00 29.11  ? 244 LEU D CB  1 
ATOM   5112  C CG  . LEU B 1 215 ? 18.237  20.909  44.700  1.00 29.21  ? 244 LEU D CG  1 
ATOM   5113  C CD1 . LEU B 1 215 ? 18.441  22.128  43.796  1.00 29.40  ? 244 LEU D CD1 1 
ATOM   5114  C CD2 . LEU B 1 215 ? 19.198  19.796  44.277  1.00 31.54  ? 244 LEU D CD2 1 
ATOM   5115  N N   . GLY B 1 216 ? 17.500  21.074  49.420  1.00 33.44  ? 245 GLY D N   1 
ATOM   5116  C CA  . GLY B 1 216 ? 17.816  21.457  50.783  1.00 35.26  ? 245 GLY D CA  1 
ATOM   5117  C C   . GLY B 1 216 ? 18.101  22.944  50.923  1.00 35.86  ? 245 GLY D C   1 
ATOM   5118  O O   . GLY B 1 216 ? 18.727  23.342  51.893  1.00 38.97  ? 245 GLY D O   1 
ATOM   5119  N N   . TYR B 1 217 ? 17.638  23.738  49.953  1.00 35.09  ? 246 TYR D N   1 
ATOM   5120  C CA  . TYR B 1 217 ? 17.794  25.176  49.963  1.00 36.89  ? 246 TYR D CA  1 
ATOM   5121  C C   . TYR B 1 217 ? 16.510  25.825  50.476  1.00 35.33  ? 246 TYR D C   1 
ATOM   5122  O O   . TYR B 1 217 ? 15.426  25.321  50.232  1.00 33.96  ? 246 TYR D O   1 
ATOM   5123  C CB  . TYR B 1 217 ? 18.117  25.597  48.526  1.00 37.19  ? 246 TYR D CB  1 
ATOM   5124  C CG  . TYR B 1 217 ? 19.543  25.306  48.107  1.00 39.96  ? 246 TYR D CG  1 
ATOM   5125  C CD1 . TYR B 1 217 ? 19.914  24.031  47.706  1.00 38.40  ? 246 TYR D CD1 1 
ATOM   5126  C CD2 . TYR B 1 217 ? 20.518  26.305  48.116  1.00 39.20  ? 246 TYR D CD2 1 
ATOM   5127  C CE1 . TYR B 1 217 ? 21.216  23.755  47.326  1.00 38.66  ? 246 TYR D CE1 1 
ATOM   5128  C CE2 . TYR B 1 217 ? 21.829  26.031  47.765  1.00 39.84  ? 246 TYR D CE2 1 
ATOM   5129  C CZ  . TYR B 1 217 ? 22.172  24.754  47.355  1.00 37.80  ? 246 TYR D CZ  1 
ATOM   5130  O OH  . TYR B 1 217 ? 23.458  24.448  47.046  1.00 36.58  ? 246 TYR D OH  1 
ATOM   5131  N N   . THR B 1 218 ? 16.648  26.950  51.178  1.00 40.36  ? 247 THR D N   1 
ATOM   5132  C CA  . THR B 1 218 ? 15.517  27.717  51.691  1.00 46.33  ? 247 THR D CA  1 
ATOM   5133  C C   . THR B 1 218 ? 15.858  29.201  51.589  1.00 45.15  ? 247 THR D C   1 
ATOM   5134  O O   . THR B 1 218 ? 16.146  29.868  52.578  1.00 56.80  ? 247 THR D O   1 
ATOM   5135  C CB  . THR B 1 218 ? 15.211  27.329  53.142  1.00 57.84  ? 247 THR D CB  1 
ATOM   5136  O OG1 . THR B 1 218 ? 16.473  27.447  53.809  1.00 64.70  ? 247 THR D OG1 1 
ATOM   5137  C CG2 . THR B 1 218 ? 14.625  25.933  53.281  1.00 56.00  ? 247 THR D CG2 1 
ATOM   5138  N N   . ASP B 1 219 ? 15.800  29.709  50.370  1.00 47.72  ? 248 ASP D N   1 
ATOM   5139  C CA  . ASP B 1 219 ? 16.246  31.046  50.041  1.00 37.07  ? 248 ASP D CA  1 
ATOM   5140  C C   . ASP B 1 219 ? 15.435  31.445  48.826  1.00 36.62  ? 248 ASP D C   1 
ATOM   5141  O O   . ASP B 1 219 ? 15.587  30.819  47.755  1.00 27.21  ? 248 ASP D O   1 
ATOM   5142  C CB  . ASP B 1 219 ? 17.732  31.014  49.803  1.00 38.21  ? 248 ASP D CB  1 
ATOM   5143  C CG  . ASP B 1 219 ? 18.345  32.253  49.181  1.00 38.10  ? 248 ASP D CG  1 
ATOM   5144  O OD1 . ASP B 1 219 ? 17.613  33.145  48.720  1.00 50.97  ? 248 ASP D OD1 1 
ATOM   5145  O OD2 . ASP B 1 219 ? 19.566  32.302  49.162  1.00 37.51  ? 248 ASP D OD2 1 
ATOM   5146  N N   . HIS B 1 220 ? 14.518  32.402  49.057  1.00 27.17  ? 249 HIS D N   1 
ATOM   5147  C CA  . HIS B 1 220 ? 13.511  32.788  48.090  1.00 32.76  ? 249 HIS D CA  1 
ATOM   5148  C C   . HIS B 1 220 ? 14.240  33.198  46.811  1.00 31.88  ? 249 HIS D C   1 
ATOM   5149  O O   . HIS B 1 220 ? 13.777  32.897  45.723  1.00 30.23  ? 249 HIS D O   1 
ATOM   5150  C CB  . HIS B 1 220 ? 12.587  33.898  48.636  1.00 34.54  ? 249 HIS D CB  1 
ATOM   5151  C CG  . HIS B 1 220 ? 11.788  34.666  47.613  1.00 40.63  ? 249 HIS D CG  1 
ATOM   5152  N ND1 . HIS B 1 220 ? 10.567  34.253  47.109  1.00 45.55  ? 249 HIS D ND1 1 
ATOM   5153  C CD2 . HIS B 1 220 ? 12.051  35.844  46.978  1.00 42.24  ? 249 HIS D CD2 1 
ATOM   5154  C CE1 . HIS B 1 220 ? 10.113  35.145  46.219  1.00 41.80  ? 249 HIS D CE1 1 
ATOM   5155  N NE2 . HIS B 1 220 ? 10.990  36.123  46.123  1.00 42.49  ? 249 HIS D NE2 1 
ATOM   5156  N N   . GLN B 1 221 ? 15.392  33.851  46.946  1.00 32.26  ? 250 GLN D N   1 
ATOM   5157  C CA  . GLN B 1 221 ? 16.058  34.391  45.774  1.00 37.55  ? 250 GLN D CA  1 
ATOM   5158  C C   . GLN B 1 221 ? 16.672  33.290  44.910  1.00 37.21  ? 250 GLN D C   1 
ATOM   5159  O O   . GLN B 1 221 ? 16.768  33.465  43.706  1.00 35.07  ? 250 GLN D O   1 
ATOM   5160  C CB  . GLN B 1 221 ? 17.202  35.325  46.120  1.00 41.13  ? 250 GLN D CB  1 
ATOM   5161  C CG  . GLN B 1 221 ? 16.754  36.760  46.338  1.00 49.11  ? 250 GLN D CG  1 
ATOM   5162  C CD  . GLN B 1 221 ? 17.903  37.701  46.659  1.00 56.92  ? 250 GLN D CD  1 
ATOM   5163  O OE1 . GLN B 1 221 ? 17.675  38.901  46.883  1.00 51.48  ? 250 GLN D OE1 1 
ATOM   5164  N NE2 . GLN B 1 221 ? 19.131  37.173  46.698  1.00 40.94  ? 250 GLN D NE2 1 
ATOM   5165  N N   . PHE B 1 222 ? 17.117  32.194  45.537  1.00 33.61  ? 251 PHE D N   1 
ATOM   5166  C CA  . PHE B 1 222 ? 17.655  31.059  44.806  1.00 33.60  ? 251 PHE D CA  1 
ATOM   5167  C C   . PHE B 1 222 ? 16.539  30.336  44.056  1.00 31.38  ? 251 PHE D C   1 
ATOM   5168  O O   . PHE B 1 222 ? 16.755  29.788  42.969  1.00 32.17  ? 251 PHE D O   1 
ATOM   5169  C CB  . PHE B 1 222 ? 18.365  30.108  45.766  1.00 30.55  ? 251 PHE D CB  1 
ATOM   5170  C CG  . PHE B 1 222 ? 18.903  28.888  45.055  1.00 30.26  ? 251 PHE D CG  1 
ATOM   5171  C CD1 . PHE B 1 222 ? 19.872  29.008  44.070  1.00 30.90  ? 251 PHE D CD1 1 
ATOM   5172  C CD2 . PHE B 1 222 ? 18.419  27.629  45.356  1.00 30.69  ? 251 PHE D CD2 1 
ATOM   5173  C CE1 . PHE B 1 222 ? 20.338  27.888  43.393  1.00 30.52  ? 251 PHE D CE1 1 
ATOM   5174  C CE2 . PHE B 1 222 ? 18.887  26.518  44.673  1.00 32.65  ? 251 PHE D CE2 1 
ATOM   5175  C CZ  . PHE B 1 222 ? 19.869  26.649  43.719  1.00 35.24  ? 251 PHE D CZ  1 
ATOM   5176  N N   . THR B 1 223 ? 15.361  30.260  44.680  1.00 29.52  ? 252 THR D N   1 
ATOM   5177  C CA  . THR B 1 223 ? 14.205  29.735  43.997  1.00 28.47  ? 252 THR D CA  1 
ATOM   5178  C C   . THR B 1 223 ? 13.819  30.623  42.821  1.00 29.27  ? 252 THR D C   1 
ATOM   5179  O O   . THR B 1 223 ? 13.373  30.098  41.800  1.00 35.69  ? 252 THR D O   1 
ATOM   5180  C CB  . THR B 1 223 ? 13.028  29.545  44.935  1.00 30.88  ? 252 THR D CB  1 
ATOM   5181  O OG1 . THR B 1 223 ? 13.520  28.675  45.955  1.00 30.84  ? 252 THR D OG1 1 
ATOM   5182  C CG2 . THR B 1 223 ? 11.878  28.928  44.172  1.00 27.44  ? 252 THR D CG2 1 
ATOM   5183  N N   . GLU B 1 224 ? 13.955  31.943  42.960  1.00 26.92  ? 253 GLU D N   1 
ATOM   5184  C CA  . GLU B 1 224 ? 13.704  32.850  41.851  1.00 28.47  ? 253 GLU D CA  1 
ATOM   5185  C C   . GLU B 1 224 ? 14.696  32.613  40.707  1.00 29.51  ? 253 GLU D C   1 
ATOM   5186  O O   . GLU B 1 224 ? 14.268  32.524  39.562  1.00 25.76  ? 253 GLU D O   1 
ATOM   5187  C CB  . GLU B 1 224 ? 13.670  34.308  42.288  1.00 31.72  ? 253 GLU D CB  1 
ATOM   5188  C CG  . GLU B 1 224 ? 12.348  34.687  42.956  1.00 35.48  ? 253 GLU D CG  1 
ATOM   5189  C CD  . GLU B 1 224 ? 11.193  34.739  41.962  1.00 38.25  ? 253 GLU D CD  1 
ATOM   5190  O OE1 . GLU B 1 224 ? 11.182  35.702  41.153  1.00 40.64  ? 253 GLU D OE1 1 
ATOM   5191  O OE2 . GLU B 1 224 ? 10.366  33.794  41.902  1.00 34.73  ? 253 GLU D OE2 1 
ATOM   5192  N N   . LEU B 1 225 ? 15.995  32.499  41.027  1.00 28.89  ? 254 LEU D N   1 
ATOM   5193  C CA  . LEU B 1 225 ? 17.038  32.176  40.064  1.00 27.99  ? 254 LEU D CA  1 
ATOM   5194  C C   . LEU B 1 225 ? 16.765  30.857  39.329  1.00 26.90  ? 254 LEU D C   1 
ATOM   5195  O O   . LEU B 1 225 ? 16.895  30.792  38.107  1.00 27.73  ? 254 LEU D O   1 
ATOM   5196  C CB  . LEU B 1 225 ? 18.399  32.157  40.748  1.00 26.73  ? 254 LEU D CB  1 
ATOM   5197  C CG  . LEU B 1 225 ? 19.573  31.646  39.902  1.00 28.13  ? 254 LEU D CG  1 
ATOM   5198  C CD1 . LEU B 1 225 ? 19.833  32.612  38.787  1.00 30.20  ? 254 LEU D CD1 1 
ATOM   5199  C CD2 . LEU B 1 225 ? 20.835  31.486  40.703  1.00 31.55  ? 254 LEU D CD2 1 
ATOM   5200  N N   . THR B 1 226 ? 16.409  29.817  40.095  1.00 30.38  ? 255 THR D N   1 
ATOM   5201  C CA  . THR B 1 226 ? 16.097  28.500  39.587  1.00 27.23  ? 255 THR D CA  1 
ATOM   5202  C C   . THR B 1 226 ? 14.932  28.560  38.595  1.00 27.54  ? 255 THR D C   1 
ATOM   5203  O O   . THR B 1 226 ? 15.050  27.979  37.525  1.00 23.88  ? 255 THR D O   1 
ATOM   5204  C CB  . THR B 1 226 ? 15.752  27.567  40.734  1.00 29.79  ? 255 THR D CB  1 
ATOM   5205  O OG1 . THR B 1 226 ? 16.923  27.476  41.526  1.00 29.53  ? 255 THR D OG1 1 
ATOM   5206  C CG2 . THR B 1 226 ? 15.406  26.183  40.226  1.00 31.78  ? 255 THR D CG2 1 
ATOM   5207  N N   . ARG B 1 227 ? 13.837  29.254  38.945  1.00 22.21  ? 256 ARG D N   1 
ATOM   5208  C CA  . ARG B 1 227 ? 12.735  29.530  38.031  1.00 25.80  ? 256 ARG D CA  1 
ATOM   5209  C C   . ARG B 1 227 ? 13.275  30.128  36.736  1.00 26.86  ? 256 ARG D C   1 
ATOM   5210  O O   . ARG B 1 227 ? 12.886  29.728  35.646  1.00 29.39  ? 256 ARG D O   1 
ATOM   5211  C CB  . ARG B 1 227 ? 11.686  30.526  38.562  1.00 27.56  ? 256 ARG D CB  1 
ATOM   5212  C CG  . ARG B 1 227 ? 10.869  29.908  39.681  1.00 30.44  ? 256 ARG D CG  1 
ATOM   5213  C CD  . ARG B 1 227 ? 10.093  30.899  40.525  1.00 32.31  ? 256 ARG D CD  1 
ATOM   5214  N NE  . ARG B 1 227 ? 9.438   30.117  41.579  1.00 33.98  ? 256 ARG D NE  1 
ATOM   5215  C CZ  . ARG B 1 227 ? 9.071   30.528  42.795  1.00 35.00  ? 256 ARG D CZ  1 
ATOM   5216  N NH1 . ARG B 1 227 ? 9.396   31.710  43.241  1.00 34.47  ? 256 ARG D NH1 1 
ATOM   5217  N NH2 . ARG B 1 227 ? 8.352   29.748  43.562  1.00 35.81  ? 256 ARG D NH2 1 
ATOM   5218  N N   . LEU B 1 228 ? 14.110  31.150  36.836  1.00 28.35  ? 257 LEU D N   1 
ATOM   5219  C CA  . LEU B 1 228 ? 14.577  31.816  35.622  1.00 24.52  ? 257 LEU D CA  1 
ATOM   5220  C C   . LEU B 1 228 ? 15.508  30.856  34.871  1.00 27.94  ? 257 LEU D C   1 
ATOM   5221  O O   . LEU B 1 228 ? 15.463  30.783  33.646  1.00 26.15  ? 257 LEU D O   1 
ATOM   5222  C CB  . LEU B 1 228 ? 15.289  33.103  35.993  1.00 28.64  ? 257 LEU D CB  1 
ATOM   5223  C CG  . LEU B 1 228 ? 16.046  33.831  34.875  1.00 32.05  ? 257 LEU D CG  1 
ATOM   5224  C CD1 . LEU B 1 228 ? 15.071  34.442  33.904  1.00 31.81  ? 257 LEU D CD1 1 
ATOM   5225  C CD2 . LEU B 1 228 ? 16.956  34.883  35.458  1.00 37.20  ? 257 LEU D CD2 1 
ATOM   5226  N N   . TYR B 1 229 ? 16.363  30.154  35.611  1.00 25.53  ? 258 TYR D N   1 
ATOM   5227  C CA  . TYR B 1 229 ? 17.386  29.317  35.019  1.00 30.32  ? 258 TYR D CA  1 
ATOM   5228  C C   . TYR B 1 229 ? 16.722  28.207  34.204  1.00 31.04  ? 258 TYR D C   1 
ATOM   5229  O O   . TYR B 1 229 ? 17.143  27.959  33.078  1.00 27.35  ? 258 TYR D O   1 
ATOM   5230  C CB  . TYR B 1 229 ? 18.384  28.865  36.092  1.00 30.35  ? 258 TYR D CB  1 
ATOM   5231  C CG  . TYR B 1 229 ? 19.489  28.006  35.512  1.00 32.13  ? 258 TYR D CG  1 
ATOM   5232  C CD1 . TYR B 1 229 ? 19.200  26.709  35.118  1.00 38.31  ? 258 TYR D CD1 1 
ATOM   5233  C CD2 . TYR B 1 229 ? 20.799  28.445  35.373  1.00 38.87  ? 258 TYR D CD2 1 
ATOM   5234  C CE1 . TYR B 1 229 ? 20.159  25.886  34.559  1.00 38.46  ? 258 TYR D CE1 1 
ATOM   5235  C CE2 . TYR B 1 229 ? 21.781  27.607  34.845  1.00 42.46  ? 258 TYR D CE2 1 
ATOM   5236  C CZ  . TYR B 1 229 ? 21.454  26.334  34.416  1.00 38.41  ? 258 TYR D CZ  1 
ATOM   5237  O OH  . TYR B 1 229 ? 22.330  25.432  33.859  1.00 47.82  ? 258 TYR D OH  1 
ATOM   5238  N N   . LEU B 1 230 ? 15.670  27.577  34.752  1.00 27.72  ? 259 LEU D N   1 
ATOM   5239  C CA  . LEU B 1 230 ? 15.021  26.469  34.098  1.00 27.50  ? 259 LEU D CA  1 
ATOM   5240  C C   . LEU B 1 230 ? 14.226  26.957  32.891  1.00 27.54  ? 259 LEU D C   1 
ATOM   5241  O O   . LEU B 1 230 ? 14.057  26.232  31.920  1.00 26.58  ? 259 LEU D O   1 
ATOM   5242  C CB  . LEU B 1 230 ? 14.150  25.698  35.085  1.00 27.48  ? 259 LEU D CB  1 
ATOM   5243  C CG  . LEU B 1 230 ? 14.894  25.089  36.277  1.00 27.58  ? 259 LEU D CG  1 
ATOM   5244  C CD1 . LEU B 1 230 ? 13.963  24.435  37.303  1.00 30.80  ? 259 LEU D CD1 1 
ATOM   5245  C CD2 . LEU B 1 230 ? 15.958  24.062  35.830  1.00 28.87  ? 259 LEU D CD2 1 
ATOM   5246  N N   . THR B 1 231 ? 13.683  28.165  32.970  1.00 23.83  ? 260 THR D N   1 
ATOM   5247  C CA  . THR B 1 231 ? 12.960  28.733  31.858  1.00 25.30  ? 260 THR D CA  1 
ATOM   5248  C C   . THR B 1 231 ? 13.912  28.904  30.676  1.00 24.95  ? 260 THR D C   1 
ATOM   5249  O O   . THR B 1 231 ? 13.637  28.367  29.594  1.00 25.53  ? 260 THR D O   1 
ATOM   5250  C CB  . THR B 1 231 ? 12.260  30.023  32.272  1.00 25.85  ? 260 THR D CB  1 
ATOM   5251  O OG1 . THR B 1 231 ? 11.273  29.581  33.200  1.00 27.33  ? 260 THR D OG1 1 
ATOM   5252  C CG2 . THR B 1 231 ? 11.518  30.679  31.136  1.00 25.09  ? 260 THR D CG2 1 
ATOM   5253  N N   . ILE B 1 232 ? 15.051  29.542  30.896  1.00 25.85  ? 261 ILE D N   1 
ATOM   5254  C CA  . ILE B 1 232 ? 15.866  30.048  29.781  1.00 28.61  ? 261 ILE D CA  1 
ATOM   5255  C C   . ILE B 1 232 ? 16.761  28.983  29.126  1.00 29.16  ? 261 ILE D C   1 
ATOM   5256  O O   . ILE B 1 232 ? 17.184  29.169  27.980  1.00 30.01  ? 261 ILE D O   1 
ATOM   5257  C CB  . ILE B 1 232 ? 16.707  31.257  30.201  1.00 29.98  ? 261 ILE D CB  1 
ATOM   5258  C CG1 . ILE B 1 232 ? 17.808  30.873  31.220  1.00 31.89  ? 261 ILE D CG1 1 
ATOM   5259  C CG2 . ILE B 1 232 ? 15.796  32.384  30.697  1.00 33.63  ? 261 ILE D CG2 1 
ATOM   5260  C CD1 . ILE B 1 232 ? 18.748  32.008  31.578  1.00 35.92  ? 261 ILE D CD1 1 
ATOM   5261  N N   . HIS B 1 233 ? 17.156  27.946  29.867  1.00 26.82  ? 262 HIS D N   1 
ATOM   5262  C CA  . HIS B 1 233 ? 17.891  26.833  29.282  1.00 29.08  ? 262 HIS D CA  1 
ATOM   5263  C C   . HIS B 1 233 ? 16.985  25.751  28.676  1.00 24.06  ? 262 HIS D C   1 
ATOM   5264  O O   . HIS B 1 233 ? 17.506  24.763  28.145  1.00 25.52  ? 262 HIS D O   1 
ATOM   5265  C CB  . HIS B 1 233 ? 18.816  26.183  30.313  1.00 33.21  ? 262 HIS D CB  1 
ATOM   5266  C CG  . HIS B 1 233 ? 19.983  26.991  30.709  1.00 40.77  ? 262 HIS D CG  1 
ATOM   5267  N ND1 . HIS B 1 233 ? 19.860  27.996  31.647  1.00 41.97  ? 262 HIS D ND1 1 
ATOM   5268  C CD2 . HIS B 1 233 ? 21.265  26.954  30.340  1.00 43.23  ? 262 HIS D CD2 1 
ATOM   5269  C CE1 . HIS B 1 233 ? 21.046  28.562  31.813  1.00 47.54  ? 262 HIS D CE1 1 
ATOM   5270  N NE2 . HIS B 1 233 ? 21.911  27.940  31.040  1.00 43.87  ? 262 HIS D NE2 1 
ATOM   5271  N N   . SER B 1 234 ? 15.656  25.945  28.705  1.00 25.73  ? 263 SER D N   1 
ATOM   5272  C CA  . SER B 1 234 ? 14.666  24.939  28.323  1.00 26.37  ? 263 SER D CA  1 
ATOM   5273  C C   . SER B 1 234 ? 14.826  24.406  26.901  1.00 25.84  ? 263 SER D C   1 
ATOM   5274  O O   . SER B 1 234 ? 14.586  23.229  26.673  1.00 25.67  ? 263 SER D O   1 
ATOM   5275  C CB  . SER B 1 234 ? 13.299  25.456  28.484  1.00 27.13  ? 263 SER D CB  1 
ATOM   5276  O OG  . SER B 1 234 ? 13.099  26.558  27.621  1.00 25.48  ? 263 SER D OG  1 
ATOM   5277  N N   . ASP B 1 235 ? 15.183  25.268  25.931  1.00 29.15  ? 264 ASP D N   1 
ATOM   5278  C CA  . ASP B 1 235 ? 15.254  24.853  24.534  1.00 31.14  ? 264 ASP D CA  1 
ATOM   5279  C C   . ASP B 1 235 ? 16.178  25.806  23.793  1.00 29.17  ? 264 ASP D C   1 
ATOM   5280  O O   . ASP B 1 235 ? 16.207  26.989  24.097  1.00 28.25  ? 264 ASP D O   1 
ATOM   5281  C CB  . ASP B 1 235 ? 13.886  24.890  23.860  1.00 32.63  ? 264 ASP D CB  1 
ATOM   5282  C CG  . ASP B 1 235 ? 13.603  23.847  22.780  1.00 35.80  ? 264 ASP D CG  1 
ATOM   5283  O OD1 . ASP B 1 235 ? 13.996  22.664  22.967  1.00 34.96  ? 264 ASP D OD1 1 
ATOM   5284  O OD2 . ASP B 1 235 ? 12.893  24.190  21.812  1.00 36.63  ? 264 ASP D OD2 1 
ATOM   5285  N N   . HIS B 1 236 ? 16.842  25.295  22.773  1.00 25.79  ? 265 HIS D N   1 
ATOM   5286  C CA  . HIS B 1 236 ? 17.667  26.100  21.892  1.00 26.08  ? 265 HIS D CA  1 
ATOM   5287  C C   . HIS B 1 236 ? 17.757  25.470  20.483  1.00 26.65  ? 265 HIS D C   1 
ATOM   5288  O O   . HIS B 1 236 ? 18.839  25.059  20.059  1.00 29.93  ? 265 HIS D O   1 
ATOM   5289  C CB  . HIS B 1 236 ? 19.025  26.230  22.583  1.00 29.64  ? 265 HIS D CB  1 
ATOM   5290  C CG  . HIS B 1 236 ? 19.705  27.484  22.195  1.00 36.82  ? 265 HIS D CG  1 
ATOM   5291  N ND1 . HIS B 1 236 ? 20.471  27.595  21.059  1.00 43.49  ? 265 HIS D ND1 1 
ATOM   5292  C CD2 . HIS B 1 236 ? 19.635  28.706  22.728  1.00 37.49  ? 265 HIS D CD2 1 
ATOM   5293  C CE1 . HIS B 1 236 ? 20.901  28.848  20.948  1.00 39.12  ? 265 HIS D CE1 1 
ATOM   5294  N NE2 . HIS B 1 236 ? 20.402  29.538  21.947  1.00 41.15  ? 265 HIS D NE2 1 
ATOM   5295  N N   . GLU B 1 237 ? 16.629  25.392  19.766  1.00 30.00  ? 266 GLU D N   1 
ATOM   5296  C CA  . GLU B 1 237 ? 16.552  24.759  18.442  1.00 33.46  ? 266 GLU D CA  1 
ATOM   5297  C C   . GLU B 1 237 ? 16.789  23.244  18.546  1.00 29.23  ? 266 GLU D C   1 
ATOM   5298  O O   . GLU B 1 237 ? 16.912  22.682  19.636  1.00 28.16  ? 266 GLU D O   1 
ATOM   5299  C CB  . GLU B 1 237 ? 17.534  25.331  17.405  1.00 33.20  ? 266 GLU D CB  1 
ATOM   5300  C CG  . GLU B 1 237 ? 17.357  26.813  17.103  1.00 41.66  ? 266 GLU D CG  1 
ATOM   5301  C CD  . GLU B 1 237 ? 17.952  27.284  15.769  1.00 42.90  ? 266 GLU D CD  1 
ATOM   5302  O OE1 . GLU B 1 237 ? 19.095  26.908  15.435  1.00 42.92  ? 266 GLU D OE1 1 
ATOM   5303  O OE2 . GLU B 1 237 ? 17.243  28.028  15.043  1.00 43.63  ? 266 GLU D OE2 1 
ATOM   5304  N N   . GLY B 1 238 ? 16.841  22.555  17.399  1.00 29.07  ? 267 GLY D N   1 
ATOM   5305  C CA  . GLY B 1 238 ? 16.858  21.103  17.414  1.00 27.53  ? 267 GLY D CA  1 
ATOM   5306  C C   . GLY B 1 238 ? 18.234  20.599  17.052  1.00 30.08  ? 267 GLY D C   1 
ATOM   5307  O O   . GLY B 1 238 ? 18.488  19.397  17.120  1.00 33.34  ? 267 GLY D O   1 
ATOM   5308  N N   . GLY B 1 239 ? 19.091  21.532  16.639  1.00 31.41  ? 268 GLY D N   1 
ATOM   5309  C CA  . GLY B 1 239 ? 20.397  21.181  16.113  1.00 29.89  ? 268 GLY D CA  1 
ATOM   5310  C C   . GLY B 1 239 ? 21.409  20.870  17.209  1.00 28.29  ? 268 GLY D C   1 
ATOM   5311  O O   . GLY B 1 239 ? 22.416  20.226  16.948  1.00 29.25  ? 268 GLY D O   1 
ATOM   5312  N N   . ASN B 1 240 ? 21.181  21.378  18.423  1.00 27.23  ? 269 ASN D N   1 
ATOM   5313  C CA  . ASN B 1 240 ? 22.160  21.218  19.490  1.00 28.11  ? 269 ASN D CA  1 
ATOM   5314  C C   . ASN B 1 240 ? 22.155  19.737  19.887  1.00 26.71  ? 269 ASN D C   1 
ATOM   5315  O O   . ASN B 1 240 ? 21.179  19.046  19.646  1.00 31.93  ? 269 ASN D O   1 
ATOM   5316  C CB  . ASN B 1 240 ? 21.861  22.179  20.649  1.00 24.89  ? 269 ASN D CB  1 
ATOM   5317  C CG  . ASN B 1 240 ? 20.583  21.817  21.380  1.00 30.05  ? 269 ASN D CG  1 
ATOM   5318  O OD1 . ASN B 1 240 ? 20.519  20.843  22.137  1.00 25.57  ? 269 ASN D OD1 1 
ATOM   5319  N ND2 . ASN B 1 240 ? 19.546  22.623  21.219  1.00 35.79  ? 269 ASN D ND2 1 
ATOM   5320  N N   . VAL B 1 241 ? 23.200  19.243  20.542  1.00 26.58  ? 270 VAL D N   1 
ATOM   5321  C CA  . VAL B 1 241 ? 23.406  17.801  20.605  1.00 28.49  ? 270 VAL D CA  1 
ATOM   5322  C C   . VAL B 1 241 ? 22.349  17.143  21.479  1.00 25.23  ? 270 VAL D C   1 
ATOM   5323  O O   . VAL B 1 241 ? 21.884  16.062  21.178  1.00 24.06  ? 270 VAL D O   1 
ATOM   5324  C CB  . VAL B 1 241 ? 24.822  17.441  21.073  1.00 32.99  ? 270 VAL D CB  1 
ATOM   5325  C CG1 . VAL B 1 241 ? 24.994  15.943  21.318  1.00 33.81  ? 270 VAL D CG1 1 
ATOM   5326  C CG2 . VAL B 1 241 ? 25.835  17.870  20.015  1.00 40.14  ? 270 VAL D CG2 1 
ATOM   5327  N N   . SER B 1 242 ? 21.901  17.826  22.523  1.00 24.48  ? 271 SER D N   1 
ATOM   5328  C CA  . SER B 1 242 ? 20.961  17.178  23.417  1.00 28.33  ? 271 SER D CA  1 
ATOM   5329  C C   . SER B 1 242 ? 19.577  17.130  22.772  1.00 26.01  ? 271 SER D C   1 
ATOM   5330  O O   . SER B 1 242 ? 18.923  16.095  22.785  1.00 29.21  ? 271 SER D O   1 
ATOM   5331  C CB  . SER B 1 242 ? 20.999  17.781  24.789  1.00 28.12  ? 271 SER D CB  1 
ATOM   5332  O OG  . SER B 1 242 ? 20.356  19.035  24.824  1.00 30.21  ? 271 SER D OG  1 
ATOM   5333  N N   . ALA B 1 243 ? 19.176  18.197  22.084  1.00 25.63  ? 272 ALA D N   1 
ATOM   5334  C CA  . ALA B 1 243 ? 17.911  18.196  21.385  1.00 25.76  ? 272 ALA D CA  1 
ATOM   5335  C C   . ALA B 1 243 ? 17.982  17.206  20.229  1.00 22.47  ? 272 ALA D C   1 
ATOM   5336  O O   . ALA B 1 243 ? 17.042  16.473  19.990  1.00 20.32  ? 272 ALA D O   1 
ATOM   5337  C CB  . ALA B 1 243 ? 17.523  19.580  20.911  1.00 24.80  ? 272 ALA D CB  1 
ATOM   5338  N N   . HIS B 1 244 ? 19.080  17.222  19.477  1.00 23.17  ? 273 HIS D N   1 
ATOM   5339  C CA  . HIS B 1 244 ? 19.126  16.383  18.302  1.00 24.17  ? 273 HIS D CA  1 
ATOM   5340  C C   . HIS B 1 244 ? 19.103  14.911  18.753  1.00 23.27  ? 273 HIS D C   1 
ATOM   5341  O O   . HIS B 1 244 ? 18.488  14.047  18.122  1.00 24.80  ? 273 HIS D O   1 
ATOM   5342  C CB  . HIS B 1 244 ? 20.304  16.781  17.411  1.00 22.85  ? 273 HIS D CB  1 
ATOM   5343  C CG  . HIS B 1 244 ? 20.375  15.977  16.157  1.00 24.76  ? 273 HIS D CG  1 
ATOM   5344  N ND1 . HIS B 1 244 ? 21.509  15.894  15.380  1.00 25.16  ? 273 HIS D ND1 1 
ATOM   5345  C CD2 . HIS B 1 244 ? 19.457  15.220  15.538  1.00 26.20  ? 273 HIS D CD2 1 
ATOM   5346  C CE1 . HIS B 1 244 ? 21.279  15.111  14.351  1.00 24.23  ? 273 HIS D CE1 1 
ATOM   5347  N NE2 . HIS B 1 244 ? 20.051  14.674  14.418  1.00 24.48  ? 273 HIS D NE2 1 
ATOM   5348  N N   . THR B 1 245 ? 19.777  14.619  19.848  1.00 21.08  ? 274 THR D N   1 
ATOM   5349  C CA  . THR B 1 245 ? 19.848  13.236  20.297  1.00 24.74  ? 274 THR D CA  1 
ATOM   5350  C C   . THR B 1 245 ? 18.448  12.743  20.706  1.00 24.09  ? 274 THR D C   1 
ATOM   5351  O O   . THR B 1 245 ? 18.111  11.619  20.400  1.00 20.55  ? 274 THR D O   1 
ATOM   5352  C CB  . THR B 1 245 ? 20.862  13.119  21.443  1.00 22.77  ? 274 THR D CB  1 
ATOM   5353  O OG1 . THR B 1 245 ? 22.146  13.424  20.906  1.00 24.40  ? 274 THR D OG1 1 
ATOM   5354  C CG2 . THR B 1 245 ? 20.927  11.725  22.027  1.00 23.18  ? 274 THR D CG2 1 
ATOM   5355  N N   . SER B 1 246 ? 17.672  13.546  21.457  1.00 19.85  ? 275 SER D N   1 
ATOM   5356  C CA  . SER B 1 246 ? 16.326  13.182  21.852  1.00 22.86  ? 275 SER D CA  1 
ATOM   5357  C C   . SER B 1 246 ? 15.443  12.944  20.638  1.00 20.17  ? 275 SER D C   1 
ATOM   5358  O O   . SER B 1 246 ? 14.547  12.117  20.671  1.00 23.13  ? 275 SER D O   1 
ATOM   5359  C CB  . SER B 1 246 ? 15.679  14.217  22.733  1.00 21.68  ? 275 SER D CB  1 
ATOM   5360  O OG  . SER B 1 246 ? 15.513  15.415  22.001  1.00 27.38  ? 275 SER D OG  1 
ATOM   5361  N N   . HIS B 1 247 ? 15.629  13.758  19.592  1.00 21.05  ? 276 HIS D N   1 
ATOM   5362  C CA  . HIS B 1 247 ? 14.840  13.658  18.384  1.00 23.19  ? 276 HIS D CA  1 
ATOM   5363  C C   . HIS B 1 247 ? 15.199  12.390  17.616  1.00 23.52  ? 276 HIS D C   1 
ATOM   5364  O O   . HIS B 1 247 ? 14.329  11.777  17.001  1.00 25.02  ? 276 HIS D O   1 
ATOM   5365  C CB  . HIS B 1 247 ? 15.149  14.888  17.514  1.00 28.18  ? 276 HIS D CB  1 
ATOM   5366  C CG  . HIS B 1 247 ? 14.280  15.096  16.360  1.00 33.01  ? 276 HIS D CG  1 
ATOM   5367  N ND1 . HIS B 1 247 ? 14.726  14.874  15.067  1.00 37.23  ? 276 HIS D ND1 1 
ATOM   5368  C CD2 . HIS B 1 247 ? 13.020  15.569  16.280  1.00 34.29  ? 276 HIS D CD2 1 
ATOM   5369  C CE1 . HIS B 1 247 ? 13.742  15.184  14.239  1.00 31.92  ? 276 HIS D CE1 1 
ATOM   5370  N NE2 . HIS B 1 247 ? 12.695  15.606  14.953  1.00 38.78  ? 276 HIS D NE2 1 
ATOM   5371  N N   . LEU B 1 248 ? 16.496  12.067  17.581  1.00 22.72  ? 277 LEU D N   1 
ATOM   5372  C CA  . LEU B 1 248 ? 16.965  10.901  16.836  1.00 22.95  ? 277 LEU D CA  1 
ATOM   5373  C C   . LEU B 1 248 ? 16.502  9.609   17.521  1.00 22.04  ? 277 LEU D C   1 
ATOM   5374  O O   . LEU B 1 248 ? 15.819  8.784   16.933  1.00 20.55  ? 277 LEU D O   1 
ATOM   5375  C CB  . LEU B 1 248 ? 18.481  10.998  16.771  1.00 22.77  ? 277 LEU D CB  1 
ATOM   5376  C CG  . LEU B 1 248 ? 19.218  9.784   16.204  1.00 27.70  ? 277 LEU D CG  1 
ATOM   5377  C CD1 . LEU B 1 248 ? 18.627  9.426   14.840  1.00 28.39  ? 277 LEU D CD1 1 
ATOM   5378  C CD2 . LEU B 1 248 ? 20.700  10.106  16.078  1.00 28.72  ? 277 LEU D CD2 1 
ATOM   5379  N N   . VAL B 1 249 ? 16.796  9.491   18.810  1.00 22.30  ? 278 VAL D N   1 
ATOM   5380  C CA  . VAL B 1 249 ? 16.357  8.334   19.581  1.00 20.98  ? 278 VAL D CA  1 
ATOM   5381  C C   . VAL B 1 249 ? 14.841  8.263   19.589  1.00 23.87  ? 278 VAL D C   1 
ATOM   5382  O O   . VAL B 1 249 ? 14.293  7.195   19.394  1.00 24.43  ? 278 VAL D O   1 
ATOM   5383  C CB  . VAL B 1 249 ? 16.997  8.383   20.982  1.00 21.48  ? 278 VAL D CB  1 
ATOM   5384  C CG1 . VAL B 1 249 ? 16.420  7.369   21.969  1.00 20.69  ? 278 VAL D CG1 1 
ATOM   5385  C CG2 . VAL B 1 249 ? 18.499  8.197   20.888  1.00 23.64  ? 278 VAL D CG2 1 
ATOM   5386  N N   . GLY B 1 250 ? 14.152  9.402   19.780  1.00 25.00  ? 279 GLY D N   1 
ATOM   5387  C CA  . GLY B 1 250 ? 12.690  9.454   19.717  1.00 25.29  ? 279 GLY D CA  1 
ATOM   5388  C C   . GLY B 1 250 ? 12.079  8.970   18.395  1.00 24.80  ? 279 GLY D C   1 
ATOM   5389  O O   . GLY B 1 250 ? 10.996  8.379   18.404  1.00 25.85  ? 279 GLY D O   1 
ATOM   5390  N N   . SER B 1 251 ? 12.720  9.270   17.252  1.00 22.43  ? 280 SER D N   1 
ATOM   5391  C CA  . SER B 1 251 ? 12.216  8.875   15.935  1.00 22.35  ? 280 SER D CA  1 
ATOM   5392  C C   . SER B 1 251 ? 12.206  7.365   15.724  1.00 23.50  ? 280 SER D C   1 
ATOM   5393  O O   . SER B 1 251 ? 11.526  6.866   14.822  1.00 29.15  ? 280 SER D O   1 
ATOM   5394  C CB  . SER B 1 251 ? 13.014  9.482   14.812  1.00 22.53  ? 280 SER D CB  1 
ATOM   5395  O OG  . SER B 1 251 ? 14.259  8.803   14.628  1.00 20.19  ? 280 SER D OG  1 
ATOM   5396  N N   . ALA B 1 252 ? 12.888  6.628   16.604  1.00 27.01  ? 281 ALA D N   1 
ATOM   5397  C CA  . ALA B 1 252 ? 12.878  5.145   16.563  1.00 24.51  ? 281 ALA D CA  1 
ATOM   5398  C C   . ALA B 1 252 ? 11.720  4.637   17.415  1.00 24.17  ? 281 ALA D C   1 
ATOM   5399  O O   . ALA B 1 252 ? 11.599  3.418   17.558  1.00 23.21  ? 281 ALA D O   1 
ATOM   5400  C CB  . ALA B 1 252 ? 14.186  4.610   17.064  1.00 25.55  ? 281 ALA D CB  1 
ATOM   5401  N N   . LEU B 1 253 ? 10.944  5.555   17.985  1.00 24.43  ? 282 LEU D N   1 
ATOM   5402  C CA  . LEU B 1 253 ? 9.776   5.227   18.852  1.00 23.74  ? 282 LEU D CA  1 
ATOM   5403  C C   . LEU B 1 253 ? 10.264  4.782   20.239  1.00 26.93  ? 282 LEU D C   1 
ATOM   5404  O O   . LEU B 1 253 ? 9.507   4.121   20.951  1.00 25.93  ? 282 LEU D O   1 
ATOM   5405  C CB  . LEU B 1 253 ? 8.756   4.281   18.223  1.00 24.70  ? 282 LEU D CB  1 
ATOM   5406  C CG  . LEU B 1 253 ? 8.006   4.845   17.015  1.00 29.75  ? 282 LEU D CG  1 
ATOM   5407  C CD1 . LEU B 1 253 ? 6.875   3.934   16.614  1.00 30.75  ? 282 LEU D CD1 1 
ATOM   5408  C CD2 . LEU B 1 253 ? 7.492   6.242   17.288  1.00 32.10  ? 282 LEU D CD2 1 
ATOM   5409  N N   . SER B 1 254 ? 11.498  5.128   20.589  1.00 28.57  ? 283 SER D N   1 
ATOM   5410  C CA  . SER B 1 254 ? 11.958  4.903   21.976  1.00 29.64  ? 283 SER D CA  1 
ATOM   5411  C C   . SER B 1 254 ? 11.178  5.922   22.819  1.00 29.23  ? 283 SER D C   1 
ATOM   5412  O O   . SER B 1 254 ? 10.934  7.023   22.317  1.00 30.65  ? 283 SER D O   1 
ATOM   5413  C CB  . SER B 1 254 ? 13.460  4.987   22.130  1.00 25.59  ? 283 SER D CB  1 
ATOM   5414  O OG  . SER B 1 254 ? 14.162  4.264   21.138  1.00 33.42  ? 283 SER D OG  1 
ATOM   5415  N N   . ASP B 1 255 ? 10.781  5.571   24.031  1.00 28.23  ? 284 ASP D N   1 
ATOM   5416  C CA  . ASP B 1 255 ? 9.921   6.375   24.873  1.00 29.29  ? 284 ASP D CA  1 
ATOM   5417  C C   . ASP B 1 255 ? 10.655  7.606   25.421  1.00 27.96  ? 284 ASP D C   1 
ATOM   5418  O O   . ASP B 1 255 ? 11.867  7.723   25.344  1.00 25.11  ? 284 ASP D O   1 
ATOM   5419  C CB  . ASP B 1 255 ? 9.310   5.470   25.924  1.00 35.12  ? 284 ASP D CB  1 
ATOM   5420  C CG  . ASP B 1 255 ? 10.303  4.923   26.931  1.00 37.92  ? 284 ASP D CG  1 
ATOM   5421  O OD1 . ASP B 1 255 ? 11.049  5.753   27.471  1.00 41.15  ? 284 ASP D OD1 1 
ATOM   5422  O OD2 . ASP B 1 255 ? 10.283  3.674   27.191  1.00 41.10  ? 284 ASP D OD2 1 
ATOM   5423  N N   . PRO B 1 256 ? 9.948   8.579   26.038  1.00 25.08  ? 285 PRO D N   1 
ATOM   5424  C CA  . PRO B 1 256 ? 10.584  9.787   26.530  1.00 24.83  ? 285 PRO D CA  1 
ATOM   5425  C C   . PRO B 1 256 ? 11.733  9.552   27.500  1.00 24.88  ? 285 PRO D C   1 
ATOM   5426  O O   . PRO B 1 256 ? 12.699  10.322  27.502  1.00 23.35  ? 285 PRO D O   1 
ATOM   5427  C CB  . PRO B 1 256 ? 9.354   10.534  27.161  1.00 24.24  ? 285 PRO D CB  1 
ATOM   5428  C CG  . PRO B 1 256 ? 8.198   10.033  26.344  1.00 23.77  ? 285 PRO D CG  1 
ATOM   5429  C CD  . PRO B 1 256 ? 8.500   8.563   26.278  1.00 25.65  ? 285 PRO D CD  1 
ATOM   5430  N N   . TYR B 1 257 ? 11.631  8.486   28.305  1.00 22.06  ? 286 TYR D N   1 
ATOM   5431  C CA  . TYR B 1 257 ? 12.680  8.134   29.247  1.00 23.29  ? 286 TYR D CA  1 
ATOM   5432  C C   . TYR B 1 257 ? 13.961  7.795   28.491  1.00 23.23  ? 286 TYR D C   1 
ATOM   5433  O O   . TYR B 1 257 ? 15.013  8.333   28.789  1.00 24.69  ? 286 TYR D O   1 
ATOM   5434  C CB  . TYR B 1 257 ? 12.283  7.007   30.210  1.00 23.49  ? 286 TYR D CB  1 
ATOM   5435  C CG  . TYR B 1 257 ? 11.097  7.391   31.094  1.00 24.50  ? 286 TYR D CG  1 
ATOM   5436  C CD1 . TYR B 1 257 ? 11.265  8.131   32.252  1.00 23.23  ? 286 TYR D CD1 1 
ATOM   5437  C CD2 . TYR B 1 257 ? 9.819   6.973   30.775  1.00 26.40  ? 286 TYR D CD2 1 
ATOM   5438  C CE1 . TYR B 1 257 ? 10.184  8.481   33.047  1.00 23.48  ? 286 TYR D CE1 1 
ATOM   5439  C CE2 . TYR B 1 257 ? 8.737   7.274   31.579  1.00 25.97  ? 286 TYR D CE2 1 
ATOM   5440  C CZ  . TYR B 1 257 ? 8.913   8.045   32.704  1.00 25.41  ? 286 TYR D CZ  1 
ATOM   5441  O OH  . TYR B 1 257 ? 7.800   8.315   33.470  1.00 30.10  ? 286 TYR D OH  1 
ATOM   5442  N N   . LEU B 1 258 ? 13.887  6.925   27.496  1.00 23.45  ? 287 LEU D N   1 
ATOM   5443  C CA  . LEU B 1 258 ? 15.124  6.550   26.840  1.00 21.53  ? 287 LEU D CA  1 
ATOM   5444  C C   . LEU B 1 258 ? 15.646  7.724   26.014  1.00 22.41  ? 287 LEU D C   1 
ATOM   5445  O O   . LEU B 1 258 ? 16.841  7.918   25.932  1.00 24.80  ? 287 LEU D O   1 
ATOM   5446  C CB  . LEU B 1 258 ? 14.866  5.307   25.994  1.00 21.74  ? 287 LEU D CB  1 
ATOM   5447  C CG  . LEU B 1 258 ? 14.307  4.090   26.743  1.00 22.87  ? 287 LEU D CG  1 
ATOM   5448  C CD1 . LEU B 1 258 ? 14.005  2.989   25.752  1.00 26.41  ? 287 LEU D CD1 1 
ATOM   5449  C CD2 . LEU B 1 258 ? 15.276  3.625   27.820  1.00 24.28  ? 287 LEU D CD2 1 
ATOM   5450  N N   . SER B 1 259 ? 14.746  8.516   25.420  1.00 24.42  ? 288 SER D N   1 
ATOM   5451  C CA  . SER B 1 259 ? 15.151  9.635   24.583  1.00 26.68  ? 288 SER D CA  1 
ATOM   5452  C C   . SER B 1 259 ? 15.947  10.635  25.397  1.00 28.23  ? 288 SER D C   1 
ATOM   5453  O O   . SER B 1 259 ? 16.969  11.134  24.943  1.00 27.69  ? 288 SER D O   1 
ATOM   5454  C CB  . SER B 1 259 ? 13.956  10.320  23.936  1.00 26.73  ? 288 SER D CB  1 
ATOM   5455  O OG  . SER B 1 259 ? 13.202  9.321   23.277  1.00 27.05  ? 288 SER D OG  1 
ATOM   5456  N N   . PHE B 1 260 ? 15.387  10.997  26.553  1.00 26.00  ? 289 PHE D N   1 
ATOM   5457  C CA  . PHE B 1 260 ? 15.982  12.017  27.382  1.00 27.63  ? 289 PHE D CA  1 
ATOM   5458  C C   . PHE B 1 260 ? 17.302  11.483  27.927  1.00 27.07  ? 289 PHE D C   1 
ATOM   5459  O O   . PHE B 1 260 ? 18.294  12.184  27.922  1.00 28.14  ? 289 PHE D O   1 
ATOM   5460  C CB  . PHE B 1 260 ? 14.948  12.447  28.427  1.00 26.56  ? 289 PHE D CB  1 
ATOM   5461  C CG  . PHE B 1 260 ? 15.453  13.531  29.346  1.00 28.59  ? 289 PHE D CG  1 
ATOM   5462  C CD1 . PHE B 1 260 ? 15.592  14.827  28.894  1.00 33.93  ? 289 PHE D CD1 1 
ATOM   5463  C CD2 . PHE B 1 260 ? 15.865  13.241  30.625  1.00 29.56  ? 289 PHE D CD2 1 
ATOM   5464  C CE1 . PHE B 1 260 ? 16.121  15.809  29.708  1.00 30.24  ? 289 PHE D CE1 1 
ATOM   5465  C CE2 . PHE B 1 260 ? 16.383  14.229  31.431  1.00 29.70  ? 289 PHE D CE2 1 
ATOM   5466  C CZ  . PHE B 1 260 ? 16.482  15.516  30.970  1.00 28.75  ? 289 PHE D CZ  1 
ATOM   5467  N N   . ALA B 1 261 ? 17.321  10.235  28.381  1.00 30.23  ? 290 ALA D N   1 
ATOM   5468  C CA  . ALA B 1 261 ? 18.532  9.670   28.946  1.00 29.70  ? 290 ALA D CA  1 
ATOM   5469  C C   . ALA B 1 261 ? 19.649  9.735   27.919  1.00 25.35  ? 290 ALA D C   1 
ATOM   5470  O O   . ALA B 1 261 ? 20.767  10.048  28.272  1.00 24.01  ? 290 ALA D O   1 
ATOM   5471  C CB  . ALA B 1 261 ? 18.307  8.239   29.387  1.00 28.18  ? 290 ALA D CB  1 
ATOM   5472  N N   . ALA B 1 262 ? 19.345  9.405   26.663  1.00 26.67  ? 291 ALA D N   1 
ATOM   5473  C CA  . ALA B 1 262 ? 20.322  9.557   25.581  1.00 27.44  ? 291 ALA D CA  1 
ATOM   5474  C C   . ALA B 1 262 ? 20.759  11.020  25.451  1.00 25.89  ? 291 ALA D C   1 
ATOM   5475  O O   . ALA B 1 262 ? 21.937  11.342  25.252  1.00 25.70  ? 291 ALA D O   1 
ATOM   5476  C CB  . ALA B 1 262 ? 19.750  9.047   24.275  1.00 25.64  ? 291 ALA D CB  1 
ATOM   5477  N N   . ALA B 1 263 ? 19.800  11.926  25.599  1.00 26.62  ? 292 ALA D N   1 
ATOM   5478  C CA  . ALA B 1 263 ? 20.069  13.335  25.372  1.00 25.98  ? 292 ALA D CA  1 
ATOM   5479  C C   . ALA B 1 263 ? 21.013  13.864  26.445  1.00 27.35  ? 292 ALA D C   1 
ATOM   5480  O O   . ALA B 1 263 ? 21.843  14.720  26.169  1.00 24.54  ? 292 ALA D O   1 
ATOM   5481  C CB  . ALA B 1 263 ? 18.783  14.137  25.316  1.00 23.61  ? 292 ALA D CB  1 
ATOM   5482  N N   . MET B 1 264 ? 20.853  13.365  27.672  1.00 26.28  ? 293 MET D N   1 
ATOM   5483  C CA  . MET B 1 264 ? 21.725  13.702  28.777  1.00 24.58  ? 293 MET D CA  1 
ATOM   5484  C C   . MET B 1 264 ? 23.134  13.134  28.539  1.00 23.54  ? 293 MET D C   1 
ATOM   5485  O O   . MET B 1 264 ? 24.108  13.734  28.931  1.00 25.15  ? 293 MET D O   1 
ATOM   5486  C CB  . MET B 1 264 ? 21.182  13.127  30.102  1.00 24.38  ? 293 MET D CB  1 
ATOM   5487  C CG  . MET B 1 264 ? 19.932  13.832  30.672  1.00 27.28  ? 293 MET D CG  1 
ATOM   5488  S SD  . MET B 1 264 ? 19.987  15.634  30.677  1.00 33.69  ? 293 MET D SD  1 
ATOM   5489  C CE  . MET B 1 264 ? 19.401  16.180  29.070  1.00 30.10  ? 293 MET D CE  1 
ATOM   5490  N N   . ASN B 1 265 ? 23.260  11.933  27.970  1.00 22.23  ? 294 ASN D N   1 
ATOM   5491  C CA  . ASN B 1 265 ? 24.571  11.437  27.606  1.00 20.79  ? 294 ASN D CA  1 
ATOM   5492  C C   . ASN B 1 265 ? 25.226  12.472  26.691  1.00 21.84  ? 294 ASN D C   1 
ATOM   5493  O O   . ASN B 1 265 ? 26.412  12.803  26.825  1.00 30.34  ? 294 ASN D O   1 
ATOM   5494  C CB  . ASN B 1 265 ? 24.475  9.998   27.116  1.00 24.38  ? 294 ASN D CB  1 
ATOM   5495  C CG  . ASN B 1 265 ? 24.292  9.010   28.247  1.00 29.33  ? 294 ASN D CG  1 
ATOM   5496  O OD1 . ASN B 1 265 ? 24.126  9.383   29.413  1.00 25.99  ? 294 ASN D OD1 1 
ATOM   5497  N ND2 . ASN B 1 265 ? 24.284  7.735   27.925  1.00 35.26  ? 294 ASN D ND2 1 
ATOM   5498  N N   . GLY B 1 266 ? 24.446  13.042  25.785  1.00 21.93  ? 295 GLY D N   1 
ATOM   5499  C CA  . GLY B 1 266 ? 24.974  14.020  24.852  1.00 27.13  ? 295 GLY D CA  1 
ATOM   5500  C C   . GLY B 1 266 ? 25.304  15.345  25.548  1.00 30.65  ? 295 GLY D C   1 
ATOM   5501  O O   . GLY B 1 266 ? 26.306  15.993  25.255  1.00 25.26  ? 295 GLY D O   1 
ATOM   5502  N N   . LEU B 1 267 ? 24.431  15.767  26.462  1.00 28.70  ? 296 LEU D N   1 
ATOM   5503  C CA  . LEU B 1 267 ? 24.662  16.977  27.216  1.00 30.92  ? 296 LEU D CA  1 
ATOM   5504  C C   . LEU B 1 267 ? 25.894  16.813  28.086  1.00 30.84  ? 296 LEU D C   1 
ATOM   5505  O O   . LEU B 1 267 ? 26.462  17.792  28.490  1.00 31.66  ? 296 LEU D O   1 
ATOM   5506  C CB  . LEU B 1 267 ? 23.428  17.276  28.060  1.00 34.95  ? 296 LEU D CB  1 
ATOM   5507  C CG  . LEU B 1 267 ? 23.356  18.645  28.751  1.00 31.96  ? 296 LEU D CG  1 
ATOM   5508  C CD1 . LEU B 1 267 ? 23.251  19.745  27.724  1.00 32.25  ? 296 LEU D CD1 1 
ATOM   5509  C CD2 . LEU B 1 267 ? 22.149  18.659  29.587  1.00 30.65  ? 296 LEU D CD2 1 
ATOM   5510  N N   . ALA B 1 268 ? 26.235  15.589  28.490  1.00 28.38  ? 297 ALA D N   1 
ATOM   5511  C CA  . ALA B 1 268 ? 27.356  15.404  29.386  1.00 28.29  ? 297 ALA D CA  1 
ATOM   5512  C C   . ALA B 1 268 ? 28.651  15.619  28.600  1.00 27.69  ? 297 ALA D C   1 
ATOM   5513  O O   . ALA B 1 268 ? 29.678  15.804  29.190  1.00 30.97  ? 297 ALA D O   1 
ATOM   5514  C CB  . ALA B 1 268 ? 27.325  14.029  30.058  1.00 28.96  ? 297 ALA D CB  1 
ATOM   5515  N N   . GLY B 1 269 ? 28.596  15.618  27.273  1.00 29.61  ? 298 GLY D N   1 
ATOM   5516  C CA  . GLY B 1 269 ? 29.767  15.909  26.455  1.00 31.60  ? 298 GLY D CA  1 
ATOM   5517  C C   . GLY B 1 269 ? 30.406  17.237  26.870  1.00 28.74  ? 298 GLY D C   1 
ATOM   5518  O O   . GLY B 1 269 ? 29.713  18.242  27.011  1.00 28.22  ? 298 GLY D O   1 
ATOM   5519  N N   . PRO B 1 270 ? 31.734  17.291  27.072  1.00 28.09  ? 299 PRO D N   1 
ATOM   5520  C CA  . PRO B 1 270 ? 32.385  18.544  27.447  1.00 35.94  ? 299 PRO D CA  1 
ATOM   5521  C C   . PRO B 1 270 ? 32.420  19.646  26.375  1.00 38.32  ? 299 PRO D C   1 
ATOM   5522  O O   . PRO B 1 270 ? 32.814  20.762  26.662  1.00 45.23  ? 299 PRO D O   1 
ATOM   5523  C CB  . PRO B 1 270 ? 33.783  18.095  27.885  1.00 34.15  ? 299 PRO D CB  1 
ATOM   5524  C CG  . PRO B 1 270 ? 34.011  16.745  27.264  1.00 30.61  ? 299 PRO D CG  1 
ATOM   5525  C CD  . PRO B 1 270 ? 32.646  16.149  27.023  1.00 28.91  ? 299 PRO D CD  1 
ATOM   5526  N N   . LEU B 1 271 ? 31.954  19.363  25.160  1.00 36.67  ? 300 LEU D N   1 
ATOM   5527  C CA  . LEU B 1 271 ? 31.744  20.378  24.132  1.00 38.04  ? 300 LEU D CA  1 
ATOM   5528  C C   . LEU B 1 271 ? 30.292  20.891  24.141  1.00 41.79  ? 300 LEU D C   1 
ATOM   5529  O O   . LEU B 1 271 ? 29.979  21.855  23.447  1.00 44.46  ? 300 LEU D O   1 
ATOM   5530  C CB  . LEU B 1 271 ? 32.097  19.744  22.779  1.00 37.81  ? 300 LEU D CB  1 
ATOM   5531  C CG  . LEU B 1 271 ? 33.355  20.224  22.056  1.00 42.36  ? 300 LEU D CG  1 
ATOM   5532  C CD1 . LEU B 1 271 ? 34.542  20.215  22.989  1.00 50.14  ? 300 LEU D CD1 1 
ATOM   5533  C CD2 . LEU B 1 271 ? 33.664  19.418  20.775  1.00 39.35  ? 300 LEU D CD2 1 
ATOM   5534  N N   . HIS B 1 272 ? 29.379  20.229  24.872  1.00 44.33  ? 301 HIS D N   1 
ATOM   5535  C CA  . HIS B 1 272 ? 28.009  20.713  25.034  1.00 46.00  ? 301 HIS D CA  1 
ATOM   5536  C C   . HIS B 1 272 ? 27.696  21.216  26.446  1.00 44.11  ? 301 HIS D C   1 
ATOM   5537  O O   . HIS B 1 272 ? 26.983  22.205  26.611  1.00 39.45  ? 301 HIS D O   1 
ATOM   5538  C CB  . HIS B 1 272 ? 26.973  19.616  24.760  1.00 44.39  ? 301 HIS D CB  1 
ATOM   5539  C CG  . HIS B 1 272 ? 25.603  20.178  24.551  1.00 49.23  ? 301 HIS D CG  1 
ATOM   5540  N ND1 . HIS B 1 272 ? 24.450  19.417  24.482  1.00 53.04  ? 301 HIS D ND1 1 
ATOM   5541  C CD2 . HIS B 1 272 ? 25.221  21.436  24.284  1.00 47.81  ? 301 HIS D CD2 1 
ATOM   5542  C CE1 . HIS B 1 272 ? 23.405  20.213  24.231  1.00 44.49  ? 301 HIS D CE1 1 
ATOM   5543  N NE2 . HIS B 1 272 ? 23.855  21.435  24.116  1.00 53.34  ? 301 HIS D NE2 1 
ATOM   5544  N N   . GLY B 1 273 ? 28.207  20.520  27.471  1.00 49.04  ? 302 GLY D N   1 
ATOM   5545  C CA  . GLY B 1 273 ? 27.620  20.601  28.795  1.00 52.51  ? 302 GLY D CA  1 
ATOM   5546  C C   . GLY B 1 273 ? 28.516  21.217  29.862  1.00 48.19  ? 302 GLY D C   1 
ATOM   5547  O O   . GLY B 1 273 ? 28.010  21.462  30.951  1.00 53.21  ? 302 GLY D O   1 
ATOM   5548  N N   . LEU B 1 274 ? 29.802  21.472  29.568  1.00 53.09  ? 303 LEU D N   1 
ATOM   5549  C CA  . LEU B 1 274 ? 30.775  21.797  30.605  1.00 54.47  ? 303 LEU D CA  1 
ATOM   5550  C C   . LEU B 1 274 ? 31.181  23.278  30.632  1.00 53.54  ? 303 LEU D C   1 
ATOM   5551  O O   . LEU B 1 274 ? 32.113  23.645  31.356  1.00 49.40  ? 303 LEU D O   1 
ATOM   5552  C CB  . LEU B 1 274 ? 32.011  20.924  30.385  1.00 67.31  ? 303 LEU D CB  1 
ATOM   5553  C CG  . LEU B 1 274 ? 32.759  20.494  31.656  1.00 77.09  ? 303 LEU D CG  1 
ATOM   5554  C CD1 . LEU B 1 274 ? 31.896  19.506  32.440  1.00 75.89  ? 303 LEU D CD1 1 
ATOM   5555  C CD2 . LEU B 1 274 ? 34.141  19.905  31.378  1.00 76.39  ? 303 LEU D CD2 1 
ATOM   5556  N N   . ALA B 1 275 ? 30.524  24.146  29.854  1.00 45.39  ? 304 ALA D N   1 
ATOM   5557  C CA  . ALA B 1 275 ? 31.041  25.494  29.672  1.00 42.94  ? 304 ALA D CA  1 
ATOM   5558  C C   . ALA B 1 275 ? 30.845  26.309  30.957  1.00 42.36  ? 304 ALA D C   1 
ATOM   5559  O O   . ALA B 1 275 ? 31.729  27.055  31.366  1.00 42.52  ? 304 ALA D O   1 
ATOM   5560  C CB  . ALA B 1 275 ? 30.371  26.165  28.487  1.00 43.11  ? 304 ALA D CB  1 
ATOM   5561  N N   . ASN B 1 276 ? 29.664  26.181  31.559  1.00 36.73  ? 305 ASN D N   1 
ATOM   5562  C CA  . ASN B 1 276 ? 29.342  26.817  32.823  1.00 42.65  ? 305 ASN D CA  1 
ATOM   5563  C C   . ASN B 1 276 ? 30.557  26.645  33.744  1.00 38.89  ? 305 ASN D C   1 
ATOM   5564  O O   . ASN B 1 276 ? 31.109  27.618  34.268  1.00 31.21  ? 305 ASN D O   1 
ATOM   5565  C CB  . ASN B 1 276 ? 27.992  26.280  33.312  1.00 42.97  ? 305 ASN D CB  1 
ATOM   5566  C CG  . ASN B 1 276 ? 27.558  26.885  34.624  1.00 47.90  ? 305 ASN D CG  1 
ATOM   5567  O OD1 . ASN B 1 276 ? 28.371  27.546  35.295  1.00 44.68  ? 305 ASN D OD1 1 
ATOM   5568  N ND2 . ASN B 1 276 ? 26.321  26.609  35.033  1.00 38.33  ? 305 ASN D ND2 1 
ATOM   5569  N N   . GLN B 1 277 ? 31.008  25.397  33.874  1.00 34.18  ? 306 GLN D N   1 
ATOM   5570  C CA  . GLN B 1 277 ? 32.072  25.035  34.788  1.00 39.02  ? 306 GLN D CA  1 
ATOM   5571  C C   . GLN B 1 277 ? 33.420  25.617  34.384  1.00 36.14  ? 306 GLN D C   1 
ATOM   5572  O O   . GLN B 1 277 ? 34.157  26.110  35.236  1.00 31.27  ? 306 GLN D O   1 
ATOM   5573  C CB  . GLN B 1 277 ? 32.270  23.531  34.927  1.00 42.81  ? 306 GLN D CB  1 
ATOM   5574  C CG  . GLN B 1 277 ? 31.065  22.842  35.549  1.00 50.86  ? 306 GLN D CG  1 
ATOM   5575  C CD  . GLN B 1 277 ? 29.988  22.442  34.556  1.00 50.30  ? 306 GLN D CD  1 
ATOM   5576  O OE1 . GLN B 1 277 ? 29.659  23.159  33.599  1.00 49.12  ? 306 GLN D OE1 1 
ATOM   5577  N NE2 . GLN B 1 277 ? 29.442  21.255  34.777  1.00 46.63  ? 306 GLN D NE2 1 
ATOM   5578  N N   . GLU B 1 278 ? 33.768  25.555  33.110  1.00 43.26  ? 307 GLU D N   1 
ATOM   5579  C CA  . GLU B 1 278 ? 35.064  26.083  32.704  1.00 48.79  ? 307 GLU D CA  1 
ATOM   5580  C C   . GLU B 1 278 ? 35.111  27.600  32.946  1.00 43.72  ? 307 GLU D C   1 
ATOM   5581  O O   . GLU B 1 278 ? 36.136  28.138  33.338  1.00 45.11  ? 307 GLU D O   1 
ATOM   5582  C CB  . GLU B 1 278 ? 35.443  25.698  31.272  1.00 48.08  ? 307 GLU D CB  1 
ATOM   5583  C CG  . GLU B 1 278 ? 36.934  25.916  30.974  1.00 70.60  ? 307 GLU D CG  1 
ATOM   5584  C CD  . GLU B 1 278 ? 38.005  25.554  32.027  1.00 78.59  ? 307 GLU D CD  1 
ATOM   5585  O OE1 . GLU B 1 278 ? 38.182  24.341  32.312  1.00 71.03  ? 307 GLU D OE1 1 
ATOM   5586  O OE2 . GLU B 1 278 ? 38.678  26.484  32.574  1.00 70.50  ? 307 GLU D OE2 1 
ATOM   5587  N N   . VAL B 1 279 ? 34.018  28.312  32.692  1.00 39.34  ? 308 VAL D N   1 
ATOM   5588  C CA  . VAL B 1 279 ? 33.995  29.743  32.955  1.00 37.43  ? 308 VAL D CA  1 
ATOM   5589  C C   . VAL B 1 279 ? 34.255  29.979  34.442  1.00 36.29  ? 308 VAL D C   1 
ATOM   5590  O O   . VAL B 1 279 ? 35.030  30.859  34.788  1.00 34.09  ? 308 VAL D O   1 
ATOM   5591  C CB  . VAL B 1 279 ? 32.683  30.404  32.495  1.00 37.44  ? 308 VAL D CB  1 
ATOM   5592  C CG1 . VAL B 1 279 ? 32.508  31.837  32.993  1.00 38.51  ? 308 VAL D CG1 1 
ATOM   5593  C CG2 . VAL B 1 279 ? 32.567  30.387  30.983  1.00 39.98  ? 308 VAL D CG2 1 
ATOM   5594  N N   . LEU B 1 280 ? 33.626  29.195  35.333  1.00 38.47  ? 309 LEU D N   1 
ATOM   5595  C CA  . LEU B 1 280 ? 33.735  29.497  36.749  1.00 33.93  ? 309 LEU D CA  1 
ATOM   5596  C C   . LEU B 1 280 ? 35.158  29.221  37.226  1.00 34.64  ? 309 LEU D C   1 
ATOM   5597  O O   . LEU B 1 280 ? 35.652  29.934  38.094  1.00 32.50  ? 309 LEU D O   1 
ATOM   5598  C CB  . LEU B 1 280 ? 32.683  28.753  37.575  1.00 34.39  ? 309 LEU D CB  1 
ATOM   5599  C CG  . LEU B 1 280 ? 32.555  29.164  39.046  1.00 33.75  ? 309 LEU D CG  1 
ATOM   5600  C CD1 . LEU B 1 280 ? 32.297  30.662  39.259  1.00 34.47  ? 309 LEU D CD1 1 
ATOM   5601  C CD2 . LEU B 1 280 ? 31.446  28.344  39.675  1.00 36.40  ? 309 LEU D CD2 1 
ATOM   5602  N N   . VAL B 1 281 ? 35.790  28.163  36.705  1.00 38.64  ? 310 VAL D N   1 
ATOM   5603  C CA  . VAL B 1 281 ? 37.139  27.793  37.105  1.00 39.89  ? 310 VAL D CA  1 
ATOM   5604  C C   . VAL B 1 281 ? 38.087  28.941  36.752  1.00 41.29  ? 310 VAL D C   1 
ATOM   5605  O O   . VAL B 1 281 ? 38.975  29.306  37.523  1.00 41.83  ? 310 VAL D O   1 
ATOM   5606  C CB  . VAL B 1 281 ? 37.597  26.491  36.415  1.00 41.48  ? 310 VAL D CB  1 
ATOM   5607  C CG1 . VAL B 1 281 ? 39.103  26.271  36.579  1.00 39.81  ? 310 VAL D CG1 1 
ATOM   5608  C CG2 . VAL B 1 281 ? 36.805  25.268  36.916  1.00 41.32  ? 310 VAL D CG2 1 
ATOM   5609  N N   . TRP B 1 282 ? 37.894  29.480  35.551  1.00 36.10  ? 311 TRP D N   1 
ATOM   5610  C CA  . TRP B 1 282 ? 38.661  30.610  35.062  1.00 39.60  ? 311 TRP D CA  1 
ATOM   5611  C C   . TRP B 1 282 ? 38.434  31.868  35.933  1.00 39.20  ? 311 TRP D C   1 
ATOM   5612  O O   . TRP B 1 282 ? 39.386  32.455  36.452  1.00 35.23  ? 311 TRP D O   1 
ATOM   5613  C CB  . TRP B 1 282 ? 38.289  30.799  33.585  1.00 38.80  ? 311 TRP D CB  1 
ATOM   5614  C CG  . TRP B 1 282 ? 39.137  31.792  32.836  1.00 45.10  ? 311 TRP D CG  1 
ATOM   5615  C CD1 . TRP B 1 282 ? 40.390  31.603  32.318  1.00 49.15  ? 311 TRP D CD1 1 
ATOM   5616  C CD2 . TRP B 1 282 ? 38.754  33.139  32.495  1.00 44.53  ? 311 TRP D CD2 1 
ATOM   5617  N NE1 . TRP B 1 282 ? 40.826  32.741  31.693  1.00 51.50  ? 311 TRP D NE1 1 
ATOM   5618  C CE2 . TRP B 1 282 ? 39.840  33.698  31.783  1.00 54.78  ? 311 TRP D CE2 1 
ATOM   5619  C CE3 . TRP B 1 282 ? 37.606  33.914  32.708  1.00 46.35  ? 311 TRP D CE3 1 
ATOM   5620  C CZ2 . TRP B 1 282 ? 39.802  35.009  31.318  1.00 47.04  ? 311 TRP D CZ2 1 
ATOM   5621  C CZ3 . TRP B 1 282 ? 37.572  35.204  32.241  1.00 43.85  ? 311 TRP D CZ3 1 
ATOM   5622  C CH2 . TRP B 1 282 ? 38.658  35.742  31.559  1.00 46.80  ? 311 TRP D CH2 1 
ATOM   5623  N N   . LEU B 1 283 ? 37.177  32.287  36.129  1.00 33.45  ? 312 LEU D N   1 
ATOM   5624  C CA  . LEU B 1 283 ? 36.887  33.450  36.965  1.00 33.61  ? 312 LEU D CA  1 
ATOM   5625  C C   . LEU B 1 283 ? 37.518  33.312  38.351  1.00 34.93  ? 312 LEU D C   1 
ATOM   5626  O O   . LEU B 1 283 ? 37.982  34.296  38.918  1.00 39.45  ? 312 LEU D O   1 
ATOM   5627  C CB  . LEU B 1 283 ? 35.395  33.705  37.145  1.00 31.51  ? 312 LEU D CB  1 
ATOM   5628  C CG  . LEU B 1 283 ? 34.609  33.960  35.864  1.00 33.71  ? 312 LEU D CG  1 
ATOM   5629  C CD1 . LEU B 1 283 ? 33.127  33.896  36.136  1.00 35.41  ? 312 LEU D CD1 1 
ATOM   5630  C CD2 . LEU B 1 283 ? 35.009  35.280  35.271  1.00 32.35  ? 312 LEU D CD2 1 
ATOM   5631  N N   . THR B 1 284 ? 37.470  32.116  38.935  1.00 35.25  ? 313 THR D N   1 
ATOM   5632  C CA  . THR B 1 284 ? 37.949  31.939  40.295  1.00 38.61  ? 313 THR D CA  1 
ATOM   5633  C C   . THR B 1 284 ? 39.461  32.201  40.321  1.00 45.26  ? 313 THR D C   1 
ATOM   5634  O O   . THR B 1 284 ? 39.960  32.953  41.173  1.00 35.75  ? 313 THR D O   1 
ATOM   5635  C CB  . THR B 1 284 ? 37.563  30.553  40.804  1.00 37.27  ? 313 THR D CB  1 
ATOM   5636  O OG1 . THR B 1 284 ? 36.138  30.487  40.695  1.00 41.86  ? 313 THR D OG1 1 
ATOM   5637  C CG2 . THR B 1 284 ? 37.951  30.339  42.258  1.00 37.39  ? 313 THR D CG2 1 
ATOM   5638  N N   . GLN B 1 285 ? 40.143  31.629  39.313  1.00 40.33  ? 314 GLN D N   1 
ATOM   5639  C CA  . GLN B 1 285 ? 41.583  31.708  39.146  1.00 44.12  ? 314 GLN D CA  1 
ATOM   5640  C C   . GLN B 1 285 ? 41.999  33.166  38.896  1.00 38.63  ? 314 GLN D C   1 
ATOM   5641  O O   . GLN B 1 285 ? 42.970  33.660  39.472  1.00 36.75  ? 314 GLN D O   1 
ATOM   5642  C CB  . GLN B 1 285 ? 41.785  30.640  38.062  1.00 44.85  ? 314 GLN D CB  1 
ATOM   5643  C CG  . GLN B 1 285 ? 43.180  30.600  37.474  1.00 54.88  ? 314 GLN D CG  1 
ATOM   5644  C CD  . GLN B 1 285 ? 43.415  31.550  36.319  1.00 50.05  ? 314 GLN D CD  1 
ATOM   5645  O OE1 . GLN B 1 285 ? 44.552  31.641  35.843  1.00 61.11  ? 314 GLN D OE1 1 
ATOM   5646  N NE2 . GLN B 1 285 ? 42.388  32.240  35.825  1.00 46.49  ? 314 GLN D NE2 1 
ATOM   5647  N N   . LEU B 1 286 ? 41.198  33.873  38.091  1.00 35.50  ? 315 LEU D N   1 
ATOM   5648  C CA  . LEU B 1 286 ? 41.433  35.270  37.755  1.00 41.22  ? 315 LEU D CA  1 
ATOM   5649  C C   . LEU B 1 286 ? 41.355  36.109  39.024  1.00 42.52  ? 315 LEU D C   1 
ATOM   5650  O O   . LEU B 1 286 ? 42.314  36.801  39.335  1.00 41.13  ? 315 LEU D O   1 
ATOM   5651  C CB  . LEU B 1 286 ? 40.427  35.759  36.716  1.00 42.88  ? 315 LEU D CB  1 
ATOM   5652  C CG  . LEU B 1 286 ? 40.548  37.214  36.240  1.00 50.24  ? 315 LEU D CG  1 
ATOM   5653  C CD1 . LEU B 1 286 ? 41.927  37.537  35.679  1.00 49.81  ? 315 LEU D CD1 1 
ATOM   5654  C CD2 . LEU B 1 286 ? 39.494  37.523  35.166  1.00 52.12  ? 315 LEU D CD2 1 
ATOM   5655  N N   . GLN B 1 287 ? 40.236  36.016  39.766  1.00 38.06  ? 316 GLN D N   1 
ATOM   5656  C CA  . GLN B 1 287 ? 39.998  36.884  40.913  1.00 39.35  ? 316 GLN D CA  1 
ATOM   5657  C C   . GLN B 1 287 ? 41.063  36.708  42.001  1.00 39.60  ? 316 GLN D C   1 
ATOM   5658  O O   . GLN B 1 287 ? 41.476  37.684  42.646  1.00 35.24  ? 316 GLN D O   1 
ATOM   5659  C CB  . GLN B 1 287 ? 38.599  36.607  41.454  1.00 44.55  ? 316 GLN D CB  1 
ATOM   5660  C CG  . GLN B 1 287 ? 38.262  37.414  42.697  1.00 45.84  ? 316 GLN D CG  1 
ATOM   5661  C CD  . GLN B 1 287 ? 36.838  37.915  42.667  1.00 49.13  ? 316 GLN D CD  1 
ATOM   5662  O OE1 . GLN B 1 287 ? 36.499  38.791  41.861  1.00 49.91  ? 316 GLN D OE1 1 
ATOM   5663  N NE2 . GLN B 1 287 ? 36.004  37.401  43.563  1.00 43.16  ? 316 GLN D NE2 1 
ATOM   5664  N N   . LYS B 1 288 ? 41.495  35.459  42.217  1.00 41.75  ? 317 LYS D N   1 
ATOM   5665  C CA  . LYS B 1 288 ? 42.476  35.142  43.249  1.00 48.28  ? 317 LYS D CA  1 
ATOM   5666  C C   . LYS B 1 288 ? 43.827  35.769  42.907  1.00 50.93  ? 317 LYS D C   1 
ATOM   5667  O O   . LYS B 1 288 ? 44.568  36.162  43.811  1.00 47.29  ? 317 LYS D O   1 
ATOM   5668  C CB  . LYS B 1 288 ? 42.671  33.631  43.413  1.00 50.12  ? 317 LYS D CB  1 
ATOM   5669  C CG  . LYS B 1 288 ? 41.557  32.979  44.223  1.00 51.40  ? 317 LYS D CG  1 
ATOM   5670  C CD  . LYS B 1 288 ? 41.624  31.456  44.264  1.00 57.17  ? 317 LYS D CD  1 
ATOM   5671  C CE  . LYS B 1 288 ? 40.589  30.824  45.179  1.00 66.15  ? 317 LYS D CE  1 
ATOM   5672  N NZ  . LYS B 1 288 ? 39.267  31.470  45.200  1.00 64.82  ? 317 LYS D NZ  1 
ATOM   5673  N N   . GLU B 1 289 ? 44.113  35.839  41.599  1.00 47.99  ? 318 GLU D N   1 
ATOM   5674  C CA  . GLU B 1 289 ? 45.369  36.357  41.089  1.00 51.10  ? 318 GLU D CA  1 
ATOM   5675  C C   . GLU B 1 289 ? 45.417  37.875  41.220  1.00 47.06  ? 318 GLU D C   1 
ATOM   5676  O O   . GLU B 1 289 ? 46.358  38.392  41.819  1.00 44.89  ? 318 GLU D O   1 
ATOM   5677  C CB  . GLU B 1 289 ? 45.562  35.996  39.620  1.00 52.53  ? 318 GLU D CB  1 
ATOM   5678  C CG  . GLU B 1 289 ? 46.892  36.477  39.052  1.00 59.61  ? 318 GLU D CG  1 
ATOM   5679  C CD  . GLU B 1 289 ? 47.197  35.825  37.718  1.00 66.23  ? 318 GLU D CD  1 
ATOM   5680  O OE1 . GLU B 1 289 ? 47.069  34.582  37.612  1.00 65.29  ? 318 GLU D OE1 1 
ATOM   5681  O OE2 . GLU B 1 289 ? 47.557  36.573  36.784  1.00 78.95  ? 318 GLU D OE2 1 
ATOM   5682  N N   . VAL B 1 290 ? 44.397  38.560  40.672  1.00 40.78  ? 319 VAL D N   1 
ATOM   5683  C CA  . VAL B 1 290 ? 44.439  40.002  40.462  1.00 44.13  ? 319 VAL D CA  1 
ATOM   5684  C C   . VAL B 1 290 ? 43.652  40.728  41.549  1.00 45.50  ? 319 VAL D C   1 
ATOM   5685  O O   . VAL B 1 290 ? 43.592  41.961  41.537  1.00 55.87  ? 319 VAL D O   1 
ATOM   5686  C CB  . VAL B 1 290 ? 43.945  40.441  39.062  1.00 47.43  ? 319 VAL D CB  1 
ATOM   5687  C CG1 . VAL B 1 290 ? 44.735  39.779  37.928  1.00 50.16  ? 319 VAL D CG1 1 
ATOM   5688  C CG2 . VAL B 1 290 ? 42.453  40.219  38.876  1.00 45.01  ? 319 VAL D CG2 1 
ATOM   5689  N N   . GLY B 1 291 ? 43.037  39.983  42.470  1.00 44.24  ? 320 GLY D N   1 
ATOM   5690  C CA  . GLY B 1 291 ? 42.249  40.587  43.536  1.00 46.00  ? 320 GLY D CA  1 
ATOM   5691  C C   . GLY B 1 291 ? 40.912  41.132  43.038  1.00 48.23  ? 320 GLY D C   1 
ATOM   5692  O O   . GLY B 1 291 ? 40.715  41.385  41.848  1.00 48.86  ? 320 GLY D O   1 
ATOM   5693  N N   . LYS B 1 292 ? 39.995  41.355  43.983  1.00 57.20  ? 321 LYS D N   1 
ATOM   5694  C CA  . LYS B 1 292 ? 38.618  41.683  43.644  1.00 62.07  ? 321 LYS D CA  1 
ATOM   5695  C C   . LYS B 1 292 ? 38.440  43.158  43.257  1.00 59.09  ? 321 LYS D C   1 
ATOM   5696  O O   . LYS B 1 292 ? 37.418  43.507  42.672  1.00 61.04  ? 321 LYS D O   1 
ATOM   5697  C CB  . LYS B 1 292 ? 37.690  41.245  44.783  1.00 66.55  ? 321 LYS D CB  1 
ATOM   5698  C CG  . LYS B 1 292 ? 37.416  42.252  45.895  1.00 67.71  ? 321 LYS D CG  1 
ATOM   5699  C CD  . LYS B 1 292 ? 36.420  41.744  46.939  1.00 75.50  ? 321 LYS D CD  1 
ATOM   5700  C CE  . LYS B 1 292 ? 36.692  40.341  47.424  1.00 76.05  ? 321 LYS D CE  1 
ATOM   5701  N NZ  . LYS B 1 292 ? 35.923  40.011  48.629  1.00 79.40  ? 321 LYS D NZ  1 
ATOM   5702  N N   . ASP B 1 293 ? 39.418  44.029  43.543  1.00 55.51  ? 322 ASP D N   1 
ATOM   5703  C CA  . ASP B 1 293 ? 39.290  45.428  43.144  1.00 66.57  ? 322 ASP D CA  1 
ATOM   5704  C C   . ASP B 1 293 ? 40.277  45.770  42.021  1.00 62.89  ? 322 ASP D C   1 
ATOM   5705  O O   . ASP B 1 293 ? 40.878  46.838  42.017  1.00 57.27  ? 322 ASP D O   1 
ATOM   5706  C CB  . ASP B 1 293 ? 39.293  46.353  44.356  1.00 72.30  ? 322 ASP D CB  1 
ATOM   5707  C CG  . ASP B 1 293 ? 38.048  46.236  45.227  1.00 78.61  ? 322 ASP D CG  1 
ATOM   5708  O OD1 . ASP B 1 293 ? 36.925  46.421  44.682  1.00 81.06  ? 322 ASP D OD1 1 
ATOM   5709  O OD2 . ASP B 1 293 ? 38.202  45.916  46.427  1.00 72.65  ? 322 ASP D OD2 1 
ATOM   5710  N N   . VAL B 1 294 ? 40.402  44.869  41.041  1.00 51.42  ? 323 VAL D N   1 
ATOM   5711  C CA  . VAL B 1 294 ? 41.250  45.085  39.886  1.00 44.72  ? 323 VAL D CA  1 
ATOM   5712  C C   . VAL B 1 294 ? 40.687  46.226  39.037  1.00 46.50  ? 323 VAL D C   1 
ATOM   5713  O O   . VAL B 1 294 ? 39.469  46.382  38.894  1.00 46.11  ? 323 VAL D O   1 
ATOM   5714  C CB  . VAL B 1 294 ? 41.342  43.785  39.067  1.00 44.55  ? 323 VAL D CB  1 
ATOM   5715  C CG1 . VAL B 1 294 ? 39.961  43.239  38.679  1.00 41.91  ? 323 VAL D CG1 1 
ATOM   5716  C CG2 . VAL B 1 294 ? 42.205  43.981  37.831  1.00 45.46  ? 323 VAL D CG2 1 
ATOM   5717  N N   . SER B 1 295 ? 41.598  47.021  38.467  1.00 43.47  ? 324 SER D N   1 
ATOM   5718  C CA  . SER B 1 295 ? 41.213  48.092  37.567  1.00 47.03  ? 324 SER D CA  1 
ATOM   5719  C C   . SER B 1 295 ? 40.908  47.493  36.196  1.00 44.52  ? 324 SER D C   1 
ATOM   5720  O O   . SER B 1 295 ? 41.488  46.462  35.819  1.00 43.47  ? 324 SER D O   1 
ATOM   5721  C CB  . SER B 1 295 ? 42.280  49.178  37.475  1.00 48.78  ? 324 SER D CB  1 
ATOM   5722  O OG  . SER B 1 295 ? 43.451  48.705  36.818  1.00 47.96  ? 324 SER D OG  1 
ATOM   5723  N N   . ASP B 1 296 ? 40.004  48.174  35.477  1.00 44.11  ? 325 ASP D N   1 
ATOM   5724  C CA  . ASP B 1 296 ? 39.753  47.949  34.060  1.00 49.42  ? 325 ASP D CA  1 
ATOM   5725  C C   . ASP B 1 296 ? 41.070  47.812  33.287  1.00 49.51  ? 325 ASP D C   1 
ATOM   5726  O O   . ASP B 1 296 ? 41.208  46.877  32.486  1.00 44.41  ? 325 ASP D O   1 
ATOM   5727  C CB  . ASP B 1 296 ? 38.849  49.028  33.485  1.00 48.50  ? 325 ASP D CB  1 
ATOM   5728  C CG  . ASP B 1 296 ? 37.446  49.121  34.075  1.00 52.38  ? 325 ASP D CG  1 
ATOM   5729  O OD1 . ASP B 1 296 ? 37.081  48.281  34.950  1.00 50.62  ? 325 ASP D OD1 1 
ATOM   5730  O OD2 . ASP B 1 296 ? 36.716  50.047  33.667  1.00 57.08  ? 325 ASP D OD2 1 
ATOM   5731  N N   . GLU B 1 297 ? 42.038  48.701  33.577  1.00 42.97  ? 326 GLU D N   1 
ATOM   5732  C CA  . GLU B 1 297 ? 43.301  48.777  32.846  1.00 56.76  ? 326 GLU D CA  1 
ATOM   5733  C C   . GLU B 1 297 ? 44.003  47.429  32.983  1.00 52.31  ? 326 GLU D C   1 
ATOM   5734  O O   . GLU B 1 297 ? 44.366  46.799  31.987  1.00 48.12  ? 326 GLU D O   1 
ATOM   5735  C CB  . GLU B 1 297 ? 44.237  49.906  33.319  1.00 59.35  ? 326 GLU D CB  1 
ATOM   5736  C CG  . GLU B 1 297 ? 45.214  50.416  32.251  1.00 72.69  ? 326 GLU D CG  1 
ATOM   5737  C CD  . GLU B 1 297 ? 46.439  51.268  32.647  1.00 78.56  ? 326 GLU D CD  1 
ATOM   5738  O OE1 . GLU B 1 297 ? 46.313  52.291  33.378  1.00 74.10  ? 326 GLU D OE1 1 
ATOM   5739  O OE2 . GLU B 1 297 ? 47.561  50.928  32.175  1.00 61.15  ? 326 GLU D OE2 1 
ATOM   5740  N N   . LYS B 1 298 ? 44.155  46.996  34.237  1.00 44.27  ? 327 LYS D N   1 
ATOM   5741  C CA  . LYS B 1 298 ? 44.874  45.775  34.548  1.00 49.82  ? 327 LYS D CA  1 
ATOM   5742  C C   . LYS B 1 298 ? 44.070  44.570  34.056  1.00 46.47  ? 327 LYS D C   1 
ATOM   5743  O O   . LYS B 1 298 ? 44.646  43.554  33.655  1.00 44.67  ? 327 LYS D O   1 
ATOM   5744  C CB  . LYS B 1 298 ? 45.128  45.782  36.058  1.00 52.91  ? 327 LYS D CB  1 
ATOM   5745  C CG  . LYS B 1 298 ? 45.852  44.566  36.590  1.00 65.48  ? 327 LYS D CG  1 
ATOM   5746  C CD  . LYS B 1 298 ? 47.333  44.484  36.248  1.00 72.71  ? 327 LYS D CD  1 
ATOM   5747  C CE  . LYS B 1 298 ? 47.845  43.088  36.436  1.00 80.17  ? 327 LYS D CE  1 
ATOM   5748  N NZ  . LYS B 1 298 ? 47.476  42.573  37.761  1.00 81.16  ? 327 LYS D NZ  1 
ATOM   5749  N N   . LEU B 1 299 ? 42.737  44.685  34.094  1.00 41.20  ? 328 LEU D N   1 
ATOM   5750  C CA  . LEU B 1 299 ? 41.883  43.601  33.612  1.00 47.29  ? 328 LEU D CA  1 
ATOM   5751  C C   . LEU B 1 299 ? 42.040  43.463  32.100  1.00 38.70  ? 328 LEU D C   1 
ATOM   5752  O O   . LEU B 1 299 ? 42.243  42.359  31.600  1.00 40.04  ? 328 LEU D O   1 
ATOM   5753  C CB  . LEU B 1 299 ? 40.422  43.843  34.002  1.00 52.14  ? 328 LEU D CB  1 
ATOM   5754  C CG  . LEU B 1 299 ? 39.431  42.711  33.710  1.00 57.36  ? 328 LEU D CG  1 
ATOM   5755  C CD1 . LEU B 1 299 ? 39.926  41.373  34.258  1.00 56.81  ? 328 LEU D CD1 1 
ATOM   5756  C CD2 . LEU B 1 299 ? 38.053  43.042  34.277  1.00 54.86  ? 328 LEU D CD2 1 
ATOM   5757  N N   . ARG B 1 300 ? 41.969  44.598  31.396  1.00 41.10  ? 329 ARG D N   1 
ATOM   5758  C CA  . ARG B 1 300 ? 42.096  44.651  29.944  1.00 46.85  ? 329 ARG D CA  1 
ATOM   5759  C C   . ARG B 1 300 ? 43.416  44.039  29.478  1.00 44.31  ? 329 ARG D C   1 
ATOM   5760  O O   . ARG B 1 300 ? 43.407  43.284  28.506  1.00 50.79  ? 329 ARG D O   1 
ATOM   5761  C CB  . ARG B 1 300 ? 41.912  46.085  29.442  1.00 47.79  ? 329 ARG D CB  1 
ATOM   5762  C CG  . ARG B 1 300 ? 42.131  46.282  27.948  1.00 53.02  ? 329 ARG D CG  1 
ATOM   5763  C CD  . ARG B 1 300 ? 41.691  47.677  27.516  1.00 55.13  ? 329 ARG D CD  1 
ATOM   5764  N NE  . ARG B 1 300 ? 40.224  47.816  27.537  1.00 61.76  ? 329 ARG D NE  1 
ATOM   5765  C CZ  . ARG B 1 300 ? 39.464  48.586  28.332  1.00 64.66  ? 329 ARG D CZ  1 
ATOM   5766  N NH1 . ARG B 1 300 ? 39.994  49.280  29.323  1.00 68.68  ? 329 ARG D NH1 1 
ATOM   5767  N NH2 . ARG B 1 300 ? 38.152  48.648  28.141  1.00 68.48  ? 329 ARG D NH2 1 
ATOM   5768  N N   . ASP B 1 301 ? 44.509  44.323  30.216  1.00 50.42  ? 330 ASP D N   1 
ATOM   5769  C CA  . ASP B 1 301 ? 45.859  43.807  29.972  1.00 52.44  ? 330 ASP D CA  1 
ATOM   5770  C C   . ASP B 1 301 ? 45.932  42.293  30.114  1.00 47.20  ? 330 ASP D C   1 
ATOM   5771  O O   . ASP B 1 301 ? 46.538  41.624  29.272  1.00 47.75  ? 330 ASP D O   1 
ATOM   5772  C CB  . ASP B 1 301 ? 46.883  44.377  30.949  1.00 59.38  ? 330 ASP D CB  1 
ATOM   5773  C CG  . ASP B 1 301 ? 47.252  45.841  30.752  1.00 65.37  ? 330 ASP D CG  1 
ATOM   5774  O OD1 . ASP B 1 301 ? 47.169  46.318  29.596  1.00 67.65  ? 330 ASP D OD1 1 
ATOM   5775  O OD2 . ASP B 1 301 ? 47.570  46.501  31.765  1.00 73.86  ? 330 ASP D OD2 1 
ATOM   5776  N N   . TYR B 1 302 ? 45.360  41.774  31.207  1.00 47.03  ? 331 TYR D N   1 
ATOM   5777  C CA  . TYR B 1 302 ? 45.287  40.338  31.445  1.00 45.50  ? 331 TYR D CA  1 
ATOM   5778  C C   . TYR B 1 302 ? 44.570  39.618  30.292  1.00 46.39  ? 331 TYR D C   1 
ATOM   5779  O O   . TYR B 1 302 ? 44.932  38.498  29.908  1.00 49.68  ? 331 TYR D O   1 
ATOM   5780  C CB  . TYR B 1 302 ? 44.524  40.079  32.748  1.00 50.15  ? 331 TYR D CB  1 
ATOM   5781  C CG  . TYR B 1 302 ? 44.411  38.600  33.095  1.00 51.46  ? 331 TYR D CG  1 
ATOM   5782  C CD1 . TYR B 1 302 ? 43.427  37.801  32.509  1.00 51.63  ? 331 TYR D CD1 1 
ATOM   5783  C CD2 . TYR B 1 302 ? 45.307  37.996  33.980  1.00 53.39  ? 331 TYR D CD2 1 
ATOM   5784  C CE1 . TYR B 1 302 ? 43.325  36.442  32.792  1.00 54.26  ? 331 TYR D CE1 1 
ATOM   5785  C CE2 . TYR B 1 302 ? 45.222  36.638  34.261  1.00 52.66  ? 331 TYR D CE2 1 
ATOM   5786  C CZ  . TYR B 1 302 ? 44.230  35.864  33.668  1.00 54.89  ? 331 TYR D CZ  1 
ATOM   5787  O OH  . TYR B 1 302 ? 44.119  34.536  33.938  1.00 59.10  ? 331 TYR D OH  1 
ATOM   5788  N N   . ILE B 1 303 ? 43.491  40.230  29.790  1.00 40.31  ? 332 ILE D N   1 
ATOM   5789  C CA  . ILE B 1 303 ? 42.716  39.656  28.695  1.00 46.24  ? 332 ILE D CA  1 
ATOM   5790  C C   . ILE B 1 303 ? 43.568  39.657  27.422  1.00 50.94  ? 332 ILE D C   1 
ATOM   5791  O O   . ILE B 1 303 ? 43.592  38.667  26.676  1.00 46.36  ? 332 ILE D O   1 
ATOM   5792  C CB  . ILE B 1 303 ? 41.395  40.421  28.487  1.00 42.92  ? 332 ILE D CB  1 
ATOM   5793  C CG1 . ILE B 1 303 ? 40.503  40.449  29.743  1.00 44.57  ? 332 ILE D CG1 1 
ATOM   5794  C CG2 . ILE B 1 303 ? 40.650  39.866  27.284  1.00 41.98  ? 332 ILE D CG2 1 
ATOM   5795  C CD1 . ILE B 1 303 ? 39.978  39.091  30.161  1.00 50.97  ? 332 ILE D CD1 1 
ATOM   5796  N N   . TRP B 1 304 ? 44.250  40.786  27.179  1.00 43.59  ? 333 TRP D N   1 
ATOM   5797  C CA  . TRP B 1 304 ? 45.119  40.879  26.016  1.00 48.74  ? 333 TRP D CA  1 
ATOM   5798  C C   . TRP B 1 304 ? 46.174  39.787  26.081  1.00 48.25  ? 333 TRP D C   1 
ATOM   5799  O O   . TRP B 1 304 ? 46.417  39.104  25.097  1.00 44.40  ? 333 TRP D O   1 
ATOM   5800  C CB  . TRP B 1 304 ? 45.747  42.270  25.869  1.00 52.28  ? 333 TRP D CB  1 
ATOM   5801  C CG  . TRP B 1 304 ? 44.940  43.162  24.965  1.00 60.44  ? 333 TRP D CG  1 
ATOM   5802  C CD1 . TRP B 1 304 ? 44.254  44.302  25.284  1.00 64.79  ? 333 TRP D CD1 1 
ATOM   5803  C CD2 . TRP B 1 304 ? 44.705  42.930  23.558  1.00 68.45  ? 333 TRP D CD2 1 
ATOM   5804  N NE1 . TRP B 1 304 ? 43.634  44.811  24.171  1.00 63.85  ? 333 TRP D NE1 1 
ATOM   5805  C CE2 . TRP B 1 304 ? 43.886  43.988  23.100  1.00 71.67  ? 333 TRP D CE2 1 
ATOM   5806  C CE3 . TRP B 1 304 ? 45.109  41.938  22.650  1.00 74.20  ? 333 TRP D CE3 1 
ATOM   5807  C CZ2 . TRP B 1 304 ? 43.465  44.069  21.771  1.00 83.49  ? 333 TRP D CZ2 1 
ATOM   5808  C CZ3 . TRP B 1 304 ? 44.678  42.012  21.343  1.00 76.39  ? 333 TRP D CZ3 1 
ATOM   5809  C CH2 . TRP B 1 304 ? 43.867  43.065  20.913  1.00 84.17  ? 333 TRP D CH2 1 
ATOM   5810  N N   . ASN B 1 305 ? 46.746  39.571  27.261  1.00 52.13  ? 334 ASN D N   1 
ATOM   5811  C CA  . ASN B 1 305 ? 47.724  38.513  27.399  1.00 53.49  ? 334 ASN D CA  1 
ATOM   5812  C C   . ASN B 1 305 ? 47.131  37.164  27.051  1.00 54.69  ? 334 ASN D C   1 
ATOM   5813  O O   . ASN B 1 305 ? 47.748  36.399  26.315  1.00 59.64  ? 334 ASN D O   1 
ATOM   5814  C CB  . ASN B 1 305 ? 48.323  38.411  28.789  1.00 59.37  ? 334 ASN D CB  1 
ATOM   5815  C CG  . ASN B 1 305 ? 49.749  38.889  28.763  1.00 67.88  ? 334 ASN D CG  1 
ATOM   5816  O OD1 . ASN B 1 305 ? 50.658  38.083  28.524  1.00 81.08  ? 334 ASN D OD1 1 
ATOM   5817  N ND2 . ASN B 1 305 ? 49.944  40.195  28.893  1.00 65.07  ? 334 ASN D ND2 1 
ATOM   5818  N N   . THR B 1 306 ? 45.982  36.850  27.643  1.00 49.65  ? 335 THR D N   1 
ATOM   5819  C CA  . THR B 1 306 ? 45.389  35.550  27.400  1.00 58.44  ? 335 THR D CA  1 
ATOM   5820  C C   . THR B 1 306 ? 45.193  35.361  25.889  1.00 54.01  ? 335 THR D C   1 
ATOM   5821  O O   . THR B 1 306 ? 45.570  34.334  25.327  1.00 53.21  ? 335 THR D O   1 
ATOM   5822  C CB  . THR B 1 306 ? 44.085  35.427  28.190  1.00 61.12  ? 335 THR D CB  1 
ATOM   5823  O OG1 . THR B 1 306 ? 44.382  35.664  29.561  1.00 57.42  ? 335 THR D OG1 1 
ATOM   5824  C CG2 . THR B 1 306 ? 43.478  34.042  28.080  1.00 67.09  ? 335 THR D CG2 1 
ATOM   5825  N N   . LEU B 1 307 ? 44.628  36.370  25.221  1.00 57.47  ? 336 LEU D N   1 
ATOM   5826  C CA  . LEU B 1 307 ? 44.347  36.258  23.795  1.00 66.84  ? 336 LEU D CA  1 
ATOM   5827  C C   . LEU B 1 307 ? 45.632  36.055  22.989  1.00 70.17  ? 336 LEU D C   1 
ATOM   5828  O O   . LEU B 1 307 ? 45.652  35.237  22.076  1.00 71.44  ? 336 LEU D O   1 
ATOM   5829  C CB  . LEU B 1 307 ? 43.542  37.451  23.285  1.00 63.94  ? 336 LEU D CB  1 
ATOM   5830  C CG  . LEU B 1 307 ? 42.018  37.302  23.336  1.00 67.39  ? 336 LEU D CG  1 
ATOM   5831  C CD1 . LEU B 1 307 ? 41.576  36.624  24.599  1.00 70.08  ? 336 LEU D CD1 1 
ATOM   5832  C CD2 . LEU B 1 307 ? 41.322  38.652  23.224  1.00 68.20  ? 336 LEU D CD2 1 
ATOM   5833  N N   . ASN B 1 308 ? 46.712  36.768  23.328  1.00 67.71  ? 337 ASN D N   1 
ATOM   5834  C CA  . ASN B 1 308 ? 47.923  36.682  22.527  1.00 78.29  ? 337 ASN D CA  1 
ATOM   5835  C C   . ASN B 1 308 ? 48.671  35.377  22.797  1.00 73.45  ? 337 ASN D C   1 
ATOM   5836  O O   . ASN B 1 308 ? 49.577  35.052  22.036  1.00 71.96  ? 337 ASN D O   1 
ATOM   5837  C CB  . ASN B 1 308 ? 48.809  37.916  22.676  1.00 83.07  ? 337 ASN D CB  1 
ATOM   5838  C CG  . ASN B 1 308 ? 48.287  39.094  21.882  1.00 92.22  ? 337 ASN D CG  1 
ATOM   5839  O OD1 . ASN B 1 308 ? 47.458  38.931  20.973  1.00 95.74  ? 337 ASN D OD1 1 
ATOM   5840  N ND2 . ASN B 1 308 ? 48.759  40.289  22.206  1.00 99.81  ? 337 ASN D ND2 1 
ATOM   5841  N N   . SER B 1 309 ? 48.273  34.610  23.829  1.00 79.46  ? 338 SER D N   1 
ATOM   5842  C CA  . SER B 1 309 ? 48.887  33.315  24.108  1.00 74.85  ? 338 SER D CA  1 
ATOM   5843  C C   . SER B 1 309 ? 48.230  32.190  23.300  1.00 70.61  ? 338 SER D C   1 
ATOM   5844  O O   . SER B 1 309 ? 48.600  31.024  23.463  1.00 71.34  ? 338 SER D O   1 
ATOM   5845  C CB  . SER B 1 309 ? 48.848  32.997  25.584  1.00 77.27  ? 338 SER D CB  1 
ATOM   5846  O OG  . SER B 1 309 ? 47.634  32.343  25.934  1.00 83.86  ? 338 SER D OG  1 
ATOM   5847  N N   . GLY B 1 310 ? 47.262  32.542  22.437  1.00 61.40  ? 339 GLY D N   1 
ATOM   5848  C CA  . GLY B 1 310 ? 46.499  31.574  21.665  1.00 60.04  ? 339 GLY D CA  1 
ATOM   5849  C C   . GLY B 1 310 ? 45.394  30.930  22.501  1.00 65.83  ? 339 GLY D C   1 
ATOM   5850  O O   . GLY B 1 310 ? 44.953  29.819  22.214  1.00 70.34  ? 339 GLY D O   1 
ATOM   5851  N N   . ARG B 1 311 ? 44.938  31.645  23.532  1.00 66.14  ? 340 ARG D N   1 
ATOM   5852  C CA  . ARG B 1 311 ? 43.960  31.121  24.472  1.00 69.11  ? 340 ARG D CA  1 
ATOM   5853  C C   . ARG B 1 311 ? 42.679  31.937  24.289  1.00 66.85  ? 340 ARG D C   1 
ATOM   5854  O O   . ARG B 1 311 ? 42.761  33.062  23.786  1.00 53.26  ? 340 ARG D O   1 
ATOM   5855  C CB  . ARG B 1 311 ? 44.656  31.184  25.839  1.00 72.15  ? 340 ARG D CB  1 
ATOM   5856  C CG  . ARG B 1 311 ? 44.110  30.354  26.993  1.00 78.10  ? 340 ARG D CG  1 
ATOM   5857  C CD  . ARG B 1 311 ? 45.100  30.315  28.171  1.00 84.16  ? 340 ARG D CD  1 
ATOM   5858  N NE  . ARG B 1 311 ? 46.353  29.620  27.841  1.00 86.43  ? 340 ARG D NE  1 
ATOM   5859  C CZ  . ARG B 1 311 ? 46.478  28.324  27.523  1.00 92.22  ? 340 ARG D CZ  1 
ATOM   5860  N NH1 . ARG B 1 311 ? 45.446  27.503  27.623  1.00 92.88  ? 340 ARG D NH1 1 
ATOM   5861  N NH2 . ARG B 1 311 ? 47.645  27.839  27.124  1.00 85.31  ? 340 ARG D NH2 1 
ATOM   5862  N N   . VAL B 1 312 ? 41.521  31.346  24.666  1.00 65.95  ? 341 VAL D N   1 
ATOM   5863  C CA  . VAL B 1 312 ? 40.193  31.948  24.515  1.00 62.99  ? 341 VAL D CA  1 
ATOM   5864  C C   . VAL B 1 312 ? 39.762  32.542  25.861  1.00 57.43  ? 341 VAL D C   1 
ATOM   5865  O O   . VAL B 1 312 ? 40.271  32.141  26.906  1.00 48.47  ? 341 VAL D O   1 
ATOM   5866  C CB  . VAL B 1 312 ? 39.081  30.999  23.994  1.00 61.49  ? 341 VAL D CB  1 
ATOM   5867  C CG1 . VAL B 1 312 ? 38.966  30.979  22.474  1.00 57.61  ? 341 VAL D CG1 1 
ATOM   5868  C CG2 . VAL B 1 312 ? 39.200  29.580  24.551  1.00 60.35  ? 341 VAL D CG2 1 
ATOM   5869  N N   . VAL B 1 313 ? 38.853  33.527  25.814  1.00 49.51  ? 342 VAL D N   1 
ATOM   5870  C CA  . VAL B 1 313 ? 38.147  33.989  27.000  1.00 53.02  ? 342 VAL D CA  1 
ATOM   5871  C C   . VAL B 1 313 ? 36.910  33.095  27.150  1.00 48.58  ? 342 VAL D C   1 
ATOM   5872  O O   . VAL B 1 313 ? 35.941  33.252  26.409  1.00 47.22  ? 342 VAL D O   1 
ATOM   5873  C CB  . VAL B 1 313 ? 37.752  35.484  26.953  1.00 53.94  ? 342 VAL D CB  1 
ATOM   5874  C CG1 . VAL B 1 313 ? 36.994  35.942  28.197  1.00 54.31  ? 342 VAL D CG1 1 
ATOM   5875  C CG2 . VAL B 1 313 ? 38.956  36.388  26.735  1.00 57.82  ? 342 VAL D CG2 1 
ATOM   5876  N N   . PRO B 1 314 ? 36.873  32.144  28.110  1.00 49.71  ? 343 PRO D N   1 
ATOM   5877  C CA  . PRO B 1 314 ? 35.719  31.251  28.231  1.00 51.33  ? 343 PRO D CA  1 
ATOM   5878  C C   . PRO B 1 314 ? 34.408  32.025  28.386  1.00 45.59  ? 343 PRO D C   1 
ATOM   5879  O O   . PRO B 1 314 ? 34.306  32.959  29.182  1.00 46.00  ? 343 PRO D O   1 
ATOM   5880  C CB  . PRO B 1 314 ? 36.083  30.389  29.476  1.00 55.37  ? 343 PRO D CB  1 
ATOM   5881  C CG  . PRO B 1 314 ? 37.592  30.471  29.568  1.00 53.58  ? 343 PRO D CG  1 
ATOM   5882  C CD  . PRO B 1 314 ? 37.893  31.899  29.152  1.00 52.39  ? 343 PRO D CD  1 
ATOM   5883  N N   . GLY B 1 315 ? 33.419  31.663  27.564  1.00 47.69  ? 344 GLY D N   1 
ATOM   5884  C CA  . GLY B 1 315 ? 32.076  32.203  27.672  1.00 46.81  ? 344 GLY D CA  1 
ATOM   5885  C C   . GLY B 1 315 ? 31.829  33.365  26.713  1.00 50.17  ? 344 GLY D C   1 
ATOM   5886  O O   . GLY B 1 315 ? 30.707  33.871  26.658  1.00 54.99  ? 344 GLY D O   1 
ATOM   5887  N N   . TYR B 1 316 ? 32.887  33.788  26.019  1.00 48.96  ? 345 TYR D N   1 
ATOM   5888  C CA  . TYR B 1 316 ? 32.777  34.838  24.975  1.00 47.72  ? 345 TYR D CA  1 
ATOM   5889  C C   . TYR B 1 316 ? 33.153  34.188  23.641  1.00 58.43  ? 345 TYR D C   1 
ATOM   5890  O O   . TYR B 1 316 ? 34.356  34.001  23.406  1.00 54.34  ? 345 TYR D O   1 
ATOM   5891  C CB  . TYR B 1 316 ? 33.697  36.000  25.331  1.00 44.63  ? 345 TYR D CB  1 
ATOM   5892  C CG  . TYR B 1 316 ? 33.197  36.893  26.453  1.00 46.11  ? 345 TYR D CG  1 
ATOM   5893  C CD1 . TYR B 1 316 ? 33.322  36.507  27.779  1.00 44.76  ? 345 TYR D CD1 1 
ATOM   5894  C CD2 . TYR B 1 316 ? 32.607  38.119  26.181  1.00 42.91  ? 345 TYR D CD2 1 
ATOM   5895  C CE1 . TYR B 1 316 ? 32.873  37.314  28.805  1.00 38.45  ? 345 TYR D CE1 1 
ATOM   5896  C CE2 . TYR B 1 316 ? 32.161  38.941  27.200  1.00 42.37  ? 345 TYR D CE2 1 
ATOM   5897  C CZ  . TYR B 1 316 ? 32.291  38.532  28.513  1.00 41.40  ? 345 TYR D CZ  1 
ATOM   5898  O OH  . TYR B 1 316 ? 31.846  39.314  29.530  1.00 41.36  ? 345 TYR D OH  1 
ATOM   5899  N N   . GLY B 1 317 ? 32.166  33.834  22.809  1.00 79.07  ? 346 GLY D N   1 
ATOM   5900  C CA  . GLY B 1 317 ? 32.388  33.150  21.509  1.00 93.10  ? 346 GLY D CA  1 
ATOM   5901  C C   . GLY B 1 317 ? 31.032  32.863  20.912  1.00 112.43 ? 346 GLY D C   1 
ATOM   5902  O O   . GLY B 1 317 ? 30.445  31.823  21.277  1.00 96.92  ? 346 GLY D O   1 
ATOM   5903  N N   . HIS B 1 318 ? 30.554  33.707  19.991  1.00 141.17 ? 347 HIS D N   1 
ATOM   5904  C CA  . HIS B 1 318 ? 29.159  33.585  19.576  1.00 161.83 ? 347 HIS D CA  1 
ATOM   5905  C C   . HIS B 1 318 ? 28.983  32.927  18.207  1.00 171.49 ? 347 HIS D C   1 
ATOM   5906  O O   . HIS B 1 318 ? 29.932  32.811  17.433  1.00 176.57 ? 347 HIS D O   1 
ATOM   5907  C CB  . HIS B 1 318 ? 28.465  34.953  19.572  1.00 165.06 ? 347 HIS D CB  1 
ATOM   5908  C CG  . HIS B 1 318 ? 27.659  35.216  20.797  1.00 167.74 ? 347 HIS D CG  1 
ATOM   5909  N ND1 . HIS B 1 318 ? 27.282  36.489  21.161  1.00 169.59 ? 347 HIS D ND1 1 
ATOM   5910  C CD2 . HIS B 1 318 ? 27.132  34.393  21.715  1.00 164.27 ? 347 HIS D CD2 1 
ATOM   5911  C CE1 . HIS B 1 318 ? 26.569  36.424  22.273  1.00 160.95 ? 347 HIS D CE1 1 
ATOM   5912  N NE2 . HIS B 1 318 ? 26.467  35.164  22.630  1.00 167.05 ? 347 HIS D NE2 1 
ATOM   5913  N N   . ALA B 1 319 ? 27.728  32.522  17.934  1.00 167.98 ? 348 ALA D N   1 
ATOM   5914  C CA  . ALA B 1 319 ? 27.334  31.878  16.690  1.00 151.98 ? 348 ALA D CA  1 
ATOM   5915  C C   . ALA B 1 319 ? 27.033  32.946  15.643  1.00 152.45 ? 348 ALA D C   1 
ATOM   5916  O O   . ALA B 1 319 ? 27.954  33.527  15.078  1.00 159.28 ? 348 ALA D O   1 
ATOM   5917  C CB  . ALA B 1 319 ? 26.150  30.956  16.926  1.00 134.37 ? 348 ALA D CB  1 
ATOM   5918  N N   . VAL B 1 320 ? 25.745  33.206  15.393  1.00 156.32 ? 349 VAL D N   1 
ATOM   5919  C CA  . VAL B 1 320 ? 25.341  34.307  14.535  1.00 169.67 ? 349 VAL D CA  1 
ATOM   5920  C C   . VAL B 1 320 ? 24.830  35.432  15.433  1.00 162.78 ? 349 VAL D C   1 
ATOM   5921  O O   . VAL B 1 320 ? 24.091  36.303  14.979  1.00 185.35 ? 349 VAL D O   1 
ATOM   5922  C CB  . VAL B 1 320 ? 24.287  33.874  13.488  1.00 179.07 ? 349 VAL D CB  1 
ATOM   5923  C CG1 . VAL B 1 320 ? 22.917  33.587  14.103  1.00 176.35 ? 349 VAL D CG1 1 
ATOM   5924  C CG2 . VAL B 1 320 ? 24.156  34.877  12.343  1.00 174.80 ? 349 VAL D CG2 1 
ATOM   5925  N N   . LEU B 1 321 ? 25.236  35.422  16.709  1.00 134.59 ? 350 LEU D N   1 
ATOM   5926  C CA  . LEU B 1 321 ? 24.611  36.308  17.674  1.00 127.90 ? 350 LEU D CA  1 
ATOM   5927  C C   . LEU B 1 321 ? 25.247  37.689  17.526  1.00 102.22 ? 350 LEU D C   1 
ATOM   5928  O O   . LEU B 1 321 ? 26.309  37.958  18.080  1.00 81.84  ? 350 LEU D O   1 
ATOM   5929  C CB  . LEU B 1 321 ? 24.703  35.767  19.103  1.00 141.83 ? 350 LEU D CB  1 
ATOM   5930  C CG  . LEU B 1 321 ? 23.393  35.678  19.906  1.00 145.15 ? 350 LEU D CG  1 
ATOM   5931  C CD1 . LEU B 1 321 ? 22.224  36.492  19.346  1.00 136.25 ? 350 LEU D CD1 1 
ATOM   5932  C CD2 . LEU B 1 321 ? 22.969  34.226  20.104  1.00 139.26 ? 350 LEU D CD2 1 
ATOM   5933  N N   . ARG B 1 322 ? 24.555  38.551  16.771  1.00 95.23  ? 351 ARG D N   1 
ATOM   5934  C CA  . ARG B 1 322 ? 24.991  39.903  16.454  1.00 99.39  ? 351 ARG D CA  1 
ATOM   5935  C C   . ARG B 1 322 ? 24.907  40.795  17.692  1.00 88.35  ? 351 ARG D C   1 
ATOM   5936  O O   . ARG B 1 322 ? 25.378  41.928  17.671  1.00 86.09  ? 351 ARG D O   1 
ATOM   5937  C CB  . ARG B 1 322 ? 24.101  40.486  15.347  1.00 109.54 ? 351 ARG D CB  1 
ATOM   5938  C CG  . ARG B 1 322 ? 23.968  39.638  14.088  1.00 112.20 ? 351 ARG D CG  1 
ATOM   5939  C CD  . ARG B 1 322 ? 22.730  39.992  13.273  1.00 115.33 ? 351 ARG D CD  1 
ATOM   5940  N NE  . ARG B 1 322 ? 22.887  41.266  12.562  1.00 117.70 ? 351 ARG D NE  1 
ATOM   5941  C CZ  . ARG B 1 322 ? 22.304  42.421  12.874  1.00 108.73 ? 351 ARG D CZ  1 
ATOM   5942  N NH1 . ARG B 1 322 ? 21.527  42.521  13.939  1.00 101.78 ? 351 ARG D NH1 1 
ATOM   5943  N NH2 . ARG B 1 322 ? 22.521  43.486  12.120  1.00 108.13 ? 351 ARG D NH2 1 
ATOM   5944  N N   . LYS B 1 323 ? 24.267  40.291  18.754  1.00 86.60  ? 352 LYS D N   1 
ATOM   5945  C CA  . LYS B 1 323 ? 24.329  40.915  20.065  1.00 82.23  ? 352 LYS D CA  1 
ATOM   5946  C C   . LYS B 1 323 ? 24.700  39.872  21.121  1.00 70.61  ? 352 LYS D C   1 
ATOM   5947  O O   . LYS B 1 323 ? 24.971  38.708  20.822  1.00 61.68  ? 352 LYS D O   1 
ATOM   5948  C CB  . LYS B 1 323 ? 22.991  41.587  20.403  1.00 84.36  ? 352 LYS D CB  1 
ATOM   5949  C CG  . LYS B 1 323 ? 21.823  40.643  20.681  1.00 84.87  ? 352 LYS D CG  1 
ATOM   5950  C CD  . LYS B 1 323 ? 20.646  41.319  21.373  1.00 96.70  ? 352 LYS D CD  1 
ATOM   5951  C CE  . LYS B 1 323 ? 20.223  42.586  20.685  1.00 93.28  ? 352 LYS D CE  1 
ATOM   5952  N NZ  . LYS B 1 323 ? 19.938  42.367  19.264  1.00 91.17  ? 352 LYS D NZ  1 
ATOM   5953  N N   . THR B 1 324 ? 24.709  40.326  22.375  1.00 64.14  ? 353 THR D N   1 
ATOM   5954  C CA  . THR B 1 324 ? 24.806  39.449  23.524  1.00 62.32  ? 353 THR D CA  1 
ATOM   5955  C C   . THR B 1 324 ? 23.579  38.531  23.563  1.00 53.17  ? 353 THR D C   1 
ATOM   5956  O O   . THR B 1 324 ? 22.445  38.988  23.408  1.00 52.04  ? 353 THR D O   1 
ATOM   5957  C CB  . THR B 1 324 ? 24.910  40.309  24.782  1.00 57.39  ? 353 THR D CB  1 
ATOM   5958  O OG1 . THR B 1 324 ? 26.092  41.096  24.612  1.00 59.16  ? 353 THR D OG1 1 
ATOM   5959  C CG2 . THR B 1 324 ? 24.907  39.459  26.042  1.00 52.60  ? 353 THR D CG2 1 
ATOM   5960  N N   . ASP B 1 325 ? 23.847  37.242  23.793  1.00 45.66  ? 354 ASP D N   1 
ATOM   5961  C CA  . ASP B 1 325 ? 22.840  36.243  24.114  1.00 45.06  ? 354 ASP D CA  1 
ATOM   5962  C C   . ASP B 1 325 ? 21.881  36.811  25.160  1.00 42.39  ? 354 ASP D C   1 
ATOM   5963  O O   . ASP B 1 325 ? 22.289  37.253  26.230  1.00 34.20  ? 354 ASP D O   1 
ATOM   5964  C CB  . ASP B 1 325 ? 23.526  34.960  24.534  1.00 46.46  ? 354 ASP D CB  1 
ATOM   5965  C CG  . ASP B 1 325 ? 22.618  33.796  24.892  1.00 56.07  ? 354 ASP D CG  1 
ATOM   5966  O OD1 . ASP B 1 325 ? 21.361  33.969  24.843  1.00 48.00  ? 354 ASP D OD1 1 
ATOM   5967  O OD2 . ASP B 1 325 ? 23.193  32.731  25.221  1.00 51.41  ? 354 ASP D OD2 1 
ATOM   5968  N N   . PRO B 1 326 ? 20.568  36.888  24.865  1.00 43.80  ? 355 PRO D N   1 
ATOM   5969  C CA  . PRO B 1 326 ? 19.606  37.401  25.836  1.00 42.18  ? 355 PRO D CA  1 
ATOM   5970  C C   . PRO B 1 326 ? 19.569  36.520  27.080  1.00 36.50  ? 355 PRO D C   1 
ATOM   5971  O O   . PRO B 1 326 ? 19.117  36.968  28.113  1.00 38.24  ? 355 PRO D O   1 
ATOM   5972  C CB  . PRO B 1 326 ? 18.282  37.379  25.036  1.00 41.04  ? 355 PRO D CB  1 
ATOM   5973  C CG  . PRO B 1 326 ? 18.505  36.248  24.089  1.00 46.54  ? 355 PRO D CG  1 
ATOM   5974  C CD  . PRO B 1 326 ? 19.935  36.459  23.612  1.00 45.58  ? 355 PRO D CD  1 
ATOM   5975  N N   . ARG B 1 327 ? 20.054  35.277  26.983  1.00 40.85  ? 356 ARG D N   1 
ATOM   5976  C CA  . ARG B 1 327 ? 20.136  34.396  28.148  1.00 40.49  ? 356 ARG D CA  1 
ATOM   5977  C C   . ARG B 1 327 ? 21.154  34.941  29.159  1.00 40.19  ? 356 ARG D C   1 
ATOM   5978  O O   . ARG B 1 327 ? 20.955  34.796  30.369  1.00 40.75  ? 356 ARG D O   1 
ATOM   5979  C CB  . ARG B 1 327 ? 20.432  32.951  27.717  1.00 41.17  ? 356 ARG D CB  1 
ATOM   5980  C CG  . ARG B 1 327 ? 19.279  32.343  26.935  1.00 39.67  ? 356 ARG D CG  1 
ATOM   5981  C CD  . ARG B 1 327 ? 19.492  30.918  26.521  1.00 37.40  ? 356 ARG D CD  1 
ATOM   5982  N NE  . ARG B 1 327 ? 20.630  30.845  25.612  1.00 36.15  ? 356 ARG D NE  1 
ATOM   5983  C CZ  . ARG B 1 327 ? 21.319  29.748  25.374  1.00 39.70  ? 356 ARG D CZ  1 
ATOM   5984  N NH1 . ARG B 1 327 ? 20.879  28.581  25.806  1.00 39.34  ? 356 ARG D NH1 1 
ATOM   5985  N NH2 . ARG B 1 327 ? 22.416  29.790  24.642  1.00 41.16  ? 356 ARG D NH2 1 
ATOM   5986  N N   . TYR B 1 328 ? 22.229  35.586  28.665  1.00 36.52  ? 357 TYR D N   1 
ATOM   5987  C CA  . TYR B 1 328 ? 23.205  36.270  29.512  1.00 36.71  ? 357 TYR D CA  1 
ATOM   5988  C C   . TYR B 1 328 ? 22.580  37.484  30.192  1.00 34.79  ? 357 TYR D C   1 
ATOM   5989  O O   . TYR B 1 328 ? 22.706  37.679  31.406  1.00 35.13  ? 357 TYR D O   1 
ATOM   5990  C CB  . TYR B 1 328 ? 24.418  36.725  28.692  1.00 36.56  ? 357 TYR D CB  1 
ATOM   5991  C CG  . TYR B 1 328 ? 25.509  37.438  29.477  1.00 33.04  ? 357 TYR D CG  1 
ATOM   5992  C CD1 . TYR B 1 328 ? 25.443  38.801  29.676  1.00 34.20  ? 357 TYR D CD1 1 
ATOM   5993  C CD2 . TYR B 1 328 ? 26.624  36.761  29.954  1.00 32.91  ? 357 TYR D CD2 1 
ATOM   5994  C CE1 . TYR B 1 328 ? 26.413  39.474  30.393  1.00 33.84  ? 357 TYR D CE1 1 
ATOM   5995  C CE2 . TYR B 1 328 ? 27.643  37.432  30.610  1.00 39.79  ? 357 TYR D CE2 1 
ATOM   5996  C CZ  . TYR B 1 328 ? 27.522  38.795  30.848  1.00 37.42  ? 357 TYR D CZ  1 
ATOM   5997  O OH  . TYR B 1 328 ? 28.459  39.499  31.546  1.00 38.42  ? 357 TYR D OH  1 
ATOM   5998  N N   . THR B 1 329 ? 21.910  38.287  29.365  1.00 35.84  ? 358 THR D N   1 
ATOM   5999  C CA  . THR B 1 329 ? 21.359  39.562  29.767  1.00 37.04  ? 358 THR D CA  1 
ATOM   6000  C C   . THR B 1 329 ? 20.365  39.378  30.910  1.00 40.68  ? 358 THR D C   1 
ATOM   6001  O O   . THR B 1 329 ? 20.382  40.154  31.869  1.00 38.55  ? 358 THR D O   1 
ATOM   6002  C CB  . THR B 1 329 ? 20.744  40.177  28.513  1.00 41.69  ? 358 THR D CB  1 
ATOM   6003  O OG1 . THR B 1 329 ? 21.915  40.289  27.710  1.00 39.99  ? 358 THR D OG1 1 
ATOM   6004  C CG2 . THR B 1 329 ? 20.043  41.505  28.729  1.00 42.18  ? 358 THR D CG2 1 
ATOM   6005  N N   . CYS B 1 330 ? 19.476  38.378  30.822  1.00 39.98  ? 359 CYS D N   1 
ATOM   6006  C CA  . CYS B 1 330 ? 18.493  38.232  31.888  1.00 42.48  ? 359 CYS D CA  1 
ATOM   6007  C C   . CYS B 1 330 ? 19.184  37.774  33.177  1.00 37.51  ? 359 CYS D C   1 
ATOM   6008  O O   . CYS B 1 330 ? 18.714  38.081  34.266  1.00 40.19  ? 359 CYS D O   1 
ATOM   6009  C CB  . CYS B 1 330 ? 17.340  37.332  31.477  1.00 45.80  ? 359 CYS D CB  1 
ATOM   6010  S SG  . CYS B 1 330 ? 17.896  35.628  31.258  1.00 52.79  ? 359 CYS D SG  1 
ATOM   6011  N N   . GLN B 1 331 ? 20.293  37.041  33.071  1.00 35.73  ? 360 GLN D N   1 
ATOM   6012  C CA  . GLN B 1 331 ? 21.036  36.650  34.262  1.00 39.12  ? 360 GLN D CA  1 
ATOM   6013  C C   . GLN B 1 331 ? 21.767  37.855  34.848  1.00 38.70  ? 360 GLN D C   1 
ATOM   6014  O O   . GLN B 1 331 ? 21.912  37.973  36.066  1.00 38.43  ? 360 GLN D O   1 
ATOM   6015  C CB  . GLN B 1 331 ? 22.060  35.569  33.943  1.00 40.63  ? 360 GLN D CB  1 
ATOM   6016  C CG  . GLN B 1 331 ? 21.412  34.226  33.670  1.00 40.53  ? 360 GLN D CG  1 
ATOM   6017  C CD  . GLN B 1 331 ? 22.430  33.154  33.389  1.00 40.66  ? 360 GLN D CD  1 
ATOM   6018  O OE1 . GLN B 1 331 ? 22.925  33.000  32.271  1.00 49.20  ? 360 GLN D OE1 1 
ATOM   6019  N NE2 . GLN B 1 331 ? 22.687  32.349  34.396  1.00 45.56  ? 360 GLN D NE2 1 
ATOM   6020  N N   . ARG B 1 332 ? 22.259  38.718  33.954  1.00 32.96  ? 361 ARG D N   1 
ATOM   6021  C CA  . ARG B 1 332 ? 22.927  39.939  34.349  1.00 35.23  ? 361 ARG D CA  1 
ATOM   6022  C C   . ARG B 1 332 ? 21.952  40.831  35.107  1.00 33.25  ? 361 ARG D C   1 
ATOM   6023  O O   . ARG B 1 332 ? 22.315  41.384  36.131  1.00 33.78  ? 361 ARG D O   1 
ATOM   6024  C CB  . ARG B 1 332 ? 23.558  40.614  33.111  1.00 38.79  ? 361 ARG D CB  1 
ATOM   6025  C CG  . ARG B 1 332 ? 23.919  42.072  33.333  1.00 38.20  ? 361 ARG D CG  1 
ATOM   6026  C CD  . ARG B 1 332 ? 24.622  42.749  32.153  1.00 38.17  ? 361 ARG D CD  1 
ATOM   6027  N NE  . ARG B 1 332 ? 24.794  44.178  32.425  1.00 36.85  ? 361 ARG D NE  1 
ATOM   6028  C CZ  . ARG B 1 332 ? 25.767  44.691  33.175  1.00 45.73  ? 361 ARG D CZ  1 
ATOM   6029  N NH1 . ARG B 1 332 ? 26.730  43.926  33.665  1.00 47.29  ? 361 ARG D NH1 1 
ATOM   6030  N NH2 . ARG B 1 332 ? 25.788  45.985  33.423  1.00 49.84  ? 361 ARG D NH2 1 
ATOM   6031  N N   . GLU B 1 333 ? 20.741  41.003  34.589  1.00 35.98  ? 362 GLU D N   1 
ATOM   6032  C CA  . GLU B 1 333 ? 19.782  41.924  35.182  1.00 40.47  ? 362 GLU D CA  1 
ATOM   6033  C C   . GLU B 1 333 ? 19.363  41.355  36.538  1.00 43.15  ? 362 GLU D C   1 
ATOM   6034  O O   . GLU B 1 333 ? 19.103  42.080  37.525  1.00 36.12  ? 362 GLU D O   1 
ATOM   6035  C CB  . GLU B 1 333 ? 18.540  42.075  34.296  1.00 48.32  ? 362 GLU D CB  1 
ATOM   6036  C CG  . GLU B 1 333 ? 18.777  42.845  32.993  1.00 61.00  ? 362 GLU D CG  1 
ATOM   6037  C CD  . GLU B 1 333 ? 17.801  42.630  31.826  1.00 71.93  ? 362 GLU D CD  1 
ATOM   6038  O OE1 . GLU B 1 333 ? 16.938  41.702  31.870  1.00 67.19  ? 362 GLU D OE1 1 
ATOM   6039  O OE2 . GLU B 1 333 ? 17.915  43.414  30.838  1.00 67.44  ? 362 GLU D OE2 1 
ATOM   6040  N N   . PHE B 1 334 ? 19.270  40.024  36.574  1.00 31.67  ? 363 PHE D N   1 
ATOM   6041  C CA  . PHE B 1 334 ? 18.959  39.379  37.837  1.00 35.11  ? 363 PHE D CA  1 
ATOM   6042  C C   . PHE B 1 334 ? 20.045  39.749  38.855  1.00 36.25  ? 363 PHE D C   1 
ATOM   6043  O O   . PHE B 1 334 ? 19.728  40.199  39.968  1.00 32.38  ? 363 PHE D O   1 
ATOM   6044  C CB  . PHE B 1 334 ? 18.805  37.884  37.627  1.00 32.21  ? 363 PHE D CB  1 
ATOM   6045  C CG  . PHE B 1 334 ? 18.464  37.173  38.920  1.00 30.56  ? 363 PHE D CG  1 
ATOM   6046  C CD1 . PHE B 1 334 ? 19.459  36.867  39.841  1.00 34.07  ? 363 PHE D CD1 1 
ATOM   6047  C CD2 . PHE B 1 334 ? 17.159  36.797  39.186  1.00 34.33  ? 363 PHE D CD2 1 
ATOM   6048  C CE1 . PHE B 1 334 ? 19.152  36.212  41.024  1.00 36.42  ? 363 PHE D CE1 1 
ATOM   6049  C CE2 . PHE B 1 334 ? 16.857  36.134  40.370  1.00 35.79  ? 363 PHE D CE2 1 
ATOM   6050  C CZ  . PHE B 1 334 ? 17.852  35.836  41.280  1.00 33.13  ? 363 PHE D CZ  1 
ATOM   6051  N N   . ALA B 1 335 ? 21.315  39.581  38.453  1.00 36.13  ? 364 ALA D N   1 
ATOM   6052  C CA  . ALA B 1 335 ? 22.448  39.838  39.336  1.00 42.07  ? 364 ALA D CA  1 
ATOM   6053  C C   . ALA B 1 335 ? 22.473  41.310  39.792  1.00 43.27  ? 364 ALA D C   1 
ATOM   6054  O O   . ALA B 1 335 ? 22.771  41.603  40.955  1.00 37.58  ? 364 ALA D O   1 
ATOM   6055  C CB  . ALA B 1 335 ? 23.739  39.442  38.664  1.00 39.75  ? 364 ALA D CB  1 
ATOM   6056  N N   . LEU B 1 336 ? 22.192  42.231  38.864  1.00 38.03  ? 365 LEU D N   1 
ATOM   6057  C CA  . LEU B 1 336 ? 22.236  43.655  39.150  1.00 39.00  ? 365 LEU D CA  1 
ATOM   6058  C C   . LEU B 1 336 ? 21.232  43.978  40.257  1.00 41.19  ? 365 LEU D C   1 
ATOM   6059  O O   . LEU B 1 336 ? 21.504  44.790  41.146  1.00 41.71  ? 365 LEU D O   1 
ATOM   6060  C CB  . LEU B 1 336 ? 21.968  44.468  37.881  1.00 38.43  ? 365 LEU D CB  1 
ATOM   6061  C CG  . LEU B 1 336 ? 23.162  44.653  36.930  1.00 43.35  ? 365 LEU D CG  1 
ATOM   6062  C CD1 . LEU B 1 336 ? 22.785  45.367  35.618  1.00 40.24  ? 365 LEU D CD1 1 
ATOM   6063  C CD2 . LEU B 1 336 ? 24.300  45.426  37.617  1.00 48.45  ? 365 LEU D CD2 1 
ATOM   6064  N N   . LYS B 1 337 ? 20.085  43.304  40.230  1.00 35.15  ? 366 LYS D N   1 
ATOM   6065  C CA  . LYS B 1 337 ? 19.026  43.592  41.172  1.00 43.15  ? 366 LYS D CA  1 
ATOM   6066  C C   . LYS B 1 337 ? 19.343  42.979  42.540  1.00 41.41  ? 366 LYS D C   1 
ATOM   6067  O O   . LYS B 1 337 ? 19.124  43.620  43.566  1.00 40.54  ? 366 LYS D O   1 
ATOM   6068  C CB  . LYS B 1 337 ? 17.708  43.132  40.537  1.00 51.54  ? 366 LYS D CB  1 
ATOM   6069  C CG  . LYS B 1 337 ? 16.469  43.759  41.140  1.00 69.02  ? 366 LYS D CG  1 
ATOM   6070  C CD  . LYS B 1 337 ? 15.174  43.078  40.710  1.00 82.17  ? 366 LYS D CD  1 
ATOM   6071  C CE  . LYS B 1 337 ? 14.011  43.430  41.594  1.00 92.01  ? 366 LYS D CE  1 
ATOM   6072  N NZ  . LYS B 1 337 ? 12.849  42.537  41.474  1.00 94.73  ? 366 LYS D NZ  1 
ATOM   6073  N N   . HIS B 1 338 ? 19.880  41.756  42.584  1.00 36.59  ? 367 HIS D N   1 
ATOM   6074  C CA  . HIS B 1 338 ? 19.791  40.998  43.823  1.00 38.66  ? 367 HIS D CA  1 
ATOM   6075  C C   . HIS B 1 338 ? 21.143  40.746  44.470  1.00 35.33  ? 367 HIS D C   1 
ATOM   6076  O O   . HIS B 1 338 ? 21.178  40.415  45.655  1.00 35.45  ? 367 HIS D O   1 
ATOM   6077  C CB  . HIS B 1 338 ? 19.101  39.645  43.639  1.00 39.25  ? 367 HIS D CB  1 
ATOM   6078  C CG  . HIS B 1 338 ? 17.714  39.730  43.153  1.00 40.50  ? 367 HIS D CG  1 
ATOM   6079  N ND1 . HIS B 1 338 ? 16.695  40.237  43.921  1.00 44.82  ? 367 HIS D ND1 1 
ATOM   6080  C CD2 . HIS B 1 338 ? 17.169  39.365  41.973  1.00 41.82  ? 367 HIS D CD2 1 
ATOM   6081  C CE1 . HIS B 1 338 ? 15.576  40.194  43.222  1.00 42.21  ? 367 HIS D CE1 1 
ATOM   6082  N NE2 . HIS B 1 338 ? 15.852  39.667  42.034  1.00 42.89  ? 367 HIS D NE2 1 
ATOM   6083  N N   . LEU B 1 339 ? 22.237  40.859  43.710  1.00 33.68  ? 368 LEU D N   1 
ATOM   6084  C CA  . LEU B 1 339 ? 23.560  40.613  44.267  1.00 34.17  ? 368 LEU D CA  1 
ATOM   6085  C C   . LEU B 1 339 ? 24.559  41.583  43.656  1.00 34.83  ? 368 LEU D C   1 
ATOM   6086  O O   . LEU B 1 339 ? 25.626  41.178  43.229  1.00 37.05  ? 368 LEU D O   1 
ATOM   6087  C CB  . LEU B 1 339 ? 24.046  39.180  44.067  1.00 38.97  ? 368 LEU D CB  1 
ATOM   6088  C CG  . LEU B 1 339 ? 23.943  38.634  42.642  1.00 36.79  ? 368 LEU D CG  1 
ATOM   6089  C CD1 . LEU B 1 339 ? 25.145  37.858  42.249  1.00 36.74  ? 368 LEU D CD1 1 
ATOM   6090  C CD2 . LEU B 1 339 ? 22.696  37.762  42.573  1.00 40.16  ? 368 LEU D CD2 1 
ATOM   6091  N N   . PRO B 1 340 ? 24.263  42.898  43.620  1.00 34.22  ? 369 PRO D N   1 
ATOM   6092  C CA  . PRO B 1 340 ? 25.212  43.839  43.041  1.00 31.02  ? 369 PRO D CA  1 
ATOM   6093  C C   . PRO B 1 340 ? 26.541  43.960  43.815  1.00 33.87  ? 369 PRO D C   1 
ATOM   6094  O O   . PRO B 1 340 ? 27.553  44.361  43.251  1.00 38.74  ? 369 PRO D O   1 
ATOM   6095  C CB  . PRO B 1 340 ? 24.361  45.126  43.002  1.00 33.65  ? 369 PRO D CB  1 
ATOM   6096  C CG  . PRO B 1 340 ? 23.369  45.012  44.167  1.00 33.82  ? 369 PRO D CG  1 
ATOM   6097  C CD  . PRO B 1 340 ? 23.059  43.530  44.204  1.00 36.15  ? 369 PRO D CD  1 
ATOM   6098  N N   . ASN B 1 341 ? 26.592  43.566  45.102  1.00 41.24  ? 370 ASN D N   1 
ATOM   6099  C CA  . ASN B 1 341 ? 27.810  43.736  45.898  1.00 41.41  ? 370 ASN D CA  1 
ATOM   6100  C C   . ASN B 1 341 ? 28.728  42.514  45.780  1.00 36.56  ? 370 ASN D C   1 
ATOM   6101  O O   . ASN B 1 341 ? 29.857  42.546  46.242  1.00 35.58  ? 370 ASN D O   1 
ATOM   6102  C CB  . ASN B 1 341 ? 27.512  44.043  47.367  1.00 36.69  ? 370 ASN D CB  1 
ATOM   6103  C CG  . ASN B 1 341 ? 26.803  45.381  47.518  1.00 38.69  ? 370 ASN D CG  1 
ATOM   6104  O OD1 . ASN B 1 341 ? 25.629  45.454  47.927  1.00 37.98  ? 370 ASN D OD1 1 
ATOM   6105  N ND2 . ASN B 1 341 ? 27.473  46.451  47.115  1.00 40.73  ? 370 ASN D ND2 1 
ATOM   6106  N N   . ASP B 1 342 ? 28.249  41.447  45.168  1.00 32.97  ? 371 ASP D N   1 
ATOM   6107  C CA  . ASP B 1 342 ? 29.022  40.211  45.126  1.00 35.08  ? 371 ASP D CA  1 
ATOM   6108  C C   . ASP B 1 342 ? 30.308  40.460  44.343  1.00 33.55  ? 371 ASP D C   1 
ATOM   6109  O O   . ASP B 1 342 ? 30.233  40.945  43.218  1.00 34.34  ? 371 ASP D O   1 
ATOM   6110  C CB  . ASP B 1 342 ? 28.262  39.051  44.503  1.00 35.25  ? 371 ASP D CB  1 
ATOM   6111  C CG  . ASP B 1 342 ? 29.093  37.773  44.347  1.00 40.84  ? 371 ASP D CG  1 
ATOM   6112  O OD1 . ASP B 1 342 ? 29.488  37.181  45.399  1.00 37.70  ? 371 ASP D OD1 1 
ATOM   6113  O OD2 . ASP B 1 342 ? 29.399  37.402  43.184  1.00 39.20  ? 371 ASP D OD2 1 
ATOM   6114  N N   . PRO B 1 343 ? 31.506  40.207  44.925  1.00 36.22  ? 372 PRO D N   1 
ATOM   6115  C CA  . PRO B 1 343 ? 32.780  40.343  44.186  1.00 41.74  ? 372 PRO D CA  1 
ATOM   6116  C C   . PRO B 1 343 ? 32.903  39.630  42.830  1.00 39.45  ? 372 PRO D C   1 
ATOM   6117  O O   . PRO B 1 343 ? 33.359  40.241  41.863  1.00 37.51  ? 372 PRO D O   1 
ATOM   6118  C CB  . PRO B 1 343 ? 33.806  39.806  45.191  1.00 42.30  ? 372 PRO D CB  1 
ATOM   6119  C CG  . PRO B 1 343 ? 33.172  40.090  46.543  1.00 42.92  ? 372 PRO D CG  1 
ATOM   6120  C CD  . PRO B 1 343 ? 31.690  39.854  46.339  1.00 39.36  ? 372 PRO D CD  1 
ATOM   6121  N N   . MET B 1 344 ? 32.489  38.345  42.738  1.00 44.97  ? 373 MET D N   1 
ATOM   6122  C CA  . MET B 1 344 ? 32.645  37.572  41.499  1.00 38.10  ? 373 MET D CA  1 
ATOM   6123  C C   . MET B 1 344 ? 31.655  38.038  40.442  1.00 34.98  ? 373 MET D C   1 
ATOM   6124  O O   . MET B 1 344 ? 32.002  38.101  39.259  1.00 33.29  ? 373 MET D O   1 
ATOM   6125  C CB  . MET B 1 344 ? 32.471  36.063  41.679  1.00 36.66  ? 373 MET D CB  1 
ATOM   6126  C CG  . MET B 1 344 ? 33.618  35.398  42.417  1.00 44.19  ? 373 MET D CG  1 
ATOM   6127  S SD  . MET B 1 344 ? 35.082  35.047  41.419  1.00 49.69  ? 373 MET D SD  1 
ATOM   6128  C CE  . MET B 1 344 ? 34.358  33.795  40.350  1.00 46.50  ? 373 MET D CE  1 
ATOM   6129  N N   . PHE B 1 345 ? 30.433  38.385  40.869  1.00 35.34  ? 374 PHE D N   1 
ATOM   6130  C CA  . PHE B 1 345 ? 29.511  39.045  39.961  1.00 38.70  ? 374 PHE D CA  1 
ATOM   6131  C C   . PHE B 1 345 ? 30.166  40.308  39.388  1.00 42.27  ? 374 PHE D C   1 
ATOM   6132  O O   . PHE B 1 345 ? 30.013  40.610  38.200  1.00 37.40  ? 374 PHE D O   1 
ATOM   6133  C CB  . PHE B 1 345 ? 28.182  39.471  40.597  1.00 34.21  ? 374 PHE D CB  1 
ATOM   6134  C CG  . PHE B 1 345 ? 27.377  40.363  39.663  1.00 34.69  ? 374 PHE D CG  1 
ATOM   6135  C CD1 . PHE B 1 345 ? 27.184  40.009  38.329  1.00 37.20  ? 374 PHE D CD1 1 
ATOM   6136  C CD2 . PHE B 1 345 ? 26.866  41.584  40.100  1.00 38.83  ? 374 PHE D CD2 1 
ATOM   6137  C CE1 . PHE B 1 345 ? 26.487  40.850  37.465  1.00 40.70  ? 374 PHE D CE1 1 
ATOM   6138  C CE2 . PHE B 1 345 ? 26.195  42.434  39.230  1.00 40.81  ? 374 PHE D CE2 1 
ATOM   6139  C CZ  . PHE B 1 345 ? 25.993  42.056  37.909  1.00 42.07  ? 374 PHE D CZ  1 
ATOM   6140  N N   . LYS B 1 346 ? 30.830  41.092  40.259  1.00 42.29  ? 375 LYS D N   1 
ATOM   6141  C CA  . LYS B 1 346 ? 31.438  42.357  39.838  1.00 46.57  ? 375 LYS D CA  1 
ATOM   6142  C C   . LYS B 1 346 ? 32.528  42.097  38.794  1.00 34.55  ? 375 LYS D C   1 
ATOM   6143  O O   . LYS B 1 346 ? 32.737  42.893  37.894  1.00 38.29  ? 375 LYS D O   1 
ATOM   6144  C CB  . LYS B 1 346 ? 31.896  43.214  41.027  1.00 48.11  ? 375 LYS D CB  1 
ATOM   6145  C CG  . LYS B 1 346 ? 30.726  43.932  41.756  1.00 54.68  ? 375 LYS D CG  1 
ATOM   6146  C CD  . LYS B 1 346 ? 31.140  44.671  43.028  1.00 60.03  ? 375 LYS D CD  1 
ATOM   6147  C CE  . LYS B 1 346 ? 31.863  45.945  42.745  1.00 61.40  ? 375 LYS D CE  1 
ATOM   6148  N NZ  . LYS B 1 346 ? 32.327  46.589  43.976  1.00 65.61  ? 375 LYS D NZ  1 
ATOM   6149  N N   . LEU B 1 347 ? 33.216  40.970  38.912  1.00 34.65  ? 376 LEU D N   1 
ATOM   6150  C CA  . LEU B 1 347 ? 34.237  40.617  37.939  1.00 33.16  ? 376 LEU D CA  1 
ATOM   6151  C C   . LEU B 1 347 ? 33.581  40.257  36.605  1.00 36.15  ? 376 LEU D C   1 
ATOM   6152  O O   . LEU B 1 347 ? 34.000  40.746  35.557  1.00 30.53  ? 376 LEU D O   1 
ATOM   6153  C CB  . LEU B 1 347 ? 35.068  39.483  38.495  1.00 32.84  ? 376 LEU D CB  1 
ATOM   6154  C CG  . LEU B 1 347 ? 36.018  38.849  37.482  1.00 35.40  ? 376 LEU D CG  1 
ATOM   6155  C CD1 . LEU B 1 347 ? 36.981  39.867  36.922  1.00 33.77  ? 376 LEU D CD1 1 
ATOM   6156  C CD2 . LEU B 1 347 ? 36.737  37.747  38.209  1.00 36.50  ? 376 LEU D CD2 1 
ATOM   6157  N N   . VAL B 1 348 ? 32.463  39.522  36.683  1.00 33.60  ? 377 VAL D N   1 
ATOM   6158  C CA  . VAL B 1 348 ? 31.714  39.162  35.499  1.00 35.63  ? 377 VAL D CA  1 
ATOM   6159  C C   . VAL B 1 348 ? 31.245  40.417  34.764  1.00 35.08  ? 377 VAL D C   1 
ATOM   6160  O O   . VAL B 1 348 ? 31.466  40.499  33.559  1.00 34.81  ? 377 VAL D O   1 
ATOM   6161  C CB  . VAL B 1 348 ? 30.564  38.197  35.869  1.00 39.33  ? 377 VAL D CB  1 
ATOM   6162  C CG1 . VAL B 1 348 ? 29.474  38.142  34.802  1.00 42.52  ? 377 VAL D CG1 1 
ATOM   6163  C CG2 . VAL B 1 348 ? 31.091  36.789  36.144  1.00 39.40  ? 377 VAL D CG2 1 
ATOM   6164  N N   . ALA B 1 349 ? 30.642  41.404  35.468  1.00 34.72  ? 378 ALA D N   1 
ATOM   6165  C CA  . ALA B 1 349 ? 30.110  42.599  34.809  1.00 39.42  ? 378 ALA D CA  1 
ATOM   6166  C C   . ALA B 1 349 ? 31.253  43.457  34.248  1.00 41.68  ? 378 ALA D C   1 
ATOM   6167  O O   . ALA B 1 349 ? 31.061  44.203  33.287  1.00 38.11  ? 378 ALA D O   1 
ATOM   6168  C CB  . ALA B 1 349 ? 29.194  43.413  35.734  1.00 36.90  ? 378 ALA D CB  1 
ATOM   6169  N N   . GLN B 1 350 ? 32.455  43.317  34.825  1.00 42.79  ? 379 GLN D N   1 
ATOM   6170  C CA  . GLN B 1 350 ? 33.606  44.123  34.434  1.00 43.89  ? 379 GLN D CA  1 
ATOM   6171  C C   . GLN B 1 350 ? 34.195  43.583  33.131  1.00 45.87  ? 379 GLN D C   1 
ATOM   6172  O O   . GLN B 1 350 ? 34.540  44.334  32.206  1.00 43.10  ? 379 GLN D O   1 
ATOM   6173  C CB  . GLN B 1 350 ? 34.613  44.068  35.580  1.00 44.51  ? 379 GLN D CB  1 
ATOM   6174  C CG  . GLN B 1 350 ? 35.550  45.260  35.695  1.00 50.69  ? 379 GLN D CG  1 
ATOM   6175  C CD  . GLN B 1 350 ? 36.541  45.144  36.835  1.00 53.52  ? 379 GLN D CD  1 
ATOM   6176  O OE1 . GLN B 1 350 ? 36.557  44.175  37.614  1.00 51.93  ? 379 GLN D OE1 1 
ATOM   6177  N NE2 . GLN B 1 350 ? 37.404  46.144  36.921  1.00 53.23  ? 379 GLN D NE2 1 
ATOM   6178  N N   . LEU B 1 351 ? 34.325  42.263  33.071  1.00 39.98  ? 380 LEU D N   1 
ATOM   6179  C CA  . LEU B 1 351 ? 34.652  41.600  31.825  1.00 40.03  ? 380 LEU D CA  1 
ATOM   6180  C C   . LEU B 1 351 ? 33.638  41.939  30.738  1.00 39.52  ? 380 LEU D C   1 
ATOM   6181  O O   . LEU B 1 351 ? 34.000  42.182  29.603  1.00 39.11  ? 380 LEU D O   1 
ATOM   6182  C CB  . LEU B 1 351 ? 34.654  40.110  32.112  1.00 47.07  ? 380 LEU D CB  1 
ATOM   6183  C CG  . LEU B 1 351 ? 35.813  39.607  32.967  1.00 46.40  ? 380 LEU D CG  1 
ATOM   6184  C CD1 . LEU B 1 351 ? 35.478  38.218  33.445  1.00 47.48  ? 380 LEU D CD1 1 
ATOM   6185  C CD2 . LEU B 1 351 ? 37.102  39.619  32.159  1.00 51.04  ? 380 LEU D CD2 1 
ATOM   6186  N N   . TYR B 1 352 ? 32.353  41.940  31.071  1.00 41.24  ? 381 TYR D N   1 
ATOM   6187  C CA  . TYR B 1 352 ? 31.340  42.258  30.079  1.00 48.56  ? 381 TYR D CA  1 
ATOM   6188  C C   . TYR B 1 352 ? 31.664  43.582  29.382  1.00 48.20  ? 381 TYR D C   1 
ATOM   6189  O O   . TYR B 1 352 ? 31.431  43.681  28.186  1.00 40.64  ? 381 TYR D O   1 
ATOM   6190  C CB  . TYR B 1 352 ? 29.924  42.408  30.650  1.00 52.51  ? 381 TYR D CB  1 
ATOM   6191  C CG  . TYR B 1 352 ? 28.803  42.571  29.630  1.00 52.26  ? 381 TYR D CG  1 
ATOM   6192  C CD1 . TYR B 1 352 ? 28.835  41.894  28.410  1.00 48.87  ? 381 TYR D CD1 1 
ATOM   6193  C CD2 . TYR B 1 352 ? 27.708  43.390  29.900  1.00 51.43  ? 381 TYR D CD2 1 
ATOM   6194  C CE1 . TYR B 1 352 ? 27.817  42.036  27.485  1.00 49.19  ? 381 TYR D CE1 1 
ATOM   6195  C CE2 . TYR B 1 352 ? 26.672  43.520  28.988  1.00 55.12  ? 381 TYR D CE2 1 
ATOM   6196  C CZ  . TYR B 1 352 ? 26.729  42.833  27.784  1.00 47.98  ? 381 TYR D CZ  1 
ATOM   6197  O OH  . TYR B 1 352 ? 25.724  42.930  26.882  1.00 52.15  ? 381 TYR D OH  1 
ATOM   6198  N N   . LYS B 1 353 ? 32.144  44.598  30.124  1.00 50.11  ? 382 LYS D N   1 
ATOM   6199  C CA  . LYS B 1 353 ? 32.317  45.939  29.567  1.00 55.70  ? 382 LYS D CA  1 
ATOM   6200  C C   . LYS B 1 353 ? 33.655  46.072  28.824  1.00 46.44  ? 382 LYS D C   1 
ATOM   6201  O O   . LYS B 1 353 ? 33.833  47.017  28.070  1.00 45.53  ? 382 LYS D O   1 
ATOM   6202  C CB  . LYS B 1 353 ? 32.080  47.026  30.630  1.00 64.33  ? 382 LYS D CB  1 
ATOM   6203  C CG  . LYS B 1 353 ? 33.298  47.649  31.314  1.00 68.47  ? 382 LYS D CG  1 
ATOM   6204  C CD  . LYS B 1 353 ? 32.962  48.525  32.520  1.00 73.19  ? 382 LYS D CD  1 
ATOM   6205  C CE  . LYS B 1 353 ? 32.836  49.985  32.217  1.00 72.40  ? 382 LYS D CE  1 
ATOM   6206  N NZ  . LYS B 1 353 ? 34.155  50.622  32.139  1.00 65.54  ? 382 LYS D NZ  1 
ATOM   6207  N N   . ILE B 1 354 ? 34.551  45.091  28.980  1.00 43.48  ? 383 ILE D N   1 
ATOM   6208  C CA  . ILE B 1 354 ? 35.941  45.175  28.556  1.00 44.36  ? 383 ILE D CA  1 
ATOM   6209  C C   . ILE B 1 354 ? 36.242  44.184  27.431  1.00 45.73  ? 383 ILE D C   1 
ATOM   6210  O O   . ILE B 1 354 ? 36.963  44.500  26.491  1.00 44.56  ? 383 ILE D O   1 
ATOM   6211  C CB  . ILE B 1 354 ? 36.856  44.885  29.759  1.00 47.14  ? 383 ILE D CB  1 
ATOM   6212  C CG1 . ILE B 1 354 ? 36.898  46.069  30.699  1.00 49.10  ? 383 ILE D CG1 1 
ATOM   6213  C CG2 . ILE B 1 354 ? 38.251  44.442  29.306  1.00 47.88  ? 383 ILE D CG2 1 
ATOM   6214  C CD1 . ILE B 1 354 ? 37.781  45.834  31.906  1.00 54.79  ? 383 ILE D CD1 1 
ATOM   6215  N N   . VAL B 1 355 ? 35.735  42.956  27.567  1.00 42.30  ? 384 VAL D N   1 
ATOM   6216  C CA  . VAL B 1 355 ? 36.140  41.862  26.705  1.00 43.74  ? 384 VAL D CA  1 
ATOM   6217  C C   . VAL B 1 355 ? 35.637  42.053  25.264  1.00 48.01  ? 384 VAL D C   1 
ATOM   6218  O O   . VAL B 1 355 ? 36.395  41.754  24.335  1.00 46.88  ? 384 VAL D O   1 
ATOM   6219  C CB  . VAL B 1 355 ? 35.670  40.538  27.329  1.00 40.34  ? 384 VAL D CB  1 
ATOM   6220  C CG1 . VAL B 1 355 ? 35.892  39.351  26.391  1.00 42.70  ? 384 VAL D CG1 1 
ATOM   6221  C CG2 . VAL B 1 355 ? 36.341  40.287  28.687  1.00 41.46  ? 384 VAL D CG2 1 
ATOM   6222  N N   . PRO B 1 356 ? 34.358  42.463  25.013  1.00 45.44  ? 385 PRO D N   1 
ATOM   6223  C CA  . PRO B 1 356 ? 33.846  42.604  23.646  1.00 45.53  ? 385 PRO D CA  1 
ATOM   6224  C C   . PRO B 1 356 ? 34.778  43.454  22.778  1.00 56.75  ? 385 PRO D C   1 
ATOM   6225  O O   . PRO B 1 356 ? 35.153  43.058  21.667  1.00 53.03  ? 385 PRO D O   1 
ATOM   6226  C CB  . PRO B 1 356 ? 32.466  43.265  23.842  1.00 45.66  ? 385 PRO D CB  1 
ATOM   6227  C CG  . PRO B 1 356 ? 32.024  42.786  25.208  1.00 44.73  ? 385 PRO D CG  1 
ATOM   6228  C CD  . PRO B 1 356 ? 33.320  42.775  26.015  1.00 42.21  ? 385 PRO D CD  1 
ATOM   6229  N N   . ASN B 1 357 ? 35.178  44.611  23.324  1.00 54.77  ? 386 ASN D N   1 
ATOM   6230  C CA  . ASN B 1 357 ? 36.040  45.543  22.613  1.00 58.64  ? 386 ASN D CA  1 
ATOM   6231  C C   . ASN B 1 357 ? 37.382  44.883  22.303  1.00 52.49  ? 386 ASN D C   1 
ATOM   6232  O O   . ASN B 1 357 ? 37.811  44.887  21.154  1.00 54.62  ? 386 ASN D O   1 
ATOM   6233  C CB  . ASN B 1 357 ? 36.142  46.889  23.322  1.00 58.42  ? 386 ASN D CB  1 
ATOM   6234  C CG  . ASN B 1 357 ? 35.345  47.949  22.597  1.00 67.00  ? 386 ASN D CG  1 
ATOM   6235  O OD1 . ASN B 1 357 ? 35.912  48.950  22.133  1.00 77.74  ? 386 ASN D OD1 1 
ATOM   6236  N ND2 . ASN B 1 357 ? 34.054  47.720  22.426  1.00 69.88  ? 386 ASN D ND2 1 
ATOM   6237  N N   . VAL B 1 358 ? 38.029  44.283  23.299  1.00 44.47  ? 387 VAL D N   1 
ATOM   6238  C CA  . VAL B 1 358 ? 39.294  43.624  23.044  1.00 45.90  ? 387 VAL D CA  1 
ATOM   6239  C C   . VAL B 1 358 ? 39.141  42.560  21.947  1.00 55.11  ? 387 VAL D C   1 
ATOM   6240  O O   . VAL B 1 358 ? 40.030  42.404  21.120  1.00 56.51  ? 387 VAL D O   1 
ATOM   6241  C CB  . VAL B 1 358 ? 39.878  43.047  24.339  1.00 48.17  ? 387 VAL D CB  1 
ATOM   6242  C CG1 . VAL B 1 358 ? 41.135  42.221  24.068  1.00 46.46  ? 387 VAL D CG1 1 
ATOM   6243  C CG2 . VAL B 1 358 ? 40.148  44.146  25.364  1.00 45.21  ? 387 VAL D CG2 1 
ATOM   6244  N N   . LEU B 1 359 ? 38.029  41.815  21.921  1.00 57.59  ? 388 LEU D N   1 
ATOM   6245  C CA  . LEU B 1 359 ? 37.827  40.774  20.918  1.00 55.44  ? 388 LEU D CA  1 
ATOM   6246  C C   . LEU B 1 359 ? 37.638  41.357  19.513  1.00 52.22  ? 388 LEU D C   1 
ATOM   6247  O O   . LEU B 1 359 ? 38.023  40.715  18.542  1.00 46.77  ? 388 LEU D O   1 
ATOM   6248  C CB  . LEU B 1 359 ? 36.637  39.891  21.297  1.00 51.07  ? 388 LEU D CB  1 
ATOM   6249  C CG  . LEU B 1 359 ? 36.928  38.820  22.349  1.00 52.35  ? 388 LEU D CG  1 
ATOM   6250  C CD1 . LEU B 1 359 ? 35.632  38.138  22.756  1.00 54.52  ? 388 LEU D CD1 1 
ATOM   6251  C CD2 . LEU B 1 359 ? 37.927  37.792  21.842  1.00 51.83  ? 388 LEU D CD2 1 
ATOM   6252  N N   . LEU B 1 360 ? 36.975  42.518  19.409  1.00 55.08  ? 389 LEU D N   1 
ATOM   6253  C CA  . LEU B 1 360 ? 36.813  43.221  18.143  1.00 61.51  ? 389 LEU D CA  1 
ATOM   6254  C C   . LEU B 1 360 ? 38.164  43.724  17.607  1.00 69.73  ? 389 LEU D C   1 
ATOM   6255  O O   . LEU B 1 360 ? 38.401  43.641  16.396  1.00 62.36  ? 389 LEU D O   1 
ATOM   6256  C CB  . LEU B 1 360 ? 35.817  44.368  18.305  1.00 59.03  ? 389 LEU D CB  1 
ATOM   6257  C CG  . LEU B 1 360 ? 34.376  43.957  18.599  1.00 60.28  ? 389 LEU D CG  1 
ATOM   6258  C CD1 . LEU B 1 360 ? 33.543  45.205  18.826  1.00 62.44  ? 389 LEU D CD1 1 
ATOM   6259  C CD2 . LEU B 1 360 ? 33.810  43.092  17.466  1.00 63.35  ? 389 LEU D CD2 1 
ATOM   6260  N N   . GLU B 1 361 ? 39.035  44.248  18.493  1.00 66.65  ? 390 GLU D N   1 
ATOM   6261  C CA  . GLU B 1 361 ? 40.357  44.739  18.103  1.00 76.55  ? 390 GLU D CA  1 
ATOM   6262  C C   . GLU B 1 361 ? 41.159  43.608  17.460  1.00 71.69  ? 390 GLU D C   1 
ATOM   6263  O O   . GLU B 1 361 ? 41.843  43.836  16.466  1.00 70.44  ? 390 GLU D O   1 
ATOM   6264  C CB  . GLU B 1 361 ? 41.293  45.280  19.195  1.00 82.43  ? 390 GLU D CB  1 
ATOM   6265  C CG  . GLU B 1 361 ? 40.666  46.230  20.216  1.00 100.86 ? 390 GLU D CG  1 
ATOM   6266  C CD  . GLU B 1 361 ? 39.897  47.414  19.664  1.00 116.29 ? 390 GLU D CD  1 
ATOM   6267  O OE1 . GLU B 1 361 ? 40.582  48.322  19.155  1.00 143.85 ? 390 GLU D OE1 1 
ATOM   6268  O OE2 . GLU B 1 361 ? 38.646  47.440  19.739  1.00 113.35 ? 390 GLU D OE2 1 
ATOM   6269  N N   . GLN B 1 362 ? 41.066  42.423  18.061  1.00 69.44  ? 391 GLN D N   1 
ATOM   6270  C CA  . GLN B 1 362 ? 41.838  41.259  17.579  1.00 69.45  ? 391 GLN D CA  1 
ATOM   6271  C C   . GLN B 1 362 ? 41.179  40.672  16.343  1.00 69.55  ? 391 GLN D C   1 
ATOM   6272  O O   . GLN B 1 362 ? 39.957  40.811  16.192  1.00 66.93  ? 391 GLN D O   1 
ATOM   6273  C CB  . GLN B 1 362 ? 41.799  40.160  18.636  1.00 77.50  ? 391 GLN D CB  1 
ATOM   6274  C CG  . GLN B 1 362 ? 42.909  39.122  18.518  1.00 77.95  ? 391 GLN D CG  1 
ATOM   6275  C CD  . GLN B 1 362 ? 42.591  37.821  19.222  1.00 76.54  ? 391 GLN D CD  1 
ATOM   6276  O OE1 . GLN B 1 362 ? 41.463  37.583  19.665  1.00 68.22  ? 391 GLN D OE1 1 
ATOM   6277  N NE2 . GLN B 1 362 ? 43.592  36.962  19.338  1.00 72.11  ? 391 GLN D NE2 1 
ATOM   6278  N N   . GLY B 1 363 ? 41.978  40.050  15.488  1.00 80.23  ? 392 GLY D N   1 
ATOM   6279  C CA  . GLY B 1 363 ? 41.383  39.343  14.349  1.00 89.99  ? 392 GLY D CA  1 
ATOM   6280  C C   . GLY B 1 363 ? 40.756  38.081  14.891  1.00 91.73  ? 392 GLY D C   1 
ATOM   6281  O O   . GLY B 1 363 ? 41.505  37.135  15.193  1.00 93.10  ? 392 GLY D O   1 
ATOM   6282  N N   . LYS B 1 364 ? 39.439  38.068  15.033  1.00 88.37  ? 393 LYS D N   1 
ATOM   6283  C CA  . LYS B 1 364 ? 38.777  36.914  15.671  1.00 95.88  ? 393 LYS D CA  1 
ATOM   6284  C C   . LYS B 1 364 ? 37.360  36.793  15.117  1.00 107.42 ? 393 LYS D C   1 
ATOM   6285  O O   . LYS B 1 364 ? 37.184  36.921  13.883  1.00 97.50  ? 393 LYS D O   1 
ATOM   6286  C CB  . LYS B 1 364 ? 38.674  37.226  17.165  1.00 101.41 ? 393 LYS D CB  1 
ATOM   6287  C CG  . LYS B 1 364 ? 38.967  36.057  18.092  1.00 114.52 ? 393 LYS D CG  1 
ATOM   6288  C CD  . LYS B 1 364 ? 39.242  34.749  17.357  1.00 116.07 ? 393 LYS D CD  1 
ATOM   6289  C CE  . LYS B 1 364 ? 40.634  34.250  17.568  1.00 110.49 ? 393 LYS D CE  1 
ATOM   6290  N NZ  . LYS B 1 364 ? 41.619  35.173  17.000  1.00 105.85 ? 393 LYS D NZ  1 
ATOM   6291  N N   . ALA B 1 365 ? 36.386  36.587  16.004  1.00 110.30 ? 394 ALA D N   1 
ATOM   6292  C CA  . ALA B 1 365 ? 34.995  36.531  15.586  1.00 104.54 ? 394 ALA D CA  1 
ATOM   6293  C C   . ALA B 1 365 ? 34.484  37.951  15.371  1.00 110.17 ? 394 ALA D C   1 
ATOM   6294  O O   . ALA B 1 365 ? 34.936  38.894  16.022  1.00 99.93  ? 394 ALA D O   1 
ATOM   6295  C CB  . ALA B 1 365 ? 34.144  35.792  16.603  1.00 101.47 ? 394 ALA D CB  1 
ATOM   6296  N N   . LYS B 1 366 ? 33.534  38.079  14.441  1.00 120.04 ? 395 LYS D N   1 
ATOM   6297  C CA  . LYS B 1 366 ? 32.829  39.330  14.230  1.00 121.79 ? 395 LYS D CA  1 
ATOM   6298  C C   . LYS B 1 366 ? 31.761  39.474  15.318  1.00 117.65 ? 395 LYS D C   1 
ATOM   6299  O O   . LYS B 1 366 ? 31.155  40.538  15.437  1.00 120.35 ? 395 LYS D O   1 
ATOM   6300  C CB  . LYS B 1 366 ? 32.291  39.355  12.793  1.00 121.86 ? 395 LYS D CB  1 
ATOM   6301  C CG  . LYS B 1 366 ? 31.939  40.729  12.227  1.00 116.95 ? 395 LYS D CG  1 
ATOM   6302  C CD  . LYS B 1 366 ? 31.233  40.676  10.876  1.00 118.39 ? 395 LYS D CD  1 
ATOM   6303  C CE  . LYS B 1 366 ? 29.950  39.881  10.872  1.00 118.46 ? 395 LYS D CE  1 
ATOM   6304  N NZ  . LYS B 1 366 ? 28.986  40.330  11.881  1.00 115.88 ? 395 LYS D NZ  1 
ATOM   6305  N N   . ASN B 1 367 ? 31.535  38.394  16.094  1.00 111.83 ? 396 ASN D N   1 
ATOM   6306  C CA  . ASN B 1 367 ? 30.725  38.436  17.308  1.00 100.74 ? 396 ASN D CA  1 
ATOM   6307  C C   . ASN B 1 367 ? 31.591  38.118  18.532  1.00 88.52  ? 396 ASN D C   1 
ATOM   6308  O O   . ASN B 1 367 ? 32.002  36.976  18.762  1.00 77.19  ? 396 ASN D O   1 
ATOM   6309  C CB  . ASN B 1 367 ? 29.506  37.519  17.240  1.00 102.39 ? 396 ASN D CB  1 
ATOM   6310  C CG  . ASN B 1 367 ? 28.528  37.906  16.149  1.00 100.28 ? 396 ASN D CG  1 
ATOM   6311  O OD1 . ASN B 1 367 ? 28.262  39.096  15.926  1.00 88.75  ? 396 ASN D OD1 1 
ATOM   6312  N ND2 . ASN B 1 367 ? 27.974  36.912  15.465  1.00 89.47  ? 396 ASN D ND2 1 
ATOM   6313  N N   . PRO B 1 368 ? 31.888  39.142  19.362  1.00 78.79  ? 397 PRO D N   1 
ATOM   6314  C CA  . PRO B 1 368 ? 32.657  38.954  20.593  1.00 73.39  ? 397 PRO D CA  1 
ATOM   6315  C C   . PRO B 1 368 ? 31.869  38.899  21.904  1.00 66.96  ? 397 PRO D C   1 
ATOM   6316  O O   . PRO B 1 368 ? 32.432  39.118  22.969  1.00 58.66  ? 397 PRO D O   1 
ATOM   6317  C CB  . PRO B 1 368 ? 33.443  40.269  20.464  1.00 74.26  ? 397 PRO D CB  1 
ATOM   6318  C CG  . PRO B 1 368 ? 32.360  41.283  20.162  1.00 71.53  ? 397 PRO D CG  1 
ATOM   6319  C CD  . PRO B 1 368 ? 31.531  40.556  19.129  1.00 72.34  ? 397 PRO D CD  1 
ATOM   6320  N N   . TRP B 1 369 ? 30.560  38.636  21.827  1.00 61.42  ? 398 TRP D N   1 
ATOM   6321  C CA  . TRP B 1 369 ? 29.692  38.813  22.975  1.00 57.79  ? 398 TRP D CA  1 
ATOM   6322  C C   . TRP B 1 369 ? 29.637  37.523  23.792  1.00 51.48  ? 398 TRP D C   1 
ATOM   6323  O O   . TRP B 1 369 ? 30.077  36.459  23.337  1.00 46.80  ? 398 TRP D O   1 
ATOM   6324  C CB  . TRP B 1 369 ? 28.309  39.292  22.520  1.00 67.03  ? 398 TRP D CB  1 
ATOM   6325  C CG  . TRP B 1 369 ? 28.385  40.401  21.508  1.00 72.80  ? 398 TRP D CG  1 
ATOM   6326  C CD1 . TRP B 1 369 ? 28.224  40.299  20.159  1.00 76.29  ? 398 TRP D CD1 1 
ATOM   6327  C CD2 . TRP B 1 369 ? 28.682  41.783  21.778  1.00 72.80  ? 398 TRP D CD2 1 
ATOM   6328  N NE1 . TRP B 1 369 ? 28.389  41.522  19.569  1.00 80.02  ? 398 TRP D NE1 1 
ATOM   6329  C CE2 . TRP B 1 369 ? 28.671  42.449  20.536  1.00 78.04  ? 398 TRP D CE2 1 
ATOM   6330  C CE3 . TRP B 1 369 ? 28.950  42.515  22.938  1.00 74.59  ? 398 TRP D CE3 1 
ATOM   6331  C CZ2 . TRP B 1 369 ? 28.916  43.814  20.429  1.00 81.25  ? 398 TRP D CZ2 1 
ATOM   6332  C CZ3 . TRP B 1 369 ? 29.186  43.868  22.830  1.00 78.55  ? 398 TRP D CZ3 1 
ATOM   6333  C CH2 . TRP B 1 369 ? 29.173  44.505  21.591  1.00 82.53  ? 398 TRP D CH2 1 
ATOM   6334  N N   . PRO B 1 370 ? 29.187  37.607  25.066  1.00 48.43  ? 399 PRO D N   1 
ATOM   6335  C CA  . PRO B 1 370 ? 29.169  36.434  25.949  1.00 49.47  ? 399 PRO D CA  1 
ATOM   6336  C C   . PRO B 1 370 ? 27.957  35.520  25.749  1.00 43.84  ? 399 PRO D C   1 
ATOM   6337  O O   . PRO B 1 370 ? 26.841  35.996  25.549  1.00 46.25  ? 399 PRO D O   1 
ATOM   6338  C CB  . PRO B 1 370 ? 29.190  37.077  27.363  1.00 49.89  ? 399 PRO D CB  1 
ATOM   6339  C CG  . PRO B 1 370 ? 28.435  38.387  27.174  1.00 52.05  ? 399 PRO D CG  1 
ATOM   6340  C CD  . PRO B 1 370 ? 28.739  38.843  25.740  1.00 48.20  ? 399 PRO D CD  1 
ATOM   6341  N N   . ASN B 1 371 ? 28.189  34.206  25.821  1.00 46.12  ? 400 ASN D N   1 
ATOM   6342  C CA  . ASN B 1 371 ? 27.119  33.217  25.809  1.00 44.92  ? 400 ASN D CA  1 
ATOM   6343  C C   . ASN B 1 371 ? 26.494  33.098  27.204  1.00 46.98  ? 400 ASN D C   1 
ATOM   6344  O O   . ASN B 1 371 ? 26.971  33.704  28.169  1.00 44.89  ? 400 ASN D O   1 
ATOM   6345  C CB  . ASN B 1 371 ? 27.638  31.891  25.282  1.00 48.77  ? 400 ASN D CB  1 
ATOM   6346  C CG  . ASN B 1 371 ? 28.122  30.964  26.371  1.00 64.41  ? 400 ASN D CG  1 
ATOM   6347  O OD1 . ASN B 1 371 ? 29.022  31.296  27.151  1.00 76.23  ? 400 ASN D OD1 1 
ATOM   6348  N ND2 . ASN B 1 371 ? 27.526  29.785  26.449  1.00 79.44  ? 400 ASN D ND2 1 
ATOM   6349  N N   . VAL B 1 372 ? 25.424  32.295  27.314  1.00 43.22  ? 401 VAL D N   1 
ATOM   6350  C CA  . VAL B 1 372 ? 24.722  32.117  28.571  1.00 40.47  ? 401 VAL D CA  1 
ATOM   6351  C C   . VAL B 1 372 ? 25.665  31.647  29.691  1.00 41.17  ? 401 VAL D C   1 
ATOM   6352  O O   . VAL B 1 372 ? 25.489  32.042  30.842  1.00 43.41  ? 401 VAL D O   1 
ATOM   6353  C CB  . VAL B 1 372 ? 23.513  31.172  28.397  1.00 40.80  ? 401 VAL D CB  1 
ATOM   6354  C CG1 . VAL B 1 372 ? 23.866  29.831  27.756  1.00 39.84  ? 401 VAL D CG1 1 
ATOM   6355  C CG2 . VAL B 1 372 ? 22.818  30.954  29.727  1.00 45.74  ? 401 VAL D CG2 1 
ATOM   6356  N N   . ASP B 1 373 ? 26.672  30.829  29.363  1.00 40.87  ? 402 ASP D N   1 
ATOM   6357  C CA  . ASP B 1 373 ? 27.520  30.125  30.326  1.00 42.95  ? 402 ASP D CA  1 
ATOM   6358  C C   . ASP B 1 373 ? 28.562  31.041  30.985  1.00 39.51  ? 402 ASP D C   1 
ATOM   6359  O O   . ASP B 1 373 ? 29.237  30.688  31.943  1.00 34.47  ? 402 ASP D O   1 
ATOM   6360  C CB  . ASP B 1 373 ? 28.192  28.939  29.651  1.00 47.27  ? 402 ASP D CB  1 
ATOM   6361  C CG  . ASP B 1 373 ? 27.267  27.807  29.200  1.00 57.09  ? 402 ASP D CG  1 
ATOM   6362  O OD1 . ASP B 1 373 ? 26.329  27.457  29.967  1.00 57.69  ? 402 ASP D OD1 1 
ATOM   6363  O OD2 . ASP B 1 373 ? 27.507  27.235  28.103  1.00 64.95  ? 402 ASP D OD2 1 
ATOM   6364  N N   . ALA B 1 374 ? 28.723  32.240  30.460  1.00 37.77  ? 403 ALA D N   1 
ATOM   6365  C CA  . ALA B 1 374 ? 29.652  33.167  31.047  1.00 37.92  ? 403 ALA D CA  1 
ATOM   6366  C C   . ALA B 1 374 ? 29.090  33.741  32.357  1.00 36.65  ? 403 ALA D C   1 
ATOM   6367  O O   . ALA B 1 374 ? 29.872  34.266  33.143  1.00 31.62  ? 403 ALA D O   1 
ATOM   6368  C CB  . ALA B 1 374 ? 29.941  34.254  30.033  1.00 41.07  ? 403 ALA D CB  1 
ATOM   6369  N N   . HIS B 1 375 ? 27.764  33.663  32.591  1.00 32.13  ? 404 HIS D N   1 
ATOM   6370  C CA  . HIS B 1 375 ? 27.150  34.282  33.763  1.00 32.10  ? 404 HIS D CA  1 
ATOM   6371  C C   . HIS B 1 375 ? 26.567  33.273  34.753  1.00 34.31  ? 404 HIS D C   1 
ATOM   6372  O O   . HIS B 1 375 ? 26.172  33.617  35.863  1.00 34.96  ? 404 HIS D O   1 
ATOM   6373  C CB  . HIS B 1 375 ? 25.974  35.168  33.361  1.00 34.00  ? 404 HIS D CB  1 
ATOM   6374  C CG  . HIS B 1 375 ? 25.852  36.345  34.251  1.00 36.51  ? 404 HIS D CG  1 
ATOM   6375  N ND1 . HIS B 1 375 ? 25.727  36.270  35.618  1.00 38.11  ? 404 HIS D ND1 1 
ATOM   6376  C CD2 . HIS B 1 375 ? 25.875  37.656  33.949  1.00 39.63  ? 404 HIS D CD2 1 
ATOM   6377  C CE1 . HIS B 1 375 ? 25.678  37.508  36.115  1.00 44.82  ? 404 HIS D CE1 1 
ATOM   6378  N NE2 . HIS B 1 375 ? 25.757  38.367  35.118  1.00 38.51  ? 404 HIS D NE2 1 
ATOM   6379  N N   . SER B 1 376 ? 26.457  32.017  34.352  1.00 32.47  ? 405 SER D N   1 
ATOM   6380  C CA  . SER B 1 376 ? 25.579  31.118  35.074  1.00 35.78  ? 405 SER D CA  1 
ATOM   6381  C C   . SER B 1 376 ? 26.232  30.680  36.391  1.00 33.33  ? 405 SER D C   1 
ATOM   6382  O O   . SER B 1 376 ? 25.611  30.740  37.458  1.00 36.58  ? 405 SER D O   1 
ATOM   6383  C CB  . SER B 1 376 ? 25.182  29.989  34.159  1.00 38.99  ? 405 SER D CB  1 
ATOM   6384  O OG  . SER B 1 376 ? 24.937  28.826  34.925  1.00 59.32  ? 405 SER D OG  1 
ATOM   6385  N N   . GLY B 1 377 ? 27.529  30.362  36.338  1.00 27.17  ? 406 GLY D N   1 
ATOM   6386  C CA  . GLY B 1 377 ? 28.264  29.751  37.427  1.00 28.07  ? 406 GLY D CA  1 
ATOM   6387  C C   . GLY B 1 377 ? 28.379  30.707  38.620  1.00 31.49  ? 406 GLY D C   1 
ATOM   6388  O O   . GLY B 1 377 ? 28.323  30.270  39.759  1.00 32.46  ? 406 GLY D O   1 
ATOM   6389  N N   . VAL B 1 378 ? 28.480  32.010  38.368  1.00 34.56  ? 407 VAL D N   1 
ATOM   6390  C CA  . VAL B 1 378 ? 28.696  32.958  39.456  1.00 33.89  ? 407 VAL D CA  1 
ATOM   6391  C C   . VAL B 1 378 ? 27.419  33.085  40.284  1.00 26.78  ? 407 VAL D C   1 
ATOM   6392  O O   . VAL B 1 378 ? 27.500  33.201  41.504  1.00 29.09  ? 407 VAL D O   1 
ATOM   6393  C CB  . VAL B 1 378 ? 29.236  34.327  39.020  1.00 33.78  ? 407 VAL D CB  1 
ATOM   6394  C CG1 . VAL B 1 378 ? 30.662  34.192  38.500  1.00 37.16  ? 407 VAL D CG1 1 
ATOM   6395  C CG2 . VAL B 1 378 ? 28.345  34.984  37.985  1.00 35.88  ? 407 VAL D CG2 1 
ATOM   6396  N N   . LEU B 1 379 ? 26.262  32.947  39.638  1.00 28.43  ? 408 LEU D N   1 
ATOM   6397  C CA  . LEU B 1 379 ? 24.983  33.025  40.321  1.00 30.57  ? 408 LEU D CA  1 
ATOM   6398  C C   . LEU B 1 379 ? 24.778  31.798  41.203  1.00 30.01  ? 408 LEU D C   1 
ATOM   6399  O O   . LEU B 1 379 ? 24.416  31.911  42.362  1.00 28.36  ? 408 LEU D O   1 
ATOM   6400  C CB  . LEU B 1 379 ? 23.886  33.234  39.280  1.00 34.10  ? 408 LEU D CB  1 
ATOM   6401  C CG  . LEU B 1 379 ? 23.943  34.571  38.536  1.00 38.83  ? 408 LEU D CG  1 
ATOM   6402  C CD1 . LEU B 1 379 ? 22.724  34.767  37.668  1.00 40.46  ? 408 LEU D CD1 1 
ATOM   6403  C CD2 . LEU B 1 379 ? 24.057  35.711  39.530  1.00 45.21  ? 408 LEU D CD2 1 
ATOM   6404  N N   . LEU B 1 380 ? 25.046  30.618  40.658  1.00 27.06  ? 409 LEU D N   1 
ATOM   6405  C CA  . LEU B 1 380 ? 24.841  29.393  41.403  1.00 29.04  ? 409 LEU D CA  1 
ATOM   6406  C C   . LEU B 1 380 ? 25.754  29.374  42.627  1.00 30.00  ? 409 LEU D C   1 
ATOM   6407  O O   . LEU B 1 380 ? 25.316  29.064  43.734  1.00 29.08  ? 409 LEU D O   1 
ATOM   6408  C CB  . LEU B 1 380 ? 25.121  28.224  40.471  1.00 27.64  ? 409 LEU D CB  1 
ATOM   6409  C CG  . LEU B 1 380 ? 24.150  28.053  39.315  1.00 28.86  ? 409 LEU D CG  1 
ATOM   6410  C CD1 . LEU B 1 380 ? 24.812  26.973  38.448  1.00 34.65  ? 409 LEU D CD1 1 
ATOM   6411  C CD2 . LEU B 1 380 ? 22.756  27.667  39.808  1.00 30.01  ? 409 LEU D CD2 1 
ATOM   6412  N N   . GLN B 1 381 ? 27.031  29.698  42.399  1.00 31.89  ? 410 GLN D N   1 
ATOM   6413  C CA  . GLN B 1 381 ? 28.014  29.762  43.450  1.00 32.54  ? 410 GLN D CA  1 
ATOM   6414  C C   . GLN B 1 381 ? 27.543  30.686  44.584  1.00 32.73  ? 410 GLN D C   1 
ATOM   6415  O O   . GLN B 1 381 ? 27.560  30.307  45.761  1.00 31.53  ? 410 GLN D O   1 
ATOM   6416  C CB  . GLN B 1 381 ? 29.345  30.210  42.863  1.00 37.24  ? 410 GLN D CB  1 
ATOM   6417  C CG  . GLN B 1 381 ? 30.466  30.119  43.886  1.00 40.27  ? 410 GLN D CG  1 
ATOM   6418  C CD  . GLN B 1 381 ? 31.816  30.449  43.301  1.00 51.86  ? 410 GLN D CD  1 
ATOM   6419  O OE1 . GLN B 1 381 ? 32.602  29.549  42.987  1.00 53.10  ? 410 GLN D OE1 1 
ATOM   6420  N NE2 . GLN B 1 381 ? 32.073  31.738  43.107  1.00 54.31  ? 410 GLN D NE2 1 
ATOM   6421  N N   . TYR B 1 382 ? 27.066  31.867  44.210  1.00 27.29  ? 411 TYR D N   1 
ATOM   6422  C CA  . TYR B 1 382 ? 26.614  32.870  45.162  1.00 31.95  ? 411 TYR D CA  1 
ATOM   6423  C C   . TYR B 1 382 ? 25.587  32.312  46.148  1.00 32.91  ? 411 TYR D C   1 
ATOM   6424  O O   . TYR B 1 382 ? 25.596  32.731  47.312  1.00 30.03  ? 411 TYR D O   1 
ATOM   6425  C CB  . TYR B 1 382 ? 26.028  34.061  44.407  1.00 31.81  ? 411 TYR D CB  1 
ATOM   6426  C CG  . TYR B 1 382 ? 25.538  35.145  45.351  1.00 32.56  ? 411 TYR D CG  1 
ATOM   6427  C CD1 . TYR B 1 382 ? 26.424  36.029  45.957  1.00 33.16  ? 411 TYR D CD1 1 
ATOM   6428  C CD2 . TYR B 1 382 ? 24.180  35.290  45.622  1.00 30.13  ? 411 TYR D CD2 1 
ATOM   6429  C CE1 . TYR B 1 382 ? 25.977  37.008  46.835  1.00 30.28  ? 411 TYR D CE1 1 
ATOM   6430  C CE2 . TYR B 1 382 ? 23.719  36.294  46.464  1.00 35.30  ? 411 TYR D CE2 1 
ATOM   6431  C CZ  . TYR B 1 382 ? 24.624  37.137  47.094  1.00 34.05  ? 411 TYR D CZ  1 
ATOM   6432  O OH  . TYR B 1 382 ? 24.160  38.119  47.938  1.00 40.16  ? 411 TYR D OH  1 
ATOM   6433  N N   . TYR B 1 383 ? 24.709  31.393  45.685  1.00 26.44  ? 412 TYR D N   1 
ATOM   6434  C CA  . TYR B 1 383 ? 23.602  30.905  46.507  1.00 26.86  ? 412 TYR D CA  1 
ATOM   6435  C C   . TYR B 1 383 ? 24.006  29.624  47.206  1.00 27.38  ? 412 TYR D C   1 
ATOM   6436  O O   . TYR B 1 383 ? 23.172  28.977  47.821  1.00 29.15  ? 412 TYR D O   1 
ATOM   6437  C CB  . TYR B 1 383 ? 22.283  30.697  45.753  1.00 28.64  ? 412 TYR D CB  1 
ATOM   6438  C CG  . TYR B 1 383 ? 21.701  32.049  45.391  1.00 27.26  ? 412 TYR D CG  1 
ATOM   6439  C CD1 . TYR B 1 383 ? 21.107  32.829  46.366  1.00 29.02  ? 412 TYR D CD1 1 
ATOM   6440  C CD2 . TYR B 1 383 ? 21.830  32.592  44.124  1.00 28.43  ? 412 TYR D CD2 1 
ATOM   6441  C CE1 . TYR B 1 383 ? 20.618  34.090  46.073  1.00 28.67  ? 412 TYR D CE1 1 
ATOM   6442  C CE2 . TYR B 1 383 ? 21.324  33.843  43.813  1.00 25.74  ? 412 TYR D CE2 1 
ATOM   6443  C CZ  . TYR B 1 383 ? 20.705  34.593  44.789  1.00 27.04  ? 412 TYR D CZ  1 
ATOM   6444  O OH  . TYR B 1 383 ? 20.215  35.833  44.498  1.00 26.54  ? 412 TYR D OH  1 
ATOM   6445  N N   . GLY B 1 384 ? 25.298  29.296  47.134  1.00 28.62  ? 413 GLY D N   1 
ATOM   6446  C CA  . GLY B 1 384 ? 25.848  28.233  47.946  1.00 27.66  ? 413 GLY D CA  1 
ATOM   6447  C C   . GLY B 1 384 ? 25.917  26.945  47.130  1.00 34.21  ? 413 GLY D C   1 
ATOM   6448  O O   . GLY B 1 384 ? 26.426  25.964  47.616  1.00 32.09  ? 413 GLY D O   1 
ATOM   6449  N N   . MET B 1 385 ? 25.495  26.945  45.860  1.00 32.06  ? 414 MET D N   1 
ATOM   6450  C CA  . MET B 1 385 ? 25.719  25.739  45.081  1.00 32.28  ? 414 MET D CA  1 
ATOM   6451  C C   . MET B 1 385 ? 27.082  25.757  44.400  1.00 31.98  ? 414 MET D C   1 
ATOM   6452  O O   . MET B 1 385 ? 27.248  26.269  43.288  1.00 32.82  ? 414 MET D O   1 
ATOM   6453  C CB  . MET B 1 385 ? 24.675  25.496  44.019  1.00 32.64  ? 414 MET D CB  1 
ATOM   6454  C CG  . MET B 1 385 ? 24.869  24.092  43.499  1.00 35.84  ? 414 MET D CG  1 
ATOM   6455  S SD  . MET B 1 385 ? 23.599  23.815  42.285  1.00 42.49  ? 414 MET D SD  1 
ATOM   6456  C CE  . MET B 1 385 ? 22.164  23.440  43.301  1.00 40.34  ? 414 MET D CE  1 
ATOM   6457  N N   . THR B 1 386 ? 28.061  25.279  45.157  1.00 31.85  ? 415 THR D N   1 
ATOM   6458  C CA  . THR B 1 386 ? 29.447  25.377  44.775  1.00 33.46  ? 415 THR D CA  1 
ATOM   6459  C C   . THR B 1 386 ? 29.886  24.097  44.053  1.00 37.77  ? 415 THR D C   1 
ATOM   6460  O O   . THR B 1 386 ? 31.018  24.031  43.579  1.00 35.59  ? 415 THR D O   1 
ATOM   6461  C CB  . THR B 1 386 ? 30.231  25.634  46.054  1.00 35.39  ? 415 THR D CB  1 
ATOM   6462  O OG1 . THR B 1 386 ? 29.911  24.509  46.860  1.00 34.91  ? 415 THR D OG1 1 
ATOM   6463  C CG2 . THR B 1 386 ? 29.811  26.911  46.770  1.00 38.54  ? 415 THR D CG2 1 
ATOM   6464  N N   . GLU B 1 387 ? 29.001  23.087  43.929  1.00 38.17  ? 416 GLU D N   1 
ATOM   6465  C CA  . GLU B 1 387 ? 29.414  21.785  43.389  1.00 36.19  ? 416 GLU D CA  1 
ATOM   6466  C C   . GLU B 1 387 ? 29.296  21.785  41.863  1.00 32.44  ? 416 GLU D C   1 
ATOM   6467  O O   . GLU B 1 387 ? 28.280  21.410  41.270  1.00 28.94  ? 416 GLU D O   1 
ATOM   6468  C CB  . GLU B 1 387 ? 28.652  20.643  44.058  1.00 38.92  ? 416 GLU D CB  1 
ATOM   6469  C CG  . GLU B 1 387 ? 28.717  20.678  45.585  1.00 38.26  ? 416 GLU D CG  1 
ATOM   6470  C CD  . GLU B 1 387 ? 27.676  21.516  46.299  1.00 40.18  ? 416 GLU D CD  1 
ATOM   6471  O OE1 . GLU B 1 387 ? 26.909  22.280  45.652  1.00 38.08  ? 416 GLU D OE1 1 
ATOM   6472  O OE2 . GLU B 1 387 ? 27.626  21.369  47.538  1.00 38.27  ? 416 GLU D OE2 1 
ATOM   6473  N N   . MET B 1 388 ? 30.371  22.231  41.221  1.00 32.57  ? 417 MET D N   1 
ATOM   6474  C CA  . MET B 1 388 ? 30.378  22.547  39.803  1.00 33.86  ? 417 MET D CA  1 
ATOM   6475  C C   . MET B 1 388 ? 30.104  21.305  38.956  1.00 32.27  ? 417 MET D C   1 
ATOM   6476  O O   . MET B 1 388 ? 29.580  21.440  37.872  1.00 31.15  ? 417 MET D O   1 
ATOM   6477  C CB  . MET B 1 388 ? 31.740  23.085  39.369  1.00 34.98  ? 417 MET D CB  1 
ATOM   6478  C CG  . MET B 1 388 ? 32.008  24.447  39.900  1.00 38.73  ? 417 MET D CG  1 
ATOM   6479  S SD  . MET B 1 388 ? 33.622  25.058  39.385  1.00 44.66  ? 417 MET D SD  1 
ATOM   6480  C CE  . MET B 1 388 ? 33.269  25.582  37.718  1.00 56.99  ? 417 MET D CE  1 
ATOM   6481  N N   . ASN B 1 389 ? 30.468  20.112  39.454  1.00 38.93  ? 418 ASN D N   1 
ATOM   6482  C CA  . ASN B 1 389 ? 30.198  18.863  38.766  1.00 37.47  ? 418 ASN D CA  1 
ATOM   6483  C C   . ASN B 1 389 ? 28.704  18.682  38.546  1.00 39.04  ? 418 ASN D C   1 
ATOM   6484  O O   . ASN B 1 389 ? 28.327  18.043  37.573  1.00 41.38  ? 418 ASN D O   1 
ATOM   6485  C CB  . ASN B 1 389 ? 30.740  17.655  39.518  1.00 39.84  ? 418 ASN D CB  1 
ATOM   6486  C CG  . ASN B 1 389 ? 32.172  17.394  39.140  1.00 44.35  ? 418 ASN D CG  1 
ATOM   6487  O OD1 . ASN B 1 389 ? 32.684  17.987  38.183  1.00 39.38  ? 418 ASN D OD1 1 
ATOM   6488  N ND2 . ASN B 1 389 ? 32.830  16.526  39.890  1.00 48.84  ? 418 ASN D ND2 1 
ATOM   6489  N N   . TYR B 1 390 ? 27.878  19.300  39.403  1.00 31.31  ? 419 TYR D N   1 
ATOM   6490  C CA  . TYR B 1 390 ? 26.439  19.173  39.329  1.00 28.05  ? 419 TYR D CA  1 
ATOM   6491  C C   . TYR B 1 390 ? 25.761  20.190  38.409  1.00 27.63  ? 419 TYR D C   1 
ATOM   6492  O O   . TYR B 1 390 ? 24.607  19.983  38.090  1.00 27.74  ? 419 TYR D O   1 
ATOM   6493  C CB  . TYR B 1 390 ? 25.888  19.402  40.728  1.00 27.78  ? 419 TYR D CB  1 
ATOM   6494  C CG  . TYR B 1 390 ? 24.403  19.121  40.870  1.00 25.68  ? 419 TYR D CG  1 
ATOM   6495  C CD1 . TYR B 1 390 ? 23.936  17.815  40.972  1.00 26.65  ? 419 TYR D CD1 1 
ATOM   6496  C CD2 . TYR B 1 390 ? 23.484  20.160  40.950  1.00 25.93  ? 419 TYR D CD2 1 
ATOM   6497  C CE1 . TYR B 1 390 ? 22.592  17.545  41.158  1.00 25.78  ? 419 TYR D CE1 1 
ATOM   6498  C CE2 . TYR B 1 390 ? 22.135  19.911  41.119  1.00 26.87  ? 419 TYR D CE2 1 
ATOM   6499  C CZ  . TYR B 1 390 ? 21.696  18.597  41.246  1.00 27.07  ? 419 TYR D CZ  1 
ATOM   6500  O OH  . TYR B 1 390 ? 20.397  18.272  41.395  1.00 22.44  ? 419 TYR D OH  1 
ATOM   6501  N N   . TYR B 1 391 ? 26.454  21.246  37.947  1.00 24.40  ? 420 TYR D N   1 
ATOM   6502  C CA  . TYR B 1 391 ? 25.803  22.305  37.205  1.00 25.85  ? 420 TYR D CA  1 
ATOM   6503  C C   . TYR B 1 391 ? 25.074  21.772  35.987  1.00 26.07  ? 420 TYR D C   1 
ATOM   6504  O O   . TYR B 1 391 ? 23.988  22.204  35.687  1.00 25.59  ? 420 TYR D O   1 
ATOM   6505  C CB  . TYR B 1 391 ? 26.724  23.450  36.769  1.00 28.91  ? 420 TYR D CB  1 
ATOM   6506  C CG  . TYR B 1 391 ? 27.281  24.260  37.943  1.00 33.92  ? 420 TYR D CG  1 
ATOM   6507  C CD1 . TYR B 1 391 ? 26.792  24.103  39.229  1.00 31.17  ? 420 TYR D CD1 1 
ATOM   6508  C CD2 . TYR B 1 391 ? 28.240  25.244  37.746  1.00 30.92  ? 420 TYR D CD2 1 
ATOM   6509  C CE1 . TYR B 1 391 ? 27.299  24.845  40.285  1.00 36.55  ? 420 TYR D CE1 1 
ATOM   6510  C CE2 . TYR B 1 391 ? 28.705  26.039  38.779  1.00 30.18  ? 420 TYR D CE2 1 
ATOM   6511  C CZ  . TYR B 1 391 ? 28.260  25.815  40.062  1.00 32.51  ? 420 TYR D CZ  1 
ATOM   6512  O OH  . TYR B 1 391 ? 28.764  26.550  41.092  1.00 34.66  ? 420 TYR D OH  1 
ATOM   6513  N N   . THR B 1 392 ? 25.665  20.841  35.261  1.00 27.55  ? 421 THR D N   1 
ATOM   6514  C CA  . THR B 1 392 ? 25.039  20.394  34.041  1.00 26.72  ? 421 THR D CA  1 
ATOM   6515  C C   . THR B 1 392 ? 23.732  19.648  34.331  1.00 26.70  ? 421 THR D C   1 
ATOM   6516  O O   . THR B 1 392 ? 22.843  19.601  33.488  1.00 25.70  ? 421 THR D O   1 
ATOM   6517  C CB  . THR B 1 392 ? 26.040  19.542  33.277  1.00 32.83  ? 421 THR D CB  1 
ATOM   6518  O OG1 . THR B 1 392 ? 27.189  20.358  33.062  1.00 40.39  ? 421 THR D OG1 1 
ATOM   6519  C CG2 . THR B 1 392 ? 25.474  19.166  31.920  1.00 40.88  ? 421 THR D CG2 1 
ATOM   6520  N N   . VAL B 1 393 ? 23.600  19.018  35.497  1.00 25.42  ? 422 VAL D N   1 
ATOM   6521  C CA  . VAL B 1 393 ? 22.305  18.460  35.866  1.00 26.91  ? 422 VAL D CA  1 
ATOM   6522  C C   . VAL B 1 393 ? 21.190  19.526  35.837  1.00 27.14  ? 422 VAL D C   1 
ATOM   6523  O O   . VAL B 1 393 ? 20.072  19.276  35.388  1.00 24.95  ? 422 VAL D O   1 
ATOM   6524  C CB  . VAL B 1 393 ? 22.426  17.779  37.240  1.00 23.26  ? 422 VAL D CB  1 
ATOM   6525  C CG1 . VAL B 1 393 ? 21.087  17.296  37.733  1.00 24.89  ? 422 VAL D CG1 1 
ATOM   6526  C CG2 . VAL B 1 393 ? 23.390  16.611  37.167  1.00 27.32  ? 422 VAL D CG2 1 
ATOM   6527  N N   . LEU B 1 394 ? 21.472  20.723  36.321  1.00 30.83  ? 423 LEU D N   1 
ATOM   6528  C CA  . LEU B 1 394 ? 20.464  21.775  36.276  1.00 34.75  ? 423 LEU D CA  1 
ATOM   6529  C C   . LEU B 1 394 ? 20.113  22.094  34.825  1.00 32.11  ? 423 LEU D C   1 
ATOM   6530  O O   . LEU B 1 394 ? 18.955  22.305  34.501  1.00 30.66  ? 423 LEU D O   1 
ATOM   6531  C CB  . LEU B 1 394 ? 20.910  23.040  36.996  1.00 31.91  ? 423 LEU D CB  1 
ATOM   6532  C CG  . LEU B 1 394 ? 21.254  22.875  38.477  1.00 34.52  ? 423 LEU D CG  1 
ATOM   6533  C CD1 . LEU B 1 394 ? 21.894  24.190  38.966  1.00 35.46  ? 423 LEU D CD1 1 
ATOM   6534  C CD2 . LEU B 1 394 ? 20.052  22.488  39.294  1.00 31.57  ? 423 LEU D CD2 1 
ATOM   6535  N N   . PHE B 1 395 ? 21.131  22.155  33.968  1.00 31.15  ? 424 PHE D N   1 
ATOM   6536  C CA  . PHE B 1 395 ? 20.893  22.395  32.563  1.00 32.27  ? 424 PHE D CA  1 
ATOM   6537  C C   . PHE B 1 395 ? 19.969  21.303  32.030  1.00 30.57  ? 424 PHE D C   1 
ATOM   6538  O O   . PHE B 1 395 ? 19.042  21.590  31.279  1.00 31.00  ? 424 PHE D O   1 
ATOM   6539  C CB  . PHE B 1 395 ? 22.274  22.474  31.909  1.00 36.51  ? 424 PHE D CB  1 
ATOM   6540  C CG  . PHE B 1 395 ? 22.352  22.918  30.447  1.00 35.33  ? 424 PHE D CG  1 
ATOM   6541  C CD1 . PHE B 1 395 ? 21.236  23.029  29.646  1.00 37.80  ? 424 PHE D CD1 1 
ATOM   6542  C CD2 . PHE B 1 395 ? 23.591  23.210  29.875  1.00 45.62  ? 424 PHE D CD2 1 
ATOM   6543  C CE1 . PHE B 1 395 ? 21.353  23.401  28.312  1.00 40.23  ? 424 PHE D CE1 1 
ATOM   6544  C CE2 . PHE B 1 395 ? 23.704  23.592  28.545  1.00 44.42  ? 424 PHE D CE2 1 
ATOM   6545  C CZ  . PHE B 1 395 ? 22.579  23.666  27.770  1.00 44.83  ? 424 PHE D CZ  1 
ATOM   6546  N N   . GLY B 1 396 ? 20.179  20.069  32.499  1.00 31.45  ? 425 GLY D N   1 
ATOM   6547  C CA  . GLY B 1 396 ? 19.478  18.915  31.981  1.00 27.49  ? 425 GLY D CA  1 
ATOM   6548  C C   . GLY B 1 396 ? 18.016  18.965  32.387  1.00 27.33  ? 425 GLY D C   1 
ATOM   6549  O O   . GLY B 1 396 ? 17.121  18.710  31.579  1.00 25.82  ? 425 GLY D O   1 
ATOM   6550  N N   . VAL B 1 397 ? 17.769  19.289  33.646  1.00 28.92  ? 426 VAL D N   1 
ATOM   6551  C CA  . VAL B 1 397 ? 16.398  19.413  34.091  1.00 27.39  ? 426 VAL D CA  1 
ATOM   6552  C C   . VAL B 1 397 ? 15.703  20.496  33.240  1.00 27.44  ? 426 VAL D C   1 
ATOM   6553  O O   . VAL B 1 397 ? 14.554  20.379  32.837  1.00 30.16  ? 426 VAL D O   1 
ATOM   6554  C CB  . VAL B 1 397 ? 16.328  19.692  35.595  1.00 27.16  ? 426 VAL D CB  1 
ATOM   6555  C CG1 . VAL B 1 397 ? 14.913  20.015  36.051  1.00 28.27  ? 426 VAL D CG1 1 
ATOM   6556  C CG2 . VAL B 1 397 ? 16.881  18.553  36.426  1.00 32.57  ? 426 VAL D CG2 1 
ATOM   6557  N N   . SER B 1 398 ? 16.388  21.585  32.958  1.00 27.33  ? 427 SER D N   1 
ATOM   6558  C CA  . SER B 1 398 ? 15.803  22.637  32.144  1.00 25.01  ? 427 SER D CA  1 
ATOM   6559  C C   . SER B 1 398 ? 15.441  22.116  30.752  1.00 29.98  ? 427 SER D C   1 
ATOM   6560  O O   . SER B 1 398 ? 14.295  22.252  30.298  1.00 26.54  ? 427 SER D O   1 
ATOM   6561  C CB  . SER B 1 398 ? 16.732  23.805  32.050  1.00 25.57  ? 427 SER D CB  1 
ATOM   6562  O OG  . SER B 1 398 ? 16.196  24.802  31.192  1.00 24.90  ? 427 SER D OG  1 
ATOM   6563  N N   . ARG B 1 399 ? 16.433  21.479  30.102  1.00 28.57  ? 428 ARG D N   1 
ATOM   6564  C CA  . ARG B 1 399 ? 16.310  21.068  28.714  1.00 28.43  ? 428 ARG D CA  1 
ATOM   6565  C C   . ARG B 1 399 ? 15.212  20.017  28.560  1.00 24.78  ? 428 ARG D C   1 
ATOM   6566  O O   . ARG B 1 399 ? 14.616  19.897  27.490  1.00 23.54  ? 428 ARG D O   1 
ATOM   6567  C CB  . ARG B 1 399 ? 17.695  20.647  28.218  1.00 29.56  ? 428 ARG D CB  1 
ATOM   6568  C CG  . ARG B 1 399 ? 17.840  20.234  26.763  1.00 30.02  ? 428 ARG D CG  1 
ATOM   6569  C CD  . ARG B 1 399 ? 17.447  21.354  25.844  1.00 29.52  ? 428 ARG D CD  1 
ATOM   6570  N NE  . ARG B 1 399 ? 18.022  22.670  26.149  1.00 28.94  ? 428 ARG D NE  1 
ATOM   6571  C CZ  . ARG B 1 399 ? 19.035  23.240  25.476  1.00 27.99  ? 428 ARG D CZ  1 
ATOM   6572  N NH1 . ARG B 1 399 ? 19.765  22.522  24.638  1.00 28.19  ? 428 ARG D NH1 1 
ATOM   6573  N NH2 . ARG B 1 399 ? 19.347  24.504  25.681  1.00 25.10  ? 428 ARG D NH2 1 
ATOM   6574  N N   . ALA B 1 400 ? 14.910  19.256  29.618  1.00 23.60  ? 429 ALA D N   1 
ATOM   6575  C CA  . ALA B 1 400 ? 13.796  18.321  29.525  1.00 22.96  ? 429 ALA D CA  1 
ATOM   6576  C C   . ALA B 1 400 ? 12.584  19.025  28.922  1.00 22.07  ? 429 ALA D C   1 
ATOM   6577  O O   . ALA B 1 400 ? 11.825  18.409  28.174  1.00 25.58  ? 429 ALA D O   1 
ATOM   6578  C CB  . ALA B 1 400 ? 13.459  17.708  30.879  1.00 24.12  ? 429 ALA D CB  1 
ATOM   6579  N N   . LEU B 1 401 ? 12.357  20.289  29.284  1.00 21.46  ? 430 LEU D N   1 
ATOM   6580  C CA  . LEU B 1 401 ? 11.126  20.971  28.958  1.00 26.18  ? 430 LEU D CA  1 
ATOM   6581  C C   . LEU B 1 401 ? 11.009  21.138  27.459  1.00 27.53  ? 430 LEU D C   1 
ATOM   6582  O O   . LEU B 1 401 ? 9.910   20.975  26.900  1.00 27.28  ? 430 LEU D O   1 
ATOM   6583  C CB  . LEU B 1 401 ? 10.993  22.346  29.637  1.00 25.72  ? 430 LEU D CB  1 
ATOM   6584  C CG  . LEU B 1 401 ? 11.009  22.301  31.168  1.00 30.00  ? 430 LEU D CG  1 
ATOM   6585  C CD1 . LEU B 1 401 ? 10.914  23.682  31.820  1.00 32.10  ? 430 LEU D CD1 1 
ATOM   6586  C CD2 . LEU B 1 401 ? 9.882   21.411  31.685  1.00 32.86  ? 430 LEU D CD2 1 
ATOM   6587  N N   . GLY B 1 402 ? 12.131  21.515  26.836  1.00 23.33  ? 431 GLY D N   1 
ATOM   6588  C CA  . GLY B 1 402 ? 12.093  21.798  25.419  1.00 25.81  ? 431 GLY D CA  1 
ATOM   6589  C C   . GLY B 1 402 ? 12.052  20.511  24.590  1.00 25.99  ? 431 GLY D C   1 
ATOM   6590  O O   . GLY B 1 402 ? 11.232  20.361  23.691  1.00 25.78  ? 431 GLY D O   1 
ATOM   6591  N N   . VAL B 1 403 ? 12.937  19.572  24.894  1.00 25.18  ? 432 VAL D N   1 
ATOM   6592  C CA  . VAL B 1 403 ? 13.044  18.372  24.088  1.00 28.99  ? 432 VAL D CA  1 
ATOM   6593  C C   . VAL B 1 403 ? 11.777  17.520  24.247  1.00 28.70  ? 432 VAL D C   1 
ATOM   6594  O O   . VAL B 1 403 ? 11.390  16.848  23.312  1.00 25.55  ? 432 VAL D O   1 
ATOM   6595  C CB  . VAL B 1 403 ? 14.341  17.589  24.376  1.00 31.14  ? 432 VAL D CB  1 
ATOM   6596  C CG1 . VAL B 1 403 ? 15.547  18.482  24.214  1.00 33.96  ? 432 VAL D CG1 1 
ATOM   6597  C CG2 . VAL B 1 403 ? 14.368  16.932  25.755  1.00 29.72  ? 432 VAL D CG2 1 
ATOM   6598  N N   . LEU B 1 404 ? 11.128  17.519  25.416  1.00 25.96  ? 433 LEU D N   1 
ATOM   6599  C CA  . LEU B 1 404 ? 9.914   16.733  25.596  1.00 24.08  ? 433 LEU D CA  1 
ATOM   6600  C C   . LEU B 1 404 ? 8.704   17.379  24.926  1.00 27.42  ? 433 LEU D C   1 
ATOM   6601  O O   . LEU B 1 404 ? 7.883   16.676  24.354  1.00 25.90  ? 433 LEU D O   1 
ATOM   6602  C CB  . LEU B 1 404 ? 9.627   16.452  27.069  1.00 25.37  ? 433 LEU D CB  1 
ATOM   6603  C CG  . LEU B 1 404 ? 10.698  15.616  27.780  1.00 27.20  ? 433 LEU D CG  1 
ATOM   6604  C CD1 . LEU B 1 404 ? 10.221  15.408  29.186  1.00 29.48  ? 433 LEU D CD1 1 
ATOM   6605  C CD2 . LEU B 1 404 ? 10.964  14.286  27.102  1.00 30.92  ? 433 LEU D CD2 1 
ATOM   6606  N N   . ALA B 1 405 ? 8.601   18.705  24.999  1.00 29.08  ? 434 ALA D N   1 
ATOM   6607  C CA  . ALA B 1 405 ? 7.587   19.434  24.277  1.00 29.10  ? 434 ALA D CA  1 
ATOM   6608  C C   . ALA B 1 405 ? 7.685   19.123  22.791  1.00 29.47  ? 434 ALA D C   1 
ATOM   6609  O O   . ALA B 1 405 ? 6.664   18.946  22.136  1.00 27.20  ? 434 ALA D O   1 
ATOM   6610  C CB  . ALA B 1 405 ? 7.723   20.902  24.551  1.00 35.16  ? 434 ALA D CB  1 
ATOM   6611  N N   . GLN B 1 406 ? 8.907   19.012  22.270  1.00 28.43  ? 435 GLN D N   1 
ATOM   6612  C CA  . GLN B 1 406 ? 9.079   18.768  20.844  1.00 33.06  ? 435 GLN D CA  1 
ATOM   6613  C C   . GLN B 1 406 ? 8.797   17.290  20.541  1.00 28.36  ? 435 GLN D C   1 
ATOM   6614  O O   . GLN B 1 406 ? 8.201   16.969  19.513  1.00 27.69  ? 435 GLN D O   1 
ATOM   6615  C CB  . GLN B 1 406 ? 10.450  19.155  20.293  1.00 33.97  ? 435 GLN D CB  1 
ATOM   6616  C CG  . GLN B 1 406 ? 10.697  18.686  18.861  1.00 39.77  ? 435 GLN D CG  1 
ATOM   6617  C CD  . GLN B 1 406 ? 9.728   19.283  17.853  1.00 36.18  ? 435 GLN D CD  1 
ATOM   6618  O OE1 . GLN B 1 406 ? 9.412   20.474  17.888  1.00 30.97  ? 435 GLN D OE1 1 
ATOM   6619  N NE2 . GLN B 1 406 ? 9.242   18.462  16.939  1.00 38.33  ? 435 GLN D NE2 1 
ATOM   6620  N N   . LEU B 1 407 ? 9.210   16.410  21.449  1.00 26.70  ? 436 LEU D N   1 
ATOM   6621  C CA  . LEU B 1 407 ? 9.003   14.984  21.275  1.00 27.86  ? 436 LEU D CA  1 
ATOM   6622  C C   . LEU B 1 407 ? 7.506   14.689  21.112  1.00 27.15  ? 436 LEU D C   1 
ATOM   6623  O O   . LEU B 1 407 ? 7.148   13.870  20.266  1.00 25.05  ? 436 LEU D O   1 
ATOM   6624  C CB  . LEU B 1 407 ? 9.598   14.250  22.470  1.00 25.62  ? 436 LEU D CB  1 
ATOM   6625  C CG  . LEU B 1 407 ? 9.502   12.736  22.426  1.00 29.87  ? 436 LEU D CG  1 
ATOM   6626  C CD1 . LEU B 1 407 ? 10.327  12.250  21.218  1.00 31.04  ? 436 LEU D CD1 1 
ATOM   6627  C CD2 . LEU B 1 407 ? 9.998   12.054  23.692  1.00 32.75  ? 436 LEU D CD2 1 
ATOM   6628  N N   . ILE B 1 408 ? 6.643   15.317  21.937  1.00 22.65  ? 437 ILE D N   1 
ATOM   6629  C CA  . ILE B 1 408 ? 5.190   15.151  21.825  1.00 22.13  ? 437 ILE D CA  1 
ATOM   6630  C C   . ILE B 1 408 ? 4.700   15.484  20.410  1.00 23.48  ? 437 ILE D C   1 
ATOM   6631  O O   . ILE B 1 408 ? 3.961   14.719  19.770  1.00 22.46  ? 437 ILE D O   1 
ATOM   6632  C CB  . ILE B 1 408 ? 4.491   16.052  22.863  1.00 25.43  ? 437 ILE D CB  1 
ATOM   6633  C CG1 . ILE B 1 408 ? 4.767   15.533  24.238  1.00 28.48  ? 437 ILE D CG1 1 
ATOM   6634  C CG2 . ILE B 1 408 ? 2.990   16.165  22.587  1.00 26.76  ? 437 ILE D CG2 1 
ATOM   6635  C CD1 . ILE B 1 408 ? 4.422   16.498  25.357  1.00 29.68  ? 437 ILE D CD1 1 
ATOM   6636  N N   . TRP B 1 409 ? 5.169   16.625  19.907  1.00 24.98  ? 438 TRP D N   1 
ATOM   6637  C CA  . TRP B 1 409 ? 4.872   17.124  18.568  1.00 24.46  ? 438 TRP D CA  1 
ATOM   6638  C C   . TRP B 1 409 ? 5.489   16.265  17.456  1.00 23.67  ? 438 TRP D C   1 
ATOM   6639  O O   . TRP B 1 409 ? 4.828   15.962  16.487  1.00 28.55  ? 438 TRP D O   1 
ATOM   6640  C CB  . TRP B 1 409 ? 5.300   18.593  18.473  1.00 23.66  ? 438 TRP D CB  1 
ATOM   6641  C CG  . TRP B 1 409 ? 4.246   19.507  19.048  1.00 29.24  ? 438 TRP D CG  1 
ATOM   6642  C CD1 . TRP B 1 409 ? 4.247   20.164  20.238  1.00 28.78  ? 438 TRP D CD1 1 
ATOM   6643  C CD2 . TRP B 1 409 ? 2.972   19.784  18.443  1.00 30.94  ? 438 TRP D CD2 1 
ATOM   6644  N NE1 . TRP B 1 409 ? 3.068   20.842  20.417  1.00 30.12  ? 438 TRP D NE1 1 
ATOM   6645  C CE2 . TRP B 1 409 ? 2.276   20.634  19.322  1.00 30.18  ? 438 TRP D CE2 1 
ATOM   6646  C CE3 . TRP B 1 409 ? 2.370   19.415  17.236  1.00 29.86  ? 438 TRP D CE3 1 
ATOM   6647  C CZ2 . TRP B 1 409 ? 1.017   21.122  19.016  1.00 29.09  ? 438 TRP D CZ2 1 
ATOM   6648  C CZ3 . TRP B 1 409 ? 1.118   19.895  16.951  1.00 33.12  ? 438 TRP D CZ3 1 
ATOM   6649  C CH2 . TRP B 1 409 ? 0.455   20.741  17.829  1.00 26.76  ? 438 TRP D CH2 1 
ATOM   6650  N N   . SER B 1 410 ? 6.707   15.785  17.611  1.00 26.53  ? 439 SER D N   1 
ATOM   6651  C CA  . SER B 1 410 ? 7.264   14.857  16.627  1.00 27.07  ? 439 SER D CA  1 
ATOM   6652  C C   . SER B 1 410 ? 6.359   13.653  16.404  1.00 24.12  ? 439 SER D C   1 
ATOM   6653  O O   . SER B 1 410 ? 6.032   13.336  15.270  1.00 22.65  ? 439 SER D O   1 
ATOM   6654  C CB  . SER B 1 410 ? 8.688   14.430  16.974  1.00 24.48  ? 439 SER D CB  1 
ATOM   6655  O OG  . SER B 1 410 ? 9.503   15.583  16.885  1.00 24.79  ? 439 SER D OG  1 
ATOM   6656  N N   . ARG B 1 411 ? 5.903   13.019  17.483  1.00 27.68  ? 440 ARG D N   1 
ATOM   6657  C CA  . ARG B 1 411 ? 4.956   11.914  17.385  1.00 24.46  ? 440 ARG D CA  1 
ATOM   6658  C C   . ARG B 1 411 ? 3.576   12.342  16.898  1.00 23.51  ? 440 ARG D C   1 
ATOM   6659  O O   . ARG B 1 411 ? 2.958   11.627  16.118  1.00 24.73  ? 440 ARG D O   1 
ATOM   6660  C CB  . ARG B 1 411 ? 4.831   11.213  18.735  1.00 24.94  ? 440 ARG D CB  1 
ATOM   6661  C CG  . ARG B 1 411 ? 6.190   10.656  19.093  1.00 28.01  ? 440 ARG D CG  1 
ATOM   6662  C CD  . ARG B 1 411 ? 6.511   9.664   17.976  1.00 32.91  ? 440 ARG D CD  1 
ATOM   6663  N NE  . ARG B 1 411 ? 7.950   9.723   17.866  1.00 35.80  ? 440 ARG D NE  1 
ATOM   6664  C CZ  . ARG B 1 411 ? 8.716   10.630  17.348  1.00 33.46  ? 440 ARG D CZ  1 
ATOM   6665  N NH1 . ARG B 1 411 ? 8.752   10.866  16.061  1.00 29.91  ? 440 ARG D NH1 1 
ATOM   6666  N NH2 . ARG B 1 411 ? 9.674   11.034  18.144  1.00 41.39  ? 440 ARG D NH2 1 
ATOM   6667  N N   . ALA B 1 412 ? 3.033   13.459  17.390  1.00 24.99  ? 441 ALA D N   1 
ATOM   6668  C CA  . ALA B 1 412 ? 1.711   13.883  16.958  1.00 26.87  ? 441 ALA D CA  1 
ATOM   6669  C C   . ALA B 1 412 ? 1.743   14.140  15.456  1.00 28.96  ? 441 ALA D C   1 
ATOM   6670  O O   . ALA B 1 412 ? 0.764   13.931  14.751  1.00 29.99  ? 441 ALA D O   1 
ATOM   6671  C CB  . ALA B 1 412 ? 1.242   15.118  17.724  1.00 28.02  ? 441 ALA D CB  1 
ATOM   6672  N N   . LEU B 1 413 ? 2.877   14.619  14.958  1.00 28.98  ? 442 LEU D N   1 
ATOM   6673  C CA  . LEU B 1 413 ? 2.947   14.936  13.543  1.00 31.52  ? 442 LEU D CA  1 
ATOM   6674  C C   . LEU B 1 413 ? 3.421   13.736  12.718  1.00 33.60  ? 442 LEU D C   1 
ATOM   6675  O O   . LEU B 1 413 ? 3.517   13.845  11.496  1.00 37.98  ? 442 LEU D O   1 
ATOM   6676  C CB  . LEU B 1 413 ? 3.867   16.143  13.387  1.00 28.90  ? 442 LEU D CB  1 
ATOM   6677  C CG  . LEU B 1 413 ? 3.341   17.431  14.030  1.00 28.49  ? 442 LEU D CG  1 
ATOM   6678  C CD1 . LEU B 1 413 ? 4.386   18.524  13.856  1.00 29.86  ? 442 LEU D CD1 1 
ATOM   6679  C CD2 . LEU B 1 413 ? 2.022   17.871  13.422  1.00 30.70  ? 442 LEU D CD2 1 
ATOM   6680  N N   . GLY B 1 414 ? 3.780   12.636  13.384  1.00 29.74  ? 443 GLY D N   1 
ATOM   6681  C CA  . GLY B 1 414 ? 4.176   11.431  12.680  1.00 30.27  ? 443 GLY D CA  1 
ATOM   6682  C C   . GLY B 1 414 ? 5.515   11.603  11.972  1.00 29.83  ? 443 GLY D C   1 
ATOM   6683  O O   . GLY B 1 414 ? 5.714   11.054  10.916  1.00 27.66  ? 443 GLY D O   1 
ATOM   6684  N N   . PHE B 1 415 ? 6.479   12.299  12.558  1.00 25.80  ? 444 PHE D N   1 
ATOM   6685  C CA  . PHE B 1 415 ? 7.795   12.316  11.943  1.00 28.56  ? 444 PHE D CA  1 
ATOM   6686  C C   . PHE B 1 415 ? 8.344   10.886  11.919  1.00 27.55  ? 444 PHE D C   1 
ATOM   6687  O O   . PHE B 1 415 ? 8.320   10.204  12.941  1.00 28.56  ? 444 PHE D O   1 
ATOM   6688  C CB  . PHE B 1 415 ? 8.786   13.259  12.626  1.00 26.82  ? 444 PHE D CB  1 
ATOM   6689  C CG  . PHE B 1 415 ? 8.436   14.739  12.636  1.00 30.98  ? 444 PHE D CG  1 
ATOM   6690  C CD1 . PHE B 1 415 ? 7.440   15.258  11.817  1.00 29.88  ? 444 PHE D CD1 1 
ATOM   6691  C CD2 . PHE B 1 415 ? 9.157   15.617  13.436  1.00 28.50  ? 444 PHE D CD2 1 
ATOM   6692  C CE1 . PHE B 1 415 ? 7.181   16.609  11.816  1.00 31.45  ? 444 PHE D CE1 1 
ATOM   6693  C CE2 . PHE B 1 415 ? 8.858   16.957  13.457  1.00 28.37  ? 444 PHE D CE2 1 
ATOM   6694  C CZ  . PHE B 1 415 ? 7.874   17.451  12.652  1.00 30.99  ? 444 PHE D CZ  1 
ATOM   6695  N N   . PRO B 1 416 ? 8.923   10.427  10.784  1.00 24.42  ? 445 PRO D N   1 
ATOM   6696  C CA  . PRO B 1 416 ? 9.463   9.084   10.677  1.00 24.12  ? 445 PRO D CA  1 
ATOM   6697  C C   . PRO B 1 416 ? 10.854  8.956   11.311  1.00 25.26  ? 445 PRO D C   1 
ATOM   6698  O O   . PRO B 1 416 ? 11.352  9.855   11.956  1.00 24.66  ? 445 PRO D O   1 
ATOM   6699  C CB  . PRO B 1 416 ? 9.449   8.853   9.155   1.00 24.06  ? 445 PRO D CB  1 
ATOM   6700  C CG  . PRO B 1 416 ? 9.855   10.216  8.622   1.00 28.61  ? 445 PRO D CG  1 
ATOM   6701  C CD  . PRO B 1 416 ? 9.164   11.217  9.561   1.00 27.88  ? 445 PRO D CD  1 
ATOM   6702  N N   . LEU B 1 417 ? 11.435  7.768   11.199  1.00 24.68  ? 446 LEU D N   1 
ATOM   6703  C CA  . LEU B 1 417 ? 12.745  7.498   11.708  1.00 24.94  ? 446 LEU D CA  1 
ATOM   6704  C C   . LEU B 1 417 ? 13.759  8.421   11.036  1.00 26.78  ? 446 LEU D C   1 
ATOM   6705  O O   . LEU B 1 417 ? 13.706  8.599   9.829   1.00 27.18  ? 446 LEU D O   1 
ATOM   6706  C CB  . LEU B 1 417 ? 12.983  6.048   11.320  1.00 26.47  ? 446 LEU D CB  1 
ATOM   6707  C CG  . LEU B 1 417 ? 14.287  5.426   11.797  1.00 27.51  ? 446 LEU D CG  1 
ATOM   6708  C CD1 . LEU B 1 417 ? 14.207  5.006   13.245  1.00 28.42  ? 446 LEU D CD1 1 
ATOM   6709  C CD2 . LEU B 1 417 ? 14.559  4.222   10.924  1.00 33.44  ? 446 LEU D CD2 1 
ATOM   6710  N N   . GLU B 1 418 ? 14.694  8.961   11.824  1.00 21.79  ? 447 GLU D N   1 
ATOM   6711  C CA  . GLU B 1 418 ? 15.788  9.735   11.266  1.00 26.50  ? 447 GLU D CA  1 
ATOM   6712  C C   . GLU B 1 418 ? 16.830  8.727   10.779  1.00 28.00  ? 447 GLU D C   1 
ATOM   6713  O O   . GLU B 1 418 ? 17.289  7.881   11.525  1.00 26.66  ? 447 GLU D O   1 
ATOM   6714  C CB  . GLU B 1 418 ? 16.341  10.703  12.313  1.00 28.21  ? 447 GLU D CB  1 
ATOM   6715  C CG  . GLU B 1 418 ? 17.473  11.582  11.770  1.00 28.40  ? 447 GLU D CG  1 
ATOM   6716  C CD  . GLU B 1 418 ? 18.021  12.623  12.717  1.00 30.29  ? 447 GLU D CD  1 
ATOM   6717  O OE1 . GLU B 1 418 ? 17.195  13.474  13.165  1.00 31.29  ? 447 GLU D OE1 1 
ATOM   6718  O OE2 . GLU B 1 418 ? 19.264  12.629  13.002  1.00 34.03  ? 447 GLU D OE2 1 
ATOM   6719  N N   . ARG B 1 419 ? 17.123  8.755   9.487   1.00 29.40  ? 448 ARG D N   1 
ATOM   6720  C CA  . ARG B 1 419 ? 17.961  7.734   8.866   1.00 29.54  ? 448 ARG D CA  1 
ATOM   6721  C C   . ARG B 1 419 ? 18.648  8.345   7.647   1.00 29.99  ? 448 ARG D C   1 
ATOM   6722  O O   . ARG B 1 419 ? 18.193  8.149   6.535   1.00 35.30  ? 448 ARG D O   1 
ATOM   6723  C CB  . ARG B 1 419 ? 17.153  6.471   8.558   1.00 30.88  ? 448 ARG D CB  1 
ATOM   6724  C CG  . ARG B 1 419 ? 17.782  5.349   7.736   1.00 33.94  ? 448 ARG D CG  1 
ATOM   6725  C CD  . ARG B 1 419 ? 19.250  5.118   8.040   1.00 39.01  ? 448 ARG D CD  1 
ATOM   6726  N NE  . ARG B 1 419 ? 19.910  3.837   7.728   1.00 33.81  ? 448 ARG D NE  1 
ATOM   6727  C CZ  . ARG B 1 419 ? 21.164  3.701   7.275   1.00 38.53  ? 448 ARG D CZ  1 
ATOM   6728  N NH1 . ARG B 1 419 ? 21.722  4.687   6.590   1.00 35.70  ? 448 ARG D NH1 1 
ATOM   6729  N NH2 . ARG B 1 419 ? 21.845  2.566   7.436   1.00 33.89  ? 448 ARG D NH2 1 
ATOM   6730  N N   . PRO B 1 420 ? 19.709  9.168   7.815   1.00 26.52  ? 449 PRO D N   1 
ATOM   6731  C CA  . PRO B 1 420 ? 20.420  9.766   6.686   1.00 28.36  ? 449 PRO D CA  1 
ATOM   6732  C C   . PRO B 1 420 ? 21.340  8.700   6.117   1.00 27.17  ? 449 PRO D C   1 
ATOM   6733  O O   . PRO B 1 420 ? 21.439  7.614   6.666   1.00 22.54  ? 449 PRO D O   1 
ATOM   6734  C CB  . PRO B 1 420 ? 21.196  10.925  7.285   1.00 25.53  ? 449 PRO D CB  1 
ATOM   6735  C CG  . PRO B 1 420 ? 21.479  10.398  8.670   1.00 28.24  ? 449 PRO D CG  1 
ATOM   6736  C CD  . PRO B 1 420 ? 20.205  9.684   9.090   1.00 26.04  ? 449 PRO D CD  1 
ATOM   6737  N N   . LYS B 1 421 ? 21.927  9.026   4.979   1.00 26.90  ? 450 LYS D N   1 
ATOM   6738  C CA  . LYS B 1 421 ? 22.893  8.160   4.318   1.00 29.69  ? 450 LYS D CA  1 
ATOM   6739  C C   . LYS B 1 421 ? 24.274  8.577   4.818   1.00 28.31  ? 450 LYS D C   1 
ATOM   6740  O O   . LYS B 1 421 ? 24.536  9.766   4.965   1.00 30.68  ? 450 LYS D O   1 
ATOM   6741  C CB  . LYS B 1 421 ? 22.763  8.413   2.806   1.00 30.86  ? 450 LYS D CB  1 
ATOM   6742  C CG  . LYS B 1 421 ? 23.547  7.459   1.895   1.00 36.11  ? 450 LYS D CG  1 
ATOM   6743  C CD  . LYS B 1 421 ? 23.242  5.979   2.097   1.00 46.04  ? 450 LYS D CD  1 
ATOM   6744  C CE  . LYS B 1 421 ? 23.833  5.075   1.027   1.00 57.52  ? 450 LYS D CE  1 
ATOM   6745  N NZ  . LYS B 1 421 ? 25.288  4.886   1.116   1.00 59.12  ? 450 LYS D NZ  1 
ATOM   6746  N N   . SER B 1 422 ? 25.149  7.609   5.084   1.00 28.07  ? 451 SER D N   1 
ATOM   6747  C CA  . SER B 1 422 ? 26.550  7.880   5.341   1.00 25.86  ? 451 SER D CA  1 
ATOM   6748  C C   . SER B 1 422 ? 27.392  7.444   4.142   1.00 26.42  ? 451 SER D C   1 
ATOM   6749  O O   . SER B 1 422 ? 26.936  6.659   3.335   1.00 30.36  ? 451 SER D O   1 
ATOM   6750  C CB  . SER B 1 422 ? 27.020  7.231   6.597   1.00 26.96  ? 451 SER D CB  1 
ATOM   6751  O OG  . SER B 1 422 ? 27.154  5.832   6.455   1.00 22.66  ? 451 SER D OG  1 
ATOM   6752  N N   . MET B 1 423 ? 28.609  7.994   4.043   1.00 30.51  ? 452 MET D N   1 
ATOM   6753  C CA  . MET B 1 423 ? 29.594  7.611   3.046   1.00 30.78  ? 452 MET D CA  1 
ATOM   6754  C C   . MET B 1 423 ? 30.950  7.514   3.722   1.00 27.69  ? 452 MET D C   1 
ATOM   6755  O O   . MET B 1 423 ? 31.199  8.224   4.680   1.00 33.91  ? 452 MET D O   1 
ATOM   6756  C CB  . MET B 1 423 ? 29.735  8.701   1.986   1.00 34.20  ? 452 MET D CB  1 
ATOM   6757  C CG  . MET B 1 423 ? 28.465  9.107   1.320   1.00 41.04  ? 452 MET D CG  1 
ATOM   6758  S SD  . MET B 1 423 ? 28.028  7.845   0.123   1.00 65.03  ? 452 MET D SD  1 
ATOM   6759  C CE  . MET B 1 423 ? 29.131  8.292   -1.228  1.00 68.56  ? 452 MET D CE  1 
ATOM   6760  N N   . SER B 1 424 ? 31.841  6.659   3.216   1.00 28.44  ? 453 SER D N   1 
ATOM   6761  C CA  . SER B 1 424 ? 33.218  6.641   3.667   1.00 28.83  ? 453 SER D CA  1 
ATOM   6762  C C   . SER B 1 424 ? 34.013  7.673   2.864   1.00 34.84  ? 453 SER D C   1 
ATOM   6763  O O   . SER B 1 424 ? 33.545  8.137   1.825   1.00 32.97  ? 453 SER D O   1 
ATOM   6764  C CB  . SER B 1 424 ? 33.833  5.280   3.498   1.00 36.72  ? 453 SER D CB  1 
ATOM   6765  O OG  . SER B 1 424 ? 33.933  4.950   2.111   1.00 35.31  ? 453 SER D OG  1 
ATOM   6766  N N   . THR B 1 425 ? 35.240  7.939   3.311   1.00 29.53  ? 454 THR D N   1 
ATOM   6767  C CA  . THR B 1 425 ? 36.180  8.763   2.571   1.00 35.94  ? 454 THR D CA  1 
ATOM   6768  C C   . THR B 1 425 ? 36.464  8.118   1.210   1.00 37.03  ? 454 THR D C   1 
ATOM   6769  O O   . THR B 1 425 ? 36.403  8.798   0.186   1.00 36.00  ? 454 THR D O   1 
ATOM   6770  C CB  . THR B 1 425 ? 37.455  9.023   3.381   1.00 35.40  ? 454 THR D CB  1 
ATOM   6771  O OG1 . THR B 1 425 ? 37.110  9.892   4.473   1.00 34.68  ? 454 THR D OG1 1 
ATOM   6772  C CG2 . THR B 1 425 ? 38.519  9.688   2.514   1.00 33.22  ? 454 THR D CG2 1 
ATOM   6773  N N   . GLU B 1 426 ? 36.693  6.812   1.181   1.00 35.48  ? 455 GLU D N   1 
ATOM   6774  C CA  . GLU B 1 426 ? 36.900  6.139   -0.096  1.00 48.52  ? 455 GLU D CA  1 
ATOM   6775  C C   . GLU B 1 426 ? 35.668  6.278   -1.004  1.00 50.03  ? 455 GLU D C   1 
ATOM   6776  O O   . GLU B 1 426 ? 35.781  6.644   -2.182  1.00 43.32  ? 455 GLU D O   1 
ATOM   6777  C CB  . GLU B 1 426 ? 37.291  4.669   0.052   1.00 57.24  ? 455 GLU D CB  1 
ATOM   6778  C CG  . GLU B 1 426 ? 37.822  4.083   -1.259  1.00 74.87  ? 455 GLU D CG  1 
ATOM   6779  C CD  . GLU B 1 426 ? 38.841  4.918   -2.059  1.00 82.25  ? 455 GLU D CD  1 
ATOM   6780  O OE1 . GLU B 1 426 ? 40.015  5.003   -1.609  1.00 76.51  ? 455 GLU D OE1 1 
ATOM   6781  O OE2 . GLU B 1 426 ? 38.477  5.505   -3.129  1.00 71.67  ? 455 GLU D OE2 1 
ATOM   6782  N N   . GLY B 1 427 ? 34.480  6.006   -0.453  1.00 40.06  ? 456 GLY D N   1 
ATOM   6783  C CA  . GLY B 1 427 ? 33.245  6.179   -1.203  1.00 36.75  ? 456 GLY D CA  1 
ATOM   6784  C C   . GLY B 1 427 ? 33.085  7.588   -1.757  1.00 34.32  ? 456 GLY D C   1 
ATOM   6785  O O   . GLY B 1 427 ? 32.680  7.795   -2.892  1.00 39.72  ? 456 GLY D O   1 
ATOM   6786  N N   . LEU B 1 428 ? 33.443  8.592   -0.969  1.00 39.54  ? 457 LEU D N   1 
ATOM   6787  C CA  . LEU B 1 428 ? 33.159  9.960   -1.364  1.00 38.32  ? 457 LEU D CA  1 
ATOM   6788  C C   . LEU B 1 428 ? 34.187  10.444  -2.391  1.00 43.91  ? 457 LEU D C   1 
ATOM   6789  O O   . LEU B 1 428 ? 33.912  11.339  -3.204  1.00 45.54  ? 457 LEU D O   1 
ATOM   6790  C CB  . LEU B 1 428 ? 33.173  10.688  -0.024  1.00 38.45  ? 457 LEU D CB  1 
ATOM   6791  C CG  . LEU B 1 428 ? 32.381  11.983  0.082   1.00 40.07  ? 457 LEU D CG  1 
ATOM   6792  C CD1 . LEU B 1 428 ? 30.952  11.877  -0.423  1.00 36.56  ? 457 LEU D CD1 1 
ATOM   6793  C CD2 . LEU B 1 428 ? 32.439  12.411  1.541   1.00 39.14  ? 457 LEU D CD2 1 
ATOM   6794  N N   . MET B 1 429 ? 35.370  9.824   -2.374  1.00 42.76  ? 458 MET D N   1 
ATOM   6795  C CA  . MET B 1 429 ? 36.405  10.114  -3.354  1.00 49.47  ? 458 MET D CA  1 
ATOM   6796  C C   . MET B 1 429 ? 35.989  9.596   -4.722  1.00 53.00  ? 458 MET D C   1 
ATOM   6797  O O   . MET B 1 429 ? 36.206  10.266  -5.732  1.00 58.59  ? 458 MET D O   1 
ATOM   6798  C CB  . MET B 1 429 ? 37.731  9.444   -2.985  1.00 48.84  ? 458 MET D CB  1 
ATOM   6799  C CG  . MET B 1 429 ? 38.470  10.195  -1.924  1.00 57.14  ? 458 MET D CG  1 
ATOM   6800  S SD  . MET B 1 429 ? 39.895  9.271   -1.336  1.00 59.72  ? 458 MET D SD  1 
ATOM   6801  C CE  . MET B 1 429 ? 40.951  10.713  -1.176  1.00 59.95  ? 458 MET D CE  1 
ATOM   6802  N N   . LYS B 1 430 ? 35.455  8.373   -4.744  1.00 54.75  ? 459 LYS D N   1 
ATOM   6803  C CA  . LYS B 1 430 ? 34.885  7.822   -5.963  1.00 63.44  ? 459 LYS D CA  1 
ATOM   6804  C C   . LYS B 1 430 ? 33.689  8.669   -6.393  1.00 58.03  ? 459 LYS D C   1 
ATOM   6805  O O   . LYS B 1 430 ? 33.644  9.119   -7.529  1.00 56.68  ? 459 LYS D O   1 
ATOM   6806  C CB  . LYS B 1 430 ? 34.466  6.353   -5.829  1.00 71.26  ? 459 LYS D CB  1 
ATOM   6807  C CG  . LYS B 1 430 ? 35.607  5.338   -5.807  1.00 78.60  ? 459 LYS D CG  1 
ATOM   6808  C CD  . LYS B 1 430 ? 35.165  3.895   -6.036  1.00 88.15  ? 459 LYS D CD  1 
ATOM   6809  C CE  . LYS B 1 430 ? 34.042  3.473   -5.125  1.00 94.27  ? 459 LYS D CE  1 
ATOM   6810  N NZ  . LYS B 1 430 ? 33.724  2.045   -5.208  1.00 91.76  ? 459 LYS D NZ  1 
ATOM   6811  N N   . PHE B 1 431 ? 32.741  8.907   -5.478  1.00 54.10  ? 460 PHE D N   1 
ATOM   6812  C CA  . PHE B 1 431 ? 31.501  9.586   -5.811  1.00 54.79  ? 460 PHE D CA  1 
ATOM   6813  C C   . PHE B 1 431 ? 31.750  10.883  -6.565  1.00 60.64  ? 460 PHE D C   1 
ATOM   6814  O O   . PHE B 1 431 ? 30.883  11.317  -7.307  1.00 65.35  ? 460 PHE D O   1 
ATOM   6815  C CB  . PHE B 1 431 ? 30.716  9.954   -4.556  1.00 60.31  ? 460 PHE D CB  1 
ATOM   6816  C CG  . PHE B 1 431 ? 29.308  10.454  -4.835  1.00 59.38  ? 460 PHE D CG  1 
ATOM   6817  C CD1 . PHE B 1 431 ? 28.300  9.558   -5.182  1.00 63.17  ? 460 PHE D CD1 1 
ATOM   6818  C CD2 . PHE B 1 431 ? 28.991  11.799  -4.729  1.00 58.78  ? 460 PHE D CD2 1 
ATOM   6819  C CE1 . PHE B 1 431 ? 27.009  9.999   -5.426  1.00 66.97  ? 460 PHE D CE1 1 
ATOM   6820  C CE2 . PHE B 1 431 ? 27.699  12.237  -4.978  1.00 66.86  ? 460 PHE D CE2 1 
ATOM   6821  C CZ  . PHE B 1 431 ? 26.708  11.338  -5.317  1.00 67.16  ? 460 PHE D CZ  1 
ATOM   6822  N N   . VAL B 1 432 ? 32.918  11.502  -6.349  1.00 68.36  ? 461 VAL D N   1 
ATOM   6823  C CA  . VAL B 1 432 ? 33.253  12.801  -6.910  1.00 69.40  ? 461 VAL D CA  1 
ATOM   6824  C C   . VAL B 1 432 ? 34.146  12.678  -8.150  1.00 74.67  ? 461 VAL D C   1 
ATOM   6825  O O   . VAL B 1 432 ? 34.209  13.598  -8.963  1.00 73.88  ? 461 VAL D O   1 
ATOM   6826  C CB  . VAL B 1 432 ? 33.909  13.623  -5.783  1.00 72.08  ? 461 VAL D CB  1 
ATOM   6827  C CG1 . VAL B 1 432 ? 34.598  14.879  -6.301  1.00 71.91  ? 461 VAL D CG1 1 
ATOM   6828  C CG2 . VAL B 1 432 ? 32.901  13.965  -4.688  1.00 61.35  ? 461 VAL D CG2 1 
ATOM   6829  N N   . ASP B 1 433 ? 34.841  11.550  -8.316  1.00 87.81  ? 462 ASP D N   1 
ATOM   6830  C CA  . ASP B 1 433 ? 35.546  11.278  -9.564  1.00 95.41  ? 462 ASP D CA  1 
ATOM   6831  C C   . ASP B 1 433 ? 34.540  10.992  -10.685 1.00 95.48  ? 462 ASP D C   1 
ATOM   6832  O O   . ASP B 1 433 ? 34.745  11.435  -11.813 1.00 98.45  ? 462 ASP D O   1 
ATOM   6833  C CB  . ASP B 1 433 ? 36.620  10.213  -9.389  1.00 90.03  ? 462 ASP D CB  1 
ATOM   6834  C CG  . ASP B 1 433 ? 37.910  10.690  -8.731  1.00 91.77  ? 462 ASP D CG  1 
ATOM   6835  O OD1 . ASP B 1 433 ? 37.952  11.856  -8.254  1.00 88.85  ? 462 ASP D OD1 1 
ATOM   6836  O OD2 . ASP B 1 433 ? 38.876  9.900   -8.715  1.00 84.83  ? 462 ASP D OD2 1 
ATOM   6837  N N   . SER B 1 434 ? 33.458  10.263  -10.369 1.00 95.34  ? 463 SER D N   1 
ATOM   6838  C CA  . SER B 1 434 ? 32.322  10.116  -11.271 1.00 90.96  ? 463 SER D CA  1 
ATOM   6839  C C   . SER B 1 434 ? 31.546  11.432  -11.322 1.00 94.35  ? 463 SER D C   1 
ATOM   6840  O O   . SER B 1 434 ? 31.837  12.350  -10.557 1.00 105.89 ? 463 SER D O   1 
ATOM   6841  C CB  . SER B 1 434 ? 31.436  8.959   -10.863 1.00 84.26  ? 463 SER D CB  1 
ATOM   6842  O OG  . SER B 1 434 ? 30.867  9.154   -9.575  1.00 76.13  ? 463 SER D OG  1 
ATOM   6843  N N   . LYS B 1 435 ? 30.574  11.530  -12.239 1.00 97.68  ? 464 LYS D N   1 
ATOM   6844  C CA  . LYS B 1 435 ? 29.776  12.740  -12.397 1.00 102.27 ? 464 LYS D CA  1 
ATOM   6845  C C   . LYS B 1 435 ? 30.681  13.991  -12.365 1.00 100.25 ? 464 LYS D C   1 
ATOM   6846  O O   . LYS B 1 435 ? 31.422  14.220  -13.347 1.00 86.73  ? 464 LYS D O   1 
ATOM   6847  C CB  . LYS B 1 435 ? 28.729  12.889  -11.281 1.00 106.58 ? 464 LYS D CB  1 
ATOM   6848  C CG  . LYS B 1 435 ? 27.614  11.852  -11.220 1.00 103.17 ? 464 LYS D CG  1 
ATOM   6849  C CD  . LYS B 1 435 ? 26.672  12.085  -10.045 1.00 101.63 ? 464 LYS D CD  1 
ATOM   6850  C CE  . LYS B 1 435 ? 25.495  11.161  -10.036 1.00 98.69  ? 464 LYS D CE  1 
ATOM   6851  N NZ  . LYS B 1 435 ? 24.647  11.407  -8.866  1.00 94.43  ? 464 LYS D NZ  1 
ATOM   6852  N N   . SER C 1 1   ? 26.903  18.319  -33.702 1.00 70.33  ? 30  SER B N   1 
ATOM   6853  C CA  . SER C 1 1   ? 27.191  17.179  -32.793 1.00 83.26  ? 30  SER B CA  1 
ATOM   6854  C C   . SER C 1 1   ? 25.892  16.679  -32.174 1.00 91.39  ? 30  SER B C   1 
ATOM   6855  O O   . SER C 1 1   ? 24.871  17.350  -32.267 1.00 103.43 ? 30  SER B O   1 
ATOM   6856  C CB  . SER C 1 1   ? 28.183  17.578  -31.742 1.00 92.75  ? 30  SER B CB  1 
ATOM   6857  O OG  . SER C 1 1   ? 27.736  18.753  -31.086 1.00 88.80  ? 30  SER B OG  1 
ATOM   6858  N N   . THR C 1 2   ? 25.929  15.519  -31.512 1.00 87.42  ? 31  THR B N   1 
ATOM   6859  C CA  . THR C 1 2   ? 24.688  14.843  -31.156 1.00 87.26  ? 31  THR B CA  1 
ATOM   6860  C C   . THR C 1 2   ? 23.729  15.763  -30.387 1.00 67.36  ? 31  THR B C   1 
ATOM   6861  O O   . THR C 1 2   ? 22.566  15.378  -30.243 1.00 70.05  ? 31  THR B O   1 
ATOM   6862  C CB  . THR C 1 2   ? 24.958  13.549  -30.374 1.00 96.66  ? 31  THR B CB  1 
ATOM   6863  O OG1 . THR C 1 2   ? 23.711  12.854  -30.298 1.00 86.17  ? 31  THR B OG1 1 
ATOM   6864  C CG2 . THR C 1 2   ? 25.545  13.786  -28.989 1.00 93.09  ? 31  THR B CG2 1 
ATOM   6865  N N   . ASN C 1 3   ? 24.191  16.917  -29.847 1.00 47.60  ? 32  ASN B N   1 
ATOM   6866  C CA  . ASN C 1 3   ? 23.310  17.759  -29.034 1.00 39.17  ? 32  ASN B CA  1 
ATOM   6867  C C   . ASN C 1 3   ? 22.421  18.581  -29.964 1.00 28.42  ? 32  ASN B C   1 
ATOM   6868  O O   . ASN C 1 3   ? 22.899  19.352  -30.777 1.00 26.95  ? 32  ASN B O   1 
ATOM   6869  C CB  . ASN C 1 3   ? 24.018  18.633  -28.001 1.00 37.52  ? 32  ASN B CB  1 
ATOM   6870  C CG  . ASN C 1 3   ? 23.066  19.124  -26.922 1.00 44.00  ? 32  ASN B CG  1 
ATOM   6871  O OD1 . ASN C 1 3   ? 21.970  19.645  -27.194 1.00 34.58  ? 32  ASN B OD1 1 
ATOM   6872  N ND2 . ASN C 1 3   ? 23.413  18.868  -25.670 1.00 49.58  ? 32  ASN B ND2 1 
ATOM   6873  N N   . LEU C 1 4   ? 21.108  18.393  -29.824 1.00 30.56  ? 33  LEU B N   1 
ATOM   6874  C CA  . LEU C 1 4   ? 20.128  19.046  -30.666 1.00 28.06  ? 33  LEU B CA  1 
ATOM   6875  C C   . LEU C 1 4   ? 20.318  20.543  -30.551 1.00 26.79  ? 33  LEU B C   1 
ATOM   6876  O O   . LEU C 1 4   ? 20.141  21.251  -31.533 1.00 28.81  ? 33  LEU B O   1 
ATOM   6877  C CB  . LEU C 1 4   ? 18.721  18.614  -30.243 1.00 30.80  ? 33  LEU B CB  1 
ATOM   6878  C CG  . LEU C 1 4   ? 17.555  19.291  -30.974 1.00 29.80  ? 33  LEU B CG  1 
ATOM   6879  C CD1 . LEU C 1 4   ? 17.633  19.126  -32.488 1.00 28.69  ? 33  LEU B CD1 1 
ATOM   6880  C CD2 . LEU C 1 4   ? 16.273  18.721  -30.467 1.00 30.90  ? 33  LEU B CD2 1 
ATOM   6881  N N   . LYS C 1 5   ? 20.719  21.026  -29.375 1.00 28.05  ? 34  LYS B N   1 
ATOM   6882  C CA  . LYS C 1 5   ? 20.834  22.464  -29.156 1.00 31.81  ? 34  LYS B CA  1 
ATOM   6883  C C   . LYS C 1 5   ? 21.986  23.105  -29.972 1.00 33.53  ? 34  LYS B C   1 
ATOM   6884  O O   . LYS C 1 5   ? 21.852  24.221  -30.494 1.00 31.17  ? 34  LYS B O   1 
ATOM   6885  C CB  . LYS C 1 5   ? 20.900  22.739  -27.647 1.00 31.35  ? 34  LYS B CB  1 
ATOM   6886  C CG  . LYS C 1 5   ? 20.575  24.165  -27.253 1.00 31.13  ? 34  LYS B CG  1 
ATOM   6887  C CD  . LYS C 1 5   ? 20.658  24.390  -25.746 1.00 34.97  ? 34  LYS B CD  1 
ATOM   6888  C CE  . LYS C 1 5   ? 20.399  25.801  -25.400 1.00 33.99  ? 34  LYS B CE  1 
ATOM   6889  N NZ  . LYS C 1 5   ? 20.817  26.162  -24.057 1.00 33.64  ? 34  LYS B NZ  1 
ATOM   6890  N N   . ASP C 1 6   ? 23.112  22.401  -30.104 1.00 32.73  ? 35  ASP B N   1 
ATOM   6891  C CA  . ASP C 1 6   ? 24.246  22.844  -30.907 1.00 34.10  ? 35  ASP B CA  1 
ATOM   6892  C C   . ASP C 1 6   ? 23.962  22.704  -32.399 1.00 32.64  ? 35  ASP B C   1 
ATOM   6893  O O   . ASP C 1 6   ? 24.312  23.586  -33.173 1.00 30.16  ? 35  ASP B O   1 
ATOM   6894  C CB  . ASP C 1 6   ? 25.493  22.100  -30.477 1.00 40.41  ? 35  ASP B CB  1 
ATOM   6895  C CG  . ASP C 1 6   ? 25.771  22.194  -28.982 1.00 44.85  ? 35  ASP B CG  1 
ATOM   6896  O OD1 . ASP C 1 6   ? 25.843  23.343  -28.464 1.00 55.31  ? 35  ASP B OD1 1 
ATOM   6897  O OD2 . ASP C 1 6   ? 25.879  21.127  -28.343 1.00 48.65  ? 35  ASP B OD2 1 
ATOM   6898  N N   . ILE C 1 7   ? 23.248  21.644  -32.802 1.00 32.39  ? 36  ILE B N   1 
ATOM   6899  C CA  . ILE C 1 7   ? 22.815  21.531  -34.189 1.00 34.64  ? 36  ILE B CA  1 
ATOM   6900  C C   . ILE C 1 7   ? 21.870  22.687  -34.542 1.00 34.88  ? 36  ILE B C   1 
ATOM   6901  O O   . ILE C 1 7   ? 21.990  23.333  -35.577 1.00 32.42  ? 36  ILE B O   1 
ATOM   6902  C CB  . ILE C 1 7   ? 22.208  20.143  -34.433 1.00 39.60  ? 36  ILE B CB  1 
ATOM   6903  C CG1 . ILE C 1 7   ? 23.322  19.057  -34.368 1.00 39.62  ? 36  ILE B CG1 1 
ATOM   6904  C CG2 . ILE C 1 7   ? 21.458  20.119  -35.762 1.00 43.50  ? 36  ILE B CG2 1 
ATOM   6905  C CD1 . ILE C 1 7   ? 22.825  17.639  -34.130 1.00 38.90  ? 36  ILE B CD1 1 
ATOM   6906  N N   . LEU C 1 8   ? 20.942  22.997  -33.641 1.00 31.48  ? 37  LEU B N   1 
ATOM   6907  C CA  . LEU C 1 8   ? 20.013  24.079  -33.872 1.00 32.04  ? 37  LEU B CA  1 
ATOM   6908  C C   . LEU C 1 8   ? 20.757  25.410  -33.963 1.00 28.60  ? 37  LEU B C   1 
ATOM   6909  O O   . LEU C 1 8   ? 20.507  26.216  -34.850 1.00 35.61  ? 37  LEU B O   1 
ATOM   6910  C CB  . LEU C 1 8   ? 19.039  23.995  -32.705 1.00 39.27  ? 37  LEU B CB  1 
ATOM   6911  C CG  . LEU C 1 8   ? 17.611  24.438  -32.963 1.00 42.37  ? 37  LEU B CG  1 
ATOM   6912  C CD1 . LEU C 1 8   ? 17.077  23.629  -34.115 1.00 48.01  ? 37  LEU B CD1 1 
ATOM   6913  C CD2 . LEU C 1 8   ? 16.794  24.244  -31.692 1.00 42.94  ? 37  LEU B CD2 1 
ATOM   6914  N N   . ALA C 1 9   ? 21.707  25.631  -33.050 1.00 29.09  ? 38  ALA B N   1 
ATOM   6915  C CA  . ALA C 1 9   ? 22.562  26.804  -33.052 1.00 32.07  ? 38  ALA B CA  1 
ATOM   6916  C C   . ALA C 1 9   ? 23.232  27.035  -34.412 1.00 32.39  ? 38  ALA B C   1 
ATOM   6917  O O   . ALA C 1 9   ? 23.244  28.160  -34.890 1.00 27.38  ? 38  ALA B O   1 
ATOM   6918  C CB  . ALA C 1 9   ? 23.569  26.682  -31.911 1.00 30.93  ? 38  ALA B CB  1 
ATOM   6919  N N   . ASP C 1 10  ? 23.778  25.973  -35.042 1.00 28.90  ? 39  ASP B N   1 
ATOM   6920  C CA  . ASP C 1 10  ? 24.425  26.114  -36.332 1.00 31.77  ? 39  ASP B CA  1 
ATOM   6921  C C   . ASP C 1 10  ? 23.419  26.435  -37.440 1.00 33.09  ? 39  ASP B C   1 
ATOM   6922  O O   . ASP C 1 10  ? 23.761  27.104  -38.411 1.00 34.88  ? 39  ASP B O   1 
ATOM   6923  C CB  . ASP C 1 10  ? 25.213  24.851  -36.645 1.00 36.16  ? 39  ASP B CB  1 
ATOM   6924  C CG  . ASP C 1 10  ? 26.442  24.568  -35.787 1.00 44.46  ? 39  ASP B CG  1 
ATOM   6925  O OD1 . ASP C 1 10  ? 26.853  25.441  -34.982 1.00 45.64  ? 39  ASP B OD1 1 
ATOM   6926  O OD2 . ASP C 1 10  ? 26.975  23.456  -35.910 1.00 53.05  ? 39  ASP B OD2 1 
ATOM   6927  N N   . LEU C 1 11  ? 22.192  25.889  -37.368 1.00 30.89  ? 40  LEU B N   1 
ATOM   6928  C CA  . LEU C 1 11  ? 21.208  26.078  -38.424 1.00 29.18  ? 40  LEU B CA  1 
ATOM   6929  C C   . LEU C 1 11  ? 20.647  27.490  -38.388 1.00 30.95  ? 40  LEU B C   1 
ATOM   6930  O O   . LEU C 1 11  ? 20.283  28.024  -39.426 1.00 30.63  ? 40  LEU B O   1 
ATOM   6931  C CB  . LEU C 1 11  ? 20.019  25.115  -38.347 1.00 32.66  ? 40  LEU B CB  1 
ATOM   6932  C CG  . LEU C 1 11  ? 20.319  23.637  -38.565 1.00 43.32  ? 40  LEU B CG  1 
ATOM   6933  C CD1 . LEU C 1 11  ? 19.068  22.805  -38.314 1.00 46.91  ? 40  LEU B CD1 1 
ATOM   6934  C CD2 . LEU C 1 11  ? 20.866  23.415  -39.973 1.00 42.07  ? 40  LEU B CD2 1 
ATOM   6935  N N   . ILE C 1 12  ? 20.457  28.068  -37.200 1.00 27.40  ? 41  ILE B N   1 
ATOM   6936  C CA  . ILE C 1 12  ? 19.637  29.269  -37.141 1.00 26.68  ? 41  ILE B CA  1 
ATOM   6937  C C   . ILE C 1 12  ? 20.204  30.404  -37.996 1.00 26.37  ? 41  ILE B C   1 
ATOM   6938  O O   . ILE C 1 12  ? 19.435  31.011  -38.742 1.00 32.78  ? 41  ILE B O   1 
ATOM   6939  C CB  . ILE C 1 12  ? 19.412  29.674  -35.683 1.00 29.56  ? 41  ILE B CB  1 
ATOM   6940  C CG1 . ILE C 1 12  ? 18.350  28.766  -35.019 1.00 31.83  ? 41  ILE B CG1 1 
ATOM   6941  C CG2 . ILE C 1 12  ? 19.061  31.149  -35.552 1.00 30.64  ? 41  ILE B CG2 1 
ATOM   6942  C CD1 . ILE C 1 12  ? 18.532  28.669  -33.504 1.00 33.03  ? 41  ILE B CD1 1 
ATOM   6943  N N   . PRO C 1 13  ? 21.519  30.744  -37.926 1.00 30.74  ? 42  PRO B N   1 
ATOM   6944  C CA  . PRO C 1 13  ? 22.088  31.856  -38.705 1.00 31.08  ? 42  PRO B CA  1 
ATOM   6945  C C   . PRO C 1 13  ? 21.903  31.767  -40.217 1.00 31.49  ? 42  PRO B C   1 
ATOM   6946  O O   . PRO C 1 13  ? 21.694  32.784  -40.870 1.00 37.11  ? 42  PRO B O   1 
ATOM   6947  C CB  . PRO C 1 13  ? 23.615  31.910  -38.317 1.00 30.38  ? 42  PRO B CB  1 
ATOM   6948  C CG  . PRO C 1 13  ? 23.752  31.025  -37.112 1.00 30.12  ? 42  PRO B CG  1 
ATOM   6949  C CD  . PRO C 1 13  ? 22.497  30.198  -36.959 1.00 28.68  ? 42  PRO B CD  1 
ATOM   6950  N N   . LYS C 1 14  ? 22.036  30.558  -40.775 1.00 36.50  ? 43  LYS B N   1 
ATOM   6951  C CA  . LYS C 1 14  ? 21.765  30.323  -42.182 1.00 37.64  ? 43  LYS B CA  1 
ATOM   6952  C C   . LYS C 1 14  ? 20.301  30.636  -42.501 1.00 40.56  ? 43  LYS B C   1 
ATOM   6953  O O   . LYS C 1 14  ? 20.011  31.215  -43.534 1.00 34.52  ? 43  LYS B O   1 
ATOM   6954  C CB  . LYS C 1 14  ? 21.950  28.851  -42.569 1.00 44.86  ? 43  LYS B CB  1 
ATOM   6955  C CG  . LYS C 1 14  ? 23.107  28.108  -41.911 1.00 48.18  ? 43  LYS B CG  1 
ATOM   6956  C CD  . LYS C 1 14  ? 23.065  26.611  -42.214 1.00 58.27  ? 43  LYS B CD  1 
ATOM   6957  C CE  . LYS C 1 14  ? 24.081  26.169  -43.200 1.00 58.89  ? 43  LYS B CE  1 
ATOM   6958  N NZ  . LYS C 1 14  ? 25.394  26.215  -42.545 1.00 61.81  ? 43  LYS B NZ  1 
ATOM   6959  N N   . GLU C 1 15  ? 19.354  30.235  -41.636 1.00 36.48  ? 44  GLU B N   1 
ATOM   6960  C CA  . GLU C 1 15  ? 17.945  30.502  -41.915 1.00 35.18  ? 44  GLU B CA  1 
ATOM   6961  C C   . GLU C 1 15  ? 17.613  31.997  -41.747 1.00 34.78  ? 44  GLU B C   1 
ATOM   6962  O O   . GLU C 1 15  ? 16.815  32.577  -42.493 1.00 33.01  ? 44  GLU B O   1 
ATOM   6963  C CB  . GLU C 1 15  ? 17.132  29.543  -41.044 1.00 41.24  ? 44  GLU B CB  1 
ATOM   6964  C CG  . GLU C 1 15  ? 15.733  29.246  -41.567 1.00 53.29  ? 44  GLU B CG  1 
ATOM   6965  C CD  . GLU C 1 15  ? 15.666  28.819  -43.028 1.00 59.20  ? 44  GLU B CD  1 
ATOM   6966  O OE1 . GLU C 1 15  ? 16.478  27.948  -43.418 1.00 61.69  ? 44  GLU B OE1 1 
ATOM   6967  O OE2 . GLU C 1 15  ? 14.801  29.363  -43.760 1.00 67.94  ? 44  GLU B OE2 1 
ATOM   6968  N N   . GLN C 1 16  ? 18.258  32.654  -40.788 1.00 32.12  ? 45  GLN B N   1 
ATOM   6969  C CA  . GLN C 1 16  ? 18.154  34.095  -40.655 1.00 35.46  ? 45  GLN B CA  1 
ATOM   6970  C C   . GLN C 1 16  ? 18.619  34.806  -41.933 1.00 34.39  ? 45  GLN B C   1 
ATOM   6971  O O   . GLN C 1 16  ? 17.934  35.690  -42.387 1.00 32.46  ? 45  GLN B O   1 
ATOM   6972  C CB  . GLN C 1 16  ? 18.965  34.596  -39.462 1.00 36.50  ? 45  GLN B CB  1 
ATOM   6973  C CG  . GLN C 1 16  ? 18.471  34.076  -38.111 1.00 41.14  ? 45  GLN B CG  1 
ATOM   6974  C CD  . GLN C 1 16  ? 19.330  34.524  -36.952 1.00 36.37  ? 45  GLN B CD  1 
ATOM   6975  O OE1 . GLN C 1 16  ? 20.554  34.526  -37.044 1.00 36.79  ? 45  GLN B OE1 1 
ATOM   6976  N NE2 . GLN C 1 16  ? 18.711  34.864  -35.833 1.00 39.83  ? 45  GLN B NE2 1 
ATOM   6977  N N   . ALA C 1 17  ? 19.773  34.440  -42.498 1.00 38.36  ? 46  ALA B N   1 
ATOM   6978  C CA  . ALA C 1 17  ? 20.302  35.126  -43.674 1.00 45.57  ? 46  ALA B CA  1 
ATOM   6979  C C   . ALA C 1 17  ? 19.402  34.893  -44.888 1.00 41.02  ? 46  ALA B C   1 
ATOM   6980  O O   . ALA C 1 17  ? 19.165  35.820  -45.668 1.00 42.08  ? 46  ALA B O   1 
ATOM   6981  C CB  . ALA C 1 17  ? 21.728  34.685  -43.964 1.00 43.66  ? 46  ALA B CB  1 
ATOM   6982  N N   . ARG C 1 18  ? 18.929  33.653  -45.023 1.00 40.50  ? 47  ARG B N   1 
ATOM   6983  C CA  . ARG C 1 18  ? 18.045  33.232  -46.098 1.00 43.31  ? 47  ARG B CA  1 
ATOM   6984  C C   . ARG C 1 18  ? 16.790  34.102  -46.107 1.00 40.26  ? 47  ARG B C   1 
ATOM   6985  O O   . ARG C 1 18  ? 16.371  34.591  -47.156 1.00 38.28  ? 47  ARG B O   1 
ATOM   6986  C CB  . ARG C 1 18  ? 17.667  31.754  -45.963 1.00 47.61  ? 47  ARG B CB  1 
ATOM   6987  C CG  . ARG C 1 18  ? 17.723  30.994  -47.282 1.00 58.65  ? 47  ARG B CG  1 
ATOM   6988  C CD  . ARG C 1 18  ? 17.315  29.519  -47.244 1.00 66.45  ? 47  ARG B CD  1 
ATOM   6989  N NE  . ARG C 1 18  ? 15.918  29.293  -46.848 1.00 74.69  ? 47  ARG B NE  1 
ATOM   6990  C CZ  . ARG C 1 18  ? 15.215  28.160  -46.981 1.00 89.86  ? 47  ARG B CZ  1 
ATOM   6991  N NH1 . ARG C 1 18  ? 15.708  27.130  -47.650 1.00 87.56  ? 47  ARG B NH1 1 
ATOM   6992  N NH2 . ARG C 1 18  ? 13.996  28.068  -46.462 1.00 90.38  ? 47  ARG B NH2 1 
ATOM   6993  N N   . ILE C 1 19  ? 16.204  34.300  -44.925 1.00 34.88  ? 48  ILE B N   1 
ATOM   6994  C CA  . ILE C 1 19  ? 14.992  35.088  -44.794 1.00 35.52  ? 48  ILE B CA  1 
ATOM   6995  C C   . ILE C 1 19  ? 15.297  36.562  -44.981 1.00 35.39  ? 48  ILE B C   1 
ATOM   6996  O O   . ILE C 1 19  ? 14.441  37.290  -45.491 1.00 36.28  ? 48  ILE B O   1 
ATOM   6997  C CB  . ILE C 1 19  ? 14.314  34.832  -43.447 1.00 32.75  ? 48  ILE B CB  1 
ATOM   6998  C CG1 . ILE C 1 19  ? 13.741  33.424  -43.412 1.00 35.57  ? 48  ILE B CG1 1 
ATOM   6999  C CG2 . ILE C 1 19  ? 13.257  35.892  -43.120 1.00 31.65  ? 48  ILE B CG2 1 
ATOM   7000  C CD1 . ILE C 1 19  ? 13.592  32.843  -42.020 1.00 36.44  ? 48  ILE B CD1 1 
ATOM   7001  N N   . LYS C 1 20  ? 16.443  37.015  -44.460 1.00 36.90  ? 49  LYS B N   1 
ATOM   7002  C CA  . LYS C 1 20  ? 16.824  38.407  -44.619 1.00 39.50  ? 49  LYS B CA  1 
ATOM   7003  C C   . LYS C 1 20  ? 16.857  38.729  -46.113 1.00 41.57  ? 49  LYS B C   1 
ATOM   7004  O O   . LYS C 1 20  ? 16.240  39.691  -46.554 1.00 39.78  ? 49  LYS B O   1 
ATOM   7005  C CB  . LYS C 1 20  ? 18.169  38.718  -43.964 1.00 45.84  ? 49  LYS B CB  1 
ATOM   7006  C CG  . LYS C 1 20  ? 18.634  40.191  -44.034 1.00 48.68  ? 49  LYS B CG  1 
ATOM   7007  C CD  . LYS C 1 20  ? 19.945  40.389  -43.270 1.00 48.34  ? 49  LYS B CD  1 
ATOM   7008  C CE  . LYS C 1 20  ? 20.571  41.763  -43.345 1.00 52.35  ? 49  LYS B CE  1 
ATOM   7009  N NZ  . LYS C 1 20  ? 19.839  42.715  -42.503 1.00 53.53  ? 49  LYS B NZ  1 
ATOM   7010  N N   . THR C 1 21  ? 17.538  37.883  -46.892 1.00 44.60  ? 50  THR B N   1 
ATOM   7011  C CA  . THR C 1 21  ? 17.726  38.139  -48.313 1.00 51.85  ? 50  THR B CA  1 
ATOM   7012  C C   . THR C 1 21  ? 16.387  38.077  -49.060 1.00 52.91  ? 50  THR B C   1 
ATOM   7013  O O   . THR C 1 21  ? 16.120  38.907  -49.934 1.00 44.64  ? 50  THR B O   1 
ATOM   7014  C CB  . THR C 1 21  ? 18.739  37.133  -48.851 1.00 50.26  ? 50  THR B CB  1 
ATOM   7015  O OG1 . THR C 1 21  ? 19.895  37.474  -48.090 1.00 55.01  ? 50  THR B OG1 1 
ATOM   7016  C CG2 . THR C 1 21  ? 18.993  37.295  -50.337 1.00 59.68  ? 50  THR B CG2 1 
ATOM   7017  N N   . PHE C 1 22  ? 15.553  37.090  -48.696 1.00 43.68  ? 51  PHE B N   1 
ATOM   7018  C CA  . PHE C 1 22  ? 14.242  36.892  -49.292 1.00 38.55  ? 51  PHE B CA  1 
ATOM   7019  C C   . PHE C 1 22  ? 13.344  38.091  -49.034 1.00 36.13  ? 51  PHE B C   1 
ATOM   7020  O O   . PHE C 1 22  ? 12.691  38.589  -49.950 1.00 44.73  ? 51  PHE B O   1 
ATOM   7021  C CB  . PHE C 1 22  ? 13.598  35.631  -48.723 1.00 42.13  ? 51  PHE B CB  1 
ATOM   7022  C CG  . PHE C 1 22  ? 12.194  35.370  -49.227 1.00 38.81  ? 51  PHE B CG  1 
ATOM   7023  C CD1 . PHE C 1 22  ? 11.912  35.412  -50.585 1.00 46.35  ? 51  PHE B CD1 1 
ATOM   7024  C CD2 . PHE C 1 22  ? 11.161  35.107  -48.340 1.00 38.21  ? 51  PHE B CD2 1 
ATOM   7025  C CE1 . PHE C 1 22  ? 10.626  35.161  -51.040 1.00 52.83  ? 51  PHE B CE1 1 
ATOM   7026  C CE2 . PHE C 1 22  ? 9.879   34.849  -48.793 1.00 39.75  ? 51  PHE B CE2 1 
ATOM   7027  C CZ  . PHE C 1 22  ? 9.613   34.868  -50.146 1.00 47.42  ? 51  PHE B CZ  1 
ATOM   7028  N N   . ARG C 1 23  ? 13.335  38.607  -47.813 1.00 34.19  ? 52  ARG B N   1 
ATOM   7029  C CA  . ARG C 1 23  ? 12.453  39.726  -47.528 1.00 37.45  ? 52  ARG B CA  1 
ATOM   7030  C C   . ARG C 1 23  ? 12.945  40.999  -48.223 1.00 48.41  ? 52  ARG B C   1 
ATOM   7031  O O   . ARG C 1 23  ? 12.146  41.904  -48.477 1.00 40.51  ? 52  ARG B O   1 
ATOM   7032  C CB  . ARG C 1 23  ? 12.317  39.999  -46.033 1.00 36.58  ? 52  ARG B CB  1 
ATOM   7033  C CG  . ARG C 1 23  ? 11.560  38.873  -45.335 1.00 38.51  ? 52  ARG B CG  1 
ATOM   7034  C CD  . ARG C 1 23  ? 11.565  39.060  -43.865 1.00 33.50  ? 52  ARG B CD  1 
ATOM   7035  N NE  . ARG C 1 23  ? 10.721  40.204  -43.557 1.00 37.51  ? 52  ARG B NE  1 
ATOM   7036  C CZ  . ARG C 1 23  ? 10.514  40.659  -42.347 1.00 37.37  ? 52  ARG B CZ  1 
ATOM   7037  N NH1 . ARG C 1 23  ? 11.135  40.098  -41.333 1.00 38.30  ? 52  ARG B NH1 1 
ATOM   7038  N NH2 . ARG C 1 23  ? 9.692   41.670  -42.178 1.00 38.37  ? 52  ARG B NH2 1 
ATOM   7039  N N   . GLN C 1 24  ? 14.259  41.080  -48.495 1.00 53.15  ? 53  GLN B N   1 
ATOM   7040  C CA  . GLN C 1 24  ? 14.840  42.231  -49.187 1.00 58.49  ? 53  GLN B CA  1 
ATOM   7041  C C   . GLN C 1 24  ? 14.348  42.270  -50.636 1.00 50.09  ? 53  GLN B C   1 
ATOM   7042  O O   . GLN C 1 24  ? 13.745  43.240  -51.063 1.00 51.54  ? 53  GLN B O   1 
ATOM   7043  C CB  . GLN C 1 24  ? 16.371  42.183  -49.157 1.00 55.39  ? 53  GLN B CB  1 
ATOM   7044  C CG  . GLN C 1 24  ? 16.995  42.746  -47.885 1.00 55.10  ? 53  GLN B CG  1 
ATOM   7045  C CD  . GLN C 1 24  ? 18.488  42.508  -47.837 1.00 55.79  ? 53  GLN B CD  1 
ATOM   7046  O OE1 . GLN C 1 24  ? 19.046  41.746  -48.632 1.00 53.76  ? 53  GLN B OE1 1 
ATOM   7047  N NE2 . GLN C 1 24  ? 19.151  43.168  -46.906 1.00 60.35  ? 53  GLN B NE2 1 
ATOM   7048  N N   . GLN C 1 25  ? 14.585  41.179  -51.364 1.00 45.11  ? 54  GLN B N   1 
ATOM   7049  C CA  . GLN C 1 25  ? 14.046  40.993  -52.693 1.00 55.33  ? 54  GLN B CA  1 
ATOM   7050  C C   . GLN C 1 25  ? 12.515  41.128  -52.732 1.00 57.08  ? 54  GLN B C   1 
ATOM   7051  O O   . GLN C 1 25  ? 11.995  41.970  -53.463 1.00 56.36  ? 54  GLN B O   1 
ATOM   7052  C CB  . GLN C 1 25  ? 14.572  39.642  -53.166 1.00 62.34  ? 54  GLN B CB  1 
ATOM   7053  C CG  . GLN C 1 25  ? 14.557  39.476  -54.682 1.00 71.64  ? 54  GLN B CG  1 
ATOM   7054  C CD  . GLN C 1 25  ? 15.313  38.252  -55.157 1.00 79.64  ? 54  GLN B CD  1 
ATOM   7055  O OE1 . GLN C 1 25  ? 16.257  37.778  -54.508 1.00 84.73  ? 54  GLN B OE1 1 
ATOM   7056  N NE2 . GLN C 1 25  ? 14.928  37.753  -56.323 1.00 80.65  ? 54  GLN B NE2 1 
ATOM   7057  N N   . HIS C 1 26  ? 11.789  40.318  -51.948 1.00 49.43  ? 55  HIS B N   1 
ATOM   7058  C CA  . HIS C 1 26  ? 10.381  40.058  -52.205 1.00 50.66  ? 55  HIS B CA  1 
ATOM   7059  C C   . HIS C 1 26  ? 9.458   40.449  -51.041 1.00 51.60  ? 55  HIS B C   1 
ATOM   7060  O O   . HIS C 1 26  ? 8.293   40.045  -51.030 1.00 50.34  ? 55  HIS B O   1 
ATOM   7061  C CB  . HIS C 1 26  ? 10.183  38.584  -52.573 1.00 50.41  ? 55  HIS B CB  1 
ATOM   7062  C CG  . HIS C 1 26  ? 10.887  38.140  -53.813 1.00 61.00  ? 55  HIS B CG  1 
ATOM   7063  N ND1 . HIS C 1 26  ? 10.371  38.339  -55.078 1.00 67.51  ? 55  HIS B ND1 1 
ATOM   7064  C CD2 . HIS C 1 26  ? 12.049  37.502  -53.983 1.00 63.39  ? 55  HIS B CD2 1 
ATOM   7065  C CE1 . HIS C 1 26  ? 11.205  37.828  -55.973 1.00 69.56  ? 55  HIS B CE1 1 
ATOM   7066  N NE2 . HIS C 1 26  ? 12.233  37.319  -55.331 1.00 63.80  ? 55  HIS B NE2 1 
ATOM   7067  N N   . GLY C 1 27  ? 9.954   41.276  -50.109 1.00 43.70  ? 56  GLY B N   1 
ATOM   7068  C CA  . GLY C 1 27  ? 9.187   41.755  -48.973 1.00 40.31  ? 56  GLY B CA  1 
ATOM   7069  C C   . GLY C 1 27  ? 7.872   42.429  -49.380 1.00 47.77  ? 56  GLY B C   1 
ATOM   7070  O O   . GLY C 1 27  ? 6.872   42.377  -48.637 1.00 42.41  ? 56  GLY B O   1 
ATOM   7071  N N   . LYS C 1 28  ? 7.888   43.062  -50.562 1.00 45.86  ? 57  LYS B N   1 
ATOM   7072  C CA  . LYS C 1 28  ? 6.776   43.876  -51.035 1.00 50.32  ? 57  LYS B CA  1 
ATOM   7073  C C   . LYS C 1 28  ? 5.893   43.089  -52.007 1.00 39.69  ? 57  LYS B C   1 
ATOM   7074  O O   . LYS C 1 28  ? 4.857   43.588  -52.420 1.00 41.43  ? 57  LYS B O   1 
ATOM   7075  C CB  . LYS C 1 28  ? 7.311   45.135  -51.740 1.00 52.19  ? 57  LYS B CB  1 
ATOM   7076  C CG  . LYS C 1 28  ? 8.187   46.060  -50.894 1.00 60.48  ? 57  LYS B CG  1 
ATOM   7077  C CD  . LYS C 1 28  ? 7.449   47.029  -49.970 1.00 66.29  ? 57  LYS B CD  1 
ATOM   7078  C CE  . LYS C 1 28  ? 8.217   47.337  -48.714 1.00 69.80  ? 57  LYS B CE  1 
ATOM   7079  N NZ  . LYS C 1 28  ? 7.947   46.329  -47.675 1.00 69.78  ? 57  LYS B NZ  1 
ATOM   7080  N N   . THR C 1 29  ? 6.317   41.897  -52.424 1.00 36.29  ? 58  THR B N   1 
ATOM   7081  C CA  . THR C 1 29  ? 5.502   41.095  -53.316 1.00 36.92  ? 58  THR B CA  1 
ATOM   7082  C C   . THR C 1 29  ? 4.189   40.731  -52.626 1.00 40.86  ? 58  THR B C   1 
ATOM   7083  O O   . THR C 1 29  ? 4.173   40.304  -51.462 1.00 38.91  ? 58  THR B O   1 
ATOM   7084  C CB  . THR C 1 29  ? 6.267   39.851  -53.738 1.00 40.91  ? 58  THR B CB  1 
ATOM   7085  O OG1 . THR C 1 29  ? 7.600   40.278  -53.992 1.00 46.04  ? 58  THR B OG1 1 
ATOM   7086  C CG2 . THR C 1 29  ? 5.695   39.211  -54.986 1.00 45.72  ? 58  THR B CG2 1 
ATOM   7087  N N   . VAL C 1 30  ? 3.090   40.918  -53.368 1.00 38.68  ? 59  VAL B N   1 
ATOM   7088  C CA  . VAL C 1 30  ? 1.749   40.590  -52.919 1.00 38.97  ? 59  VAL B CA  1 
ATOM   7089  C C   . VAL C 1 30  ? 1.509   39.093  -53.140 1.00 39.94  ? 59  VAL B C   1 
ATOM   7090  O O   . VAL C 1 30  ? 1.738   38.574  -54.234 1.00 36.68  ? 59  VAL B O   1 
ATOM   7091  C CB  . VAL C 1 30  ? 0.740   41.481  -53.674 1.00 44.37  ? 59  VAL B CB  1 
ATOM   7092  C CG1 . VAL C 1 30  ? -0.714  41.121  -53.386 1.00 42.56  ? 59  VAL B CG1 1 
ATOM   7093  C CG2 . VAL C 1 30  ? 0.961   42.961  -53.372 1.00 40.57  ? 59  VAL B CG2 1 
ATOM   7094  N N   . VAL C 1 31  ? 1.089   38.394  -52.073 1.00 33.04  ? 60  VAL B N   1 
ATOM   7095  C CA  . VAL C 1 31  ? 0.850   36.975  -52.146 1.00 35.10  ? 60  VAL B CA  1 
ATOM   7096  C C   . VAL C 1 31  ? -0.645  36.687  -52.045 1.00 35.43  ? 60  VAL B C   1 
ATOM   7097  O O   . VAL C 1 31  ? -1.087  35.608  -52.396 1.00 37.39  ? 60  VAL B O   1 
ATOM   7098  C CB  . VAL C 1 31  ? 1.666   36.293  -51.037 1.00 39.23  ? 60  VAL B CB  1 
ATOM   7099  C CG1 . VAL C 1 31  ? 3.146   36.292  -51.396 1.00 42.87  ? 60  VAL B CG1 1 
ATOM   7100  C CG2 . VAL C 1 31  ? 1.447   36.964  -49.686 1.00 39.15  ? 60  VAL B CG2 1 
ATOM   7101  N N   . GLY C 1 32  ? -1.436  37.652  -51.595 1.00 35.53  ? 61  GLY B N   1 
ATOM   7102  C CA  . GLY C 1 32  ? -2.875  37.450  -51.534 1.00 39.40  ? 61  GLY B CA  1 
ATOM   7103  C C   . GLY C 1 32  ? -3.626  38.767  -51.343 1.00 37.54  ? 61  GLY B C   1 
ATOM   7104  O O   . GLY C 1 32  ? -3.027  39.845  -51.326 1.00 35.13  ? 61  GLY B O   1 
ATOM   7105  N N   . GLN C 1 33  ? -4.953  38.660  -51.241 1.00 37.49  ? 62  GLN B N   1 
ATOM   7106  C CA  . GLN C 1 33  ? -5.799  39.800  -50.959 1.00 35.60  ? 62  GLN B CA  1 
ATOM   7107  C C   . GLN C 1 33  ? -6.672  39.465  -49.766 1.00 34.98  ? 62  GLN B C   1 
ATOM   7108  O O   . GLN C 1 33  ? -6.939  38.304  -49.479 1.00 37.56  ? 62  GLN B O   1 
ATOM   7109  C CB  . GLN C 1 33  ? -6.760  40.173  -52.085 1.00 42.75  ? 62  GLN B CB  1 
ATOM   7110  C CG  . GLN C 1 33  ? -6.206  39.973  -53.486 1.00 50.31  ? 62  GLN B CG  1 
ATOM   7111  C CD  . GLN C 1 33  ? -5.522  41.203  -54.014 1.00 54.11  ? 62  GLN B CD  1 
ATOM   7112  O OE1 . GLN C 1 33  ? -6.144  42.255  -54.165 1.00 58.77  ? 62  GLN B OE1 1 
ATOM   7113  N NE2 . GLN C 1 33  ? -4.236  41.081  -54.302 1.00 61.26  ? 62  GLN B NE2 1 
ATOM   7114  N N   . ILE C 1 34  ? -7.143  40.516  -49.095 1.00 34.56  ? 63  ILE B N   1 
ATOM   7115  C CA  . ILE C 1 34  ? -8.136  40.369  -48.053 1.00 37.24  ? 63  ILE B CA  1 
ATOM   7116  C C   . ILE C 1 34  ? -9.483  40.862  -48.589 1.00 36.16  ? 63  ILE B C   1 
ATOM   7117  O O   . ILE C 1 34  ? -9.560  41.971  -49.106 1.00 34.64  ? 63  ILE B O   1 
ATOM   7118  C CB  . ILE C 1 34  ? -7.703  41.150  -46.801 1.00 34.54  ? 63  ILE B CB  1 
ATOM   7119  C CG1 . ILE C 1 34  ? -6.260  40.855  -46.430 1.00 40.25  ? 63  ILE B CG1 1 
ATOM   7120  C CG2 . ILE C 1 34  ? -8.652  40.832  -45.648 1.00 37.66  ? 63  ILE B CG2 1 
ATOM   7121  C CD1 . ILE C 1 34  ? -5.785  41.535  -45.152 1.00 41.30  ? 63  ILE B CD1 1 
ATOM   7122  N N   . THR C 1 35  ? -10.555 40.057  -48.431 1.00 33.93  ? 64  THR B N   1 
ATOM   7123  C CA  . THR C 1 35  ? -11.896 40.514  -48.766 1.00 29.95  ? 64  THR B CA  1 
ATOM   7124  C C   . THR C 1 35  ? -12.692 40.757  -47.492 1.00 30.40  ? 64  THR B C   1 
ATOM   7125  O O   . THR C 1 35  ? -12.362 40.223  -46.442 1.00 32.37  ? 64  THR B O   1 
ATOM   7126  C CB  . THR C 1 35  ? -12.630 39.532  -49.670 1.00 29.67  ? 64  THR B CB  1 
ATOM   7127  O OG1 . THR C 1 35  ? -12.740 38.300  -48.965 1.00 29.90  ? 64  THR B OG1 1 
ATOM   7128  C CG2 . THR C 1 35  ? -11.920 39.323  -50.995 1.00 34.58  ? 64  THR B CG2 1 
ATOM   7129  N N   . VAL C 1 36  ? -13.770 41.530  -47.604 1.00 29.89  ? 65  VAL B N   1 
ATOM   7130  C CA  . VAL C 1 36  ? -14.769 41.604  -46.547 1.00 31.63  ? 65  VAL B CA  1 
ATOM   7131  C C   . VAL C 1 36  ? -15.175 40.202  -46.067 1.00 31.26  ? 65  VAL B C   1 
ATOM   7132  O O   . VAL C 1 36  ? -15.195 39.950  -44.861 1.00 29.25  ? 65  VAL B O   1 
ATOM   7133  C CB  . VAL C 1 36  ? -15.979 42.418  -47.038 1.00 30.76  ? 65  VAL B CB  1 
ATOM   7134  C CG1 . VAL C 1 36  ? -17.133 42.392  -46.043 1.00 31.70  ? 65  VAL B CG1 1 
ATOM   7135  C CG2 . VAL C 1 36  ? -15.593 43.852  -47.335 1.00 31.63  ? 65  VAL B CG2 1 
ATOM   7136  N N   . ASP C 1 37  ? -15.466 39.288  -46.997 1.00 27.67  ? 66  ASP B N   1 
ATOM   7137  C CA  . ASP C 1 37  ? -15.864 37.928  -46.665 1.00 33.31  ? 66  ASP B CA  1 
ATOM   7138  C C   . ASP C 1 37  ? -14.818 37.164  -45.832 1.00 37.68  ? 66  ASP B C   1 
ATOM   7139  O O   . ASP C 1 37  ? -15.198 36.429  -44.922 1.00 31.68  ? 66  ASP B O   1 
ATOM   7140  C CB  . ASP C 1 37  ? -16.376 37.179  -47.893 1.00 37.16  ? 66  ASP B CB  1 
ATOM   7141  C CG  . ASP C 1 37  ? -17.877 37.365  -48.104 1.00 43.24  ? 66  ASP B CG  1 
ATOM   7142  O OD1 . ASP C 1 37  ? -18.503 37.983  -47.215 1.00 42.60  ? 66  ASP B OD1 1 
ATOM   7143  O OD2 . ASP C 1 37  ? -18.408 36.924  -49.146 1.00 49.09  ? 66  ASP B OD2 1 
ATOM   7144  N N   . MET C 1 38  ? -13.520 37.321  -46.120 1.00 35.92  ? 67  MET B N   1 
ATOM   7145  C CA  . MET C 1 38  ? -12.475 36.697  -45.323 1.00 37.58  ? 67  MET B CA  1 
ATOM   7146  C C   . MET C 1 38  ? -12.461 37.218  -43.894 1.00 33.01  ? 67  MET B C   1 
ATOM   7147  O O   . MET C 1 38  ? -12.064 36.514  -42.980 1.00 36.16  ? 67  MET B O   1 
ATOM   7148  C CB  . MET C 1 38  ? -11.085 36.999  -45.873 1.00 38.56  ? 67  MET B CB  1 
ATOM   7149  C CG  . MET C 1 38  ? -10.827 36.320  -47.168 1.00 44.54  ? 67  MET B CG  1 
ATOM   7150  S SD  . MET C 1 38  ? -9.165  36.766  -47.699 1.00 46.74  ? 67  MET B SD  1 
ATOM   7151  C CE  . MET C 1 38  ? -9.483  36.128  -49.353 1.00 48.26  ? 67  MET B CE  1 
ATOM   7152  N N   . MET C 1 39  ? -12.845 38.473  -43.719 1.00 31.28  ? 68  MET B N   1 
ATOM   7153  C CA  . MET C 1 39  ? -12.834 39.072  -42.399 1.00 31.41  ? 68  MET B CA  1 
ATOM   7154  C C   . MET C 1 39  ? -13.973 38.542  -41.540 1.00 30.54  ? 68  MET B C   1 
ATOM   7155  O O   . MET C 1 39  ? -13.765 38.339  -40.349 1.00 32.52  ? 68  MET B O   1 
ATOM   7156  C CB  . MET C 1 39  ? -12.929 40.585  -42.513 1.00 32.38  ? 68  MET B CB  1 
ATOM   7157  C CG  . MET C 1 39  ? -11.669 41.189  -43.093 1.00 42.05  ? 68  MET B CG  1 
ATOM   7158  S SD  . MET C 1 39  ? -11.749 42.980  -43.208 1.00 38.78  ? 68  MET B SD  1 
ATOM   7159  C CE  . MET C 1 39  ? -11.720 43.488  -41.484 1.00 42.05  ? 68  MET B CE  1 
ATOM   7160  N N   . TYR C 1 40  ? -15.152 38.345  -42.154 1.00 30.25  ? 69  TYR B N   1 
ATOM   7161  C CA  . TYR C 1 40  ? -16.297 37.755  -41.474 1.00 32.65  ? 69  TYR B CA  1 
ATOM   7162  C C   . TYR C 1 40  ? -16.143 36.242  -41.406 1.00 33.54  ? 69  TYR B C   1 
ATOM   7163  O O   . TYR C 1 40  ? -16.757 35.631  -40.538 1.00 41.94  ? 69  TYR B O   1 
ATOM   7164  C CB  . TYR C 1 40  ? -17.663 38.092  -42.088 1.00 29.61  ? 69  TYR B CB  1 
ATOM   7165  C CG  . TYR C 1 40  ? -18.046 39.533  -41.780 1.00 30.10  ? 69  TYR B CG  1 
ATOM   7166  C CD1 . TYR C 1 40  ? -18.633 39.895  -40.574 1.00 29.49  ? 69  TYR B CD1 1 
ATOM   7167  C CD2 . TYR C 1 40  ? -17.748 40.541  -42.692 1.00 31.24  ? 69  TYR B CD2 1 
ATOM   7168  C CE1 . TYR C 1 40  ? -18.927 41.219  -40.287 1.00 30.69  ? 69  TYR B CE1 1 
ATOM   7169  C CE2 . TYR C 1 40  ? -18.023 41.865  -42.417 1.00 28.32  ? 69  TYR B CE2 1 
ATOM   7170  C CZ  . TYR C 1 40  ? -18.630 42.199  -41.221 1.00 32.01  ? 69  TYR B CZ  1 
ATOM   7171  O OH  . TYR C 1 40  ? -18.885 43.525  -41.040 1.00 28.41  ? 69  TYR B OH  1 
ATOM   7172  N N   . GLY C 1 41  ? -15.345 35.653  -42.315 1.00 33.90  ? 70  GLY B N   1 
ATOM   7173  C CA  . GLY C 1 41  ? -15.237 34.208  -42.462 1.00 29.12  ? 70  GLY B CA  1 
ATOM   7174  C C   . GLY C 1 41  ? -14.008 33.649  -41.746 1.00 29.21  ? 70  GLY B C   1 
ATOM   7175  O O   . GLY C 1 41  ? -13.454 32.637  -42.167 1.00 32.48  ? 70  GLY B O   1 
ATOM   7176  N N   . GLY C 1 42  ? -13.598 34.320  -40.661 1.00 29.85  ? 71  GLY B N   1 
ATOM   7177  C CA  . GLY C 1 42  ? -12.470 33.906  -39.844 1.00 32.83  ? 71  GLY B CA  1 
ATOM   7178  C C   . GLY C 1 42  ? -11.215 33.611  -40.654 1.00 28.72  ? 71  GLY B C   1 
ATOM   7179  O O   . GLY C 1 42  ? -10.606 32.591  -40.452 1.00 28.63  ? 71  GLY B O   1 
ATOM   7180  N N   . MET C 1 43  ? -10.820 34.548  -41.510 1.00 29.02  ? 72  MET B N   1 
ATOM   7181  C CA  . MET C 1 43  ? -9.567  34.518  -42.250 1.00 28.60  ? 72  MET B CA  1 
ATOM   7182  C C   . MET C 1 43  ? -9.472  33.327  -43.215 1.00 31.15  ? 72  MET B C   1 
ATOM   7183  O O   . MET C 1 43  ? -8.380  32.926  -43.595 1.00 31.55  ? 72  MET B O   1 
ATOM   7184  C CB  . MET C 1 43  ? -8.387  34.482  -41.284 1.00 32.47  ? 72  MET B CB  1 
ATOM   7185  C CG  . MET C 1 43  ? -8.350  35.585  -40.240 1.00 33.55  ? 72  MET B CG  1 
ATOM   7186  S SD  . MET C 1 43  ? -6.854  35.480  -39.232 1.00 39.89  ? 72  MET B SD  1 
ATOM   7187  C CE  . MET C 1 43  ? -6.689  36.956  -38.209 1.00 44.11  ? 72  MET B CE  1 
ATOM   7188  N N   . ARG C 1 44  ? -10.593 32.705  -43.576 1.00 35.95  ? 73  ARG B N   1 
ATOM   7189  C CA  . ARG C 1 44  ? -10.547 31.505  -44.394 1.00 42.80  ? 73  ARG B CA  1 
ATOM   7190  C C   . ARG C 1 44  ? -9.827  31.874  -45.696 1.00 44.59  ? 73  ARG B C   1 
ATOM   7191  O O   . ARG C 1 44  ? -10.192 32.861  -46.331 1.00 38.54  ? 73  ARG B O   1 
ATOM   7192  C CB  . ARG C 1 44  ? -11.975 30.958  -44.537 1.00 48.85  ? 73  ARG B CB  1 
ATOM   7193  C CG  . ARG C 1 44  ? -12.295 30.257  -45.850 1.00 66.75  ? 73  ARG B CG  1 
ATOM   7194  C CD  . ARG C 1 44  ? -13.799 30.257  -46.232 1.00 78.25  ? 73  ARG B CD  1 
ATOM   7195  N NE  . ARG C 1 44  ? -14.548 31.525  -46.181 1.00 84.37  ? 73  ARG B NE  1 
ATOM   7196  C CZ  . ARG C 1 44  ? -14.312 32.683  -46.830 1.00 87.57  ? 73  ARG B CZ  1 
ATOM   7197  N NH1 . ARG C 1 44  ? -15.211 33.651  -46.753 1.00 82.51  ? 73  ARG B NH1 1 
ATOM   7198  N NH2 . ARG C 1 44  ? -13.220 32.881  -47.562 1.00 80.22  ? 73  ARG B NH2 1 
ATOM   7199  N N   . GLY C 1 45  ? -8.753  31.136  -46.032 1.00 42.05  ? 74  GLY B N   1 
ATOM   7200  C CA  . GLY C 1 45  ? -8.039  31.365  -47.276 1.00 43.01  ? 74  GLY B CA  1 
ATOM   7201  C C   . GLY C 1 45  ? -7.027  32.514  -47.197 1.00 39.95  ? 74  GLY B C   1 
ATOM   7202  O O   . GLY C 1 45  ? -6.281  32.747  -48.139 1.00 48.75  ? 74  GLY B O   1 
ATOM   7203  N N   . MET C 1 46  ? -6.955  33.224  -46.073 1.00 34.01  ? 75  MET B N   1 
ATOM   7204  C CA  . MET C 1 46  ? -6.074  34.365  -45.982 1.00 35.93  ? 75  MET B CA  1 
ATOM   7205  C C   . MET C 1 46  ? -4.680  33.872  -45.588 1.00 34.98  ? 75  MET B C   1 
ATOM   7206  O O   . MET C 1 46  ? -4.527  33.065  -44.665 1.00 33.69  ? 75  MET B O   1 
ATOM   7207  C CB  . MET C 1 46  ? -6.650  35.326  -44.940 1.00 39.51  ? 75  MET B CB  1 
ATOM   7208  C CG  . MET C 1 46  ? -6.121  36.744  -45.006 1.00 41.19  ? 75  MET B CG  1 
ATOM   7209  S SD  . MET C 1 46  ? -6.620  37.751  -43.585 1.00 45.00  ? 75  MET B SD  1 
ATOM   7210  C CE  . MET C 1 46  ? -5.419  37.017  -42.466 1.00 44.42  ? 75  MET B CE  1 
ATOM   7211  N N   . LYS C 1 47  ? -3.659  34.327  -46.310 1.00 30.94  ? 76  LYS B N   1 
ATOM   7212  C CA  . LYS C 1 47  ? -2.277  33.990  -45.990 1.00 39.45  ? 76  LYS B CA  1 
ATOM   7213  C C   . LYS C 1 47  ? -1.798  34.875  -44.835 1.00 43.01  ? 76  LYS B C   1 
ATOM   7214  O O   . LYS C 1 47  ? -1.526  36.061  -45.004 1.00 49.89  ? 76  LYS B O   1 
ATOM   7215  C CB  . LYS C 1 47  ? -1.370  34.098  -47.222 1.00 43.39  ? 76  LYS B CB  1 
ATOM   7216  C CG  . LYS C 1 47  ? -1.535  32.933  -48.214 1.00 46.30  ? 76  LYS B CG  1 
ATOM   7217  C CD  . LYS C 1 47  ? -0.832  33.175  -49.544 1.00 52.15  ? 76  LYS B CD  1 
ATOM   7218  C CE  . LYS C 1 47  ? -1.003  32.043  -50.519 1.00 58.77  ? 76  LYS B CE  1 
ATOM   7219  N NZ  . LYS C 1 47  ? -0.579  30.756  -49.954 1.00 62.79  ? 76  LYS B NZ  1 
ATOM   7220  N N   . GLY C 1 48  ? -1.710  34.270  -43.648 1.00 40.85  ? 77  GLY B N   1 
ATOM   7221  C CA  . GLY C 1 48  ? -1.680  35.031  -42.422 1.00 37.33  ? 77  GLY B CA  1 
ATOM   7222  C C   . GLY C 1 48  ? -0.307  35.024  -41.756 1.00 35.28  ? 77  GLY B C   1 
ATOM   7223  O O   . GLY C 1 48  ? 0.031   35.958  -41.017 1.00 34.75  ? 77  GLY B O   1 
ATOM   7224  N N   . LEU C 1 49  ? 0.444   33.936  -41.926 1.00 27.87  ? 78  LEU B N   1 
ATOM   7225  C CA  . LEU C 1 49  ? 1.611   33.763  -41.083 1.00 30.12  ? 78  LEU B CA  1 
ATOM   7226  C C   . LEU C 1 49  ? 2.542   32.749  -41.711 1.00 26.53  ? 78  LEU B C   1 
ATOM   7227  O O   . LEU C 1 49  ? 2.137   31.961  -42.559 1.00 24.36  ? 78  LEU B O   1 
ATOM   7228  C CB  . LEU C 1 49  ? 1.240   33.319  -39.669 1.00 37.74  ? 78  LEU B CB  1 
ATOM   7229  C CG  . LEU C 1 49  ? 0.680   31.902  -39.515 1.00 39.08  ? 78  LEU B CG  1 
ATOM   7230  C CD1 . LEU C 1 49  ? 0.779   31.455  -38.060 1.00 41.83  ? 78  LEU B CD1 1 
ATOM   7231  C CD2 . LEU C 1 49  ? -0.741  31.801  -39.984 1.00 44.08  ? 78  LEU B CD2 1 
ATOM   7232  N N   . VAL C 1 50  ? 3.781   32.868  -41.260 1.00 27.57  ? 79  VAL B N   1 
ATOM   7233  C CA  . VAL C 1 50  ? 4.865   31.994  -41.609 1.00 27.51  ? 79  VAL B CA  1 
ATOM   7234  C C   . VAL C 1 50  ? 5.005   31.023  -40.455 1.00 27.73  ? 79  VAL B C   1 
ATOM   7235  O O   . VAL C 1 50  ? 5.073   31.397  -39.291 1.00 24.13  ? 79  VAL B O   1 
ATOM   7236  C CB  . VAL C 1 50  ? 6.156   32.798  -41.842 1.00 27.86  ? 79  VAL B CB  1 
ATOM   7237  C CG1 . VAL C 1 50  ? 7.313   31.878  -42.202 1.00 31.27  ? 79  VAL B CG1 1 
ATOM   7238  C CG2 . VAL C 1 50  ? 5.944   33.874  -42.926 1.00 28.05  ? 79  VAL B CG2 1 
ATOM   7239  N N   . TYR C 1 51  ? 5.016   29.767  -40.832 1.00 27.95  ? 80  TYR B N   1 
ATOM   7240  C CA  . TYR C 1 51  ? 5.128   28.675  -39.896 1.00 29.53  ? 80  TYR B CA  1 
ATOM   7241  C C   . TYR C 1 51  ? 5.963   27.618  -40.606 1.00 30.40  ? 80  TYR B C   1 
ATOM   7242  O O   . TYR C 1 51  ? 5.574   27.161  -41.695 1.00 33.15  ? 80  TYR B O   1 
ATOM   7243  C CB  . TYR C 1 51  ? 3.678   28.309  -39.589 1.00 24.52  ? 80  TYR B CB  1 
ATOM   7244  C CG  . TYR C 1 51  ? 3.477   27.365  -38.422 1.00 23.99  ? 80  TYR B CG  1 
ATOM   7245  C CD1 . TYR C 1 51  ? 3.602   26.011  -38.598 1.00 24.67  ? 80  TYR B CD1 1 
ATOM   7246  C CD2 . TYR C 1 51  ? 3.136   27.839  -37.171 1.00 25.71  ? 80  TYR B CD2 1 
ATOM   7247  C CE1 . TYR C 1 51  ? 3.436   25.138  -37.538 1.00 33.86  ? 80  TYR B CE1 1 
ATOM   7248  C CE2 . TYR C 1 51  ? 2.955   26.971  -36.110 1.00 29.36  ? 80  TYR B CE2 1 
ATOM   7249  C CZ  . TYR C 1 51  ? 3.098   25.612  -36.291 1.00 29.83  ? 80  TYR B CZ  1 
ATOM   7250  O OH  . TYR C 1 51  ? 2.892   24.706  -35.263 1.00 40.15  ? 80  TYR B OH  1 
ATOM   7251  N N   . GLU C 1 52  ? 7.126   27.326  -40.033 1.00 31.61  ? 81  GLU B N   1 
ATOM   7252  C CA  . GLU C 1 52  ? 8.187   26.635  -40.755 1.00 32.62  ? 81  GLU B CA  1 
ATOM   7253  C C   . GLU C 1 52  ? 8.040   25.121  -40.698 1.00 30.81  ? 81  GLU B C   1 
ATOM   7254  O O   . GLU C 1 52  ? 8.484   24.444  -41.622 1.00 29.20  ? 81  GLU B O   1 
ATOM   7255  C CB  . GLU C 1 52  ? 9.559   27.024  -40.228 1.00 37.54  ? 81  GLU B CB  1 
ATOM   7256  C CG  . GLU C 1 52  ? 9.860   28.522  -40.324 1.00 38.20  ? 81  GLU B CG  1 
ATOM   7257  C CD  . GLU C 1 52  ? 9.981   29.140  -41.721 1.00 40.82  ? 81  GLU B CD  1 
ATOM   7258  O OE1 . GLU C 1 52  ? 9.622   28.530  -42.752 1.00 35.44  ? 81  GLU B OE1 1 
ATOM   7259  O OE2 . GLU C 1 52  ? 10.452  30.292  -41.750 1.00 35.69  ? 81  GLU B OE2 1 
ATOM   7260  N N   . THR C 1 53  ? 7.391   24.584  -39.657 1.00 29.72  ? 82  THR B N   1 
ATOM   7261  C CA  . THR C 1 53  ? 7.551   23.171  -39.323 1.00 29.86  ? 82  THR B CA  1 
ATOM   7262  C C   . THR C 1 53  ? 6.747   22.245  -40.237 1.00 30.18  ? 82  THR B C   1 
ATOM   7263  O O   . THR C 1 53  ? 7.211   21.164  -40.606 1.00 29.66  ? 82  THR B O   1 
ATOM   7264  C CB  . THR C 1 53  ? 7.223   22.969  -37.851 1.00 29.05  ? 82  THR B CB  1 
ATOM   7265  O OG1 . THR C 1 53  ? 6.100   23.781  -37.521 1.00 28.31  ? 82  THR B OG1 1 
ATOM   7266  C CG2 . THR C 1 53  ? 8.380   23.411  -36.976 1.00 33.72  ? 82  THR B CG2 1 
ATOM   7267  N N   . SER C 1 54  ? 5.526   22.632  -40.587 1.00 30.51  ? 83  SER B N   1 
ATOM   7268  C CA  . SER C 1 54  ? 4.704   21.798  -41.434 1.00 29.23  ? 83  SER B CA  1 
ATOM   7269  C C   . SER C 1 54  ? 3.898   22.694  -42.350 1.00 31.20  ? 83  SER B C   1 
ATOM   7270  O O   . SER C 1 54  ? 3.674   23.849  -42.020 1.00 31.54  ? 83  SER B O   1 
ATOM   7271  C CB  . SER C 1 54  ? 3.785   20.903  -40.646 1.00 28.59  ? 83  SER B CB  1 
ATOM   7272  O OG  . SER C 1 54  ? 2.864   21.700  -39.919 1.00 28.73  ? 83  SER B OG  1 
ATOM   7273  N N   . VAL C 1 55  ? 3.437   22.095  -43.452 1.00 31.87  ? 84  VAL B N   1 
ATOM   7274  C CA  . VAL C 1 55  ? 2.696   22.773  -44.497 1.00 33.21  ? 84  VAL B CA  1 
ATOM   7275  C C   . VAL C 1 55  ? 1.593   21.838  -44.980 1.00 30.49  ? 84  VAL B C   1 
ATOM   7276  O O   . VAL C 1 55  ? 1.872   20.705  -45.345 1.00 30.99  ? 84  VAL B O   1 
ATOM   7277  C CB  . VAL C 1 55  ? 3.567   23.218  -45.689 1.00 34.05  ? 84  VAL B CB  1 
ATOM   7278  C CG1 . VAL C 1 55  ? 2.748   24.084  -46.651 1.00 34.84  ? 84  VAL B CG1 1 
ATOM   7279  C CG2 . VAL C 1 55  ? 4.799   23.997  -45.245 1.00 34.21  ? 84  VAL B CG2 1 
ATOM   7280  N N   . LEU C 1 56  ? 0.361   22.354  -45.065 1.00 32.19  ? 85  LEU B N   1 
ATOM   7281  C CA  . LEU C 1 56  ? -0.805  21.539  -45.373 1.00 39.01  ? 85  LEU B CA  1 
ATOM   7282  C C   . LEU C 1 56  ? -1.152  21.777  -46.833 1.00 44.82  ? 85  LEU B C   1 
ATOM   7283  O O   . LEU C 1 56  ? -1.599  22.862  -47.205 1.00 45.29  ? 85  LEU B O   1 
ATOM   7284  C CB  . LEU C 1 56  ? -1.991  21.844  -44.451 1.00 40.07  ? 85  LEU B CB  1 
ATOM   7285  C CG  . LEU C 1 56  ? -3.300  21.064  -44.669 1.00 42.53  ? 85  LEU B CG  1 
ATOM   7286  C CD1 . LEU C 1 56  ? -3.238  19.592  -44.337 1.00 39.42  ? 85  LEU B CD1 1 
ATOM   7287  C CD2 . LEU C 1 56  ? -4.411  21.711  -43.832 1.00 47.47  ? 85  LEU B CD2 1 
ATOM   7288  N N   . ASP C 1 57  ? -0.834  20.782  -47.661 1.00 45.63  ? 86  ASP B N   1 
ATOM   7289  C CA  . ASP C 1 57  ? -1.360  20.719  -49.007 1.00 48.58  ? 86  ASP B CA  1 
ATOM   7290  C C   . ASP C 1 57  ? -2.826  20.300  -48.923 1.00 44.85  ? 86  ASP B C   1 
ATOM   7291  O O   . ASP C 1 57  ? -3.129  19.251  -48.351 1.00 51.12  ? 86  ASP B O   1 
ATOM   7292  C CB  . ASP C 1 57  ? -0.577  19.742  -49.872 1.00 51.47  ? 86  ASP B CB  1 
ATOM   7293  C CG  . ASP C 1 57  ? -0.921  19.840  -51.348 1.00 55.28  ? 86  ASP B CG  1 
ATOM   7294  O OD1 . ASP C 1 57  ? -2.037  19.422  -51.709 1.00 51.07  ? 86  ASP B OD1 1 
ATOM   7295  O OD2 . ASP C 1 57  ? -0.102  20.403  -52.105 1.00 67.87  ? 86  ASP B OD2 1 
ATOM   7296  N N   . PRO C 1 58  ? -3.777  21.093  -49.459 1.00 44.25  ? 87  PRO B N   1 
ATOM   7297  C CA  . PRO C 1 58  ? -5.199  20.722  -49.410 1.00 50.36  ? 87  PRO B CA  1 
ATOM   7298  C C   . PRO C 1 58  ? -5.534  19.416  -50.153 1.00 60.44  ? 87  PRO B C   1 
ATOM   7299  O O   . PRO C 1 58  ? -6.389  18.631  -49.729 1.00 57.35  ? 87  PRO B O   1 
ATOM   7300  C CB  . PRO C 1 58  ? -5.925  21.955  -49.970 1.00 50.75  ? 87  PRO B CB  1 
ATOM   7301  C CG  . PRO C 1 58  ? -4.879  22.773  -50.696 1.00 53.70  ? 87  PRO B CG  1 
ATOM   7302  C CD  . PRO C 1 58  ? -3.523  22.376  -50.133 1.00 50.94  ? 87  PRO B CD  1 
ATOM   7303  N N   . ASP C 1 59  ? -4.774  19.165  -51.226 1.00 64.09  ? 88  ASP B N   1 
ATOM   7304  C CA  . ASP C 1 59  ? -4.933  18.026  -52.117 1.00 70.32  ? 88  ASP B CA  1 
ATOM   7305  C C   . ASP C 1 59  ? -4.308  16.787  -51.459 1.00 60.08  ? 88  ASP B C   1 
ATOM   7306  O O   . ASP C 1 59  ? -4.949  15.746  -51.381 1.00 59.39  ? 88  ASP B O   1 
ATOM   7307  C CB  . ASP C 1 59  ? -4.416  18.469  -53.487 1.00 85.62  ? 88  ASP B CB  1 
ATOM   7308  C CG  . ASP C 1 59  ? -4.753  17.625  -54.710 1.00 105.86 ? 88  ASP B CG  1 
ATOM   7309  O OD1 . ASP C 1 59  ? -5.942  17.282  -54.884 1.00 112.56 ? 88  ASP B OD1 1 
ATOM   7310  O OD2 . ASP C 1 59  ? -3.829  17.375  -55.519 1.00 116.70 ? 88  ASP B OD2 1 
ATOM   7311  N N   . GLU C 1 60  ? -3.087  16.930  -50.907 1.00 59.38  ? 89  GLU B N   1 
ATOM   7312  C CA  . GLU C 1 60  ? -2.247  15.813  -50.480 1.00 53.91  ? 89  GLU B CA  1 
ATOM   7313  C C   . GLU C 1 60  ? -2.055  15.719  -48.961 1.00 48.72  ? 89  GLU B C   1 
ATOM   7314  O O   . GLU C 1 60  ? -1.499  14.744  -48.477 1.00 40.03  ? 89  GLU B O   1 
ATOM   7315  C CB  . GLU C 1 60  ? -0.856  16.005  -51.082 1.00 59.18  ? 89  GLU B CB  1 
ATOM   7316  C CG  . GLU C 1 60  ? -0.863  16.093  -52.607 1.00 67.25  ? 89  GLU B CG  1 
ATOM   7317  C CD  . GLU C 1 60  ? -1.649  14.959  -53.233 1.00 82.57  ? 89  GLU B CD  1 
ATOM   7318  O OE1 . GLU C 1 60  ? -1.497  13.796  -52.775 1.00 86.87  ? 89  GLU B OE1 1 
ATOM   7319  O OE2 . GLU C 1 60  ? -2.437  15.254  -54.157 1.00 90.39  ? 89  GLU B OE2 1 
ATOM   7320  N N   . GLY C 1 61  ? -2.469  16.738  -48.195 1.00 45.77  ? 90  GLY B N   1 
ATOM   7321  C CA  . GLY C 1 61  ? -2.379  16.677  -46.746 1.00 40.79  ? 90  GLY B CA  1 
ATOM   7322  C C   . GLY C 1 61  ? -1.048  17.204  -46.229 1.00 38.75  ? 90  GLY B C   1 
ATOM   7323  O O   . GLY C 1 61  ? -0.310  17.886  -46.936 1.00 34.25  ? 90  GLY B O   1 
ATOM   7324  N N   . ILE C 1 62  ? -0.780  16.874  -44.959 1.00 36.96  ? 91  ILE B N   1 
ATOM   7325  C CA  . ILE C 1 62  ? 0.276   17.529  -44.199 1.00 32.66  ? 91  ILE B CA  1 
ATOM   7326  C C   . ILE C 1 62  ? 1.651   17.001  -44.610 1.00 33.56  ? 91  ILE B C   1 
ATOM   7327  O O   . ILE C 1 62  ? 1.830   15.813  -44.872 1.00 34.47  ? 91  ILE B O   1 
ATOM   7328  C CB  . ILE C 1 62  ? 0.023   17.394  -42.690 1.00 26.87  ? 91  ILE B CB  1 
ATOM   7329  C CG1 . ILE C 1 62  ? 0.905   18.379  -41.901 1.00 25.67  ? 91  ILE B CG1 1 
ATOM   7330  C CG2 . ILE C 1 62  ? 0.151   15.932  -42.222 1.00 28.18  ? 91  ILE B CG2 1 
ATOM   7331  C CD1 . ILE C 1 62  ? 0.515   19.830  -42.163 1.00 23.97  ? 91  ILE B CD1 1 
ATOM   7332  N N   . ARG C 1 63  ? 2.597   17.932  -44.738 1.00 33.35  ? 92  ARG B N   1 
ATOM   7333  C CA  . ARG C 1 63  ? 4.012   17.604  -44.854 1.00 34.06  ? 92  ARG B CA  1 
ATOM   7334  C C   . ARG C 1 63  ? 4.759   18.196  -43.662 1.00 30.06  ? 92  ARG B C   1 
ATOM   7335  O O   . ARG C 1 63  ? 4.618   19.390  -43.388 1.00 28.96  ? 92  ARG B O   1 
ATOM   7336  C CB  . ARG C 1 63  ? 4.601   18.175  -46.156 1.00 32.75  ? 92  ARG B CB  1 
ATOM   7337  C CG  . ARG C 1 63  ? 3.982   17.556  -47.408 1.00 40.64  ? 92  ARG B CG  1 
ATOM   7338  C CD  . ARG C 1 63  ? 4.599   18.125  -48.681 1.00 51.05  ? 92  ARG B CD  1 
ATOM   7339  N NE  . ARG C 1 63  ? 4.217   17.290  -49.824 1.00 68.71  ? 92  ARG B NE  1 
ATOM   7340  C CZ  . ARG C 1 63  ? 3.248   17.560  -50.701 1.00 69.32  ? 92  ARG B CZ  1 
ATOM   7341  N NH1 . ARG C 1 63  ? 2.599   18.715  -50.664 1.00 68.28  ? 92  ARG B NH1 1 
ATOM   7342  N NH2 . ARG C 1 63  ? 2.929   16.665  -51.625 1.00 62.24  ? 92  ARG B NH2 1 
ATOM   7343  N N   . PHE C 1 64  ? 5.548   17.350  -42.981 1.00 30.45  ? 93  PHE B N   1 
ATOM   7344  C CA  . PHE C 1 64  ? 6.521   17.767  -41.986 1.00 28.86  ? 93  PHE B CA  1 
ATOM   7345  C C   . PHE C 1 64  ? 7.851   18.049  -42.669 1.00 29.57  ? 93  PHE B C   1 
ATOM   7346  O O   . PHE C 1 64  ? 8.505   17.127  -43.158 1.00 25.56  ? 93  PHE B O   1 
ATOM   7347  C CB  . PHE C 1 64  ? 6.694   16.597  -41.021 1.00 32.21  ? 93  PHE B CB  1 
ATOM   7348  C CG  . PHE C 1 64  ? 5.393   16.141  -40.394 1.00 32.71  ? 93  PHE B CG  1 
ATOM   7349  C CD1 . PHE C 1 64  ? 4.518   17.057  -39.838 1.00 34.34  ? 93  PHE B CD1 1 
ATOM   7350  C CD2 . PHE C 1 64  ? 5.049   14.806  -40.365 1.00 38.41  ? 93  PHE B CD2 1 
ATOM   7351  C CE1 . PHE C 1 64  ? 3.321   16.642  -39.316 1.00 33.81  ? 93  PHE B CE1 1 
ATOM   7352  C CE2 . PHE C 1 64  ? 3.838   14.403  -39.829 1.00 38.71  ? 93  PHE B CE2 1 
ATOM   7353  C CZ  . PHE C 1 64  ? 2.999   15.319  -39.279 1.00 33.83  ? 93  PHE B CZ  1 
ATOM   7354  N N   . ARG C 1 65  ? 8.241   19.326  -42.710 1.00 27.41  ? 94  ARG B N   1 
ATOM   7355  C CA  . ARG C 1 65  ? 9.484   19.750  -43.333 1.00 26.16  ? 94  ARG B CA  1 
ATOM   7356  C C   . ARG C 1 65  ? 9.659   19.079  -44.686 1.00 28.32  ? 94  ARG B C   1 
ATOM   7357  O O   . ARG C 1 65  ? 10.750  18.639  -45.042 1.00 29.75  ? 94  ARG B O   1 
ATOM   7358  C CB  . ARG C 1 65  ? 10.661  19.461  -42.395 1.00 28.88  ? 94  ARG B CB  1 
ATOM   7359  C CG  . ARG C 1 65  ? 10.616  20.268  -41.104 1.00 26.04  ? 94  ARG B CG  1 
ATOM   7360  C CD  . ARG C 1 65  ? 11.013  21.690  -41.359 1.00 25.71  ? 94  ARG B CD  1 
ATOM   7361  N NE  . ARG C 1 65  ? 11.335  22.388  -40.112 1.00 31.78  ? 94  ARG B NE  1 
ATOM   7362  C CZ  . ARG C 1 65  ? 11.823  23.617  -40.023 1.00 31.53  ? 94  ARG B CZ  1 
ATOM   7363  N NH1 . ARG C 1 65  ? 12.010  24.295  -41.128 1.00 35.25  ? 94  ARG B NH1 1 
ATOM   7364  N NH2 . ARG C 1 65  ? 12.111  24.167  -38.846 1.00 31.08  ? 94  ARG B NH2 1 
ATOM   7365  N N   . GLY C 1 66  ? 8.553   18.967  -45.415 1.00 31.00  ? 95  GLY B N   1 
ATOM   7366  C CA  . GLY C 1 66  ? 8.604   18.515  -46.789 1.00 32.87  ? 95  GLY B CA  1 
ATOM   7367  C C   . GLY C 1 66  ? 8.421   17.008  -46.918 1.00 32.98  ? 95  GLY B C   1 
ATOM   7368  O O   . GLY C 1 66  ? 8.282   16.542  -48.026 1.00 36.68  ? 95  GLY B O   1 
ATOM   7369  N N   . PHE C 1 67  ? 8.323   16.281  -45.793 1.00 33.72  ? 96  PHE B N   1 
ATOM   7370  C CA  . PHE C 1 67  ? 8.043   14.858  -45.789 1.00 34.43  ? 96  PHE B CA  1 
ATOM   7371  C C   . PHE C 1 67  ? 6.587   14.544  -45.465 1.00 36.29  ? 96  PHE B C   1 
ATOM   7372  O O   . PHE C 1 67  ? 6.022   15.021  -44.487 1.00 33.81  ? 96  PHE B O   1 
ATOM   7373  C CB  . PHE C 1 67  ? 8.894   14.179  -44.727 1.00 31.09  ? 96  PHE B CB  1 
ATOM   7374  C CG  . PHE C 1 67  ? 10.369  14.294  -45.062 1.00 35.16  ? 96  PHE B CG  1 
ATOM   7375  C CD1 . PHE C 1 67  ? 10.969  13.370  -45.915 1.00 35.94  ? 96  PHE B CD1 1 
ATOM   7376  C CD2 . PHE C 1 67  ? 11.140  15.326  -44.542 1.00 34.06  ? 96  PHE B CD2 1 
ATOM   7377  C CE1 . PHE C 1 67  ? 12.331  13.445  -46.201 1.00 37.63  ? 96  PHE B CE1 1 
ATOM   7378  C CE2 . PHE C 1 67  ? 12.494  15.414  -44.854 1.00 36.48  ? 96  PHE B CE2 1 
ATOM   7379  C CZ  . PHE C 1 67  ? 13.084  14.475  -45.687 1.00 39.61  ? 96  PHE B CZ  1 
ATOM   7380  N N   . SER C 1 68  ? 6.007   13.644  -46.252 1.00 33.88  ? 97  SER B N   1 
ATOM   7381  C CA  . SER C 1 68  ? 4.633   13.230  -46.053 1.00 30.47  ? 97  SER B CA  1 
ATOM   7382  C C   . SER C 1 68  ? 4.606   12.235  -44.900 1.00 31.05  ? 97  SER B C   1 
ATOM   7383  O O   . SER C 1 68  ? 5.629   11.698  -44.469 1.00 32.84  ? 97  SER B O   1 
ATOM   7384  C CB  . SER C 1 68  ? 4.064   12.609  -47.333 1.00 32.41  ? 97  SER B CB  1 
ATOM   7385  O OG  . SER C 1 68  ? 4.451   11.243  -47.344 1.00 38.81  ? 97  SER B OG  1 
ATOM   7386  N N   . ILE C 1 69  ? 3.411   11.946  -44.417 1.00 29.24  ? 98  ILE B N   1 
ATOM   7387  C CA  . ILE C 1 69  ? 3.287   11.008  -43.318 1.00 31.00  ? 98  ILE B CA  1 
ATOM   7388  C C   . ILE C 1 69  ? 3.859   9.670   -43.761 1.00 28.20  ? 98  ILE B C   1 
ATOM   7389  O O   . ILE C 1 69  ? 4.690   9.110   -43.057 1.00 30.11  ? 98  ILE B O   1 
ATOM   7390  C CB  . ILE C 1 69  ? 1.823   10.916  -42.880 1.00 30.33  ? 98  ILE B CB  1 
ATOM   7391  C CG1 . ILE C 1 69  ? 1.355   12.264  -42.307 1.00 38.10  ? 98  ILE B CG1 1 
ATOM   7392  C CG2 . ILE C 1 69  ? 1.626   9.755   -41.921 1.00 33.20  ? 98  ILE B CG2 1 
ATOM   7393  C CD1 . ILE C 1 69  ? 1.169   12.312  -40.816 1.00 42.38  ? 98  ILE B CD1 1 
ATOM   7394  N N   . PRO C 1 70  ? 3.456   9.118   -44.929 1.00 28.25  ? 99  PRO B N   1 
ATOM   7395  C CA  . PRO C 1 70  ? 4.053   7.859   -45.390 1.00 31.99  ? 99  PRO B CA  1 
ATOM   7396  C C   . PRO C 1 70  ? 5.576   7.891   -45.520 1.00 30.56  ? 99  PRO B C   1 
ATOM   7397  O O   . PRO C 1 70  ? 6.238   6.974   -45.061 1.00 32.55  ? 99  PRO B O   1 
ATOM   7398  C CB  . PRO C 1 70  ? 3.346   7.561   -46.712 1.00 31.24  ? 99  PRO B CB  1 
ATOM   7399  C CG  . PRO C 1 70  ? 2.066   8.361   -46.641 1.00 32.08  ? 99  PRO B CG  1 
ATOM   7400  C CD  . PRO C 1 70  ? 2.382   9.597   -45.807 1.00 29.58  ? 99  PRO B CD  1 
ATOM   7401  N N   . GLU C 1 71  ? 6.169   8.946   -46.084 1.00 33.07  ? 100 GLU B N   1 
ATOM   7402  C CA  . GLU C 1 71  ? 7.633   9.039   -46.065 1.00 30.67  ? 100 GLU B CA  1 
ATOM   7403  C C   . GLU C 1 71  ? 8.171   8.981   -44.630 1.00 31.98  ? 100 GLU B C   1 
ATOM   7404  O O   . GLU C 1 71  ? 9.115   8.253   -44.308 1.00 28.87  ? 100 GLU B O   1 
ATOM   7405  C CB  . GLU C 1 71  ? 8.126   10.302  -46.750 1.00 31.12  ? 100 GLU B CB  1 
ATOM   7406  C CG  . GLU C 1 71  ? 7.783   10.369  -48.236 1.00 36.29  ? 100 GLU B CG  1 
ATOM   7407  C CD  . GLU C 1 71  ? 8.187   11.647  -48.983 1.00 45.09  ? 100 GLU B CD  1 
ATOM   7408  O OE1 . GLU C 1 71  ? 7.658   12.705  -48.589 1.00 45.75  ? 100 GLU B OE1 1 
ATOM   7409  O OE2 . GLU C 1 71  ? 8.998   11.618  -49.959 1.00 45.44  ? 100 GLU B OE2 1 
ATOM   7410  N N   . CYS C 1 72  ? 7.569   9.747   -43.719 1.00 28.95  ? 101 CYS B N   1 
ATOM   7411  C CA  . CYS C 1 72  ? 8.032   9.738   -42.348 1.00 30.62  ? 101 CYS B CA  1 
ATOM   7412  C C   . CYS C 1 72  ? 7.942   8.356   -41.716 1.00 30.81  ? 101 CYS B C   1 
ATOM   7413  O O   . CYS C 1 72  ? 8.806   8.018   -40.907 1.00 29.96  ? 101 CYS B O   1 
ATOM   7414  C CB  . CYS C 1 72  ? 7.248   10.710  -41.463 1.00 30.62  ? 101 CYS B CB  1 
ATOM   7415  S SG  . CYS C 1 72  ? 7.585   12.424  -41.920 1.00 33.20  ? 101 CYS B SG  1 
ATOM   7416  N N   . GLN C 1 73  ? 6.868   7.611   -42.025 1.00 31.76  ? 102 GLN B N   1 
ATOM   7417  C CA  . GLN C 1 73  ? 6.662   6.302   -41.434 1.00 39.20  ? 102 GLN B CA  1 
ATOM   7418  C C   . GLN C 1 73  ? 7.797   5.388   -41.861 1.00 39.15  ? 102 GLN B C   1 
ATOM   7419  O O   . GLN C 1 73  ? 8.210   4.548   -41.066 1.00 37.14  ? 102 GLN B O   1 
ATOM   7420  C CB  . GLN C 1 73  ? 5.367   5.579   -41.808 1.00 43.70  ? 102 GLN B CB  1 
ATOM   7421  C CG  . GLN C 1 73  ? 4.125   6.282   -41.279 1.00 46.90  ? 102 GLN B CG  1 
ATOM   7422  C CD  . GLN C 1 73  ? 2.848   5.639   -41.771 1.00 48.42  ? 102 GLN B CD  1 
ATOM   7423  O OE1 . GLN C 1 73  ? 2.345   5.940   -42.862 1.00 49.93  ? 102 GLN B OE1 1 
ATOM   7424  N NE2 . GLN C 1 73  ? 2.312   4.744   -40.955 1.00 43.93  ? 102 GLN B NE2 1 
ATOM   7425  N N   . LYS C 1 74  ? 8.316   5.580   -43.084 1.00 36.06  ? 103 LYS B N   1 
ATOM   7426  C CA  . LYS C 1 74  ? 9.454   4.786   -43.539 1.00 42.82  ? 103 LYS B CA  1 
ATOM   7427  C C   . LYS C 1 74  ? 10.766  5.276   -42.919 1.00 42.94  ? 103 LYS B C   1 
ATOM   7428  O O   . LYS C 1 74  ? 11.545  4.458   -42.419 1.00 39.22  ? 103 LYS B O   1 
ATOM   7429  C CB  . LYS C 1 74  ? 9.551   4.716   -45.066 1.00 44.28  ? 103 LYS B CB  1 
ATOM   7430  C CG  . LYS C 1 74  ? 8.354   4.026   -45.664 1.00 50.46  ? 103 LYS B CG  1 
ATOM   7431  C CD  . LYS C 1 74  ? 8.444   3.725   -47.161 1.00 53.85  ? 103 LYS B CD  1 
ATOM   7432  C CE  . LYS C 1 74  ? 7.682   2.480   -47.531 1.00 50.74  ? 103 LYS B CE  1 
ATOM   7433  N NZ  . LYS C 1 74  ? 6.259   2.585   -47.204 1.00 49.38  ? 103 LYS B NZ  1 
ATOM   7434  N N   . LEU C 1 75  ? 11.007  6.600   -42.923 1.00 37.75  ? 104 LEU B N   1 
ATOM   7435  C CA  . LEU C 1 75  ? 12.337  7.129   -42.618 1.00 35.33  ? 104 LEU B CA  1 
ATOM   7436  C C   . LEU C 1 75  ? 12.624  7.257   -41.120 1.00 30.59  ? 104 LEU B C   1 
ATOM   7437  O O   . LEU C 1 75  ? 13.781  7.217   -40.691 1.00 29.06  ? 104 LEU B O   1 
ATOM   7438  C CB  . LEU C 1 75  ? 12.483  8.481   -43.307 1.00 35.41  ? 104 LEU B CB  1 
ATOM   7439  C CG  . LEU C 1 75  ? 12.612  8.437   -44.836 1.00 38.33  ? 104 LEU B CG  1 
ATOM   7440  C CD1 . LEU C 1 75  ? 12.443  9.846   -45.389 1.00 34.52  ? 104 LEU B CD1 1 
ATOM   7441  C CD2 . LEU C 1 75  ? 13.952  7.851   -45.269 1.00 37.32  ? 104 LEU B CD2 1 
ATOM   7442  N N   . LEU C 1 76  ? 11.597  7.566   -40.336 1.00 30.43  ? 105 LEU B N   1 
ATOM   7443  C CA  . LEU C 1 76  ? 11.810  7.911   -38.947 1.00 32.03  ? 105 LEU B CA  1 
ATOM   7444  C C   . LEU C 1 76  ? 12.180  6.671   -38.143 1.00 34.70  ? 105 LEU B C   1 
ATOM   7445  O O   . LEU C 1 76  ? 11.569  5.622   -38.297 1.00 33.64  ? 105 LEU B O   1 
ATOM   7446  C CB  . LEU C 1 76  ? 10.539  8.549   -38.415 1.00 31.60  ? 105 LEU B CB  1 
ATOM   7447  C CG  . LEU C 1 76  ? 10.336  10.017  -38.794 1.00 33.37  ? 105 LEU B CG  1 
ATOM   7448  C CD1 . LEU C 1 76  ? 9.074   10.465  -38.124 1.00 34.89  ? 105 LEU B CD1 1 
ATOM   7449  C CD2 . LEU C 1 76  ? 11.482  10.895  -38.359 1.00 34.13  ? 105 LEU B CD2 1 
ATOM   7450  N N   . PRO C 1 77  ? 13.172  6.750   -37.237 1.00 32.91  ? 106 PRO B N   1 
ATOM   7451  C CA  . PRO C 1 77  ? 13.466  5.616   -36.370 1.00 33.74  ? 106 PRO B CA  1 
ATOM   7452  C C   . PRO C 1 77  ? 12.268  5.052   -35.613 1.00 37.81  ? 106 PRO B C   1 
ATOM   7453  O O   . PRO C 1 77  ? 11.342  5.769   -35.206 1.00 30.33  ? 106 PRO B O   1 
ATOM   7454  C CB  . PRO C 1 77  ? 14.533  6.203   -35.437 1.00 35.56  ? 106 PRO B CB  1 
ATOM   7455  C CG  . PRO C 1 77  ? 15.248  7.237   -36.308 1.00 33.22  ? 106 PRO B CG  1 
ATOM   7456  C CD  . PRO C 1 77  ? 14.108  7.866   -37.075 1.00 29.31  ? 106 PRO B CD  1 
ATOM   7457  N N   . LYS C 1 78  ? 12.347  3.741   -35.395 1.00 34.30  ? 107 LYS B N   1 
ATOM   7458  C CA  . LYS C 1 78  ? 11.343  2.988   -34.684 1.00 35.63  ? 107 LYS B CA  1 
ATOM   7459  C C   . LYS C 1 78  ? 11.948  2.520   -33.379 1.00 33.86  ? 107 LYS B C   1 
ATOM   7460  O O   . LYS C 1 78  ? 13.159  2.507   -33.243 1.00 35.99  ? 107 LYS B O   1 
ATOM   7461  C CB  . LYS C 1 78  ? 10.952  1.830   -35.612 1.00 44.50  ? 107 LYS B CB  1 
ATOM   7462  C CG  . LYS C 1 78  ? 10.200  2.269   -36.866 1.00 46.50  ? 107 LYS B CG  1 
ATOM   7463  C CD  . LYS C 1 78  ? 10.529  1.481   -38.130 1.00 52.31  ? 107 LYS B CD  1 
ATOM   7464  C CE  . LYS C 1 78  ? 9.761   2.001   -39.321 1.00 54.84  ? 107 LYS B CE  1 
ATOM   7465  N NZ  . LYS C 1 78  ? 10.176  3.355   -39.717 1.00 52.29  ? 107 LYS B NZ  1 
ATOM   7466  N N   . ALA C 1 79  ? 11.084  2.121   -32.437 1.00 36.74  ? 108 ALA B N   1 
ATOM   7467  C CA  . ALA C 1 79  ? 11.497  1.373   -31.266 1.00 38.78  ? 108 ALA B CA  1 
ATOM   7468  C C   . ALA C 1 79  ? 12.089  0.030   -31.693 1.00 46.69  ? 108 ALA B C   1 
ATOM   7469  O O   . ALA C 1 79  ? 11.725  -0.515  -32.743 1.00 40.29  ? 108 ALA B O   1 
ATOM   7470  C CB  . ALA C 1 79  ? 10.311  1.168   -30.356 1.00 39.78  ? 108 ALA B CB  1 
ATOM   7471  N N   . LYS C 1 80  ? 12.995  -0.485  -30.846 1.00 55.34  ? 109 LYS B N   1 
ATOM   7472  C CA  . LYS C 1 80  ? 13.517  -1.834  -30.973 1.00 58.04  ? 109 LYS B CA  1 
ATOM   7473  C C   . LYS C 1 80  ? 12.332  -2.798  -30.940 1.00 52.75  ? 109 LYS B C   1 
ATOM   7474  O O   . LYS C 1 80  ? 11.579  -2.836  -29.966 1.00 51.35  ? 109 LYS B O   1 
ATOM   7475  C CB  . LYS C 1 80  ? 14.534  -2.047  -29.844 1.00 66.94  ? 109 LYS B CB  1 
ATOM   7476  C CG  . LYS C 1 80  ? 15.261  -3.387  -29.835 1.00 80.34  ? 109 LYS B CG  1 
ATOM   7477  C CD  . LYS C 1 80  ? 15.935  -3.752  -28.512 1.00 91.51  ? 109 LYS B CD  1 
ATOM   7478  C CE  . LYS C 1 80  ? 16.514  -5.141  -28.521 1.00 92.96  ? 109 LYS B CE  1 
ATOM   7479  N NZ  . LYS C 1 80  ? 16.897  -5.584  -27.178 1.00 92.45  ? 109 LYS B NZ  1 
ATOM   7480  N N   . GLY C 1 81  ? 12.135  -3.531  -32.039 1.00 53.46  ? 110 GLY B N   1 
ATOM   7481  C CA  . GLY C 1 81  ? 11.069  -4.514  -32.118 1.00 57.15  ? 110 GLY B CA  1 
ATOM   7482  C C   . GLY C 1 81  ? 9.732   -3.875  -32.490 1.00 59.39  ? 110 GLY B C   1 
ATOM   7483  O O   . GLY C 1 81  ? 8.680   -4.472  -32.259 1.00 60.45  ? 110 GLY B O   1 
ATOM   7484  N N   . GLY C 1 82  ? 9.790   -2.689  -33.113 1.00 54.27  ? 111 GLY B N   1 
ATOM   7485  C CA  . GLY C 1 82  ? 8.605   -1.895  -33.386 1.00 53.13  ? 111 GLY B CA  1 
ATOM   7486  C C   . GLY C 1 82  ? 8.507   -1.536  -34.861 1.00 47.03  ? 111 GLY B C   1 
ATOM   7487  O O   . GLY C 1 82  ? 9.461   -1.699  -35.611 1.00 47.69  ? 111 GLY B O   1 
ATOM   7488  N N   . GLU C 1 83  ? 7.326   -1.063  -35.261 1.00 44.89  ? 112 GLU B N   1 
ATOM   7489  C CA  . GLU C 1 83  ? 7.067   -0.719  -36.645 1.00 52.15  ? 112 GLU B CA  1 
ATOM   7490  C C   . GLU C 1 83  ? 6.675   0.749   -36.795 1.00 47.48  ? 112 GLU B C   1 
ATOM   7491  O O   . GLU C 1 83  ? 6.771   1.271   -37.894 1.00 40.65  ? 112 GLU B O   1 
ATOM   7492  C CB  . GLU C 1 83  ? 5.946   -1.609  -37.185 1.00 63.33  ? 112 GLU B CB  1 
ATOM   7493  C CG  . GLU C 1 83  ? 6.303   -3.096  -37.147 1.00 79.91  ? 112 GLU B CG  1 
ATOM   7494  C CD  . GLU C 1 83  ? 7.369   -3.551  -38.139 1.00 86.13  ? 112 GLU B CD  1 
ATOM   7495  O OE1 . GLU C 1 83  ? 7.083   -3.536  -39.356 1.00 86.03  ? 112 GLU B OE1 1 
ATOM   7496  O OE2 . GLU C 1 83  ? 8.483   -3.926  -37.698 1.00 90.03  ? 112 GLU B OE2 1 
ATOM   7497  N N   . GLU C 1 84  ? 6.195   1.388   -35.716 1.00 42.91  ? 113 GLU B N   1 
ATOM   7498  C CA  . GLU C 1 84  ? 5.639   2.735   -35.795 1.00 41.03  ? 113 GLU B CA  1 
ATOM   7499  C C   . GLU C 1 84  ? 6.701   3.778   -35.438 1.00 37.68  ? 113 GLU B C   1 
ATOM   7500  O O   . GLU C 1 84  ? 7.534   3.551   -34.575 1.00 30.39  ? 113 GLU B O   1 
ATOM   7501  C CB  . GLU C 1 84  ? 4.374   2.791   -34.939 1.00 39.02  ? 113 GLU B CB  1 
ATOM   7502  C CG  . GLU C 1 84  ? 3.258   1.895   -35.480 1.00 43.40  ? 113 GLU B CG  1 
ATOM   7503  C CD  . GLU C 1 84  ? 2.761   2.164   -36.905 1.00 45.97  ? 113 GLU B CD  1 
ATOM   7504  O OE1 . GLU C 1 84  ? 3.030   3.241   -37.482 1.00 46.38  ? 113 GLU B OE1 1 
ATOM   7505  O OE2 . GLU C 1 84  ? 2.109   1.252   -37.470 1.00 47.63  ? 113 GLU B OE2 1 
ATOM   7506  N N   . PRO C 1 85  ? 6.751   4.943   -36.131 1.00 39.78  ? 114 PRO B N   1 
ATOM   7507  C CA  . PRO C 1 85  ? 7.756   5.966   -35.829 1.00 35.17  ? 114 PRO B CA  1 
ATOM   7508  C C   . PRO C 1 85  ? 7.652   6.589   -34.434 1.00 34.48  ? 114 PRO B C   1 
ATOM   7509  O O   . PRO C 1 85  ? 6.567   6.774   -33.850 1.00 28.51  ? 114 PRO B O   1 
ATOM   7510  C CB  . PRO C 1 85  ? 7.624   6.987   -36.968 1.00 38.92  ? 114 PRO B CB  1 
ATOM   7511  C CG  . PRO C 1 85  ? 6.217   6.783   -37.497 1.00 43.34  ? 114 PRO B CG  1 
ATOM   7512  C CD  . PRO C 1 85  ? 5.897   5.307   -37.274 1.00 45.04  ? 114 PRO B CD  1 
ATOM   7513  N N   . LEU C 1 86  ? 8.834   6.843   -33.869 1.00 29.71  ? 115 LEU B N   1 
ATOM   7514  C CA  . LEU C 1 86  ? 8.921   7.440   -32.552 1.00 30.88  ? 115 LEU B CA  1 
ATOM   7515  C C   . LEU C 1 86  ? 8.612   8.932   -32.657 1.00 29.81  ? 115 LEU B C   1 
ATOM   7516  O O   . LEU C 1 86  ? 9.184   9.627   -33.489 1.00 28.33  ? 115 LEU B O   1 
ATOM   7517  C CB  . LEU C 1 86  ? 10.301  7.152   -31.969 1.00 32.68  ? 115 LEU B CB  1 
ATOM   7518  C CG  . LEU C 1 86  ? 10.549  5.680   -31.608 1.00 37.05  ? 115 LEU B CG  1 
ATOM   7519  C CD1 . LEU C 1 86  ? 11.914  5.533   -30.981 1.00 39.35  ? 115 LEU B CD1 1 
ATOM   7520  C CD2 . LEU C 1 86  ? 9.492   5.139   -30.646 1.00 40.44  ? 115 LEU B CD2 1 
ATOM   7521  N N   . PRO C 1 87  ? 7.669   9.476   -31.850 1.00 30.61  ? 116 PRO B N   1 
ATOM   7522  C CA  . PRO C 1 87  ? 7.461   10.924  -31.803 1.00 29.56  ? 116 PRO B CA  1 
ATOM   7523  C C   . PRO C 1 87  ? 8.720   11.759  -31.599 1.00 27.02  ? 116 PRO B C   1 
ATOM   7524  O O   . PRO C 1 87  ? 8.807   12.800  -32.247 1.00 26.35  ? 116 PRO B O   1 
ATOM   7525  C CB  . PRO C 1 87  ? 6.443   11.170  -30.691 1.00 30.51  ? 116 PRO B CB  1 
ATOM   7526  C CG  . PRO C 1 87  ? 5.945   9.821   -30.279 1.00 32.76  ? 116 PRO B CG  1 
ATOM   7527  C CD  . PRO C 1 87  ? 6.778   8.739   -30.946 1.00 30.27  ? 116 PRO B CD  1 
ATOM   7528  N N   . GLU C 1 88  ? 9.682   11.270  -30.780 1.00 25.32  ? 117 GLU B N   1 
ATOM   7529  C CA  . GLU C 1 88  ? 10.997  11.887  -30.616 1.00 28.68  ? 117 GLU B CA  1 
ATOM   7530  C C   . GLU C 1 88  ? 11.608  12.262  -31.968 1.00 26.00  ? 117 GLU B C   1 
ATOM   7531  O O   . GLU C 1 88  ? 12.172  13.346  -32.153 1.00 29.44  ? 117 GLU B O   1 
ATOM   7532  C CB  . GLU C 1 88  ? 12.112  11.024  -30.028 1.00 31.39  ? 117 GLU B CB  1 
ATOM   7533  C CG  . GLU C 1 88  ? 11.977  10.624  -28.559 1.00 32.55  ? 117 GLU B CG  1 
ATOM   7534  C CD  . GLU C 1 88  ? 10.956  9.561   -28.226 1.00 31.55  ? 117 GLU B CD  1 
ATOM   7535  O OE1 . GLU C 1 88  ? 9.991   9.335   -29.008 1.00 32.76  ? 117 GLU B OE1 1 
ATOM   7536  O OE2 . GLU C 1 88  ? 11.132  8.959   -27.128 1.00 35.50  ? 117 GLU B OE2 1 
ATOM   7537  N N   . GLY C 1 89  ? 11.544  11.340  -32.929 1.00 30.80  ? 118 GLY B N   1 
ATOM   7538  C CA  . GLY C 1 89  ? 12.223  11.566  -34.195 1.00 25.95  ? 118 GLY B CA  1 
ATOM   7539  C C   . GLY C 1 89  ? 11.481  12.568  -35.055 1.00 23.14  ? 118 GLY B C   1 
ATOM   7540  O O   . GLY C 1 89  ? 12.077  13.339  -35.815 1.00 27.05  ? 118 GLY B O   1 
ATOM   7541  N N   . LEU C 1 90  ? 10.165  12.577  -34.907 1.00 28.20  ? 119 LEU B N   1 
ATOM   7542  C CA  . LEU C 1 90  ? 9.370   13.562  -35.592 1.00 28.80  ? 119 LEU B CA  1 
ATOM   7543  C C   . LEU C 1 90  ? 9.738   14.956  -35.074 1.00 28.66  ? 119 LEU B C   1 
ATOM   7544  O O   . LEU C 1 90  ? 9.849   15.944  -35.839 1.00 25.89  ? 119 LEU B O   1 
ATOM   7545  C CB  . LEU C 1 90  ? 7.871   13.339  -35.467 1.00 31.44  ? 119 LEU B CB  1 
ATOM   7546  C CG  . LEU C 1 90  ? 7.187   14.649  -35.849 1.00 36.29  ? 119 LEU B CG  1 
ATOM   7547  C CD1 . LEU C 1 90  ? 6.806   14.702  -37.312 1.00 29.97  ? 119 LEU B CD1 1 
ATOM   7548  C CD2 . LEU C 1 90  ? 6.153   15.028  -34.845 1.00 44.56  ? 119 LEU B CD2 1 
ATOM   7549  N N   . PHE C 1 91  ? 9.923   15.040  -33.761 1.00 29.12  ? 120 PHE B N   1 
ATOM   7550  C CA  . PHE C 1 91  ? 10.286  16.324  -33.175 1.00 30.42  ? 120 PHE B CA  1 
ATOM   7551  C C   . PHE C 1 91  ? 11.628  16.805  -33.747 1.00 25.76  ? 120 PHE B C   1 
ATOM   7552  O O   . PHE C 1 91  ? 11.769  17.942  -34.176 1.00 27.96  ? 120 PHE B O   1 
ATOM   7553  C CB  . PHE C 1 91  ? 10.241  16.205  -31.655 1.00 26.41  ? 120 PHE B CB  1 
ATOM   7554  C CG  . PHE C 1 91  ? 10.642  17.508  -30.990 1.00 24.37  ? 120 PHE B CG  1 
ATOM   7555  C CD1 . PHE C 1 91  ? 9.737   18.547  -30.870 1.00 23.46  ? 120 PHE B CD1 1 
ATOM   7556  C CD2 . PHE C 1 91  ? 11.945  17.727  -30.578 1.00 26.80  ? 120 PHE B CD2 1 
ATOM   7557  C CE1 . PHE C 1 91  ? 10.114  19.750  -30.295 1.00 21.95  ? 120 PHE B CE1 1 
ATOM   7558  C CE2 . PHE C 1 91  ? 12.318  18.939  -30.022 1.00 26.86  ? 120 PHE B CE2 1 
ATOM   7559  C CZ  . PHE C 1 91  ? 11.384  19.924  -29.831 1.00 24.95  ? 120 PHE B CZ  1 
ATOM   7560  N N   . TRP C 1 92  ? 12.601  15.904  -33.830 1.00 28.58  ? 121 TRP B N   1 
ATOM   7561  C CA  . TRP C 1 92  ? 13.904  16.208  -34.393 1.00 21.77  ? 121 TRP B CA  1 
ATOM   7562  C C   . TRP C 1 92  ? 13.789  16.738  -35.802 1.00 21.31  ? 121 TRP B C   1 
ATOM   7563  O O   . TRP C 1 92  ? 14.418  17.735  -36.136 1.00 25.51  ? 121 TRP B O   1 
ATOM   7564  C CB  . TRP C 1 92  ? 14.790  14.963  -34.324 1.00 23.89  ? 121 TRP B CB  1 
ATOM   7565  C CG  . TRP C 1 92  ? 16.225  15.264  -34.617 1.00 23.71  ? 121 TRP B CG  1 
ATOM   7566  C CD1 . TRP C 1 92  ? 16.758  15.576  -35.827 1.00 28.32  ? 121 TRP B CD1 1 
ATOM   7567  C CD2 . TRP C 1 92  ? 17.317  15.286  -33.689 1.00 25.50  ? 121 TRP B CD2 1 
ATOM   7568  N NE1 . TRP C 1 92  ? 18.095  15.804  -35.703 1.00 25.88  ? 121 TRP B NE1 1 
ATOM   7569  C CE2 . TRP C 1 92  ? 18.467  15.634  -34.410 1.00 25.37  ? 121 TRP B CE2 1 
ATOM   7570  C CE3 . TRP C 1 92  ? 17.429  15.098  -32.326 1.00 24.00  ? 121 TRP B CE3 1 
ATOM   7571  C CZ2 . TRP C 1 92  ? 19.723  15.747  -33.824 1.00 26.92  ? 121 TRP B CZ2 1 
ATOM   7572  C CZ3 . TRP C 1 92  ? 18.679  15.151  -31.756 1.00 26.29  ? 121 TRP B CZ3 1 
ATOM   7573  C CH2 . TRP C 1 92  ? 19.799  15.499  -32.484 1.00 25.29  ? 121 TRP B CH2 1 
ATOM   7574  N N   . LEU C 1 93  ? 12.964  16.088  -36.626 1.00 24.50  ? 122 LEU B N   1 
ATOM   7575  C CA  . LEU C 1 93  ? 12.716  16.553  -37.977 1.00 25.17  ? 122 LEU B CA  1 
ATOM   7576  C C   . LEU C 1 93  ? 12.101  17.945  -37.989 1.00 25.17  ? 122 LEU B C   1 
ATOM   7577  O O   . LEU C 1 93  ? 12.528  18.820  -38.745 1.00 22.35  ? 122 LEU B O   1 
ATOM   7578  C CB  . LEU C 1 93  ? 11.785  15.567  -38.670 1.00 28.57  ? 122 LEU B CB  1 
ATOM   7579  C CG  . LEU C 1 93  ? 11.198  16.062  -39.990 1.00 28.21  ? 122 LEU B CG  1 
ATOM   7580  C CD1 . LEU C 1 93  ? 12.329  16.214  -40.970 1.00 30.72  ? 122 LEU B CD1 1 
ATOM   7581  C CD2 . LEU C 1 93  ? 10.127  15.092  -40.452 1.00 31.32  ? 122 LEU B CD2 1 
ATOM   7582  N N   . LEU C 1 94  ? 11.040  18.131  -37.216 1.00 25.61  ? 123 LEU B N   1 
ATOM   7583  C CA  . LEU C 1 94  ? 10.415  19.454  -37.157 1.00 26.30  ? 123 LEU B CA  1 
ATOM   7584  C C   . LEU C 1 94  ? 11.391  20.546  -36.739 1.00 23.90  ? 123 LEU B C   1 
ATOM   7585  O O   . LEU C 1 94  ? 11.398  21.621  -37.323 1.00 29.14  ? 123 LEU B O   1 
ATOM   7586  C CB  . LEU C 1 94  ? 9.204   19.425  -36.239 1.00 28.26  ? 123 LEU B CB  1 
ATOM   7587  C CG  . LEU C 1 94  ? 8.020   18.598  -36.752 1.00 28.66  ? 123 LEU B CG  1 
ATOM   7588  C CD1 . LEU C 1 94  ? 6.848   19.025  -35.910 1.00 26.83  ? 123 LEU B CD1 1 
ATOM   7589  C CD2 . LEU C 1 94  ? 7.720   18.784  -38.242 1.00 26.99  ? 123 LEU B CD2 1 
ATOM   7590  N N   . VAL C 1 95  ? 12.234  20.277  -35.748 1.00 27.13  ? 124 VAL B N   1 
ATOM   7591  C CA  . VAL C 1 95  ? 13.186  21.249  -35.239 1.00 29.87  ? 124 VAL B CA  1 
ATOM   7592  C C   . VAL C 1 95  ? 14.328  21.507  -36.237 1.00 32.42  ? 124 VAL B C   1 
ATOM   7593  O O   . VAL C 1 95  ? 14.758  22.657  -36.394 1.00 30.93  ? 124 VAL B O   1 
ATOM   7594  C CB  . VAL C 1 95  ? 13.713  20.738  -33.877 1.00 33.66  ? 124 VAL B CB  1 
ATOM   7595  C CG1 . VAL C 1 95  ? 15.046  21.346  -33.509 1.00 38.40  ? 124 VAL B CG1 1 
ATOM   7596  C CG2 . VAL C 1 95  ? 12.720  21.025  -32.771 1.00 33.83  ? 124 VAL B CG2 1 
ATOM   7597  N N   . THR C 1 96  ? 14.875  20.460  -36.868 1.00 29.65  ? 125 THR B N   1 
ATOM   7598  C CA  . THR C 1 96  ? 16.135  20.620  -37.590 1.00 31.91  ? 125 THR B CA  1 
ATOM   7599  C C   . THR C 1 96  ? 15.932  20.681  -39.094 1.00 33.09  ? 125 THR B C   1 
ATOM   7600  O O   . THR C 1 96  ? 16.844  21.072  -39.808 1.00 31.63  ? 125 THR B O   1 
ATOM   7601  C CB  . THR C 1 96  ? 17.110  19.489  -37.297 1.00 30.06  ? 125 THR B CB  1 
ATOM   7602  O OG1 . THR C 1 96  ? 16.455  18.378  -37.875 1.00 27.39  ? 125 THR B OG1 1 
ATOM   7603  C CG2 . THR C 1 96  ? 17.285  19.297  -35.811 1.00 31.66  ? 125 THR B CG2 1 
ATOM   7604  N N   . GLY C 1 97  ? 14.771  20.209  -39.548 1.00 33.70  ? 126 GLY B N   1 
ATOM   7605  C CA  . GLY C 1 97  ? 14.526  19.974  -40.952 1.00 34.58  ? 126 GLY B CA  1 
ATOM   7606  C C   . GLY C 1 97  ? 15.146  18.666  -41.457 1.00 31.46  ? 126 GLY B C   1 
ATOM   7607  O O   . GLY C 1 97  ? 14.968  18.385  -42.625 1.00 33.32  ? 126 GLY B O   1 
ATOM   7608  N N   . HIS C 1 98  ? 15.799  17.867  -40.594 1.00 29.63  ? 127 HIS B N   1 
ATOM   7609  C CA  . HIS C 1 98  ? 16.502  16.662  -41.005 1.00 31.24  ? 127 HIS B CA  1 
ATOM   7610  C C   . HIS C 1 98  ? 15.931  15.448  -40.302 1.00 34.15  ? 127 HIS B C   1 
ATOM   7611  O O   . HIS C 1 98  ? 15.464  15.503  -39.168 1.00 28.59  ? 127 HIS B O   1 
ATOM   7612  C CB  . HIS C 1 98  ? 17.998  16.747  -40.680 1.00 45.00  ? 127 HIS B CB  1 
ATOM   7613  C CG  . HIS C 1 98  ? 18.639  17.939  -41.317 1.00 48.07  ? 127 HIS B CG  1 
ATOM   7614  N ND1 . HIS C 1 98  ? 19.522  18.790  -40.681 1.00 54.54  ? 127 HIS B ND1 1 
ATOM   7615  C CD2 . HIS C 1 98  ? 18.444  18.448  -42.538 1.00 54.31  ? 127 HIS B CD2 1 
ATOM   7616  C CE1 . HIS C 1 98  ? 19.868  19.754  -41.517 1.00 55.80  ? 127 HIS B CE1 1 
ATOM   7617  N NE2 . HIS C 1 98  ? 19.195  19.584  -42.643 1.00 51.99  ? 127 HIS B NE2 1 
ATOM   7618  N N   . ILE C 1 99  ? 15.972  14.336  -41.020 1.00 34.34  ? 128 ILE B N   1 
ATOM   7619  C CA  . ILE C 1 99  ? 15.556  13.070  -40.479 1.00 34.84  ? 128 ILE B CA  1 
ATOM   7620  C C   . ILE C 1 99  ? 16.601  12.689  -39.442 1.00 35.05  ? 128 ILE B C   1 
ATOM   7621  O O   . ILE C 1 99  ? 17.780  12.677  -39.761 1.00 33.99  ? 128 ILE B O   1 
ATOM   7622  C CB  . ILE C 1 99  ? 15.472  12.016  -41.607 1.00 32.88  ? 128 ILE B CB  1 
ATOM   7623  C CG1 . ILE C 1 99  ? 14.392  12.363  -42.634 1.00 34.74  ? 128 ILE B CG1 1 
ATOM   7624  C CG2 . ILE C 1 99  ? 15.264  10.632  -41.000 1.00 28.88  ? 128 ILE B CG2 1 
ATOM   7625  C CD1 . ILE C 1 99  ? 12.980  12.284  -42.095 1.00 31.52  ? 128 ILE B CD1 1 
ATOM   7626  N N   . PRO C 1 100 ? 16.225  12.313  -38.203 1.00 30.34  ? 129 PRO B N   1 
ATOM   7627  C CA  . PRO C 1 100 ? 17.217  11.913  -37.215 1.00 30.63  ? 129 PRO B CA  1 
ATOM   7628  C C   . PRO C 1 100 ? 17.806  10.548  -37.553 1.00 31.19  ? 129 PRO B C   1 
ATOM   7629  O O   . PRO C 1 100 ? 17.102  9.728   -38.132 1.00 31.54  ? 129 PRO B O   1 
ATOM   7630  C CB  . PRO C 1 100 ? 16.409  11.831  -35.913 1.00 25.51  ? 129 PRO B CB  1 
ATOM   7631  C CG  . PRO C 1 100 ? 15.061  11.449  -36.382 1.00 25.87  ? 129 PRO B CG  1 
ATOM   7632  C CD  . PRO C 1 100 ? 14.860  12.212  -37.703 1.00 27.19  ? 129 PRO B CD  1 
ATOM   7633  N N   . THR C 1 101 ? 19.046  10.315  -37.078 1.00 30.71  ? 130 THR B N   1 
ATOM   7634  C CA  . THR C 1 101 ? 19.618  8.981   -36.936 1.00 33.21  ? 130 THR B CA  1 
ATOM   7635  C C   . THR C 1 101 ? 19.015  8.278   -35.719 1.00 34.33  ? 130 THR B C   1 
ATOM   7636  O O   . THR C 1 101 ? 18.346  8.899   -34.900 1.00 36.51  ? 130 THR B O   1 
ATOM   7637  C CB  . THR C 1 101 ? 21.135  9.072   -36.779 1.00 35.83  ? 130 THR B CB  1 
ATOM   7638  O OG1 . THR C 1 101 ? 21.377  9.706   -35.520 1.00 34.11  ? 130 THR B OG1 1 
ATOM   7639  C CG2 . THR C 1 101 ? 21.813  9.791   -37.936 1.00 36.47  ? 130 THR B CG2 1 
ATOM   7640  N N   . GLU C 1 102 ? 19.245  6.968   -35.617 1.00 33.50  ? 131 GLU B N   1 
ATOM   7641  C CA  . GLU C 1 102 ? 18.859  6.168   -34.464 1.00 40.73  ? 131 GLU B CA  1 
ATOM   7642  C C   . GLU C 1 102 ? 19.485  6.733   -33.185 1.00 35.72  ? 131 GLU B C   1 
ATOM   7643  O O   . GLU C 1 102 ? 18.853  6.750   -32.146 1.00 31.23  ? 131 GLU B O   1 
ATOM   7644  C CB  . GLU C 1 102 ? 19.402  4.733   -34.539 1.00 49.07  ? 131 GLU B CB  1 
ATOM   7645  C CG  . GLU C 1 102 ? 18.821  3.879   -35.663 1.00 50.39  ? 131 GLU B CG  1 
ATOM   7646  C CD  . GLU C 1 102 ? 17.341  3.554   -35.506 1.00 57.33  ? 131 GLU B CD  1 
ATOM   7647  O OE1 . GLU C 1 102 ? 16.813  3.556   -34.370 1.00 59.08  ? 131 GLU B OE1 1 
ATOM   7648  O OE2 . GLU C 1 102 ? 16.699  3.344   -36.555 1.00 62.45  ? 131 GLU B OE2 1 
ATOM   7649  N N   . GLU C 1 103 ? 20.741  7.166   -33.263 1.00 35.10  ? 132 GLU B N   1 
ATOM   7650  C CA  . GLU C 1 103 ? 21.453  7.627   -32.087 1.00 39.95  ? 132 GLU B CA  1 
ATOM   7651  C C   . GLU C 1 103 ? 20.824  8.937   -31.588 1.00 34.42  ? 132 GLU B C   1 
ATOM   7652  O O   . GLU C 1 103 ? 20.732  9.174   -30.393 1.00 35.46  ? 132 GLU B O   1 
ATOM   7653  C CB  . GLU C 1 103 ? 22.932  7.773   -32.442 1.00 41.24  ? 132 GLU B CB  1 
ATOM   7654  C CG  . GLU C 1 103 ? 23.584  6.475   -32.937 1.00 53.20  ? 132 GLU B CG  1 
ATOM   7655  C CD  . GLU C 1 103 ? 23.121  5.848   -34.261 1.00 54.73  ? 132 GLU B CD  1 
ATOM   7656  O OE1 . GLU C 1 103 ? 22.920  6.508   -35.315 1.00 47.83  ? 132 GLU B OE1 1 
ATOM   7657  O OE2 . GLU C 1 103 ? 22.959  4.611   -34.229 1.00 70.37  ? 132 GLU B OE2 1 
ATOM   7658  N N   . GLN C 1 104 ? 20.393  9.780   -32.515 1.00 31.02  ? 133 GLN B N   1 
ATOM   7659  C CA  . GLN C 1 104 ? 19.792  11.069  -32.190 1.00 33.39  ? 133 GLN B CA  1 
ATOM   7660  C C   . GLN C 1 104 ? 18.465  10.898  -31.463 1.00 32.60  ? 133 GLN B C   1 
ATOM   7661  O O   . GLN C 1 104 ? 18.256  11.509  -30.422 1.00 37.28  ? 133 GLN B O   1 
ATOM   7662  C CB  . GLN C 1 104 ? 19.663  11.870  -33.482 1.00 30.76  ? 133 GLN B CB  1 
ATOM   7663  C CG  . GLN C 1 104 ? 21.034  12.266  -34.012 1.00 31.26  ? 133 GLN B CG  1 
ATOM   7664  C CD  . GLN C 1 104 ? 20.992  13.070  -35.293 1.00 31.95  ? 133 GLN B CD  1 
ATOM   7665  O OE1 . GLN C 1 104 ? 20.135  12.876  -36.160 1.00 32.26  ? 133 GLN B OE1 1 
ATOM   7666  N NE2 . GLN C 1 104 ? 21.918  14.002  -35.408 1.00 32.56  ? 133 GLN B NE2 1 
ATOM   7667  N N   . VAL C 1 105 ? 17.604  10.038  -32.004 1.00 29.94  ? 134 VAL B N   1 
ATOM   7668  C CA  . VAL C 1 105 ? 16.352  9.696   -31.363 1.00 29.51  ? 134 VAL B CA  1 
ATOM   7669  C C   . VAL C 1 105 ? 16.627  9.079   -29.991 1.00 30.93  ? 134 VAL B C   1 
ATOM   7670  O O   . VAL C 1 105 ? 15.943  9.415   -29.016 1.00 29.79  ? 134 VAL B O   1 
ATOM   7671  C CB  . VAL C 1 105 ? 15.528  8.770   -32.287 1.00 29.46  ? 134 VAL B CB  1 
ATOM   7672  C CG1 . VAL C 1 105 ? 14.378  8.055   -31.577 1.00 30.75  ? 134 VAL B CG1 1 
ATOM   7673  C CG2 . VAL C 1 105 ? 15.035  9.521   -33.506 1.00 31.72  ? 134 VAL B CG2 1 
ATOM   7674  N N   . SER C 1 106 ? 17.624  8.195   -29.911 1.00 29.82  ? 135 SER B N   1 
ATOM   7675  C CA  A SER C 1 106 ? 17.990  7.584   -28.638 0.50 34.07  ? 135 SER B CA  1 
ATOM   7676  C CA  B SER C 1 106 ? 18.003  7.582   -28.641 0.50 34.22  ? 135 SER B CA  1 
ATOM   7677  C C   . SER C 1 106 ? 18.424  8.646   -27.624 1.00 29.69  ? 135 SER B C   1 
ATOM   7678  O O   . SER C 1 106 ? 17.989  8.639   -26.478 1.00 27.96  ? 135 SER B O   1 
ATOM   7679  C CB  A SER C 1 106 ? 19.051  6.530   -28.797 0.50 33.16  ? 135 SER B CB  1 
ATOM   7680  C CB  B SER C 1 106 ? 19.088  6.549   -28.824 0.50 33.58  ? 135 SER B CB  1 
ATOM   7681  O OG  A SER C 1 106 ? 19.306  5.922   -27.542 0.50 32.97  ? 135 SER B OG  1 
ATOM   7682  O OG  B SER C 1 106 ? 18.758  5.683   -29.900 0.50 33.66  ? 135 SER B OG  1 
ATOM   7683  N N   . TRP C 1 107 ? 19.276  9.573   -28.034 1.00 31.34  ? 136 TRP B N   1 
ATOM   7684  C CA  . TRP C 1 107 ? 19.692  10.651  -27.149 1.00 32.87  ? 136 TRP B CA  1 
ATOM   7685  C C   . TRP C 1 107 ? 18.491  11.530  -26.720 1.00 31.91  ? 136 TRP B C   1 
ATOM   7686  O O   . TRP C 1 107 ? 18.336  11.894  -25.570 1.00 30.03  ? 136 TRP B O   1 
ATOM   7687  C CB  . TRP C 1 107 ? 20.785  11.452  -27.860 1.00 36.38  ? 136 TRP B CB  1 
ATOM   7688  C CG  . TRP C 1 107 ? 21.227  12.642  -27.074 1.00 41.07  ? 136 TRP B CG  1 
ATOM   7689  C CD1 . TRP C 1 107 ? 22.228  12.721  -26.146 1.00 42.81  ? 136 TRP B CD1 1 
ATOM   7690  C CD2 . TRP C 1 107 ? 20.595  13.939  -27.122 1.00 38.86  ? 136 TRP B CD2 1 
ATOM   7691  N NE1 . TRP C 1 107 ? 22.297  14.004  -25.658 1.00 43.96  ? 136 TRP B NE1 1 
ATOM   7692  C CE2 . TRP C 1 107 ? 21.299  14.764  -26.217 1.00 41.78  ? 136 TRP B CE2 1 
ATOM   7693  C CE3 . TRP C 1 107 ? 19.530  14.474  -27.853 1.00 38.06  ? 136 TRP B CE3 1 
ATOM   7694  C CZ2 . TRP C 1 107 ? 20.941  16.093  -26.002 1.00 42.60  ? 136 TRP B CZ2 1 
ATOM   7695  C CZ3 . TRP C 1 107 ? 19.165  15.779  -27.623 1.00 40.43  ? 136 TRP B CZ3 1 
ATOM   7696  C CH2 . TRP C 1 107 ? 19.857  16.572  -26.698 1.00 41.51  ? 136 TRP B CH2 1 
ATOM   7697  N N   . LEU C 1 108 ? 17.569  11.818  -27.633 1.00 34.17  ? 137 LEU B N   1 
ATOM   7698  C CA  . LEU C 1 108 ? 16.391  12.598  -27.296 1.00 33.14  ? 137 LEU B CA  1 
ATOM   7699  C C   . LEU C 1 108 ? 15.479  11.866  -26.314 1.00 31.59  ? 137 LEU B C   1 
ATOM   7700  O O   . LEU C 1 108 ? 15.010  12.467  -25.366 1.00 31.38  ? 137 LEU B O   1 
ATOM   7701  C CB  . LEU C 1 108 ? 15.673  12.959  -28.581 1.00 35.20  ? 137 LEU B CB  1 
ATOM   7702  C CG  . LEU C 1 108 ? 14.573  14.006  -28.441 1.00 33.62  ? 137 LEU B CG  1 
ATOM   7703  C CD1 . LEU C 1 108 ? 15.044  15.239  -27.720 1.00 37.73  ? 137 LEU B CD1 1 
ATOM   7704  C CD2 . LEU C 1 108 ? 14.088  14.344  -29.839 1.00 32.67  ? 137 LEU B CD2 1 
ATOM   7705  N N   . SER C 1 109 ? 15.261  10.567  -26.485 1.00 32.03  ? 138 SER B N   1 
ATOM   7706  C CA  . SER C 1 109 ? 14.515  9.795   -25.495 1.00 31.73  ? 138 SER B CA  1 
ATOM   7707  C C   . SER C 1 109 ? 15.123  9.962   -24.097 1.00 33.84  ? 138 SER B C   1 
ATOM   7708  O O   . SER C 1 109 ? 14.385  10.182  -23.115 1.00 28.99  ? 138 SER B O   1 
ATOM   7709  C CB  . SER C 1 109 ? 14.422  8.336   -25.883 1.00 34.24  ? 138 SER B CB  1 
ATOM   7710  O OG  . SER C 1 109 ? 13.678  8.147   -27.092 1.00 31.84  ? 138 SER B OG  1 
ATOM   7711  N N   . LYS C 1 110 ? 16.463  9.907   -24.015 1.00 31.87  ? 139 LYS B N   1 
ATOM   7712  C CA  . LYS C 1 110 ? 17.132  9.980   -22.728 1.00 36.95  ? 139 LYS B CA  1 
ATOM   7713  C C   . LYS C 1 110 ? 16.930  11.372  -22.157 1.00 33.29  ? 139 LYS B C   1 
ATOM   7714  O O   . LYS C 1 110 ? 16.704  11.524  -20.956 1.00 30.37  ? 139 LYS B O   1 
ATOM   7715  C CB  . LYS C 1 110 ? 18.627  9.631   -22.774 1.00 44.65  ? 139 LYS B CB  1 
ATOM   7716  C CG  . LYS C 1 110 ? 18.926  8.140   -22.959 1.00 51.44  ? 139 LYS B CG  1 
ATOM   7717  C CD  . LYS C 1 110 ? 20.409  7.759   -23.027 1.00 55.00  ? 139 LYS B CD  1 
ATOM   7718  C CE  . LYS C 1 110 ? 20.746  6.561   -23.913 1.00 64.09  ? 139 LYS B CE  1 
ATOM   7719  N NZ  . LYS C 1 110 ? 21.141  6.918   -25.288 1.00 65.83  ? 139 LYS B NZ  1 
ATOM   7720  N N   . GLU C 1 111 ? 17.033  12.372  -23.034 1.00 32.18  ? 140 GLU B N   1 
ATOM   7721  C CA  . GLU C 1 111 ? 16.888  13.765  -22.641 1.00 37.10  ? 140 GLU B CA  1 
ATOM   7722  C C   . GLU C 1 111 ? 15.526  14.030  -22.013 1.00 36.79  ? 140 GLU B C   1 
ATOM   7723  O O   . GLU C 1 111 ? 15.452  14.672  -20.977 1.00 38.72  ? 140 GLU B O   1 
ATOM   7724  C CB  . GLU C 1 111 ? 17.041  14.676  -23.862 1.00 41.80  ? 140 GLU B CB  1 
ATOM   7725  C CG  . GLU C 1 111 ? 18.460  15.184  -24.035 1.00 44.32  ? 140 GLU B CG  1 
ATOM   7726  C CD  . GLU C 1 111 ? 18.884  16.046  -22.850 1.00 54.19  ? 140 GLU B CD  1 
ATOM   7727  O OE1 . GLU C 1 111 ? 18.204  17.046  -22.493 1.00 60.37  ? 140 GLU B OE1 1 
ATOM   7728  O OE2 . GLU C 1 111 ? 19.922  15.701  -22.280 1.00 43.49  ? 140 GLU B OE2 1 
ATOM   7729  N N   . TRP C 1 112 ? 14.456  13.570  -22.671 1.00 31.89  ? 141 TRP B N   1 
ATOM   7730  C CA  . TRP C 1 112 ? 13.109  13.794  -22.186 1.00 29.47  ? 141 TRP B CA  1 
ATOM   7731  C C   . TRP C 1 112 ? 12.871  12.984  -20.911 1.00 35.91  ? 141 TRP B C   1 
ATOM   7732  O O   . TRP C 1 112 ? 12.181  13.445  -19.990 1.00 32.39  ? 141 TRP B O   1 
ATOM   7733  C CB  . TRP C 1 112 ? 12.070  13.478  -23.269 1.00 29.55  ? 141 TRP B CB  1 
ATOM   7734  C CG  . TRP C 1 112 ? 12.004  14.502  -24.372 1.00 27.05  ? 141 TRP B CG  1 
ATOM   7735  C CD1 . TRP C 1 112 ? 12.627  15.710  -24.370 1.00 28.13  ? 141 TRP B CD1 1 
ATOM   7736  C CD2 . TRP C 1 112 ? 11.331  14.404  -25.638 1.00 26.12  ? 141 TRP B CD2 1 
ATOM   7737  N NE1 . TRP C 1 112 ? 12.413  16.359  -25.549 1.00 30.05  ? 141 TRP B NE1 1 
ATOM   7738  C CE2 . TRP C 1 112 ? 11.597  15.598  -26.335 1.00 29.33  ? 141 TRP B CE2 1 
ATOM   7739  C CE3 . TRP C 1 112 ? 10.537  13.441  -26.256 1.00 26.84  ? 141 TRP B CE3 1 
ATOM   7740  C CZ2 . TRP C 1 112 ? 11.106  15.844  -27.607 1.00 26.92  ? 141 TRP B CZ2 1 
ATOM   7741  C CZ3 . TRP C 1 112 ? 10.040  13.692  -27.507 1.00 29.24  ? 141 TRP B CZ3 1 
ATOM   7742  C CH2 . TRP C 1 112 ? 10.342  14.871  -28.188 1.00 25.60  ? 141 TRP B CH2 1 
ATOM   7743  N N   . ALA C 1 113 ? 13.475  11.790  -20.841 1.00 34.17  ? 142 ALA B N   1 
ATOM   7744  C CA  . ALA C 1 113 ? 13.431  10.990  -19.617 1.00 33.48  ? 142 ALA B CA  1 
ATOM   7745  C C   . ALA C 1 113 ? 14.024  11.739  -18.418 1.00 34.20  ? 142 ALA B C   1 
ATOM   7746  O O   . ALA C 1 113 ? 13.445  11.714  -17.325 1.00 36.89  ? 142 ALA B O   1 
ATOM   7747  C CB  . ALA C 1 113 ? 14.118  9.665   -19.833 1.00 33.66  ? 142 ALA B CB  1 
ATOM   7748  N N   . LYS C 1 114 ? 15.151  12.444  -18.602 1.00 34.47  ? 143 LYS B N   1 
ATOM   7749  C CA  . LYS C 1 114 ? 15.830  13.052  -17.461 1.00 34.83  ? 143 LYS B CA  1 
ATOM   7750  C C   . LYS C 1 114 ? 15.068  14.272  -16.939 1.00 34.14  ? 143 LYS B C   1 
ATOM   7751  O O   . LYS C 1 114 ? 15.234  14.671  -15.791 1.00 33.96  ? 143 LYS B O   1 
ATOM   7752  C CB  . LYS C 1 114 ? 17.205  13.623  -17.815 1.00 41.20  ? 143 LYS B CB  1 
ATOM   7753  C CG  . LYS C 1 114 ? 18.290  12.635  -18.182 1.00 55.82  ? 143 LYS B CG  1 
ATOM   7754  C CD  . LYS C 1 114 ? 19.592  13.346  -18.546 1.00 65.66  ? 143 LYS B CD  1 
ATOM   7755  C CE  . LYS C 1 114 ? 20.595  12.490  -19.274 1.00 68.96  ? 143 LYS B CE  1 
ATOM   7756  N NZ  . LYS C 1 114 ? 21.657  13.346  -19.817 1.00 66.42  ? 143 LYS B NZ  1 
ATOM   7757  N N   . ARG C 1 115 ? 14.249  14.900  -17.795 1.00 33.05  ? 144 ARG B N   1 
ATOM   7758  C CA  . ARG C 1 115 ? 13.655  16.190  -17.466 1.00 32.26  ? 144 ARG B CA  1 
ATOM   7759  C C   . ARG C 1 115 ? 12.245  16.089  -16.889 1.00 32.40  ? 144 ARG B C   1 
ATOM   7760  O O   . ARG C 1 115 ? 11.648  17.120  -16.643 1.00 41.00  ? 144 ARG B O   1 
ATOM   7761  C CB  . ARG C 1 115 ? 13.646  17.071  -18.726 1.00 30.79  ? 144 ARG B CB  1 
ATOM   7762  C CG  . ARG C 1 115 ? 15.025  17.498  -19.212 1.00 31.83  ? 144 ARG B CG  1 
ATOM   7763  C CD  . ARG C 1 115 ? 14.867  18.111  -20.591 1.00 31.60  ? 144 ARG B CD  1 
ATOM   7764  N NE  . ARG C 1 115 ? 16.114  18.659  -21.142 1.00 35.25  ? 144 ARG B NE  1 
ATOM   7765  C CZ  . ARG C 1 115 ? 16.424  19.940  -21.257 1.00 37.74  ? 144 ARG B CZ  1 
ATOM   7766  N NH1 . ARG C 1 115 ? 15.719  20.870  -20.622 1.00 36.90  ? 144 ARG B NH1 1 
ATOM   7767  N NH2 . ARG C 1 115 ? 17.490  20.280  -21.957 1.00 37.96  ? 144 ARG B NH2 1 
ATOM   7768  N N   . ALA C 1 116 ? 11.728  14.888  -16.624 1.00 33.44  ? 145 ALA B N   1 
ATOM   7769  C CA  . ALA C 1 116 ? 10.287  14.672  -16.559 1.00 41.46  ? 145 ALA B CA  1 
ATOM   7770  C C   . ALA C 1 116 ? 9.654   14.888  -15.169 1.00 44.34  ? 145 ALA B C   1 
ATOM   7771  O O   . ALA C 1 116 ? 8.441   14.701  -15.021 1.00 52.85  ? 145 ALA B O   1 
ATOM   7772  C CB  . ALA C 1 116 ? 9.970   13.288  -17.114 1.00 37.83  ? 145 ALA B CB  1 
ATOM   7773  N N   . ALA C 1 117 ? 10.419  15.329  -14.165 1.00 41.27  ? 146 ALA B N   1 
ATOM   7774  C CA  . ALA C 1 117 ? 9.912   15.483  -12.801 1.00 43.58  ? 146 ALA B CA  1 
ATOM   7775  C C   . ALA C 1 117 ? 8.877   16.602  -12.713 1.00 37.81  ? 146 ALA B C   1 
ATOM   7776  O O   . ALA C 1 117 ? 9.049   17.642  -13.344 1.00 36.63  ? 146 ALA B O   1 
ATOM   7777  C CB  . ALA C 1 117 ? 11.065  15.782  -11.862 1.00 43.40  ? 146 ALA B CB  1 
ATOM   7778  N N   . LEU C 1 118 ? 7.818   16.408  -11.924 1.00 30.10  ? 147 LEU B N   1 
ATOM   7779  C CA  . LEU C 1 118 ? 6.897   17.503  -11.661 1.00 31.11  ? 147 LEU B CA  1 
ATOM   7780  C C   . LEU C 1 118 ? 7.192   18.154  -10.307 1.00 36.13  ? 147 LEU B C   1 
ATOM   7781  O O   . LEU C 1 118 ? 7.617   17.470  -9.370  1.00 34.59  ? 147 LEU B O   1 
ATOM   7782  C CB  . LEU C 1 118 ? 5.450   17.018  -11.714 1.00 31.86  ? 147 LEU B CB  1 
ATOM   7783  C CG  . LEU C 1 118 ? 5.013   16.351  -13.009 1.00 30.87  ? 147 LEU B CG  1 
ATOM   7784  C CD1 . LEU C 1 118 ? 3.571   15.958  -12.841 1.00 34.77  ? 147 LEU B CD1 1 
ATOM   7785  C CD2 . LEU C 1 118 ? 5.219   17.278  -14.169 1.00 31.34  ? 147 LEU B CD2 1 
ATOM   7786  N N   . PRO C 1 119 ? 6.978   19.489  -10.136 1.00 32.85  ? 148 PRO B N   1 
ATOM   7787  C CA  . PRO C 1 119 ? 7.029   20.098  -8.803  1.00 35.16  ? 148 PRO B CA  1 
ATOM   7788  C C   . PRO C 1 119 ? 5.779   19.784  -7.969  1.00 31.87  ? 148 PRO B C   1 
ATOM   7789  O O   . PRO C 1 119 ? 4.699   19.482  -8.474  1.00 30.24  ? 148 PRO B O   1 
ATOM   7790  C CB  . PRO C 1 119 ? 7.222   21.606  -9.075  1.00 35.70  ? 148 PRO B CB  1 
ATOM   7791  C CG  . PRO C 1 119 ? 6.568   21.801  -10.430 1.00 34.24  ? 148 PRO B CG  1 
ATOM   7792  C CD  . PRO C 1 119 ? 6.681   20.464  -11.195 1.00 31.35  ? 148 PRO B CD  1 
ATOM   7793  N N   . SER C 1 120 ? 5.939   19.889  -6.662  1.00 32.21  ? 149 SER B N   1 
ATOM   7794  C CA  . SER C 1 120 ? 4.959   19.398  -5.713  1.00 31.80  ? 149 SER B CA  1 
ATOM   7795  C C   . SER C 1 120 ? 3.634   20.100  -5.933  1.00 29.31  ? 149 SER B C   1 
ATOM   7796  O O   . SER C 1 120 ? 2.578   19.477  -5.853  1.00 30.30  ? 149 SER B O   1 
ATOM   7797  C CB  . SER C 1 120 ? 5.450   19.589  -4.319  1.00 32.34  ? 149 SER B CB  1 
ATOM   7798  O OG  . SER C 1 120 ? 6.658   18.859  -4.217  1.00 30.05  ? 149 SER B OG  1 
ATOM   7799  N N   . HIS C 1 121 ? 3.702   21.379  -6.281  1.00 27.45  ? 150 HIS B N   1 
ATOM   7800  C CA  . HIS C 1 121 ? 2.480   22.147  -6.341  1.00 27.74  ? 150 HIS B CA  1 
ATOM   7801  C C   . HIS C 1 121 ? 1.642   21.620  -7.495  1.00 27.57  ? 150 HIS B C   1 
ATOM   7802  O O   . HIS C 1 121 ? 0.420   21.644  -7.410  1.00 27.41  ? 150 HIS B O   1 
ATOM   7803  C CB  . HIS C 1 121 ? 2.713   23.656  -6.433  1.00 27.89  ? 150 HIS B CB  1 
ATOM   7804  C CG  . HIS C 1 121 ? 3.284   24.188  -7.695  1.00 29.46  ? 150 HIS B CG  1 
ATOM   7805  N ND1 . HIS C 1 121 ? 4.618   24.058  -8.012  1.00 32.37  ? 150 HIS B ND1 1 
ATOM   7806  C CD2 . HIS C 1 121 ? 2.722   24.864  -8.688  1.00 30.28  ? 150 HIS B CD2 1 
ATOM   7807  C CE1 . HIS C 1 121 ? 4.830   24.649  -9.170  1.00 35.07  ? 150 HIS B CE1 1 
ATOM   7808  N NE2 . HIS C 1 121 ? 3.696   25.160  -9.588  1.00 31.58  ? 150 HIS B NE2 1 
ATOM   7809  N N   . VAL C 1 122 ? 2.305   21.118  -8.541  1.00 28.30  ? 151 VAL B N   1 
ATOM   7810  C CA  . VAL C 1 122 ? 1.576   20.673  -9.711  1.00 29.32  ? 151 VAL B CA  1 
ATOM   7811  C C   . VAL C 1 122 ? 0.939   19.325  -9.422  1.00 28.74  ? 151 VAL B C   1 
ATOM   7812  O O   . VAL C 1 122 ? -0.242  19.121  -9.699  1.00 32.44  ? 151 VAL B O   1 
ATOM   7813  C CB  . VAL C 1 122 ? 2.430   20.644  -10.984 1.00 26.00  ? 151 VAL B CB  1 
ATOM   7814  C CG1 . VAL C 1 122 ? 1.692   19.998  -12.153 1.00 25.55  ? 151 VAL B CG1 1 
ATOM   7815  C CG2 . VAL C 1 122 ? 2.825   22.066  -11.354 1.00 24.30  ? 151 VAL B CG2 1 
ATOM   7816  N N   . VAL C 1 123 ? 1.729   18.431  -8.860  1.00 31.35  ? 152 VAL B N   1 
ATOM   7817  C CA  . VAL C 1 123 ? 1.221   17.143  -8.403  1.00 29.26  ? 152 VAL B CA  1 
ATOM   7818  C C   . VAL C 1 123 ? -0.019  17.316  -7.536  1.00 28.00  ? 152 VAL B C   1 
ATOM   7819  O O   . VAL C 1 123 ? -0.989  16.604  -7.708  1.00 31.63  ? 152 VAL B O   1 
ATOM   7820  C CB  . VAL C 1 123 ? 2.322   16.369  -7.660  1.00 32.17  ? 152 VAL B CB  1 
ATOM   7821  C CG1 . VAL C 1 123 ? 1.805   15.058  -7.041  1.00 36.61  ? 152 VAL B CG1 1 
ATOM   7822  C CG2 . VAL C 1 123 ? 3.503   16.063  -8.572  1.00 36.18  ? 152 VAL B CG2 1 
ATOM   7823  N N   . THR C 1 124 ? 0.056   18.210  -6.554  1.00 30.64  ? 153 THR B N   1 
ATOM   7824  C CA  . THR C 1 124 ? -0.985  18.417  -5.566  1.00 29.90  ? 153 THR B CA  1 
ATOM   7825  C C   . THR C 1 124 ? -2.232  18.970  -6.223  1.00 32.70  ? 153 THR B C   1 
ATOM   7826  O O   . THR C 1 124 ? -3.342  18.555  -5.903  1.00 33.05  ? 153 THR B O   1 
ATOM   7827  C CB  . THR C 1 124 ? -0.440  19.399  -4.532  1.00 31.25  ? 153 THR B CB  1 
ATOM   7828  O OG1 . THR C 1 124 ? 0.542   18.593  -3.917  1.00 34.00  ? 153 THR B OG1 1 
ATOM   7829  C CG2 . THR C 1 124 ? -1.461  19.866  -3.512  1.00 33.09  ? 153 THR B CG2 1 
ATOM   7830  N N   . MET C 1 125 ? -2.032  19.963  -7.103  1.00 32.37  ? 154 MET B N   1 
ATOM   7831  C CA  . MET C 1 125 ? -3.118  20.573  -7.846  1.00 34.04  ? 154 MET B CA  1 
ATOM   7832  C C   . MET C 1 125 ? -3.935  19.529  -8.618  1.00 34.38  ? 154 MET B C   1 
ATOM   7833  O O   . MET C 1 125 ? -5.167  19.560  -8.634  1.00 30.91  ? 154 MET B O   1 
ATOM   7834  C CB  . MET C 1 125 ? -2.463  21.565  -8.804  1.00 41.95  ? 154 MET B CB  1 
ATOM   7835  C CG  . MET C 1 125 ? -3.311  22.028  -9.937  1.00 48.61  ? 154 MET B CG  1 
ATOM   7836  S SD  . MET C 1 125 ? -2.373  23.198  -10.944 1.00 49.01  ? 154 MET B SD  1 
ATOM   7837  C CE  . MET C 1 125 ? -3.803  24.177  -11.390 1.00 46.81  ? 154 MET B CE  1 
ATOM   7838  N N   . LEU C 1 126 ? -3.240  18.628  -9.323  1.00 32.55  ? 155 LEU B N   1 
ATOM   7839  C CA  . LEU C 1 126 ? -3.886  17.559  -10.067 1.00 32.13  ? 155 LEU B CA  1 
ATOM   7840  C C   . LEU C 1 126 ? -4.636  16.589  -9.145  1.00 40.44  ? 155 LEU B C   1 
ATOM   7841  O O   . LEU C 1 126 ? -5.716  16.124  -9.488  1.00 41.97  ? 155 LEU B O   1 
ATOM   7842  C CB  . LEU C 1 126 ? -2.804  16.816  -10.836 1.00 29.36  ? 155 LEU B CB  1 
ATOM   7843  C CG  . LEU C 1 126 ? -2.298  17.523  -12.097 1.00 31.00  ? 155 LEU B CG  1 
ATOM   7844  C CD1 . LEU C 1 126 ? -1.028  16.864  -12.623 1.00 30.44  ? 155 LEU B CD1 1 
ATOM   7845  C CD2 . LEU C 1 126 ? -3.366  17.455  -13.148 1.00 37.22  ? 155 LEU B CD2 1 
ATOM   7846  N N   . ASP C 1 127 ? -4.046  16.269  -7.986  1.00 36.73  ? 156 ASP B N   1 
ATOM   7847  C CA  . ASP C 1 127 ? -4.631  15.317  -7.059  1.00 39.66  ? 156 ASP B CA  1 
ATOM   7848  C C   . ASP C 1 127 ? -5.832  15.917  -6.334  1.00 39.34  ? 156 ASP B C   1 
ATOM   7849  O O   . ASP C 1 127 ? -6.594  15.189  -5.691  1.00 44.62  ? 156 ASP B O   1 
ATOM   7850  C CB  . ASP C 1 127 ? -3.606  14.858  -6.031  1.00 38.02  ? 156 ASP B CB  1 
ATOM   7851  C CG  . ASP C 1 127 ? -2.485  13.975  -6.558  1.00 43.21  ? 156 ASP B CG  1 
ATOM   7852  O OD1 . ASP C 1 127 ? -2.653  13.358  -7.661  1.00 36.80  ? 156 ASP B OD1 1 
ATOM   7853  O OD2 . ASP C 1 127 ? -1.437  13.906  -5.860  1.00 54.20  ? 156 ASP B OD2 1 
ATOM   7854  N N   . ASN C 1 128 ? -5.962  17.242  -6.367  1.00 36.67  ? 157 ASN B N   1 
ATOM   7855  C CA  . ASN C 1 128 ? -7.079  17.896  -5.713  1.00 41.95  ? 157 ASN B CA  1 
ATOM   7856  C C   . ASN C 1 128 ? -8.165  18.281  -6.713  1.00 40.43  ? 157 ASN B C   1 
ATOM   7857  O O   . ASN C 1 128 ? -9.236  18.689  -6.304  1.00 40.40  ? 157 ASN B O   1 
ATOM   7858  C CB  . ASN C 1 128 ? -6.643  19.105  -4.893  1.00 42.76  ? 157 ASN B CB  1 
ATOM   7859  C CG  . ASN C 1 128 ? -5.703  18.742  -3.758  1.00 44.93  ? 157 ASN B CG  1 
ATOM   7860  O OD1 . ASN C 1 128 ? -5.956  17.813  -2.993  1.00 45.07  ? 157 ASN B OD1 1 
ATOM   7861  N ND2 . ASN C 1 128 ? -4.625  19.492  -3.597  1.00 50.68  ? 157 ASN B ND2 1 
ATOM   7862  N N   . PHE C 1 129 ? -7.902  18.194  -8.017  1.00 38.26  ? 158 PHE B N   1 
ATOM   7863  C CA  . PHE C 1 129 ? -8.933  18.544  -8.979  1.00 41.56  ? 158 PHE B CA  1 
ATOM   7864  C C   . PHE C 1 129 ? -10.163 17.676  -8.706  1.00 39.33  ? 158 PHE B C   1 
ATOM   7865  O O   . PHE C 1 129 ? -10.038 16.500  -8.392  1.00 46.11  ? 158 PHE B O   1 
ATOM   7866  C CB  . PHE C 1 129 ? -8.405  18.427  -10.415 1.00 35.50  ? 158 PHE B CB  1 
ATOM   7867  C CG  . PHE C 1 129 ? -7.652  19.648  -10.911 1.00 34.64  ? 158 PHE B CG  1 
ATOM   7868  C CD1 . PHE C 1 129 ? -7.943  20.913  -10.433 1.00 35.41  ? 158 PHE B CD1 1 
ATOM   7869  C CD2 . PHE C 1 129 ? -6.663  19.520  -11.870 1.00 37.64  ? 158 PHE B CD2 1 
ATOM   7870  C CE1 . PHE C 1 129 ? -7.256  22.023  -10.903 1.00 38.83  ? 158 PHE B CE1 1 
ATOM   7871  C CE2 . PHE C 1 129 ? -5.990  20.631  -12.341 1.00 35.82  ? 158 PHE B CE2 1 
ATOM   7872  C CZ  . PHE C 1 129 ? -6.298  21.877  -11.867 1.00 34.84  ? 158 PHE B CZ  1 
ATOM   7873  N N   . PRO C 1 130 ? -11.387 18.223  -8.811  1.00 38.20  ? 159 PRO B N   1 
ATOM   7874  C CA  . PRO C 1 130 ? -12.602 17.408  -8.760  1.00 36.98  ? 159 PRO B CA  1 
ATOM   7875  C C   . PRO C 1 130 ? -12.830 16.631  -10.050 1.00 35.37  ? 159 PRO B C   1 
ATOM   7876  O O   . PRO C 1 130 ? -12.241 16.942  -11.079 1.00 31.30  ? 159 PRO B O   1 
ATOM   7877  C CB  . PRO C 1 130 ? -13.728 18.404  -8.484  1.00 33.92  ? 159 PRO B CB  1 
ATOM   7878  C CG  . PRO C 1 130 ? -13.209 19.719  -8.974  1.00 36.84  ? 159 PRO B CG  1 
ATOM   7879  C CD  . PRO C 1 130 ? -11.682 19.657  -8.930  1.00 38.49  ? 159 PRO B CD  1 
ATOM   7880  N N   . THR C 1 131 ? -13.717 15.635  -9.977  1.00 35.10  ? 160 THR B N   1 
ATOM   7881  C CA  . THR C 1 131 ? -13.894 14.683  -11.060 1.00 39.09  ? 160 THR B CA  1 
ATOM   7882  C C   . THR C 1 131 ? -14.807 15.270  -12.127 1.00 34.17  ? 160 THR B C   1 
ATOM   7883  O O   . THR C 1 131 ? -14.914 14.701  -13.204 1.00 43.53  ? 160 THR B O   1 
ATOM   7884  C CB  . THR C 1 131 ? -14.468 13.367  -10.534 1.00 48.56  ? 160 THR B CB  1 
ATOM   7885  O OG1 . THR C 1 131 ? -15.810 13.715  -10.204 1.00 52.22  ? 160 THR B OG1 1 
ATOM   7886  C CG2 . THR C 1 131 ? -13.691 12.797  -9.361  1.00 48.92  ? 160 THR B CG2 1 
ATOM   7887  N N   . ASN C 1 132 ? -15.480 16.390  -11.839 1.00 36.45  ? 161 ASN B N   1 
ATOM   7888  C CA  . ASN C 1 132 ? -16.337 17.019  -12.825 1.00 36.32  ? 161 ASN B CA  1 
ATOM   7889  C C   . ASN C 1 132 ? -15.557 18.105  -13.563 1.00 38.47  ? 161 ASN B C   1 
ATOM   7890  O O   . ASN C 1 132 ? -16.168 18.812  -14.350 1.00 46.55  ? 161 ASN B O   1 
ATOM   7891  C CB  . ASN C 1 132 ? -17.600 17.626  -12.210 1.00 36.23  ? 161 ASN B CB  1 
ATOM   7892  C CG  . ASN C 1 132 ? -17.266 18.703  -11.209 1.00 41.07  ? 161 ASN B CG  1 
ATOM   7893  O OD1 . ASN C 1 132 ? -16.290 18.560  -10.472 1.00 38.62  ? 161 ASN B OD1 1 
ATOM   7894  N ND2 . ASN C 1 132 ? -18.022 19.789  -11.182 1.00 44.27  ? 161 ASN B ND2 1 
ATOM   7895  N N   . LEU C 1 133 ? -14.252 18.279  -13.260 1.00 34.65  ? 162 LEU B N   1 
ATOM   7896  C CA  . LEU C 1 133 ? -13.380 19.157  -14.038 1.00 31.50  ? 162 LEU B CA  1 
ATOM   7897  C C   . LEU C 1 133 ? -12.841 18.407  -15.261 1.00 28.59  ? 162 LEU B C   1 
ATOM   7898  O O   . LEU C 1 133 ? -12.143 17.418  -15.151 1.00 31.31  ? 162 LEU B O   1 
ATOM   7899  C CB  . LEU C 1 133 ? -12.250 19.704  -13.182 1.00 31.43  ? 162 LEU B CB  1 
ATOM   7900  C CG  . LEU C 1 133 ? -11.364 20.747  -13.872 1.00 32.17  ? 162 LEU B CG  1 
ATOM   7901  C CD1 . LEU C 1 133 ? -12.177 21.890  -14.478 1.00 34.24  ? 162 LEU B CD1 1 
ATOM   7902  C CD2 . LEU C 1 133 ? -10.307 21.249  -12.884 1.00 32.17  ? 162 LEU B CD2 1 
ATOM   7903  N N   . HIS C 1 134 ? -13.186 18.876  -16.454 1.00 31.20  ? 163 HIS B N   1 
ATOM   7904  C CA  . HIS C 1 134 ? -12.905 18.142  -17.679 1.00 31.70  ? 163 HIS B CA  1 
ATOM   7905  C C   . HIS C 1 134 ? -11.410 17.875  -17.742 1.00 27.84  ? 163 HIS B C   1 
ATOM   7906  O O   . HIS C 1 134 ? -10.667 18.723  -17.294 1.00 28.73  ? 163 HIS B O   1 
ATOM   7907  C CB  . HIS C 1 134 ? -13.413 19.010  -18.841 1.00 34.01  ? 163 HIS B CB  1 
ATOM   7908  C CG  . HIS C 1 134 ? -13.314 18.343  -20.149 1.00 36.25  ? 163 HIS B CG  1 
ATOM   7909  N ND1 . HIS C 1 134 ? -12.111 18.131  -20.783 1.00 39.27  ? 163 HIS B ND1 1 
ATOM   7910  C CD2 . HIS C 1 134 ? -14.254 17.750  -20.905 1.00 40.22  ? 163 HIS B CD2 1 
ATOM   7911  C CE1 . HIS C 1 134 ? -12.312 17.449  -21.898 1.00 36.03  ? 163 HIS B CE1 1 
ATOM   7912  N NE2 . HIS C 1 134 ? -13.606 17.216  -21.992 1.00 39.83  ? 163 HIS B NE2 1 
ATOM   7913  N N   . PRO C 1 135 ? -10.889 16.744  -18.285 1.00 31.71  ? 164 PRO B N   1 
ATOM   7914  C CA  . PRO C 1 135 ? -9.437  16.537  -18.375 1.00 29.50  ? 164 PRO B CA  1 
ATOM   7915  C C   . PRO C 1 135 ? -8.636  17.616  -19.118 1.00 29.36  ? 164 PRO B C   1 
ATOM   7916  O O   . PRO C 1 135 ? -7.461  17.863  -18.786 1.00 28.49  ? 164 PRO B O   1 
ATOM   7917  C CB  . PRO C 1 135 ? -9.251  15.170  -19.041 1.00 32.29  ? 164 PRO B CB  1 
ATOM   7918  C CG  . PRO C 1 135 ? -10.624 14.740  -19.459 1.00 32.30  ? 164 PRO B CG  1 
ATOM   7919  C CD  . PRO C 1 135 ? -11.646 15.575  -18.732 1.00 31.87  ? 164 PRO B CD  1 
ATOM   7920  N N   . MET C 1 136 ? -9.262  18.264  -20.116 1.00 29.36  ? 165 MET B N   1 
ATOM   7921  C CA  . MET C 1 136 ? -8.576  19.269  -20.915 1.00 29.16  ? 165 MET B CA  1 
ATOM   7922  C C   . MET C 1 136 ? -8.346  20.528  -20.093 1.00 26.17  ? 165 MET B C   1 
ATOM   7923  O O   . MET C 1 136 ? -7.318  21.173  -20.229 1.00 32.51  ? 165 MET B O   1 
ATOM   7924  C CB  . MET C 1 136 ? -9.344  19.585  -22.203 1.00 31.34  ? 165 MET B CB  1 
ATOM   7925  C CG  . MET C 1 136 ? -9.043  18.570  -23.298 1.00 36.26  ? 165 MET B CG  1 
ATOM   7926  S SD  . MET C 1 136 ? -7.274  18.452  -23.645 1.00 33.70  ? 165 MET B SD  1 
ATOM   7927  C CE  . MET C 1 136 ? -6.926  19.947  -24.588 1.00 37.66  ? 165 MET B CE  1 
ATOM   7928  N N   . SER C 1 137 ? -9.291  20.844  -19.208 1.00 26.67  ? 166 SER B N   1 
ATOM   7929  C CA  . SER C 1 137 ? -9.150  21.967  -18.319 1.00 25.02  ? 166 SER B CA  1 
ATOM   7930  C C   . SER C 1 137 ? -8.046  21.665  -17.335 1.00 25.01  ? 166 SER B C   1 
ATOM   7931  O O   . SER C 1 137 ? -7.227  22.530  -17.018 1.00 27.97  ? 166 SER B O   1 
ATOM   7932  C CB  . SER C 1 137 ? -10.469 22.285  -17.608 1.00 25.80  ? 166 SER B CB  1 
ATOM   7933  O OG  . SER C 1 137 ? -11.511 22.438  -18.556 1.00 28.76  ? 166 SER B OG  1 
ATOM   7934  N N   . GLN C 1 138 ? -8.001  20.414  -16.895 1.00 25.13  ? 167 GLN B N   1 
ATOM   7935  C CA  . GLN C 1 138 ? -6.990  20.011  -15.933 1.00 28.02  ? 167 GLN B CA  1 
ATOM   7936  C C   . GLN C 1 138 ? -5.607  20.103  -16.562 1.00 26.22  ? 167 GLN B C   1 
ATOM   7937  O O   . GLN C 1 138 ? -4.653  20.505  -15.920 1.00 26.36  ? 167 GLN B O   1 
ATOM   7938  C CB  . GLN C 1 138 ? -7.179  18.592  -15.405 1.00 28.15  ? 167 GLN B CB  1 
ATOM   7939  C CG  . GLN C 1 138 ? -8.510  18.391  -14.697 1.00 30.57  ? 167 GLN B CG  1 
ATOM   7940  C CD  . GLN C 1 138 ? -8.502  17.122  -13.878 1.00 34.35  ? 167 GLN B CD  1 
ATOM   7941  O OE1 . GLN C 1 138 ? -7.456  16.499  -13.717 1.00 33.75  ? 167 GLN B OE1 1 
ATOM   7942  N NE2 . GLN C 1 138 ? -9.660  16.718  -13.368 1.00 35.34  ? 167 GLN B NE2 1 
ATOM   7943  N N   . LEU C 1 139 ? -5.506  19.719  -17.823 1.00 27.13  ? 168 LEU B N   1 
ATOM   7944  C CA  . LEU C 1 139 ? -4.235  19.809  -18.514 1.00 29.32  ? 168 LEU B CA  1 
ATOM   7945  C C   . LEU C 1 139 ? -3.782  21.262  -18.609 1.00 28.00  ? 168 LEU B C   1 
ATOM   7946  O O   . LEU C 1 139 ? -2.627  21.575  -18.350 1.00 29.75  ? 168 LEU B O   1 
ATOM   7947  C CB  . LEU C 1 139 ? -4.429  19.261  -19.924 1.00 27.17  ? 168 LEU B CB  1 
ATOM   7948  C CG  . LEU C 1 139 ? -3.166  19.203  -20.772 1.00 30.52  ? 168 LEU B CG  1 
ATOM   7949  C CD1 . LEU C 1 139 ? -2.073  18.380  -20.132 1.00 33.03  ? 168 LEU B CD1 1 
ATOM   7950  C CD2 . LEU C 1 139 ? -3.531  18.706  -22.149 1.00 27.80  ? 168 LEU B CD2 1 
ATOM   7951  N N   . SER C 1 140 ? -4.670  22.112  -19.121 1.00 28.29  ? 169 SER B N   1 
ATOM   7952  C CA  . SER C 1 140 ? -4.323  23.501  -19.367 1.00 29.27  ? 169 SER B CA  1 
ATOM   7953  C C   . SER C 1 140 ? -3.927  24.183  -18.060 1.00 25.90  ? 169 SER B C   1 
ATOM   7954  O O   . SER C 1 140 ? -2.909  24.846  -18.026 1.00 23.50  ? 169 SER B O   1 
ATOM   7955  C CB  . SER C 1 140 ? -5.401  24.268  -20.048 1.00 27.46  ? 169 SER B CB  1 
ATOM   7956  O OG  . SER C 1 140 ? -4.996  25.632  -20.135 1.00 33.05  ? 169 SER B OG  1 
ATOM   7957  N N   . ALA C 1 141 ? -4.699  23.958  -16.984 1.00 26.54  ? 170 ALA B N   1 
ATOM   7958  C CA  . ALA C 1 141 ? -4.416  24.556  -15.690 1.00 25.40  ? 170 ALA B CA  1 
ATOM   7959  C C   . ALA C 1 141 ? -3.058  24.090  -15.153 1.00 25.64  ? 170 ALA B C   1 
ATOM   7960  O O   . ALA C 1 141 ? -2.269  24.905  -14.677 1.00 24.69  ? 170 ALA B O   1 
ATOM   7961  C CB  . ALA C 1 141 ? -5.504  24.222  -14.724 1.00 24.20  ? 170 ALA B CB  1 
ATOM   7962  N N   . ALA C 1 142 ? -2.773  22.792  -15.255 1.00 25.39  ? 171 ALA B N   1 
ATOM   7963  C CA  . ALA C 1 142 ? -1.519  22.257  -14.751 1.00 26.74  ? 171 ALA B CA  1 
ATOM   7964  C C   . ALA C 1 142 ? -0.323  22.767  -15.550 1.00 32.30  ? 171 ALA B C   1 
ATOM   7965  O O   . ALA C 1 142 ? 0.711   23.017  -14.954 1.00 29.36  ? 171 ALA B O   1 
ATOM   7966  C CB  . ALA C 1 142 ? -1.534  20.747  -14.759 1.00 26.67  ? 171 ALA B CB  1 
ATOM   7967  N N   . VAL C 1 143 ? -0.456  22.912  -16.886 1.00 32.03  ? 172 VAL B N   1 
ATOM   7968  C CA  . VAL C 1 143 ? 0.636   23.455  -17.698 1.00 29.71  ? 172 VAL B CA  1 
ATOM   7969  C C   . VAL C 1 143 ? 0.878   24.907  -17.302 1.00 26.05  ? 172 VAL B C   1 
ATOM   7970  O O   . VAL C 1 143 ? 2.022   25.343  -17.172 1.00 27.42  ? 172 VAL B O   1 
ATOM   7971  C CB  . VAL C 1 143 ? 0.439   23.290  -19.220 1.00 28.58  ? 172 VAL B CB  1 
ATOM   7972  C CG1 . VAL C 1 143 ? 1.434   24.107  -20.019 1.00 28.19  ? 172 VAL B CG1 1 
ATOM   7973  C CG2 . VAL C 1 143 ? 0.553   21.833  -19.615 1.00 28.63  ? 172 VAL B CG2 1 
ATOM   7974  N N   . THR C 1 144 ? -0.196  25.649  -17.050 1.00 25.82  ? 173 THR B N   1 
ATOM   7975  C CA  . THR C 1 144 ? -0.080  27.028  -16.625 1.00 24.16  ? 173 THR B CA  1 
ATOM   7976  C C   . THR C 1 144 ? 0.675   27.089  -15.301 1.00 27.86  ? 173 THR B C   1 
ATOM   7977  O O   . THR C 1 144 ? 1.576   27.905  -15.153 1.00 27.04  ? 173 THR B O   1 
ATOM   7978  C CB  . THR C 1 144 ? -1.459  27.695  -16.594 1.00 25.09  ? 173 THR B CB  1 
ATOM   7979  O OG1 . THR C 1 144 ? -1.910  27.846  -17.946 1.00 26.30  ? 173 THR B OG1 1 
ATOM   7980  C CG2 . THR C 1 144 ? -1.423  29.106  -16.042 1.00 23.00  ? 173 THR B CG2 1 
ATOM   7981  N N   . ALA C 1 145 ? 0.412   26.137  -14.393 1.00 22.94  ? 174 ALA B N   1 
ATOM   7982  C CA  . ALA C 1 145 ? 1.017   26.146  -13.086 1.00 23.68  ? 174 ALA B CA  1 
ATOM   7983  C C   . ALA C 1 145 ? 2.504   25.796  -13.161 1.00 25.12  ? 174 ALA B C   1 
ATOM   7984  O O   . ALA C 1 145 ? 3.305   26.290  -12.373 1.00 23.19  ? 174 ALA B O   1 
ATOM   7985  C CB  . ALA C 1 145 ? 0.200   25.240  -12.154 1.00 23.78  ? 174 ALA B CB  1 
ATOM   7986  N N   . LEU C 1 146 ? 2.900   25.007  -14.150 1.00 27.36  ? 175 LEU B N   1 
ATOM   7987  C CA  . LEU C 1 146 ? 4.285   24.621  -14.335 1.00 26.36  ? 175 LEU B CA  1 
ATOM   7988  C C   . LEU C 1 146 ? 5.153   25.816  -14.759 1.00 30.53  ? 175 LEU B C   1 
ATOM   7989  O O   . LEU C 1 146 ? 6.367   25.697  -14.803 1.00 30.73  ? 175 LEU B O   1 
ATOM   7990  C CB  . LEU C 1 146 ? 4.339   23.542  -15.414 1.00 28.73  ? 175 LEU B CB  1 
ATOM   7991  C CG  . LEU C 1 146 ? 4.213   22.079  -14.989 1.00 31.07  ? 175 LEU B CG  1 
ATOM   7992  C CD1 . LEU C 1 146 ? 4.121   21.245  -16.232 1.00 30.44  ? 175 LEU B CD1 1 
ATOM   7993  C CD2 . LEU C 1 146 ? 5.399   21.606  -14.188 1.00 34.94  ? 175 LEU B CD2 1 
ATOM   7994  N N   . ASN C 1 147 ? 4.550   26.940  -15.156 1.00 27.64  ? 176 ASN B N   1 
ATOM   7995  C CA  . ASN C 1 147 ? 5.313   28.085  -15.640 1.00 28.80  ? 176 ASN B CA  1 
ATOM   7996  C C   . ASN C 1 147 ? 6.195   28.679  -14.531 1.00 30.68  ? 176 ASN B C   1 
ATOM   7997  O O   . ASN C 1 147 ? 7.110   29.425  -14.822 1.00 26.61  ? 176 ASN B O   1 
ATOM   7998  C CB  . ASN C 1 147 ? 4.427   29.051  -16.414 1.00 28.96  ? 176 ASN B CB  1 
ATOM   7999  C CG  . ASN C 1 147 ? 4.531   30.457  -15.904 1.00 34.94  ? 176 ASN B CG  1 
ATOM   8000  O OD1 . ASN C 1 147 ? 5.202   31.308  -16.503 1.00 35.04  ? 176 ASN B OD1 1 
ATOM   8001  N ND2 . ASN C 1 147 ? 3.952   30.674  -14.737 1.00 37.52  ? 176 ASN B ND2 1 
ATOM   8002  N N   . SER C 1 148 ? 6.019   28.237  -13.283 1.00 30.81  ? 177 SER B N   1 
ATOM   8003  C CA  . SER C 1 148 ? 6.902   28.572  -12.195 1.00 30.37  ? 177 SER B CA  1 
ATOM   8004  C C   . SER C 1 148 ? 8.306   28.043  -12.454 1.00 33.47  ? 177 SER B C   1 
ATOM   8005  O O   . SER C 1 148 ? 9.258   28.545  -11.894 1.00 35.30  ? 177 SER B O   1 
ATOM   8006  C CB  . SER C 1 148 ? 6.376   28.002  -10.908 1.00 30.68  ? 177 SER B CB  1 
ATOM   8007  O OG  . SER C 1 148 ? 6.167   26.602  -11.008 1.00 32.61  ? 177 SER B OG  1 
ATOM   8008  N N   . GLU C 1 149 ? 8.393   26.994  -13.264 1.00 34.01  ? 178 GLU B N   1 
ATOM   8009  C CA  . GLU C 1 149 ? 9.644   26.398  -13.683 1.00 35.90  ? 178 GLU B CA  1 
ATOM   8010  C C   . GLU C 1 149 ? 10.233  27.072  -14.925 1.00 32.61  ? 178 GLU B C   1 
ATOM   8011  O O   . GLU C 1 149 ? 11.243  26.609  -15.426 1.00 36.56  ? 178 GLU B O   1 
ATOM   8012  C CB  . GLU C 1 149 ? 9.335   24.928  -13.979 1.00 39.18  ? 178 GLU B CB  1 
ATOM   8013  C CG  . GLU C 1 149 ? 8.582   24.209  -12.860 1.00 52.28  ? 178 GLU B CG  1 
ATOM   8014  C CD  . GLU C 1 149 ? 9.084   24.338  -11.421 1.00 61.01  ? 178 GLU B CD  1 
ATOM   8015  O OE1 . GLU C 1 149 ? 10.073  23.604  -11.169 1.00 63.25  ? 178 GLU B OE1 1 
ATOM   8016  O OE2 . GLU C 1 149 ? 8.497   25.081  -10.546 1.00 56.72  ? 178 GLU B OE2 1 
ATOM   8017  N N   . SER C 1 150 ? 9.591   28.110  -15.487 1.00 31.66  ? 179 SER B N   1 
ATOM   8018  C CA  . SER C 1 150 ? 10.046  28.694  -16.756 1.00 30.08  ? 179 SER B CA  1 
ATOM   8019  C C   . SER C 1 150 ? 11.401  29.391  -16.596 1.00 33.38  ? 179 SER B C   1 
ATOM   8020  O O   . SER C 1 150 ? 11.526  30.414  -15.900 1.00 30.56  ? 179 SER B O   1 
ATOM   8021  C CB  . SER C 1 150 ? 9.075   29.691  -17.365 1.00 26.46  ? 179 SER B CB  1 
ATOM   8022  O OG  . SER C 1 150 ? 9.610   30.160  -18.611 1.00 25.69  ? 179 SER B OG  1 
ATOM   8023  N N   . ASN C 1 151 ? 12.404  28.866  -17.304 1.00 36.80  ? 180 ASN B N   1 
ATOM   8024  C CA  . ASN C 1 151 ? 13.687  29.546  -17.440 1.00 39.86  ? 180 ASN B CA  1 
ATOM   8025  C C   . ASN C 1 151 ? 13.560  30.775  -18.337 1.00 38.70  ? 180 ASN B C   1 
ATOM   8026  O O   . ASN C 1 151 ? 14.315  31.732  -18.183 1.00 42.32  ? 180 ASN B O   1 
ATOM   8027  C CB  . ASN C 1 151 ? 14.752  28.647  -18.069 1.00 45.09  ? 180 ASN B CB  1 
ATOM   8028  C CG  . ASN C 1 151 ? 14.951  27.368  -17.293 1.00 54.93  ? 180 ASN B CG  1 
ATOM   8029  O OD1 . ASN C 1 151 ? 14.821  26.275  -17.868 1.00 56.41  ? 180 ASN B OD1 1 
ATOM   8030  N ND2 . ASN C 1 151 ? 15.235  27.498  -16.003 1.00 48.81  ? 180 ASN B ND2 1 
ATOM   8031  N N   . PHE C 1 152 ? 12.627  30.748  -19.303 1.00 34.89  ? 181 PHE B N   1 
ATOM   8032  C CA  . PHE C 1 152 ? 12.509  31.865  -20.228 1.00 35.42  ? 181 PHE B CA  1 
ATOM   8033  C C   . PHE C 1 152 ? 11.944  33.104  -19.520 1.00 34.91  ? 181 PHE B C   1 
ATOM   8034  O O   . PHE C 1 152 ? 12.398  34.227  -19.749 1.00 33.31  ? 181 PHE B O   1 
ATOM   8035  C CB  . PHE C 1 152 ? 11.653  31.588  -21.451 1.00 34.19  ? 181 PHE B CB  1 
ATOM   8036  C CG  . PHE C 1 152 ? 11.543  32.815  -22.331 1.00 32.96  ? 181 PHE B CG  1 
ATOM   8037  C CD1 . PHE C 1 152 ? 12.543  33.120  -23.243 1.00 32.01  ? 181 PHE B CD1 1 
ATOM   8038  C CD2 . PHE C 1 152 ? 10.462  33.671  -22.211 1.00 36.37  ? 181 PHE B CD2 1 
ATOM   8039  C CE1 . PHE C 1 152 ? 12.433  34.222  -24.057 1.00 35.05  ? 181 PHE B CE1 1 
ATOM   8040  C CE2 . PHE C 1 152 ? 10.362  34.777  -23.024 1.00 35.96  ? 181 PHE B CE2 1 
ATOM   8041  C CZ  . PHE C 1 152 ? 11.352  35.064  -23.930 1.00 37.78  ? 181 PHE B CZ  1 
ATOM   8042  N N   . ALA C 1 153 ? 10.964  32.910  -18.641 1.00 32.94  ? 182 ALA B N   1 
ATOM   8043  C CA  . ALA C 1 153 ? 10.338  34.046  -17.976 1.00 32.91  ? 182 ALA B CA  1 
ATOM   8044  C C   . ALA C 1 153 ? 11.338  34.739  -17.036 1.00 36.05  ? 182 ALA B C   1 
ATOM   8045  O O   . ALA C 1 153 ? 11.403  35.954  -17.013 1.00 40.41  ? 182 ALA B O   1 
ATOM   8046  C CB  . ALA C 1 153 ? 9.079   33.549  -17.292 1.00 31.56  ? 182 ALA B CB  1 
ATOM   8047  N N   . ARG C 1 154 ? 12.152  33.959  -16.304 1.00 40.19  ? 183 ARG B N   1 
ATOM   8048  C CA  . ARG C 1 154 ? 13.164  34.469  -15.393 1.00 51.64  ? 183 ARG B CA  1 
ATOM   8049  C C   . ARG C 1 154 ? 14.248  35.216  -16.162 1.00 51.53  ? 183 ARG B C   1 
ATOM   8050  O O   . ARG C 1 154 ? 14.654  36.296  -15.755 1.00 50.34  ? 183 ARG B O   1 
ATOM   8051  C CB  . ARG C 1 154 ? 13.881  33.383  -14.581 1.00 60.41  ? 183 ARG B CB  1 
ATOM   8052  C CG  . ARG C 1 154 ? 13.027  32.699  -13.519 1.00 76.54  ? 183 ARG B CG  1 
ATOM   8053  C CD  . ARG C 1 154 ? 13.802  31.777  -12.547 1.00 91.32  ? 183 ARG B CD  1 
ATOM   8054  N NE  . ARG C 1 154 ? 13.973  30.364  -12.929 1.00 99.30  ? 183 ARG B NE  1 
ATOM   8055  C CZ  . ARG C 1 154 ? 13.100  29.360  -12.758 1.00 99.50  ? 183 ARG B CZ  1 
ATOM   8056  N NH1 . ARG C 1 154 ? 13.394  28.145  -13.202 1.00 96.99  ? 183 ARG B NH1 1 
ATOM   8057  N NH2 . ARG C 1 154 ? 11.936  29.564  -12.159 1.00 94.54  ? 183 ARG B NH2 1 
ATOM   8058  N N   . ALA C 1 155 ? 14.716  34.661  -17.280 1.00 48.68  ? 184 ALA B N   1 
ATOM   8059  C CA  . ALA C 1 155 ? 15.786  35.321  -18.028 1.00 41.97  ? 184 ALA B CA  1 
ATOM   8060  C C   . ALA C 1 155 ? 15.338  36.655  -18.620 1.00 40.51  ? 184 ALA B C   1 
ATOM   8061  O O   . ALA C 1 155 ? 16.106  37.621  -18.643 1.00 41.99  ? 184 ALA B O   1 
ATOM   8062  C CB  . ALA C 1 155 ? 16.296  34.422  -19.120 1.00 42.29  ? 184 ALA B CB  1 
ATOM   8063  N N   . TYR C 1 156 ? 14.111  36.723  -19.143 1.00 38.86  ? 185 TYR B N   1 
ATOM   8064  C CA  . TYR C 1 156 ? 13.668  37.953  -19.788 1.00 37.01  ? 185 TYR B CA  1 
ATOM   8065  C C   . TYR C 1 156 ? 13.645  39.102  -18.765 1.00 38.67  ? 185 TYR B C   1 
ATOM   8066  O O   . TYR C 1 156 ? 13.962  40.249  -19.072 1.00 41.25  ? 185 TYR B O   1 
ATOM   8067  C CB  . TYR C 1 156 ? 12.313  37.749  -20.473 1.00 40.68  ? 185 TYR B CB  1 
ATOM   8068  C CG  . TYR C 1 156 ? 11.869  38.987  -21.236 1.00 41.48  ? 185 TYR B CG  1 
ATOM   8069  C CD1 . TYR C 1 156 ? 11.225  40.030  -20.588 1.00 38.15  ? 185 TYR B CD1 1 
ATOM   8070  C CD2 . TYR C 1 156 ? 12.115  39.113  -22.599 1.00 47.26  ? 185 TYR B CD2 1 
ATOM   8071  C CE1 . TYR C 1 156 ? 10.862  41.182  -21.267 1.00 39.23  ? 185 TYR B CE1 1 
ATOM   8072  C CE2 . TYR C 1 156 ? 11.751  40.256  -23.292 1.00 50.00  ? 185 TYR B CE2 1 
ATOM   8073  C CZ  . TYR C 1 156 ? 11.113  41.287  -22.623 1.00 43.01  ? 185 TYR B CZ  1 
ATOM   8074  O OH  . TYR C 1 156 ? 10.728  42.400  -23.307 1.00 55.51  ? 185 TYR B OH  1 
ATOM   8075  N N   . ALA C 1 157 ? 13.254  38.811  -17.531 1.00 45.88  ? 186 ALA B N   1 
ATOM   8076  C CA  . ALA C 1 157 ? 13.214  39.844  -16.514 1.00 55.17  ? 186 ALA B CA  1 
ATOM   8077  C C   . ALA C 1 157 ? 14.602  40.479  -16.357 1.00 55.38  ? 186 ALA B C   1 
ATOM   8078  O O   . ALA C 1 157 ? 14.715  41.685  -16.174 1.00 55.87  ? 186 ALA B O   1 
ATOM   8079  C CB  . ALA C 1 157 ? 12.693  39.253  -15.215 1.00 56.76  ? 186 ALA B CB  1 
ATOM   8080  N N   . GLN C 1 158 ? 15.666  39.673  -16.490 1.00 53.40  ? 187 GLN B N   1 
ATOM   8081  C CA  . GLN C 1 158 ? 17.025  40.137  -16.262 1.00 49.24  ? 187 GLN B CA  1 
ATOM   8082  C C   . GLN C 1 158 ? 17.621  40.834  -17.488 1.00 46.80  ? 187 GLN B C   1 
ATOM   8083  O O   . GLN C 1 158 ? 18.751  41.296  -17.412 1.00 45.23  ? 187 GLN B O   1 
ATOM   8084  C CB  . GLN C 1 158 ? 17.887  38.947  -15.861 1.00 55.44  ? 187 GLN B CB  1 
ATOM   8085  C CG  . GLN C 1 158 ? 17.512  38.335  -14.515 1.00 60.34  ? 187 GLN B CG  1 
ATOM   8086  C CD  . GLN C 1 158 ? 18.167  36.984  -14.313 1.00 74.83  ? 187 GLN B CD  1 
ATOM   8087  O OE1 . GLN C 1 158 ? 18.730  36.392  -15.246 1.00 75.65  ? 187 GLN B OE1 1 
ATOM   8088  N NE2 . GLN C 1 158 ? 18.099  36.475  -13.092 1.00 76.98  ? 187 GLN B NE2 1 
ATOM   8089  N N   . GLY C 1 159 ? 16.885  40.900  -18.605 1.00 38.06  ? 188 GLY B N   1 
ATOM   8090  C CA  . GLY C 1 159 ? 17.312  41.610  -19.796 1.00 42.22  ? 188 GLY B CA  1 
ATOM   8091  C C   . GLY C 1 159 ? 18.236  40.799  -20.717 1.00 40.43  ? 188 GLY B C   1 
ATOM   8092  O O   . GLY C 1 159 ? 19.059  41.397  -21.411 1.00 46.32  ? 188 GLY B O   1 
ATOM   8093  N N   . ILE C 1 160 ? 18.029  39.479  -20.846 1.00 38.16  ? 189 ILE B N   1 
ATOM   8094  C CA  . ILE C 1 160 ? 18.784  38.681  -21.822 1.00 33.51  ? 189 ILE B CA  1 
ATOM   8095  C C   . ILE C 1 160 ? 18.655  39.231  -23.254 1.00 31.40  ? 189 ILE B C   1 
ATOM   8096  O O   . ILE C 1 160 ? 17.623  39.722  -23.679 1.00 29.34  ? 189 ILE B O   1 
ATOM   8097  C CB  . ILE C 1 160 ? 18.434  37.185  -21.726 1.00 36.97  ? 189 ILE B CB  1 
ATOM   8098  C CG1 . ILE C 1 160 ? 19.348  36.327  -22.610 1.00 44.67  ? 189 ILE B CG1 1 
ATOM   8099  C CG2 . ILE C 1 160 ? 16.969  36.913  -22.083 1.00 37.88  ? 189 ILE B CG2 1 
ATOM   8100  C CD1 . ILE C 1 160 ? 20.651  35.864  -21.984 1.00 47.37  ? 189 ILE B CD1 1 
ATOM   8101  N N   . SER C 1 161 ? 19.748  39.163  -24.026 1.00 30.40  ? 190 SER B N   1 
ATOM   8102  C CA  . SER C 1 161 ? 19.751  39.509  -25.435 1.00 28.81  ? 190 SER B CA  1 
ATOM   8103  C C   . SER C 1 161 ? 18.648  38.757  -26.186 1.00 33.33  ? 190 SER B C   1 
ATOM   8104  O O   . SER C 1 161 ? 18.385  37.590  -25.906 1.00 31.04  ? 190 SER B O   1 
ATOM   8105  C CB  . SER C 1 161 ? 21.083  39.162  -26.057 1.00 33.04  ? 190 SER B CB  1 
ATOM   8106  O OG  . SER C 1 161 ? 21.003  39.206  -27.479 1.00 31.85  ? 190 SER B OG  1 
ATOM   8107  N N   . ARG C 1 162 ? 18.009  39.433  -27.150 1.00 29.54  ? 191 ARG B N   1 
ATOM   8108  C CA  . ARG C 1 162 ? 17.002  38.822  -27.999 1.00 34.94  ? 191 ARG B CA  1 
ATOM   8109  C C   . ARG C 1 162 ? 17.631  37.731  -28.875 1.00 33.68  ? 191 ARG B C   1 
ATOM   8110  O O   . ARG C 1 162 ? 16.937  36.853  -29.366 1.00 30.68  ? 191 ARG B O   1 
ATOM   8111  C CB  . ARG C 1 162 ? 16.375  39.899  -28.883 1.00 40.33  ? 191 ARG B CB  1 
ATOM   8112  C CG  . ARG C 1 162 ? 17.351  40.536  -29.875 1.00 51.54  ? 191 ARG B CG  1 
ATOM   8113  C CD  . ARG C 1 162 ? 16.657  41.472  -30.870 1.00 61.40  ? 191 ARG B CD  1 
ATOM   8114  N NE  . ARG C 1 162 ? 15.837  42.455  -30.145 1.00 76.74  ? 191 ARG B NE  1 
ATOM   8115  C CZ  . ARG C 1 162 ? 14.517  42.396  -29.921 1.00 93.01  ? 191 ARG B CZ  1 
ATOM   8116  N NH1 . ARG C 1 162 ? 13.781  41.397  -30.395 1.00 94.09  ? 191 ARG B NH1 1 
ATOM   8117  N NH2 . ARG C 1 162 ? 13.933  43.351  -29.209 1.00 98.04  ? 191 ARG B NH2 1 
ATOM   8118  N N   . THR C 1 163 ? 18.960  37.782  -29.053 1.00 33.52  ? 192 THR B N   1 
ATOM   8119  C CA  . THR C 1 163 ? 19.656  36.790  -29.852 1.00 30.86  ? 192 THR B CA  1 
ATOM   8120  C C   . THR C 1 163 ? 19.571  35.446  -29.147 1.00 28.78  ? 192 THR B C   1 
ATOM   8121  O O   . THR C 1 163 ? 19.830  34.435  -29.771 1.00 36.52  ? 192 THR B O   1 
ATOM   8122  C CB  . THR C 1 163 ? 21.125  37.162  -30.093 1.00 31.76  ? 192 THR B CB  1 
ATOM   8123  O OG1 . THR C 1 163 ? 21.740  37.184  -28.806 1.00 26.82  ? 192 THR B OG1 1 
ATOM   8124  C CG2 . THR C 1 163 ? 21.298  38.468  -30.842 1.00 33.55  ? 192 THR B CG2 1 
ATOM   8125  N N   . LYS C 1 164 ? 19.275  35.434  -27.849 1.00 30.38  ? 193 LYS B N   1 
ATOM   8126  C CA  . LYS C 1 164 ? 19.349  34.205  -27.070 1.00 33.06  ? 193 LYS B CA  1 
ATOM   8127  C C   . LYS C 1 164 ? 17.976  33.734  -26.606 1.00 29.23  ? 193 LYS B C   1 
ATOM   8128  O O   . LYS C 1 164 ? 17.882  32.736  -25.897 1.00 28.89  ? 193 LYS B O   1 
ATOM   8129  C CB  . LYS C 1 164 ? 20.284  34.388  -25.870 1.00 35.63  ? 193 LYS B CB  1 
ATOM   8130  C CG  . LYS C 1 164 ? 21.683  34.896  -26.239 1.00 43.39  ? 193 LYS B CG  1 
ATOM   8131  C CD  . LYS C 1 164 ? 22.496  33.994  -27.165 1.00 51.24  ? 193 LYS B CD  1 
ATOM   8132  C CE  . LYS C 1 164 ? 23.828  34.571  -27.600 1.00 59.44  ? 193 LYS B CE  1 
ATOM   8133  N NZ  . LYS C 1 164 ? 23.767  35.552  -28.694 1.00 64.48  ? 193 LYS B NZ  1 
ATOM   8134  N N   . TYR C 1 165 ? 16.908  34.419  -27.015 1.00 28.37  ? 194 TYR B N   1 
ATOM   8135  C CA  . TYR C 1 165 ? 15.572  33.972  -26.641 1.00 29.44  ? 194 TYR B CA  1 
ATOM   8136  C C   . TYR C 1 165 ? 15.352  32.518  -27.022 1.00 24.96  ? 194 TYR B C   1 
ATOM   8137  O O   . TYR C 1 165 ? 14.784  31.743  -26.267 1.00 29.03  ? 194 TYR B O   1 
ATOM   8138  C CB  . TYR C 1 165 ? 14.483  34.791  -27.329 1.00 30.09  ? 194 TYR B CB  1 
ATOM   8139  C CG  . TYR C 1 165 ? 14.282  36.206  -26.818 1.00 29.16  ? 194 TYR B CG  1 
ATOM   8140  C CD1 . TYR C 1 165 ? 14.805  36.620  -25.592 1.00 31.80  ? 194 TYR B CD1 1 
ATOM   8141  C CD2 . TYR C 1 165 ? 13.591  37.138  -27.588 1.00 29.15  ? 194 TYR B CD2 1 
ATOM   8142  C CE1 . TYR C 1 165 ? 14.637  37.918  -25.134 1.00 34.15  ? 194 TYR B CE1 1 
ATOM   8143  C CE2 . TYR C 1 165 ? 13.430  38.438  -27.138 1.00 32.12  ? 194 TYR B CE2 1 
ATOM   8144  C CZ  . TYR C 1 165 ? 13.954  38.832  -25.916 1.00 33.83  ? 194 TYR B CZ  1 
ATOM   8145  O OH  . TYR C 1 165 ? 13.783  40.108  -25.439 1.00 34.21  ? 194 TYR B OH  1 
ATOM   8146  N N   . TRP C 1 166 ? 15.771  32.118  -28.213 1.00 28.48  ? 195 TRP B N   1 
ATOM   8147  C CA  . TRP C 1 166 ? 15.435  30.779  -28.680 1.00 26.77  ? 195 TRP B CA  1 
ATOM   8148  C C   . TRP C 1 166 ? 16.011  29.722  -27.751 1.00 28.06  ? 195 TRP B C   1 
ATOM   8149  O O   . TRP C 1 166 ? 15.469  28.625  -27.667 1.00 25.97  ? 195 TRP B O   1 
ATOM   8150  C CB  . TRP C 1 166 ? 15.908  30.535  -30.119 1.00 28.05  ? 195 TRP B CB  1 
ATOM   8151  C CG  . TRP C 1 166 ? 17.389  30.350  -30.248 1.00 30.86  ? 195 TRP B CG  1 
ATOM   8152  C CD1 . TRP C 1 166 ? 18.310  31.325  -30.534 1.00 38.10  ? 195 TRP B CD1 1 
ATOM   8153  C CD2 . TRP C 1 166 ? 18.126  29.115  -30.129 1.00 30.20  ? 195 TRP B CD2 1 
ATOM   8154  N NE1 . TRP C 1 166 ? 19.566  30.777  -30.588 1.00 38.08  ? 195 TRP B NE1 1 
ATOM   8155  C CE2 . TRP C 1 166 ? 19.486  29.426  -30.360 1.00 31.66  ? 195 TRP B CE2 1 
ATOM   8156  C CE3 . TRP C 1 166 ? 17.772  27.798  -29.845 1.00 28.43  ? 195 TRP B CE3 1 
ATOM   8157  C CZ2 . TRP C 1 166 ? 20.484  28.464  -30.318 1.00 30.63  ? 195 TRP B CZ2 1 
ATOM   8158  C CZ3 . TRP C 1 166 ? 18.758  26.843  -29.819 1.00 29.78  ? 195 TRP B CZ3 1 
ATOM   8159  C CH2 . TRP C 1 166 ? 20.090  27.169  -30.067 1.00 31.09  ? 195 TRP B CH2 1 
ATOM   8160  N N   . GLU C 1 167 ? 17.168  30.014  -27.156 1.00 28.02  ? 196 GLU B N   1 
ATOM   8161  C CA  . GLU C 1 167 ? 17.866  29.064  -26.307 1.00 30.56  ? 196 GLU B CA  1 
ATOM   8162  C C   . GLU C 1 167 ? 17.041  28.691  -25.082 1.00 27.50  ? 196 GLU B C   1 
ATOM   8163  O O   . GLU C 1 167 ? 16.963  27.535  -24.727 1.00 27.71  ? 196 GLU B O   1 
ATOM   8164  C CB  . GLU C 1 167 ? 19.246  29.595  -25.913 1.00 35.69  ? 196 GLU B CB  1 
ATOM   8165  C CG  . GLU C 1 167 ? 20.196  29.708  -27.101 1.00 37.50  ? 196 GLU B CG  1 
ATOM   8166  C CD  . GLU C 1 167 ? 21.545  30.360  -26.809 1.00 46.00  ? 196 GLU B CD  1 
ATOM   8167  O OE1 . GLU C 1 167 ? 21.741  30.714  -25.636 1.00 51.70  ? 196 GLU B OE1 1 
ATOM   8168  O OE2 . GLU C 1 167 ? 22.395  30.511  -27.717 1.00 61.28  ? 196 GLU B OE2 1 
ATOM   8169  N N   . LEU C 1 168 ? 16.389  29.659  -24.457 1.00 29.11  ? 197 LEU B N   1 
ATOM   8170  C CA  . LEU C 1 168 ? 15.590  29.413  -23.272 1.00 28.27  ? 197 LEU B CA  1 
ATOM   8171  C C   . LEU C 1 168 ? 14.217  28.858  -23.619 1.00 23.09  ? 197 LEU B C   1 
ATOM   8172  O O   . LEU C 1 168 ? 13.700  28.060  -22.879 1.00 28.59  ? 197 LEU B O   1 
ATOM   8173  C CB  . LEU C 1 168 ? 15.511  30.726  -22.491 1.00 34.97  ? 197 LEU B CB  1 
ATOM   8174  C CG  . LEU C 1 168 ? 16.868  31.244  -22.002 1.00 45.54  ? 197 LEU B CG  1 
ATOM   8175  C CD1 . LEU C 1 168 ? 16.734  32.716  -21.708 1.00 51.37  ? 197 LEU B CD1 1 
ATOM   8176  C CD2 . LEU C 1 168 ? 17.413  30.493  -20.794 1.00 42.53  ? 197 LEU B CD2 1 
ATOM   8177  N N   . ILE C 1 169 ? 13.631  29.280  -24.727 1.00 20.19  ? 198 ILE B N   1 
ATOM   8178  C CA  . ILE C 1 169 ? 12.459  28.690  -25.308 1.00 21.39  ? 198 ILE B CA  1 
ATOM   8179  C C   . ILE C 1 169 ? 12.723  27.203  -25.557 1.00 23.82  ? 198 ILE B C   1 
ATOM   8180  O O   . ILE C 1 169 ? 11.879  26.369  -25.197 1.00 27.92  ? 198 ILE B O   1 
ATOM   8181  C CB  . ILE C 1 169 ? 12.020  29.458  -26.581 1.00 22.92  ? 198 ILE B CB  1 
ATOM   8182  C CG1 . ILE C 1 169 ? 11.623  30.905  -26.279 1.00 28.81  ? 198 ILE B CG1 1 
ATOM   8183  C CG2 . ILE C 1 169 ? 10.899  28.722  -27.314 1.00 24.80  ? 198 ILE B CG2 1 
ATOM   8184  C CD1 . ILE C 1 169 ? 10.329  31.061  -25.486 1.00 26.66  ? 198 ILE B CD1 1 
ATOM   8185  N N   . TYR C 1 170 ? 13.915  26.867  -26.060 1.00 22.42  ? 199 TYR B N   1 
ATOM   8186  C CA  . TYR C 1 170 ? 14.233  25.463  -26.295 1.00 24.67  ? 199 TYR B CA  1 
ATOM   8187  C C   . TYR C 1 170 ? 14.289  24.673  -24.973 1.00 26.21  ? 199 TYR B C   1 
ATOM   8188  O O   . TYR C 1 170 ? 13.707  23.594  -24.859 1.00 26.94  ? 199 TYR B O   1 
ATOM   8189  C CB  . TYR C 1 170 ? 15.529  25.371  -27.103 1.00 25.94  ? 199 TYR B CB  1 
ATOM   8190  C CG  . TYR C 1 170 ? 16.203  24.004  -27.093 1.00 26.69  ? 199 TYR B CG  1 
ATOM   8191  C CD1 . TYR C 1 170 ? 17.011  23.616  -26.038 1.00 28.68  ? 199 TYR B CD1 1 
ATOM   8192  C CD2 . TYR C 1 170 ? 15.985  23.084  -28.112 1.00 31.38  ? 199 TYR B CD2 1 
ATOM   8193  C CE1 . TYR C 1 170 ? 17.595  22.365  -25.993 1.00 28.42  ? 199 TYR B CE1 1 
ATOM   8194  C CE2 . TYR C 1 170 ? 16.594  21.840  -28.106 1.00 27.77  ? 199 TYR B CE2 1 
ATOM   8195  C CZ  . TYR C 1 170 ? 17.397  21.483  -27.042 1.00 29.15  ? 199 TYR B CZ  1 
ATOM   8196  O OH  . TYR C 1 170 ? 17.953  20.236  -26.990 1.00 30.08  ? 199 TYR B OH  1 
ATOM   8197  N N   . GLU C 1 171 ? 15.013  25.157  -23.965 1.00 25.92  ? 200 GLU B N   1 
ATOM   8198  C CA  . GLU C 1 171 ? 15.064  24.419  -22.698 1.00 27.14  ? 200 GLU B CA  1 
ATOM   8199  C C   . GLU C 1 171 ? 13.666  24.258  -22.099 1.00 25.45  ? 200 GLU B C   1 
ATOM   8200  O O   . GLU C 1 171 ? 13.320  23.192  -21.636 1.00 26.23  ? 200 GLU B O   1 
ATOM   8201  C CB  . GLU C 1 171 ? 15.935  25.100  -21.642 1.00 26.81  ? 200 GLU B CB  1 
ATOM   8202  C CG  . GLU C 1 171 ? 17.396  25.199  -22.074 1.00 30.10  ? 200 GLU B CG  1 
ATOM   8203  C CD  . GLU C 1 171 ? 18.123  23.869  -22.148 1.00 31.06  ? 200 GLU B CD  1 
ATOM   8204  O OE1 . GLU C 1 171 ? 17.720  22.899  -21.477 1.00 40.50  ? 200 GLU B OE1 1 
ATOM   8205  O OE2 . GLU C 1 171 ? 19.114  23.819  -22.872 1.00 34.46  ? 200 GLU B OE2 1 
ATOM   8206  N N   . ASP C 1 172 ? 12.889  25.330  -22.008 1.00 27.41  ? 201 ASP B N   1 
ATOM   8207  C CA  . ASP C 1 172 ? 11.551  25.239  -21.447 1.00 29.50  ? 201 ASP B CA  1 
ATOM   8208  C C   . ASP C 1 172 ? 10.694  24.302  -22.312 1.00 29.69  ? 201 ASP B C   1 
ATOM   8209  O O   . ASP C 1 172 ? 9.861   23.574  -21.779 1.00 27.12  ? 201 ASP B O   1 
ATOM   8210  C CB  . ASP C 1 172 ? 10.874  26.605  -21.309 1.00 33.71  ? 201 ASP B CB  1 
ATOM   8211  C CG  . ASP C 1 172 ? 11.343  27.562  -20.213 1.00 38.87  ? 201 ASP B CG  1 
ATOM   8212  O OD1 . ASP C 1 172 ? 12.205  27.202  -19.375 1.00 34.72  ? 201 ASP B OD1 1 
ATOM   8213  O OD2 . ASP C 1 172 ? 10.812  28.685  -20.188 1.00 41.03  ? 201 ASP B OD2 1 
ATOM   8214  N N   . SER C 1 173 ? 10.886  24.303  -23.634 1.00 30.18  ? 202 SER B N   1 
ATOM   8215  C CA  . SER C 1 173 ? 10.133  23.403  -24.503 1.00 29.72  ? 202 SER B CA  1 
ATOM   8216  C C   . SER C 1 173 ? 10.530  21.958  -24.222 1.00 27.21  ? 202 SER B C   1 
ATOM   8217  O O   . SER C 1 173 ? 9.673   21.079  -24.136 1.00 26.44  ? 202 SER B O   1 
ATOM   8218  C CB  . SER C 1 173 ? 10.251  23.767  -25.984 1.00 27.82  ? 202 SER B CB  1 
ATOM   8219  O OG  . SER C 1 173 ? 9.598   25.012  -26.247 1.00 28.73  ? 202 SER B OG  1 
ATOM   8220  N N   . MET C 1 174 ? 11.819  21.705  -24.001 1.00 25.59  ? 203 MET B N   1 
ATOM   8221  C CA  . MET C 1 174 ? 12.249  20.351  -23.705 1.00 24.63  ? 203 MET B CA  1 
ATOM   8222  C C   . MET C 1 174 ? 11.733  19.857  -22.356 1.00 26.28  ? 203 MET B C   1 
ATOM   8223  O O   . MET C 1 174 ? 11.310  18.702  -22.232 1.00 24.99  ? 203 MET B O   1 
ATOM   8224  C CB  . MET C 1 174 ? 13.760  20.229  -23.774 1.00 26.98  ? 203 MET B CB  1 
ATOM   8225  C CG  . MET C 1 174 ? 14.255  20.498  -25.193 1.00 27.30  ? 203 MET B CG  1 
ATOM   8226  S SD  . MET C 1 174 ? 14.228  19.099  -26.331 1.00 30.62  ? 203 MET B SD  1 
ATOM   8227  C CE  . MET C 1 174 ? 15.580  18.188  -25.575 1.00 29.55  ? 203 MET B CE  1 
ATOM   8228  N N   . ASP C 1 175 ? 11.684  20.762  -21.384 1.00 27.34  ? 204 ASP B N   1 
ATOM   8229  C CA  . ASP C 1 175 ? 11.117  20.481  -20.078 1.00 28.26  ? 204 ASP B CA  1 
ATOM   8230  C C   . ASP C 1 175 ? 9.625   20.153  -20.202 1.00 26.29  ? 204 ASP B C   1 
ATOM   8231  O O   . ASP C 1 175 ? 9.167   19.202  -19.579 1.00 27.67  ? 204 ASP B O   1 
ATOM   8232  C CB  . ASP C 1 175 ? 11.423  21.646  -19.137 1.00 26.16  ? 204 ASP B CB  1 
ATOM   8233  C CG  . ASP C 1 175 ? 12.876  21.730  -18.681 1.00 31.37  ? 204 ASP B CG  1 
ATOM   8234  O OD1 . ASP C 1 175 ? 13.670  20.820  -19.053 1.00 31.24  ? 204 ASP B OD1 1 
ATOM   8235  O OD2 . ASP C 1 175 ? 13.212  22.691  -17.941 1.00 30.10  ? 204 ASP B OD2 1 
ATOM   8236  N N   . LEU C 1 176 ? 8.856   20.984  -20.925 1.00 23.83  ? 205 LEU B N   1 
ATOM   8237  C CA  . LEU C 1 176 ? 7.413   20.842  -21.049 1.00 24.82  ? 205 LEU B CA  1 
ATOM   8238  C C   . LEU C 1 176 ? 7.119   19.515  -21.738 1.00 24.43  ? 205 LEU B C   1 
ATOM   8239  O O   . LEU C 1 176 ? 6.336   18.709  -21.244 1.00 24.30  ? 205 LEU B O   1 
ATOM   8240  C CB  . LEU C 1 176 ? 6.791   22.015  -21.827 1.00 27.46  ? 205 LEU B CB  1 
ATOM   8241  C CG  . LEU C 1 176 ? 5.279   21.917  -22.104 1.00 27.38  ? 205 LEU B CG  1 
ATOM   8242  C CD1 . LEU C 1 176 ? 4.491   21.561  -20.848 1.00 29.54  ? 205 LEU B CD1 1 
ATOM   8243  C CD2 . LEU C 1 176 ? 4.702   23.198  -22.672 1.00 25.91  ? 205 LEU B CD2 1 
ATOM   8244  N N   . ILE C 1 177 ? 7.784   19.257  -22.866 1.00 23.47  ? 206 ILE B N   1 
ATOM   8245  C CA  . ILE C 1 177 ? 7.598   17.998  -23.587 1.00 25.70  ? 206 ILE B CA  1 
ATOM   8246  C C   . ILE C 1 177 ? 7.837   16.817  -22.657 1.00 24.81  ? 206 ILE B C   1 
ATOM   8247  O O   . ILE C 1 177 ? 6.970   15.926  -22.559 1.00 24.15  ? 206 ILE B O   1 
ATOM   8248  C CB  . ILE C 1 177 ? 8.456   17.940  -24.855 1.00 26.71  ? 206 ILE B CB  1 
ATOM   8249  C CG1 . ILE C 1 177 ? 7.855   18.877  -25.915 1.00 26.91  ? 206 ILE B CG1 1 
ATOM   8250  C CG2 . ILE C 1 177 ? 8.538   16.511  -25.381 1.00 32.95  ? 206 ILE B CG2 1 
ATOM   8251  C CD1 . ILE C 1 177 ? 8.785   19.263  -27.043 1.00 29.99  ? 206 ILE B CD1 1 
ATOM   8252  N N   . ALA C 1 178 ? 8.936   16.868  -21.899 1.00 26.89  ? 207 ALA B N   1 
ATOM   8253  C CA  . ALA C 1 178 ? 9.283   15.775  -20.992 1.00 27.25  ? 207 ALA B CA  1 
ATOM   8254  C C   . ALA C 1 178 ? 8.261   15.622  -19.868 1.00 29.62  ? 207 ALA B C   1 
ATOM   8255  O O   . ALA C 1 178 ? 8.034   14.506  -19.426 1.00 28.04  ? 207 ALA B O   1 
ATOM   8256  C CB  . ALA C 1 178 ? 10.646  15.995  -20.434 1.00 27.30  ? 207 ALA B CB  1 
ATOM   8257  N N   . LYS C 1 179 ? 7.607   16.728  -19.446 1.00 30.02  ? 208 LYS B N   1 
ATOM   8258  C CA  . LYS C 1 179 ? 6.711   16.702  -18.304 1.00 28.26  ? 208 LYS B CA  1 
ATOM   8259  C C   . LYS C 1 179 ? 5.304   16.249  -18.660 1.00 31.39  ? 208 LYS B C   1 
ATOM   8260  O O   . LYS C 1 179 ? 4.532   15.796  -17.811 1.00 28.73  ? 208 LYS B O   1 
ATOM   8261  C CB  . LYS C 1 179 ? 6.632   18.072  -17.630 1.00 28.21  ? 208 LYS B CB  1 
ATOM   8262  C CG  . LYS C 1 179 ? 7.958   18.385  -16.890 1.00 28.79  ? 208 LYS B CG  1 
ATOM   8263  C CD  . LYS C 1 179 ? 7.913   19.741  -16.191 1.00 27.64  ? 208 LYS B CD  1 
ATOM   8264  C CE  . LYS C 1 179 ? 9.243   20.428  -16.239 1.00 32.91  ? 208 LYS B CE  1 
ATOM   8265  N NZ  . LYS C 1 179 ? 10.201  19.494  -15.643 1.00 34.48  ? 208 LYS B NZ  1 
ATOM   8266  N N   . LEU C 1 180 ? 4.958   16.382  -19.924 1.00 30.50  ? 209 LEU B N   1 
ATOM   8267  C CA  . LEU C 1 180 ? 3.566   16.367  -20.304 1.00 32.22  ? 209 LEU B CA  1 
ATOM   8268  C C   . LEU C 1 180 ? 2.939   14.988  -20.073 1.00 30.33  ? 209 LEU B C   1 
ATOM   8269  O O   . LEU C 1 180 ? 1.803   14.914  -19.610 1.00 27.12  ? 209 LEU B O   1 
ATOM   8270  C CB  . LEU C 1 180 ? 3.598   16.809  -21.762 1.00 29.47  ? 209 LEU B CB  1 
ATOM   8271  C CG  . LEU C 1 180 ? 2.522   17.766  -22.268 1.00 34.83  ? 209 LEU B CG  1 
ATOM   8272  C CD1 . LEU C 1 180 ? 1.704   18.599  -21.298 1.00 33.61  ? 209 LEU B CD1 1 
ATOM   8273  C CD2 . LEU C 1 180 ? 3.267   18.664  -23.250 1.00 33.20  ? 209 LEU B CD2 1 
ATOM   8274  N N   . PRO C 1 181 ? 3.613   13.868  -20.419 1.00 30.70  ? 210 PRO B N   1 
ATOM   8275  C CA  . PRO C 1 181 ? 3.074   12.538  -20.169 1.00 32.56  ? 210 PRO B CA  1 
ATOM   8276  C C   . PRO C 1 181 ? 2.761   12.275  -18.699 1.00 33.71  ? 210 PRO B C   1 
ATOM   8277  O O   . PRO C 1 181 ? 1.778   11.608  -18.411 1.00 32.62  ? 210 PRO B O   1 
ATOM   8278  C CB  . PRO C 1 181 ? 4.205   11.637  -20.680 1.00 32.99  ? 210 PRO B CB  1 
ATOM   8279  C CG  . PRO C 1 181 ? 4.854   12.464  -21.763 1.00 32.51  ? 210 PRO B CG  1 
ATOM   8280  C CD  . PRO C 1 181 ? 4.933   13.806  -21.075 1.00 30.64  ? 210 PRO B CD  1 
ATOM   8281  N N   . CYS C 1 182 ? 3.568   12.810  -17.769 1.00 33.38  ? 211 CYS B N   1 
ATOM   8282  C CA  . CYS C 1 182 ? 3.261   12.645  -16.353 1.00 36.61  ? 211 CYS B CA  1 
ATOM   8283  C C   . CYS C 1 182 ? 2.044   13.449  -15.931 1.00 33.07  ? 211 CYS B C   1 
ATOM   8284  O O   . CYS C 1 182 ? 1.280   12.966  -15.112 1.00 28.14  ? 211 CYS B O   1 
ATOM   8285  C CB  . CYS C 1 182 ? 4.383   13.125  -15.435 1.00 38.72  ? 211 CYS B CB  1 
ATOM   8286  S SG  . CYS C 1 182 ? 6.000   12.545  -15.976 1.00 46.64  ? 211 CYS B SG  1 
ATOM   8287  N N   . VAL C 1 183 ? 1.939   14.707  -16.402 1.00 26.59  ? 212 VAL B N   1 
ATOM   8288  C CA  . VAL C 1 183 ? 0.732   15.501  -16.250 1.00 27.05  ? 212 VAL B CA  1 
ATOM   8289  C C   . VAL C 1 183 ? -0.452  14.697  -16.773 1.00 26.48  ? 212 VAL B C   1 
ATOM   8290  O O   . VAL C 1 183 ? -1.386  14.408  -16.025 1.00 27.42  ? 212 VAL B O   1 
ATOM   8291  C CB  . VAL C 1 183 ? 0.802   16.875  -16.949 1.00 27.99  ? 212 VAL B CB  1 
ATOM   8292  C CG1 . VAL C 1 183 ? -0.520  17.626  -16.875 1.00 28.68  ? 212 VAL B CG1 1 
ATOM   8293  C CG2 . VAL C 1 183 ? 1.923   17.702  -16.367 1.00 29.98  ? 212 VAL B CG2 1 
ATOM   8294  N N   . ALA C 1 184 ? -0.336  14.235  -18.015 1.00 23.57  ? 213 ALA B N   1 
ATOM   8295  C CA  . ALA C 1 184 ? -1.438  13.594  -18.700 1.00 26.11  ? 213 ALA B CA  1 
ATOM   8296  C C   . ALA C 1 184 ? -1.869  12.309  -17.968 1.00 30.15  ? 213 ALA B C   1 
ATOM   8297  O O   . ALA C 1 184 ? -3.069  12.027  -17.842 1.00 28.14  ? 213 ALA B O   1 
ATOM   8298  C CB  . ALA C 1 184 ? -1.051  13.325  -20.127 1.00 25.79  ? 213 ALA B CB  1 
ATOM   8299  N N   . ALA C 1 185 ? -0.897  11.568  -17.432 1.00 26.58  ? 214 ALA B N   1 
ATOM   8300  C CA  . ALA C 1 185 ? -1.160  10.252  -16.870 1.00 28.47  ? 214 ALA B CA  1 
ATOM   8301  C C   . ALA C 1 185 ? -1.744  10.393  -15.468 1.00 31.75  ? 214 ALA B C   1 
ATOM   8302  O O   . ALA C 1 185 ? -2.608  9.608   -15.080 1.00 32.06  ? 214 ALA B O   1 
ATOM   8303  C CB  . ALA C 1 185 ? 0.096   9.458   -16.859 1.00 28.08  ? 214 ALA B CB  1 
ATOM   8304  N N   . LYS C 1 186 ? -1.280  11.416  -14.747 1.00 29.88  ? 215 LYS B N   1 
ATOM   8305  C CA  . LYS C 1 186 ? -1.854  11.826  -13.479 1.00 32.22  ? 215 LYS B CA  1 
ATOM   8306  C C   . LYS C 1 186 ? -3.348  12.099  -13.615 1.00 35.17  ? 215 LYS B C   1 
ATOM   8307  O O   . LYS C 1 186 ? -4.147  11.584  -12.832 1.00 29.77  ? 215 LYS B O   1 
ATOM   8308  C CB  . LYS C 1 186 ? -0.964  12.942  -12.945 1.00 35.62  ? 215 LYS B CB  1 
ATOM   8309  C CG  . LYS C 1 186 ? -1.042  13.188  -11.442 1.00 43.54  ? 215 LYS B CG  1 
ATOM   8310  C CD  . LYS C 1 186 ? 0.042   12.544  -10.589 1.00 44.11  ? 215 LYS B CD  1 
ATOM   8311  C CE  . LYS C 1 186 ? -0.509  12.174  -9.209  1.00 44.65  ? 215 LYS B CE  1 
ATOM   8312  N N   . ILE C 1 187 ? -3.710  12.896  -14.623 1.00 33.26  ? 216 ILE B N   1 
ATOM   8313  C CA  . ILE C 1 187 ? -5.089  13.230  -14.919 1.00 33.51  ? 216 ILE B CA  1 
ATOM   8314  C C   . ILE C 1 187 ? -5.903  11.969  -15.168 1.00 33.84  ? 216 ILE B C   1 
ATOM   8315  O O   . ILE C 1 187 ? -6.998  11.807  -14.627 1.00 32.28  ? 216 ILE B O   1 
ATOM   8316  C CB  . ILE C 1 187 ? -5.163  14.158  -16.142 1.00 32.49  ? 216 ILE B CB  1 
ATOM   8317  C CG1 . ILE C 1 187 ? -4.631  15.547  -15.776 1.00 35.13  ? 216 ILE B CG1 1 
ATOM   8318  C CG2 . ILE C 1 187 ? -6.581  14.202  -16.726 1.00 35.05  ? 216 ILE B CG2 1 
ATOM   8319  C CD1 . ILE C 1 187 ? -4.601  16.533  -16.923 1.00 34.89  ? 216 ILE B CD1 1 
ATOM   8320  N N   . TYR C 1 188 ? -5.365  11.105  -16.023 1.00 28.00  ? 217 TYR B N   1 
ATOM   8321  C CA  . TYR C 1 188 ? -6.062  9.895   -16.383 1.00 29.87  ? 217 TYR B CA  1 
ATOM   8322  C C   . TYR C 1 188 ? -6.351  9.067   -15.124 1.00 30.79  ? 217 TYR B C   1 
ATOM   8323  O O   . TYR C 1 188 ? -7.490  8.647   -14.889 1.00 30.67  ? 217 TYR B O   1 
ATOM   8324  C CB  . TYR C 1 188 ? -5.216  9.179   -17.434 1.00 30.00  ? 217 TYR B CB  1 
ATOM   8325  C CG  . TYR C 1 188 ? -5.899  7.930   -17.975 1.00 32.22  ? 217 TYR B CG  1 
ATOM   8326  C CD1 . TYR C 1 188 ? -6.866  8.024   -18.961 1.00 35.36  ? 217 TYR B CD1 1 
ATOM   8327  C CD2 . TYR C 1 188 ? -5.579  6.660   -17.515 1.00 30.98  ? 217 TYR B CD2 1 
ATOM   8328  C CE1 . TYR C 1 188 ? -7.521  6.912   -19.462 1.00 32.66  ? 217 TYR B CE1 1 
ATOM   8329  C CE2 . TYR C 1 188 ? -6.189  5.531   -18.038 1.00 33.16  ? 217 TYR B CE2 1 
ATOM   8330  C CZ  . TYR C 1 188 ? -7.170  5.652   -19.007 1.00 36.47  ? 217 TYR B CZ  1 
ATOM   8331  O OH  . TYR C 1 188 ? -7.817  4.568   -19.542 1.00 37.30  ? 217 TYR B OH  1 
ATOM   8332  N N   . ARG C 1 189 ? -5.315  8.839   -14.324 1.00 27.65  ? 218 ARG B N   1 
ATOM   8333  C CA  . ARG C 1 189 ? -5.433  7.969   -13.168 1.00 35.00  ? 218 ARG B CA  1 
ATOM   8334  C C   . ARG C 1 189 ? -6.236  8.600   -12.027 1.00 34.33  ? 218 ARG B C   1 
ATOM   8335  O O   . ARG C 1 189 ? -6.898  7.891   -11.278 1.00 42.58  ? 218 ARG B O   1 
ATOM   8336  C CB  . ARG C 1 189 ? -4.053  7.583   -12.651 1.00 34.81  ? 218 ARG B CB  1 
ATOM   8337  C CG  . ARG C 1 189 ? -3.261  6.666   -13.566 1.00 42.43  ? 218 ARG B CG  1 
ATOM   8338  C CD  . ARG C 1 189 ? -2.549  5.653   -12.699 1.00 49.10  ? 218 ARG B CD  1 
ATOM   8339  N NE  . ARG C 1 189 ? -1.373  5.133   -13.385 1.00 58.66  ? 218 ARG B NE  1 
ATOM   8340  C CZ  . ARG C 1 189 ? -1.028  3.860   -13.402 1.00 62.33  ? 218 ARG B CZ  1 
ATOM   8341  N NH1 . ARG C 1 189 ? -1.865  2.952   -12.925 1.00 66.91  ? 218 ARG B NH1 1 
ATOM   8342  N NH2 . ARG C 1 189 ? 0.150   3.519   -13.893 1.00 54.73  ? 218 ARG B NH2 1 
ATOM   8343  N N   . ASN C 1 190 ? -6.132  9.908   -11.830 1.00 36.39  ? 219 ASN B N   1 
ATOM   8344  C CA  . ASN C 1 190 ? -6.966  10.573  -10.841 1.00 35.43  ? 219 ASN B CA  1 
ATOM   8345  C C   . ASN C 1 190 ? -8.420  10.528  -11.283 1.00 37.78  ? 219 ASN B C   1 
ATOM   8346  O O   . ASN C 1 190 ? -9.297  10.444  -10.427 1.00 42.52  ? 219 ASN B O   1 
ATOM   8347  C CB  . ASN C 1 190 ? -6.563  12.017  -10.572 1.00 32.36  ? 219 ASN B CB  1 
ATOM   8348  C CG  . ASN C 1 190 ? -5.230  12.122  -9.872  1.00 35.37  ? 219 ASN B CG  1 
ATOM   8349  O OD1 . ASN C 1 190 ? -4.678  11.113  -9.427  1.00 36.26  ? 219 ASN B OD1 1 
ATOM   8350  N ND2 . ASN C 1 190 ? -4.676  13.321  -9.785  1.00 38.03  ? 219 ASN B ND2 1 
ATOM   8351  N N   . LEU C 1 191 ? -8.688  10.586  -12.601 1.00 34.80  ? 220 LEU B N   1 
ATOM   8352  C CA  . LEU C 1 191 ? -10.067 10.590  -13.058 1.00 33.98  ? 220 LEU B CA  1 
ATOM   8353  C C   . LEU C 1 191 ? -10.624 9.164   -13.115 1.00 34.58  ? 220 LEU B C   1 
ATOM   8354  O O   . LEU C 1 191 ? -11.792 8.937   -12.796 1.00 35.83  ? 220 LEU B O   1 
ATOM   8355  C CB  . LEU C 1 191 ? -10.228 11.275  -14.416 1.00 33.54  ? 220 LEU B CB  1 
ATOM   8356  C CG  . LEU C 1 191 ? -10.105 12.804  -14.425 1.00 39.35  ? 220 LEU B CG  1 
ATOM   8357  C CD1 . LEU C 1 191 ? -10.198 13.356  -15.834 1.00 37.69  ? 220 LEU B CD1 1 
ATOM   8358  C CD2 . LEU C 1 191 ? -11.182 13.418  -13.530 1.00 42.61  ? 220 LEU B CD2 1 
ATOM   8359  N N   . TYR C 1 192 ? -9.840  8.220   -13.620 1.00 34.84  ? 221 TYR B N   1 
ATOM   8360  C CA  . TYR C 1 192 ? -10.408 6.958   -14.071 1.00 40.06  ? 221 TYR B CA  1 
ATOM   8361  C C   . TYR C 1 192 ? -9.768  5.742   -13.391 1.00 42.93  ? 221 TYR B C   1 
ATOM   8362  O O   . TYR C 1 192 ? -10.110 4.613   -13.740 1.00 37.70  ? 221 TYR B O   1 
ATOM   8363  C CB  . TYR C 1 192 ? -10.304 6.853   -15.594 1.00 39.36  ? 221 TYR B CB  1 
ATOM   8364  C CG  . TYR C 1 192 ? -10.799 8.090   -16.340 1.00 42.46  ? 221 TYR B CG  1 
ATOM   8365  C CD1 . TYR C 1 192 ? -12.137 8.487   -16.295 1.00 42.99  ? 221 TYR B CD1 1 
ATOM   8366  C CD2 . TYR C 1 192 ? -9.934  8.836   -17.130 1.00 43.25  ? 221 TYR B CD2 1 
ATOM   8367  C CE1 . TYR C 1 192 ? -12.582 9.607   -16.978 1.00 41.19  ? 221 TYR B CE1 1 
ATOM   8368  C CE2 . TYR C 1 192 ? -10.361 9.962   -17.810 1.00 38.36  ? 221 TYR B CE2 1 
ATOM   8369  C CZ  . TYR C 1 192 ? -11.684 10.352  -17.729 1.00 44.49  ? 221 TYR B CZ  1 
ATOM   8370  O OH  . TYR C 1 192 ? -12.057 11.475  -18.412 1.00 47.51  ? 221 TYR B OH  1 
ATOM   8371  N N   . ARG C 1 193 ? -8.837  5.945   -12.443 1.00 41.18  ? 222 ARG B N   1 
ATOM   8372  C CA  . ARG C 1 193 ? -8.220  4.823   -11.742 1.00 39.77  ? 222 ARG B CA  1 
ATOM   8373  C C   . ARG C 1 193 ? -8.137  5.106   -10.243 1.00 37.05  ? 222 ARG B C   1 
ATOM   8374  O O   . ARG C 1 193 ? -7.164  4.742   -9.593  1.00 41.61  ? 222 ARG B O   1 
ATOM   8375  C CB  . ARG C 1 193 ? -6.838  4.550   -12.330 1.00 37.29  ? 222 ARG B CB  1 
ATOM   8376  C CG  . ARG C 1 193 ? -6.792  4.127   -13.797 1.00 36.82  ? 222 ARG B CG  1 
ATOM   8377  C CD  . ARG C 1 193 ? -7.237  2.704   -14.022 1.00 39.47  ? 222 ARG B CD  1 
ATOM   8378  N NE  . ARG C 1 193 ? -7.060  2.240   -15.403 1.00 41.08  ? 222 ARG B NE  1 
ATOM   8379  C CZ  . ARG C 1 193 ? -7.885  2.487   -16.439 1.00 43.50  ? 222 ARG B CZ  1 
ATOM   8380  N NH1 . ARG C 1 193 ? -8.954  3.248   -16.288 1.00 38.14  ? 222 ARG B NH1 1 
ATOM   8381  N NH2 . ARG C 1 193 ? -7.645  1.947   -17.632 1.00 40.86  ? 222 ARG B NH2 1 
ATOM   8382  N N   . GLU C 1 194 ? -9.128  5.832   -9.721  1.00 41.51  ? 223 GLU B N   1 
ATOM   8383  C CA  . GLU C 1 194 ? -9.247  6.120   -8.296  1.00 53.51  ? 223 GLU B CA  1 
ATOM   8384  C C   . GLU C 1 194 ? -7.956  6.687   -7.706  1.00 48.56  ? 223 GLU B C   1 
ATOM   8385  O O   . GLU C 1 194 ? -7.684  6.490   -6.531  1.00 43.42  ? 223 GLU B O   1 
ATOM   8386  C CB  . GLU C 1 194 ? -9.557  4.854   -7.488  1.00 55.74  ? 223 GLU B CB  1 
ATOM   8387  C CG  . GLU C 1 194 ? -10.576 3.914   -8.131  1.00 64.04  ? 223 GLU B CG  1 
ATOM   8388  C CD  . GLU C 1 194 ? -10.412 2.471   -7.674  1.00 76.04  ? 223 GLU B CD  1 
ATOM   8389  O OE1 . GLU C 1 194 ? -10.346 1.567   -8.543  1.00 86.06  ? 223 GLU B OE1 1 
ATOM   8390  O OE2 . GLU C 1 194 ? -10.305 2.252   -6.444  1.00 81.16  ? 223 GLU B OE2 1 
ATOM   8391  N N   . GLY C 1 195 ? -7.134  7.373   -8.503  1.00 45.47  ? 224 GLY B N   1 
ATOM   8392  C CA  . GLY C 1 195 ? -6.011  8.097   -7.932  1.00 46.80  ? 224 GLY B CA  1 
ATOM   8393  C C   . GLY C 1 195 ? -4.793  7.227   -7.640  1.00 43.36  ? 224 GLY B C   1 
ATOM   8394  O O   . GLY C 1 195 ? -3.868  7.682   -6.973  1.00 51.79  ? 224 GLY B O   1 
ATOM   8395  N N   . SER C 1 196 ? -4.743  6.006   -8.173  1.00 42.82  ? 225 SER B N   1 
ATOM   8396  C CA  . SER C 1 196 ? -3.530  5.203   -8.078  1.00 46.68  ? 225 SER B CA  1 
ATOM   8397  C C   . SER C 1 196 ? -2.346  5.974   -8.654  1.00 54.26  ? 225 SER B C   1 
ATOM   8398  O O   . SER C 1 196 ? -2.550  6.878   -9.468  1.00 52.43  ? 225 SER B O   1 
ATOM   8399  C CB  . SER C 1 196 ? -3.699  3.904   -8.776  1.00 49.60  ? 225 SER B CB  1 
ATOM   8400  O OG  . SER C 1 196 ? -4.302  4.125   -10.038 1.00 60.10  ? 225 SER B OG  1 
ATOM   8401  N N   . GLY C 1 197 ? -1.125  5.612   -8.223  1.00 47.11  ? 226 GLY B N   1 
ATOM   8402  C CA  . GLY C 1 197 ? 0.083   6.326   -8.607  1.00 46.20  ? 226 GLY B CA  1 
ATOM   8403  C C   . GLY C 1 197 ? 0.450   6.071   -10.075 1.00 47.42  ? 226 GLY B C   1 
ATOM   8404  O O   . GLY C 1 197 ? 0.015   5.082   -10.651 1.00 47.16  ? 226 GLY B O   1 
ATOM   8405  N N   . ILE C 1 198 ? 1.229   6.986   -10.680 1.00 39.08  ? 227 ILE B N   1 
ATOM   8406  C CA  . ILE C 1 198 ? 1.634   6.862   -12.075 1.00 43.10  ? 227 ILE B CA  1 
ATOM   8407  C C   . ILE C 1 198 ? 2.910   6.039   -12.131 1.00 44.79  ? 227 ILE B C   1 
ATOM   8408  O O   . ILE C 1 198 ? 3.313   5.600   -13.205 1.00 42.98  ? 227 ILE B O   1 
ATOM   8409  C CB  . ILE C 1 198 ? 1.819   8.219   -12.796 1.00 38.48  ? 227 ILE B CB  1 
ATOM   8410  C CG1 . ILE C 1 198 ? 2.665   9.219   -12.008 1.00 36.00  ? 227 ILE B CG1 1 
ATOM   8411  C CG2 . ILE C 1 198 ? 0.471   8.838   -13.175 1.00 40.04  ? 227 ILE B CG2 1 
ATOM   8412  C CD1 . ILE C 1 198 ? 2.946   10.498  -12.789 1.00 41.76  ? 227 ILE B CD1 1 
ATOM   8413  N N   . GLY C 1 199 ? 3.543   5.861   -10.964 1.00 48.63  ? 228 GLY B N   1 
ATOM   8414  C CA  . GLY C 1 199 ? 4.769   5.098   -10.877 1.00 49.68  ? 228 GLY B CA  1 
ATOM   8415  C C   . GLY C 1 199 ? 5.924   5.945   -11.393 1.00 52.74  ? 228 GLY B C   1 
ATOM   8416  O O   . GLY C 1 199 ? 5.908   7.169   -11.251 1.00 47.53  ? 228 GLY B O   1 
ATOM   8417  N N   . ALA C 1 200 ? 6.887   5.278   -12.032 1.00 50.98  ? 229 ALA B N   1 
ATOM   8418  C CA  . ALA C 1 200 ? 8.195   5.865   -12.263 1.00 44.86  ? 229 ALA B CA  1 
ATOM   8419  C C   . ALA C 1 200 ? 8.477   5.941   -13.756 1.00 44.84  ? 229 ALA B C   1 
ATOM   8420  O O   . ALA C 1 200 ? 7.769   5.354   -14.579 1.00 42.37  ? 229 ALA B O   1 
ATOM   8421  C CB  . ALA C 1 200 ? 9.257   5.066   -11.535 1.00 43.80  ? 229 ALA B CB  1 
ATOM   8422  N N   . ILE C 1 201 ? 9.479   6.761   -14.056 1.00 42.29  ? 230 ILE B N   1 
ATOM   8423  C CA  . ILE C 1 201 ? 9.990   6.980   -15.388 1.00 42.61  ? 230 ILE B CA  1 
ATOM   8424  C C   . ILE C 1 201 ? 11.195  6.069   -15.536 1.00 44.25  ? 230 ILE B C   1 
ATOM   8425  O O   . ILE C 1 201 ? 12.081  6.074   -14.685 1.00 50.18  ? 230 ILE B O   1 
ATOM   8426  C CB  . ILE C 1 201 ? 10.397  8.457   -15.549 1.00 42.29  ? 230 ILE B CB  1 
ATOM   8427  C CG1 . ILE C 1 201 ? 9.197   9.400   -15.584 1.00 46.41  ? 230 ILE B CG1 1 
ATOM   8428  C CG2 . ILE C 1 201 ? 11.271  8.648   -16.779 1.00 42.70  ? 230 ILE B CG2 1 
ATOM   8429  C CD1 . ILE C 1 201 ? 8.418   9.374   -16.892 1.00 47.35  ? 230 ILE B CD1 1 
ATOM   8430  N N   . ASP C 1 202 ? 11.235  5.307   -16.622 1.00 39.96  ? 231 ASP B N   1 
ATOM   8431  C CA  . ASP C 1 202 ? 12.392  4.488   -16.923 1.00 41.25  ? 231 ASP B CA  1 
ATOM   8432  C C   . ASP C 1 202 ? 13.271  5.231   -17.927 1.00 41.86  ? 231 ASP B C   1 
ATOM   8433  O O   . ASP C 1 202 ? 12.818  5.588   -19.013 1.00 42.78  ? 231 ASP B O   1 
ATOM   8434  C CB  . ASP C 1 202 ? 11.958  3.106   -17.373 1.00 42.28  ? 231 ASP B CB  1 
ATOM   8435  C CG  . ASP C 1 202 ? 13.078  2.248   -17.941 1.00 46.86  ? 231 ASP B CG  1 
ATOM   8436  O OD1 . ASP C 1 202 ? 14.192  2.796   -18.216 1.00 47.96  ? 231 ASP B OD1 1 
ATOM   8437  O OD2 . ASP C 1 202 ? 12.827  1.039   -18.104 1.00 58.80  ? 231 ASP B OD2 1 
ATOM   8438  N N   . SER C 1 203 ? 14.550  5.418   -17.588 1.00 38.70  ? 232 SER B N   1 
ATOM   8439  C CA  . SER C 1 203 ? 15.366  6.397   -18.295 1.00 44.68  ? 232 SER B CA  1 
ATOM   8440  C C   . SER C 1 203 ? 15.841  5.849   -19.641 1.00 41.09  ? 232 SER B C   1 
ATOM   8441  O O   . SER C 1 203 ? 16.325  6.606   -20.472 1.00 47.75  ? 232 SER B O   1 
ATOM   8442  C CB  . SER C 1 203 ? 16.515  6.882   -17.441 1.00 43.33  ? 232 SER B CB  1 
ATOM   8443  O OG  . SER C 1 203 ? 17.439  5.833   -17.249 1.00 54.94  ? 232 SER B OG  1 
ATOM   8444  N N   . ASN C 1 204 ? 15.660  4.544   -19.867 1.00 42.77  ? 233 ASN B N   1 
ATOM   8445  C CA  . ASN C 1 204 ? 16.060  3.894   -21.100 1.00 42.46  ? 233 ASN B CA  1 
ATOM   8446  C C   . ASN C 1 204 ? 14.870  3.628   -22.024 1.00 40.89  ? 233 ASN B C   1 
ATOM   8447  O O   . ASN C 1 204 ? 15.042  3.026   -23.077 1.00 40.58  ? 233 ASN B O   1 
ATOM   8448  C CB  . ASN C 1 204 ? 16.750  2.566   -20.795 1.00 53.04  ? 233 ASN B CB  1 
ATOM   8449  C CG  . ASN C 1 204 ? 18.042  2.748   -20.035 1.00 54.65  ? 233 ASN B CG  1 
ATOM   8450  O OD1 . ASN C 1 204 ? 18.206  2.162   -18.962 1.00 55.57  ? 233 ASN B OD1 1 
ATOM   8451  N ND2 . ASN C 1 204 ? 18.960  3.547   -20.566 1.00 49.91  ? 233 ASN B ND2 1 
ATOM   8452  N N   . LEU C 1 205 ? 13.657  4.052   -21.652 1.00 37.83  ? 234 LEU B N   1 
ATOM   8453  C CA  . LEU C 1 205 ? 12.499  3.836   -22.501 1.00 39.63  ? 234 LEU B CA  1 
ATOM   8454  C C   . LEU C 1 205 ? 12.261  5.099   -23.318 1.00 37.20  ? 234 LEU B C   1 
ATOM   8455  O O   . LEU C 1 205 ? 12.689  6.163   -22.932 1.00 33.15  ? 234 LEU B O   1 
ATOM   8456  C CB  . LEU C 1 205 ? 11.230  3.462   -21.730 1.00 38.17  ? 234 LEU B CB  1 
ATOM   8457  C CG  . LEU C 1 205 ? 11.264  2.152   -20.935 1.00 43.63  ? 234 LEU B CG  1 
ATOM   8458  C CD1 . LEU C 1 205 ? 9.955   1.981   -20.186 1.00 42.98  ? 234 LEU B CD1 1 
ATOM   8459  C CD2 . LEU C 1 205 ? 11.520  0.940   -21.838 1.00 45.77  ? 234 LEU B CD2 1 
ATOM   8460  N N   . ASP C 1 206 ? 11.530  4.960   -24.419 1.00 35.13  ? 235 ASP B N   1 
ATOM   8461  C CA  . ASP C 1 206 ? 11.052  6.099   -25.180 1.00 32.31  ? 235 ASP B CA  1 
ATOM   8462  C C   . ASP C 1 206 ? 9.870   6.780   -24.471 1.00 29.75  ? 235 ASP B C   1 
ATOM   8463  O O   . ASP C 1 206 ? 9.192   6.242   -23.576 1.00 26.44  ? 235 ASP B O   1 
ATOM   8464  C CB  . ASP C 1 206 ? 10.842  5.703   -26.642 1.00 34.55  ? 235 ASP B CB  1 
ATOM   8465  C CG  . ASP C 1 206 ? 9.726   4.706   -26.920 1.00 40.04  ? 235 ASP B CG  1 
ATOM   8466  O OD1 . ASP C 1 206 ? 9.933   3.507   -26.613 1.00 46.26  ? 235 ASP B OD1 1 
ATOM   8467  O OD2 . ASP C 1 206 ? 8.642   5.134   -27.409 1.00 34.23  ? 235 ASP B OD2 1 
ATOM   8468  N N   . TRP C 1 207 ? 9.631   8.011   -24.913 1.00 25.76  ? 236 TRP B N   1 
ATOM   8469  C CA  . TRP C 1 207 ? 8.645   8.929   -24.377 1.00 24.43  ? 236 TRP B CA  1 
ATOM   8470  C C   . TRP C 1 207 ? 7.250   8.282   -24.375 1.00 26.68  ? 236 TRP B C   1 
ATOM   8471  O O   . TRP C 1 207 ? 6.535   8.348   -23.366 1.00 25.80  ? 236 TRP B O   1 
ATOM   8472  C CB  . TRP C 1 207 ? 8.760   10.199  -25.256 1.00 27.68  ? 236 TRP B CB  1 
ATOM   8473  C CG  . TRP C 1 207 ? 7.974   11.402  -24.809 1.00 29.73  ? 236 TRP B CG  1 
ATOM   8474  C CD1 . TRP C 1 207 ? 8.140   12.134  -23.668 1.00 31.14  ? 236 TRP B CD1 1 
ATOM   8475  C CD2 . TRP C 1 207 ? 6.954   12.072  -25.575 1.00 28.99  ? 236 TRP B CD2 1 
ATOM   8476  N NE1 . TRP C 1 207 ? 7.254   13.174  -23.648 1.00 29.77  ? 236 TRP B NE1 1 
ATOM   8477  C CE2 . TRP C 1 207 ? 6.508   13.156  -24.801 1.00 28.56  ? 236 TRP B CE2 1 
ATOM   8478  C CE3 . TRP C 1 207 ? 6.359   11.833  -26.816 1.00 32.73  ? 236 TRP B CE3 1 
ATOM   8479  C CZ2 . TRP C 1 207 ? 5.502   14.008  -25.243 1.00 30.62  ? 236 TRP B CZ2 1 
ATOM   8480  C CZ3 . TRP C 1 207 ? 5.345   12.660  -27.241 1.00 33.44  ? 236 TRP B CZ3 1 
ATOM   8481  C CH2 . TRP C 1 207 ? 4.940   13.752  -26.475 1.00 30.21  ? 236 TRP B CH2 1 
ATOM   8482  N N   . SER C 1 208 ? 6.907   7.587   -25.481 1.00 25.80  ? 237 SER B N   1 
ATOM   8483  C CA  . SER C 1 208 ? 5.618   6.943   -25.669 1.00 29.04  ? 237 SER B CA  1 
ATOM   8484  C C   . SER C 1 208 ? 5.395   5.779   -24.701 1.00 32.01  ? 237 SER B C   1 
ATOM   8485  O O   . SER C 1 208 ? 4.282   5.597   -24.200 1.00 29.41  ? 237 SER B O   1 
ATOM   8486  C CB  . SER C 1 208 ? 5.447   6.458   -27.067 1.00 28.49  ? 237 SER B CB  1 
ATOM   8487  O OG  . SER C 1 208 ? 5.430   7.544   -27.982 1.00 28.27  ? 237 SER B OG  1 
ATOM   8488  N N   . HIS C 1 209 ? 6.455   5.003   -24.459 1.00 33.62  ? 238 HIS B N   1 
ATOM   8489  C CA  . HIS C 1 209 ? 6.385   3.834   -23.603 1.00 32.05  ? 238 HIS B CA  1 
ATOM   8490  C C   . HIS C 1 209 ? 6.300   4.261   -22.135 1.00 32.17  ? 238 HIS B C   1 
ATOM   8491  O O   . HIS C 1 209 ? 5.505   3.723   -21.384 1.00 36.45  ? 238 HIS B O   1 
ATOM   8492  C CB  . HIS C 1 209 ? 7.569   2.914   -23.909 1.00 36.54  ? 238 HIS B CB  1 
ATOM   8493  C CG  . HIS C 1 209 ? 7.400   1.531   -23.391 1.00 47.77  ? 238 HIS B CG  1 
ATOM   8494  N ND1 . HIS C 1 209 ? 8.396   0.584   -23.519 1.00 47.60  ? 238 HIS B ND1 1 
ATOM   8495  C CD2 . HIS C 1 209 ? 6.367   0.925   -22.757 1.00 50.27  ? 238 HIS B CD2 1 
ATOM   8496  C CE1 . HIS C 1 209 ? 7.971   -0.555  -22.974 1.00 54.74  ? 238 HIS B CE1 1 
ATOM   8497  N NE2 . HIS C 1 209 ? 6.744   -0.378  -22.517 1.00 49.85  ? 238 HIS B NE2 1 
ATOM   8498  N N   . ASN C 1 210 ? 7.099   5.248   -21.721 1.00 31.52  ? 239 ASN B N   1 
ATOM   8499  C CA  . ASN C 1 210 ? 6.940   5.818   -20.395 1.00 32.37  ? 239 ASN B CA  1 
ATOM   8500  C C   . ASN C 1 210 ? 5.491   6.260   -20.218 1.00 29.46  ? 239 ASN B C   1 
ATOM   8501  O O   . ASN C 1 210 ? 4.890   6.039   -19.176 1.00 33.38  ? 239 ASN B O   1 
ATOM   8502  C CB  . ASN C 1 210 ? 7.958   6.930   -20.114 1.00 30.46  ? 239 ASN B CB  1 
ATOM   8503  C CG  . ASN C 1 210 ? 9.325   6.400   -19.730 1.00 33.75  ? 239 ASN B CG  1 
ATOM   8504  O OD1 . ASN C 1 210 ? 10.366  6.838   -20.237 1.00 34.39  ? 239 ASN B OD1 1 
ATOM   8505  N ND2 . ASN C 1 210 ? 9.351   5.487   -18.786 1.00 29.18  ? 239 ASN B ND2 1 
ATOM   8506  N N   . PHE C 1 211 ? 4.929   6.918   -21.231 1.00 31.79  ? 240 PHE B N   1 
ATOM   8507  C CA  . PHE C 1 211 ? 3.586   7.447   -21.124 1.00 30.46  ? 240 PHE B CA  1 
ATOM   8508  C C   . PHE C 1 211 ? 2.582   6.299   -20.940 1.00 33.43  ? 240 PHE B C   1 
ATOM   8509  O O   . PHE C 1 211 ? 1.731   6.342   -20.049 1.00 37.62  ? 240 PHE B O   1 
ATOM   8510  C CB  . PHE C 1 211 ? 3.339   8.349   -22.336 1.00 29.24  ? 240 PHE B CB  1 
ATOM   8511  C CG  . PHE C 1 211 ? 1.997   9.054   -22.344 1.00 29.76  ? 240 PHE B CG  1 
ATOM   8512  C CD1 . PHE C 1 211 ? 1.342   9.366   -21.165 1.00 27.44  ? 240 PHE B CD1 1 
ATOM   8513  C CD2 . PHE C 1 211 ? 1.352   9.340   -23.545 1.00 33.70  ? 240 PHE B CD2 1 
ATOM   8514  C CE1 . PHE C 1 211 ? 0.106   10.003  -21.188 1.00 28.28  ? 240 PHE B CE1 1 
ATOM   8515  C CE2 . PHE C 1 211 ? 0.132   9.994   -23.553 1.00 31.94  ? 240 PHE B CE2 1 
ATOM   8516  C CZ  . PHE C 1 211 ? -0.486  10.330  -22.376 1.00 30.13  ? 240 PHE B CZ  1 
ATOM   8517  N N   . THR C 1 212 ? 2.687   5.234   -21.732 1.00 32.39  ? 241 THR B N   1 
ATOM   8518  C CA  . THR C 1 212 ? 1.698   4.182   -21.595 1.00 33.07  ? 241 THR B CA  1 
ATOM   8519  C C   . THR C 1 212 ? 1.863   3.468   -20.246 1.00 34.28  ? 241 THR B C   1 
ATOM   8520  O O   . THR C 1 212 ? 0.842   3.083   -19.678 1.00 36.45  ? 241 THR B O   1 
ATOM   8521  C CB  . THR C 1 212 ? 1.720   3.212   -22.780 1.00 33.75  ? 241 THR B CB  1 
ATOM   8522  O OG1 . THR C 1 212 ? 2.992   2.621   -22.931 1.00 28.52  ? 241 THR B OG1 1 
ATOM   8523  C CG2 . THR C 1 212 ? 1.413   3.889   -24.098 1.00 32.37  ? 241 THR B CG2 1 
ATOM   8524  N N   . ASN C 1 213 ? 3.113   3.305   -19.758 1.00 34.06  ? 242 ASN B N   1 
ATOM   8525  C CA  . ASN C 1 213 ? 3.411   2.737   -18.445 1.00 37.06  ? 242 ASN B CA  1 
ATOM   8526  C C   . ASN C 1 213 ? 2.717   3.579   -17.384 1.00 38.05  ? 242 ASN B C   1 
ATOM   8527  O O   . ASN C 1 213 ? 2.127   3.092   -16.427 1.00 37.34  ? 242 ASN B O   1 
ATOM   8528  C CB  . ASN C 1 213 ? 4.909   2.716   -18.121 1.00 38.43  ? 242 ASN B CB  1 
ATOM   8529  C CG  . ASN C 1 213 ? 5.686   1.584   -18.768 1.00 40.69  ? 242 ASN B CG  1 
ATOM   8530  O OD1 . ASN C 1 213 ? 5.140   0.756   -19.503 1.00 37.08  ? 242 ASN B OD1 1 
ATOM   8531  N ND2 . ASN C 1 213 ? 6.976   1.512   -18.492 1.00 44.15  ? 242 ASN B ND2 1 
ATOM   8532  N N   . MET C 1 214 ? 2.762   4.879   -17.570 1.00 32.22  ? 243 MET B N   1 
ATOM   8533  C CA  . MET C 1 214 ? 2.209   5.731   -16.551 1.00 34.65  ? 243 MET B CA  1 
ATOM   8534  C C   . MET C 1 214 ? 0.692   5.669   -16.647 1.00 35.71  ? 243 MET B C   1 
ATOM   8535  O O   . MET C 1 214 ? 0.046   5.703   -15.609 1.00 33.65  ? 243 MET B O   1 
ATOM   8536  C CB  . MET C 1 214 ? 2.754   7.150   -16.660 1.00 34.77  ? 243 MET B CB  1 
ATOM   8537  C CG  . MET C 1 214 ? 4.212   7.245   -16.217 1.00 36.25  ? 243 MET B CG  1 
ATOM   8538  S SD  . MET C 1 214 ? 4.744   8.965   -16.158 1.00 41.46  ? 243 MET B SD  1 
ATOM   8539  C CE  . MET C 1 214 ? 5.016   9.349   -17.890 1.00 34.69  ? 243 MET B CE  1 
ATOM   8540  N N   . LEU C 1 215 ? 0.138   5.529   -17.857 1.00 31.62  ? 244 LEU B N   1 
ATOM   8541  C CA  . LEU C 1 215 ? -1.305  5.396   -17.984 1.00 34.72  ? 244 LEU B CA  1 
ATOM   8542  C C   . LEU C 1 215 ? -1.808  4.111   -17.289 1.00 37.02  ? 244 LEU B C   1 
ATOM   8543  O O   . LEU C 1 215 ? -2.952  4.055   -16.841 1.00 39.30  ? 244 LEU B O   1 
ATOM   8544  C CB  . LEU C 1 215 ? -1.715  5.442   -19.457 1.00 33.19  ? 244 LEU B CB  1 
ATOM   8545  C CG  . LEU C 1 215 ? -1.566  6.781   -20.197 1.00 31.79  ? 244 LEU B CG  1 
ATOM   8546  C CD1 . LEU C 1 215 ? -1.927  6.635   -21.654 1.00 31.58  ? 244 LEU B CD1 1 
ATOM   8547  C CD2 . LEU C 1 215 ? -2.451  7.808   -19.550 1.00 36.04  ? 244 LEU B CD2 1 
ATOM   8548  N N   . GLY C 1 216 ? -0.964  3.071   -17.202 1.00 44.37  ? 245 GLY B N   1 
ATOM   8549  C CA  . GLY C 1 216 ? -1.369  1.778   -16.664 1.00 44.99  ? 245 GLY B CA  1 
ATOM   8550  C C   . GLY C 1 216 ? -1.630  0.729   -17.752 1.00 47.92  ? 245 GLY B C   1 
ATOM   8551  O O   . GLY C 1 216 ? -2.161  -0.334  -17.447 1.00 52.39  ? 245 GLY B O   1 
ATOM   8552  N N   . TYR C 1 217 ? -1.248  1.015   -19.011 1.00 42.09  ? 246 TYR B N   1 
ATOM   8553  C CA  . TYR C 1 217 ? -1.444  0.102   -20.129 1.00 38.57  ? 246 TYR B CA  1 
ATOM   8554  C C   . TYR C 1 217 ? -0.148  -0.673  -20.324 1.00 42.96  ? 246 TYR B C   1 
ATOM   8555  O O   . TYR C 1 217 ? 0.929   -0.148  -20.064 1.00 53.94  ? 246 TYR B O   1 
ATOM   8556  C CB  . TYR C 1 217 ? -1.817  0.894   -21.393 1.00 37.74  ? 246 TYR B CB  1 
ATOM   8557  C CG  . TYR C 1 217 ? -3.217  1.476   -21.309 1.00 36.14  ? 246 TYR B CG  1 
ATOM   8558  C CD1 . TYR C 1 217 ? -3.532  2.487   -20.420 1.00 35.65  ? 246 TYR B CD1 1 
ATOM   8559  C CD2 . TYR C 1 217 ? -4.242  0.954   -22.083 1.00 38.88  ? 246 TYR B CD2 1 
ATOM   8560  C CE1 . TYR C 1 217 ? -4.827  2.960   -20.292 1.00 35.39  ? 246 TYR B CE1 1 
ATOM   8561  C CE2 . TYR C 1 217 ? -5.533  1.443   -22.006 1.00 37.81  ? 246 TYR B CE2 1 
ATOM   8562  C CZ  . TYR C 1 217 ? -5.828  2.441   -21.099 1.00 36.65  ? 246 TYR B CZ  1 
ATOM   8563  O OH  . TYR C 1 217 ? -7.117  2.840   -21.005 1.00 31.37  ? 246 TYR B OH  1 
ATOM   8564  N N   . THR C 1 218 ? -0.217  -1.918  -20.786 1.00 36.41  ? 247 THR B N   1 
ATOM   8565  C CA  . THR C 1 218 ? 1.013   -2.673  -20.988 1.00 41.93  ? 247 THR B CA  1 
ATOM   8566  C C   . THR C 1 218 ? 1.031   -3.422  -22.315 1.00 38.84  ? 247 THR B C   1 
ATOM   8567  O O   . THR C 1 218 ? 2.030   -4.032  -22.649 1.00 44.70  ? 247 THR B O   1 
ATOM   8568  C CB  . THR C 1 218 ? 1.172   -3.659  -19.830 1.00 46.29  ? 247 THR B CB  1 
ATOM   8569  O OG1 . THR C 1 218 ? -0.163  -4.156  -19.721 1.00 41.51  ? 247 THR B OG1 1 
ATOM   8570  C CG2 . THR C 1 218 ? 1.659   -2.995  -18.555 1.00 47.59  ? 247 THR B CG2 1 
ATOM   8571  N N   . ASP C 1 219 ? -0.086  -3.449  -23.030 1.00 45.20  ? 248 ASP B N   1 
ATOM   8572  C CA  . ASP C 1 219 ? -0.144  -4.084  -24.334 1.00 44.68  ? 248 ASP B CA  1 
ATOM   8573  C C   . ASP C 1 219 ? 0.872   -3.380  -25.227 1.00 43.02  ? 248 ASP B C   1 
ATOM   8574  O O   . ASP C 1 219 ? 0.767   -2.181  -25.414 1.00 41.51  ? 248 ASP B O   1 
ATOM   8575  C CB  . ASP C 1 219 ? -1.587  -4.003  -24.821 1.00 48.10  ? 248 ASP B CB  1 
ATOM   8576  C CG  . ASP C 1 219 ? -1.943  -4.674  -26.141 1.00 50.69  ? 248 ASP B CG  1 
ATOM   8577  O OD1 . ASP C 1 219 ? -1.034  -4.816  -26.991 1.00 48.00  ? 248 ASP B OD1 1 
ATOM   8578  O OD2 . ASP C 1 219 ? -3.137  -5.067  -26.296 1.00 49.24  ? 248 ASP B OD2 1 
ATOM   8579  N N   . HIS C 1 220 ? 1.859   -4.106  -25.767 1.00 43.92  ? 249 HIS B N   1 
ATOM   8580  C CA  . HIS C 1 220 ? 2.817   -3.536  -26.707 1.00 42.84  ? 249 HIS B CA  1 
ATOM   8581  C C   . HIS C 1 220 ? 2.091   -2.810  -27.841 1.00 38.44  ? 249 HIS B C   1 
ATOM   8582  O O   . HIS C 1 220 ? 2.589   -1.817  -28.360 1.00 40.78  ? 249 HIS B O   1 
ATOM   8583  C CB  . HIS C 1 220 ? 3.751   -4.623  -27.268 1.00 48.12  ? 249 HIS B CB  1 
ATOM   8584  C CG  . HIS C 1 220 ? 4.566   -4.277  -28.503 1.00 55.35  ? 249 HIS B CG  1 
ATOM   8585  N ND1 . HIS C 1 220 ? 5.754   -3.565  -28.479 1.00 54.62  ? 249 HIS B ND1 1 
ATOM   8586  C CD2 . HIS C 1 220 ? 4.364   -4.601  -29.813 1.00 52.45  ? 249 HIS B CD2 1 
ATOM   8587  C CE1 . HIS C 1 220 ? 6.232   -3.447  -29.721 1.00 52.05  ? 249 HIS B CE1 1 
ATOM   8588  N NE2 . HIS C 1 220 ? 5.403   -4.067  -30.550 1.00 54.63  ? 249 HIS B NE2 1 
ATOM   8589  N N   . GLN C 1 221 ? 0.931   -3.319  -28.260 1.00 34.75  ? 250 GLN B N   1 
ATOM   8590  C CA  . GLN C 1 221 ? 0.271   -2.782  -29.437 1.00 38.50  ? 250 GLN B CA  1 
ATOM   8591  C C   . GLN C 1 221 ? -0.316  -1.402  -29.138 1.00 37.44  ? 250 GLN B C   1 
ATOM   8592  O O   . GLN C 1 221 ? -0.310  -0.543  -30.006 1.00 35.59  ? 250 GLN B O   1 
ATOM   8593  C CB  . GLN C 1 221 ? -0.799  -3.722  -29.984 1.00 44.37  ? 250 GLN B CB  1 
ATOM   8594  C CG  . GLN C 1 221 ? -0.743  -3.838  -31.503 1.00 53.65  ? 250 GLN B CG  1 
ATOM   8595  C CD  . GLN C 1 221 ? 0.653   -4.112  -32.016 1.00 55.25  ? 250 GLN B CD  1 
ATOM   8596  O OE1 . GLN C 1 221 ? 1.252   -3.314  -32.752 1.00 51.81  ? 250 GLN B OE1 1 
ATOM   8597  N NE2 . GLN C 1 221 ? 1.198   -5.241  -31.591 1.00 55.65  ? 250 GLN B NE2 1 
ATOM   8598  N N   . PHE C 1 222 ? -0.768  -1.180  -27.904 1.00 34.73  ? 251 PHE B N   1 
ATOM   8599  C CA  . PHE C 1 222 ? -1.223  0.132   -27.486 1.00 35.08  ? 251 PHE B CA  1 
ATOM   8600  C C   . PHE C 1 222 ? -0.054  1.125   -27.487 1.00 33.90  ? 251 PHE B C   1 
ATOM   8601  O O   . PHE C 1 222 ? -0.229  2.280   -27.874 1.00 33.62  ? 251 PHE B O   1 
ATOM   8602  C CB  . PHE C 1 222 ? -1.942  0.065   -26.140 1.00 31.56  ? 251 PHE B CB  1 
ATOM   8603  C CG  . PHE C 1 222 ? -2.481  1.427   -25.755 1.00 31.73  ? 251 PHE B CG  1 
ATOM   8604  C CD1 . PHE C 1 222 ? -3.502  2.012   -26.491 1.00 31.39  ? 251 PHE B CD1 1 
ATOM   8605  C CD2 . PHE C 1 222 ? -1.932  2.141   -24.696 1.00 34.17  ? 251 PHE B CD2 1 
ATOM   8606  C CE1 . PHE C 1 222 ? -3.983  3.259   -26.155 1.00 34.47  ? 251 PHE B CE1 1 
ATOM   8607  C CE2 . PHE C 1 222 ? -2.412  3.395   -24.375 1.00 33.38  ? 251 PHE B CE2 1 
ATOM   8608  C CZ  . PHE C 1 222 ? -3.441  3.946   -25.091 1.00 35.89  ? 251 PHE B CZ  1 
ATOM   8609  N N   . THR C 1 223 ? 1.143   0.707   -27.074 1.00 32.70  ? 252 THR B N   1 
ATOM   8610  C CA  . THR C 1 223 ? 2.307   1.579   -27.161 1.00 30.96  ? 252 THR B CA  1 
ATOM   8611  C C   . THR C 1 223 ? 2.600   1.960   -28.614 1.00 33.43  ? 252 THR B C   1 
ATOM   8612  O O   . THR C 1 223 ? 2.885   3.120   -28.910 1.00 27.38  ? 252 THR B O   1 
ATOM   8613  C CB  . THR C 1 223 ? 3.517   0.927   -26.507 1.00 33.49  ? 252 THR B CB  1 
ATOM   8614  O OG1 . THR C 1 223 ? 3.066   0.670   -25.181 1.00 35.86  ? 252 THR B OG1 1 
ATOM   8615  C CG2 . THR C 1 223 ? 4.691   1.887   -26.488 1.00 32.42  ? 252 THR B CG2 1 
ATOM   8616  N N   . GLU C 1 224 ? 2.532   0.965   -29.500 1.00 32.06  ? 253 GLU B N   1 
ATOM   8617  C CA  . GLU C 1 224 ? 2.750   1.175   -30.911 1.00 31.09  ? 253 GLU B CA  1 
ATOM   8618  C C   . GLU C 1 224 ? 1.703   2.120   -31.482 1.00 32.13  ? 253 GLU B C   1 
ATOM   8619  O O   . GLU C 1 224 ? 2.064   2.993   -32.279 1.00 32.62  ? 253 GLU B O   1 
ATOM   8620  C CB  . GLU C 1 224 ? 2.802   -0.173  -31.611 1.00 29.73  ? 253 GLU B CB  1 
ATOM   8621  C CG  . GLU C 1 224 ? 4.107   -0.901  -31.318 1.00 31.86  ? 253 GLU B CG  1 
ATOM   8622  C CD  . GLU C 1 224 ? 5.221   -0.287  -32.152 1.00 38.36  ? 253 GLU B CD  1 
ATOM   8623  O OE1 . GLU C 1 224 ? 5.156   -0.358  -33.414 1.00 38.57  ? 253 GLU B OE1 1 
ATOM   8624  O OE2 . GLU C 1 224 ? 6.160   0.281   -31.520 1.00 37.36  ? 253 GLU B OE2 1 
ATOM   8625  N N   . LEU C 1 225 ? 0.449   1.999   -31.014 1.00 31.75  ? 254 LEU B N   1 
ATOM   8626  C CA  . LEU C 1 225 ? -0.606  2.923   -31.393 1.00 29.82  ? 254 LEU B CA  1 
ATOM   8627  C C   . LEU C 1 225 ? -0.238  4.339   -30.944 1.00 29.93  ? 254 LEU B C   1 
ATOM   8628  O O   . LEU C 1 225 ? -0.350  5.297   -31.733 1.00 31.57  ? 254 LEU B O   1 
ATOM   8629  C CB  . LEU C 1 225 ? -1.994  2.546   -30.875 1.00 32.89  ? 254 LEU B CB  1 
ATOM   8630  C CG  . LEU C 1 225 ? -3.130  3.544   -31.179 1.00 33.44  ? 254 LEU B CG  1 
ATOM   8631  C CD1 . LEU C 1 225 ? -3.332  3.817   -32.673 1.00 35.16  ? 254 LEU B CD1 1 
ATOM   8632  C CD2 . LEU C 1 225 ? -4.466  3.121   -30.617 1.00 35.34  ? 254 LEU B CD2 1 
ATOM   8633  N N   . THR C 1 226 ? 0.115   4.465   -29.664 1.00 25.36  ? 255 THR B N   1 
ATOM   8634  C CA  . THR C 1 226 ? 0.475   5.734   -29.058 1.00 29.34  ? 255 THR B CA  1 
ATOM   8635  C C   . THR C 1 226 ? 1.626   6.392   -29.841 1.00 32.75  ? 255 THR B C   1 
ATOM   8636  O O   . THR C 1 226 ? 1.528   7.550   -30.251 1.00 29.89  ? 255 THR B O   1 
ATOM   8637  C CB  . THR C 1 226 ? 0.776   5.517   -27.577 1.00 30.71  ? 255 THR B CB  1 
ATOM   8638  O OG1 . THR C 1 226 ? -0.430  5.074   -26.940 1.00 29.00  ? 255 THR B OG1 1 
ATOM   8639  C CG2 . THR C 1 226 ? 1.268   6.782   -26.901 1.00 29.78  ? 255 THR B CG2 1 
ATOM   8640  N N   . ARG C 1 227 ? 2.691   5.647   -30.146 1.00 29.98  ? 256 ARG B N   1 
ATOM   8641  C CA  . ARG C 1 227 ? 3.786   6.230   -30.905 1.00 28.51  ? 256 ARG B CA  1 
ATOM   8642  C C   . ARG C 1 227 ? 3.268   6.811   -32.210 1.00 29.68  ? 256 ARG B C   1 
ATOM   8643  O O   . ARG C 1 227 ? 3.639   7.911   -32.607 1.00 32.03  ? 256 ARG B O   1 
ATOM   8644  C CB  . ARG C 1 227 ? 4.919   5.249   -31.197 1.00 29.34  ? 256 ARG B CB  1 
ATOM   8645  C CG  . ARG C 1 227 ? 5.592   4.722   -29.950 1.00 29.19  ? 256 ARG B CG  1 
ATOM   8646  C CD  . ARG C 1 227 ? 6.204   3.349   -30.196 1.00 29.42  ? 256 ARG B CD  1 
ATOM   8647  N NE  . ARG C 1 227 ? 7.194   3.095   -29.160 1.00 33.46  ? 256 ARG B NE  1 
ATOM   8648  C CZ  . ARG C 1 227 ? 7.380   1.923   -28.555 1.00 34.40  ? 256 ARG B CZ  1 
ATOM   8649  N NH1 . ARG C 1 227 ? 6.900   0.796   -29.043 1.00 37.83  ? 256 ARG B NH1 1 
ATOM   8650  N NH2 . ARG C 1 227 ? 8.120   1.881   -27.488 1.00 30.58  ? 256 ARG B NH2 1 
ATOM   8651  N N   . LEU C 1 228 ? 2.407   6.060   -32.899 1.00 32.89  ? 257 LEU B N   1 
ATOM   8652  C CA  . LEU C 1 228 ? 1.888   6.493   -34.187 1.00 30.78  ? 257 LEU B CA  1 
ATOM   8653  C C   . LEU C 1 228 ? 0.991   7.719   -34.026 1.00 29.14  ? 257 LEU B C   1 
ATOM   8654  O O   . LEU C 1 228 ? 1.074   8.651   -34.811 1.00 32.08  ? 257 LEU B O   1 
ATOM   8655  C CB  . LEU C 1 228 ? 1.108   5.348   -34.829 1.00 35.64  ? 257 LEU B CB  1 
ATOM   8656  C CG  . LEU C 1 228 ? 0.381   5.705   -36.126 1.00 33.03  ? 257 LEU B CG  1 
ATOM   8657  C CD1 . LEU C 1 228 ? 1.414   6.131   -37.191 1.00 32.09  ? 257 LEU B CD1 1 
ATOM   8658  C CD2 . LEU C 1 228 ? -0.523  4.610   -36.666 1.00 38.75  ? 257 LEU B CD2 1 
ATOM   8659  N N   . TYR C 1 229 ? 0.111   7.684   -33.029 1.00 27.26  ? 258 TYR B N   1 
ATOM   8660  C CA  . TYR C 1 229 ? -0.879  8.716   -32.779 1.00 27.51  ? 258 TYR B CA  1 
ATOM   8661  C C   . TYR C 1 229 ? -0.180  10.016  -32.414 1.00 29.29  ? 258 TYR B C   1 
ATOM   8662  O O   . TYR C 1 229 ? -0.519  11.063  -32.986 1.00 25.09  ? 258 TYR B O   1 
ATOM   8663  C CB  . TYR C 1 229 ? -1.832  8.272   -31.665 1.00 27.10  ? 258 TYR B CB  1 
ATOM   8664  C CG  . TYR C 1 229 ? -2.900  9.274   -31.297 1.00 31.67  ? 258 TYR B CG  1 
ATOM   8665  C CD1 . TYR C 1 229 ? -2.544  10.363  -30.529 1.00 33.70  ? 258 TYR B CD1 1 
ATOM   8666  C CD2 . TYR C 1 229 ? -4.233  9.134   -31.678 1.00 36.74  ? 258 TYR B CD2 1 
ATOM   8667  C CE1 . TYR C 1 229 ? -3.470  11.302  -30.147 1.00 33.39  ? 258 TYR B CE1 1 
ATOM   8668  C CE2 . TYR C 1 229 ? -5.183  10.066  -31.274 1.00 40.02  ? 258 TYR B CE2 1 
ATOM   8669  C CZ  . TYR C 1 229 ? -4.783  11.177  -30.548 1.00 35.41  ? 258 TYR B CZ  1 
ATOM   8670  O OH  . TYR C 1 229 ? -5.585  12.195  -30.080 1.00 43.68  ? 258 TYR B OH  1 
ATOM   8671  N N   . LEU C 1 230 ? 0.835   9.916   -31.533 1.00 29.22  ? 259 LEU B N   1 
ATOM   8672  C CA  . LEU C 1 230 ? 1.606   11.078  -31.125 1.00 26.63  ? 259 LEU B CA  1 
ATOM   8673  C C   . LEU C 1 230 ? 2.445   11.647  -32.269 1.00 28.39  ? 259 LEU B C   1 
ATOM   8674  O O   . LEU C 1 230 ? 2.642   12.843  -32.302 1.00 28.39  ? 259 LEU B O   1 
ATOM   8675  C CB  . LEU C 1 230 ? 2.450   10.806  -29.891 1.00 26.02  ? 259 LEU B CB  1 
ATOM   8676  C CG  . LEU C 1 230 ? 1.638   10.449  -28.655 1.00 28.78  ? 259 LEU B CG  1 
ATOM   8677  C CD1 . LEU C 1 230 ? 2.529   9.944   -27.576 1.00 28.53  ? 259 LEU B CD1 1 
ATOM   8678  C CD2 . LEU C 1 230 ? 0.813   11.627  -28.161 1.00 30.56  ? 259 LEU B CD2 1 
ATOM   8679  N N   . THR C 1 231 ? 2.898   10.843  -33.238 1.00 27.29  ? 260 THR B N   1 
ATOM   8680  C CA  . THR C 1 231 ? 3.611   11.394  -34.382 1.00 25.58  ? 260 THR B CA  1 
ATOM   8681  C C   . THR C 1 231 ? 2.668   12.178  -35.305 1.00 23.68  ? 260 THR B C   1 
ATOM   8682  O O   . THR C 1 231 ? 2.982   13.290  -35.721 1.00 28.54  ? 260 THR B O   1 
ATOM   8683  C CB  . THR C 1 231 ? 4.304   10.236  -35.118 1.00 28.68  ? 260 THR B CB  1 
ATOM   8684  O OG1 . THR C 1 231 ? 5.276   9.661   -34.241 1.00 28.51  ? 260 THR B OG1 1 
ATOM   8685  C CG2 . THR C 1 231 ? 4.996   10.689  -36.387 1.00 27.40  ? 260 THR B CG2 1 
ATOM   8686  N N   . ILE C 1 232 ? 1.515   11.612  -35.672 1.00 28.63  ? 261 ILE B N   1 
ATOM   8687  C CA  . ILE C 1 232 ? 0.687   12.148  -36.755 1.00 30.86  ? 261 ILE B CA  1 
ATOM   8688  C C   . ILE C 1 232 ? -0.192  13.323  -36.315 1.00 30.93  ? 261 ILE B C   1 
ATOM   8689  O O   . ILE C 1 232 ? -0.674  14.098  -37.158 1.00 26.20  ? 261 ILE B O   1 
ATOM   8690  C CB  . ILE C 1 232 ? -0.187  11.077  -37.446 1.00 32.97  ? 261 ILE B CB  1 
ATOM   8691  C CG1 . ILE C 1 232 ? -1.234  10.439  -36.514 1.00 34.21  ? 261 ILE B CG1 1 
ATOM   8692  C CG2 . ILE C 1 232 ? 0.695   10.022  -38.146 1.00 33.95  ? 261 ILE B CG2 1 
ATOM   8693  C CD1 . ILE C 1 232 ? -2.233  9.548   -37.251 1.00 36.94  ? 261 ILE B CD1 1 
ATOM   8694  N N   . HIS C 1 233 ? -0.453  13.420  -35.017 1.00 28.60  ? 262 HIS B N   1 
ATOM   8695  C CA  . HIS C 1 233 ? -1.233  14.537  -34.505 1.00 31.92  ? 262 HIS B CA  1 
ATOM   8696  C C   . HIS C 1 233 ? -0.343  15.722  -34.134 1.00 28.57  ? 262 HIS B C   1 
ATOM   8697  O O   . HIS C 1 233 ? -0.838  16.745  -33.643 1.00 25.63  ? 262 HIS B O   1 
ATOM   8698  C CB  . HIS C 1 233 ? -2.052  14.086  -33.299 1.00 34.16  ? 262 HIS B CB  1 
ATOM   8699  C CG  . HIS C 1 233 ? -3.276  13.331  -33.636 1.00 35.78  ? 262 HIS B CG  1 
ATOM   8700  N ND1 . HIS C 1 233 ? -3.273  11.989  -33.931 1.00 42.02  ? 262 HIS B ND1 1 
ATOM   8701  C CD2 . HIS C 1 233 ? -4.561  13.732  -33.668 1.00 45.70  ? 262 HIS B CD2 1 
ATOM   8702  C CE1 . HIS C 1 233 ? -4.510  11.597  -34.166 1.00 47.40  ? 262 HIS B CE1 1 
ATOM   8703  N NE2 . HIS C 1 233 ? -5.314  12.635  -33.990 1.00 52.29  ? 262 HIS B NE2 1 
ATOM   8704  N N   . SER C 1 234 ? 0.956   15.611  -34.414 1.00 24.43  ? 263 SER B N   1 
ATOM   8705  C CA  . SER C 1 234 ? 1.922   16.509  -33.815 1.00 28.38  ? 263 SER B CA  1 
ATOM   8706  C C   . SER C 1 234 ? 1.807   17.926  -34.379 1.00 25.09  ? 263 SER B C   1 
ATOM   8707  O O   . SER C 1 234 ? 2.074   18.864  -33.665 1.00 29.73  ? 263 SER B O   1 
ATOM   8708  C CB  . SER C 1 234 ? 3.308   15.993  -34.034 1.00 29.55  ? 263 SER B CB  1 
ATOM   8709  O OG  . SER C 1 234 ? 3.508   16.039  -35.437 1.00 26.14  ? 263 SER B OG  1 
ATOM   8710  N N   . ASP C 1 235 ? 1.472   18.099  -35.661 1.00 28.40  ? 264 ASP B N   1 
ATOM   8711  C CA  . ASP C 1 235 ? 1.493   19.425  -36.274 1.00 29.35  ? 264 ASP B CA  1 
ATOM   8712  C C   . ASP C 1 235 ? 0.564   19.439  -37.474 1.00 29.30  ? 264 ASP B C   1 
ATOM   8713  O O   . ASP C 1 235 ? 0.379   18.409  -38.116 1.00 29.09  ? 264 ASP B O   1 
ATOM   8714  C CB  . ASP C 1 235 ? 2.880   19.801  -36.804 1.00 34.74  ? 264 ASP B CB  1 
ATOM   8715  C CG  . ASP C 1 235 ? 3.244   21.283  -36.839 1.00 40.41  ? 264 ASP B CG  1 
ATOM   8716  O OD1 . ASP C 1 235 ? 2.911   22.004  -35.854 1.00 33.77  ? 264 ASP B OD1 1 
ATOM   8717  O OD2 . ASP C 1 235 ? 3.920   21.713  -37.825 1.00 46.38  ? 264 ASP B OD2 1 
ATOM   8718  N N   . HIS C 1 236 ? 0.010   20.604  -37.804 1.00 27.35  ? 265 HIS B N   1 
ATOM   8719  C CA  . HIS C 1 236 ? -0.879  20.679  -38.942 1.00 25.43  ? 265 HIS B CA  1 
ATOM   8720  C C   . HIS C 1 236 ? -0.916  22.082  -39.520 1.00 25.55  ? 265 HIS B C   1 
ATOM   8721  O O   . HIS C 1 236 ? -1.995  22.650  -39.642 1.00 26.92  ? 265 HIS B O   1 
ATOM   8722  C CB  . HIS C 1 236 ? -2.269  20.187  -38.568 1.00 25.19  ? 265 HIS B CB  1 
ATOM   8723  C CG  . HIS C 1 236 ? -2.987  19.533  -39.704 1.00 30.70  ? 265 HIS B CG  1 
ATOM   8724  N ND1 . HIS C 1 236 ? -2.575  18.322  -40.234 1.00 36.96  ? 265 HIS B ND1 1 
ATOM   8725  C CD2 . HIS C 1 236 ? -4.053  19.900  -40.415 1.00 30.13  ? 265 HIS B CD2 1 
ATOM   8726  C CE1 . HIS C 1 236 ? -3.388  17.990  -41.235 1.00 36.32  ? 265 HIS B CE1 1 
ATOM   8727  N NE2 . HIS C 1 236 ? -4.292  18.935  -41.365 1.00 39.33  ? 265 HIS B NE2 1 
ATOM   8728  N N   . GLU C 1 237 ? 0.264   22.634  -39.817 1.00 27.05  ? 266 GLU B N   1 
ATOM   8729  C CA  . GLU C 1 237 ? 0.372   24.000  -40.307 1.00 33.42  ? 266 GLU B CA  1 
ATOM   8730  C C   . GLU C 1 237 ? 0.156   24.967  -39.138 1.00 30.74  ? 266 GLU B C   1 
ATOM   8731  O O   . GLU C 1 237 ? -0.064  24.553  -38.008 1.00 26.60  ? 266 GLU B O   1 
ATOM   8732  C CB  . GLU C 1 237 ? -0.665  24.344  -41.369 1.00 33.13  ? 266 GLU B CB  1 
ATOM   8733  C CG  . GLU C 1 237 ? -0.030  24.427  -42.734 1.00 44.81  ? 266 GLU B CG  1 
ATOM   8734  C CD  . GLU C 1 237 ? -0.934  25.146  -43.719 1.00 46.95  ? 266 GLU B CD  1 
ATOM   8735  O OE1 . GLU C 1 237 ? -1.974  25.785  -43.353 1.00 42.68  ? 266 GLU B OE1 1 
ATOM   8736  O OE2 . GLU C 1 237 ? -0.492  25.073  -44.883 1.00 48.40  ? 266 GLU B OE2 1 
ATOM   8737  N N   . GLY C 1 238 ? 0.159   26.261  -39.445 1.00 22.71  ? 267 GLY B N   1 
ATOM   8738  C CA  . GLY C 1 238 ? 0.186   27.289  -38.427 1.00 21.52  ? 267 GLY B CA  1 
ATOM   8739  C C   . GLY C 1 238 ? -1.191  27.835  -38.152 1.00 22.61  ? 267 GLY B C   1 
ATOM   8740  O O   . GLY C 1 238 ? -1.343  28.485  -37.132 1.00 24.28  ? 267 GLY B O   1 
ATOM   8741  N N   . GLY C 1 239 ? -2.157  27.524  -39.057 1.00 26.07  ? 268 GLY B N   1 
ATOM   8742  C CA  . GLY C 1 239 ? -3.451  28.168  -39.116 1.00 24.41  ? 268 GLY B CA  1 
ATOM   8743  C C   . GLY C 1 239 ? -4.541  27.456  -38.306 1.00 24.44  ? 268 GLY B C   1 
ATOM   8744  O O   . GLY C 1 239 ? -5.562  28.053  -37.997 1.00 22.23  ? 268 GLY B O   1 
ATOM   8745  N N   . ASN C 1 240 ? -4.323  26.212  -37.900 1.00 24.14  ? 269 ASN B N   1 
ATOM   8746  C CA  . ASN C 1 240 ? -5.273  25.566  -37.004 1.00 24.06  ? 269 ASN B CA  1 
ATOM   8747  C C   . ASN C 1 240 ? -5.234  26.303  -35.672 1.00 24.52  ? 269 ASN B C   1 
ATOM   8748  O O   . ASN C 1 240 ? -4.227  26.932  -35.329 1.00 23.27  ? 269 ASN B O   1 
ATOM   8749  C CB  . ASN C 1 240 ? -4.976  24.085  -36.758 1.00 23.95  ? 269 ASN B CB  1 
ATOM   8750  C CG  . ASN C 1 240 ? -3.729  23.836  -35.951 1.00 25.68  ? 269 ASN B CG  1 
ATOM   8751  O OD1 . ASN C 1 240 ? -3.720  23.981  -34.717 1.00 25.68  ? 269 ASN B OD1 1 
ATOM   8752  N ND2 . ASN C 1 240 ? -2.690  23.329  -36.608 1.00 26.64  ? 269 ASN B ND2 1 
ATOM   8753  N N   . VAL C 1 241 ? -6.313  26.172  -34.911 1.00 26.19  ? 270 VAL B N   1 
ATOM   8754  C CA  . VAL C 1 241 ? -6.538  27.032  -33.757 1.00 27.28  ? 270 VAL B CA  1 
ATOM   8755  C C   . VAL C 1 241 ? -5.495  26.824  -32.664 1.00 23.43  ? 270 VAL B C   1 
ATOM   8756  O O   . VAL C 1 241 ? -5.054  27.805  -32.039 1.00 23.58  ? 270 VAL B O   1 
ATOM   8757  C CB  . VAL C 1 241 ? -7.971  26.859  -33.232 1.00 28.21  ? 270 VAL B CB  1 
ATOM   8758  C CG1 . VAL C 1 241 ? -8.136  27.479  -31.845 1.00 26.38  ? 270 VAL B CG1 1 
ATOM   8759  C CG2 . VAL C 1 241 ? -8.934  27.538  -34.198 1.00 36.68  ? 270 VAL B CG2 1 
ATOM   8760  N N   . SER C 1 242 ? -5.048  25.582  -32.468 1.00 23.27  ? 271 SER B N   1 
ATOM   8761  C CA  . SER C 1 242 ? -4.123  25.300  -31.377 1.00 27.58  ? 271 SER B CA  1 
ATOM   8762  C C   . SER C 1 242 ? -2.742  25.875  -31.707 1.00 24.10  ? 271 SER B C   1 
ATOM   8763  O O   . SER C 1 242 ? -2.166  26.564  -30.883 1.00 20.25  ? 271 SER B O   1 
ATOM   8764  C CB  . SER C 1 242 ? -4.043  23.829  -30.977 1.00 24.81  ? 271 SER B CB  1 
ATOM   8765  O OG  . SER C 1 242 ? -3.889  22.966  -32.098 1.00 28.26  ? 271 SER B OG  1 
ATOM   8766  N N   . ALA C 1 243 ? -2.240  25.611  -32.908 1.00 22.21  ? 272 ALA B N   1 
ATOM   8767  C CA  . ALA C 1 243 ? -0.955  26.146  -33.337 1.00 25.02  ? 272 ALA B CA  1 
ATOM   8768  C C   . ALA C 1 243 ? -0.991  27.659  -33.459 1.00 20.49  ? 272 ALA B C   1 
ATOM   8769  O O   . ALA C 1 243 ? -0.044  28.359  -33.091 1.00 23.73  ? 272 ALA B O   1 
ATOM   8770  C CB  . ALA C 1 243 ? -0.514  25.549  -34.659 1.00 23.74  ? 272 ALA B CB  1 
ATOM   8771  N N   . HIS C 1 244 ? -2.074  28.179  -33.975 1.00 22.87  ? 273 HIS B N   1 
ATOM   8772  C CA  . HIS C 1 244 ? -2.175  29.626  -34.157 1.00 22.03  ? 273 HIS B CA  1 
ATOM   8773  C C   . HIS C 1 244 ? -2.227  30.321  -32.801 1.00 23.41  ? 273 HIS B C   1 
ATOM   8774  O O   . HIS C 1 244 ? -1.583  31.339  -32.605 1.00 22.02  ? 273 HIS B O   1 
ATOM   8775  C CB  . HIS C 1 244 ? -3.420  29.973  -34.964 1.00 21.95  ? 273 HIS B CB  1 
ATOM   8776  C CG  . HIS C 1 244 ? -3.557  31.402  -35.337 1.00 23.51  ? 273 HIS B CG  1 
ATOM   8777  N ND1 . HIS C 1 244 ? -4.697  31.914  -35.911 1.00 25.55  ? 273 HIS B ND1 1 
ATOM   8778  C CD2 . HIS C 1 244 ? -2.693  32.422  -35.255 1.00 27.60  ? 273 HIS B CD2 1 
ATOM   8779  C CE1 . HIS C 1 244 ? -4.527  33.207  -36.112 1.00 28.37  ? 273 HIS B CE1 1 
ATOM   8780  N NE2 . HIS C 1 244 ? -3.318  33.541  -35.746 1.00 27.49  ? 273 HIS B NE2 1 
ATOM   8781  N N   . THR C 1 245 ? -2.973  29.746  -31.851 1.00 23.20  ? 274 THR B N   1 
ATOM   8782  C CA  . THR C 1 245 ? -3.040  30.282  -30.503 1.00 22.16  ? 274 THR B CA  1 
ATOM   8783  C C   . THR C 1 245 ? -1.648  30.281  -29.883 1.00 21.53  ? 274 THR B C   1 
ATOM   8784  O O   . THR C 1 245 ? -1.260  31.230  -29.217 1.00 26.30  ? 274 THR B O   1 
ATOM   8785  C CB  . THR C 1 245 ? -4.012  29.469  -29.634 1.00 22.40  ? 274 THR B CB  1 
ATOM   8786  O OG1 . THR C 1 245 ? -5.314  29.747  -30.151 1.00 21.31  ? 274 THR B OG1 1 
ATOM   8787  C CG2 . THR C 1 245 ? -4.042  29.949  -28.203 1.00 24.33  ? 274 THR B CG2 1 
ATOM   8788  N N   . SER C 1 246 ? -0.899  29.196  -30.006 1.00 23.67  ? 275 SER B N   1 
ATOM   8789  C CA  . SER C 1 246 ? 0.410   29.123  -29.366 1.00 24.03  ? 275 SER B CA  1 
ATOM   8790  C C   . SER C 1 246 ? 1.388   30.116  -29.993 1.00 23.22  ? 275 SER B C   1 
ATOM   8791  O O   . SER C 1 246 ? 2.241   30.675  -29.300 1.00 26.09  ? 275 SER B O   1 
ATOM   8792  C CB  . SER C 1 246 ? 0.964   27.723  -29.384 1.00 27.13  ? 275 SER B CB  1 
ATOM   8793  O OG  . SER C 1 246 ? 1.599   27.452  -30.616 1.00 31.91  ? 275 SER B OG  1 
ATOM   8794  N N   . HIS C 1 247 ? 1.280   30.321  -31.308 1.00 22.19  ? 276 HIS B N   1 
ATOM   8795  C CA  . HIS C 1 247 ? 2.074   31.295  -32.031 1.00 21.29  ? 276 HIS B CA  1 
ATOM   8796  C C   . HIS C 1 247 ? 1.709   32.722  -31.575 1.00 24.97  ? 276 HIS B C   1 
ATOM   8797  O O   . HIS C 1 247 ? 2.540   33.573  -31.281 1.00 24.07  ? 276 HIS B O   1 
ATOM   8798  C CB  . HIS C 1 247 ? 1.715   31.127  -33.498 1.00 27.94  ? 276 HIS B CB  1 
ATOM   8799  C CG  . HIS C 1 247 ? 2.496   31.945  -34.474 1.00 33.18  ? 276 HIS B CG  1 
ATOM   8800  N ND1 . HIS C 1 247 ? 3.790   31.611  -34.800 1.00 29.04  ? 276 HIS B ND1 1 
ATOM   8801  C CD2 . HIS C 1 247 ? 2.185   33.036  -35.194 1.00 31.79  ? 276 HIS B CD2 1 
ATOM   8802  C CE1 . HIS C 1 247 ? 4.262   32.505  -35.676 1.00 33.08  ? 276 HIS B CE1 1 
ATOM   8803  N NE2 . HIS C 1 247 ? 3.300   33.373  -35.940 1.00 32.03  ? 276 HIS B NE2 1 
ATOM   8804  N N   . LEU C 1 248 ? 0.418   32.992  -31.489 1.00 26.48  ? 277 LEU B N   1 
ATOM   8805  C CA  . LEU C 1 248 ? -0.077  34.293  -31.051 1.00 23.91  ? 277 LEU B CA  1 
ATOM   8806  C C   . LEU C 1 248 ? 0.434   34.610  -29.643 1.00 22.40  ? 277 LEU B C   1 
ATOM   8807  O O   . LEU C 1 248 ? 1.052   35.645  -29.435 1.00 22.12  ? 277 LEU B O   1 
ATOM   8808  C CB  . LEU C 1 248 ? -1.591  34.215  -31.140 1.00 21.74  ? 277 LEU B CB  1 
ATOM   8809  C CG  . LEU C 1 248 ? -2.366  35.412  -30.602 1.00 26.59  ? 277 LEU B CG  1 
ATOM   8810  C CD1 . LEU C 1 248 ? -1.828  36.707  -31.211 1.00 32.08  ? 277 LEU B CD1 1 
ATOM   8811  C CD2 . LEU C 1 248 ? -3.837  35.236  -30.934 1.00 25.65  ? 277 LEU B CD2 1 
ATOM   8812  N N   . VAL C 1 249 ? 0.206   33.714  -28.680 1.00 23.90  ? 278 VAL B N   1 
ATOM   8813  C CA  . VAL C 1 249 ? 0.596   33.968  -27.306 1.00 22.22  ? 278 VAL B CA  1 
ATOM   8814  C C   . VAL C 1 249 ? 2.128   34.011  -27.184 1.00 24.45  ? 278 VAL B C   1 
ATOM   8815  O O   . VAL C 1 249 ? 2.705   34.856  -26.514 1.00 20.51  ? 278 VAL B O   1 
ATOM   8816  C CB  . VAL C 1 249 ? -0.077  32.938  -26.383 1.00 24.53  ? 278 VAL B CB  1 
ATOM   8817  C CG1 . VAL C 1 249 ? 0.453   33.001  -24.959 1.00 24.56  ? 278 VAL B CG1 1 
ATOM   8818  C CG2 . VAL C 1 249 ? -1.605  33.056  -26.390 1.00 25.10  ? 278 VAL B CG2 1 
ATOM   8819  N N   . GLY C 1 250 ? 2.847   33.150  -27.898 1.00 20.42  ? 279 GLY B N   1 
ATOM   8820  C CA  . GLY C 1 250 ? 4.285   33.195  -27.835 1.00 21.55  ? 279 GLY B CA  1 
ATOM   8821  C C   . GLY C 1 250 ? 4.904   34.420  -28.494 1.00 20.25  ? 279 GLY B C   1 
ATOM   8822  O O   . GLY C 1 250 ? 5.978   34.853  -28.065 1.00 27.03  ? 279 GLY B O   1 
ATOM   8823  N N   . SER C 1 251 ? 4.237   34.991  -29.498 1.00 23.02  ? 280 SER B N   1 
ATOM   8824  C CA  . SER C 1 251 ? 4.684   36.229  -30.116 1.00 24.77  ? 280 SER B CA  1 
ATOM   8825  C C   . SER C 1 251 ? 4.714   37.379  -29.099 1.00 25.22  ? 280 SER B C   1 
ATOM   8826  O O   . SER C 1 251 ? 5.363   38.390  -29.370 1.00 22.74  ? 280 SER B O   1 
ATOM   8827  C CB  . SER C 1 251 ? 3.815   36.617  -31.298 1.00 26.16  ? 280 SER B CB  1 
ATOM   8828  O OG  . SER C 1 251 ? 2.565   37.222  -30.950 1.00 23.25  ? 280 SER B OG  1 
ATOM   8829  N N   . ALA C 1 252 ? 3.979   37.255  -27.978 1.00 26.76  ? 281 ALA B N   1 
ATOM   8830  C CA  . ALA C 1 252 ? 4.028   38.269  -26.910 1.00 26.46  ? 281 ALA B CA  1 
ATOM   8831  C C   . ALA C 1 252 ? 5.159   37.961  -25.927 1.00 21.94  ? 281 ALA B C   1 
ATOM   8832  O O   . ALA C 1 252 ? 5.354   38.671  -24.946 1.00 24.78  ? 281 ALA B O   1 
ATOM   8833  C CB  . ALA C 1 252 ? 2.702   38.372  -26.180 1.00 28.30  ? 281 ALA B CB  1 
ATOM   8834  N N   . LEU C 1 253 ? 5.969   36.958  -26.257 1.00 20.26  ? 282 LEU B N   1 
ATOM   8835  C CA  . LEU C 1 253 ? 7.087   36.491  -25.472 1.00 23.00  ? 282 LEU B CA  1 
ATOM   8836  C C   . LEU C 1 253 ? 6.588   35.854  -24.183 1.00 24.95  ? 282 LEU B C   1 
ATOM   8837  O O   . LEU C 1 253 ? 7.375   35.635  -23.273 1.00 26.70  ? 282 LEU B O   1 
ATOM   8838  C CB  . LEU C 1 253 ? 8.196   37.495  -25.187 1.00 24.36  ? 282 LEU B CB  1 
ATOM   8839  C CG  . LEU C 1 253 ? 8.861   38.148  -26.402 1.00 27.13  ? 282 LEU B CG  1 
ATOM   8840  C CD1 . LEU C 1 253 ? 9.917   39.161  -25.969 1.00 24.90  ? 282 LEU B CD1 1 
ATOM   8841  C CD2 . LEU C 1 253 ? 9.479   37.059  -27.287 1.00 31.01  ? 282 LEU B CD2 1 
ATOM   8842  N N   . SER C 1 254 ? 5.336   35.422  -24.158 1.00 25.78  ? 283 SER B N   1 
ATOM   8843  C CA  . SER C 1 254 ? 4.957   34.450  -23.140 1.00 30.86  ? 283 SER B CA  1 
ATOM   8844  C C   . SER C 1 254 ? 5.798   33.183  -23.320 1.00 32.58  ? 283 SER B C   1 
ATOM   8845  O O   . SER C 1 254 ? 6.092   32.797  -24.460 1.00 31.68  ? 283 SER B O   1 
ATOM   8846  C CB  . SER C 1 254 ? 3.465   34.136  -23.203 1.00 28.36  ? 283 SER B CB  1 
ATOM   8847  O OG  . SER C 1 254 ? 2.689   35.319  -23.077 1.00 26.82  ? 283 SER B OG  1 
ATOM   8848  N N   . ASP C 1 255 ? 6.066   32.490  -22.197 1.00 27.03  ? 284 ASP B N   1 
ATOM   8849  C CA  . ASP C 1 255 ? 6.931   31.328  -22.194 1.00 28.07  ? 284 ASP B CA  1 
ATOM   8850  C C   . ASP C 1 255 ? 6.196   30.140  -22.802 1.00 27.97  ? 284 ASP B C   1 
ATOM   8851  O O   . ASP C 1 255 ? 5.001   30.176  -23.026 1.00 27.95  ? 284 ASP B O   1 
ATOM   8852  C CB  . ASP C 1 255 ? 7.493   31.085  -20.799 1.00 33.18  ? 284 ASP B CB  1 
ATOM   8853  C CG  . ASP C 1 255 ? 6.437   30.759  -19.753 1.00 34.70  ? 284 ASP B CG  1 
ATOM   8854  O OD1 . ASP C 1 255 ? 5.737   29.767  -19.984 1.00 35.45  ? 284 ASP B OD1 1 
ATOM   8855  O OD2 . ASP C 1 255 ? 6.283   31.538  -18.761 1.00 35.36  ? 284 ASP B OD2 1 
ATOM   8856  N N   . PRO C 1 256 ? 6.904   29.055  -23.161 1.00 25.60  ? 285 PRO B N   1 
ATOM   8857  C CA  . PRO C 1 256 ? 6.264   27.891  -23.772 1.00 26.99  ? 285 PRO B CA  1 
ATOM   8858  C C   . PRO C 1 256 ? 5.125   27.287  -22.956 1.00 27.03  ? 285 PRO B C   1 
ATOM   8859  O O   . PRO C 1 256 ? 4.176   26.752  -23.511 1.00 26.36  ? 285 PRO B O   1 
ATOM   8860  C CB  . PRO C 1 256 ? 7.440   26.930  -23.901 1.00 29.07  ? 285 PRO B CB  1 
ATOM   8861  C CG  . PRO C 1 256 ? 8.615   27.855  -24.074 1.00 28.37  ? 285 PRO B CG  1 
ATOM   8862  C CD  . PRO C 1 256 ? 8.354   28.927  -23.027 1.00 27.52  ? 285 PRO B CD  1 
ATOM   8863  N N   . TYR C 1 257 ? 5.198   27.397  -21.627 1.00 26.95  ? 286 TYR B N   1 
ATOM   8864  C CA  . TYR C 1 257 ? 4.116   26.891  -20.799 1.00 26.24  ? 286 TYR B CA  1 
ATOM   8865  C C   . TYR C 1 257 ? 2.839   27.694  -21.043 1.00 25.23  ? 286 TYR B C   1 
ATOM   8866  O O   . TYR C 1 257 ? 1.787   27.138  -21.334 1.00 28.52  ? 286 TYR B O   1 
ATOM   8867  C CB  . TYR C 1 257 ? 4.578   26.912  -19.352 1.00 23.50  ? 286 TYR B CB  1 
ATOM   8868  C CG  . TYR C 1 257 ? 5.775   26.030  -19.043 1.00 24.78  ? 286 TYR B CG  1 
ATOM   8869  C CD1 . TYR C 1 257 ? 5.590   24.705  -18.714 1.00 27.35  ? 286 TYR B CD1 1 
ATOM   8870  C CD2 . TYR C 1 257 ? 7.063   26.533  -18.957 1.00 27.54  ? 286 TYR B CD2 1 
ATOM   8871  C CE1 . TYR C 1 257 ? 6.645   23.874  -18.404 1.00 26.90  ? 286 TYR B CE1 1 
ATOM   8872  C CE2 . TYR C 1 257 ? 8.132   25.725  -18.611 1.00 27.26  ? 286 TYR B CE2 1 
ATOM   8873  C CZ  . TYR C 1 257 ? 7.915   24.387  -18.331 1.00 29.85  ? 286 TYR B CZ  1 
ATOM   8874  O OH  . TYR C 1 257 ? 8.862   23.494  -17.971 1.00 33.10  ? 286 TYR B OH  1 
ATOM   8875  N N   . LEU C 1 258 ? 2.923   29.015  -20.961 1.00 26.73  ? 287 LEU B N   1 
ATOM   8876  C CA  . LEU C 1 258 ? 1.729   29.792  -21.167 1.00 27.20  ? 287 LEU B CA  1 
ATOM   8877  C C   . LEU C 1 258 ? 1.223   29.631  -22.606 1.00 27.95  ? 287 LEU B C   1 
ATOM   8878  O O   . LEU C 1 258 ? 0.016   29.580  -22.832 1.00 22.36  ? 287 LEU B O   1 
ATOM   8879  C CB  . LEU C 1 258 ? 2.030   31.228  -20.802 1.00 30.96  ? 287 LEU B CB  1 
ATOM   8880  C CG  . LEU C 1 258 ? 2.440   31.470  -19.350 1.00 33.79  ? 287 LEU B CG  1 
ATOM   8881  C CD1 . LEU C 1 258 ? 2.519   32.971  -19.231 1.00 35.46  ? 287 LEU B CD1 1 
ATOM   8882  C CD2 . LEU C 1 258 ? 1.541   30.884  -18.303 1.00 31.55  ? 287 LEU B CD2 1 
ATOM   8883  N N   . SER C 1 259 ? 2.145   29.534  -23.581 1.00 26.67  ? 288 SER B N   1 
ATOM   8884  C CA  . SER C 1 259 ? 1.761   29.433  -24.968 1.00 26.57  ? 288 SER B CA  1 
ATOM   8885  C C   . SER C 1 259 ? 1.015   28.133  -25.174 1.00 26.68  ? 288 SER B C   1 
ATOM   8886  O O   . SER C 1 259 ? 0.017   28.127  -25.869 1.00 23.65  ? 288 SER B O   1 
ATOM   8887  C CB  . SER C 1 259 ? 2.935   29.528  -25.915 1.00 31.14  ? 288 SER B CB  1 
ATOM   8888  O OG  . SER C 1 259 ? 3.620   30.747  -25.623 1.00 39.39  ? 288 SER B OG  1 
ATOM   8889  N N   . PHE C 1 260 ? 1.527   27.059  -24.578 1.00 24.60  ? 289 PHE B N   1 
ATOM   8890  C CA  . PHE C 1 260 ? 0.944   25.750  -24.743 1.00 26.68  ? 289 PHE B CA  1 
ATOM   8891  C C   . PHE C 1 260 ? -0.394  25.704  -24.021 1.00 24.44  ? 289 PHE B C   1 
ATOM   8892  O O   . PHE C 1 260 ? -1.333  25.153  -24.538 1.00 25.00  ? 289 PHE B O   1 
ATOM   8893  C CB  . PHE C 1 260 ? 1.945   24.691  -24.292 1.00 26.91  ? 289 PHE B CB  1 
ATOM   8894  C CG  . PHE C 1 260 ? 1.445   23.293  -24.535 1.00 25.95  ? 289 PHE B CG  1 
ATOM   8895  C CD1 . PHE C 1 260 ? 1.320   22.805  -25.820 1.00 29.47  ? 289 PHE B CD1 1 
ATOM   8896  C CD2 . PHE C 1 260 ? 1.026   22.484  -23.483 1.00 33.94  ? 289 PHE B CD2 1 
ATOM   8897  C CE1 . PHE C 1 260 ? 0.792   21.551  -26.040 1.00 26.42  ? 289 PHE B CE1 1 
ATOM   8898  C CE2 . PHE C 1 260 ? 0.525   21.215  -23.722 1.00 32.54  ? 289 PHE B CE2 1 
ATOM   8899  C CZ  . PHE C 1 260 ? 0.404   20.763  -25.011 1.00 27.56  ? 289 PHE B CZ  1 
ATOM   8900  N N   . ALA C 1 261 ? -0.483  26.272  -22.829 1.00 27.56  ? 290 ALA B N   1 
ATOM   8901  C CA  . ALA C 1 261 ? -1.718  26.202  -22.076 1.00 26.51  ? 290 ALA B CA  1 
ATOM   8902  C C   . ALA C 1 261 ? -2.825  26.906  -22.831 1.00 23.96  ? 290 ALA B C   1 
ATOM   8903  O O   . ALA C 1 261 ? -3.928  26.423  -22.834 1.00 26.00  ? 290 ALA B O   1 
ATOM   8904  C CB  . ALA C 1 261 ? -1.556  26.827  -20.721 1.00 29.21  ? 290 ALA B CB  1 
ATOM   8905  N N   . ALA C 1 262 ? -2.517  28.038  -23.482 1.00 25.09  ? 291 ALA B N   1 
ATOM   8906  C CA  . ALA C 1 262 ? -3.479  28.721  -24.333 1.00 24.17  ? 291 ALA B CA  1 
ATOM   8907  C C   . ALA C 1 262 ? -3.885  27.835  -25.510 1.00 25.51  ? 291 ALA B C   1 
ATOM   8908  O O   . ALA C 1 262 ? -5.051  27.759  -25.876 1.00 29.53  ? 291 ALA B O   1 
ATOM   8909  C CB  . ALA C 1 262 ? -2.922  30.045  -24.859 1.00 22.88  ? 291 ALA B CB  1 
ATOM   8910  N N   . ALA C 1 263 ? -2.911  27.217  -26.169 1.00 23.78  ? 292 ALA B N   1 
ATOM   8911  C CA  . ALA C 1 263 ? -3.231  26.337  -27.286 1.00 23.58  ? 292 ALA B CA  1 
ATOM   8912  C C   . ALA C 1 263 ? -4.197  25.241  -26.853 1.00 25.10  ? 292 ALA B C   1 
ATOM   8913  O O   . ALA C 1 263 ? -5.157  24.956  -27.553 1.00 25.53  ? 292 ALA B O   1 
ATOM   8914  C CB  . ALA C 1 263 ? -1.964  25.773  -27.834 1.00 24.04  ? 292 ALA B CB  1 
ATOM   8915  N N   . MET C 1 264 ? -3.986  24.696  -25.657 1.00 24.58  ? 293 MET B N   1 
ATOM   8916  C CA  . MET C 1 264 ? -4.840  23.638  -25.142 1.00 26.71  ? 293 MET B CA  1 
ATOM   8917  C C   . MET C 1 264 ? -6.272  24.126  -24.937 1.00 25.77  ? 293 MET B C   1 
ATOM   8918  O O   . MET C 1 264 ? -7.220  23.396  -25.237 1.00 26.71  ? 293 MET B O   1 
ATOM   8919  C CB  . MET C 1 264 ? -4.265  23.046  -23.851 1.00 23.81  ? 293 MET B CB  1 
ATOM   8920  C CG  . MET C 1 264 ? -2.985  22.308  -24.054 1.00 26.17  ? 293 MET B CG  1 
ATOM   8921  S SD  . MET C 1 264 ? -3.136  21.040  -25.321 1.00 30.36  ? 293 MET B SD  1 
ATOM   8922  C CE  . MET C 1 264 ? -2.754  21.744  -26.939 1.00 30.87  ? 293 MET B CE  1 
ATOM   8923  N N   . ASN C 1 265 ? -6.430  25.343  -24.424 1.00 25.33  ? 294 ASN B N   1 
ATOM   8924  C CA  . ASN C 1 265 ? -7.750  25.945  -24.314 1.00 25.63  ? 294 ASN B CA  1 
ATOM   8925  C C   . ASN C 1 265 ? -8.439  25.993  -25.680 1.00 26.65  ? 294 ASN B C   1 
ATOM   8926  O O   . ASN C 1 265 ? -9.645  25.788  -25.784 1.00 29.60  ? 294 ASN B O   1 
ATOM   8927  C CB  . ASN C 1 265 ? -7.660  27.273  -23.573 1.00 28.54  ? 294 ASN B CB  1 
ATOM   8928  C CG  . ASN C 1 265 ? -7.535  27.045  -22.080 1.00 32.43  ? 294 ASN B CG  1 
ATOM   8929  O OD1 . ASN C 1 265 ? -7.401  25.910  -21.621 1.00 33.59  ? 294 ASN B OD1 1 
ATOM   8930  N ND2 . ASN C 1 265 ? -7.546  28.097  -21.293 1.00 33.28  ? 294 ASN B ND2 1 
ATOM   8931  N N   . GLY C 1 266 ? -7.664  26.226  -26.727 1.00 23.23  ? 295 GLY B N   1 
ATOM   8932  C CA  . GLY C 1 266 ? -8.181  26.265  -28.071 1.00 26.44  ? 295 GLY B CA  1 
ATOM   8933  C C   . GLY C 1 266 ? -8.450  24.861  -28.610 1.00 28.92  ? 295 GLY B C   1 
ATOM   8934  O O   . GLY C 1 266 ? -9.442  24.645  -29.273 1.00 25.04  ? 295 GLY B O   1 
ATOM   8935  N N   . LEU C 1 267 ? -7.574  23.911  -28.296 1.00 28.79  ? 296 LEU B N   1 
ATOM   8936  C CA  . LEU C 1 267 ? -7.787  22.504  -28.602 1.00 29.49  ? 296 LEU B CA  1 
ATOM   8937  C C   . LEU C 1 267 ? -9.062  21.986  -27.933 1.00 30.62  ? 296 LEU B C   1 
ATOM   8938  O O   . LEU C 1 267 ? -9.754  21.162  -28.515 1.00 29.93  ? 296 LEU B O   1 
ATOM   8939  C CB  . LEU C 1 267 ? -6.586  21.650  -28.187 1.00 31.21  ? 296 LEU B CB  1 
ATOM   8940  C CG  . LEU C 1 267 ? -6.450  20.306  -28.904 1.00 32.98  ? 296 LEU B CG  1 
ATOM   8941  C CD1 . LEU C 1 267 ? -6.316  20.531  -30.410 1.00 37.94  ? 296 LEU B CD1 1 
ATOM   8942  C CD2 . LEU C 1 267 ? -5.296  19.529  -28.400 1.00 32.62  ? 296 LEU B CD2 1 
ATOM   8943  N N   . ALA C 1 268 ? -9.433  22.515  -26.758 1.00 28.44  ? 297 ALA B N   1 
ATOM   8944  C CA  . ALA C 1 268 ? -10.554 21.975  -26.002 1.00 28.43  ? 297 ALA B CA  1 
ATOM   8945  C C   . ALA C 1 268 ? -11.902 22.330  -26.640 1.00 30.26  ? 297 ALA B C   1 
ATOM   8946  O O   . ALA C 1 268 ? -12.937 21.811  -26.238 1.00 29.62  ? 297 ALA B O   1 
ATOM   8947  C CB  . ALA C 1 268 ? -10.476 22.487  -24.582 1.00 28.97  ? 297 ALA B CB  1 
ATOM   8948  N N   . GLY C 1 269 ? -11.905 23.218  -27.648 1.00 29.28  ? 298 GLY B N   1 
ATOM   8949  C CA  . GLY C 1 269 ? -13.144 23.713  -28.209 1.00 27.09  ? 298 GLY B CA  1 
ATOM   8950  C C   . GLY C 1 269 ? -13.770 22.649  -29.094 1.00 28.82  ? 298 GLY B C   1 
ATOM   8951  O O   . GLY C 1 269 ? -13.036 21.948  -29.796 1.00 33.73  ? 298 GLY B O   1 
ATOM   8952  N N   . PRO C 1 270 ? -15.116 22.484  -29.059 1.00 27.03  ? 299 PRO B N   1 
ATOM   8953  C CA  . PRO C 1 270 ? -15.824 21.519  -29.895 1.00 31.80  ? 299 PRO B CA  1 
ATOM   8954  C C   . PRO C 1 270 ? -15.454 21.506  -31.379 1.00 31.84  ? 299 PRO B C   1 
ATOM   8955  O O   . PRO C 1 270 ? -15.467 20.452  -32.006 1.00 32.66  ? 299 PRO B O   1 
ATOM   8956  C CB  . PRO C 1 270 ? -17.324 21.906  -29.693 1.00 34.24  ? 299 PRO B CB  1 
ATOM   8957  C CG  . PRO C 1 270 ? -17.380 22.580  -28.350 1.00 30.45  ? 299 PRO B CG  1 
ATOM   8958  C CD  . PRO C 1 270 ? -16.024 23.209  -28.164 1.00 28.35  ? 299 PRO B CD  1 
ATOM   8959  N N   . LEU C 1 271 ? -15.114 22.663  -31.937 1.00 29.20  ? 300 LEU B N   1 
ATOM   8960  C CA  . LEU C 1 271 ? -14.802 22.770  -33.362 1.00 33.09  ? 300 LEU B CA  1 
ATOM   8961  C C   . LEU C 1 271 ? -13.344 22.423  -33.694 1.00 35.36  ? 300 LEU B C   1 
ATOM   8962  O O   . LEU C 1 271 ? -12.925 22.539  -34.845 1.00 31.17  ? 300 LEU B O   1 
ATOM   8963  C CB  . LEU C 1 271 ? -15.132 24.194  -33.838 1.00 33.29  ? 300 LEU B CB  1 
ATOM   8964  C CG  . LEU C 1 271 ? -16.554 24.454  -34.320 1.00 39.46  ? 300 LEU B CG  1 
ATOM   8965  C CD1 . LEU C 1 271 ? -17.495 24.045  -33.251 1.00 44.36  ? 300 LEU B CD1 1 
ATOM   8966  C CD2 . LEU C 1 271 ? -16.827 25.901  -34.748 1.00 44.57  ? 300 LEU B CD2 1 
ATOM   8967  N N   . HIS C 1 272 ? -12.524 22.046  -32.716 1.00 34.40  ? 301 HIS B N   1 
ATOM   8968  C CA  . HIS C 1 272 ? -11.136 21.772  -33.047 1.00 35.66  ? 301 HIS B CA  1 
ATOM   8969  C C   . HIS C 1 272 ? -10.690 20.397  -32.562 1.00 35.27  ? 301 HIS B C   1 
ATOM   8970  O O   . HIS C 1 272 ? -10.212 19.612  -33.354 1.00 43.14  ? 301 HIS B O   1 
ATOM   8971  C CB  . HIS C 1 272 ? -10.204 22.878  -32.532 1.00 35.63  ? 301 HIS B CB  1 
ATOM   8972  C CG  . HIS C 1 272 ? -8.790  22.634  -32.893 1.00 33.10  ? 301 HIS B CG  1 
ATOM   8973  N ND1 . HIS C 1 272 ? -7.725  23.130  -32.172 1.00 34.90  ? 301 HIS B ND1 1 
ATOM   8974  C CD2 . HIS C 1 272 ? -8.267  21.915  -33.889 1.00 33.50  ? 301 HIS B CD2 1 
ATOM   8975  C CE1 . HIS C 1 272 ? -6.581  22.735  -32.766 1.00 33.14  ? 301 HIS B CE1 1 
ATOM   8976  N NE2 . HIS C 1 272 ? -6.892  22.033  -33.824 1.00 35.78  ? 301 HIS B NE2 1 
ATOM   8977  N N   . GLY C 1 273 ? -10.803 20.113  -31.270 1.00 36.95  ? 302 GLY B N   1 
ATOM   8978  C CA  . GLY C 1 273 ? -10.144 18.931  -30.741 1.00 39.18  ? 302 GLY B CA  1 
ATOM   8979  C C   . GLY C 1 273 ? -11.098 17.906  -30.146 1.00 39.48  ? 302 GLY B C   1 
ATOM   8980  O O   . GLY C 1 273 ? -10.620 16.880  -29.668 1.00 38.26  ? 302 GLY B O   1 
ATOM   8981  N N   . LEU C 1 274 ? -12.417 18.144  -30.219 1.00 40.53  ? 303 LEU B N   1 
ATOM   8982  C CA  . LEU C 1 274 ? -13.369 17.236  -29.587 1.00 44.37  ? 303 LEU B CA  1 
ATOM   8983  C C   . LEU C 1 274 ? -14.064 16.326  -30.599 1.00 41.52  ? 303 LEU B C   1 
ATOM   8984  O O   . LEU C 1 274 ? -14.963 15.575  -30.227 1.00 37.03  ? 303 LEU B O   1 
ATOM   8985  C CB  . LEU C 1 274 ? -14.414 17.981  -28.760 1.00 46.92  ? 303 LEU B CB  1 
ATOM   8986  C CG  . LEU C 1 274 ? -13.913 18.830  -27.581 1.00 52.31  ? 303 LEU B CG  1 
ATOM   8987  C CD1 . LEU C 1 274 ? -15.114 19.163  -26.670 1.00 53.81  ? 303 LEU B CD1 1 
ATOM   8988  C CD2 . LEU C 1 274 ? -12.803 18.209  -26.741 1.00 56.53  ? 303 LEU B CD2 1 
ATOM   8989  N N   . ALA C 1 275 ? -13.646 16.349  -31.870 1.00 40.70  ? 304 ALA B N   1 
ATOM   8990  C CA  . ALA C 1 275 ? -14.384 15.647  -32.922 1.00 42.57  ? 304 ALA B CA  1 
ATOM   8991  C C   . ALA C 1 275 ? -14.186 14.125  -32.857 1.00 38.56  ? 304 ALA B C   1 
ATOM   8992  O O   . ALA C 1 275 ? -15.061 13.372  -33.293 1.00 37.58  ? 304 ALA B O   1 
ATOM   8993  C CB  . ALA C 1 275 ? -13.989 16.173  -34.283 1.00 40.48  ? 304 ALA B CB  1 
ATOM   8994  N N   . ASN C 1 276 ? -13.035 13.671  -32.348 1.00 38.35  ? 305 ASN B N   1 
ATOM   8995  C CA  . ASN C 1 276 ? -12.780 12.244  -32.133 1.00 41.86  ? 305 ASN B CA  1 
ATOM   8996  C C   . ASN C 1 276 ? -13.944 11.627  -31.335 1.00 40.93  ? 305 ASN B C   1 
ATOM   8997  O O   . ASN C 1 276 ? -14.556 10.633  -31.734 1.00 35.38  ? 305 ASN B O   1 
ATOM   8998  C CB  . ASN C 1 276 ? -11.409 12.083  -31.481 1.00 42.18  ? 305 ASN B CB  1 
ATOM   8999  C CG  . ASN C 1 276 ? -11.118 10.667  -31.035 1.00 48.39  ? 305 ASN B CG  1 
ATOM   9000  O OD1 . ASN C 1 276 ? -12.020 9.816   -31.005 1.00 46.45  ? 305 ASN B OD1 1 
ATOM   9001  N ND2 . ASN C 1 276 ? -9.876  10.404  -30.649 1.00 39.26  ? 305 ASN B ND2 1 
ATOM   9002  N N   . GLN C 1 277 ? -14.258 12.274  -30.209 1.00 37.87  ? 306 GLN B N   1 
ATOM   9003  C CA  . GLN C 1 277 ? -15.293 11.846  -29.286 1.00 38.49  ? 306 GLN B CA  1 
ATOM   9004  C C   . GLN C 1 277 ? -16.660 11.932  -29.973 1.00 38.50  ? 306 GLN B C   1 
ATOM   9005  O O   . GLN C 1 277 ? -17.470 11.044  -29.825 1.00 36.23  ? 306 GLN B O   1 
ATOM   9006  C CB  . GLN C 1 277 ? -15.149 12.623  -27.966 1.00 40.85  ? 306 GLN B CB  1 
ATOM   9007  C CG  . GLN C 1 277 ? -16.426 12.682  -27.133 1.00 48.68  ? 306 GLN B CG  1 
ATOM   9008  C CD  . GLN C 1 277 ? -16.246 13.292  -25.756 1.00 54.44  ? 306 GLN B CD  1 
ATOM   9009  O OE1 . GLN C 1 277 ? -15.312 14.055  -25.498 1.00 60.14  ? 306 GLN B OE1 1 
ATOM   9010  N NE2 . GLN C 1 277 ? -17.175 12.987  -24.860 1.00 55.29  ? 306 GLN B NE2 1 
ATOM   9011  N N   . GLU C 1 278 ? -16.912 12.966  -30.773 1.00 36.23  ? 307 GLU B N   1 
ATOM   9012  C CA  . GLU C 1 278 ? -18.202 13.156  -31.415 1.00 41.13  ? 307 GLU B CA  1 
ATOM   9013  C C   . GLU C 1 278 ? -18.396 12.094  -32.496 1.00 40.60  ? 307 GLU B C   1 
ATOM   9014  O O   . GLU C 1 278 ? -19.512 11.670  -32.748 1.00 39.72  ? 307 GLU B O   1 
ATOM   9015  C CB  . GLU C 1 278 ? -18.250 14.576  -31.986 1.00 45.06  ? 307 GLU B CB  1 
ATOM   9016  C CG  . GLU C 1 278 ? -19.515 14.933  -32.756 1.00 50.69  ? 307 GLU B CG  1 
ATOM   9017  C CD  . GLU C 1 278 ? -19.381 16.158  -33.669 1.00 62.17  ? 307 GLU B CD  1 
ATOM   9018  O OE1 . GLU C 1 278 ? -18.324 16.858  -33.687 1.00 53.51  ? 307 GLU B OE1 1 
ATOM   9019  O OE2 . GLU C 1 278 ? -20.363 16.392  -34.410 1.00 58.90  ? 307 GLU B OE2 1 
ATOM   9020  N N   . VAL C 1 279 ? -17.317 11.704  -33.178 1.00 36.67  ? 308 VAL B N   1 
ATOM   9021  C CA  . VAL C 1 279 ? -17.387 10.579  -34.090 1.00 30.65  ? 308 VAL B CA  1 
ATOM   9022  C C   . VAL C 1 279 ? -17.797 9.325   -33.333 1.00 33.89  ? 308 VAL B C   1 
ATOM   9023  O O   . VAL C 1 279 ? -18.734 8.650   -33.726 1.00 32.68  ? 308 VAL B O   1 
ATOM   9024  C CB  . VAL C 1 279 ? -16.050 10.393  -34.816 1.00 29.84  ? 308 VAL B CB  1 
ATOM   9025  C CG1 . VAL C 1 279 ? -15.962 9.011   -35.486 1.00 33.91  ? 308 VAL B CG1 1 
ATOM   9026  C CG2 . VAL C 1 279 ? -15.883 11.487  -35.865 1.00 33.04  ? 308 VAL B CG2 1 
ATOM   9027  N N   . LEU C 1 280 ? -17.127 9.033   -32.222 1.00 33.76  ? 309 LEU B N   1 
ATOM   9028  C CA  . LEU C 1 280 ? -17.324 7.743   -31.572 1.00 37.65  ? 309 LEU B CA  1 
ATOM   9029  C C   . LEU C 1 280 ? -18.760 7.613   -31.064 1.00 40.00  ? 309 LEU B C   1 
ATOM   9030  O O   . LEU C 1 280 ? -19.371 6.575   -31.254 1.00 37.59  ? 309 LEU B O   1 
ATOM   9031  C CB  . LEU C 1 280 ? -16.309 7.574   -30.446 1.00 38.98  ? 309 LEU B CB  1 
ATOM   9032  C CG  . LEU C 1 280 ? -16.138 6.171   -29.867 1.00 40.45  ? 309 LEU B CG  1 
ATOM   9033  C CD1 . LEU C 1 280 ? -15.894 5.124   -30.967 1.00 38.10  ? 309 LEU B CD1 1 
ATOM   9034  C CD2 . LEU C 1 280 ? -14.983 6.266   -28.896 1.00 41.07  ? 309 LEU B CD2 1 
ATOM   9035  N N   . VAL C 1 281 ? -19.284 8.674   -30.428 1.00 40.48  ? 310 VAL B N   1 
ATOM   9036  C CA  . VAL C 1 281 ? -20.641 8.723   -29.922 1.00 42.39  ? 310 VAL B CA  1 
ATOM   9037  C C   . VAL C 1 281 ? -21.638 8.488   -31.063 1.00 46.60  ? 310 VAL B C   1 
ATOM   9038  O O   . VAL C 1 281 ? -22.594 7.718   -30.922 1.00 48.17  ? 310 VAL B O   1 
ATOM   9039  C CB  . VAL C 1 281 ? -20.887 10.087  -29.234 1.00 47.88  ? 310 VAL B CB  1 
ATOM   9040  C CG1 . VAL C 1 281 ? -22.367 10.318  -28.959 1.00 47.75  ? 310 VAL B CG1 1 
ATOM   9041  C CG2 . VAL C 1 281 ? -20.074 10.253  -27.952 1.00 43.97  ? 310 VAL B CG2 1 
ATOM   9042  N N   . TRP C 1 282 ? -21.411 9.170   -32.191 1.00 41.46  ? 311 TRP B N   1 
ATOM   9043  C CA  . TRP C 1 282 ? -22.195 8.945   -33.397 1.00 44.11  ? 311 TRP B CA  1 
ATOM   9044  C C   . TRP C 1 282 ? -22.110 7.492   -33.898 1.00 43.50  ? 311 TRP B C   1 
ATOM   9045  O O   . TRP C 1 282 ? -23.127 6.885   -34.222 1.00 39.77  ? 311 TRP B O   1 
ATOM   9046  C CB  . TRP C 1 282 ? -21.760 9.952   -34.467 1.00 42.40  ? 311 TRP B CB  1 
ATOM   9047  C CG  . TRP C 1 282 ? -22.650 9.980   -35.673 1.00 41.39  ? 311 TRP B CG  1 
ATOM   9048  C CD1 . TRP C 1 282 ? -23.802 10.694  -35.854 1.00 41.08  ? 311 TRP B CD1 1 
ATOM   9049  C CD2 . TRP C 1 282 ? -22.415 9.263   -36.899 1.00 39.59  ? 311 TRP B CD2 1 
ATOM   9050  N NE1 . TRP C 1 282 ? -24.290 10.474  -37.113 1.00 41.75  ? 311 TRP B NE1 1 
ATOM   9051  C CE2 . TRP C 1 282 ? -23.467 9.603   -37.778 1.00 37.39  ? 311 TRP B CE2 1 
ATOM   9052  C CE3 . TRP C 1 282 ? -21.420 8.388   -37.335 1.00 40.16  ? 311 TRP B CE3 1 
ATOM   9053  C CZ2 . TRP C 1 282 ? -23.556 9.078   -39.063 1.00 41.98  ? 311 TRP B CZ2 1 
ATOM   9054  C CZ3 . TRP C 1 282 ? -21.514 7.866   -38.607 1.00 42.14  ? 311 TRP B CZ3 1 
ATOM   9055  C CH2 . TRP C 1 282 ? -22.561 8.216   -39.461 1.00 39.73  ? 311 TRP B CH2 1 
ATOM   9056  N N   . LEU C 1 283 ? -20.901 6.919   -33.948 1.00 47.32  ? 312 LEU B N   1 
ATOM   9057  C CA  . LEU C 1 283 ? -20.694 5.544   -34.383 1.00 45.41  ? 312 LEU B CA  1 
ATOM   9058  C C   . LEU C 1 283 ? -21.432 4.568   -33.454 1.00 48.40  ? 312 LEU B C   1 
ATOM   9059  O O   . LEU C 1 283 ? -22.001 3.589   -33.926 1.00 46.09  ? 312 LEU B O   1 
ATOM   9060  C CB  . LEU C 1 283 ? -19.201 5.208   -34.426 1.00 44.57  ? 312 LEU B CB  1 
ATOM   9061  C CG  . LEU C 1 283 ? -18.363 5.867   -35.530 1.00 48.88  ? 312 LEU B CG  1 
ATOM   9062  C CD1 . LEU C 1 283 ? -16.914 5.418   -35.412 1.00 46.71  ? 312 LEU B CD1 1 
ATOM   9063  C CD2 . LEU C 1 283 ? -18.882 5.587   -36.925 1.00 42.94  ? 312 LEU B CD2 1 
ATOM   9064  N N   . THR C 1 284 ? -21.351 4.800   -32.135 1.00 46.50  ? 313 THR B N   1 
ATOM   9065  C CA  . THR C 1 284 ? -21.967 3.940   -31.137 1.00 48.47  ? 313 THR B CA  1 
ATOM   9066  C C   . THR C 1 284 ? -23.489 4.028   -31.272 1.00 54.92  ? 313 THR B C   1 
ATOM   9067  O O   . THR C 1 284 ? -24.175 3.028   -31.082 1.00 63.27  ? 313 THR B O   1 
ATOM   9068  C CB  . THR C 1 284 ? -21.491 4.344   -29.739 1.00 53.59  ? 313 THR B CB  1 
ATOM   9069  O OG1 . THR C 1 284 ? -20.069 4.242   -29.794 1.00 55.55  ? 313 THR B OG1 1 
ATOM   9070  C CG2 . THR C 1 284 ? -22.062 3.461   -28.641 1.00 51.13  ? 313 THR B CG2 1 
ATOM   9071  N N   . GLN C 1 285 ? -24.000 5.220   -31.620 1.00 53.44  ? 314 GLN B N   1 
ATOM   9072  C CA  . GLN C 1 285 ? -25.423 5.442   -31.844 1.00 59.60  ? 314 GLN B CA  1 
ATOM   9073  C C   . GLN C 1 285 ? -25.917 4.716   -33.106 1.00 59.27  ? 314 GLN B C   1 
ATOM   9074  O O   . GLN C 1 285 ? -27.037 4.218   -33.120 1.00 64.25  ? 314 GLN B O   1 
ATOM   9075  C CB  . GLN C 1 285 ? -25.644 6.956   -31.878 1.00 62.02  ? 314 GLN B CB  1 
ATOM   9076  C CG  . GLN C 1 285 ? -27.036 7.394   -32.323 1.00 70.59  ? 314 GLN B CG  1 
ATOM   9077  C CD  . GLN C 1 285 ? -28.084 7.225   -31.247 1.00 77.07  ? 314 GLN B CD  1 
ATOM   9078  O OE1 . GLN C 1 285 ? -29.024 6.434   -31.380 1.00 91.78  ? 314 GLN B OE1 1 
ATOM   9079  N NE2 . GLN C 1 285 ? -27.927 7.966   -30.160 1.00 74.73  ? 314 GLN B NE2 1 
ATOM   9080  N N   . LEU C 1 286 ? -25.092 4.671   -34.165 1.00 58.08  ? 315 LEU B N   1 
ATOM   9081  C CA  . LEU C 1 286 ? -25.427 4.032   -35.441 1.00 57.22  ? 315 LEU B CA  1 
ATOM   9082  C C   . LEU C 1 286 ? -25.261 2.512   -35.378 1.00 60.86  ? 315 LEU B C   1 
ATOM   9083  O O   . LEU C 1 286 ? -26.044 1.797   -35.993 1.00 56.60  ? 315 LEU B O   1 
ATOM   9084  C CB  . LEU C 1 286 ? -24.555 4.613   -36.554 1.00 53.41  ? 315 LEU B CB  1 
ATOM   9085  C CG  . LEU C 1 286 ? -24.450 3.831   -37.868 1.00 53.37  ? 315 LEU B CG  1 
ATOM   9086  C CD1 . LEU C 1 286 ? -25.785 3.588   -38.519 1.00 57.24  ? 315 LEU B CD1 1 
ATOM   9087  C CD2 . LEU C 1 286 ? -23.561 4.604   -38.830 1.00 56.68  ? 315 LEU B CD2 1 
ATOM   9088  N N   . GLN C 1 287 ? -24.203 2.040   -34.701 1.00 61.31  ? 316 GLN B N   1 
ATOM   9089  C CA  . GLN C 1 287 ? -23.954 0.622   -34.492 1.00 59.48  ? 316 GLN B CA  1 
ATOM   9090  C C   . GLN C 1 287 ? -25.130 -0.017  -33.751 1.00 60.76  ? 316 GLN B C   1 
ATOM   9091  O O   . GLN C 1 287 ? -25.480 -1.159  -34.022 1.00 66.00  ? 316 GLN B O   1 
ATOM   9092  C CB  . GLN C 1 287 ? -22.656 0.483   -33.696 1.00 63.97  ? 316 GLN B CB  1 
ATOM   9093  C CG  . GLN C 1 287 ? -22.135 -0.942  -33.567 1.00 73.54  ? 316 GLN B CG  1 
ATOM   9094  C CD  . GLN C 1 287 ? -21.484 -1.438  -34.842 1.00 81.76  ? 316 GLN B CD  1 
ATOM   9095  O OE1 . GLN C 1 287 ? -22.008 -1.261  -35.951 1.00 83.09  ? 316 GLN B OE1 1 
ATOM   9096  N NE2 . GLN C 1 287 ? -20.315 -2.049  -34.699 1.00 83.72  ? 316 GLN B NE2 1 
ATOM   9097  N N   . LYS C 1 288 ? -25.734 0.721   -32.811 1.00 66.84  ? 317 LYS B N   1 
ATOM   9098  C CA  . LYS C 1 288 ? -26.882 0.236   -32.059 1.00 66.22  ? 317 LYS B CA  1 
ATOM   9099  C C   . LYS C 1 288 ? -28.119 0.157   -32.948 1.00 64.12  ? 317 LYS B C   1 
ATOM   9100  O O   . LYS C 1 288 ? -28.923 -0.742  -32.749 1.00 75.43  ? 317 LYS B O   1 
ATOM   9101  C CB  . LYS C 1 288 ? -27.176 1.075   -30.807 1.00 73.33  ? 317 LYS B CB  1 
ATOM   9102  C CG  . LYS C 1 288 ? -26.215 0.817   -29.650 1.00 73.21  ? 317 LYS B CG  1 
ATOM   9103  C CD  . LYS C 1 288 ? -26.168 1.872   -28.547 1.00 86.15  ? 317 LYS B CD  1 
ATOM   9104  C CE  . LYS C 1 288 ? -27.393 1.973   -27.679 1.00 88.62  ? 317 LYS B CE  1 
ATOM   9105  N NZ  . LYS C 1 288 ? -28.479 2.755   -28.278 1.00 85.15  ? 317 LYS B NZ  1 
ATOM   9106  N N   . GLU C 1 289 ? -28.278 1.071   -33.920 1.00 67.73  ? 318 GLU B N   1 
ATOM   9107  C CA  . GLU C 1 289 ? -29.512 1.140   -34.700 1.00 75.34  ? 318 GLU B CA  1 
ATOM   9108  C C   . GLU C 1 289 ? -29.468 0.332   -36.003 1.00 72.33  ? 318 GLU B C   1 
ATOM   9109  O O   . GLU C 1 289 ? -30.345 0.523   -36.838 1.00 66.51  ? 318 GLU B O   1 
ATOM   9110  C CB  . GLU C 1 289 ? -29.904 2.566   -35.089 1.00 72.56  ? 318 GLU B CB  1 
ATOM   9111  C CG  . GLU C 1 289 ? -30.280 3.448   -33.903 1.00 76.10  ? 318 GLU B CG  1 
ATOM   9112  C CD  . GLU C 1 289 ? -30.582 4.890   -34.288 1.00 83.27  ? 318 GLU B CD  1 
ATOM   9113  O OE1 . GLU C 1 289 ? -30.740 5.142   -35.504 1.00 78.90  ? 318 GLU B OE1 1 
ATOM   9114  O OE2 . GLU C 1 289 ? -30.641 5.764   -33.392 1.00 78.99  ? 318 GLU B OE2 1 
ATOM   9115  N N   . VAL C 1 290 ? -28.267 -0.505  -36.319 1.00 76.85  ? 319 VAL B N   1 
ATOM   9116  C CA  . VAL C 1 290 ? -28.629 -1.555  -37.269 1.00 75.78  ? 319 VAL B CA  1 
ATOM   9117  C C   . VAL C 1 290 ? -27.903 -2.874  -36.962 1.00 79.70  ? 319 VAL B C   1 
ATOM   9118  O O   . VAL C 1 290 ? -28.052 -3.835  -37.719 1.00 94.00  ? 319 VAL B O   1 
ATOM   9119  C CB  . VAL C 1 290 ? -28.375 -1.121  -38.733 1.00 70.06  ? 319 VAL B CB  1 
ATOM   9120  C CG1 . VAL C 1 290 ? -29.192 0.095   -39.137 1.00 65.92  ? 319 VAL B CG1 1 
ATOM   9121  C CG2 . VAL C 1 290 ? -26.906 -0.843  -39.032 1.00 67.96  ? 319 VAL B CG2 1 
ATOM   9122  N N   . GLY C 1 291 ? -27.231 -2.924  -35.712 1.00 76.66  ? 320 GLY B N   1 
ATOM   9123  C CA  . GLY C 1 291 ? -26.365 -4.035  -35.336 1.00 77.95  ? 320 GLY B CA  1 
ATOM   9124  C C   . GLY C 1 291 ? -24.997 -3.915  -36.008 1.00 82.37  ? 320 GLY B C   1 
ATOM   9125  O O   . GLY C 1 291 ? -24.692 -2.875  -36.590 1.00 85.87  ? 320 GLY B O   1 
ATOM   9126  N N   . LYS C 1 292 ? -24.184 -4.980  -35.932 1.00 76.95  ? 321 LYS B N   1 
ATOM   9127  C CA  . LYS C 1 292 ? -22.899 -5.024  -36.620 1.00 79.78  ? 321 LYS B CA  1 
ATOM   9128  C C   . LYS C 1 292 ? -23.010 -5.819  -37.920 1.00 80.98  ? 321 LYS B C   1 
ATOM   9129  O O   . LYS C 1 292 ? -22.059 -5.876  -38.693 1.00 74.04  ? 321 LYS B O   1 
ATOM   9130  C CB  . LYS C 1 292 ? -21.792 -5.606  -35.731 1.00 85.32  ? 321 LYS B CB  1 
ATOM   9131  C CG  . LYS C 1 292 ? -22.038 -7.000  -35.164 1.00 84.86  ? 321 LYS B CG  1 
ATOM   9132  C CD  . LYS C 1 292 ? -20.784 -7.604  -34.550 1.00 90.13  ? 321 LYS B CD  1 
ATOM   9133  C CE  . LYS C 1 292 ? -21.046 -8.912  -33.877 1.00 92.24  ? 321 LYS B CE  1 
ATOM   9134  N NZ  . LYS C 1 292 ? -19.816 -9.455  -33.297 1.00 93.54  ? 321 LYS B NZ  1 
ATOM   9135  N N   . ASP C 1 293 ? -24.185 -6.417  -38.158 1.00 91.19  ? 322 ASP B N   1 
ATOM   9136  C CA  . ASP C 1 293 ? -24.433 -7.235  -39.335 1.00 94.16  ? 322 ASP B CA  1 
ATOM   9137  C C   . ASP C 1 293 ? -24.661 -6.341  -40.556 1.00 83.98  ? 322 ASP B C   1 
ATOM   9138  O O   . ASP C 1 293 ? -24.642 -6.825  -41.684 1.00 74.19  ? 322 ASP B O   1 
ATOM   9139  C CB  . ASP C 1 293 ? -25.605 -8.177  -39.081 1.00 100.31 ? 322 ASP B CB  1 
ATOM   9140  C CG  . ASP C 1 293 ? -25.771 -9.356  -40.035 1.00 99.25  ? 322 ASP B CG  1 
ATOM   9141  O OD1 . ASP C 1 293 ? -24.778 -10.079 -40.277 1.00 91.29  ? 322 ASP B OD1 1 
ATOM   9142  O OD2 . ASP C 1 293 ? -26.909 -9.575  -40.498 1.00 99.08  ? 322 ASP B OD2 1 
ATOM   9143  N N   . VAL C 1 294 ? -24.837 -5.034  -40.326 1.00 76.21  ? 323 VAL B N   1 
ATOM   9144  C CA  . VAL C 1 294 ? -25.455 -4.143  -41.295 1.00 68.86  ? 323 VAL B CA  1 
ATOM   9145  C C   . VAL C 1 294 ? -24.840 -4.346  -42.676 1.00 56.91  ? 323 VAL B C   1 
ATOM   9146  O O   . VAL C 1 294 ? -23.627 -4.306  -42.824 1.00 49.74  ? 323 VAL B O   1 
ATOM   9147  C CB  . VAL C 1 294 ? -25.339 -2.669  -40.861 1.00 75.02  ? 323 VAL B CB  1 
ATOM   9148  C CG1 . VAL C 1 294 ? -23.884 -2.212  -40.704 1.00 76.53  ? 323 VAL B CG1 1 
ATOM   9149  C CG2 . VAL C 1 294 ? -26.113 -1.749  -41.802 1.00 72.40  ? 323 VAL B CG2 1 
ATOM   9150  N N   . SER C 1 295 ? -25.715 -4.505  -43.674 1.00 56.77  ? 324 SER B N   1 
ATOM   9151  C CA  . SER C 1 295 ? -25.346 -4.548  -45.076 1.00 54.20  ? 324 SER B CA  1 
ATOM   9152  C C   . SER C 1 295 ? -24.970 -3.150  -45.561 1.00 49.93  ? 324 SER B C   1 
ATOM   9153  O O   . SER C 1 295 ? -25.382 -2.140  -44.978 1.00 46.55  ? 324 SER B O   1 
ATOM   9154  C CB  . SER C 1 295 ? -26.472 -5.118  -45.922 1.00 57.32  ? 324 SER B CB  1 
ATOM   9155  O OG  . SER C 1 295 ? -27.590 -4.236  -46.008 1.00 59.19  ? 324 SER B OG  1 
ATOM   9156  N N   . ASP C 1 296 ? -24.204 -3.122  -46.655 1.00 46.70  ? 325 ASP B N   1 
ATOM   9157  C CA  . ASP C 1 296 ? -23.832 -1.891  -47.334 1.00 53.28  ? 325 ASP B CA  1 
ATOM   9158  C C   . ASP C 1 296 ? -25.085 -1.118  -47.746 1.00 55.33  ? 325 ASP B C   1 
ATOM   9159  O O   . ASP C 1 296 ? -25.106 0.105   -47.606 1.00 48.25  ? 325 ASP B O   1 
ATOM   9160  C CB  . ASP C 1 296 ? -22.850 -2.163  -48.467 1.00 56.65  ? 325 ASP B CB  1 
ATOM   9161  C CG  . ASP C 1 296 ? -21.421 -2.504  -48.047 1.00 63.25  ? 325 ASP B CG  1 
ATOM   9162  O OD1 . ASP C 1 296 ? -21.104 -2.363  -46.839 1.00 71.64  ? 325 ASP B OD1 1 
ATOM   9163  O OD2 . ASP C 1 296 ? -20.621 -2.916  -48.925 1.00 60.99  ? 325 ASP B OD2 1 
ATOM   9164  N N   . GLU C 1 297 ? -26.121 -1.832  -48.229 1.00 58.36  ? 326 GLU B N   1 
ATOM   9165  C CA  . GLU C 1 297 ? -27.374 -1.215  -48.662 1.00 60.36  ? 326 GLU B CA  1 
ATOM   9166  C C   . GLU C 1 297 ? -28.027 -0.458  -47.505 1.00 57.54  ? 326 GLU B C   1 
ATOM   9167  O O   . GLU C 1 297 ? -28.475 0.677   -47.673 1.00 42.40  ? 326 GLU B O   1 
ATOM   9168  C CB  . GLU C 1 297 ? -28.448 -2.179  -49.182 1.00 69.79  ? 326 GLU B CB  1 
ATOM   9169  C CG  . GLU C 1 297 ? -28.407 -2.471  -50.681 1.00 80.50  ? 326 GLU B CG  1 
ATOM   9170  C CD  . GLU C 1 297 ? -29.625 -3.228  -51.211 1.00 84.33  ? 326 GLU B CD  1 
ATOM   9171  O OE1 . GLU C 1 297 ? -29.522 -4.458  -51.403 1.00 84.93  ? 326 GLU B OE1 1 
ATOM   9172  O OE2 . GLU C 1 297 ? -30.678 -2.605  -51.460 1.00 84.21  ? 326 GLU B OE2 1 
ATOM   9173  N N   . LYS C 1 298 ? -28.123 -1.096  -46.333 1.00 50.50  ? 327 LYS B N   1 
ATOM   9174  C CA  . LYS C 1 298 ? -28.813 -0.450  -45.229 1.00 51.26  ? 327 LYS B CA  1 
ATOM   9175  C C   . LYS C 1 298 ? -27.956 0.701   -44.691 1.00 51.05  ? 327 LYS B C   1 
ATOM   9176  O O   . LYS C 1 298 ? -28.480 1.719   -44.227 1.00 47.77  ? 327 LYS B O   1 
ATOM   9177  C CB  . LYS C 1 298 ? -29.218 -1.453  -44.142 1.00 57.43  ? 327 LYS B CB  1 
ATOM   9178  C CG  . LYS C 1 298 ? -30.021 -0.818  -43.018 1.00 67.78  ? 327 LYS B CG  1 
ATOM   9179  C CD  . LYS C 1 298 ? -31.149 0.100   -43.487 1.00 78.34  ? 327 LYS B CD  1 
ATOM   9180  C CE  . LYS C 1 298 ? -31.651 1.021   -42.420 1.00 87.54  ? 327 LYS B CE  1 
ATOM   9181  N NZ  . LYS C 1 298 ? -32.215 0.279   -41.287 1.00 93.16  ? 327 LYS B NZ  1 
ATOM   9182  N N   . LEU C 1 299 ? -26.630 0.542   -44.744 1.00 46.64  ? 328 LEU B N   1 
ATOM   9183  C CA  . LEU C 1 299 ? -25.753 1.603   -44.289 1.00 47.57  ? 328 LEU B CA  1 
ATOM   9184  C C   . LEU C 1 299 ? -25.864 2.796   -45.239 1.00 43.35  ? 328 LEU B C   1 
ATOM   9185  O O   . LEU C 1 299 ? -25.957 3.925   -44.774 1.00 44.27  ? 328 LEU B O   1 
ATOM   9186  C CB  . LEU C 1 299 ? -24.328 1.077   -44.143 1.00 54.07  ? 328 LEU B CB  1 
ATOM   9187  C CG  . LEU C 1 299 ? -23.317 2.027   -43.489 1.00 59.03  ? 328 LEU B CG  1 
ATOM   9188  C CD1 . LEU C 1 299 ? -23.897 2.741   -42.265 1.00 54.05  ? 328 LEU B CD1 1 
ATOM   9189  C CD2 . LEU C 1 299 ? -22.067 1.219   -43.154 1.00 56.39  ? 328 LEU B CD2 1 
ATOM   9190  N N   . ARG C 1 300 ? -25.893 2.561   -46.557 1.00 39.93  ? 329 ARG B N   1 
ATOM   9191  C CA  . ARG C 1 300 ? -26.038 3.640   -47.535 1.00 44.00  ? 329 ARG B CA  1 
ATOM   9192  C C   . ARG C 1 300 ? -27.418 4.305   -47.436 1.00 49.81  ? 329 ARG B C   1 
ATOM   9193  O O   . ARG C 1 300 ? -27.596 5.471   -47.804 1.00 54.96  ? 329 ARG B O   1 
ATOM   9194  C CB  . ARG C 1 300 ? -25.830 3.142   -48.972 1.00 42.81  ? 329 ARG B CB  1 
ATOM   9195  C CG  . ARG C 1 300 ? -25.891 4.198   -50.066 1.00 44.82  ? 329 ARG B CG  1 
ATOM   9196  C CD  . ARG C 1 300 ? -25.769 3.531   -51.445 1.00 44.87  ? 329 ARG B CD  1 
ATOM   9197  N NE  . ARG C 1 300 ? -25.730 4.520   -52.525 1.00 48.32  ? 329 ARG B NE  1 
ATOM   9198  C CZ  . ARG C 1 300 ? -24.633 5.115   -53.021 1.00 52.30  ? 329 ARG B CZ  1 
ATOM   9199  N NH1 . ARG C 1 300 ? -23.420 4.795   -52.592 1.00 53.81  ? 329 ARG B NH1 1 
ATOM   9200  N NH2 . ARG C 1 300 ? -24.751 6.032   -53.967 1.00 55.19  ? 329 ARG B NH2 1 
ATOM   9201  N N   . ASP C 1 301 ? -28.413 3.546   -46.976 1.00 47.63  ? 330 ASP B N   1 
ATOM   9202  C CA  . ASP C 1 301 ? -29.735 4.102   -46.737 1.00 48.02  ? 330 ASP B CA  1 
ATOM   9203  C C   . ASP C 1 301 ? -29.678 5.034   -45.534 1.00 46.37  ? 330 ASP B C   1 
ATOM   9204  O O   . ASP C 1 301 ? -30.249 6.113   -45.587 1.00 41.75  ? 330 ASP B O   1 
ATOM   9205  C CB  . ASP C 1 301 ? -30.767 2.999   -46.544 1.00 57.27  ? 330 ASP B CB  1 
ATOM   9206  C CG  . ASP C 1 301 ? -32.167 3.430   -46.115 1.00 65.57  ? 330 ASP B CG  1 
ATOM   9207  O OD1 . ASP C 1 301 ? -32.770 4.272   -46.824 1.00 71.71  ? 330 ASP B OD1 1 
ATOM   9208  O OD2 . ASP C 1 301 ? -32.664 2.893   -45.092 1.00 74.41  ? 330 ASP B OD2 1 
ATOM   9209  N N   . TYR C 1 302 ? -29.028 4.585   -44.444 1.00 48.01  ? 331 TYR B N   1 
ATOM   9210  C CA  . TYR C 1 302 ? -28.919 5.377   -43.224 1.00 48.12  ? 331 TYR B CA  1 
ATOM   9211  C C   . TYR C 1 302 ? -28.214 6.709   -43.536 1.00 42.81  ? 331 TYR B C   1 
ATOM   9212  O O   . TYR C 1 302 ? -28.645 7.768   -43.103 1.00 44.02  ? 331 TYR B O   1 
ATOM   9213  C CB  . TYR C 1 302 ? -28.292 4.493   -42.131 1.00 48.26  ? 331 TYR B CB  1 
ATOM   9214  C CG  . TYR C 1 302 ? -28.071 5.270   -40.836 1.00 51.77  ? 331 TYR B CG  1 
ATOM   9215  C CD1 . TYR C 1 302 ? -26.914 6.032   -40.648 1.00 49.56  ? 331 TYR B CD1 1 
ATOM   9216  C CD2 . TYR C 1 302 ? -29.041 5.307   -39.838 1.00 50.40  ? 331 TYR B CD2 1 
ATOM   9217  C CE1 . TYR C 1 302 ? -26.722 6.797   -39.508 1.00 43.86  ? 331 TYR B CE1 1 
ATOM   9218  C CE2 . TYR C 1 302 ? -28.857 6.064   -38.688 1.00 52.57  ? 331 TYR B CE2 1 
ATOM   9219  C CZ  . TYR C 1 302 ? -27.696 6.807   -38.526 1.00 48.73  ? 331 TYR B CZ  1 
ATOM   9220  O OH  . TYR C 1 302 ? -27.481 7.547   -37.398 1.00 65.23  ? 331 TYR B OH  1 
ATOM   9221  N N   . ILE C 1 303 ? -27.141 6.680   -44.334 1.00 42.78  ? 332 ILE B N   1 
ATOM   9222  C CA  . ILE C 1 303 ? -26.391 7.889   -44.648 1.00 39.68  ? 332 ILE B CA  1 
ATOM   9223  C C   . ILE C 1 303 ? -27.245 8.866   -45.448 1.00 38.66  ? 332 ILE B C   1 
ATOM   9224  O O   . ILE C 1 303 ? -27.146 10.074  -45.232 1.00 41.84  ? 332 ILE B O   1 
ATOM   9225  C CB  . ILE C 1 303 ? -25.077 7.550   -45.375 1.00 42.99  ? 332 ILE B CB  1 
ATOM   9226  C CG1 . ILE C 1 303 ? -24.170 6.686   -44.502 1.00 44.44  ? 332 ILE B CG1 1 
ATOM   9227  C CG2 . ILE C 1 303 ? -24.359 8.814   -45.844 1.00 47.03  ? 332 ILE B CG2 1 
ATOM   9228  C CD1 . ILE C 1 303 ? -24.009 7.203   -43.083 1.00 42.19  ? 332 ILE B CD1 1 
ATOM   9229  N N   . TRP C 1 304 ? -28.064 8.347   -46.370 1.00 40.18  ? 333 TRP B N   1 
ATOM   9230  C CA  . TRP C 1 304 ? -28.891 9.197   -47.214 1.00 40.47  ? 333 TRP B CA  1 
ATOM   9231  C C   . TRP C 1 304 ? -29.891 9.929   -46.340 1.00 38.15  ? 333 TRP B C   1 
ATOM   9232  O O   . TRP C 1 304 ? -30.087 11.129  -46.498 1.00 41.57  ? 333 TRP B O   1 
ATOM   9233  C CB  . TRP C 1 304 ? -29.599 8.414   -48.335 1.00 43.36  ? 333 TRP B CB  1 
ATOM   9234  C CG  . TRP C 1 304 ? -28.904 8.491   -49.672 1.00 40.26  ? 333 TRP B CG  1 
ATOM   9235  C CD1 . TRP C 1 304 ? -28.459 7.432   -50.411 1.00 47.23  ? 333 TRP B CD1 1 
ATOM   9236  C CD2 . TRP C 1 304 ? -28.568 9.675   -50.439 1.00 44.01  ? 333 TRP B CD2 1 
ATOM   9237  N NE1 . TRP C 1 304 ? -27.852 7.865   -51.561 1.00 44.33  ? 333 TRP B NE1 1 
ATOM   9238  C CE2 . TRP C 1 304 ? -27.908 9.235   -51.613 1.00 42.68  ? 333 TRP B CE2 1 
ATOM   9239  C CE3 . TRP C 1 304 ? -28.739 11.052  -50.250 1.00 44.33  ? 333 TRP B CE3 1 
ATOM   9240  C CZ2 . TRP C 1 304 ? -27.420 10.116  -52.578 1.00 40.43  ? 333 TRP B CZ2 1 
ATOM   9241  C CZ3 . TRP C 1 304 ? -28.265 11.923  -51.211 1.00 45.39  ? 333 TRP B CZ3 1 
ATOM   9242  C CH2 . TRP C 1 304 ? -27.612 11.454  -52.357 1.00 42.74  ? 333 TRP B CH2 1 
ATOM   9243  N N   . ASN C 1 305 ? -30.486 9.210   -45.386 1.00 40.57  ? 334 ASN B N   1 
ATOM   9244  C CA  . ASN C 1 305 ? -31.494 9.813   -44.529 1.00 45.61  ? 334 ASN B CA  1 
ATOM   9245  C C   . ASN C 1 305 ? -30.857 10.916  -43.682 1.00 49.77  ? 334 ASN B C   1 
ATOM   9246  O O   . ASN C 1 305 ? -31.405 12.017  -43.621 1.00 55.68  ? 334 ASN B O   1 
ATOM   9247  C CB  . ASN C 1 305 ? -32.224 8.758   -43.705 1.00 51.28  ? 334 ASN B CB  1 
ATOM   9248  C CG  . ASN C 1 305 ? -33.391 8.180   -44.461 1.00 56.07  ? 334 ASN B CG  1 
ATOM   9249  O OD1 . ASN C 1 305 ? -34.533 8.255   -43.989 1.00 76.03  ? 334 ASN B OD1 1 
ATOM   9250  N ND2 . ASN C 1 305 ? -33.140 7.639   -45.640 1.00 58.41  ? 334 ASN B ND2 1 
ATOM   9251  N N   . THR C 1 306 ? -29.699 10.620  -43.057 1.00 41.83  ? 335 THR B N   1 
ATOM   9252  C CA  . THR C 1 306 ? -28.947 11.609  -42.292 1.00 46.04  ? 335 THR B CA  1 
ATOM   9253  C C   . THR C 1 306 ? -28.775 12.889  -43.108 1.00 46.11  ? 335 THR B C   1 
ATOM   9254  O O   . THR C 1 306 ? -29.003 13.979  -42.592 1.00 41.36  ? 335 THR B O   1 
ATOM   9255  C CB  . THR C 1 306 ? -27.581 11.043  -41.890 1.00 46.87  ? 335 THR B CB  1 
ATOM   9256  O OG1 . THR C 1 306 ? -27.832 9.880   -41.111 1.00 46.82  ? 335 THR B OG1 1 
ATOM   9257  C CG2 . THR C 1 306 ? -26.738 12.014  -41.087 1.00 49.68  ? 335 THR B CG2 1 
ATOM   9258  N N   . LEU C 1 307 ? -28.324 12.742  -44.357 1.00 42.69  ? 336 LEU B N   1 
ATOM   9259  C CA  . LEU C 1 307 ? -28.066 13.877  -45.238 1.00 53.09  ? 336 LEU B CA  1 
ATOM   9260  C C   . LEU C 1 307 ? -29.347 14.591  -45.680 1.00 58.87  ? 336 LEU B C   1 
ATOM   9261  O O   . LEU C 1 307 ? -29.357 15.818  -45.783 1.00 60.65  ? 336 LEU B O   1 
ATOM   9262  C CB  . LEU C 1 307 ? -27.290 13.386  -46.460 1.00 52.75  ? 336 LEU B CB  1 
ATOM   9263  C CG  . LEU C 1 307 ? -25.765 13.335  -46.323 1.00 51.36  ? 336 LEU B CG  1 
ATOM   9264  C CD1 . LEU C 1 307 ? -25.288 12.821  -44.988 1.00 57.40  ? 336 LEU B CD1 1 
ATOM   9265  C CD2 . LEU C 1 307 ? -25.219 12.463  -47.455 1.00 57.92  ? 336 LEU B CD2 1 
ATOM   9266  N N   . ASN C 1 308 ? -30.402 13.830  -46.003 1.00 58.79  ? 337 ASN B N   1 
ATOM   9267  C CA  . ASN C 1 308 ? -31.640 14.425  -46.491 1.00 62.41  ? 337 ASN B CA  1 
ATOM   9268  C C   . ASN C 1 308 ? -32.318 15.168  -45.334 1.00 68.51  ? 337 ASN B C   1 
ATOM   9269  O O   . ASN C 1 308 ? -32.846 16.262  -45.527 1.00 64.84  ? 337 ASN B O   1 
ATOM   9270  C CB  . ASN C 1 308 ? -32.571 13.390  -47.125 1.00 63.25  ? 337 ASN B CB  1 
ATOM   9271  C CG  . ASN C 1 308 ? -31.968 12.602  -48.276 1.00 54.39  ? 337 ASN B CG  1 
ATOM   9272  O OD1 . ASN C 1 308 ? -32.360 11.448  -48.493 1.00 50.00  ? 337 ASN B OD1 1 
ATOM   9273  N ND2 . ASN C 1 308 ? -31.008 13.158  -49.004 1.00 49.88  ? 337 ASN B ND2 1 
ATOM   9274  N N   . SER C 1 309 ? -32.232 14.599  -44.118 1.00 65.82  ? 338 SER B N   1 
ATOM   9275  C CA  . SER C 1 309 ? -32.792 15.195  -42.910 1.00 62.17  ? 338 SER B CA  1 
ATOM   9276  C C   . SER C 1 309 ? -32.044 16.466  -42.499 1.00 60.24  ? 338 SER B C   1 
ATOM   9277  O O   . SER C 1 309 ? -32.429 17.113  -41.525 1.00 55.67  ? 338 SER B O   1 
ATOM   9278  C CB  . SER C 1 309 ? -32.792 14.199  -41.760 1.00 60.88  ? 338 SER B CB  1 
ATOM   9279  O OG  . SER C 1 309 ? -31.490 14.061  -41.193 1.00 62.56  ? 338 SER B OG  1 
ATOM   9280  N N   . GLY C 1 310 ? -30.933 16.764  -43.183 1.00 52.17  ? 339 GLY B N   1 
ATOM   9281  C CA  . GLY C 1 310 ? -30.207 18.010  -42.989 1.00 54.72  ? 339 GLY B CA  1 
ATOM   9282  C C   . GLY C 1 310 ? -28.924 17.873  -42.159 1.00 55.50  ? 339 GLY B C   1 
ATOM   9283  O O   . GLY C 1 310 ? -28.244 18.876  -41.978 1.00 60.16  ? 339 GLY B O   1 
ATOM   9284  N N   . ARG C 1 311 ? -28.588 16.672  -41.646 1.00 53.90  ? 340 ARG B N   1 
ATOM   9285  C CA  . ARG C 1 311 ? -27.486 16.502  -40.693 1.00 53.22  ? 340 ARG B CA  1 
ATOM   9286  C C   . ARG C 1 311 ? -26.195 16.045  -41.383 1.00 52.60  ? 340 ARG B C   1 
ATOM   9287  O O   . ARG C 1 311 ? -26.196 15.629  -42.543 1.00 50.28  ? 340 ARG B O   1 
ATOM   9288  C CB  . ARG C 1 311 ? -27.844 15.458  -39.629 1.00 57.37  ? 340 ARG B CB  1 
ATOM   9289  C CG  . ARG C 1 311 ? -28.892 15.894  -38.615 1.00 66.64  ? 340 ARG B CG  1 
ATOM   9290  C CD  . ARG C 1 311 ? -29.211 14.816  -37.575 1.00 70.41  ? 340 ARG B CD  1 
ATOM   9291  N NE  . ARG C 1 311 ? -29.773 13.606  -38.190 1.00 78.16  ? 340 ARG B NE  1 
ATOM   9292  C CZ  . ARG C 1 311 ? -31.060 13.231  -38.204 1.00 84.55  ? 340 ARG B CZ  1 
ATOM   9293  N NH1 . ARG C 1 311 ? -31.425 12.138  -38.866 1.00 83.06  ? 340 ARG B NH1 1 
ATOM   9294  N NH2 . ARG C 1 311 ? -31.987 13.955  -37.593 1.00 77.76  ? 340 ARG B NH2 1 
ATOM   9295  N N   . VAL C 1 312 ? -25.075 16.080  -40.655 1.00 56.09  ? 341 VAL B N   1 
ATOM   9296  C CA  . VAL C 1 312 ? -23.788 15.751  -41.264 1.00 59.75  ? 341 VAL B CA  1 
ATOM   9297  C C   . VAL C 1 312 ? -23.255 14.431  -40.708 1.00 51.55  ? 341 VAL B C   1 
ATOM   9298  O O   . VAL C 1 312 ? -23.608 13.990  -39.618 1.00 49.97  ? 341 VAL B O   1 
ATOM   9299  C CB  . VAL C 1 312 ? -22.729 16.857  -41.105 1.00 63.76  ? 341 VAL B CB  1 
ATOM   9300  C CG1 . VAL C 1 312 ? -23.177 18.155  -41.769 1.00 61.60  ? 341 VAL B CG1 1 
ATOM   9301  C CG2 . VAL C 1 312 ? -22.343 17.071  -39.644 1.00 61.60  ? 341 VAL B CG2 1 
ATOM   9302  N N   . VAL C 1 313 ? -22.370 13.815  -41.482 1.00 45.25  ? 342 VAL B N   1 
ATOM   9303  C CA  . VAL C 1 313 ? -21.592 12.694  -40.991 1.00 42.76  ? 342 VAL B CA  1 
ATOM   9304  C C   . VAL C 1 313 ? -20.342 13.254  -40.303 1.00 41.01  ? 342 VAL B C   1 
ATOM   9305  O O   . VAL C 1 313 ? -19.439 13.805  -40.938 1.00 43.89  ? 342 VAL B O   1 
ATOM   9306  C CB  . VAL C 1 313 ? -21.270 11.713  -42.141 1.00 42.88  ? 342 VAL B CB  1 
ATOM   9307  C CG1 . VAL C 1 313 ? -20.492 10.476  -41.665 1.00 35.57  ? 342 VAL B CG1 1 
ATOM   9308  C CG2 . VAL C 1 313 ? -22.540 11.303  -42.887 1.00 42.19  ? 342 VAL B CG2 1 
ATOM   9309  N N   . PRO C 1 314 ? -20.220 13.113  -38.968 1.00 42.23  ? 343 PRO B N   1 
ATOM   9310  C CA  . PRO C 1 314 ? -19.057 13.629  -38.256 1.00 42.04  ? 343 PRO B CA  1 
ATOM   9311  C C   . PRO C 1 314 ? -17.820 12.888  -38.740 1.00 43.65  ? 343 PRO B C   1 
ATOM   9312  O O   . PRO C 1 314 ? -17.911 11.706  -39.079 1.00 39.96  ? 343 PRO B O   1 
ATOM   9313  C CB  . PRO C 1 314 ? -19.347 13.361  -36.787 1.00 44.10  ? 343 PRO B CB  1 
ATOM   9314  C CG  . PRO C 1 314 ? -20.364 12.262  -36.803 1.00 43.79  ? 343 PRO B CG  1 
ATOM   9315  C CD  . PRO C 1 314 ? -21.143 12.389  -38.088 1.00 45.20  ? 343 PRO B CD  1 
ATOM   9316  N N   . GLY C 1 315 ? -16.680 13.596  -38.757 1.00 40.66  ? 344 GLY B N   1 
ATOM   9317  C CA  . GLY C 1 315 ? -15.425 13.010  -39.172 1.00 41.70  ? 344 GLY B CA  1 
ATOM   9318  C C   . GLY C 1 315 ? -15.213 13.074  -40.684 1.00 40.04  ? 344 GLY B C   1 
ATOM   9319  O O   . GLY C 1 315 ? -14.146 12.684  -41.160 1.00 43.80  ? 344 GLY B O   1 
ATOM   9320  N N   . TYR C 1 316 ? -16.221 13.529  -41.438 1.00 40.63  ? 345 TYR B N   1 
ATOM   9321  C CA  . TYR C 1 316 ? -16.110 13.714  -42.887 1.00 44.12  ? 345 TYR B CA  1 
ATOM   9322  C C   . TYR C 1 316 ? -16.087 15.223  -43.158 1.00 51.35  ? 345 TYR B C   1 
ATOM   9323  O O   . TYR C 1 316 ? -16.952 15.941  -42.671 1.00 49.14  ? 345 TYR B O   1 
ATOM   9324  C CB  . TYR C 1 316 ? -17.232 12.921  -43.576 1.00 39.73  ? 345 TYR B CB  1 
ATOM   9325  C CG  . TYR C 1 316 ? -16.867 11.443  -43.707 1.00 40.85  ? 345 TYR B CG  1 
ATOM   9326  C CD1 . TYR C 1 316 ? -17.007 10.566  -42.619 1.00 37.56  ? 345 TYR B CD1 1 
ATOM   9327  C CD2 . TYR C 1 316 ? -16.330 10.934  -44.891 1.00 32.38  ? 345 TYR B CD2 1 
ATOM   9328  C CE1 . TYR C 1 316 ? -16.635 9.233   -42.710 1.00 32.32  ? 345 TYR B CE1 1 
ATOM   9329  C CE2 . TYR C 1 316 ? -15.967 9.604   -44.988 1.00 28.62  ? 345 TYR B CE2 1 
ATOM   9330  C CZ  . TYR C 1 316 ? -16.117 8.757   -43.900 1.00 33.25  ? 345 TYR B CZ  1 
ATOM   9331  O OH  . TYR C 1 316 ? -15.713 7.459   -43.958 1.00 33.15  ? 345 TYR B OH  1 
ATOM   9332  N N   . GLY C 1 317 ? -15.048 15.726  -43.843 1.00 50.57  ? 346 GLY B N   1 
ATOM   9333  C CA  . GLY C 1 317 ? -14.920 17.156  -44.112 1.00 51.61  ? 346 GLY B CA  1 
ATOM   9334  C C   . GLY C 1 317 ? -13.736 17.809  -43.387 1.00 54.44  ? 346 GLY B C   1 
ATOM   9335  O O   . GLY C 1 317 ? -13.262 17.333  -42.350 1.00 47.42  ? 346 GLY B O   1 
ATOM   9336  N N   . HIS C 1 318 ? -13.234 18.912  -43.959 1.00 48.16  ? 347 HIS B N   1 
ATOM   9337  C CA  . HIS C 1 318 ? -12.209 19.686  -43.294 1.00 49.12  ? 347 HIS B CA  1 
ATOM   9338  C C   . HIS C 1 318 ? -12.259 21.142  -43.764 1.00 50.45  ? 347 HIS B C   1 
ATOM   9339  O O   . HIS C 1 318 ? -12.764 21.444  -44.845 1.00 46.15  ? 347 HIS B O   1 
ATOM   9340  C CB  . HIS C 1 318 ? -10.845 19.047  -43.551 1.00 46.64  ? 347 HIS B CB  1 
ATOM   9341  C CG  . HIS C 1 318 ? -9.788  19.383  -42.545 1.00 43.78  ? 347 HIS B CG  1 
ATOM   9342  N ND1 . HIS C 1 318 ? -8.790  20.306  -42.782 1.00 40.81  ? 347 HIS B ND1 1 
ATOM   9343  C CD2 . HIS C 1 318 ? -9.523  18.846  -41.336 1.00 42.73  ? 347 HIS B CD2 1 
ATOM   9344  C CE1 . HIS C 1 318 ? -7.972  20.348  -41.741 1.00 43.23  ? 347 HIS B CE1 1 
ATOM   9345  N NE2 . HIS C 1 318 ? -8.392  19.460  -40.852 1.00 47.42  ? 347 HIS B NE2 1 
ATOM   9346  N N   . ALA C 1 319 ? -11.675 22.023  -42.945 1.00 47.71  ? 348 ALA B N   1 
ATOM   9347  C CA  . ALA C 1 319 ? -11.577 23.442  -43.250 1.00 56.50  ? 348 ALA B CA  1 
ATOM   9348  C C   . ALA C 1 319 ? -10.643 23.677  -44.440 1.00 56.60  ? 348 ALA B C   1 
ATOM   9349  O O   . ALA C 1 319 ? -10.801 24.664  -45.151 1.00 55.95  ? 348 ALA B O   1 
ATOM   9350  C CB  . ALA C 1 319 ? -11.114 24.203  -42.020 1.00 54.14  ? 348 ALA B CB  1 
ATOM   9351  N N   . VAL C 1 320 ? -9.658  22.786  -44.648 1.00 56.02  ? 349 VAL B N   1 
ATOM   9352  C CA  . VAL C 1 320 ? -8.655  22.994  -45.685 1.00 49.71  ? 349 VAL B CA  1 
ATOM   9353  C C   . VAL C 1 320 ? -8.508  21.746  -46.563 1.00 48.97  ? 349 VAL B C   1 
ATOM   9354  O O   . VAL C 1 320 ? -8.464  21.859  -47.789 1.00 42.95  ? 349 VAL B O   1 
ATOM   9355  C CB  . VAL C 1 320 ? -7.297  23.414  -45.084 1.00 54.08  ? 349 VAL B CB  1 
ATOM   9356  C CG1 . VAL C 1 320 ? -6.326  23.878  -46.166 1.00 53.03  ? 349 VAL B CG1 1 
ATOM   9357  C CG2 . VAL C 1 320 ? -7.427  24.479  -43.995 1.00 45.95  ? 349 VAL B CG2 1 
ATOM   9358  N N   . LEU C 1 321 ? -8.418  20.552  -45.959 1.00 46.66  ? 350 LEU B N   1 
ATOM   9359  C CA  . LEU C 1 321 ? -8.224  19.335  -46.749 1.00 46.59  ? 350 LEU B CA  1 
ATOM   9360  C C   . LEU C 1 321 ? -9.387  19.179  -47.724 1.00 46.48  ? 350 LEU B C   1 
ATOM   9361  O O   . LEU C 1 321 ? -10.522 19.579  -47.429 1.00 45.42  ? 350 LEU B O   1 
ATOM   9362  C CB  . LEU C 1 321 ? -8.080  18.082  -45.886 1.00 48.80  ? 350 LEU B CB  1 
ATOM   9363  C CG  . LEU C 1 321 ? -6.716  17.910  -45.208 1.00 49.22  ? 350 LEU B CG  1 
ATOM   9364  C CD1 . LEU C 1 321 ? -6.851  17.082  -43.951 1.00 55.27  ? 350 LEU B CD1 1 
ATOM   9365  C CD2 . LEU C 1 321 ? -5.745  17.276  -46.175 1.00 47.58  ? 350 LEU B CD2 1 
ATOM   9366  N N   . ARG C 1 322 ? -9.073  18.578  -48.873 1.00 40.33  ? 351 ARG B N   1 
ATOM   9367  C CA  . ARG C 1 322 ? -10.047 18.318  -49.919 1.00 47.57  ? 351 ARG B CA  1 
ATOM   9368  C C   . ARG C 1 322 ? -10.048 16.836  -50.320 1.00 47.41  ? 351 ARG B C   1 
ATOM   9369  O O   . ARG C 1 322 ? -10.886 16.436  -51.133 1.00 50.21  ? 351 ARG B O   1 
ATOM   9370  C CB  . ARG C 1 322 ? -9.723  19.192  -51.144 1.00 58.03  ? 351 ARG B CB  1 
ATOM   9371  C CG  . ARG C 1 322 ? -9.238  20.614  -50.863 1.00 71.21  ? 351 ARG B CG  1 
ATOM   9372  C CD  . ARG C 1 322 ? -9.007  21.502  -52.114 1.00 81.41  ? 351 ARG B CD  1 
ATOM   9373  N NE  . ARG C 1 322 ? -8.170  20.896  -53.166 1.00 90.55  ? 351 ARG B NE  1 
ATOM   9374  C CZ  . ARG C 1 322 ? -7.656  21.498  -54.248 1.00 91.96  ? 351 ARG B CZ  1 
ATOM   9375  N NH1 . ARG C 1 322 ? -7.002  20.791  -55.164 1.00 89.39  ? 351 ARG B NH1 1 
ATOM   9376  N NH2 . ARG C 1 322 ? -7.798  22.801  -54.418 1.00 92.38  ? 351 ARG B NH2 1 
ATOM   9377  N N   . LYS C 1 323 ? -9.118  16.033  -49.770 1.00 41.06  ? 352 LYS B N   1 
ATOM   9378  C CA  . LYS C 1 323 ? -8.982  14.617  -50.088 1.00 39.14  ? 352 LYS B CA  1 
ATOM   9379  C C   . LYS C 1 323 ? -8.819  13.847  -48.779 1.00 42.32  ? 352 LYS B C   1 
ATOM   9380  O O   . LYS C 1 323 ? -8.858  14.461  -47.706 1.00 35.66  ? 352 LYS B O   1 
ATOM   9381  C CB  . LYS C 1 323 ? -7.798  14.427  -51.041 1.00 47.82  ? 352 LYS B CB  1 
ATOM   9382  C CG  . LYS C 1 323 ? -7.881  15.267  -52.313 1.00 56.25  ? 352 LYS B CG  1 
ATOM   9383  C CD  . LYS C 1 323 ? -9.044  14.909  -53.241 1.00 65.49  ? 352 LYS B CD  1 
ATOM   9384  C CE  . LYS C 1 323 ? -9.590  16.077  -54.035 1.00 73.50  ? 352 LYS B CE  1 
ATOM   9385  N NZ  . LYS C 1 323 ? -8.589  16.868  -54.762 1.00 72.79  ? 352 LYS B NZ  1 
ATOM   9386  N N   . THR C 1 324 ? -8.678  12.511  -48.852 1.00 33.41  ? 353 THR B N   1 
ATOM   9387  C CA  . THR C 1 324 ? -8.568  11.740  -47.615 1.00 39.31  ? 353 THR B CA  1 
ATOM   9388  C C   . THR C 1 324 ? -7.348  12.255  -46.824 1.00 41.23  ? 353 THR B C   1 
ATOM   9389  O O   . THR C 1 324 ? -6.243  12.437  -47.346 1.00 40.05  ? 353 THR B O   1 
ATOM   9390  C CB  . THR C 1 324 ? -8.539  10.238  -47.907 1.00 31.57  ? 353 THR B CB  1 
ATOM   9391  O OG1 . THR C 1 324 ? -9.813  10.016  -48.471 1.00 32.14  ? 353 THR B OG1 1 
ATOM   9392  C CG2 . THR C 1 324 ? -8.669  9.294   -46.722 1.00 28.11  ? 353 THR B CG2 1 
ATOM   9393  N N   . ASP C 1 325 ? -7.595  12.585  -45.554 1.00 35.35  ? 354 ASP B N   1 
ATOM   9394  C CA  . ASP C 1 325 ? -6.549  12.983  -44.639 1.00 33.89  ? 354 ASP B CA  1 
ATOM   9395  C C   . ASP C 1 325 ? -5.567  11.826  -44.558 1.00 31.64  ? 354 ASP B C   1 
ATOM   9396  O O   . ASP C 1 325 ? -5.990  10.716  -44.238 1.00 31.82  ? 354 ASP B O   1 
ATOM   9397  C CB  . ASP C 1 325 ? -7.135  13.243  -43.263 1.00 33.28  ? 354 ASP B CB  1 
ATOM   9398  C CG  . ASP C 1 325 ? -6.216  13.840  -42.211 1.00 32.88  ? 354 ASP B CG  1 
ATOM   9399  O OD1 . ASP C 1 325 ? -4.983  13.902  -42.440 1.00 32.56  ? 354 ASP B OD1 1 
ATOM   9400  O OD2 . ASP C 1 325 ? -6.756  14.293  -41.177 1.00 30.50  ? 354 ASP B OD2 1 
ATOM   9401  N N   . PRO C 1 326 ? -4.273  12.030  -44.882 1.00 32.35  ? 355 PRO B N   1 
ATOM   9402  C CA  . PRO C 1 326 ? -3.254  10.985  -44.675 1.00 33.67  ? 355 PRO B CA  1 
ATOM   9403  C C   . PRO C 1 326 ? -3.207  10.488  -43.230 1.00 32.41  ? 355 PRO B C   1 
ATOM   9404  O O   . PRO C 1 326 ? -2.763  9.378   -42.948 1.00 29.27  ? 355 PRO B O   1 
ATOM   9405  C CB  . PRO C 1 326 ? -1.938  11.621  -45.072 1.00 37.77  ? 355 PRO B CB  1 
ATOM   9406  C CG  . PRO C 1 326 ? -2.319  12.891  -45.856 1.00 41.29  ? 355 PRO B CG  1 
ATOM   9407  C CD  . PRO C 1 326 ? -3.736  13.258  -45.490 1.00 35.47  ? 355 PRO B CD  1 
ATOM   9408  N N   . ARG C 1 327 ? -3.657  11.326  -42.293 1.00 30.52  ? 356 ARG B N   1 
ATOM   9409  C CA  . ARG C 1 327 ? -3.697  10.904  -40.903 1.00 30.50  ? 356 ARG B CA  1 
ATOM   9410  C C   . ARG C 1 327 ? -4.757  9.822   -40.693 1.00 27.48  ? 356 ARG B C   1 
ATOM   9411  O O   . ARG C 1 327 ? -4.574  8.958   -39.834 1.00 32.01  ? 356 ARG B O   1 
ATOM   9412  C CB  . ARG C 1 327 ? -3.853  12.169  -40.054 1.00 33.74  ? 356 ARG B CB  1 
ATOM   9413  C CG  . ARG C 1 327 ? -2.733  13.195  -40.225 1.00 32.37  ? 356 ARG B CG  1 
ATOM   9414  C CD  . ARG C 1 327 ? -2.964  14.331  -39.270 1.00 31.04  ? 356 ARG B CD  1 
ATOM   9415  N NE  . ARG C 1 327 ? -4.178  15.022  -39.695 1.00 29.51  ? 356 ARG B NE  1 
ATOM   9416  C CZ  . ARG C 1 327 ? -4.846  15.964  -39.026 1.00 32.70  ? 356 ARG B CZ  1 
ATOM   9417  N NH1 . ARG C 1 327 ? -4.348  16.476  -37.904 1.00 26.33  ? 356 ARG B NH1 1 
ATOM   9418  N NH2 . ARG C 1 327 ? -5.990  16.418  -39.547 1.00 28.56  ? 356 ARG B NH2 1 
ATOM   9419  N N   . TYR C 1 328 ? -5.891  9.888   -41.427 1.00 28.99  ? 357 TYR B N   1 
ATOM   9420  C CA  . TYR C 1 328 ? -6.872  8.794   -41.489 1.00 26.92  ? 357 TYR B CA  1 
ATOM   9421  C C   . TYR C 1 328 ? -6.258  7.516   -42.085 1.00 27.20  ? 357 TYR B C   1 
ATOM   9422  O O   . TYR C 1 328 ? -6.348  6.418   -41.495 1.00 25.82  ? 357 TYR B O   1 
ATOM   9423  C CB  . TYR C 1 328 ? -8.103  9.218   -42.292 1.00 26.38  ? 357 TYR B CB  1 
ATOM   9424  C CG  . TYR C 1 328 ? -9.231  8.216   -42.331 1.00 25.74  ? 357 TYR B CG  1 
ATOM   9425  C CD1 . TYR C 1 328 ? -9.270  7.245   -43.328 1.00 26.88  ? 357 TYR B CD1 1 
ATOM   9426  C CD2 . TYR C 1 328 ? -10.263 8.227   -41.387 1.00 24.58  ? 357 TYR B CD2 1 
ATOM   9427  C CE1 . TYR C 1 328 ? -10.269 6.295   -43.373 1.00 26.43  ? 357 TYR B CE1 1 
ATOM   9428  C CE2 . TYR C 1 328 ? -11.307 7.309   -41.456 1.00 30.92  ? 357 TYR B CE2 1 
ATOM   9429  C CZ  . TYR C 1 328 ? -11.314 6.341   -42.457 1.00 32.43  ? 357 TYR B CZ  1 
ATOM   9430  O OH  . TYR C 1 328 ? -12.306 5.391   -42.522 1.00 29.22  ? 357 TYR B OH  1 
ATOM   9431  N N   . THR C 1 329 ? -5.614  7.645   -43.241 1.00 26.87  ? 358 THR B N   1 
ATOM   9432  C CA  . THR C 1 329 ? -5.049  6.489   -43.932 1.00 28.62  ? 358 THR B CA  1 
ATOM   9433  C C   . THR C 1 329 ? -4.100  5.728   -43.018 1.00 26.69  ? 358 THR B C   1 
ATOM   9434  O O   . THR C 1 329 ? -4.150  4.504   -42.968 1.00 30.66  ? 358 THR B O   1 
ATOM   9435  C CB  . THR C 1 329 ? -4.343  6.938   -45.207 1.00 29.78  ? 358 THR B CB  1 
ATOM   9436  O OG1 . THR C 1 329 ? -5.443  7.508   -45.898 1.00 32.88  ? 358 THR B OG1 1 
ATOM   9437  C CG2 . THR C 1 329 ? -3.770  5.801   -46.037 1.00 30.42  ? 358 THR B CG2 1 
ATOM   9438  N N   . CYS C 1 330 ? -3.243  6.443   -42.278 1.00 30.11  ? 359 CYS B N   1 
ATOM   9439  C CA  . CYS C 1 330 ? -2.301  5.817   -41.362 1.00 34.27  ? 359 CYS B CA  1 
ATOM   9440  C C   . CYS C 1 330 ? -3.034  4.903   -40.411 1.00 32.22  ? 359 CYS B C   1 
ATOM   9441  O O   . CYS C 1 330 ? -2.545  3.834   -40.117 1.00 31.67  ? 359 CYS B O   1 
ATOM   9442  C CB  . CYS C 1 330 ? -1.683  6.795   -40.357 1.00 40.47  ? 359 CYS B CB  1 
ATOM   9443  S SG  . CYS C 1 330 ? -0.471  7.839   -41.159 1.00 64.07  ? 359 CYS B SG  1 
ATOM   9444  N N   . GLN C 1 331 ? -4.157  5.402   -39.869 1.00 31.98  ? 360 GLN B N   1 
ATOM   9445  C CA  . GLN C 1 331 ? -4.855  4.699   -38.801 1.00 35.91  ? 360 GLN B CA  1 
ATOM   9446  C C   . GLN C 1 331 ? -5.608  3.488   -39.345 1.00 34.64  ? 360 GLN B C   1 
ATOM   9447  O O   . GLN C 1 331 ? -5.805  2.497   -38.635 1.00 36.30  ? 360 GLN B O   1 
ATOM   9448  C CB  . GLN C 1 331 ? -5.788  5.681   -38.087 1.00 35.00  ? 360 GLN B CB  1 
ATOM   9449  C CG  . GLN C 1 331 ? -5.029  6.756   -37.312 1.00 38.85  ? 360 GLN B CG  1 
ATOM   9450  C CD  . GLN C 1 331 ? -5.957  7.670   -36.545 1.00 47.17  ? 360 GLN B CD  1 
ATOM   9451  O OE1 . GLN C 1 331 ? -6.658  8.501   -37.126 1.00 52.54  ? 360 GLN B OE1 1 
ATOM   9452  N NE2 . GLN C 1 331 ? -5.981  7.516   -35.231 1.00 47.12  ? 360 GLN B NE2 1 
ATOM   9453  N N   . ARG C 1 332 ? -6.129  3.640   -40.564 1.00 31.46  ? 361 ARG B N   1 
ATOM   9454  C CA  . ARG C 1 332 ? -6.743  2.545   -41.286 1.00 37.02  ? 361 ARG B CA  1 
ATOM   9455  C C   . ARG C 1 332 ? -5.717  1.419   -41.400 1.00 33.18  ? 361 ARG B C   1 
ATOM   9456  O O   . ARG C 1 332 ? -5.990  0.294   -40.986 1.00 32.13  ? 361 ARG B O   1 
ATOM   9457  C CB  . ARG C 1 332 ? -7.266  3.031   -42.649 1.00 41.01  ? 361 ARG B CB  1 
ATOM   9458  C CG  . ARG C 1 332 ? -7.954  1.950   -43.474 1.00 45.21  ? 361 ARG B CG  1 
ATOM   9459  C CD  . ARG C 1 332 ? -8.389  2.459   -44.855 1.00 47.08  ? 361 ARG B CD  1 
ATOM   9460  N NE  . ARG C 1 332 ? -8.999  1.402   -45.675 1.00 42.81  ? 361 ARG B NE  1 
ATOM   9461  C CZ  . ARG C 1 332 ? -10.133 0.740   -45.399 1.00 49.18  ? 361 ARG B CZ  1 
ATOM   9462  N NH1 . ARG C 1 332 ? -10.587 -0.182  -46.225 1.00 50.95  ? 361 ARG B NH1 1 
ATOM   9463  N NH2 . ARG C 1 332 ? -10.824 0.953   -44.290 1.00 44.92  ? 361 ARG B NH2 1 
ATOM   9464  N N   . GLU C 1 333 ? -4.508  1.760   -41.848 1.00 33.21  ? 362 GLU B N   1 
ATOM   9465  C CA  . GLU C 1 333 ? -3.451  0.760   -42.011 1.00 36.98  ? 362 GLU B CA  1 
ATOM   9466  C C   . GLU C 1 333 ? -3.192  0.074   -40.669 1.00 38.17  ? 362 GLU B C   1 
ATOM   9467  O O   . GLU C 1 333 ? -3.106  -1.139  -40.599 1.00 33.59  ? 362 GLU B O   1 
ATOM   9468  C CB  . GLU C 1 333 ? -2.173  1.376   -42.571 1.00 40.63  ? 362 GLU B CB  1 
ATOM   9469  C CG  . GLU C 1 333 ? -2.283  1.795   -44.039 1.00 44.98  ? 362 GLU B CG  1 
ATOM   9470  C CD  . GLU C 1 333 ? -1.122  2.667   -44.529 1.00 50.31  ? 362 GLU B CD  1 
ATOM   9471  O OE1 . GLU C 1 333 ? -0.297  3.111   -43.701 1.00 49.98  ? 362 GLU B OE1 1 
ATOM   9472  O OE2 . GLU C 1 333 ? -1.054  2.958   -45.740 1.00 43.37  ? 362 GLU B OE2 1 
ATOM   9473  N N   . PHE C 1 334 ? -3.073  0.862   -39.595 1.00 34.48  ? 363 PHE B N   1 
ATOM   9474  C CA  . PHE C 1 334 ? -2.845  0.322   -38.271 1.00 32.81  ? 363 PHE B CA  1 
ATOM   9475  C C   . PHE C 1 334 ? -3.924  -0.680  -37.870 1.00 35.07  ? 363 PHE B C   1 
ATOM   9476  O O   . PHE C 1 334 ? -3.589  -1.775  -37.408 1.00 32.57  ? 363 PHE B O   1 
ATOM   9477  C CB  . PHE C 1 334 ? -2.864  1.393   -37.179 1.00 30.49  ? 363 PHE B CB  1 
ATOM   9478  C CG  . PHE C 1 334 ? -2.398  0.821   -35.877 1.00 28.61  ? 363 PHE B CG  1 
ATOM   9479  C CD1 . PHE C 1 334 ? -1.040  0.840   -35.569 1.00 34.17  ? 363 PHE B CD1 1 
ATOM   9480  C CD2 . PHE C 1 334 ? -3.297  0.256   -34.974 1.00 32.31  ? 363 PHE B CD2 1 
ATOM   9481  C CE1 . PHE C 1 334 ? -0.597  0.312   -34.370 1.00 31.18  ? 363 PHE B CE1 1 
ATOM   9482  C CE2 . PHE C 1 334 ? -2.840  -0.258  -33.771 1.00 33.85  ? 363 PHE B CE2 1 
ATOM   9483  C CZ  . PHE C 1 334 ? -1.495  -0.234  -33.477 1.00 31.10  ? 363 PHE B CZ  1 
ATOM   9484  N N   . ALA C 1 335 ? -5.198  -0.292  -38.021 1.00 35.44  ? 364 ALA B N   1 
ATOM   9485  C CA  . ALA C 1 335 ? -6.333  -1.146  -37.685 1.00 36.36  ? 364 ALA B CA  1 
ATOM   9486  C C   . ALA C 1 335 ? -6.354  -2.452  -38.492 1.00 40.68  ? 364 ALA B C   1 
ATOM   9487  O O   . ALA C 1 335 ? -6.633  -3.534  -37.935 1.00 35.18  ? 364 ALA B O   1 
ATOM   9488  C CB  . ALA C 1 335 ? -7.596  -0.384  -37.917 1.00 36.37  ? 364 ALA B CB  1 
ATOM   9489  N N   . LEU C 1 336 ? -6.105  -2.333  -39.802 1.00 33.80  ? 365 LEU B N   1 
ATOM   9490  C CA  . LEU C 1 336 ? -6.096  -3.467  -40.723 1.00 38.15  ? 365 LEU B CA  1 
ATOM   9491  C C   . LEU C 1 336 ? -4.996  -4.456  -40.344 1.00 46.69  ? 365 LEU B C   1 
ATOM   9492  O O   . LEU C 1 336 ? -5.085  -5.639  -40.655 1.00 48.04  ? 365 LEU B O   1 
ATOM   9493  C CB  . LEU C 1 336 ? -5.931  -3.058  -42.185 1.00 37.82  ? 365 LEU B CB  1 
ATOM   9494  C CG  . LEU C 1 336 ? -7.173  -2.493  -42.878 1.00 37.21  ? 365 LEU B CG  1 
ATOM   9495  C CD1 . LEU C 1 336 ? -6.790  -1.921  -44.238 1.00 36.46  ? 365 LEU B CD1 1 
ATOM   9496  C CD2 . LEU C 1 336 ? -8.304  -3.515  -43.087 1.00 39.38  ? 365 LEU B CD2 1 
ATOM   9497  N N   . LYS C 1 337 ? -3.965  -3.992  -39.644 1.00 44.49  ? 366 LYS B N   1 
ATOM   9498  C CA  . LYS C 1 337 ? -2.917  -4.888  -39.210 1.00 45.51  ? 366 LYS B CA  1 
ATOM   9499  C C   . LYS C 1 337 ? -3.283  -5.488  -37.846 1.00 50.47  ? 366 LYS B C   1 
ATOM   9500  O O   . LYS C 1 337 ? -3.001  -6.648  -37.558 1.00 51.08  ? 366 LYS B O   1 
ATOM   9501  C CB  . LYS C 1 337 ? -1.687  -3.983  -39.317 1.00 55.54  ? 366 LYS B CB  1 
ATOM   9502  C CG  . LYS C 1 337 ? -0.300  -4.593  -39.304 1.00 67.21  ? 366 LYS B CG  1 
ATOM   9503  C CD  . LYS C 1 337 ? 0.679   -3.688  -40.051 1.00 78.30  ? 366 LYS B CD  1 
ATOM   9504  C CE  . LYS C 1 337 ? 0.679   -2.242  -39.621 1.00 84.15  ? 366 LYS B CE  1 
ATOM   9505  N NZ  . LYS C 1 337 ? 1.050   -1.316  -40.698 1.00 84.02  ? 366 LYS B NZ  1 
ATOM   9506  N N   . HIS C 1 338 ? -3.920  -4.716  -36.964 1.00 42.17  ? 367 HIS B N   1 
ATOM   9507  C CA  . HIS C 1 338 ? -3.887  -5.113  -35.565 1.00 39.36  ? 367 HIS B CA  1 
ATOM   9508  C C   . HIS C 1 338 ? -5.258  -5.557  -35.086 1.00 37.20  ? 367 HIS B C   1 
ATOM   9509  O O   . HIS C 1 338 ? -5.319  -6.376  -34.166 1.00 49.99  ? 367 HIS B O   1 
ATOM   9510  C CB  . HIS C 1 338 ? -3.192  -4.038  -34.715 1.00 40.48  ? 367 HIS B CB  1 
ATOM   9511  C CG  . HIS C 1 338 ? -1.775  -3.801  -35.126 1.00 39.52  ? 367 HIS B CG  1 
ATOM   9512  N ND1 . HIS C 1 338 ? -0.822  -4.802  -35.102 1.00 44.34  ? 367 HIS B ND1 1 
ATOM   9513  C CD2 . HIS C 1 338 ? -1.148  -2.708  -35.619 1.00 39.65  ? 367 HIS B CD2 1 
ATOM   9514  C CE1 . HIS C 1 338 ? 0.338   -4.325  -35.546 1.00 43.47  ? 367 HIS B CE1 1 
ATOM   9515  N NE2 . HIS C 1 338 ? 0.166   -3.044  -35.859 1.00 40.22  ? 367 HIS B NE2 1 
ATOM   9516  N N   . LEU C 1 339 ? -6.332  -5.027  -35.695 1.00 37.32  ? 368 LEU B N   1 
ATOM   9517  C CA  . LEU C 1 339 ? -7.684  -5.227  -35.185 1.00 40.15  ? 368 LEU B CA  1 
ATOM   9518  C C   . LEU C 1 339 ? -8.709  -5.241  -36.312 1.00 37.04  ? 368 LEU B C   1 
ATOM   9519  O O   . LEU C 1 339 ? -9.795  -4.668  -36.166 1.00 38.94  ? 368 LEU B O   1 
ATOM   9520  C CB  . LEU C 1 339 ? -8.043  -4.165  -34.141 1.00 42.60  ? 368 LEU B CB  1 
ATOM   9521  C CG  . LEU C 1 339 ? -8.111  -2.709  -34.625 1.00 41.50  ? 368 LEU B CG  1 
ATOM   9522  C CD1 . LEU C 1 339 ? -9.307  -1.972  -34.032 1.00 37.24  ? 368 LEU B CD1 1 
ATOM   9523  C CD2 . LEU C 1 339 ? -6.826  -1.989  -34.253 1.00 42.17  ? 368 LEU B CD2 1 
ATOM   9524  N N   . PRO C 1 340 ? -8.416  -5.929  -37.438 1.00 41.52  ? 369 PRO B N   1 
ATOM   9525  C CA  . PRO C 1 340 ? -9.314  -5.944  -38.600 1.00 43.51  ? 369 PRO B CA  1 
ATOM   9526  C C   . PRO C 1 340 ? -10.713 -6.540  -38.413 1.00 45.89  ? 369 PRO B C   1 
ATOM   9527  O O   . PRO C 1 340 ? -11.591 -6.238  -39.216 1.00 42.54  ? 369 PRO B O   1 
ATOM   9528  C CB  . PRO C 1 340 ? -8.514  -6.724  -39.665 1.00 47.41  ? 369 PRO B CB  1 
ATOM   9529  C CG  . PRO C 1 340 ? -7.531  -7.559  -38.882 1.00 49.41  ? 369 PRO B CG  1 
ATOM   9530  C CD  . PRO C 1 340 ? -7.199  -6.740  -37.641 1.00 46.88  ? 369 PRO B CD  1 
ATOM   9531  N N   . ASN C 1 341 ? -10.909 -7.368  -37.364 1.00 47.08  ? 370 ASN B N   1 
ATOM   9532  C CA  . ASN C 1 341 ? -12.182 -8.034  -37.117 1.00 53.36  ? 370 ASN B CA  1 
ATOM   9533  C C   . ASN C 1 341 ? -12.927 -7.391  -35.941 1.00 55.76  ? 370 ASN B C   1 
ATOM   9534  O O   . ASN C 1 341 ? -13.979 -7.886  -35.533 1.00 59.46  ? 370 ASN B O   1 
ATOM   9535  C CB  . ASN C 1 341 ? -12.008 -9.533  -36.883 1.00 56.72  ? 370 ASN B CB  1 
ATOM   9536  C CG  . ASN C 1 341 ? -11.130 -10.199 -37.927 1.00 59.74  ? 370 ASN B CG  1 
ATOM   9537  O OD1 . ASN C 1 341 ? -11.421 -10.136 -39.130 1.00 47.67  ? 370 ASN B OD1 1 
ATOM   9538  N ND2 . ASN C 1 341 ? -10.034 -10.813 -37.497 1.00 58.80  ? 370 ASN B ND2 1 
ATOM   9539  N N   . ASP C 1 342 ? -12.394 -6.285  -35.401 1.00 46.62  ? 371 ASP B N   1 
ATOM   9540  C CA  . ASP C 1 342 ? -13.121 -5.482  -34.429 1.00 45.76  ? 371 ASP B CA  1 
ATOM   9541  C C   . ASP C 1 342 ? -14.334 -4.853  -35.123 1.00 41.52  ? 371 ASP B C   1 
ATOM   9542  O O   . ASP C 1 342 ? -14.203 -4.275  -36.201 1.00 41.30  ? 371 ASP B O   1 
ATOM   9543  C CB  . ASP C 1 342 ? -12.227 -4.453  -33.757 1.00 47.94  ? 371 ASP B CB  1 
ATOM   9544  C CG  . ASP C 1 342 ? -12.977 -3.417  -32.942 1.00 52.44  ? 371 ASP B CG  1 
ATOM   9545  O OD1 . ASP C 1 342 ? -13.282 -3.727  -31.760 1.00 46.33  ? 371 ASP B OD1 1 
ATOM   9546  O OD2 . ASP C 1 342 ? -13.319 -2.350  -33.528 1.00 45.39  ? 371 ASP B OD2 1 
ATOM   9547  N N   . PRO C 1 343 ? -15.555 -5.046  -34.574 1.00 43.27  ? 372 PRO B N   1 
ATOM   9548  C CA  . PRO C 1 343 ? -16.793 -4.555  -35.190 1.00 49.90  ? 372 PRO B CA  1 
ATOM   9549  C C   . PRO C 1 343 ? -16.886 -3.053  -35.445 1.00 49.00  ? 372 PRO B C   1 
ATOM   9550  O O   . PRO C 1 343 ? -17.398 -2.631  -36.482 1.00 40.96  ? 372 PRO B O   1 
ATOM   9551  C CB  . PRO C 1 343 ? -17.848 -4.986  -34.163 1.00 51.50  ? 372 PRO B CB  1 
ATOM   9552  C CG  . PRO C 1 343 ? -17.264 -6.224  -33.535 1.00 49.01  ? 372 PRO B CG  1 
ATOM   9553  C CD  . PRO C 1 343 ? -15.816 -5.862  -33.374 1.00 46.10  ? 372 PRO B CD  1 
ATOM   9554  N N   . MET C 1 344 ? -16.432 -2.250  -34.469 1.00 48.04  ? 373 MET B N   1 
ATOM   9555  C CA  . MET C 1 344 ? -16.524 -0.802  -34.609 1.00 46.29  ? 373 MET B CA  1 
ATOM   9556  C C   . MET C 1 344 ? -15.572 -0.392  -35.721 1.00 34.66  ? 373 MET B C   1 
ATOM   9557  O O   . MET C 1 344 ? -15.920 0.428   -36.555 1.00 40.02  ? 373 MET B O   1 
ATOM   9558  C CB  . MET C 1 344 ? -16.156 -0.067  -33.313 1.00 53.28  ? 373 MET B CB  1 
ATOM   9559  C CG  . MET C 1 344 ? -17.177 -0.189  -32.194 1.00 54.88  ? 373 MET B CG  1 
ATOM   9560  S SD  . MET C 1 344 ? -18.677 0.732   -32.575 1.00 63.03  ? 373 MET B SD  1 
ATOM   9561  C CE  . MET C 1 344 ? -18.033 2.408   -32.609 1.00 62.98  ? 373 MET B CE  1 
ATOM   9562  N N   . PHE C 1 345 ? -14.393 -1.021  -35.768 1.00 38.04  ? 374 PHE B N   1 
ATOM   9563  C CA  . PHE C 1 345 ? -13.464 -0.762  -36.862 1.00 37.12  ? 374 PHE B CA  1 
ATOM   9564  C C   . PHE C 1 345 ? -14.176 -1.082  -38.175 1.00 41.41  ? 374 PHE B C   1 
ATOM   9565  O O   . PHE C 1 345 ? -14.270 -0.216  -39.049 1.00 39.85  ? 374 PHE B O   1 
ATOM   9566  C CB  . PHE C 1 345 ? -12.131 -1.502  -36.808 1.00 38.39  ? 374 PHE B CB  1 
ATOM   9567  C CG  . PHE C 1 345 ? -11.399 -1.398  -38.140 1.00 40.44  ? 374 PHE B CG  1 
ATOM   9568  C CD1 . PHE C 1 345 ? -11.243 -0.171  -38.778 1.00 39.82  ? 374 PHE B CD1 1 
ATOM   9569  C CD2 . PHE C 1 345 ? -10.974 -2.534  -38.814 1.00 44.70  ? 374 PHE B CD2 1 
ATOM   9570  C CE1 . PHE C 1 345 ? -10.655 -0.089  -40.028 1.00 40.48  ? 374 PHE B CE1 1 
ATOM   9571  C CE2 . PHE C 1 345 ? -10.328 -2.439  -40.042 1.00 41.26  ? 374 PHE B CE2 1 
ATOM   9572  C CZ  . PHE C 1 345 ? -10.178 -1.222  -40.644 1.00 43.57  ? 374 PHE B CZ  1 
ATOM   9573  N N   . LYS C 1 346 ? -14.708 -2.314  -38.272 1.00 41.95  ? 375 LYS B N   1 
ATOM   9574  C CA  . LYS C 1 346 ? -15.419 -2.792  -39.456 1.00 46.33  ? 375 LYS B CA  1 
ATOM   9575  C C   . LYS C 1 346 ? -16.473 -1.782  -39.927 1.00 45.89  ? 375 LYS B C   1 
ATOM   9576  O O   . LYS C 1 346 ? -16.650 -1.574  -41.130 1.00 43.71  ? 375 LYS B O   1 
ATOM   9577  C CB  . LYS C 1 346 ? -16.118 -4.137  -39.198 1.00 50.67  ? 375 LYS B CB  1 
ATOM   9578  C CG  . LYS C 1 346 ? -15.314 -5.412  -39.472 1.00 58.56  ? 375 LYS B CG  1 
ATOM   9579  C CD  . LYS C 1 346 ? -16.227 -6.481  -40.074 1.00 71.68  ? 375 LYS B CD  1 
ATOM   9580  C CE  . LYS C 1 346 ? -15.750 -7.901  -40.078 1.00 74.66  ? 375 LYS B CE  1 
ATOM   9581  N NZ  . LYS C 1 346 ? -15.919 -8.477  -38.743 1.00 77.22  ? 375 LYS B NZ  1 
ATOM   9582  N N   . LEU C 1 347 ? -17.178 -1.154  -38.972 1.00 44.79  ? 376 LEU B N   1 
ATOM   9583  C CA  . LEU C 1 347 ? -18.131 -0.112  -39.302 1.00 38.32  ? 376 LEU B CA  1 
ATOM   9584  C C   . LEU C 1 347 ? -17.376 1.097   -39.853 1.00 37.94  ? 376 LEU B C   1 
ATOM   9585  O O   . LEU C 1 347 ? -17.759 1.679   -40.873 1.00 33.34  ? 376 LEU B O   1 
ATOM   9586  C CB  . LEU C 1 347 ? -18.973 0.250   -38.078 1.00 41.29  ? 376 LEU B CB  1 
ATOM   9587  C CG  . LEU C 1 347 ? -20.006 1.364   -38.269 1.00 41.36  ? 376 LEU B CG  1 
ATOM   9588  C CD1 . LEU C 1 347 ? -21.088 0.939   -39.257 1.00 47.16  ? 376 LEU B CD1 1 
ATOM   9589  C CD2 . LEU C 1 347 ? -20.583 1.737   -36.916 1.00 42.47  ? 376 LEU B CD2 1 
ATOM   9590  N N   . VAL C 1 348 ? -16.293 1.498   -39.186 1.00 39.20  ? 377 VAL B N   1 
ATOM   9591  C CA  . VAL C 1 348 ? -15.586 2.682   -39.667 1.00 42.94  ? 377 VAL B CA  1 
ATOM   9592  C C   . VAL C 1 348 ? -15.172 2.465   -41.133 1.00 37.57  ? 377 VAL B C   1 
ATOM   9593  O O   . VAL C 1 348 ? -15.334 3.377   -41.958 1.00 34.17  ? 377 VAL B O   1 
ATOM   9594  C CB  . VAL C 1 348 ? -14.417 3.113   -38.749 1.00 39.88  ? 377 VAL B CB  1 
ATOM   9595  C CG1 . VAL C 1 348 ? -13.383 3.965   -39.469 1.00 40.87  ? 377 VAL B CG1 1 
ATOM   9596  C CG2 . VAL C 1 348 ? -14.932 3.856   -37.523 1.00 38.85  ? 377 VAL B CG2 1 
ATOM   9597  N N   . ALA C 1 349 ? -14.686 1.253   -41.472 1.00 35.67  ? 378 ALA B N   1 
ATOM   9598  C CA  . ALA C 1 349 ? -14.213 0.955   -42.826 1.00 36.09  ? 378 ALA B CA  1 
ATOM   9599  C C   . ALA C 1 349 ? -15.355 0.884   -43.854 1.00 36.49  ? 378 ALA B C   1 
ATOM   9600  O O   . ALA C 1 349 ? -15.266 1.433   -44.963 1.00 36.46  ? 378 ALA B O   1 
ATOM   9601  C CB  . ALA C 1 349 ? -13.405 -0.328  -42.783 1.00 39.29  ? 378 ALA B CB  1 
ATOM   9602  N N   . GLN C 1 350 ? -16.464 0.237   -43.492 1.00 40.56  ? 379 GLN B N   1 
ATOM   9603  C CA  . GLN C 1 350 ? -17.675 0.313   -44.299 1.00 45.95  ? 379 GLN B CA  1 
ATOM   9604  C C   . GLN C 1 350 ? -18.072 1.755   -44.624 1.00 38.66  ? 379 GLN B C   1 
ATOM   9605  O O   . GLN C 1 350 ? -18.494 2.043   -45.733 1.00 37.46  ? 379 GLN B O   1 
ATOM   9606  C CB  . GLN C 1 350 ? -18.899 -0.254  -43.591 1.00 54.39  ? 379 GLN B CB  1 
ATOM   9607  C CG  . GLN C 1 350 ? -19.116 -1.749  -43.767 1.00 65.37  ? 379 GLN B CG  1 
ATOM   9608  C CD  . GLN C 1 350 ? -20.481 -2.161  -43.261 1.00 66.84  ? 379 GLN B CD  1 
ATOM   9609  O OE1 . GLN C 1 350 ? -20.747 -2.158  -42.050 1.00 58.00  ? 379 GLN B OE1 1 
ATOM   9610  N NE2 . GLN C 1 350 ? -21.365 -2.499  -44.191 1.00 64.66  ? 379 GLN B NE2 1 
ATOM   9611  N N   . LEU C 1 351 ? -18.014 2.654   -43.640 1.00 37.54  ? 380 LEU B N   1 
ATOM   9612  C CA  . LEU C 1 351 ? -18.382 4.045   -43.879 1.00 43.60  ? 380 LEU B CA  1 
ATOM   9613  C C   . LEU C 1 351 ? -17.427 4.709   -44.887 1.00 39.00  ? 380 LEU B C   1 
ATOM   9614  O O   . LEU C 1 351 ? -17.832 5.551   -45.700 1.00 36.50  ? 380 LEU B O   1 
ATOM   9615  C CB  . LEU C 1 351 ? -18.402 4.745   -42.516 1.00 45.85  ? 380 LEU B CB  1 
ATOM   9616  C CG  . LEU C 1 351 ? -19.725 5.330   -42.000 1.00 43.93  ? 380 LEU B CG  1 
ATOM   9617  C CD1 . LEU C 1 351 ? -21.032 4.766   -42.491 1.00 46.64  ? 380 LEU B CD1 1 
ATOM   9618  C CD2 . LEU C 1 351 ? -19.650 5.217   -40.488 1.00 43.90  ? 380 LEU B CD2 1 
ATOM   9619  N N   . TYR C 1 352 ? -16.138 4.336   -44.850 1.00 40.64  ? 381 TYR B N   1 
ATOM   9620  C CA  . TYR C 1 352 ? -15.163 4.885   -45.789 1.00 40.67  ? 381 TYR B CA  1 
ATOM   9621  C C   . TYR C 1 352 ? -15.569 4.514   -47.221 1.00 39.74  ? 381 TYR B C   1 
ATOM   9622  O O   . TYR C 1 352 ? -15.347 5.293   -48.128 1.00 34.86  ? 381 TYR B O   1 
ATOM   9623  C CB  . TYR C 1 352 ? -13.723 4.423   -45.509 1.00 38.01  ? 381 TYR B CB  1 
ATOM   9624  C CG  . TYR C 1 352 ? -12.638 5.054   -46.382 1.00 43.06  ? 381 TYR B CG  1 
ATOM   9625  C CD1 . TYR C 1 352 ? -12.618 6.425   -46.632 1.00 40.98  ? 381 TYR B CD1 1 
ATOM   9626  C CD2 . TYR C 1 352 ? -11.606 4.288   -46.935 1.00 42.72  ? 381 TYR B CD2 1 
ATOM   9627  C CE1 . TYR C 1 352 ? -11.626 7.014   -47.401 1.00 38.95  ? 381 TYR B CE1 1 
ATOM   9628  C CE2 . TYR C 1 352 ? -10.613 4.870   -47.718 1.00 44.13  ? 381 TYR B CE2 1 
ATOM   9629  C CZ  . TYR C 1 352 ? -10.631 6.233   -47.970 1.00 40.52  ? 381 TYR B CZ  1 
ATOM   9630  O OH  . TYR C 1 352 ? -9.663  6.853   -48.736 1.00 43.00  ? 381 TYR B OH  1 
ATOM   9631  N N   . LYS C 1 353 ? -16.189 3.341   -47.428 1.00 48.13  ? 382 LYS B N   1 
ATOM   9632  C CA  . LYS C 1 353 ? -16.538 2.914   -48.784 1.00 53.98  ? 382 LYS B CA  1 
ATOM   9633  C C   . LYS C 1 353 ? -17.850 3.520   -49.284 1.00 42.12  ? 382 LYS B C   1 
ATOM   9634  O O   . LYS C 1 353 ? -18.082 3.552   -50.481 1.00 46.27  ? 382 LYS B O   1 
ATOM   9635  C CB  . LYS C 1 353 ? -16.584 1.390   -48.938 1.00 59.27  ? 382 LYS B CB  1 
ATOM   9636  C CG  . LYS C 1 353 ? -15.197 0.742   -49.021 1.00 75.09  ? 382 LYS B CG  1 
ATOM   9637  C CD  . LYS C 1 353 ? -15.068 -0.374  -50.060 1.00 88.25  ? 382 LYS B CD  1 
ATOM   9638  C CE  . LYS C 1 353 ? -16.060 -1.503  -49.905 1.00 94.24  ? 382 LYS B CE  1 
ATOM   9639  N NZ  . LYS C 1 353 ? -17.385 -1.256  -50.488 1.00 89.38  ? 382 LYS B NZ  1 
ATOM   9640  N N   . ILE C 1 354 ? -18.696 3.987   -48.369 1.00 41.05  ? 383 ILE B N   1 
ATOM   9641  C CA  . ILE C 1 354 ? -20.079 4.355   -48.636 1.00 40.72  ? 383 ILE B CA  1 
ATOM   9642  C C   . ILE C 1 354 ? -20.229 5.880   -48.559 1.00 36.74  ? 383 ILE B C   1 
ATOM   9643  O O   . ILE C 1 354 ? -20.745 6.507   -49.479 1.00 34.15  ? 383 ILE B O   1 
ATOM   9644  C CB  . ILE C 1 354 ? -20.986 3.602   -47.629 1.00 40.97  ? 383 ILE B CB  1 
ATOM   9645  C CG1 . ILE C 1 354 ? -21.125 2.103   -47.987 1.00 47.97  ? 383 ILE B CG1 1 
ATOM   9646  C CG2 . ILE C 1 354 ? -22.363 4.248   -47.479 1.00 40.97  ? 383 ILE B CG2 1 
ATOM   9647  C CD1 . ILE C 1 354 ? -21.627 1.206   -46.855 1.00 45.39  ? 383 ILE B CD1 1 
ATOM   9648  N N   . VAL C 1 355 ? -19.720 6.497   -47.475 1.00 33.58  ? 384 VAL B N   1 
ATOM   9649  C CA  . VAL C 1 355 ? -20.043 7.883   -47.182 1.00 34.31  ? 384 VAL B CA  1 
ATOM   9650  C C   . VAL C 1 355 ? -19.478 8.800   -48.273 1.00 35.86  ? 384 VAL B C   1 
ATOM   9651  O O   . VAL C 1 355 ? -20.167 9.701   -48.731 1.00 32.10  ? 384 VAL B O   1 
ATOM   9652  C CB  . VAL C 1 355 ? -19.579 8.343   -45.784 1.00 33.79  ? 384 VAL B CB  1 
ATOM   9653  C CG1 . VAL C 1 355 ? -19.685 9.856   -45.643 1.00 35.15  ? 384 VAL B CG1 1 
ATOM   9654  C CG2 . VAL C 1 355 ? -20.371 7.644   -44.693 1.00 36.46  ? 384 VAL B CG2 1 
ATOM   9655  N N   . PRO C 1 356 ? -18.204 8.662   -48.710 1.00 38.70  ? 385 PRO B N   1 
ATOM   9656  C CA  . PRO C 1 356 ? -17.681 9.561   -49.729 1.00 39.19  ? 385 PRO B CA  1 
ATOM   9657  C C   . PRO C 1 356 ? -18.533 9.506   -50.989 1.00 37.87  ? 385 PRO B C   1 
ATOM   9658  O O   . PRO C 1 356 ? -18.863 10.540  -51.553 1.00 36.49  ? 385 PRO B O   1 
ATOM   9659  C CB  . PRO C 1 356 ? -16.243 9.109   -49.935 1.00 39.67  ? 385 PRO B CB  1 
ATOM   9660  C CG  . PRO C 1 356 ? -15.912 8.394   -48.640 1.00 43.69  ? 385 PRO B CG  1 
ATOM   9661  C CD  . PRO C 1 356 ? -17.207 7.679   -48.261 1.00 42.67  ? 385 PRO B CD  1 
ATOM   9662  N N   . ASN C 1 357 ? -18.919 8.297   -51.386 1.00 41.20  ? 386 ASN B N   1 
ATOM   9663  C CA  . ASN C 1 357 ? -19.713 8.114   -52.595 1.00 47.59  ? 386 ASN B CA  1 
ATOM   9664  C C   . ASN C 1 357 ? -21.069 8.810   -52.491 1.00 41.31  ? 386 ASN B C   1 
ATOM   9665  O O   . ASN C 1 357 ? -21.515 9.410   -53.450 1.00 42.11  ? 386 ASN B O   1 
ATOM   9666  C CB  . ASN C 1 357 ? -19.853 6.651   -52.999 1.00 51.35  ? 386 ASN B CB  1 
ATOM   9667  C CG  . ASN C 1 357 ? -19.026 6.366   -54.232 1.00 59.89  ? 386 ASN B CG  1 
ATOM   9668  O OD1 . ASN C 1 357 ? -19.593 6.257   -55.322 1.00 61.09  ? 386 ASN B OD1 1 
ATOM   9669  N ND2 . ASN C 1 357 ? -17.704 6.308   -54.095 1.00 64.07  ? 386 ASN B ND2 1 
ATOM   9670  N N   . VAL C 1 358 ? -21.733 8.720   -51.344 1.00 41.72  ? 387 VAL B N   1 
ATOM   9671  C CA  . VAL C 1 358 ? -23.034 9.343   -51.183 1.00 40.38  ? 387 VAL B CA  1 
ATOM   9672  C C   . VAL C 1 358 ? -22.865 10.855  -51.231 1.00 39.38  ? 387 VAL B C   1 
ATOM   9673  O O   . VAL C 1 358 ? -23.686 11.542  -51.820 1.00 44.96  ? 387 VAL B O   1 
ATOM   9674  C CB  . VAL C 1 358 ? -23.740 8.909   -49.890 1.00 38.65  ? 387 VAL B CB  1 
ATOM   9675  C CG1 . VAL C 1 358 ? -24.972 9.756   -49.619 1.00 43.84  ? 387 VAL B CG1 1 
ATOM   9676  C CG2 . VAL C 1 358 ? -24.101 7.433   -49.931 1.00 41.72  ? 387 VAL B CG2 1 
ATOM   9677  N N   . LEU C 1 359 ? -21.809 11.374  -50.597 1.00 45.05  ? 388 LEU B N   1 
ATOM   9678  C CA  . LEU C 1 359 ? -21.611 12.818  -50.533 1.00 47.80  ? 388 LEU B CA  1 
ATOM   9679  C C   . LEU C 1 359 ? -21.282 13.358  -51.917 1.00 41.60  ? 388 LEU B C   1 
ATOM   9680  O O   . LEU C 1 359 ? -21.535 14.524  -52.177 1.00 43.95  ? 388 LEU B O   1 
ATOM   9681  C CB  . LEU C 1 359 ? -20.523 13.222  -49.534 1.00 48.07  ? 388 LEU B CB  1 
ATOM   9682  C CG  . LEU C 1 359 ? -20.924 13.129  -48.061 1.00 48.23  ? 388 LEU B CG  1 
ATOM   9683  C CD1 . LEU C 1 359 ? -19.678 13.260  -47.172 1.00 43.42  ? 388 LEU B CD1 1 
ATOM   9684  C CD2 . LEU C 1 359 ? -22.000 14.166  -47.709 1.00 45.49  ? 388 LEU B CD2 1 
ATOM   9685  N N   . LEU C 1 360 ? -20.662 12.522  -52.758 1.00 43.14  ? 389 LEU B N   1 
ATOM   9686  C CA  . LEU C 1 360 ? -20.356 12.899  -54.129 1.00 46.27  ? 389 LEU B CA  1 
ATOM   9687  C C   . LEU C 1 360 ? -21.640 12.942  -54.955 1.00 48.34  ? 389 LEU B C   1 
ATOM   9688  O O   . LEU C 1 360 ? -21.917 13.935  -55.637 1.00 43.99  ? 389 LEU B O   1 
ATOM   9689  C CB  . LEU C 1 360 ? -19.300 11.955  -54.698 1.00 48.19  ? 389 LEU B CB  1 
ATOM   9690  C CG  . LEU C 1 360 ? -17.862 12.256  -54.251 1.00 53.31  ? 389 LEU B CG  1 
ATOM   9691  C CD1 . LEU C 1 360 ? -16.905 11.068  -54.493 1.00 57.11  ? 389 LEU B CD1 1 
ATOM   9692  C CD2 . LEU C 1 360 ? -17.329 13.523  -54.940 1.00 50.68  ? 389 LEU B CD2 1 
ATOM   9693  N N   . GLU C 1 361 ? -22.465 11.900  -54.813 1.00 51.44  ? 390 GLU B N   1 
ATOM   9694  C CA  . GLU C 1 361 ? -23.784 11.852  -55.440 1.00 54.30  ? 390 GLU B CA  1 
ATOM   9695  C C   . GLU C 1 361 ? -24.663 13.007  -54.967 1.00 51.67  ? 390 GLU B C   1 
ATOM   9696  O O   . GLU C 1 361 ? -25.376 13.609  -55.763 1.00 54.81  ? 390 GLU B O   1 
ATOM   9697  C CB  . GLU C 1 361 ? -24.506 10.542  -55.111 1.00 62.38  ? 390 GLU B CB  1 
ATOM   9698  C CG  . GLU C 1 361 ? -23.900 9.344   -55.831 1.00 62.91  ? 390 GLU B CG  1 
ATOM   9699  C CD  . GLU C 1 361 ? -24.279 9.286   -57.293 1.00 67.70  ? 390 GLU B CD  1 
ATOM   9700  O OE1 . GLU C 1 361 ? -25.091 10.139  -57.738 1.00 60.62  ? 390 GLU B OE1 1 
ATOM   9701  O OE2 . GLU C 1 361 ? -23.774 8.363   -57.967 1.00 72.12  ? 390 GLU B OE2 1 
ATOM   9702  N N   . GLN C 1 362 ? -24.624 13.322  -53.669 1.00 52.14  ? 391 GLN B N   1 
ATOM   9703  C CA  . GLN C 1 362 ? -25.353 14.483  -53.183 1.00 56.14  ? 391 GLN B CA  1 
ATOM   9704  C C   . GLN C 1 362 ? -24.813 15.737  -53.865 1.00 59.12  ? 391 GLN B C   1 
ATOM   9705  O O   . GLN C 1 362 ? -25.585 16.621  -54.216 1.00 60.35  ? 391 GLN B O   1 
ATOM   9706  C CB  . GLN C 1 362 ? -25.270 14.632  -51.665 1.00 57.31  ? 391 GLN B CB  1 
ATOM   9707  C CG  . GLN C 1 362 ? -26.115 15.762  -51.082 1.00 51.86  ? 391 GLN B CG  1 
ATOM   9708  C CD  . GLN C 1 362 ? -25.806 16.009  -49.619 1.00 52.88  ? 391 GLN B CD  1 
ATOM   9709  O OE1 . GLN C 1 362 ? -24.656 16.243  -49.221 1.00 50.27  ? 391 GLN B OE1 1 
ATOM   9710  N NE2 . GLN C 1 362 ? -26.836 15.939  -48.792 1.00 50.75  ? 391 GLN B NE2 1 
ATOM   9711  N N   . GLY C 1 363 ? -23.480 15.822  -53.981 1.00 65.46  ? 392 GLY B N   1 
ATOM   9712  C CA  . GLY C 1 363 ? -22.811 16.879  -54.726 1.00 67.17  ? 392 GLY B CA  1 
ATOM   9713  C C   . GLY C 1 363 ? -22.793 18.244  -54.022 1.00 71.06  ? 392 GLY B C   1 
ATOM   9714  O O   . GLY C 1 363 ? -22.626 19.253  -54.709 1.00 63.34  ? 392 GLY B O   1 
ATOM   9715  N N   . LYS C 1 364 ? -22.912 18.283  -52.677 1.00 63.60  ? 393 LYS B N   1 
ATOM   9716  C CA  . LYS C 1 364 ? -22.900 19.541  -51.929 1.00 69.98  ? 393 LYS B CA  1 
ATOM   9717  C C   . LYS C 1 364 ? -21.530 19.834  -51.307 1.00 66.42  ? 393 LYS B C   1 
ATOM   9718  O O   . LYS C 1 364 ? -21.122 20.992  -51.236 1.00 61.69  ? 393 LYS B O   1 
ATOM   9719  C CB  . LYS C 1 364 ? -23.978 19.587  -50.836 1.00 72.56  ? 393 LYS B CB  1 
ATOM   9720  C CG  . LYS C 1 364 ? -25.408 19.611  -51.370 1.00 76.26  ? 393 LYS B CG  1 
ATOM   9721  C CD  . LYS C 1 364 ? -26.501 19.596  -50.306 1.00 83.69  ? 393 LYS B CD  1 
ATOM   9722  C CE  . LYS C 1 364 ? -27.851 19.468  -50.930 1.00 85.95  ? 393 LYS B CE  1 
ATOM   9723  N NZ  . LYS C 1 364 ? -28.901 19.477  -49.912 1.00 92.55  ? 393 LYS B NZ  1 
ATOM   9724  N N   . ALA C 1 365 ? -20.818 18.786  -50.871 1.00 55.49  ? 394 ALA B N   1 
ATOM   9725  C CA  . ALA C 1 365 ? -19.682 18.954  -49.983 1.00 58.55  ? 394 ALA B CA  1 
ATOM   9726  C C   . ALA C 1 365 ? -18.404 19.222  -50.777 1.00 62.27  ? 394 ALA B C   1 
ATOM   9727  O O   . ALA C 1 365 ? -18.120 18.539  -51.760 1.00 57.11  ? 394 ALA B O   1 
ATOM   9728  C CB  . ALA C 1 365 ? -19.534 17.731  -49.102 1.00 57.98  ? 394 ALA B CB  1 
ATOM   9729  N N   . LYS C 1 366 ? -17.596 20.167  -50.285 1.00 58.64  ? 395 LYS B N   1 
ATOM   9730  C CA  . LYS C 1 366 ? -16.299 20.445  -50.893 1.00 71.67  ? 395 LYS B CA  1 
ATOM   9731  C C   . LYS C 1 366 ? -15.262 19.381  -50.504 1.00 61.58  ? 395 LYS B C   1 
ATOM   9732  O O   . LYS C 1 366 ? -14.270 19.221  -51.207 1.00 57.78  ? 395 LYS B O   1 
ATOM   9733  C CB  . LYS C 1 366 ? -15.819 21.888  -50.664 1.00 78.41  ? 395 LYS B CB  1 
ATOM   9734  C CG  . LYS C 1 366 ? -16.331 22.695  -49.458 1.00 86.43  ? 395 LYS B CG  1 
ATOM   9735  C CD  . LYS C 1 366 ? -15.650 22.431  -48.118 1.00 88.46  ? 395 LYS B CD  1 
ATOM   9736  C CE  . LYS C 1 366 ? -15.858 23.556  -47.139 1.00 79.10  ? 395 LYS B CE  1 
ATOM   9737  N NZ  . LYS C 1 366 ? -15.166 23.304  -45.872 1.00 75.36  ? 395 LYS B NZ  1 
ATOM   9738  N N   . ASN C 1 367 ? -15.490 18.647  -49.399 1.00 60.37  ? 396 ASN B N   1 
ATOM   9739  C CA  . ASN C 1 367 ? -14.616 17.555  -48.982 1.00 53.55  ? 396 ASN B CA  1 
ATOM   9740  C C   . ASN C 1 367 ? -15.461 16.376  -48.485 1.00 50.32  ? 396 ASN B C   1 
ATOM   9741  O O   . ASN C 1 367 ? -15.847 16.305  -47.308 1.00 40.68  ? 396 ASN B O   1 
ATOM   9742  C CB  . ASN C 1 367 ? -13.593 17.970  -47.922 1.00 52.75  ? 396 ASN B CB  1 
ATOM   9743  C CG  . ASN C 1 367 ? -12.722 16.801  -47.528 1.00 50.55  ? 396 ASN B CG  1 
ATOM   9744  O OD1 . ASN C 1 367 ? -12.667 15.806  -48.261 1.00 44.64  ? 396 ASN B OD1 1 
ATOM   9745  N ND2 . ASN C 1 367 ? -12.032 16.896  -46.400 1.00 49.84  ? 396 ASN B ND2 1 
ATOM   9746  N N   . PRO C 1 368 ? -15.722 15.382  -49.361 1.00 43.40  ? 397 PRO B N   1 
ATOM   9747  C CA  . PRO C 1 368 ? -16.493 14.195  -48.991 1.00 44.44  ? 397 PRO B CA  1 
ATOM   9748  C C   . PRO C 1 368 ? -15.657 13.111  -48.298 1.00 41.65  ? 397 PRO B C   1 
ATOM   9749  O O   . PRO C 1 368 ? -16.144 12.017  -47.994 1.00 40.00  ? 397 PRO B O   1 
ATOM   9750  C CB  . PRO C 1 368 ? -17.021 13.751  -50.363 1.00 42.60  ? 397 PRO B CB  1 
ATOM   9751  C CG  . PRO C 1 368 ? -15.914 14.093  -51.318 1.00 43.09  ? 397 PRO B CG  1 
ATOM   9752  C CD  . PRO C 1 368 ? -15.299 15.369  -50.767 1.00 46.72  ? 397 PRO B CD  1 
ATOM   9753  N N   . TRP C 1 369 ? -14.400 13.439  -48.008 1.00 40.25  ? 398 TRP B N   1 
ATOM   9754  C CA  . TRP C 1 369 ? -13.466 12.452  -47.505 1.00 34.82  ? 398 TRP B CA  1 
ATOM   9755  C C   . TRP C 1 369 ? -13.334 12.620  -46.005 1.00 34.47  ? 398 TRP B C   1 
ATOM   9756  O O   . TRP C 1 369 ? -13.599 13.692  -45.471 1.00 36.62  ? 398 TRP B O   1 
ATOM   9757  C CB  . TRP C 1 369 ? -12.132 12.613  -48.226 1.00 36.84  ? 398 TRP B CB  1 
ATOM   9758  C CG  . TRP C 1 369 ? -12.320 12.484  -49.707 1.00 35.67  ? 398 TRP B CG  1 
ATOM   9759  C CD1 . TRP C 1 369 ? -12.380 13.457  -50.657 1.00 42.00  ? 398 TRP B CD1 1 
ATOM   9760  C CD2 . TRP C 1 369 ? -12.551 11.232  -50.380 1.00 41.23  ? 398 TRP B CD2 1 
ATOM   9761  N NE1 . TRP C 1 369 ? -12.584 12.890  -51.889 1.00 45.64  ? 398 TRP B NE1 1 
ATOM   9762  C CE2 . TRP C 1 369 ? -12.710 11.529  -51.747 1.00 43.26  ? 398 TRP B CE2 1 
ATOM   9763  C CE3 . TRP C 1 369 ? -12.631 9.901   -49.949 1.00 41.61  ? 398 TRP B CE3 1 
ATOM   9764  C CZ2 . TRP C 1 369 ? -12.964 10.532  -52.688 1.00 45.68  ? 398 TRP B CZ2 1 
ATOM   9765  C CZ3 . TRP C 1 369 ? -12.865 8.914   -50.881 1.00 43.93  ? 398 TRP B CZ3 1 
ATOM   9766  C CH2 . TRP C 1 369 ? -13.043 9.233   -52.233 1.00 42.86  ? 398 TRP B CH2 1 
ATOM   9767  N N   . PRO C 1 370 ? -12.932 11.561  -45.284 1.00 31.57  ? 399 PRO B N   1 
ATOM   9768  C CA  . PRO C 1 370 ? -12.785 11.657  -43.845 1.00 35.07  ? 399 PRO B CA  1 
ATOM   9769  C C   . PRO C 1 370 ? -11.498 12.378  -43.477 1.00 35.65  ? 399 PRO B C   1 
ATOM   9770  O O   . PRO C 1 370 ? -10.567 12.500  -44.288 1.00 31.95  ? 399 PRO B O   1 
ATOM   9771  C CB  . PRO C 1 370 ? -12.806 10.172  -43.435 1.00 33.51  ? 399 PRO B CB  1 
ATOM   9772  C CG  . PRO C 1 370 ? -12.132 9.462   -44.588 1.00 34.20  ? 399 PRO B CG  1 
ATOM   9773  C CD  . PRO C 1 370 ? -12.561 10.236  -45.819 1.00 33.53  ? 399 PRO B CD  1 
ATOM   9774  N N   . ASN C 1 371 ? -11.479 12.858  -42.239 1.00 33.61  ? 400 ASN B N   1 
ATOM   9775  C CA  . ASN C 1 371 ? -10.275 13.363  -41.624 1.00 32.13  ? 400 ASN B CA  1 
ATOM   9776  C C   . ASN C 1 371 ? -9.928  12.446  -40.447 1.00 37.15  ? 400 ASN B C   1 
ATOM   9777  O O   . ASN C 1 371 ? -10.653 11.499  -40.151 1.00 33.69  ? 400 ASN B O   1 
ATOM   9778  C CB  . ASN C 1 371 ? -10.425 14.827  -41.235 1.00 36.46  ? 400 ASN B CB  1 
ATOM   9779  C CG  . ASN C 1 371 ? -11.450 14.994  -40.139 1.00 38.93  ? 400 ASN B CG  1 
ATOM   9780  O OD1 . ASN C 1 371 ? -11.285 14.417  -39.068 1.00 39.44  ? 400 ASN B OD1 1 
ATOM   9781  N ND2 . ASN C 1 371 ? -12.538 15.703  -40.408 1.00 37.78  ? 400 ASN B ND2 1 
ATOM   9782  N N   . VAL C 1 372 ? -8.833  12.785  -39.755 1.00 33.81  ? 401 VAL B N   1 
ATOM   9783  C CA  . VAL C 1 372 ? -8.228  11.914  -38.778 1.00 32.75  ? 401 VAL B CA  1 
ATOM   9784  C C   . VAL C 1 372 ? -9.268  11.501  -37.746 1.00 33.99  ? 401 VAL B C   1 
ATOM   9785  O O   . VAL C 1 372 ? -9.255  10.373  -37.274 1.00 28.99  ? 401 VAL B O   1 
ATOM   9786  C CB  . VAL C 1 372 ? -7.019  12.628  -38.124 1.00 38.79  ? 401 VAL B CB  1 
ATOM   9787  C CG1 . VAL C 1 372 ? -7.335  14.039  -37.634 1.00 41.18  ? 401 VAL B CG1 1 
ATOM   9788  C CG2 . VAL C 1 372 ? -6.454  11.822  -36.966 1.00 40.37  ? 401 VAL B CG2 1 
ATOM   9789  N N   . ASP C 1 373 ? -10.132 12.437  -37.331 1.00 33.05  ? 402 ASP B N   1 
ATOM   9790  C CA  . ASP C 1 373 ? -10.982 12.191  -36.176 1.00 35.82  ? 402 ASP B CA  1 
ATOM   9791  C C   . ASP C 1 373 ? -12.031 11.122  -36.512 1.00 36.31  ? 402 ASP B C   1 
ATOM   9792  O O   . ASP C 1 373 ? -12.613 10.536  -35.612 1.00 38.06  ? 402 ASP B O   1 
ATOM   9793  C CB  . ASP C 1 373 ? -11.529 13.488  -35.583 1.00 43.86  ? 402 ASP B CB  1 
ATOM   9794  C CG  . ASP C 1 373 ? -10.505 14.524  -35.106 1.00 49.86  ? 402 ASP B CG  1 
ATOM   9795  O OD1 . ASP C 1 373 ? -9.727  14.252  -34.142 1.00 49.56  ? 402 ASP B OD1 1 
ATOM   9796  O OD2 . ASP C 1 373 ? -10.468 15.619  -35.719 1.00 50.51  ? 402 ASP B OD2 1 
ATOM   9797  N N   . ALA C 1 374 ? -12.214 10.794  -37.805 1.00 35.90  ? 403 ALA B N   1 
ATOM   9798  C CA  . ALA C 1 374 ? -13.119 9.719   -38.170 1.00 36.79  ? 403 ALA B CA  1 
ATOM   9799  C C   . ALA C 1 374 ? -12.596 8.357   -37.703 1.00 33.76  ? 403 ALA B C   1 
ATOM   9800  O O   . ALA C 1 374 ? -13.401 7.463   -37.450 1.00 34.29  ? 403 ALA B O   1 
ATOM   9801  C CB  . ALA C 1 374 ? -13.425 9.751   -39.643 1.00 35.51  ? 403 ALA B CB  1 
ATOM   9802  N N   . HIS C 1 375 ? -11.275 8.203   -37.505 1.00 33.77  ? 404 HIS B N   1 
ATOM   9803  C CA  . HIS C 1 375 ? -10.689 6.886   -37.275 1.00 30.80  ? 404 HIS B CA  1 
ATOM   9804  C C   . HIS C 1 375 ? -10.198 6.660   -35.840 1.00 37.48  ? 404 HIS B C   1 
ATOM   9805  O O   . HIS C 1 375 ? -9.952  5.507   -35.453 1.00 35.54  ? 404 HIS B O   1 
ATOM   9806  C CB  . HIS C 1 375 ? -9.498  6.661   -38.205 1.00 30.71  ? 404 HIS B CB  1 
ATOM   9807  C CG  . HIS C 1 375 ? -9.472  5.279   -38.740 1.00 34.63  ? 404 HIS B CG  1 
ATOM   9808  N ND1 . HIS C 1 375 ? -9.366  4.173   -37.921 1.00 39.69  ? 404 HIS B ND1 1 
ATOM   9809  C CD2 . HIS C 1 375 ? -9.616  4.814   -39.983 1.00 33.26  ? 404 HIS B CD2 1 
ATOM   9810  C CE1 . HIS C 1 375 ? -9.426  3.074   -38.677 1.00 34.52  ? 404 HIS B CE1 1 
ATOM   9811  N NE2 . HIS C 1 375 ? -9.594  3.452   -39.929 1.00 34.33  ? 404 HIS B NE2 1 
ATOM   9812  N N   . SER C 1 376 ? -10.007 7.736   -35.058 1.00 33.80  ? 405 SER B N   1 
ATOM   9813  C CA  . SER C 1 376 ? -9.115  7.665   -33.906 1.00 33.35  ? 405 SER B CA  1 
ATOM   9814  C C   . SER C 1 376 ? -9.739  6.889   -32.750 1.00 34.62  ? 405 SER B C   1 
ATOM   9815  O O   . SER C 1 376 ? -9.083  6.032   -32.129 1.00 32.64  ? 405 SER B O   1 
ATOM   9816  C CB  . SER C 1 376 ? -8.683  9.039   -33.461 1.00 37.71  ? 405 SER B CB  1 
ATOM   9817  O OG  . SER C 1 376 ? -7.926  9.678   -34.479 1.00 34.97  ? 405 SER B OG  1 
ATOM   9818  N N   . GLY C 1 377 ? -11.003 7.224   -32.483 1.00 32.58  ? 406 GLY B N   1 
ATOM   9819  C CA  . GLY C 1 377 ? -11.757 6.716   -31.353 1.00 32.47  ? 406 GLY B CA  1 
ATOM   9820  C C   . GLY C 1 377 ? -11.806 5.192   -31.300 1.00 32.80  ? 406 GLY B C   1 
ATOM   9821  O O   . GLY C 1 377 ? -11.622 4.610   -30.232 1.00 38.02  ? 406 GLY B O   1 
ATOM   9822  N N   . VAL C 1 378 ? -12.050 4.564   -32.454 1.00 39.61  ? 407 VAL B N   1 
ATOM   9823  C CA  . VAL C 1 378 ? -12.268 3.124   -32.503 1.00 39.72  ? 407 VAL B CA  1 
ATOM   9824  C C   . VAL C 1 378 ? -10.969 2.412   -32.135 1.00 36.72  ? 407 VAL B C   1 
ATOM   9825  O O   . VAL C 1 378 ? -11.009 1.441   -31.380 1.00 40.00  ? 407 VAL B O   1 
ATOM   9826  C CB  . VAL C 1 378 ? -12.911 2.664   -33.826 1.00 36.28  ? 407 VAL B CB  1 
ATOM   9827  C CG1 . VAL C 1 378 ? -14.251 3.361   -34.010 1.00 33.65  ? 407 VAL B CG1 1 
ATOM   9828  C CG2 . VAL C 1 378 ? -12.038 2.871   -35.048 1.00 39.25  ? 407 VAL B CG2 1 
ATOM   9829  N N   . LEU C 1 379 ? -9.818  3.003   -32.496 1.00 36.50  ? 408 LEU B N   1 
ATOM   9830  C CA  . LEU C 1 379 ? -8.521  2.474   -32.091 1.00 35.90  ? 408 LEU B CA  1 
ATOM   9831  C C   . LEU C 1 379 ? -8.335  2.554   -30.577 1.00 35.64  ? 408 LEU B C   1 
ATOM   9832  O O   . LEU C 1 379 ? -8.031  1.565   -29.927 1.00 34.02  ? 408 LEU B O   1 
ATOM   9833  C CB  . LEU C 1 379 ? -7.405  3.191   -32.839 1.00 39.36  ? 408 LEU B CB  1 
ATOM   9834  C CG  . LEU C 1 379 ? -7.563  3.227   -34.360 1.00 38.18  ? 408 LEU B CG  1 
ATOM   9835  C CD1 . LEU C 1 379 ? -6.271  3.559   -35.053 1.00 38.91  ? 408 LEU B CD1 1 
ATOM   9836  C CD2 . LEU C 1 379 ? -8.101  1.936   -34.880 1.00 42.41  ? 408 LEU B CD2 1 
ATOM   9837  N N   . LEU C 1 380 ? -8.539  3.726   -29.991 1.00 33.46  ? 409 LEU B N   1 
ATOM   9838  C CA  . LEU C 1 380 ? -8.331  3.867   -28.570 1.00 34.54  ? 409 LEU B CA  1 
ATOM   9839  C C   . LEU C 1 380 ? -9.251  2.932   -27.772 1.00 33.29  ? 409 LEU B C   1 
ATOM   9840  O O   . LEU C 1 380 ? -8.826  2.360   -26.764 1.00 31.92  ? 409 LEU B O   1 
ATOM   9841  C CB  . LEU C 1 380 ? -8.578  5.324   -28.182 1.00 34.04  ? 409 LEU B CB  1 
ATOM   9842  C CG  . LEU C 1 380 ? -7.585  6.353   -28.735 1.00 37.80  ? 409 LEU B CG  1 
ATOM   9843  C CD1 . LEU C 1 380 ? -8.081  7.722   -28.242 1.00 38.15  ? 409 LEU B CD1 1 
ATOM   9844  C CD2 . LEU C 1 380 ? -6.159  6.072   -28.338 1.00 31.63  ? 409 LEU B CD2 1 
ATOM   9845  N N   . GLN C 1 381 ? -10.526 2.888   -28.161 1.00 39.11  ? 410 GLN B N   1 
ATOM   9846  C CA  . GLN C 1 381 ? -11.563 2.162   -27.445 1.00 40.21  ? 410 GLN B CA  1 
ATOM   9847  C C   . GLN C 1 381 ? -11.228 0.672   -27.449 1.00 40.61  ? 410 GLN B C   1 
ATOM   9848  O O   . GLN C 1 381 ? -11.469 -0.026  -26.461 1.00 44.68  ? 410 GLN B O   1 
ATOM   9849  C CB  . GLN C 1 381 ? -12.935 2.395   -28.079 1.00 42.09  ? 410 GLN B CB  1 
ATOM   9850  C CG  . GLN C 1 381 ? -14.065 1.990   -27.147 1.00 47.23  ? 410 GLN B CG  1 
ATOM   9851  C CD  . GLN C 1 381 ? -15.441 2.005   -27.778 1.00 49.42  ? 410 GLN B CD  1 
ATOM   9852  O OE1 . GLN C 1 381 ? -15.762 1.203   -28.661 1.00 51.92  ? 410 GLN B OE1 1 
ATOM   9853  N NE2 . GLN C 1 381 ? -16.277 2.912   -27.306 1.00 46.51  ? 410 GLN B NE2 1 
ATOM   9854  N N   . TYR C 1 382 ? -10.634 0.214   -28.555 1.00 36.55  ? 411 TYR B N   1 
ATOM   9855  C CA  . TYR C 1 382 ? -10.225 -1.176  -28.731 1.00 37.40  ? 411 TYR B CA  1 
ATOM   9856  C C   . TYR C 1 382 ? -9.194  -1.606  -27.682 1.00 40.02  ? 411 TYR B C   1 
ATOM   9857  O O   . TYR C 1 382 ? -9.259  -2.738  -27.205 1.00 35.87  ? 411 TYR B O   1 
ATOM   9858  C CB  . TYR C 1 382 ? -9.691  -1.402  -30.146 1.00 39.93  ? 411 TYR B CB  1 
ATOM   9859  C CG  . TYR C 1 382 ? -9.278  -2.849  -30.382 1.00 44.58  ? 411 TYR B CG  1 
ATOM   9860  C CD1 . TYR C 1 382 ? -10.213 -3.817  -30.703 1.00 37.16  ? 411 TYR B CD1 1 
ATOM   9861  C CD2 . TYR C 1 382 ? -7.949  -3.236  -30.260 1.00 43.22  ? 411 TYR B CD2 1 
ATOM   9862  C CE1 . TYR C 1 382 ? -9.840  -5.136  -30.902 1.00 42.82  ? 411 TYR B CE1 1 
ATOM   9863  C CE2 . TYR C 1 382 ? -7.563  -4.547  -30.457 1.00 47.27  ? 411 TYR B CE2 1 
ATOM   9864  C CZ  . TYR C 1 382 ? -8.516  -5.500  -30.766 1.00 44.25  ? 411 TYR B CZ  1 
ATOM   9865  O OH  . TYR C 1 382 ? -8.103  -6.777  -30.943 1.00 47.82  ? 411 TYR B OH  1 
ATOM   9866  N N   . TYR C 1 383 ? -8.242  -0.730  -27.323 1.00 35.26  ? 412 TYR B N   1 
ATOM   9867  C CA  . TYR C 1 383 ? -7.228  -1.094  -26.352 1.00 34.82  ? 412 TYR B CA  1 
ATOM   9868  C C   . TYR C 1 383 ? -7.702  -0.812  -24.931 1.00 37.69  ? 412 TYR B C   1 
ATOM   9869  O O   . TYR C 1 383 ? -6.935  -0.945  -23.980 1.00 38.18  ? 412 TYR B O   1 
ATOM   9870  C CB  . TYR C 1 383 ? -5.940  -0.353  -26.700 1.00 40.33  ? 412 TYR B CB  1 
ATOM   9871  C CG  . TYR C 1 383 ? -5.351  -0.969  -27.949 1.00 39.46  ? 412 TYR B CG  1 
ATOM   9872  C CD1 . TYR C 1 383 ? -4.742  -2.214  -27.906 1.00 38.64  ? 412 TYR B CD1 1 
ATOM   9873  C CD2 . TYR C 1 383 ? -5.439  -0.330  -29.165 1.00 37.24  ? 412 TYR B CD2 1 
ATOM   9874  C CE1 . TYR C 1 383 ? -4.213  -2.784  -29.051 1.00 40.12  ? 412 TYR B CE1 1 
ATOM   9875  C CE2 . TYR C 1 383 ? -4.920  -0.895  -30.318 1.00 36.72  ? 412 TYR B CE2 1 
ATOM   9876  C CZ  . TYR C 1 383 ? -4.319  -2.138  -30.271 1.00 37.65  ? 412 TYR B CZ  1 
ATOM   9877  O OH  . TYR C 1 383 ? -3.828  -2.695  -31.434 1.00 35.44  ? 412 TYR B OH  1 
ATOM   9878  N N   . GLY C 1 384 ? -8.959  -0.400  -24.780 1.00 35.92  ? 413 GLY B N   1 
ATOM   9879  C CA  . GLY C 1 384 ? -9.549  -0.328  -23.456 1.00 38.68  ? 413 GLY B CA  1 
ATOM   9880  C C   . GLY C 1 384 ? -9.619  1.103   -22.950 1.00 39.69  ? 413 GLY B C   1 
ATOM   9881  O O   . GLY C 1 384 ? -10.126 1.355   -21.849 1.00 35.79  ? 413 GLY B O   1 
ATOM   9882  N N   . MET C 1 385 ? -9.163  2.043   -23.783 1.00 38.71  ? 414 MET B N   1 
ATOM   9883  C CA  . MET C 1 385 ? -9.331  3.440   -23.426 1.00 39.80  ? 414 MET B CA  1 
ATOM   9884  C C   . MET C 1 385 ? -10.683 3.946   -23.904 1.00 40.80  ? 414 MET B C   1 
ATOM   9885  O O   . MET C 1 385 ? -10.780 4.505   -25.000 1.00 37.96  ? 414 MET B O   1 
ATOM   9886  C CB  . MET C 1 385 ? -8.240  4.358   -23.981 1.00 39.72  ? 414 MET B CB  1 
ATOM   9887  C CG  . MET C 1 385 ? -8.414  5.780   -23.434 1.00 44.32  ? 414 MET B CG  1 
ATOM   9888  S SD  . MET C 1 385 ? -6.923  6.743   -23.656 1.00 43.10  ? 414 MET B SD  1 
ATOM   9889  C CE  . MET C 1 385 ? -5.807  6.068   -22.423 1.00 35.26  ? 414 MET B CE  1 
ATOM   9890  N N   . THR C 1 386 ? -11.671 3.838   -22.999 1.00 37.75  ? 415 THR B N   1 
ATOM   9891  C CA  . THR C 1 386 ? -13.059 4.147   -23.286 1.00 40.90  ? 415 THR B CA  1 
ATOM   9892  C C   . THR C 1 386 ? -13.473 5.479   -22.651 1.00 43.65  ? 415 THR B C   1 
ATOM   9893  O O   . THR C 1 386 ? -14.644 5.834   -22.743 1.00 44.83  ? 415 THR B O   1 
ATOM   9894  C CB  . THR C 1 386 ? -13.933 3.024   -22.716 1.00 45.79  ? 415 THR B CB  1 
ATOM   9895  O OG1 . THR C 1 386 ? -13.631 3.046   -21.324 1.00 46.17  ? 415 THR B OG1 1 
ATOM   9896  C CG2 . THR C 1 386 ? -13.628 1.645   -23.282 1.00 46.83  ? 415 THR B CG2 1 
ATOM   9897  N N   . GLU C 1 387 ? -12.554 6.177   -21.960 1.00 40.63  ? 416 GLU B N   1 
ATOM   9898  C CA  . GLU C 1 387 ? -12.875 7.455   -21.334 1.00 37.92  ? 416 GLU B CA  1 
ATOM   9899  C C   . GLU C 1 387 ? -12.729 8.570   -22.372 1.00 40.37  ? 416 GLU B C   1 
ATOM   9900  O O   . GLU C 1 387 ? -11.680 9.205   -22.502 1.00 34.46  ? 416 GLU B O   1 
ATOM   9901  C CB  . GLU C 1 387 ? -12.002 7.681   -20.103 1.00 38.38  ? 416 GLU B CB  1 
ATOM   9902  C CG  . GLU C 1 387 ? -12.101 6.527   -19.111 1.00 40.98  ? 416 GLU B CG  1 
ATOM   9903  C CD  . GLU C 1 387 ? -11.150 5.380   -19.376 1.00 40.20  ? 416 GLU B CD  1 
ATOM   9904  O OE1 . GLU C 1 387 ? -10.500 5.365   -20.444 1.00 39.24  ? 416 GLU B OE1 1 
ATOM   9905  O OE2 . GLU C 1 387 ? -11.062 4.504   -18.484 1.00 40.34  ? 416 GLU B OE2 1 
ATOM   9906  N N   . MET C 1 388 ? -13.804 8.788   -23.131 1.00 39.30  ? 417 MET B N   1 
ATOM   9907  C CA  . MET C 1 388 ? -13.749 9.592   -24.339 1.00 39.55  ? 417 MET B CA  1 
ATOM   9908  C C   . MET C 1 388 ? -13.403 11.042  -24.005 1.00 37.18  ? 417 MET B C   1 
ATOM   9909  O O   . MET C 1 388 ? -12.852 11.741  -24.852 1.00 34.97  ? 417 MET B O   1 
ATOM   9910  C CB  . MET C 1 388 ? -15.083 9.557   -25.085 1.00 41.67  ? 417 MET B CB  1 
ATOM   9911  C CG  . MET C 1 388 ? -15.405 8.225   -25.711 1.00 42.79  ? 417 MET B CG  1 
ATOM   9912  S SD  . MET C 1 388 ? -17.039 8.287   -26.462 1.00 45.00  ? 417 MET B SD  1 
ATOM   9913  C CE  . MET C 1 388 ? -16.693 9.341   -27.859 1.00 50.66  ? 417 MET B CE  1 
ATOM   9914  N N   . ASN C 1 389 ? -13.758 11.489  -22.790 1.00 37.40  ? 418 ASN B N   1 
ATOM   9915  C CA  . ASN C 1 389 ? -13.415 12.827  -22.330 1.00 38.77  ? 418 ASN B CA  1 
ATOM   9916  C C   . ASN C 1 389 ? -11.899 13.068  -22.323 1.00 36.37  ? 418 ASN B C   1 
ATOM   9917  O O   . ASN C 1 389 ? -11.471 14.204  -22.494 1.00 35.80  ? 418 ASN B O   1 
ATOM   9918  C CB  . ASN C 1 389 ? -14.097 13.132  -21.006 1.00 42.27  ? 418 ASN B CB  1 
ATOM   9919  C CG  . ASN C 1 389 ? -15.587 13.234  -21.200 1.00 45.60  ? 418 ASN B CG  1 
ATOM   9920  O OD1 . ASN C 1 389 ? -16.359 12.497  -20.576 1.00 60.45  ? 418 ASN B OD1 1 
ATOM   9921  N ND2 . ASN C 1 389 ? -16.008 14.117  -22.082 1.00 41.22  ? 418 ASN B ND2 1 
ATOM   9922  N N   . TYR C 1 390 ? -11.091 12.009  -22.183 1.00 30.82  ? 419 TYR B N   1 
ATOM   9923  C CA  . TYR C 1 390 ? -9.651  12.130  -22.126 1.00 28.12  ? 419 TYR B CA  1 
ATOM   9924  C C   . TYR C 1 390 ? -8.978  12.235  -23.499 1.00 28.86  ? 419 TYR B C   1 
ATOM   9925  O O   . TYR C 1 390 ? -7.783  12.476  -23.570 1.00 26.18  ? 419 TYR B O   1 
ATOM   9926  C CB  . TYR C 1 390 ? -9.134  10.842  -21.504 1.00 28.86  ? 419 TYR B CB  1 
ATOM   9927  C CG  . TYR C 1 390 ? -7.658  10.906  -21.190 1.00 27.66  ? 419 TYR B CG  1 
ATOM   9928  C CD1 . TYR C 1 390 ? -7.214  11.693  -20.148 1.00 33.35  ? 419 TYR B CD1 1 
ATOM   9929  C CD2 . TYR C 1 390 ? -6.729  10.228  -21.936 1.00 28.24  ? 419 TYR B CD2 1 
ATOM   9930  C CE1 . TYR C 1 390 ? -5.883  11.747  -19.810 1.00 31.01  ? 419 TYR B CE1 1 
ATOM   9931  C CE2 . TYR C 1 390 ? -5.391  10.280  -21.622 1.00 27.88  ? 419 TYR B CE2 1 
ATOM   9932  C CZ  . TYR C 1 390 ? -4.975  11.042  -20.557 1.00 26.33  ? 419 TYR B CZ  1 
ATOM   9933  O OH  . TYR C 1 390 ? -3.682  11.115  -20.219 1.00 26.42  ? 419 TYR B OH  1 
ATOM   9934  N N   . TYR C 1 391 ? -9.668  11.874  -24.576 1.00 30.10  ? 420 TYR B N   1 
ATOM   9935  C CA  . TYR C 1 391 ? -8.991  11.695  -25.857 1.00 34.19  ? 420 TYR B CA  1 
ATOM   9936  C C   . TYR C 1 391 ? -8.276  12.969  -26.323 1.00 34.63  ? 420 TYR B C   1 
ATOM   9937  O O   . TYR C 1 391 ? -7.234  12.887  -26.977 1.00 29.26  ? 420 TYR B O   1 
ATOM   9938  C CB  . TYR C 1 391 ? -9.994  11.266  -26.933 1.00 41.03  ? 420 TYR B CB  1 
ATOM   9939  C CG  . TYR C 1 391 ? -10.609 9.871   -26.775 1.00 41.93  ? 420 TYR B CG  1 
ATOM   9940  C CD1 . TYR C 1 391 ? -10.206 8.997   -25.769 1.00 40.75  ? 420 TYR B CD1 1 
ATOM   9941  C CD2 . TYR C 1 391 ? -11.595 9.422   -27.659 1.00 42.32  ? 420 TYR B CD2 1 
ATOM   9942  C CE1 . TYR C 1 391 ? -10.769 7.734   -25.640 1.00 44.70  ? 420 TYR B CE1 1 
ATOM   9943  C CE2 . TYR C 1 391 ? -12.173 8.163   -27.532 1.00 41.76  ? 420 TYR B CE2 1 
ATOM   9944  C CZ  . TYR C 1 391 ? -11.746 7.312   -26.530 1.00 40.97  ? 420 TYR B CZ  1 
ATOM   9945  O OH  . TYR C 1 391 ? -12.277 6.069   -26.408 1.00 39.57  ? 420 TYR B OH  1 
ATOM   9946  N N   . THR C 1 392 ? -8.856  14.153  -26.027 1.00 31.20  ? 421 THR B N   1 
ATOM   9947  C CA  . THR C 1 392 ? -8.271  15.389  -26.515 1.00 33.77  ? 421 THR B CA  1 
ATOM   9948  C C   . THR C 1 392 ? -6.976  15.657  -25.752 1.00 28.02  ? 421 THR B C   1 
ATOM   9949  O O   . THR C 1 392 ? -6.091  16.305  -26.278 1.00 25.80  ? 421 THR B O   1 
ATOM   9950  C CB  . THR C 1 392 ? -9.283  16.544  -26.461 1.00 35.14  ? 421 THR B CB  1 
ATOM   9951  O OG1 . THR C 1 392 ? -10.460 16.079  -27.115 1.00 36.05  ? 421 THR B OG1 1 
ATOM   9952  C CG2 . THR C 1 392 ? -8.819  17.754  -27.266 1.00 35.90  ? 421 THR B CG2 1 
ATOM   9953  N N   . VAL C 1 393 ? -6.804  15.059  -24.566 1.00 26.64  ? 422 VAL B N   1 
ATOM   9954  C CA  . VAL C 1 393 ? -5.544  15.162  -23.843 1.00 26.99  ? 422 VAL B CA  1 
ATOM   9955  C C   . VAL C 1 393 ? -4.421  14.490  -24.631 1.00 26.05  ? 422 VAL B C   1 
ATOM   9956  O O   . VAL C 1 393 ? -3.319  15.018  -24.672 1.00 28.73  ? 422 VAL B O   1 
ATOM   9957  C CB  . VAL C 1 393 ? -5.633  14.572  -22.419 1.00 30.00  ? 422 VAL B CB  1 
ATOM   9958  C CG1 . VAL C 1 393 ? -4.283  14.475  -21.726 1.00 29.51  ? 422 VAL B CG1 1 
ATOM   9959  C CG2 . VAL C 1 393 ? -6.588  15.375  -21.547 1.00 28.71  ? 422 VAL B CG2 1 
ATOM   9960  N N   . LEU C 1 394 ? -4.703  13.355  -25.275 1.00 27.75  ? 423 LEU B N   1 
ATOM   9961  C CA  . LEU C 1 394 ? -3.719  12.701  -26.131 1.00 27.89  ? 423 LEU B CA  1 
ATOM   9962  C C   . LEU C 1 394 ? -3.365  13.561  -27.346 1.00 25.28  ? 423 LEU B C   1 
ATOM   9963  O O   . LEU C 1 394 ? -2.212  13.598  -27.759 1.00 26.43  ? 423 LEU B O   1 
ATOM   9964  C CB  . LEU C 1 394 ? -4.224  11.341  -26.584 1.00 33.22  ? 423 LEU B CB  1 
ATOM   9965  C CG  . LEU C 1 394 ? -4.565  10.347  -25.465 1.00 35.35  ? 423 LEU B CG  1 
ATOM   9966  C CD1 . LEU C 1 394 ? -5.191  9.091   -26.061 1.00 35.22  ? 423 LEU B CD1 1 
ATOM   9967  C CD2 . LEU C 1 394 ? -3.314  10.025  -24.687 1.00 36.77  ? 423 LEU B CD2 1 
ATOM   9968  N N   . PHE C 1 395 ? -4.356  14.227  -27.934 1.00 26.47  ? 424 PHE B N   1 
ATOM   9969  C CA  . PHE C 1 395 ? -4.099  15.125  -29.056 1.00 27.91  ? 424 PHE B CA  1 
ATOM   9970  C C   . PHE C 1 395 ? -3.199  16.268  -28.589 1.00 29.98  ? 424 PHE B C   1 
ATOM   9971  O O   . PHE C 1 395 ? -2.209  16.598  -29.232 1.00 29.67  ? 424 PHE B O   1 
ATOM   9972  C CB  . PHE C 1 395 ? -5.484  15.525  -29.575 1.00 26.13  ? 424 PHE B CB  1 
ATOM   9973  C CG  . PHE C 1 395 ? -5.574  16.302  -30.878 1.00 27.45  ? 424 PHE B CG  1 
ATOM   9974  C CD1 . PHE C 1 395 ? -4.477  16.884  -31.461 1.00 27.13  ? 424 PHE B CD1 1 
ATOM   9975  C CD2 . PHE C 1 395 ? -6.799  16.454  -31.516 1.00 37.46  ? 424 PHE B CD2 1 
ATOM   9976  C CE1 . PHE C 1 395 ? -4.591  17.606  -32.645 1.00 28.75  ? 424 PHE B CE1 1 
ATOM   9977  C CE2 . PHE C 1 395 ? -6.915  17.186  -32.698 1.00 37.37  ? 424 PHE B CE2 1 
ATOM   9978  C CZ  . PHE C 1 395 ? -5.802  17.775  -33.252 1.00 30.89  ? 424 PHE B CZ  1 
ATOM   9979  N N   . GLY C 1 396 ? -3.536  16.852  -27.434 1.00 31.00  ? 425 GLY B N   1 
ATOM   9980  C CA  . GLY C 1 396 ? -2.708  17.881  -26.831 1.00 31.41  ? 425 GLY B CA  1 
ATOM   9981  C C   . GLY C 1 396 ? -1.259  17.438  -26.624 1.00 30.09  ? 425 GLY B C   1 
ATOM   9982  O O   . GLY C 1 396 ? -0.344  18.163  -26.982 1.00 28.06  ? 425 GLY B O   1 
ATOM   9983  N N   . VAL C 1 397 ? -1.035  16.266  -26.029 1.00 24.60  ? 426 VAL B N   1 
ATOM   9984  C CA  . VAL C 1 397 ? 0.318   15.812  -25.785 1.00 25.98  ? 426 VAL B CA  1 
ATOM   9985  C C   . VAL C 1 397 ? 1.086   15.749  -27.109 1.00 27.07  ? 426 VAL B C   1 
ATOM   9986  O O   . VAL C 1 397 ? 2.269   16.114  -27.170 1.00 25.36  ? 426 VAL B O   1 
ATOM   9987  C CB  . VAL C 1 397 ? 0.396   14.457  -25.072 1.00 27.50  ? 426 VAL B CB  1 
ATOM   9988  C CG1 . VAL C 1 397 ? 1.831   13.996  -25.005 1.00 29.32  ? 426 VAL B CG1 1 
ATOM   9989  C CG2 . VAL C 1 397 ? -0.233  14.465  -23.689 1.00 29.29  ? 426 VAL B CG2 1 
ATOM   9990  N N   . SER C 1 398 ? 0.405   15.309  -28.170 1.00 25.54  ? 427 SER B N   1 
ATOM   9991  C CA  . SER C 1 398 ? 1.013   15.230  -29.492 1.00 29.36  ? 427 SER B CA  1 
ATOM   9992  C C   . SER C 1 398 ? 1.290   16.619  -30.066 1.00 26.25  ? 427 SER B C   1 
ATOM   9993  O O   . SER C 1 398 ? 2.334   16.854  -30.697 1.00 25.62  ? 427 SER B O   1 
ATOM   9994  C CB  . SER C 1 398 ? 0.148   14.436  -30.477 1.00 32.53  ? 427 SER B CB  1 
ATOM   9995  O OG  . SER C 1 398 ? 0.745   14.456  -31.775 1.00 27.18  ? 427 SER B OG  1 
ATOM   9996  N N   . ARG C 1 399 ? 0.320   17.520  -29.877 1.00 26.52  ? 428 ARG B N   1 
ATOM   9997  C CA  . ARG C 1 399 ? 0.352   18.818  -30.537 1.00 27.36  ? 428 ARG B CA  1 
ATOM   9998  C C   . ARG C 1 399 ? 1.523   19.642  -30.012 1.00 23.77  ? 428 ARG B C   1 
ATOM   9999  O O   . ARG C 1 399 ? 2.042   20.525  -30.704 1.00 22.69  ? 428 ARG B O   1 
ATOM   10000 C CB  . ARG C 1 399 ? -1.047  19.440  -30.442 1.00 26.53  ? 428 ARG B CB  1 
ATOM   10001 C CG  . ARG C 1 399 ? -1.262  20.729  -31.220 1.00 25.19  ? 428 ARG B CG  1 
ATOM   10002 C CD  . ARG C 1 399 ? -0.665  20.730  -32.616 1.00 26.99  ? 428 ARG B CD  1 
ATOM   10003 N NE  . ARG C 1 399 ? -1.181  19.776  -33.595 1.00 27.87  ? 428 ARG B NE  1 
ATOM   10004 C CZ  . ARG C 1 399 ? -2.255  19.888  -34.422 1.00 29.13  ? 428 ARG B CZ  1 
ATOM   10005 N NH1 . ARG C 1 399 ? -3.022  20.975  -34.442 1.00 25.36  ? 428 ARG B NH1 1 
ATOM   10006 N NH2 . ARG C 1 399 ? -2.525  18.881  -35.257 1.00 29.68  ? 428 ARG B NH2 1 
ATOM   10007 N N   . ALA C 1 400 ? 1.928   19.327  -28.786 1.00 21.20  ? 429 ALA B N   1 
ATOM   10008 C CA  . ALA C 1 400 ? 3.020   20.010  -28.115 1.00 24.26  ? 429 ALA B CA  1 
ATOM   10009 C C   . ALA C 1 400 ? 4.249   20.008  -29.006 1.00 22.80  ? 429 ALA B C   1 
ATOM   10010 O O   . ALA C 1 400 ? 4.984   20.975  -29.046 1.00 26.40  ? 429 ALA B O   1 
ATOM   10011 C CB  . ALA C 1 400 ? 3.337   19.330  -26.807 1.00 23.18  ? 429 ALA B CB  1 
ATOM   10012 N N   . LEU C 1 401 ? 4.494   18.879  -29.673 1.00 24.28  ? 430 LEU B N   1 
ATOM   10013 C CA  . LEU C 1 401 ? 5.703   18.706  -30.459 1.00 23.14  ? 430 LEU B CA  1 
ATOM   10014 C C   . LEU C 1 401 ? 5.751   19.706  -31.604 1.00 24.26  ? 430 LEU B C   1 
ATOM   10015 O O   . LEU C 1 401 ? 6.796   20.311  -31.850 1.00 24.00  ? 430 LEU B O   1 
ATOM   10016 C CB  . LEU C 1 401 ? 5.781   17.276  -30.993 1.00 25.28  ? 430 LEU B CB  1 
ATOM   10017 C CG  . LEU C 1 401 ? 5.776   16.160  -29.938 1.00 26.06  ? 430 LEU B CG  1 
ATOM   10018 C CD1 . LEU C 1 401 ? 5.609   14.818  -30.614 1.00 26.37  ? 430 LEU B CD1 1 
ATOM   10019 C CD2 . LEU C 1 401 ? 7.025   16.181  -29.055 1.00 29.00  ? 430 LEU B CD2 1 
ATOM   10020 N N   . GLY C 1 402 ? 4.662   19.803  -32.378 1.00 23.95  ? 431 GLY B N   1 
ATOM   10021 C CA  . GLY C 1 402 ? 4.680   20.733  -33.505 1.00 24.27  ? 431 GLY B CA  1 
ATOM   10022 C C   . GLY C 1 402 ? 4.779   22.185  -33.045 1.00 22.55  ? 431 GLY B C   1 
ATOM   10023 O O   . GLY C 1 402 ? 5.610   22.956  -33.507 1.00 24.35  ? 431 GLY B O   1 
ATOM   10024 N N   . VAL C 1 403 ? 3.887   22.579  -32.132 1.00 23.75  ? 432 VAL B N   1 
ATOM   10025 C CA  . VAL C 1 403 ? 3.772   23.986  -31.784 1.00 24.58  ? 432 VAL B CA  1 
ATOM   10026 C C   . VAL C 1 403 ? 5.042   24.431  -31.079 1.00 24.47  ? 432 VAL B C   1 
ATOM   10027 O O   . VAL C 1 403 ? 5.565   25.463  -31.438 1.00 25.88  ? 432 VAL B O   1 
ATOM   10028 C CB  . VAL C 1 403 ? 2.534   24.331  -30.945 1.00 25.09  ? 432 VAL B CB  1 
ATOM   10029 C CG1 . VAL C 1 403 ? 1.264   23.925  -31.671 1.00 28.47  ? 432 VAL B CG1 1 
ATOM   10030 C CG2 . VAL C 1 403 ? 2.581   23.720  -29.553 1.00 25.07  ? 432 VAL B CG2 1 
ATOM   10031 N N   . LEU C 1 404 ? 5.583   23.620  -30.160 1.00 22.24  ? 433 LEU B N   1 
ATOM   10032 C CA  . LEU C 1 404 ? 6.849   23.949  -29.514 1.00 21.06  ? 433 LEU B CA  1 
ATOM   10033 C C   . LEU C 1 404 ? 8.018   23.925  -30.493 1.00 22.86  ? 433 LEU B C   1 
ATOM   10034 O O   . LEU C 1 404 ? 8.937   24.726  -30.343 1.00 25.54  ? 433 LEU B O   1 
ATOM   10035 C CB  . LEU C 1 404 ? 7.166   23.102  -28.288 1.00 20.53  ? 433 LEU B CB  1 
ATOM   10036 C CG  . LEU C 1 404 ? 6.070   23.101  -27.215 1.00 26.63  ? 433 LEU B CG  1 
ATOM   10037 C CD1 . LEU C 1 404 ? 6.439   22.164  -26.094 1.00 28.95  ? 433 LEU B CD1 1 
ATOM   10038 C CD2 . LEU C 1 404 ? 5.795   24.455  -26.674 1.00 26.35  ? 433 LEU B CD2 1 
ATOM   10039 N N   . ALA C 1 405 ? 8.059   23.002  -31.459 1.00 24.98  ? 434 ALA B N   1 
ATOM   10040 C CA  . ALA C 1 405 ? 9.151   23.064  -32.419 1.00 23.33  ? 434 ALA B CA  1 
ATOM   10041 C C   . ALA C 1 405 ? 9.105   24.401  -33.166 1.00 23.08  ? 434 ALA B C   1 
ATOM   10042 O O   . ALA C 1 405 ? 10.142  25.039  -33.338 1.00 26.19  ? 434 ALA B O   1 
ATOM   10043 C CB  . ALA C 1 405 ? 9.061   21.878  -33.358 1.00 29.46  ? 434 ALA B CB  1 
ATOM   10044 N N   . GLN C 1 406 ? 7.913   24.856  -33.578 1.00 23.13  ? 435 GLN B N   1 
ATOM   10045 C CA  . GLN C 1 406 ? 7.777   26.123  -34.305 1.00 25.09  ? 435 GLN B CA  1 
ATOM   10046 C C   . GLN C 1 406 ? 8.087   27.292  -33.356 1.00 27.60  ? 435 GLN B C   1 
ATOM   10047 O O   . GLN C 1 406 ? 8.620   28.323  -33.764 1.00 24.68  ? 435 GLN B O   1 
ATOM   10048 C CB  . GLN C 1 406 ? 6.381   26.419  -34.865 1.00 26.07  ? 435 GLN B CB  1 
ATOM   10049 C CG  . GLN C 1 406 ? 6.199   27.774  -35.556 1.00 25.40  ? 435 GLN B CG  1 
ATOM   10050 C CD  . GLN C 1 406 ? 7.192   28.020  -36.679 1.00 28.98  ? 435 GLN B CD  1 
ATOM   10051 O OE1 . GLN C 1 406 ? 7.510   27.134  -37.482 1.00 34.20  ? 435 GLN B OE1 1 
ATOM   10052 N NE2 . GLN C 1 406 ? 7.811   29.188  -36.694 1.00 34.03  ? 435 GLN B NE2 1 
ATOM   10053 N N   . LEU C 1 407 ? 7.719   27.165  -32.074 1.00 26.49  ? 436 LEU B N   1 
ATOM   10054 C CA  . LEU C 1 407 ? 7.939   28.279  -31.139 1.00 26.92  ? 436 LEU B CA  1 
ATOM   10055 C C   . LEU C 1 407 ? 9.439   28.599  -30.998 1.00 23.22  ? 436 LEU B C   1 
ATOM   10056 O O   . LEU C 1 407 ? 9.846   29.760  -30.986 1.00 27.10  ? 436 LEU B O   1 
ATOM   10057 C CB  . LEU C 1 407 ? 7.292   28.041  -29.782 1.00 26.48  ? 436 LEU B CB  1 
ATOM   10058 C CG  . LEU C 1 407 ? 7.391   29.207  -28.795 1.00 29.80  ? 436 LEU B CG  1 
ATOM   10059 C CD1 . LEU C 1 407 ? 6.520   30.345  -29.308 1.00 29.40  ? 436 LEU B CD1 1 
ATOM   10060 C CD2 . LEU C 1 407 ? 6.967   28.726  -27.442 1.00 32.06  ? 436 LEU B CD2 1 
ATOM   10061 N N   . ILE C 1 408 ? 10.288  27.591  -30.948 1.00 21.77  ? 437 ILE B N   1 
ATOM   10062 C CA  . ILE C 1 408 ? 11.737  27.791  -30.973 1.00 22.52  ? 437 ILE B CA  1 
ATOM   10063 C C   . ILE C 1 408 ? 12.208  28.624  -32.178 1.00 21.90  ? 437 ILE B C   1 
ATOM   10064 O O   . ILE C 1 408 ? 12.995  29.569  -32.033 1.00 22.58  ? 437 ILE B O   1 
ATOM   10065 C CB  . ILE C 1 408 ? 12.434  26.424  -30.924 1.00 24.25  ? 437 ILE B CB  1 
ATOM   10066 C CG1 . ILE C 1 408 ? 12.116  25.731  -29.619 1.00 25.92  ? 437 ILE B CG1 1 
ATOM   10067 C CG2 . ILE C 1 408 ? 13.935  26.549  -31.153 1.00 26.45  ? 437 ILE B CG2 1 
ATOM   10068 C CD1 . ILE C 1 408 ? 12.332  24.242  -29.658 1.00 26.06  ? 437 ILE B CD1 1 
ATOM   10069 N N   . TRP C 1 409 ? 11.725  28.276  -33.364 1.00 23.67  ? 438 TRP B N   1 
ATOM   10070 C CA  . TRP C 1 409 ? 12.031  28.959  -34.621 1.00 21.48  ? 438 TRP B CA  1 
ATOM   10071 C C   . TRP C 1 409 ? 11.473  30.381  -34.674 1.00 21.94  ? 438 TRP B C   1 
ATOM   10072 O O   . TRP C 1 409 ? 12.179  31.289  -35.079 1.00 22.91  ? 438 TRP B O   1 
ATOM   10073 C CB  . TRP C 1 409 ? 11.534  28.078  -35.781 1.00 23.40  ? 438 TRP B CB  1 
ATOM   10074 C CG  . TRP C 1 409 ? 12.544  27.003  -36.088 1.00 28.11  ? 438 TRP B CG  1 
ATOM   10075 C CD1 . TRP C 1 409 ? 12.555  25.689  -35.700 1.00 29.10  ? 438 TRP B CD1 1 
ATOM   10076 C CD2 . TRP C 1 409 ? 13.809  27.257  -36.742 1.00 28.80  ? 438 TRP B CD2 1 
ATOM   10077 N NE1 . TRP C 1 409 ? 13.731  25.107  -36.120 1.00 32.04  ? 438 TRP B NE1 1 
ATOM   10078 C CE2 . TRP C 1 409 ? 14.510  26.043  -36.761 1.00 27.82  ? 438 TRP B CE2 1 
ATOM   10079 C CE3 . TRP C 1 409 ? 14.406  28.399  -37.310 1.00 32.19  ? 438 TRP B CE3 1 
ATOM   10080 C CZ2 . TRP C 1 409 ? 15.777  25.944  -37.330 1.00 29.36  ? 438 TRP B CZ2 1 
ATOM   10081 C CZ3 . TRP C 1 409 ? 15.661  28.299  -37.867 1.00 32.47  ? 438 TRP B CZ3 1 
ATOM   10082 C CH2 . TRP C 1 409 ? 16.336  27.078  -37.870 1.00 31.43  ? 438 TRP B CH2 1 
ATOM   10083 N N   . SER C 1 410 ? 10.199  30.589  -34.320 1.00 21.60  ? 439 SER B N   1 
ATOM   10084 C CA  . SER C 1 410 ? 9.630   31.922  -34.112 1.00 23.51  ? 439 SER B CA  1 
ATOM   10085 C C   . SER C 1 410 ? 10.514  32.869  -33.298 1.00 23.59  ? 439 SER B C   1 
ATOM   10086 O O   . SER C 1 410 ? 10.748  34.002  -33.699 1.00 26.54  ? 439 SER B O   1 
ATOM   10087 C CB  . SER C 1 410 ? 8.235   31.834  -33.507 1.00 23.60  ? 439 SER B CB  1 
ATOM   10088 O OG  . SER C 1 410 ? 7.473   31.135  -34.488 1.00 22.41  ? 439 SER B OG  1 
ATOM   10089 N N   . ARG C 1 411 ? 11.071  32.420  -32.182 1.00 30.49  ? 440 ARG B N   1 
ATOM   10090 C CA  . ARG C 1 411 ? 12.018  33.236  -31.428 1.00 26.20  ? 440 ARG B CA  1 
ATOM   10091 C C   . ARG C 1 411 ? 13.414  33.220  -32.044 1.00 27.72  ? 440 ARG B C   1 
ATOM   10092 O O   . ARG C 1 411 ? 14.078  34.244  -32.045 1.00 27.27  ? 440 ARG B O   1 
ATOM   10093 C CB  . ARG C 1 411 ? 12.081  32.746  -29.992 1.00 26.73  ? 440 ARG B CB  1 
ATOM   10094 C CG  . ARG C 1 411 ? 10.716  32.953  -29.350 1.00 30.93  ? 440 ARG B CG  1 
ATOM   10095 C CD  . ARG C 1 411 ? 9.956   34.308  -29.459 1.00 31.97  ? 440 ARG B CD  1 
ATOM   10096 N NE  . ARG C 1 411 ? 8.697   33.888  -28.816 1.00 62.59  ? 440 ARG B NE  1 
ATOM   10097 C CZ  . ARG C 1 411 ? 8.574   33.578  -27.479 1.00 62.87  ? 440 ARG B CZ  1 
ATOM   10098 N NH1 . ARG C 1 411 ? 9.452   34.057  -26.604 1.00 76.12  ? 440 ARG B NH1 1 
ATOM   10099 N NH2 . ARG C 1 411 ? 7.548   32.884  -26.979 1.00 36.18  ? 440 ARG B NH2 1 
ATOM   10100 N N   . ALA C 1 412 ? 13.860  32.105  -32.653 1.00 25.25  ? 441 ALA B N   1 
ATOM   10101 C CA  . ALA C 1 412 ? 15.181  32.143  -33.256 1.00 23.94  ? 441 ALA B CA  1 
ATOM   10102 C C   . ALA C 1 412 ? 15.179  33.169  -34.370 1.00 24.93  ? 441 ALA B C   1 
ATOM   10103 O O   . ALA C 1 412 ? 16.147  33.906  -34.533 1.00 25.50  ? 441 ALA B O   1 
ATOM   10104 C CB  . ALA C 1 412 ? 15.582  30.792  -33.788 1.00 27.38  ? 441 ALA B CB  1 
ATOM   10105 N N   . LEU C 1 413 ? 14.050  33.266  -35.099 1.00 25.35  ? 442 LEU B N   1 
ATOM   10106 C CA  . LEU C 1 413 ? 13.960  34.174  -36.225 1.00 23.56  ? 442 LEU B CA  1 
ATOM   10107 C C   . LEU C 1 413 ? 13.474  35.579  -35.875 1.00 27.91  ? 442 LEU B C   1 
ATOM   10108 O O   . LEU C 1 413 ? 13.431  36.434  -36.748 1.00 35.32  ? 442 LEU B O   1 
ATOM   10109 C CB  . LEU C 1 413 ? 13.029  33.491  -37.206 1.00 25.11  ? 442 LEU B CB  1 
ATOM   10110 C CG  . LEU C 1 413 ? 13.625  32.242  -37.857 1.00 25.69  ? 442 LEU B CG  1 
ATOM   10111 C CD1 . LEU C 1 413 ? 12.564  31.661  -38.741 1.00 25.05  ? 442 LEU B CD1 1 
ATOM   10112 C CD2 . LEU C 1 413 ? 14.928  32.476  -38.615 1.00 25.33  ? 442 LEU B CD2 1 
ATOM   10113 N N   . GLY C 1 414 ? 13.132  35.848  -34.616 1.00 30.62  ? 443 GLY B N   1 
ATOM   10114 C CA  . GLY C 1 414 ? 12.679  37.172  -34.208 1.00 29.99  ? 443 GLY B CA  1 
ATOM   10115 C C   . GLY C 1 414 ? 11.316  37.531  -34.811 1.00 29.72  ? 443 GLY B C   1 
ATOM   10116 O O   . GLY C 1 414 ? 11.054  38.682  -35.124 1.00 31.87  ? 443 GLY B O   1 
ATOM   10117 N N   . PHE C 1 415 ? 10.427  36.561  -34.984 1.00 29.56  ? 444 PHE B N   1 
ATOM   10118 C CA  . PHE C 1 415 ? 9.067   36.926  -35.342 1.00 32.03  ? 444 PHE B CA  1 
ATOM   10119 C C   . PHE C 1 415 ? 8.536   37.891  -34.263 1.00 29.41  ? 444 PHE B C   1 
ATOM   10120 O O   . PHE C 1 415 ? 8.726   37.671  -33.071 1.00 24.41  ? 444 PHE B O   1 
ATOM   10121 C CB  . PHE C 1 415 ? 8.147   35.725  -35.578 1.00 32.31  ? 444 PHE B CB  1 
ATOM   10122 C CG  . PHE C 1 415 ? 8.454   34.799  -36.755 1.00 31.65  ? 444 PHE B CG  1 
ATOM   10123 C CD1 . PHE C 1 415 ? 9.422   35.093  -37.690 1.00 31.01  ? 444 PHE B CD1 1 
ATOM   10124 C CD2 . PHE C 1 415 ? 7.792   33.591  -36.875 1.00 33.57  ? 444 PHE B CD2 1 
ATOM   10125 C CE1 . PHE C 1 415 ? 9.686   34.225  -38.738 1.00 37.94  ? 444 PHE B CE1 1 
ATOM   10126 C CE2 . PHE C 1 415 ? 8.067   32.725  -37.915 1.00 33.49  ? 444 PHE B CE2 1 
ATOM   10127 C CZ  . PHE C 1 415 ? 8.998   33.056  -38.861 1.00 33.62  ? 444 PHE B CZ  1 
ATOM   10128 N N   . PRO C 1 416 ? 7.937   39.033  -34.667 1.00 28.31  ? 445 PRO B N   1 
ATOM   10129 C CA  . PRO C 1 416 ? 7.403   40.026  -33.733 1.00 29.41  ? 445 PRO B CA  1 
ATOM   10130 C C   . PRO C 1 416 ? 6.010   39.684  -33.254 1.00 27.41  ? 445 PRO B C   1 
ATOM   10131 O O   . PRO C 1 416 ? 5.431   38.718  -33.699 1.00 32.46  ? 445 PRO B O   1 
ATOM   10132 C CB  . PRO C 1 416 ? 7.385   41.281  -34.592 1.00 27.26  ? 445 PRO B CB  1 
ATOM   10133 C CG  . PRO C 1 416 ? 6.961   40.731  -35.908 1.00 31.69  ? 445 PRO B CG  1 
ATOM   10134 C CD  . PRO C 1 416 ? 7.859   39.496  -36.061 1.00 30.38  ? 445 PRO B CD  1 
ATOM   10135 N N   . LEU C 1 417 ? 5.468   40.561  -32.411 1.00 27.27  ? 446 LEU B N   1 
ATOM   10136 C CA  . LEU C 1 417 ? 4.125   40.447  -31.900 1.00 25.32  ? 446 LEU B CA  1 
ATOM   10137 C C   . LEU C 1 417 ? 3.143   40.294  -33.050 1.00 24.57  ? 446 LEU B C   1 
ATOM   10138 O O   . LEU C 1 417 ? 3.231   40.995  -34.042 1.00 21.85  ? 446 LEU B O   1 
ATOM   10139 C CB  . LEU C 1 417 ? 3.936   41.730  -31.102 1.00 29.43  ? 446 LEU B CB  1 
ATOM   10140 C CG  . LEU C 1 417 ? 2.655   41.836  -30.276 1.00 30.49  ? 446 LEU B CG  1 
ATOM   10141 C CD1 . LEU C 1 417 ? 2.660   40.925  -29.096 1.00 32.73  ? 446 LEU B CD1 1 
ATOM   10142 C CD2 . LEU C 1 417 ? 2.478   43.263  -29.787 1.00 35.27  ? 446 LEU B CD2 1 
ATOM   10143 N N   . GLU C 1 418 ? 2.252   39.311  -32.949 1.00 21.26  ? 447 GLU B N   1 
ATOM   10144 C CA  . GLU C 1 418 ? 1.195   39.147  -33.923 1.00 23.51  ? 447 GLU B CA  1 
ATOM   10145 C C   . GLU C 1 418 ? 0.120   40.174  -33.563 1.00 30.39  ? 447 GLU B C   1 
ATOM   10146 O O   . GLU C 1 418 ? -0.324  40.145  -32.433 1.00 28.32  ? 447 GLU B O   1 
ATOM   10147 C CB  . GLU C 1 418 ? 0.587   37.748  -33.889 1.00 23.65  ? 447 GLU B CB  1 
ATOM   10148 C CG  . GLU C 1 418 ? -0.485  37.556  -34.958 1.00 24.27  ? 447 GLU B CG  1 
ATOM   10149 C CD  . GLU C 1 418 ? -1.077  36.169  -35.139 1.00 33.78  ? 447 GLU B CD  1 
ATOM   10150 O OE1 . GLU C 1 418 ? -0.293  35.272  -35.511 1.00 31.09  ? 447 GLU B OE1 1 
ATOM   10151 O OE2 . GLU C 1 418 ? -2.340  36.013  -35.048 1.00 34.49  ? 447 GLU B OE2 1 
ATOM   10152 N N   . ARG C 1 419 ? -0.160  41.137  -34.465 1.00 28.53  ? 448 ARG B N   1 
ATOM   10153 C CA  . ARG C 1 419 ? -1.026  42.272  -34.165 1.00 31.96  ? 448 ARG B CA  1 
ATOM   10154 C C   . ARG C 1 419 ? -1.712  42.754  -35.445 1.00 32.33  ? 448 ARG B C   1 
ATOM   10155 O O   . ARG C 1 419 ? -1.361  43.784  -36.036 1.00 36.82  ? 448 ARG B O   1 
ATOM   10156 C CB  . ARG C 1 419 ? -0.279  43.406  -33.456 1.00 37.41  ? 448 ARG B CB  1 
ATOM   10157 C CG  . ARG C 1 419 ? -1.059  44.699  -33.175 1.00 47.36  ? 448 ARG B CG  1 
ATOM   10158 C CD  . ARG C 1 419 ? -2.398  44.538  -32.468 1.00 47.23  ? 448 ARG B CD  1 
ATOM   10159 N NE  . ARG C 1 419 ? -3.051  45.698  -31.825 1.00 42.86  ? 448 ARG B NE  1 
ATOM   10160 C CZ  . ARG C 1 419 ? -4.317  46.096  -32.039 1.00 46.07  ? 448 ARG B CZ  1 
ATOM   10161 N NH1 . ARG C 1 419 ? -4.934  45.796  -33.184 1.00 46.17  ? 448 ARG B NH1 1 
ATOM   10162 N NH2 . ARG C 1 419 ? -4.958  46.864  -31.142 1.00 37.68  ? 448 ARG B NH2 1 
ATOM   10163 N N   . PRO C 1 420 ? -2.740  42.033  -35.907 1.00 32.00  ? 449 PRO B N   1 
ATOM   10164 C CA  . PRO C 1 420 ? -3.498  42.456  -37.067 1.00 32.32  ? 449 PRO B CA  1 
ATOM   10165 C C   . PRO C 1 420 ? -4.363  43.608  -36.599 1.00 33.55  ? 449 PRO B C   1 
ATOM   10166 O O   . PRO C 1 420 ? -4.475  43.874  -35.400 1.00 28.87  ? 449 PRO B O   1 
ATOM   10167 C CB  . PRO C 1 420 ? -4.304  41.232  -37.485 1.00 33.32  ? 449 PRO B CB  1 
ATOM   10168 C CG  . PRO C 1 420 ? -4.544  40.520  -36.168 1.00 34.89  ? 449 PRO B CG  1 
ATOM   10169 C CD  . PRO C 1 420 ? -3.263  40.782  -35.336 1.00 35.45  ? 449 PRO B CD  1 
ATOM   10170 N N   . LYS C 1 421 ? -4.899  44.302  -37.596 1.00 29.86  ? 450 LYS B N   1 
ATOM   10171 C CA  . LYS C 1 421 ? -5.837  45.387  -37.388 1.00 30.41  ? 450 LYS B CA  1 
ATOM   10172 C C   . LYS C 1 421 ? -7.224  44.775  -37.426 1.00 25.70  ? 450 LYS B C   1 
ATOM   10173 O O   . LYS C 1 421 ? -7.494  43.926  -38.276 1.00 25.25  ? 450 LYS B O   1 
ATOM   10174 C CB  . LYS C 1 421 ? -5.599  46.366  -38.553 1.00 35.37  ? 450 LYS B CB  1 
ATOM   10175 C CG  . LYS C 1 421 ? -6.445  47.611  -38.518 1.00 38.65  ? 450 LYS B CG  1 
ATOM   10176 C CD  . LYS C 1 421 ? -6.365  48.390  -37.213 1.00 48.02  ? 450 LYS B CD  1 
ATOM   10177 C CE  . LYS C 1 421 ? -7.358  49.521  -37.205 1.00 53.10  ? 450 LYS B CE  1 
ATOM   10178 N NZ  . LYS C 1 421 ? -7.240  50.255  -35.946 1.00 55.80  ? 450 LYS B NZ  1 
ATOM   10179 N N   . SER C 1 422 ? -8.056  45.125  -36.448 1.00 26.00  ? 451 SER B N   1 
ATOM   10180 C CA  . SER C 1 422 ? -9.460  44.786  -36.509 1.00 27.43  ? 451 SER B CA  1 
ATOM   10181 C C   . SER C 1 422 ? -10.267 45.996  -36.980 1.00 28.12  ? 451 SER B C   1 
ATOM   10182 O O   . SER C 1 422 ? -9.822  47.124  -36.843 1.00 28.98  ? 451 SER B O   1 
ATOM   10183 C CB  . SER C 1 422 ? -9.948  44.289  -35.163 1.00 28.28  ? 451 SER B CB  1 
ATOM   10184 O OG  . SER C 1 422 ? -9.983  45.340  -34.214 1.00 26.41  ? 451 SER B OG  1 
ATOM   10185 N N   . MET C 1 423 ? -11.496 45.733  -37.444 1.00 31.84  ? 452 MET B N   1 
ATOM   10186 C CA  . MET C 1 423 ? -12.476 46.750  -37.784 1.00 32.49  ? 452 MET B CA  1 
ATOM   10187 C C   . MET C 1 423 ? -13.819 46.320  -37.231 1.00 28.54  ? 452 MET B C   1 
ATOM   10188 O O   . MET C 1 423 ? -14.069 45.127  -37.126 1.00 27.87  ? 452 MET B O   1 
ATOM   10189 C CB  . MET C 1 423 ? -12.675 46.833  -39.290 1.00 35.62  ? 452 MET B CB  1 
ATOM   10190 C CG  . MET C 1 423 ? -11.389 46.981  -40.054 1.00 42.90  ? 452 MET B CG  1 
ATOM   10191 S SD  . MET C 1 423 ? -10.787 48.633  -39.709 1.00 48.14  ? 452 MET B SD  1 
ATOM   10192 C CE  . MET C 1 423 ? -11.813 49.517  -40.895 1.00 49.15  ? 452 MET B CE  1 
ATOM   10193 N N   . SER C 1 424 ? -14.653 47.283  -36.850 1.00 25.25  ? 453 SER B N   1 
ATOM   10194 C CA  . SER C 1 424 ? -16.061 47.004  -36.598 1.00 29.86  ? 453 SER B CA  1 
ATOM   10195 C C   . SER C 1 424 ? -16.788 46.897  -37.932 1.00 31.04  ? 453 SER B C   1 
ATOM   10196 O O   . SER C 1 424 ? -16.230 47.260  -38.979 1.00 34.61  ? 453 SER B O   1 
ATOM   10197 C CB  . SER C 1 424 ? -16.693 48.119  -35.757 1.00 32.30  ? 453 SER B CB  1 
ATOM   10198 O OG  . SER C 1 424 ? -16.607 49.343  -36.473 1.00 32.33  ? 453 SER B OG  1 
ATOM   10199 N N   . THR C 1 425 ? -18.044 46.447  -37.898 1.00 34.77  ? 454 THR B N   1 
ATOM   10200 C CA  . THR C 1 425 ? -18.847 46.403  -39.117 1.00 38.62  ? 454 THR B CA  1 
ATOM   10201 C C   . THR C 1 425 ? -19.033 47.835  -39.632 1.00 38.62  ? 454 THR B C   1 
ATOM   10202 O O   . THR C 1 425 ? -18.904 48.080  -40.834 1.00 36.70  ? 454 THR B O   1 
ATOM   10203 C CB  . THR C 1 425 ? -20.185 45.701  -38.866 1.00 38.20  ? 454 THR B CB  1 
ATOM   10204 O OG1 . THR C 1 425 ? -19.879 44.356  -38.502 1.00 33.83  ? 454 THR B OG1 1 
ATOM   10205 C CG2 . THR C 1 425 ? -21.086 45.745  -40.091 1.00 34.52  ? 454 THR B CG2 1 
ATOM   10206 N N   . GLU C 1 426 ? -19.315 48.767  -38.698 1.00 41.37  ? 455 GLU B N   1 
ATOM   10207 C CA  . GLU C 1 426 ? -19.582 50.165  -39.016 1.00 45.23  ? 455 GLU B CA  1 
ATOM   10208 C C   . GLU C 1 426 ? -18.359 50.782  -39.670 1.00 40.14  ? 455 GLU B C   1 
ATOM   10209 O O   . GLU C 1 426 ? -18.476 51.496  -40.662 1.00 36.49  ? 455 GLU B O   1 
ATOM   10210 C CB  . GLU C 1 426 ? -19.943 51.006  -37.782 1.00 52.64  ? 455 GLU B CB  1 
ATOM   10211 C CG  . GLU C 1 426 ? -21.425 50.899  -37.447 1.00 59.07  ? 455 GLU B CG  1 
ATOM   10212 C CD  . GLU C 1 426 ? -22.038 51.888  -36.473 1.00 70.95  ? 455 GLU B CD  1 
ATOM   10213 O OE1 . GLU C 1 426 ? -22.542 51.390  -35.432 1.00 68.92  ? 455 GLU B OE1 1 
ATOM   10214 O OE2 . GLU C 1 426 ? -22.082 53.110  -36.783 1.00 63.85  ? 455 GLU B OE2 1 
ATOM   10215 N N   . GLY C 1 427 ? -17.193 50.482  -39.090 1.00 33.30  ? 456 GLY B N   1 
ATOM   10216 C CA  . GLY C 1 427 ? -15.955 51.049  -39.559 1.00 31.77  ? 456 GLY B CA  1 
ATOM   10217 C C   . GLY C 1 427 ? -15.550 50.394  -40.872 1.00 29.40  ? 456 GLY B C   1 
ATOM   10218 O O   . GLY C 1 427 ? -14.904 51.004  -41.729 1.00 33.78  ? 456 GLY B O   1 
ATOM   10219 N N   . LEU C 1 428 ? -15.869 49.114  -40.995 1.00 30.09  ? 457 LEU B N   1 
ATOM   10220 C CA  . LEU C 1 428 ? -15.535 48.424  -42.230 1.00 31.18  ? 457 LEU B CA  1 
ATOM   10221 C C   . LEU C 1 428 ? -16.428 48.935  -43.374 1.00 35.00  ? 457 LEU B C   1 
ATOM   10222 O O   . LEU C 1 428 ? -15.931 49.132  -44.482 1.00 37.74  ? 457 LEU B O   1 
ATOM   10223 C CB  . LEU C 1 428 ? -15.581 46.921  -42.053 1.00 27.21  ? 457 LEU B CB  1 
ATOM   10224 C CG  . LEU C 1 428 ? -15.013 46.104  -43.210 1.00 33.02  ? 457 LEU B CG  1 
ATOM   10225 C CD1 . LEU C 1 428 ? -13.578 46.421  -43.465 1.00 29.78  ? 457 LEU B CD1 1 
ATOM   10226 C CD2 . LEU C 1 428 ? -15.199 44.647  -42.869 1.00 34.52  ? 457 LEU B CD2 1 
ATOM   10227 N N   . MET C 1 429 ? -17.705 49.236  -43.082 1.00 36.00  ? 458 MET B N   1 
ATOM   10228 C CA  . MET C 1 429 ? -18.613 49.812  -44.069 1.00 37.30  ? 458 MET B CA  1 
ATOM   10229 C C   . MET C 1 429 ? -18.103 51.179  -44.547 1.00 42.94  ? 458 MET B C   1 
ATOM   10230 O O   . MET C 1 429 ? -18.042 51.426  -45.749 1.00 39.34  ? 458 MET B O   1 
ATOM   10231 C CB  . MET C 1 429 ? -20.016 49.955  -43.481 1.00 40.52  ? 458 MET B CB  1 
ATOM   10232 C CG  . MET C 1 429 ? -20.791 48.666  -43.326 1.00 41.14  ? 458 MET B CG  1 
ATOM   10233 S SD  . MET C 1 429 ? -22.264 49.086  -42.377 1.00 51.49  ? 458 MET B SD  1 
ATOM   10234 C CE  . MET C 1 429 ? -23.392 47.762  -42.801 1.00 53.14  ? 458 MET B CE  1 
ATOM   10235 N N   . LYS C 1 430 ? -17.698 52.058  -43.613 1.00 43.58  ? 459 LYS B N   1 
ATOM   10236 C CA  . LYS C 1 430 ? -17.112 53.343  -43.978 1.00 46.36  ? 459 LYS B CA  1 
ATOM   10237 C C   . LYS C 1 430 ? -15.775 53.171  -44.701 1.00 45.30  ? 459 LYS B C   1 
ATOM   10238 O O   . LYS C 1 430 ? -15.480 53.889  -45.652 1.00 44.05  ? 459 LYS B O   1 
ATOM   10239 C CB  . LYS C 1 430 ? -16.956 54.271  -42.765 1.00 54.63  ? 459 LYS B CB  1 
ATOM   10240 C CG  . LYS C 1 430 ? -18.285 54.515  -42.045 1.00 59.24  ? 459 LYS B CG  1 
ATOM   10241 C CD  . LYS C 1 430 ? -18.420 55.780  -41.205 1.00 64.03  ? 459 LYS B CD  1 
ATOM   10242 C CE  . LYS C 1 430 ? -17.324 55.974  -40.208 1.00 74.53  ? 459 LYS B CE  1 
ATOM   10243 N NZ  . LYS C 1 430 ? -17.560 57.166  -39.384 1.00 78.97  ? 459 LYS B NZ  1 
ATOM   10244 N N   . PHE C 1 431 ? -14.923 52.254  -44.242 1.00 41.06  ? 460 PHE B N   1 
ATOM   10245 C CA  . PHE C 1 431 ? -13.639 52.081  -44.895 1.00 36.88  ? 460 PHE B CA  1 
ATOM   10246 C C   . PHE C 1 431 ? -13.862 51.689  -46.358 1.00 39.80  ? 460 PHE B C   1 
ATOM   10247 O O   . PHE C 1 431 ? -13.127 52.110  -47.252 1.00 41.94  ? 460 PHE B O   1 
ATOM   10248 C CB  . PHE C 1 431 ? -12.799 51.019  -44.179 1.00 37.60  ? 460 PHE B CB  1 
ATOM   10249 C CG  . PHE C 1 431 ? -11.475 50.771  -44.878 1.00 33.30  ? 460 PHE B CG  1 
ATOM   10250 C CD1 . PHE C 1 431 ? -10.418 51.656  -44.724 1.00 36.05  ? 460 PHE B CD1 1 
ATOM   10251 C CD2 . PHE C 1 431 ? -11.300 49.687  -45.726 1.00 37.44  ? 460 PHE B CD2 1 
ATOM   10252 C CE1 . PHE C 1 431 ? -9.222  51.462  -45.391 1.00 35.36  ? 460 PHE B CE1 1 
ATOM   10253 C CE2 . PHE C 1 431 ? -10.097 49.510  -46.400 1.00 36.46  ? 460 PHE B CE2 1 
ATOM   10254 C CZ  . PHE C 1 431 ? -9.065  50.395  -46.226 1.00 39.31  ? 460 PHE B CZ  1 
ATOM   10255 N N   . VAL C 1 432 ? -14.836 50.816  -46.603 1.00 41.72  ? 461 VAL B N   1 
ATOM   10256 C CA  . VAL C 1 432 ? -15.057 50.357  -47.960 1.00 47.34  ? 461 VAL B CA  1 
ATOM   10257 C C   . VAL C 1 432 ? -15.558 51.522  -48.807 1.00 44.35  ? 461 VAL B C   1 
ATOM   10258 O O   . VAL C 1 432 ? -15.144 51.683  -49.955 1.00 43.86  ? 461 VAL B O   1 
ATOM   10259 C CB  . VAL C 1 432 ? -16.013 49.159  -48.021 1.00 45.91  ? 461 VAL B CB  1 
ATOM   10260 C CG1 . VAL C 1 432 ? -16.473 48.904  -49.449 1.00 45.37  ? 461 VAL B CG1 1 
ATOM   10261 C CG2 . VAL C 1 432 ? -15.340 47.921  -47.447 1.00 44.19  ? 461 VAL B CG2 1 
ATOM   10262 N N   . ASP C 1 433 ? -16.408 52.345  -48.207 1.00 44.59  ? 462 ASP B N   1 
ATOM   10263 C CA  . ASP C 1 433 ? -17.020 53.465  -48.892 1.00 52.24  ? 462 ASP B CA  1 
ATOM   10264 C C   . ASP C 1 433 ? -15.946 54.471  -49.320 1.00 55.02  ? 462 ASP B C   1 
ATOM   10265 O O   . ASP C 1 433 ? -16.041 54.992  -50.417 1.00 57.54  ? 462 ASP B O   1 
ATOM   10266 C CB  . ASP C 1 433 ? -18.174 54.032  -48.069 1.00 54.03  ? 462 ASP B CB  1 
ATOM   10267 C CG  . ASP C 1 433 ? -19.331 53.065  -47.838 1.00 69.59  ? 462 ASP B CG  1 
ATOM   10268 O OD1 . ASP C 1 433 ? -19.302 51.955  -48.446 1.00 72.36  ? 462 ASP B OD1 1 
ATOM   10269 O OD2 . ASP C 1 433 ? -20.241 53.402  -47.038 1.00 67.54  ? 462 ASP B OD2 1 
ATOM   10270 N N   . SER C 1 434 ? -14.902 54.694  -48.502 1.00 54.96  ? 463 SER B N   1 
ATOM   10271 C CA  . SER C 1 434 ? -13.911 55.747  -48.733 1.00 52.26  ? 463 SER B CA  1 
ATOM   10272 C C   . SER C 1 434 ? -13.128 55.549  -50.047 1.00 49.10  ? 463 SER B C   1 
ATOM   10273 O O   . SER C 1 434 ? -12.665 54.397  -50.317 1.00 63.57  ? 463 SER B O   1 
ATOM   10274 C CB  . SER C 1 434 ? -12.964 55.878  -47.548 1.00 51.19  ? 463 SER B CB  1 
ATOM   10275 O OG  . SER C 1 434 ? -12.160 54.717  -47.362 1.00 50.84  ? 463 SER B OG  1 
ATOM   10276 N N   . SER D 1 1   ? -37.645 44.426  -20.927 1.00 82.29  ? 30  SER C N   1 
ATOM   10277 C CA  . SER D 1 1   ? -37.450 44.685  -19.471 1.00 82.52  ? 30  SER C CA  1 
ATOM   10278 C C   . SER D 1 1   ? -36.230 45.575  -19.275 1.00 79.23  ? 30  SER C C   1 
ATOM   10279 O O   . SER D 1 1   ? -35.747 46.161  -20.242 1.00 75.99  ? 30  SER C O   1 
ATOM   10280 C CB  . SER D 1 1   ? -37.351 43.393  -18.635 1.00 79.45  ? 30  SER C CB  1 
ATOM   10281 O OG  . SER D 1 1   ? -36.514 42.373  -19.185 1.00 52.89  ? 30  SER C OG  1 
ATOM   10282 N N   . THR D 1 2   ? -35.803 45.692  -18.005 1.00 89.42  ? 31  THR C N   1 
ATOM   10283 C CA  . THR D 1 2   ? -34.482 46.188  -17.634 1.00 87.55  ? 31  THR C CA  1 
ATOM   10284 C C   . THR D 1 2   ? -33.432 45.082  -17.774 1.00 72.48  ? 31  THR C C   1 
ATOM   10285 O O   . THR D 1 2   ? -32.274 45.314  -17.418 1.00 91.28  ? 31  THR C O   1 
ATOM   10286 C CB  . THR D 1 2   ? -34.494 46.743  -16.199 1.00 93.47  ? 31  THR C CB  1 
ATOM   10287 O OG1 . THR D 1 2   ? -33.248 47.396  -15.960 1.00 85.21  ? 31  THR C OG1 1 
ATOM   10288 C CG2 . THR D 1 2   ? -34.699 45.677  -15.131 1.00 89.99  ? 31  THR C CG2 1 
ATOM   10289 N N   . ASN D 1 3   ? -33.828 43.881  -18.232 1.00 51.50  ? 32  ASN C N   1 
ATOM   10290 C CA  . ASN D 1 3   ? -32.913 42.749  -18.239 1.00 44.69  ? 32  ASN C CA  1 
ATOM   10291 C C   . ASN D 1 3   ? -32.034 42.866  -19.471 1.00 31.96  ? 32  ASN C C   1 
ATOM   10292 O O   . ASN D 1 3   ? -32.546 42.829  -20.576 1.00 30.94  ? 32  ASN C O   1 
ATOM   10293 C CB  . ASN D 1 3   ? -33.612 41.394  -18.221 1.00 43.46  ? 32  ASN C CB  1 
ATOM   10294 C CG  . ASN D 1 3   ? -32.680 40.279  -17.789 1.00 51.67  ? 32  ASN C CG  1 
ATOM   10295 O OD1 . ASN D 1 3   ? -31.492 40.257  -18.143 1.00 47.20  ? 32  ASN C OD1 1 
ATOM   10296 N ND2 . ASN D 1 3   ? -33.185 39.352  -16.989 1.00 48.02  ? 32  ASN C ND2 1 
ATOM   10297 N N   . LEU D 1 4   ? -30.721 42.991  -19.252 1.00 36.90  ? 33  LEU C N   1 
ATOM   10298 C CA  . LEU D 1 4   ? -29.736 43.172  -20.304 1.00 30.28  ? 33  LEU C CA  1 
ATOM   10299 C C   . LEU D 1 4   ? -29.856 42.058  -21.350 1.00 29.71  ? 33  LEU C C   1 
ATOM   10300 O O   . LEU D 1 4   ? -29.658 42.269  -22.531 1.00 30.28  ? 33  LEU C O   1 
ATOM   10301 C CB  . LEU D 1 4   ? -28.350 43.227  -19.653 1.00 31.71  ? 33  LEU C CB  1 
ATOM   10302 C CG  . LEU D 1 4   ? -27.141 43.159  -20.605 1.00 34.11  ? 33  LEU C CG  1 
ATOM   10303 C CD1 . LEU D 1 4   ? -27.195 44.202  -21.727 1.00 33.18  ? 33  LEU C CD1 1 
ATOM   10304 C CD2 . LEU D 1 4   ? -25.807 43.275  -19.816 1.00 33.80  ? 33  LEU C CD2 1 
ATOM   10305 N N   . LYS D 1 5   ? -30.132 40.858  -20.902 1.00 28.16  ? 34  LYS C N   1 
ATOM   10306 C CA  . LYS D 1 5   ? -30.253 39.710  -21.775 1.00 32.68  ? 34  LYS C CA  1 
ATOM   10307 C C   . LYS D 1 5   ? -31.410 39.878  -22.765 1.00 34.64  ? 34  LYS C C   1 
ATOM   10308 O O   . LYS D 1 5   ? -31.304 39.415  -23.899 1.00 30.30  ? 34  LYS C O   1 
ATOM   10309 C CB  . LYS D 1 5   ? -30.468 38.467  -20.911 1.00 30.88  ? 34  LYS C CB  1 
ATOM   10310 C CG  . LYS D 1 5   ? -30.214 37.157  -21.624 1.00 32.30  ? 34  LYS C CG  1 
ATOM   10311 C CD  . LYS D 1 5   ? -30.570 35.946  -20.786 1.00 35.54  ? 34  LYS C CD  1 
ATOM   10312 C CE  . LYS D 1 5   ? -30.063 34.700  -21.478 1.00 37.30  ? 34  LYS C CE  1 
ATOM   10313 N NZ  . LYS D 1 5   ? -30.339 33.505  -20.669 1.00 38.11  ? 34  LYS C NZ  1 
ATOM   10314 N N   . ASP D 1 6   ? -32.507 40.510  -22.321 1.00 33.78  ? 35  ASP C N   1 
ATOM   10315 C CA  . ASP D 1 6   ? -33.663 40.738  -23.171 1.00 35.80  ? 35  ASP C CA  1 
ATOM   10316 C C   . ASP D 1 6   ? -33.407 41.908  -24.121 1.00 32.86  ? 35  ASP C C   1 
ATOM   10317 O O   . ASP D 1 6   ? -33.822 41.853  -25.274 1.00 31.66  ? 35  ASP C O   1 
ATOM   10318 C CB  . ASP D 1 6   ? -34.932 40.884  -22.357 1.00 39.98  ? 35  ASP C CB  1 
ATOM   10319 C CG  . ASP D 1 6   ? -35.358 39.599  -21.658 1.00 48.72  ? 35  ASP C CG  1 
ATOM   10320 O OD1 . ASP D 1 6   ? -35.488 38.567  -22.361 1.00 57.91  ? 35  ASP C OD1 1 
ATOM   10321 O OD2 . ASP D 1 6   ? -35.570 39.632  -20.432 1.00 51.85  ? 35  ASP C OD2 1 
ATOM   10322 N N   . ILE D 1 7   ? -32.708 42.943  -23.654 1.00 28.61  ? 36  ILE C N   1 
ATOM   10323 C CA  . ILE D 1 7   ? -32.313 44.029  -24.531 1.00 34.30  ? 36  ILE C CA  1 
ATOM   10324 C C   . ILE D 1 7   ? -31.396 43.489  -25.624 1.00 32.04  ? 36  ILE C C   1 
ATOM   10325 O O   . ILE D 1 7   ? -31.611 43.722  -26.806 1.00 34.32  ? 36  ILE C O   1 
ATOM   10326 C CB  . ILE D 1 7   ? -31.694 45.164  -23.710 1.00 42.63  ? 36  ILE C CB  1 
ATOM   10327 C CG1 . ILE D 1 7   ? -32.754 45.767  -22.792 1.00 46.41  ? 36  ILE C CG1 1 
ATOM   10328 C CG2 . ILE D 1 7   ? -31.039 46.226  -24.609 1.00 42.78  ? 36  ILE C CG2 1 
ATOM   10329 C CD1 . ILE D 1 7   ? -32.198 46.582  -21.641 1.00 50.70  ? 36  ILE C CD1 1 
ATOM   10330 N N   . LEU D 1 8   ? -30.449 42.648  -25.242 1.00 32.24  ? 37  LEU C N   1 
ATOM   10331 C CA  . LEU D 1 8   ? -29.509 42.094  -26.209 1.00 33.83  ? 37  LEU C CA  1 
ATOM   10332 C C   . LEU D 1 8   ? -30.212 41.186  -27.227 1.00 33.18  ? 37  LEU C C   1 
ATOM   10333 O O   . LEU D 1 8   ? -29.952 41.269  -28.435 1.00 30.60  ? 37  LEU C O   1 
ATOM   10334 C CB  . LEU D 1 8   ? -28.478 41.419  -25.312 1.00 34.22  ? 37  LEU C CB  1 
ATOM   10335 C CG  . LEU D 1 8   ? -27.344 40.666  -25.989 1.00 35.37  ? 37  LEU C CG  1 
ATOM   10336 C CD1 . LEU D 1 8   ? -26.701 41.474  -27.098 1.00 35.09  ? 37  LEU C CD1 1 
ATOM   10337 C CD2 . LEU D 1 8   ? -26.362 40.302  -24.881 1.00 35.08  ? 37  LEU C CD2 1 
ATOM   10338 N N   . ALA D 1 9   ? -31.173 40.375  -26.739 1.00 28.63  ? 38  ALA C N   1 
ATOM   10339 C CA  . ALA D 1 9   ? -32.003 39.548  -27.577 1.00 30.07  ? 38  ALA C CA  1 
ATOM   10340 C C   . ALA D 1 9   ? -32.700 40.351  -28.673 1.00 28.13  ? 38  ALA C C   1 
ATOM   10341 O O   . ALA D 1 9   ? -32.808 39.829  -29.766 1.00 27.74  ? 38  ALA C O   1 
ATOM   10342 C CB  . ALA D 1 9   ? -32.985 38.773  -26.749 1.00 30.99  ? 38  ALA C CB  1 
ATOM   10343 N N   . ASP D 1 10  ? -33.106 41.609  -28.416 1.00 28.48  ? 39  ASP C N   1 
ATOM   10344 C CA  . ASP D 1 10  ? -33.786 42.407  -29.427 1.00 32.51  ? 39  ASP C CA  1 
ATOM   10345 C C   . ASP D 1 10  ? -32.784 43.119  -30.341 1.00 28.85  ? 39  ASP C C   1 
ATOM   10346 O O   . ASP D 1 10  ? -33.099 43.451  -31.472 1.00 33.21  ? 39  ASP C O   1 
ATOM   10347 C CB  . ASP D 1 10  ? -34.840 43.337  -28.831 1.00 39.28  ? 39  ASP C CB  1 
ATOM   10348 C CG  . ASP D 1 10  ? -36.009 42.664  -28.101 1.00 45.51  ? 39  ASP C CG  1 
ATOM   10349 O OD1 . ASP D 1 10  ? -36.576 41.674  -28.644 1.00 57.96  ? 39  ASP C OD1 1 
ATOM   10350 O OD2 . ASP D 1 10  ? -36.382 43.142  -27.004 1.00 41.13  ? 39  ASP C OD2 1 
ATOM   10351 N N   . LEU D 1 11  ? -31.552 43.313  -29.894 1.00 28.23  ? 40  LEU C N   1 
ATOM   10352 C CA  . LEU D 1 11  ? -30.540 44.013  -30.684 1.00 30.06  ? 40  LEU C CA  1 
ATOM   10353 C C   . LEU D 1 11  ? -29.900 43.085  -31.722 1.00 33.19  ? 40  LEU C C   1 
ATOM   10354 O O   . LEU D 1 11  ? -29.435 43.529  -32.780 1.00 29.60  ? 40  LEU C O   1 
ATOM   10355 C CB  . LEU D 1 11  ? -29.464 44.556  -29.746 1.00 33.60  ? 40  LEU C CB  1 
ATOM   10356 C CG  . LEU D 1 11  ? -29.875 45.724  -28.848 1.00 36.40  ? 40  LEU C CG  1 
ATOM   10357 C CD1 . LEU D 1 11  ? -28.769 45.929  -27.815 1.00 39.26  ? 40  LEU C CD1 1 
ATOM   10358 C CD2 . LEU D 1 11  ? -30.124 46.986  -29.654 1.00 38.72  ? 40  LEU C CD2 1 
ATOM   10359 N N   . ILE D 1 12  ? -29.873 41.786  -31.410 1.00 27.62  ? 41  ILE C N   1 
ATOM   10360 C CA  . ILE D 1 12  ? -29.097 40.852  -32.206 1.00 32.83  ? 41  ILE C CA  1 
ATOM   10361 C C   . ILE D 1 12  ? -29.625 40.712  -33.641 1.00 34.74  ? 41  ILE C C   1 
ATOM   10362 O O   . ILE D 1 12  ? -28.799 40.773  -34.558 1.00 29.18  ? 41  ILE C O   1 
ATOM   10363 C CB  . ILE D 1 12  ? -28.931 39.508  -31.492 1.00 33.05  ? 41  ILE C CB  1 
ATOM   10364 C CG1 . ILE D 1 12  ? -27.894 39.658  -30.381 1.00 27.61  ? 41  ILE C CG1 1 
ATOM   10365 C CG2 . ILE D 1 12  ? -28.535 38.430  -32.511 1.00 34.72  ? 41  ILE C CG2 1 
ATOM   10366 C CD1 . ILE D 1 12  ? -27.916 38.588  -29.299 1.00 29.30  ? 41  ILE C CD1 1 
ATOM   10367 N N   . PRO D 1 13  ? -30.949 40.539  -33.890 1.00 36.07  ? 42  PRO C N   1 
ATOM   10368 C CA  . PRO D 1 13  ? -31.501 40.469  -35.256 1.00 37.95  ? 42  PRO C CA  1 
ATOM   10369 C C   . PRO D 1 13  ? -31.173 41.620  -36.194 1.00 32.46  ? 42  PRO C C   1 
ATOM   10370 O O   . PRO D 1 13  ? -30.883 41.401  -37.368 1.00 36.57  ? 42  PRO C O   1 
ATOM   10371 C CB  . PRO D 1 13  ? -33.031 40.373  -35.016 1.00 39.09  ? 42  PRO C CB  1 
ATOM   10372 C CG  . PRO D 1 13  ? -33.104 39.650  -33.706 1.00 39.34  ? 42  PRO C CG  1 
ATOM   10373 C CD  . PRO D 1 13  ? -31.994 40.295  -32.879 1.00 38.20  ? 42  PRO C CD  1 
ATOM   10374 N N   . LYS D 1 14  ? -31.218 42.836  -35.663 1.00 33.41  ? 43  LYS C N   1 
ATOM   10375 C CA  . LYS D 1 14  ? -30.852 44.026  -36.401 1.00 32.51  ? 43  LYS C CA  1 
ATOM   10376 C C   . LYS D 1 14  ? -29.378 44.036  -36.802 1.00 36.12  ? 43  LYS C C   1 
ATOM   10377 O O   . LYS D 1 14  ? -29.021 44.485  -37.883 1.00 36.00  ? 43  LYS C O   1 
ATOM   10378 C CB  . LYS D 1 14  ? -31.069 45.263  -35.518 1.00 41.68  ? 43  LYS C CB  1 
ATOM   10379 C CG  . LYS D 1 14  ? -32.485 45.480  -34.962 1.00 47.72  ? 43  LYS C CG  1 
ATOM   10380 C CD  . LYS D 1 14  ? -32.593 46.771  -34.150 1.00 55.61  ? 43  LYS C CD  1 
ATOM   10381 C CE  . LYS D 1 14  ? -33.895 46.893  -33.419 1.00 64.17  ? 43  LYS C CE  1 
ATOM   10382 N NZ  . LYS D 1 14  ? -35.005 47.193  -34.328 1.00 65.91  ? 43  LYS C NZ  1 
ATOM   10383 N N   . GLU D 1 15  ? -28.485 43.639  -35.893 1.00 37.72  ? 44  GLU C N   1 
ATOM   10384 C CA  . GLU D 1 15  ? -27.069 43.597  -36.222 1.00 36.40  ? 44  GLU C CA  1 
ATOM   10385 C C   . GLU D 1 15  ? -26.808 42.469  -37.224 1.00 32.24  ? 44  GLU C C   1 
ATOM   10386 O O   . GLU D 1 15  ? -25.977 42.627  -38.101 1.00 28.73  ? 44  GLU C O   1 
ATOM   10387 C CB  . GLU D 1 15  ? -26.229 43.455  -34.957 1.00 41.13  ? 44  GLU C CB  1 
ATOM   10388 C CG  . GLU D 1 15  ? -24.807 43.991  -35.099 1.00 58.19  ? 44  GLU C CG  1 
ATOM   10389 C CD  . GLU D 1 15  ? -24.708 45.442  -35.544 1.00 62.00  ? 44  GLU C CD  1 
ATOM   10390 O OE1 . GLU D 1 15  ? -25.606 46.223  -35.154 1.00 61.62  ? 44  GLU C OE1 1 
ATOM   10391 O OE2 . GLU D 1 15  ? -23.735 45.784  -36.262 1.00 78.61  ? 44  GLU C OE2 1 
ATOM   10392 N N   . GLN D 1 16  ? -27.525 41.347  -37.113 1.00 27.08  ? 45  GLN C N   1 
ATOM   10393 C CA  . GLN D 1 16  ? -27.352 40.231  -38.031 1.00 32.38  ? 45  GLN C CA  1 
ATOM   10394 C C   . GLN D 1 16  ? -27.758 40.611  -39.463 1.00 34.49  ? 45  GLN C C   1 
ATOM   10395 O O   . GLN D 1 16  ? -27.130 40.164  -40.408 1.00 32.86  ? 45  GLN C O   1 
ATOM   10396 C CB  . GLN D 1 16  ? -28.222 39.046  -37.621 1.00 33.55  ? 45  GLN C CB  1 
ATOM   10397 C CG  . GLN D 1 16  ? -27.722 38.271  -36.413 1.00 32.42  ? 45  GLN C CG  1 
ATOM   10398 C CD  . GLN D 1 16  ? -28.686 37.195  -35.959 1.00 32.60  ? 45  GLN C CD  1 
ATOM   10399 O OE1 . GLN D 1 16  ? -29.891 37.217  -36.238 1.00 36.91  ? 45  GLN C OE1 1 
ATOM   10400 N NE2 . GLN D 1 16  ? -28.157 36.261  -35.191 1.00 34.04  ? 45  GLN C NE2 1 
ATOM   10401 N N   . ALA D 1 17  ? -28.810 41.421  -39.614 1.00 37.48  ? 46  ALA C N   1 
ATOM   10402 C CA  . ALA D 1 17  ? -29.291 41.873  -40.921 1.00 37.60  ? 46  ALA C CA  1 
ATOM   10403 C C   . ALA D 1 17  ? -28.339 42.910  -41.536 1.00 38.84  ? 46  ALA C C   1 
ATOM   10404 O O   . ALA D 1 17  ? -28.087 42.936  -42.752 1.00 38.57  ? 46  ALA C O   1 
ATOM   10405 C CB  . ALA D 1 17  ? -30.718 42.396  -40.775 1.00 35.37  ? 46  ALA C CB  1 
ATOM   10406 N N   . ARG D 1 18  ? -27.746 43.745  -40.677 1.00 34.96  ? 47  ARG C N   1 
ATOM   10407 C CA  . ARG D 1 18  ? -26.826 44.780  -41.111 1.00 39.51  ? 47  ARG C CA  1 
ATOM   10408 C C   . ARG D 1 18  ? -25.587 44.146  -41.734 1.00 38.11  ? 47  ARG C C   1 
ATOM   10409 O O   . ARG D 1 18  ? -25.069 44.625  -42.738 1.00 44.28  ? 47  ARG C O   1 
ATOM   10410 C CB  . ARG D 1 18  ? -26.531 45.637  -39.880 1.00 46.33  ? 47  ARG C CB  1 
ATOM   10411 C CG  . ARG D 1 18  ? -25.726 46.899  -40.107 1.00 52.38  ? 47  ARG C CG  1 
ATOM   10412 C CD  . ARG D 1 18  ? -25.634 47.704  -38.820 1.00 59.53  ? 47  ARG C CD  1 
ATOM   10413 N NE  . ARG D 1 18  ? -24.706 48.817  -39.041 1.00 74.70  ? 47  ARG C NE  1 
ATOM   10414 C CZ  . ARG D 1 18  ? -24.890 49.836  -39.890 1.00 84.17  ? 47  ARG C CZ  1 
ATOM   10415 N NH1 . ARG D 1 18  ? -23.907 50.698  -40.097 1.00 88.30  ? 47  ARG C NH1 1 
ATOM   10416 N NH2 . ARG D 1 18  ? -26.030 49.987  -40.549 1.00 74.02  ? 47  ARG C NH2 1 
ATOM   10417 N N   . ILE D 1 19  ? -25.132 43.048  -41.144 1.00 31.95  ? 48  ILE C N   1 
ATOM   10418 C CA  . ILE D 1 19  ? -23.928 42.384  -41.592 1.00 33.29  ? 48  ILE C CA  1 
ATOM   10419 C C   . ILE D 1 19  ? -24.232 41.620  -42.870 1.00 34.47  ? 48  ILE C C   1 
ATOM   10420 O O   . ILE D 1 19  ? -23.382 41.599  -43.768 1.00 34.54  ? 48  ILE C O   1 
ATOM   10421 C CB  . ILE D 1 19  ? -23.392 41.470  -40.472 1.00 33.70  ? 48  ILE C CB  1 
ATOM   10422 C CG1 . ILE D 1 19  ? -22.780 42.335  -39.385 1.00 34.82  ? 48  ILE C CG1 1 
ATOM   10423 C CG2 . ILE D 1 19  ? -22.411 40.423  -41.000 1.00 34.94  ? 48  ILE C CG2 1 
ATOM   10424 C CD1 . ILE D 1 19  ? -22.425 41.592  -38.123 1.00 37.51  ? 48  ILE C CD1 1 
ATOM   10425 N N   . LYS D 1 20  ? -25.402 40.961  -42.909 1.00 35.29  ? 49  LYS C N   1 
ATOM   10426 C CA  . LYS D 1 20  ? -25.789 40.164  -44.069 1.00 42.35  ? 49  LYS C CA  1 
ATOM   10427 C C   . LYS D 1 20  ? -25.911 41.116  -45.269 1.00 40.21  ? 49  LYS C C   1 
ATOM   10428 O O   . LYS D 1 20  ? -25.390 40.835  -46.338 1.00 37.87  ? 49  LYS C O   1 
ATOM   10429 C CB  . LYS D 1 20  ? -27.021 39.320  -43.705 1.00 47.09  ? 49  LYS C CB  1 
ATOM   10430 C CG  . LYS D 1 20  ? -27.715 38.521  -44.814 1.00 51.04  ? 49  LYS C CG  1 
ATOM   10431 C CD  . LYS D 1 20  ? -29.143 38.099  -44.468 1.00 56.10  ? 49  LYS C CD  1 
ATOM   10432 C CE  . LYS D 1 20  ? -29.995 37.640  -45.624 1.00 62.65  ? 49  LYS C CE  1 
ATOM   10433 N NZ  . LYS D 1 20  ? -29.664 36.274  -46.046 1.00 66.35  ? 49  LYS C NZ  1 
ATOM   10434 N N   . THR D 1 21  ? -26.493 42.292  -45.059 1.00 31.84  ? 50  THR C N   1 
ATOM   10435 C CA  . THR D 1 21  ? -26.633 43.246  -46.132 1.00 38.62  ? 50  THR C CA  1 
ATOM   10436 C C   . THR D 1 21  ? -25.239 43.649  -46.598 1.00 35.39  ? 50  THR C C   1 
ATOM   10437 O O   . THR D 1 21  ? -24.991 43.705  -47.777 1.00 38.46  ? 50  THR C O   1 
ATOM   10438 C CB  . THR D 1 21  ? -27.485 44.424  -45.670 1.00 47.04  ? 50  THR C CB  1 
ATOM   10439 O OG1 . THR D 1 21  ? -28.768 43.867  -45.428 1.00 48.68  ? 50  THR C OG1 1 
ATOM   10440 C CG2 . THR D 1 21  ? -27.656 45.508  -46.717 1.00 50.78  ? 50  THR C CG2 1 
ATOM   10441 N N   . PHE D 1 22  ? -24.299 43.853  -45.684 1.00 36.31  ? 51  PHE C N   1 
ATOM   10442 C CA  . PHE D 1 22  ? -22.993 44.364  -46.069 1.00 31.16  ? 51  PHE C CA  1 
ATOM   10443 C C   . PHE D 1 22  ? -22.170 43.301  -46.801 1.00 29.60  ? 51  PHE C C   1 
ATOM   10444 O O   . PHE D 1 22  ? -21.438 43.594  -47.754 1.00 30.21  ? 51  PHE C O   1 
ATOM   10445 C CB  . PHE D 1 22  ? -22.338 44.935  -44.815 1.00 29.50  ? 51  PHE C CB  1 
ATOM   10446 C CG  . PHE D 1 22  ? -20.919 45.420  -45.028 1.00 27.30  ? 51  PHE C CG  1 
ATOM   10447 C CD1 . PHE D 1 22  ? -20.631 46.312  -46.046 1.00 30.46  ? 51  PHE C CD1 1 
ATOM   10448 C CD2 . PHE D 1 22  ? -19.884 44.951  -44.240 1.00 29.97  ? 51  PHE C CD2 1 
ATOM   10449 C CE1 . PHE D 1 22  ? -19.360 46.782  -46.227 1.00 26.89  ? 51  PHE C CE1 1 
ATOM   10450 C CE2 . PHE D 1 22  ? -18.602 45.397  -44.448 1.00 31.06  ? 51  PHE C CE2 1 
ATOM   10451 C CZ  . PHE D 1 22  ? -18.343 46.295  -45.457 1.00 33.36  ? 51  PHE C CZ  1 
ATOM   10452 N N   . ARG D 1 23  ? -22.270 42.073  -46.342 1.00 27.71  ? 52  ARG C N   1 
ATOM   10453 C CA  . ARG D 1 23  ? -21.591 40.965  -46.980 1.00 33.99  ? 52  ARG C CA  1 
ATOM   10454 C C   . ARG D 1 23  ? -22.174 40.716  -48.368 1.00 36.59  ? 52  ARG C C   1 
ATOM   10455 O O   . ARG D 1 23  ? -21.440 40.337  -49.273 1.00 34.33  ? 52  ARG C O   1 
ATOM   10456 C CB  . ARG D 1 23  ? -21.712 39.719  -46.096 1.00 32.61  ? 52  ARG C CB  1 
ATOM   10457 C CG  . ARG D 1 23  ? -20.887 39.863  -44.824 1.00 33.38  ? 52  ARG C CG  1 
ATOM   10458 C CD  . ARG D 1 23  ? -20.985 38.640  -43.892 1.00 31.83  ? 52  ARG C CD  1 
ATOM   10459 N NE  . ARG D 1 23  ? -20.264 37.561  -44.564 1.00 35.33  ? 52  ARG C NE  1 
ATOM   10460 C CZ  . ARG D 1 23  ? -20.078 36.326  -44.114 1.00 43.74  ? 52  ARG C CZ  1 
ATOM   10461 N NH1 . ARG D 1 23  ? -20.687 35.885  -43.023 1.00 41.39  ? 52  ARG C NH1 1 
ATOM   10462 N NH2 . ARG D 1 23  ? -19.258 35.539  -44.789 1.00 49.55  ? 52  ARG C NH2 1 
ATOM   10463 N N   . GLN D 1 24  ? -23.487 40.912  -48.501 1.00 32.34  ? 53  GLN C N   1 
ATOM   10464 C CA  . GLN D 1 24  ? -24.195 40.722  -49.755 1.00 38.33  ? 53  GLN C CA  1 
ATOM   10465 C C   . GLN D 1 24  ? -23.822 41.828  -50.745 1.00 33.86  ? 53  GLN C C   1 
ATOM   10466 O O   . GLN D 1 24  ? -23.572 41.521  -51.899 1.00 35.78  ? 53  GLN C O   1 
ATOM   10467 C CB  . GLN D 1 24  ? -25.705 40.575  -49.549 1.00 36.73  ? 53  GLN C CB  1 
ATOM   10468 C CG  . GLN D 1 24  ? -26.047 39.184  -49.039 1.00 43.43  ? 53  GLN C CG  1 
ATOM   10469 C CD  . GLN D 1 24  ? -27.525 38.933  -48.849 1.00 47.65  ? 53  GLN C CD  1 
ATOM   10470 O OE1 . GLN D 1 24  ? -28.384 39.768  -49.151 1.00 51.47  ? 53  GLN C OE1 1 
ATOM   10471 N NE2 . GLN D 1 24  ? -27.812 37.750  -48.327 1.00 55.59  ? 53  GLN C NE2 1 
ATOM   10472 N N   . GLN D 1 25  ? -23.622 43.059  -50.281 1.00 30.16  ? 54  GLN C N   1 
ATOM   10473 C CA  . GLN D 1 25  ? -23.158 44.105  -51.180 1.00 36.50  ? 54  GLN C CA  1 
ATOM   10474 C C   . GLN D 1 25  ? -21.641 44.120  -51.427 1.00 35.75  ? 54  GLN C C   1 
ATOM   10475 O O   . GLN D 1 25  ? -21.203 44.622  -52.460 1.00 35.59  ? 54  GLN C O   1 
ATOM   10476 C CB  . GLN D 1 25  ? -23.738 45.426  -50.687 1.00 39.40  ? 54  GLN C CB  1 
ATOM   10477 C CG  . GLN D 1 25  ? -22.890 46.205  -49.705 1.00 49.41  ? 54  GLN C CG  1 
ATOM   10478 C CD  . GLN D 1 25  ? -23.572 47.482  -49.247 1.00 43.20  ? 54  GLN C CD  1 
ATOM   10479 O OE1 . GLN D 1 25  ? -24.718 47.775  -49.594 1.00 42.13  ? 54  GLN C OE1 1 
ATOM   10480 N NE2 . GLN D 1 25  ? -22.858 48.265  -48.464 1.00 45.62  ? 54  GLN C NE2 1 
ATOM   10481 N N   . HIS D 1 26  ? -20.810 43.615  -50.509 1.00 32.66  ? 55  HIS C N   1 
ATOM   10482 C CA  . HIS D 1 26  ? -19.376 43.896  -50.572 1.00 37.80  ? 55  HIS C CA  1 
ATOM   10483 C C   . HIS D 1 26  ? -18.485 42.703  -50.230 1.00 34.32  ? 55  HIS C C   1 
ATOM   10484 O O   . HIS D 1 26  ? -17.285 42.903  -50.074 1.00 35.91  ? 55  HIS C O   1 
ATOM   10485 C CB  . HIS D 1 26  ? -18.996 45.053  -49.635 1.00 39.00  ? 55  HIS C CB  1 
ATOM   10486 C CG  . HIS D 1 26  ? -19.149 46.398  -50.267 1.00 39.75  ? 55  HIS C CG  1 
ATOM   10487 N ND1 . HIS D 1 26  ? -18.485 46.742  -51.427 1.00 40.15  ? 55  HIS C ND1 1 
ATOM   10488 C CD2 . HIS D 1 26  ? -19.842 47.479  -49.900 1.00 39.22  ? 55  HIS C CD2 1 
ATOM   10489 C CE1 . HIS D 1 26  ? -18.783 48.005  -51.741 1.00 40.06  ? 55  HIS C CE1 1 
ATOM   10490 N NE2 . HIS D 1 26  ? -19.624 48.461  -50.846 1.00 38.01  ? 55  HIS C NE2 1 
ATOM   10491 N N   . GLY D 1 27  ? -19.047 41.490  -50.156 1.00 32.91  ? 56  GLY C N   1 
ATOM   10492 C CA  . GLY D 1 27  ? -18.305 40.337  -49.651 1.00 36.84  ? 56  GLY C CA  1 
ATOM   10493 C C   . GLY D 1 27  ? -17.025 40.061  -50.447 1.00 34.03  ? 56  GLY C C   1 
ATOM   10494 O O   . GLY D 1 27  ? -15.988 39.729  -49.877 1.00 32.81  ? 56  GLY C O   1 
ATOM   10495 N N   . LYS D 1 28  ? -17.066 40.326  -51.752 1.00 32.93  ? 57  LYS C N   1 
ATOM   10496 C CA  . LYS D 1 28  ? -15.930 40.056  -52.605 1.00 36.53  ? 57  LYS C CA  1 
ATOM   10497 C C   . LYS D 1 28  ? -15.017 41.277  -52.708 1.00 36.60  ? 57  LYS C C   1 
ATOM   10498 O O   . LYS D 1 28  ? -13.958 41.189  -53.323 1.00 38.85  ? 57  LYS C O   1 
ATOM   10499 C CB  . LYS D 1 28  ? -16.469 39.494  -53.923 1.00 43.18  ? 57  LYS C CB  1 
ATOM   10500 C CG  . LYS D 1 28  ? -16.934 38.072  -53.783 1.00 43.91  ? 57  LYS C CG  1 
ATOM   10501 C CD  . LYS D 1 28  ? -17.855 37.601  -54.900 1.00 55.67  ? 57  LYS C CD  1 
ATOM   10502 C CE  . LYS D 1 28  ? -17.152 37.402  -56.189 1.00 58.34  ? 57  LYS C CE  1 
ATOM   10503 N NZ  . LYS D 1 28  ? -18.001 36.576  -57.051 1.00 62.81  ? 57  LYS C NZ  1 
ATOM   10504 N N   . THR D 1 29  ? -15.343 42.370  -52.009 1.00 30.35  ? 58  THR C N   1 
ATOM   10505 C CA  . THR D 1 29  ? -14.584 43.596  -52.152 1.00 32.43  ? 58  THR C CA  1 
ATOM   10506 C C   . THR D 1 29  ? -13.239 43.440  -51.444 1.00 37.81  ? 58  THR C C   1 
ATOM   10507 O O   . THR D 1 29  ? -13.190 42.908  -50.333 1.00 34.61  ? 58  THR C O   1 
ATOM   10508 C CB  . THR D 1 29  ? -15.396 44.739  -51.565 1.00 30.02  ? 58  THR C CB  1 
ATOM   10509 O OG1 . THR D 1 29  ? -16.515 44.868  -52.433 1.00 34.69  ? 58  THR C OG1 1 
ATOM   10510 C CG2 . THR D 1 29  ? -14.663 46.065  -51.548 1.00 37.40  ? 58  THR C CG2 1 
ATOM   10511 N N   . VAL D 1 30  ? -12.157 43.884  -52.106 1.00 36.32  ? 59  VAL C N   1 
ATOM   10512 C CA  . VAL D 1 30  ? -10.814 43.785  -51.560 1.00 38.83  ? 59  VAL C CA  1 
ATOM   10513 C C   . VAL D 1 30  ? -10.589 44.957  -50.601 1.00 39.53  ? 59  VAL C C   1 
ATOM   10514 O O   . VAL D 1 30  ? -10.782 46.119  -50.970 1.00 37.13  ? 59  VAL C O   1 
ATOM   10515 C CB  . VAL D 1 30  ? -9.767  43.745  -52.685 1.00 37.14  ? 59  VAL C CB  1 
ATOM   10516 C CG1 . VAL D 1 30  ? -8.345  43.915  -52.157 1.00 37.84  ? 59  VAL C CG1 1 
ATOM   10517 C CG2 . VAL D 1 30  ? -9.871  42.469  -53.498 1.00 36.30  ? 59  VAL C CG2 1 
ATOM   10518 N N   . VAL D 1 31  ? -10.165 44.643  -49.365 1.00 38.42  ? 60  VAL C N   1 
ATOM   10519 C CA  . VAL D 1 31  ? -9.981  45.647  -48.317 1.00 38.61  ? 60  VAL C CA  1 
ATOM   10520 C C   . VAL D 1 31  ? -8.494  45.915  -48.091 1.00 37.46  ? 60  VAL C C   1 
ATOM   10521 O O   . VAL D 1 31  ? -8.128  46.895  -47.447 1.00 36.34  ? 60  VAL C O   1 
ATOM   10522 C CB  . VAL D 1 31  ? -10.658 45.164  -47.018 1.00 46.36  ? 60  VAL C CB  1 
ATOM   10523 C CG1 . VAL D 1 31  ? -10.376 46.086  -45.847 1.00 50.29  ? 60  VAL C CG1 1 
ATOM   10524 C CG2 . VAL D 1 31  ? -12.170 45.023  -47.158 1.00 48.84  ? 60  VAL C CG2 1 
ATOM   10525 N N   . GLY D 1 32  ? -7.639  45.014  -48.590 1.00 35.51  ? 61  GLY C N   1 
ATOM   10526 C CA  . GLY D 1 32  ? -6.208  45.144  -48.429 1.00 34.43  ? 61  GLY C CA  1 
ATOM   10527 C C   . GLY D 1 32  ? -5.455  44.063  -49.195 1.00 36.08  ? 61  GLY C C   1 
ATOM   10528 O O   . GLY D 1 32  ? -6.005  43.054  -49.653 1.00 36.73  ? 61  GLY C O   1 
ATOM   10529 N N   . GLN D 1 33  ? -4.160  44.322  -49.351 1.00 37.68  ? 62  GLN C N   1 
ATOM   10530 C CA  . GLN D 1 33  ? -3.234  43.391  -49.955 1.00 38.29  ? 62  GLN C CA  1 
ATOM   10531 C C   . GLN D 1 33  ? -2.505  42.699  -48.817 1.00 33.78  ? 62  GLN C C   1 
ATOM   10532 O O   . GLN D 1 33  ? -2.425  43.238  -47.729 1.00 34.22  ? 62  GLN C O   1 
ATOM   10533 C CB  . GLN D 1 33  ? -2.195  44.085  -50.828 1.00 40.57  ? 62  GLN C CB  1 
ATOM   10534 C CG  . GLN D 1 33  ? -2.776  45.135  -51.771 1.00 51.46  ? 62  GLN C CG  1 
ATOM   10535 C CD  . GLN D 1 33  ? -3.504  44.534  -52.950 1.00 55.92  ? 62  GLN C CD  1 
ATOM   10536 O OE1 . GLN D 1 33  ? -4.743  44.525  -53.014 1.00 60.33  ? 62  GLN C OE1 1 
ATOM   10537 N NE2 . GLN D 1 33  ? -2.727  44.014  -53.888 1.00 55.24  ? 62  GLN C NE2 1 
ATOM   10538 N N   . ILE D 1 34  ? -1.904  41.557  -49.139 1.00 34.41  ? 63  ILE C N   1 
ATOM   10539 C CA  . ILE D 1 34  ? -1.030  40.850  -48.231 1.00 32.55  ? 63  ILE C CA  1 
ATOM   10540 C C   . ILE D 1 34  ? 0.304   40.661  -48.910 1.00 28.08  ? 63  ILE C C   1 
ATOM   10541 O O   . ILE D 1 34  ? 0.356   39.968  -49.925 1.00 30.22  ? 63  ILE C O   1 
ATOM   10542 C CB  . ILE D 1 34  ? -1.572  39.463  -47.891 1.00 29.71  ? 63  ILE C CB  1 
ATOM   10543 C CG1 . ILE D 1 34  ? -2.952  39.518  -47.301 1.00 33.41  ? 63  ILE C CG1 1 
ATOM   10544 C CG2 . ILE D 1 34  ? -0.570  38.729  -47.001 1.00 31.01  ? 63  ILE C CG2 1 
ATOM   10545 C CD1 . ILE D 1 34  ? -3.692  38.191  -47.441 1.00 36.56  ? 63  ILE C CD1 1 
ATOM   10546 N N   . THR D 1 35  ? 1.347   41.217  -48.292 1.00 31.00  ? 64  THR C N   1 
ATOM   10547 C CA  . THR D 1 35  ? 2.712   41.069  -48.759 1.00 32.56  ? 64  THR C CA  1 
ATOM   10548 C C   . THR D 1 35  ? 3.451   40.005  -47.956 1.00 33.05  ? 64  THR C C   1 
ATOM   10549 O O   . THR D 1 35  ? 3.034   39.608  -46.883 1.00 30.12  ? 64  THR C O   1 
ATOM   10550 C CB  . THR D 1 35  ? 3.406   42.417  -48.637 1.00 36.09  ? 64  THR C CB  1 
ATOM   10551 O OG1 . THR D 1 35  ? 3.500   42.674  -47.237 1.00 37.12  ? 64  THR C OG1 1 
ATOM   10552 C CG2 . THR D 1 35  ? 2.652   43.509  -49.381 1.00 35.90  ? 64  THR C CG2 1 
ATOM   10553 N N   . VAL D 1 36  ? 4.585   39.581  -48.487 1.00 31.11  ? 65  VAL C N   1 
ATOM   10554 C CA  . VAL D 1 36  ? 5.485   38.697  -47.784 1.00 33.47  ? 65  VAL C CA  1 
ATOM   10555 C C   . VAL D 1 36  ? 5.919   39.294  -46.434 1.00 34.70  ? 65  VAL C C   1 
ATOM   10556 O O   . VAL D 1 36  ? 5.957   38.583  -45.425 1.00 34.55  ? 65  VAL C O   1 
ATOM   10557 C CB  . VAL D 1 36  ? 6.644   38.500  -48.749 1.00 33.95  ? 65  VAL C CB  1 
ATOM   10558 C CG1 . VAL D 1 36  ? 7.855   37.921  -48.022 1.00 37.32  ? 65  VAL C CG1 1 
ATOM   10559 C CG2 . VAL D 1 36  ? 6.193   37.682  -49.956 1.00 30.16  ? 65  VAL C CG2 1 
ATOM   10560 N N   . ASP D 1 37  ? 6.177   40.601  -46.405 1.00 32.00  ? 66  ASP C N   1 
ATOM   10561 C CA  . ASP D 1 37  ? 6.589   41.319  -45.205 1.00 36.12  ? 66  ASP C CA  1 
ATOM   10562 C C   . ASP D 1 37  ? 5.538   41.264  -44.097 1.00 40.44  ? 66  ASP C C   1 
ATOM   10563 O O   . ASP D 1 37  ? 5.918   41.240  -42.917 1.00 31.73  ? 66  ASP C O   1 
ATOM   10564 C CB  . ASP D 1 37  ? 6.881   42.786  -45.482 1.00 45.43  ? 66  ASP C CB  1 
ATOM   10565 C CG  . ASP D 1 37  ? 8.325   43.079  -45.895 1.00 57.36  ? 66  ASP C CG  1 
ATOM   10566 O OD1 . ASP D 1 37  ? 9.217   42.272  -45.539 1.00 51.83  ? 66  ASP C OD1 1 
ATOM   10567 O OD2 . ASP D 1 37  ? 8.551   44.093  -46.593 1.00 69.71  ? 66  ASP C OD2 1 
ATOM   10568 N N   . MET D 1 38  ? 4.244   41.307  -44.472 1.00 32.57  ? 67  MET C N   1 
ATOM   10569 C CA  . MET D 1 38  ? 3.197   41.253  -43.473 1.00 34.53  ? 67  MET C CA  1 
ATOM   10570 C C   . MET D 1 38  ? 3.193   39.882  -42.830 1.00 31.16  ? 67  MET C C   1 
ATOM   10571 O O   . MET D 1 38  ? 2.869   39.788  -41.665 1.00 32.76  ? 67  MET C O   1 
ATOM   10572 C CB  . MET D 1 38  ? 1.795   41.516  -44.019 1.00 33.87  ? 67  MET C CB  1 
ATOM   10573 C CG  . MET D 1 38  ? 1.567   42.938  -44.450 1.00 39.08  ? 67  MET C CG  1 
ATOM   10574 S SD  . MET D 1 38  ? 0.087   43.106  -45.471 1.00 42.71  ? 67  MET C SD  1 
ATOM   10575 C CE  . MET D 1 38  ? 0.589   44.466  -46.540 1.00 40.91  ? 67  MET C CE  1 
ATOM   10576 N N   . MET D 1 39  ? 3.465   38.835  -43.615 1.00 28.35  ? 68  MET C N   1 
ATOM   10577 C CA  . MET D 1 39  ? 3.438   37.478  -43.103 1.00 28.66  ? 68  MET C CA  1 
ATOM   10578 C C   . MET D 1 39  ? 4.558   37.286  -42.078 1.00 31.94  ? 68  MET C C   1 
ATOM   10579 O O   . MET D 1 39  ? 4.348   36.617  -41.064 1.00 29.65  ? 68  MET C O   1 
ATOM   10580 C CB  . MET D 1 39  ? 3.552   36.468  -44.246 1.00 29.83  ? 68  MET C CB  1 
ATOM   10581 C CG  . MET D 1 39  ? 2.403   36.575  -45.217 1.00 30.46  ? 68  MET C CG  1 
ATOM   10582 S SD  . MET D 1 39  ? 2.410   35.240  -46.414 1.00 33.53  ? 68  MET C SD  1 
ATOM   10583 C CE  . MET D 1 39  ? 2.137   33.780  -45.395 1.00 33.78  ? 68  MET C CE  1 
ATOM   10584 N N   . TYR D 1 40  ? 5.752   37.824  -42.379 1.00 27.69  ? 69  TYR C N   1 
ATOM   10585 C CA  . TYR D 1 40  ? 6.875   37.770  -41.465 1.00 29.38  ? 69  TYR C CA  1 
ATOM   10586 C C   . TYR D 1 40  ? 6.678   38.770  -40.333 1.00 33.28  ? 69  TYR C C   1 
ATOM   10587 O O   . TYR D 1 40  ? 7.192   38.530  -39.261 1.00 32.66  ? 69  TYR C O   1 
ATOM   10588 C CB  . TYR D 1 40  ? 8.191   38.009  -42.200 1.00 28.02  ? 69  TYR C CB  1 
ATOM   10589 C CG  . TYR D 1 40  ? 8.723   36.843  -43.012 1.00 25.27  ? 69  TYR C CG  1 
ATOM   10590 C CD1 . TYR D 1 40  ? 9.265   35.747  -42.377 1.00 27.58  ? 69  TYR C CD1 1 
ATOM   10591 C CD2 . TYR D 1 40  ? 8.599   36.788  -44.389 1.00 32.09  ? 69  TYR C CD2 1 
ATOM   10592 C CE1 . TYR D 1 40  ? 9.741   34.651  -43.080 1.00 32.22  ? 69  TYR C CE1 1 
ATOM   10593 C CE2 . TYR D 1 40  ? 9.058   35.690  -45.109 1.00 31.83  ? 69  TYR C CE2 1 
ATOM   10594 C CZ  . TYR D 1 40  ? 9.662   34.623  -44.463 1.00 32.55  ? 69  TYR C CZ  1 
ATOM   10595 O OH  . TYR D 1 40  ? 10.142  33.512  -45.148 1.00 30.83  ? 69  TYR C OH  1 
ATOM   10596 N N   . GLY D 1 41  ? 5.898   39.835  -40.554 1.00 28.24  ? 70  GLY C N   1 
ATOM   10597 C CA  . GLY D 1 41  ? 5.780   40.935  -39.612 1.00 29.46  ? 70  GLY C CA  1 
ATOM   10598 C C   . GLY D 1 41  ? 4.574   40.815  -38.679 1.00 31.94  ? 70  GLY C C   1 
ATOM   10599 O O   . GLY D 1 41  ? 4.071   41.805  -38.156 1.00 32.27  ? 70  GLY C O   1 
ATOM   10600 N N   . GLY D 1 42  ? 4.111   39.601  -38.422 1.00 32.53  ? 71  GLY C N   1 
ATOM   10601 C CA  . GLY D 1 42  ? 3.028   39.450  -37.465 1.00 34.54  ? 71  GLY C CA  1 
ATOM   10602 C C   . GLY D 1 42  ? 1.769   40.188  -37.911 1.00 28.54  ? 71  GLY C C   1 
ATOM   10603 O O   . GLY D 1 42  ? 1.103   40.817  -37.111 1.00 32.87  ? 71  GLY C O   1 
ATOM   10604 N N   . MET D 1 43  ? 1.423   40.056  -39.181 1.00 29.73  ? 72  MET C N   1 
ATOM   10605 C CA  . MET D 1 43  ? 0.171   40.551  -39.746 1.00 36.62  ? 72  MET C CA  1 
ATOM   10606 C C   . MET D 1 43  ? -0.007  42.066  -39.596 1.00 35.99  ? 72  MET C C   1 
ATOM   10607 O O   . MET D 1 43  ? -1.141  42.563  -39.577 1.00 32.07  ? 72  MET C O   1 
ATOM   10608 C CB  . MET D 1 43  ? -1.034  39.888  -39.077 1.00 44.26  ? 72  MET C CB  1 
ATOM   10609 C CG  . MET D 1 43  ? -1.122  38.401  -39.321 1.00 47.25  ? 72  MET C CG  1 
ATOM   10610 S SD  . MET D 1 43  ? -2.732  37.737  -38.847 1.00 50.28  ? 72  MET C SD  1 
ATOM   10611 C CE  . MET D 1 43  ? -2.640  37.943  -37.079 1.00 54.30  ? 72  MET C CE  1 
ATOM   10612 N N   . ARG D 1 44  ? 1.097   42.794  -39.449 1.00 32.47  ? 73  ARG C N   1 
ATOM   10613 C CA  . ARG D 1 44  ? 1.013   44.219  -39.189 1.00 39.43  ? 73  ARG C CA  1 
ATOM   10614 C C   . ARG D 1 44  ? 0.352   44.935  -40.378 1.00 35.32  ? 73  ARG C C   1 
ATOM   10615 O O   . ARG D 1 44  ? 0.717   44.730  -41.515 1.00 33.03  ? 73  ARG C O   1 
ATOM   10616 C CB  . ARG D 1 44  ? 2.404   44.781  -38.886 1.00 40.26  ? 73  ARG C CB  1 
ATOM   10617 C CG  . ARG D 1 44  ? 2.332   46.098  -38.124 1.00 47.49  ? 73  ARG C CG  1 
ATOM   10618 C CD  . ARG D 1 44  ? 1.712   45.928  -36.729 1.00 60.26  ? 73  ARG C CD  1 
ATOM   10619 N NE  . ARG D 1 44  ? 2.253   44.757  -36.020 1.00 68.78  ? 73  ARG C NE  1 
ATOM   10620 C CZ  . ARG D 1 44  ? 3.480   44.638  -35.526 1.00 68.81  ? 73  ARG C CZ  1 
ATOM   10621 N NH1 . ARG D 1 44  ? 4.276   45.695  -35.414 1.00 75.46  ? 73  ARG C NH1 1 
ATOM   10622 N NH2 . ARG D 1 44  ? 3.885   43.448  -35.115 1.00 63.40  ? 73  ARG C NH2 1 
ATOM   10623 N N   . GLY D 1 45  ? -0.705  45.699  -40.098 1.00 49.65  ? 74  GLY C N   1 
ATOM   10624 C CA  . GLY D 1 45  ? -1.409  46.455  -41.125 1.00 51.96  ? 74  GLY C CA  1 
ATOM   10625 C C   . GLY D 1 45  ? -2.340  45.596  -41.971 1.00 49.96  ? 74  GLY C C   1 
ATOM   10626 O O   . GLY D 1 45  ? -2.812  46.077  -42.996 1.00 54.45  ? 74  GLY C O   1 
ATOM   10627 N N   . MET D 1 46  ? -2.566  44.335  -41.564 1.00 43.10  ? 75  MET C N   1 
ATOM   10628 C CA  . MET D 1 46  ? -3.549  43.493  -42.213 1.00 39.51  ? 75  MET C CA  1 
ATOM   10629 C C   . MET D 1 46  ? -4.850  43.619  -41.447 1.00 37.19  ? 75  MET C C   1 
ATOM   10630 O O   . MET D 1 46  ? -4.872  43.385  -40.240 1.00 34.55  ? 75  MET C O   1 
ATOM   10631 C CB  . MET D 1 46  ? -3.172  42.012  -42.219 1.00 42.59  ? 75  MET C CB  1 
ATOM   10632 C CG  . MET D 1 46  ? -2.218  41.615  -43.326 1.00 45.25  ? 75  MET C CG  1 
ATOM   10633 S SD  . MET D 1 46  ? -1.540  39.971  -43.005 1.00 50.62  ? 75  MET C SD  1 
ATOM   10634 C CE  . MET D 1 46  ? -3.068  39.061  -42.848 1.00 40.99  ? 75  MET C CE  1 
ATOM   10635 N N   . LYS D 1 47  ? -5.907  43.974  -42.182 1.00 30.79  ? 76  LYS C N   1 
ATOM   10636 C CA  . LYS D 1 47  ? -7.258  44.012  -41.649 1.00 36.91  ? 76  LYS C CA  1 
ATOM   10637 C C   . LYS D 1 47  ? -7.792  42.589  -41.619 1.00 36.21  ? 76  LYS C C   1 
ATOM   10638 O O   . LYS D 1 47  ? -8.327  42.130  -42.624 1.00 49.39  ? 76  LYS C O   1 
ATOM   10639 C CB  . LYS D 1 47  ? -8.147  44.920  -42.507 1.00 36.59  ? 76  LYS C CB  1 
ATOM   10640 C CG  . LYS D 1 47  ? -7.802  46.404  -42.383 1.00 37.94  ? 76  LYS C CG  1 
ATOM   10641 C CD  . LYS D 1 47  ? -8.429  47.273  -43.466 1.00 44.72  ? 76  LYS C CD  1 
ATOM   10642 C CE  . LYS D 1 47  ? -8.447  48.761  -43.170 1.00 45.22  ? 76  LYS C CE  1 
ATOM   10643 N NZ  . LYS D 1 47  ? -7.147  49.418  -43.321 1.00 48.90  ? 76  LYS C NZ  1 
ATOM   10644 N N   . GLY D 1 48  ? -7.665  41.941  -40.456 1.00 32.35  ? 77  GLY C N   1 
ATOM   10645 C CA  . GLY D 1 48  ? -7.801  40.498  -40.329 1.00 35.22  ? 77  GLY C CA  1 
ATOM   10646 C C   . GLY D 1 48  ? -9.093  40.006  -39.675 1.00 34.42  ? 77  GLY C C   1 
ATOM   10647 O O   . GLY D 1 48  ? -9.519  38.870  -39.926 1.00 33.37  ? 77  GLY C O   1 
ATOM   10648 N N   . LEU D 1 49  ? -9.765  40.883  -38.922 1.00 33.91  ? 78  LEU C N   1 
ATOM   10649 C CA  . LEU D 1 49  ? -10.704 40.457  -37.897 1.00 37.14  ? 78  LEU C CA  1 
ATOM   10650 C C   . LEU D 1 49  ? -11.829 41.491  -37.807 1.00 31.71  ? 78  LEU C C   1 
ATOM   10651 O O   . LEU D 1 49  ? -11.554 42.674  -37.936 1.00 28.47  ? 78  LEU C O   1 
ATOM   10652 C CB  . LEU D 1 49  ? -9.859  40.476  -36.613 1.00 44.07  ? 78  LEU C CB  1 
ATOM   10653 C CG  . LEU D 1 49  ? -10.365 39.574  -35.491 1.00 51.68  ? 78  LEU C CG  1 
ATOM   10654 C CD1 . LEU D 1 49  ? -10.065 38.176  -35.992 1.00 57.64  ? 78  LEU C CD1 1 
ATOM   10655 C CD2 . LEU D 1 49  ? -9.752  39.813  -34.129 1.00 57.79  ? 78  LEU C CD2 1 
ATOM   10656 N N   . VAL D 1 50  ? -13.069 41.052  -37.629 1.00 30.13  ? 79  VAL C N   1 
ATOM   10657 C CA  . VAL D 1 50  ? -14.185 41.923  -37.300 1.00 32.08  ? 79  VAL C CA  1 
ATOM   10658 C C   . VAL D 1 50  ? -14.378 41.822  -35.797 1.00 32.16  ? 79  VAL C C   1 
ATOM   10659 O O   . VAL D 1 50  ? -14.512 40.722  -35.254 1.00 30.39  ? 79  VAL C O   1 
ATOM   10660 C CB  . VAL D 1 50  ? -15.509 41.598  -38.026 1.00 35.93  ? 79  VAL C CB  1 
ATOM   10661 C CG1 . VAL D 1 50  ? -16.689 42.412  -37.471 1.00 34.89  ? 79  VAL C CG1 1 
ATOM   10662 C CG2 . VAL D 1 50  ? -15.395 41.819  -39.519 1.00 34.65  ? 79  VAL C CG2 1 
ATOM   10663 N N   . TYR D 1 51  ? -14.360 42.980  -35.153 1.00 29.98  ? 80  TYR C N   1 
ATOM   10664 C CA  . TYR D 1 51  ? -14.529 43.077  -33.719 1.00 28.22  ? 80  TYR C CA  1 
ATOM   10665 C C   . TYR D 1 51  ? -15.348 44.344  -33.459 1.00 27.67  ? 80  TYR C C   1 
ATOM   10666 O O   . TYR D 1 51  ? -14.907 45.411  -33.814 1.00 29.38  ? 80  TYR C O   1 
ATOM   10667 C CB  . TYR D 1 51  ? -13.094 43.075  -33.168 1.00 27.60  ? 80  TYR C CB  1 
ATOM   10668 C CG  . TYR D 1 51  ? -12.916 42.880  -31.666 1.00 26.59  ? 80  TYR C CG  1 
ATOM   10669 C CD1 . TYR D 1 51  ? -12.935 43.976  -30.819 1.00 33.60  ? 80  TYR C CD1 1 
ATOM   10670 C CD2 . TYR D 1 51  ? -12.648 41.639  -31.106 1.00 28.79  ? 80  TYR C CD2 1 
ATOM   10671 C CE1 . TYR D 1 51  ? -12.770 43.837  -29.450 1.00 33.67  ? 80  TYR C CE1 1 
ATOM   10672 C CE2 . TYR D 1 51  ? -12.487 41.478  -29.727 1.00 33.49  ? 80  TYR C CE2 1 
ATOM   10673 C CZ  . TYR D 1 51  ? -12.544 42.585  -28.895 1.00 33.59  ? 80  TYR C CZ  1 
ATOM   10674 O OH  . TYR D 1 51  ? -12.371 42.517  -27.533 1.00 34.26  ? 80  TYR C OH  1 
ATOM   10675 N N   . GLU D 1 52  ? -16.519 44.222  -32.822 1.00 33.20  ? 81  GLU C N   1 
ATOM   10676 C CA  . GLU D 1 52  ? -17.567 45.235  -32.885 1.00 32.55  ? 81  GLU C CA  1 
ATOM   10677 C C   . GLU D 1 52  ? -17.460 46.252  -31.740 1.00 33.71  ? 81  GLU C C   1 
ATOM   10678 O O   . GLU D 1 52  ? -17.894 47.414  -31.879 1.00 32.39  ? 81  GLU C O   1 
ATOM   10679 C CB  . GLU D 1 52  ? -18.946 44.580  -32.861 1.00 36.19  ? 81  GLU C CB  1 
ATOM   10680 C CG  . GLU D 1 52  ? -19.150 43.521  -33.942 1.00 45.78  ? 81  GLU C CG  1 
ATOM   10681 C CD  . GLU D 1 52  ? -19.224 44.065  -35.360 1.00 45.50  ? 81  GLU C CD  1 
ATOM   10682 O OE1 . GLU D 1 52  ? -18.903 45.258  -35.547 1.00 47.32  ? 81  GLU C OE1 1 
ATOM   10683 O OE2 . GLU D 1 52  ? -19.646 43.317  -36.269 1.00 46.65  ? 81  GLU C OE2 1 
ATOM   10684 N N   . THR D 1 53  ? -16.829 45.853  -30.633 1.00 30.39  ? 82  THR C N   1 
ATOM   10685 C CA  . THR D 1 53  ? -17.004 46.590  -29.393 1.00 31.77  ? 82  THR C CA  1 
ATOM   10686 C C   . THR D 1 53  ? -16.179 47.865  -29.365 1.00 31.82  ? 82  THR C C   1 
ATOM   10687 O O   . THR D 1 53  ? -16.597 48.830  -28.733 1.00 31.58  ? 82  THR C O   1 
ATOM   10688 C CB  . THR D 1 53  ? -16.725 45.718  -28.167 1.00 31.67  ? 82  THR C CB  1 
ATOM   10689 O OG1 . THR D 1 53  ? -15.445 45.123  -28.316 1.00 32.98  ? 82  THR C OG1 1 
ATOM   10690 C CG2 . THR D 1 53  ? -17.800 44.677  -27.963 1.00 28.51  ? 82  THR C CG2 1 
ATOM   10691 N N   . SER D 1 54  ? -14.986 47.854  -29.953 1.00 33.95  ? 83  SER C N   1 
ATOM   10692 C CA  . SER D 1 54  ? -14.152 49.041  -29.906 1.00 34.72  ? 83  SER C CA  1 
ATOM   10693 C C   . SER D 1 54  ? -13.270 49.144  -31.137 1.00 38.18  ? 83  SER C C   1 
ATOM   10694 O O   . SER D 1 54  ? -12.964 48.157  -31.805 1.00 35.71  ? 83  SER C O   1 
ATOM   10695 C CB  . SER D 1 54  ? -13.330 49.123  -28.660 1.00 34.89  ? 83  SER C CB  1 
ATOM   10696 O OG  . SER D 1 54  ? -12.336 48.128  -28.587 1.00 33.49  ? 83  SER C OG  1 
ATOM   10697 N N   . VAL D 1 55  ? -12.888 50.378  -31.433 1.00 39.51  ? 84  VAL C N   1 
ATOM   10698 C CA  . VAL D 1 55  ? -12.128 50.643  -32.632 1.00 39.19  ? 84  VAL C CA  1 
ATOM   10699 C C   . VAL D 1 55  ? -11.044 51.635  -32.269 1.00 38.94  ? 84  VAL C C   1 
ATOM   10700 O O   . VAL D 1 55  ? -11.292 52.567  -31.521 1.00 35.24  ? 84  VAL C O   1 
ATOM   10701 C CB  . VAL D 1 55  ? -12.939 51.127  -33.844 1.00 46.62  ? 84  VAL C CB  1 
ATOM   10702 C CG1 . VAL D 1 55  ? -12.086 51.041  -35.105 1.00 48.95  ? 84  VAL C CG1 1 
ATOM   10703 C CG2 . VAL D 1 55  ? -14.212 50.305  -34.017 1.00 45.74  ? 84  VAL C CG2 1 
ATOM   10704 N N   . LEU D 1 56  ? -9.839  51.322  -32.764 1.00 50.54  ? 85  LEU C N   1 
ATOM   10705 C CA  . LEU D 1 56  ? -8.615  52.051  -32.495 1.00 66.18  ? 85  LEU C CA  1 
ATOM   10706 C C   . LEU D 1 56  ? -8.327  52.891  -33.728 1.00 66.98  ? 85  LEU C C   1 
ATOM   10707 O O   . LEU D 1 56  ? -7.803  52.356  -34.709 1.00 67.74  ? 85  LEU C O   1 
ATOM   10708 C CB  . LEU D 1 56  ? -7.453  51.071  -32.291 1.00 70.20  ? 85  LEU C CB  1 
ATOM   10709 C CG  . LEU D 1 56  ? -6.532  51.319  -31.098 1.00 77.18  ? 85  LEU C CG  1 
ATOM   10710 C CD1 . LEU D 1 56  ? -6.313  52.792  -30.726 1.00 66.82  ? 85  LEU C CD1 1 
ATOM   10711 C CD2 . LEU D 1 56  ? -7.198  50.516  -29.990 1.00 88.75  ? 85  LEU C CD2 1 
ATOM   10712 N N   . ASP D 1 57  ? -8.702  54.169  -33.719 1.00 55.83  ? 86  ASP C N   1 
ATOM   10713 C CA  . ASP D 1 57  ? -8.145  55.047  -34.729 1.00 66.30  ? 86  ASP C CA  1 
ATOM   10714 C C   . ASP D 1 57  ? -6.630  55.145  -34.466 1.00 67.09  ? 86  ASP C C   1 
ATOM   10715 O O   . ASP D 1 57  ? -6.219  55.391  -33.331 1.00 68.75  ? 86  ASP C O   1 
ATOM   10716 C CB  . ASP D 1 57  ? -8.929  56.350  -34.775 1.00 73.00  ? 86  ASP C CB  1 
ATOM   10717 C CG  . ASP D 1 57  ? -8.643  57.217  -35.994 1.00 76.55  ? 86  ASP C CG  1 
ATOM   10718 O OD1 . ASP D 1 57  ? -7.642  56.945  -36.685 1.00 70.63  ? 86  ASP C OD1 1 
ATOM   10719 O OD2 . ASP D 1 57  ? -9.448  58.134  -36.265 1.00 95.77  ? 86  ASP C OD2 1 
ATOM   10720 N N   . PRO D 1 58  ? -5.720  54.862  -35.440 1.00 71.45  ? 87  PRO C N   1 
ATOM   10721 C CA  . PRO D 1 58  ? -4.303  55.172  -35.255 1.00 74.76  ? 87  PRO C CA  1 
ATOM   10722 C C   . PRO D 1 58  ? -4.326  56.691  -35.167 1.00 88.73  ? 87  PRO C C   1 
ATOM   10723 O O   . PRO D 1 58  ? -5.068  57.329  -35.915 1.00 101.92 ? 87  PRO C O   1 
ATOM   10724 C CB  . PRO D 1 58  ? -3.578  54.641  -36.507 1.00 69.71  ? 87  PRO C CB  1 
ATOM   10725 C CG  . PRO D 1 58  ? -4.594  53.734  -37.184 1.00 68.03  ? 87  PRO C CG  1 
ATOM   10726 C CD  . PRO D 1 58  ? -5.968  54.240  -36.753 1.00 73.15  ? 87  PRO C CD  1 
ATOM   10727 N N   . ASP D 1 59  ? -3.590  57.267  -34.215 1.00 93.76  ? 88  ASP C N   1 
ATOM   10728 C CA  . ASP D 1 59  ? -3.581  58.716  -34.054 1.00 110.40 ? 88  ASP C CA  1 
ATOM   10729 C C   . ASP D 1 59  ? -4.697  59.166  -33.104 1.00 108.00 ? 88  ASP C C   1 
ATOM   10730 O O   . ASP D 1 59  ? -4.405  59.818  -32.103 1.00 116.96 ? 88  ASP C O   1 
ATOM   10731 C CB  . ASP D 1 59  ? -3.663  59.467  -35.383 1.00 109.39 ? 88  ASP C CB  1 
ATOM   10732 C CG  . ASP D 1 59  ? -2.456  59.356  -36.308 1.00 110.63 ? 88  ASP C CG  1 
ATOM   10733 O OD1 . ASP D 1 59  ? -1.415  59.968  -35.998 1.00 116.87 ? 88  ASP C OD1 1 
ATOM   10734 O OD2 . ASP D 1 59  ? -2.571  58.684  -37.354 1.00 108.85 ? 88  ASP C OD2 1 
ATOM   10735 N N   . GLU D 1 60  ? -5.964  58.824  -33.406 1.00 96.86  ? 89  GLU C N   1 
ATOM   10736 C CA  . GLU D 1 60  ? -7.114  59.456  -32.762 1.00 91.87  ? 89  GLU C CA  1 
ATOM   10737 C C   . GLU D 1 60  ? -7.541  58.765  -31.462 1.00 88.07  ? 89  GLU C C   1 
ATOM   10738 O O   . GLU D 1 60  ? -8.234  59.381  -30.654 1.00 86.39  ? 89  GLU C O   1 
ATOM   10739 C CB  . GLU D 1 60  ? -8.319  59.545  -33.698 1.00 94.79  ? 89  GLU C CB  1 
ATOM   10740 C CG  . GLU D 1 60  ? -8.069  60.376  -34.954 1.00 98.69  ? 89  GLU C CG  1 
ATOM   10741 C CD  . GLU D 1 60  ? -7.446  61.731  -34.678 1.00 97.39  ? 89  GLU C CD  1 
ATOM   10742 O OE1 . GLU D 1 60  ? -7.865  62.369  -33.681 1.00 81.20  ? 89  GLU C OE1 1 
ATOM   10743 O OE2 . GLU D 1 60  ? -6.553  62.137  -35.462 1.00 101.45 ? 89  GLU C OE2 1 
ATOM   10744 N N   . GLY D 1 61  ? -7.165  57.494  -31.262 1.00 81.82  ? 90  GLY C N   1 
ATOM   10745 C CA  . GLY D 1 61  ? -7.358  56.830  -29.978 1.00 74.34  ? 90  GLY C CA  1 
ATOM   10746 C C   . GLY D 1 61  ? -8.515  55.830  -29.986 1.00 62.33  ? 90  GLY C C   1 
ATOM   10747 O O   . GLY D 1 61  ? -9.087  55.533  -31.029 1.00 44.53  ? 90  GLY C O   1 
ATOM   10748 N N   . ILE D 1 62  ? -8.853  55.311  -28.799 1.00 56.37  ? 91  ILE C N   1 
ATOM   10749 C CA  . ILE D 1 62  ? -9.789  54.207  -28.689 1.00 43.58  ? 91  ILE C CA  1 
ATOM   10750 C C   . ILE D 1 62  ? -11.199 54.775  -28.588 1.00 41.32  ? 91  ILE C C   1 
ATOM   10751 O O   . ILE D 1 62  ? -11.416 55.703  -27.825 1.00 39.39  ? 91  ILE C O   1 
ATOM   10752 C CB  . ILE D 1 62  ? -9.447  53.291  -27.494 1.00 41.64  ? 91  ILE C CB  1 
ATOM   10753 C CG1 . ILE D 1 62  ? -10.367 52.079  -27.406 1.00 41.49  ? 91  ILE C CG1 1 
ATOM   10754 C CG2 . ILE D 1 62  ? -9.453  54.047  -26.172 1.00 41.35  ? 91  ILE C CG2 1 
ATOM   10755 C CD1 . ILE D 1 62  ? -10.168 51.084  -28.525 1.00 47.55  ? 91  ILE C CD1 1 
ATOM   10756 N N   . ARG D 1 63  ? -12.149 54.204  -29.357 1.00 37.92  ? 92  ARG C N   1 
ATOM   10757 C CA  . ARG D 1 63  ? -13.560 54.477  -29.125 1.00 39.70  ? 92  ARG C CA  1 
ATOM   10758 C C   . ARG D 1 63  ? -14.244 53.187  -28.705 1.00 33.84  ? 92  ARG C C   1 
ATOM   10759 O O   . ARG D 1 63  ? -13.989 52.135  -29.278 1.00 36.84  ? 92  ARG C O   1 
ATOM   10760 C CB  . ARG D 1 63  ? -14.295 55.144  -30.293 1.00 43.07  ? 92  ARG C CB  1 
ATOM   10761 C CG  . ARG D 1 63  ? -13.764 56.542  -30.606 1.00 49.07  ? 92  ARG C CG  1 
ATOM   10762 C CD  . ARG D 1 63  ? -14.444 57.215  -31.794 1.00 52.90  ? 92  ARG C CD  1 
ATOM   10763 N NE  . ARG D 1 63  ? -14.028 58.608  -31.978 1.00 55.96  ? 92  ARG C NE  1 
ATOM   10764 C CZ  . ARG D 1 63  ? -14.647 59.685  -31.480 1.00 60.30  ? 92  ARG C CZ  1 
ATOM   10765 N NH1 . ARG D 1 63  ? -15.621 59.578  -30.591 1.00 58.62  ? 92  ARG C NH1 1 
ATOM   10766 N NH2 . ARG D 1 63  ? -14.259 60.888  -31.854 1.00 62.11  ? 92  ARG C NH2 1 
ATOM   10767 N N   . PHE D 1 64  ? -15.098 53.317  -27.690 1.00 34.16  ? 93  PHE C N   1 
ATOM   10768 C CA  . PHE D 1 64  ? -15.967 52.265  -27.194 1.00 35.53  ? 93  PHE C CA  1 
ATOM   10769 C C   . PHE D 1 64  ? -17.342 52.437  -27.829 1.00 37.21  ? 93  PHE C C   1 
ATOM   10770 O O   . PHE D 1 64  ? -18.061 53.393  -27.511 1.00 36.17  ? 93  PHE C O   1 
ATOM   10771 C CB  . PHE D 1 64  ? -16.024 52.397  -25.670 1.00 34.27  ? 93  PHE C CB  1 
ATOM   10772 C CG  . PHE D 1 64  ? -14.689 52.212  -24.964 1.00 37.09  ? 93  PHE C CG  1 
ATOM   10773 C CD1 . PHE D 1 64  ? -13.855 51.130  -25.274 1.00 41.46  ? 93  PHE C CD1 1 
ATOM   10774 C CD2 . PHE D 1 64  ? -14.279 53.087  -23.965 1.00 34.86  ? 93  PHE C CD2 1 
ATOM   10775 C CE1 . PHE D 1 64  ? -12.628 50.971  -24.637 1.00 43.09  ? 93  PHE C CE1 1 
ATOM   10776 C CE2 . PHE D 1 64  ? -13.051 52.921  -23.340 1.00 42.03  ? 93  PHE C CE2 1 
ATOM   10777 C CZ  . PHE D 1 64  ? -12.226 51.867  -23.669 1.00 39.24  ? 93  PHE C CZ  1 
ATOM   10778 N N   . ARG D 1 65  ? -17.653 51.578  -28.808 1.00 33.73  ? 94  ARG C N   1 
ATOM   10779 C CA  . ARG D 1 65  ? -18.907 51.671  -29.543 1.00 33.97  ? 94  ARG C CA  1 
ATOM   10780 C C   . ARG D 1 65  ? -19.185 53.114  -29.963 1.00 33.86  ? 94  ARG C C   1 
ATOM   10781 O O   . ARG D 1 65  ? -20.301 53.589  -29.760 1.00 32.23  ? 94  ARG C O   1 
ATOM   10782 C CB  . ARG D 1 65  ? -20.112 51.221  -28.723 1.00 31.40  ? 94  ARG C CB  1 
ATOM   10783 C CG  . ARG D 1 65  ? -20.144 49.748  -28.395 1.00 33.98  ? 94  ARG C CG  1 
ATOM   10784 C CD  . ARG D 1 65  ? -20.450 48.851  -29.598 1.00 37.28  ? 94  ARG C CD  1 
ATOM   10785 N NE  . ARG D 1 65  ? -20.754 47.469  -29.184 1.00 33.96  ? 94  ARG C NE  1 
ATOM   10786 C CZ  . ARG D 1 65  ? -21.273 46.588  -30.015 1.00 38.60  ? 94  ARG C CZ  1 
ATOM   10787 N NH1 . ARG D 1 65  ? -21.461 46.921  -31.284 1.00 34.58  ? 94  ARG C NH1 1 
ATOM   10788 N NH2 . ARG D 1 65  ? -21.613 45.384  -29.591 1.00 38.87  ? 94  ARG C NH2 1 
ATOM   10789 N N   . GLY D 1 66  ? -18.169 53.778  -30.538 1.00 33.36  ? 95  GLY C N   1 
ATOM   10790 C CA  . GLY D 1 66  ? -18.310 55.135  -31.060 1.00 37.09  ? 95  GLY C CA  1 
ATOM   10791 C C   . GLY D 1 66  ? -17.919 56.225  -30.052 1.00 41.02  ? 95  GLY C C   1 
ATOM   10792 O O   . GLY D 1 66  ? -17.726 57.376  -30.444 1.00 36.70  ? 95  GLY C O   1 
ATOM   10793 N N   . PHE D 1 67  ? -17.746 55.874  -28.770 1.00 39.56  ? 96  PHE C N   1 
ATOM   10794 C CA  . PHE D 1 67  ? -17.505 56.882  -27.741 1.00 42.67  ? 96  PHE C CA  1 
ATOM   10795 C C   . PHE D 1 67  ? -16.026 56.919  -27.323 1.00 44.02  ? 96  PHE C C   1 
ATOM   10796 O O   . PHE D 1 67  ? -15.441 55.908  -26.921 1.00 46.66  ? 96  PHE C O   1 
ATOM   10797 C CB  . PHE D 1 67  ? -18.396 56.660  -26.517 1.00 38.91  ? 96  PHE C CB  1 
ATOM   10798 C CG  . PHE D 1 67  ? -19.885 56.814  -26.798 1.00 47.97  ? 96  PHE C CG  1 
ATOM   10799 C CD1 . PHE D 1 67  ? -20.623 55.780  -27.367 1.00 47.61  ? 96  PHE C CD1 1 
ATOM   10800 C CD2 . PHE D 1 67  ? -20.548 58.008  -26.514 1.00 47.42  ? 96  PHE C CD2 1 
ATOM   10801 C CE1 . PHE D 1 67  ? -21.983 55.926  -27.614 1.00 51.48  ? 96  PHE C CE1 1 
ATOM   10802 C CE2 . PHE D 1 67  ? -21.899 58.152  -26.783 1.00 46.11  ? 96  PHE C CE2 1 
ATOM   10803 C CZ  . PHE D 1 67  ? -22.622 57.108  -27.313 1.00 51.25  ? 96  PHE C CZ  1 
ATOM   10804 N N   . SER D 1 68  ? -15.458 58.130  -27.352 1.00 38.14  ? 97  SER C N   1 
ATOM   10805 C CA  . SER D 1 68  ? -14.141 58.425  -26.797 1.00 40.49  ? 97  SER C CA  1 
ATOM   10806 C C   . SER D 1 68  ? -14.130 58.273  -25.279 1.00 32.18  ? 97  SER C C   1 
ATOM   10807 O O   . SER D 1 68  ? -15.159 58.351  -24.616 1.00 34.17  ? 97  SER C O   1 
ATOM   10808 C CB  . SER D 1 68  ? -13.741 59.828  -27.129 1.00 39.52  ? 97  SER C CB  1 
ATOM   10809 O OG  . SER D 1 68  ? -14.510 60.660  -26.273 1.00 39.93  ? 97  SER C OG  1 
ATOM   10810 N N   . ILE D 1 69  ? -12.936 58.147  -24.700 1.00 37.78  ? 98  ILE C N   1 
ATOM   10811 C CA  . ILE D 1 69  ? -12.829 58.042  -23.248 1.00 38.97  ? 98  ILE C CA  1 
ATOM   10812 C C   . ILE D 1 69  ? -13.368 59.316  -22.563 1.00 40.42  ? 98  ILE C C   1 
ATOM   10813 O O   . ILE D 1 69  ? -14.179 59.224  -21.636 1.00 39.02  ? 98  ILE C O   1 
ATOM   10814 C CB  . ILE D 1 69  ? -11.397 57.640  -22.838 1.00 43.21  ? 98  ILE C CB  1 
ATOM   10815 C CG1 . ILE D 1 69  ? -11.143 56.153  -23.116 1.00 40.25  ? 98  ILE C CG1 1 
ATOM   10816 C CG2 . ILE D 1 69  ? -11.106 57.960  -21.368 1.00 41.78  ? 98  ILE C CG2 1 
ATOM   10817 C CD1 . ILE D 1 69  ? -9.685  55.819  -23.353 1.00 42.53  ? 98  ILE C CD1 1 
ATOM   10818 N N   . PRO D 1 70  ? -12.997 60.558  -22.963 1.00 41.66  ? 99  PRO C N   1 
ATOM   10819 C CA  . PRO D 1 70  ? -13.665 61.740  -22.396 1.00 41.39  ? 99  PRO C CA  1 
ATOM   10820 C C   . PRO D 1 70  ? -15.197 61.630  -22.392 1.00 43.25  ? 99  PRO C C   1 
ATOM   10821 O O   . PRO D 1 70  ? -15.834 61.860  -21.353 1.00 42.05  ? 99  PRO C O   1 
ATOM   10822 C CB  . PRO D 1 70  ? -13.140 62.895  -23.276 1.00 41.39  ? 99  PRO C CB  1 
ATOM   10823 C CG  . PRO D 1 70  ? -11.755 62.439  -23.689 1.00 42.57  ? 99  PRO C CG  1 
ATOM   10824 C CD  . PRO D 1 70  ? -11.898 60.913  -23.888 1.00 41.84  ? 99  PRO C CD  1 
ATOM   10825 N N   . GLU D 1 71  ? -15.779 61.229  -23.541 1.00 42.54  ? 100 GLU C N   1 
ATOM   10826 C CA  . GLU D 1 71  ? -17.230 61.138  -23.691 1.00 39.24  ? 100 GLU C CA  1 
ATOM   10827 C C   . GLU D 1 71  ? -17.768 60.117  -22.704 1.00 40.98  ? 100 GLU C C   1 
ATOM   10828 O O   . GLU D 1 71  ? -18.805 60.339  -22.089 1.00 38.88  ? 100 GLU C O   1 
ATOM   10829 C CB  . GLU D 1 71  ? -17.678 60.751  -25.101 1.00 43.37  ? 100 GLU C CB  1 
ATOM   10830 C CG  . GLU D 1 71  ? -17.547 61.870  -26.128 1.00 48.04  ? 100 GLU C CG  1 
ATOM   10831 C CD  . GLU D 1 71  ? -17.443 61.419  -27.593 1.00 60.43  ? 100 GLU C CD  1 
ATOM   10832 O OE1 . GLU D 1 71  ? -17.154 60.233  -27.854 1.00 60.73  ? 100 GLU C OE1 1 
ATOM   10833 O OE2 . GLU D 1 71  ? -17.635 62.248  -28.513 1.00 58.75  ? 100 GLU C OE2 1 
ATOM   10834 N N   . CYS D 1 72  ? -17.029 59.005  -22.527 1.00 40.85  ? 101 CYS C N   1 
ATOM   10835 C CA  . CYS D 1 72  ? -17.409 57.995  -21.555 1.00 36.36  ? 101 CYS C CA  1 
ATOM   10836 C C   . CYS D 1 72  ? -17.383 58.555  -20.141 1.00 37.16  ? 101 CYS C C   1 
ATOM   10837 O O   . CYS D 1 72  ? -18.291 58.277  -19.365 1.00 40.60  ? 101 CYS C O   1 
ATOM   10838 C CB  . CYS D 1 72  ? -16.543 56.739  -21.638 1.00 39.98  ? 101 CYS C CB  1 
ATOM   10839 S SG  . CYS D 1 72  ? -16.921 55.730  -23.094 1.00 44.19  ? 101 CYS C SG  1 
ATOM   10840 N N   . GLN D 1 73  ? -16.315 59.272  -19.785 1.00 41.09  ? 102 GLN C N   1 
ATOM   10841 C CA  . GLN D 1 73  ? -16.196 59.833  -18.442 1.00 47.36  ? 102 GLN C CA  1 
ATOM   10842 C C   . GLN D 1 73  ? -17.334 60.799  -18.161 1.00 41.81  ? 102 GLN C C   1 
ATOM   10843 O O   . GLN D 1 73  ? -17.884 60.818  -17.063 1.00 42.30  ? 102 GLN C O   1 
ATOM   10844 C CB  . GLN D 1 73  ? -14.911 60.624  -18.260 1.00 50.20  ? 102 GLN C CB  1 
ATOM   10845 C CG  . GLN D 1 73  ? -13.720 59.741  -17.931 1.00 53.38  ? 102 GLN C CG  1 
ATOM   10846 C CD  . GLN D 1 73  ? -12.435 60.463  -18.243 1.00 56.57  ? 102 GLN C CD  1 
ATOM   10847 O OE1 . GLN D 1 73  ? -12.067 60.648  -19.410 1.00 57.09  ? 102 GLN C OE1 1 
ATOM   10848 N NE2 . GLN D 1 73  ? -11.773 60.921  -17.194 1.00 52.89  ? 102 GLN C NE2 1 
ATOM   10849 N N   . LYS D 1 74  ? -17.706 61.537  -19.203 1.00 46.33  ? 103 LYS C N   1 
ATOM   10850 C CA  . LYS D 1 74  ? -18.837 62.441  -19.159 1.00 48.07  ? 103 LYS C CA  1 
ATOM   10851 C C   . LYS D 1 74  ? -20.138 61.648  -19.047 1.00 42.89  ? 103 LYS C C   1 
ATOM   10852 O O   . LYS D 1 74  ? -20.943 61.977  -18.181 1.00 40.73  ? 103 LYS C O   1 
ATOM   10853 C CB  . LYS D 1 74  ? -18.787 63.390  -20.367 1.00 53.82  ? 103 LYS C CB  1 
ATOM   10854 C CG  . LYS D 1 74  ? -19.938 64.372  -20.476 1.00 63.58  ? 103 LYS C CG  1 
ATOM   10855 C CD  . LYS D 1 74  ? -19.607 65.630  -21.272 1.00 76.11  ? 103 LYS C CD  1 
ATOM   10856 C CE  . LYS D 1 74  ? -20.576 66.765  -21.007 1.00 86.60  ? 103 LYS C CE  1 
ATOM   10857 N NZ  . LYS D 1 74  ? -20.439 67.387  -19.679 1.00 82.42  ? 103 LYS C NZ  1 
ATOM   10858 N N   . LEU D 1 75  ? -20.373 60.647  -19.921 1.00 37.12  ? 104 LEU C N   1 
ATOM   10859 C CA  . LEU D 1 75  ? -21.731 60.121  -20.125 1.00 38.23  ? 104 LEU C CA  1 
ATOM   10860 C C   . LEU D 1 75  ? -22.085 58.919  -19.237 1.00 38.66  ? 104 LEU C C   1 
ATOM   10861 O O   . LEU D 1 75  ? -23.272 58.721  -18.954 1.00 38.61  ? 104 LEU C O   1 
ATOM   10862 C CB  . LEU D 1 75  ? -22.011 59.764  -21.583 1.00 45.48  ? 104 LEU C CB  1 
ATOM   10863 C CG  . LEU D 1 75  ? -21.996 60.919  -22.586 1.00 43.23  ? 104 LEU C CG  1 
ATOM   10864 C CD1 . LEU D 1 75  ? -21.701 60.419  -23.985 1.00 44.52  ? 104 LEU C CD1 1 
ATOM   10865 C CD2 . LEU D 1 75  ? -23.330 61.654  -22.520 1.00 44.00  ? 104 LEU C CD2 1 
ATOM   10866 N N   . LEU D 1 76  ? -21.091 58.122  -18.810 1.00 35.18  ? 105 LEU C N   1 
ATOM   10867 C CA  . LEU D 1 76  ? -21.340 56.875  -18.082 1.00 33.65  ? 105 LEU C CA  1 
ATOM   10868 C C   . LEU D 1 76  ? -21.741 57.172  -16.638 1.00 38.26  ? 105 LEU C C   1 
ATOM   10869 O O   . LEU D 1 76  ? -21.220 58.091  -16.012 1.00 44.60  ? 105 LEU C O   1 
ATOM   10870 C CB  . LEU D 1 76  ? -20.142 55.932  -18.057 1.00 34.19  ? 105 LEU C CB  1 
ATOM   10871 C CG  . LEU D 1 76  ? -19.806 55.166  -19.339 1.00 36.78  ? 105 LEU C CG  1 
ATOM   10872 C CD1 . LEU D 1 76  ? -18.668 54.220  -18.946 1.00 35.43  ? 105 LEU C CD1 1 
ATOM   10873 C CD2 . LEU D 1 76  ? -20.960 54.400  -19.911 1.00 36.24  ? 105 LEU C CD2 1 
ATOM   10874 N N   . PRO D 1 77  ? -22.700 56.413  -16.068 1.00 41.15  ? 106 PRO C N   1 
ATOM   10875 C CA  . PRO D 1 77  ? -23.045 56.546  -14.646 1.00 41.22  ? 106 PRO C CA  1 
ATOM   10876 C C   . PRO D 1 77  ? -21.864 56.370  -13.691 1.00 44.47  ? 106 PRO C C   1 
ATOM   10877 O O   . PRO D 1 77  ? -20.974 55.576  -13.961 1.00 42.81  ? 106 PRO C O   1 
ATOM   10878 C CB  . PRO D 1 77  ? -24.082 55.456  -14.451 1.00 41.21  ? 106 PRO C CB  1 
ATOM   10879 C CG  . PRO D 1 77  ? -24.724 55.323  -15.832 1.00 42.56  ? 106 PRO C CG  1 
ATOM   10880 C CD  . PRO D 1 77  ? -23.569 55.468  -16.800 1.00 38.42  ? 106 PRO C CD  1 
ATOM   10881 N N   . LYS D 1 78  ? -21.885 57.115  -12.574 1.00 42.52  ? 107 LYS C N   1 
ATOM   10882 C CA  . LYS D 1 78  ? -20.820 57.143  -11.577 1.00 39.38  ? 107 LYS C CA  1 
ATOM   10883 C C   . LYS D 1 78  ? -21.399 56.574  -10.292 1.00 38.69  ? 107 LYS C C   1 
ATOM   10884 O O   . LYS D 1 78  ? -22.611 56.474  -10.187 1.00 37.33  ? 107 LYS C O   1 
ATOM   10885 C CB  . LYS D 1 78  ? -20.379 58.596  -11.418 1.00 41.43  ? 107 LYS C CB  1 
ATOM   10886 C CG  . LYS D 1 78  ? -19.816 59.190  -12.685 1.00 48.05  ? 107 LYS C CG  1 
ATOM   10887 C CD  . LYS D 1 78  ? -20.311 60.597  -12.967 1.00 64.20  ? 107 LYS C CD  1 
ATOM   10888 C CE  . LYS D 1 78  ? -19.940 61.025  -14.347 1.00 69.94  ? 107 LYS C CE  1 
ATOM   10889 N NZ  . LYS D 1 78  ? -18.487 61.122  -14.504 1.00 74.34  ? 107 LYS C NZ  1 
ATOM   10890 N N   . ALA D 1 79  ? -20.561 56.140  -9.345  1.00 41.17  ? 108 ALA C N   1 
ATOM   10891 C CA  . ALA D 1 79  ? -21.069 55.794  -8.025  1.00 42.80  ? 108 ALA C CA  1 
ATOM   10892 C C   . ALA D 1 79  ? -21.631 57.067  -7.387  1.00 44.92  ? 108 ALA C C   1 
ATOM   10893 O O   . ALA D 1 79  ? -21.308 58.170  -7.824  1.00 42.49  ? 108 ALA C O   1 
ATOM   10894 C CB  . ALA D 1 79  ? -19.990 55.182  -7.155  1.00 43.78  ? 108 ALA C CB  1 
ATOM   10895 N N   . LYS D 1 80  ? -22.477 56.911  -6.366  1.00 47.60  ? 109 LYS C N   1 
ATOM   10896 C CA  . LYS D 1 80  ? -23.041 58.062  -5.675  1.00 62.69  ? 109 LYS C CA  1 
ATOM   10897 C C   . LYS D 1 80  ? -21.920 58.873  -5.020  1.00 59.01  ? 109 LYS C C   1 
ATOM   10898 O O   . LYS D 1 80  ? -21.240 58.393  -4.113  1.00 57.66  ? 109 LYS C O   1 
ATOM   10899 C CB  . LYS D 1 80  ? -24.113 57.626  -4.666  1.00 62.99  ? 109 LYS C CB  1 
ATOM   10900 C CG  . LYS D 1 80  ? -25.322 56.949  -5.304  1.00 69.51  ? 109 LYS C CG  1 
ATOM   10901 C CD  . LYS D 1 80  ? -26.113 57.803  -6.294  1.00 70.33  ? 109 LYS C CD  1 
ATOM   10902 C CE  . LYS D 1 80  ? -27.027 56.973  -7.151  1.00 76.46  ? 109 LYS C CE  1 
ATOM   10903 N NZ  . LYS D 1 80  ? -27.804 56.010  -6.361  1.00 77.30  ? 109 LYS C NZ  1 
ATOM   10904 N N   . GLY D 1 81  ? -21.753 60.116  -5.498  1.00 55.31  ? 110 GLY C N   1 
ATOM   10905 C CA  . GLY D 1 81  ? -20.736 61.017  -4.985  1.00 60.98  ? 110 GLY C CA  1 
ATOM   10906 C C   . GLY D 1 81  ? -19.368 60.710  -5.589  1.00 64.88  ? 110 GLY C C   1 
ATOM   10907 O O   . GLY D 1 81  ? -18.334 61.086  -5.036  1.00 53.12  ? 110 GLY C O   1 
ATOM   10908 N N   . GLY D 1 82  ? -19.383 60.025  -6.738  1.00 63.92  ? 111 GLY C N   1 
ATOM   10909 C CA  . GLY D 1 82  ? -18.164 59.681  -7.437  1.00 55.85  ? 111 GLY C CA  1 
ATOM   10910 C C   . GLY D 1 82  ? -18.008 60.552  -8.673  1.00 53.76  ? 111 GLY C C   1 
ATOM   10911 O O   . GLY D 1 82  ? -18.959 61.159  -9.159  1.00 59.07  ? 111 GLY C O   1 
ATOM   10912 N N   . GLU D 1 83  ? -16.780 60.592  -9.172  1.00 50.34  ? 112 GLU C N   1 
ATOM   10913 C CA  . GLU D 1 83  ? -16.480 61.286  -10.402 1.00 48.88  ? 112 GLU C CA  1 
ATOM   10914 C C   . GLU D 1 83  ? -16.166 60.265  -11.500 1.00 43.96  ? 112 GLU C C   1 
ATOM   10915 O O   . GLU D 1 83  ? -16.190 60.609  -12.670 1.00 40.92  ? 112 GLU C O   1 
ATOM   10916 C CB  . GLU D 1 83  ? -15.346 62.277  -10.140 1.00 52.98  ? 112 GLU C CB  1 
ATOM   10917 C CG  . GLU D 1 83  ? -14.205 61.707  -9.295  1.00 72.07  ? 112 GLU C CG  1 
ATOM   10918 C CD  . GLU D 1 83  ? -12.866 62.420  -9.444  1.00 82.92  ? 112 GLU C CD  1 
ATOM   10919 O OE1 . GLU D 1 83  ? -11.853 61.684  -9.589  1.00 74.59  ? 112 GLU C OE1 1 
ATOM   10920 O OE2 . GLU D 1 83  ? -12.837 63.685  -9.446  1.00 75.77  ? 112 GLU C OE2 1 
ATOM   10921 N N   . GLU D 1 84  ? -15.884 59.010  -11.154 1.00 36.56  ? 113 GLU C N   1 
ATOM   10922 C CA  . GLU D 1 84  ? -15.283 58.132  -12.150 1.00 41.14  ? 113 GLU C CA  1 
ATOM   10923 C C   . GLU D 1 84  ? -16.334 57.159  -12.679 1.00 37.39  ? 113 GLU C C   1 
ATOM   10924 O O   . GLU D 1 84  ? -17.140 56.629  -11.916 1.00 40.66  ? 113 GLU C O   1 
ATOM   10925 C CB  . GLU D 1 84  ? -14.042 57.422  -11.610 1.00 39.52  ? 113 GLU C CB  1 
ATOM   10926 C CG  . GLU D 1 84  ? -12.881 58.361  -11.291 1.00 41.53  ? 113 GLU C CG  1 
ATOM   10927 C CD  . GLU D 1 84  ? -12.333 59.092  -12.497 1.00 48.20  ? 113 GLU C CD  1 
ATOM   10928 O OE1 . GLU D 1 84  ? -12.786 58.844  -13.633 1.00 52.31  ? 113 GLU C OE1 1 
ATOM   10929 O OE2 . GLU D 1 84  ? -11.462 59.951  -12.280 1.00 47.88  ? 113 GLU C OE2 1 
ATOM   10930 N N   . PRO D 1 85  ? -16.318 56.839  -13.994 1.00 42.34  ? 114 PRO C N   1 
ATOM   10931 C CA  . PRO D 1 85  ? -17.333 55.958  -14.572 1.00 40.37  ? 114 PRO C CA  1 
ATOM   10932 C C   . PRO D 1 85  ? -17.239 54.542  -14.004 1.00 36.65  ? 114 PRO C C   1 
ATOM   10933 O O   . PRO D 1 85  ? -16.151 54.056  -13.706 1.00 38.43  ? 114 PRO C O   1 
ATOM   10934 C CB  . PRO D 1 85  ? -17.024 56.050  -16.066 1.00 42.19  ? 114 PRO C CB  1 
ATOM   10935 C CG  . PRO D 1 85  ? -15.553 56.341  -16.128 1.00 46.16  ? 114 PRO C CG  1 
ATOM   10936 C CD  . PRO D 1 85  ? -15.311 57.275  -14.977 1.00 44.39  ? 114 PRO C CD  1 
ATOM   10937 N N   . LEU D 1 86  ? -18.387 53.905  -13.780 1.00 29.90  ? 115 LEU C N   1 
ATOM   10938 C CA  . LEU D 1 86  ? -18.376 52.562  -13.232 1.00 34.22  ? 115 LEU C CA  1 
ATOM   10939 C C   . LEU D 1 86  ? -18.111 51.582  -14.373 1.00 33.82  ? 115 LEU C C   1 
ATOM   10940 O O   . LEU D 1 86  ? -18.686 51.722  -15.437 1.00 33.23  ? 115 LEU C O   1 
ATOM   10941 C CB  . LEU D 1 86  ? -19.703 52.225  -12.576 1.00 35.31  ? 115 LEU C CB  1 
ATOM   10942 C CG  . LEU D 1 86  ? -20.069 52.989  -11.306 1.00 39.21  ? 115 LEU C CG  1 
ATOM   10943 C CD1 . LEU D 1 86  ? -21.279 52.294  -10.659 1.00 36.66  ? 115 LEU C CD1 1 
ATOM   10944 C CD2 . LEU D 1 86  ? -18.926 53.093  -10.330 1.00 41.27  ? 115 LEU C CD2 1 
ATOM   10945 N N   . PRO D 1 87  ? -17.206 50.599  -14.228 1.00 37.45  ? 116 PRO C N   1 
ATOM   10946 C CA  . PRO D 1 87  ? -17.068 49.553  -15.248 1.00 34.94  ? 116 PRO C CA  1 
ATOM   10947 C C   . PRO D 1 87  ? -18.358 48.854  -15.677 1.00 34.28  ? 116 PRO C C   1 
ATOM   10948 O O   . PRO D 1 87  ? -18.446 48.357  -16.786 1.00 33.44  ? 116 PRO C O   1 
ATOM   10949 C CB  . PRO D 1 87  ? -16.110 48.564  -14.593 1.00 32.61  ? 116 PRO C CB  1 
ATOM   10950 C CG  . PRO D 1 87  ? -15.325 49.382  -13.635 1.00 35.83  ? 116 PRO C CG  1 
ATOM   10951 C CD  . PRO D 1 87  ? -16.193 50.528  -13.169 1.00 33.31  ? 116 PRO C CD  1 
ATOM   10952 N N   . GLU D 1 88  ? -19.359 48.795  -14.795 1.00 33.43  ? 117 GLU C N   1 
ATOM   10953 C CA  . GLU D 1 88  ? -20.628 48.180  -15.136 1.00 30.23  ? 117 GLU C CA  1 
ATOM   10954 C C   . GLU D 1 88  ? -21.211 48.866  -16.364 1.00 31.30  ? 117 GLU C C   1 
ATOM   10955 O O   . GLU D 1 88  ? -21.720 48.214  -17.269 1.00 29.56  ? 117 GLU C O   1 
ATOM   10956 C CB  . GLU D 1 88  ? -21.651 48.321  -14.006 1.00 28.85  ? 117 GLU C CB  1 
ATOM   10957 C CG  . GLU D 1 88  ? -21.435 47.372  -12.836 1.00 31.87  ? 117 GLU C CG  1 
ATOM   10958 C CD  . GLU D 1 88  ? -20.575 47.918  -11.703 1.00 32.62  ? 117 GLU C CD  1 
ATOM   10959 O OE1 . GLU D 1 88  ? -19.629 48.659  -12.009 1.00 34.79  ? 117 GLU C OE1 1 
ATOM   10960 O OE2 . GLU D 1 88  ? -20.817 47.553  -10.514 1.00 33.51  ? 117 GLU C OE2 1 
ATOM   10961 N N   . GLY D 1 89  ? -21.211 50.198  -16.324 1.00 31.31  ? 118 GLY C N   1 
ATOM   10962 C CA  . GLY D 1 89  ? -21.748 50.987  -17.411 1.00 30.39  ? 118 GLY C CA  1 
ATOM   10963 C C   . GLY D 1 89  ? -20.955 50.777  -18.691 1.00 33.41  ? 118 GLY C C   1 
ATOM   10964 O O   . GLY D 1 89  ? -21.519 50.772  -19.802 1.00 32.46  ? 118 GLY C O   1 
ATOM   10965 N N   . LEU D 1 90  ? -19.638 50.650  -18.548 1.00 33.17  ? 119 LEU C N   1 
ATOM   10966 C CA  . LEU D 1 90  ? -18.830 50.459  -19.741 1.00 32.71  ? 119 LEU C CA  1 
ATOM   10967 C C   . LEU D 1 90  ? -19.180 49.120  -20.388 1.00 25.94  ? 119 LEU C C   1 
ATOM   10968 O O   . LEU D 1 90  ? -19.276 49.022  -21.604 1.00 29.40  ? 119 LEU C O   1 
ATOM   10969 C CB  . LEU D 1 90  ? -17.322 50.590  -19.523 1.00 37.98  ? 119 LEU C CB  1 
ATOM   10970 C CG  . LEU D 1 90  ? -16.529 50.101  -20.735 1.00 38.97  ? 119 LEU C CG  1 
ATOM   10971 C CD1 . LEU D 1 90  ? -15.412 50.975  -21.096 1.00 45.44  ? 119 LEU C CD1 1 
ATOM   10972 C CD2 . LEU D 1 90  ? -16.080 48.655  -20.392 1.00 40.31  ? 119 LEU C CD2 1 
ATOM   10973 N N   . PHE D 1 91  ? -19.464 48.108  -19.573 1.00 25.85  ? 120 PHE C N   1 
ATOM   10974 C CA  . PHE D 1 91  ? -19.799 46.795  -20.079 1.00 27.50  ? 120 PHE C CA  1 
ATOM   10975 C C   . PHE D 1 91  ? -21.141 46.853  -20.810 1.00 28.16  ? 120 PHE C C   1 
ATOM   10976 O O   . PHE D 1 91  ? -21.300 46.300  -21.903 1.00 27.60  ? 120 PHE C O   1 
ATOM   10977 C CB  . PHE D 1 91  ? -19.795 45.745  -18.960 1.00 24.50  ? 120 PHE C CB  1 
ATOM   10978 C CG  . PHE D 1 91  ? -20.166 44.354  -19.464 1.00 24.32  ? 120 PHE C CG  1 
ATOM   10979 C CD1 . PHE D 1 91  ? -19.242 43.578  -20.146 1.00 25.80  ? 120 PHE C CD1 1 
ATOM   10980 C CD2 . PHE D 1 91  ? -21.438 43.814  -19.238 1.00 24.16  ? 120 PHE C CD2 1 
ATOM   10981 C CE1 . PHE D 1 91  ? -19.575 42.302  -20.584 1.00 26.52  ? 120 PHE C CE1 1 
ATOM   10982 C CE2 . PHE D 1 91  ? -21.784 42.570  -19.723 1.00 22.08  ? 120 PHE C CE2 1 
ATOM   10983 C CZ  . PHE D 1 91  ? -20.849 41.806  -20.390 1.00 26.68  ? 120 PHE C CZ  1 
ATOM   10984 N N   . TRP D 1 92  ? -22.067 47.612  -20.238 1.00 29.05  ? 121 TRP C N   1 
ATOM   10985 C CA  . TRP D 1 92  ? -23.382 47.784  -20.812 1.00 26.74  ? 121 TRP C CA  1 
ATOM   10986 C C   . TRP D 1 92  ? -23.257 48.453  -22.167 1.00 25.00  ? 121 TRP C C   1 
ATOM   10987 O O   . TRP D 1 92  ? -23.933 48.070  -23.110 1.00 31.67  ? 121 TRP C O   1 
ATOM   10988 C CB  . TRP D 1 92  ? -24.249 48.636  -19.878 1.00 28.75  ? 121 TRP C CB  1 
ATOM   10989 C CG  . TRP D 1 92  ? -25.680 48.676  -20.324 1.00 25.78  ? 121 TRP C CG  1 
ATOM   10990 C CD1 . TRP D 1 92  ? -26.182 49.362  -21.390 1.00 27.82  ? 121 TRP C CD1 1 
ATOM   10991 C CD2 . TRP D 1 92  ? -26.783 47.977  -19.723 1.00 24.15  ? 121 TRP C CD2 1 
ATOM   10992 N NE1 . TRP D 1 92  ? -27.524 49.131  -21.485 1.00 27.96  ? 121 TRP C NE1 1 
ATOM   10993 C CE2 . TRP D 1 92  ? -27.930 48.326  -20.460 1.00 28.68  ? 121 TRP C CE2 1 
ATOM   10994 C CE3 . TRP D 1 92  ? -26.926 47.147  -18.611 1.00 27.38  ? 121 TRP C CE3 1 
ATOM   10995 C CZ2 . TRP D 1 92  ? -29.192 47.827  -20.147 1.00 27.67  ? 121 TRP C CZ2 1 
ATOM   10996 C CZ3 . TRP D 1 92  ? -28.168 46.646  -18.308 1.00 29.68  ? 121 TRP C CZ3 1 
ATOM   10997 C CH2 . TRP D 1 92  ? -29.274 46.957  -19.086 1.00 28.22  ? 121 TRP C CH2 1 
ATOM   10998 N N   . LEU D 1 93  ? -22.376 49.441  -22.256 1.00 25.71  ? 122 LEU C N   1 
ATOM   10999 C CA  . LEU D 1 93  ? -22.206 50.152  -23.499 1.00 26.16  ? 122 LEU C CA  1 
ATOM   11000 C C   . LEU D 1 93  ? -21.624 49.208  -24.563 1.00 28.14  ? 122 LEU C C   1 
ATOM   11001 O O   . LEU D 1 93  ? -22.017 49.271  -25.728 1.00 24.14  ? 122 LEU C O   1 
ATOM   11002 C CB  . LEU D 1 93  ? -21.312 51.361  -23.289 1.00 28.79  ? 122 LEU C CB  1 
ATOM   11003 C CG  . LEU D 1 93  ? -20.771 51.999  -24.573 1.00 26.77  ? 122 LEU C CG  1 
ATOM   11004 C CD1 . LEU D 1 93  ? -21.903 52.517  -25.468 1.00 28.46  ? 122 LEU C CD1 1 
ATOM   11005 C CD2 . LEU D 1 93  ? -19.808 53.097  -24.196 1.00 31.05  ? 122 LEU C CD2 1 
ATOM   11006 N N   . LEU D 1 94  ? -20.736 48.302  -24.143 1.00 28.78  ? 123 LEU C N   1 
ATOM   11007 C CA  . LEU D 1 94  ? -19.986 47.474  -25.094 1.00 32.60  ? 123 LEU C CA  1 
ATOM   11008 C C   . LEU D 1 94  ? -20.901 46.440  -25.710 1.00 29.58  ? 123 LEU C C   1 
ATOM   11009 O O   . LEU D 1 94  ? -20.840 46.153  -26.894 1.00 34.16  ? 123 LEU C O   1 
ATOM   11010 C CB  . LEU D 1 94  ? -18.769 46.810  -24.448 1.00 28.61  ? 123 LEU C CB  1 
ATOM   11011 C CG  . LEU D 1 94  ? -17.630 47.753  -24.070 1.00 29.28  ? 123 LEU C CG  1 
ATOM   11012 C CD1 . LEU D 1 94  ? -16.388 46.967  -23.703 1.00 29.99  ? 123 LEU C CD1 1 
ATOM   11013 C CD2 . LEU D 1 94  ? -17.269 48.746  -25.156 1.00 31.77  ? 123 LEU C CD2 1 
ATOM   11014 N N   . VAL D 1 95  ? -21.804 45.944  -24.890 1.00 30.29  ? 124 VAL C N   1 
ATOM   11015 C CA  . VAL D 1 95  ? -22.724 44.900  -25.268 1.00 32.54  ? 124 VAL C CA  1 
ATOM   11016 C C   . VAL D 1 95  ? -23.870 45.469  -26.092 1.00 31.73  ? 124 VAL C C   1 
ATOM   11017 O O   . VAL D 1 95  ? -24.260 44.815  -27.032 1.00 29.58  ? 124 VAL C O   1 
ATOM   11018 C CB  . VAL D 1 95  ? -23.238 44.230  -23.982 1.00 36.40  ? 124 VAL C CB  1 
ATOM   11019 C CG1 . VAL D 1 95  ? -24.437 43.321  -24.231 1.00 39.93  ? 124 VAL C CG1 1 
ATOM   11020 C CG2 . VAL D 1 95  ? -22.117 43.482  -23.296 1.00 38.34  ? 124 VAL C CG2 1 
ATOM   11021 N N   . THR D 1 96  ? -24.454 46.613  -25.699 1.00 29.57  ? 125 THR C N   1 
ATOM   11022 C CA  . THR D 1 96  ? -25.689 47.084  -26.311 1.00 29.24  ? 125 THR C CA  1 
ATOM   11023 C C   . THR D 1 96  ? -25.398 48.162  -27.356 1.00 28.89  ? 125 THR C C   1 
ATOM   11024 O O   . THR D 1 96  ? -26.213 48.390  -28.250 1.00 32.42  ? 125 THR C O   1 
ATOM   11025 C CB  . THR D 1 96  ? -26.668 47.617  -25.257 1.00 29.44  ? 125 THR C CB  1 
ATOM   11026 O OG1 . THR D 1 96  ? -26.082 48.778  -24.672 1.00 26.55  ? 125 THR C OG1 1 
ATOM   11027 C CG2 . THR D 1 96  ? -26.981 46.592  -24.179 1.00 28.32  ? 125 THR C CG2 1 
ATOM   11028 N N   . GLY D 1 97  ? -24.238 48.816  -27.254 1.00 34.61  ? 126 GLY C N   1 
ATOM   11029 C CA  . GLY D 1 97  ? -23.936 49.996  -28.056 1.00 35.48  ? 126 GLY C CA  1 
ATOM   11030 C C   . GLY D 1 97  ? -24.571 51.275  -27.501 1.00 32.68  ? 126 GLY C C   1 
ATOM   11031 O O   . GLY D 1 97  ? -24.399 52.316  -28.100 1.00 34.20  ? 126 GLY C O   1 
ATOM   11032 N N   . HIS D 1 98  ? -25.322 51.179  -26.396 1.00 34.24  ? 127 HIS C N   1 
ATOM   11033 C CA  . HIS D 1 98  ? -26.019 52.311  -25.804 1.00 40.16  ? 127 HIS C CA  1 
ATOM   11034 C C   . HIS D 1 98  ? -25.409 52.655  -24.443 1.00 39.77  ? 127 HIS C C   1 
ATOM   11035 O O   . HIS D 1 98  ? -25.064 51.760  -23.678 1.00 29.24  ? 127 HIS C O   1 
ATOM   11036 C CB  . HIS D 1 98  ? -27.482 51.973  -25.458 1.00 41.68  ? 127 HIS C CB  1 
ATOM   11037 C CG  . HIS D 1 98  ? -28.353 51.666  -26.623 1.00 53.04  ? 127 HIS C CG  1 
ATOM   11038 N ND1 . HIS D 1 98  ? -28.253 52.326  -27.826 1.00 58.29  ? 127 HIS C ND1 1 
ATOM   11039 C CD2 . HIS D 1 98  ? -29.345 50.758  -26.770 1.00 56.90  ? 127 HIS C CD2 1 
ATOM   11040 C CE1 . HIS D 1 98  ? -29.148 51.818  -28.670 1.00 62.76  ? 127 HIS C CE1 1 
ATOM   11041 N NE2 . HIS D 1 98  ? -29.824 50.870  -28.048 1.00 55.12  ? 127 HIS C NE2 1 
ATOM   11042 N N   . ILE D 1 99  ? -25.364 53.954  -24.139 1.00 38.76  ? 128 ILE C N   1 
ATOM   11043 C CA  . ILE D 1 99  ? -25.072 54.462  -22.807 1.00 41.64  ? 128 ILE C CA  1 
ATOM   11044 C C   . ILE D 1 99  ? -26.164 54.022  -21.847 1.00 34.48  ? 128 ILE C C   1 
ATOM   11045 O O   . ILE D 1 99  ? -27.332 54.282  -22.103 1.00 40.61  ? 128 ILE C O   1 
ATOM   11046 C CB  . ILE D 1 99  ? -24.963 55.993  -22.859 1.00 43.22  ? 128 ILE C CB  1 
ATOM   11047 C CG1 . ILE D 1 99  ? -23.795 56.415  -23.734 1.00 44.01  ? 128 ILE C CG1 1 
ATOM   11048 C CG2 . ILE D 1 99  ? -24.876 56.604  -21.455 1.00 46.44  ? 128 ILE C CG2 1 
ATOM   11049 C CD1 . ILE D 1 99  ? -22.431 56.085  -23.157 1.00 45.88  ? 128 ILE C CD1 1 
ATOM   11050 N N   . PRO D 1 100 ? -25.844 53.324  -20.729 1.00 34.46  ? 129 PRO C N   1 
ATOM   11051 C CA  . PRO D 1 100 ? -26.875 52.869  -19.806 1.00 35.70  ? 129 PRO C CA  1 
ATOM   11052 C C   . PRO D 1 100 ? -27.423 54.025  -18.968 1.00 37.21  ? 129 PRO C C   1 
ATOM   11053 O O   . PRO D 1 100 ? -26.753 55.036  -18.839 1.00 33.18  ? 129 PRO C O   1 
ATOM   11054 C CB  . PRO D 1 100 ? -26.139 51.852  -18.924 1.00 33.93  ? 129 PRO C CB  1 
ATOM   11055 C CG  . PRO D 1 100 ? -24.706 52.313  -18.945 1.00 32.90  ? 129 PRO C CG  1 
ATOM   11056 C CD  . PRO D 1 100 ? -24.496 52.964  -20.274 1.00 30.64  ? 129 PRO C CD  1 
ATOM   11057 N N   . THR D 1 101 ? -28.619 53.813  -18.396 1.00 39.38  ? 130 THR C N   1 
ATOM   11058 C CA  . THR D 1 101 ? -29.200 54.635  -17.349 1.00 43.55  ? 130 THR C CA  1 
ATOM   11059 C C   . THR D 1 101 ? -28.606 54.153  -16.033 1.00 47.70  ? 130 THR C C   1 
ATOM   11060 O O   . THR D 1 101 ? -27.975 53.086  -16.001 1.00 39.38  ? 130 THR C O   1 
ATOM   11061 C CB  . THR D 1 101 ? -30.727 54.502  -17.304 1.00 43.86  ? 130 THR C CB  1 
ATOM   11062 O OG1 . THR D 1 101 ? -31.015 53.184  -16.843 1.00 42.98  ? 130 THR C OG1 1 
ATOM   11063 C CG2 . THR D 1 101 ? -31.414 54.701  -18.645 1.00 46.01  ? 130 THR C CG2 1 
ATOM   11064 N N   . GLU D 1 102 ? -28.855 54.931  -14.966 1.00 40.44  ? 131 GLU C N   1 
ATOM   11065 C CA  . GLU D 1 102 ? -28.329 54.646  -13.644 1.00 43.55  ? 131 GLU C CA  1 
ATOM   11066 C C   . GLU D 1 102 ? -28.973 53.376  -13.108 1.00 44.98  ? 131 GLU C C   1 
ATOM   11067 O O   . GLU D 1 102 ? -28.303 52.615  -12.415 1.00 41.91  ? 131 GLU C O   1 
ATOM   11068 C CB  . GLU D 1 102 ? -28.584 55.739  -12.600 1.00 52.90  ? 131 GLU C CB  1 
ATOM   11069 C CG  . GLU D 1 102 ? -27.574 56.883  -12.638 1.00 66.27  ? 131 GLU C CG  1 
ATOM   11070 C CD  . GLU D 1 102 ? -27.233 57.457  -11.273 1.00 73.54  ? 131 GLU C CD  1 
ATOM   11071 O OE1 . GLU D 1 102 ? -28.154 57.638  -10.433 1.00 72.16  ? 131 GLU C OE1 1 
ATOM   11072 O OE2 . GLU D 1 102 ? -26.025 57.717  -11.061 1.00 80.53  ? 131 GLU C OE2 1 
ATOM   11073 N N   . GLU D 1 103 ? -30.258 53.158  -13.451 1.00 44.85  ? 132 GLU C N   1 
ATOM   11074 C CA  . GLU D 1 103 ? -30.969 51.947  -13.058 1.00 49.24  ? 132 GLU C CA  1 
ATOM   11075 C C   . GLU D 1 103 ? -30.335 50.717  -13.716 1.00 35.93  ? 132 GLU C C   1 
ATOM   11076 O O   . GLU D 1 103 ? -30.198 49.686  -13.101 1.00 34.01  ? 132 GLU C O   1 
ATOM   11077 C CB  . GLU D 1 103 ? -32.462 52.033  -13.396 1.00 58.12  ? 132 GLU C CB  1 
ATOM   11078 C CG  . GLU D 1 103 ? -33.272 52.800  -12.351 1.00 73.92  ? 132 GLU C CG  1 
ATOM   11079 C CD  . GLU D 1 103 ? -32.792 54.216  -12.052 1.00 80.76  ? 132 GLU C CD  1 
ATOM   11080 O OE1 . GLU D 1 103 ? -32.846 55.048  -12.985 1.00 84.12  ? 132 GLU C OE1 1 
ATOM   11081 O OE2 . GLU D 1 103 ? -32.352 54.487  -10.907 1.00 83.86  ? 132 GLU C OE2 1 
ATOM   11082 N N   . GLN D 1 104 ? -29.960 50.821  -14.977 1.00 36.91  ? 133 GLN C N   1 
ATOM   11083 C CA  . GLN D 1 104 ? -29.344 49.698  -15.673 1.00 40.34  ? 133 GLN C CA  1 
ATOM   11084 C C   . GLN D 1 104 ? -28.010 49.312  -15.022 1.00 36.32  ? 133 GLN C C   1 
ATOM   11085 O O   . GLN D 1 104 ? -27.781 48.147  -14.686 1.00 38.28  ? 133 GLN C O   1 
ATOM   11086 C CB  . GLN D 1 104 ? -29.279 50.054  -17.161 1.00 37.76  ? 133 GLN C CB  1 
ATOM   11087 C CG  . GLN D 1 104 ? -30.651 50.045  -17.835 1.00 36.05  ? 133 GLN C CG  1 
ATOM   11088 C CD  . GLN D 1 104 ? -30.635 50.692  -19.202 1.00 33.37  ? 133 GLN C CD  1 
ATOM   11089 O OE1 . GLN D 1 104 ? -29.746 51.465  -19.533 1.00 38.19  ? 133 GLN C OE1 1 
ATOM   11090 N NE2 . GLN D 1 104 ? -31.607 50.364  -20.026 1.00 35.17  ? 133 GLN C NE2 1 
ATOM   11091 N N   . VAL D 1 105 ? -27.161 50.299  -14.771 1.00 35.96  ? 134 VAL C N   1 
ATOM   11092 C CA  . VAL D 1 105 ? -25.887 50.047  -14.123 1.00 37.22  ? 134 VAL C CA  1 
ATOM   11093 C C   . VAL D 1 105 ? -26.120 49.476  -12.736 1.00 41.49  ? 134 VAL C C   1 
ATOM   11094 O O   . VAL D 1 105 ? -25.463 48.514  -12.346 1.00 35.30  ? 134 VAL C O   1 
ATOM   11095 C CB  . VAL D 1 105 ? -25.092 51.352  -14.079 1.00 38.13  ? 134 VAL C CB  1 
ATOM   11096 C CG1 . VAL D 1 105 ? -23.899 51.282  -13.136 1.00 38.21  ? 134 VAL C CG1 1 
ATOM   11097 C CG2 . VAL D 1 105 ? -24.718 51.795  -15.488 1.00 36.36  ? 134 VAL C CG2 1 
ATOM   11098 N N   . SER D 1 106 ? -27.050 50.099  -12.002 1.00 42.80  ? 135 SER C N   1 
ATOM   11099 C CA  . SER D 1 106 ? -27.389 49.667  -10.659 1.00 41.20  ? 135 SER C CA  1 
ATOM   11100 C C   . SER D 1 106 ? -27.866 48.220  -10.713 1.00 38.28  ? 135 SER C C   1 
ATOM   11101 O O   . SER D 1 106 ? -27.473 47.399  -9.905  1.00 43.86  ? 135 SER C O   1 
ATOM   11102 C CB  . SER D 1 106 ? -28.409 50.628  -10.016 1.00 46.76  ? 135 SER C CB  1 
ATOM   11103 O OG  . SER D 1 106 ? -29.311 49.948  -9.152  1.00 53.38  ? 135 SER C OG  1 
ATOM   11104 N N   . TRP D 1 107 ? -28.736 47.912  -11.667 1.00 41.53  ? 136 TRP C N   1 
ATOM   11105 C CA  . TRP D 1 107 ? -29.194 46.551  -11.902 1.00 43.06  ? 136 TRP C CA  1 
ATOM   11106 C C   . TRP D 1 107 ? -28.016 45.604  -12.191 1.00 32.68  ? 136 TRP C C   1 
ATOM   11107 O O   . TRP D 1 107 ? -27.893 44.523  -11.618 1.00 31.09  ? 136 TRP C O   1 
ATOM   11108 C CB  . TRP D 1 107 ? -30.202 46.582  -13.059 1.00 40.26  ? 136 TRP C CB  1 
ATOM   11109 C CG  . TRP D 1 107 ? -30.644 45.207  -13.440 1.00 38.01  ? 136 TRP C CG  1 
ATOM   11110 C CD1 . TRP D 1 107 ? -31.687 44.506  -12.912 1.00 38.87  ? 136 TRP C CD1 1 
ATOM   11111 C CD2 . TRP D 1 107 ? -29.978 44.330  -14.370 1.00 36.20  ? 136 TRP C CD2 1 
ATOM   11112 N NE1 . TRP D 1 107 ? -31.725 43.255  -13.467 1.00 36.30  ? 136 TRP C NE1 1 
ATOM   11113 C CE2 . TRP D 1 107 ? -30.694 43.114  -14.353 1.00 35.35  ? 136 TRP C CE2 1 
ATOM   11114 C CE3 . TRP D 1 107 ? -28.850 44.442  -15.192 1.00 33.54  ? 136 TRP C CE3 1 
ATOM   11115 C CZ2 . TRP D 1 107 ? -30.328 42.032  -15.148 1.00 37.93  ? 136 TRP C CZ2 1 
ATOM   11116 C CZ3 . TRP D 1 107 ? -28.467 43.357  -15.949 1.00 33.87  ? 136 TRP C CZ3 1 
ATOM   11117 C CH2 . TRP D 1 107 ? -29.192 42.170  -15.924 1.00 38.56  ? 136 TRP C CH2 1 
ATOM   11118 N N   . LEU D 1 108 ? -27.090 46.030  -13.041 1.00 36.38  ? 137 LEU C N   1 
ATOM   11119 C CA  . LEU D 1 108 ? -25.936 45.189  -13.350 1.00 37.60  ? 137 LEU C CA  1 
ATOM   11120 C C   . LEU D 1 108 ? -25.014 45.002  -12.135 1.00 33.96  ? 137 LEU C C   1 
ATOM   11121 O O   . LEU D 1 108 ? -24.527 43.909  -11.887 1.00 32.88  ? 137 LEU C O   1 
ATOM   11122 C CB  . LEU D 1 108 ? -25.198 45.767  -14.551 1.00 36.74  ? 137 LEU C CB  1 
ATOM   11123 C CG  . LEU D 1 108 ? -24.085 44.886  -15.118 1.00 39.91  ? 137 LEU C CG  1 
ATOM   11124 C CD1 . LEU D 1 108 ? -24.510 43.453  -15.395 1.00 41.36  ? 137 LEU C CD1 1 
ATOM   11125 C CD2 . LEU D 1 108 ? -23.595 45.560  -16.369 1.00 37.51  ? 137 LEU C CD2 1 
ATOM   11126 N N   . SER D 1 109 ? -24.777 46.045  -11.336 1.00 39.41  ? 138 SER C N   1 
ATOM   11127 C CA  . SER D 1 109 ? -24.006 45.894  -10.106 1.00 34.54  ? 138 SER C CA  1 
ATOM   11128 C C   . SER D 1 109 ? -24.589 44.766  -9.253  1.00 41.14  ? 138 SER C C   1 
ATOM   11129 O O   . SER D 1 109 ? -23.847 43.897  -8.750  1.00 33.05  ? 138 SER C O   1 
ATOM   11130 C CB  . SER D 1 109 ? -23.925 47.184  -9.335  1.00 38.13  ? 138 SER C CB  1 
ATOM   11131 O OG  . SER D 1 109 ? -23.342 48.257  -10.078 1.00 39.55  ? 138 SER C OG  1 
ATOM   11132 N N   . LYS D 1 110 ? -25.934 44.750  -9.123  1.00 39.41  ? 139 LYS C N   1 
ATOM   11133 C CA  . LYS D 1 110 ? -26.588 43.737  -8.297  1.00 39.92  ? 139 LYS C CA  1 
ATOM   11134 C C   . LYS D 1 110 ? -26.469 42.395  -8.987  1.00 36.21  ? 139 LYS C C   1 
ATOM   11135 O O   . LYS D 1 110 ? -26.306 41.393  -8.320  1.00 33.91  ? 139 LYS C O   1 
ATOM   11136 C CB  . LYS D 1 110 ? -28.064 43.977  -7.946  1.00 41.30  ? 139 LYS C CB  1 
ATOM   11137 C CG  . LYS D 1 110 ? -28.251 45.175  -7.034  1.00 47.98  ? 139 LYS C CG  1 
ATOM   11138 C CD  . LYS D 1 110 ? -29.702 45.522  -6.713  1.00 60.74  ? 139 LYS C CD  1 
ATOM   11139 C CE  . LYS D 1 110 ? -29.856 46.734  -5.842  1.00 65.89  ? 139 LYS C CE  1 
ATOM   11140 N NZ  . LYS D 1 110 ? -29.543 47.962  -6.580  1.00 69.18  ? 139 LYS C NZ  1 
ATOM   11141 N N   . GLU D 1 111 ? -26.576 42.344  -10.323 1.00 36.80  ? 140 GLU C N   1 
ATOM   11142 C CA  . GLU D 1 111 ? -26.525 41.027  -10.947 1.00 40.88  ? 140 GLU C CA  1 
ATOM   11143 C C   . GLU D 1 111 ? -25.185 40.352  -10.690 1.00 36.87  ? 140 GLU C C   1 
ATOM   11144 O O   . GLU D 1 111 ? -25.142 39.155  -10.425 1.00 43.01  ? 140 GLU C O   1 
ATOM   11145 C CB  . GLU D 1 111 ? -26.824 41.000  -12.443 1.00 43.91  ? 140 GLU C CB  1 
ATOM   11146 C CG  . GLU D 1 111 ? -28.295 41.270  -12.739 1.00 53.69  ? 140 GLU C CG  1 
ATOM   11147 C CD  . GLU D 1 111 ? -29.301 40.496  -11.901 1.00 53.15  ? 140 GLU C CD  1 
ATOM   11148 O OE1 . GLU D 1 111 ? -30.100 41.082  -11.097 1.00 62.92  ? 140 GLU C OE1 1 
ATOM   11149 O OE2 . GLU D 1 111 ? -29.246 39.272  -12.075 1.00 54.52  ? 140 GLU C OE2 1 
ATOM   11150 N N   . TRP D 1 112 ? -24.095 41.118  -10.763 1.00 40.57  ? 141 TRP C N   1 
ATOM   11151 C CA  . TRP D 1 112 ? -22.753 40.567  -10.587 1.00 40.70  ? 141 TRP C CA  1 
ATOM   11152 C C   . TRP D 1 112 ? -22.476 40.221  -9.123  1.00 39.89  ? 141 TRP C C   1 
ATOM   11153 O O   . TRP D 1 112 ? -21.769 39.266  -8.853  1.00 37.46  ? 141 TRP C O   1 
ATOM   11154 C CB  . TRP D 1 112 ? -21.684 41.519  -11.153 1.00 34.95  ? 141 TRP C CB  1 
ATOM   11155 C CG  . TRP D 1 112 ? -21.660 41.615  -12.655 1.00 34.38  ? 141 TRP C CG  1 
ATOM   11156 C CD1 . TRP D 1 112 ? -22.304 40.806  -13.539 1.00 35.29  ? 141 TRP C CD1 1 
ATOM   11157 C CD2 . TRP D 1 112 ? -20.952 42.587  -13.458 1.00 34.52  ? 141 TRP C CD2 1 
ATOM   11158 N NE1 . TRP D 1 112 ? -22.033 41.193  -14.829 1.00 32.93  ? 141 TRP C NE1 1 
ATOM   11159 C CE2 . TRP D 1 112 ? -21.223 42.286  -14.809 1.00 31.77  ? 141 TRP C CE2 1 
ATOM   11160 C CE3 . TRP D 1 112 ? -20.117 43.671  -13.177 1.00 34.16  ? 141 TRP C CE3 1 
ATOM   11161 C CZ2 . TRP D 1 112 ? -20.704 43.030  -15.860 1.00 30.38  ? 141 TRP C CZ2 1 
ATOM   11162 C CZ3 . TRP D 1 112 ? -19.606 44.410  -14.218 1.00 34.04  ? 141 TRP C CZ3 1 
ATOM   11163 C CH2 . TRP D 1 112 ? -19.903 44.095  -15.543 1.00 29.01  ? 141 TRP C CH2 1 
ATOM   11164 N N   . ALA D 1 113 ? -23.044 40.966  -8.164  1.00 42.79  ? 142 ALA C N   1 
ATOM   11165 C CA  . ALA D 1 113 ? -22.886 40.602  -6.758  1.00 42.19  ? 142 ALA C CA  1 
ATOM   11166 C C   . ALA D 1 113 ? -23.513 39.242  -6.472  1.00 36.30  ? 142 ALA C C   1 
ATOM   11167 O O   . ALA D 1 113 ? -22.937 38.468  -5.717  1.00 43.53  ? 142 ALA C O   1 
ATOM   11168 C CB  . ALA D 1 113 ? -23.488 41.669  -5.873  1.00 47.58  ? 142 ALA C CB  1 
ATOM   11169 N N   . LYS D 1 114 ? -24.656 38.937  -7.114  1.00 35.98  ? 143 LYS C N   1 
ATOM   11170 C CA  . LYS D 1 114 ? -25.377 37.686  -6.904  1.00 41.03  ? 143 LYS C CA  1 
ATOM   11171 C C   . LYS D 1 114 ? -24.688 36.466  -7.520  1.00 39.45  ? 143 LYS C C   1 
ATOM   11172 O O   . LYS D 1 114 ? -25.004 35.343  -7.142  1.00 42.73  ? 143 LYS C O   1 
ATOM   11173 C CB  . LYS D 1 114 ? -26.804 37.700  -7.462  1.00 42.99  ? 143 LYS C CB  1 
ATOM   11174 C CG  . LYS D 1 114 ? -27.706 38.650  -6.706  1.00 50.39  ? 143 LYS C CG  1 
ATOM   11175 C CD  . LYS D 1 114 ? -29.200 38.479  -6.968  1.00 57.09  ? 143 LYS C CD  1 
ATOM   11176 C CE  . LYS D 1 114 ? -29.608 38.674  -8.400  1.00 61.45  ? 143 LYS C CE  1 
ATOM   11177 N NZ  . LYS D 1 114 ? -30.840 39.479  -8.459  1.00 59.15  ? 143 LYS C NZ  1 
ATOM   11178 N N   . ARG D 1 115 ? -23.752 36.642  -8.453  1.00 41.62  ? 144 ARG C N   1 
ATOM   11179 C CA  . ARG D 1 115 ? -23.160 35.498  -9.143  1.00 36.49  ? 144 ARG C CA  1 
ATOM   11180 C C   . ARG D 1 115 ? -21.696 35.303  -8.743  1.00 36.33  ? 144 ARG C C   1 
ATOM   11181 O O   . ARG D 1 115 ? -20.962 34.547  -9.375  1.00 37.23  ? 144 ARG C O   1 
ATOM   11182 C CB  . ARG D 1 115 ? -23.240 35.728  -10.653 1.00 38.30  ? 144 ARG C CB  1 
ATOM   11183 C CG  . ARG D 1 115 ? -24.613 35.898  -11.282 1.00 39.33  ? 144 ARG C CG  1 
ATOM   11184 C CD  . ARG D 1 115 ? -24.429 36.558  -12.620 1.00 39.85  ? 144 ARG C CD  1 
ATOM   11185 N NE  . ARG D 1 115 ? -25.660 36.509  -13.412 1.00 43.57  ? 144 ARG C NE  1 
ATOM   11186 C CZ  . ARG D 1 115 ? -25.951 35.714  -14.433 1.00 42.20  ? 144 ARG C CZ  1 
ATOM   11187 N NH1 . ARG D 1 115 ? -25.163 34.695  -14.759 1.00 38.03  ? 144 ARG C NH1 1 
ATOM   11188 N NH2 . ARG D 1 115 ? -27.052 35.965  -15.128 1.00 39.64  ? 144 ARG C NH2 1 
ATOM   11189 N N   . ALA D 1 116 ? -21.264 35.949  -7.663  1.00 37.51  ? 145 ALA C N   1 
ATOM   11190 C CA  . ALA D 1 116 ? -19.837 36.116  -7.438  1.00 41.72  ? 145 ALA C CA  1 
ATOM   11191 C C   . ALA D 1 116 ? -19.209 35.001  -6.584  1.00 44.61  ? 145 ALA C C   1 
ATOM   11192 O O   . ALA D 1 116 ? -18.001 35.000  -6.406  1.00 48.95  ? 145 ALA C O   1 
ATOM   11193 C CB  . ALA D 1 116 ? -19.602 37.495  -6.855  1.00 39.67  ? 145 ALA C CB  1 
ATOM   11194 N N   . ALA D 1 117 ? -19.997 34.034  -6.099  1.00 43.98  ? 146 ALA C N   1 
ATOM   11195 C CA  . ALA D 1 117 ? -19.504 32.926  -5.289  1.00 44.18  ? 146 ALA C CA  1 
ATOM   11196 C C   . ALA D 1 117 ? -18.544 32.013  -6.056  1.00 47.11  ? 146 ALA C C   1 
ATOM   11197 O O   . ALA D 1 117 ? -18.809 31.591  -7.190  1.00 36.89  ? 146 ALA C O   1 
ATOM   11198 C CB  . ALA D 1 117 ? -20.684 32.114  -4.797  1.00 49.45  ? 146 ALA C CB  1 
ATOM   11199 N N   . LEU D 1 118 ? -17.432 31.674  -5.393  1.00 42.44  ? 147 LEU C N   1 
ATOM   11200 C CA  . LEU D 1 118 ? -16.449 30.767  -5.950  1.00 44.92  ? 147 LEU C CA  1 
ATOM   11201 C C   . LEU D 1 118 ? -16.732 29.338  -5.510  1.00 45.71  ? 147 LEU C C   1 
ATOM   11202 O O   . LEU D 1 118 ? -16.977 29.103  -4.333  1.00 46.81  ? 147 LEU C O   1 
ATOM   11203 C CB  . LEU D 1 118 ? -15.066 31.226  -5.494  1.00 40.43  ? 147 LEU C CB  1 
ATOM   11204 C CG  . LEU D 1 118 ? -14.576 32.534  -6.109  1.00 38.01  ? 147 LEU C CG  1 
ATOM   11205 C CD1 . LEU D 1 118 ? -13.140 32.772  -5.659  1.00 39.16  ? 147 LEU C CD1 1 
ATOM   11206 C CD2 . LEU D 1 118 ? -14.668 32.523  -7.627  1.00 34.79  ? 147 LEU C CD2 1 
ATOM   11207 N N   . PRO D 1 119 ? -16.666 28.338  -6.423  1.00 43.45  ? 148 PRO C N   1 
ATOM   11208 C CA  . PRO D 1 119 ? -16.695 26.935  -6.015  1.00 43.85  ? 148 PRO C CA  1 
ATOM   11209 C C   . PRO D 1 119 ? -15.452 26.613  -5.193  1.00 48.76  ? 148 PRO C C   1 
ATOM   11210 O O   . PRO D 1 119 ? -14.371 27.181  -5.400  1.00 42.42  ? 148 PRO C O   1 
ATOM   11211 C CB  . PRO D 1 119 ? -16.770 26.102  -7.303  1.00 42.12  ? 148 PRO C CB  1 
ATOM   11212 C CG  . PRO D 1 119 ? -16.329 27.073  -8.394  1.00 41.99  ? 148 PRO C CG  1 
ATOM   11213 C CD  . PRO D 1 119 ? -16.557 28.491  -7.885  1.00 43.69  ? 148 PRO C CD  1 
ATOM   11214 N N   . SER D 1 120 ? -15.651 25.682  -4.252  1.00 49.18  ? 149 SER C N   1 
ATOM   11215 C CA  . SER D 1 120 ? -14.662 25.304  -3.261  1.00 44.00  ? 149 SER C CA  1 
ATOM   11216 C C   . SER D 1 120 ? -13.360 24.839  -3.930  1.00 40.96  ? 149 SER C C   1 
ATOM   11217 O O   . SER D 1 120 ? -12.273 25.123  -3.444  1.00 41.11  ? 149 SER C O   1 
ATOM   11218 C CB  . SER D 1 120 ? -15.252 24.243  -2.361  1.00 44.70  ? 149 SER C CB  1 
ATOM   11219 O OG  . SER D 1 120 ? -14.290 23.795  -1.417  1.00 54.08  ? 149 SER C OG  1 
ATOM   11220 N N   . HIS D 1 121 ? -13.430 24.124  -5.055  1.00 40.81  ? 150 HIS C N   1 
ATOM   11221 C CA  . HIS D 1 121 ? -12.205 23.575  -5.631  1.00 38.65  ? 150 HIS C CA  1 
ATOM   11222 C C   . HIS D 1 121 ? -11.300 24.709  -6.121  1.00 36.13  ? 150 HIS C C   1 
ATOM   11223 O O   . HIS D 1 121 ? -10.082 24.611  -6.084  1.00 36.35  ? 150 HIS C O   1 
ATOM   11224 C CB  . HIS D 1 121 ? -12.503 22.496  -6.678  1.00 39.17  ? 150 HIS C CB  1 
ATOM   11225 C CG  . HIS D 1 121 ? -12.936 23.014  -8.004  1.00 44.42  ? 150 HIS C CG  1 
ATOM   11226 N ND1 . HIS D 1 121 ? -14.192 23.540  -8.232  1.00 48.46  ? 150 HIS C ND1 1 
ATOM   11227 C CD2 . HIS D 1 121 ? -12.267 23.121  -9.148  1.00 41.86  ? 150 HIS C CD2 1 
ATOM   11228 C CE1 . HIS D 1 121 ? -14.281 23.919  -9.493  1.00 49.20  ? 150 HIS C CE1 1 
ATOM   11229 N NE2 . HIS D 1 121 ? -13.121 23.670  -10.075 1.00 44.56  ? 150 HIS C NE2 1 
ATOM   11230 N N   . VAL D 1 122 ? -11.878 25.842  -6.515  1.00 39.87  ? 151 VAL C N   1 
ATOM   11231 C CA  . VAL D 1 122 ? -11.033 26.926  -6.993  1.00 39.45  ? 151 VAL C CA  1 
ATOM   11232 C C   . VAL D 1 122 ? -10.391 27.645  -5.816  1.00 40.40  ? 151 VAL C C   1 
ATOM   11233 O O   . VAL D 1 122 ? -9.252  28.098  -5.937  1.00 38.60  ? 151 VAL C O   1 
ATOM   11234 C CB  . VAL D 1 122 ? -11.782 27.888  -7.923  1.00 35.53  ? 151 VAL C CB  1 
ATOM   11235 C CG1 . VAL D 1 122 ? -10.980 29.154  -8.190  1.00 35.70  ? 151 VAL C CG1 1 
ATOM   11236 C CG2 . VAL D 1 122 ? -12.120 27.184  -9.240  1.00 36.56  ? 151 VAL C CG2 1 
ATOM   11237 N N   . VAL D 1 123 ? -11.140 27.791  -4.713  1.00 38.66  ? 152 VAL C N   1 
ATOM   11238 C CA  . VAL D 1 123 ? -10.600 28.400  -3.507  1.00 38.87  ? 152 VAL C CA  1 
ATOM   11239 C C   . VAL D 1 123 ? -9.396  27.569  -3.046  1.00 38.72  ? 152 VAL C C   1 
ATOM   11240 O O   . VAL D 1 123 ? -8.319  28.072  -2.780  1.00 37.86  ? 152 VAL C O   1 
ATOM   11241 C CB  . VAL D 1 123 ? -11.710 28.455  -2.439  1.00 37.75  ? 152 VAL C CB  1 
ATOM   11242 C CG1 . VAL D 1 123 ? -11.164 28.941  -1.092  1.00 38.13  ? 152 VAL C CG1 1 
ATOM   11243 C CG2 . VAL D 1 123 ? -12.901 29.299  -2.900  1.00 36.25  ? 152 VAL C CG2 1 
ATOM   11244 N N   . THR D 1 124 ? -9.602  26.260  -3.005  1.00 44.48  ? 153 THR C N   1 
ATOM   11245 C CA  . THR D 1 124 ? -8.640  25.277  -2.541  1.00 46.91  ? 153 THR C CA  1 
ATOM   11246 C C   . THR D 1 124 ? -7.374  25.386  -3.384  1.00 50.50  ? 153 THR C C   1 
ATOM   11247 O O   . THR D 1 124 ? -6.249  25.426  -2.869  1.00 49.19  ? 153 THR C O   1 
ATOM   11248 C CB  . THR D 1 124 ? -9.300  23.891  -2.668  1.00 43.87  ? 153 THR C CB  1 
ATOM   11249 O OG1 . THR D 1 124 ? -10.276 23.788  -1.638  1.00 41.18  ? 153 THR C OG1 1 
ATOM   11250 C CG2 . THR D 1 124 ? -8.322  22.742  -2.513  1.00 49.06  ? 153 THR C CG2 1 
ATOM   11251 N N   . MET D 1 125 ? -7.571  25.394  -4.704  1.00 46.93  ? 154 MET C N   1 
ATOM   11252 C CA  . MET D 1 125 ? -6.431  25.400  -5.594  1.00 45.02  ? 154 MET C CA  1 
ATOM   11253 C C   . MET D 1 125 ? -5.710  26.737  -5.418  1.00 36.35  ? 154 MET C C   1 
ATOM   11254 O O   . MET D 1 125 ? -4.486  26.768  -5.415  1.00 34.21  ? 154 MET C O   1 
ATOM   11255 C CB  . MET D 1 125 ? -6.856  25.000  -7.018  1.00 53.23  ? 154 MET C CB  1 
ATOM   11256 C CG  . MET D 1 125 ? -6.785  26.071  -8.087  1.00 65.72  ? 154 MET C CG  1 
ATOM   11257 S SD  . MET D 1 125 ? -6.931  25.370  -9.748  1.00 54.14  ? 154 MET C SD  1 
ATOM   11258 C CE  . MET D 1 125 ? -6.003  26.590  -10.663 1.00 57.11  ? 154 MET C CE  1 
ATOM   11259 N N   . LEU D 1 126 ? -6.449  27.837  -5.185  1.00 34.52  ? 155 LEU C N   1 
ATOM   11260 C CA  . LEU D 1 126 ? -5.818  29.131  -4.990  1.00 32.64  ? 155 LEU C CA  1 
ATOM   11261 C C   . LEU D 1 126 ? -5.001  29.147  -3.705  1.00 36.24  ? 155 LEU C C   1 
ATOM   11262 O O   . LEU D 1 126 ? -3.889  29.680  -3.698  1.00 34.88  ? 155 LEU C O   1 
ATOM   11263 C CB  . LEU D 1 126 ? -6.804  30.288  -5.020  1.00 35.37  ? 155 LEU C CB  1 
ATOM   11264 C CG  . LEU D 1 126 ? -7.264  30.695  -6.428  1.00 36.02  ? 155 LEU C CG  1 
ATOM   11265 C CD1 . LEU D 1 126 ? -8.313  31.763  -6.337  1.00 34.92  ? 155 LEU C CD1 1 
ATOM   11266 C CD2 . LEU D 1 126 ? -6.119  31.123  -7.331  1.00 39.48  ? 155 LEU C CD2 1 
ATOM   11267 N N   . ASP D 1 127 ? -5.533  28.507  -2.651  1.00 39.19  ? 156 ASP C N   1 
ATOM   11268 C CA  . ASP D 1 127 ? -4.863  28.467  -1.359  1.00 41.46  ? 156 ASP C CA  1 
ATOM   11269 C C   . ASP D 1 127 ? -3.623  27.583  -1.420  1.00 43.97  ? 156 ASP C C   1 
ATOM   11270 O O   . ASP D 1 127 ? -2.702  27.764  -0.620  1.00 47.43  ? 156 ASP C O   1 
ATOM   11271 C CB  . ASP D 1 127 ? -5.814  28.062  -0.249  1.00 44.03  ? 156 ASP C CB  1 
ATOM   11272 C CG  . ASP D 1 127 ? -7.038  28.962  -0.134  1.00 49.83  ? 156 ASP C CG  1 
ATOM   11273 O OD1 . ASP D 1 127 ? -6.882  30.212  -0.177  1.00 43.89  ? 156 ASP C OD1 1 
ATOM   11274 O OD2 . ASP D 1 127 ? -8.148  28.405  -0.035  1.00 68.86  ? 156 ASP C OD2 1 
ATOM   11275 N N   . ASN D 1 128 ? -3.563  26.676  -2.401  1.00 39.24  ? 157 ASN C N   1 
ATOM   11276 C CA  . ASN D 1 128 ? -2.452  25.739  -2.479  1.00 37.57  ? 157 ASN C CA  1 
ATOM   11277 C C   . ASN D 1 128 ? -1.340  26.222  -3.412  1.00 36.70  ? 157 ASN C C   1 
ATOM   11278 O O   . ASN D 1 128 ? -0.280  25.634  -3.385  1.00 38.66  ? 157 ASN C O   1 
ATOM   11279 C CB  . ASN D 1 128 ? -2.905  24.339  -2.864  1.00 41.91  ? 157 ASN C CB  1 
ATOM   11280 C CG  . ASN D 1 128 ? -3.663  23.671  -1.732  1.00 47.20  ? 157 ASN C CG  1 
ATOM   11281 O OD1 . ASN D 1 128 ? -3.720  24.199  -0.621  1.00 53.02  ? 157 ASN C OD1 1 
ATOM   11282 N ND2 . ASN D 1 128 ? -4.288  22.539  -1.991  1.00 48.54  ? 157 ASN C ND2 1 
ATOM   11283 N N   . PHE D 1 129 ? -1.544  27.289  -4.198  1.00 33.04  ? 158 PHE C N   1 
ATOM   11284 C CA  . PHE D 1 129 ? -0.510  27.762  -5.114  1.00 31.73  ? 158 PHE C CA  1 
ATOM   11285 C C   . PHE D 1 129 ? 0.663   28.341  -4.332  1.00 33.00  ? 158 PHE C C   1 
ATOM   11286 O O   . PHE D 1 129 ? 0.447   29.109  -3.408  1.00 34.73  ? 158 PHE C O   1 
ATOM   11287 C CB  . PHE D 1 129 ? -1.091  28.845  -6.022  1.00 35.82  ? 158 PHE C CB  1 
ATOM   11288 C CG  . PHE D 1 129 ? -1.920  28.387  -7.213  1.00 31.00  ? 158 PHE C CG  1 
ATOM   11289 C CD1 . PHE D 1 129 ? -1.706  27.156  -7.809  1.00 34.97  ? 158 PHE C CD1 1 
ATOM   11290 C CD2 . PHE D 1 129 ? -2.889  29.214  -7.754  1.00 35.58  ? 158 PHE C CD2 1 
ATOM   11291 C CE1 . PHE D 1 129 ? -2.438  26.769  -8.921  1.00 33.34  ? 158 PHE C CE1 1 
ATOM   11292 C CE2 . PHE D 1 129 ? -3.615  28.825  -8.874  1.00 32.93  ? 158 PHE C CE2 1 
ATOM   11293 C CZ  . PHE D 1 129 ? -3.380  27.609  -9.440  1.00 32.89  ? 158 PHE C CZ  1 
ATOM   11294 N N   . PRO D 1 130 ? 1.928   28.053  -4.702  1.00 33.27  ? 159 PRO C N   1 
ATOM   11295 C CA  . PRO D 1 130 ? 3.090   28.664  -4.044  1.00 31.46  ? 159 PRO C CA  1 
ATOM   11296 C C   . PRO D 1 130 ? 3.287   30.124  -4.415  1.00 33.84  ? 159 PRO C C   1 
ATOM   11297 O O   . PRO D 1 130 ? 2.840   30.521  -5.481  1.00 39.24  ? 159 PRO C O   1 
ATOM   11298 C CB  . PRO D 1 130 ? 4.231   27.825  -4.632  1.00 33.89  ? 159 PRO C CB  1 
ATOM   11299 C CG  . PRO D 1 130 ? 3.762   27.547  -6.059  1.00 33.87  ? 159 PRO C CG  1 
ATOM   11300 C CD  . PRO D 1 130 ? 2.311   27.185  -5.835  1.00 32.77  ? 159 PRO C CD  1 
ATOM   11301 N N   . THR D 1 131 ? 4.042   30.867  -3.587  1.00 35.57  ? 160 THR C N   1 
ATOM   11302 C CA  . THR D 1 131 ? 4.268   32.289  -3.788  1.00 37.70  ? 160 THR C CA  1 
ATOM   11303 C C   . THR D 1 131 ? 5.173   32.513  -4.991  1.00 34.56  ? 160 THR C C   1 
ATOM   11304 O O   . THR D 1 131 ? 5.217   33.623  -5.509  1.00 35.80  ? 160 THR C O   1 
ATOM   11305 C CB  . THR D 1 131 ? 4.814   33.028  -2.557  1.00 40.51  ? 160 THR C CB  1 
ATOM   11306 O OG1 . THR D 1 131 ? 6.065   32.482  -2.169  1.00 42.25  ? 160 THR C OG1 1 
ATOM   11307 C CG2 . THR D 1 131 ? 3.874   32.978  -1.365  1.00 41.32  ? 160 THR C CG2 1 
ATOM   11308 N N   . ASN D 1 132 ? 5.832   31.473  -5.504  1.00 32.73  ? 161 ASN C N   1 
ATOM   11309 C CA  . ASN D 1 132 ? 6.650   31.688  -6.681  1.00 35.62  ? 161 ASN C CA  1 
ATOM   11310 C C   . ASN D 1 132 ? 5.855   31.467  -7.976  1.00 35.15  ? 161 ASN C C   1 
ATOM   11311 O O   . ASN D 1 132 ? 6.426   31.546  -9.057  1.00 38.37  ? 161 ASN C O   1 
ATOM   11312 C CB  . ASN D 1 132 ? 7.915   30.841  -6.641  1.00 37.93  ? 161 ASN C CB  1 
ATOM   11313 C CG  . ASN D 1 132 ? 7.605   29.372  -6.610  1.00 40.94  ? 161 ASN C CG  1 
ATOM   11314 O OD1 . ASN D 1 132 ? 6.779   28.933  -5.809  1.00 51.68  ? 161 ASN C OD1 1 
ATOM   11315 N ND2 . ASN D 1 132 ? 8.291   28.585  -7.421  1.00 44.70  ? 161 ASN C ND2 1 
ATOM   11316 N N   . LEU D 1 133 ? 4.558   31.157  -7.901  1.00 35.40  ? 162 LEU C N   1 
ATOM   11317 C CA  . LEU D 1 133 ? 3.757   31.070  -9.123  1.00 27.39  ? 162 LEU C CA  1 
ATOM   11318 C C   . LEU D 1 133 ? 3.200   32.454  -9.346  1.00 28.30  ? 162 LEU C C   1 
ATOM   11319 O O   . LEU D 1 133 ? 2.460   32.901  -8.482  1.00 27.14  ? 162 LEU C O   1 
ATOM   11320 C CB  . LEU D 1 133 ? 2.644   30.042  -8.993  1.00 26.98  ? 162 LEU C CB  1 
ATOM   11321 C CG  . LEU D 1 133 ? 1.832   29.747  -10.256 1.00 28.98  ? 162 LEU C CG  1 
ATOM   11322 C CD1 . LEU D 1 133 ? 2.774   29.142  -11.280 1.00 30.70  ? 162 LEU C CD1 1 
ATOM   11323 C CD2 . LEU D 1 133 ? 0.716   28.808  -9.926  1.00 32.00  ? 162 LEU C CD2 1 
ATOM   11324 N N   . HIS D 1 134 ? 3.589   33.083  -10.479 1.00 28.29  ? 163 HIS C N   1 
ATOM   11325 C CA  . HIS D 1 134 ? 3.258   34.456  -10.817 1.00 31.14  ? 163 HIS C CA  1 
ATOM   11326 C C   . HIS D 1 134 ? 1.749   34.632  -10.739 1.00 32.19  ? 163 HIS C C   1 
ATOM   11327 O O   . HIS D 1 134 ? 1.004   33.733  -11.115 1.00 29.50  ? 163 HIS C O   1 
ATOM   11328 C CB  . HIS D 1 134 ? 3.725   34.779  -12.240 1.00 36.35  ? 163 HIS C CB  1 
ATOM   11329 C CG  . HIS D 1 134 ? 3.646   36.208  -12.644 1.00 38.51  ? 163 HIS C CG  1 
ATOM   11330 N ND1 . HIS D 1 134 ? 2.497   36.792  -13.139 1.00 39.11  ? 163 HIS C ND1 1 
ATOM   11331 C CD2 . HIS D 1 134 ? 4.590   37.176  -12.639 1.00 40.18  ? 163 HIS C CD2 1 
ATOM   11332 C CE1 . HIS D 1 134 ? 2.715   38.082  -13.367 1.00 41.34  ? 163 HIS C CE1 1 
ATOM   11333 N NE2 . HIS D 1 134 ? 3.992   38.330  -13.100 1.00 48.62  ? 163 HIS C NE2 1 
ATOM   11334 N N   . PRO D 1 135 ? 1.261   35.789  -10.238 1.00 31.07  ? 164 PRO C N   1 
ATOM   11335 C CA  . PRO D 1 135 ? -0.170  36.052  -10.138 1.00 27.79  ? 164 PRO C CA  1 
ATOM   11336 C C   . PRO D 1 135 ? -0.986  35.878  -11.419 1.00 27.34  ? 164 PRO C C   1 
ATOM   11337 O O   . PRO D 1 135 ? -2.122  35.397  -11.344 1.00 26.20  ? 164 PRO C O   1 
ATOM   11338 C CB  . PRO D 1 135 ? -0.274  37.501  -9.604  1.00 29.84  ? 164 PRO C CB  1 
ATOM   11339 C CG  . PRO D 1 135 ? 1.068   37.813  -9.041  1.00 31.72  ? 164 PRO C CG  1 
ATOM   11340 C CD  . PRO D 1 135 ? 2.080   36.881  -9.721  1.00 29.32  ? 164 PRO C CD  1 
ATOM   11341 N N   . MET D 1 136 ? -0.447  36.284  -12.577 1.00 25.22  ? 165 MET C N   1 
ATOM   11342 C CA  . MET D 1 136 ? -1.118  36.010  -13.854 1.00 31.46  ? 165 MET C CA  1 
ATOM   11343 C C   . MET D 1 136 ? -1.360  34.505  -14.088 1.00 27.54  ? 165 MET C C   1 
ATOM   11344 O O   . MET D 1 136 ? -2.388  34.111  -14.620 1.00 26.19  ? 165 MET C O   1 
ATOM   11345 C CB  . MET D 1 136 ? -0.360  36.600  -15.058 1.00 30.44  ? 165 MET C CB  1 
ATOM   11346 C CG  . MET D 1 136 ? -0.537  38.108  -15.187 1.00 35.10  ? 165 MET C CG  1 
ATOM   11347 S SD  . MET D 1 136 ? -2.271  38.626  -15.301 1.00 36.93  ? 165 MET C SD  1 
ATOM   11348 C CE  . MET D 1 136 ? -2.651  38.234  -17.018 1.00 37.75  ? 165 MET C CE  1 
ATOM   11349 N N   . SER D 1 137 ? -0.395  33.671  -13.739 1.00 30.55  ? 166 SER C N   1 
ATOM   11350 C CA  . SER D 1 137 ? -0.478  32.245  -13.977 1.00 31.15  ? 166 SER C CA  1 
ATOM   11351 C C   . SER D 1 137 ? -1.514  31.649  -13.031 1.00 29.56  ? 166 SER C C   1 
ATOM   11352 O O   . SER D 1 137 ? -2.276  30.760  -13.409 1.00 26.81  ? 166 SER C O   1 
ATOM   11353 C CB  . SER D 1 137 ? 0.879   31.592  -13.802 1.00 32.45  ? 166 SER C CB  1 
ATOM   11354 O OG  . SER D 1 137 ? 1.811   32.213  -14.678 1.00 34.87  ? 166 SER C OG  1 
ATOM   11355 N N   . GLN D 1 138 ? -1.583  32.217  -11.825 1.00 26.80  ? 167 GLN C N   1 
ATOM   11356 C CA  . GLN D 1 138 ? -2.601  31.818  -10.869 1.00 28.61  ? 167 GLN C CA  1 
ATOM   11357 C C   . GLN D 1 138 ? -3.962  32.241  -11.395 1.00 25.51  ? 167 GLN C C   1 
ATOM   11358 O O   . GLN D 1 138 ? -4.912  31.488  -11.277 1.00 28.53  ? 167 GLN C O   1 
ATOM   11359 C CB  . GLN D 1 138 ? -2.388  32.438  -9.489  1.00 28.28  ? 167 GLN C CB  1 
ATOM   11360 C CG  . GLN D 1 138 ? -1.066  32.041  -8.853  1.00 27.17  ? 167 GLN C CG  1 
ATOM   11361 C CD  . GLN D 1 138 ? -1.040  32.295  -7.361  1.00 30.18  ? 167 GLN C CD  1 
ATOM   11362 O OE1 . GLN D 1 138 ? -2.077  32.334  -6.688  1.00 35.88  ? 167 GLN C OE1 1 
ATOM   11363 N NE2 . GLN D 1 138 ? 0.157   32.349  -6.813  1.00 28.64  ? 167 GLN C NE2 1 
ATOM   11364 N N   . LEU D 1 139 ? -4.036  33.421  -12.010 1.00 25.08  ? 168 LEU C N   1 
ATOM   11365 C CA  . LEU D 1 139 ? -5.290  33.923  -12.536 1.00 25.31  ? 168 LEU C CA  1 
ATOM   11366 C C   . LEU D 1 139 ? -5.777  33.007  -13.659 1.00 25.58  ? 168 LEU C C   1 
ATOM   11367 O O   . LEU D 1 139 ? -6.902  32.498  -13.633 1.00 25.37  ? 168 LEU C O   1 
ATOM   11368 C CB  . LEU D 1 139 ? -5.149  35.369  -12.995 1.00 27.75  ? 168 LEU C CB  1 
ATOM   11369 C CG  . LEU D 1 139 ? -6.425  35.964  -13.594 1.00 29.58  ? 168 LEU C CG  1 
ATOM   11370 C CD1 . LEU D 1 139 ? -7.562  36.020  -12.621 1.00 27.55  ? 168 LEU C CD1 1 
ATOM   11371 C CD2 . LEU D 1 139 ? -6.190  37.301  -14.209 1.00 31.06  ? 168 LEU C CD2 1 
ATOM   11372 N N   . SER D 1 140 ? -4.885  32.717  -14.602 1.00 24.74  ? 169 SER C N   1 
ATOM   11373 C CA  . SER D 1 140 ? -5.221  31.888  -15.740 1.00 26.47  ? 169 SER C CA  1 
ATOM   11374 C C   . SER D 1 140 ? -5.634  30.474  -15.310 1.00 26.08  ? 169 SER C C   1 
ATOM   11375 O O   . SER D 1 140 ? -6.640  29.947  -15.785 1.00 28.19  ? 169 SER C O   1 
ATOM   11376 C CB  . SER D 1 140 ? -4.076  31.854  -16.745 1.00 27.23  ? 169 SER C CB  1 
ATOM   11377 O OG  . SER D 1 140 ? -4.511  31.082  -17.858 1.00 35.84  ? 169 SER C OG  1 
ATOM   11378 N N   . ALA D 1 141 ? -4.877  29.843  -14.416 1.00 25.94  ? 170 ALA C N   1 
ATOM   11379 C CA  . ALA D 1 141 ? -5.216  28.497  -13.964 1.00 26.39  ? 170 ALA C CA  1 
ATOM   11380 C C   . ALA D 1 141 ? -6.557  28.472  -13.234 1.00 26.75  ? 170 ALA C C   1 
ATOM   11381 O O   . ALA D 1 141 ? -7.348  27.567  -13.474 1.00 27.54  ? 170 ALA C O   1 
ATOM   11382 C CB  . ALA D 1 141 ? -4.137  27.961  -13.055 1.00 31.59  ? 170 ALA C CB  1 
ATOM   11383 N N   . ALA D 1 142 ? -6.799  29.435  -12.324 1.00 27.40  ? 171 ALA C N   1 
ATOM   11384 C CA  . ALA D 1 142 ? -8.050  29.473  -11.598 1.00 28.82  ? 171 ALA C CA  1 
ATOM   11385 C C   . ALA D 1 142 ? -9.252  29.642  -12.540 1.00 28.95  ? 171 ALA C C   1 
ATOM   11386 O O   . ALA D 1 142 ? -10.289 29.001  -12.356 1.00 29.59  ? 171 ALA C O   1 
ATOM   11387 C CB  . ALA D 1 142 ? -7.996  30.550  -10.553 1.00 29.63  ? 171 ALA C CB  1 
ATOM   11388 N N   . VAL D 1 143 ? -9.113  30.482  -13.563 1.00 27.96  ? 172 VAL C N   1 
ATOM   11389 C CA  . VAL D 1 143 ? -10.198 30.709  -14.497 1.00 27.71  ? 172 VAL C CA  1 
ATOM   11390 C C   . VAL D 1 143 ? -10.447 29.427  -15.287 1.00 26.56  ? 172 VAL C C   1 
ATOM   11391 O O   . VAL D 1 143 ? -11.594 29.000  -15.405 1.00 27.46  ? 172 VAL C O   1 
ATOM   11392 C CB  . VAL D 1 143 ? -9.994  31.924  -15.420 1.00 33.60  ? 172 VAL C CB  1 
ATOM   11393 C CG1 . VAL D 1 143 ? -11.057 31.972  -16.500 1.00 33.97  ? 172 VAL C CG1 1 
ATOM   11394 C CG2 . VAL D 1 143 ? -10.014 33.235  -14.651 1.00 32.26  ? 172 VAL C CG2 1 
ATOM   11395 N N   . THR D 1 144 ? -9.380  28.777  -15.757 1.00 28.11  ? 173 THR C N   1 
ATOM   11396 C CA  . THR D 1 144 ? -9.504  27.509  -16.464 1.00 26.98  ? 173 THR C CA  1 
ATOM   11397 C C   . THR D 1 144 ? -10.283 26.507  -15.610 1.00 32.22  ? 173 THR C C   1 
ATOM   11398 O O   . THR D 1 144 ? -11.173 25.848  -16.127 1.00 33.67  ? 173 THR C O   1 
ATOM   11399 C CB  . THR D 1 144 ? -8.141  26.977  -16.893 1.00 25.30  ? 173 THR C CB  1 
ATOM   11400 O OG1 . THR D 1 144 ? -7.593  27.903  -17.832 1.00 27.27  ? 173 THR C OG1 1 
ATOM   11401 C CG2 . THR D 1 144 ? -8.265  25.670  -17.641 1.00 26.30  ? 173 THR C CG2 1 
ATOM   11402 N N   . ALA D 1 145 ? -9.976  26.426  -14.311 1.00 29.50  ? 174 ALA C N   1 
ATOM   11403 C CA  . ALA D 1 145 ? -10.633 25.474  -13.436 1.00 32.03  ? 174 ALA C CA  1 
ATOM   11404 C C   . ALA D 1 145 ? -12.099 25.824  -13.179 1.00 35.41  ? 174 ALA C C   1 
ATOM   11405 O O   . ALA D 1 145 ? -12.861 24.937  -12.790 1.00 32.99  ? 174 ALA C O   1 
ATOM   11406 C CB  . ALA D 1 145 ? -9.872  25.324  -12.135 1.00 32.96  ? 174 ALA C CB  1 
ATOM   11407 N N   . LEU D 1 146 ? -12.474 27.103  -13.359 1.00 33.05  ? 175 LEU C N   1 
ATOM   11408 C CA  . LEU D 1 146 ? -13.849 27.541  -13.198 1.00 32.65  ? 175 LEU C CA  1 
ATOM   11409 C C   . LEU D 1 146 ? -14.713 27.037  -14.342 1.00 33.23  ? 175 LEU C C   1 
ATOM   11410 O O   . LEU D 1 146 ? -15.923 27.216  -14.289 1.00 31.30  ? 175 LEU C O   1 
ATOM   11411 C CB  . LEU D 1 146 ? -14.024 29.057  -13.127 1.00 30.45  ? 175 LEU C CB  1 
ATOM   11412 C CG  . LEU D 1 146 ? -13.750 29.726  -11.785 1.00 28.21  ? 175 LEU C CG  1 
ATOM   11413 C CD1 . LEU D 1 146 ? -13.752 31.186  -12.019 1.00 28.02  ? 175 LEU C CD1 1 
ATOM   11414 C CD2 . LEU D 1 146 ? -14.683 29.379  -10.655 1.00 34.31  ? 175 LEU C CD2 1 
ATOM   11415 N N   . ASN D 1 147 ? -14.122 26.487  -15.409 1.00 31.10  ? 176 ASN C N   1 
ATOM   11416 C CA  . ASN D 1 147 ? -14.955 26.093  -16.534 1.00 31.49  ? 176 ASN C CA  1 
ATOM   11417 C C   . ASN D 1 147 ? -15.791 24.863  -16.160 1.00 27.37  ? 176 ASN C C   1 
ATOM   11418 O O   . ASN D 1 147 ? -16.731 24.514  -16.853 1.00 25.24  ? 176 ASN C O   1 
ATOM   11419 C CB  . ASN D 1 147 ? -14.165 25.917  -17.828 1.00 33.86  ? 176 ASN C CB  1 
ATOM   11420 C CG  . ASN D 1 147 ? -14.059 24.469  -18.198 1.00 39.08  ? 176 ASN C CG  1 
ATOM   11421 O OD1 . ASN D 1 147 ? -13.590 23.690  -17.366 1.00 43.16  ? 176 ASN C OD1 1 
ATOM   11422 N ND2 . ASN D 1 147 ? -14.536 24.091  -19.378 1.00 41.12  ? 176 ASN C ND2 1 
ATOM   11423 N N   . SER D 1 148 ? -15.486 24.199  -15.037 1.00 31.05  ? 177 SER C N   1 
ATOM   11424 C CA  . SER D 1 148 ? -16.419 23.226  -14.488 1.00 32.95  ? 177 SER C CA  1 
ATOM   11425 C C   . SER D 1 148 ? -17.790 23.870  -14.226 1.00 37.14  ? 177 SER C C   1 
ATOM   11426 O O   . SER D 1 148 ? -18.800 23.192  -14.194 1.00 39.10  ? 177 SER C O   1 
ATOM   11427 C CB  . SER D 1 148 ? -15.851 22.554  -13.264 1.00 33.41  ? 177 SER C CB  1 
ATOM   11428 O OG  . SER D 1 148 ? -15.569 23.480  -12.232 1.00 33.64  ? 177 SER C OG  1 
ATOM   11429 N N   . GLU D 1 149 ? -17.869 25.200  -14.098 1.00 38.67  ? 178 GLU C N   1 
ATOM   11430 C CA  . GLU D 1 149 ? -19.161 25.836  -13.901 1.00 42.17  ? 178 GLU C CA  1 
ATOM   11431 C C   . GLU D 1 149 ? -19.783 26.296  -15.226 1.00 36.61  ? 178 GLU C C   1 
ATOM   11432 O O   . GLU D 1 149 ? -20.734 27.072  -15.180 1.00 31.83  ? 178 GLU C O   1 
ATOM   11433 C CB  . GLU D 1 149 ? -19.040 27.057  -12.981 1.00 43.74  ? 178 GLU C CB  1 
ATOM   11434 C CG  . GLU D 1 149 ? -18.206 26.809  -11.730 1.00 50.93  ? 178 GLU C CG  1 
ATOM   11435 C CD  . GLU D 1 149 ? -18.683 25.624  -10.906 1.00 55.95  ? 178 GLU C CD  1 
ATOM   11436 O OE1 . GLU D 1 149 ? -19.841 25.670  -10.424 1.00 66.80  ? 178 GLU C OE1 1 
ATOM   11437 O OE2 . GLU D 1 149 ? -17.891 24.666  -10.737 1.00 57.42  ? 178 GLU C OE2 1 
ATOM   11438 N N   . SER D 1 150 ? -19.275 25.841  -16.389 1.00 32.88  ? 179 SER C N   1 
ATOM   11439 C CA  . SER D 1 150 ? -19.677 26.420  -17.664 1.00 32.08  ? 179 SER C CA  1 
ATOM   11440 C C   . SER D 1 150 ? -21.031 25.873  -18.128 1.00 33.74  ? 179 SER C C   1 
ATOM   11441 O O   . SER D 1 150 ? -21.167 24.701  -18.393 1.00 38.46  ? 179 SER C O   1 
ATOM   11442 C CB  . SER D 1 150 ? -18.628 26.212  -18.763 1.00 30.28  ? 179 SER C CB  1 
ATOM   11443 O OG  . SER D 1 150 ? -19.162 26.746  -19.971 1.00 26.78  ? 179 SER C OG  1 
ATOM   11444 N N   . ASN D 1 151 ? -22.007 26.756  -18.308 1.00 37.52  ? 180 ASN C N   1 
ATOM   11445 C CA  . ASN D 1 151 ? -23.283 26.421  -18.916 1.00 39.04  ? 180 ASN C CA  1 
ATOM   11446 C C   . ASN D 1 151 ? -23.103 26.087  -20.395 1.00 39.07  ? 180 ASN C C   1 
ATOM   11447 O O   . ASN D 1 151 ? -23.840 25.262  -20.933 1.00 34.51  ? 180 ASN C O   1 
ATOM   11448 C CB  . ASN D 1 151 ? -24.285 27.563  -18.781 1.00 42.54  ? 180 ASN C CB  1 
ATOM   11449 C CG  . ASN D 1 151 ? -24.469 27.999  -17.342 1.00 50.72  ? 180 ASN C CG  1 
ATOM   11450 O OD1 . ASN D 1 151 ? -24.270 29.182  -17.025 1.00 51.06  ? 180 ASN C OD1 1 
ATOM   11451 N ND2 . ASN D 1 151 ? -24.785 27.055  -16.461 1.00 48.90  ? 180 ASN C ND2 1 
ATOM   11452 N N   . PHE D 1 152 ? -22.146 26.746  -21.060 1.00 38.32  ? 181 PHE C N   1 
ATOM   11453 C CA  . PHE D 1 152 ? -22.029 26.627  -22.503 1.00 35.59  ? 181 PHE C CA  1 
ATOM   11454 C C   . PHE D 1 152 ? -21.330 25.333  -22.910 1.00 36.38  ? 181 PHE C C   1 
ATOM   11455 O O   . PHE D 1 152 ? -21.697 24.711  -23.897 1.00 36.98  ? 181 PHE C O   1 
ATOM   11456 C CB  . PHE D 1 152 ? -21.241 27.767  -23.135 1.00 36.48  ? 181 PHE C CB  1 
ATOM   11457 C CG  . PHE D 1 152 ? -21.135 27.616  -24.647 1.00 35.98  ? 181 PHE C CG  1 
ATOM   11458 C CD1 . PHE D 1 152 ? -22.184 27.971  -25.467 1.00 34.34  ? 181 PHE C CD1 1 
ATOM   11459 C CD2 . PHE D 1 152 ? -19.966 27.171  -25.241 1.00 37.04  ? 181 PHE C CD2 1 
ATOM   11460 C CE1 . PHE D 1 152 ? -22.064 27.903  -26.846 1.00 35.65  ? 181 PHE C CE1 1 
ATOM   11461 C CE2 . PHE D 1 152 ? -19.866 27.064  -26.615 1.00 35.85  ? 181 PHE C CE2 1 
ATOM   11462 C CZ  . PHE D 1 152 ? -20.908 27.448  -27.414 1.00 35.06  ? 181 PHE C CZ  1 
ATOM   11463 N N   . ALA D 1 153 ? -20.305 24.916  -22.173 1.00 39.61  ? 182 ALA C N   1 
ATOM   11464 C CA  . ALA D 1 153 ? -19.682 23.630  -22.460 1.00 37.10  ? 182 ALA C CA  1 
ATOM   11465 C C   . ALA D 1 153 ? -20.746 22.516  -22.432 1.00 42.19  ? 182 ALA C C   1 
ATOM   11466 O O   . ALA D 1 153 ? -20.927 21.804  -23.402 1.00 42.89  ? 182 ALA C O   1 
ATOM   11467 C CB  . ALA D 1 153 ? -18.540 23.406  -21.479 1.00 36.10  ? 182 ALA C CB  1 
ATOM   11468 N N   . ARG D 1 154 ? -21.486 22.396  -21.324 1.00 56.18  ? 183 ARG C N   1 
ATOM   11469 C CA  . ARG D 1 154 ? -22.484 21.350  -21.143 1.00 68.43  ? 183 ARG C CA  1 
ATOM   11470 C C   . ARG D 1 154 ? -23.377 21.302  -22.377 1.00 78.73  ? 183 ARG C C   1 
ATOM   11471 O O   . ARG D 1 154 ? -23.376 20.326  -23.124 1.00 93.84  ? 183 ARG C O   1 
ATOM   11472 C CB  . ARG D 1 154 ? -23.371 21.598  -19.908 1.00 77.68  ? 183 ARG C CB  1 
ATOM   11473 C CG  . ARG D 1 154 ? -22.707 21.599  -18.534 1.00 85.63  ? 183 ARG C CG  1 
ATOM   11474 C CD  . ARG D 1 154 ? -23.593 22.172  -17.400 1.00 92.39  ? 183 ARG C CD  1 
ATOM   11475 N NE  . ARG D 1 154 ? -22.900 22.312  -16.107 1.00 95.81  ? 183 ARG C NE  1 
ATOM   11476 C CZ  . ARG D 1 154 ? -22.832 23.381  -15.292 1.00 87.72  ? 183 ARG C CZ  1 
ATOM   11477 N NH1 . ARG D 1 154 ? -23.511 24.491  -15.543 1.00 87.43  ? 183 ARG C NH1 1 
ATOM   11478 N NH2 . ARG D 1 154 ? -22.083 23.323  -14.201 1.00 76.99  ? 183 ARG C NH2 1 
ATOM   11479 N N   . ALA D 1 155 ? -24.063 22.424  -22.608 1.00 77.73  ? 184 ALA C N   1 
ATOM   11480 C CA  . ALA D 1 155 ? -25.192 22.498  -23.515 1.00 74.24  ? 184 ALA C CA  1 
ATOM   11481 C C   . ALA D 1 155 ? -24.813 22.204  -24.969 1.00 66.29  ? 184 ALA C C   1 
ATOM   11482 O O   . ALA D 1 155 ? -25.678 21.762  -25.721 1.00 72.83  ? 184 ALA C O   1 
ATOM   11483 C CB  . ALA D 1 155 ? -25.848 23.855  -23.363 1.00 76.13  ? 184 ALA C CB  1 
ATOM   11484 N N   . TYR D 1 156 ? -23.551 22.405  -25.379 1.00 57.17  ? 185 TYR C N   1 
ATOM   11485 C CA  . TYR D 1 156 ? -23.165 22.091  -26.758 1.00 52.52  ? 185 TYR C CA  1 
ATOM   11486 C C   . TYR D 1 156 ? -23.157 20.580  -26.975 1.00 59.79  ? 185 TYR C C   1 
ATOM   11487 O O   . TYR D 1 156 ? -23.295 20.099  -28.110 1.00 60.99  ? 185 TYR C O   1 
ATOM   11488 C CB  . TYR D 1 156 ? -21.780 22.603  -27.169 1.00 47.67  ? 185 TYR C CB  1 
ATOM   11489 C CG  . TYR D 1 156 ? -21.360 22.308  -28.609 1.00 45.00  ? 185 TYR C CG  1 
ATOM   11490 C CD1 . TYR D 1 156 ? -20.812 21.084  -28.968 1.00 46.31  ? 185 TYR C CD1 1 
ATOM   11491 C CD2 . TYR D 1 156 ? -21.452 23.270  -29.606 1.00 48.98  ? 185 TYR C CD2 1 
ATOM   11492 C CE1 . TYR D 1 156 ? -20.412 20.803  -30.265 1.00 43.36  ? 185 TYR C CE1 1 
ATOM   11493 C CE2 . TYR D 1 156 ? -21.054 23.000  -30.908 1.00 47.41  ? 185 TYR C CE2 1 
ATOM   11494 C CZ  . TYR D 1 156 ? -20.519 21.772  -31.236 1.00 41.87  ? 185 TYR C CZ  1 
ATOM   11495 O OH  . TYR D 1 156 ? -20.133 21.467  -32.513 1.00 56.96  ? 185 TYR C OH  1 
ATOM   11496 N N   . ALA D 1 157 ? -22.910 19.835  -25.891 1.00 65.39  ? 186 ALA C N   1 
ATOM   11497 C CA  . ALA D 1 157 ? -22.896 18.378  -25.966 1.00 65.64  ? 186 ALA C CA  1 
ATOM   11498 C C   . ALA D 1 157 ? -24.293 17.889  -26.348 1.00 56.39  ? 186 ALA C C   1 
ATOM   11499 O O   . ALA D 1 157 ? -24.464 17.068  -27.257 1.00 46.89  ? 186 ALA C O   1 
ATOM   11500 C CB  . ALA D 1 157 ? -22.431 17.799  -24.640 1.00 67.21  ? 186 ALA C CB  1 
ATOM   11501 N N   . GLN D 1 158 ? -25.284 18.506  -25.693 1.00 56.00  ? 187 GLN C N   1 
ATOM   11502 C CA  . GLN D 1 158 ? -26.686 18.161  -25.825 1.00 52.83  ? 187 GLN C CA  1 
ATOM   11503 C C   . GLN D 1 158 ? -27.268 18.562  -27.177 1.00 38.62  ? 187 GLN C C   1 
ATOM   11504 O O   . GLN D 1 158 ? -28.396 18.206  -27.448 1.00 55.16  ? 187 GLN C O   1 
ATOM   11505 C CB  . GLN D 1 158 ? -27.463 18.858  -24.716 1.00 58.39  ? 187 GLN C CB  1 
ATOM   11506 C CG  . GLN D 1 158 ? -26.972 18.515  -23.312 1.00 61.39  ? 187 GLN C CG  1 
ATOM   11507 C CD  . GLN D 1 158 ? -27.519 19.475  -22.281 1.00 66.60  ? 187 GLN C CD  1 
ATOM   11508 O OE1 . GLN D 1 158 ? -28.084 20.523  -22.622 1.00 69.86  ? 187 GLN C OE1 1 
ATOM   11509 N NE2 . GLN D 1 158 ? -27.350 19.138  -21.010 1.00 68.64  ? 187 GLN C NE2 1 
ATOM   11510 N N   . GLY D 1 159 ? -26.524 19.276  -28.027 1.00 42.73  ? 188 GLY C N   1 
ATOM   11511 C CA  . GLY D 1 159 ? -26.963 19.603  -29.385 1.00 40.33  ? 188 GLY C CA  1 
ATOM   11512 C C   . GLY D 1 159 ? -27.892 20.829  -29.424 1.00 45.32  ? 188 GLY C C   1 
ATOM   11513 O O   . GLY D 1 159 ? -28.859 20.902  -30.210 1.00 41.42  ? 188 GLY C O   1 
ATOM   11514 N N   . ILE D 1 160 ? -27.590 21.813  -28.574 1.00 37.34  ? 189 ILE C N   1 
ATOM   11515 C CA  . ILE D 1 160 ? -28.323 23.071  -28.561 1.00 35.75  ? 189 ILE C CA  1 
ATOM   11516 C C   . ILE D 1 160 ? -28.141 23.830  -29.891 1.00 33.58  ? 189 ILE C C   1 
ATOM   11517 O O   . ILE D 1 160 ? -27.142 23.698  -30.557 1.00 31.88  ? 189 ILE C O   1 
ATOM   11518 C CB  . ILE D 1 160 ? -27.872 23.853  -27.316 1.00 45.86  ? 189 ILE C CB  1 
ATOM   11519 C CG1 . ILE D 1 160 ? -28.860 24.967  -26.955 1.00 52.82  ? 189 ILE C CG1 1 
ATOM   11520 C CG2 . ILE D 1 160 ? -26.440 24.360  -27.491 1.00 52.24  ? 189 ILE C CG2 1 
ATOM   11521 C CD1 . ILE D 1 160 ? -28.530 25.731  -25.686 1.00 57.90  ? 189 ILE C CD1 1 
ATOM   11522 N N   . SER D 1 161 ? -29.143 24.604  -30.320 1.00 33.27  ? 190 SER C N   1 
ATOM   11523 C CA  . SER D 1 161 ? -29.163 25.300  -31.602 1.00 33.77  ? 190 SER C CA  1 
ATOM   11524 C C   . SER D 1 161 ? -28.084 26.389  -31.626 1.00 29.72  ? 190 SER C C   1 
ATOM   11525 O O   . SER D 1 161 ? -27.899 27.061  -30.624 1.00 28.45  ? 190 SER C O   1 
ATOM   11526 C CB  . SER D 1 161 ? -30.557 25.883  -31.830 1.00 32.69  ? 190 SER C CB  1 
ATOM   11527 O OG  . SER D 1 161 ? -30.639 26.752  -32.962 1.00 35.78  ? 190 SER C OG  1 
ATOM   11528 N N   . ARG D 1 162 ? -27.396 26.560  -32.765 1.00 31.00  ? 191 ARG C N   1 
ATOM   11529 C CA  . ARG D 1 162 ? -26.474 27.660  -33.022 1.00 35.90  ? 191 ARG C CA  1 
ATOM   11530 C C   . ARG D 1 162 ? -27.107 29.007  -32.634 1.00 39.06  ? 191 ARG C C   1 
ATOM   11531 O O   . ARG D 1 162 ? -26.406 29.882  -32.118 1.00 28.34  ? 191 ARG C O   1 
ATOM   11532 C CB  . ARG D 1 162 ? -25.994 27.717  -34.484 1.00 40.73  ? 191 ARG C CB  1 
ATOM   11533 C CG  . ARG D 1 162 ? -24.918 26.698  -34.854 1.00 56.06  ? 191 ARG C CG  1 
ATOM   11534 C CD  . ARG D 1 162 ? -24.500 26.667  -36.334 1.00 59.32  ? 191 ARG C CD  1 
ATOM   11535 N NE  . ARG D 1 162 ? -25.473 25.919  -37.147 1.00 74.91  ? 191 ARG C NE  1 
ATOM   11536 C CZ  . ARG D 1 162 ? -25.550 24.580  -37.298 1.00 83.83  ? 191 ARG C CZ  1 
ATOM   11537 N NH1 . ARG D 1 162 ? -26.631 24.032  -37.833 1.00 76.69  ? 191 ARG C NH1 1 
ATOM   11538 N NH2 . ARG D 1 162 ? -24.586 23.776  -36.870 1.00 89.09  ? 191 ARG C NH2 1 
ATOM   11539 N N   . THR D 1 163 ? -28.429 29.151  -32.853 1.00 35.30  ? 192 THR C N   1 
ATOM   11540 C CA  . THR D 1 163 ? -29.136 30.406  -32.611 1.00 35.62  ? 192 THR C CA  1 
ATOM   11541 C C   . THR D 1 163 ? -29.123 30.751  -31.123 1.00 31.66  ? 192 THR C C   1 
ATOM   11542 O O   . THR D 1 163 ? -29.450 31.871  -30.752 1.00 37.11  ? 192 THR C O   1 
ATOM   11543 C CB  . THR D 1 163 ? -30.593 30.355  -33.122 1.00 31.23  ? 192 THR C CB  1 
ATOM   11544 O OG1 . THR D 1 163 ? -31.326 29.382  -32.397 1.00 26.85  ? 192 THR C OG1 1 
ATOM   11545 C CG2 . THR D 1 163 ? -30.720 29.977  -34.578 1.00 33.15  ? 192 THR C CG2 1 
ATOM   11546 N N   . LYS D 1 164 ? -28.783 29.792  -30.262 1.00 30.40  ? 193 LYS C N   1 
ATOM   11547 C CA  . LYS D 1 164 ? -28.855 29.995  -28.820 1.00 32.97  ? 193 LYS C CA  1 
ATOM   11548 C C   . LYS D 1 164 ? -27.489 30.049  -28.119 1.00 29.04  ? 193 LYS C C   1 
ATOM   11549 O O   . LYS D 1 164 ? -27.413 30.388  -26.937 1.00 35.62  ? 193 LYS C O   1 
ATOM   11550 C CB  . LYS D 1 164 ? -29.749 28.920  -28.184 1.00 39.73  ? 193 LYS C CB  1 
ATOM   11551 C CG  . LYS D 1 164 ? -31.233 29.114  -28.488 1.00 47.66  ? 193 LYS C CG  1 
ATOM   11552 C CD  . LYS D 1 164 ? -32.112 28.025  -27.875 1.00 60.82  ? 193 LYS C CD  1 
ATOM   11553 C CE  . LYS D 1 164 ? -32.176 28.056  -26.371 1.00 63.17  ? 193 LYS C CE  1 
ATOM   11554 N NZ  . LYS D 1 164 ? -32.548 29.396  -25.901 1.00 61.64  ? 193 LYS C NZ  1 
ATOM   11555 N N   . TYR D 1 165 ? -26.395 29.771  -28.813 1.00 28.90  ? 194 TYR C N   1 
ATOM   11556 C CA  . TYR D 1 165 ? -25.072 29.938  -28.232 1.00 25.22  ? 194 TYR C CA  1 
ATOM   11557 C C   . TYR D 1 165 ? -24.942 31.251  -27.470 1.00 28.76  ? 194 TYR C C   1 
ATOM   11558 O O   . TYR D 1 165 ? -24.545 31.260  -26.315 1.00 31.64  ? 194 TYR C O   1 
ATOM   11559 C CB  . TYR D 1 165 ? -24.017 29.886  -29.326 1.00 27.01  ? 194 TYR C CB  1 
ATOM   11560 C CG  . TYR D 1 165 ? -23.864 28.510  -29.943 1.00 25.90  ? 194 TYR C CG  1 
ATOM   11561 C CD1 . TYR D 1 165 ? -24.548 27.412  -29.452 1.00 27.03  ? 194 TYR C CD1 1 
ATOM   11562 C CD2 . TYR D 1 165 ? -23.055 28.326  -31.052 1.00 28.65  ? 194 TYR C CD2 1 
ATOM   11563 C CE1 . TYR D 1 165 ? -24.412 26.157  -30.033 1.00 29.00  ? 194 TYR C CE1 1 
ATOM   11564 C CE2 . TYR D 1 165 ? -22.917 27.086  -31.646 1.00 29.70  ? 194 TYR C CE2 1 
ATOM   11565 C CZ  . TYR D 1 165 ? -23.601 26.003  -31.139 1.00 31.12  ? 194 TYR C CZ  1 
ATOM   11566 O OH  . TYR D 1 165 ? -23.439 24.795  -31.732 1.00 36.62  ? 194 TYR C OH  1 
ATOM   11567 N N   . TRP D 1 166 ? -25.247 32.382  -28.102 1.00 29.56  ? 195 TRP C N   1 
ATOM   11568 C CA  . TRP D 1 166 ? -25.016 33.663  -27.470 1.00 28.85  ? 195 TRP C CA  1 
ATOM   11569 C C   . TRP D 1 166 ? -25.573 33.676  -26.048 1.00 30.06  ? 195 TRP C C   1 
ATOM   11570 O O   . TRP D 1 166 ? -25.021 34.337  -25.189 1.00 26.74  ? 195 TRP C O   1 
ATOM   11571 C CB  . TRP D 1 166 ? -25.613 34.809  -28.293 1.00 28.56  ? 195 TRP C CB  1 
ATOM   11572 C CG  . TRP D 1 166 ? -27.107 35.007  -28.183 1.00 32.76  ? 195 TRP C CG  1 
ATOM   11573 C CD1 . TRP D 1 166 ? -28.059 34.588  -29.067 1.00 32.00  ? 195 TRP C CD1 1 
ATOM   11574 C CD2 . TRP D 1 166 ? -27.811 35.809  -27.210 1.00 29.33  ? 195 TRP C CD2 1 
ATOM   11575 N NE1 . TRP D 1 166 ? -29.295 34.998  -28.659 1.00 30.43  ? 195 TRP C NE1 1 
ATOM   11576 C CE2 . TRP D 1 166 ? -29.185 35.759  -27.538 1.00 31.29  ? 195 TRP C CE2 1 
ATOM   11577 C CE3 . TRP D 1 166 ? -27.419 36.525  -26.089 1.00 28.31  ? 195 TRP C CE3 1 
ATOM   11578 C CZ2 . TRP D 1 166 ? -30.168 36.422  -26.803 1.00 31.15  ? 195 TRP C CZ2 1 
ATOM   11579 C CZ3 . TRP D 1 166 ? -28.387 37.185  -25.354 1.00 33.46  ? 195 TRP C CZ3 1 
ATOM   11580 C CH2 . TRP D 1 166 ? -29.741 37.140  -25.706 1.00 32.19  ? 195 TRP C CH2 1 
ATOM   11581 N N   . GLU D 1 167 ? -26.703 32.998  -25.831 1.00 28.93  ? 196 GLU C N   1 
ATOM   11582 C CA  . GLU D 1 167 ? -27.412 33.076  -24.567 1.00 32.96  ? 196 GLU C CA  1 
ATOM   11583 C C   . GLU D 1 167 ? -26.583 32.454  -23.454 1.00 30.38  ? 196 GLU C C   1 
ATOM   11584 O O   . GLU D 1 167 ? -26.514 33.000  -22.361 1.00 26.49  ? 196 GLU C O   1 
ATOM   11585 C CB  . GLU D 1 167 ? -28.761 32.379  -24.664 1.00 33.90  ? 196 GLU C CB  1 
ATOM   11586 C CG  . GLU D 1 167 ? -29.779 33.168  -25.486 1.00 37.70  ? 196 GLU C CG  1 
ATOM   11587 C CD  . GLU D 1 167 ? -31.161 32.534  -25.445 1.00 43.70  ? 196 GLU C CD  1 
ATOM   11588 O OE1 . GLU D 1 167 ? -31.588 32.170  -24.333 1.00 52.67  ? 196 GLU C OE1 1 
ATOM   11589 O OE2 . GLU D 1 167 ? -31.802 32.392  -26.495 1.00 51.33  ? 196 GLU C OE2 1 
ATOM   11590 N N   . LEU D 1 168 ? -25.936 31.333  -23.763 1.00 28.84  ? 197 LEU C N   1 
ATOM   11591 C CA  . LEU D 1 168 ? -25.147 30.631  -22.777 1.00 33.08  ? 197 LEU C CA  1 
ATOM   11592 C C   . LEU D 1 168 ? -23.811 31.333  -22.572 1.00 31.20  ? 197 LEU C C   1 
ATOM   11593 O O   . LEU D 1 168 ? -23.308 31.351  -21.465 1.00 28.19  ? 197 LEU C O   1 
ATOM   11594 C CB  . LEU D 1 168 ? -24.945 29.203  -23.268 1.00 39.11  ? 197 LEU C CB  1 
ATOM   11595 C CG  . LEU D 1 168 ? -26.214 28.364  -23.409 1.00 43.68  ? 197 LEU C CG  1 
ATOM   11596 C CD1 . LEU D 1 168 ? -25.808 27.112  -24.201 1.00 48.79  ? 197 LEU C CD1 1 
ATOM   11597 C CD2 . LEU D 1 168 ? -26.849 28.012  -22.062 1.00 44.03  ? 197 LEU C CD2 1 
ATOM   11598 N N   . ILE D 1 169 ? -23.199 31.825  -23.658 1.00 29.55  ? 198 ILE C N   1 
ATOM   11599 C CA  . ILE D 1 169 ? -22.024 32.670  -23.564 1.00 28.71  ? 198 ILE C CA  1 
ATOM   11600 C C   . ILE D 1 169 ? -22.352 33.839  -22.633 1.00 28.65  ? 198 ILE C C   1 
ATOM   11601 O O   . ILE D 1 169 ? -21.618 34.125  -21.695 1.00 30.18  ? 198 ILE C O   1 
ATOM   11602 C CB  . ILE D 1 169 ? -21.593 33.166  -24.949 1.00 30.37  ? 198 ILE C CB  1 
ATOM   11603 C CG1 . ILE D 1 169 ? -21.266 32.039  -25.877 1.00 31.37  ? 198 ILE C CG1 1 
ATOM   11604 C CG2 . ILE D 1 169 ? -20.397 34.091  -24.798 1.00 35.74  ? 198 ILE C CG2 1 
ATOM   11605 C CD1 . ILE D 1 169 ? -20.073 31.238  -25.404 1.00 30.16  ? 198 ILE C CD1 1 
ATOM   11606 N N   . TYR D 1 170 ? -23.459 34.530  -22.904 1.00 25.86  ? 199 TYR C N   1 
ATOM   11607 C CA  . TYR D 1 170 ? -23.885 35.600  -22.014 1.00 26.05  ? 199 TYR C CA  1 
ATOM   11608 C C   . TYR D 1 170 ? -23.821 35.148  -20.549 1.00 23.12  ? 199 TYR C C   1 
ATOM   11609 O O   . TYR D 1 170 ? -23.255 35.858  -19.722 1.00 23.56  ? 199 TYR C O   1 
ATOM   11610 C CB  . TYR D 1 170 ? -25.260 36.114  -22.429 1.00 27.77  ? 199 TYR C CB  1 
ATOM   11611 C CG  . TYR D 1 170 ? -25.866 37.078  -21.421 1.00 23.92  ? 199 TYR C CG  1 
ATOM   11612 C CD1 . TYR D 1 170 ? -25.593 38.428  -21.465 1.00 23.70  ? 199 TYR C CD1 1 
ATOM   11613 C CD2 . TYR D 1 170 ? -26.698 36.620  -20.412 1.00 26.08  ? 199 TYR C CD2 1 
ATOM   11614 C CE1 . TYR D 1 170 ? -26.136 39.303  -20.535 1.00 25.61  ? 199 TYR C CE1 1 
ATOM   11615 C CE2 . TYR D 1 170 ? -27.231 37.482  -19.467 1.00 29.24  ? 199 TYR C CE2 1 
ATOM   11616 C CZ  . TYR D 1 170 ? -26.964 38.830  -19.540 1.00 25.08  ? 199 TYR C CZ  1 
ATOM   11617 O OH  . TYR D 1 170 ? -27.539 39.682  -18.636 1.00 32.08  ? 199 TYR C OH  1 
ATOM   11618 N N   . GLU D 1 171 ? -24.379 33.972  -20.220 1.00 27.66  ? 200 GLU C N   1 
ATOM   11619 C CA  . GLU D 1 171 ? -24.522 33.571  -18.824 1.00 27.77  ? 200 GLU C CA  1 
ATOM   11620 C C   . GLU D 1 171 ? -23.153 33.326  -18.199 1.00 25.27  ? 200 GLU C C   1 
ATOM   11621 O O   . GLU D 1 171 ? -22.869 33.829  -17.115 1.00 24.29  ? 200 GLU C O   1 
ATOM   11622 C CB  . GLU D 1 171 ? -25.417 32.365  -18.530 1.00 26.14  ? 200 GLU C CB  1 
ATOM   11623 C CG  . GLU D 1 171 ? -26.896 32.559  -18.846 1.00 28.89  ? 200 GLU C CG  1 
ATOM   11624 C CD  . GLU D 1 171 ? -27.625 33.518  -17.938 1.00 31.85  ? 200 GLU C CD  1 
ATOM   11625 O OE1 . GLU D 1 171 ? -27.189 33.693  -16.785 1.00 34.57  ? 200 GLU C OE1 1 
ATOM   11626 O OE2 . GLU D 1 171 ? -28.581 34.155  -18.435 1.00 38.07  ? 200 GLU C OE2 1 
ATOM   11627 N N   . ASP D 1 172 ? -22.344 32.510  -18.878 1.00 26.89  ? 201 ASP C N   1 
ATOM   11628 C CA  . ASP D 1 172 ? -20.997 32.205  -18.473 1.00 29.19  ? 201 ASP C CA  1 
ATOM   11629 C C   . ASP D 1 172 ? -20.194 33.482  -18.314 1.00 28.00  ? 201 ASP C C   1 
ATOM   11630 O O   . ASP D 1 172 ? -19.455 33.629  -17.336 1.00 30.03  ? 201 ASP C O   1 
ATOM   11631 C CB  . ASP D 1 172 ? -20.354 31.225  -19.437 1.00 31.94  ? 201 ASP C CB  1 
ATOM   11632 C CG  . ASP D 1 172 ? -20.827 29.790  -19.301 1.00 32.56  ? 201 ASP C CG  1 
ATOM   11633 O OD1 . ASP D 1 172 ? -21.634 29.550  -18.392 1.00 33.47  ? 201 ASP C OD1 1 
ATOM   11634 O OD2 . ASP D 1 172 ? -20.390 28.921  -20.112 1.00 33.59  ? 201 ASP C OD2 1 
ATOM   11635 N N   . SER D 1 173 ? -20.360 34.407  -19.261 1.00 28.98  ? 202 SER C N   1 
ATOM   11636 C CA  . SER D 1 173 ? -19.650 35.673  -19.226 1.00 27.42  ? 202 SER C CA  1 
ATOM   11637 C C   . SER D 1 173 ? -20.047 36.529  -18.023 1.00 28.90  ? 202 SER C C   1 
ATOM   11638 O O   . SER D 1 173 ? -19.193 37.113  -17.355 1.00 25.77  ? 202 SER C O   1 
ATOM   11639 C CB  . SER D 1 173 ? -19.884 36.414  -20.460 1.00 27.33  ? 202 SER C CB  1 
ATOM   11640 O OG  . SER D 1 173 ? -19.202 35.766  -21.510 1.00 24.84  ? 202 SER C OG  1 
ATOM   11641 N N   . MET D 1 174 ? -21.344 36.621  -17.745 1.00 28.48  ? 203 MET C N   1 
ATOM   11642 C CA  . MET D 1 174 ? -21.793 37.368  -16.582 1.00 26.39  ? 203 MET C CA  1 
ATOM   11643 C C   . MET D 1 174 ? -21.255 36.712  -15.318 1.00 29.46  ? 203 MET C C   1 
ATOM   11644 O O   . MET D 1 174 ? -20.888 37.430  -14.380 1.00 29.31  ? 203 MET C O   1 
ATOM   11645 C CB  . MET D 1 174 ? -23.322 37.442  -16.537 1.00 30.38  ? 203 MET C CB  1 
ATOM   11646 C CG  . MET D 1 174 ? -23.898 38.270  -17.684 1.00 33.01  ? 203 MET C CG  1 
ATOM   11647 S SD  . MET D 1 174 ? -23.843 40.036  -17.364 1.00 32.11  ? 203 MET C SD  1 
ATOM   11648 C CE  . MET D 1 174 ? -25.123 40.096  -16.098 1.00 37.62  ? 203 MET C CE  1 
ATOM   11649 N N   . ASP D 1 175 ? -21.168 35.356  -15.311 1.00 32.67  ? 204 ASP C N   1 
ATOM   11650 C CA  . ASP D 1 175 ? -20.682 34.641  -14.139 1.00 30.43  ? 204 ASP C CA  1 
ATOM   11651 C C   . ASP D 1 175 ? -19.179 34.864  -13.954 1.00 32.23  ? 204 ASP C C   1 
ATOM   11652 O O   . ASP D 1 175 ? -18.739 35.114  -12.842 1.00 30.62  ? 204 ASP C O   1 
ATOM   11653 C CB  . ASP D 1 175 ? -20.953 33.156  -14.195 1.00 32.87  ? 204 ASP C CB  1 
ATOM   11654 C CG  . ASP D 1 175 ? -22.383 32.744  -13.889 1.00 35.73  ? 204 ASP C CG  1 
ATOM   11655 O OD1 . ASP D 1 175 ? -23.119 33.576  -13.310 1.00 42.40  ? 204 ASP C OD1 1 
ATOM   11656 O OD2 . ASP D 1 175 ? -22.751 31.623  -14.279 1.00 36.63  ? 204 ASP C OD2 1 
ATOM   11657 N N   . LEU D 1 176 ? -18.398 34.839  -15.047 1.00 25.22  ? 205 LEU C N   1 
ATOM   11658 C CA  . LEU D 1 176 ? -16.979 34.979  -14.894 1.00 26.10  ? 205 LEU C CA  1 
ATOM   11659 C C   . LEU D 1 176 ? -16.650 36.407  -14.444 1.00 27.33  ? 205 LEU C C   1 
ATOM   11660 O O   . LEU D 1 176 ? -15.784 36.604  -13.593 1.00 23.60  ? 205 LEU C O   1 
ATOM   11661 C CB  . LEU D 1 176 ? -16.316 34.527  -16.191 1.00 25.58  ? 205 LEU C CB  1 
ATOM   11662 C CG  . LEU D 1 176 ? -14.855 34.902  -16.392 1.00 25.49  ? 205 LEU C CG  1 
ATOM   11663 C CD1 . LEU D 1 176 ? -14.001 34.420  -15.259 1.00 27.08  ? 205 LEU C CD1 1 
ATOM   11664 C CD2 . LEU D 1 176 ? -14.378 34.325  -17.725 1.00 26.87  ? 205 LEU C CD2 1 
ATOM   11665 N N   . ILE D 1 177 ? -17.298 37.407  -15.046 1.00 29.41  ? 206 ILE C N   1 
ATOM   11666 C CA  . ILE D 1 177 ? -17.100 38.765  -14.596 1.00 31.55  ? 206 ILE C CA  1 
ATOM   11667 C C   . ILE D 1 177 ? -17.390 38.864  -13.091 1.00 28.65  ? 206 ILE C C   1 
ATOM   11668 O O   . ILE D 1 177 ? -16.592 39.423  -12.338 1.00 28.19  ? 206 ILE C O   1 
ATOM   11669 C CB  . ILE D 1 177 ? -17.926 39.743  -15.446 1.00 27.36  ? 206 ILE C CB  1 
ATOM   11670 C CG1 . ILE D 1 177 ? -17.368 39.811  -16.861 1.00 27.81  ? 206 ILE C CG1 1 
ATOM   11671 C CG2 . ILE D 1 177 ? -17.965 41.127  -14.807 1.00 28.34  ? 206 ILE C CG2 1 
ATOM   11672 C CD1 . ILE D 1 177 ? -18.346 40.365  -17.891 1.00 30.24  ? 206 ILE C CD1 1 
ATOM   11673 N N   . ALA D 1 178 ? -18.524 38.332  -12.649 1.00 29.68  ? 207 ALA C N   1 
ATOM   11674 C CA  . ALA D 1 178 ? -18.890 38.408  -11.242 1.00 32.34  ? 207 ALA C CA  1 
ATOM   11675 C C   . ALA D 1 178 ? -17.781 37.805  -10.367 1.00 31.49  ? 207 ALA C C   1 
ATOM   11676 O O   . ALA D 1 178 ? -17.483 38.302  -9.282  1.00 27.17  ? 207 ALA C O   1 
ATOM   11677 C CB  . ALA D 1 178 ? -20.214 37.691  -11.018 1.00 33.99  ? 207 ALA C CB  1 
ATOM   11678 N N   . LYS D 1 179 ? -17.120 36.758  -10.880 1.00 31.60  ? 208 LYS C N   1 
ATOM   11679 C CA  . LYS D 1 179 ? -16.210 35.967  -10.076 1.00 33.88  ? 208 LYS C CA  1 
ATOM   11680 C C   . LYS D 1 179 ? -14.781 36.517  -10.084 1.00 33.12  ? 208 LYS C C   1 
ATOM   11681 O O   . LYS D 1 179 ? -14.020 36.215  -9.175  1.00 32.27  ? 208 LYS C O   1 
ATOM   11682 C CB  . LYS D 1 179 ? -16.254 34.501  -10.535 1.00 35.37  ? 208 LYS C CB  1 
ATOM   11683 C CG  . LYS D 1 179 ? -17.515 33.717  -10.101 1.00 34.73  ? 208 LYS C CG  1 
ATOM   11684 C CD  . LYS D 1 179 ? -17.571 32.292  -10.626 1.00 37.44  ? 208 LYS C CD  1 
ATOM   11685 C CE  . LYS D 1 179 ? -18.963 31.819  -10.997 1.00 42.40  ? 208 LYS C CE  1 
ATOM   11686 N NZ  . LYS D 1 179 ? -19.901 31.895  -9.870  1.00 42.21  ? 208 LYS C NZ  1 
ATOM   11687 N N   . LEU D 1 180 ? -14.402 37.277  -11.113 1.00 31.70  ? 209 LEU C N   1 
ATOM   11688 C CA  . LEU D 1 180 ? -13.017 37.643  -11.316 1.00 29.99  ? 209 LEU C CA  1 
ATOM   11689 C C   . LEU D 1 180 ? -12.477 38.405  -10.110 1.00 31.26  ? 209 LEU C C   1 
ATOM   11690 O O   . LEU D 1 180 ? -11.367 38.131  -9.673  1.00 30.10  ? 209 LEU C O   1 
ATOM   11691 C CB  . LEU D 1 180 ? -12.852 38.445  -12.615 1.00 29.52  ? 209 LEU C CB  1 
ATOM   11692 C CG  . LEU D 1 180 ? -12.585 37.576  -13.848 1.00 30.26  ? 209 LEU C CG  1 
ATOM   11693 C CD1 . LEU D 1 180 ? -12.751 38.325  -15.166 1.00 34.11  ? 209 LEU C CD1 1 
ATOM   11694 C CD2 . LEU D 1 180 ? -11.216 37.006  -13.734 1.00 32.62  ? 209 LEU C CD2 1 
ATOM   11695 N N   . PRO D 1 181 ? -13.198 39.409  -9.555  1.00 28.56  ? 210 PRO C N   1 
ATOM   11696 C CA  . PRO D 1 181 ? -12.679 40.174  -8.429  1.00 29.91  ? 210 PRO C CA  1 
ATOM   11697 C C   . PRO D 1 181 ? -12.324 39.298  -7.242  1.00 31.08  ? 210 PRO C C   1 
ATOM   11698 O O   . PRO D 1 181 ? -11.281 39.506  -6.620  1.00 30.81  ? 210 PRO C O   1 
ATOM   11699 C CB  . PRO D 1 181 ? -13.807 41.190  -8.085  1.00 31.62  ? 210 PRO C CB  1 
ATOM   11700 C CG  . PRO D 1 181 ? -14.666 41.263  -9.331  1.00 34.16  ? 210 PRO C CG  1 
ATOM   11701 C CD  . PRO D 1 181 ? -14.415 39.998  -10.117 1.00 29.29  ? 210 PRO C CD  1 
ATOM   11702 N N   . CYS D 1 182 ? -13.201 38.328  -6.947  1.00 34.85  ? 211 CYS C N   1 
ATOM   11703 C CA  . CYS D 1 182 ? -12.961 37.345  -5.902  1.00 32.99  ? 211 CYS C CA  1 
ATOM   11704 C C   . CYS D 1 182 ? -11.688 36.531  -6.133  1.00 34.66  ? 211 CYS C C   1 
ATOM   11705 O O   . CYS D 1 182 ? -10.918 36.307  -5.203  1.00 29.87  ? 211 CYS C O   1 
ATOM   11706 C CB  . CYS D 1 182 ? -14.091 36.326  -5.828  1.00 35.12  ? 211 CYS C CB  1 
ATOM   11707 S SG  . CYS D 1 182 ? -15.708 37.081  -5.520  1.00 47.03  ? 211 CYS C SG  1 
ATOM   11708 N N   . VAL D 1 183 ? -11.504 36.043  -7.364  1.00 29.49  ? 212 VAL C N   1 
ATOM   11709 C CA  . VAL D 1 183 ? -10.325 35.257  -7.707  1.00 33.68  ? 212 VAL C CA  1 
ATOM   11710 C C   . VAL D 1 183 ? -9.092  36.138  -7.582  1.00 27.62  ? 212 VAL C C   1 
ATOM   11711 O O   . VAL D 1 183 ? -8.139  35.760  -6.913  1.00 27.36  ? 212 VAL C O   1 
ATOM   11712 C CB  . VAL D 1 183 ? -10.381 34.652  -9.120  1.00 32.87  ? 212 VAL C CB  1 
ATOM   11713 C CG1 . VAL D 1 183 ? -9.089  33.937  -9.506  1.00 29.36  ? 212 VAL C CG1 1 
ATOM   11714 C CG2 . VAL D 1 183 ? -11.576 33.733  -9.274  1.00 32.68  ? 212 VAL C CG2 1 
ATOM   11715 N N   . ALA D 1 184 ? -9.164  37.318  -8.198  1.00 28.78  ? 213 ALA C N   1 
ATOM   11716 C CA  . ALA D 1 184 ? -8.070  38.264  -8.203  1.00 28.29  ? 213 ALA C CA  1 
ATOM   11717 C C   . ALA D 1 184 ? -7.703  38.702  -6.776  1.00 34.46  ? 213 ALA C C   1 
ATOM   11718 O O   . ALA D 1 184 ? -6.517  38.950  -6.461  1.00 32.64  ? 213 ALA C O   1 
ATOM   11719 C CB  . ALA D 1 184 ? -8.451  39.450  -9.047  1.00 29.40  ? 213 ALA C CB  1 
ATOM   11720 N N   . ALA D 1 185 ? -8.725  38.836  -5.924  1.00 28.00  ? 214 ALA C N   1 
ATOM   11721 C CA  . ALA D 1 185 ? -8.497  39.296  -4.567  1.00 30.51  ? 214 ALA C CA  1 
ATOM   11722 C C   . ALA D 1 185 ? -7.913  38.168  -3.725  1.00 33.07  ? 214 ALA C C   1 
ATOM   11723 O O   . ALA D 1 185 ? -7.038  38.422  -2.902  1.00 32.69  ? 214 ALA C O   1 
ATOM   11724 C CB  . ALA D 1 185 ? -9.763  39.839  -3.958  1.00 36.14  ? 214 ALA C CB  1 
ATOM   11725 N N   . LYS D 1 186 ? -8.428  36.949  -3.901  1.00 32.73  ? 215 LYS C N   1 
ATOM   11726 C CA  . LYS D 1 186 ? -7.871  35.771  -3.250  1.00 35.50  ? 215 LYS C CA  1 
ATOM   11727 C C   . LYS D 1 186 ? -6.381  35.606  -3.582  1.00 38.10  ? 215 LYS C C   1 
ATOM   11728 O O   . LYS D 1 186 ? -5.603  35.245  -2.696  1.00 34.99  ? 215 LYS C O   1 
ATOM   11729 C CB  . LYS D 1 186 ? -8.762  34.572  -3.584  1.00 42.49  ? 215 LYS C CB  1 
ATOM   11730 C CG  . LYS D 1 186 ? -8.353  33.235  -2.997  1.00 55.46  ? 215 LYS C CG  1 
ATOM   11731 C CD  . LYS D 1 186 ? -9.506  32.322  -2.573  1.00 63.68  ? 215 LYS C CD  1 
ATOM   11732 C CE  . LYS D 1 186 ? -10.013 32.609  -1.186  1.00 67.19  ? 215 LYS C CE  1 
ATOM   11733 N NZ  . LYS D 1 186 ? -9.016  32.304  -0.146  1.00 64.96  ? 215 LYS C NZ  1 
ATOM   11734 N N   . ILE D 1 187 ? -5.959  35.928  -4.824  1.00 37.25  ? 216 ILE C N   1 
ATOM   11735 C CA  . ILE D 1 187 ? -4.552  35.852  -5.232  1.00 29.24  ? 216 ILE C CA  1 
ATOM   11736 C C   . ILE D 1 187 ? -3.768  36.925  -4.501  1.00 30.25  ? 216 ILE C C   1 
ATOM   11737 O O   . ILE D 1 187 ? -2.747  36.648  -3.896  1.00 29.39  ? 216 ILE C O   1 
ATOM   11738 C CB  . ILE D 1 187 ? -4.360  35.980  -6.752  1.00 26.66  ? 216 ILE C CB  1 
ATOM   11739 C CG1 . ILE D 1 187 ? -4.816  34.699  -7.506  1.00 27.83  ? 216 ILE C CG1 1 
ATOM   11740 C CG2 . ILE D 1 187 ? -2.919  36.314  -7.105  1.00 29.03  ? 216 ILE C CG2 1 
ATOM   11741 C CD1 . ILE D 1 187 ? -5.203  34.951  -8.953  1.00 32.83  ? 216 ILE C CD1 1 
ATOM   11742 N N   . TYR D 1 188 ? -4.247  38.156  -4.562  1.00 25.99  ? 217 TYR C N   1 
ATOM   11743 C CA  . TYR D 1 188 ? -3.584  39.225  -3.846  1.00 28.43  ? 217 TYR C CA  1 
ATOM   11744 C C   . TYR D 1 188 ? -3.349  38.821  -2.398  1.00 29.56  ? 217 TYR C C   1 
ATOM   11745 O O   . TYR D 1 188 ? -2.218  38.888  -1.942  1.00 29.29  ? 217 TYR C O   1 
ATOM   11746 C CB  . TYR D 1 188 ? -4.436  40.477  -3.848  1.00 28.21  ? 217 TYR C CB  1 
ATOM   11747 C CG  . TYR D 1 188 ? -3.677  41.688  -3.377  1.00 29.91  ? 217 TYR C CG  1 
ATOM   11748 C CD1 . TYR D 1 188 ? -2.742  42.263  -4.223  1.00 32.15  ? 217 TYR C CD1 1 
ATOM   11749 C CD2 . TYR D 1 188 ? -3.930  42.290  -2.146  1.00 30.44  ? 217 TYR C CD2 1 
ATOM   11750 C CE1 . TYR D 1 188 ? -2.015  43.370  -3.841  1.00 30.81  ? 217 TYR C CE1 1 
ATOM   11751 C CE2 . TYR D 1 188 ? -3.256  43.447  -1.784  1.00 34.22  ? 217 TYR C CE2 1 
ATOM   11752 C CZ  . TYR D 1 188 ? -2.289  43.973  -2.630  1.00 33.77  ? 217 TYR C CZ  1 
ATOM   11753 O OH  . TYR D 1 188 ? -1.571  45.102  -2.399  1.00 33.20  ? 217 TYR C OH  1 
ATOM   11754 N N   . ARG D 1 189 ? -4.410  38.381  -1.705  1.00 30.45  ? 218 ARG C N   1 
ATOM   11755 C CA  . ARG D 1 189 ? -4.340  38.149  -0.265  1.00 36.54  ? 218 ARG C CA  1 
ATOM   11756 C C   . ARG D 1 189 ? -3.408  36.985  0.032   1.00 32.71  ? 218 ARG C C   1 
ATOM   11757 O O   . ARG D 1 189 ? -2.600  37.035  0.943   1.00 35.01  ? 218 ARG C O   1 
ATOM   11758 C CB  . ARG D 1 189 ? -5.700  37.918  0.396   1.00 36.18  ? 218 ARG C CB  1 
ATOM   11759 C CG  . ARG D 1 189 ? -6.495  39.209  0.433   1.00 46.12  ? 218 ARG C CG  1 
ATOM   11760 C CD  . ARG D 1 189 ? -7.758  39.222  1.294   1.00 53.77  ? 218 ARG C CD  1 
ATOM   11761 N NE  . ARG D 1 189 ? -7.447  39.618  2.670   1.00 68.20  ? 218 ARG C NE  1 
ATOM   11762 C CZ  . ARG D 1 189 ? -6.808  40.724  3.031   1.00 76.41  ? 218 ARG C CZ  1 
ATOM   11763 N NH1 . ARG D 1 189 ? -6.604  41.703  2.164   1.00 88.16  ? 218 ARG C NH1 1 
ATOM   11764 N NH2 . ARG D 1 189 ? -6.392  40.861  4.275   1.00 73.91  ? 218 ARG C NH2 1 
ATOM   11765 N N   . ASN D 1 190 ? -3.533  35.935  -0.749  1.00 34.96  ? 219 ASN C N   1 
ATOM   11766 C CA  . ASN D 1 190 ? -2.700  34.756  -0.608  1.00 32.04  ? 219 ASN C CA  1 
ATOM   11767 C C   . ASN D 1 190 ? -1.229  35.125  -0.771  1.00 32.33  ? 219 ASN C C   1 
ATOM   11768 O O   . ASN D 1 190 ? -0.418  34.617  -0.001  1.00 33.08  ? 219 ASN C O   1 
ATOM   11769 C CB  . ASN D 1 190 ? -3.185  33.620  -1.508  1.00 29.48  ? 219 ASN C CB  1 
ATOM   11770 C CG  . ASN D 1 190 ? -4.462  33.020  -0.969  1.00 35.28  ? 219 ASN C CG  1 
ATOM   11771 O OD1 . ASN D 1 190 ? -4.883  33.350  0.142   1.00 40.68  ? 219 ASN C OD1 1 
ATOM   11772 N ND2 . ASN D 1 190 ? -5.126  32.170  -1.734  1.00 40.83  ? 219 ASN C ND2 1 
ATOM   11773 N N   . LEU D 1 191 ? -0.894  36.041  -1.691  1.00 29.99  ? 220 LEU C N   1 
ATOM   11774 C CA  . LEU D 1 191 ? 0.494   36.345  -1.974  1.00 30.64  ? 220 LEU C CA  1 
ATOM   11775 C C   . LEU D 1 191 ? 1.060   37.428  -1.051  1.00 34.02  ? 220 LEU C C   1 
ATOM   11776 O O   . LEU D 1 191 ? 2.254   37.402  -0.781  1.00 33.92  ? 220 LEU C O   1 
ATOM   11777 C CB  . LEU D 1 191 ? 0.661   36.754  -3.429  1.00 30.98  ? 220 LEU C CB  1 
ATOM   11778 C CG  . LEU D 1 191 ? 0.626   35.623  -4.466  1.00 34.04  ? 220 LEU C CG  1 
ATOM   11779 C CD1 . LEU D 1 191 ? 0.688   36.260  -5.839  1.00 33.72  ? 220 LEU C CD1 1 
ATOM   11780 C CD2 . LEU D 1 191 ? 1.763   34.648  -4.303  1.00 35.24  ? 220 LEU C CD2 1 
ATOM   11781 N N   . TYR D 1 192 ? 0.260   38.397  -0.597  1.00 37.83  ? 221 TYR C N   1 
ATOM   11782 C CA  . TYR D 1 192 ? 0.841   39.577  0.019   1.00 36.42  ? 221 TYR C CA  1 
ATOM   11783 C C   . TYR D 1 192 ? 0.191   39.994  1.332   1.00 37.45  ? 221 TYR C C   1 
ATOM   11784 O O   . TYR D 1 192 ? 0.561   41.037  1.860   1.00 39.34  ? 221 TYR C O   1 
ATOM   11785 C CB  . TYR D 1 192 ? 0.687   40.755  -0.937  1.00 46.42  ? 221 TYR C CB  1 
ATOM   11786 C CG  . TYR D 1 192 ? 1.125   40.471  -2.361  1.00 42.85  ? 221 TYR C CG  1 
ATOM   11787 C CD1 . TYR D 1 192 ? 2.386   39.957  -2.638  1.00 44.82  ? 221 TYR C CD1 1 
ATOM   11788 C CD2 . TYR D 1 192 ? 0.268   40.723  -3.418  1.00 44.67  ? 221 TYR C CD2 1 
ATOM   11789 C CE1 . TYR D 1 192 ? 2.793   39.712  -3.935  1.00 40.54  ? 221 TYR C CE1 1 
ATOM   11790 C CE2 . TYR D 1 192 ? 0.655   40.472  -4.719  1.00 40.00  ? 221 TYR C CE2 1 
ATOM   11791 C CZ  . TYR D 1 192 ? 1.914   39.964  -4.972  1.00 40.63  ? 221 TYR C CZ  1 
ATOM   11792 O OH  . TYR D 1 192 ? 2.255   39.710  -6.259  1.00 37.87  ? 221 TYR C OH  1 
ATOM   11793 N N   . ARG D 1 193 ? -0.817  39.251  1.800   1.00 45.23  ? 222 ARG C N   1 
ATOM   11794 C CA  . ARG D 1 193 ? -1.518  39.536  3.049   1.00 41.35  ? 222 ARG C CA  1 
ATOM   11795 C C   . ARG D 1 193 ? -1.704  38.257  3.881   1.00 40.27  ? 222 ARG C C   1 
ATOM   11796 O O   . ARG D 1 193 ? -2.736  38.100  4.533   1.00 39.30  ? 222 ARG C O   1 
ATOM   11797 C CB  . ARG D 1 193 ? -2.866  40.213  2.773   1.00 38.66  ? 222 ARG C CB  1 
ATOM   11798 C CG  . ARG D 1 193 ? -2.799  41.552  2.048   1.00 40.27  ? 222 ARG C CG  1 
ATOM   11799 C CD  . ARG D 1 193 ? -2.123  42.613  2.895   1.00 41.16  ? 222 ARG C CD  1 
ATOM   11800 N NE  . ARG D 1 193 ? -2.260  43.963  2.332   1.00 41.25  ? 222 ARG C NE  1 
ATOM   11801 C CZ  . ARG D 1 193 ? -1.570  44.425  1.308   1.00 43.41  ? 222 ARG C CZ  1 
ATOM   11802 N NH1 . ARG D 1 193 ? -0.737  43.628  0.666   1.00 48.26  ? 222 ARG C NH1 1 
ATOM   11803 N NH2 . ARG D 1 193 ? -1.751  45.663  0.889   1.00 43.82  ? 222 ARG C NH2 1 
ATOM   11804 N N   . GLU D 1 194 ? -0.727  37.334  3.812   1.00 42.80  ? 223 GLU C N   1 
ATOM   11805 C CA  . GLU D 1 194 ? -0.613  36.191  4.718   1.00 53.96  ? 223 GLU C CA  1 
ATOM   11806 C C   . GLU D 1 194 ? -1.808  35.250  4.606   1.00 52.69  ? 223 GLU C C   1 
ATOM   11807 O O   . GLU D 1 194 ? -2.164  34.600  5.589   1.00 53.96  ? 223 GLU C O   1 
ATOM   11808 C CB  . GLU D 1 194 ? -0.573  36.566  6.206   1.00 62.80  ? 223 GLU C CB  1 
ATOM   11809 C CG  . GLU D 1 194 ? 0.672   37.325  6.661   1.00 76.69  ? 223 GLU C CG  1 
ATOM   11810 C CD  . GLU D 1 194 ? 0.600   37.804  8.111   1.00 92.67  ? 223 GLU C CD  1 
ATOM   11811 O OE1 . GLU D 1 194 ? 0.313   36.975  9.012   1.00 104.82 ? 223 GLU C OE1 1 
ATOM   11812 O OE2 . GLU D 1 194 ? 0.831   39.012  8.356   1.00 84.77  ? 223 GLU C OE2 1 
ATOM   11813 N N   . GLY D 1 195 ? -2.451  35.191  3.431   1.00 47.82  ? 224 GLY C N   1 
ATOM   11814 C CA  . GLY D 1 195 ? -3.483  34.188  3.198   1.00 42.64  ? 224 GLY C CA  1 
ATOM   11815 C C   . GLY D 1 195 ? -4.792  34.484  3.924   1.00 41.10  ? 224 GLY C C   1 
ATOM   11816 O O   . GLY D 1 195 ? -5.662  33.622  3.969   1.00 45.86  ? 224 GLY C O   1 
ATOM   11817 N N   . SER D 1 196 ? -4.936  35.708  4.456   1.00 42.67  ? 225 SER C N   1 
ATOM   11818 C CA  . SER D 1 196 ? -6.162  36.129  5.118   1.00 45.38  ? 225 SER C CA  1 
ATOM   11819 C C   . SER D 1 196 ? -7.316  36.086  4.119   1.00 51.12  ? 225 SER C C   1 
ATOM   11820 O O   . SER D 1 196 ? -7.083  36.008  2.907   1.00 44.06  ? 225 SER C O   1 
ATOM   11821 C CB  . SER D 1 196 ? -6.012  37.493  5.760   1.00 42.37  ? 225 SER C CB  1 
ATOM   11822 O OG  . SER D 1 196 ? -5.397  38.440  4.886   1.00 49.97  ? 225 SER C OG  1 
ATOM   11823 N N   . GLY D 1 197 ? -8.546  36.177  4.657   1.00 51.50  ? 226 GLY C N   1 
ATOM   11824 C CA  . GLY D 1 197 ? -9.781  35.935  3.924   1.00 45.96  ? 226 GLY C CA  1 
ATOM   11825 C C   . GLY D 1 197 ? -10.298 37.171  3.183   1.00 48.34  ? 226 GLY C C   1 
ATOM   11826 O O   . GLY D 1 197 ? -10.161 38.299  3.650   1.00 44.13  ? 226 GLY C O   1 
ATOM   11827 N N   . ILE D 1 198 ? -10.954 36.938  2.038   1.00 49.94  ? 227 ILE C N   1 
ATOM   11828 C CA  . ILE D 1 198 ? -11.436 38.017  1.185   1.00 52.75  ? 227 ILE C CA  1 
ATOM   11829 C C   . ILE D 1 198 ? -12.706 38.673  1.745   1.00 54.66  ? 227 ILE C C   1 
ATOM   11830 O O   . ILE D 1 198 ? -13.090 39.756  1.301   1.00 50.00  ? 227 ILE C O   1 
ATOM   11831 C CB  . ILE D 1 198 ? -11.598 37.530  -0.270  1.00 54.78  ? 227 ILE C CB  1 
ATOM   11832 C CG1 . ILE D 1 198 ? -12.615 36.381  -0.424  1.00 56.28  ? 227 ILE C CG1 1 
ATOM   11833 C CG2 . ILE D 1 198 ? -10.223 37.137  -0.820  1.00 51.96  ? 227 ILE C CG2 1 
ATOM   11834 C CD1 . ILE D 1 198 ? -12.972 36.051  -1.869  1.00 54.53  ? 227 ILE C CD1 1 
ATOM   11835 N N   . GLY D 1 199 ? -13.350 38.060  2.746   1.00 61.60  ? 228 GLY C N   1 
ATOM   11836 C CA  . GLY D 1 199 ? -14.595 38.604  3.274   1.00 60.72  ? 228 GLY C CA  1 
ATOM   11837 C C   . GLY D 1 199 ? -15.748 38.471  2.273   1.00 60.32  ? 228 GLY C C   1 
ATOM   11838 O O   . GLY D 1 199 ? -15.679 37.699  1.309   1.00 49.50  ? 228 GLY C O   1 
ATOM   11839 N N   . ALA D 1 200 ? -16.806 39.257  2.503   1.00 57.96  ? 229 ALA C N   1 
ATOM   11840 C CA  . ALA D 1 200 ? -18.085 39.026  1.857   1.00 57.31  ? 229 ALA C CA  1 
ATOM   11841 C C   . ALA D 1 200 ? -18.293 40.011  0.715   1.00 55.59  ? 229 ALA C C   1 
ATOM   11842 O O   . ALA D 1 200 ? -17.736 41.106  0.718   1.00 54.05  ? 229 ALA C O   1 
ATOM   11843 C CB  . ALA D 1 200 ? -19.197 39.149  2.867   1.00 56.04  ? 229 ALA C CB  1 
ATOM   11844 N N   . ILE D 1 201 ? -19.134 39.600  -0.236  1.00 50.75  ? 230 ILE C N   1 
ATOM   11845 C CA  . ILE D 1 201 ? -19.696 40.498  -1.229  1.00 51.46  ? 230 ILE C CA  1 
ATOM   11846 C C   . ILE D 1 201 ? -20.778 41.336  -0.548  1.00 52.10  ? 230 ILE C C   1 
ATOM   11847 O O   . ILE D 1 201 ? -21.569 40.804  0.215   1.00 56.94  ? 230 ILE C O   1 
ATOM   11848 C CB  . ILE D 1 201 ? -20.256 39.684  -2.416  1.00 52.50  ? 230 ILE C CB  1 
ATOM   11849 C CG1 . ILE D 1 201 ? -19.174 38.828  -3.085  1.00 52.55  ? 230 ILE C CG1 1 
ATOM   11850 C CG2 . ILE D 1 201 ? -20.933 40.590  -3.446  1.00 55.33  ? 230 ILE C CG2 1 
ATOM   11851 C CD1 . ILE D 1 201 ? -18.067 39.632  -3.764  1.00 51.66  ? 230 ILE C CD1 1 
ATOM   11852 N N   . ASP D 1 202 ? -20.822 42.640  -0.838  1.00 49.16  ? 231 ASP C N   1 
ATOM   11853 C CA  . ASP D 1 202 ? -21.918 43.483  -0.395  1.00 55.93  ? 231 ASP C CA  1 
ATOM   11854 C C   . ASP D 1 202 ? -22.826 43.764  -1.595  1.00 58.95  ? 231 ASP C C   1 
ATOM   11855 O O   . ASP D 1 202 ? -22.433 44.440  -2.555  1.00 59.25  ? 231 ASP C O   1 
ATOM   11856 C CB  . ASP D 1 202 ? -21.399 44.706  0.346   1.00 58.75  ? 231 ASP C CB  1 
ATOM   11857 C CG  . ASP D 1 202 ? -22.467 45.641  0.902   1.00 68.83  ? 231 ASP C CG  1 
ATOM   11858 O OD1 . ASP D 1 202 ? -23.655 45.503  0.512   1.00 68.66  ? 231 ASP C OD1 1 
ATOM   11859 O OD2 . ASP D 1 202 ? -22.098 46.505  1.730   1.00 87.48  ? 231 ASP C OD2 1 
ATOM   11860 N N   . SER D 1 203 ? -24.065 43.270  -1.513  1.00 51.59  ? 232 SER C N   1 
ATOM   11861 C CA  . SER D 1 203 ? -24.925 43.224  -2.681  1.00 57.31  ? 232 SER C CA  1 
ATOM   11862 C C   . SER D 1 203 ? -25.447 44.610  -3.063  1.00 59.27  ? 232 SER C C   1 
ATOM   11863 O O   . SER D 1 203 ? -26.143 44.737  -4.063  1.00 69.18  ? 232 SER C O   1 
ATOM   11864 C CB  . SER D 1 203 ? -26.040 42.253  -2.480  1.00 64.16  ? 232 SER C CB  1 
ATOM   11865 O OG  . SER D 1 203 ? -26.456 41.754  -3.745  1.00 83.12  ? 232 SER C OG  1 
ATOM   11866 N N   . ASN D 1 204 ? -25.073 45.658  -2.316  1.00 51.18  ? 233 ASN C N   1 
ATOM   11867 C CA  . ASN D 1 204 ? -25.447 47.010  -2.686  1.00 63.54  ? 233 ASN C CA  1 
ATOM   11868 C C   . ASN D 1 204 ? -24.204 47.877  -2.898  1.00 66.23  ? 233 ASN C C   1 
ATOM   11869 O O   . ASN D 1 204 ? -24.295 49.097  -2.797  1.00 71.63  ? 233 ASN C O   1 
ATOM   11870 C CB  . ASN D 1 204 ? -26.393 47.633  -1.657  1.00 70.35  ? 233 ASN C CB  1 
ATOM   11871 C CG  . ASN D 1 204 ? -27.422 46.650  -1.139  1.00 69.61  ? 233 ASN C CG  1 
ATOM   11872 O OD1 . ASN D 1 204 ? -27.515 46.454  0.078   1.00 68.00  ? 233 ASN C OD1 1 
ATOM   11873 N ND2 . ASN D 1 204 ? -28.178 46.007  -2.022  1.00 64.55  ? 233 ASN C ND2 1 
ATOM   11874 N N   . LEU D 1 205 ? -23.048 47.257  -3.190  1.00 59.54  ? 234 LEU C N   1 
ATOM   11875 C CA  . LEU D 1 205 ? -21.877 47.997  -3.644  1.00 50.50  ? 234 LEU C CA  1 
ATOM   11876 C C   . LEU D 1 205 ? -21.567 47.632  -5.095  1.00 43.42  ? 234 LEU C C   1 
ATOM   11877 O O   . LEU D 1 205 ? -21.894 46.551  -5.578  1.00 46.79  ? 234 LEU C O   1 
ATOM   11878 C CB  . LEU D 1 205 ? -20.674 47.735  -2.743  1.00 56.08  ? 234 LEU C CB  1 
ATOM   11879 C CG  . LEU D 1 205 ? -20.709 48.370  -1.351  1.00 62.57  ? 234 LEU C CG  1 
ATOM   11880 C CD1 . LEU D 1 205 ? -19.391 48.014  -0.664  1.00 64.76  ? 234 LEU C CD1 1 
ATOM   11881 C CD2 . LEU D 1 205 ? -20.959 49.892  -1.378  1.00 60.16  ? 234 LEU C CD2 1 
ATOM   11882 N N   . ASP D 1 206 ? -20.973 48.576  -5.815  1.00 40.53  ? 235 ASP C N   1 
ATOM   11883 C CA  . ASP D 1 206 ? -20.613 48.320  -7.195  1.00 46.55  ? 235 ASP C CA  1 
ATOM   11884 C C   . ASP D 1 206 ? -19.453 47.325  -7.215  1.00 42.15  ? 235 ASP C C   1 
ATOM   11885 O O   . ASP D 1 206 ? -18.858 46.999  -6.182  1.00 40.40  ? 235 ASP C O   1 
ATOM   11886 C CB  . ASP D 1 206 ? -20.317 49.600  -7.957  1.00 41.66  ? 235 ASP C CB  1 
ATOM   11887 C CG  . ASP D 1 206 ? -19.174 50.430  -7.406  1.00 45.17  ? 235 ASP C CG  1 
ATOM   11888 O OD1 . ASP D 1 206 ? -19.398 51.169  -6.419  1.00 57.16  ? 235 ASP C OD1 1 
ATOM   11889 O OD2 . ASP D 1 206 ? -18.077 50.371  -7.992  1.00 47.62  ? 235 ASP C OD2 1 
ATOM   11890 N N   . TRP D 1 207 ? -19.172 46.850  -8.420  1.00 35.63  ? 236 TRP C N   1 
ATOM   11891 C CA  . TRP D 1 207 ? -18.182 45.806  -8.675  1.00 35.26  ? 236 TRP C CA  1 
ATOM   11892 C C   . TRP D 1 207 ? -16.776 46.273  -8.265  1.00 31.35  ? 236 TRP C C   1 
ATOM   11893 O O   . TRP D 1 207 ? -16.062 45.569  -7.562  1.00 28.60  ? 236 TRP C O   1 
ATOM   11894 C CB  . TRP D 1 207 ? -18.297 45.475  -10.172 1.00 33.35  ? 236 TRP C CB  1 
ATOM   11895 C CG  . TRP D 1 207 ? -17.506 44.347  -10.752 1.00 29.14  ? 236 TRP C CG  1 
ATOM   11896 C CD1 . TRP D 1 207 ? -17.749 43.015  -10.618 1.00 33.69  ? 236 TRP C CD1 1 
ATOM   11897 C CD2 . TRP D 1 207 ? -16.458 44.461  -11.742 1.00 29.93  ? 236 TRP C CD2 1 
ATOM   11898 N NE1 . TRP D 1 207 ? -16.890 42.282  -11.403 1.00 29.82  ? 236 TRP C NE1 1 
ATOM   11899 C CE2 . TRP D 1 207 ? -16.094 43.144  -12.112 1.00 29.91  ? 236 TRP C CE2 1 
ATOM   11900 C CE3 . TRP D 1 207 ? -15.797 45.533  -12.352 1.00 29.81  ? 236 TRP C CE3 1 
ATOM   11901 C CZ2 . TRP D 1 207 ? -15.108 42.886  -13.057 1.00 29.67  ? 236 TRP C CZ2 1 
ATOM   11902 C CZ3 . TRP D 1 207 ? -14.815 45.275  -13.287 1.00 30.58  ? 236 TRP C CZ3 1 
ATOM   11903 C CH2 . TRP D 1 207 ? -14.492 43.968  -13.653 1.00 29.58  ? 236 TRP C CH2 1 
ATOM   11904 N N   . SER D 1 208 ? -16.365 47.472  -8.684  1.00 27.51  ? 237 SER C N   1 
ATOM   11905 C CA  . SER D 1 208 ? -15.032 47.914  -8.313  1.00 32.57  ? 237 SER C CA  1 
ATOM   11906 C C   . SER D 1 208 ? -14.878 48.051  -6.786  1.00 37.06  ? 237 SER C C   1 
ATOM   11907 O O   . SER D 1 208 ? -13.767 47.959  -6.248  1.00 33.87  ? 237 SER C O   1 
ATOM   11908 C CB  . SER D 1 208 ? -14.687 49.201  -8.968  1.00 34.46  ? 237 SER C CB  1 
ATOM   11909 O OG  . SER D 1 208 ? -15.105 49.242  -10.323 1.00 30.43  ? 237 SER C OG  1 
ATOM   11910 N N   . HIS D 1 209 ? -15.984 48.302  -6.077  1.00 40.13  ? 238 HIS C N   1 
ATOM   11911 C CA  . HIS D 1 209 ? -15.941 48.611  -4.661  1.00 42.34  ? 238 HIS C CA  1 
ATOM   11912 C C   . HIS D 1 209 ? -15.835 47.297  -3.896  1.00 37.00  ? 238 HIS C C   1 
ATOM   11913 O O   . HIS D 1 209 ? -15.023 47.152  -2.982  1.00 33.71  ? 238 HIS C O   1 
ATOM   11914 C CB  . HIS D 1 209 ? -17.192 49.400  -4.220  1.00 45.99  ? 238 HIS C CB  1 
ATOM   11915 C CG  . HIS D 1 209 ? -17.078 50.030  -2.873  1.00 55.30  ? 238 HIS C CG  1 
ATOM   11916 N ND1 . HIS D 1 209 ? -17.769 51.184  -2.558  1.00 62.21  ? 238 HIS C ND1 1 
ATOM   11917 C CD2 . HIS D 1 209 ? -16.359 49.716  -1.773  1.00 57.26  ? 238 HIS C CD2 1 
ATOM   11918 C CE1 . HIS D 1 209 ? -17.466 51.552  -1.318  1.00 59.01  ? 238 HIS C CE1 1 
ATOM   11919 N NE2 . HIS D 1 209 ? -16.611 50.677  -0.820  1.00 59.80  ? 238 HIS C NE2 1 
ATOM   11920 N N   . ASN D 1 210 ? -16.691 46.341  -4.228  1.00 35.26  ? 239 ASN C N   1 
ATOM   11921 C CA  . ASN D 1 210 ? -16.487 45.016  -3.673  1.00 38.77  ? 239 ASN C CA  1 
ATOM   11922 C C   . ASN D 1 210 ? -15.053 44.568  -3.980  1.00 38.72  ? 239 ASN C C   1 
ATOM   11923 O O   . ASN D 1 210 ? -14.407 43.921  -3.160  1.00 41.94  ? 239 ASN C O   1 
ATOM   11924 C CB  . ASN D 1 210 ? -17.464 43.978  -4.211  1.00 42.48  ? 239 ASN C CB  1 
ATOM   11925 C CG  . ASN D 1 210 ? -18.824 44.048  -3.563  1.00 45.43  ? 239 ASN C CG  1 
ATOM   11926 O OD1 . ASN D 1 210 ? -18.914 44.196  -2.346  1.00 49.80  ? 239 ASN C OD1 1 
ATOM   11927 N ND2 . ASN D 1 210 ? -19.889 43.904  -4.342  1.00 47.90  ? 239 ASN C ND2 1 
ATOM   11928 N N   . PHE D 1 211 ? -14.545 44.860  -5.179  1.00 35.49  ? 240 PHE C N   1 
ATOM   11929 C CA  . PHE D 1 211 ? -13.182 44.439  -5.490  1.00 38.15  ? 240 PHE C CA  1 
ATOM   11930 C C   . PHE D 1 211 ? -12.183 45.067  -4.497  1.00 33.25  ? 240 PHE C C   1 
ATOM   11931 O O   . PHE D 1 211 ? -11.390 44.349  -3.921  1.00 31.88  ? 240 PHE C O   1 
ATOM   11932 C CB  . PHE D 1 211 ? -12.867 44.698  -6.969  1.00 34.12  ? 240 PHE C CB  1 
ATOM   11933 C CG  . PHE D 1 211 ? -11.521 44.166  -7.439  1.00 30.55  ? 240 PHE C CG  1 
ATOM   11934 C CD1 . PHE D 1 211 ? -10.875 43.133  -6.768  1.00 26.45  ? 240 PHE C CD1 1 
ATOM   11935 C CD2 . PHE D 1 211 ? -10.893 44.742  -8.525  1.00 28.98  ? 240 PHE C CD2 1 
ATOM   11936 C CE1 . PHE D 1 211 ? -9.664  42.660  -7.201  1.00 26.09  ? 240 PHE C CE1 1 
ATOM   11937 C CE2 . PHE D 1 211 ? -9.659  44.267  -8.947  1.00 31.18  ? 240 PHE C CE2 1 
ATOM   11938 C CZ  . PHE D 1 211 ? -9.039  43.250  -8.264  1.00 28.59  ? 240 PHE C CZ  1 
ATOM   11939 N N   . THR D 1 212 ? -12.179 46.391  -4.292  1.00 36.33  ? 241 THR C N   1 
ATOM   11940 C CA  . THR D 1 212 ? -11.193 47.001  -3.401  1.00 38.35  ? 241 THR C CA  1 
ATOM   11941 C C   . THR D 1 212 ? -11.395 46.544  -1.949  1.00 42.32  ? 241 THR C C   1 
ATOM   11942 O O   . THR D 1 212 ? -10.427 46.380  -1.215  1.00 40.85  ? 241 THR C O   1 
ATOM   11943 C CB  . THR D 1 212 ? -11.166 48.528  -3.511  1.00 37.85  ? 241 THR C CB  1 
ATOM   11944 O OG1 . THR D 1 212 ? -12.473 49.003  -3.244  1.00 37.77  ? 241 THR C OG1 1 
ATOM   11945 C CG2 . THR D 1 212 ? -10.723 48.995  -4.885  1.00 37.73  ? 241 THR C CG2 1 
ATOM   11946 N N   . ASN D 1 213 ? -12.650 46.339  -1.540  1.00 41.23  ? 242 ASN C N   1 
ATOM   11947 C CA  . ASN D 1 213 ? -12.968 45.677  -0.286  1.00 45.38  ? 242 ASN C CA  1 
ATOM   11948 C C   . ASN D 1 213 ? -12.156 44.409  -0.130  1.00 40.99  ? 242 ASN C C   1 
ATOM   11949 O O   . ASN D 1 213 ? -11.423 44.290  0.841   1.00 47.52  ? 242 ASN C O   1 
ATOM   11950 C CB  . ASN D 1 213 ? -14.427 45.245  -0.146  1.00 44.29  ? 242 ASN C CB  1 
ATOM   11951 C CG  . ASN D 1 213 ? -15.261 46.268  0.577   1.00 48.31  ? 242 ASN C CG  1 
ATOM   11952 O OD1 . ASN D 1 213 ? -14.797 47.384  0.787   1.00 42.28  ? 242 ASN C OD1 1 
ATOM   11953 N ND2 . ASN D 1 213 ? -16.497 45.924  0.917   1.00 54.98  ? 242 ASN C ND2 1 
ATOM   11954 N N   . MET D 1 214 ? -12.333 43.463  -1.060  1.00 40.06  ? 243 MET C N   1 
ATOM   11955 C CA  . MET D 1 214 ? -11.765 42.126  -0.924  1.00 39.75  ? 243 MET C CA  1 
ATOM   11956 C C   . MET D 1 214 ? -10.240 42.142  -0.968  1.00 33.09  ? 243 MET C C   1 
ATOM   11957 O O   . MET D 1 214 ? -9.619  41.221  -0.461  1.00 39.04  ? 243 MET C O   1 
ATOM   11958 C CB  . MET D 1 214 ? -12.283 41.179  -2.011  1.00 38.70  ? 243 MET C CB  1 
ATOM   11959 C CG  . MET D 1 214 ? -13.746 40.887  -1.842  1.00 38.69  ? 243 MET C CG  1 
ATOM   11960 S SD  . MET D 1 214 ? -14.433 39.755  -3.058  1.00 40.08  ? 243 MET C SD  1 
ATOM   11961 C CE  . MET D 1 214 ? -14.582 40.824  -4.494  1.00 33.91  ? 243 MET C CE  1 
ATOM   11962 N N   . LEU D 1 215 ? -9.655  43.136  -1.642  1.00 34.38  ? 244 LEU C N   1 
ATOM   11963 C CA  . LEU D 1 215 ? -8.215  43.368  -1.662  1.00 36.72  ? 244 LEU C CA  1 
ATOM   11964 C C   . LEU D 1 215 ? -7.717  43.867  -0.301  1.00 42.77  ? 244 LEU C C   1 
ATOM   11965 O O   . LEU D 1 215 ? -6.515  43.863  -0.073  1.00 42.83  ? 244 LEU C O   1 
ATOM   11966 C CB  . LEU D 1 215 ? -7.869  44.399  -2.741  1.00 32.38  ? 244 LEU C CB  1 
ATOM   11967 C CG  . LEU D 1 215 ? -7.951  43.938  -4.199  1.00 32.82  ? 244 LEU C CG  1 
ATOM   11968 C CD1 . LEU D 1 215 ? -7.658  45.104  -5.109  1.00 35.86  ? 244 LEU C CD1 1 
ATOM   11969 C CD2 . LEU D 1 215 ? -6.972  42.828  -4.497  1.00 34.32  ? 244 LEU C CD2 1 
ATOM   11970 N N   . GLY D 1 216 ? -8.623  44.379  0.555   1.00 47.29  ? 245 GLY C N   1 
ATOM   11971 C CA  . GLY D 1 216 ? -8.270  44.911  1.865   1.00 42.88  ? 245 GLY C CA  1 
ATOM   11972 C C   . GLY D 1 216 ? -8.032  46.418  1.850   1.00 39.41  ? 245 GLY C C   1 
ATOM   11973 O O   . GLY D 1 216 ? -7.446  46.972  2.773   1.00 40.61  ? 245 GLY C O   1 
ATOM   11974 N N   . TYR D 1 217 ? -8.461  47.110  0.796   1.00 39.46  ? 246 TYR C N   1 
ATOM   11975 C CA  . TYR D 1 217 ? -8.320  48.554  0.779   1.00 42.60  ? 246 TYR C CA  1 
ATOM   11976 C C   . TYR D 1 217 ? -9.609  49.148  1.361   1.00 47.24  ? 246 TYR C C   1 
ATOM   11977 O O   . TYR D 1 217 ? -10.602 48.436  1.537   1.00 49.78  ? 246 TYR C O   1 
ATOM   11978 C CB  . TYR D 1 217 ? -7.907  49.008  -0.625  1.00 41.86  ? 246 TYR C CB  1 
ATOM   11979 C CG  . TYR D 1 217 ? -6.496  48.585  -1.015  1.00 37.95  ? 246 TYR C CG  1 
ATOM   11980 C CD1 . TYR D 1 217 ? -6.203  47.264  -1.343  1.00 36.24  ? 246 TYR C CD1 1 
ATOM   11981 C CD2 . TYR D 1 217 ? -5.453  49.502  -1.050  1.00 35.88  ? 246 TYR C CD2 1 
ATOM   11982 C CE1 . TYR D 1 217 ? -4.921  46.868  -1.697  1.00 31.84  ? 246 TYR C CE1 1 
ATOM   11983 C CE2 . TYR D 1 217 ? -4.169  49.123  -1.412  1.00 37.47  ? 246 TYR C CE2 1 
ATOM   11984 C CZ  . TYR D 1 217 ? -3.909  47.803  -1.741  1.00 33.17  ? 246 TYR C CZ  1 
ATOM   11985 O OH  . TYR D 1 217 ? -2.647  47.436  -2.059  1.00 38.93  ? 246 TYR C OH  1 
ATOM   11986 N N   . THR D 1 218 ? -9.513  50.423  1.757   1.00 48.31  ? 247 THR C N   1 
ATOM   11987 C CA  . THR D 1 218 ? -10.564 51.184  2.416   1.00 53.38  ? 247 THR C CA  1 
ATOM   11988 C C   . THR D 1 218 ? -10.212 52.654  2.219   1.00 53.21  ? 247 THR C C   1 
ATOM   11989 O O   . THR D 1 218 ? -9.817  53.344  3.165   1.00 54.63  ? 247 THR C O   1 
ATOM   11990 C CB  . THR D 1 218 ? -10.659 50.847  3.909   1.00 65.23  ? 247 THR C CB  1 
ATOM   11991 O OG1 . THR D 1 218 ? -9.349  50.995  4.455   1.00 65.06  ? 247 THR C OG1 1 
ATOM   11992 C CG2 . THR D 1 218 ? -11.213 49.456  4.169   1.00 65.38  ? 247 THR C CG2 1 
ATOM   11993 N N   . ASP D 1 219 ? -10.324 53.091  0.964   1.00 39.71  ? 248 ASP C N   1 
ATOM   11994 C CA  . ASP D 1 219 ? -9.783  54.353  0.518   1.00 38.85  ? 248 ASP C CA  1 
ATOM   11995 C C   . ASP D 1 219 ? -10.582 54.770  -0.711  1.00 44.05  ? 248 ASP C C   1 
ATOM   11996 O O   . ASP D 1 219 ? -10.511 54.154  -1.773  1.00 37.81  ? 248 ASP C O   1 
ATOM   11997 C CB  . ASP D 1 219 ? -8.273  54.248  0.342   1.00 39.09  ? 248 ASP C CB  1 
ATOM   11998 C CG  . ASP D 1 219 ? -7.612  55.437  -0.334  1.00 40.55  ? 248 ASP C CG  1 
ATOM   11999 O OD1 . ASP D 1 219 ? -8.344  56.288  -0.848  1.00 45.38  ? 248 ASP C OD1 1 
ATOM   12000 O OD2 . ASP D 1 219 ? -6.369  55.526  -0.323  1.00 49.46  ? 248 ASP C OD2 1 
ATOM   12001 N N   . HIS D 1 220 ? -11.363 55.829  -0.554  1.00 40.60  ? 249 HIS C N   1 
ATOM   12002 C CA  . HIS D 1 220 ? -12.327 56.200  -1.565  1.00 41.53  ? 249 HIS C CA  1 
ATOM   12003 C C   . HIS D 1 220 ? -11.617 56.566  -2.863  1.00 39.85  ? 249 HIS C C   1 
ATOM   12004 O O   . HIS D 1 220 ? -12.132 56.235  -3.931  1.00 39.13  ? 249 HIS C O   1 
ATOM   12005 C CB  . HIS D 1 220 ? -13.205 57.343  -1.041  1.00 44.78  ? 249 HIS C CB  1 
ATOM   12006 C CG  . HIS D 1 220 ? -14.123 57.902  -2.064  1.00 40.33  ? 249 HIS C CG  1 
ATOM   12007 N ND1 . HIS D 1 220 ? -13.894 59.106  -2.699  1.00 42.31  ? 249 HIS C ND1 1 
ATOM   12008 C CD2 . HIS D 1 220 ? -15.265 57.436  -2.537  1.00 41.72  ? 249 HIS C CD2 1 
ATOM   12009 C CE1 . HIS D 1 220 ? -14.895 59.352  -3.521  1.00 41.93  ? 249 HIS C CE1 1 
ATOM   12010 N NE2 . HIS D 1 220 ? -15.726 58.345  -3.452  1.00 36.30  ? 249 HIS C NE2 1 
ATOM   12011 N N   . GLN D 1 221 ? -10.490 57.297  -2.765  1.00 36.01  ? 250 GLN C N   1 
ATOM   12012 C CA  . GLN D 1 221 ? -9.780  57.772  -3.949  1.00 45.32  ? 250 GLN C CA  1 
ATOM   12013 C C   . GLN D 1 221 ? -9.245  56.565  -4.732  1.00 39.32  ? 250 GLN C C   1 
ATOM   12014 O O   . GLN D 1 221 ? -9.082  56.633  -5.944  1.00 35.25  ? 250 GLN C O   1 
ATOM   12015 C CB  . GLN D 1 221 ? -8.579  58.676  -3.647  1.00 50.26  ? 250 GLN C CB  1 
ATOM   12016 C CG  . GLN D 1 221 ? -8.852  60.175  -3.739  1.00 63.40  ? 250 GLN C CG  1 
ATOM   12017 C CD  . GLN D 1 221 ? -7.657  61.052  -3.403  1.00 74.26  ? 250 GLN C CD  1 
ATOM   12018 O OE1 . GLN D 1 221 ? -7.755  62.288  -3.338  1.00 67.12  ? 250 GLN C OE1 1 
ATOM   12019 N NE2 . GLN D 1 221 ? -6.503  60.428  -3.200  1.00 71.99  ? 250 GLN C NE2 1 
ATOM   12020 N N   . PHE D 1 222 ? -8.930  55.502  -3.995  1.00 31.02  ? 251 PHE C N   1 
ATOM   12021 C CA  . PHE D 1 222 ? -8.356  54.297  -4.555  1.00 36.12  ? 251 PHE C CA  1 
ATOM   12022 C C   . PHE D 1 222 ? -9.450  53.592  -5.345  1.00 37.16  ? 251 PHE C C   1 
ATOM   12023 O O   . PHE D 1 222 ? -9.228  53.205  -6.489  1.00 35.39  ? 251 PHE C O   1 
ATOM   12024 C CB  . PHE D 1 222 ? -7.791  53.321  -3.518  1.00 34.36  ? 251 PHE C CB  1 
ATOM   12025 C CG  . PHE D 1 222 ? -7.193  52.078  -4.157  1.00 36.64  ? 251 PHE C CG  1 
ATOM   12026 C CD1 . PHE D 1 222 ? -6.210  52.188  -5.131  1.00 39.48  ? 251 PHE C CD1 1 
ATOM   12027 C CD2 . PHE D 1 222 ? -7.648  50.807  -3.824  1.00 33.45  ? 251 PHE C CD2 1 
ATOM   12028 C CE1 . PHE D 1 222 ? -5.660  51.055  -5.706  1.00 40.42  ? 251 PHE C CE1 1 
ATOM   12029 C CE2 . PHE D 1 222 ? -7.104  49.686  -4.422  1.00 34.55  ? 251 PHE C CE2 1 
ATOM   12030 C CZ  . PHE D 1 222 ? -6.116  49.802  -5.348  1.00 33.74  ? 251 PHE C CZ  1 
ATOM   12031 N N   . THR D 1 223 ? -10.627 53.422  -4.735  1.00 33.81  ? 252 THR C N   1 
ATOM   12032 C CA  . THR D 1 223 ? -11.767 52.869  -5.455  1.00 34.90  ? 252 THR C CA  1 
ATOM   12033 C C   . THR D 1 223 ? -12.108 53.701  -6.701  1.00 34.72  ? 252 THR C C   1 
ATOM   12034 O O   . THR D 1 223 ? -12.457 53.158  -7.751  1.00 36.83  ? 252 THR C O   1 
ATOM   12035 C CB  . THR D 1 223 ? -12.938 52.734  -4.495  1.00 34.87  ? 252 THR C CB  1 
ATOM   12036 O OG1 . THR D 1 223 ? -12.450 51.838  -3.501  1.00 31.65  ? 252 THR C OG1 1 
ATOM   12037 C CG2 . THR D 1 223 ? -14.165 52.170  -5.178  1.00 33.70  ? 252 THR C CG2 1 
ATOM   12038 N N   . GLU D 1 224 ? -12.023 55.022  -6.602  1.00 32.97  ? 253 GLU C N   1 
ATOM   12039 C CA  . GLU D 1 224 ? -12.262 55.878  -7.744  1.00 34.85  ? 253 GLU C CA  1 
ATOM   12040 C C   . GLU D 1 224 ? -11.258 55.552  -8.843  1.00 34.83  ? 253 GLU C C   1 
ATOM   12041 O O   . GLU D 1 224 ? -11.626 55.509  -10.013 1.00 32.06  ? 253 GLU C O   1 
ATOM   12042 C CB  . GLU D 1 224 ? -12.240 57.341  -7.296  1.00 35.20  ? 253 GLU C CB  1 
ATOM   12043 C CG  . GLU D 1 224 ? -13.517 57.695  -6.533  1.00 39.37  ? 253 GLU C CG  1 
ATOM   12044 C CD  . GLU D 1 224 ? -14.700 57.724  -7.484  1.00 43.42  ? 253 GLU C CD  1 
ATOM   12045 O OE1 . GLU D 1 224 ? -14.737 58.644  -8.333  1.00 39.11  ? 253 GLU C OE1 1 
ATOM   12046 O OE2 . GLU D 1 224 ? -15.544 56.800  -7.432  1.00 42.27  ? 253 GLU C OE2 1 
ATOM   12047 N N   . LEU D 1 225 ? -9.991  55.359  -8.470  1.00 32.64  ? 254 LEU C N   1 
ATOM   12048 C CA  . LEU D 1 225 ? -8.969  55.023  -9.444  1.00 34.08  ? 254 LEU C CA  1 
ATOM   12049 C C   . LEU D 1 225 ? -9.290  53.689  -10.126 1.00 30.52  ? 254 LEU C C   1 
ATOM   12050 O O   . LEU D 1 225 ? -9.209  53.576  -11.333 1.00 31.95  ? 254 LEU C O   1 
ATOM   12051 C CB  . LEU D 1 225 ? -7.611  54.976  -8.753  1.00 35.37  ? 254 LEU C CB  1 
ATOM   12052 C CG  . LEU D 1 225 ? -6.490  54.472  -9.662  1.00 31.22  ? 254 LEU C CG  1 
ATOM   12053 C CD1 . LEU D 1 225 ? -6.247  55.444  -10.833 1.00 31.65  ? 254 LEU C CD1 1 
ATOM   12054 C CD2 . LEU D 1 225 ? -5.265  54.269  -8.829  1.00 36.29  ? 254 LEU C CD2 1 
ATOM   12055 N N   . THR D 1 226 ? -9.668  52.690  -9.327  1.00 28.74  ? 255 THR C N   1 
ATOM   12056 C CA  . THR D 1 226 ? -9.991  51.356  -9.776  1.00 33.88  ? 255 THR C CA  1 
ATOM   12057 C C   . THR D 1 226 ? -11.124 51.405  -10.807 1.00 37.18  ? 255 THR C C   1 
ATOM   12058 O O   . THR D 1 226 ? -11.035 50.772  -11.870 1.00 32.10  ? 255 THR C O   1 
ATOM   12059 C CB  . THR D 1 226 ? -10.359 50.522  -8.549  1.00 30.95  ? 255 THR C CB  1 
ATOM   12060 O OG1 . THR D 1 226 ? -9.214  50.370  -7.729  1.00 30.25  ? 255 THR C OG1 1 
ATOM   12061 C CG2 . THR D 1 226 ? -10.808 49.123  -8.906  1.00 37.15  ? 255 THR C CG2 1 
ATOM   12062 N N   . ARG D 1 227 ? -12.187 52.149  -10.467 1.00 28.14  ? 256 ARG C N   1 
ATOM   12063 C CA  . ARG D 1 227 ? -13.321 52.334  -11.338 1.00 27.48  ? 256 ARG C CA  1 
ATOM   12064 C C   . ARG D 1 227 ? -12.825 52.886  -12.661 1.00 30.53  ? 256 ARG C C   1 
ATOM   12065 O O   . ARG D 1 227 ? -13.217 52.384  -13.709 1.00 34.11  ? 256 ARG C O   1 
ATOM   12066 C CB  . ARG D 1 227 ? -14.383 53.281  -10.771 1.00 29.26  ? 256 ARG C CB  1 
ATOM   12067 C CG  . ARG D 1 227 ? -15.182 52.663  -9.640  1.00 31.09  ? 256 ARG C CG  1 
ATOM   12068 C CD  . ARG D 1 227 ? -15.954 53.731  -8.889  1.00 35.16  ? 256 ARG C CD  1 
ATOM   12069 N NE  . ARG D 1 227 ? -16.700 53.129  -7.787  1.00 37.09  ? 256 ARG C NE  1 
ATOM   12070 C CZ  . ARG D 1 227 ? -16.869 53.700  -6.601  1.00 39.51  ? 256 ARG C CZ  1 
ATOM   12071 N NH1 . ARG D 1 227 ? -16.325 54.876  -6.362  1.00 38.35  ? 256 ARG C NH1 1 
ATOM   12072 N NH2 . ARG D 1 227 ? -17.591 53.101  -5.665  1.00 41.51  ? 256 ARG C NH2 1 
ATOM   12073 N N   . LEU D 1 228 ? -11.943 53.882  -12.604 1.00 29.25  ? 257 LEU C N   1 
ATOM   12074 C CA  . LEU D 1 228 ? -11.440 54.458  -13.834 1.00 32.57  ? 257 LEU C CA  1 
ATOM   12075 C C   . LEU D 1 228 ? -10.541 53.441  -14.548 1.00 35.13  ? 257 LEU C C   1 
ATOM   12076 O O   . LEU D 1 228 ? -10.609 53.349  -15.767 1.00 36.59  ? 257 LEU C O   1 
ATOM   12077 C CB  . LEU D 1 228 ? -10.705 55.768  -13.568 1.00 32.34  ? 257 LEU C CB  1 
ATOM   12078 C CG  . LEU D 1 228 ? -10.050 56.412  -14.791 1.00 33.65  ? 257 LEU C CG  1 
ATOM   12079 C CD1 . LEU D 1 228 ? -11.167 56.870  -15.699 1.00 37.53  ? 257 LEU C CD1 1 
ATOM   12080 C CD2 . LEU D 1 228 ? -9.059  57.533  -14.486 1.00 36.67  ? 257 LEU C CD2 1 
ATOM   12081 N N   . TYR D 1 229 ? -9.691  52.739  -13.785 1.00 30.89  ? 258 TYR C N   1 
ATOM   12082 C CA  . TYR D 1 229 ? -8.668  51.846  -14.313 1.00 32.55  ? 258 TYR C CA  1 
ATOM   12083 C C   . TYR D 1 229 ? -9.351  50.710  -15.061 1.00 28.75  ? 258 TYR C C   1 
ATOM   12084 O O   . TYR D 1 229 ? -8.972  50.348  -16.165 1.00 27.35  ? 258 TYR C O   1 
ATOM   12085 C CB  . TYR D 1 229 ? -7.811  51.308  -13.156 1.00 34.05  ? 258 TYR C CB  1 
ATOM   12086 C CG  . TYR D 1 229 ? -6.722  50.345  -13.592 1.00 32.34  ? 258 TYR C CG  1 
ATOM   12087 C CD1 . TYR D 1 229 ? -7.017  49.038  -13.921 1.00 38.21  ? 258 TYR C CD1 1 
ATOM   12088 C CD2 . TYR D 1 229 ? -5.405  50.737  -13.671 1.00 39.28  ? 258 TYR C CD2 1 
ATOM   12089 C CE1 . TYR D 1 229 ? -6.043  48.165  -14.374 1.00 39.66  ? 258 TYR C CE1 1 
ATOM   12090 C CE2 . TYR D 1 229 ? -4.414  49.866  -14.089 1.00 40.45  ? 258 TYR C CE2 1 
ATOM   12091 C CZ  . TYR D 1 229 ? -4.733  48.579  -14.462 1.00 42.74  ? 258 TYR C CZ  1 
ATOM   12092 O OH  . TYR D 1 229 ? -3.748  47.720  -14.874 1.00 51.21  ? 258 TYR C OH  1 
ATOM   12093 N N   . LEU D 1 230 ? -10.387 50.169  -14.425 1.00 28.92  ? 259 LEU C N   1 
ATOM   12094 C CA  . LEU D 1 230 ? -11.117 49.047  -14.943 1.00 26.96  ? 259 LEU C CA  1 
ATOM   12095 C C   . LEU D 1 230 ? -11.932 49.472  -16.144 1.00 28.27  ? 259 LEU C C   1 
ATOM   12096 O O   . LEU D 1 230 ? -12.153 48.643  -17.004 1.00 28.48  ? 259 LEU C O   1 
ATOM   12097 C CB  . LEU D 1 230 ? -11.987 48.362  -13.896 1.00 28.81  ? 259 LEU C CB  1 
ATOM   12098 C CG  . LEU D 1 230 ? -11.201 47.655  -12.787 1.00 29.46  ? 259 LEU C CG  1 
ATOM   12099 C CD1 . LEU D 1 230 ? -12.171 47.128  -11.790 1.00 28.21  ? 259 LEU C CD1 1 
ATOM   12100 C CD2 . LEU D 1 230 ? -10.273 46.531  -13.295 1.00 35.03  ? 259 LEU C CD2 1 
ATOM   12101 N N   . THR D 1 231 ? -12.388 50.724  -16.209 1.00 26.55  ? 260 THR C N   1 
ATOM   12102 C CA  . THR D 1 231 ? -13.123 51.187  -17.370 1.00 25.94  ? 260 THR C CA  1 
ATOM   12103 C C   . THR D 1 231 ? -12.173 51.269  -18.549 1.00 25.92  ? 260 THR C C   1 
ATOM   12104 O O   . THR D 1 231 ? -12.503 50.813  -19.631 1.00 30.59  ? 260 THR C O   1 
ATOM   12105 C CB  . THR D 1 231 ? -13.823 52.524  -17.102 1.00 26.67  ? 260 THR C CB  1 
ATOM   12106 O OG1 . THR D 1 231 ? -14.869 52.262  -16.176 1.00 25.34  ? 260 THR C OG1 1 
ATOM   12107 C CG2 . THR D 1 231 ? -14.464 53.100  -18.345 1.00 26.33  ? 260 THR C CG2 1 
ATOM   12108 N N   . ILE D 1 232 ? -10.981 51.821  -18.340 1.00 28.42  ? 261 ILE C N   1 
ATOM   12109 C CA  . ILE D 1 232 ? -10.219 52.280  -19.494 1.00 29.05  ? 261 ILE C CA  1 
ATOM   12110 C C   . ILE D 1 232 ? -9.345  51.170  -20.060 1.00 27.03  ? 261 ILE C C   1 
ATOM   12111 O O   . ILE D 1 232 ? -8.854  51.332  -21.158 1.00 29.93  ? 261 ILE C O   1 
ATOM   12112 C CB  . ILE D 1 232 ? -9.375  53.521  -19.168 1.00 31.81  ? 261 ILE C CB  1 
ATOM   12113 C CG1 . ILE D 1 232 ? -8.339  53.229  -18.107 1.00 32.61  ? 261 ILE C CG1 1 
ATOM   12114 C CG2 . ILE D 1 232 ? -10.271 54.701  -18.784 1.00 33.95  ? 261 ILE C CG2 1 
ATOM   12115 C CD1 . ILE D 1 232 ? -7.239  54.267  -18.038 1.00 39.39  ? 261 ILE C CD1 1 
ATOM   12116 N N   . HIS D 1 233 ? -9.095  50.085  -19.313 1.00 25.56  ? 262 HIS C N   1 
ATOM   12117 C CA  . HIS D 1 233 ? -8.311  49.006  -19.888 1.00 28.85  ? 262 HIS C CA  1 
ATOM   12118 C C   . HIS D 1 233 ? -9.215  47.935  -20.492 1.00 25.82  ? 262 HIS C C   1 
ATOM   12119 O O   . HIS D 1 233 ? -8.707  46.892  -20.873 1.00 24.26  ? 262 HIS C O   1 
ATOM   12120 C CB  . HIS D 1 233 ? -7.398  48.334  -18.864 1.00 33.36  ? 262 HIS C CB  1 
ATOM   12121 C CG  . HIS D 1 233 ? -6.279  49.161  -18.361 1.00 36.13  ? 262 HIS C CG  1 
ATOM   12122 N ND1 . HIS D 1 233 ? -6.490  50.221  -17.508 1.00 31.17  ? 262 HIS C ND1 1 
ATOM   12123 C CD2 . HIS D 1 233 ? -4.951  49.051  -18.526 1.00 36.20  ? 262 HIS C CD2 1 
ATOM   12124 C CE1 . HIS D 1 233 ? -5.309  50.751  -17.213 1.00 40.45  ? 262 HIS C CE1 1 
ATOM   12125 N NE2 . HIS D 1 233 ? -4.366  50.036  -17.790 1.00 37.11  ? 262 HIS C NE2 1 
ATOM   12126 N N   . SER D 1 234 ? -10.528 48.200  -20.580 1.00 26.90  ? 263 SER C N   1 
ATOM   12127 C CA  . SER D 1 234 ? -11.540 47.184  -20.790 1.00 25.96  ? 263 SER C CA  1 
ATOM   12128 C C   . SER D 1 234 ? -11.404 46.541  -22.171 1.00 27.02  ? 263 SER C C   1 
ATOM   12129 O O   . SER D 1 234 ? -11.626 45.346  -22.302 1.00 27.30  ? 263 SER C O   1 
ATOM   12130 C CB  . SER D 1 234 ? -12.915 47.785  -20.597 1.00 28.46  ? 263 SER C CB  1 
ATOM   12131 O OG  . SER D 1 234 ? -13.108 48.893  -21.477 1.00 33.73  ? 263 SER C OG  1 
ATOM   12132 N N   . ASP D 1 235 ? -11.038 47.350  -23.185 1.00 28.21  ? 264 ASP C N   1 
ATOM   12133 C CA  . ASP D 1 235 ? -11.041 46.938  -24.578 1.00 31.17  ? 264 ASP C CA  1 
ATOM   12134 C C   . ASP D 1 235 ? -10.115 47.859  -25.381 1.00 32.01  ? 264 ASP C C   1 
ATOM   12135 O O   . ASP D 1 235 ? -9.999  49.047  -25.110 1.00 33.53  ? 264 ASP C O   1 
ATOM   12136 C CB  . ASP D 1 235 ? -12.467 46.903  -25.117 1.00 31.44  ? 264 ASP C CB  1 
ATOM   12137 C CG  . ASP D 1 235 ? -12.766 45.891  -26.219 1.00 32.96  ? 264 ASP C CG  1 
ATOM   12138 O OD1 . ASP D 1 235 ? -12.303 44.714  -26.119 1.00 31.84  ? 264 ASP C OD1 1 
ATOM   12139 O OD2 . ASP D 1 235 ? -13.501 46.265  -27.161 1.00 42.14  ? 264 ASP C OD2 1 
ATOM   12140 N N   . HIS D 1 236 ? -9.444  47.285  -26.364 1.00 27.50  ? 265 HIS C N   1 
ATOM   12141 C CA  . HIS D 1 236 ? -8.588  48.046  -27.255 1.00 32.41  ? 265 HIS C CA  1 
ATOM   12142 C C   . HIS D 1 236 ? -8.566  47.407  -28.647 1.00 28.96  ? 265 HIS C C   1 
ATOM   12143 O O   . HIS D 1 236 ? -7.509  47.004  -29.132 1.00 29.81  ? 265 HIS C O   1 
ATOM   12144 C CB  . HIS D 1 236 ? -7.207  48.126  -26.596 1.00 34.98  ? 265 HIS C CB  1 
ATOM   12145 C CG  . HIS D 1 236 ? -6.470  49.348  -26.962 1.00 37.16  ? 265 HIS C CG  1 
ATOM   12146 N ND1 . HIS D 1 236 ? -5.302  49.322  -27.687 1.00 36.35  ? 265 HIS C ND1 1 
ATOM   12147 C CD2 . HIS D 1 236 ? -6.729  50.636  -26.673 1.00 39.33  ? 265 HIS C CD2 1 
ATOM   12148 C CE1 . HIS D 1 236 ? -4.907  50.573  -27.893 1.00 39.93  ? 265 HIS C CE1 1 
ATOM   12149 N NE2 . HIS D 1 236 ? -5.763  51.389  -27.276 1.00 43.64  ? 265 HIS C NE2 1 
ATOM   12150 N N   . GLU D 1 237 ? -9.738  47.252  -29.266 1.00 32.50  ? 266 GLU C N   1 
ATOM   12151 C CA  . GLU D 1 237 ? -9.825  46.581  -30.556 1.00 35.69  ? 266 GLU C CA  1 
ATOM   12152 C C   . GLU D 1 237 ? -9.611  45.078  -30.390 1.00 30.95  ? 266 GLU C C   1 
ATOM   12153 O O   . GLU D 1 237 ? -9.410  44.586  -29.277 1.00 33.12  ? 266 GLU C O   1 
ATOM   12154 C CB  . GLU D 1 237 ? -8.775  47.076  -31.557 1.00 41.97  ? 266 GLU C CB  1 
ATOM   12155 C CG  . GLU D 1 237 ? -9.356  47.945  -32.659 1.00 53.15  ? 266 GLU C CG  1 
ATOM   12156 C CD  . GLU D 1 237 ? -8.429  48.172  -33.841 1.00 59.28  ? 266 GLU C CD  1 
ATOM   12157 O OE1 . GLU D 1 237 ? -7.396  47.461  -34.062 1.00 56.22  ? 266 GLU C OE1 1 
ATOM   12158 O OE2 . GLU D 1 237 ? -8.823  49.121  -34.555 1.00 67.70  ? 266 GLU C OE2 1 
ATOM   12159 N N   . GLY D 1 238 ? -9.665  44.362  -31.519 1.00 29.64  ? 267 GLY C N   1 
ATOM   12160 C CA  . GLY D 1 238 ? -9.594  42.911  -31.501 1.00 29.41  ? 267 GLY C CA  1 
ATOM   12161 C C   . GLY D 1 238 ? -8.209  42.408  -31.881 1.00 32.00  ? 267 GLY C C   1 
ATOM   12162 O O   . GLY D 1 238 ? -7.966  41.210  -31.783 1.00 33.56  ? 267 GLY C O   1 
ATOM   12163 N N   . GLY D 1 239 ? -7.329  43.317  -32.327 1.00 29.79  ? 268 GLY C N   1 
ATOM   12164 C CA  . GLY D 1 239 ? -6.040  42.899  -32.838 1.00 32.08  ? 268 GLY C CA  1 
ATOM   12165 C C   . GLY D 1 239 ? -4.987  42.718  -31.745 1.00 31.27  ? 268 GLY C C   1 
ATOM   12166 O O   . GLY D 1 239 ? -3.938  42.132  -32.004 1.00 29.55  ? 268 GLY C O   1 
ATOM   12167 N N   . ASN D 1 240 ? -5.219  43.268  -30.540 1.00 26.03  ? 269 ASN C N   1 
ATOM   12168 C CA  . ASN D 1 240 ? -4.239  43.112  -29.479 1.00 28.84  ? 269 ASN C CA  1 
ATOM   12169 C C   . ASN D 1 240 ? -4.259  41.633  -29.117 1.00 25.13  ? 269 ASN C C   1 
ATOM   12170 O O   . ASN D 1 240 ? -5.286  40.986  -29.329 1.00 24.82  ? 269 ASN C O   1 
ATOM   12171 C CB  . ASN D 1 240 ? -4.510  44.077  -28.317 1.00 27.20  ? 269 ASN C CB  1 
ATOM   12172 C CG  . ASN D 1 240 ? -5.740  43.687  -27.544 1.00 26.29  ? 269 ASN C CG  1 
ATOM   12173 O OD1 . ASN D 1 240 ? -5.713  42.760  -26.734 1.00 27.31  ? 269 ASN C OD1 1 
ATOM   12174 N ND2 . ASN D 1 240 ? -6.821  44.407  -27.745 1.00 33.40  ? 269 ASN C ND2 1 
ATOM   12175 N N   . VAL D 1 241 ? -3.185  41.156  -28.490 1.00 26.85  ? 270 VAL C N   1 
ATOM   12176 C CA  . VAL D 1 241 ? -2.944  39.734  -28.345 1.00 27.10  ? 270 VAL C CA  1 
ATOM   12177 C C   . VAL D 1 241 ? -3.977  39.118  -27.396 1.00 25.87  ? 270 VAL C C   1 
ATOM   12178 O O   . VAL D 1 241 ? -4.439  38.020  -27.656 1.00 23.51  ? 270 VAL C O   1 
ATOM   12179 C CB  . VAL D 1 241 ? -1.493  39.479  -27.887 1.00 31.05  ? 270 VAL C CB  1 
ATOM   12180 C CG1 . VAL D 1 241 ? -1.256  38.023  -27.474 1.00 29.40  ? 270 VAL C CG1 1 
ATOM   12181 C CG2 . VAL D 1 241 ? -0.504  39.862  -28.976 1.00 35.70  ? 270 VAL C CG2 1 
ATOM   12182 N N   . SER D 1 242 ? -4.412  39.837  -26.353 1.00 24.92  ? 271 SER C N   1 
ATOM   12183 C CA  . SER D 1 242 ? -5.352  39.252  -25.407 1.00 28.77  ? 271 SER C CA  1 
ATOM   12184 C C   . SER D 1 242 ? -6.737  39.132  -26.050 1.00 26.95  ? 271 SER C C   1 
ATOM   12185 O O   . SER D 1 242 ? -7.394  38.110  -25.921 1.00 28.08  ? 271 SER C O   1 
ATOM   12186 C CB  . SER D 1 242 ? -5.372  39.974  -24.069 1.00 29.90  ? 271 SER C CB  1 
ATOM   12187 O OG  . SER D 1 242 ? -5.759  41.336  -24.198 1.00 28.13  ? 271 SER C OG  1 
ATOM   12188 N N   . ALA D 1 243 ? -7.174  40.146  -26.789 1.00 24.53  ? 272 ALA C N   1 
ATOM   12189 C CA  . ALA D 1 243 ? -8.486  40.123  -27.393 1.00 25.21  ? 272 ALA C CA  1 
ATOM   12190 C C   . ALA D 1 243 ? -8.482  39.132  -28.553 1.00 24.36  ? 272 ALA C C   1 
ATOM   12191 O O   . ALA D 1 243 ? -9.441  38.400  -28.756 1.00 22.22  ? 272 ALA C O   1 
ATOM   12192 C CB  . ALA D 1 243 ? -8.911  41.518  -27.816 1.00 23.92  ? 272 ALA C CB  1 
ATOM   12193 N N   . HIS D 1 244 ? -7.385  39.102  -29.300 1.00 25.15  ? 273 HIS C N   1 
ATOM   12194 C CA  . HIS D 1 244 ? -7.317  38.238  -30.461 1.00 24.99  ? 273 HIS C CA  1 
ATOM   12195 C C   . HIS D 1 244 ? -7.315  36.784  -29.996 1.00 22.07  ? 273 HIS C C   1 
ATOM   12196 O O   . HIS D 1 244 ? -7.954  35.921  -30.589 1.00 22.30  ? 273 HIS C O   1 
ATOM   12197 C CB  . HIS D 1 244 ? -6.096  38.615  -31.305 1.00 25.24  ? 273 HIS C CB  1 
ATOM   12198 C CG  . HIS D 1 244 ? -5.979  37.827  -32.565 1.00 24.88  ? 273 HIS C CG  1 
ATOM   12199 N ND1 . HIS D 1 244 ? -4.848  37.884  -33.353 1.00 23.71  ? 273 HIS C ND1 1 
ATOM   12200 C CD2 . HIS D 1 244 ? -6.849  37.040  -33.215 1.00 24.31  ? 273 HIS C CD2 1 
ATOM   12201 C CE1 . HIS D 1 244 ? -5.036  37.114  -34.412 1.00 23.02  ? 273 HIS C CE1 1 
ATOM   12202 N NE2 . HIS D 1 244 ? -6.229  36.563  -34.345 1.00 22.18  ? 273 HIS C NE2 1 
ATOM   12203 N N   . THR D 1 245 ? -6.570  36.520  -28.933 1.00 21.50  ? 274 THR C N   1 
ATOM   12204 C CA  . THR D 1 245 ? -6.475  35.186  -28.361 1.00 21.81  ? 274 THR C CA  1 
ATOM   12205 C C   . THR D 1 245 ? -7.869  34.743  -27.930 1.00 21.10  ? 274 THR C C   1 
ATOM   12206 O O   . THR D 1 245 ? -8.241  33.633  -28.257 1.00 21.36  ? 274 THR C O   1 
ATOM   12207 C CB  . THR D 1 245 ? -5.481  35.116  -27.192 1.00 21.43  ? 274 THR C CB  1 
ATOM   12208 O OG1 . THR D 1 245 ? -4.213  35.412  -27.764 1.00 24.01  ? 274 THR C OG1 1 
ATOM   12209 C CG2 . THR D 1 245 ? -5.443  33.743  -26.525 1.00 20.76  ? 274 THR C CG2 1 
ATOM   12210 N N   . SER D 1 246 ? -8.643  35.607  -27.234 1.00 20.65  ? 275 SER C N   1 
ATOM   12211 C CA  . SER D 1 246 ? -9.980  35.232  -26.787 1.00 22.67  ? 275 SER C CA  1 
ATOM   12212 C C   . SER D 1 246 ? -10.879 34.955  -27.977 1.00 19.76  ? 275 SER C C   1 
ATOM   12213 O O   . SER D 1 246 ? -11.749 34.100  -27.895 1.00 22.90  ? 275 SER C O   1 
ATOM   12214 C CB  . SER D 1 246 ? -10.635 36.282  -25.914 1.00 24.92  ? 275 SER C CB  1 
ATOM   12215 O OG  . SER D 1 246 ? -10.953 37.429  -26.675 1.00 28.47  ? 275 SER C OG  1 
ATOM   12216 N N   . HIS D 1 247 ? -10.690 35.739  -29.051 1.00 19.54  ? 276 HIS C N   1 
ATOM   12217 C CA  . HIS D 1 247 ? -11.496 35.634  -30.241 1.00 23.37  ? 276 HIS C CA  1 
ATOM   12218 C C   . HIS D 1 247 ? -11.200 34.304  -30.949 1.00 25.11  ? 276 HIS C C   1 
ATOM   12219 O O   . HIS D 1 247 ? -12.087 33.668  -31.524 1.00 23.38  ? 276 HIS C O   1 
ATOM   12220 C CB  . HIS D 1 247 ? -11.246 36.887  -31.085 1.00 25.78  ? 276 HIS C CB  1 
ATOM   12221 C CG  . HIS D 1 247 ? -12.026 37.011  -32.315 1.00 26.69  ? 276 HIS C CG  1 
ATOM   12222 N ND1 . HIS D 1 247 ? -13.311 37.486  -32.401 1.00 29.85  ? 276 HIS C ND1 1 
ATOM   12223 C CD2 . HIS D 1 247 ? -11.652 36.673  -33.551 1.00 34.54  ? 276 HIS C CD2 1 
ATOM   12224 C CE1 . HIS D 1 247 ? -13.689 37.456  -33.660 1.00 34.92  ? 276 HIS C CE1 1 
ATOM   12225 N NE2 . HIS D 1 247 ? -12.684 36.956  -34.386 1.00 31.04  ? 276 HIS C NE2 1 
ATOM   12226 N N   . LEU D 1 248 ? -9.926  33.931  -30.956 1.00 22.69  ? 277 LEU C N   1 
ATOM   12227 C CA  . LEU D 1 248 ? -9.473  32.767  -31.691 1.00 20.41  ? 277 LEU C CA  1 
ATOM   12228 C C   . LEU D 1 248 ? -9.916  31.492  -30.958 1.00 22.26  ? 277 LEU C C   1 
ATOM   12229 O O   . LEU D 1 248 ? -10.588 30.640  -31.519 1.00 24.21  ? 277 LEU C O   1 
ATOM   12230 C CB  . LEU D 1 248 ? -7.965  32.959  -31.822 1.00 20.54  ? 277 LEU C CB  1 
ATOM   12231 C CG  . LEU D 1 248 ? -7.167  31.749  -32.314 1.00 23.03  ? 277 LEU C CG  1 
ATOM   12232 C CD1 . LEU D 1 248 ? -7.638  31.375  -33.729 1.00 22.47  ? 277 LEU C CD1 1 
ATOM   12233 C CD2 . LEU D 1 248 ? -5.677  32.045  -32.270 1.00 23.67  ? 277 LEU C CD2 1 
ATOM   12234 N N   . VAL D 1 249 ? -9.665  31.425  -29.663 1.00 21.84  ? 278 VAL C N   1 
ATOM   12235 C CA  . VAL D 1 249 ? -10.060 30.272  -28.869 1.00 20.14  ? 278 VAL C CA  1 
ATOM   12236 C C   . VAL D 1 249 ? -11.571 30.204  -28.881 1.00 23.57  ? 278 VAL C C   1 
ATOM   12237 O O   . VAL D 1 249 ? -12.121 29.153  -29.118 1.00 24.34  ? 278 VAL C O   1 
ATOM   12238 C CB  . VAL D 1 249 ? -9.417  30.408  -27.475 1.00 20.46  ? 278 VAL C CB  1 
ATOM   12239 C CG1 . VAL D 1 249 ? -9.934  29.406  -26.428 1.00 19.59  ? 278 VAL C CG1 1 
ATOM   12240 C CG2 . VAL D 1 249 ? -7.912  30.356  -27.589 1.00 20.97  ? 278 VAL C CG2 1 
ATOM   12241 N N   . GLY D 1 250 ? -12.255 31.349  -28.681 1.00 25.70  ? 279 GLY C N   1 
ATOM   12242 C CA  . GLY D 1 250 ? -13.708 31.344  -28.656 1.00 23.13  ? 279 GLY C CA  1 
ATOM   12243 C C   . GLY D 1 250 ? -14.320 30.894  -29.980 1.00 25.17  ? 279 GLY C C   1 
ATOM   12244 O O   . GLY D 1 250 ? -15.409 30.310  -29.990 1.00 23.30  ? 279 GLY C O   1 
ATOM   12245 N N   . SER D 1 251 ? -13.625 31.153  -31.107 1.00 24.81  ? 280 SER C N   1 
ATOM   12246 C CA  . SER D 1 251 ? -14.140 30.799  -32.420 1.00 26.59  ? 280 SER C CA  1 
ATOM   12247 C C   . SER D 1 251 ? -14.222 29.271  -32.581 1.00 26.90  ? 280 SER C C   1 
ATOM   12248 O O   . SER D 1 251 ? -14.955 28.774  -33.421 1.00 26.31  ? 280 SER C O   1 
ATOM   12249 C CB  . SER D 1 251 ? -13.326 31.437  -33.555 1.00 24.55  ? 280 SER C CB  1 
ATOM   12250 O OG  . SER D 1 251 ? -12.173 30.650  -33.832 1.00 23.11  ? 280 SER C OG  1 
ATOM   12251 N N   . ALA D 1 252 ? -13.521 28.527  -31.720 1.00 28.36  ? 281 ALA C N   1 
ATOM   12252 C CA  . ALA D 1 252 ? -13.566 27.069  -31.675 1.00 26.10  ? 281 ALA C CA  1 
ATOM   12253 C C   . ALA D 1 252 ? -14.734 26.586  -30.821 1.00 28.10  ? 281 ALA C C   1 
ATOM   12254 O O   . ALA D 1 252 ? -14.919 25.387  -30.631 1.00 23.75  ? 281 ALA C O   1 
ATOM   12255 C CB  . ALA D 1 252 ? -12.276 26.585  -31.072 1.00 27.12  ? 281 ALA C CB  1 
ATOM   12256 N N   . LEU D 1 253 ? -15.472 27.549  -30.255 1.00 25.91  ? 282 LEU C N   1 
ATOM   12257 C CA  . LEU D 1 253 ? -16.573 27.328  -29.343 1.00 25.23  ? 282 LEU C CA  1 
ATOM   12258 C C   . LEU D 1 253 ? -16.060 26.809  -28.001 1.00 26.78  ? 282 LEU C C   1 
ATOM   12259 O O   . LEU D 1 253 ? -16.796 26.208  -27.221 1.00 25.75  ? 282 LEU C O   1 
ATOM   12260 C CB  . LEU D 1 253 ? -17.710 26.489  -29.921 1.00 25.83  ? 282 LEU C CB  1 
ATOM   12261 C CG  . LEU D 1 253 ? -18.277 26.955  -31.269 1.00 31.01  ? 282 LEU C CG  1 
ATOM   12262 C CD1 . LEU D 1 253 ? -19.351 25.994  -31.783 1.00 35.84  ? 282 LEU C CD1 1 
ATOM   12263 C CD2 . LEU D 1 253 ? -18.854 28.355  -31.209 1.00 31.60  ? 282 LEU C CD2 1 
ATOM   12264 N N   . SER D 1 254 ? -14.820 27.139  -27.658 1.00 28.10  ? 283 SER C N   1 
ATOM   12265 C CA  . SER D 1 254 ? -14.422 27.011  -26.267 1.00 26.81  ? 283 SER C CA  1 
ATOM   12266 C C   . SER D 1 254 ? -15.206 28.047  -25.470 1.00 29.25  ? 283 SER C C   1 
ATOM   12267 O O   . SER D 1 254 ? -15.442 29.150  -25.962 1.00 32.68  ? 283 SER C O   1 
ATOM   12268 C CB  . SER D 1 254 ? -12.974 27.175  -26.079 1.00 22.74  ? 283 SER C CB  1 
ATOM   12269 O OG  . SER D 1 254 ? -12.298 26.191  -26.836 1.00 25.33  ? 283 SER C OG  1 
ATOM   12270 N N   . ASP D 1 255 ? -15.626 27.672  -24.264 1.00 27.83  ? 284 ASP C N   1 
ATOM   12271 C CA  . ASP D 1 255 ? -16.491 28.523  -23.452 1.00 30.34  ? 284 ASP C CA  1 
ATOM   12272 C C   . ASP D 1 255 ? -15.747 29.767  -22.943 1.00 28.53  ? 284 ASP C C   1 
ATOM   12273 O O   . ASP D 1 255 ? -14.528 29.872  -23.042 1.00 25.33  ? 284 ASP C O   1 
ATOM   12274 C CB  . ASP D 1 255 ? -17.114 27.679  -22.354 1.00 33.19  ? 284 ASP C CB  1 
ATOM   12275 C CG  . ASP D 1 255 ? -16.097 27.242  -21.316 1.00 38.85  ? 284 ASP C CG  1 
ATOM   12276 O OD1 . ASP D 1 255 ? -15.468 28.141  -20.728 1.00 45.87  ? 284 ASP C OD1 1 
ATOM   12277 O OD2 . ASP D 1 255 ? -15.921 26.017  -21.128 1.00 40.74  ? 284 ASP C OD2 1 
ATOM   12278 N N   . PRO D 1 256 ? -16.460 30.762  -22.365 1.00 26.62  ? 285 PRO C N   1 
ATOM   12279 C CA  . PRO D 1 256 ? -15.841 32.002  -21.908 1.00 28.08  ? 285 PRO C CA  1 
ATOM   12280 C C   . PRO D 1 256 ? -14.674 31.821  -20.939 1.00 25.40  ? 285 PRO C C   1 
ATOM   12281 O O   . PRO D 1 256 ? -13.704 32.553  -21.029 1.00 22.26  ? 285 PRO C O   1 
ATOM   12282 C CB  . PRO D 1 256 ? -17.021 32.741  -21.281 1.00 28.05  ? 285 PRO C CB  1 
ATOM   12283 C CG  . PRO D 1 256 ? -18.178 32.212  -22.043 1.00 28.77  ? 285 PRO C CG  1 
ATOM   12284 C CD  . PRO D 1 256 ? -17.902 30.738  -22.101 1.00 29.09  ? 285 PRO C CD  1 
ATOM   12285 N N   . TYR D 1 257 ? -14.745 30.827  -20.049 1.00 22.10  ? 286 TYR C N   1 
ATOM   12286 C CA  . TYR D 1 257 ? -13.663 30.577  -19.114 1.00 23.35  ? 286 TYR C CA  1 
ATOM   12287 C C   . TYR D 1 257 ? -12.358 30.175  -19.834 1.00 24.08  ? 286 TYR C C   1 
ATOM   12288 O O   . TYR D 1 257 ? -11.275 30.689  -19.562 1.00 26.65  ? 286 TYR C O   1 
ATOM   12289 C CB  . TYR D 1 257 ? -14.146 29.491  -18.147 1.00 26.35  ? 286 TYR C CB  1 
ATOM   12290 C CG  . TYR D 1 257 ? -15.335 29.916  -17.284 1.00 27.03  ? 286 TYR C CG  1 
ATOM   12291 C CD1 . TYR D 1 257 ? -15.152 30.609  -16.101 1.00 26.95  ? 286 TYR C CD1 1 
ATOM   12292 C CD2 . TYR D 1 257 ? -16.635 29.576  -17.634 1.00 30.10  ? 286 TYR C CD2 1 
ATOM   12293 C CE1 . TYR D 1 257 ? -16.230 30.974  -15.309 1.00 27.77  ? 286 TYR C CE1 1 
ATOM   12294 C CE2 . TYR D 1 257 ? -17.721 29.911  -16.841 1.00 30.63  ? 286 TYR C CE2 1 
ATOM   12295 C CZ  . TYR D 1 257 ? -17.527 30.630  -15.683 1.00 29.83  ? 286 TYR C CZ  1 
ATOM   12296 O OH  . TYR D 1 257 ? -18.604 31.017  -14.926 1.00 31.12  ? 286 TYR C OH  1 
ATOM   12297 N N   . LEU D 1 258 ? -12.439 29.239  -20.755 1.00 22.81  ? 287 LEU C N   1 
ATOM   12298 C CA  . LEU D 1 258 ? -11.249 28.829  -21.478 1.00 21.72  ? 287 LEU C CA  1 
ATOM   12299 C C   . LEU D 1 258 ? -10.730 29.957  -22.379 1.00 23.56  ? 287 LEU C C   1 
ATOM   12300 O O   . LEU D 1 258 ? -9.523  30.144  -22.503 1.00 25.38  ? 287 LEU C O   1 
ATOM   12301 C CB  . LEU D 1 258 ? -11.609 27.581  -22.282 1.00 21.99  ? 287 LEU C CB  1 
ATOM   12302 C CG  . LEU D 1 258 ? -12.125 26.381  -21.492 1.00 26.02  ? 287 LEU C CG  1 
ATOM   12303 C CD1 . LEU D 1 258 ? -12.468 25.216  -22.408 1.00 29.30  ? 287 LEU C CD1 1 
ATOM   12304 C CD2 . LEU D 1 258 ? -11.121 25.974  -20.454 1.00 23.64  ? 287 LEU C CD2 1 
ATOM   12305 N N   . SER D 1 259 ? -11.634 30.663  -23.076 1.00 26.56  ? 288 SER C N   1 
ATOM   12306 C CA  . SER D 1 259 ? -11.241 31.770  -23.929 1.00 25.83  ? 288 SER C CA  1 
ATOM   12307 C C   . SER D 1 259 ? -10.499 32.853  -23.130 1.00 28.78  ? 288 SER C C   1 
ATOM   12308 O O   . SER D 1 259 ? -9.439  33.341  -23.518 1.00 26.80  ? 288 SER C O   1 
ATOM   12309 C CB  . SER D 1 259 ? -12.459 32.344  -24.640 1.00 28.70  ? 288 SER C CB  1 
ATOM   12310 O OG  . SER D 1 259 ? -13.218 31.292  -25.227 1.00 26.02  ? 288 SER C OG  1 
ATOM   12311 N N   . PHE D 1 260 ? -11.109 33.316  -22.037 1.00 29.46  ? 289 PHE C N   1 
ATOM   12312 C CA  . PHE D 1 260 ? -10.489 34.340  -21.228 1.00 28.63  ? 289 PHE C CA  1 
ATOM   12313 C C   . PHE D 1 260 ? -9.185  33.805  -20.629 1.00 27.80  ? 289 PHE C C   1 
ATOM   12314 O O   . PHE D 1 260 ? -8.189  34.504  -20.594 1.00 26.90  ? 289 PHE C O   1 
ATOM   12315 C CB  . PHE D 1 260 ? -11.503 34.796  -20.182 1.00 33.10  ? 289 PHE C CB  1 
ATOM   12316 C CG  . PHE D 1 260 ? -10.951 35.910  -19.316 1.00 32.34  ? 289 PHE C CG  1 
ATOM   12317 C CD1 . PHE D 1 260 ? -10.756 37.177  -19.841 1.00 35.41  ? 289 PHE C CD1 1 
ATOM   12318 C CD2 . PHE D 1 260 ? -10.570 35.668  -18.007 1.00 34.26  ? 289 PHE C CD2 1 
ATOM   12319 C CE1 . PHE D 1 260 ? -10.180 38.176  -19.071 1.00 34.58  ? 289 PHE C CE1 1 
ATOM   12320 C CE2 . PHE D 1 260 ? -10.016 36.678  -17.239 1.00 34.26  ? 289 PHE C CE2 1 
ATOM   12321 C CZ  . PHE D 1 260 ? -9.823  37.923  -17.780 1.00 29.97  ? 289 PHE C CZ  1 
ATOM   12322 N N   . ALA D 1 261 ? -9.169  32.563  -20.142 1.00 29.43  ? 290 ALA C N   1 
ATOM   12323 C CA  . ALA D 1 261 ? -7.951  32.049  -19.536 1.00 31.54  ? 290 ALA C CA  1 
ATOM   12324 C C   . ALA D 1 261 ? -6.799  32.078  -20.553 1.00 28.17  ? 290 ALA C C   1 
ATOM   12325 O O   . ALA D 1 261 ? -5.694  32.496  -20.224 1.00 23.96  ? 290 ALA C O   1 
ATOM   12326 C CB  . ALA D 1 261 ? -8.174  30.667  -19.010 1.00 31.47  ? 290 ALA C CB  1 
ATOM   12327 N N   . ALA D 1 262 ? -7.077  31.685  -21.793 1.00 26.57  ? 291 ALA C N   1 
ATOM   12328 C CA  . ALA D 1 262 ? -6.082  31.786  -22.868 1.00 28.22  ? 291 ALA C CA  1 
ATOM   12329 C C   . ALA D 1 262 ? -5.695  33.236  -23.079 1.00 25.48  ? 291 ALA C C   1 
ATOM   12330 O O   . ALA D 1 262 ? -4.511  33.534  -23.212 1.00 26.68  ? 291 ALA C O   1 
ATOM   12331 C CB  . ALA D 1 262 ? -6.588  31.205  -24.166 1.00 25.96  ? 291 ALA C CB  1 
ATOM   12332 N N   . ALA D 1 263 ? -6.691  34.131  -23.120 1.00 26.40  ? 292 ALA C N   1 
ATOM   12333 C CA  . ALA D 1 263 ? -6.377  35.540  -23.311 1.00 26.34  ? 292 ALA C CA  1 
ATOM   12334 C C   . ALA D 1 263 ? -5.404  36.028  -22.233 1.00 26.77  ? 292 ALA C C   1 
ATOM   12335 O O   . ALA D 1 263 ? -4.569  36.882  -22.491 1.00 26.29  ? 292 ALA C O   1 
ATOM   12336 C CB  . ALA D 1 263 ? -7.612  36.411  -23.326 1.00 25.55  ? 292 ALA C CB  1 
ATOM   12337 N N   . MET D 1 264 ? -5.496  35.474  -21.030 1.00 25.53  ? 293 MET C N   1 
ATOM   12338 C CA  . MET D 1 264 ? -4.659  35.923  -19.926 1.00 26.55  ? 293 MET C CA  1 
ATOM   12339 C C   . MET D 1 264 ? -3.209  35.448  -20.121 1.00 24.55  ? 293 MET C C   1 
ATOM   12340 O O   . MET D 1 264 ? -2.267  36.156  -19.756 1.00 26.76  ? 293 MET C O   1 
ATOM   12341 C CB  . MET D 1 264 ? -5.167  35.420  -18.571 1.00 23.90  ? 293 MET C CB  1 
ATOM   12342 C CG  . MET D 1 264 ? -6.428  36.068  -18.026 1.00 29.02  ? 293 MET C CG  1 
ATOM   12343 S SD  . MET D 1 264 ? -6.371  37.865  -17.925 1.00 32.87  ? 293 MET C SD  1 
ATOM   12344 C CE  . MET D 1 264 ? -6.797  38.495  -19.546 1.00 31.29  ? 293 MET C CE  1 
ATOM   12345 N N   . ASN D 1 265 ? -3.018  34.257  -20.686 1.00 20.62  ? 294 ASN C N   1 
ATOM   12346 C CA  . ASN D 1 265 ? -1.689  33.788  -21.023 1.00 21.26  ? 294 ASN C CA  1 
ATOM   12347 C C   . ASN D 1 265 ? -1.041  34.750  -22.017 1.00 20.55  ? 294 ASN C C   1 
ATOM   12348 O O   . ASN D 1 265 ? 0.149   35.015  -21.916 1.00 29.93  ? 294 ASN C O   1 
ATOM   12349 C CB  . ASN D 1 265 ? -1.715  32.323  -21.449 1.00 25.38  ? 294 ASN C CB  1 
ATOM   12350 C CG  . ASN D 1 265 ? -1.979  31.432  -20.260 1.00 30.25  ? 294 ASN C CG  1 
ATOM   12351 O OD1 . ASN D 1 265 ? -2.257  31.934  -19.180 1.00 28.93  ? 294 ASN C OD1 1 
ATOM   12352 N ND2 . ASN D 1 265 ? -1.931  30.128  -20.421 1.00 37.83  ? 294 ASN C ND2 1 
ATOM   12353 N N   . GLY D 1 266 ? -1.842  35.313  -22.907 1.00 20.01  ? 295 GLY C N   1 
ATOM   12354 C CA  . GLY D 1 266 ? -1.394  36.297  -23.871 1.00 22.73  ? 295 GLY C CA  1 
ATOM   12355 C C   . GLY D 1 266 ? -1.073  37.623  -23.196 1.00 26.82  ? 295 GLY C C   1 
ATOM   12356 O O   . GLY D 1 266 ? -0.088  38.255  -23.529 1.00 24.68  ? 295 GLY C O   1 
ATOM   12357 N N   . LEU D 1 267 ? -1.941  38.043  -22.263 1.00 24.33  ? 296 LEU C N   1 
ATOM   12358 C CA  . LEU D 1 267 ? -1.724  39.295  -21.564 1.00 29.29  ? 296 LEU C CA  1 
ATOM   12359 C C   . LEU D 1 267 ? -0.513  39.178  -20.640 1.00 30.35  ? 296 LEU C C   1 
ATOM   12360 O O   . LEU D 1 267 ? 0.111   40.196  -20.352 1.00 32.71  ? 296 LEU C O   1 
ATOM   12361 C CB  . LEU D 1 267 ? -3.005  39.655  -20.820 1.00 26.77  ? 296 LEU C CB  1 
ATOM   12362 C CG  . LEU D 1 267 ? -3.091  41.068  -20.276 1.00 29.44  ? 296 LEU C CG  1 
ATOM   12363 C CD1 . LEU D 1 267 ? -3.321  42.011  -21.431 1.00 29.98  ? 296 LEU C CD1 1 
ATOM   12364 C CD2 . LEU D 1 267 ? -4.174  41.121  -19.251 1.00 29.60  ? 296 LEU C CD2 1 
ATOM   12365 N N   . ALA D 1 268 ? -0.123  37.948  -20.237 1.00 27.61  ? 297 ALA C N   1 
ATOM   12366 C CA  . ALA D 1 268 ? 0.995   37.771  -19.315 1.00 26.28  ? 297 ALA C CA  1 
ATOM   12367 C C   . ALA D 1 268 ? 2.317   37.915  -20.069 1.00 26.83  ? 297 ALA C C   1 
ATOM   12368 O O   . ALA D 1 268 ? 3.365   37.884  -19.466 1.00 32.66  ? 297 ALA C O   1 
ATOM   12369 C CB  . ALA D 1 268 ? 0.925   36.423  -18.579 1.00 27.80  ? 297 ALA C CB  1 
ATOM   12370 N N   . GLY D 1 269 ? 2.254   38.114  -21.387 1.00 29.26  ? 298 GLY C N   1 
ATOM   12371 C CA  . GLY D 1 269 ? 3.438   38.285  -22.203 1.00 31.62  ? 298 GLY C CA  1 
ATOM   12372 C C   . GLY D 1 269 ? 4.115   39.635  -21.952 1.00 30.39  ? 298 GLY C C   1 
ATOM   12373 O O   . GLY D 1 269 ? 3.470   40.677  -21.963 1.00 30.19  ? 298 GLY C O   1 
ATOM   12374 N N   . PRO D 1 270 ? 5.455   39.663  -21.805 1.00 31.51  ? 299 PRO C N   1 
ATOM   12375 C CA  . PRO D 1 270 ? 6.187   40.929  -21.666 1.00 33.73  ? 299 PRO C CA  1 
ATOM   12376 C C   . PRO D 1 270 ? 5.941   41.960  -22.762 1.00 30.96  ? 299 PRO C C   1 
ATOM   12377 O O   . PRO D 1 270 ? 6.032   43.150  -22.519 1.00 34.42  ? 299 PRO C O   1 
ATOM   12378 C CB  . PRO D 1 270 ? 7.653   40.559  -21.588 1.00 36.29  ? 299 PRO C CB  1 
ATOM   12379 C CG  . PRO D 1 270 ? 7.694   39.045  -21.602 1.00 32.24  ? 299 PRO C CG  1 
ATOM   12380 C CD  . PRO D 1 270 ? 6.307   38.472  -21.750 1.00 29.24  ? 299 PRO C CD  1 
ATOM   12381 N N   . LEU D 1 271 ? 5.567   41.550  -23.964 1.00 29.74  ? 300 LEU C N   1 
ATOM   12382 C CA  . LEU D 1 271 ? 5.308   42.553  -24.983 1.00 33.55  ? 300 LEU C CA  1 
ATOM   12383 C C   . LEU D 1 271 ? 3.836   42.965  -24.978 1.00 34.93  ? 300 LEU C C   1 
ATOM   12384 O O   . LEU D 1 271 ? 3.433   43.721  -25.853 1.00 36.29  ? 300 LEU C O   1 
ATOM   12385 C CB  . LEU D 1 271 ? 5.691   41.994  -26.351 1.00 32.49  ? 300 LEU C CB  1 
ATOM   12386 C CG  . LEU D 1 271 ? 7.174   41.755  -26.585 1.00 33.58  ? 300 LEU C CG  1 
ATOM   12387 C CD1 . LEU D 1 271 ? 7.356   41.229  -28.009 1.00 34.74  ? 300 LEU C CD1 1 
ATOM   12388 C CD2 . LEU D 1 271 ? 7.977   43.033  -26.350 1.00 36.89  ? 300 LEU C CD2 1 
ATOM   12389 N N   . HIS D 1 272 ? 3.033   42.392  -24.069 1.00 33.05  ? 301 HIS C N   1 
ATOM   12390 C CA  . HIS D 1 272 ? 1.648   42.781  -23.891 1.00 37.99  ? 301 HIS C CA  1 
ATOM   12391 C C   . HIS D 1 272 ? 1.467   43.417  -22.507 1.00 36.51  ? 301 HIS C C   1 
ATOM   12392 O O   . HIS D 1 272 ? 2.094   44.420  -22.192 1.00 43.97  ? 301 HIS C O   1 
ATOM   12393 C CB  . HIS D 1 272 ? 0.710   41.640  -24.306 1.00 36.76  ? 301 HIS C CB  1 
ATOM   12394 C CG  . HIS D 1 272 ? -0.679  42.117  -24.587 1.00 40.92  ? 301 HIS C CG  1 
ATOM   12395 N ND1 . HIS D 1 272 ? -1.794  41.306  -24.672 1.00 46.76  ? 301 HIS C ND1 1 
ATOM   12396 C CD2 . HIS D 1 272 ? -1.132  43.365  -24.771 1.00 40.23  ? 301 HIS C CD2 1 
ATOM   12397 C CE1 . HIS D 1 272 ? -2.866  42.072  -24.895 1.00 42.64  ? 301 HIS C CE1 1 
ATOM   12398 N NE2 . HIS D 1 272 ? -2.477  43.313  -24.974 1.00 40.47  ? 301 HIS C NE2 1 
ATOM   12399 N N   . GLY D 1 273 ? 0.661   42.819  -21.645 1.00 41.76  ? 302 GLY C N   1 
ATOM   12400 C CA  . GLY D 1 273 ? 0.161   43.546  -20.484 1.00 45.31  ? 302 GLY C CA  1 
ATOM   12401 C C   . GLY D 1 273 ? 1.198   43.675  -19.377 1.00 45.04  ? 302 GLY C C   1 
ATOM   12402 O O   . GLY D 1 273 ? 0.993   44.451  -18.447 1.00 41.34  ? 302 GLY C O   1 
ATOM   12403 N N   . LEU D 1 274 ? 2.311   42.937  -19.505 1.00 41.85  ? 303 LEU C N   1 
ATOM   12404 C CA  . LEU D 1 274 ? 3.362   42.963  -18.496 1.00 46.01  ? 303 LEU C CA  1 
ATOM   12405 C C   . LEU D 1 274 ? 4.169   44.258  -18.557 1.00 45.30  ? 303 LEU C C   1 
ATOM   12406 O O   . LEU D 1 274 ? 5.033   44.449  -17.716 1.00 45.05  ? 303 LEU C O   1 
ATOM   12407 C CB  . LEU D 1 274 ? 4.285   41.740  -18.606 1.00 50.97  ? 303 LEU C CB  1 
ATOM   12408 C CG  . LEU D 1 274 ? 4.325   40.785  -17.401 1.00 51.30  ? 303 LEU C CG  1 
ATOM   12409 C CD1 . LEU D 1 274 ? 2.960   40.171  -17.094 1.00 49.04  ? 303 LEU C CD1 1 
ATOM   12410 C CD2 . LEU D 1 274 ? 5.406   39.706  -17.585 1.00 53.31  ? 303 LEU C CD2 1 
ATOM   12411 N N   . ALA D 1 275 ? 3.899   45.137  -19.534 1.00 51.67  ? 304 ALA C N   1 
ATOM   12412 C CA  . ALA D 1 275 ? 4.654   46.381  -19.683 1.00 53.40  ? 304 ALA C CA  1 
ATOM   12413 C C   . ALA D 1 275 ? 4.367   47.392  -18.568 1.00 47.72  ? 304 ALA C C   1 
ATOM   12414 O O   . ALA D 1 275 ? 5.194   48.255  -18.336 1.00 45.93  ? 304 ALA C O   1 
ATOM   12415 C CB  . ALA D 1 275 ? 4.393   46.999  -21.051 1.00 54.02  ? 304 ALA C CB  1 
ATOM   12416 N N   . ASN D 1 276 ? 3.197   47.340  -17.907 1.00 48.08  ? 305 ASN C N   1 
ATOM   12417 C CA  . ASN D 1 276 ? 2.932   48.178  -16.733 1.00 45.05  ? 305 ASN C CA  1 
ATOM   12418 C C   . ASN D 1 276 ? 4.018   47.949  -15.687 1.00 38.92  ? 305 ASN C C   1 
ATOM   12419 O O   . ASN D 1 276 ? 4.643   48.911  -15.264 1.00 39.99  ? 305 ASN C O   1 
ATOM   12420 C CB  . ASN D 1 276 ? 1.558   47.932  -16.098 1.00 53.09  ? 305 ASN C CB  1 
ATOM   12421 C CG  . ASN D 1 276 ? 1.278   48.764  -14.852 1.00 57.29  ? 305 ASN C CG  1 
ATOM   12422 O OD1 . ASN D 1 276 ? 2.188   49.361  -14.261 1.00 65.19  ? 305 ASN C OD1 1 
ATOM   12423 N ND2 . ASN D 1 276 ? 0.024   48.818  -14.412 1.00 50.25  ? 305 ASN C ND2 1 
ATOM   12424 N N   . GLN D 1 277 ? 4.275   46.688  -15.295 1.00 45.79  ? 306 GLN C N   1 
ATOM   12425 C CA  . GLN D 1 277 ? 5.250   46.458  -14.235 1.00 53.33  ? 306 GLN C CA  1 
ATOM   12426 C C   . GLN D 1 277 ? 6.650   46.780  -14.753 1.00 46.62  ? 306 GLN C C   1 
ATOM   12427 O O   . GLN D 1 277 ? 7.396   47.431  -14.039 1.00 38.57  ? 306 GLN C O   1 
ATOM   12428 C CB  . GLN D 1 277 ? 5.288   45.131  -13.462 1.00 64.89  ? 306 GLN C CB  1 
ATOM   12429 C CG  . GLN D 1 277 ? 5.005   43.858  -14.251 1.00 70.73  ? 306 GLN C CG  1 
ATOM   12430 C CD  . GLN D 1 277 ? 3.606   43.323  -14.007 1.00 83.36  ? 306 GLN C CD  1 
ATOM   12431 O OE1 . GLN D 1 277 ? 2.609   44.037  -14.179 1.00 73.03  ? 306 GLN C OE1 1 
ATOM   12432 N NE2 . GLN D 1 277 ? 3.511   42.069  -13.578 1.00 83.93  ? 306 GLN C NE2 1 
ATOM   12433 N N   . GLU D 1 278 ? 6.995   46.357  -15.981 1.00 51.47  ? 307 GLU C N   1 
ATOM   12434 C CA  . GLU D 1 278 ? 8.307   46.661  -16.564 1.00 50.19  ? 307 GLU C CA  1 
ATOM   12435 C C   . GLU D 1 278 ? 8.589   48.158  -16.466 1.00 45.00  ? 307 GLU C C   1 
ATOM   12436 O O   . GLU D 1 278 ? 9.699   48.549  -16.115 1.00 38.79  ? 307 GLU C O   1 
ATOM   12437 C CB  . GLU D 1 278 ? 8.452   46.318  -18.052 1.00 56.77  ? 307 GLU C CB  1 
ATOM   12438 C CG  . GLU D 1 278 ? 8.199   44.843  -18.357 1.00 75.90  ? 307 GLU C CG  1 
ATOM   12439 C CD  . GLU D 1 278 ? 8.290   44.416  -19.816 1.00 86.55  ? 307 GLU C CD  1 
ATOM   12440 O OE1 . GLU D 1 278 ? 9.433   44.346  -20.346 1.00 78.17  ? 307 GLU C OE1 1 
ATOM   12441 O OE2 . GLU D 1 278 ? 7.207   44.145  -20.410 1.00 75.79  ? 307 GLU C OE2 1 
ATOM   12442 N N   . VAL D 1 279 ? 7.566   48.982  -16.743 1.00 40.40  ? 308 VAL C N   1 
ATOM   12443 C CA  . VAL D 1 279 ? 7.696   50.434  -16.645 1.00 41.55  ? 308 VAL C CA  1 
ATOM   12444 C C   . VAL D 1 279 ? 8.053   50.869  -15.224 1.00 40.04  ? 308 VAL C C   1 
ATOM   12445 O O   . VAL D 1 279 ? 8.897   51.719  -15.057 1.00 36.81  ? 308 VAL C O   1 
ATOM   12446 C CB  . VAL D 1 279 ? 6.448   51.218  -17.107 1.00 43.00  ? 308 VAL C CB  1 
ATOM   12447 C CG1 . VAL D 1 279 ? 6.516   52.698  -16.708 1.00 40.99  ? 308 VAL C CG1 1 
ATOM   12448 C CG2 . VAL D 1 279 ? 6.202   51.085  -18.609 1.00 48.50  ? 308 VAL C CG2 1 
ATOM   12449 N N   . LEU D 1 280 ? 7.334   50.402  -14.194 1.00 45.77  ? 309 LEU C N   1 
ATOM   12450 C CA  . LEU D 1 280 ? 7.572   50.937  -12.856 1.00 45.95  ? 309 LEU C CA  1 
ATOM   12451 C C   . LEU D 1 280 ? 8.912   50.402  -12.347 1.00 47.09  ? 309 LEU C C   1 
ATOM   12452 O O   . LEU D 1 280 ? 9.597   51.090  -11.597 1.00 41.63  ? 309 LEU C O   1 
ATOM   12453 C CB  . LEU D 1 280 ? 6.452   50.642  -11.852 1.00 47.20  ? 309 LEU C CB  1 
ATOM   12454 C CG  . LEU D 1 280 ? 6.573   51.340  -10.488 1.00 43.83  ? 309 LEU C CG  1 
ATOM   12455 C CD1 . LEU D 1 280 ? 6.191   52.796  -10.570 1.00 42.47  ? 309 LEU C CD1 1 
ATOM   12456 C CD2 . LEU D 1 280 ? 5.748   50.632  -9.411  1.00 44.13  ? 309 LEU C CD2 1 
ATOM   12457 N N   . VAL D 1 281 ? 9.247   49.161  -12.746 1.00 52.49  ? 310 VAL C N   1 
ATOM   12458 C CA  . VAL D 1 281 ? 10.545  48.553  -12.478 1.00 54.77  ? 310 VAL C CA  1 
ATOM   12459 C C   . VAL D 1 281 ? 11.630  49.478  -13.019 1.00 52.47  ? 310 VAL C C   1 
ATOM   12460 O O   . VAL D 1 281 ? 12.597  49.774  -12.322 1.00 49.76  ? 310 VAL C O   1 
ATOM   12461 C CB  . VAL D 1 281 ? 10.648  47.122  -13.062 1.00 66.93  ? 310 VAL C CB  1 
ATOM   12462 C CG1 . VAL D 1 281 ? 12.086  46.642  -13.238 1.00 68.80  ? 310 VAL C CG1 1 
ATOM   12463 C CG2 . VAL D 1 281 ? 9.856   46.106  -12.236 1.00 65.90  ? 310 VAL C CG2 1 
ATOM   12464 N N   . TRP D 1 282 ? 11.435  49.959  -14.259 1.00 53.33  ? 311 TRP C N   1 
ATOM   12465 C CA  . TRP D 1 282 ? 12.378  50.861  -14.905 1.00 48.27  ? 311 TRP C CA  1 
ATOM   12466 C C   . TRP D 1 282 ? 12.340  52.265  -14.279 1.00 46.44  ? 311 TRP C C   1 
ATOM   12467 O O   . TRP D 1 282 ? 13.361  52.929  -14.221 1.00 52.83  ? 311 TRP C O   1 
ATOM   12468 C CB  . TRP D 1 282 ? 12.113  50.863  -16.417 1.00 57.56  ? 311 TRP C CB  1 
ATOM   12469 C CG  . TRP D 1 282 ? 13.017  51.743  -17.250 1.00 62.68  ? 311 TRP C CG  1 
ATOM   12470 C CD1 . TRP D 1 282 ? 14.195  51.413  -17.866 1.00 60.94  ? 311 TRP C CD1 1 
ATOM   12471 C CD2 . TRP D 1 282 ? 12.755  53.120  -17.600 1.00 58.26  ? 311 TRP C CD2 1 
ATOM   12472 N NE1 . TRP D 1 282 ? 14.695  52.497  -18.547 1.00 55.42  ? 311 TRP C NE1 1 
ATOM   12473 C CE2 . TRP D 1 282 ? 13.835  53.555  -18.405 1.00 55.47  ? 311 TRP C CE2 1 
ATOM   12474 C CE3 . TRP D 1 282 ? 11.718  54.017  -17.308 1.00 57.26  ? 311 TRP C CE3 1 
ATOM   12475 C CZ2 . TRP D 1 282 ? 13.897  54.849  -18.919 1.00 52.05  ? 311 TRP C CZ2 1 
ATOM   12476 C CZ3 . TRP D 1 282 ? 11.787  55.297  -17.814 1.00 63.85  ? 311 TRP C CZ3 1 
ATOM   12477 C CH2 . TRP D 1 282 ? 12.860  55.703  -18.613 1.00 59.79  ? 311 TRP C CH2 1 
ATOM   12478 N N   . LEU D 1 283 ? 11.175  52.734  -13.827 1.00 48.29  ? 312 LEU C N   1 
ATOM   12479 C CA  . LEU D 1 283 ? 11.054  53.984  -13.090 1.00 51.39  ? 312 LEU C CA  1 
ATOM   12480 C C   . LEU D 1 283 ? 11.770  53.847  -11.753 1.00 59.78  ? 312 LEU C C   1 
ATOM   12481 O O   . LEU D 1 283 ? 12.340  54.820  -11.273 1.00 59.15  ? 312 LEU C O   1 
ATOM   12482 C CB  . LEU D 1 283 ? 9.595   54.345  -12.823 1.00 52.52  ? 312 LEU C CB  1 
ATOM   12483 C CG  . LEU D 1 283 ? 8.707   54.688  -14.026 1.00 54.47  ? 312 LEU C CG  1 
ATOM   12484 C CD1 . LEU D 1 283 ? 7.318   55.088  -13.523 1.00 53.23  ? 312 LEU C CD1 1 
ATOM   12485 C CD2 . LEU D 1 283 ? 9.288   55.812  -14.889 1.00 50.10  ? 312 LEU C CD2 1 
ATOM   12486 N N   . THR D 1 284 ? 11.671  52.648  -11.154 1.00 59.88  ? 313 THR C N   1 
ATOM   12487 C CA  . THR D 1 284 ? 12.308  52.328  -9.885  1.00 63.67  ? 313 THR C CA  1 
ATOM   12488 C C   . THR D 1 284 ? 13.825  52.369  -10.081 1.00 66.63  ? 313 THR C C   1 
ATOM   12489 O O   . THR D 1 284 ? 14.526  53.051  -9.326  1.00 55.61  ? 313 THR C O   1 
ATOM   12490 C CB  . THR D 1 284 ? 11.818  50.958  -9.391  1.00 67.36  ? 313 THR C CB  1 
ATOM   12491 O OG1 . THR D 1 284 ? 10.419  51.047  -9.124  1.00 64.15  ? 313 THR C OG1 1 
ATOM   12492 C CG2 . THR D 1 284 ? 12.502  50.466  -8.125  1.00 62.44  ? 313 THR C CG2 1 
ATOM   12493 N N   . GLN D 1 285 ? 14.301  51.657  -11.122 1.00 58.27  ? 314 GLN C N   1 
ATOM   12494 C CA  . GLN D 1 285 ? 15.721  51.515  -11.413 1.00 55.75  ? 314 GLN C CA  1 
ATOM   12495 C C   . GLN D 1 285 ? 16.356  52.862  -11.730 1.00 51.62  ? 314 GLN C C   1 
ATOM   12496 O O   . GLN D 1 285 ? 17.465  53.128  -11.281 1.00 47.14  ? 314 GLN C O   1 
ATOM   12497 C CB  . GLN D 1 285 ? 16.067  50.560  -12.558 1.00 57.45  ? 314 GLN C CB  1 
ATOM   12498 C CG  . GLN D 1 285 ? 16.597  49.206  -12.094 1.00 66.52  ? 314 GLN C CG  1 
ATOM   12499 C CD  . GLN D 1 285 ? 17.853  49.312  -11.244 1.00 67.27  ? 314 GLN C CD  1 
ATOM   12500 O OE1 . GLN D 1 285 ? 18.787  50.063  -11.555 1.00 63.36  ? 314 GLN C OE1 1 
ATOM   12501 N NE2 . GLN D 1 285 ? 17.884  48.577  -10.142 1.00 68.01  ? 314 GLN C NE2 1 
ATOM   12502 N N   . LEU D 1 286 ? 15.664  53.698  -12.507 1.00 60.88  ? 315 LEU C N   1 
ATOM   12503 C CA  . LEU D 1 286 ? 16.192  55.007  -12.841 1.00 67.54  ? 315 LEU C CA  1 
ATOM   12504 C C   . LEU D 1 286 ? 16.256  55.856  -11.568 1.00 66.84  ? 315 LEU C C   1 
ATOM   12505 O O   . LEU D 1 286 ? 17.252  56.540  -11.362 1.00 62.80  ? 315 LEU C O   1 
ATOM   12506 C CB  . LEU D 1 286 ? 15.439  55.694  -13.984 1.00 79.98  ? 315 LEU C CB  1 
ATOM   12507 C CG  . LEU D 1 286 ? 14.286  56.653  -13.648 1.00 91.02  ? 315 LEU C CG  1 
ATOM   12508 C CD1 . LEU D 1 286 ? 14.716  58.070  -13.226 1.00 81.87  ? 315 LEU C CD1 1 
ATOM   12509 C CD2 . LEU D 1 286 ? 13.363  56.719  -14.873 1.00 93.17  ? 315 LEU C CD2 1 
ATOM   12510 N N   . GLN D 1 287 ? 15.240  55.798  -10.694 1.00 61.05  ? 316 GLN C N   1 
ATOM   12511 C CA  . GLN D 1 287 ? 15.299  56.580  -9.462  1.00 72.25  ? 316 GLN C CA  1 
ATOM   12512 C C   . GLN D 1 287 ? 16.359  56.014  -8.507  1.00 73.33  ? 316 GLN C C   1 
ATOM   12513 O O   . GLN D 1 287 ? 16.789  56.689  -7.575  1.00 66.16  ? 316 GLN C O   1 
ATOM   12514 C CB  . GLN D 1 287 ? 13.965  56.719  -8.727  1.00 78.33  ? 316 GLN C CB  1 
ATOM   12515 C CG  . GLN D 1 287 ? 12.972  57.642  -9.426  1.00 86.24  ? 316 GLN C CG  1 
ATOM   12516 C CD  . GLN D 1 287 ? 11.973  58.279  -8.481  1.00 98.05  ? 316 GLN C CD  1 
ATOM   12517 O OE1 . GLN D 1 287 ? 11.529  59.422  -8.665  1.00 87.22  ? 316 GLN C OE1 1 
ATOM   12518 N NE2 . GLN D 1 287 ? 11.586  57.524  -7.464  1.00 111.10 ? 316 GLN C NE2 1 
ATOM   12519 N N   . LYS D 1 288 ? 16.789  54.767  -8.737  1.00 78.08  ? 317 LYS C N   1 
ATOM   12520 C CA  . LYS D 1 288 ? 17.916  54.202  -8.009  1.00 78.58  ? 317 LYS C CA  1 
ATOM   12521 C C   . LYS D 1 288 ? 19.233  54.842  -8.460  1.00 81.89  ? 317 LYS C C   1 
ATOM   12522 O O   . LYS D 1 288 ? 20.062  55.186  -7.620  1.00 89.82  ? 317 LYS C O   1 
ATOM   12523 C CB  . LYS D 1 288 ? 17.948  52.673  -8.141  1.00 76.06  ? 317 LYS C CB  1 
ATOM   12524 C CG  . LYS D 1 288 ? 18.965  51.955  -7.256  1.00 75.52  ? 317 LYS C CG  1 
ATOM   12525 C CD  . LYS D 1 288 ? 18.760  50.447  -7.169  1.00 84.93  ? 317 LYS C CD  1 
ATOM   12526 C CE  . LYS D 1 288 ? 17.535  50.049  -6.385  1.00 88.74  ? 317 LYS C CE  1 
ATOM   12527 N NZ  . LYS D 1 288 ? 17.636  50.376  -4.958  1.00 86.47  ? 317 LYS C NZ  1 
ATOM   12528 N N   . GLU D 1 289 ? 19.437  54.918  -9.778  1.00 84.55  ? 318 GLU C N   1 
ATOM   12529 C CA  . GLU D 1 289 ? 20.744  55.390  -10.312 1.00 92.20  ? 318 GLU C CA  1 
ATOM   12530 C C   . GLU D 1 289 ? 20.741  56.880  -10.708 1.00 84.46  ? 318 GLU C C   1 
ATOM   12531 O O   . GLU D 1 289 ? 21.727  57.303  -11.340 1.00 80.67  ? 318 GLU C O   1 
ATOM   12532 C CB  . GLU D 1 289 ? 21.127  54.501  -11.498 1.00 94.76  ? 318 GLU C CB  1 
ATOM   12533 C CG  . GLU D 1 289 ? 20.095  54.471  -12.618 1.00 98.13  ? 318 GLU C CG  1 
ATOM   12534 C CD  . GLU D 1 289 ? 20.277  53.208  -13.435 1.00 98.27  ? 318 GLU C CD  1 
ATOM   12535 O OE1 . GLU D 1 289 ? 20.472  53.300  -14.661 1.00 89.70  ? 318 GLU C OE1 1 
ATOM   12536 O OE2 . GLU D 1 289 ? 20.240  52.122  -12.826 1.00 104.38 ? 318 GLU C OE2 1 
ATOM   12537 N N   . VAL D 1 290 ? 19.542  57.658  -10.475 1.00 89.05  ? 319 VAL C N   1 
ATOM   12538 C CA  . VAL D 1 290 ? 19.715  59.142  -10.625 1.00 96.45  ? 319 VAL C CA  1 
ATOM   12539 C C   . VAL D 1 290 ? 19.160  59.864  -9.378  1.00 86.36  ? 319 VAL C C   1 
ATOM   12540 O O   . VAL D 1 290 ? 19.677  60.947  -9.060  1.00 98.70  ? 319 VAL C O   1 
ATOM   12541 C CB  . VAL D 1 290 ? 19.137  59.773  -11.914 1.00 107.76 ? 319 VAL C CB  1 
ATOM   12542 C CG1 . VAL D 1 290 ? 19.230  58.861  -13.129 1.00 113.87 ? 319 VAL C CG1 1 
ATOM   12543 C CG2 . VAL D 1 290 ? 17.712  60.279  -11.735 1.00 110.65 ? 319 VAL C CG2 1 
ATOM   12544 N N   . GLY D 1 291 ? 18.143  59.275  -8.721  1.00 84.53  ? 320 GLY C N   1 
ATOM   12545 C CA  . GLY D 1 291 ? 17.509  59.939  -7.568  1.00 86.33  ? 320 GLY C CA  1 
ATOM   12546 C C   . GLY D 1 291 ? 16.001  60.028  -7.672  1.00 78.62  ? 320 GLY C C   1 
ATOM   12547 O O   . GLY D 1 291 ? 15.469  59.747  -8.755  1.00 73.58  ? 320 GLY C O   1 
ATOM   12548 N N   . LYS D 1 292 ? 15.344  60.461  -6.600  1.00 82.13  ? 321 LYS C N   1 
ATOM   12549 C CA  . LYS D 1 292 ? 13.889  60.557  -6.556  1.00 93.48  ? 321 LYS C CA  1 
ATOM   12550 C C   . LYS D 1 292 ? 13.403  61.973  -6.917  1.00 100.85 ? 321 LYS C C   1 
ATOM   12551 O O   . LYS D 1 292 ? 12.203  62.161  -7.154  1.00 99.15  ? 321 LYS C O   1 
ATOM   12552 C CB  . LYS D 1 292 ? 13.378  60.058  -5.196  1.00 89.95  ? 321 LYS C CB  1 
ATOM   12553 N N   . ASP D 1 293 ? 14.321  62.962  -6.957  1.00 98.44  ? 322 ASP C N   1 
ATOM   12554 C CA  . ASP D 1 293 ? 14.070  64.281  -7.538  1.00 105.12 ? 322 ASP C CA  1 
ATOM   12555 C C   . ASP D 1 293 ? 15.224  64.651  -8.469  1.00 110.81 ? 322 ASP C C   1 
ATOM   12556 O O   . ASP D 1 293 ? 16.385  64.524  -8.076  1.00 121.59 ? 322 ASP C O   1 
ATOM   12557 C CB  . ASP D 1 293 ? 13.883  65.363  -6.482  1.00 106.33 ? 322 ASP C CB  1 
ATOM   12558 C CG  . ASP D 1 293 ? 12.442  65.654  -6.093  1.00 106.08 ? 322 ASP C CG  1 
ATOM   12559 O OD1 . ASP D 1 293 ? 11.853  64.844  -5.340  1.00 105.51 ? 322 ASP C OD1 1 
ATOM   12560 O OD2 . ASP D 1 293 ? 11.917  66.675  -6.578  1.00 92.28  ? 322 ASP C OD2 1 
ATOM   12561 N N   . VAL D 1 294 ? 14.900  65.119  -9.689  1.00 100.04 ? 323 VAL C N   1 
ATOM   12562 C CA  . VAL D 1 294 ? 15.874  65.160  -10.773 1.00 93.27  ? 323 VAL C CA  1 
ATOM   12563 C C   . VAL D 1 294 ? 15.720  66.443  -11.587 1.00 83.95  ? 323 VAL C C   1 
ATOM   12564 O O   . VAL D 1 294 ? 14.698  67.123  -11.522 1.00 87.61  ? 323 VAL C O   1 
ATOM   12565 C CB  . VAL D 1 294 ? 15.772  63.923  -11.688 1.00 97.77  ? 323 VAL C CB  1 
ATOM   12566 C CG1 . VAL D 1 294 ? 14.707  64.089  -12.770 1.00 97.23  ? 323 VAL C CG1 1 
ATOM   12567 C CG2 . VAL D 1 294 ? 17.117  63.564  -12.314 1.00 101.56 ? 323 VAL C CG2 1 
ATOM   12568 N N   . SER D 1 295 ? 16.787  66.751  -12.337 1.00 74.63  ? 324 SER C N   1 
ATOM   12569 C CA  . SER D 1 295 ? 16.818  67.822  -13.320 1.00 71.72  ? 324 SER C CA  1 
ATOM   12570 C C   . SER D 1 295 ? 16.495  67.275  -14.707 1.00 72.21  ? 324 SER C C   1 
ATOM   12571 O O   . SER D 1 295 ? 16.823  66.133  -15.031 1.00 68.07  ? 324 SER C O   1 
ATOM   12572 C CB  . SER D 1 295 ? 18.174  68.490  -13.339 1.00 67.68  ? 324 SER C CB  1 
ATOM   12573 O OG  . SER D 1 295 ? 19.203  67.522  -13.492 1.00 58.96  ? 324 SER C OG  1 
ATOM   12574 N N   . ASP D 1 296 ? 15.931  68.156  -15.537 1.00 75.08  ? 325 ASP C N   1 
ATOM   12575 C CA  . ASP D 1 296 ? 15.531  67.851  -16.899 1.00 76.22  ? 325 ASP C CA  1 
ATOM   12576 C C   . ASP D 1 296 ? 16.729  67.360  -17.707 1.00 79.90  ? 325 ASP C C   1 
ATOM   12577 O O   . ASP D 1 296 ? 16.538  66.729  -18.742 1.00 83.36  ? 325 ASP C O   1 
ATOM   12578 C CB  . ASP D 1 296 ? 14.902  69.072  -17.548 1.00 75.39  ? 325 ASP C CB  1 
ATOM   12579 C CG  . ASP D 1 296 ? 13.859  69.792  -16.700 1.00 86.68  ? 325 ASP C CG  1 
ATOM   12580 O OD1 . ASP D 1 296 ? 14.249  70.488  -15.722 1.00 81.04  ? 325 ASP C OD1 1 
ATOM   12581 O OD2 . ASP D 1 296 ? 12.661  69.639  -17.007 1.00 90.42  ? 325 ASP C OD2 1 
ATOM   12582 N N   . GLU D 1 297 ? 17.947  67.666  -17.227 1.00 83.13  ? 326 GLU C N   1 
ATOM   12583 C CA  . GLU D 1 297 ? 19.179  67.343  -17.932 1.00 92.08  ? 326 GLU C CA  1 
ATOM   12584 C C   . GLU D 1 297 ? 19.640  65.934  -17.582 1.00 80.98  ? 326 GLU C C   1 
ATOM   12585 O O   . GLU D 1 297 ? 19.858  65.113  -18.474 1.00 66.85  ? 326 GLU C O   1 
ATOM   12586 C CB  . GLU D 1 297 ? 20.329  68.302  -17.601 1.00 105.04 ? 326 GLU C CB  1 
ATOM   12587 C CG  . GLU D 1 297 ? 21.399  68.363  -18.700 1.00 119.50 ? 326 GLU C CG  1 
ATOM   12588 C CD  . GLU D 1 297 ? 20.852  68.592  -20.110 1.00 151.03 ? 326 GLU C CD  1 
ATOM   12589 O OE1 . GLU D 1 297 ? 21.618  68.365  -21.081 1.00 156.97 ? 326 GLU C OE1 1 
ATOM   12590 O OE2 . GLU D 1 297 ? 19.677  69.025  -20.246 1.00 181.37 ? 326 GLU C OE2 1 
ATOM   12591 N N   . LYS D 1 298 ? 19.825  65.667  -16.285 1.00 72.68  ? 327 LYS C N   1 
ATOM   12592 C CA  . LYS D 1 298 ? 20.200  64.319  -15.906 1.00 77.57  ? 327 LYS C CA  1 
ATOM   12593 C C   . LYS D 1 298 ? 19.190  63.380  -16.561 1.00 66.81  ? 327 LYS C C   1 
ATOM   12594 O O   . LYS D 1 298 ? 19.576  62.367  -17.116 1.00 65.58  ? 327 LYS C O   1 
ATOM   12595 C CB  . LYS D 1 298 ? 20.371  64.136  -14.394 1.00 86.38  ? 327 LYS C CB  1 
ATOM   12596 C CG  . LYS D 1 298 ? 21.782  64.398  -13.854 1.00 88.38  ? 327 LYS C CG  1 
ATOM   12597 C CD  . LYS D 1 298 ? 21.927  64.084  -12.367 1.00 96.41  ? 327 LYS C CD  1 
ATOM   12598 C CE  . LYS D 1 298 ? 20.860  64.722  -11.498 1.00 97.52  ? 327 LYS C CE  1 
ATOM   12599 N NZ  . LYS D 1 298 ? 20.772  66.183  -11.610 1.00 87.27  ? 327 LYS C NZ  1 
ATOM   12600 N N   . LEU D 1 299 ? 17.910  63.765  -16.570 1.00 79.71  ? 328 LEU C N   1 
ATOM   12601 C CA  . LEU D 1 299 ? 16.877  62.972  -17.220 1.00 87.53  ? 328 LEU C CA  1 
ATOM   12602 C C   . LEU D 1 299 ? 17.180  62.825  -18.713 1.00 82.35  ? 328 LEU C C   1 
ATOM   12603 O O   . LEU D 1 299 ? 17.358  61.710  -19.190 1.00 74.43  ? 328 LEU C O   1 
ATOM   12604 C CB  . LEU D 1 299 ? 15.504  63.594  -16.965 1.00 93.88  ? 328 LEU C CB  1 
ATOM   12605 C CG  . LEU D 1 299 ? 14.295  62.782  -17.452 1.00 103.37 ? 328 LEU C CG  1 
ATOM   12606 C CD1 . LEU D 1 299 ? 13.071  63.126  -16.611 1.00 106.55 ? 328 LEU C CD1 1 
ATOM   12607 C CD2 . LEU D 1 299 ? 14.004  63.009  -18.937 1.00 105.19 ? 328 LEU C CD2 1 
ATOM   12608 N N   . ARG D 1 300 ? 17.242  63.950  -19.439 1.00 84.69  ? 329 ARG C N   1 
ATOM   12609 C CA  . ARG D 1 300 ? 17.476  63.951  -20.878 1.00 81.41  ? 329 ARG C CA  1 
ATOM   12610 C C   . ARG D 1 300 ? 18.726  63.132  -21.201 1.00 74.28  ? 329 ARG C C   1 
ATOM   12611 O O   . ARG D 1 300 ? 18.655  62.202  -22.003 1.00 62.98  ? 329 ARG C O   1 
ATOM   12612 C CB  . ARG D 1 300 ? 17.500  65.414  -21.334 1.00 86.34  ? 329 ARG C CB  1 
ATOM   12613 C CG  . ARG D 1 300 ? 17.646  65.714  -22.820 1.00 94.86  ? 329 ARG C CG  1 
ATOM   12614 C CD  . ARG D 1 300 ? 16.878  66.990  -23.207 1.00 100.72 ? 329 ARG C CD  1 
ATOM   12615 N NE  . ARG D 1 300 ? 16.860  68.044  -22.178 1.00 103.64 ? 329 ARG C NE  1 
ATOM   12616 C CZ  . ARG D 1 300 ? 16.085  69.139  -22.163 1.00 100.91 ? 329 ARG C CZ  1 
ATOM   12617 N NH1 . ARG D 1 300 ? 15.298  69.418  -23.187 1.00 99.85  ? 329 ARG C NH1 1 
ATOM   12618 N NH2 . ARG D 1 300 ? 16.110  69.966  -21.128 1.00 91.72  ? 329 ARG C NH2 1 
ATOM   12619 N N   . ASP D 1 301 ? 19.848  63.453  -20.534 1.00 74.07  ? 330 ASP C N   1 
ATOM   12620 C CA  . ASP D 1 301 ? 21.082  62.688  -20.664 1.00 77.91  ? 330 ASP C CA  1 
ATOM   12621 C C   . ASP D 1 301 ? 20.778  61.202  -20.512 1.00 78.09  ? 330 ASP C C   1 
ATOM   12622 O O   . ASP D 1 301 ? 21.216  60.397  -21.327 1.00 69.99  ? 330 ASP C O   1 
ATOM   12623 C CB  . ASP D 1 301 ? 22.122  62.995  -19.590 1.00 85.89  ? 330 ASP C CB  1 
ATOM   12624 C CG  . ASP D 1 301 ? 22.823  64.349  -19.609 1.00 87.77  ? 330 ASP C CG  1 
ATOM   12625 O OD1 . ASP D 1 301 ? 22.471  65.211  -20.446 1.00 87.71  ? 330 ASP C OD1 1 
ATOM   12626 O OD2 . ASP D 1 301 ? 23.724  64.531  -18.762 1.00 82.67  ? 330 ASP C OD2 1 
ATOM   12627 N N   . TYR D 1 302 ? 20.030  60.862  -19.448 1.00 83.27  ? 331 TYR C N   1 
ATOM   12628 C CA  . TYR D 1 302 ? 19.677  59.482  -19.133 1.00 75.98  ? 331 TYR C CA  1 
ATOM   12629 C C   . TYR D 1 302 ? 18.962  58.849  -20.329 1.00 70.15  ? 331 TYR C C   1 
ATOM   12630 O O   . TYR D 1 302 ? 19.258  57.715  -20.688 1.00 65.66  ? 331 TYR C O   1 
ATOM   12631 C CB  . TYR D 1 302 ? 18.840  59.374  -17.849 1.00 79.18  ? 331 TYR C CB  1 
ATOM   12632 C CG  . TYR D 1 302 ? 18.667  57.960  -17.297 1.00 87.29  ? 331 TYR C CG  1 
ATOM   12633 C CD1 . TYR D 1 302 ? 19.644  57.368  -16.496 1.00 91.20  ? 331 TYR C CD1 1 
ATOM   12634 C CD2 . TYR D 1 302 ? 17.522  57.211  -17.563 1.00 87.01  ? 331 TYR C CD2 1 
ATOM   12635 C CE1 . TYR D 1 302 ? 19.491  56.085  -15.988 1.00 82.62  ? 331 TYR C CE1 1 
ATOM   12636 C CE2 . TYR D 1 302 ? 17.362  55.922  -17.071 1.00 77.97  ? 331 TYR C CE2 1 
ATOM   12637 C CZ  . TYR D 1 302 ? 18.348  55.359  -16.278 1.00 78.90  ? 331 TYR C CZ  1 
ATOM   12638 O OH  . TYR D 1 302 ? 18.195  54.099  -15.783 1.00 76.21  ? 331 TYR C OH  1 
ATOM   12639 N N   . ILE D 1 303 ? 18.029  59.582  -20.948 1.00 69.66  ? 332 ILE C N   1 
ATOM   12640 C CA  . ILE D 1 303 ? 17.326  59.070  -22.116 1.00 73.49  ? 332 ILE C CA  1 
ATOM   12641 C C   . ILE D 1 303 ? 18.375  58.758  -23.178 1.00 70.09  ? 332 ILE C C   1 
ATOM   12642 O O   . ILE D 1 303 ? 18.452  57.635  -23.655 1.00 58.51  ? 332 ILE C O   1 
ATOM   12643 C CB  . ILE D 1 303 ? 16.238  60.041  -22.634 1.00 75.78  ? 332 ILE C CB  1 
ATOM   12644 C CG1 . ILE D 1 303 ? 15.256  60.459  -21.531 1.00 81.84  ? 332 ILE C CG1 1 
ATOM   12645 C CG2 . ILE D 1 303 ? 15.484  59.466  -23.838 1.00 67.90  ? 332 ILE C CG2 1 
ATOM   12646 C CD1 . ILE D 1 303 ? 14.613  59.296  -20.795 1.00 78.30  ? 332 ILE C CD1 1 
ATOM   12647 N N   . TRP D 1 304 ? 19.223  59.741  -23.497 1.00 85.32  ? 333 TRP C N   1 
ATOM   12648 C CA  . TRP D 1 304 ? 20.131  59.597  -24.623 1.00 87.08  ? 333 TRP C CA  1 
ATOM   12649 C C   . TRP D 1 304 ? 21.061  58.404  -24.429 1.00 80.95  ? 333 TRP C C   1 
ATOM   12650 O O   . TRP D 1 304 ? 21.321  57.700  -25.393 1.00 83.44  ? 333 TRP C O   1 
ATOM   12651 C CB  . TRP D 1 304 ? 20.910  60.889  -24.914 1.00 97.53  ? 333 TRP C CB  1 
ATOM   12652 C CG  . TRP D 1 304 ? 20.224  61.790  -25.911 1.00 109.29 ? 333 TRP C CG  1 
ATOM   12653 C CD1 . TRP D 1 304 ? 19.705  63.032  -25.682 1.00 107.05 ? 333 TRP C CD1 1 
ATOM   12654 C CD2 . TRP D 1 304 ? 19.949  61.489  -27.302 1.00 120.82 ? 333 TRP C CD2 1 
ATOM   12655 N NE1 . TRP D 1 304 ? 19.152  63.535  -26.830 1.00 116.21 ? 333 TRP C NE1 1 
ATOM   12656 C CE2 . TRP D 1 304 ? 19.279  62.612  -27.838 1.00 124.49 ? 333 TRP C CE2 1 
ATOM   12657 C CE3 . TRP D 1 304 ? 20.202  60.393  -28.141 1.00 118.59 ? 333 TRP C CE3 1 
ATOM   12658 C CZ2 . TRP D 1 304 ? 18.865  62.663  -29.170 1.00 129.68 ? 333 TRP C CZ2 1 
ATOM   12659 C CZ3 . TRP D 1 304 ? 19.787  60.443  -29.454 1.00 122.42 ? 333 TRP C CZ3 1 
ATOM   12660 C CH2 . TRP D 1 304 ? 19.127  61.564  -29.960 1.00 129.35 ? 333 TRP C CH2 1 
ATOM   12661 N N   . ASN D 1 305 ? 21.518  58.132  -23.202 1.00 83.02  ? 334 ASN C N   1 
ATOM   12662 C CA  . ASN D 1 305 ? 22.407  56.995  -22.993 1.00 97.46  ? 334 ASN C CA  1 
ATOM   12663 C C   . ASN D 1 305 ? 21.639  55.668  -23.069 1.00 106.85 ? 334 ASN C C   1 
ATOM   12664 O O   . ASN D 1 305 ? 22.259  54.644  -23.353 1.00 111.17 ? 334 ASN C O   1 
ATOM   12665 C CB  . ASN D 1 305 ? 23.298  57.117  -21.754 1.00 111.26 ? 334 ASN C CB  1 
ATOM   12666 C CG  . ASN D 1 305 ? 22.604  57.639  -20.517 1.00 132.88 ? 334 ASN C CG  1 
ATOM   12667 O OD1 . ASN D 1 305 ? 22.993  58.688  -19.990 1.00 140.68 ? 334 ASN C OD1 1 
ATOM   12668 N ND2 . ASN D 1 305 ? 21.622  56.911  -20.007 1.00 146.81 ? 334 ASN C ND2 1 
ATOM   12669 N N   . THR D 1 306 ? 20.312  55.672  -22.835 1.00 105.71 ? 335 THR C N   1 
ATOM   12670 C CA  . THR D 1 306 ? 19.496  54.466  -22.979 1.00 95.59  ? 335 THR C CA  1 
ATOM   12671 C C   . THR D 1 306 ? 19.389  54.126  -24.464 1.00 93.06  ? 335 THR C C   1 
ATOM   12672 O O   . THR D 1 306 ? 19.802  53.056  -24.907 1.00 83.55  ? 335 THR C O   1 
ATOM   12673 C CB  . THR D 1 306 ? 18.110  54.641  -22.342 1.00 91.78  ? 335 THR C CB  1 
ATOM   12674 O OG1 . THR D 1 306 ? 18.196  54.322  -20.957 1.00 91.16  ? 335 THR C OG1 1 
ATOM   12675 C CG2 . THR D 1 306 ? 17.051  53.703  -22.895 1.00 89.00  ? 335 THR C CG2 1 
ATOM   12676 N N   . LEU D 1 307 ? 18.834  55.067  -25.228 1.00 98.07  ? 336 LEU C N   1 
ATOM   12677 C CA  . LEU D 1 307 ? 18.653  54.881  -26.657 1.00 108.76 ? 336 LEU C CA  1 
ATOM   12678 C C   . LEU D 1 307 ? 20.003  54.520  -27.278 1.00 107.88 ? 336 LEU C C   1 
ATOM   12679 O O   . LEU D 1 307 ? 20.129  53.462  -27.894 1.00 99.36  ? 336 LEU C O   1 
ATOM   12680 C CB  . LEU D 1 307 ? 18.048  56.138  -27.284 1.00 115.50 ? 336 LEU C CB  1 
ATOM   12681 C CG  . LEU D 1 307 ? 16.880  56.785  -26.529 1.00 123.80 ? 336 LEU C CG  1 
ATOM   12682 C CD1 . LEU D 1 307 ? 16.371  58.019  -27.262 1.00 128.54 ? 336 LEU C CD1 1 
ATOM   12683 C CD2 . LEU D 1 307 ? 15.755  55.791  -26.284 1.00 123.28 ? 336 LEU C CD2 1 
ATOM   12684 N N   . ASN D 1 308 ? 21.013  55.380  -27.049 1.00 106.86 ? 337 ASN C N   1 
ATOM   12685 C CA  . ASN D 1 308 ? 22.314  55.288  -27.702 1.00 100.54 ? 337 ASN C CA  1 
ATOM   12686 C C   . ASN D 1 308 ? 22.960  53.928  -27.439 1.00 98.33  ? 337 ASN C C   1 
ATOM   12687 O O   . ASN D 1 308 ? 23.706  53.435  -28.285 1.00 91.66  ? 337 ASN C O   1 
ATOM   12688 C CB  . ASN D 1 308 ? 23.282  56.396  -27.285 1.00 102.59 ? 337 ASN C CB  1 
ATOM   12689 C CG  . ASN D 1 308 ? 22.900  57.771  -27.794 1.00 103.90 ? 337 ASN C CG  1 
ATOM   12690 O OD1 . ASN D 1 308 ? 22.509  57.927  -28.957 1.00 112.30 ? 337 ASN C OD1 1 
ATOM   12691 N ND2 . ASN D 1 308 ? 23.014  58.787  -26.950 1.00 96.33  ? 337 ASN C ND2 1 
ATOM   12692 N N   . SER D 1 309 ? 22.686  53.328  -26.269 1.00 95.04  ? 338 SER C N   1 
ATOM   12693 C CA  . SER D 1 309 ? 23.201  51.998  -25.972 1.00 86.26  ? 338 SER C CA  1 
ATOM   12694 C C   . SER D 1 309 ? 22.202  50.931  -26.418 1.00 82.22  ? 338 SER C C   1 
ATOM   12695 O O   . SER D 1 309 ? 22.266  49.805  -25.942 1.00 79.38  ? 338 SER C O   1 
ATOM   12696 C CB  . SER D 1 309 ? 23.556  51.844  -24.513 1.00 83.83  ? 338 SER C CB  1 
ATOM   12697 O OG  . SER D 1 309 ? 22.422  51.501  -23.733 1.00 82.44  ? 338 SER C OG  1 
ATOM   12698 N N   . GLY D 1 310 ? 21.280  51.299  -27.323 1.00 86.06  ? 339 GLY C N   1 
ATOM   12699 C CA  . GLY D 1 310 ? 20.383  50.359  -27.981 1.00 80.00  ? 339 GLY C CA  1 
ATOM   12700 C C   . GLY D 1 310 ? 19.257  49.890  -27.064 1.00 77.53  ? 339 GLY C C   1 
ATOM   12701 O O   . GLY D 1 310 ? 18.796  48.760  -27.180 1.00 66.18  ? 339 GLY C O   1 
ATOM   12702 N N   . ARG D 1 311 ? 18.810  50.757  -26.152 1.00 81.48  ? 340 ARG C N   1 
ATOM   12703 C CA  . ARG D 1 311 ? 17.805  50.362  -25.178 1.00 83.25  ? 340 ARG C CA  1 
ATOM   12704 C C   . ARG D 1 311 ? 16.533  51.151  -25.468 1.00 79.11  ? 340 ARG C C   1 
ATOM   12705 O O   . ARG D 1 311 ? 16.566  52.106  -26.242 1.00 75.57  ? 340 ARG C O   1 
ATOM   12706 C CB  . ARG D 1 311 ? 18.347  50.474  -23.745 1.00 87.73  ? 340 ARG C CB  1 
ATOM   12707 C CG  . ARG D 1 311 ? 19.480  49.510  -23.404 1.00 91.92  ? 340 ARG C CG  1 
ATOM   12708 C CD  . ARG D 1 311 ? 19.878  49.475  -21.919 1.00 94.25  ? 340 ARG C CD  1 
ATOM   12709 N NE  . ARG D 1 311 ? 20.965  50.396  -21.553 1.00 101.77 ? 340 ARG C NE  1 
ATOM   12710 C CZ  . ARG D 1 311 ? 20.981  51.296  -20.560 1.00 100.92 ? 340 ARG C CZ  1 
ATOM   12711 N NH1 . ARG D 1 311 ? 22.067  52.032  -20.363 1.00 95.52  ? 340 ARG C NH1 1 
ATOM   12712 N NH2 . ARG D 1 311 ? 19.932  51.464  -19.768 1.00 94.32  ? 340 ARG C NH2 1 
ATOM   12713 N N   . VAL D 1 312 ? 15.417  50.708  -24.867 1.00 75.79  ? 341 VAL C N   1 
ATOM   12714 C CA  . VAL D 1 312 ? 14.089  51.210  -25.201 1.00 73.48  ? 341 VAL C CA  1 
ATOM   12715 C C   . VAL D 1 312 ? 13.496  51.849  -23.946 1.00 63.54  ? 341 VAL C C   1 
ATOM   12716 O O   . VAL D 1 312 ? 13.686  51.355  -22.834 1.00 59.73  ? 341 VAL C O   1 
ATOM   12717 C CB  . VAL D 1 312 ? 13.160  50.116  -25.786 1.00 73.07  ? 341 VAL C CB  1 
ATOM   12718 C CG1 . VAL D 1 312 ? 12.380  49.357  -24.713 1.00 73.79  ? 341 VAL C CG1 1 
ATOM   12719 C CG2 . VAL D 1 312 ? 12.199  50.672  -26.838 1.00 72.60  ? 341 VAL C CG2 1 
ATOM   12720 N N   . VAL D 1 313 ? 12.793  52.969  -24.133 1.00 55.10  ? 342 VAL C N   1 
ATOM   12721 C CA  . VAL D 1 313 ? 12.076  53.591  -23.034 1.00 58.35  ? 342 VAL C CA  1 
ATOM   12722 C C   . VAL D 1 313 ? 10.735  52.857  -22.902 1.00 57.87  ? 342 VAL C C   1 
ATOM   12723 O O   . VAL D 1 313 ? 9.849   52.970  -23.764 1.00 48.97  ? 342 VAL C O   1 
ATOM   12724 C CB  . VAL D 1 313 ? 11.928  55.125  -23.164 1.00 61.40  ? 342 VAL C CB  1 
ATOM   12725 C CG1 . VAL D 1 313 ? 11.090  55.747  -22.042 1.00 59.49  ? 342 VAL C CG1 1 
ATOM   12726 C CG2 . VAL D 1 313 ? 13.293  55.797  -23.218 1.00 57.43  ? 342 VAL C CG2 1 
ATOM   12727 N N   . PRO D 1 314 ? 10.547  52.090  -21.799 1.00 51.71  ? 343 PRO C N   1 
ATOM   12728 C CA  . PRO D 1 314 ? 9.340   51.286  -21.608 1.00 55.20  ? 343 PRO C CA  1 
ATOM   12729 C C   . PRO D 1 314 ? 8.088   52.158  -21.531 1.00 48.39  ? 343 PRO C C   1 
ATOM   12730 O O   . PRO D 1 314 ? 8.135   53.277  -21.001 1.00 36.80  ? 343 PRO C O   1 
ATOM   12731 C CB  . PRO D 1 314 ? 9.631   50.546  -20.283 1.00 59.20  ? 343 PRO C CB  1 
ATOM   12732 C CG  . PRO D 1 314 ? 11.135  50.636  -20.136 1.00 58.17  ? 343 PRO C CG  1 
ATOM   12733 C CD  . PRO D 1 314 ? 11.436  52.028  -20.626 1.00 54.31  ? 343 PRO C CD  1 
ATOM   12734 N N   . GLY D 1 315 ? 7.005   51.645  -22.136 1.00 41.89  ? 344 GLY C N   1 
ATOM   12735 C CA  . GLY D 1 315 ? 5.727   52.335  -22.192 1.00 44.69  ? 344 GLY C CA  1 
ATOM   12736 C C   . GLY D 1 315 ? 5.657   53.500  -23.194 1.00 44.27  ? 344 GLY C C   1 
ATOM   12737 O O   . GLY D 1 315 ? 4.665   54.223  -23.171 1.00 42.71  ? 344 GLY C O   1 
ATOM   12738 N N   . TYR D 1 316 ? 6.674   53.697  -24.056 1.00 46.59  ? 345 TYR C N   1 
ATOM   12739 C CA  . TYR D 1 316 ? 6.581   54.640  -25.172 1.00 52.35  ? 345 TYR C CA  1 
ATOM   12740 C C   . TYR D 1 316 ? 6.646   53.845  -26.474 1.00 55.25  ? 345 TYR C C   1 
ATOM   12741 O O   . TYR D 1 316 ? 7.540   53.019  -26.653 1.00 59.32  ? 345 TYR C O   1 
ATOM   12742 C CB  . TYR D 1 316 ? 7.648   55.747  -25.161 1.00 50.05  ? 345 TYR C CB  1 
ATOM   12743 C CG  . TYR D 1 316 ? 7.367   56.867  -24.168 1.00 51.12  ? 345 TYR C CG  1 
ATOM   12744 C CD1 . TYR D 1 316 ? 7.523   56.674  -22.803 1.00 52.50  ? 345 TYR C CD1 1 
ATOM   12745 C CD2 . TYR D 1 316 ? 6.944   58.123  -24.590 1.00 50.92  ? 345 TYR C CD2 1 
ATOM   12746 C CE1 . TYR D 1 316 ? 7.281   57.698  -21.897 1.00 57.16  ? 345 TYR C CE1 1 
ATOM   12747 C CE2 . TYR D 1 316 ? 6.701   59.152  -23.699 1.00 47.47  ? 345 TYR C CE2 1 
ATOM   12748 C CZ  . TYR D 1 316 ? 6.864   58.941  -22.339 1.00 49.45  ? 345 TYR C CZ  1 
ATOM   12749 O OH  . TYR D 1 316 ? 6.582   59.940  -21.438 1.00 54.16  ? 345 TYR C OH  1 
ATOM   12750 N N   . GLY D 1 317 ? 5.712   54.104  -27.395 1.00 56.70  ? 346 GLY C N   1 
ATOM   12751 C CA  . GLY D 1 317 ? 5.601   53.283  -28.593 1.00 56.83  ? 346 GLY C CA  1 
ATOM   12752 C C   . GLY D 1 317 ? 4.322   52.444  -28.570 1.00 62.01  ? 346 GLY C C   1 
ATOM   12753 O O   . GLY D 1 317 ? 3.686   52.307  -27.522 1.00 65.22  ? 346 GLY C O   1 
ATOM   12754 N N   . HIS D 1 318 ? 3.951   51.905  -29.743 1.00 51.71  ? 347 HIS C N   1 
ATOM   12755 C CA  . HIS D 1 318 ? 2.799   51.035  -29.885 1.00 51.89  ? 347 HIS C CA  1 
ATOM   12756 C C   . HIS D 1 318 ? 2.870   50.374  -31.259 1.00 54.26  ? 347 HIS C C   1 
ATOM   12757 O O   . HIS D 1 318 ? 3.470   50.912  -32.187 1.00 50.15  ? 347 HIS C O   1 
ATOM   12758 C CB  . HIS D 1 318 ? 1.493   51.822  -29.674 1.00 47.67  ? 347 HIS C CB  1 
ATOM   12759 C CG  . HIS D 1 318 ? 0.318   51.008  -29.242 1.00 45.99  ? 347 HIS C CG  1 
ATOM   12760 N ND1 . HIS D 1 318 ? 0.213   50.519  -27.951 1.00 53.08  ? 347 HIS C ND1 1 
ATOM   12761 C CD2 . HIS D 1 318 ? -0.800  50.605  -29.870 1.00 48.11  ? 347 HIS C CD2 1 
ATOM   12762 C CE1 . HIS D 1 318 ? -0.934  49.840  -27.824 1.00 55.27  ? 347 HIS C CE1 1 
ATOM   12763 N NE2 . HIS D 1 318 ? -1.568  49.873  -28.978 1.00 48.22  ? 347 HIS C NE2 1 
ATOM   12764 N N   . ALA D 1 319 ? 2.189   49.237  -31.400 1.00 59.17  ? 348 ALA C N   1 
ATOM   12765 C CA  . ALA D 1 319 ? 2.099   48.544  -32.682 1.00 61.80  ? 348 ALA C CA  1 
ATOM   12766 C C   . ALA D 1 319 ? 1.186   49.290  -33.668 1.00 55.46  ? 348 ALA C C   1 
ATOM   12767 O O   . ALA D 1 319 ? 1.353   49.166  -34.876 1.00 58.94  ? 348 ALA C O   1 
ATOM   12768 C CB  . ALA D 1 319 ? 1.619   47.126  -32.448 1.00 62.14  ? 348 ALA C CB  1 
ATOM   12769 N N   . VAL D 1 320 ? 0.220   50.067  -33.156 1.00 58.90  ? 349 VAL C N   1 
ATOM   12770 C CA  . VAL D 1 320 ? -0.800  50.696  -33.993 1.00 65.15  ? 349 VAL C CA  1 
ATOM   12771 C C   . VAL D 1 320 ? -0.916  52.202  -33.706 1.00 59.15  ? 349 VAL C C   1 
ATOM   12772 O O   . VAL D 1 320 ? -0.965  53.001  -34.645 1.00 62.05  ? 349 VAL C O   1 
ATOM   12773 C CB  . VAL D 1 320 ? -2.161  49.971  -33.868 1.00 62.69  ? 349 VAL C CB  1 
ATOM   12774 C CG1 . VAL D 1 320 ? -2.196  48.975  -32.715 1.00 63.65  ? 349 VAL C CG1 1 
ATOM   12775 C CG2 . VAL D 1 320 ? -3.338  50.937  -33.799 1.00 65.49  ? 349 VAL C CG2 1 
ATOM   12776 N N   . LEU D 1 321 ? -1.013  52.578  -32.419 1.00 53.65  ? 350 LEU C N   1 
ATOM   12777 C CA  . LEU D 1 321 ? -1.171  53.966  -32.010 1.00 50.75  ? 350 LEU C CA  1 
ATOM   12778 C C   . LEU D 1 321 ? -0.007  54.798  -32.544 1.00 47.49  ? 350 LEU C C   1 
ATOM   12779 O O   . LEU D 1 321 ? 1.153   54.411  -32.384 1.00 43.15  ? 350 LEU C O   1 
ATOM   12780 C CB  . LEU D 1 321 ? -1.271  54.093  -30.491 1.00 49.20  ? 350 LEU C CB  1 
ATOM   12781 C CG  . LEU D 1 321 ? -2.682  54.081  -29.899 1.00 56.75  ? 350 LEU C CG  1 
ATOM   12782 C CD1 . LEU D 1 321 ? -2.593  53.937  -28.371 1.00 54.40  ? 350 LEU C CD1 1 
ATOM   12783 C CD2 . LEU D 1 321 ? -3.463  55.329  -30.300 1.00 54.18  ? 350 LEU C CD2 1 
ATOM   12784 N N   . ARG D 1 322 ? -0.351  55.947  -33.147 1.00 53.25  ? 351 ARG C N   1 
ATOM   12785 C CA  . ARG D 1 322 ? 0.605   56.841  -33.791 1.00 59.99  ? 351 ARG C CA  1 
ATOM   12786 C C   . ARG D 1 322 ? 0.800   58.127  -32.976 1.00 60.86  ? 351 ARG C C   1 
ATOM   12787 O O   . ARG D 1 322 ? 1.777   58.848  -33.199 1.00 56.05  ? 351 ARG C O   1 
ATOM   12788 C CB  . ARG D 1 322 ? 0.098   57.242  -35.180 1.00 63.44  ? 351 ARG C CB  1 
ATOM   12789 C CG  . ARG D 1 322 ? -0.603  56.158  -35.988 1.00 79.03  ? 351 ARG C CG  1 
ATOM   12790 C CD  . ARG D 1 322 ? 0.343   55.256  -36.765 1.00 85.45  ? 351 ARG C CD  1 
ATOM   12791 N NE  . ARG D 1 322 ? 1.325   54.599  -35.893 1.00 89.32  ? 351 ARG C NE  1 
ATOM   12792 C CZ  . ARG D 1 322 ? 2.593   54.961  -35.713 1.00 95.42  ? 351 ARG C CZ  1 
ATOM   12793 N NH1 . ARG D 1 322 ? 3.379   54.202  -34.972 1.00 102.83 ? 351 ARG C NH1 1 
ATOM   12794 N NH2 . ARG D 1 322 ? 3.084   56.061  -36.263 1.00 102.19 ? 351 ARG C NH2 1 
ATOM   12795 N N   . LYS D 1 323 ? -0.146  58.411  -32.064 1.00 55.00  ? 352 LYS C N   1 
ATOM   12796 C CA  . LYS D 1 323 ? -0.102  59.581  -31.195 1.00 54.78  ? 352 LYS C CA  1 
ATOM   12797 C C   . LYS D 1 323 ? -0.307  59.129  -29.748 1.00 57.22  ? 352 LYS C C   1 
ATOM   12798 O O   . LYS D 1 323 ? -0.319  57.919  -29.478 1.00 49.92  ? 352 LYS C O   1 
ATOM   12799 C CB  . LYS D 1 323 ? -1.125  60.619  -31.678 1.00 51.86  ? 352 LYS C CB  1 
ATOM   12800 C CG  . LYS D 1 323 ? -0.624  61.392  -32.885 1.00 59.98  ? 352 LYS C CG  1 
ATOM   12801 C CD  . LYS D 1 323 ? -1.392  62.668  -33.203 1.00 74.00  ? 352 LYS C CD  1 
ATOM   12802 C CE  . LYS D 1 323 ? -2.639  62.432  -34.000 1.00 78.71  ? 352 LYS C CE  1 
ATOM   12803 N NZ  . LYS D 1 323 ? -3.484  63.624  -34.114 1.00 81.29  ? 352 LYS C NZ  1 
ATOM   12804 N N   . THR D 1 324 ? -0.470  60.123  -28.855 1.00 57.15  ? 353 THR C N   1 
ATOM   12805 C CA  . THR D 1 324 ? -0.625  59.943  -27.415 1.00 59.13  ? 353 THR C CA  1 
ATOM   12806 C C   . THR D 1 324 ? -1.900  59.158  -27.122 1.00 52.97  ? 353 THR C C   1 
ATOM   12807 O O   . THR D 1 324 ? -3.010  59.577  -27.453 1.00 49.98  ? 353 THR C O   1 
ATOM   12808 C CB  . THR D 1 324 ? -0.612  61.303  -26.694 1.00 54.91  ? 353 THR C CB  1 
ATOM   12809 O OG1 . THR D 1 324 ? 0.778   61.463  -26.436 1.00 57.68  ? 353 THR C OG1 1 
ATOM   12810 C CG2 . THR D 1 324 ? -1.307  61.345  -25.339 1.00 57.69  ? 353 THR C CG2 1 
ATOM   12811 N N   . ASP D 1 325 ? -1.703  58.026  -26.449 1.00 53.44  ? 354 ASP C N   1 
ATOM   12812 C CA  . ASP D 1 325 ? -2.784  57.172  -25.993 1.00 52.51  ? 354 ASP C CA  1 
ATOM   12813 C C   . ASP D 1 325 ? -3.696  57.958  -25.037 1.00 45.20  ? 354 ASP C C   1 
ATOM   12814 O O   . ASP D 1 325 ? -3.230  58.376  -23.990 1.00 43.12  ? 354 ASP C O   1 
ATOM   12815 C CB  . ASP D 1 325 ? -2.162  55.923  -25.381 1.00 48.24  ? 354 ASP C CB  1 
ATOM   12816 C CG  . ASP D 1 325 ? -3.152  54.843  -24.975 1.00 55.16  ? 354 ASP C CG  1 
ATOM   12817 O OD1 . ASP D 1 325 ? -4.376  55.097  -25.131 1.00 50.70  ? 354 ASP C OD1 1 
ATOM   12818 O OD2 . ASP D 1 325 ? -2.693  53.755  -24.539 1.00 50.53  ? 354 ASP C OD2 1 
ATOM   12819 N N   . PRO D 1 326 ? -5.005  58.204  -25.336 1.00 45.93  ? 355 PRO C N   1 
ATOM   12820 C CA  . PRO D 1 326 ? -5.914  58.876  -24.389 1.00 46.81  ? 355 PRO C CA  1 
ATOM   12821 C C   . PRO D 1 326 ? -6.106  58.146  -23.055 1.00 45.91  ? 355 PRO C C   1 
ATOM   12822 O O   . PRO D 1 326 ? -6.595  58.711  -22.077 1.00 38.86  ? 355 PRO C O   1 
ATOM   12823 C CB  . PRO D 1 326 ? -7.262  58.947  -25.159 1.00 42.79  ? 355 PRO C CB  1 
ATOM   12824 C CG  . PRO D 1 326 ? -7.163  57.828  -26.173 1.00 44.67  ? 355 PRO C CG  1 
ATOM   12825 C CD  . PRO D 1 326 ? -5.693  57.856  -26.595 1.00 48.39  ? 355 PRO C CD  1 
ATOM   12826 N N   . ARG D 1 327 ? -5.778  56.850  -23.026 1.00 42.87  ? 356 ARG C N   1 
ATOM   12827 C CA  . ARG D 1 327 ? -5.814  56.145  -21.752 1.00 44.36  ? 356 ARG C CA  1 
ATOM   12828 C C   . ARG D 1 327 ? -4.771  56.787  -20.835 1.00 46.47  ? 356 ARG C C   1 
ATOM   12829 O O   . ARG D 1 327 ? -5.034  57.001  -19.644 1.00 47.90  ? 356 ARG C O   1 
ATOM   12830 C CB  . ARG D 1 327 ? -5.627  54.647  -22.011 1.00 40.76  ? 356 ARG C CB  1 
ATOM   12831 C CG  . ARG D 1 327 ? -6.716  54.042  -22.885 1.00 37.45  ? 356 ARG C CG  1 
ATOM   12832 C CD  . ARG D 1 327 ? -6.483  52.570  -23.111 1.00 33.76  ? 356 ARG C CD  1 
ATOM   12833 N NE  . ARG D 1 327 ? -5.276  52.388  -23.927 1.00 35.83  ? 356 ARG C NE  1 
ATOM   12834 C CZ  . ARG D 1 327 ? -4.730  51.200  -24.150 1.00 40.46  ? 356 ARG C CZ  1 
ATOM   12835 N NH1 . ARG D 1 327 ? -5.314  50.124  -23.650 1.00 36.87  ? 356 ARG C NH1 1 
ATOM   12836 N NH2 . ARG D 1 327 ? -3.613  51.071  -24.857 1.00 39.38  ? 356 ARG C NH2 1 
ATOM   12837 N N   . TYR D 1 328 ? -3.616  57.132  -21.439 1.00 43.54  ? 357 TYR C N   1 
ATOM   12838 C CA  . TYR D 1 328 ? -2.530  57.845  -20.769 1.00 51.48  ? 357 TYR C CA  1 
ATOM   12839 C C   . TYR D 1 328 ? -2.977  59.243  -20.334 1.00 45.13  ? 357 TYR C C   1 
ATOM   12840 O O   . TYR D 1 328 ? -2.746  59.610  -19.193 1.00 41.15  ? 357 TYR C O   1 
ATOM   12841 C CB  . TYR D 1 328 ? -1.254  57.992  -21.611 1.00 50.32  ? 357 TYR C CB  1 
ATOM   12842 C CG  . TYR D 1 328 ? -0.152  58.744  -20.880 1.00 71.29  ? 357 TYR C CG  1 
ATOM   12843 C CD1 . TYR D 1 328 ? -0.208  60.133  -20.737 1.00 78.12  ? 357 TYR C CD1 1 
ATOM   12844 C CD2 . TYR D 1 328 ? 0.929   58.070  -20.313 1.00 73.82  ? 357 TYR C CD2 1 
ATOM   12845 C CE1 . TYR D 1 328 ? 0.774   60.828  -20.048 1.00 81.60  ? 357 TYR C CE1 1 
ATOM   12846 C CE2 . TYR D 1 328 ? 1.920   58.759  -19.625 1.00 78.97  ? 357 TYR C CE2 1 
ATOM   12847 C CZ  . TYR D 1 328 ? 1.841   60.141  -19.492 1.00 76.22  ? 357 TYR C CZ  1 
ATOM   12848 O OH  . TYR D 1 328 ? 2.793   60.850  -18.813 1.00 64.97  ? 357 TYR C OH  1 
ATOM   12849 N N   . THR D 1 329 ? -3.602  60.016  -21.237 1.00 47.60  ? 358 THR C N   1 
ATOM   12850 C CA  . THR D 1 329 ? -4.059  61.360  -20.895 1.00 47.30  ? 358 THR C CA  1 
ATOM   12851 C C   . THR D 1 329 ? -4.949  61.284  -19.670 1.00 46.35  ? 358 THR C C   1 
ATOM   12852 O O   . THR D 1 329 ? -4.827  62.066  -18.741 1.00 47.61  ? 358 THR C O   1 
ATOM   12853 C CB  . THR D 1 329 ? -4.857  62.005  -22.031 1.00 52.17  ? 358 THR C CB  1 
ATOM   12854 O OG1 . THR D 1 329 ? -3.977  62.174  -23.140 1.00 50.67  ? 358 THR C OG1 1 
ATOM   12855 C CG2 . THR D 1 329 ? -5.489  63.319  -21.597 1.00 47.15  ? 358 THR C CG2 1 
ATOM   12856 N N   . CYS D 1 330 ? -5.921  60.385  -19.770 1.00 47.52  ? 359 CYS C N   1 
ATOM   12857 C CA  . CYS D 1 330 ? -6.946  60.193  -18.768 1.00 47.32  ? 359 CYS C CA  1 
ATOM   12858 C C   . CYS D 1 330 ? -6.383  59.977  -17.350 1.00 46.78  ? 359 CYS C C   1 
ATOM   12859 O O   . CYS D 1 330 ? -6.939  60.431  -16.353 1.00 40.05  ? 359 CYS C O   1 
ATOM   12860 C CB  . CYS D 1 330 ? -7.734  58.997  -19.261 1.00 61.25  ? 359 CYS C CB  1 
ATOM   12861 S SG  . CYS D 1 330 ? -8.881  58.417  -18.011 1.00 69.12  ? 359 CYS C SG  1 
ATOM   12862 N N   . GLN D 1 331 ? -5.305  59.198  -17.231 1.00 45.36  ? 360 GLN C N   1 
ATOM   12863 C CA  . GLN D 1 331 ? -4.724  58.909  -15.922 1.00 48.23  ? 360 GLN C CA  1 
ATOM   12864 C C   . GLN D 1 331 ? -3.883  60.097  -15.460 1.00 44.35  ? 360 GLN C C   1 
ATOM   12865 O O   . GLN D 1 331 ? -3.964  60.521  -14.305 1.00 43.67  ? 360 GLN C O   1 
ATOM   12866 C CB  . GLN D 1 331 ? -3.896  57.625  -15.993 1.00 50.76  ? 360 GLN C CB  1 
ATOM   12867 C CG  . GLN D 1 331 ? -4.716  56.343  -16.114 1.00 49.92  ? 360 GLN C CG  1 
ATOM   12868 C CD  . GLN D 1 331 ? -3.833  55.117  -16.058 1.00 52.57  ? 360 GLN C CD  1 
ATOM   12869 O OE1 . GLN D 1 331 ? -3.792  54.402  -15.051 1.00 58.96  ? 360 GLN C OE1 1 
ATOM   12870 N NE2 . GLN D 1 331 ? -3.062  54.909  -17.120 1.00 58.98  ? 360 GLN C NE2 1 
ATOM   12871 N N   . ARG D 1 332 ? -3.113  60.660  -16.399 1.00 45.78  ? 361 ARG C N   1 
ATOM   12872 C CA  . ARG D 1 332 ? -2.434  61.928  -16.155 1.00 54.86  ? 361 ARG C CA  1 
ATOM   12873 C C   . ARG D 1 332 ? -3.370  62.943  -15.486 1.00 48.38  ? 361 ARG C C   1 
ATOM   12874 O O   . ARG D 1 332 ? -2.962  63.637  -14.565 1.00 49.64  ? 361 ARG C O   1 
ATOM   12875 C CB  . ARG D 1 332 ? -1.797  62.458  -17.444 1.00 56.94  ? 361 ARG C CB  1 
ATOM   12876 C CG  . ARG D 1 332 ? -1.396  63.925  -17.344 1.00 66.08  ? 361 ARG C CG  1 
ATOM   12877 C CD  . ARG D 1 332 ? -0.561  64.331  -18.538 1.00 66.77  ? 361 ARG C CD  1 
ATOM   12878 N NE  . ARG D 1 332 ? 0.175   65.592  -18.387 1.00 73.58  ? 361 ARG C NE  1 
ATOM   12879 C CZ  . ARG D 1 332 ? 1.222   65.793  -17.592 1.00 66.69  ? 361 ARG C CZ  1 
ATOM   12880 N NH1 . ARG D 1 332 ? 2.113   66.700  -17.919 1.00 77.12  ? 361 ARG C NH1 1 
ATOM   12881 N NH2 . ARG D 1 332 ? 1.477   65.011  -16.565 1.00 62.66  ? 361 ARG C NH2 1 
ATOM   12882 N N   . GLU D 1 333 ? -4.636  63.019  -15.911 1.00 55.05  ? 362 GLU C N   1 
ATOM   12883 C CA  . GLU D 1 333 ? -5.543  64.038  -15.400 1.00 52.99  ? 362 GLU C CA  1 
ATOM   12884 C C   . GLU D 1 333 ? -6.003  63.707  -13.988 1.00 48.14  ? 362 GLU C C   1 
ATOM   12885 O O   . GLU D 1 333 ? -6.264  64.593  -13.181 1.00 45.97  ? 362 GLU C O   1 
ATOM   12886 C CB  . GLU D 1 333 ? -6.786  64.165  -16.273 1.00 61.31  ? 362 GLU C CB  1 
ATOM   12887 C CG  . GLU D 1 333 ? -6.493  64.729  -17.657 1.00 65.20  ? 362 GLU C CG  1 
ATOM   12888 C CD  . GLU D 1 333 ? -7.777  64.935  -18.435 1.00 75.32  ? 362 GLU C CD  1 
ATOM   12889 O OE1 . GLU D 1 333 ? -8.414  63.931  -18.827 1.00 77.43  ? 362 GLU C OE1 1 
ATOM   12890 O OE2 . GLU D 1 333 ? -8.161  66.112  -18.591 1.00 82.77  ? 362 GLU C OE2 1 
ATOM   12891 N N   . PHE D 1 334 ? -6.198  62.416  -13.736 1.00 44.59  ? 363 PHE C N   1 
ATOM   12892 C CA  . PHE D 1 334 ? -6.549  61.954  -12.412 1.00 45.10  ? 363 PHE C CA  1 
ATOM   12893 C C   . PHE D 1 334 ? -5.398  62.282  -11.465 1.00 41.58  ? 363 PHE C C   1 
ATOM   12894 O O   . PHE D 1 334 ? -5.644  62.682  -10.335 1.00 40.71  ? 363 PHE C O   1 
ATOM   12895 C CB  . PHE D 1 334 ? -6.824  60.448  -12.429 1.00 49.19  ? 363 PHE C CB  1 
ATOM   12896 C CG  . PHE D 1 334 ? -7.168  59.853  -11.069 1.00 42.18  ? 363 PHE C CG  1 
ATOM   12897 C CD1 . PHE D 1 334 ? -6.175  59.549  -10.137 1.00 40.19  ? 363 PHE C CD1 1 
ATOM   12898 C CD2 . PHE D 1 334 ? -8.491  59.613  -10.727 1.00 38.50  ? 363 PHE C CD2 1 
ATOM   12899 C CE1 . PHE D 1 334 ? -6.519  59.024  -8.904  1.00 41.68  ? 363 PHE C CE1 1 
ATOM   12900 C CE2 . PHE D 1 334 ? -8.819  59.057  -9.509  1.00 39.76  ? 363 PHE C CE2 1 
ATOM   12901 C CZ  . PHE D 1 334 ? -7.836  58.772  -8.601  1.00 41.60  ? 363 PHE C CZ  1 
ATOM   12902 N N   . ALA D 1 335 ? -4.171  62.086  -11.934 1.00 44.50  ? 364 ALA C N   1 
ATOM   12903 C CA  . ALA D 1 335 ? -2.985  62.385  -11.103 1.00 51.78  ? 364 ALA C CA  1 
ATOM   12904 C C   . ALA D 1 335 ? -2.883  63.894  -10.874 1.00 60.30  ? 364 ALA C C   1 
ATOM   12905 O O   . ALA D 1 335 ? -2.842  64.315  -9.701  1.00 62.44  ? 364 ALA C O   1 
ATOM   12906 C CB  . ALA D 1 335 ? -1.752  61.837  -11.772 1.00 48.17  ? 364 ALA C CB  1 
ATOM   12907 N N   . LEU D 1 336 ? -2.956  64.696  -12.033 1.00 56.55  ? 365 LEU C N   1 
ATOM   12908 C CA  . LEU D 1 336 ? -2.745  66.156  -11.847 1.00 61.94  ? 365 LEU C CA  1 
ATOM   12909 C C   . LEU D 1 336 ? -3.826  66.760  -10.937 1.00 59.73  ? 365 LEU C C   1 
ATOM   12910 O O   . LEU D 1 336 ? -3.660  67.918  -10.545 1.00 73.40  ? 365 LEU C O   1 
ATOM   12911 C CB  . LEU D 1 336 ? -2.726  66.863  -13.199 1.00 61.87  ? 365 LEU C CB  1 
ATOM   12912 C CG  . LEU D 1 336 ? -1.451  66.689  -14.030 1.00 66.84  ? 365 LEU C CG  1 
ATOM   12913 C CD1 . LEU D 1 336 ? -1.649  67.164  -15.457 1.00 64.63  ? 365 LEU C CD1 1 
ATOM   12914 C CD2 . LEU D 1 336 ? -0.302  67.428  -13.381 1.00 65.29  ? 365 LEU C CD2 1 
ATOM   12915 N N   . LYS D 1 337 ? -4.812  65.939  -10.511 1.00 64.14  ? 366 LYS C N   1 
ATOM   12916 C CA  . LYS D 1 337 ? -5.819  66.474  -9.599  1.00 70.30  ? 366 LYS C CA  1 
ATOM   12917 C C   . LYS D 1 337 ? -5.816  65.832  -8.202  1.00 61.10  ? 366 LYS C C   1 
ATOM   12918 O O   . LYS D 1 337 ? -6.355  66.428  -7.283  1.00 57.64  ? 366 LYS C O   1 
ATOM   12919 C CB  . LYS D 1 337 ? -7.210  66.385  -10.245 1.00 78.92  ? 366 LYS C CB  1 
ATOM   12920 C CG  . LYS D 1 337 ? -8.026  65.136  -9.940  1.00 90.63  ? 366 LYS C CG  1 
ATOM   12921 C CD  . LYS D 1 337 ? -9.542  65.291  -10.079 1.00 102.74 ? 366 LYS C CD  1 
ATOM   12922 C CE  . LYS D 1 337 ? -10.106 64.878  -11.418 1.00 112.34 ? 366 LYS C CE  1 
ATOM   12923 N NZ  . LYS D 1 337 ? -9.995  65.894  -12.472 1.00 112.60 ? 366 LYS C NZ  1 
ATOM   12924 N N   . HIS D 1 338 ? -5.278  64.618  -8.011  1.00 58.71  ? 367 HIS C N   1 
ATOM   12925 C CA  . HIS D 1 338 ? -5.495  63.897  -6.756  1.00 59.08  ? 367 HIS C CA  1 
ATOM   12926 C C   . HIS D 1 338 ? -4.193  63.624  -5.996  1.00 52.35  ? 367 HIS C C   1 
ATOM   12927 O O   . HIS D 1 338 ? -4.230  63.376  -4.785  1.00 52.59  ? 367 HIS C O   1 
ATOM   12928 C CB  . HIS D 1 338 ? -6.207  62.561  -7.020  1.00 65.78  ? 367 HIS C CB  1 
ATOM   12929 C CG  . HIS D 1 338 ? -7.672  62.663  -7.274  1.00 72.53  ? 367 HIS C CG  1 
ATOM   12930 N ND1 . HIS D 1 338 ? -8.558  63.259  -6.399  1.00 76.83  ? 367 HIS C ND1 1 
ATOM   12931 C CD2 . HIS D 1 338 ? -8.409  62.197  -8.286  1.00 67.72  ? 367 HIS C CD2 1 
ATOM   12932 C CE1 . HIS D 1 338 ? -9.785  63.174  -6.895  1.00 74.68  ? 367 HIS C CE1 1 
ATOM   12933 N NE2 . HIS D 1 338 ? -9.716  62.531  -8.040  1.00 66.34  ? 367 HIS C NE2 1 
ATOM   12934 N N   . LEU D 1 339 ? -3.069  63.590  -6.725  1.00 49.58  ? 368 LEU C N   1 
ATOM   12935 C CA  . LEU D 1 339 ? -1.745  63.389  -6.141  1.00 49.44  ? 368 LEU C CA  1 
ATOM   12936 C C   . LEU D 1 339 ? -0.683  64.142  -6.954  1.00 45.86  ? 368 LEU C C   1 
ATOM   12937 O O   . LEU D 1 339 ? 0.295   63.580  -7.426  1.00 38.87  ? 368 LEU C O   1 
ATOM   12938 C CB  . LEU D 1 339 ? -1.468  61.886  -6.110  1.00 48.21  ? 368 LEU C CB  1 
ATOM   12939 C CG  . LEU D 1 339 ? -1.738  61.121  -7.416  1.00 49.10  ? 368 LEU C CG  1 
ATOM   12940 C CD1 . LEU D 1 339 ? -0.487  60.392  -7.905  1.00 48.25  ? 368 LEU C CD1 1 
ATOM   12941 C CD2 . LEU D 1 339 ? -2.890  60.133  -7.247  1.00 50.66  ? 368 LEU C CD2 1 
ATOM   12942 N N   . PRO D 1 340 ? -0.803  65.470  -7.154  1.00 58.39  ? 369 PRO C N   1 
ATOM   12943 C CA  . PRO D 1 340 ? 0.088   66.178  -8.088  1.00 57.70  ? 369 PRO C CA  1 
ATOM   12944 C C   . PRO D 1 340 ? 1.555   66.329  -7.670  1.00 60.19  ? 369 PRO C C   1 
ATOM   12945 O O   . PRO D 1 340 ? 2.410   66.574  -8.525  1.00 64.41  ? 369 PRO C O   1 
ATOM   12946 C CB  . PRO D 1 340 ? -0.608  67.556  -8.218  1.00 57.30  ? 369 PRO C CB  1 
ATOM   12947 C CG  . PRO D 1 340 ? -1.301  67.742  -6.881  1.00 57.82  ? 369 PRO C CG  1 
ATOM   12948 C CD  . PRO D 1 340 ? -1.747  66.349  -6.450  1.00 55.28  ? 369 PRO C CD  1 
ATOM   12949 N N   . ASN D 1 341 ? 1.834   66.199  -6.361  1.00 58.36  ? 370 ASN C N   1 
ATOM   12950 C CA  . ASN D 1 341 ? 3.165   66.417  -5.800  1.00 64.63  ? 370 ASN C CA  1 
ATOM   12951 C C   . ASN D 1 341 ? 3.891   65.101  -5.518  1.00 63.11  ? 370 ASN C C   1 
ATOM   12952 O O   . ASN D 1 341 ? 5.020   65.102  -5.022  1.00 60.78  ? 370 ASN C O   1 
ATOM   12953 C CB  . ASN D 1 341 ? 3.103   67.215  -4.501  1.00 69.82  ? 370 ASN C CB  1 
ATOM   12954 C CG  . ASN D 1 341 ? 2.283   68.477  -4.651  1.00 74.35  ? 370 ASN C CG  1 
ATOM   12955 O OD1 . ASN D 1 341 ? 2.458   69.222  -5.626  1.00 70.66  ? 370 ASN C OD1 1 
ATOM   12956 N ND2 . ASN D 1 341 ? 1.365   68.714  -3.723  1.00 73.14  ? 370 ASN C ND2 1 
ATOM   12957 N N   . ASP D 1 342 ? 3.241   63.970  -5.807  1.00 53.17  ? 371 ASP C N   1 
ATOM   12958 C CA  . ASP D 1 342 ? 3.890   62.691  -5.630  1.00 52.09  ? 371 ASP C CA  1 
ATOM   12959 C C   . ASP D 1 342 ? 5.149   62.670  -6.505  1.00 53.90  ? 371 ASP C C   1 
ATOM   12960 O O   . ASP D 1 342 ? 5.064   62.975  -7.696  1.00 56.64  ? 371 ASP C O   1 
ATOM   12961 C CB  . ASP D 1 342 ? 2.928   61.554  -5.923  1.00 52.75  ? 371 ASP C CB  1 
ATOM   12962 C CG  . ASP D 1 342 ? 3.594   60.198  -5.859  1.00 49.75  ? 371 ASP C CG  1 
ATOM   12963 O OD1 . ASP D 1 342 ? 3.836   59.731  -4.722  1.00 47.11  ? 371 ASP C OD1 1 
ATOM   12964 O OD2 . ASP D 1 342 ? 3.951   59.688  -6.945  1.00 54.72  ? 371 ASP C OD2 1 
ATOM   12965 N N   . PRO D 1 343 ? 6.350   62.383  -5.938  1.00 52.74  ? 372 PRO C N   1 
ATOM   12966 C CA  . PRO D 1 343 ? 7.607   62.462  -6.694  1.00 60.15  ? 372 PRO C CA  1 
ATOM   12967 C C   . PRO D 1 343 ? 7.669   61.530  -7.905  1.00 64.27  ? 372 PRO C C   1 
ATOM   12968 O O   . PRO D 1 343 ? 8.277   61.847  -8.935  1.00 60.48  ? 372 PRO C O   1 
ATOM   12969 C CB  . PRO D 1 343 ? 8.699   62.106  -5.644  1.00 60.24  ? 372 PRO C CB  1 
ATOM   12970 C CG  . PRO D 1 343 ? 8.033   62.335  -4.282  1.00 60.40  ? 372 PRO C CG  1 
ATOM   12971 C CD  . PRO D 1 343 ? 6.564   62.038  -4.517  1.00 55.78  ? 372 PRO C CD  1 
ATOM   12972 N N   . MET D 1 344 ? 7.039   60.359  -7.763  1.00 59.07  ? 373 MET C N   1 
ATOM   12973 C CA  . MET D 1 344 ? 7.022   59.373  -8.826  1.00 59.36  ? 373 MET C CA  1 
ATOM   12974 C C   . MET D 1 344 ? 6.210   59.913  -10.000 1.00 52.48  ? 373 MET C C   1 
ATOM   12975 O O   . MET D 1 344 ? 6.594   59.732  -11.154 1.00 42.72  ? 373 MET C O   1 
ATOM   12976 C CB  . MET D 1 344 ? 6.420   58.055  -8.329  1.00 66.43  ? 373 MET C CB  1 
ATOM   12977 C CG  . MET D 1 344 ? 7.333   57.271  -7.423  1.00 74.00  ? 373 MET C CG  1 
ATOM   12978 S SD  . MET D 1 344 ? 8.858   56.847  -8.283  1.00 85.11  ? 373 MET C SD  1 
ATOM   12979 C CE  . MET D 1 344 ? 8.313   56.212  -9.875  1.00 68.45  ? 373 MET C CE  1 
ATOM   12980 N N   . PHE D 1 345 ? 5.071   60.542  -9.685  1.00 47.88  ? 374 PHE C N   1 
ATOM   12981 C CA  . PHE D 1 345 ? 4.217   61.129  -10.702 1.00 52.71  ? 374 PHE C CA  1 
ATOM   12982 C C   . PHE D 1 345 ? 5.033   62.171  -11.465 1.00 50.14  ? 374 PHE C C   1 
ATOM   12983 O O   . PHE D 1 345 ? 5.199   62.070  -12.680 1.00 43.48  ? 374 PHE C O   1 
ATOM   12984 C CB  . PHE D 1 345 ? 2.947   61.691  -10.057 1.00 51.19  ? 374 PHE C CB  1 
ATOM   12985 C CG  . PHE D 1 345 ? 2.171   62.561  -11.030 1.00 60.78  ? 374 PHE C CG  1 
ATOM   12986 C CD1 . PHE D 1 345 ? 1.963   62.145  -12.346 1.00 56.88  ? 374 PHE C CD1 1 
ATOM   12987 C CD2 . PHE D 1 345 ? 1.695   63.808  -10.647 1.00 63.11  ? 374 PHE C CD2 1 
ATOM   12988 C CE1 . PHE D 1 345 ? 1.270   62.941  -13.238 1.00 55.86  ? 374 PHE C CE1 1 
ATOM   12989 C CE2 . PHE D 1 345 ? 1.004   64.603  -11.544 1.00 61.76  ? 374 PHE C CE2 1 
ATOM   12990 C CZ  . PHE D 1 345 ? 0.787   64.165  -12.832 1.00 64.01  ? 374 PHE C CZ  1 
ATOM   12991 N N   . LYS D 1 346 ? 5.603   63.124  -10.715 1.00 57.64  ? 375 LYS C N   1 
ATOM   12992 C CA  . LYS D 1 346 ? 6.448   64.168  -11.286 1.00 55.87  ? 375 LYS C CA  1 
ATOM   12993 C C   . LYS D 1 346 ? 7.493   63.565  -12.236 1.00 50.30  ? 375 LYS C C   1 
ATOM   12994 O O   . LYS D 1 346 ? 7.676   64.058  -13.350 1.00 50.84  ? 375 LYS C O   1 
ATOM   12995 C CB  . LYS D 1 346 ? 6.993   65.070  -10.172 1.00 54.52  ? 375 LYS C CB  1 
ATOM   12996 C CG  . LYS D 1 346 ? 5.967   66.056  -9.608  1.00 61.91  ? 375 LYS C CG  1 
ATOM   12997 C CD  . LYS D 1 346 ? 6.447   66.867  -8.402  1.00 70.76  ? 375 LYS C CD  1 
ATOM   12998 C CE  . LYS D 1 346 ? 5.617   68.105  -8.138  1.00 75.59  ? 375 LYS C CE  1 
ATOM   12999 N NZ  . LYS D 1 346 ? 5.870   68.750  -6.839  1.00 77.92  ? 375 LYS C NZ  1 
ATOM   13000 N N   . LEU D 1 347 ? 8.166   62.484  -11.842 1.00 48.50  ? 376 LEU C N   1 
ATOM   13001 C CA  . LEU D 1 347 ? 9.151   61.883  -12.734 1.00 48.30  ? 376 LEU C CA  1 
ATOM   13002 C C   . LEU D 1 347 ? 8.480   61.401  -14.034 1.00 55.26  ? 376 LEU C C   1 
ATOM   13003 O O   . LEU D 1 347 ? 9.082   61.480  -15.118 1.00 49.03  ? 376 LEU C O   1 
ATOM   13004 C CB  . LEU D 1 347 ? 9.922   60.763  -12.046 1.00 47.08  ? 376 LEU C CB  1 
ATOM   13005 C CG  . LEU D 1 347 ? 10.578  59.749  -12.998 1.00 51.64  ? 376 LEU C CG  1 
ATOM   13006 C CD1 . LEU D 1 347 ? 11.799  60.316  -13.718 1.00 52.74  ? 376 LEU C CD1 1 
ATOM   13007 C CD2 . LEU D 1 347 ? 10.945  58.482  -12.258 1.00 55.41  ? 376 LEU C CD2 1 
ATOM   13008 N N   . VAL D 1 348 ? 7.228   60.919  -13.930 1.00 51.57  ? 377 VAL C N   1 
ATOM   13009 C CA  . VAL D 1 348 ? 6.493   60.415  -15.081 1.00 54.49  ? 377 VAL C CA  1 
ATOM   13010 C C   . VAL D 1 348 ? 6.080   61.581  -15.988 1.00 54.58  ? 377 VAL C C   1 
ATOM   13011 O O   . VAL D 1 348 ? 6.204   61.468  -17.214 1.00 43.98  ? 377 VAL C O   1 
ATOM   13012 C CB  . VAL D 1 348 ? 5.291   59.522  -14.686 1.00 54.53  ? 377 VAL C CB  1 
ATOM   13013 C CG1 . VAL D 1 348 ? 4.150   59.533  -15.714 1.00 53.31  ? 377 VAL C CG1 1 
ATOM   13014 C CG2 . VAL D 1 348 ? 5.731   58.088  -14.420 1.00 51.25  ? 377 VAL C CG2 1 
ATOM   13015 N N   . ALA D 1 349 ? 5.557   62.673  -15.401 1.00 53.06  ? 378 ALA C N   1 
ATOM   13016 C CA  . ALA D 1 349 ? 5.201   63.858  -16.172 1.00 52.90  ? 378 ALA C CA  1 
ATOM   13017 C C   . ALA D 1 349 ? 6.442   64.403  -16.895 1.00 55.40  ? 378 ALA C C   1 
ATOM   13018 O O   . ALA D 1 349 ? 6.403   64.747  -18.073 1.00 56.12  ? 378 ALA C O   1 
ATOM   13019 C CB  . ALA D 1 349 ? 4.570   64.880  -15.245 1.00 57.82  ? 378 ALA C CB  1 
ATOM   13020 N N   . GLN D 1 350 ? 7.575   64.425  -16.190 1.00 57.26  ? 379 GLN C N   1 
ATOM   13021 C CA  . GLN D 1 350 ? 8.813   64.932  -16.749 1.00 63.41  ? 379 GLN C CA  1 
ATOM   13022 C C   . GLN D 1 350 ? 9.202   64.114  -17.980 1.00 66.93  ? 379 GLN C C   1 
ATOM   13023 O O   . GLN D 1 350 ? 9.558   64.671  -19.017 1.00 59.17  ? 379 GLN C O   1 
ATOM   13024 C CB  . GLN D 1 350 ? 9.957   64.911  -15.728 1.00 77.64  ? 379 GLN C CB  1 
ATOM   13025 C CG  . GLN D 1 350 ? 9.946   66.054  -14.712 1.00 76.89  ? 379 GLN C CG  1 
ATOM   13026 C CD  . GLN D 1 350 ? 11.275  66.263  -14.007 1.00 80.57  ? 379 GLN C CD  1 
ATOM   13027 O OE1 . GLN D 1 350 ? 12.281  65.580  -14.259 1.00 71.61  ? 379 GLN C OE1 1 
ATOM   13028 N NE2 . GLN D 1 350 ? 11.287  67.241  -13.109 1.00 86.73  ? 379 GLN C NE2 1 
ATOM   13029 N N   . LEU D 1 351 ? 9.176   62.784  -17.865 1.00 65.25  ? 380 LEU C N   1 
ATOM   13030 C CA  . LEU D 1 351 ? 9.483   61.942  -19.013 1.00 66.51  ? 380 LEU C CA  1 
ATOM   13031 C C   . LEU D 1 351 ? 8.593   62.303  -20.214 1.00 63.55  ? 380 LEU C C   1 
ATOM   13032 O O   . LEU D 1 351 ? 9.092   62.318  -21.345 1.00 48.48  ? 380 LEU C O   1 
ATOM   13033 C CB  . LEU D 1 351 ? 9.352   60.471  -18.621 1.00 73.65  ? 380 LEU C CB  1 
ATOM   13034 C CG  . LEU D 1 351 ? 10.394  59.935  -17.629 1.00 82.36  ? 380 LEU C CG  1 
ATOM   13035 C CD1 . LEU D 1 351 ? 10.070  58.508  -17.201 1.00 77.24  ? 380 LEU C CD1 1 
ATOM   13036 C CD2 . LEU D 1 351 ? 11.809  59.997  -18.191 1.00 83.02  ? 380 LEU C CD2 1 
ATOM   13037 N N   . TYR D 1 352 ? 7.294   62.587  -19.955 1.00 64.92  ? 381 TYR C N   1 
ATOM   13038 C CA  . TYR D 1 352 ? 6.308   63.016  -20.951 1.00 65.52  ? 381 TYR C CA  1 
ATOM   13039 C C   . TYR D 1 352 ? 6.789   64.298  -21.648 1.00 62.11  ? 381 TYR C C   1 
ATOM   13040 O O   . TYR D 1 352 ? 6.794   64.362  -22.880 1.00 46.29  ? 381 TYR C O   1 
ATOM   13041 C CB  . TYR D 1 352 ? 4.926   63.205  -20.297 1.00 60.91  ? 381 TYR C CB  1 
ATOM   13042 C CG  . TYR D 1 352 ? 3.745   63.562  -21.204 1.00 56.05  ? 381 TYR C CG  1 
ATOM   13043 C CD1 . TYR D 1 352 ? 3.616   63.001  -22.474 1.00 58.30  ? 381 TYR C CD1 1 
ATOM   13044 C CD2 . TYR D 1 352 ? 2.740   64.446  -20.788 1.00 50.28  ? 381 TYR C CD2 1 
ATOM   13045 C CE1 . TYR D 1 352 ? 2.545   63.316  -23.303 1.00 65.78  ? 381 TYR C CE1 1 
ATOM   13046 C CE2 . TYR D 1 352 ? 1.665   64.768  -21.609 1.00 51.50  ? 381 TYR C CE2 1 
ATOM   13047 C CZ  . TYR D 1 352 ? 1.569   64.205  -22.874 1.00 60.56  ? 381 TYR C CZ  1 
ATOM   13048 O OH  . TYR D 1 352 ? 0.532   64.463  -23.727 1.00 59.04  ? 381 TYR C OH  1 
ATOM   13049 N N   . LYS D 1 353 ? 7.225   65.293  -20.856 1.00 68.37  ? 382 LYS C N   1 
ATOM   13050 C CA  . LYS D 1 353 ? 7.687   66.576  -21.381 1.00 73.99  ? 382 LYS C CA  1 
ATOM   13051 C C   . LYS D 1 353 ? 9.063   66.456  -22.041 1.00 69.40  ? 382 LYS C C   1 
ATOM   13052 O O   . LYS D 1 353 ? 9.626   67.473  -22.428 1.00 78.33  ? 382 LYS C O   1 
ATOM   13053 C CB  . LYS D 1 353 ? 7.828   67.686  -20.324 1.00 75.63  ? 382 LYS C CB  1 
ATOM   13054 C CG  . LYS D 1 353 ? 6.553   68.100  -19.592 1.00 89.23  ? 382 LYS C CG  1 
ATOM   13055 C CD  . LYS D 1 353 ? 6.763   69.123  -18.475 1.00 96.92  ? 382 LYS C CD  1 
ATOM   13056 C CE  . LYS D 1 353 ? 7.107   70.520  -18.935 1.00 96.52  ? 382 LYS C CE  1 
ATOM   13057 N NZ  . LYS D 1 353 ? 7.410   71.446  -17.830 1.00 95.39  ? 382 LYS C NZ  1 
ATOM   13058 N N   . ILE D 1 354 ? 9.637   65.252  -22.166 1.00 57.26  ? 383 ILE C N   1 
ATOM   13059 C CA  . ILE D 1 354 ? 11.003  65.188  -22.657 1.00 65.25  ? 383 ILE C CA  1 
ATOM   13060 C C   . ILE D 1 354 ? 11.226  64.047  -23.655 1.00 64.37  ? 383 ILE C C   1 
ATOM   13061 O O   . ILE D 1 354 ? 11.802  64.280  -24.714 1.00 68.15  ? 383 ILE C O   1 
ATOM   13062 C CB  . ILE D 1 354 ? 11.987  65.168  -21.469 1.00 76.26  ? 383 ILE C CB  1 
ATOM   13063 C CG1 . ILE D 1 354 ? 11.861  66.482  -20.641 1.00 68.92  ? 383 ILE C CG1 1 
ATOM   13064 C CG2 . ILE D 1 354 ? 13.426  64.908  -21.933 1.00 74.12  ? 383 ILE C CG2 1 
ATOM   13065 C CD1 . ILE D 1 354 ? 12.985  66.743  -19.658 1.00 71.54  ? 383 ILE C CD1 1 
ATOM   13066 N N   . VAL D 1 355 ? 10.795  62.822  -23.337 1.00 62.23  ? 384 VAL C N   1 
ATOM   13067 C CA  . VAL D 1 355 ? 11.207  61.643  -24.091 1.00 57.19  ? 384 VAL C CA  1 
ATOM   13068 C C   . VAL D 1 355 ? 10.700  61.660  -25.541 1.00 52.55  ? 384 VAL C C   1 
ATOM   13069 O O   . VAL D 1 355 ? 11.364  61.111  -26.420 1.00 48.58  ? 384 VAL C O   1 
ATOM   13070 C CB  . VAL D 1 355 ? 10.738  60.347  -23.395 1.00 64.23  ? 384 VAL C CB  1 
ATOM   13071 C CG1 . VAL D 1 355 ? 10.870  59.130  -24.310 1.00 56.55  ? 384 VAL C CG1 1 
ATOM   13072 C CG2 . VAL D 1 355 ? 11.453  60.099  -22.069 1.00 63.25  ? 384 VAL C CG2 1 
ATOM   13073 N N   . PRO D 1 356 ? 9.479   62.151  -25.860 1.00 53.39  ? 385 PRO C N   1 
ATOM   13074 C CA  . PRO D 1 356 ? 8.984   62.044  -27.230 1.00 58.21  ? 385 PRO C CA  1 
ATOM   13075 C C   . PRO D 1 356 ? 9.983   62.702  -28.179 1.00 70.63  ? 385 PRO C C   1 
ATOM   13076 O O   . PRO D 1 356 ? 10.528  62.046  -29.067 1.00 74.56  ? 385 PRO C O   1 
ATOM   13077 C CB  . PRO D 1 356 ? 7.571   62.704  -27.234 1.00 57.62  ? 385 PRO C CB  1 
ATOM   13078 C CG  . PRO D 1 356 ? 7.429   63.372  -25.877 1.00 62.18  ? 385 PRO C CG  1 
ATOM   13079 C CD  . PRO D 1 356 ? 8.497   62.780  -24.956 1.00 59.75  ? 385 PRO C CD  1 
ATOM   13080 N N   . ASN D 1 357 ? 10.255  63.988  -27.926 1.00 75.25  ? 386 ASN C N   1 
ATOM   13081 C CA  . ASN D 1 357 ? 11.112  64.805  -28.772 1.00 82.76  ? 386 ASN C CA  1 
ATOM   13082 C C   . ASN D 1 357 ? 12.514  64.195  -28.867 1.00 76.28  ? 386 ASN C C   1 
ATOM   13083 O O   . ASN D 1 357 ? 13.216  64.455  -29.839 1.00 85.08  ? 386 ASN C O   1 
ATOM   13084 C CB  . ASN D 1 357 ? 11.074  66.269  -28.327 1.00 91.87  ? 386 ASN C CB  1 
ATOM   13085 C CG  . ASN D 1 357 ? 10.830  66.425  -26.840 1.00 98.43  ? 386 ASN C CG  1 
ATOM   13086 O OD1 . ASN D 1 357 ? 9.794   65.975  -26.323 1.00 94.00  ? 386 ASN C OD1 1 
ATOM   13087 N ND2 . ASN D 1 357 ? 11.772  67.035  -26.133 1.00 89.48  ? 386 ASN C ND2 1 
ATOM   13088 N N   . VAL D 1 358 ? 12.910  63.371  -27.885 1.00 63.33  ? 387 VAL C N   1 
ATOM   13089 C CA  . VAL D 1 358 ? 14.174  62.646  -27.938 1.00 67.31  ? 387 VAL C CA  1 
ATOM   13090 C C   . VAL D 1 358 ? 14.055  61.398  -28.826 1.00 74.51  ? 387 VAL C C   1 
ATOM   13091 O O   . VAL D 1 358 ? 15.029  61.001  -29.470 1.00 71.66  ? 387 VAL C O   1 
ATOM   13092 C CB  . VAL D 1 358 ? 14.667  62.272  -26.524 1.00 68.59  ? 387 VAL C CB  1 
ATOM   13093 C CG1 . VAL D 1 358 ? 16.070  61.685  -26.558 1.00 70.39  ? 387 VAL C CG1 1 
ATOM   13094 C CG2 . VAL D 1 358 ? 14.629  63.450  -25.551 1.00 68.80  ? 387 VAL C CG2 1 
ATOM   13095 N N   . LEU D 1 359 ? 12.878  60.746  -28.820 1.00 81.54  ? 388 LEU C N   1 
ATOM   13096 C CA  . LEU D 1 359 ? 12.610  59.573  -29.650 1.00 77.72  ? 388 LEU C CA  1 
ATOM   13097 C C   . LEU D 1 359 ? 12.443  59.996  -31.107 1.00 74.34  ? 388 LEU C C   1 
ATOM   13098 O O   . LEU D 1 359 ? 12.927  59.311  -32.011 1.00 64.10  ? 388 LEU C O   1 
ATOM   13099 C CB  . LEU D 1 359 ? 11.362  58.831  -29.161 1.00 72.37  ? 388 LEU C CB  1 
ATOM   13100 C CG  . LEU D 1 359 ? 11.503  58.044  -27.850 1.00 68.35  ? 388 LEU C CG  1 
ATOM   13101 C CD1 . LEU D 1 359 ? 10.225  57.292  -27.528 1.00 62.35  ? 388 LEU C CD1 1 
ATOM   13102 C CD2 . LEU D 1 359 ? 12.683  57.077  -27.887 1.00 68.42  ? 388 LEU C CD2 1 
ATOM   13103 N N   . LEU D 1 360 ? 11.720  61.113  -31.285 1.00 77.06  ? 389 LEU C N   1 
ATOM   13104 C CA  . LEU D 1 360 ? 11.494  61.733  -32.579 1.00 88.23  ? 389 LEU C CA  1 
ATOM   13105 C C   . LEU D 1 360 ? 12.832  62.222  -33.138 1.00 96.13  ? 389 LEU C C   1 
ATOM   13106 O O   . LEU D 1 360 ? 13.259  61.736  -34.184 1.00 93.94  ? 389 LEU C O   1 
ATOM   13107 C CB  . LEU D 1 360 ? 10.457  62.849  -32.417 1.00 84.17  ? 389 LEU C CB  1 
ATOM   13108 C CG  . LEU D 1 360 ? 9.508   63.094  -33.597 1.00 94.58  ? 389 LEU C CG  1 
ATOM   13109 C CD1 . LEU D 1 360 ? 9.151   61.821  -34.370 1.00 97.65  ? 389 LEU C CD1 1 
ATOM   13110 C CD2 . LEU D 1 360 ? 8.241   63.782  -33.089 1.00 92.74  ? 389 LEU C CD2 1 
ATOM   13111 N N   . GLU D 1 361 ? 13.519  63.115  -32.400 1.00 89.18  ? 390 GLU C N   1 
ATOM   13112 C CA  . GLU D 1 361 ? 14.834  63.611  -32.789 1.00 89.25  ? 390 GLU C CA  1 
ATOM   13113 C C   . GLU D 1 361 ? 15.808  62.458  -33.034 1.00 83.13  ? 390 GLU C C   1 
ATOM   13114 O O   . GLU D 1 361 ? 16.813  62.655  -33.708 1.00 83.69  ? 390 GLU C O   1 
ATOM   13115 C CB  . GLU D 1 361 ? 15.485  64.556  -31.772 1.00 87.76  ? 390 GLU C CB  1 
ATOM   13116 C CG  . GLU D 1 361 ? 15.069  66.022  -31.897 1.00 84.84  ? 390 GLU C CG  1 
ATOM   13117 C CD  . GLU D 1 361 ? 15.636  66.929  -30.810 1.00 78.72  ? 390 GLU C CD  1 
ATOM   13118 O OE1 . GLU D 1 361 ? 14.907  67.797  -30.276 1.00 66.21  ? 390 GLU C OE1 1 
ATOM   13119 O OE2 . GLU D 1 361 ? 16.825  66.743  -30.475 1.00 77.29  ? 390 GLU C OE2 1 
ATOM   13120 N N   . GLN D 1 362 ? 15.535  61.273  -32.473 1.00 85.13  ? 391 GLN C N   1 
ATOM   13121 C CA  . GLN D 1 362 ? 16.288  60.079  -32.827 1.00 90.43  ? 391 GLN C CA  1 
ATOM   13122 C C   . GLN D 1 362 ? 15.822  59.566  -34.190 1.00 87.30  ? 391 GLN C C   1 
ATOM   13123 O O   . GLN D 1 362 ? 16.641  59.073  -34.961 1.00 79.78  ? 391 GLN C O   1 
ATOM   13124 C CB  . GLN D 1 362 ? 16.198  58.950  -31.797 1.00 90.44  ? 391 GLN C CB  1 
ATOM   13125 C CG  . GLN D 1 362 ? 17.441  58.061  -31.781 1.00 91.61  ? 391 GLN C CG  1 
ATOM   13126 C CD  . GLN D 1 362 ? 17.171  56.614  -31.417 1.00 90.57  ? 391 GLN C CD  1 
ATOM   13127 O OE1 . GLN D 1 362 ? 17.832  56.019  -30.558 1.00 79.29  ? 391 GLN C OE1 1 
ATOM   13128 N NE2 . GLN D 1 362 ? 16.218  56.013  -32.109 1.00 82.95  ? 391 GLN C NE2 1 
ATOM   13129 N N   . GLY D 1 363 ? 14.504  59.635  -34.453 1.00 95.50  ? 392 GLY C N   1 
ATOM   13130 C CA  . GLY D 1 363 ? 13.943  59.380  -35.778 1.00 102.21 ? 392 GLY C CA  1 
ATOM   13131 C C   . GLY D 1 363 ? 13.446  57.943  -35.957 1.00 108.29 ? 392 GLY C C   1 
ATOM   13132 O O   . GLY D 1 363 ? 12.444  57.719  -36.639 1.00 105.00 ? 392 GLY C O   1 
ATOM   13133 N N   . LYS D 1 364 ? 14.140  56.984  -35.321 1.00 107.71 ? 393 LYS C N   1 
ATOM   13134 C CA  . LYS D 1 364 ? 13.964  55.558  -35.567 1.00 101.23 ? 393 LYS C CA  1 
ATOM   13135 C C   . LYS D 1 364 ? 12.821  54.977  -34.728 1.00 94.37  ? 393 LYS C C   1 
ATOM   13136 O O   . LYS D 1 364 ? 12.970  53.884  -34.187 1.00 93.40  ? 393 LYS C O   1 
ATOM   13137 C CB  . LYS D 1 364 ? 15.273  54.829  -35.216 1.00 97.66  ? 393 LYS C CB  1 
ATOM   13138 C CG  . LYS D 1 364 ? 16.556  55.282  -35.931 1.00 100.80 ? 393 LYS C CG  1 
ATOM   13139 C CD  . LYS D 1 364 ? 17.168  54.302  -36.933 1.00 101.72 ? 393 LYS C CD  1 
ATOM   13140 C CE  . LYS D 1 364 ? 16.217  53.659  -37.907 1.00 100.62 ? 393 LYS C CE  1 
ATOM   13141 N NZ  . LYS D 1 364 ? 15.493  54.632  -38.729 1.00 104.19 ? 393 LYS C NZ  1 
ATOM   13142 N N   . ALA D 1 365 ? 11.674  55.674  -34.645 1.00 89.30  ? 394 ALA C N   1 
ATOM   13143 C CA  . ALA D 1 365 ? 10.554  55.215  -33.829 1.00 82.58  ? 394 ALA C CA  1 
ATOM   13144 C C   . ALA D 1 365 ? 9.219   55.666  -34.423 1.00 82.36  ? 394 ALA C C   1 
ATOM   13145 O O   . ALA D 1 365 ? 8.994   56.854  -34.645 1.00 77.54  ? 394 ALA C O   1 
ATOM   13146 C CB  . ALA D 1 365 ? 10.705  55.703  -32.403 1.00 82.77  ? 394 ALA C CB  1 
ATOM   13147 N N   . LYS D 1 366 ? 8.316   54.698  -34.633 1.00 76.77  ? 395 LYS C N   1 
ATOM   13148 C CA  . LYS D 1 366 ? 7.043   54.947  -35.288 1.00 78.98  ? 395 LYS C CA  1 
ATOM   13149 C C   . LYS D 1 366 ? 6.166   55.840  -34.405 1.00 83.06  ? 395 LYS C C   1 
ATOM   13150 O O   . LYS D 1 366 ? 5.583   56.813  -34.890 1.00 85.31  ? 395 LYS C O   1 
ATOM   13151 C CB  . LYS D 1 366 ? 6.401   53.604  -35.666 1.00 69.71  ? 395 LYS C CB  1 
ATOM   13152 N N   . ASN D 1 367 ? 6.077   55.498  -33.112 1.00 80.32  ? 396 ASN C N   1 
ATOM   13153 C CA  . ASN D 1 367 ? 5.227   56.203  -32.161 1.00 79.46  ? 396 ASN C CA  1 
ATOM   13154 C C   . ASN D 1 367 ? 6.082   56.693  -30.989 1.00 81.63  ? 396 ASN C C   1 
ATOM   13155 O O   . ASN D 1 367 ? 6.235   55.987  -29.988 1.00 69.06  ? 396 ASN C O   1 
ATOM   13156 C CB  . ASN D 1 367 ? 4.063   55.319  -31.718 1.00 72.72  ? 396 ASN C CB  1 
ATOM   13157 C CG  . ASN D 1 367 ? 3.248   55.918  -30.595 1.00 77.92  ? 396 ASN C CG  1 
ATOM   13158 O OD1 . ASN D 1 367 ? 2.953   55.233  -29.606 1.00 82.63  ? 396 ASN C OD1 1 
ATOM   13159 N ND2 . ASN D 1 367 ? 2.847   57.176  -30.729 1.00 71.90  ? 396 ASN C ND2 1 
ATOM   13160 N N   . PRO D 1 368 ? 6.643   57.926  -31.047 1.00 81.26  ? 397 PRO C N   1 
ATOM   13161 C CA  . PRO D 1 368 ? 7.498   58.424  -29.968 1.00 78.87  ? 397 PRO C CA  1 
ATOM   13162 C C   . PRO D 1 368 ? 6.715   58.921  -28.752 1.00 67.98  ? 397 PRO C C   1 
ATOM   13163 O O   . PRO D 1 368 ? 7.274   59.560  -27.866 1.00 67.45  ? 397 PRO C O   1 
ATOM   13164 C CB  . PRO D 1 368 ? 8.228   59.562  -30.709 1.00 84.75  ? 397 PRO C CB  1 
ATOM   13165 C CG  . PRO D 1 368 ? 7.140   60.161  -31.571 1.00 83.54  ? 397 PRO C CG  1 
ATOM   13166 C CD  . PRO D 1 368 ? 6.452   58.920  -32.120 1.00 85.58  ? 397 PRO C CD  1 
ATOM   13167 N N   . TRP D 1 369 ? 5.408   58.645  -28.724 1.00 58.38  ? 398 TRP C N   1 
ATOM   13168 C CA  . TRP D 1 369 ? 4.526   59.146  -27.680 1.00 61.46  ? 398 TRP C CA  1 
ATOM   13169 C C   . TRP D 1 369 ? 4.189   58.043  -26.669 1.00 54.47  ? 398 TRP C C   1 
ATOM   13170 O O   . TRP D 1 369 ? 4.290   56.848  -26.977 1.00 41.41  ? 398 TRP C O   1 
ATOM   13171 C CB  . TRP D 1 369 ? 3.267   59.724  -28.339 1.00 68.41  ? 398 TRP C CB  1 
ATOM   13172 C CG  . TRP D 1 369 ? 3.559   60.954  -29.154 1.00 85.23  ? 398 TRP C CG  1 
ATOM   13173 C CD1 . TRP D 1 369 ? 3.984   60.998  -30.449 1.00 81.44  ? 398 TRP C CD1 1 
ATOM   13174 C CD2 . TRP D 1 369 ? 3.457   62.325  -28.705 1.00 104.47 ? 398 TRP C CD2 1 
ATOM   13175 N NE1 . TRP D 1 369 ? 4.156   62.298  -30.839 1.00 92.96  ? 398 TRP C NE1 1 
ATOM   13176 C CE2 . TRP D 1 369 ? 3.836   63.135  -29.797 1.00 107.91 ? 398 TRP C CE2 1 
ATOM   13177 C CE3 . TRP D 1 369 ? 3.082   62.945  -27.502 1.00 106.08 ? 398 TRP C CE3 1 
ATOM   13178 C CZ2 . TRP D 1 369 ? 3.848   64.529  -29.710 1.00 106.77 ? 398 TRP C CZ2 1 
ATOM   13179 C CZ3 . TRP D 1 369 ? 3.092   64.322  -27.421 1.00 102.59 ? 398 TRP C CZ3 1 
ATOM   13180 C CH2 . TRP D 1 369 ? 3.473   65.102  -28.513 1.00 104.45 ? 398 TRP C CH2 1 
ATOM   13181 N N   . PRO D 1 370 ? 3.739   58.407  -25.444 1.00 46.75  ? 399 PRO C N   1 
ATOM   13182 C CA  . PRO D 1 370 ? 3.424   57.409  -24.404 1.00 51.14  ? 399 PRO C CA  1 
ATOM   13183 C C   . PRO D 1 370 ? 2.152   56.581  -24.613 1.00 47.75  ? 399 PRO C C   1 
ATOM   13184 O O   . PRO D 1 370 ? 1.162   57.094  -25.137 1.00 46.71  ? 399 PRO C O   1 
ATOM   13185 C CB  . PRO D 1 370 ? 3.274   58.310  -23.158 1.00 47.26  ? 399 PRO C CB  1 
ATOM   13186 C CG  . PRO D 1 370 ? 2.719   59.623  -23.698 1.00 46.90  ? 399 PRO C CG  1 
ATOM   13187 C CD  . PRO D 1 370 ? 3.445   59.788  -25.022 1.00 49.84  ? 399 PRO C CD  1 
ATOM   13188 N N   . ASN D 1 371 ? 2.166   55.317  -24.154 1.00 47.50  ? 400 ASN C N   1 
ATOM   13189 C CA  . ASN D 1 371 ? 0.955   54.517  -24.055 1.00 41.71  ? 400 ASN C CA  1 
ATOM   13190 C C   . ASN D 1 371 ? 0.515   54.367  -22.594 1.00 38.71  ? 400 ASN C C   1 
ATOM   13191 O O   . ASN D 1 371 ? 1.197   54.797  -21.669 1.00 45.82  ? 400 ASN C O   1 
ATOM   13192 C CB  . ASN D 1 371 ? 1.094   53.176  -24.777 1.00 48.34  ? 400 ASN C CB  1 
ATOM   13193 C CG  . ASN D 1 371 ? 1.942   52.197  -24.007 1.00 46.59  ? 400 ASN C CG  1 
ATOM   13194 O OD1 . ASN D 1 371 ? 1.600   51.844  -22.868 1.00 53.35  ? 400 ASN C OD1 1 
ATOM   13195 N ND2 . ASN D 1 371 ? 3.053   51.775  -24.592 1.00 50.04  ? 400 ASN C ND2 1 
ATOM   13196 N N   . VAL D 1 372 ? -0.673  53.767  -22.400 1.00 37.76  ? 401 VAL C N   1 
ATOM   13197 C CA  . VAL D 1 372 ? -1.312  53.674  -21.095 1.00 39.47  ? 401 VAL C CA  1 
ATOM   13198 C C   . VAL D 1 372 ? -0.320  53.154  -20.042 1.00 44.81  ? 401 VAL C C   1 
ATOM   13199 O O   . VAL D 1 372 ? -0.319  53.619  -18.898 1.00 36.67  ? 401 VAL C O   1 
ATOM   13200 C CB  . VAL D 1 372 ? -2.559  52.773  -21.215 1.00 34.85  ? 401 VAL C CB  1 
ATOM   13201 C CG1 . VAL D 1 372 ? -2.226  51.312  -21.473 1.00 34.86  ? 401 VAL C CG1 1 
ATOM   13202 C CG2 . VAL D 1 372 ? -3.440  52.891  -19.985 1.00 43.01  ? 401 VAL C CG2 1 
ATOM   13203 N N   . ASP D 1 373 ? 0.536   52.189  -20.436 1.00 44.30  ? 402 ASP C N   1 
ATOM   13204 C CA  . ASP D 1 373 ? 1.369   51.463  -19.488 1.00 47.56  ? 402 ASP C CA  1 
ATOM   13205 C C   . ASP D 1 373 ? 2.366   52.416  -18.824 1.00 46.61  ? 402 ASP C C   1 
ATOM   13206 O O   . ASP D 1 373 ? 2.820   52.179  -17.706 1.00 46.63  ? 402 ASP C O   1 
ATOM   13207 C CB  . ASP D 1 373 ? 2.080   50.266  -20.123 1.00 55.02  ? 402 ASP C CB  1 
ATOM   13208 C CG  . ASP D 1 373 ? 1.218   49.196  -20.801 1.00 60.66  ? 402 ASP C CG  1 
ATOM   13209 O OD1 . ASP D 1 373 ? 0.215   48.739  -20.187 1.00 57.58  ? 402 ASP C OD1 1 
ATOM   13210 O OD2 . ASP D 1 373 ? 1.579   48.791  -21.938 1.00 63.69  ? 402 ASP C OD2 1 
ATOM   13211 N N   . ALA D 1 374 ? 2.688   53.521  -19.501 1.00 39.94  ? 403 ALA C N   1 
ATOM   13212 C CA  . ALA D 1 374 ? 3.618   54.499  -18.961 1.00 39.00  ? 403 ALA C CA  1 
ATOM   13213 C C   . ALA D 1 374 ? 3.122   55.151  -17.669 1.00 36.15  ? 403 ALA C C   1 
ATOM   13214 O O   . ALA D 1 374 ? 3.967   55.662  -16.949 1.00 34.11  ? 403 ALA C O   1 
ATOM   13215 C CB  . ALA D 1 374 ? 3.917   55.575  -19.991 1.00 40.39  ? 403 ALA C CB  1 
ATOM   13216 N N   . HIS D 1 375 ? 1.807   55.184  -17.372 1.00 35.51  ? 404 HIS C N   1 
ATOM   13217 C CA  . HIS D 1 375 ? 1.321   56.012  -16.254 1.00 39.30  ? 404 HIS C CA  1 
ATOM   13218 C C   . HIS D 1 375 ? 0.540   55.260  -15.156 1.00 37.02  ? 404 HIS C C   1 
ATOM   13219 O O   . HIS D 1 375 ? 0.233   55.828  -14.106 1.00 39.37  ? 404 HIS C O   1 
ATOM   13220 C CB  . HIS D 1 375 ? 0.457   57.155  -16.797 1.00 42.46  ? 404 HIS C CB  1 
ATOM   13221 C CG  . HIS D 1 375 ? 0.237   58.342  -15.895 1.00 49.57  ? 404 HIS C CG  1 
ATOM   13222 N ND1 . HIS D 1 375 ? -0.191  58.273  -14.586 1.00 50.82  ? 404 HIS C ND1 1 
ATOM   13223 C CD2 . HIS D 1 375 ? 0.336   59.663  -16.180 1.00 51.44  ? 404 HIS C CD2 1 
ATOM   13224 C CE1 . HIS D 1 375 ? -0.303  59.503  -14.093 1.00 49.78  ? 404 HIS C CE1 1 
ATOM   13225 N NE2 . HIS D 1 375 ? 0.001   60.358  -15.040 1.00 51.95  ? 404 HIS C NE2 1 
ATOM   13226 N N   . SER D 1 376 ? 0.189   53.989  -15.354 1.00 41.81  ? 405 SER C N   1 
ATOM   13227 C CA  . SER D 1 376 ? -0.763  53.335  -14.459 1.00 42.19  ? 405 SER C CA  1 
ATOM   13228 C C   . SER D 1 376 ? -0.116  52.940  -13.127 1.00 40.92  ? 405 SER C C   1 
ATOM   13229 O O   . SER D 1 376 ? -0.710  53.117  -12.063 1.00 39.43  ? 405 SER C O   1 
ATOM   13230 C CB  . SER D 1 376 ? -1.504  52.198  -15.144 1.00 42.90  ? 405 SER C CB  1 
ATOM   13231 O OG  . SER D 1 376 ? -0.628  51.268  -15.764 1.00 46.13  ? 405 SER C OG  1 
ATOM   13232 N N   . GLY D 1 377 ? 1.127   52.462  -13.155 1.00 39.95  ? 406 GLY C N   1 
ATOM   13233 C CA  . GLY D 1 377 ? 1.768   51.950  -11.957 1.00 38.86  ? 406 GLY C CA  1 
ATOM   13234 C C   . GLY D 1 377 ? 2.078   53.000  -10.889 1.00 41.48  ? 406 GLY C C   1 
ATOM   13235 O O   . GLY D 1 377 ? 2.103   52.651  -9.711  1.00 42.66  ? 406 GLY C O   1 
ATOM   13236 N N   . VAL D 1 378 ? 2.376   54.257  -11.272 1.00 42.13  ? 407 VAL C N   1 
ATOM   13237 C CA  . VAL D 1 378 ? 2.648   55.304  -10.288 1.00 48.37  ? 407 VAL C CA  1 
ATOM   13238 C C   . VAL D 1 378 ? 1.389   55.527  -9.445  1.00 43.59  ? 407 VAL C C   1 
ATOM   13239 O O   . VAL D 1 378 ? 1.479   55.729  -8.227  1.00 43.65  ? 407 VAL C O   1 
ATOM   13240 C CB  . VAL D 1 378 ? 3.189   56.629  -10.878 1.00 59.75  ? 407 VAL C CB  1 
ATOM   13241 C CG1 . VAL D 1 378 ? 4.616   56.461  -11.384 1.00 62.02  ? 407 VAL C CG1 1 
ATOM   13242 C CG2 . VAL D 1 378 ? 2.313   57.201  -11.993 1.00 59.22  ? 407 VAL C CG2 1 
ATOM   13243 N N   . LEU D 1 379 ? 0.211   55.397  -10.083 1.00 40.73  ? 408 LEU C N   1 
ATOM   13244 C CA  . LEU D 1 379 ? -1.070  55.574  -9.401  1.00 35.62  ? 408 LEU C CA  1 
ATOM   13245 C C   . LEU D 1 379 ? -1.325  54.449  -8.405  1.00 37.21  ? 408 LEU C C   1 
ATOM   13246 O O   . LEU D 1 379 ? -1.681  54.674  -7.254  1.00 34.23  ? 408 LEU C O   1 
ATOM   13247 C CB  . LEU D 1 379 ? -2.141  55.643  -10.475 1.00 39.00  ? 408 LEU C CB  1 
ATOM   13248 C CG  . LEU D 1 379 ? -2.559  57.033  -10.949 1.00 44.65  ? 408 LEU C CG  1 
ATOM   13249 C CD1 . LEU D 1 379 ? -1.406  58.011  -11.030 1.00 55.10  ? 408 LEU C CD1 1 
ATOM   13250 C CD2 . LEU D 1 379 ? -3.238  56.922  -12.292 1.00 43.61  ? 408 LEU C CD2 1 
ATOM   13251 N N   . LEU D 1 380 ? -1.174  53.210  -8.875  1.00 32.91  ? 409 LEU C N   1 
ATOM   13252 C CA  . LEU D 1 380 ? -1.335  52.063  -8.003  1.00 31.17  ? 409 LEU C CA  1 
ATOM   13253 C C   . LEU D 1 380 ? -0.435  52.204  -6.774  1.00 32.71  ? 409 LEU C C   1 
ATOM   13254 O O   . LEU D 1 380 ? -0.913  52.071  -5.649  1.00 34.03  ? 409 LEU C O   1 
ATOM   13255 C CB  . LEU D 1 380 ? -1.032  50.795  -8.811  1.00 32.31  ? 409 LEU C CB  1 
ATOM   13256 C CG  . LEU D 1 380 ? -1.999  50.513  -9.968  1.00 33.32  ? 409 LEU C CG  1 
ATOM   13257 C CD1 . LEU D 1 380 ? -1.560  49.282  -10.729 1.00 31.48  ? 409 LEU C CD1 1 
ATOM   13258 C CD2 . LEU D 1 380 ? -3.432  50.432  -9.438  1.00 31.61  ? 409 LEU C CD2 1 
ATOM   13259 N N   . GLN D 1 381 ? 0.878   52.388  -7.005  1.00 34.43  ? 410 GLN C N   1 
ATOM   13260 C CA  . GLN D 1 381 ? 1.867   52.504  -5.947  1.00 39.34  ? 410 GLN C CA  1 
ATOM   13261 C C   . GLN D 1 381 ? 1.471   53.612  -4.964  1.00 37.76  ? 410 GLN C C   1 
ATOM   13262 O O   . GLN D 1 381 ? 1.489   53.421  -3.746  1.00 42.19  ? 410 GLN C O   1 
ATOM   13263 C CB  . GLN D 1 381 ? 3.233   52.811  -6.554  1.00 38.65  ? 410 GLN C CB  1 
ATOM   13264 C CG  . GLN D 1 381 ? 4.331   52.887  -5.504  1.00 45.37  ? 410 GLN C CG  1 
ATOM   13265 C CD  . GLN D 1 381 ? 5.708   52.931  -6.125  1.00 50.16  ? 410 GLN C CD  1 
ATOM   13266 O OE1 . GLN D 1 381 ? 6.507   52.001  -5.986  1.00 46.88  ? 410 GLN C OE1 1 
ATOM   13267 N NE2 . GLN D 1 381 ? 5.968   53.994  -6.868  1.00 53.44  ? 410 GLN C NE2 1 
ATOM   13268 N N   . TYR D 1 382 ? 1.046   54.751  -5.503  1.00 36.92  ? 411 TYR C N   1 
ATOM   13269 C CA  . TYR D 1 382 ? 0.648   55.857  -4.651  1.00 40.38  ? 411 TYR C CA  1 
ATOM   13270 C C   . TYR D 1 382 ? -0.388  55.404  -3.632  1.00 39.96  ? 411 TYR C C   1 
ATOM   13271 O O   . TYR D 1 382 ? -0.342  55.901  -2.509  1.00 38.79  ? 411 TYR C O   1 
ATOM   13272 C CB  . TYR D 1 382 ? 0.070   57.044  -5.413  1.00 43.46  ? 411 TYR C CB  1 
ATOM   13273 C CG  . TYR D 1 382 ? -0.397  58.123  -4.450  1.00 46.45  ? 411 TYR C CG  1 
ATOM   13274 C CD1 . TYR D 1 382 ? 0.495   59.050  -3.919  1.00 53.18  ? 411 TYR C CD1 1 
ATOM   13275 C CD2 . TYR D 1 382 ? -1.731  58.223  -4.089  1.00 48.18  ? 411 TYR C CD2 1 
ATOM   13276 C CE1 . TYR D 1 382 ? 0.075   60.043  -3.048  1.00 51.75  ? 411 TYR C CE1 1 
ATOM   13277 C CE2 . TYR D 1 382 ? -2.163  59.208  -3.215  1.00 57.01  ? 411 TYR C CE2 1 
ATOM   13278 C CZ  . TYR D 1 382 ? -1.258  60.117  -2.690  1.00 52.87  ? 411 TYR C CZ  1 
ATOM   13279 O OH  . TYR D 1 382 ? -1.708  61.076  -1.839  1.00 57.50  ? 411 TYR C OH  1 
ATOM   13280 N N   . TYR D 1 383 ? -1.319  54.510  -4.025  1.00 33.80  ? 412 TYR C N   1 
ATOM   13281 C CA  . TYR D 1 383 ? -2.385  54.070  -3.122  1.00 33.79  ? 412 TYR C CA  1 
ATOM   13282 C C   . TYR D 1 383 ? -1.933  52.890  -2.271  1.00 36.96  ? 412 TYR C C   1 
ATOM   13283 O O   . TYR D 1 383 ? -2.742  52.338  -1.522  1.00 46.60  ? 412 TYR C O   1 
ATOM   13284 C CB  . TYR D 1 383 ? -3.741  53.875  -3.840  1.00 35.99  ? 412 TYR C CB  1 
ATOM   13285 C CG  . TYR D 1 383 ? -4.308  55.212  -4.321  1.00 35.69  ? 412 TYR C CG  1 
ATOM   13286 C CD1 . TYR D 1 383 ? -4.947  56.099  -3.447  1.00 39.25  ? 412 TYR C CD1 1 
ATOM   13287 C CD2 . TYR D 1 383 ? -4.088  55.653  -5.608  1.00 38.73  ? 412 TYR C CD2 1 
ATOM   13288 C CE1 . TYR D 1 383 ? -5.403  57.344  -3.861  1.00 35.61  ? 412 TYR C CE1 1 
ATOM   13289 C CE2 . TYR D 1 383 ? -4.521  56.895  -6.034  1.00 39.07  ? 412 TYR C CE2 1 
ATOM   13290 C CZ  . TYR D 1 383 ? -5.179  57.750  -5.160  1.00 40.39  ? 412 TYR C CZ  1 
ATOM   13291 O OH  . TYR D 1 383 ? -5.592  58.960  -5.650  1.00 42.78  ? 412 TYR C OH  1 
ATOM   13292 N N   . GLY D 1 384 ? -0.645  52.515  -2.307  1.00 41.35  ? 413 GLY C N   1 
ATOM   13293 C CA  . GLY D 1 384 ? -0.157  51.463  -1.420  1.00 40.87  ? 413 GLY C CA  1 
ATOM   13294 C C   . GLY D 1 384 ? -0.182  50.060  -2.059  1.00 44.69  ? 413 GLY C C   1 
ATOM   13295 O O   . GLY D 1 384 ? 0.225   49.083  -1.445  1.00 39.25  ? 413 GLY C O   1 
ATOM   13296 N N   . MET D 1 385 ? -0.620  49.957  -3.314  1.00 41.07  ? 414 MET C N   1 
ATOM   13297 C CA  . MET D 1 385 ? -0.501  48.731  -4.106  1.00 39.58  ? 414 MET C CA  1 
ATOM   13298 C C   . MET D 1 385 ? 0.870   48.691  -4.790  1.00 35.82  ? 414 MET C C   1 
ATOM   13299 O O   . MET D 1 385 ? 1.025   49.184  -5.909  1.00 37.01  ? 414 MET C O   1 
ATOM   13300 C CB  . MET D 1 385 ? -1.626  48.730  -5.139  1.00 41.53  ? 414 MET C CB  1 
ATOM   13301 C CG  . MET D 1 385 ? -1.400  47.847  -6.314  1.00 48.41  ? 414 MET C CG  1 
ATOM   13302 S SD  . MET D 1 385 ? -2.618  46.549  -6.507  1.00 43.73  ? 414 MET C SD  1 
ATOM   13303 C CE  . MET D 1 385 ? -4.017  46.406  -5.388  1.00 41.28  ? 414 MET C CE  1 
ATOM   13304 N N   . THR D 1 386 ? 1.867   48.195  -4.050  1.00 33.62  ? 415 THR C N   1 
ATOM   13305 C CA  . THR D 1 386 ? 3.256   48.259  -4.445  1.00 40.43  ? 415 THR C CA  1 
ATOM   13306 C C   . THR D 1 386 ? 3.703   46.926  -5.048  1.00 39.71  ? 415 THR C C   1 
ATOM   13307 O O   . THR D 1 386 ? 4.839   46.829  -5.493  1.00 44.45  ? 415 THR C O   1 
ATOM   13308 C CB  . THR D 1 386 ? 4.104   48.617  -3.229  1.00 42.44  ? 415 THR C CB  1 
ATOM   13309 O OG1 . THR D 1 386 ? 3.828   47.604  -2.268  1.00 40.52  ? 415 THR C OG1 1 
ATOM   13310 C CG2 . THR D 1 386 ? 3.753   49.976  -2.650  1.00 48.98  ? 415 THR C CG2 1 
ATOM   13311 N N   . GLU D 1 387 ? 2.830   45.908  -5.063  1.00 39.74  ? 416 GLU C N   1 
ATOM   13312 C CA  . GLU D 1 387 ? 3.215   44.589  -5.570  1.00 37.98  ? 416 GLU C CA  1 
ATOM   13313 C C   . GLU D 1 387 ? 3.074   44.589  -7.096  1.00 37.49  ? 416 GLU C C   1 
ATOM   13314 O O   . GLU D 1 387 ? 2.046   44.226  -7.655  1.00 41.83  ? 416 GLU C O   1 
ATOM   13315 C CB  . GLU D 1 387 ? 2.427   43.497  -4.853  1.00 37.36  ? 416 GLU C CB  1 
ATOM   13316 C CG  . GLU D 1 387 ? 2.574   43.530  -3.331  1.00 38.12  ? 416 GLU C CG  1 
ATOM   13317 C CD  . GLU D 1 387 ? 1.544   44.377  -2.558  1.00 43.32  ? 416 GLU C CD  1 
ATOM   13318 O OE1 . GLU D 1 387 ? 1.511   44.267  -1.317  1.00 43.75  ? 416 GLU C OE1 1 
ATOM   13319 O OE2 . GLU D 1 387 ? 0.773   45.154  -3.166  1.00 42.08  ? 416 GLU C OE2 1 
ATOM   13320 N N   . MET D 1 388 ? 4.117   45.080  -7.759  1.00 33.99  ? 417 MET C N   1 
ATOM   13321 C CA  . MET D 1 388 ? 4.151   45.263  -9.199  1.00 40.31  ? 417 MET C CA  1 
ATOM   13322 C C   . MET D 1 388 ? 3.840   43.989  -9.991  1.00 35.59  ? 417 MET C C   1 
ATOM   13323 O O   . MET D 1 388 ? 3.360   44.098  -11.115 1.00 31.28  ? 417 MET C O   1 
ATOM   13324 C CB  . MET D 1 388 ? 5.538   45.699  -9.663  1.00 42.45  ? 417 MET C CB  1 
ATOM   13325 C CG  . MET D 1 388 ? 6.080   46.819  -8.845  1.00 47.92  ? 417 MET C CG  1 
ATOM   13326 S SD  . MET D 1 388 ? 7.558   47.385  -9.688  1.00 57.79  ? 417 MET C SD  1 
ATOM   13327 C CE  . MET D 1 388 ? 8.403   47.997  -8.215  1.00 57.92  ? 417 MET C CE  1 
ATOM   13328 N N   . ASN D 1 389 ? 4.142   42.821  -9.427  1.00 31.76  ? 418 ASN C N   1 
ATOM   13329 C CA  . ASN D 1 389 ? 3.912   41.546  -10.082 1.00 37.20  ? 418 ASN C CA  1 
ATOM   13330 C C   . ASN D 1 389 ? 2.419   41.334  -10.296 1.00 36.66  ? 418 ASN C C   1 
ATOM   13331 O O   . ASN D 1 389 ? 2.025   40.604  -11.193 1.00 36.92  ? 418 ASN C O   1 
ATOM   13332 C CB  . ASN D 1 389 ? 4.509   40.389  -9.282  1.00 41.68  ? 418 ASN C CB  1 
ATOM   13333 C CG  . ASN D 1 389 ? 5.935   40.035  -9.651  1.00 49.54  ? 418 ASN C CG  1 
ATOM   13334 O OD1 . ASN D 1 389 ? 6.477   40.464  -10.681 1.00 40.72  ? 418 ASN C OD1 1 
ATOM   13335 N ND2 . ASN D 1 389 ? 6.547   39.193  -8.827  1.00 52.53  ? 418 ASN C ND2 1 
ATOM   13336 N N   . TYR D 1 390 ? 1.597   42.015  -9.495  1.00 35.07  ? 419 TYR C N   1 
ATOM   13337 C CA  . TYR D 1 390 ? 0.169   41.825  -9.513  1.00 29.49  ? 419 TYR C CA  1 
ATOM   13338 C C   . TYR D 1 390 ? -0.535  42.750  -10.501 1.00 30.91  ? 419 TYR C C   1 
ATOM   13339 O O   . TYR D 1 390 ? -1.716  42.551  -10.755 1.00 35.02  ? 419 TYR C O   1 
ATOM   13340 C CB  . TYR D 1 390 ? -0.338  42.128  -8.105  1.00 31.45  ? 419 TYR C CB  1 
ATOM   13341 C CG  . TYR D 1 390 ? -1.815  41.826  -7.922  1.00 31.16  ? 419 TYR C CG  1 
ATOM   13342 C CD1 . TYR D 1 390 ? -2.254  40.527  -7.752  1.00 30.45  ? 419 TYR C CD1 1 
ATOM   13343 C CD2 . TYR D 1 390 ? -2.764  42.842  -7.906  1.00 32.42  ? 419 TYR C CD2 1 
ATOM   13344 C CE1 . TYR D 1 390 ? -3.604  40.246  -7.604  1.00 30.82  ? 419 TYR C CE1 1 
ATOM   13345 C CE2 . TYR D 1 390 ? -4.117  42.577  -7.752  1.00 30.17  ? 419 TYR C CE2 1 
ATOM   13346 C CZ  . TYR D 1 390 ? -4.536  41.275  -7.565  1.00 28.95  ? 419 TYR C CZ  1 
ATOM   13347 O OH  . TYR D 1 390 ? -5.867  41.015  -7.380  1.00 25.90  ? 419 TYR C OH  1 
ATOM   13348 N N   . TYR D 1 391 ? 0.150   43.772  -11.012 1.00 26.03  ? 420 TYR C N   1 
ATOM   13349 C CA  . TYR D 1 391 ? -0.496  44.812  -11.788 1.00 27.61  ? 420 TYR C CA  1 
ATOM   13350 C C   . TYR D 1 391 ? -1.199  44.243  -13.008 1.00 28.17  ? 420 TYR C C   1 
ATOM   13351 O O   . TYR D 1 391 ? -2.287  44.678  -13.376 1.00 27.00  ? 420 TYR C O   1 
ATOM   13352 C CB  . TYR D 1 391 ? 0.541   45.847  -12.230 1.00 29.00  ? 420 TYR C CB  1 
ATOM   13353 C CG  . TYR D 1 391 ? 1.093   46.735  -11.123 1.00 31.25  ? 420 TYR C CG  1 
ATOM   13354 C CD1 . TYR D 1 391 ? 0.592   46.693  -9.831  1.00 31.16  ? 420 TYR C CD1 1 
ATOM   13355 C CD2 . TYR D 1 391 ? 2.046   47.706  -11.405 1.00 32.31  ? 420 TYR C CD2 1 
ATOM   13356 C CE1 . TYR D 1 391 ? 1.063   47.540  -8.844  1.00 32.07  ? 420 TYR C CE1 1 
ATOM   13357 C CE2 . TYR D 1 391 ? 2.495   48.576  -10.432 1.00 33.59  ? 420 TYR C CE2 1 
ATOM   13358 C CZ  . TYR D 1 391 ? 2.042   48.464  -9.132  1.00 32.37  ? 420 TYR C CZ  1 
ATOM   13359 O OH  . TYR D 1 391 ? 2.497   49.322  -8.158  1.00 37.22  ? 420 TYR C OH  1 
ATOM   13360 N N   . THR D 1 392 ? -0.610  43.221  -13.628 1.00 25.03  ? 421 THR C N   1 
ATOM   13361 C CA  . THR D 1 392 ? -1.250  42.685  -14.808 1.00 26.67  ? 421 THR C CA  1 
ATOM   13362 C C   . THR D 1 392 ? -2.574  42.004  -14.486 1.00 25.28  ? 421 THR C C   1 
ATOM   13363 O O   . THR D 1 392 ? -3.462  41.964  -15.318 1.00 29.58  ? 421 THR C O   1 
ATOM   13364 C CB  . THR D 1 392 ? -0.310  41.771  -15.569 1.00 30.61  ? 421 THR C CB  1 
ATOM   13365 O OG1 . THR D 1 392 ? 0.826   42.603  -15.817 1.00 35.56  ? 421 THR C OG1 1 
ATOM   13366 C CG2 . THR D 1 392 ? -0.939  41.439  -16.911 1.00 35.70  ? 421 THR C CG2 1 
ATOM   13367 N N   . VAL D 1 393 ? -2.726  41.462  -13.290 1.00 27.11  ? 422 VAL C N   1 
ATOM   13368 C CA  . VAL D 1 393 ? -3.998  40.898  -12.885 1.00 28.78  ? 422 VAL C CA  1 
ATOM   13369 C C   . VAL D 1 393 ? -5.126  41.940  -12.967 1.00 30.07  ? 422 VAL C C   1 
ATOM   13370 O O   . VAL D 1 393 ? -6.239  41.623  -13.395 1.00 27.85  ? 422 VAL C O   1 
ATOM   13371 C CB  . VAL D 1 393 ? -3.882  40.295  -11.475 1.00 27.96  ? 422 VAL C CB  1 
ATOM   13372 C CG1 . VAL D 1 393 ? -5.232  39.885  -10.923 1.00 27.92  ? 422 VAL C CG1 1 
ATOM   13373 C CG2 . VAL D 1 393 ? -2.935  39.124  -11.459 1.00 32.36  ? 422 VAL C CG2 1 
ATOM   13374 N N   . LEU D 1 394 ? -4.842  43.185  -12.593 1.00 33.05  ? 423 LEU C N   1 
ATOM   13375 C CA  . LEU D 1 394 ? -5.846  44.234  -12.666 1.00 35.51  ? 423 LEU C CA  1 
ATOM   13376 C C   . LEU D 1 394 ? -6.219  44.521  -14.124 1.00 35.07  ? 423 LEU C C   1 
ATOM   13377 O O   . LEU D 1 394 ? -7.397  44.704  -14.454 1.00 31.42  ? 423 LEU C O   1 
ATOM   13378 C CB  . LEU D 1 394 ? -5.322  45.479  -11.946 1.00 36.53  ? 423 LEU C CB  1 
ATOM   13379 C CG  . LEU D 1 394 ? -5.165  45.328  -10.425 1.00 38.44  ? 423 LEU C CG  1 
ATOM   13380 C CD1 . LEU D 1 394 ? -4.360  46.440  -9.776  1.00 44.78  ? 423 LEU C CD1 1 
ATOM   13381 C CD2 . LEU D 1 394 ? -6.526  45.268  -9.797  1.00 37.63  ? 423 LEU C CD2 1 
ATOM   13382 N N   . PHE D 1 395 ? -5.202  44.607  -14.979 1.00 30.31  ? 424 PHE C N   1 
ATOM   13383 C CA  . PHE D 1 395 ? -5.403  44.738  -16.410 1.00 30.85  ? 424 PHE C CA  1 
ATOM   13384 C C   . PHE D 1 395 ? -6.307  43.612  -16.900 1.00 28.53  ? 424 PHE C C   1 
ATOM   13385 O O   . PHE D 1 395 ? -7.255  43.864  -17.627 1.00 33.63  ? 424 PHE C O   1 
ATOM   13386 C CB  . PHE D 1 395 ? -4.049  44.714  -17.131 1.00 35.05  ? 424 PHE C CB  1 
ATOM   13387 C CG  . PHE D 1 395 ? -3.963  45.232  -18.562 1.00 33.74  ? 424 PHE C CG  1 
ATOM   13388 C CD1 . PHE D 1 395 ? -5.085  45.340  -19.384 1.00 39.76  ? 424 PHE C CD1 1 
ATOM   13389 C CD2 . PHE D 1 395 ? -2.718  45.549  -19.105 1.00 40.07  ? 424 PHE C CD2 1 
ATOM   13390 C CE1 . PHE D 1 395 ? -4.968  45.789  -20.704 1.00 38.23  ? 424 PHE C CE1 1 
ATOM   13391 C CE2 . PHE D 1 395 ? -2.599  46.016  -20.418 1.00 39.91  ? 424 PHE C CE2 1 
ATOM   13392 C CZ  . PHE D 1 395 ? -3.724  46.122  -21.222 1.00 39.07  ? 424 PHE C CZ  1 
ATOM   13393 N N   . GLY D 1 396 ? -6.035  42.389  -16.464 1.00 27.30  ? 425 GLY C N   1 
ATOM   13394 C CA  . GLY D 1 396 ? -6.855  41.230  -16.782 1.00 29.51  ? 425 GLY C CA  1 
ATOM   13395 C C   . GLY D 1 396 ? -8.330  41.350  -16.370 1.00 29.90  ? 425 GLY C C   1 
ATOM   13396 O O   . GLY D 1 396 ? -9.243  41.054  -17.160 1.00 27.49  ? 425 GLY C O   1 
ATOM   13397 N N   . VAL D 1 397 ? -8.577  41.729  -15.124 1.00 27.26  ? 426 VAL C N   1 
ATOM   13398 C CA  . VAL D 1 397 ? -9.945  41.882  -14.659 1.00 25.99  ? 426 VAL C CA  1 
ATOM   13399 C C   . VAL D 1 397 ? -10.706 42.896  -15.528 1.00 23.13  ? 426 VAL C C   1 
ATOM   13400 O O   . VAL D 1 397 ? -11.881 42.709  -15.854 1.00 24.81  ? 426 VAL C O   1 
ATOM   13401 C CB  . VAL D 1 397 ? -10.001 42.263  -13.176 1.00 27.47  ? 426 VAL C CB  1 
ATOM   13402 C CG1 . VAL D 1 397 ? -11.427 42.545  -12.743 1.00 27.34  ? 426 VAL C CG1 1 
ATOM   13403 C CG2 . VAL D 1 397 ? -9.414  41.159  -12.301 1.00 29.49  ? 426 VAL C CG2 1 
ATOM   13404 N N   . SER D 1 398 ? -10.013 43.937  -15.936 1.00 22.69  ? 427 SER C N   1 
ATOM   13405 C CA  . SER D 1 398 ? -10.538 44.949  -16.837 1.00 26.48  ? 427 SER C CA  1 
ATOM   13406 C C   . SER D 1 398 ? -10.823 44.364  -18.222 1.00 30.57  ? 427 SER C C   1 
ATOM   13407 O O   . SER D 1 398 ? -11.910 44.570  -18.776 1.00 27.38  ? 427 SER C O   1 
ATOM   13408 C CB  . SER D 1 398 ? -9.598  46.089  -16.950 1.00 24.49  ? 427 SER C CB  1 
ATOM   13409 O OG  . SER D 1 398 ? -10.141 47.085  -17.827 1.00 28.35  ? 427 SER C OG  1 
ATOM   13410 N N   . ARG D 1 399 ? -9.837  43.651  -18.784 1.00 26.77  ? 428 ARG C N   1 
ATOM   13411 C CA  . ARG D 1 399 ? -9.936  43.252  -20.181 1.00 26.93  ? 428 ARG C CA  1 
ATOM   13412 C C   . ARG D 1 399 ? -11.100 42.278  -20.379 1.00 26.49  ? 428 ARG C C   1 
ATOM   13413 O O   . ARG D 1 399 ? -11.672 42.166  -21.465 1.00 29.83  ? 428 ARG C O   1 
ATOM   13414 C CB  . ARG D 1 399 ? -8.573  42.755  -20.642 1.00 26.40  ? 428 ARG C CB  1 
ATOM   13415 C CG  . ARG D 1 399 ? -8.440  42.386  -22.109 1.00 30.87  ? 428 ARG C CG  1 
ATOM   13416 C CD  . ARG D 1 399 ? -8.855  43.522  -23.055 1.00 30.30  ? 428 ARG C CD  1 
ATOM   13417 N NE  . ARG D 1 399 ? -8.189  44.805  -22.816 1.00 28.26  ? 428 ARG C NE  1 
ATOM   13418 C CZ  . ARG D 1 399 ? -7.197  45.270  -23.566 1.00 29.57  ? 428 ARG C CZ  1 
ATOM   13419 N NH1 . ARG D 1 399 ? -6.533  44.479  -24.405 1.00 30.89  ? 428 ARG C NH1 1 
ATOM   13420 N NH2 . ARG D 1 399 ? -6.818  46.501  -23.422 1.00 27.33  ? 428 ARG C NH2 1 
ATOM   13421 N N   . ALA D 1 400 ? -11.414 41.534  -19.339 1.00 25.29  ? 429 ALA C N   1 
ATOM   13422 C CA  . ALA D 1 400 ? -12.560 40.657  -19.322 1.00 26.91  ? 429 ALA C CA  1 
ATOM   13423 C C   . ALA D 1 400 ? -13.786 41.356  -19.886 1.00 28.11  ? 429 ALA C C   1 
ATOM   13424 O O   . ALA D 1 400 ? -14.604 40.704  -20.526 1.00 26.22  ? 429 ALA C O   1 
ATOM   13425 C CB  . ALA D 1 400 ? -12.824 40.190  -17.901 1.00 28.40  ? 429 ALA C CB  1 
ATOM   13426 N N   . LEU D 1 401 ? -13.965 42.649  -19.575 1.00 26.46  ? 430 LEU C N   1 
ATOM   13427 C CA  . LEU D 1 401 ? -15.185 43.324  -19.934 1.00 27.31  ? 430 LEU C CA  1 
ATOM   13428 C C   . LEU D 1 401 ? -15.259 43.419  -21.445 1.00 26.85  ? 430 LEU C C   1 
ATOM   13429 O O   . LEU D 1 401 ? -16.308 43.178  -22.026 1.00 26.55  ? 430 LEU C O   1 
ATOM   13430 C CB  . LEU D 1 401 ? -15.256 44.722  -19.302 1.00 28.15  ? 430 LEU C CB  1 
ATOM   13431 C CG  . LEU D 1 401 ? -15.115 44.719  -17.779 1.00 31.11  ? 430 LEU C CG  1 
ATOM   13432 C CD1 . LEU D 1 401 ? -15.217 46.132  -17.257 1.00 34.49  ? 430 LEU C CD1 1 
ATOM   13433 C CD2 . LEU D 1 401 ? -16.113 43.788  -17.106 1.00 33.18  ? 430 LEU C CD2 1 
ATOM   13434 N N   . GLY D 1 402 ? -14.158 43.832  -22.064 1.00 25.97  ? 431 GLY C N   1 
ATOM   13435 C CA  . GLY D 1 402 ? -14.165 44.038  -23.506 1.00 27.94  ? 431 GLY C CA  1 
ATOM   13436 C C   . GLY D 1 402 ? -14.213 42.728  -24.313 1.00 23.64  ? 431 GLY C C   1 
ATOM   13437 O O   . GLY D 1 402 ? -14.978 42.599  -25.256 1.00 28.09  ? 431 GLY C O   1 
ATOM   13438 N N   . VAL D 1 403 ? -13.418 41.747  -23.925 1.00 24.27  ? 432 VAL C N   1 
ATOM   13439 C CA  . VAL D 1 403 ? -13.310 40.519  -24.693 1.00 25.63  ? 432 VAL C CA  1 
ATOM   13440 C C   . VAL D 1 403 ? -14.571 39.672  -24.547 1.00 25.55  ? 432 VAL C C   1 
ATOM   13441 O O   . VAL D 1 403 ? -14.931 38.965  -25.478 1.00 24.29  ? 432 VAL C O   1 
ATOM   13442 C CB  . VAL D 1 403 ? -12.038 39.720  -24.376 1.00 27.87  ? 432 VAL C CB  1 
ATOM   13443 C CG1 . VAL D 1 403 ? -10.806 40.581  -24.587 1.00 30.17  ? 432 VAL C CG1 1 
ATOM   13444 C CG2 . VAL D 1 403 ? -12.054 39.076  -22.989 1.00 27.50  ? 432 VAL C CG2 1 
ATOM   13445 N N   . LEU D 1 404 ? -15.222 39.712  -23.374 1.00 25.70  ? 433 LEU C N   1 
ATOM   13446 C CA  . LEU D 1 404 ? -16.440 38.954  -23.161 1.00 25.12  ? 433 LEU C CA  1 
ATOM   13447 C C   . LEU D 1 404 ? -17.630 39.648  -23.824 1.00 26.00  ? 433 LEU C C   1 
ATOM   13448 O O   . LEU D 1 404 ? -18.499 38.981  -24.362 1.00 25.06  ? 433 LEU C O   1 
ATOM   13449 C CB  . LEU D 1 404 ? -16.661 38.701  -21.673 1.00 26.12  ? 433 LEU C CB  1 
ATOM   13450 C CG  . LEU D 1 404 ? -15.605 37.793  -21.012 1.00 28.65  ? 433 LEU C CG  1 
ATOM   13451 C CD1 . LEU D 1 404 ? -15.890 37.639  -19.520 1.00 30.34  ? 433 LEU C CD1 1 
ATOM   13452 C CD2 . LEU D 1 404 ? -15.509 36.428  -21.655 1.00 31.39  ? 433 LEU C CD2 1 
ATOM   13453 N N   . ALA D 1 405 ? -17.697 40.974  -23.778 1.00 27.29  ? 434 ALA C N   1 
ATOM   13454 C CA  . ALA D 1 405 ? -18.731 41.671  -24.507 1.00 29.33  ? 434 ALA C CA  1 
ATOM   13455 C C   . ALA D 1 405 ? -18.648 41.273  -25.981 1.00 28.46  ? 434 ALA C C   1 
ATOM   13456 O O   . ALA D 1 405 ? -19.669 40.962  -26.589 1.00 26.17  ? 434 ALA C O   1 
ATOM   13457 C CB  . ALA D 1 405 ? -18.603 43.168  -24.310 1.00 34.21  ? 434 ALA C CB  1 
ATOM   13458 N N   . GLN D 1 406 ? -17.433 41.242  -26.547 1.00 27.73  ? 435 GLN C N   1 
ATOM   13459 C CA  . GLN D 1 406 ? -17.269 40.878  -27.945 1.00 27.27  ? 435 GLN C CA  1 
ATOM   13460 C C   . GLN D 1 406 ? -17.601 39.396  -28.192 1.00 26.11  ? 435 GLN C C   1 
ATOM   13461 O O   . GLN D 1 406 ? -18.162 39.017  -29.239 1.00 24.32  ? 435 GLN C O   1 
ATOM   13462 C CB  . GLN D 1 406 ? -15.843 41.163  -28.395 1.00 30.65  ? 435 GLN C CB  1 
ATOM   13463 C CG  . GLN D 1 406 ? -15.585 40.695  -29.820 1.00 31.74  ? 435 GLN C CG  1 
ATOM   13464 C CD  . GLN D 1 406 ? -16.587 41.249  -30.817 1.00 35.83  ? 435 GLN C CD  1 
ATOM   13465 O OE1 . GLN D 1 406 ? -16.946 42.437  -30.812 1.00 36.88  ? 435 GLN C OE1 1 
ATOM   13466 N NE2 . GLN D 1 406 ? -17.075 40.392  -31.692 1.00 34.86  ? 435 GLN C NE2 1 
ATOM   13467 N N   . LEU D 1 407 ? -17.256 38.547  -27.228 1.00 24.86  ? 436 LEU C N   1 
ATOM   13468 C CA  . LEU D 1 407 ? -17.413 37.109  -27.390 1.00 26.58  ? 436 LEU C CA  1 
ATOM   13469 C C   . LEU D 1 407 ? -18.884 36.740  -27.560 1.00 24.44  ? 436 LEU C C   1 
ATOM   13470 O O   . LEU D 1 407 ? -19.236 35.874  -28.366 1.00 21.02  ? 436 LEU C O   1 
ATOM   13471 C CB  . LEU D 1 407 ? -16.811 36.426  -26.169 1.00 25.41  ? 436 LEU C CB  1 
ATOM   13472 C CG  . LEU D 1 407 ? -16.898 34.908  -26.185 1.00 29.45  ? 436 LEU C CG  1 
ATOM   13473 C CD1 . LEU D 1 407 ? -16.046 34.347  -27.303 1.00 32.38  ? 436 LEU C CD1 1 
ATOM   13474 C CD2 . LEU D 1 407 ? -16.456 34.297  -24.839 1.00 34.09  ? 436 LEU C CD2 1 
ATOM   13475 N N   . ILE D 1 408 ? -19.742 37.405  -26.779 1.00 25.76  ? 437 ILE C N   1 
ATOM   13476 C CA  . ILE D 1 408 ? -21.184 37.259  -26.844 1.00 23.39  ? 437 ILE C CA  1 
ATOM   13477 C C   . ILE D 1 408 ? -21.693 37.561  -28.247 1.00 22.11  ? 437 ILE C C   1 
ATOM   13478 O O   . ILE D 1 408 ? -22.491 36.821  -28.804 1.00 21.06  ? 437 ILE C O   1 
ATOM   13479 C CB  . ILE D 1 408 ? -21.834 38.216  -25.823 1.00 26.62  ? 437 ILE C CB  1 
ATOM   13480 C CG1 . ILE D 1 408 ? -21.579 37.744  -24.405 1.00 25.62  ? 437 ILE C CG1 1 
ATOM   13481 C CG2 . ILE D 1 408 ? -23.328 38.358  -26.153 1.00 26.59  ? 437 ILE C CG2 1 
ATOM   13482 C CD1 . ILE D 1 408 ? -21.828 38.773  -23.295 1.00 26.57  ? 437 ILE C CD1 1 
ATOM   13483 N N   . TRP D 1 409 ? -21.212 38.667  -28.804 1.00 25.03  ? 438 TRP C N   1 
ATOM   13484 C CA  . TRP D 1 409 ? -21.528 39.103  -30.152 1.00 25.36  ? 438 TRP C CA  1 
ATOM   13485 C C   . TRP D 1 409 ? -20.953 38.193  -31.244 1.00 28.15  ? 438 TRP C C   1 
ATOM   13486 O O   . TRP D 1 409 ? -21.637 37.890  -32.218 1.00 29.31  ? 438 TRP C O   1 
ATOM   13487 C CB  . TRP D 1 409 ? -21.029 40.542  -30.330 1.00 25.87  ? 438 TRP C CB  1 
ATOM   13488 C CG  . TRP D 1 409 ? -22.054 41.516  -29.797 1.00 27.78  ? 438 TRP C CG  1 
ATOM   13489 C CD1 . TRP D 1 409 ? -22.008 42.240  -28.645 1.00 26.65  ? 438 TRP C CD1 1 
ATOM   13490 C CD2 . TRP D 1 409 ? -23.335 41.780  -30.392 1.00 29.28  ? 438 TRP C CD2 1 
ATOM   13491 N NE1 . TRP D 1 409 ? -23.149 42.980  -28.508 1.00 28.70  ? 438 TRP C NE1 1 
ATOM   13492 C CE2 . TRP D 1 409 ? -23.980 42.724  -29.570 1.00 29.95  ? 438 TRP C CE2 1 
ATOM   13493 C CE3 . TRP D 1 409 ? -23.980 41.346  -31.552 1.00 30.42  ? 438 TRP C CE3 1 
ATOM   13494 C CZ2 . TRP D 1 409 ? -25.243 43.216  -29.877 1.00 32.47  ? 438 TRP C CZ2 1 
ATOM   13495 C CZ3 . TRP D 1 409 ? -25.198 41.885  -31.888 1.00 31.56  ? 438 TRP C CZ3 1 
ATOM   13496 C CH2 . TRP D 1 409 ? -25.839 42.783  -31.044 1.00 31.69  ? 438 TRP C CH2 1 
ATOM   13497 N N   . SER D 1 410 ? -19.703 37.776  -31.094 1.00 26.75  ? 439 SER C N   1 
ATOM   13498 C CA  . SER D 1 410 ? -19.143 36.798  -32.011 1.00 26.75  ? 439 SER C CA  1 
ATOM   13499 C C   . SER D 1 410 ? -20.089 35.610  -32.143 1.00 26.76  ? 439 SER C C   1 
ATOM   13500 O O   . SER D 1 410 ? -20.412 35.216  -33.250 1.00 23.95  ? 439 SER C O   1 
ATOM   13501 C CB  . SER D 1 410 ? -17.773 36.392  -31.591 1.00 24.56  ? 439 SER C CB  1 
ATOM   13502 O OG  . SER D 1 410 ? -16.959 37.544  -31.734 1.00 25.91  ? 439 SER C OG  1 
ATOM   13503 N N   . ARG D 1 411 ? -20.574 35.059  -31.018 1.00 32.35  ? 440 ARG C N   1 
ATOM   13504 C CA  . ARG D 1 411 ? -21.412 33.874  -31.091 1.00 26.71  ? 440 ARG C CA  1 
ATOM   13505 C C   . ARG D 1 411 ? -22.813 34.248  -31.571 1.00 25.29  ? 440 ARG C C   1 
ATOM   13506 O O   . ARG D 1 411 ? -23.421 33.491  -32.303 1.00 24.62  ? 440 ARG C O   1 
ATOM   13507 C CB  . ARG D 1 411 ? -21.417 33.087  -29.782 1.00 28.91  ? 440 ARG C CB  1 
ATOM   13508 C CG  . ARG D 1 411 ? -20.074 32.572  -29.309 1.00 27.43  ? 440 ARG C CG  1 
ATOM   13509 C CD  . ARG D 1 411 ? -19.506 31.434  -30.139 1.00 32.07  ? 440 ARG C CD  1 
ATOM   13510 N NE  . ARG D 1 411 ? -18.886 31.874  -31.393 1.00 29.89  ? 440 ARG C NE  1 
ATOM   13511 C CZ  . ARG D 1 411 ? -17.810 32.572  -31.466 1.00 24.78  ? 440 ARG C CZ  1 
ATOM   13512 N NH1 . ARG D 1 411 ? -17.216 32.925  -30.354 1.00 30.62  ? 440 ARG C NH1 1 
ATOM   13513 N NH2 . ARG D 1 411 ? -17.347 32.924  -32.643 1.00 29.41  ? 440 ARG C NH2 1 
ATOM   13514 N N   . ALA D 1 412 ? -23.323 35.435  -31.215 1.00 24.46  ? 441 ALA C N   1 
ATOM   13515 C CA  . ALA D 1 412 ? -24.623 35.887  -31.678 1.00 27.23  ? 441 ALA C CA  1 
ATOM   13516 C C   . ALA D 1 412 ? -24.625 36.058  -33.191 1.00 28.28  ? 441 ALA C C   1 
ATOM   13517 O O   . ALA D 1 412 ? -25.625 35.806  -33.840 1.00 27.14  ? 441 ALA C O   1 
ATOM   13518 C CB  . ALA D 1 412 ? -24.996 37.211  -31.000 1.00 30.05  ? 441 ALA C CB  1 
ATOM   13519 N N   . LEU D 1 413 ? -23.533 36.603  -33.729 1.00 27.45  ? 442 LEU C N   1 
ATOM   13520 C CA  . LEU D 1 413 ? -23.450 36.873  -35.146 1.00 25.81  ? 442 LEU C CA  1 
ATOM   13521 C C   . LEU D 1 413 ? -22.959 35.617  -35.878 1.00 27.90  ? 442 LEU C C   1 
ATOM   13522 O O   . LEU D 1 413 ? -22.877 35.600  -37.101 1.00 32.09  ? 442 LEU C O   1 
ATOM   13523 C CB  . LEU D 1 413 ? -22.536 38.073  -35.378 1.00 27.34  ? 442 LEU C CB  1 
ATOM   13524 C CG  . LEU D 1 413 ? -23.012 39.405  -34.770 1.00 30.32  ? 442 LEU C CG  1 
ATOM   13525 C CD1 . LEU D 1 413 ? -21.894 40.467  -34.829 1.00 31.31  ? 442 LEU C CD1 1 
ATOM   13526 C CD2 . LEU D 1 413 ? -24.282 39.913  -35.468 1.00 27.59  ? 442 LEU C CD2 1 
ATOM   13527 N N   . GLY D 1 414 ? -22.641 34.545  -35.147 1.00 28.40  ? 443 GLY C N   1 
ATOM   13528 C CA  . GLY D 1 414 ? -22.274 33.292  -35.796 1.00 31.72  ? 443 GLY C CA  1 
ATOM   13529 C C   . GLY D 1 414 ? -20.944 33.385  -36.546 1.00 27.01  ? 443 GLY C C   1 
ATOM   13530 O O   . GLY D 1 414 ? -20.715 32.648  -37.492 1.00 29.83  ? 443 GLY C O   1 
ATOM   13531 N N   . PHE D 1 415 ? -19.994 34.156  -36.024 1.00 29.47  ? 444 PHE C N   1 
ATOM   13532 C CA  . PHE D 1 415 ? -18.619 34.139  -36.529 1.00 27.46  ? 444 PHE C CA  1 
ATOM   13533 C C   . PHE D 1 415 ? -18.015 32.732  -36.572 1.00 25.06  ? 444 PHE C C   1 
ATOM   13534 O O   . PHE D 1 415 ? -17.963 32.021  -35.581 1.00 30.16  ? 444 PHE C O   1 
ATOM   13535 C CB  . PHE D 1 415 ? -17.706 35.045  -35.709 1.00 26.61  ? 444 PHE C CB  1 
ATOM   13536 C CG  . PHE D 1 415 ? -17.979 36.539  -35.819 1.00 27.80  ? 444 PHE C CG  1 
ATOM   13537 C CD1 . PHE D 1 415 ? -18.960 37.039  -36.670 1.00 28.89  ? 444 PHE C CD1 1 
ATOM   13538 C CD2 . PHE D 1 415 ? -17.206 37.447  -35.103 1.00 28.33  ? 444 PHE C CD2 1 
ATOM   13539 C CE1 . PHE D 1 415 ? -19.184 38.397  -36.755 1.00 33.17  ? 444 PHE C CE1 1 
ATOM   13540 C CE2 . PHE D 1 415 ? -17.438 38.815  -35.195 1.00 29.28  ? 444 PHE C CE2 1 
ATOM   13541 C CZ  . PHE D 1 415 ? -18.417 39.282  -36.019 1.00 28.96  ? 444 PHE C CZ  1 
ATOM   13542 N N   . PRO D 1 416 ? -17.422 32.299  -37.703 1.00 24.30  ? 445 PRO C N   1 
ATOM   13543 C CA  . PRO D 1 416 ? -16.871 30.952  -37.774 1.00 26.26  ? 445 PRO C CA  1 
ATOM   13544 C C   . PRO D 1 416 ? -15.491 30.782  -37.139 1.00 25.07  ? 445 PRO C C   1 
ATOM   13545 O O   . PRO D 1 416 ? -14.884 31.716  -36.625 1.00 23.29  ? 445 PRO C O   1 
ATOM   13546 C CB  . PRO D 1 416 ? -16.882 30.722  -39.306 1.00 25.50  ? 445 PRO C CB  1 
ATOM   13547 C CG  . PRO D 1 416 ? -16.512 32.055  -39.857 1.00 28.96  ? 445 PRO C CG  1 
ATOM   13548 C CD  . PRO D 1 416 ? -17.188 33.087  -38.926 1.00 23.79  ? 445 PRO C CD  1 
ATOM   13549 N N   . LEU D 1 417 ? -15.022 29.543  -37.132 1.00 24.43  ? 446 LEU C N   1 
ATOM   13550 C CA  . LEU D 1 417 ? -13.695 29.223  -36.670 1.00 28.92  ? 446 LEU C CA  1 
ATOM   13551 C C   . LEU D 1 417 ? -12.667 30.099  -37.364 1.00 26.09  ? 446 LEU C C   1 
ATOM   13552 O O   . LEU D 1 417 ? -12.768 30.343  -38.551 1.00 24.26  ? 446 LEU C O   1 
ATOM   13553 C CB  . LEU D 1 417 ? -13.432 27.764  -36.999 1.00 31.77  ? 446 LEU C CB  1 
ATOM   13554 C CG  . LEU D 1 417 ? -12.120 27.215  -36.471 1.00 33.96  ? 446 LEU C CG  1 
ATOM   13555 C CD1 . LEU D 1 417 ? -12.379 26.731  -35.065 1.00 33.80  ? 446 LEU C CD1 1 
ATOM   13556 C CD2 . LEU D 1 417 ? -11.658 26.091  -37.392 1.00 37.15  ? 446 LEU C CD2 1 
ATOM   13557 N N   . GLU D 1 418 ? -11.724 30.643  -36.604 1.00 24.02  ? 447 GLU C N   1 
ATOM   13558 C CA  . GLU D 1 418 ? -10.658 31.406  -37.227 1.00 27.31  ? 447 GLU C CA  1 
ATOM   13559 C C   . GLU D 1 418 ? -9.576  30.421  -37.675 1.00 26.25  ? 447 GLU C C   1 
ATOM   13560 O O   . GLU D 1 418 ? -9.040  29.683  -36.848 1.00 25.44  ? 447 GLU C O   1 
ATOM   13561 C CB  . GLU D 1 418 ? -10.155 32.452  -36.241 1.00 29.37  ? 447 GLU C CB  1 
ATOM   13562 C CG  . GLU D 1 418 ? -8.921  33.205  -36.734 1.00 33.92  ? 447 GLU C CG  1 
ATOM   13563 C CD  . GLU D 1 418 ? -8.480  34.392  -35.889 1.00 40.25  ? 447 GLU C CD  1 
ATOM   13564 O OE1 . GLU D 1 418 ? -7.259  34.497  -35.587 1.00 42.76  ? 447 GLU C OE1 1 
ATOM   13565 O OE2 . GLU D 1 418 ? -9.355  35.223  -35.542 1.00 43.51  ? 447 GLU C OE2 1 
ATOM   13566 N N   . ARG D 1 419 ? -9.276  30.420  -38.976 1.00 24.99  ? 448 ARG C N   1 
ATOM   13567 C CA  . ARG D 1 419 ? -8.360  29.459  -39.564 1.00 27.50  ? 448 ARG C CA  1 
ATOM   13568 C C   . ARG D 1 419 ? -7.716  30.046  -40.820 1.00 29.42  ? 448 ARG C C   1 
ATOM   13569 O O   . ARG D 1 419 ? -8.174  29.791  -41.931 1.00 29.25  ? 448 ARG C O   1 
ATOM   13570 C CB  . ARG D 1 419 ? -9.086  28.180  -39.972 1.00 33.12  ? 448 ARG C CB  1 
ATOM   13571 C CG  . ARG D 1 419 ? -8.286  26.900  -39.787 1.00 40.15  ? 448 ARG C CG  1 
ATOM   13572 C CD  . ARG D 1 419 ? -7.653  26.237  -40.989 1.00 43.96  ? 448 ARG C CD  1 
ATOM   13573 N NE  . ARG D 1 419 ? -6.248  26.539  -41.256 1.00 54.76  ? 448 ARG C NE  1 
ATOM   13574 C CZ  . ARG D 1 419 ? -5.194  25.722  -41.394 1.00 43.52  ? 448 ARG C CZ  1 
ATOM   13575 N NH1 . ARG D 1 419 ? -5.138  24.490  -40.926 1.00 44.34  ? 448 ARG C NH1 1 
ATOM   13576 N NH2 . ARG D 1 419 ? -4.113  26.227  -41.943 1.00 41.15  ? 448 ARG C NH2 1 
ATOM   13577 N N   . PRO D 1 420 ? -6.636  30.833  -40.687 1.00 26.53  ? 449 PRO C N   1 
ATOM   13578 C CA  . PRO D 1 420 ? -5.901  31.332  -41.834 1.00 28.06  ? 449 PRO C CA  1 
ATOM   13579 C C   . PRO D 1 420 ? -4.989  30.254  -42.377 1.00 26.96  ? 449 PRO C C   1 
ATOM   13580 O O   . PRO D 1 420 ? -4.950  29.147  -41.851 1.00 28.74  ? 449 PRO C O   1 
ATOM   13581 C CB  . PRO D 1 420 ? -5.132  32.489  -41.290 1.00 28.35  ? 449 PRO C CB  1 
ATOM   13582 C CG  . PRO D 1 420 ? -4.884  32.097  -39.857 1.00 30.04  ? 449 PRO C CG  1 
ATOM   13583 C CD  . PRO D 1 420 ? -6.118  31.369  -39.422 1.00 28.97  ? 449 PRO C CD  1 
ATOM   13584 N N   . LYS D 1 421 ? -4.360  30.612  -43.480 1.00 28.58  ? 450 LYS C N   1 
ATOM   13585 C CA  . LYS D 1 421 ? -3.400  29.780  -44.182 1.00 32.06  ? 450 LYS C CA  1 
ATOM   13586 C C   . LYS D 1 421 ? -2.024  30.219  -43.698 1.00 27.11  ? 450 LYS C C   1 
ATOM   13587 O O   . LYS D 1 421 ? -1.798  31.404  -43.613 1.00 28.26  ? 450 LYS C O   1 
ATOM   13588 C CB  . LYS D 1 421 ? -3.627  30.058  -45.674 1.00 38.53  ? 450 LYS C CB  1 
ATOM   13589 C CG  . LYS D 1 421 ? -2.690  29.357  -46.637 1.00 44.48  ? 450 LYS C CG  1 
ATOM   13590 C CD  . LYS D 1 421 ? -3.022  27.886  -46.816 1.00 51.35  ? 450 LYS C CD  1 
ATOM   13591 C CE  . LYS D 1 421 ? -1.884  27.085  -47.433 1.00 58.48  ? 450 LYS C CE  1 
ATOM   13592 N NZ  . LYS D 1 421 ? -1.961  25.693  -46.973 1.00 52.67  ? 450 LYS C NZ  1 
ATOM   13593 N N   . SER D 1 422 ? -1.165  29.271  -43.301 1.00 27.40  ? 451 SER C N   1 
ATOM   13594 C CA  . SER D 1 422 ? 0.238   29.518  -43.092 1.00 24.90  ? 451 SER C CA  1 
ATOM   13595 C C   . SER D 1 422 ? 1.059   29.076  -44.309 1.00 28.48  ? 451 SER C C   1 
ATOM   13596 O O   . SER D 1 422 ? 0.606   28.282  -45.145 1.00 25.32  ? 451 SER C O   1 
ATOM   13597 C CB  . SER D 1 422 ? 0.713   28.885  -41.845 1.00 27.30  ? 451 SER C CB  1 
ATOM   13598 O OG  . SER D 1 422 ? 0.659   27.475  -41.917 1.00 25.63  ? 451 SER C OG  1 
ATOM   13599 N N   . MET D 1 423 ? 2.280   29.619  -44.393 1.00 32.72  ? 452 MET C N   1 
ATOM   13600 C CA  . MET D 1 423 ? 3.263   29.165  -45.364 1.00 34.15  ? 452 MET C CA  1 
ATOM   13601 C C   . MET D 1 423 ? 4.631   29.076  -44.704 1.00 27.86  ? 452 MET C C   1 
ATOM   13602 O O   . MET D 1 423 ? 4.923   29.786  -43.754 1.00 29.88  ? 452 MET C O   1 
ATOM   13603 C CB  . MET D 1 423 ? 3.247   30.106  -46.566 1.00 38.07  ? 452 MET C CB  1 
ATOM   13604 C CG  . MET D 1 423 ? 1.932   30.025  -47.344 1.00 45.46  ? 452 MET C CG  1 
ATOM   13605 S SD  . MET D 1 423 ? 2.091   30.855  -48.936 1.00 60.71  ? 452 MET C SD  1 
ATOM   13606 C CE  . MET D 1 423 ? 3.113   29.579  -49.683 1.00 50.50  ? 452 MET C CE  1 
ATOM   13607 N N   . SER D 1 424 ? 5.457   28.121  -45.131 1.00 24.69  ? 453 SER C N   1 
ATOM   13608 C CA  . SER D 1 424 ? 6.836   28.092  -44.695 1.00 27.34  ? 453 SER C CA  1 
ATOM   13609 C C   . SER D 1 424 ? 7.594   29.097  -45.559 1.00 32.29  ? 453 SER C C   1 
ATOM   13610 O O   . SER D 1 424 ? 7.054   29.567  -46.557 1.00 30.16  ? 453 SER C O   1 
ATOM   13611 C CB  . SER D 1 424 ? 7.431   26.711  -44.804 1.00 31.31  ? 453 SER C CB  1 
ATOM   13612 O OG  . SER D 1 424 ? 7.531   26.280  -46.158 1.00 28.09  ? 453 SER C OG  1 
ATOM   13613 N N   . THR D 1 425 ? 8.809   29.433  -45.126 1.00 33.18  ? 454 THR C N   1 
ATOM   13614 C CA  . THR D 1 425 ? 9.755   30.210  -45.910 1.00 33.40  ? 454 THR C CA  1 
ATOM   13615 C C   . THR D 1 425 ? 10.031  29.517  -47.244 1.00 36.65  ? 454 THR C C   1 
ATOM   13616 O O   . THR D 1 425 ? 10.017  30.170  -48.278 1.00 39.74  ? 454 THR C O   1 
ATOM   13617 C CB  . THR D 1 425 ? 11.033  30.412  -45.097 1.00 38.05  ? 454 THR C CB  1 
ATOM   13618 O OG1 . THR D 1 425 ? 10.683  31.296  -44.024 1.00 36.50  ? 454 THR C OG1 1 
ATOM   13619 C CG2 . THR D 1 425 ? 12.149  31.012  -45.940 1.00 37.02  ? 454 THR C CG2 1 
ATOM   13620 N N   . GLU D 1 426 ? 10.293  28.208  -47.220 1.00 34.36  ? 455 GLU C N   1 
ATOM   13621 C CA  . GLU D 1 426 ? 10.530  27.435  -48.433 1.00 37.61  ? 455 GLU C CA  1 
ATOM   13622 C C   . GLU D 1 426 ? 9.310   27.514  -49.354 1.00 35.94  ? 455 GLU C C   1 
ATOM   13623 O O   . GLU D 1 426 ? 9.420   27.653  -50.590 1.00 34.00  ? 455 GLU C O   1 
ATOM   13624 C CB  . GLU D 1 426 ? 10.880  26.032  -47.928 1.00 47.79  ? 455 GLU C CB  1 
ATOM   13625 C CG  . GLU D 1 426 ? 10.965  24.918  -48.964 1.00 57.59  ? 455 GLU C CG  1 
ATOM   13626 C CD  . GLU D 1 426 ? 11.251  23.527  -48.375 1.00 73.95  ? 455 GLU C CD  1 
ATOM   13627 O OE1 . GLU D 1 426 ? 10.449  22.963  -47.563 1.00 68.02  ? 455 GLU C OE1 1 
ATOM   13628 O OE2 . GLU D 1 426 ? 12.324  22.989  -48.750 1.00 75.60  ? 455 GLU C OE2 1 
ATOM   13629 N N   . GLY D 1 427 ? 8.119   27.417  -48.758 1.00 32.23  ? 456 GLY C N   1 
ATOM   13630 C CA  . GLY D 1 427 ? 6.897   27.462  -49.538 1.00 33.15  ? 456 GLY C CA  1 
ATOM   13631 C C   . GLY D 1 427 ? 6.672   28.829  -50.178 1.00 33.70  ? 456 GLY C C   1 
ATOM   13632 O O   . GLY D 1 427 ? 6.256   28.918  -51.330 1.00 34.20  ? 456 GLY C O   1 
ATOM   13633 N N   . LEU D 1 428 ? 6.921   29.894  -49.417 1.00 36.17  ? 457 LEU C N   1 
ATOM   13634 C CA  . LEU D 1 428 ? 6.743   31.261  -49.890 1.00 37.51  ? 457 LEU C CA  1 
ATOM   13635 C C   . LEU D 1 428 ? 7.734   31.579  -51.004 1.00 37.18  ? 457 LEU C C   1 
ATOM   13636 O O   . LEU D 1 428 ? 7.390   32.325  -51.907 1.00 42.94  ? 457 LEU C O   1 
ATOM   13637 C CB  . LEU D 1 428 ? 6.932   32.310  -48.793 1.00 36.55  ? 457 LEU C CB  1 
ATOM   13638 C CG  . LEU D 1 428 ? 5.692   32.897  -48.118 1.00 38.61  ? 457 LEU C CG  1 
ATOM   13639 C CD1 . LEU D 1 428 ? 6.194   33.999  -47.195 1.00 40.24  ? 457 LEU C CD1 1 
ATOM   13640 C CD2 . LEU D 1 428 ? 4.599   33.457  -49.014 1.00 38.77  ? 457 LEU C CD2 1 
ATOM   13641 N N   . MET D 1 429 ? 8.978   31.107  -50.886 1.00 40.15  ? 458 MET C N   1 
ATOM   13642 C CA  . MET D 1 429 ? 9.982   31.363  -51.910 1.00 43.33  ? 458 MET C CA  1 
ATOM   13643 C C   . MET D 1 429 ? 9.528   30.767  -53.238 1.00 45.46  ? 458 MET C C   1 
ATOM   13644 O O   . MET D 1 429 ? 9.623   31.441  -54.269 1.00 49.51  ? 458 MET C O   1 
ATOM   13645 C CB  . MET D 1 429 ? 11.350  30.795  -51.529 1.00 46.39  ? 458 MET C CB  1 
ATOM   13646 C CG  . MET D 1 429 ? 12.067  31.614  -50.468 1.00 44.34  ? 458 MET C CG  1 
ATOM   13647 S SD  . MET D 1 429 ? 13.620  30.862  -49.934 1.00 46.19  ? 458 MET C SD  1 
ATOM   13648 C CE  . MET D 1 429 ? 14.018  32.112  -48.714 1.00 50.64  ? 458 MET C CE  1 
ATOM   13649 N N   . LYS D 1 430 ? 9.002   29.532  -53.197 1.00 47.13  ? 459 LYS C N   1 
ATOM   13650 C CA  . LYS D 1 430 ? 8.497   28.863  -54.394 1.00 49.96  ? 459 LYS C CA  1 
ATOM   13651 C C   . LYS D 1 430 ? 7.238   29.557  -54.923 1.00 50.08  ? 459 LYS C C   1 
ATOM   13652 O O   . LYS D 1 430 ? 7.013   29.610  -56.126 1.00 43.33  ? 459 LYS C O   1 
ATOM   13653 C CB  . LYS D 1 430 ? 8.220   27.372  -54.177 1.00 56.25  ? 459 LYS C CB  1 
ATOM   13654 C CG  . LYS D 1 430 ? 9.401   26.477  -54.512 1.00 67.01  ? 459 LYS C CG  1 
ATOM   13655 C CD  . LYS D 1 430 ? 9.222   25.003  -54.167 1.00 78.55  ? 459 LYS C CD  1 
ATOM   13656 C CE  . LYS D 1 430 ? 9.196   24.775  -52.682 1.00 88.00  ? 459 LYS C CE  1 
ATOM   13657 N NZ  . LYS D 1 430 ? 9.615   23.420  -52.314 1.00 83.99  ? 459 LYS C NZ  1 
ATOM   13658 N N   . PHE D 1 431 ? 6.404   30.072  -54.023 1.00 49.07  ? 460 PHE C N   1 
ATOM   13659 C CA  . PHE D 1 431 ? 5.144   30.678  -54.408 1.00 51.42  ? 460 PHE C CA  1 
ATOM   13660 C C   . PHE D 1 431 ? 5.360   31.984  -55.165 1.00 51.43  ? 460 PHE C C   1 
ATOM   13661 O O   . PHE D 1 431 ? 4.606   32.267  -56.084 1.00 52.04  ? 460 PHE C O   1 
ATOM   13662 C CB  . PHE D 1 431 ? 4.296   30.939  -53.162 1.00 53.94  ? 460 PHE C CB  1 
ATOM   13663 C CG  . PHE D 1 431 ? 2.971   31.618  -53.455 1.00 51.61  ? 460 PHE C CG  1 
ATOM   13664 C CD1 . PHE D 1 431 ? 1.861   30.871  -53.817 1.00 56.23  ? 460 PHE C CD1 1 
ATOM   13665 C CD2 . PHE D 1 431 ? 2.847   32.999  -53.384 1.00 48.66  ? 460 PHE C CD2 1 
ATOM   13666 C CE1 . PHE D 1 431 ? 0.647   31.490  -54.078 1.00 54.23  ? 460 PHE C CE1 1 
ATOM   13667 C CE2 . PHE D 1 431 ? 1.630   33.601  -53.618 1.00 50.19  ? 460 PHE C CE2 1 
ATOM   13668 C CZ  . PHE D 1 431 ? 0.536   32.850  -53.976 1.00 50.71  ? 460 PHE C CZ  1 
ATOM   13669 N N   . VAL D 1 432 ? 6.356   32.788  -54.758 1.00 54.34  ? 461 VAL C N   1 
ATOM   13670 C CA  . VAL D 1 432 ? 6.582   34.089  -55.374 1.00 52.93  ? 461 VAL C CA  1 
ATOM   13671 C C   . VAL D 1 432 ? 7.410   33.951  -56.657 1.00 64.50  ? 461 VAL C C   1 
ATOM   13672 O O   . VAL D 1 432 ? 7.552   34.939  -57.368 1.00 57.15  ? 461 VAL C O   1 
ATOM   13673 C CB  . VAL D 1 432 ? 7.211   35.139  -54.437 1.00 52.67  ? 461 VAL C CB  1 
ATOM   13674 C CG1 . VAL D 1 432 ? 6.446   35.265  -53.120 1.00 51.27  ? 461 VAL C CG1 1 
ATOM   13675 C CG2 . VAL D 1 432 ? 8.677   34.877  -54.171 1.00 52.69  ? 461 VAL C CG2 1 
ATOM   13676 N N   . ASP D 1 433 ? 8.008   32.780  -56.894 1.00 73.49  ? 462 ASP C N   1 
ATOM   13677 C CA  . ASP D 1 433 ? 8.692   32.580  -58.199 1.00 74.37  ? 462 ASP C CA  1 
ATOM   13678 C C   . ASP D 1 433 ? 7.573   32.231  -59.169 1.00 82.77  ? 462 ASP C C   1 
ATOM   13679 O O   . ASP D 1 433 ? 7.543   32.799  -60.278 1.00 84.27  ? 462 ASP C O   1 
ATOM   13680 C CB  . ASP D 1 433 ? 9.796   31.547  -58.135 1.00 69.50  ? 462 ASP C CB  1 
ATOM   13681 C CG  . ASP D 1 433 ? 11.086  32.033  -57.495 1.00 77.04  ? 462 ASP C CG  1 
ATOM   13682 O OD1 . ASP D 1 433 ? 11.147  33.229  -57.146 1.00 77.81  ? 462 ASP C OD1 1 
ATOM   13683 O OD2 . ASP D 1 433 ? 12.012  31.210  -57.351 1.00 86.30  ? 462 ASP C OD2 1 
ATOM   13684 N N   . SER D 1 434 ? 6.691   31.325  -58.758 1.00 82.71  ? 463 SER C N   1 
ATOM   13685 C CA  . SER D 1 434 ? 5.494   31.051  -59.579 1.00 93.53  ? 463 SER C CA  1 
ATOM   13686 C C   . SER D 1 434 ? 4.757   32.387  -59.708 1.00 98.35  ? 463 SER C C   1 
ATOM   13687 O O   . SER D 1 434 ? 4.364   32.905  -58.656 1.00 104.68 ? 463 SER C O   1 
ATOM   13688 C CB  . SER D 1 434 ? 4.658   30.003  -58.925 1.00 94.39  ? 463 SER C CB  1 
ATOM   13689 O OG  . SER D 1 434 ? 3.820   30.564  -57.924 1.00 95.81  ? 463 SER C OG  1 
ATOM   13690 N N   . LYS D 1 435 ? 4.650   32.948  -60.916 1.00 95.51  ? 464 LYS C N   1 
ATOM   13691 C CA  . LYS D 1 435 ? 4.048   34.294  -61.133 1.00 96.54  ? 464 LYS C CA  1 
ATOM   13692 C C   . LYS D 1 435 ? 5.149   35.354  -60.942 1.00 90.65  ? 464 LYS C C   1 
ATOM   13693 O O   . LYS D 1 435 ? 5.978   35.183  -60.028 1.00 72.50  ? 464 LYS C O   1 
ATOM   13694 C CB  . LYS D 1 435 ? 2.827   34.636  -60.267 1.00 101.75 ? 464 LYS C CB  1 
ATOM   13695 C CG  . LYS D 1 435 ? 1.532   33.945  -60.656 1.00 105.79 ? 464 LYS C CG  1 
ATOM   13696 C CD  . LYS D 1 435 ? 0.448   34.141  -59.605 1.00 104.78 ? 464 LYS C CD  1 
ATOM   13697 C CE  . LYS D 1 435 ? 0.839   33.579  -58.277 1.00 101.95 ? 464 LYS C CE  1 
ATOM   13698 N NZ  . LYS D 1 435 ? -0.207  33.804  -57.276 1.00 96.22  ? 464 LYS C NZ  1 
HETATM 13699 O O1  . OAA E 2 .   ? 18.887  1.682   9.102   1.00 36.31  ? 601 OAA A O1  1 
HETATM 13700 O O2  . OAA E 2 .   ? 20.590  0.312   8.715   1.00 36.14  ? 601 OAA A O2  1 
HETATM 13701 O O4  . OAA E 2 .   ? 21.391  -2.887  11.292  1.00 36.75  ? 601 OAA A O4  1 
HETATM 13702 O O5  . OAA E 2 .   ? 21.209  -0.834  11.892  1.00 32.02  ? 601 OAA A O5  1 
HETATM 13703 O O3  . OAA E 2 .   ? 19.464  -2.548  9.564   1.00 41.09  ? 601 OAA A O3  1 
HETATM 13704 C C1  . OAA E 2 .   ? 19.488  0.591   9.270   1.00 41.34  ? 601 OAA A C1  1 
HETATM 13705 C C2  . OAA E 2 .   ? 18.905  -0.411  10.270  1.00 37.15  ? 601 OAA A C2  1 
HETATM 13706 C C3  . OAA E 2 .   ? 19.768  -1.644  10.342  1.00 42.85  ? 601 OAA A C3  1 
HETATM 13707 C C4  . OAA E 2 .   ? 20.821  -1.787  11.201  1.00 38.93  ? 601 OAA A C4  1 
HETATM 13708 O O1  . OAA F 2 .   ? 24.457  25.124  21.056  1.00 87.34  ? 501 OAA D O1  1 
HETATM 13709 O O2  . OAA F 2 .   ? 24.649  25.637  23.184  1.00 69.89  ? 501 OAA D O2  1 
HETATM 13710 O O4  . OAA F 2 .   ? 22.283  25.219  25.641  1.00 76.42  ? 501 OAA D O4  1 
HETATM 13711 O O5  . OAA F 2 .   ? 21.438  26.819  24.540  1.00 78.00  ? 501 OAA D O5  1 
HETATM 13712 O O3  . OAA F 2 .   ? 22.073  23.818  23.568  1.00 38.45  ? 501 OAA D O3  1 
HETATM 13713 C C1  . OAA F 2 .   ? 23.984  25.479  22.146  1.00 71.49  ? 501 OAA D C1  1 
HETATM 13714 C C2  . OAA F 2 .   ? 22.484  25.682  22.237  1.00 69.09  ? 501 OAA D C2  1 
HETATM 13715 C C3  . OAA F 2 .   ? 22.068  25.031  23.522  1.00 57.61  ? 501 OAA D C3  1 
HETATM 13716 C C4  . OAA F 2 .   ? 21.940  25.715  24.596  1.00 53.58  ? 501 OAA D C4  1 
HETATM 13717 O O1  . OAA G 2 .   ? -7.572  23.374  -38.956 1.00 33.43  ? 501 OAA B O1  1 
HETATM 13718 O O2  . OAA G 2 .   ? -5.907  21.980  -39.401 1.00 34.13  ? 501 OAA B O2  1 
HETATM 13719 O O4  . OAA G 2 .   ? -5.065  18.850  -36.765 1.00 37.27  ? 501 OAA B O4  1 
HETATM 13720 O O5  . OAA G 2 .   ? -5.251  20.921  -36.268 1.00 32.86  ? 501 OAA B O5  1 
HETATM 13721 O O3  . OAA G 2 .   ? -7.077  19.070  -38.436 1.00 33.75  ? 501 OAA B O3  1 
HETATM 13722 C C1  . OAA G 2 .   ? -7.011  22.271  -38.814 1.00 41.37  ? 501 OAA B C1  1 
HETATM 13723 C C2  . OAA G 2 .   ? -7.648  21.248  -37.835 1.00 34.72  ? 501 OAA B C2  1 
HETATM 13724 C C3  . OAA G 2 .   ? -6.772  20.015  -37.711 1.00 40.17  ? 501 OAA B C3  1 
HETATM 13725 C C4  . OAA G 2 .   ? -5.667  19.931  -36.888 1.00 38.69  ? 501 OAA B C4  1 
HETATM 13726 O O   . HOH H 3 .   ? 40.423  15.737  -9.318  1.00 50.56  ? 701 HOH A O   1 
HETATM 13727 O O   . HOH H 3 .   ? 24.596  24.021  11.563  1.00 39.97  ? 702 HOH A O   1 
HETATM 13728 O O   . HOH H 3 .   ? 42.515  -14.141 5.671   1.00 35.23  ? 703 HOH A O   1 
HETATM 13729 O O   . HOH H 3 .   ? 6.533   -3.660  11.702  1.00 50.05  ? 704 HOH A O   1 
HETATM 13730 O O   . HOH H 3 .   ? 13.147  -27.429 16.237  1.00 46.85  ? 705 HOH A O   1 
HETATM 13731 O O   . HOH H 3 .   ? 2.982   -15.136 18.686  1.00 52.63  ? 706 HOH A O   1 
HETATM 13732 O O   . HOH H 3 .   ? 25.529  -12.999 2.869   1.00 32.20  ? 707 HOH A O   1 
HETATM 13733 O O   . HOH H 3 .   ? 33.794  0.307   32.652  1.00 61.93  ? 708 HOH A O   1 
HETATM 13734 O O   . HOH H 3 .   ? -3.130  -15.752 15.327  1.00 70.68  ? 709 HOH A O   1 
HETATM 13735 O O   . HOH H 3 .   ? 19.948  7.963   12.158  1.00 25.55  ? 710 HOH A O   1 
HETATM 13736 O O   . HOH H 3 .   ? 26.541  0.986   11.999  1.00 28.21  ? 711 HOH A O   1 
HETATM 13737 O O   . HOH H 3 .   ? 34.476  -14.576 19.327  1.00 31.96  ? 712 HOH A O   1 
HETATM 13738 O O   . HOH H 3 .   ? 9.603   -24.963 -3.739  1.00 60.12  ? 713 HOH A O   1 
HETATM 13739 O O   . HOH H 3 .   ? 46.774  -0.737  24.884  1.00 35.18  ? 714 HOH A O   1 
HETATM 13740 O O   . HOH H 3 .   ? 31.529  9.119   36.060  1.00 34.28  ? 715 HOH A O   1 
HETATM 13741 O O   . HOH H 3 .   ? 15.765  -26.970 18.878  1.00 47.98  ? 716 HOH A O   1 
HETATM 13742 O O   . HOH H 3 .   ? 49.481  10.110  24.168  1.00 45.54  ? 717 HOH A O   1 
HETATM 13743 O O   . HOH H 3 .   ? 50.219  -7.433  14.577  1.00 38.69  ? 718 HOH A O   1 
HETATM 13744 O O   . HOH H 3 .   ? 40.201  6.046   3.347   1.00 45.01  ? 719 HOH A O   1 
HETATM 13745 O O   . HOH H 3 .   ? 8.217   -2.944  31.976  1.00 40.35  ? 720 HOH A O   1 
HETATM 13746 O O   . HOH H 3 .   ? 18.562  -9.598  14.107  1.00 40.49  ? 721 HOH A O   1 
HETATM 13747 O O   . HOH H 3 .   ? 32.701  -0.584  3.129   1.00 36.35  ? 722 HOH A O   1 
HETATM 13748 O O   . HOH H 3 .   ? 46.946  -22.360 19.146  1.00 54.95  ? 723 HOH A O   1 
HETATM 13749 O O   . HOH H 3 .   ? 27.072  -8.020  -0.356  1.00 47.01  ? 724 HOH A O   1 
HETATM 13750 O O   . HOH H 3 .   ? 28.431  14.288  12.046  1.00 34.22  ? 725 HOH A O   1 
HETATM 13751 O O   . HOH H 3 .   ? 49.521  -6.363  10.408  1.00 58.37  ? 726 HOH A O   1 
HETATM 13752 O O   . HOH H 3 .   ? 48.443  10.126  3.259   1.00 52.55  ? 727 HOH A O   1 
HETATM 13753 O O   . HOH H 3 .   ? 8.460   29.243  14.398  1.00 43.03  ? 728 HOH A O   1 
HETATM 13754 O O   . HOH H 3 .   ? 39.206  -18.730 34.195  1.00 46.35  ? 729 HOH A O   1 
HETATM 13755 O O   . HOH H 3 .   ? 41.553  -15.390 24.636  1.00 39.04  ? 730 HOH A O   1 
HETATM 13756 O O   . HOH H 3 .   ? 24.856  -5.138  10.919  1.00 33.32  ? 731 HOH A O   1 
HETATM 13757 O O   . HOH H 3 .   ? 37.687  2.160   30.745  1.00 35.69  ? 732 HOH A O   1 
HETATM 13758 O O   . HOH H 3 .   ? 46.429  -2.374  22.788  1.00 31.99  ? 733 HOH A O   1 
HETATM 13759 O O   . HOH H 3 .   ? 16.484  -6.208  2.517   1.00 38.57  ? 734 HOH A O   1 
HETATM 13760 O O   . HOH H 3 .   ? 40.707  -19.346 10.549  1.00 30.23  ? 735 HOH A O   1 
HETATM 13761 O O   . HOH H 3 .   ? 27.619  -8.043  2.209   1.00 38.70  ? 736 HOH A O   1 
HETATM 13762 O O   . HOH H 3 .   ? 29.605  5.114   5.403   1.00 24.57  ? 737 HOH A O   1 
HETATM 13763 O O   . HOH H 3 .   ? 25.528  -19.116 40.852  1.00 55.22  ? 738 HOH A O   1 
HETATM 13764 O O   . HOH H 3 .   ? 10.039  29.967  -3.508  1.00 51.38  ? 739 HOH A O   1 
HETATM 13765 O O   . HOH H 3 .   ? 46.605  -7.926  9.078   1.00 44.56  ? 740 HOH A O   1 
HETATM 13766 O O   . HOH H 3 .   ? 20.824  -29.189 15.011  1.00 40.50  ? 741 HOH A O   1 
HETATM 13767 O O   . HOH H 3 .   ? 37.836  -19.479 3.902   1.00 48.37  ? 742 HOH A O   1 
HETATM 13768 O O   . HOH H 3 .   ? 9.311   34.844  3.147   1.00 55.07  ? 743 HOH A O   1 
HETATM 13769 O O   . HOH H 3 .   ? 53.587  -3.177  18.548  1.00 38.74  ? 744 HOH A O   1 
HETATM 13770 O O   . HOH H 3 .   ? 37.292  18.552  16.081  1.00 41.36  ? 745 HOH A O   1 
HETATM 13771 O O   . HOH H 3 .   ? 37.974  -18.131 7.377   1.00 52.20  ? 746 HOH A O   1 
HETATM 13772 O O   . HOH H 3 .   ? 41.109  -21.553 13.934  1.00 47.04  ? 747 HOH A O   1 
HETATM 13773 O O   . HOH H 3 .   ? 34.081  1.240   4.618   1.00 40.64  ? 748 HOH A O   1 
HETATM 13774 O O   . HOH H 3 .   ? 42.430  4.845   35.953  1.00 57.30  ? 749 HOH A O   1 
HETATM 13775 O O   . HOH H 3 .   ? 47.309  -15.926 9.626   1.00 45.40  ? 750 HOH A O   1 
HETATM 13776 O O   . HOH H 3 .   ? 9.728   -3.720  16.627  1.00 45.69  ? 751 HOH A O   1 
HETATM 13777 O O   . HOH H 3 .   ? 13.312  -22.108 15.563  1.00 40.05  ? 752 HOH A O   1 
HETATM 13778 O O   . HOH H 3 .   ? 17.265  -4.161  9.282   1.00 40.34  ? 753 HOH A O   1 
HETATM 13779 O O   . HOH H 3 .   ? 25.302  0.742   42.082  1.00 44.29  ? 754 HOH A O   1 
HETATM 13780 O O   . HOH H 3 .   ? 33.834  -8.646  37.029  1.00 35.90  ? 755 HOH A O   1 
HETATM 13781 O O   . HOH H 3 .   ? 43.862  18.279  -4.261  1.00 55.56  ? 756 HOH A O   1 
HETATM 13782 O O   . HOH H 3 .   ? 38.610  -26.013 19.616  1.00 55.64  ? 757 HOH A O   1 
HETATM 13783 O O   . HOH H 3 .   ? 37.868  -13.242 12.756  1.00 34.52  ? 758 HOH A O   1 
HETATM 13784 O O   . HOH H 3 .   ? 39.876  -6.820  33.850  1.00 41.45  ? 759 HOH A O   1 
HETATM 13785 O O   . HOH H 3 .   ? 12.430  -7.258  31.899  1.00 39.82  ? 760 HOH A O   1 
HETATM 13786 O O   . HOH H 3 .   ? 3.836   -23.802 20.980  1.00 55.97  ? 761 HOH A O   1 
HETATM 13787 O O   . HOH H 3 .   ? 21.915  -21.187 30.509  1.00 54.47  ? 762 HOH A O   1 
HETATM 13788 O O   . HOH H 3 .   ? 17.155  -29.801 11.496  1.00 41.22  ? 763 HOH A O   1 
HETATM 13789 O O   . HOH H 3 .   ? 23.228  -5.391  4.441   1.00 30.08  ? 764 HOH A O   1 
HETATM 13790 O O   . HOH H 3 .   ? 38.379  19.852  22.484  1.00 40.90  ? 765 HOH A O   1 
HETATM 13791 O O   . HOH H 3 .   ? 30.740  12.455  10.135  1.00 31.78  ? 766 HOH A O   1 
HETATM 13792 O O   . HOH H 3 .   ? 19.871  -1.271  40.759  1.00 31.50  ? 767 HOH A O   1 
HETATM 13793 O O   . HOH H 3 .   ? 40.762  14.923  17.745  1.00 39.84  ? 768 HOH A O   1 
HETATM 13794 O O   . HOH H 3 .   ? 13.302  31.497  8.145   1.00 42.65  ? 769 HOH A O   1 
HETATM 13795 O O   . HOH H 3 .   ? 17.861  1.120   26.464  1.00 29.91  ? 770 HOH A O   1 
HETATM 13796 O O   . HOH H 3 .   ? 49.567  8.743   15.200  1.00 36.13  ? 771 HOH A O   1 
HETATM 13797 O O   . HOH H 3 .   ? 42.663  15.850  8.164   1.00 46.42  ? 772 HOH A O   1 
HETATM 13798 O O   . HOH H 3 .   ? 10.124  -24.441 3.823   1.00 42.75  ? 773 HOH A O   1 
HETATM 13799 O O   . HOH H 3 .   ? 22.653  7.718   -2.024  1.00 53.29  ? 774 HOH A O   1 
HETATM 13800 O O   . HOH H 3 .   ? 46.281  12.711  16.026  1.00 56.97  ? 775 HOH A O   1 
HETATM 13801 O O   . HOH H 3 .   ? 18.092  3.017   11.806  1.00 38.44  ? 776 HOH A O   1 
HETATM 13802 O O   . HOH H 3 .   ? 11.480  -17.690 21.480  1.00 67.35  ? 777 HOH A O   1 
HETATM 13803 O O   . HOH H 3 .   ? 34.628  13.273  28.149  1.00 31.63  ? 778 HOH A O   1 
HETATM 13804 O O   . HOH H 3 .   ? 38.519  14.847  9.294   1.00 38.53  ? 779 HOH A O   1 
HETATM 13805 O O   . HOH H 3 .   ? 26.525  -15.208 3.410   1.00 46.04  ? 780 HOH A O   1 
HETATM 13806 O O   . HOH H 3 .   ? 29.358  -1.007  0.187   1.00 44.42  ? 781 HOH A O   1 
HETATM 13807 O O   . HOH H 3 .   ? 31.141  14.769  13.436  1.00 29.58  ? 782 HOH A O   1 
HETATM 13808 O O   . HOH H 3 .   ? 28.510  14.994  9.378   1.00 35.19  ? 783 HOH A O   1 
HETATM 13809 O O   . HOH H 3 .   ? 29.701  20.996  -7.021  1.00 45.67  ? 784 HOH A O   1 
HETATM 13810 O O   . HOH H 3 .   ? 37.055  2.897   4.623   1.00 38.04  ? 785 HOH A O   1 
HETATM 13811 O O   . HOH H 3 .   ? 45.898  5.800   26.010  1.00 36.07  ? 786 HOH A O   1 
HETATM 13812 O O   . HOH H 3 .   ? 46.354  -4.953  10.249  1.00 41.68  ? 787 HOH A O   1 
HETATM 13813 O O   . HOH H 3 .   ? 16.172  1.043   12.048  1.00 38.76  ? 788 HOH A O   1 
HETATM 13814 O O   . HOH H 3 .   ? 17.720  4.194   -7.232  1.00 56.91  ? 789 HOH A O   1 
HETATM 13815 O O   . HOH H 3 .   ? 28.887  -28.996 21.578  1.00 45.61  ? 790 HOH A O   1 
HETATM 13816 O O   . HOH H 3 .   ? 36.875  -22.379 29.847  1.00 43.85  ? 791 HOH A O   1 
HETATM 13817 O O   . HOH H 3 .   ? 35.183  -23.156 20.034  1.00 41.37  ? 792 HOH A O   1 
HETATM 13818 O O   . HOH H 3 .   ? 32.123  -18.580 7.112   1.00 52.76  ? 793 HOH A O   1 
HETATM 13819 O O   . HOH H 3 .   ? 42.723  12.178  18.293  1.00 25.28  ? 794 HOH A O   1 
HETATM 13820 O O   . HOH H 3 .   ? 12.587  -28.986 6.008   1.00 52.75  ? 795 HOH A O   1 
HETATM 13821 O O   . HOH H 3 .   ? 34.751  -23.604 28.095  1.00 45.41  ? 796 HOH A O   1 
HETATM 13822 O O   . HOH H 3 .   ? -2.229  -18.008 16.696  1.00 54.86  ? 797 HOH A O   1 
HETATM 13823 O O   . HOH H 3 .   ? 44.857  20.179  21.717  1.00 37.65  ? 798 HOH A O   1 
HETATM 13824 O O   . HOH H 3 .   ? 48.908  13.864  8.454   1.00 50.86  ? 799 HOH A O   1 
HETATM 13825 O O   . HOH H 3 .   ? 6.696   -25.597 9.091   1.00 41.97  ? 800 HOH A O   1 
HETATM 13826 O O   . HOH H 3 .   ? 32.745  -23.434 20.231  1.00 61.59  ? 801 HOH A O   1 
HETATM 13827 O O   . HOH H 3 .   ? 13.027  28.220  11.583  1.00 33.83  ? 802 HOH A O   1 
HETATM 13828 O O   . HOH H 3 .   ? 9.819   -14.150 25.217  1.00 44.48  ? 803 HOH A O   1 
HETATM 13829 O O   . HOH H 3 .   ? 8.938   -0.300  -6.117  1.00 53.02  ? 804 HOH A O   1 
HETATM 13830 O O   . HOH H 3 .   ? 33.521  20.997  17.438  1.00 37.01  ? 805 HOH A O   1 
HETATM 13831 O O   . HOH H 3 .   ? 42.524  14.705  10.766  1.00 44.68  ? 806 HOH A O   1 
HETATM 13832 O O   . HOH H 3 .   ? 47.353  8.310   25.957  1.00 46.10  ? 807 HOH A O   1 
HETATM 13833 O O   . HOH H 3 .   ? 4.422   -7.438  13.920  1.00 44.03  ? 808 HOH A O   1 
HETATM 13834 O O   . HOH H 3 .   ? 39.834  5.290   8.316   1.00 38.46  ? 809 HOH A O   1 
HETATM 13835 O O   . HOH H 3 .   ? 43.152  -21.823 24.025  1.00 56.46  ? 810 HOH A O   1 
HETATM 13836 O O   . HOH H 3 .   ? 40.450  21.970  32.787  1.00 51.83  ? 811 HOH A O   1 
HETATM 13837 O O   . HOH H 3 .   ? 33.292  -6.251  12.943  1.00 43.56  ? 812 HOH A O   1 
HETATM 13838 O O   . HOH H 3 .   ? 48.113  -14.386 21.660  1.00 43.59  ? 813 HOH A O   1 
HETATM 13839 O O   . HOH H 3 .   ? 10.588  -14.519 8.123   1.00 36.46  ? 814 HOH A O   1 
HETATM 13840 O O   . HOH H 3 .   ? 9.974   -24.790 15.393  1.00 46.17  ? 815 HOH A O   1 
HETATM 13841 O O   . HOH H 3 .   ? 34.082  -7.513  -4.395  1.00 56.91  ? 816 HOH A O   1 
HETATM 13842 O O   . HOH H 3 .   ? 5.059   31.131  8.222   1.00 44.75  ? 817 HOH A O   1 
HETATM 13843 O O   . HOH H 3 .   ? 47.404  20.089  29.869  1.00 48.59  ? 818 HOH A O   1 
HETATM 13844 O O   . HOH H 3 .   ? 13.880  -29.385 14.091  1.00 45.28  ? 819 HOH A O   1 
HETATM 13845 O O   . HOH H 3 .   ? 49.086  -4.730  25.457  1.00 52.62  ? 820 HOH A O   1 
HETATM 13846 O O   . HOH H 3 .   ? 32.246  11.717  33.520  1.00 42.14  ? 821 HOH A O   1 
HETATM 13847 O O   . HOH H 3 .   ? 24.921  16.718  -6.307  1.00 56.94  ? 822 HOH A O   1 
HETATM 13848 O O   . HOH H 3 .   ? -5.363  -2.040  -0.118  1.00 46.92  ? 823 HOH A O   1 
HETATM 13849 O O   . HOH H 3 .   ? 19.866  -1.572  -10.653 1.00 58.33  ? 824 HOH A O   1 
HETATM 13850 O O   . HOH H 3 .   ? 41.982  16.369  36.744  1.00 60.06  ? 825 HOH A O   1 
HETATM 13851 O O   . HOH H 3 .   ? 44.939  16.925  8.887   1.00 57.21  ? 826 HOH A O   1 
HETATM 13852 O O   . HOH H 3 .   ? 10.096  -23.368 1.113   1.00 47.05  ? 827 HOH A O   1 
HETATM 13853 O O   . HOH H 3 .   ? 13.107  -0.904  25.948  1.00 37.46  ? 828 HOH A O   1 
HETATM 13854 O O   . HOH H 3 .   ? 16.360  29.793  11.140  1.00 36.78  ? 829 HOH A O   1 
HETATM 13855 O O   . HOH H 3 .   ? 39.925  18.240  16.412  1.00 52.35  ? 830 HOH A O   1 
HETATM 13856 O O   . HOH H 3 .   ? 32.121  12.776  15.012  1.00 30.89  ? 831 HOH A O   1 
HETATM 13857 O O   . HOH H 3 .   ? 5.910   -4.971  17.480  1.00 44.78  ? 832 HOH A O   1 
HETATM 13858 O O   . HOH H 3 .   ? -8.981  -8.206  7.477   1.00 51.17  ? 833 HOH A O   1 
HETATM 13859 O O   . HOH H 3 .   ? 20.795  7.804   -0.300  1.00 55.10  ? 834 HOH A O   1 
HETATM 13860 O O   . HOH H 3 .   ? 9.872   37.643  2.666   1.00 57.43  ? 835 HOH A O   1 
HETATM 13861 O O   . HOH H 3 .   ? 7.453   -11.371 25.782  1.00 61.16  ? 836 HOH A O   1 
HETATM 13862 O O   . HOH H 3 .   ? 49.477  14.597  16.109  1.00 46.22  ? 837 HOH A O   1 
HETATM 13863 O O   . HOH H 3 .   ? 20.524  8.905   -3.243  1.00 57.49  ? 838 HOH A O   1 
HETATM 13864 O O   . HOH H 3 .   ? 35.937  -20.948 31.874  1.00 48.13  ? 839 HOH A O   1 
HETATM 13865 O O   . HOH H 3 .   ? 8.160   -4.056  18.882  1.00 42.15  ? 840 HOH A O   1 
HETATM 13866 O O   . HOH H 3 .   ? 5.366   -7.875  18.435  1.00 51.75  ? 841 HOH A O   1 
HETATM 13867 O O   . HOH H 3 .   ? 5.029   -14.968 20.833  1.00 49.65  ? 842 HOH A O   1 
HETATM 13868 O O   . HOH H 3 .   ? -0.125  -26.255 16.119  1.00 63.00  ? 843 HOH A O   1 
HETATM 13869 O O   . HOH H 3 .   ? 51.407  0.557   3.400   1.00 53.09  ? 844 HOH A O   1 
HETATM 13870 O O   . HOH H 3 .   ? 43.138  18.896  9.249   1.00 50.66  ? 845 HOH A O   1 
HETATM 13871 O O   . HOH H 3 .   ? 40.818  19.275  10.812  1.00 53.45  ? 846 HOH A O   1 
HETATM 13872 O O   . HOH H 3 .   ? 22.949  5.715   -4.009  1.00 54.02  ? 847 HOH A O   1 
HETATM 13873 O O   . HOH H 3 .   ? 6.451   -23.846 19.456  1.00 55.40  ? 848 HOH A O   1 
HETATM 13874 O O   . HOH H 3 .   ? 6.370   -22.638 17.201  1.00 56.93  ? 849 HOH A O   1 
HETATM 13875 O O   . HOH H 3 .   ? 43.788  -24.217 24.470  1.00 47.12  ? 850 HOH A O   1 
HETATM 13876 O O   . HOH H 3 .   ? 8.426   4.118   6.336   1.00 53.53  ? 851 HOH A O   1 
HETATM 13877 O O   . HOH I 3 .   ? 13.653  7.325   23.825  1.00 114.58 ? 601 HOH D O   1 
HETATM 13878 O O   . HOH I 3 .   ? 24.695  28.058  31.618  1.00 49.90  ? 602 HOH D O   1 
HETATM 13879 O O   . HOH I 3 .   ? 3.184   31.223  19.352  1.00 34.03  ? 603 HOH D O   1 
HETATM 13880 O O   . HOH I 3 .   ? 39.911  28.269  39.520  1.00 48.13  ? 604 HOH D O   1 
HETATM 13881 O O   . HOH I 3 .   ? 34.391  12.598  -13.944 1.00 56.08  ? 605 HOH D O   1 
HETATM 13882 O O   . HOH I 3 .   ? 30.267  12.229  41.501  1.00 39.01  ? 606 HOH D O   1 
HETATM 13883 O O   . HOH I 3 .   ? 3.570   3.925   34.548  1.00 49.88  ? 607 HOH D O   1 
HETATM 13884 O O   . HOH I 3 .   ? -3.728  13.224  31.498  1.00 35.46  ? 608 HOH D O   1 
HETATM 13885 O O   . HOH I 3 .   ? 24.773  27.333  19.973  1.00 49.67  ? 609 HOH D O   1 
HETATM 13886 O O   . HOH I 3 .   ? 16.040  39.917  29.993  1.00 38.92  ? 610 HOH D O   1 
HETATM 13887 O O   . HOH I 3 .   ? 31.385  22.503  46.674  1.00 51.17  ? 611 HOH D O   1 
HETATM 13888 O O   . HOH I 3 .   ? 6.018   22.957  51.442  1.00 43.93  ? 612 HOH D O   1 
HETATM 13889 O O   . HOH I 3 .   ? 29.303  37.711  47.851  1.00 34.95  ? 613 HOH D O   1 
HETATM 13890 O O   . HOH I 3 .   ? 1.315   18.647  49.504  1.00 47.35  ? 614 HOH D O   1 
HETATM 13891 O O   . HOH I 3 .   ? -5.563  17.643  10.214  1.00 41.03  ? 615 HOH D O   1 
HETATM 13892 O O   . HOH I 3 .   ? 9.082   27.964  17.336  1.00 39.65  ? 616 HOH D O   1 
HETATM 13893 O O   . HOH I 3 .   ? 0.528   1.673   28.258  1.00 48.61  ? 617 HOH D O   1 
HETATM 13894 O O   . HOH I 3 .   ? 8.713   20.589  48.612  1.00 47.38  ? 618 HOH D O   1 
HETATM 13895 O O   . HOH I 3 .   ? 15.112  15.526  9.481   1.00 30.23  ? 619 HOH D O   1 
HETATM 13896 O O   . HOH I 3 .   ? 21.671  38.586  47.389  1.00 42.13  ? 620 HOH D O   1 
HETATM 13897 O O   . HOH I 3 .   ? 25.673  27.499  24.630  1.00 47.51  ? 621 HOH D O   1 
HETATM 13898 O O   . HOH I 3 .   ? 26.847  3.708   -0.566  1.00 40.11  ? 622 HOH D O   1 
HETATM 13899 O O   . HOH I 3 .   ? 13.300  37.631  41.895  1.00 43.54  ? 623 HOH D O   1 
HETATM 13900 O O   . HOH I 3 .   ? 5.459   7.361   32.930  1.00 29.51  ? 624 HOH D O   1 
HETATM 13901 O O   . HOH I 3 .   ? 2.210   27.217  40.585  1.00 36.01  ? 625 HOH D O   1 
HETATM 13902 O O   . HOH I 3 .   ? 15.356  35.840  23.299  1.00 34.56  ? 626 HOH D O   1 
HETATM 13903 O O   . HOH I 3 .   ? -3.116  15.946  31.520  1.00 30.82  ? 627 HOH D O   1 
HETATM 13904 O O   . HOH I 3 .   ? 2.897   -7.665  19.515  1.00 38.03  ? 628 HOH D O   1 
HETATM 13905 O O   . HOH I 3 .   ? 37.616  34.223  23.643  1.00 51.79  ? 629 HOH D O   1 
HETATM 13906 O O   . HOH I 3 .   ? 18.433  44.422  36.630  1.00 45.36  ? 630 HOH D O   1 
HETATM 13907 O O   . HOH I 3 .   ? 8.418   34.017  40.089  1.00 34.71  ? 631 HOH D O   1 
HETATM 13908 O O   . HOH I 3 .   ? 13.824  24.946  15.007  1.00 30.08  ? 632 HOH D O   1 
HETATM 13909 O O   . HOH I 3 .   ? 18.678  7.587   4.023   1.00 32.32  ? 633 HOH D O   1 
HETATM 13910 O O   . HOH I 3 .   ? 8.513   26.338  38.976  1.00 31.15  ? 634 HOH D O   1 
HETATM 13911 O O   . HOH I 3 .   ? 23.312  17.781  16.621  1.00 31.54  ? 635 HOH D O   1 
HETATM 13912 O O   . HOH I 3 .   ? 37.175  45.737  39.997  1.00 51.30  ? 636 HOH D O   1 
HETATM 13913 O O   . HOH I 3 .   ? 35.226  42.294  41.883  1.00 50.38  ? 637 HOH D O   1 
HETATM 13914 O O   . HOH I 3 .   ? -3.261  12.618  0.996   1.00 49.93  ? 638 HOH D O   1 
HETATM 13915 O O   . HOH I 3 .   ? 30.536  15.298  41.815  1.00 36.05  ? 639 HOH D O   1 
HETATM 13916 O O   . HOH I 3 .   ? 2.288   35.822  40.643  1.00 45.38  ? 640 HOH D O   1 
HETATM 13917 O O   . HOH I 3 .   ? -9.106  20.954  16.104  1.00 41.07  ? 641 HOH D O   1 
HETATM 13918 O O   . HOH I 3 .   ? 21.410  22.048  50.757  1.00 44.74  ? 642 HOH D O   1 
HETATM 13919 O O   . HOH I 3 .   ? 36.838  42.733  39.815  1.00 49.59  ? 643 HOH D O   1 
HETATM 13920 O O   . HOH I 3 .   ? 1.344   15.143  10.719  1.00 43.86  ? 644 HOH D O   1 
HETATM 13921 O O   . HOH I 3 .   ? 32.008  36.403  45.137  1.00 44.35  ? 645 HOH D O   1 
HETATM 13922 O O   . HOH I 3 .   ? 39.087  50.468  36.438  1.00 51.36  ? 646 HOH D O   1 
HETATM 13923 O O   . HOH I 3 .   ? -0.487  22.331  -0.826  1.00 39.52  ? 647 HOH D O   1 
HETATM 13924 O O   . HOH I 3 .   ? 0.527   25.212  4.978   1.00 44.21  ? 648 HOH D O   1 
HETATM 13925 O O   . HOH I 3 .   ? 1.108   8.149   33.528  1.00 42.47  ? 649 HOH D O   1 
HETATM 13926 O O   . HOH I 3 .   ? 5.244   30.837  33.535  1.00 33.44  ? 650 HOH D O   1 
HETATM 13927 O O   . HOH I 3 .   ? 16.317  39.209  34.485  1.00 36.03  ? 651 HOH D O   1 
HETATM 13928 O O   . HOH I 3 .   ? 19.647  44.945  29.524  1.00 55.99  ? 652 HOH D O   1 
HETATM 13929 O O   . HOH I 3 .   ? 40.545  40.134  46.284  1.00 47.20  ? 653 HOH D O   1 
HETATM 13930 O O   . HOH I 3 .   ? 9.289   8.675   20.428  1.00 23.25  ? 654 HOH D O   1 
HETATM 13931 O O   . HOH I 3 .   ? -1.083  34.895  31.444  1.00 42.66  ? 655 HOH D O   1 
HETATM 13932 O O   . HOH I 3 .   ? 31.823  45.404  38.105  1.00 41.26  ? 656 HOH D O   1 
HETATM 13933 O O   . HOH I 3 .   ? -6.385  15.411  17.964  1.00 43.58  ? 657 HOH D O   1 
HETATM 13934 O O   . HOH I 3 .   ? 22.437  47.250  40.613  1.00 40.19  ? 658 HOH D O   1 
HETATM 13935 O O   . HOH I 3 .   ? 45.127  43.833  40.366  1.00 48.03  ? 659 HOH D O   1 
HETATM 13936 O O   . HOH I 3 .   ? 9.093   7.802   14.112  1.00 25.40  ? 660 HOH D O   1 
HETATM 13937 O O   . HOH I 3 .   ? 10.950  41.465  30.279  1.00 48.99  ? 661 HOH D O   1 
HETATM 13938 O O   . HOH I 3 .   ? 17.413  -0.807  41.683  1.00 49.69  ? 662 HOH D O   1 
HETATM 13939 O O   . HOH I 3 .   ? 20.109  44.538  45.923  1.00 47.44  ? 663 HOH D O   1 
HETATM 13940 O O   . HOH I 3 .   ? 22.805  1.465   41.808  1.00 37.65  ? 664 HOH D O   1 
HETATM 13941 O O   . HOH I 3 .   ? 15.574  27.802  12.908  1.00 48.43  ? 665 HOH D O   1 
HETATM 13942 O O   . HOH I 3 .   ? 47.800  32.269  28.651  1.00 53.87  ? 666 HOH D O   1 
HETATM 13943 O O   . HOH I 3 .   ? 43.640  33.578  31.163  1.00 46.24  ? 667 HOH D O   1 
HETATM 13944 O O   . HOH I 3 .   ? 23.350  42.492  28.479  1.00 47.34  ? 668 HOH D O   1 
HETATM 13945 O O   . HOH I 3 .   ? 6.203   26.030  13.039  1.00 43.76  ? 669 HOH D O   1 
HETATM 13946 O O   . HOH I 3 .   ? 14.692  22.441  52.060  1.00 48.29  ? 670 HOH D O   1 
HETATM 13947 O O   . HOH I 3 .   ? -0.726  18.024  43.169  1.00 51.13  ? 671 HOH D O   1 
HETATM 13948 O O   . HOH I 3 .   ? 11.535  -1.329  31.331  1.00 34.65  ? 672 HOH D O   1 
HETATM 13949 O O   . HOH I 3 .   ? -8.085  27.557  15.040  1.00 54.02  ? 673 HOH D O   1 
HETATM 13950 O O   . HOH I 3 .   ? 0.358   10.387  17.397  1.00 29.01  ? 674 HOH D O   1 
HETATM 13951 O O   . HOH I 3 .   ? -2.235  24.130  15.701  1.00 44.91  ? 675 HOH D O   1 
HETATM 13952 O O   . HOH I 3 .   ? 5.511   27.422  45.306  1.00 51.07  ? 676 HOH D O   1 
HETATM 13953 O O   . HOH I 3 .   ? -0.846  0.254   15.267  1.00 47.77  ? 677 HOH D O   1 
HETATM 13954 O O   . HOH I 3 .   ? 38.144  40.358  40.250  1.00 44.54  ? 678 HOH D O   1 
HETATM 13955 O O   . HOH I 3 .   ? 10.294  30.391  17.933  1.00 31.54  ? 679 HOH D O   1 
HETATM 13956 O O   . HOH I 3 .   ? -3.273  18.324  48.324  1.00 52.27  ? 680 HOH D O   1 
HETATM 13957 O O   . HOH I 3 .   ? 4.603   15.589  9.600   1.00 36.86  ? 681 HOH D O   1 
HETATM 13958 O O   . HOH I 3 .   ? 16.742  22.494  22.422  1.00 32.26  ? 682 HOH D O   1 
HETATM 13959 O O   . HOH I 3 .   ? 31.292  23.490  21.589  1.00 41.41  ? 683 HOH D O   1 
HETATM 13960 O O   . HOH I 3 .   ? -3.675  19.259  37.898  1.00 48.44  ? 684 HOH D O   1 
HETATM 13961 O O   . HOH I 3 .   ? 25.411  31.214  49.684  1.00 62.87  ? 685 HOH D O   1 
HETATM 13962 O O   . HOH I 3 .   ? 29.653  34.423  42.858  1.00 34.85  ? 686 HOH D O   1 
HETATM 13963 O O   . HOH I 3 .   ? 41.324  33.244  21.359  1.00 52.13  ? 687 HOH D O   1 
HETATM 13964 O O   . HOH I 3 .   ? 9.606   5.797   10.318  1.00 30.28  ? 688 HOH D O   1 
HETATM 13965 O O   . HOH I 3 .   ? 27.501  24.365  31.150  1.00 49.92  ? 689 HOH D O   1 
HETATM 13966 O O   . HOH I 3 .   ? 1.311   23.056  42.979  1.00 49.16  ? 690 HOH D O   1 
HETATM 13967 O O   . HOH I 3 .   ? 13.781  23.598  -5.913  1.00 41.75  ? 691 HOH D O   1 
HETATM 13968 O O   . HOH I 3 .   ? 31.624  19.285  41.939  1.00 55.30  ? 692 HOH D O   1 
HETATM 13969 O O   . HOH I 3 .   ? 24.556  25.421  50.111  1.00 58.19  ? 693 HOH D O   1 
HETATM 13970 O O   . HOH I 3 .   ? 33.102  21.953  42.131  1.00 42.14  ? 694 HOH D O   1 
HETATM 13971 O O   . HOH I 3 .   ? 20.288  -2.278  47.694  1.00 52.78  ? 695 HOH D O   1 
HETATM 13972 O O   . HOH I 3 .   ? 2.458   9.004   14.918  1.00 39.58  ? 696 HOH D O   1 
HETATM 13973 O O   . HOH I 3 .   ? -7.378  29.421  31.417  1.00 51.19  ? 697 HOH D O   1 
HETATM 13974 O O   . HOH I 3 .   ? 30.246  22.597  26.901  1.00 51.75  ? 698 HOH D O   1 
HETATM 13975 O O   . HOH I 3 .   ? -6.161  26.015  37.972  1.00 48.95  ? 699 HOH D O   1 
HETATM 13976 O O   . HOH I 3 .   ? 10.460  -0.232  42.011  1.00 41.85  ? 700 HOH D O   1 
HETATM 13977 O O   . HOH I 3 .   ? 12.550  29.250  48.678  1.00 43.16  ? 701 HOH D O   1 
HETATM 13978 O O   . HOH I 3 .   ? 19.827  32.934  22.478  1.00 42.95  ? 702 HOH D O   1 
HETATM 13979 O O   . HOH I 3 .   ? 30.690  5.651   0.688   1.00 32.75  ? 703 HOH D O   1 
HETATM 13980 O O   . HOH I 3 .   ? 26.039  8.974   45.059  1.00 32.85  ? 704 HOH D O   1 
HETATM 13981 O O   . HOH I 3 .   ? -7.100  24.010  21.829  1.00 39.93  ? 705 HOH D O   1 
HETATM 13982 O O   . HOH I 3 .   ? 8.131   31.705  45.925  1.00 43.13  ? 706 HOH D O   1 
HETATM 13983 O O   . HOH I 3 .   ? 32.785  22.949  13.042  1.00 50.67  ? 707 HOH D O   1 
HETATM 13984 O O   . HOH I 3 .   ? -3.700  28.151  17.927  1.00 48.64  ? 708 HOH D O   1 
HETATM 13985 O O   . HOH I 3 .   ? -1.223  9.388   33.748  1.00 52.16  ? 709 HOH D O   1 
HETATM 13986 O O   . HOH I 3 .   ? -7.034  17.723  36.144  1.00 40.45  ? 710 HOH D O   1 
HETATM 13987 O O   . HOH I 3 .   ? -7.561  24.730  19.219  1.00 48.31  ? 711 HOH D O   1 
HETATM 13988 O O   . HOH I 3 .   ? 42.969  28.261  29.130  1.00 58.58  ? 712 HOH D O   1 
HETATM 13989 O O   . HOH I 3 .   ? -6.062  27.655  19.989  1.00 52.08  ? 713 HOH D O   1 
HETATM 13990 O O   . HOH I 3 .   ? 19.455  28.016  51.376  1.00 41.39  ? 714 HOH D O   1 
HETATM 13991 O O   . HOH I 3 .   ? 4.880   7.472   36.734  1.00 49.17  ? 715 HOH D O   1 
HETATM 13992 O O   . HOH I 3 .   ? -0.490  33.670  23.289  1.00 35.51  ? 716 HOH D O   1 
HETATM 13993 O O   . HOH I 3 .   ? 47.307  49.407  34.809  1.00 56.63  ? 717 HOH D O   1 
HETATM 13994 O O   . HOH I 3 .   ? 21.524  26.750  7.554   1.00 51.54  ? 718 HOH D O   1 
HETATM 13995 O O   . HOH I 3 .   ? 37.599  21.892  30.511  1.00 46.50  ? 719 HOH D O   1 
HETATM 13996 O O   . HOH I 3 .   ? 34.525  17.317  42.375  1.00 53.13  ? 720 HOH D O   1 
HETATM 13997 O O   . HOH I 3 .   ? 5.923   7.973   11.333  1.00 35.77  ? 721 HOH D O   1 
HETATM 13998 O O   . HOH I 3 .   ? -5.849  13.772  4.159   1.00 52.21  ? 722 HOH D O   1 
HETATM 13999 O O   . HOH I 3 .   ? -7.029  11.405  28.321  1.00 62.76  ? 723 HOH D O   1 
HETATM 14000 O O   . HOH I 3 .   ? 30.424  45.977  48.093  1.00 50.09  ? 724 HOH D O   1 
HETATM 14001 O O   . HOH I 3 .   ? 3.595   22.264  16.658  1.00 38.90  ? 725 HOH D O   1 
HETATM 14002 O O   . HOH I 3 .   ? -0.947  12.175  43.535  1.00 46.55  ? 726 HOH D O   1 
HETATM 14003 O O   . HOH I 3 .   ? 15.905  39.987  22.692  1.00 43.70  ? 727 HOH D O   1 
HETATM 14004 O O   . HOH I 3 .   ? 48.841  36.529  30.674  1.00 53.32  ? 728 HOH D O   1 
HETATM 14005 O O   . HOH I 3 .   ? 1.910   15.851  47.602  1.00 61.93  ? 729 HOH D O   1 
HETATM 14006 O O   . HOH I 3 .   ? 33.651  2.907   41.107  1.00 46.87  ? 730 HOH D O   1 
HETATM 14007 O O   . HOH I 3 .   ? -3.028  24.339  51.010  1.00 55.88  ? 731 HOH D O   1 
HETATM 14008 O O   . HOH I 3 .   ? 9.386   -0.950  30.197  1.00 43.04  ? 732 HOH D O   1 
HETATM 14009 O O   . HOH I 3 .   ? 3.522   4.878   9.712   1.00 59.70  ? 733 HOH D O   1 
HETATM 14010 O O   . HOH I 3 .   ? -9.033  24.500  13.186  1.00 46.87  ? 734 HOH D O   1 
HETATM 14011 O O   . HOH I 3 .   ? 24.510  21.492  54.401  1.00 57.04  ? 735 HOH D O   1 
HETATM 14012 O O   . HOH I 3 .   ? 36.766  2.557   -3.575  1.00 57.42  ? 736 HOH D O   1 
HETATM 14013 O O   . HOH I 3 .   ? 32.486  51.079  35.304  1.00 48.69  ? 737 HOH D O   1 
HETATM 14014 O O   . HOH I 3 .   ? -7.757  18.678  9.843   1.00 46.89  ? 738 HOH D O   1 
HETATM 14015 O O   . HOH I 3 .   ? 6.642   -3.610  26.880  1.00 60.35  ? 739 HOH D O   1 
HETATM 14016 O O   . HOH I 3 .   ? 26.483  29.366  19.735  1.00 48.74  ? 740 HOH D O   1 
HETATM 14017 O O   . HOH I 3 .   ? 32.205  47.134  35.762  1.00 43.88  ? 741 HOH D O   1 
HETATM 14018 O O   . HOH I 3 .   ? 7.021   6.437   12.824  1.00 42.06  ? 742 HOH D O   1 
HETATM 14019 O O   . HOH I 3 .   ? -6.762  28.332  39.577  1.00 48.48  ? 743 HOH D O   1 
HETATM 14020 O O   . HOH I 3 .   ? 9.236   6.043   7.754   1.00 48.31  ? 744 HOH D O   1 
HETATM 14021 O O   . HOH I 3 .   ? 21.436  48.210  38.264  1.00 54.11  ? 745 HOH D O   1 
HETATM 14022 O O   . HOH I 3 .   ? 10.351  3.398   10.092  1.00 43.78  ? 746 HOH D O   1 
HETATM 14023 O O   . HOH I 3 .   ? 6.136   7.134   8.256   1.00 46.78  ? 747 HOH D O   1 
HETATM 14024 O O   . HOH I 3 .   ? 22.691  15.636  -10.187 1.00 52.54  ? 748 HOH D O   1 
HETATM 14025 O O   . HOH I 3 .   ? 32.510  20.215  46.979  1.00 56.19  ? 749 HOH D O   1 
HETATM 14026 O O   . HOH I 3 .   ? 4.108   5.458   5.777   1.00 50.97  ? 750 HOH D O   1 
HETATM 14027 O O   . HOH J 3 .   ? 26.880  18.778  -29.091 1.00 52.53  ? 601 HOH B O   1 
HETATM 14028 O O   . HOH J 3 .   ? 22.379  34.488  -35.557 1.00 43.80  ? 602 HOH B O   1 
HETATM 14029 O O   . HOH J 3 .   ? -12.060 21.833  -47.118 1.00 45.08  ? 603 HOH B O   1 
HETATM 14030 O O   . HOH J 3 .   ? 19.912  13.876  -38.357 1.00 38.87  ? 604 HOH B O   1 
HETATM 14031 O O   . HOH J 3 .   ? 8.140   1.717   -33.073 1.00 35.83  ? 605 HOH B O   1 
HETATM 14032 O O   . HOH J 3 .   ? 3.735   10.260  -49.468 1.00 44.37  ? 606 HOH B O   1 
HETATM 14033 O O   . HOH J 3 .   ? -29.648 3.164   -30.390 1.00 59.85  ? 607 HOH B O   1 
HETATM 14034 O O   . HOH J 3 .   ? -14.256 15.283  -15.518 1.00 40.57  ? 608 HOH B O   1 
HETATM 14035 O O   . HOH J 3 .   ? 7.906   7.401   -28.088 1.00 32.32  ? 609 HOH B O   1 
HETATM 14036 O O   . HOH J 3 .   ? -1.445  16.492  -37.191 1.00 29.87  ? 610 HOH B O   1 
HETATM 14037 O O   . HOH J 3 .   ? -1.607  45.934  -37.324 1.00 31.59  ? 611 HOH B O   1 
HETATM 14038 O O   . HOH J 3 .   ? 7.363   14.134  -10.906 1.00 37.29  ? 612 HOH B O   1 
HETATM 14039 O O   . HOH J 3 .   ? -14.387 22.642  -24.323 1.00 32.35  ? 613 HOH B O   1 
HETATM 14040 O O   . HOH J 3 .   ? 2.250   16.708  -3.983  1.00 56.33  ? 614 HOH B O   1 
HETATM 14041 O O   . HOH J 3 .   ? -10.490 2.145   -19.277 1.00 42.45  ? 615 HOH B O   1 
HETATM 14042 O O   . HOH J 3 .   ? -15.990 -3.076  -43.116 1.00 44.37  ? 616 HOH B O   1 
HETATM 14043 O O   . HOH J 3 .   ? -21.786 12.716  -32.119 1.00 38.16  ? 617 HOH B O   1 
HETATM 14044 O O   . HOH J 3 .   ? -15.793 -3.140  -31.593 1.00 40.95  ? 618 HOH B O   1 
HETATM 14045 O O   . HOH J 3 .   ? 16.098  7.161   -41.842 1.00 39.18  ? 619 HOH B O   1 
HETATM 14046 O O   . HOH J 3 .   ? 0.267   5.950   -44.410 1.00 42.17  ? 620 HOH B O   1 
HETATM 14047 O O   . HOH J 3 .   ? 17.018  33.833  -49.548 1.00 42.89  ? 621 HOH B O   1 
HETATM 14048 O O   . HOH J 3 .   ? 17.601  39.688  -53.382 1.00 54.04  ? 622 HOH B O   1 
HETATM 14049 O O   . HOH J 3 .   ? 7.289   -0.186  -39.977 1.00 52.90  ? 623 HOH B O   1 
HETATM 14050 O O   . HOH J 3 .   ? 15.295  40.762  -23.142 1.00 32.99  ? 624 HOH B O   1 
HETATM 14051 O O   . HOH J 3 .   ? -19.165 -4.163  -37.636 1.00 42.45  ? 625 HOH B O   1 
HETATM 14052 O O   . HOH J 3 .   ? 10.728  9.674   -50.196 1.00 49.33  ? 626 HOH B O   1 
HETATM 14053 O O   . HOH J 3 .   ? 19.923  19.730  -25.333 1.00 30.86  ? 627 HOH B O   1 
HETATM 14054 O O   . HOH J 3 .   ? 3.363   0.505   -21.418 1.00 36.54  ? 628 HOH B O   1 
HETATM 14055 O O   . HOH J 3 .   ? 22.386  8.014   -28.713 1.00 42.20  ? 629 HOH B O   1 
HETATM 14056 O O   . HOH J 3 .   ? -0.851  23.556  -6.124  1.00 39.69  ? 630 HOH B O   1 
HETATM 14057 O O   . HOH J 3 .   ? -12.424 13.867  -54.349 1.00 52.52  ? 631 HOH B O   1 
HETATM 14058 O O   . HOH J 3 .   ? -13.151 4.357   -16.857 1.00 44.90  ? 632 HOH B O   1 
HETATM 14059 O O   . HOH J 3 .   ? -7.954  12.240  -33.791 1.00 31.89  ? 633 HOH B O   1 
HETATM 14060 O O   . HOH J 3 .   ? -3.461  -5.317  -31.225 1.00 37.71  ? 634 HOH B O   1 
HETATM 14061 O O   . HOH J 3 .   ? 7.803   22.779  -43.590 1.00 39.41  ? 635 HOH B O   1 
HETATM 14062 O O   . HOH J 3 .   ? -2.877  33.647  -52.119 1.00 54.25  ? 636 HOH B O   1 
HETATM 14063 O O   . HOH J 3 .   ? -9.299  10.693  -51.015 1.00 48.96  ? 637 HOH B O   1 
HETATM 14064 O O   . HOH J 3 .   ? -14.704 21.084  -16.748 1.00 40.28  ? 638 HOH B O   1 
HETATM 14065 O O   . HOH J 3 .   ? 10.250  24.407  -43.659 1.00 40.86  ? 639 HOH B O   1 
HETATM 14066 O O   . HOH J 3 .   ? -5.948  36.258  -51.970 1.00 44.52  ? 640 HOH B O   1 
HETATM 14067 O O   . HOH J 3 .   ? -4.980  30.662  -49.261 1.00 50.48  ? 641 HOH B O   1 
HETATM 14068 O O   . HOH J 3 .   ? 6.112   34.137  -19.569 1.00 34.93  ? 642 HOH B O   1 
HETATM 14069 O O   . HOH J 3 .   ? -8.401  23.398  -21.979 1.00 32.77  ? 643 HOH B O   1 
HETATM 14070 O O   . HOH J 3 .   ? 3.566   45.874  -51.666 1.00 44.75  ? 644 HOH B O   1 
HETATM 14071 O O   . HOH J 3 .   ? 14.110  7.797   -14.070 1.00 50.98  ? 645 HOH B O   1 
HETATM 14072 O O   . HOH J 3 .   ? 4.881   36.580  -35.316 1.00 28.13  ? 646 HOH B O   1 
HETATM 14073 O O   . HOH J 3 .   ? -4.540  34.881  -48.841 1.00 47.85  ? 647 HOH B O   1 
HETATM 14074 O O   . HOH J 3 .   ? 3.221   42.205  -55.782 1.00 46.84  ? 648 HOH B O   1 
HETATM 14075 O O   . HOH J 3 .   ? -21.763 14.412  -44.089 1.00 49.64  ? 649 HOH B O   1 
HETATM 14076 O O   . HOH J 3 .   ? 13.995  1.323   -29.039 1.00 48.66  ? 650 HOH B O   1 
HETATM 14077 O O   . HOH J 3 .   ? 5.060   4.178   -45.315 1.00 39.21  ? 651 HOH B O   1 
HETATM 14078 O O   . HOH J 3 .   ? 11.981  17.410  -47.168 1.00 41.40  ? 652 HOH B O   1 
HETATM 14079 O O   . HOH J 3 .   ? 15.790  36.313  -38.151 1.00 39.10  ? 653 HOH B O   1 
HETATM 14080 O O   . HOH J 3 .   ? 1.003   13.117  -45.041 1.00 25.71  ? 654 HOH B O   1 
HETATM 14081 O O   . HOH J 3 .   ? -10.107 15.137  -45.349 1.00 27.84  ? 655 HOH B O   1 
HETATM 14082 O O   . HOH J 3 .   ? -13.437 53.169  -40.857 1.00 41.11  ? 656 HOH B O   1 
HETATM 14083 O O   . HOH J 3 .   ? 7.849   38.517  -30.563 1.00 24.29  ? 657 HOH B O   1 
HETATM 14084 O O   . HOH J 3 .   ? 17.619  7.427   -39.568 1.00 41.60  ? 658 HOH B O   1 
HETATM 14085 O O   . HOH J 3 .   ? -19.790 16.551  -52.885 1.00 52.13  ? 659 HOH B O   1 
HETATM 14086 O O   . HOH J 3 .   ? 18.920  10.773  -41.418 1.00 55.46  ? 660 HOH B O   1 
HETATM 14087 O O   . HOH J 3 .   ? 4.339   -3.200  -39.176 1.00 51.77  ? 661 HOH B O   1 
HETATM 14088 O O   . HOH J 3 .   ? -22.274 14.406  -34.104 1.00 43.64  ? 662 HOH B O   1 
HETATM 14089 O O   . HOH J 3 .   ? -2.165  9.561   -10.059 1.00 45.21  ? 663 HOH B O   1 
HETATM 14090 O O   . HOH J 3 .   ? -13.046 -1.678  -24.885 1.00 48.84  ? 664 HOH B O   1 
HETATM 14091 O O   . HOH J 3 .   ? -19.419 35.603  -39.750 1.00 36.86  ? 665 HOH B O   1 
HETATM 14092 O O   . HOH J 3 .   ? 18.606  42.148  -27.019 1.00 36.48  ? 666 HOH B O   1 
HETATM 14093 O O   . HOH J 3 .   ? -14.865 10.136  -20.615 1.00 51.08  ? 667 HOH B O   1 
HETATM 14094 O O   . HOH J 3 .   ? 4.347   34.186  -38.399 1.00 37.15  ? 668 HOH B O   1 
HETATM 14095 O O   . HOH J 3 .   ? 20.785  44.746  -40.822 1.00 48.27  ? 669 HOH B O   1 
HETATM 14096 O O   . HOH J 3 .   ? 20.663  13.256  -23.432 1.00 50.83  ? 670 HOH B O   1 
HETATM 14097 O O   . HOH J 3 .   ? -0.832  8.237   -44.634 1.00 34.69  ? 671 HOH B O   1 
HETATM 14098 O O   . HOH J 3 .   ? 2.168   35.913  -36.712 1.00 43.20  ? 672 HOH B O   1 
HETATM 14099 O O   . HOH J 3 .   ? -12.694 17.055  -36.672 1.00 41.85  ? 673 HOH B O   1 
HETATM 14100 O O   . HOH J 3 .   ? 16.264  1.217   -17.118 1.00 52.38  ? 674 HOH B O   1 
HETATM 14101 O O   . HOH J 3 .   ? 13.749  19.444  -44.946 1.00 50.78  ? 675 HOH B O   1 
HETATM 14102 O O   . HOH J 3 .   ? 16.352  34.258  -30.330 1.00 29.13  ? 676 HOH B O   1 
HETATM 14103 O O   . HOH J 3 .   ? 3.318   -2.225  -34.498 1.00 43.55  ? 677 HOH B O   1 
HETATM 14104 O O   . HOH J 3 .   ? 13.460  16.052  -14.048 1.00 39.88  ? 678 HOH B O   1 
HETATM 14105 O O   . HOH J 3 .   ? -10.387 22.819  -36.100 1.00 40.93  ? 679 HOH B O   1 
HETATM 14106 O O   . HOH J 3 .   ? -3.287  15.978  -43.403 1.00 27.37  ? 680 HOH B O   1 
HETATM 14107 O O   . HOH J 3 .   ? 16.797  14.472  -43.744 1.00 44.02  ? 681 HOH B O   1 
HETATM 14108 O O   . HOH J 3 .   ? -25.642 8.003   -34.962 1.00 49.77  ? 682 HOH B O   1 
HETATM 14109 O O   . HOH J 3 .   ? 14.405  0.113   -34.164 1.00 59.63  ? 683 HOH B O   1 
HETATM 14110 O O   . HOH J 3 .   ? 0.939   -0.161  -23.408 1.00 49.33  ? 684 HOH B O   1 
HETATM 14111 O O   . HOH J 3 .   ? 11.453  8.628   -34.905 1.00 31.93  ? 685 HOH B O   1 
HETATM 14112 O O   . HOH J 3 .   ? 23.670  22.259  -37.629 1.00 44.59  ? 686 HOH B O   1 
HETATM 14113 O O   . HOH J 3 .   ? -17.088 15.824  -28.314 1.00 48.08  ? 687 HOH B O   1 
HETATM 14114 O O   . HOH J 3 .   ? -14.052 13.315  -17.448 1.00 50.91  ? 688 HOH B O   1 
HETATM 14115 O O   . HOH J 3 .   ? -13.141 -0.494  -31.214 1.00 44.56  ? 689 HOH B O   1 
HETATM 14116 O O   . HOH J 3 .   ? -8.358  24.610  -36.227 1.00 32.55  ? 690 HOH B O   1 
HETATM 14117 O O   . HOH J 3 .   ? 5.420   -1.468  -24.847 1.00 57.39  ? 691 HOH B O   1 
HETATM 14118 O O   . HOH J 3 .   ? 20.082  16.782  -37.601 1.00 42.42  ? 692 HOH B O   1 
HETATM 14119 O O   . HOH J 3 .   ? -4.405  -2.407  -24.051 1.00 47.55  ? 693 HOH B O   1 
HETATM 14120 O O   . HOH J 3 .   ? 16.292  16.919  -44.781 1.00 47.80  ? 694 HOH B O   1 
HETATM 14121 O O   . HOH J 3 .   ? -14.653 36.084  -38.552 1.00 36.24  ? 695 HOH B O   1 
HETATM 14122 O O   . HOH J 3 .   ? 20.210  5.725   -38.099 1.00 41.04  ? 696 HOH B O   1 
HETATM 14123 O O   . HOH J 3 .   ? 8.052   35.539  -20.414 1.00 26.84  ? 697 HOH B O   1 
HETATM 14124 O O   . HOH J 3 .   ? 20.345  22.262  -43.147 1.00 45.79  ? 698 HOH B O   1 
HETATM 14125 O O   . HOH J 3 .   ? -1.217  -8.626  -36.231 1.00 55.51  ? 699 HOH B O   1 
HETATM 14126 O O   . HOH J 3 .   ? -26.802 2.361   -54.292 1.00 47.11  ? 700 HOH B O   1 
HETATM 14127 O O   . HOH J 3 .   ? 14.719  36.072  -12.768 1.00 55.56  ? 701 HOH B O   1 
HETATM 14128 O O   . HOH J 3 .   ? 19.603  28.325  -22.374 1.00 37.26  ? 702 HOH B O   1 
HETATM 14129 O O   . HOH J 3 .   ? 20.840  30.339  -22.794 1.00 51.63  ? 703 HOH B O   1 
HETATM 14130 O O   . HOH J 3 .   ? 15.314  5.300   -14.672 1.00 55.63  ? 704 HOH B O   1 
HETATM 14131 O O   . HOH J 3 .   ? 12.316  36.576  -39.548 1.00 43.43  ? 705 HOH B O   1 
HETATM 14132 O O   . HOH J 3 .   ? -26.610 12.259  -37.902 1.00 59.80  ? 706 HOH B O   1 
HETATM 14133 O O   . HOH J 3 .   ? 13.216  26.865  -40.050 1.00 36.79  ? 707 HOH B O   1 
HETATM 14134 O O   . HOH J 3 .   ? 7.271   42.832  -31.463 1.00 33.91  ? 708 HOH B O   1 
HETATM 14135 O O   . HOH J 3 .   ? -25.886 -4.460  -49.773 1.00 57.24  ? 709 HOH B O   1 
HETATM 14136 O O   . HOH J 3 .   ? -11.999 -4.078  -26.899 1.00 53.33  ? 710 HOH B O   1 
HETATM 14137 O O   . HOH J 3 .   ? 2.649   -7.491  -30.083 1.00 54.39  ? 711 HOH B O   1 
HETATM 14138 O O   . HOH J 3 .   ? -9.632  14.604  -10.777 1.00 39.74  ? 712 HOH B O   1 
HETATM 14139 O O   . HOH J 3 .   ? -21.309 52.774  -40.829 1.00 51.35  ? 713 HOH B O   1 
HETATM 14140 O O   . HOH J 3 .   ? -15.857 5.616   -51.213 1.00 51.48  ? 714 HOH B O   1 
HETATM 14141 O O   . HOH J 3 .   ? -9.017  -8.591  -35.198 1.00 44.48  ? 715 HOH B O   1 
HETATM 14142 O O   . HOH J 3 .   ? -25.493 0.246   -50.722 1.00 50.39  ? 716 HOH B O   1 
HETATM 14143 O O   . HOH J 3 .   ? -22.986 0.235   -30.264 1.00 43.34  ? 717 HOH B O   1 
HETATM 14144 O O   . HOH J 3 .   ? 13.908  38.612  -41.102 1.00 44.26  ? 718 HOH B O   1 
HETATM 14145 O O   . HOH J 3 .   ? 21.719  37.755  -45.505 1.00 47.49  ? 719 HOH B O   1 
HETATM 14146 O O   . HOH J 3 .   ? 8.434   21.554  -5.612  1.00 33.09  ? 720 HOH B O   1 
HETATM 14147 O O   . HOH J 3 .   ? 16.985  6.016   -24.975 1.00 54.18  ? 721 HOH B O   1 
HETATM 14148 O O   . HOH J 3 .   ? -12.937 19.440  -35.593 1.00 48.51  ? 722 HOH B O   1 
HETATM 14149 O O   . HOH J 3 .   ? 13.198  44.873  -54.251 1.00 56.84  ? 723 HOH B O   1 
HETATM 14150 O O   . HOH J 3 .   ? -22.742 22.491  -48.723 1.00 59.53  ? 724 HOH B O   1 
HETATM 14151 O O   . HOH J 3 .   ? -32.269 1.262   -48.321 1.00 47.28  ? 725 HOH B O   1 
HETATM 14152 O O   . HOH J 3 .   ? -31.631 -2.468  -39.272 1.00 49.84  ? 726 HOH B O   1 
HETATM 14153 O O   . HOH J 3 .   ? 6.146   34.302  -14.849 1.00 47.05  ? 727 HOH B O   1 
HETATM 14154 O O   . HOH J 3 .   ? 12.877  42.894  -39.887 1.00 49.99  ? 728 HOH B O   1 
HETATM 14155 O O   . HOH J 3 .   ? -20.070 37.662  -52.384 1.00 43.91  ? 729 HOH B O   1 
HETATM 14156 O O   . HOH J 3 .   ? 5.772   34.753  -33.490 1.00 27.74  ? 730 HOH B O   1 
HETATM 14157 O O   . HOH J 3 .   ? -31.819 -2.011  -54.990 1.00 39.02  ? 731 HOH B O   1 
HETATM 14158 O O   . HOH J 3 .   ? -8.537  26.451  -55.374 1.00 55.51  ? 732 HOH B O   1 
HETATM 14159 O O   . HOH J 3 .   ? 19.517  34.420  -50.462 1.00 61.86  ? 733 HOH B O   1 
HETATM 14160 O O   . HOH J 3 .   ? 8.186   37.227  -18.973 1.00 47.13  ? 734 HOH B O   1 
HETATM 14161 O O   . HOH J 3 .   ? 24.229  23.325  -39.934 1.00 41.26  ? 735 HOH B O   1 
HETATM 14162 O O   . HOH J 3 .   ? 4.337   15.570  -5.160  1.00 46.97  ? 736 HOH B O   1 
HETATM 14163 O O   . HOH J 3 .   ? -18.370 17.836  -29.101 1.00 33.31  ? 737 HOH B O   1 
HETATM 14164 O O   . HOH J 3 .   ? -21.538 20.700  -8.844  1.00 60.14  ? 738 HOH B O   1 
HETATM 14165 O O   . HOH J 3 .   ? 16.410  4.953   -43.458 1.00 51.70  ? 739 HOH B O   1 
HETATM 14166 O O   . HOH J 3 .   ? -24.673 14.563  -35.113 1.00 54.56  ? 740 HOH B O   1 
HETATM 14167 O O   . HOH J 3 .   ? 22.323  38.265  -42.977 1.00 46.85  ? 741 HOH B O   1 
HETATM 14168 O O   . HOH J 3 .   ? 16.779  9.410   -43.732 1.00 50.45  ? 742 HOH B O   1 
HETATM 14169 O O   . HOH J 3 .   ? 6.340   44.681  -29.984 1.00 36.99  ? 743 HOH B O   1 
HETATM 14170 O O   . HOH J 3 .   ? 16.495  11.889  -45.351 1.00 50.67  ? 744 HOH B O   1 
HETATM 14171 O O   . HOH J 3 .   ? -21.276 -1.145  -28.164 1.00 58.44  ? 745 HOH B O   1 
HETATM 14172 O O   . HOH J 3 .   ? 15.276  43.379  -38.545 1.00 55.72  ? 746 HOH B O   1 
HETATM 14173 O O   . HOH J 3 .   ? 5.510   46.674  -57.584 1.00 52.54  ? 747 HOH B O   1 
HETATM 14174 O O   . HOH K 3 .   ? 19.022  68.531  -22.114 1.00 46.23  ? 501 HOH C O   1 
HETATM 14175 O O   . HOH K 3 .   ? 15.401  70.615  -24.869 1.00 42.72  ? 502 HOH C O   1 
HETATM 14176 O O   . HOH K 3 .   ? 2.345   52.479  -33.838 1.00 56.44  ? 503 HOH C O   1 
HETATM 14177 O O   . HOH K 3 .   ? -22.437 24.745  -33.897 1.00 45.28  ? 504 HOH C O   1 
HETATM 14178 O O   . HOH K 3 .   ? -17.505 57.015  -9.580  1.00 51.44  ? 505 HOH C O   1 
HETATM 14179 O O   . HOH K 3 .   ? 1.329   66.848  -2.083  1.00 50.54  ? 506 HOH C O   1 
HETATM 14180 O O   . HOH K 3 .   ? -17.717 22.695  -9.218  1.00 53.80  ? 507 HOH C O   1 
HETATM 14181 O O   . HOH K 3 .   ? -8.102  49.646  -22.837 1.00 38.75  ? 508 HOH C O   1 
HETATM 14182 O O   . HOH K 3 .   ? -11.576 42.304  2.357   1.00 60.13  ? 509 HOH C O   1 
HETATM 14183 O O   . HOH K 3 .   ? -19.970 44.599  -54.647 1.00 30.73  ? 510 HOH C O   1 
HETATM 14184 O O   . HOH K 3 .   ? -4.892  53.482  -0.485  1.00 47.53  ? 511 HOH C O   1 
HETATM 14185 O O   . HOH K 3 .   ? 8.476   23.790  -46.215 1.00 49.99  ? 512 HOH C O   1 
HETATM 14186 O O   . HOH K 3 .   ? -30.003 34.440  -47.770 1.00 49.65  ? 513 HOH C O   1 
HETATM 14187 O O   . HOH K 3 .   ? -3.017  39.765  -32.071 1.00 31.91  ? 514 HOH C O   1 
HETATM 14188 O O   . HOH K 3 .   ? -9.448  41.179  2.819   1.00 66.15  ? 515 HOH C O   1 
HETATM 14189 O O   . HOH K 3 .   ? -22.608 27.051  -13.462 1.00 40.95  ? 516 HOH C O   1 
HETATM 14190 O O   . HOH K 3 .   ? -17.661 49.238  -10.230 1.00 27.01  ? 517 HOH C O   1 
HETATM 14191 O O   . HOH K 3 .   ? -6.581  29.647  -36.191 1.00 26.48  ? 518 HOH C O   1 
HETATM 14192 O O   . HOH K 3 .   ? -14.164 34.126  -36.207 1.00 33.16  ? 519 HOH C O   1 
HETATM 14193 O O   . HOH K 3 .   ? -17.268 29.489  -34.274 1.00 23.01  ? 520 HOH C O   1 
HETATM 14194 O O   . HOH K 3 .   ? -19.784 34.725  -57.281 1.00 47.98  ? 521 HOH C O   1 
HETATM 14195 O O   . HOH K 3 .   ? -8.978  55.109  4.890   1.00 42.49  ? 522 HOH C O   1 
HETATM 14196 O O   . HOH K 3 .   ? -25.035 30.398  -14.614 1.00 41.33  ? 523 HOH C O   1 
HETATM 14197 O O   . HOH K 3 .   ? -9.729  44.350  -26.498 1.00 32.43  ? 524 HOH C O   1 
HETATM 14198 O O   . HOH K 3 .   ? -17.111 30.885  -28.066 1.00 26.60  ? 525 HOH C O   1 
HETATM 14199 O O   . HOH K 3 .   ? -25.810 46.966  -43.690 1.00 49.36  ? 526 HOH C O   1 
HETATM 14200 O O   . HOH K 3 .   ? -17.057 49.911  -31.831 1.00 44.24  ? 527 HOH C O   1 
HETATM 14201 O O   . HOH K 3 .   ? -13.643 37.954  -27.576 1.00 25.38  ? 528 HOH C O   1 
HETATM 14202 O O   . HOH K 3 .   ? -29.473 38.631  -17.139 1.00 35.50  ? 529 HOH C O   1 
HETATM 14203 O O   . HOH K 3 .   ? -17.743 24.498  -25.412 1.00 31.77  ? 530 HOH C O   1 
HETATM 14204 O O   . HOH K 3 .   ? -32.622 37.361  -30.760 1.00 40.90  ? 531 HOH C O   1 
HETATM 14205 O O   . HOH K 3 .   ? -7.613  28.847  -44.364 1.00 36.20  ? 532 HOH C O   1 
HETATM 14206 O O   . HOH K 3 .   ? -19.908 48.471  -33.311 1.00 43.53  ? 533 HOH C O   1 
HETATM 14207 O O   . HOH K 3 .   ? -20.405 29.978  -37.473 1.00 35.49  ? 534 HOH C O   1 
HETATM 14208 O O   . HOH K 3 .   ? -33.569 48.731  -19.144 1.00 43.34  ? 535 HOH C O   1 
HETATM 14209 O O   . HOH K 3 .   ? 2.187   36.667  -39.439 1.00 34.53  ? 536 HOH C O   1 
HETATM 14210 O O   . HOH K 3 .   ? -24.535 46.156  -6.024  1.00 56.21  ? 537 HOH C O   1 
HETATM 14211 O O   . HOH K 3 .   ? -29.630 36.089  -16.857 1.00 42.59  ? 538 HOH C O   1 
HETATM 14212 O O   . HOH K 3 .   ? 11.237  43.945  -18.362 1.00 42.53  ? 539 HOH C O   1 
HETATM 14213 O O   . HOH K 3 .   ? 4.643   36.831  -1.932  1.00 45.03  ? 540 HOH C O   1 
HETATM 14214 O O   . HOH K 3 .   ? -2.322  33.719  -55.577 1.00 59.30  ? 541 HOH C O   1 
HETATM 14215 O O   . HOH K 3 .   ? -20.488 31.172  -33.471 1.00 30.50  ? 542 HOH C O   1 
HETATM 14216 O O   . HOH K 3 .   ? 11.227  33.629  -54.460 1.00 59.07  ? 543 HOH C O   1 
HETATM 14217 O O   . HOH K 3 .   ? 3.054   26.789  -43.001 1.00 30.98  ? 544 HOH C O   1 
HETATM 14218 O O   . HOH K 3 .   ? -23.686 50.374  -8.402  1.00 44.76  ? 545 HOH C O   1 
HETATM 14219 O O   . HOH K 3 .   ? 12.821  54.773  -39.263 1.00 54.11  ? 546 HOH C O   1 
HETATM 14220 O O   . HOH K 3 .   ? 11.858  27.331  -51.826 1.00 39.85  ? 547 HOH C O   1 
HETATM 14221 O O   . HOH K 3 .   ? -27.506 31.820  -14.791 1.00 47.38  ? 548 HOH C O   1 
HETATM 14222 O O   . HOH K 3 .   ? -4.287  61.882  -2.395  1.00 49.04  ? 549 HOH C O   1 
HETATM 14223 O O   . HOH K 3 .   ? -10.700 57.982  -26.429 1.00 38.63  ? 550 HOH C O   1 
HETATM 14224 O O   . HOH K 3 .   ? -25.861 59.270  -19.776 1.00 45.48  ? 551 HOH C O   1 
HETATM 14225 O O   . HOH K 3 .   ? -33.188 45.996  -27.160 1.00 45.72  ? 552 HOH C O   1 
HETATM 14226 O O   . HOH K 3 .   ? -6.226  54.142  -27.217 1.00 37.89  ? 553 HOH C O   1 
HETATM 14227 O O   . HOH K 3 .   ? 3.606   53.730  -1.944  1.00 47.26  ? 554 HOH C O   1 
HETATM 14228 O O   . HOH K 3 .   ? -26.016 32.455  -31.085 1.00 25.35  ? 555 HOH C O   1 
HETATM 14229 O O   . HOH K 3 .   ? -20.334 47.661  -35.809 1.00 43.91  ? 556 HOH C O   1 
HETATM 14230 O O   . HOH K 3 .   ? 3.986   35.140  -7.534  1.00 31.89  ? 557 HOH C O   1 
HETATM 14231 O O   . HOH K 3 .   ? -14.170 63.085  -27.661 1.00 52.01  ? 558 HOH C O   1 
HETATM 14232 O O   . HOH K 3 .   ? -14.710 34.320  -30.729 1.00 25.38  ? 559 HOH C O   1 
HETATM 14233 O O   . HOH K 3 .   ? 0.944   44.430  -26.970 1.00 35.53  ? 560 HOH C O   1 
HETATM 14234 O O   . HOH K 3 .   ? -15.141 34.456  -33.508 1.00 30.89  ? 561 HOH C O   1 
HETATM 14235 O O   . HOH K 3 .   ? -27.880 24.572  -34.716 1.00 42.10  ? 562 HOH C O   1 
HETATM 14236 O O   . HOH K 3 .   ? -4.339  70.452  -9.483  1.00 48.92  ? 563 HOH C O   1 
HETATM 14237 O O   . HOH K 3 .   ? -11.836 35.536  -36.908 1.00 36.12  ? 564 HOH C O   1 
HETATM 14238 O O   . HOH K 3 .   ? -22.671 31.423  -10.363 1.00 49.95  ? 565 HOH C O   1 
HETATM 14239 O O   . HOH K 3 .   ? 6.362   70.055  -4.342  1.00 57.87  ? 566 HOH C O   1 
HETATM 14240 O O   . HOH K 3 .   ? -12.425 45.119  -54.718 1.00 38.22  ? 567 HOH C O   1 
HETATM 14241 O O   . HOH K 3 .   ? -31.633 38.892  -38.623 1.00 39.14  ? 568 HOH C O   1 
HETATM 14242 O O   . HOH K 3 .   ? 5.337   31.615  -12.275 1.00 39.13  ? 569 HOH C O   1 
HETATM 14243 O O   . HOH K 3 .   ? -26.632 55.790  -26.018 1.00 40.64  ? 570 HOH C O   1 
HETATM 14244 O O   . HOH K 3 .   ? -16.648 27.306  -38.139 1.00 30.39  ? 571 HOH C O   1 
HETATM 14245 O O   . HOH K 3 .   ? -21.633 37.340  -39.123 1.00 38.28  ? 572 HOH C O   1 
HETATM 14246 O O   . HOH K 3 .   ? 4.145   27.182  -52.437 1.00 45.07  ? 573 HOH C O   1 
HETATM 14247 O O   . HOH K 3 .   ? -25.379 36.571  -38.327 1.00 39.99  ? 574 HOH C O   1 
HETATM 14248 O O   . HOH K 3 .   ? -17.512 54.847  -3.280  1.00 50.97  ? 575 HOH C O   1 
HETATM 14249 O O   . HOH K 3 .   ? -15.783 52.312  -31.623 1.00 33.10  ? 576 HOH C O   1 
HETATM 14250 O O   . HOH K 3 .   ? 15.877  51.905  -15.415 1.00 53.99  ? 577 HOH C O   1 
HETATM 14251 O O   . HOH K 3 .   ? -1.144  43.313  -28.415 1.00 32.88  ? 578 HOH C O   1 
HETATM 14252 O O   . HOH K 3 .   ? -24.893 31.924  -11.592 1.00 51.79  ? 579 HOH C O   1 
HETATM 14253 O O   . HOH K 3 .   ? 4.263   26.897  -47.568 1.00 27.46  ? 580 HOH C O   1 
HETATM 14254 O O   . HOH K 3 .   ? -13.885 38.234  -36.811 1.00 33.07  ? 581 HOH C O   1 
HETATM 14255 O O   . HOH K 3 .   ? 0.080   32.153  -3.815  1.00 38.83  ? 582 HOH C O   1 
HETATM 14256 O O   . HOH K 3 .   ? -26.015 49.522  -36.425 1.00 59.98  ? 583 HOH C O   1 
HETATM 14257 O O   . HOH K 3 .   ? -22.729 44.210  -32.127 1.00 40.95  ? 584 HOH C O   1 
HETATM 14258 O O   . HOH K 3 .   ? -14.747 36.890  -29.800 1.00 28.42  ? 585 HOH C O   1 
HETATM 14259 O O   . HOH K 3 .   ? -5.925  20.925  -0.023  1.00 45.19  ? 586 HOH C O   1 
HETATM 14260 O O   . HOH K 3 .   ? -33.865 46.231  -30.345 1.00 53.46  ? 587 HOH C O   1 
HETATM 14261 O O   . HOH K 3 .   ? -2.869  46.955  -48.164 1.00 44.24  ? 588 HOH C O   1 
HETATM 14262 O O   . HOH K 3 .   ? 4.263   71.853  -17.582 1.00 55.68  ? 589 HOH C O   1 
HETATM 14263 O O   . HOH K 3 .   ? -19.976 19.876  -20.087 1.00 51.87  ? 590 HOH C O   1 
HETATM 14264 O O   . HOH K 3 .   ? -13.431 51.976  0.637   1.00 49.79  ? 591 HOH C O   1 
HETATM 14265 O O   . HOH K 3 .   ? -26.185 48.248  -6.323  1.00 57.99  ? 592 HOH C O   1 
HETATM 14266 O O   . HOH K 3 .   ? -32.746 39.250  -12.742 1.00 52.57  ? 593 HOH C O   1 
HETATM 14267 O O   . HOH K 3 .   ? -10.884 60.204  -5.569  1.00 58.58  ? 594 HOH C O   1 
HETATM 14268 O O   . HOH K 3 .   ? 3.654   34.973  -16.150 1.00 51.47  ? 595 HOH C O   1 
HETATM 14269 O O   . HOH K 3 .   ? 5.737   37.033  -4.247  1.00 50.20  ? 596 HOH C O   1 
HETATM 14270 O O   . HOH K 3 .   ? -30.614 35.095  -14.615 1.00 40.29  ? 597 HOH C O   1 
HETATM 14271 O O   . HOH K 3 .   ? 7.557   44.511  -33.688 1.00 45.04  ? 598 HOH C O   1 
HETATM 14272 O O   . HOH K 3 .   ? 5.238   24.685  -48.933 1.00 47.03  ? 599 HOH C O   1 
HETATM 14273 O O   . HOH K 3 .   ? -15.389 53.529  -33.811 1.00 43.22  ? 600 HOH C O   1 
HETATM 14274 O O   . HOH K 3 .   ? -21.018 34.231  -59.196 1.00 48.42  ? 601 HOH C O   1 
HETATM 14275 O O   . HOH K 3 .   ? -16.194 33.988  -53.827 1.00 54.27  ? 602 HOH C O   1 
HETATM 14276 O O   . HOH K 3 .   ? -34.552 30.441  -21.142 1.00 53.04  ? 603 HOH C O   1 
HETATM 14277 O O   . HOH K 3 .   ? -27.050 31.726  -9.809  1.00 55.58  ? 604 HOH C O   1 
HETATM 14278 O O   . HOH K 3 .   ? -15.244 65.956  -17.866 1.00 60.11  ? 605 HOH C O   1 
HETATM 14279 O O   . HOH K 3 .   ? -27.301 38.130  -0.051  1.00 46.33  ? 606 HOH C O   1 
HETATM 14280 O O   . HOH K 3 .   ? -25.558 36.244  0.776   1.00 50.82  ? 607 HOH C O   1 
# 
